Log page index: User:ProteinBoxBot/PBB_Log_Index
Protein Status Quick Log - Date: 05:36, 19 November 2007 (UTC)
[edit]Proteins without matches (7)
[edit]Proteins with a High Potential Match (7)
[edit]Redirected Proteins (11)
[edit]Manual Inspection (Page not found) (14)
[edit]
Protein Status Grid - Date: 05:36, 19 November 2007 (UTC)
[edit]Vebose Log - Date: 05:36, 19 November 2007 (UTC)
[edit]- INFO: Beginning work on ANP32A... {November 18, 2007 9:23:46 PM PST}
- SEARCH REDIRECT: Control Box Found: ANP32A {November 18, 2007 9:24:37 PM PST}
- UPDATE PROTEIN BOX: Updating Protein Box, No errors. {November 18, 2007 9:24:39 PM PST}
- UPDATE SUMMARY: Updating Summary, No Errors. {November 18, 2007 9:24:39 PM PST}
- UPDATE CITATIONS: Updating Citations, No Errors. {November 18, 2007 9:24:39 PM PST}
- UPDATED: Updated protein page: ANP32A {November 18, 2007 9:24:46 PM PST}
- INFO: Beginning work on ARHGEF7... {November 18, 2007 9:26:57 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 18, 2007 9:27:56 PM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}
<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image = PBB_Protein_ARHGEF7_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1by1.
| PDB = {{PDB2|1by1}}, {{PDB2|1zsg}}, {{PDB2|2ak5}}, {{PDB2|2df6}}, {{PDB2|2esw}}, {{PDB2|2g6f}}
| Name = Rho guanine nucleotide exchange factor (GEF) 7
| HGNCid = 15607
| Symbol = ARHGEF7
| AltSymbols =; PAK3; BETA-PIX; COOL1; DKFZp761K1021; KIAA0142; KIAA0412; Nbla10314; P50; P50BP; P85; P85COOL1; P85SPR; PIXB
| OMIM = 605477
| ECnumber =
| Homologene = 2895
| MGIid = 1860493
| GeneAtlas_image1 = PBB_GE_ARHGEF7_202548_s_at_tn.png
| GeneAtlas_image2 = PBB_GE_ARHGEF7_202547_s_at_tn.png
| Function = {{GNF_GO|id=GO:0005085 |text = guanyl-nucleotide exchange factor activity}} {{GNF_GO|id=GO:0005089 |text = Rho guanyl-nucleotide exchange factor activity}} {{GNF_GO|id=GO:0005515 |text = protein binding}}
| Component = {{GNF_GO|id=GO:0005622 |text = intracellular}}
| Process = {{GNF_GO|id=GO:0007165 |text = signal transduction}} {{GNF_GO|id=GO:0035023 |text = regulation of Rho protein signal transduction}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 8874
| Hs_Ensembl = ENSG00000102606
| Hs_RefseqProtein = NP_003890
| Hs_RefseqmRNA = NM_003899
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 13
| Hs_GenLoc_start = 110565783
| Hs_GenLoc_end = 110756081
| Hs_Uniprot = Q14155
| Mm_EntrezGene = 54126
| Mm_Ensembl = ENSMUSG00000031511
| Mm_RefseqmRNA = NM_017402
| Mm_RefseqProtein = NP_059098
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 8
| Mm_GenLoc_start = 11728141
| Mm_GenLoc_end = 11835191
| Mm_Uniprot = Q6XPA5
}}
}}
'''Rho guanine nucleotide exchange factor (GEF) 7''', also known as '''ARHGEF7''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: ARHGEF7 Rho guanine nucleotide exchange factor (GEF) 7| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=8874| accessdate = }}</ref>
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text = Rho GTPases play a fundamental role in numerous cellular processes that are initiated by extracellular stimuli that work through G protein coupled receptors. The encoded protein belongs to a family of cytoplasmic proteins that activate the Ras-like family of Rho proteins by exchanging bound GDP for GTP. It may form a complex with G proteins and stimulate Rho-dependent signals. This protein can induce membrane ruffling. Multiple alternatively spliced transcript variants encoding different isoforms have been described for this gene, but some of their full-length sequences have not been determined.<ref name="entrez">{{cite web | title = Entrez Gene: ARHGEF7 Rho guanine nucleotide exchange factor (GEF) 7| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=8874| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Matoba R, Okubo K, Hori N, ''et al.'' |title=The addition of 5'-coding information to a 3'-directed cDNA library improves analysis of gene expression. |journal=Gene |volume=146 |issue= 2 |pages= 199-207 |year= 1994 |pmid= 8076819 |doi= }}
*{{cite journal | author=Nagase T, Seki N, Tanaka A, ''et al.'' |title=Prediction of the coding sequences of unidentified human genes. IV. The coding sequences of 40 new genes (KIAA0121-KIAA0160) deduced by analysis of cDNA clones from human cell line KG-1. |journal=DNA Res. |volume=2 |issue= 4 |pages= 167-74, 199-210 |year= 1996 |pmid= 8590280 |doi= }}
*{{cite journal | author=Oh WK, Yoo JC, Jo D, ''et al.'' |title=Cloning of a SH3 domain-containing proline-rich protein, p85SPR, and its localization in focal adhesion. |journal=Biochem. Biophys. Res. Commun. |volume=235 |issue= 3 |pages= 794-8 |year= 1997 |pmid= 9207241 |doi= 10.1006/bbrc.1997.6875 }}
*{{cite journal | author=Manser E, Loo TH, Koh CG, ''et al.'' |title=PAK kinases are directly coupled to the PIX family of nucleotide exchange factors. |journal=Mol. Cell |volume=1 |issue= 2 |pages= 183-92 |year= 1998 |pmid= 9659915 |doi= }}
*{{cite journal | author=Bagrodia S, Taylor SJ, Jordon KA, ''et al.'' |title=A novel regulator of p21-activated kinases. |journal=J. Biol. Chem. |volume=273 |issue= 37 |pages= 23633-6 |year= 1998 |pmid= 9726964 |doi= }}
*{{cite journal | author=Turner CE, Brown MC, Perrotta JA, ''et al.'' |title=Paxillin LD4 motif binds PAK and PIX through a novel 95-kD ankyrin repeat, ARF-GAP protein: A role in cytoskeletal remodeling. |journal=J. Cell Biol. |volume=145 |issue= 4 |pages= 851-63 |year= 1999 |pmid= 10330411 |doi= }}
*{{cite journal | author=Bagrodia S, Bailey D, Lenard Z, ''et al.'' |title=A tyrosine-phosphorylated protein that binds to an important regulatory region on the cool family of p21-activated kinase-binding proteins. |journal=J. Biol. Chem. |volume=274 |issue= 32 |pages= 22393-400 |year= 1999 |pmid= 10428811 |doi= }}
*{{cite journal | author=Premont RT, Claing A, Vitale N, ''et al.'' |title=The GIT family of ADP-ribosylation factor GTPase-activating proteins. Functional diversity of GIT2 through alternative splicing. |journal=J. Biol. Chem. |volume=275 |issue= 29 |pages= 22373-80 |year= 2000 |pmid= 10896954 |doi= }}
*{{cite journal | author=Ku GM, Yablonski D, Manser E, ''et al.'' |title=A PAK1-PIX-PKL complex is activated by the T-cell receptor independent of Nck, Slp-76 and LAT. |journal=EMBO J. |volume=20 |issue= 3 |pages= 457-65 |year= 2001 |pmid= 11157752 |doi= 10.1093/emboj/20.3.457 }}
*{{cite journal | author=Koh CG, Tan EJ, Manser E, Lim L |title=The p21-activated kinase PAK is negatively regulated by POPX1 and POPX2, a pair of serine/threonine phosphatases of the PP2C family. |journal=Curr. Biol. |volume=12 |issue= 4 |pages= 317-21 |year= 2002 |pmid= 11864573 |doi= }}
*{{cite journal | author=Brown MC, West KA, Turner CE |title=Paxillin-dependent paxillin kinase linker and p21-activated kinase localization to focal adhesions involves a multistep activation pathway. |journal=Mol. Biol. Cell |volume=13 |issue= 5 |pages= 1550-65 |year= 2002 |pmid= 12006652 |doi= 10.1091/mbc.02-02-0015 }}
*{{cite journal | author=Shin EY, Shin KS, Lee CS, ''et al.'' |title=Phosphorylation of p85 beta PIX, a Rac/Cdc42-specific guanine nucleotide exchange factor, via the Ras/ERK/PAK2 pathway is required for basic fibroblast growth factor-induced neurite outgrowth. |journal=J. Biol. Chem. |volume=277 |issue= 46 |pages= 44417-30 |year= 2003 |pmid= 12226077 |doi= 10.1074/jbc.M203754200 }}
*{{cite journal | author=Strausberg RL, Feingold EA, Grouse LH, ''et al.'' |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899-903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899 }}
*{{cite journal | author=Rosenberger G, Jantke I, Gal A, Kutsche K |title=Interaction of alphaPIX (ARHGEF6) with beta-parvin (PARVB) suggests an involvement of alphaPIX in integrin-mediated signaling. |journal=Hum. Mol. Genet. |volume=12 |issue= 2 |pages= 155-67 |year= 2003 |pmid= 12499396 |doi= }}
*{{cite journal | author=Park E, Na M, Choi J, ''et al.'' |title=The Shank family of postsynaptic density proteins interacts with and promotes synaptic accumulation of the beta PIX guanine nucleotide exchange factor for Rac1 and Cdc42. |journal=J. Biol. Chem. |volume=278 |issue= 21 |pages= 19220-9 |year= 2003 |pmid= 12626503 |doi= 10.1074/jbc.M301052200 }}
*{{cite journal | author=Mignone F, Grillo G, Liuni S, Pesole G |title=Computational identification of protein coding potential of conserved sequence tags through cross-species evolutionary analysis. |journal=Nucleic Acids Res. |volume=31 |issue= 15 |pages= 4639-45 |year= 2003 |pmid= 12888525 |doi= }}
*{{cite journal | author=Yamamoto Y, Fujimoto Y, Arai R, ''et al.'' |title=Retrotransposon-mediated restoration of Chlorella telomeres: accumulation of Zepp retrotransposons at termini of newly formed minichromosomes. |journal=Nucleic Acids Res. |volume=31 |issue= 15 |pages= 4646-53 |year= 2003 |pmid= 12888526 |doi= }}
*{{cite journal | author=Flanders JA, Feng Q, Bagrodia S, ''et al.'' |title=The Cbl proteins are binding partners for the Cool/Pix family of p21-activated kinase-binding proteins. |journal=FEBS Lett. |volume=550 |issue= 1-3 |pages= 119-23 |year= 2003 |pmid= 12935897 |doi= }}
*{{cite journal | author=Shin EY, Woo KN, Lee CS, ''et al.'' |title=Basic fibroblast growth factor stimulates activation of Rac1 through a p85 betaPIX phosphorylation-dependent pathway. |journal=J. Biol. Chem. |volume=279 |issue= 3 |pages= 1994-2004 |year= 2004 |pmid= 14557270 |doi= 10.1074/jbc.M307330200 }}
*{{cite journal | author=Lim CS, Kim SH, Jung JG, ''et al.'' |title=Regulation of SPIN90 phosphorylation and interaction with Nck by ERK and cell adhesion. |journal=J. Biol. Chem. |volume=278 |issue= 52 |pages= 52116-23 |year= 2004 |pmid= 14559906 |doi= 10.1074/jbc.M310974200 }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on C1QA... {November 18, 2007 9:12:04 PM PST}
- SEARCH REDIRECT: Control Box Found: C1QA {November 18, 2007 9:12:23 PM PST}
- UPDATE PROTEIN BOX: Updating Protein Box, No errors. {November 18, 2007 9:12:24 PM PST}
- UPDATE SUMMARY: Updating Summary, No Errors. {November 18, 2007 9:12:24 PM PST}
- UPDATE CITATIONS: Updating Citations, No Errors. {November 18, 2007 9:12:24 PM PST}
- UPDATED: Updated protein page: C1QA {November 18, 2007 9:12:30 PM PST}
- INFO: Beginning work on CALM2... {November 18, 2007 9:12:31 PM PST}
- SEARCH REDIRECT: Control Box Found: CALM2 {November 18, 2007 9:12:57 PM PST}
- UPDATE PROTEIN BOX: Updating Protein Box, No errors. {November 18, 2007 9:12:58 PM PST}
- UPDATE SUMMARY: Updating Summary, No Errors. {November 18, 2007 9:12:58 PM PST}
- UPDATE CITATIONS: Updating Citations, No Errors. {November 18, 2007 9:12:58 PM PST}
- UPDATED: Updated protein page: CALM2 {November 18, 2007 9:13:04 PM PST}
- INFO: Beginning work on CBLB... {November 18, 2007 9:13:04 PM PST}
- SEARCH REDIRECT: Control Box Found: CBLB {November 18, 2007 9:13:52 PM PST}
- UPDATE PROTEIN BOX: Updating Protein Box, No errors. {November 18, 2007 9:13:54 PM PST}
- UPDATE SUMMARY: Updating Summary, No Errors. {November 18, 2007 9:13:54 PM PST}
- UPDATE CITATIONS: Updating Citations, No Errors. {November 18, 2007 9:13:54 PM PST}
- UPDATED: Updated protein page: CBLB {November 18, 2007 9:14:00 PM PST}
- INFO: Beginning work on CLCN5... {November 18, 2007 9:14:00 PM PST}
- SEARCH REDIRECT: Control Box Found: CLCN5 {November 18, 2007 9:14:54 PM PST}
- UPDATE PROTEIN BOX: Updating Protein Box, No errors. {November 18, 2007 9:15:51 PM PST}
- UPDATE SUMMARY: Updating Summary, No Errors. {November 18, 2007 9:15:51 PM PST}
- UPDATE CITATIONS: Updating Citations, No Errors. {November 18, 2007 9:15:51 PM PST}
- UPDATED: Updated protein page: CLCN5 {November 18, 2007 9:15:58 PM PST}
- INFO: Beginning work on DYSF... {November 18, 2007 9:25:12 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 18, 2007 9:25:39 PM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}
<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image =
| image_source =
| PDB =
| Name = Dysferlin, limb girdle muscular dystrophy 2B (autosomal recessive)
| HGNCid = 3097
| Symbol = DYSF
| AltSymbols =; FER1L1; FLJ00175; FLJ90168; LGMD2B
| OMIM = 603009
| ECnumber =
| Homologene = 20748
| MGIid = 1349385
| GeneAtlas_image1 = PBB_GE_DYSF_218660_at_tn.png
| Function = {{GNF_GO|id=GO:0005515 |text = protein binding}}
| Component = {{GNF_GO|id=GO:0016021 |text = integral to membrane}} {{GNF_GO|id=GO:0042383 |text = sarcolemma}}
| Process = {{GNF_GO|id=GO:0001778 |text = plasma membrane repair}} {{GNF_GO|id=GO:0006936 |text = muscle contraction}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 8291
| Hs_Ensembl = ENSG00000135636
| Hs_RefseqProtein = NP_003485
| Hs_RefseqmRNA = NM_003494
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 2
| Hs_GenLoc_start = 71534268
| Hs_GenLoc_end = 71767398
| Hs_Uniprot = O75923
| Mm_EntrezGene = 26903
| Mm_Ensembl = ENSMUSG00000033788
| Mm_RefseqmRNA = NM_001077694
| Mm_RefseqProtein = NP_001071162
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 6
| Mm_GenLoc_start = 83985047
| Mm_GenLoc_end = 84176717
| Mm_Uniprot = Q7TQI2
}}
}}
'''Dysferlin, limb girdle muscular dystrophy 2B (autosomal recessive)''', also known as '''DYSF''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: DYSF dysferlin, limb girdle muscular dystrophy 2B (autosomal recessive)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=8291| accessdate = }}</ref>
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text = The protein encoded by this gene belongs to the ferlin family and is a skeletal muscle protein found associated with the sarcolemma. It is involved in muscle contraction and contains C2 domains that play a role in calcium-mediated membrane fusion events, suggesting that it may be involved in membrane regeneration and repair. In addition, the protein encoded by this gene binds caveolin-3, a skeletal muscle membrane protein which is important in the formation of caveolae. Specific mutations in this gene have been shown to cause autosomal recessive limb girdle muscular dystrophy type 2B (LGMD2B) as well as Miyoshi myopathy.<ref name="entrez">{{cite web | title = Entrez Gene: DYSF dysferlin, limb girdle muscular dystrophy 2B (autosomal recessive)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=8291| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Bejaoui K, Hirabayashi K, Hentati F, ''et al.'' |title=Linkage of Miyoshi myopathy (distal autosomal recessive muscular dystrophy) locus to chromosome 2p12-14. |journal=Neurology |volume=45 |issue= 4 |pages= 768-72 |year= 1995 |pmid= 7723968 |doi= }}
*{{cite journal | author=Bashir R, Strachan T, Keers S, ''et al.'' |title=A gene for autosomal recessive limb-girdle muscular dystrophy maps to chromosome 2p. |journal=Hum. Mol. Genet. |volume=3 |issue= 3 |pages= 455-7 |year= 1994 |pmid= 8012357 |doi= }}
*{{cite journal | author=Passos-Bueno MR, Richard I, Vainzof M, ''et al.'' |title=Evidence of genetic heterogeneity in the autosomal recessive adult forms of limb-girdle muscular dystrophy following linkage analysis with 15q probes in Brazilian families. |journal=J. Med. Genet. |volume=30 |issue= 5 |pages= 385-7 |year= 1993 |pmid= 8320700 |doi= }}
*{{cite journal | author=Liu J, Aoki M, Illa I, ''et al.'' |title=Dysferlin, a novel skeletal muscle gene, is mutated in Miyoshi myopathy and limb girdle muscular dystrophy. |journal=Nat. Genet. |volume=20 |issue= 1 |pages= 31-6 |year= 1998 |pmid= 9731526 |doi= 10.1038/1682 }}
*{{cite journal | author=Bashir R, Britton S, Strachan T, ''et al.'' |title=A gene related to Caenorhabditis elegans spermatogenesis factor fer-1 is mutated in limb-girdle muscular dystrophy type 2B. |journal=Nat. Genet. |volume=20 |issue= 1 |pages= 37-42 |year= 1998 |pmid= 9731527 |doi= 10.1038/1689 }}
*{{cite journal | author=Anderson LV, Davison K, Moss JA, ''et al.'' |title=Dysferlin is a plasma membrane protein and is expressed early in human development. |journal=Hum. Mol. Genet. |volume=8 |issue= 5 |pages= 855-61 |year= 1999 |pmid= 10196375 |doi= }}
*{{cite journal | author=Weiler T, Bashir R, Anderson LV, ''et al.'' |title=Identical mutation in patients with limb girdle muscular dystrophy type 2B or Miyoshi myopathy suggests a role for modifier gene(s). |journal=Hum. Mol. Genet. |volume=8 |issue= 5 |pages= 871-7 |year= 1999 |pmid= 10196377 |doi= }}
*{{cite journal | author=Matsuda C, Aoki M, Hayashi YK, ''et al.'' |title=Dysferlin is a surface membrane-associated protein that is absent in Miyoshi myopathy. |journal=Neurology |volume=53 |issue= 5 |pages= 1119-22 |year= 1999 |pmid= 10496277 |doi= }}
*{{cite journal | author=Illa I, Serrano-Munuera C, Gallardo E, ''et al.'' |title=Distal anterior compartment myopathy: a dysferlin mutation causing a new muscular dystrophy phenotype. |journal=Ann. Neurol. |volume=49 |issue= 1 |pages= 130-4 |year= 2001 |pmid= 11198284 |doi= }}
*{{cite journal | author=Aoki M, Liu J, Richard I, ''et al.'' |title=Genomic organization of the dysferlin gene and novel mutations in Miyoshi myopathy. |journal=Neurology |volume=57 |issue= 2 |pages= 271-8 |year= 2001 |pmid= 11468312 |doi= }}
*{{cite journal | author=Matsuda C, Hayashi YK, Ogawa M, ''et al.'' |title=The sarcolemmal proteins dysferlin and caveolin-3 interact in skeletal muscle. |journal=Hum. Mol. Genet. |volume=10 |issue= 17 |pages= 1761-6 |year= 2002 |pmid= 11532985 |doi= }}
*{{cite journal | author=Ikezoe K, Furuya H, Ohyagi Y, ''et al.'' |title=Dysferlin expression in tubular aggregates: their possible relationship to endoplasmic reticulum stress. |journal=Acta Neuropathol. |volume=105 |issue= 6 |pages= 603-9 |year= 2003 |pmid= 12664320 |doi= 10.1007/s00401-003-0686-1 }}
*{{cite journal | author=von Tell D, Bruder CE, Anderson LV, ''et al.'' |title=Refined mapping of the Welander distal myopathy region on chromosome 2p13 positions the new candidate region telomeric of the DYSF locus. |journal=Neurogenetics |volume=4 |issue= 4 |pages= 173-7 |year= 2003 |pmid= 12836053 |doi= 10.1007/s10048-003-0154-z }}
*{{cite journal | author=Lennon NJ, Kho A, Bacskai BJ, ''et al.'' |title=Dysferlin interacts with annexins A1 and A2 and mediates sarcolemmal wound-healing. |journal=J. Biol. Chem. |volume=278 |issue= 50 |pages= 50466-73 |year= 2004 |pmid= 14506282 |doi= 10.1074/jbc.M307247200 }}
*{{cite journal | author=Katz JS, Rando TA, Barohn RJ, ''et al.'' |title=Late-onset distal muscular dystrophy affecting the posterior calves. |journal=Muscle Nerve |volume=28 |issue= 4 |pages= 443-8 |year= 2003 |pmid= 14506716 |doi= 10.1002/mus.10458 }}
*{{cite journal | author=Confalonieri P, Oliva L, Andreetta F, ''et al.'' |title=Muscle inflammation and MHC class I up-regulation in muscular dystrophy with lack of dysferlin: an immunopathological study. |journal=J. Neuroimmunol. |volume=142 |issue= 1-2 |pages= 130-6 |year= 2004 |pmid= 14512171 |doi= }}
*{{cite journal | author=Foxton RM, Laval SH, Bushby KM |title=Characterisation of the dysferlin skeletal muscle promoter. |journal=Eur. J. Hum. Genet. |volume=12 |issue= 2 |pages= 127-31 |year= 2004 |pmid= 14560310 |doi= 10.1038/sj.ejhg.5201092 }}
*{{cite journal | author=Cagliani R, Fortunato F, Giorda R, ''et al.'' |title=Molecular analysis of LGMD-2B and MM patients: identification of novel DYSF mutations and possible founder effect in the Italian population. |journal=Neuromuscul. Disord. |volume=13 |issue= 10 |pages= 788-95 |year= 2004 |pmid= 14678801 |doi= }}
*{{cite journal | author=Capanni C, Sabatelli P, Mattioli E, ''et al.'' |title=Dysferlin in a hyperCKaemic patient with caveolin 3 mutation and in C2C12 cells after p38 MAP kinase inhibition. |journal=Exp. Mol. Med. |volume=35 |issue= 6 |pages= 538-44 |year= 2004 |pmid= 14749532 |doi= }}
*{{cite journal | author=Brüss M, Homann J, Molderings GJ |title=[Dysferlinopathy as an extrahepatic cause for the elevation of serum transaminases] |journal=Med. Klin. (Munich) |volume=99 |issue= 6 |pages= 326-9 |year= 2004 |pmid= 15221058 |doi= 10.1007/s00063-004-1046-1 }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on HDAC6... {November 18, 2007 9:29:29 PM PST}
- SEARCH REDIRECT: Control Box Found: HDAC6 {November 18, 2007 9:30:08 PM PST}
- UPDATE PROTEIN BOX: Updating Protein Box, No errors. {November 18, 2007 9:30:11 PM PST}
- UPDATE SUMMARY: Updating Summary, No Errors. {November 18, 2007 9:30:11 PM PST}
- UPDATE CITATIONS: Updating Citations, No Errors. {November 18, 2007 9:30:11 PM PST}
- UPDATED: Updated protein page: HDAC6 {November 18, 2007 9:30:18 PM PST}
- INFO: Beginning work on MAD1L1... {November 18, 2007 9:25:39 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 18, 2007 9:26:11 PM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}
<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image = PBB_Protein_MAD1L1_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1go4.
| PDB = {{PDB2|1go4}}
| Name = MAD1 mitotic arrest deficient-like 1 (yeast)
| HGNCid = 6762
| Symbol = MAD1L1
| AltSymbols =; MAD1; HsMAD1; PIG9; TP53I9; TXBP181
| OMIM = 602686
| ECnumber =
| Homologene = 74500
| MGIid = 1341857
| GeneAtlas_image1 = PBB_GE_MAD1L1_204857_at_tn.png
| Function = {{GNF_GO|id=GO:0003674 |text = molecular_function}}
| Component = {{GNF_GO|id=GO:0005634 |text = nucleus}} {{GNF_GO|id=GO:0005813 |text = centrosome}} {{GNF_GO|id=GO:0005819 |text = spindle}}
| Process = {{GNF_GO|id=GO:0000089 |text = mitotic metaphase}} {{GNF_GO|id=GO:0000090 |text = mitotic anaphase}} {{GNF_GO|id=GO:0000093 |text = mitotic telophase}} {{GNF_GO|id=GO:0007049 |text = cell cycle}} {{GNF_GO|id=GO:0007093 |text = mitotic cell cycle checkpoint}} {{GNF_GO|id=GO:0051301 |text = cell division}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 8379
| Hs_Ensembl = ENSG00000002822
| Hs_RefseqProtein = NP_001013858
| Hs_RefseqmRNA = NM_001013836
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 7
| Hs_GenLoc_start = 1821956
| Hs_GenLoc_end = 2236304
| Hs_Uniprot = Q9Y6D9
| Mm_EntrezGene = 17120
| Mm_Ensembl = ENSMUSG00000029554
| Mm_RefseqmRNA = NM_010752
| Mm_RefseqProtein = NP_034882
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 5
| Mm_GenLoc_start = 140261163
| Mm_GenLoc_end = 140574024
| Mm_Uniprot = Q9WTX8
}}
}}
'''MAD1 mitotic arrest deficient-like 1 (yeast)''', also known as '''MAD1L1''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: MAD1L1 MAD1 mitotic arrest deficient-like 1 (yeast)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=8379| accessdate = }}</ref>
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text = MAD1L1 is a component of the mitotic spindle-assembly checkpoint that prevents the onset of anaphase until all chromosome are properly aligned at the metaphase plate. MAD1L1 functions as a homodimer and interacts with MAD2L1. MAD1L1 may play a role in cell cycle control and tumor suppression. Three transcript variants encoding the same protein have been found for this gene.<ref name="entrez">{{cite web | title = Entrez Gene: MAD1L1 MAD1 mitotic arrest deficient-like 1 (yeast)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=8379| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Polyak K, Xia Y, Zweier JL, ''et al.'' |title=A model for p53-induced apoptosis. |journal=Nature |volume=389 |issue= 6648 |pages= 300-5 |year= 1997 |pmid= 9305847 |doi= 10.1038/38525 }}
*{{cite journal | author=Jin DY, Spencer F, Jeang KT |title=Human T cell leukemia virus type 1 oncoprotein Tax targets the human mitotic checkpoint protein MAD1. |journal=Cell |volume=93 |issue= 1 |pages= 81-91 |year= 1998 |pmid= 9546394 |doi= }}
*{{cite journal | author=Jin DY, Kozak CA, Pangilinan F, ''et al.'' |title=Mitotic checkpoint locus MAD1L1 maps to human chromosome 7p22 and mouse chromosome 5. |journal=Genomics |volume=55 |issue= 3 |pages= 363-4 |year= 1999 |pmid= 10049595 |doi= 10.1006/geno.1998.5654 }}
*{{cite journal | author=Seeley TW, Wang L, Zhen JY |title=Phosphorylation of human MAD1 by the BUB1 kinase in vitro. |journal=Biochem. Biophys. Res. Commun. |volume=257 |issue= 2 |pages= 589-95 |year= 1999 |pmid= 10198256 |doi= 10.1006/bbrc.1999.0514 }}
*{{cite journal | author=FitzGerald MJ, Arsura M, Bellas RE, ''et al.'' |title=Differential effects of the widely expressed dMax splice variant of Max on E-box vs initiator element-mediated regulation by c-Myc. |journal=Oncogene |volume=18 |issue= 15 |pages= 2489-98 |year= 1999 |pmid= 10229200 |doi= 10.1038/sj.onc.1202611 }}
*{{cite journal | author=Cahill DP, da Costa LT, Carson-Walter EB, ''et al.'' |title=Characterization of MAD2B and other mitotic spindle checkpoint genes. |journal=Genomics |volume=58 |issue= 2 |pages= 181-7 |year= 1999 |pmid= 10366450 |doi= 10.1006/geno.1999.5831 }}
*{{cite journal | author=Billin AN, Eilers AL, Queva C, Ayer DE |title=Mlx, a novel Max-like BHLHZip protein that interacts with the Max network of transcription factors. |journal=J. Biol. Chem. |volume=274 |issue= 51 |pages= 36344-50 |year= 2000 |pmid= 10593926 |doi= }}
*{{cite journal | author=Nomoto S, Haruki N, Takahashi T, ''et al.'' |title=Search for in vivo somatic mutations in the mitotic checkpoint gene, hMAD1, in human lung cancers. |journal=Oncogene |volume=18 |issue= 50 |pages= 7180-3 |year= 2000 |pmid= 10597320 |doi= 10.1038/sj.onc.1203141 }}
*{{cite journal | author=Spronk CA, Tessari M, Kaan AM, ''et al.'' |title=The Mad1-Sin3B interaction involves a novel helical fold. |journal=Nat. Struct. Biol. |volume=7 |issue= 12 |pages= 1100-4 |year= 2001 |pmid= 11101889 |doi= 10.1038/81944 }}
*{{cite journal | author=Brubaker K, Cowley SM, Huang K, ''et al.'' |title=Solution structure of the interacting domains of the Mad-Sin3 complex: implications for recruitment of a chromatin-modifying complex. |journal=Cell |volume=103 |issue= 4 |pages= 655-65 |year= 2001 |pmid= 11106735 |doi= }}
*{{cite journal | author=Spronk CA, Jansen JF, Tessari M, ''et al.'' |title=Sequence-specific assignment of the PAH2 domain of Sin3B free and bound to Mad1. |journal=J. Biomol. NMR |volume=19 |issue= 4 |pages= 377-8 |year= 2001 |pmid= 11370785 |doi= }}
*{{cite journal | author=Tsukasaki K, Miller CW, Greenspun E, ''et al.'' |title=Mutations in the mitotic check point gene, MAD1L1, in human cancers. |journal=Oncogene |volume=20 |issue= 25 |pages= 3301-5 |year= 2001 |pmid= 11423979 |doi= 10.1038/sj.onc.1204421 }}
*{{cite journal | author=Sironi L, Melixetian M, Faretta M, ''et al.'' |title=Mad2 binding to Mad1 and Cdc20, rather than oligomerization, is required for the spindle checkpoint. |journal=EMBO J. |volume=20 |issue= 22 |pages= 6371-82 |year= 2002 |pmid= 11707408 |doi= 10.1093/emboj/20.22.6371 }}
*{{cite journal | author=Luo X, Tang Z, Rizo J, Yu H |title=The Mad2 spindle checkpoint protein undergoes similar major conformational changes upon binding to either Mad1 or Cdc20. |journal=Mol. Cell |volume=9 |issue= 1 |pages= 59-71 |year= 2002 |pmid= 11804586 |doi= }}
*{{cite journal | author=Iwanaga Y, Jeang KT |title=Expression of mitotic spindle checkpoint protein hsMAD1 correlates with cellular proliferation and is activated by a gain-of-function p53 mutant. |journal=Cancer Res. |volume=62 |issue= 9 |pages= 2618-24 |year= 2002 |pmid= 11980658 |doi= }}
*{{cite journal | author=Sironi L, Mapelli M, Knapp S, ''et al.'' |title=Crystal structure of the tetrameric Mad1-Mad2 core complex: implications of a 'safety belt' binding mechanism for the spindle checkpoint. |journal=EMBO J. |volume=21 |issue= 10 |pages= 2496-506 |year= 2002 |pmid= 12006501 |doi= 10.1093/emboj/21.10.2496 }}
*{{cite journal | author=Martin-Lluesma S, Stucke VM, Nigg EA |title=Role of Hec1 in spindle checkpoint signaling and kinetochore recruitment of Mad1/Mad2. |journal=Science |volume=297 |issue= 5590 |pages= 2267-70 |year= 2002 |pmid= 12351790 |doi= 10.1126/science.1075596 }}
*{{cite journal | author=Ohta Y, Hamada Y, Saitoh N, Katsuoka K |title=Effect of the transcriptional repressor Mad1 on proliferation of human melanoma cells. |journal=Exp. Dermatol. |volume=11 |issue= 5 |pages= 439-47 |year= 2003 |pmid= 12366697 |doi= }}
*{{cite journal | author=Strausberg RL, Feingold EA, Grouse LH, ''et al.'' |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899-903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899 }}
*{{cite journal | author=Hillier LW, Fulton RS, Fulton LA, ''et al.'' |title=The DNA sequence of human chromosome 7. |journal=Nature |volume=424 |issue= 6945 |pages= 157-64 |year= 2003 |pmid= 12853948 |doi= 10.1038/nature01782 }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on NR1H2... {November 18, 2007 9:22:18 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 18, 2007 9:22:57 PM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}
<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image = PBB_Protein_NR1H2_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1p8d.
| PDB = {{PDB2|1p8d}}, {{PDB2|1pq6}}, {{PDB2|1pq9}}, {{PDB2|1pqc}}, {{PDB2|1upv}}, {{PDB2|1upw}}
| Name = Nuclear receptor subfamily 1, group H, member 2
| HGNCid = 7965
| Symbol = NR1H2
| AltSymbols =; UNR; LXR-b; LXRB; NER; NER-I; RIP15
| OMIM = 600380
| ECnumber =
| Homologene = 21397
| MGIid = 1352463
| GeneAtlas_image1 = PBB_GE_NR1H2_218215_s_at_tn.png
| Function = {{GNF_GO|id=GO:0003700 |text = transcription factor activity}} {{GNF_GO|id=GO:0003707 |text = steroid hormone receptor activity}} {{GNF_GO|id=GO:0005515 |text = protein binding}} {{GNF_GO|id=GO:0008270 |text = zinc ion binding}} {{GNF_GO|id=GO:0043565 |text = sequence-specific DNA binding}} {{GNF_GO|id=GO:0046872 |text = metal ion binding}}
| Component = {{GNF_GO|id=GO:0005634 |text = nucleus}} {{GNF_GO|id=GO:0005737 |text = cytoplasm}}
| Process = {{GNF_GO|id=GO:0006350 |text = transcription}} {{GNF_GO|id=GO:0006355 |text = regulation of transcription, DNA-dependent}} {{GNF_GO|id=GO:0016481 |text = negative regulation of transcription}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 7376
| Hs_Ensembl = ENSG00000131408
| Hs_RefseqProtein = NP_009052
| Hs_RefseqmRNA = NM_007121
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 19
| Hs_GenLoc_start = 55571515
| Hs_GenLoc_end = 55578030
| Hs_Uniprot = P55055
| Mm_EntrezGene = 22260
| Mm_Ensembl = ENSMUSG00000060601
| Mm_RefseqmRNA = XM_001002072
| Mm_RefseqProtein = XP_001002072
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 7
| Mm_GenLoc_start = 44417659
| Mm_GenLoc_end = 44421965
| Mm_Uniprot = Q8BP65
}}
}}
'''Nuclear receptor subfamily 1, group H, member 2''', also known as '''NR1H2''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: NR1H2 nuclear receptor subfamily 1, group H, member 2| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=7376| accessdate = }}</ref>
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text = The LX receptors (LXRs) were originally identified as orphan members of the nuclear receptor superfamily because their ligands were unknown. Like other receptors in the family, LXRs heterodimerize with retinoid X receptor (see MIM 180245) and bind to specific response elements (LXREs) characterized by direct repeats separated by 4 nucleotides. Two genes, alpha (LXRA, MIM 602423) and beta, are known to encode LXR proteins (Song et al., 1995).[supplied by OMIM]<ref name="entrez">{{cite web | title = Entrez Gene: NR1H2 nuclear receptor subfamily 1, group H, member 2| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=7376| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Song C, Hiipakka RA, Kokontis JM, Liao S |title=Ubiquitous receptor: structures, immunocytochemical localization, and modulation of gene activation by receptors for retinoic acids and thyroid hormones. |journal=Ann. N. Y. Acad. Sci. |volume=761 |issue= |pages= 38-49 |year= 1995 |pmid= 7625741 |doi= }}
*{{cite journal | author=Seol W, Choi HS, Moore DD |title=Isolation of proteins that interact specifically with the retinoid X receptor: two novel orphan receptors. |journal=Mol. Endocrinol. |volume=9 |issue= 1 |pages= 72-85 |year= 1995 |pmid= 7760852 |doi= }}
*{{cite journal | author=Le Beau MM, Song C, Davis EM, ''et al.'' |title=Assignment of the human ubiquitous receptor gene (UNR) to 19q13.3 using fluorescence in situ hybridization. |journal=Genomics |volume=26 |issue= 1 |pages= 166-8 |year= 1995 |pmid= 7782080 |doi= }}
*{{cite journal | author=Shinar DM, Endo N, Rutledge SJ, ''et al.'' |title=NER, a new member of the gene family encoding the human steroid hormone nuclear receptor. |journal=Gene |volume=147 |issue= 2 |pages= 273-6 |year= 1994 |pmid= 7926814 |doi= }}
*{{cite journal | author=Song C, Kokontis JM, Hiipakka RA, Liao S |title=Ubiquitous receptor: a receptor that modulates gene activation by retinoic acid and thyroid hormone receptors. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=91 |issue= 23 |pages= 10809-13 |year= 1994 |pmid= 7971966 |doi= }}
*{{cite journal | author=Janowski BA, Grogan MJ, Jones SA, ''et al.'' |title=Structural requirements of ligands for the oxysterol liver X receptors LXRalpha and LXRbeta. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=96 |issue= 1 |pages= 266-71 |year= 1999 |pmid= 9874807 |doi= }}
*{{cite journal | author=Feltkamp D, Wiebel FF, Alberti S, Gustafsson JA |title=Identification of a novel DNA binding site for nuclear orphan receptor OR1. |journal=J. Biol. Chem. |volume=274 |issue= 15 |pages= 10421-9 |year= 1999 |pmid= 10187832 |doi= }}
*{{cite journal | author=Lee SK, Jung SY, Kim YS, ''et al.'' |title=Two distinct nuclear receptor-interaction domains and CREB-binding protein-dependent transactivation function of activating signal cointegrator-2. |journal=Mol. Endocrinol. |volume=15 |issue= 2 |pages= 241-54 |year= 2001 |pmid= 11158331 |doi= }}
*{{cite journal | author=Whitney KD, Watson MA, Goodwin B, ''et al.'' |title=Liver X receptor (LXR) regulation of the LXRalpha gene in human macrophages. |journal=J. Biol. Chem. |volume=276 |issue= 47 |pages= 43509-15 |year= 2001 |pmid= 11546778 |doi= 10.1074/jbc.M106155200 }}
*{{cite journal | author=Whitney KD, Watson MA, Collins JL, ''et al.'' |title=Regulation of cholesterol homeostasis by the liver X receptors in the central nervous system. |journal=Mol. Endocrinol. |volume=16 |issue= 6 |pages= 1378-85 |year= 2003 |pmid= 12040022 |doi= }}
*{{cite journal | author=Brendel C, Schoonjans K, Botrugno OA, ''et al.'' |title=The small heterodimer partner interacts with the liver X receptor alpha and represses its transcriptional activity. |journal=Mol. Endocrinol. |volume=16 |issue= 9 |pages= 2065-76 |year= 2003 |pmid= 12198243 |doi= }}
*{{cite journal | author=Mo J, Fang SJ, Chen W, Blobe GC |title=Regulation of ALK-1 signaling by the nuclear receptor LXRbeta. |journal=J. Biol. Chem. |volume=277 |issue= 52 |pages= 50788-94 |year= 2003 |pmid= 12393874 |doi= 10.1074/jbc.M210376200 }}
*{{cite journal | author=Strausberg RL, Feingold EA, Grouse LH, ''et al.'' |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899-903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899 }}
*{{cite journal | author=Williams S, Bledsoe RK, Collins JL, ''et al.'' |title=X-ray crystal structure of the liver X receptor beta ligand binding domain: regulation by a histidine-tryptophan switch. |journal=J. Biol. Chem. |volume=278 |issue= 29 |pages= 27138-43 |year= 2003 |pmid= 12736258 |doi= 10.1074/jbc.M302260200 }}
*{{cite journal | author=Färnegårdh M, Bonn T, Sun S, ''et al.'' |title=The three-dimensional structure of the liver X receptor beta reveals a flexible ligand-binding pocket that can accommodate fundamentally different ligands. |journal=J. Biol. Chem. |volume=278 |issue= 40 |pages= 38821-8 |year= 2003 |pmid= 12819202 |doi= 10.1074/jbc.M304842200 }}
*{{cite journal | author=Fukuchi J, Song C, Ko AL, Liao S |title=Transcriptional regulation of farnesyl pyrophosphate synthase by liver X receptors. |journal=Steroids |volume=68 |issue= 7-8 |pages= 685-91 |year= 2004 |pmid= 12957674 |doi= }}
*{{cite journal | author=Hoerer S, Schmid A, Heckel A, ''et al.'' |title=Crystal structure of the human liver X receptor beta ligand-binding domain in complex with a synthetic agonist. |journal=J. Mol. Biol. |volume=334 |issue= 5 |pages= 853-61 |year= 2004 |pmid= 14643652 |doi= }}
*{{cite journal | author=Walczak R, Joseph SB, Laffitte BA, ''et al.'' |title=Transcription of the vascular endothelial growth factor gene in macrophages is regulated by liver X receptors. |journal=J. Biol. Chem. |volume=279 |issue= 11 |pages= 9905-11 |year= 2004 |pmid= 14699103 |doi= 10.1074/jbc.M310587200 }}
*{{cite journal | author=Ota T, Suzuki Y, Nishikawa T, ''et al.'' |title=Complete sequencing and characterization of 21,243 full-length human cDNAs. |journal=Nat. Genet. |volume=36 |issue= 1 |pages= 40-5 |year= 2004 |pmid= 14702039 |doi= 10.1038/ng1285 }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on NRIP1... {November 18, 2007 9:24:46 PM PST}
- SEARCH REDIRECT: Control Box Found: NRIP1 {November 18, 2007 9:25:04 PM PST}
- UPDATE PROTEIN BOX: Updating Protein Box, No errors. {November 18, 2007 9:25:06 PM PST}
- UPDATE SUMMARY: Updating Summary, No Errors. {November 18, 2007 9:25:06 PM PST}
- UPDATE CITATIONS: Updating Citations, No Errors. {November 18, 2007 9:25:06 PM PST}
- UPDATED: Updated protein page: NRIP1 {November 18, 2007 9:25:12 PM PST}
- INFO: Beginning work on NUP214... {November 18, 2007 9:22:57 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 18, 2007 9:23:46 PM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}
<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image = PBB_Protein_NUP214_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 2oit.
| PDB = {{PDB2|2oit}}
| Name = Nucleoporin 214kDa
| HGNCid = 8064
| Symbol = NUP214
| AltSymbols =; CAIN; CAN; D9S46E; MGC104525; N214
| OMIM = 114350
| ECnumber =
| Homologene = 38008
| MGIid = 1095411
| GeneAtlas_image1 = PBB_GE_NUP214_202155_s_at_tn.png
| GeneAtlas_image2 = PBB_GE_NUP214_211261_at_tn.png
| Function = {{GNF_GO|id=GO:0003674 |text = molecular_function}} {{GNF_GO|id=GO:0005215 |text = transporter activity}} {{GNF_GO|id=GO:0005515 |text = protein binding}} {{GNF_GO|id=GO:0015288 |text = porin activity}}
| Component = {{GNF_GO|id=GO:0005634 |text = nucleus}} {{GNF_GO|id=GO:0005643 |text = nuclear pore}} {{GNF_GO|id=GO:0016021 |text = integral to membrane}} {{GNF_GO|id=GO:0019867 |text = outer membrane}}
| Process = {{GNF_GO|id=GO:0006611 |text = protein export from nucleus}} {{GNF_GO|id=GO:0006810 |text = transport}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 8021
| Hs_Ensembl = ENSG00000126883
| Hs_RefseqProtein = NP_005076
| Hs_RefseqmRNA = NM_005085
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 9
| Hs_GenLoc_start = 132990797
| Hs_GenLoc_end = 133099878
| Hs_Uniprot = P35658
| Mm_EntrezGene = 227720
| Mm_Ensembl = ENSMUSG00000001855
| Mm_RefseqmRNA = XM_358340
| Mm_RefseqProtein = XP_358340
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 2
| Mm_GenLoc_start = 31796490
| Mm_GenLoc_end = 31874378
| Mm_Uniprot =
}}
}}
'''Nucleoporin 214kDa''', also known as '''NUP214''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: NUP214 nucleoporin 214kDa| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=8021| accessdate = }}</ref>
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text = The nuclear pore complex is a massive structure that extends across the nuclear envelope, forming a gateway that regulates the flow of macromolecules between the nucleus and the cytoplasm. Nucleoporins are the main components of the nuclear pore complex in eukaryotic cells. This gene is a member of the FG-repeat-containing nucleoporins. The protein encoded by this gene is localized to the cytoplasmic face of the nuclear pore complex where it is required for proper cell cycle progression and nucleocytoplasmic transport. The 3' portion of this gene forms a fusion gene with the DEK gene on chromosome 6 in a t(6,9) translocation associated with acute myeloid leukemia and myelodysplastic syndrome.<ref name="entrez">{{cite web | title = Entrez Gene: NUP214 nucleoporin 214kDa| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=8021| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Stoffler D, Fahrenkrog B, Aebi U |title=The nuclear pore complex: from molecular architecture to functional dynamics. |journal=Curr. Opin. Cell Biol. |volume=11 |issue= 3 |pages= 391-401 |year= 1999 |pmid= 10395558 |doi= 10.1016/S0955-0674(99)80055-6 }}
*{{cite journal | author=von Lindern M, Fornerod M, van Baal S, ''et al.'' |title=The translocation (6;9), associated with a specific subtype of acute myeloid leukemia, results in the fusion of two genes, dek and can, and the expression of a chimeric, leukemia-specific dek-can mRNA. |journal=Mol. Cell. Biol. |volume=12 |issue= 4 |pages= 1687-97 |year= 1992 |pmid= 1549122 |doi= }}
*{{cite journal | author=von Lindern M, Poustka A, Lerach H, Grosveld G |title=The (6;9) chromosome translocation, associated with a specific subtype of acute nonlymphocytic leukemia, leads to aberrant transcription of a target gene on 9q34. |journal=Mol. Cell. Biol. |volume=10 |issue= 8 |pages= 4016-26 |year= 1990 |pmid= 2370860 |doi= }}
*{{cite journal | author=Nomura N, Miyajima N, Sazuka T, ''et al.'' |title=Prediction of the coding sequences of unidentified human genes. I. The coding sequences of 40 new genes (KIAA0001-KIAA0040) deduced by analysis of randomly sampled cDNA clones from human immature myeloid cell line KG-1. |journal=DNA Res. |volume=1 |issue= 1 |pages= 27-35 |year= 1995 |pmid= 7584026 |doi= }}
*{{cite journal | author=Nomura N, Miyajima N, Sazuka T, ''et al.'' |title=Prediction of the coding sequences of unidentified human genes. I. The coding sequences of 40 new genes (KIAA0001-KIAA0040) deduced by analysis of randomly sampled cDNA clones from human immature myeloid cell line KG-1 (supplement). |journal=DNA Res. |volume=1 |issue= 1 |pages= 47-56 |year= 1995 |pmid= 7584028 |doi= }}
*{{cite journal | author=Pilz A, Woodward K, Povey S, Abbott C |title=Comparative mapping of 50 human chromosome 9 loci in the laboratory mouse. |journal=Genomics |volume=25 |issue= 1 |pages= 139-49 |year= 1995 |pmid= 7774911 |doi= }}
*{{cite journal | author=Kraemer D, Wozniak RW, Blobel G, Radu A |title=The human CAN protein, a putative oncogene product associated with myeloid leukemogenesis, is a nuclear pore complex protein that faces the cytoplasm. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=91 |issue= 4 |pages= 1519-23 |year= 1994 |pmid= 8108440 |doi= }}
*{{cite journal | author=Stutz F, Izaurralde E, Mattaj IW, Rosbash M |title=A role for nucleoporin FG repeat domains in export of human immunodeficiency virus type 1 Rev protein and RNA from the nucleus. |journal=Mol. Cell. Biol. |volume=16 |issue= 12 |pages= 7144-50 |year= 1997 |pmid= 8943370 |doi= }}
*{{cite journal | author=Fornerod M, van Deursen J, van Baal S, ''et al.'' |title=The human homologue of yeast CRM1 is in a dynamic subcomplex with CAN/Nup214 and a novel nuclear pore component Nup88. |journal=EMBO J. |volume=16 |issue= 4 |pages= 807-16 |year= 1997 |pmid= 9049309 |doi= 10.1093/emboj/16.4.807 }}
*{{cite journal | author=Yaseen NR, Blobel G |title=Cloning and characterization of human karyopherin beta3. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=94 |issue= 9 |pages= 4451-6 |year= 1997 |pmid= 9114010 |doi= }}
*{{cite journal | author=Bonifaci N, Moroianu J, Radu A, Blobel G |title=Karyopherin beta2 mediates nuclear import of a mRNA binding protein. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=94 |issue= 10 |pages= 5055-60 |year= 1997 |pmid= 9144189 |doi= }}
*{{cite journal | author=Bastos R, Ribas de Pouplana L, Enarson M, ''et al.'' |title=Nup84, a novel nucleoporin that is associated with CAN/Nup214 on the cytoplasmic face of the nuclear pore complex. |journal=J. Cell Biol. |volume=137 |issue= 5 |pages= 989-1000 |year= 1997 |pmid= 9166401 |doi= }}
*{{cite journal | author=Boer J, Bonten-Surtel J, Grosveld G |title=Overexpression of the nucleoporin CAN/NUP214 induces growth arrest, nucleocytoplasmic transport defects, and apoptosis. |journal=Mol. Cell. Biol. |volume=18 |issue= 3 |pages= 1236-47 |year= 1998 |pmid= 9488438 |doi= }}
*{{cite journal | author=Bogerd HP, Echarri A, Ross TM, Cullen BR |title=Inhibition of human immunodeficiency virus Rev and human T-cell leukemia virus Rex function, but not Mason-Pfizer monkey virus constitutive transport element activity, by a mutant human nucleoporin targeted to Crm1. |journal=J. Virol. |volume=72 |issue= 11 |pages= 8627-35 |year= 1998 |pmid= 9765402 |doi= }}
*{{cite journal | author=Zolotukhin AS, Felber BK |title=Nucleoporins nup98 and nup214 participate in nuclear export of human immunodeficiency virus type 1 Rev. |journal=J. Virol. |volume=73 |issue= 1 |pages= 120-7 |year= 1999 |pmid= 9847314 |doi= }}
*{{cite journal | author=Schmitt C, von Kobbe C, Bachi A, ''et al.'' |title=Dbp5, a DEAD-box protein required for mRNA export, is recruited to the cytoplasmic fibrils of nuclear pore complex via a conserved interaction with CAN/Nup159p. |journal=EMBO J. |volume=18 |issue= 15 |pages= 4332-47 |year= 1999 |pmid= 10428971 |doi= 10.1093/emboj/18.15.4332 }}
*{{cite journal | author=Bachi A, Braun IC, Rodrigues JP, ''et al.'' |title=The C-terminal domain of TAP interacts with the nuclear pore complex and promotes export of specific CTE-bearing RNA substrates. |journal=RNA |volume=6 |issue= 1 |pages= 136-58 |year= 2000 |pmid= 10668806 |doi= }}
*{{cite journal | author=Herold A, Suyama M, Rodrigues JP, ''et al.'' |title=TAP (NXF1) belongs to a multigene family of putative RNA export factors with a conserved modular architecture. |journal=Mol. Cell. Biol. |volume=20 |issue= 23 |pages= 8996-9008 |year= 2000 |pmid= 11073998 |doi= }}
*{{cite journal | author=Hofmann W, Reichart B, Ewald A, ''et al.'' |title=Cofactor requirements for nuclear export of Rev response element (RRE)- and constitutive transport element (CTE)-containing retroviral RNAs. An unexpected role for actin. |journal=J. Cell Biol. |volume=152 |issue= 5 |pages= 895-910 |year= 2001 |pmid= 11238447 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on PDE5A... {November 18, 2007 9:26:11 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 18, 2007 9:26:57 PM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
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<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image = PBB_Protein_PDE5A_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1rkp.
| PDB = {{PDB2|1rkp}}, {{PDB2|1t9r}}, {{PDB2|1t9s}}, {{PDB2|1tbf}}, {{PDB2|1udt}}, {{PDB2|1udu}}, {{PDB2|1uho}}, {{PDB2|1xoz}}, {{PDB2|1xp0}}, {{PDB2|2chm}}, {{PDB2|2h40}}, {{PDB2|2h42}}, {{PDB2|2h44}}
| Name = Phosphodiesterase 5A, cGMP-specific
| HGNCid = 8784
| Symbol = PDE5A
| AltSymbols =; CGB-PDE; CN5A; PDE5; PDE5A1
| OMIM = 603310
| ECnumber =
| Homologene = 842
| MGIid = 2651499
| GeneAtlas_image1 = PBB_GE_PDE5A_206757_at_tn.png
| Function = {{GNF_GO|id=GO:0000166 |text = nucleotide binding}} {{GNF_GO|id=GO:0000287 |text = magnesium ion binding}} {{GNF_GO|id=GO:0003824 |text = catalytic activity}} {{GNF_GO|id=GO:0004114 |text = 3',5'-cyclic-nucleotide phosphodiesterase activity}} {{GNF_GO|id=GO:0008270 |text = zinc ion binding}} {{GNF_GO|id=GO:0016787 |text = hydrolase activity}} {{GNF_GO|id=GO:0030553 |text = cGMP binding}} {{GNF_GO|id=GO:0047555 |text = 3',5'-cyclic-GMP phosphodiesterase activity}}
| Component = {{GNF_GO|id=GO:0005575 |text = cellular_component}}
| Process = {{GNF_GO|id=GO:0007165 |text = signal transduction}} {{GNF_GO|id=GO:0008150 |text = biological_process}} {{GNF_GO|id=GO:0009187 |text = cyclic nucleotide metabolic process}} {{GNF_GO|id=GO:0046069 |text = cGMP catabolic process}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 8654
| Hs_Ensembl = ENSG00000138735
| Hs_RefseqProtein = NP_001074
| Hs_RefseqmRNA = NM_001083
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 4
| Hs_GenLoc_start = 120635000
| Hs_GenLoc_end = 120769429
| Hs_Uniprot = O76074
| Mm_EntrezGene = 242202
| Mm_Ensembl = ENSMUSG00000053965
| Mm_RefseqmRNA = XM_001001000
| Mm_RefseqProtein = XP_001001000
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 3
| Mm_GenLoc_start = 122721180
| Mm_GenLoc_end = 122848174
| Mm_Uniprot = Q0VBW0
}}
}}
'''Phosphodiesterase 5A, cGMP-specific''', also known as '''PDE5A''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: PDE5A phosphodiesterase 5A, cGMP-specific| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=8654| accessdate = }}</ref>
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text = This gene encodes a cGMP-binding, cGMP-specific phosphodiesterase, a member of the cyclic nucleotide phosphodiesterase family. This phosphodiesterase specifically hydrolyzes cGMP to 5'-GMP. It is involved in the regulation of intracellular concentrations of cyclic nucleotides and is important for smooth muscle relaxation in the cardiovascular system. Alternative splicing of this gene results in three transcript variants encoding distinct isoforms.<ref name="entrez">{{cite web | title = Entrez Gene: PDE5A phosphodiesterase 5A, cGMP-specific| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=8654| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Lin CS, Lin G, Xin ZC, Lue TF |title=Expression, distribution and regulation of phosphodiesterase 5. |journal=Curr. Pharm. Des. |volume=12 |issue= 27 |pages= 3439-57 |year= 2006 |pmid= 17017938 |doi= }}
*{{cite journal | author=Thomas MK, Francis SH, Corbin JD |title=Substrate- and kinase-directed regulation of phosphorylation of a cGMP-binding phosphodiesterase by cGMP. |journal=J. Biol. Chem. |volume=265 |issue= 25 |pages= 14971-8 |year= 1990 |pmid= 2168396 |doi= }}
*{{cite journal | author=Bonaldo MF, Lennon G, Soares MB |title=Normalization and subtraction: two approaches to facilitate gene discovery. |journal=Genome Res. |volume=6 |issue= 9 |pages= 791-806 |year= 1997 |pmid= 8889548 |doi= }}
*{{cite journal | author=Ito M, Nishikawa M, Fujioka M, ''et al.'' |title=Characterization of the isoenzymes of cyclic nucleotide phosphodiesterase in human platelets and the effects of E4021. |journal=Cell. Signal. |volume=8 |issue= 8 |pages= 575-81 |year= 1997 |pmid= 9115850 |doi= }}
*{{cite journal | author=Stacey P, Rulten S, Dapling A, Phillips SC |title=Molecular cloning and expression of human cGMP-binding cGMP-specific phosphodiesterase (PDE5). |journal=Biochem. Biophys. Res. Commun. |volume=247 |issue= 2 |pages= 249-54 |year= 1998 |pmid= 9642111 |doi= 10.1006/bbrc.1998.8769 }}
*{{cite journal | author=Loughney K, Hill TR, Florio VA, ''et al.'' |title=Isolation and characterization of cDNAs encoding PDE5A, a human cGMP-binding, cGMP-specific 3',5'-cyclic nucleotide phosphodiesterase. |journal=Gene |volume=216 |issue= 1 |pages= 139-47 |year= 1998 |pmid= 9714779 |doi= }}
*{{cite journal | author=Yanaka N, Kotera J, Ohtsuka A, ''et al.'' |title=Expression, structure and chromosomal localization of the human cGMP-binding cGMP-specific phosphodiesterase PDE5A gene. |journal=Eur. J. Biochem. |volume=255 |issue= 2 |pages= 391-9 |year= 1998 |pmid= 9716380 |doi= }}
*{{cite journal | author=Zhou L, Thompson WJ, Potter DE |title=Multiple cyclic nucleotide phosphodiesterases in human trabecular meshwork cells. |journal=Invest. Ophthalmol. Vis. Sci. |volume=40 |issue= 8 |pages= 1745-52 |year= 1999 |pmid= 10393044 |doi= }}
*{{cite journal | author=Kotera J, Fujishige K, Imai Y, ''et al.'' |title=Genomic origin and transcriptional regulation of two variants of cGMP-binding cGMP-specific phosphodiesterases. |journal=Eur. J. Biochem. |volume=262 |issue= 3 |pages= 866-73 |year= 1999 |pmid= 10411650 |doi= }}
*{{cite journal | author=Lin CS, Lau A, Tu R, Lue TF |title=Identification of three alternative first exons and an intronic promoter of human PDE5A gene. |journal=Biochem. Biophys. Res. Commun. |volume=268 |issue= 2 |pages= 596-602 |year= 2000 |pmid= 10679249 |doi= 10.1006/bbrc.2000.2186 }}
*{{cite journal | author=Lin CS, Lau A, Tu R, Lue TF |title=Expression of three isoforms of cGMP-binding cGMP-specific phosphodiesterase (PDE5) in human penile cavernosum. |journal=Biochem. Biophys. Res. Commun. |volume=268 |issue= 2 |pages= 628-35 |year= 2000 |pmid= 10679255 |doi= 10.1006/bbrc.2000.2187 }}
*{{cite journal | author=Küthe A, Mägert H, Uckert S, ''et al.'' |title=Gene expression of the phosphodiesterases 3A and 5A in human corpus cavernosum penis. |journal=Eur. Urol. |volume=38 |issue= 1 |pages= 108-14 |year= 2000 |pmid= 10859452 |doi= }}
*{{cite journal | author=Hartley JL, Temple GF, Brasch MA |title=DNA cloning using in vitro site-specific recombination. |journal=Genome Res. |volume=10 |issue= 11 |pages= 1788-95 |year= 2001 |pmid= 11076863 |doi= }}
*{{cite journal | author=Lin CS, Chow S, Lau A, ''et al.'' |title=Identification and regulation of human PDE5A gene promoter. |journal=Biochem. Biophys. Res. Commun. |volume=280 |issue= 3 |pages= 684-92 |year= 2001 |pmid= 11162575 |doi= 10.1006/bbrc.2000.4220 }}
*{{cite journal | author=Wiemann S, Weil B, Wellenreuther R, ''et al.'' |title=Toward a catalog of human genes and proteins: sequencing and analysis of 500 novel complete protein coding human cDNAs. |journal=Genome Res. |volume=11 |issue= 3 |pages= 422-35 |year= 2001 |pmid= 11230166 |doi= 10.1101/gr.154701 }}
*{{cite journal | author=Piazza GA, Thompson WJ, Pamukcu R, ''et al.'' |title=Exisulind, a novel proapoptotic drug, inhibits rat urinary bladder tumorigenesis. |journal=Cancer Res. |volume=61 |issue= 10 |pages= 3961-8 |year= 2001 |pmid= 11358813 |doi= }}
*{{cite journal | author=Frame M, Wan KF, Tate R, ''et al.'' |title=The gamma subunit of the rod photoreceptor cGMP phosphodiesterase can modulate the proteolysis of two cGMP binding cGMP-specific phosphodiesterases (PDE6 and PDE5) by caspase-3. |journal=Cell. Signal. |volume=13 |issue= 10 |pages= 735-41 |year= 2001 |pmid= 11602184 |doi= }}
*{{cite journal | author=Lin CS, Chow S, Lau A, ''et al.'' |title=Human PDE5A gene encodes three PDE5 isoforms from two alternate promoters. |journal=Int. J. Impot. Res. |volume=14 |issue= 1 |pages= 15-24 |year= 2002 |pmid= 11896473 |doi= 10.1038/sj.ijir.3900802 }}
*{{cite journal | author=Francis SH, Bessay EP, Kotera J, ''et al.'' |title=Phosphorylation of isolated human phosphodiesterase-5 regulatory domain induces an apparent conformational change and increases cGMP binding affinity. |journal=J. Biol. Chem. |volume=277 |issue= 49 |pages= 47581-7 |year= 2003 |pmid= 12359732 |doi= 10.1074/jbc.M206088200 }}
*{{cite journal | author=Strausberg RL, Feingold EA, Grouse LH, ''et al.'' |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899-903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899 }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on PICK1... {November 18, 2007 9:27:57 PM PST}
- SEARCH REDIRECT: Control Box Found: PICK1 {November 18, 2007 9:28:23 PM PST}
- UPDATE PROTEIN BOX: Updating Protein Box, No errors. {November 18, 2007 9:28:24 PM PST}
- UPDATE SUMMARY: Updating Summary, No Errors. {November 18, 2007 9:28:24 PM PST}
- UPDATE CITATIONS: Updating Citations, No Errors. {November 18, 2007 9:28:24 PM PST}
- UPDATED: Updated protein page: PICK1 {November 18, 2007 9:28:32 PM PST}
- INFO: Beginning work on RAD23A... {November 18, 2007 9:15:58 PM PST}
- SEARCH REDIRECT: Control Box Found: RAD23A {November 18, 2007 9:16:37 PM PST}
- UPDATE PROTEIN BOX: Updating Protein Box, No errors. {November 18, 2007 9:16:39 PM PST}
- UPDATE SUMMARY: Updating Summary, No Errors. {November 18, 2007 9:16:39 PM PST}
- UPDATE CITATIONS: Updating Citations, No Errors. {November 18, 2007 9:16:39 PM PST}
- UPDATED: Updated protein page: RAD23A {November 18, 2007 9:16:45 PM PST}
- INFO: Beginning work on RBM8A... {November 18, 2007 9:28:32 PM PST}
- SEARCH REDIRECT: Control Box Found: RBM8A {November 18, 2007 9:29:22 PM PST}
- UPDATE PROTEIN BOX: Updating Protein Box, No errors. {November 18, 2007 9:29:23 PM PST}
- UPDATE SUMMARY: Updating Summary, No Errors. {November 18, 2007 9:29:23 PM PST}
- UPDATE CITATIONS: Updating Citations, No Errors. {November 18, 2007 9:29:23 PM PST}
- UPDATED: Updated protein page: RBM8A {November 18, 2007 9:29:29 PM PST}
- INFO: Beginning work on RHEB... {November 18, 2007 9:16:45 PM PST}
- SEARCH REDIRECT: Control Box Found: RHEB {November 18, 2007 9:17:28 PM PST}
- UPDATE PROTEIN BOX: Updating Protein Box, No errors. {November 18, 2007 9:17:30 PM PST}
- UPDATE SUMMARY: Updating Summary, No Errors. {November 18, 2007 9:17:30 PM PST}
- UPDATE CITATIONS: Updating Citations, No Errors. {November 18, 2007 9:17:30 PM PST}
- UPDATED: Updated protein page: RHEB {November 18, 2007 9:17:36 PM PST}
- INFO: Beginning work on SAT1... {November 18, 2007 9:17:36 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 18, 2007 9:18:13 PM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
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| update_summary = yes
| update_citations = yes
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<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image = PBB_Protein_SAT1_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 2b3u.
| PDB = {{PDB2|2b3u}}, {{PDB2|2b3v}}, {{PDB2|2b4b}}, {{PDB2|2b4d}}, {{PDB2|2b58}}, {{PDB2|2b5g}}, {{PDB2|2f5i}}, {{PDB2|2fxf}}, {{PDB2|2g3t}}, {{PDB2|2jev}}
| Name = Spermidine/spermine N1-acetyltransferase 1
| HGNCid = 10540
| Symbol = SAT1
| AltSymbols =; DC21; KFSD; SAT; SSAT; SSAT-1
| OMIM = 313020
| ECnumber =
| Homologene = 37716
| MGIid = 98233
| GeneAtlas_image1 = PBB_GE_SAT1_203455_s_at_tn.png
| GeneAtlas_image2 = PBB_GE_SAT1_210592_s_at_tn.png
| GeneAtlas_image3 = PBB_GE_SAT1_213988_s_at_tn.png
| Function = {{GNF_GO|id=GO:0004145 |text = diamine N-acetyltransferase activity}} {{GNF_GO|id=GO:0008080 |text = N-acetyltransferase activity}} {{GNF_GO|id=GO:0008415 |text = acyltransferase activity}} {{GNF_GO|id=GO:0016740 |text = transferase activity}}
| Component = {{GNF_GO|id=GO:0005622 |text = intracellular}}
| Process =
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 6303
| Hs_Ensembl = ENSG00000130066
| Hs_RefseqProtein = NP_002961
| Hs_RefseqmRNA = NM_002970
| Hs_GenLoc_db =
| Hs_GenLoc_chr = X
| Hs_GenLoc_start = 23711211
| Hs_GenLoc_end = 23714264
| Hs_Uniprot = P21673
| Mm_EntrezGene = 20229
| Mm_Ensembl =
| Mm_RefseqmRNA = NM_009121
| Mm_RefseqProtein = NP_033147
| Mm_GenLoc_db =
| Mm_GenLoc_chr =
| Mm_GenLoc_start =
| Mm_GenLoc_end =
| Mm_Uniprot =
}}
}}
'''Spermidine/spermine N1-acetyltransferase 1''', also known as '''SAT1''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: SAT1 spermidine/spermine N1-acetyltransferase 1| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=6303| accessdate = }}</ref>
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text = Spermidine/spermine N(1)-acetyltransferase (SPD/SPM acetyltransferase) is a rate-limiting enzyme in the catabolic pathway of polyamine metabolism. It catalyzes the N(1)-acetylation of spermidine and spermine and, by the successive activity of polyamine oxidase, spermine can be converted to spermidine and spermidine to putrescine.[supplied by OMIM]<ref name="entrez">{{cite web | title = Entrez Gene: SAT1 spermidine/spermine N1-acetyltransferase 1| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=6303| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Lake JA, Carr J, Feng F, ''et al.'' |title=The role of Vif during HIV-1 infection: interaction with novel host cellular factors. |journal=J. Clin. Virol. |volume=26 |issue= 2 |pages= 143-52 |year= 2003 |pmid= 12600646 |doi= }}
*{{cite journal | author=Xiao L, Celano P, Mank AR, ''et al.'' |title=Structure of the human spermidine/spermine N1-acetyltransferase gene (exon/intron gene organization and localization to Xp22.1). |journal=Biochem. Biophys. Res. Commun. |volume=187 |issue= 3 |pages= 1493-502 |year= 1992 |pmid= 1417826 |doi= }}
*{{cite journal | author=Xiao L, Celano P, Mank AR, ''et al.'' |title=Characterization of a full-length cDNA which codes for the human spermidine/spermine N1-acetyltransferase. |journal=Biochem. Biophys. Res. Commun. |volume=179 |issue= 1 |pages= 407-15 |year= 1991 |pmid= 1652956 |doi= }}
*{{cite journal | author=Casero RA, Celano P, Ervin SJ, ''et al.'' |title=Isolation and characterization of a cDNA clone that codes for human spermidine/spermine N1-acetyltransferase. |journal=J. Biol. Chem. |volume=266 |issue= 2 |pages= 810-4 |year= 1991 |pmid= 1985966 |doi= }}
*{{cite journal | author=Libby PR, Ganis B, Bergeron RJ, Porter CW |title=Characterization of human spermidine/spermine N1-acetyltransferase purified from cultured melanoma cells. |journal=Arch. Biochem. Biophys. |volume=284 |issue= 2 |pages= 238-44 |year= 1991 |pmid= 1989509 |doi= }}
*{{cite journal | author=Casero RA, Celano P, Ervin SJ, ''et al.'' |title=High specific induction of spermidine/spermine N1-acetyltransferase in a human large cell lung carcinoma. |journal=Biochem. J. |volume=270 |issue= 3 |pages= 615-20 |year= 1990 |pmid= 2241897 |doi= }}
*{{cite journal | author=Casero RA, Gabrielson EW, Pegg AE |title=Immunohistochemical staining of human spermidine/spermine N1-acetyltransferase superinduced in response to treatment with antitumor polyamine analogues. |journal=Cancer Res. |volume=54 |issue= 15 |pages= 3955-8 |year= 1994 |pmid= 8033120 |doi= }}
*{{cite journal | author=Xiao L, Casero RA |title=Differential transcription of the human spermidine/spermine N1-acetyltransferase (SSAT) gene in human lung carcinoma cells. |journal=Biochem. J. |volume=313 ( Pt 2) |issue= |pages= 691-6 |year= 1996 |pmid= 8573111 |doi= }}
*{{cite journal | author=Coleman CS, Huang H, Pegg AE |title=Structure and critical residues at the active site of spermidine/spermine-N1-acetyltransferase. |journal=Biochem. J. |volume=316 ( Pt 3) |issue= |pages= 697-701 |year= 1996 |pmid= 8670140 |doi= }}
*{{cite journal | author=Bordin L, Vargiu C, Colombatto S, ''et al.'' |title=Casein kinase 2 phosphorylates recombinant human spermidine/spermine N1-acetyltransferase on both serine and threonine residues. |journal=Biochem. Biophys. Res. Commun. |volume=229 |issue= 3 |pages= 845-51 |year= 1997 |pmid= 8954982 |doi= 10.1006/bbrc.1996.1890 }}
*{{cite journal | author=Bettuzzi S, Davalli P, Astancolle S, ''et al.'' |title=Tumor progression is accompanied by significant changes in the levels of expression of polyamine metabolism regulatory genes and clusterin (sulfated glycoprotein 2) in human prostate cancer specimens. |journal=Cancer Res. |volume=60 |issue= 1 |pages= 28-34 |year= 2000 |pmid= 10646846 |doi= }}
*{{cite journal | author=Simpson JC, Wellenreuther R, Poustka A, ''et al.'' |title=Systematic subcellular localization of novel proteins identified by large-scale cDNA sequencing. |journal=EMBO Rep. |volume=1 |issue= 3 |pages= 287-92 |year= 2001 |pmid= 11256614 |doi= 10.1093/embo-reports/kvd058 }}
*{{cite journal | author=Coleman CS, Pegg AE |title=Polyamine analogues inhibit the ubiquitination of spermidine/spermine N1-acetyltransferase and prevent its targeting to the proteasome for degradation. |journal=Biochem. J. |volume=358 |issue= Pt 1 |pages= 137-45 |year= 2001 |pmid= 11485561 |doi= }}
*{{cite journal | author=Bordin L, Vargiu C, Clari G, ''et al.'' |title=Phosphorylation of recombinant human spermidine/spermine N(1)-acetyltransferase by CK1 and modulation of its binding to mitochondria: a comparison with CK2. |journal=Biochem. Biophys. Res. Commun. |volume=290 |issue= 1 |pages= 463-8 |year= 2002 |pmid= 11779193 |doi= 10.1006/bbrc.2001.6204 }}
*{{cite journal | author=Nikiforova NN, Velikodvorskaja TV, Kachko AV, ''et al.'' |title=Induction of alternatively spliced spermidine/spermine N1-acetyltransferase mRNA in the human kidney cells infected by venezuelan equine encephalitis and tick-borne encephalitis viruses. |journal=Virology |volume=297 |issue= 2 |pages= 163-71 |year= 2002 |pmid= 12083816 |doi= }}
*{{cite journal | author=Gimelli G, Giglio S, Zuffardi O, ''et al.'' |title=Gene dosage of the spermidine/spermine N(1)-acetyltransferase ( SSAT) gene with putrescine accumulation in a patient with a Xp21.1p22.12 duplication and keratosis follicularis spinulosa decalvans (KFSD). |journal=Hum. Genet. |volume=111 |issue= 3 |pages= 235-41 |year= 2002 |pmid= 12215835 |doi= 10.1007/s00439-002-0791-6 }}
*{{cite journal | author=Tomitori H, Nenoi M, Mita K, ''et al.'' |title=Functional characterization of the human spermidine/spermine N(1)-acetyltransferase gene promoter. |journal=Biochim. Biophys. Acta |volume=1579 |issue= 2-3 |pages= 180-4 |year= 2003 |pmid= 12427553 |doi= }}
*{{cite journal | author=Strausberg RL, Feingold EA, Grouse LH, ''et al.'' |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899-903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899 }}
*{{cite journal | author=Izmailova E, Bertley FM, Huang Q, ''et al.'' |title=HIV-1 Tat reprograms immature dendritic cells to express chemoattractants for activated T cells and macrophages. |journal=Nat. Med. |volume=9 |issue= 2 |pages= 191-7 |year= 2003 |pmid= 12539042 |doi= 10.1038/nm822 }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on SLC5A1... {November 18, 2007 9:18:13 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 18, 2007 9:18:49 PM PST}
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{{PBB_Controls
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<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image =
| image_source =
| PDB =
| Name = Solute carrier family 5 (sodium/glucose cotransporter), member 1
| HGNCid = 11036
| Symbol = SLC5A1
| AltSymbols =; D22S675; NAGT; SGLT1
| OMIM = 182380
| ECnumber =
| Homologene = 55456
| MGIid = 107678
| GeneAtlas_image1 = PBB_GE_SLC5A1_206628_at_tn.png
| Function = {{GNF_GO|id=GO:0005215 |text = transporter activity}} {{GNF_GO|id=GO:0005351 |text = sugar:hydrogen ion symporter activity}} {{GNF_GO|id=GO:0005412 |text = glucose:sodium symporter activity}} {{GNF_GO|id=GO:0015293 |text = symporter activity}} {{GNF_GO|id=GO:0031402 |text = sodium ion binding}}
| Component = {{GNF_GO|id=GO:0005887 |text = integral to plasma membrane}} {{GNF_GO|id=GO:0005903 |text = brush border}} {{GNF_GO|id=GO:0016020 |text = membrane}} {{GNF_GO|id=GO:0016324 |text = apical plasma membrane}}
| Process = {{GNF_GO|id=GO:0001656 |text = metanephros development}} {{GNF_GO|id=GO:0006811 |text = ion transport}} {{GNF_GO|id=GO:0006814 |text = sodium ion transport}} {{GNF_GO|id=GO:0015758 |text = glucose transport}} {{GNF_GO|id=GO:0050892 |text = intestinal absorption}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 6523
| Hs_Ensembl = ENSG00000100170
| Hs_RefseqProtein = NP_000334
| Hs_RefseqmRNA = NM_000343
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 22
| Hs_GenLoc_start = 30769259
| Hs_GenLoc_end = 30836645
| Hs_Uniprot = P13866
| Mm_EntrezGene = 20537
| Mm_Ensembl = ENSMUSG00000011034
| Mm_RefseqmRNA = NM_019810
| Mm_RefseqProtein = NP_062784
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 5
| Mm_GenLoc_start = 33421091
| Mm_GenLoc_end = 33479554
| Mm_Uniprot = O70122
}}
}}
'''Solute carrier family 5 (sodium/glucose cotransporter), member 1''', also known as '''SLC5A1''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: SLC5A1 solute carrier family 5 (sodium/glucose cotransporter), member 1| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=6523| accessdate = }}</ref>
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text = Glucose transporters are integral membrane proteins that mediate the transport of glucose and structurally-related substances across cellular membranes. Two families of glucose transporter have been identified: the facilitated-diffusion glucose transporter family (GLUT family), also known as 'uniporters,' and the sodium-dependent glucose transporter family (SGLT family), also known as 'cotransporters' or 'symporters' (Wright et al., 1994). The SLC5A1 gene encodes a protein that is involved in the active transport of glucose and galactose into eukaryotic and some prokaryotic cells.[supplied by OMIM]<ref name="entrez">{{cite web | title = Entrez Gene: SLC5A1 solute carrier family 5 (sodium/glucose cotransporter), member 1| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=6523| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Wright EM, Loo DD, Panayotova-Heiermann M, ''et al.'' |title='Active' sugar transport in eukaryotes. |journal=J. Exp. Biol. |volume=196 |issue= |pages= 197-212 |year= 1995 |pmid= 7823022 |doi= }}
*{{cite journal | author=Wright EM, Turk E, Martin MG |title=Molecular basis for glucose-galactose malabsorption. |journal=Cell Biochem. Biophys. |volume=36 |issue= 2-3 |pages= 115-21 |year= 2003 |pmid= 12139397 |doi= }}
*{{cite journal | author=Anderson NL, Anderson NG |title=The human plasma proteome: history, character, and diagnostic prospects. |journal=Mol. Cell Proteomics |volume=1 |issue= 11 |pages= 845-67 |year= 2003 |pmid= 12488461 |doi= }}
*{{cite journal | author=Turk E, Zabel B, Mundlos S, ''et al.'' |title=Glucose/galactose malabsorption caused by a defect in the Na+/glucose cotransporter. |journal=Nature |volume=350 |issue= 6316 |pages= 354-6 |year= 1991 |pmid= 2008213 |doi= 10.1038/350354a0 }}
*{{cite journal | author=Hediger MA, Turk E, Wright EM |title=Homology of the human intestinal Na+/glucose and Escherichia coli Na+/proline cotransporters. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=86 |issue= 15 |pages= 5748-52 |year= 1989 |pmid= 2490366 |doi= }}
*{{cite journal | author=Delézay O, Baghdiguian S, Fantini J |title=The development of Na(+)-dependent glucose transport during differentiation of an intestinal epithelial cell clone is regulated by protein kinase C. |journal=J. Biol. Chem. |volume=270 |issue= 21 |pages= 12536-41 |year= 1995 |pmid= 7759499 |doi= }}
*{{cite journal | author=Turk E, Martín MG, Wright EM |title=Structure of the human Na+/glucose cotransporter gene SGLT1. |journal=J. Biol. Chem. |volume=269 |issue= 21 |pages= 15204-9 |year= 1994 |pmid= 8195156 |doi= }}
*{{cite journal | author=Turk E, Klisak I, Bacallao R, ''et al.'' |title=Assignment of the human Na+/glucose cotransporter gene SGLT1 to chromosome 22q13.1. |journal=Genomics |volume=17 |issue= 3 |pages= 752-4 |year= 1993 |pmid= 8244393 |doi= 10.1006/geno.1993.1399 }}
*{{cite journal | author=Martín MG, Turk E, Lostao MP, ''et al.'' |title=Defects in Na+/glucose cotransporter (SGLT1) trafficking and function cause glucose-galactose malabsorption. |journal=Nat. Genet. |volume=12 |issue= 2 |pages= 216-20 |year= 1996 |pmid= 8563765 |doi= 10.1038/ng0296-216 }}
*{{cite journal | author=Turk E, Kerner CJ, Lostao MP, Wright EM |title=Membrane topology of the human Na+/glucose cotransporter SGLT1. |journal=J. Biol. Chem. |volume=271 |issue= 4 |pages= 1925-34 |year= 1996 |pmid= 8567640 |doi= }}
*{{cite journal | author=Lam JT, Martín MG, Turk E, ''et al.'' |title=Missense mutations in SGLT1 cause glucose-galactose malabsorption by trafficking defects. |journal=Biochim. Biophys. Acta |volume=1453 |issue= 2 |pages= 297-303 |year= 1999 |pmid= 10036327 |doi= }}
*{{cite journal | author=Dunham I, Shimizu N, Roe BA, ''et al.'' |title=The DNA sequence of human chromosome 22. |journal=Nature |volume=402 |issue= 6761 |pages= 489-95 |year= 1999 |pmid= 10591208 |doi= 10.1038/990031 }}
*{{cite journal | author=Obermeier S, Hüselweh B, Tinel H, ''et al.'' |title=Expression of glucose transporters in lactating human mammary gland epithelial cells. |journal=European journal of nutrition |volume=39 |issue= 5 |pages= 194-200 |year= 2001 |pmid= 11131365 |doi= }}
*{{cite journal | author=Kasahara M, Maeda M, Hayashi S, ''et al.'' |title=A missense mutation in the Na(+)/glucose cotransporter gene SGLT1 in a patient with congenital glucose-galactose malabsorption: normal trafficking but inactivation of the mutant protein. |journal=Biochim. Biophys. Acta |volume=1536 |issue= 2-3 |pages= 141-7 |year= 2001 |pmid= 11406349 |doi= }}
*{{cite journal | author=Roll P, Massacrier A, Pereira S, ''et al.'' |title=New human sodium/glucose cotransporter gene (KST1): identification, characterization, and mutation analysis in ICCA (infantile convulsions and choreoathetosis) and BFIC (benign familial infantile convulsions) families. |journal=Gene |volume=285 |issue= 1-2 |pages= 141-8 |year= 2002 |pmid= 12039040 |doi= }}
*{{cite journal | author=Ikari A, Nakano M, Kawano K, Suketa Y |title=Up-regulation of sodium-dependent glucose transporter by interaction with heat shock protein 70. |journal=J. Biol. Chem. |volume=277 |issue= 36 |pages= 33338-43 |year= 2002 |pmid= 12082088 |doi= 10.1074/jbc.M200310200 }}
*{{cite journal | author=Strausberg RL, Feingold EA, Grouse LH, ''et al.'' |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899-903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899 }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on SNRPN... {November 18, 2007 9:18:49 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 18, 2007 9:19:25 PM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
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}}
<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image = PBB_Protein_SNRPN_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1d3b.
| PDB = {{PDB2|1d3b}}
| Name = Small nuclear ribonucleoprotein polypeptide N
| HGNCid = 11164
| Symbol = SNRPN
| AltSymbols =; SMN; HCERN3; RT-LI; SM-D; SNRNP-N; SNURF-SNRPN
| OMIM = 182279
| ECnumber =
| Homologene = 68297
| MGIid = 98347
| Function = {{GNF_GO|id=GO:0003674 |text = molecular_function}} {{GNF_GO|id=GO:0003723 |text = RNA binding}} {{GNF_GO|id=GO:0042802 |text = identical protein binding}}
| Component = {{GNF_GO|id=GO:0005575 |text = cellular_component}} {{GNF_GO|id=GO:0005634 |text = nucleus}} {{GNF_GO|id=GO:0005681 |text = spliceosome}} {{GNF_GO|id=GO:0030529 |text = ribonucleoprotein complex}} {{GNF_GO|id=GO:0030532 |text = small nuclear ribonucleoprotein complex}}
| Process = {{GNF_GO|id=GO:0008150 |text = biological_process}} {{GNF_GO|id=GO:0008380 |text = RNA splicing}} {{GNF_GO|id=GO:0016071 |text = mRNA metabolic process}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 6638
| Hs_Ensembl =
| Hs_RefseqProtein = NP_003088
| Hs_RefseqmRNA = NM_003097
| Hs_GenLoc_db =
| Hs_GenLoc_chr =
| Hs_GenLoc_start =
| Hs_GenLoc_end =
| Hs_Uniprot =
| Mm_EntrezGene = 20646
| Mm_Ensembl = ENSMUSG00000000948
| Mm_RefseqmRNA = NM_013670
| Mm_RefseqProtein = NP_038698
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 7
| Mm_GenLoc_start = 59862190
| Mm_GenLoc_end = 59866513
| Mm_Uniprot = O70499
}}
}}
'''Small nuclear ribonucleoprotein polypeptide N''', also known as '''SNRPN''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: SNRPN small nuclear ribonucleoprotein polypeptide N| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=6638| accessdate = }}</ref>
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text = The protein encoded by this gene is one polypeptide of a small nuclear ribonucleoprotein complex and belongs to the snRNP SMB/SMN family. The protein plays a role in pre-mRNA processing, possibly tissue-specific alternative splicing events. Although individual snRNPs are believed to recognize specific nucleic acid sequences through RNA-RNA base pairing, the specific role of this family member is unknown. The protein arises from a bicistronic transcript that also encodes a protein identified as the SNRPN upstream reading frame (SNURF). Multiple transcription initiation sites have been identified and extensive alternative splicing occurs in the 5' untranslated region. Additional splice variants have been described but sequences for the complete transcripts have not been determined. The 5' UTR of this gene has been identified as an imprinting center. Alternative splicing or deletion caused by a translocation event in this paternally-expressed region is responsible for Angelman syndrome or Prader-Willi syndrome due to parental imprint switch failure.<ref name="entrez">{{cite web | title = Entrez Gene: SNRPN small nuclear ribonucleoprotein polypeptide N| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=6638| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Ozçelik T, Leff S, Robinson W, ''et al.'' |title=Small nuclear ribonucleoprotein polypeptide N (SNRPN), an expressed gene in the Prader-Willi syndrome critical region. |journal=Nat. Genet. |volume=2 |issue= 4 |pages= 265-9 |year= 1993 |pmid= 1303277 |doi= 10.1038/ng1292-265 }}
*{{cite journal | author=Schmauss C, Brines ML, Lerner MR |title=The gene encoding the small nuclear ribonucleoprotein-associated protein N is expressed at high levels in neurons. |journal=J. Biol. Chem. |volume=267 |issue= 12 |pages= 8521-9 |year= 1992 |pmid= 1533223 |doi= }}
*{{cite journal | author=Schmauss C, McAllister G, Ohosone Y, ''et al.'' |title=A comparison of snRNP-associated Sm-autoantigens: human N, rat N and human B/B'. |journal=Nucleic Acids Res. |volume=17 |issue= 4 |pages= 1733-43 |year= 1989 |pmid= 2522186 |doi= }}
*{{cite journal | author=Rokeach LA, Jannatipour M, Haselby JA, Hoch SO |title=Primary structure of a human small nuclear ribonucleoprotein polypeptide as deduced by cDNA analysis. |journal=J. Biol. Chem. |volume=264 |issue= 9 |pages= 5024-30 |year= 1989 |pmid= 2522449 |doi= }}
*{{cite journal | author=Renz M, Heim C, Bräunling O, ''et al.'' |title=Expression of the major human ribonucleoprotein (RNP) autoantigens in Escherichia coli and their use in an EIA for screening sera from patients with autoimmune diseases. |journal=Clin. Chem. |volume=35 |issue= 9 |pages= 1861-3 |year= 1989 |pmid= 2528429 |doi= }}
*{{cite journal | author=Sharpe NG, Williams DG, Howarth DN, ''et al.'' |title=Isolation of cDNA clones encoding the human Sm B/B' auto-immune antigen and specifically reacting with human anti-Sm auto-immune sera. |journal=FEBS Lett. |volume=250 |issue= 2 |pages= 585-90 |year= 1989 |pmid= 2753153 |doi= }}
*{{cite journal | author=Reed ML, Leff SE |title=Maternal imprinting of human SNRPN, a gene deleted in Prader-Willi syndrome. |journal=Nat. Genet. |volume=6 |issue= 2 |pages= 163-7 |year= 1994 |pmid= 7512861 |doi= 10.1038/ng0294-163 }}
*{{cite journal | author=Maruyama K, Sugano S |title=Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides. |journal=Gene |volume=138 |issue= 1-2 |pages= 171-4 |year= 1994 |pmid= 8125298 |doi= }}
*{{cite journal | author=Esposito F, Fiore F, Cimino F, Russo T |title=Isolation and structural characterization of the rat gene encoding the brain specific snRNP-associated polypeptide "N". |journal=Biochem. Biophys. Res. Commun. |volume=195 |issue= 1 |pages= 317-26 |year= 1993 |pmid= 8363612 |doi= 10.1006/bbrc.1993.2047 }}
*{{cite journal | author=Glenn CC, Saitoh S, Jong MT, ''et al.'' |title=Gene structure, DNA methylation, and imprinted expression of the human SNRPN gene. |journal=Am. J. Hum. Genet. |volume=58 |issue= 2 |pages= 335-46 |year= 1996 |pmid= 8571960 |doi= }}
*{{cite journal | author=Dittrich B, Buiting K, Korn B, ''et al.'' |title=Imprint switching on human chromosome 15 may involve alternative transcripts of the SNRPN gene. |journal=Nat. Genet. |volume=14 |issue= 2 |pages= 163-70 |year= 1996 |pmid= 8841186 |doi= 10.1038/ng1096-163 }}
*{{cite journal | author=Sun Y, Nicholls RD, Butler MG, ''et al.'' |title=Breakage in the SNRPN locus in a balanced 46,XY,t(15;19) Prader-Willi syndrome patient. |journal=Hum. Mol. Genet. |volume=5 |issue= 4 |pages= 517-24 |year= 1996 |pmid= 8845846 |doi= }}
*{{cite journal | author=Buiting K, Dittrich B, Endele S, Horsthemke B |title=Identification of novel exons 3' to the human SNRPN gene. |journal=Genomics |volume=40 |issue= 1 |pages= 132-7 |year= 1997 |pmid= 9070929 |doi= 10.1006/geno.1996.4571 }}
*{{cite journal | author=Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, ''et al.'' |title=Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library. |journal=Gene |volume=200 |issue= 1-2 |pages= 149-56 |year= 1997 |pmid= 9373149 |doi= }}
*{{cite journal | author=Fury MG, Zhang W, Christodoulopoulos I, Zieve GW |title=Multiple protein: protein interactions between the snRNP common core proteins. |journal=Exp. Cell Res. |volume=237 |issue= 1 |pages= 63-9 |year= 1998 |pmid= 9417867 |doi= 10.1006/excr.1997.3750 }}
*{{cite journal | author=Yang T, Adamson TE, Resnick JL, ''et al.'' |title=A mouse model for Prader-Willi syndrome imprinting-centre mutations. |journal=Nat. Genet. |volume=19 |issue= 1 |pages= 25-31 |year= 1998 |pmid= 9590284 |doi= 10.1038/ng0598-25 }}
*{{cite journal | author=Kuslich CD, Kobori JA, Mohapatra G, ''et al.'' |title=Prader-Willi syndrome is caused by disruption of the SNRPN gene. |journal=Am. J. Hum. Genet. |volume=64 |issue= 1 |pages= 70-6 |year= 1999 |pmid= 9915945 |doi= }}
*{{cite journal | author=Färber C, Dittrich B, Buiting K, Horsthemke B |title=The chromosome 15 imprinting centre (IC) region has undergone multiple duplication events and contains an upstream exon of SNRPN that is deleted in all Angelman syndrome patients with an IC microdeletion. |journal=Hum. Mol. Genet. |volume=8 |issue= 2 |pages= 337-43 |year= 1999 |pmid= 9931342 |doi= }}
*{{cite journal | author=Gray TA, Saitoh S, Nicholls RD |title=An imprinted, mammalian bicistronic transcript encodes two independent proteins. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=96 |issue= 10 |pages= 5616-21 |year= 1999 |pmid= 10318933 |doi= }}
*{{cite journal | author=Gray TA, Smithwick MJ, Schaldach MA, ''et al.'' |title=Concerted regulation and molecular evolution of the duplicated SNRPB'/B and SNRPN loci. |journal=Nucleic Acids Res. |volume=27 |issue= 23 |pages= 4577-84 |year= 2000 |pmid= 10556313 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on SPN... {November 18, 2007 9:19:25 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 18, 2007 9:20:01 PM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}
<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image =
| image_source =
| PDB =
| Name = Sialophorin (leukosialin, CD43)
| HGNCid = 11249
| Symbol = SPN
| AltSymbols =; CD43; GPL115; LSN
| OMIM = 182160
| ECnumber =
| Homologene = 36108
| MGIid = 98384
| Function = {{GNF_GO|id=GO:0004888 |text = transmembrane receptor activity}} {{GNF_GO|id=GO:0005515 |text = protein binding}} {{GNF_GO|id=GO:0008367 |text = bacterial binding}}
| Component = {{GNF_GO|id=GO:0001931 |text = uropod}} {{GNF_GO|id=GO:0005604 |text = basement membrane}} {{GNF_GO|id=GO:0005615 |text = extracellular space}} {{GNF_GO|id=GO:0005887 |text = integral to plasma membrane}} {{GNF_GO|id=GO:0009897 |text = external side of plasma membrane}} {{GNF_GO|id=GO:0016020 |text = membrane}}
| Process = {{GNF_GO|id=GO:0001562 |text = response to protozoan}} {{GNF_GO|id=GO:0001808 |text = negative regulation of type IV hypersensitivity}} {{GNF_GO|id=GO:0006935 |text = chemotaxis}} {{GNF_GO|id=GO:0006968 |text = cellular defense response}} {{GNF_GO|id=GO:0007162 |text = negative regulation of cell adhesion}} {{GNF_GO|id=GO:0007163 |text = establishment and/or maintenance of cell polarity}} {{GNF_GO|id=GO:0007166 |text = cell surface receptor linked signal transduction}} {{GNF_GO|id=GO:0008624 |text = induction of apoptosis by extracellular signals}} {{GNF_GO|id=GO:0031295 |text = T cell costimulation}} {{GNF_GO|id=GO:0042102 |text = positive regulation of T cell proliferation}} {{GNF_GO|id=GO:0042130 |text = negative regulation of T cell proliferation}} {{GNF_GO|id=GO:0042535 |text = positive regulation of tumor necrosis factor biosynthetic process}} {{GNF_GO|id=GO:0042742 |text = defense response to bacterium}} {{GNF_GO|id=GO:0045060 |text = negative thymic T cell selection}} {{GNF_GO|id=GO:0050688 |text = regulation of antiviral response}} {{GNF_GO|id=GO:0050776 |text = regulation of immune response}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 6693
| Hs_Ensembl = ENSG00000197471
| Hs_RefseqProtein = NP_001025459
| Hs_RefseqmRNA = NM_001030288
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 16
| Hs_GenLoc_start = 29582077
| Hs_GenLoc_end = 29589688
| Hs_Uniprot = P16150
| Mm_EntrezGene = 20737
| Mm_Ensembl = ENSMUSG00000051457
| Mm_RefseqmRNA = NM_001037810
| Mm_RefseqProtein = NP_001032899
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 7
| Mm_GenLoc_start = 126924612
| Mm_GenLoc_end = 126928965
| Mm_Uniprot = Q544C5
}}
}}
'''Sialophorin (leukosialin, CD43)''', also known as '''SPN''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: SPN sialophorin (leukosialin, CD43)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=6693| accessdate = }}</ref>
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text = Sialophorin (leukosialin) is a major sialoglycoprotein on the surface of human T lymphocytes, monocytes, granulocytes, and some B lymphocytes, which appears to be important for immune function and may be part of a physiologic ligand-receptor complex involved in T-cell activation.[supplied by OMIM]<ref name="entrez">{{cite web | title = Entrez Gene: SPN sialophorin (leukosialin, CD43)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=6693| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Fukuda M, Carlsson SR |title=Leukosialin, a major sialoglycoprotein on human leukocytes as differentiation antigens. |journal=Med. Biol. |volume=64 |issue= 6 |pages= 335-43 |year= 1987 |pmid= 2950285 |doi= }}
*{{cite journal | author=Rogaev EI, Keryanov SA |title=Unusual variability of the complex dinucleotide repeat block at the SPN locus. |journal=Hum. Mol. Genet. |volume=1 |issue= 8 |pages= 657 |year= 1993 |pmid= 1301183 |doi= }}
*{{cite journal | author=Rosenstein Y, Park JK, Hahn WC, ''et al.'' |title=CD43, a molecule defective in Wiskott-Aldrich syndrome, binds ICAM-1. |journal=Nature |volume=354 |issue= 6350 |pages= 233-5 |year= 1992 |pmid= 1683685 |doi= 10.1038/354233a0 }}
*{{cite journal | author=Schmid K, Hediger MA, Brossmer R, ''et al.'' |title=Amino acid sequence of human plasma galactoglycoprotein: identity with the extracellular region of CD43 (sialophorin). |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=89 |issue= 2 |pages= 663-7 |year= 1992 |pmid= 1731338 |doi= }}
*{{cite journal | author=Kudo S, Fukuda M |title=A short, novel promoter sequence confers the expression of human leukosialin, a major sialoglycoprotein on leukocytes. |journal=J. Biol. Chem. |volume=266 |issue= 13 |pages= 8483-9 |year= 1991 |pmid= 1827122 |doi= }}
*{{cite journal | author=Park JK, Rosenstein YJ, Remold-O'Donnell E, ''et al.'' |title=Enhancement of T-cell activation by the CD43 molecule whose expression is defective in Wiskott-Aldrich syndrome. |journal=Nature |volume=350 |issue= 6320 |pages= 706-9 |year= 1991 |pmid= 2023632 |doi= 10.1038/350706a0 }}
*{{cite journal | author=Shelley CS, Remold-O'Donnell E, Rosen FS, Whitehead AS |title=Structure of the human sialophorin (CD43) gene. Identification of features atypical of genes encoding integral membrane proteins. |journal=Biochem. J. |volume=270 |issue= 3 |pages= 569-76 |year= 1990 |pmid= 2241892 |doi= }}
*{{cite journal | author=Pallant A, Eskenazi A, Mattei MG, ''et al.'' |title=Characterization of cDNAs encoding human leukosialin and localization of the leukosialin gene to chromosome 16. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=86 |issue= 4 |pages= 1328-32 |year= 1989 |pmid= 2521952 |doi= }}
*{{cite journal | author=Shelley CS, Remold-O'Donnell E, Davis AE, ''et al.'' |title=Molecular characterization of sialophorin (CD43), the lymphocyte surface sialoglycoprotein defective in Wiskott-Aldrich syndrome. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=86 |issue= 8 |pages= 2819-23 |year= 1989 |pmid= 2784859 |doi= }}
*{{cite journal | author=Srinivas RV, Su T, Trimble LA, ''et al.'' |title=Enhanced susceptibility to human immunodeficiency virus infection in CD4+ T lymphocytes genetically deficient in CD43. |journal=AIDS Res. Hum. Retroviruses |volume=11 |issue= 9 |pages= 1015-21 |year= 1996 |pmid= 8554898 |doi= }}
*{{cite journal | author=Hirao M, Sato N, Kondo T, ''et al.'' |title=Regulation mechanism of ERM (ezrin/radixin/moesin) protein/plasma membrane association: possible involvement of phosphatidylinositol turnover and Rho-dependent signaling pathway. |journal=J. Cell Biol. |volume=135 |issue= 1 |pages= 37-51 |year= 1996 |pmid= 8858161 |doi= }}
*{{cite journal | author=Yonemura S, Hirao M, Doi Y, ''et al.'' |title=Ezrin/radixin/moesin (ERM) proteins bind to a positively charged amino acid cluster in the juxta-membrane cytoplasmic domain of CD44, CD43, and ICAM-2. |journal=J. Cell Biol. |volume=140 |issue= 4 |pages= 885-95 |year= 1998 |pmid= 9472040 |doi= }}
*{{cite journal | author=Pedraza-Alva G, Mérida LB, Burakoff SJ, Rosenstein Y |title=T cell activation through the CD43 molecule leads to Vav tyrosine phosphorylation and mitogen-activated protein kinase pathway activation. |journal=J. Biol. Chem. |volume=273 |issue= 23 |pages= 14218-24 |year= 1998 |pmid= 9603925 |doi= }}
*{{cite journal | author=Serrador JM, Nieto M, Alonso-Lebrero JL, ''et al.'' |title=CD43 interacts with moesin and ezrin and regulates its redistribution to the uropods of T lymphocytes at the cell-cell contacts. |journal=Blood |volume=91 |issue= 12 |pages= 4632-44 |year= 1998 |pmid= 9616160 |doi= }}
*{{cite journal | author=Pace KE, Lee C, Stewart PL, Baum LG |title=Restricted receptor segregation into membrane microdomains occurs on human T cells during apoptosis induced by galectin-1. |journal=J. Immunol. |volume=163 |issue= 7 |pages= 3801-11 |year= 1999 |pmid= 10490978 |doi= }}
*{{cite journal | author=Seveau S, Keller H, Maxfield FR, ''et al.'' |title=Neutrophil polarity and locomotion are associated with surface redistribution of leukosialin (CD43), an antiadhesive membrane molecule. |journal=Blood |volume=95 |issue= 8 |pages= 2462-70 |year= 2000 |pmid= 10753822 |doi= }}
*{{cite journal | author=Fratazzi C, Manjunath N, Arbeit RD, ''et al.'' |title=A macrophage invasion mechanism for mycobacteria implicating the extracellular domain of CD43. |journal=J. Exp. Med. |volume=192 |issue= 2 |pages= 183-92 |year= 2000 |pmid= 10899905 |doi= }}
*{{cite journal | author=Santana MA, Pedraza-Alva G, Olivares-Zavaleta N, ''et al.'' |title=CD43-mediated signals induce DNA binding activity of AP-1, NF-AT, and NFkappa B transcription factors in human T lymphocytes. |journal=J. Biol. Chem. |volume=275 |issue= 40 |pages= 31460-8 |year= 2000 |pmid= 10908570 |doi= 10.1074/jbc.M005231200 }}
*{{cite journal | author=van den Berg TK, Nath D, Ziltener HJ, ''et al.'' |title=Cutting edge: CD43 functions as a T cell counterreceptor for the macrophage adhesion receptor sialoadhesin (Siglec-1). |journal=J. Immunol. |volume=166 |issue= 6 |pages= 3637-40 |year= 2001 |pmid= 11238599 |doi= }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on ST14... {November 18, 2007 9:20:01 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 18, 2007 9:20:46 PM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
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| update_protein_box = yes
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| update_citations = yes
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<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image = PBB_Protein_ST14_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1eaw.
| PDB = {{PDB2|1eaw}}, {{PDB2|1eax}}, {{PDB2|2gv6}}, {{PDB2|2gv7}}
| Name = Suppression of tumorigenicity 14 (colon carcinoma)
| HGNCid = 11344
| Symbol = ST14
| AltSymbols =; HAI; MT-SP1; MTSP-1; MTSP1; PRSS14; SNC19; TADG-15
| OMIM = 606797
| ECnumber =
| Homologene = 7906
| MGIid = 1338881
| GeneAtlas_image1 = PBB_GE_ST14_202005_at_tn.png
| GeneAtlas_image2 = PBB_GE_ST14_216905_s_at_tn.png
| Function = {{GNF_GO|id=GO:0004252 |text = serine-type endopeptidase activity}}
| Component = {{GNF_GO|id=GO:0005576 |text = extracellular region}} {{GNF_GO|id=GO:0005886 |text = plasma membrane}} {{GNF_GO|id=GO:0005887 |text = integral to plasma membrane}} {{GNF_GO|id=GO:0019897 |text = extrinsic to plasma membrane}}
| Process = {{GNF_GO|id=GO:0006508 |text = proteolysis}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 6768
| Hs_Ensembl = ENSG00000149418
| Hs_RefseqProtein = NP_068813
| Hs_RefseqmRNA = NM_021978
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 11
| Hs_GenLoc_start = 129534892
| Hs_GenLoc_end = 129585466
| Hs_Uniprot = Q9Y5Y6
| Mm_EntrezGene = 19143
| Mm_Ensembl = ENSMUSG00000031995
| Mm_RefseqmRNA = NM_011176
| Mm_RefseqProtein = NP_035306
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 9
| Mm_GenLoc_start = 30838155
| Mm_GenLoc_end = 30881364
| Mm_Uniprot = Q543E3
}}
}}
'''Suppression of tumorigenicity 14 (colon carcinoma)''', also known as '''ST14''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: ST14 suppression of tumorigenicity 14 (colon carcinoma)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=6768| accessdate = }}</ref>
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text = The protein encoded by this gene is an epithelial-derived, integral membrane serine protease. This protease forms a complex with the Kunitz-type serine protease inhibitor, HAI-1, and is found to be activated by sphingosine 1-phosphate. This protease has been shown to cleave and activate hepatocyte growth factor/scattering factor, and urokinase plasminogen activator, which suggest the function of this protease as an epithelial membrane activator for other proteases and latent growth factors. The expression of this protease has been associated with breast, colon, prostate, and ovarian tumors, which implicates its role in cancer invasion, and metastasis.<ref name="entrez">{{cite web | title = Entrez Gene: ST14 suppression of tumorigenicity 14 (colon carcinoma)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=6768| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Uhland K |title=Matriptase and its putative role in cancer. |journal=Cell. Mol. Life Sci. |volume=63 |issue= 24 |pages= 2968-78 |year= 2007 |pmid= 17131055 |doi= 10.1007/s00018-006-6298-x }}
*{{cite journal | author=Zhang Y, Cai X, Schlegelberger B, Zheng S |title=Assignment1 of human putative tumor suppressor genes ST13 (alias SNC6) and ST14 (alias SNC19) to human chromosome bands 22q13 and 11q24-->q25 by in situ hybridization. |journal=Cytogenet. Cell Genet. |volume=83 |issue= 1-2 |pages= 56-7 |year= 1999 |pmid= 9925927 |doi= }}
*{{cite journal | author=Lin CY, Anders J, Johnson M, ''et al.'' |title=Molecular cloning of cDNA for matriptase, a matrix-degrading serine protease with trypsin-like activity. |journal=J. Biol. Chem. |volume=274 |issue= 26 |pages= 18231-6 |year= 1999 |pmid= 10373424 |doi= }}
*{{cite journal | author=Lin CY, Anders J, Johnson M, Dickson RB |title=Purification and characterization of a complex containing matriptase and a Kunitz-type serine protease inhibitor from human milk. |journal=J. Biol. Chem. |volume=274 |issue= 26 |pages= 18237-42 |year= 1999 |pmid= 10373425 |doi= }}
*{{cite journal | author=Takeuchi T, Shuman MA, Craik CS |title=Reverse biochemistry: use of macromolecular protease inhibitors to dissect complex biological processes and identify a membrane-type serine protease in epithelial cancer and normal tissue. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=96 |issue= 20 |pages= 11054-61 |year= 1999 |pmid= 10500122 |doi= }}
*{{cite journal | author=Takeuchi T, Harris JL, Huang W, ''et al.'' |title=Cellular localization of membrane-type serine protease 1 and identification of protease-activated receptor-2 and single-chain urokinase-type plasminogen activator as substrates. |journal=J. Biol. Chem. |volume=275 |issue= 34 |pages= 26333-42 |year= 2000 |pmid= 10831593 |doi= 10.1074/jbc.M002941200 }}
*{{cite journal | author=Lee SL, Dickson RB, Lin CY |title=Activation of hepatocyte growth factor and urokinase/plasminogen activator by matriptase, an epithelial membrane serine protease. |journal=J. Biol. Chem. |volume=275 |issue= 47 |pages= 36720-5 |year= 2001 |pmid= 10962009 |doi= 10.1074/jbc.M007802200 }}
*{{cite journal | author=Tanimoto H, Underwood LJ, Wang Y, ''et al.'' |title=Ovarian tumor cells express a transmembrane serine protease: a potential candidate for early diagnosis and therapeutic intervention. |journal=Tumour Biol. |volume=22 |issue= 2 |pages= 104-14 |year= 2001 |pmid= 11125283 |doi= }}
*{{cite journal | author=Oberst M, Anders J, Xie B, ''et al.'' |title=Matriptase and HAI-1 are expressed by normal and malignant epithelial cells in vitro and in vivo. |journal=Am. J. Pathol. |volume=158 |issue= 4 |pages= 1301-11 |year= 2001 |pmid= 11290548 |doi= }}
*{{cite journal | author=Benaud C, Oberst M, Hobson JP, ''et al.'' |title=Sphingosine 1-phosphate, present in serum-derived lipoproteins, activates matriptase. |journal=J. Biol. Chem. |volume=277 |issue= 12 |pages= 10539-46 |year= 2002 |pmid= 11792696 |doi= 10.1074/jbc.M109064200 }}
*{{cite journal | author=Ihara S, Miyoshi E, Ko JH, ''et al.'' |title=Prometastatic effect of N-acetylglucosaminyltransferase V is due to modification and stabilization of active matriptase by adding beta 1-6 GlcNAc branching. |journal=J. Biol. Chem. |volume=277 |issue= 19 |pages= 16960-7 |year= 2002 |pmid= 11864986 |doi= 10.1074/jbc.M200673200 }}
*{{cite journal | author=Peek M, Moran P, Mendoza N, ''et al.'' |title=Unusual proteolytic activation of pro-hepatocyte growth factor by plasma kallikrein and coagulation factor XIa. |journal=J. Biol. Chem. |volume=277 |issue= 49 |pages= 47804-9 |year= 2003 |pmid= 12372819 |doi= 10.1074/jbc.M209778200 }}
*{{cite journal | author=Strausberg RL, Feingold EA, Grouse LH, ''et al.'' |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899-903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899 }}
*{{cite journal | author=Benaud CM, Oberst M, Dickson RB, Lin CY |title=Deregulated activation of matriptase in breast cancer cells. |journal=Clin. Exp. Metastasis |volume=19 |issue= 7 |pages= 639-49 |year= 2003 |pmid= 12498394 |doi= }}
*{{cite journal | author=Oberst MD, Williams CA, Dickson RB, ''et al.'' |title=The activation of matriptase requires its noncatalytic domains, serine protease domain, and its cognate inhibitor. |journal=J. Biol. Chem. |volume=278 |issue= 29 |pages= 26773-9 |year= 2003 |pmid= 12738778 |doi= 10.1074/jbc.M304282200 }}
*{{cite journal | author=Santin AD, Cane' S, Bellone S, ''et al.'' |title=The novel serine protease tumor-associated differentially expressed gene-15 (matriptase/MT-SP1) is highly overexpressed in cervical carcinoma. |journal=Cancer |volume=98 |issue= 9 |pages= 1898-904 |year= 2003 |pmid= 14584072 |doi= 10.1002/cncr.11753 }}
*{{cite journal | author=Suzuki M, Kobayashi H, Kanayama N, ''et al.'' |title=Inhibition of tumor invasion by genomic down-regulation of matriptase through suppression of activation of receptor-bound pro-urokinase. |journal=J. Biol. Chem. |volume=279 |issue= 15 |pages= 14899-908 |year= 2004 |pmid= 14747469 |doi= 10.1074/jbc.M313130200 }}
*{{cite journal | author=Hung RJ, Hsu IaW, Dreiling JL, ''et al.'' |title=Assembly of adherens junctions is required for sphingosine 1-phosphate-induced matriptase accumulation and activation at mammary epithelial cell-cell contacts. |journal=Am. J. Physiol., Cell Physiol. |volume=286 |issue= 5 |pages= C1159-69 |year= 2004 |pmid= 15075215 |doi= 10.1152/ajpcell.00400.2003 }}
*{{cite journal | author=Sun LF, Zheng S, Shi Y, ''et al.'' |title=[SNC19/ST14 gene transfection and expression influence the biological behavior of colorectal cancer cells] |journal=Zhonghua Yi Xue Za Zhi |volume=84 |issue= 10 |pages= 843-8 |year= 2004 |pmid= 15200890 |doi= }}
*{{cite journal | author=Gerhard DS, Wagner L, Feingold EA, ''et al.'' |title=The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). |journal=Genome Res. |volume=14 |issue= 10B |pages= 2121-7 |year= 2004 |pmid= 15489334 |doi= 10.1101/gr.2596504 }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on THY1... {November 18, 2007 9:20:46 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 18, 2007 9:21:14 PM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}
<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image =
| image_source =
| PDB =
| Name = Thy-1 cell surface antigen
| HGNCid = 11801
| Symbol = THY1
| AltSymbols =; CD90; FLJ33325
| OMIM = 188230
| ECnumber =
| Homologene = 4580
| MGIid = 98747
| GeneAtlas_image1 = PBB_GE_THY1_208850_s_at_tn.png
| GeneAtlas_image2 = PBB_GE_THY1_208851_s_at_tn.png
| GeneAtlas_image3 = PBB_GE_THY1_213869_x_at_tn.png
| Function = {{GNF_GO|id=GO:0003674 |text = molecular_function}} {{GNF_GO|id=GO:0005100 |text = Rho GTPase activator activity}} {{GNF_GO|id=GO:0005178 |text = integrin binding}} {{GNF_GO|id=GO:0005515 |text = protein binding}} {{GNF_GO|id=GO:0048503 |text = GPI anchor binding}}
| Component = {{GNF_GO|id=GO:0005575 |text = cellular_component}} {{GNF_GO|id=GO:0005783 |text = endoplasmic reticulum}} {{GNF_GO|id=GO:0005829 |text = cytosol}} {{GNF_GO|id=GO:0005886 |text = plasma membrane}} {{GNF_GO|id=GO:0005887 |text = integral to plasma membrane}} {{GNF_GO|id=GO:0009897 |text = external side of plasma membrane}} {{GNF_GO|id=GO:0030426 |text = growth cone}} {{GNF_GO|id=GO:0045121 |text = lipid raft}}
| Process = {{GNF_GO|id=GO:0001525 |text = angiogenesis}} {{GNF_GO|id=GO:0006469 |text = negative regulation of protein kinase activity}} {{GNF_GO|id=GO:0007010 |text = cytoskeleton organization and biogenesis}} {{GNF_GO|id=GO:0008150 |text = biological_process}} {{GNF_GO|id=GO:0016337 |text = cell-cell adhesion}} {{GNF_GO|id=GO:0030336 |text = negative regulation of cell migration}} {{GNF_GO|id=GO:0043066 |text = negative regulation of apoptosis}} {{GNF_GO|id=GO:0043547 |text = positive regulation of GTPase activity}} {{GNF_GO|id=GO:0045576 |text = mast cell activation}} {{GNF_GO|id=GO:0046549 |text = retinal cone cell development}} {{GNF_GO|id=GO:0048041 |text = focal adhesion formation}} {{GNF_GO|id=GO:0048147 |text = negative regulation of fibroblast proliferation}} {{GNF_GO|id=GO:0050731 |text = positive regulation of peptidyl-tyrosine phosphorylation}} {{GNF_GO|id=GO:0050771 |text = negative regulation of axonogenesis}} {{GNF_GO|id=GO:0050852 |text = T cell receptor signaling pathway}} {{GNF_GO|id=GO:0050860 |text = negative regulation of T cell receptor signaling pathway}} {{GNF_GO|id=GO:0050870 |text = positive regulation of T cell activation}} {{GNF_GO|id=GO:0051281 |text = positive regulation of release of sequestered calcium ion into cytosol}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 7070
| Hs_Ensembl = ENSG00000154096
| Hs_RefseqProtein = NP_006279
| Hs_RefseqmRNA = NM_006288
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 11
| Hs_GenLoc_start = 118794096
| Hs_GenLoc_end = 118800048
| Hs_Uniprot = P04216
| Mm_EntrezGene = 21838
| Mm_Ensembl = ENSMUSG00000032011
| Mm_RefseqmRNA = NM_009382
| Mm_RefseqProtein = NP_033408
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 9
| Mm_GenLoc_start = 43796949
| Mm_GenLoc_end = 43799574
| Mm_Uniprot = Q53YX2
}}
}}
'''Thy-1 cell surface antigen''', also known as '''THY1''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: THY1 Thy-1 cell surface antigen| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=7070| accessdate = }}</ref>
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text =
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Henniker AJ |title=CD90. |journal=J. Biol. Regul. Homeost. Agents |volume=15 |issue= 4 |pages= 392-3 |year= 2002 |pmid= 11860231 |doi= }}
*{{cite journal | author=Mahanthappa NK, Patterson PH |title=Thy-1 multimerization is correlated with neurite outgrowth. |journal=Dev. Biol. |volume=150 |issue= 1 |pages= 60-71 |year= 1992 |pmid= 1347022 |doi= }}
*{{cite journal | author=Thomas PM, Samelson LE |title=The glycophosphatidylinositol-anchored Thy-1 molecule interacts with the p60fyn protein tyrosine kinase in T cells. |journal=J. Biol. Chem. |volume=267 |issue= 17 |pages= 12317-22 |year= 1992 |pmid= 1351058 |doi= }}
*{{cite journal | author=Seki T, Chang HC, Moriuchi T, ''et al.'' |title=Thy-1: a hydrophobic transmembrane segment at the carboxyl terminus. |journal=Fed. Proc. |volume=44 |issue= 13 |pages= 2865-9 |year= 1985 |pmid= 2864289 |doi= }}
*{{cite journal | author=Seki T, Spurr N, Obata F, ''et al.'' |title=The human Thy-1 gene: structure and chromosomal location. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=82 |issue= 19 |pages= 6657-61 |year= 1985 |pmid= 2864690 |doi= }}
*{{cite journal | author=Rettig WJ, Nishimura H, Yenamandra AK, ''et al.'' |title=Differential expression of the human Thy-1 gene in rodent-human somatic cell hybrids [corrected] |journal=J. Immunol. |volume=138 |issue= 12 |pages= 4484-9 |year= 1987 |pmid= 2884261 |doi= }}
*{{cite journal | author=Hood L, Kronenberg M, Hunkapiller T |title=T cell antigen receptors and the immunoglobulin supergene family. |journal=Cell |volume=40 |issue= 2 |pages= 225-9 |year= 1985 |pmid= 3917857 |doi= }}
*{{cite journal | author=Moriuchi T, Chang HC, Denome R, Silver J |title=Thy-1 cDNA sequence suggests a novel regulatory mechanism. |journal=Nature |volume=301 |issue= 5895 |pages= 80-2 |year= 1983 |pmid= 6130472 |doi= }}
*{{cite journal | author=Dreyer EB, Leifer D, Heng JE, ''et al.'' |title=An astrocytic binding site for neuronal Thy-1 and its effect on neurite outgrowth. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=92 |issue= 24 |pages= 11195-9 |year= 1995 |pmid= 7479964 |doi= }}
*{{cite journal | author=Ley SC, Marsh M, Bebbington CR, ''et al.'' |title=Distinct intracellular localization of Lck and Fyn protein tyrosine kinases in human T lymphocytes. |journal=J. Cell Biol. |volume=125 |issue= 3 |pages= 639-49 |year= 1994 |pmid= 7513706 |doi= }}
*{{cite journal | author=Craig W, Kay R, Cutler RL, Lansdorp PM |title=Expression of Thy-1 on human hematopoietic progenitor cells. |journal=J. Exp. Med. |volume=177 |issue= 5 |pages= 1331-42 |year= 1993 |pmid= 7683034 |doi= }}
*{{cite journal | author=Mason JC, Yarwood H, Tárnok A, ''et al.'' |title=Human Thy-1 is cytokine-inducible on vascular endothelial cells and is a signaling molecule regulated by protein kinase C. |journal=J. Immunol. |volume=157 |issue= 2 |pages= 874-83 |year= 1996 |pmid= 8752941 |doi= }}
*{{cite journal | author=Nguyen DH, Hildreth JE |title=Evidence for budding of human immunodeficiency virus type 1 selectively from glycolipid-enriched membrane lipid rafts. |journal=J. Virol. |volume=74 |issue= 7 |pages= 3264-72 |year= 2000 |pmid= 10708443 |doi= }}
*{{cite journal | author=Ye Z, Connor JR |title=cDNA cloning by amplification of circularized first strand cDNAs reveals non-IRE-regulated iron-responsive mRNAs. |journal=Biochem. Biophys. Res. Commun. |volume=275 |issue= 1 |pages= 223-7 |year= 2000 |pmid= 10944468 |doi= 10.1006/bbrc.2000.3282 }}
*{{cite journal | author=Hartley JL, Temple GF, Brasch MA |title=DNA cloning using in vitro site-specific recombination. |journal=Genome Res. |volume=10 |issue= 11 |pages= 1788-95 |year= 2001 |pmid= 11076863 |doi= }}
*{{cite journal | author=Wiemann S, Weil B, Wellenreuther R, ''et al.'' |title=Toward a catalog of human genes and proteins: sequencing and analysis of 500 novel complete protein coding human cDNAs. |journal=Genome Res. |volume=11 |issue= 3 |pages= 422-35 |year= 2001 |pmid= 11230166 |doi= 10.1101/gr.154701 }}
*{{cite journal | author=Simpson JC, Wellenreuther R, Poustka A, ''et al.'' |title=Systematic subcellular localization of novel proteins identified by large-scale cDNA sequencing. |journal=EMBO Rep. |volume=1 |issue= 3 |pages= 287-92 |year= 2001 |pmid= 11256614 |doi= 10.1093/embo-reports/kvd058 }}
*{{cite journal | author=Steiniger B, Barth P, Hellinger A |title=The perifollicular and marginal zones of the human splenic white pulp : do fibroblasts guide lymphocyte immigration? |journal=Am. J. Pathol. |volume=159 |issue= 2 |pages= 501-12 |year= 2001 |pmid= 11485909 |doi= }}
*{{cite journal | author=Saalbach A, Hildebrandt G, Haustein UF, Anderegg U |title=The Thy-1/Thy-1 ligand interaction is involved in binding of melanoma cells to activated Thy-1- positive microvascular endothelial cells. |journal=Microvasc. Res. |volume=64 |issue= 1 |pages= 86-93 |year= 2002 |pmid= 12074634 |doi= 10.1006/mvre.2002.2401 }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on TP53BP2... {November 18, 2007 9:21:14 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 18, 2007 9:21:50 PM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
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<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image = PBB_Protein_TP53BP2_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1ycs.
| PDB = {{PDB2|1ycs}}
| Name = Tumor protein p53 binding protein, 2
| HGNCid = 12000
| Symbol = TP53BP2
| AltSymbols =; 53BP2; ASPP2; BBP; PPP1R13A; p53BP2
| OMIM = 602143
| ECnumber =
| Homologene = 3959
| MGIid = 2138319
| GeneAtlas_image1 = PBB_GE_TP53BP2_203120_at_tn.png
| Function = {{GNF_GO|id=GO:0005070 |text = SH3/SH2 adaptor activity}} {{GNF_GO|id=GO:0005515 |text = protein binding}} {{GNF_GO|id=GO:0051059 |text = NF-kappaB binding}}
| Component = {{GNF_GO|id=GO:0005737 |text = cytoplasm}}
| Process = {{GNF_GO|id=GO:0006915 |text = apoptosis}} {{GNF_GO|id=GO:0006917 |text = induction of apoptosis}} {{GNF_GO|id=GO:0007049 |text = cell cycle}} {{GNF_GO|id=GO:0007165 |text = signal transduction}} {{GNF_GO|id=GO:0007417 |text = central nervous system development}} {{GNF_GO|id=GO:0007507 |text = heart development}} {{GNF_GO|id=GO:0009792 |text = embryonic development ending in birth or egg hatching}} {{GNF_GO|id=GO:0010212 |text = response to ionizing radiation}} {{GNF_GO|id=GO:0045786 |text = negative regulation of progression through cell cycle}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 7159
| Hs_Ensembl = ENSG00000143514
| Hs_RefseqProtein = NP_001026855
| Hs_RefseqmRNA = NM_001031685
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 1
| Hs_GenLoc_start = 222034224
| Hs_GenLoc_end = 222100297
| Hs_Uniprot = Q13625
| Mm_EntrezGene = 209456
| Mm_Ensembl = ENSMUSG00000026510
| Mm_RefseqmRNA = NM_173378
| Mm_RefseqProtein = NP_775554
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 1
| Mm_GenLoc_start = 184265679
| Mm_GenLoc_end = 184299107
| Mm_Uniprot = Q3UZC5
}}
}}
'''Tumor protein p53 binding protein, 2''', also known as '''TP53BP2''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: TP53BP2 tumor protein p53 binding protein, 2| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=7159| accessdate = }}</ref>
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text = This gene encodes a member of the ASPP (apoptosis-stimulating protein of p53) family of p53 interacting proteins. The protein contains four ankyrin repeats and an SH3 domain involved in protein-protein interactions. It is localized to the perinuclear region of the cytoplasm, and regulates apoptosis and cell growth through interactions with other regulatory molecules including members of the p53 family. Multiple transcript variants encoding different isoforms have been found for this gene.<ref name="entrez">{{cite web | title = Entrez Gene: TP53BP2 tumor protein p53 binding protein, 2| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=7159| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Liu ZJ, Lu X, Zhong S |title=ASPP--Apoptotic specific regulator of p53. |journal=Biochim. Biophys. Acta |volume=1756 |issue= 1 |pages= 77-80 |year= 2005 |pmid= 16139958 |doi= 10.1016/j.bbcan.2005.08.002 }}
*{{cite journal | author=Iwabuchi K, Bartel PL, Li B, ''et al.'' |title=Two cellular proteins that bind to wild-type but not mutant p53. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=91 |issue= 13 |pages= 6098-102 |year= 1994 |pmid= 8016121 |doi= }}
*{{cite journal | author=Helps NR, Barker HM, Elledge SJ, Cohen PT |title=Protein phosphatase 1 interacts with p53BP2, a protein which binds to the tumour suppressor p53. |journal=FEBS Lett. |volume=377 |issue= 3 |pages= 295-300 |year= 1996 |pmid= 8549741 |doi= 10.1016/0014-5793(95)01347-4 }}
*{{cite journal | author=Naumovski L, Cleary ML |title=The p53-binding protein 53BP2 also interacts with Bc12 and impedes cell cycle progression at G2/M. |journal=Mol. Cell. Biol. |volume=16 |issue= 7 |pages= 3884-92 |year= 1996 |pmid= 8668206 |doi= }}
*{{cite journal | author=Gorina S, Pavletich NP |title=Structure of the p53 tumor suppressor bound to the ankyrin and SH3 domains of 53BP2. |journal=Science |volume=274 |issue= 5289 |pages= 1001-5 |year= 1996 |pmid= 8875926 |doi= }}
*{{cite journal | author=Pirozzi G, McConnell SJ, Uveges AJ, ''et al.'' |title=Identification of novel human WW domain-containing proteins by cloning of ligand targets. |journal=J. Biol. Chem. |volume=272 |issue= 23 |pages= 14611-6 |year= 1997 |pmid= 9169421 |doi= }}
*{{cite journal | author=Yang JP, Ono T, Sonta S, ''et al.'' |title=Assignment of p53 binding protein (TP53BP2) to human chromosome band 1q42.1 by in situ hybridization. |journal=Cytogenet. Cell Genet. |volume=78 |issue= 1 |pages= 61-2 |year= 1997 |pmid= 9345910 |doi= }}
*{{cite journal | author=Iwabuchi K, Li B, Massa HF, ''et al.'' |title=Stimulation of p53-mediated transcriptional activation by the p53-binding proteins, 53BP1 and 53BP2. |journal=J. Biol. Chem. |volume=273 |issue= 40 |pages= 26061-8 |year= 1998 |pmid= 9748285 |doi= }}
*{{cite journal | author=Yang JP, Hori M, Takahashi N, ''et al.'' |title=NF-kappaB subunit p65 binds to 53BP2 and inhibits cell death induced by 53BP2. |journal=Oncogene |volume=18 |issue= 37 |pages= 5177-86 |year= 1999 |pmid= 10498867 |doi= 10.1038/sj.onc.1202904 }}
*{{cite journal | author=Scanlan MJ, Gordan JD, Williamson B, ''et al.'' |title=Antigens recognized by autologous antibody in patients with renal-cell carcinoma. |journal=Int. J. Cancer |volume=83 |issue= 4 |pages= 456-64 |year= 1999 |pmid= 10508479 |doi= }}
*{{cite journal | author=Mori T, Okamoto H, Takahashi N, ''et al.'' |title=Aberrant overexpression of 53BP2 mRNA in lung cancer cell lines. |journal=FEBS Lett. |volume=465 |issue= 2-3 |pages= 124-8 |year= 2000 |pmid= 10631318 |doi= }}
*{{cite journal | author=Nakagawa H, Koyama K, Murata Y, ''et al.'' |title=APCL, a central nervous system-specific homologue of adenomatous polyposis coli tumor suppressor, binds to p53-binding protein 2 and translocates it to the perinucleus. |journal=Cancer Res. |volume=60 |issue= 1 |pages= 101-5 |year= 2000 |pmid= 10646860 |doi= }}
*{{cite journal | author=Lopez CD, Ao Y, Rohde LH, ''et al.'' |title=Proapoptotic p53-interacting protein 53BP2 is induced by UV irradiation but suppressed by p53. |journal=Mol. Cell. Biol. |volume=20 |issue= 21 |pages= 8018-25 |year= 2000 |pmid= 11027272 |doi= }}
*{{cite journal | author=Espanel X, Sudol M |title=Yes-associated protein and p53-binding protein-2 interact through their WW and SH3 domains. |journal=J. Biol. Chem. |volume=276 |issue= 17 |pages= 14514-23 |year= 2001 |pmid= 11278422 |doi= 10.1074/jbc.M008568200 }}
*{{cite journal | author=Kajkowski EM, Lo CF, Ning X, ''et al.'' |title=beta -Amyloid peptide-induced apoptosis regulated by a novel protein containing a g protein activation module. |journal=J. Biol. Chem. |volume=276 |issue= 22 |pages= 18748-56 |year= 2001 |pmid= 11278849 |doi= 10.1074/jbc.M011161200 }}
*{{cite journal | author=Samuels-Lev Y, O'Connor DJ, Bergamaschi D, ''et al.'' |title=ASPP proteins specifically stimulate the apoptotic function of p53. |journal=Mol. Cell |volume=8 |issue= 4 |pages= 781-94 |year= 2001 |pmid= 11684014 |doi= }}
*{{cite journal | author=Strausberg RL, Feingold EA, Grouse LH, ''et al.'' |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899-903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899 }}
*{{cite journal | author=Chen Y, Liu W, Naumovski L, Neve RL |title=ASPP2 inhibits APP-BP1-mediated NEDD8 conjugation to cullin-1 and decreases APP-BP1-induced cell proliferation and neuronal apoptosis. |journal=J. Neurochem. |volume=85 |issue= 3 |pages= 801-9 |year= 2003 |pmid= 12694406 |doi= }}
*{{cite journal | author=Bergamaschi D, Samuels Y, Jin B, ''et al.'' |title=ASPP1 and ASPP2: common activators of p53 family members. |journal=Mol. Cell. Biol. |volume=24 |issue= 3 |pages= 1341-50 |year= 2004 |pmid= 14729977 |doi= }}
*{{cite journal | author=Takahashi N, Kobayashi S, Jiang X, ''et al.'' |title=Expression of 53BP2 and ASPP2 proteins from TP53BP2 gene by alternative splicing. |journal=Biochem. Biophys. Res. Commun. |volume=315 |issue= 2 |pages= 434-8 |year= 2004 |pmid= 14766226 |doi= 10.1016/j.bbrc.2004.01.079 }}
}}
{{refend}}
{{protein-stub}}
- INFO: Beginning work on UCP1... {November 18, 2007 9:21:50 PM PST}
- AMBIGUITY: Did not locate an acceptable page to update. {November 18, 2007 9:22:17 PM PST}
<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{PBB_Controls
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}
<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{GNF_Protein_box
| image =
| image_source =
| PDB =
| Name = Uncoupling protein 1 (mitochondrial, proton carrier)
| HGNCid = 12517
| Symbol = UCP1
| AltSymbols =; SLC25A7; UCP
| OMIM = 113730
| ECnumber =
| Homologene = 22524
| MGIid = 98894
| GeneAtlas_image1 = PBB_GE_UCP1_221384_at_tn.png
| Function = {{GNF_GO|id=GO:0005215 |text = transporter activity}} {{GNF_GO|id=GO:0005515 |text = protein binding}} {{GNF_GO|id=GO:0017077 |text = oxidative phosphorylation uncoupler activity}}
| Component = {{GNF_GO|id=GO:0005624 |text = membrane fraction}} {{GNF_GO|id=GO:0005739 |text = mitochondrion}} {{GNF_GO|id=GO:0005740 |text = mitochondrial envelope}} {{GNF_GO|id=GO:0005743 |text = mitochondrial inner membrane}} {{GNF_GO|id=GO:0016020 |text = membrane}} {{GNF_GO|id=GO:0016021 |text = integral to membrane}}
| Process = {{GNF_GO|id=GO:0006091 |text = generation of precursor metabolites and energy}} {{GNF_GO|id=GO:0006810 |text = transport}} {{GNF_GO|id=GO:0006839 |text = mitochondrial transport}} {{GNF_GO|id=GO:0015992 |text = proton transport}}
| Orthologs = {{GNF_Ortholog_box
| Hs_EntrezGene = 7350
| Hs_Ensembl = ENSG00000109424
| Hs_RefseqProtein = NP_068605
| Hs_RefseqmRNA = NM_021833
| Hs_GenLoc_db =
| Hs_GenLoc_chr = 4
| Hs_GenLoc_start = 141700500
| Hs_GenLoc_end = 141709457
| Hs_Uniprot = P25874
| Mm_EntrezGene = 22227
| Mm_Ensembl = ENSMUSG00000031710
| Mm_RefseqmRNA = NM_009463
| Mm_RefseqProtein = NP_033489
| Mm_GenLoc_db =
| Mm_GenLoc_chr = 8
| Mm_GenLoc_start = 86180457
| Mm_GenLoc_end = 86188557
| Mm_Uniprot = P12242
}}
}}
'''Uncoupling protein 1 (mitochondrial, proton carrier)''', also known as '''UCP1''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: UCP1 uncoupling protein 1 (mitochondrial, proton carrier)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=7350| accessdate = }}</ref>
<!-- The PBB_Summary template is automatically maintained by Protein Box Bot. See Template:PBB_Controls to Stop updates. -->
{{PBB_Summary
| section_title =
| summary_text = Mitochondrial uncoupling proteins (UCP) are members of the family of mitochondrial anion carrier proteins (MACP). UCPs separate oxidative phosphorylation from ATP synthesis with energy dissipated as heat, also referred to as the mitochondrial proton leak. UCPs facilitate the transfer of anions from the inner to the outer mitochondrial membrane and the return transfer of protons from the outer to the inner mitochondrial membrane. They also reduce the mitochondrial membrane potential in mammalian cells. Tissue specificity occurs for the different UCPs and the exact methods of how UCPs transfer H+/OH- are not known. UCPs contain the three homologous protein domains of MACPs. This gene is expressed only in brown adipose tissue, a specialized tissue which functions to produce heat.<ref name="entrez">{{cite web | title = Entrez Gene: UCP1 uncoupling protein 1 (mitochondrial, proton carrier)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=7350| accessdate = }}</ref>
}}
==References==
{{reflist}}
==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading
| citations =
*{{cite journal | author=Ricquier D, Bouillaud F |title=The uncoupling protein homologues: UCP1, UCP2, UCP3, StUCP and AtUCP. |journal=Biochem. J. |volume=345 Pt 2 |issue= |pages= 161-79 |year= 2000 |pmid= 10620491 |doi= }}
*{{cite journal | author=Muzzin P |title=The uncoupling proteins. |journal=Ann. Endocrinol. (Paris) |volume=63 |issue= 2 Pt 1 |pages= 106-10 |year= 2002 |pmid= 11994670 |doi= }}
*{{cite journal | author=Del Mar Gonzalez-Barroso M, Ricquier D, Cassard-Doulcier AM |title=The human uncoupling protein-1 gene (UCP1): present status and perspectives in obesity research. |journal=Obesity reviews : an official journal of the International Association for the Study of Obesity |volume=1 |issue= 2 |pages= 61-72 |year= 2002 |pmid= 12119988 |doi= }}
*{{cite journal | author=Cassard AM, Bouillaud F, Mattei MG, ''et al.'' |title=Human uncoupling protein gene: structure, comparison with rat gene, and assignment to the long arm of chromosome 4. |journal=J. Cell. Biochem. |volume=43 |issue= 3 |pages= 255-64 |year= 1990 |pmid= 2380264 |doi= 10.1002/jcb.240430306 }}
*{{cite journal | author=Bouillaud F, Villarroya F, Hentz E, ''et al.'' |title=Detection of brown adipose tissue uncoupling protein mRNA in adult patients by a human genomic probe. |journal=Clin. Sci. |volume=75 |issue= 1 |pages= 21-7 |year= 1988 |pmid= 3165741 |doi= }}
*{{cite journal | author=Oppert JM, Vohl MC, Chagnon M, ''et al.'' |title=DNA polymorphism in the uncoupling protein (UCP) gene and human body fat. |journal=Int. J. Obes. Relat. Metab. Disord. |volume=18 |issue= 8 |pages= 526-31 |year= 1994 |pmid= 7951471 |doi= }}
*{{cite journal | author=Clément K, Ruiz J, Cassard-Doulcier AM, ''et al.'' |title=Additive effect of A-->G (-3826) variant of the uncoupling protein gene and the Trp64Arg mutation of the beta 3-adrenergic receptor gene on weight gain in morbid obesity. |journal=Int. J. Obes. Relat. Metab. Disord. |volume=20 |issue= 12 |pages= 1062-6 |year= 1997 |pmid= 8968850 |doi= }}
*{{cite journal | author=Schleiff E, Shore GC, Goping IS |title=Human mitochondrial import receptor, Tom20p. Use of glutathione to reveal specific interactions between Tom20-glutathione S-transferase and mitochondrial precursor proteins. |journal=FEBS Lett. |volume=404 |issue= 2-3 |pages= 314-8 |year= 1997 |pmid= 9119086 |doi= }}
*{{cite journal | author=Urhammer SA, Fridberg M, Sørensen TI, ''et al.'' |title=Studies of genetic variability of the uncoupling protein 1 gene in Caucasian subjects with juvenile-onset obesity. |journal=J. Clin. Endocrinol. Metab. |volume=82 |issue= 12 |pages= 4069-74 |year= 1998 |pmid= 9398715 |doi= }}
*{{cite journal | author=Jezek P, Urbánková E |title=Specific sequence of motifs of mitochondrial uncoupling proteins. |journal=IUBMB Life |volume=49 |issue= 1 |pages= 63-70 |year= 2000 |pmid= 10772343 |doi= }}
*{{cite journal | author=Mori H, Okazawa H, Iwamoto K, ''et al.'' |title=A polymorphism in the 5' untranslated region and a Met229-->Leu variant in exon 5 of the human UCP1 gene are associated with susceptibility to type II diabetes mellitus. |journal=Diabetologia |volume=44 |issue= 3 |pages= 373-6 |year= 2001 |pmid= 11317671 |doi= }}
*{{cite journal | author=Nibbelink M, Moulin K, Arnaud E, ''et al.'' |title=Brown fat UCP1 is specifically expressed in uterine longitudinal smooth muscle cells. |journal=J. Biol. Chem. |volume=276 |issue= 50 |pages= 47291-5 |year= 2002 |pmid= 11572862 |doi= 10.1074/jbc.M105658200 }}
*{{cite journal | author=Echtay KS, Roussel D, St-Pierre J, ''et al.'' |title=Superoxide activates mitochondrial uncoupling proteins. |journal=Nature |volume=415 |issue= 6867 |pages= 96-9 |year= 2002 |pmid= 11780125 |doi= 10.1038/415096a }}
*{{cite journal | author=Rousset S, del Mar Gonzalez-Barroso M, Gelly C, ''et al.'' |title=A new polymorphic site located in the human UCP1 gene controls the in vitro binding of CREB-like factor. |journal=Int. J. Obes. Relat. Metab. Disord. |volume=26 |issue= 5 |pages= 735-8 |year= 2002 |pmid= 12032762 |doi= 10.1038/sj.ijo.0801973 }}
*{{cite journal | author=Rim JS, Kozak LP |title=Regulatory motifs for CREB-binding protein and Nfe2l2 transcription factors in the upstream enhancer of the mitochondrial uncoupling protein 1 gene. |journal=J. Biol. Chem. |volume=277 |issue= 37 |pages= 34589-600 |year= 2002 |pmid= 12084707 |doi= 10.1074/jbc.M108866200 }}
*{{cite journal | author=Kieć-Wilk B, Wybrańska I, Malczewska-Malec M, ''et al.'' |title=Correlation of the -3826A >G polymorphism in the promoter of the uncoupling protein 1 gene with obesity and metabolic disorders in obese families from southern Poland. |journal=J. Physiol. Pharmacol. |volume=53 |issue= 3 |pages= 477-90 |year= 2003 |pmid= 12375583 |doi= }}
*{{cite journal | author=Strausberg RL, Feingold EA, Grouse LH, ''et al.'' |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899-903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899 }}
}}
{{refend}}
{{protein-stub}}
end log.
