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UniProtKB/Swiss-Prot entry O95630


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name STABP_HUMAN
Primary accession number O95630
Secondary accession number Q3MJE7
Integrated into Swiss-Prot on July 19, 2005
Sequence was last modified on May 1, 1999 (Sequence version 1)
Annotations were last modified on    November 25, 2008 (Entry version 59)
Name and origin of the protein
Protein name STAM-binding protein
Synonyms EC 3.1.2.15
Associated molecule with the SH3 domain of STAM
Gene name
Name: STAMBP
Synonyms: AMSH
From
Homo sapiens (Human) [TaxID: 9606] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND INTERACTION WITH STAM1.
TISSUE=Peripheral blood lymphocyte;
DOI=10.1074/jbc.274.27.19129; PubMed=10383417 [NCBI, ExPASy, EBI, Israel, Japan]
Tanaka N., Kaneko K., Asao H., Kasai H., Endo Y., Fujita T., Takeshita T., Sugamura K.;
"Possible involvement of a novel STAM-associated molecule 'AMSH' in intracellular signal transduction mediated by cytokines.";
J. Biol. Chem. 274:19129-19135(1999).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
DOI=10.1038/nature03466; PubMed=15815621 [NCBI, ExPASy, EBI, Israel, Japan]
Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.;
"Generation and annotation of the DNA sequences of human chromosomes 2 and 4.";
Nature 434:724-731(2005).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Brain, Eye, and Lymph;
DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan]
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[4]
FUNCTION, INTERACTION WITH SMAD6 AND SMAD7, SUBCELLULAR LOCATION, AND PHOSPHORYLATION AT SER-2; SER-48; SER-243; SER-245 AND SER-247.
DOI=10.1093/emboj/20.15.4132; PubMed=11483516 [NCBI, ExPASy, EBI, Israel, Japan]
Itoh F., Asao H., Sugamura K., Heldin C.-H., ten Dijke P., Itoh S.;
"Promoting bone morphogenetic protein signaling through negative regulation of inhibitory Smads.";
EMBO J. 20:4132-4142(2001).
[5]
ACTIVE SITE ASP-348, AND ZINC-BINDING SITES GLU-280; HIS-335 AND HIS-337.
PubMed=12370088 [NCBI, ExPASy, EBI, Israel, Japan]
Maytal-Kivity V., Reis N., Hofmann K., Glickman M.H.;
"MPN+, a putative catalytic motif found in a subset of MPN domain proteins from eukaryotes and prokaryotes, is critical for Rpn11 function.";
BMC Biochem. 3:28-28(2002).
[6]
MUTAGENESIS OF ASP-348, FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH STAM1.
DOI=10.1083/jcb.200401141; PubMed=15314065 [NCBI, ExPASy, EBI, Israel, Japan]
McCullough J., Clague M.J., Urbe S.;
"AMSH is an endosome-associated ubiquitin isopeptidase.";
J. Cell Biol. 166:487-492(2004).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
U73522; AAD05037.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AC073046; AAX88908.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC007682; AAH07682.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC065574; AAH65574.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC101467; AAI01468.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC101469; AAI01470.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq NP_006454.1; -.
NP_964010.1; -.
NP_998787.1; -.
UniGene Hs.469018
3D structure databases
ModBase O95630.
Protein-protein interaction databases
IntAct O95630; -.
Protein family/group databases
MEROPS M67.006; -.
PTM databases
PhosphoSite O95630; -.
2D gel databases
REPRODUCTION-2DPAGE IPI00007943; -.
Organism-specific databases
H-InvDB HIX0002171; -.
HGNC HGNC:16950; STAMBP.
GenAtlas STAMBP.
MIM 606247; gene. [NCBI / EBI]
PharmGKB PA134955569; -.
GeneCards O95630.
Gene expression databases
ArrayExpress O95630; -.
CleanEx HS_STAMBP; -.
Ontologies
GO
GO:0005737; Cellular component: cytoplasm (inferred from electronic annotation from UniProtKB-KW).
GO:0016020; Cellular component: membrane (inferred from electronic annotation from UniProtKB-KW).
GO:0005634; Cellular component: nucleus (traceable author statement from ProtInc).
GO:0008237; Molecular function: metallopeptidase activity (inferred from electronic annotation from UniProtKB-KW).
GO:0005515; Molecular function: protein binding (inferred from physical interaction from IntAct).
GO:0004221; Molecular function: ubiquitin thiolesterase activity (inferred from electronic annotation from EC).
GO:0008270; Molecular function: zinc ion binding (inferred from electronic annotation from UniProtKB-KW).
GO:0007259; Biological process: JAK-STAT cascade (traceable author statement from ProtInc).
GO:0008284; Biological process: positive regulation of cell proliferation (traceable author statement from ProtInc).
GO:0006511; Biological process: ubiquitin-dependent protein catabolic process (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.
Family and domain databases
InterPro IPR000555; Mov34_MPN_PAD1.
Graphical view of domain structure.
Pfam PF01398; Mov34; 1.
Pfam graphical view of domain structure.
SMART SM00232; JAB_MPN; 1.
SMART graphical view of domain structure.
ProtoNet O95630.
Proteomic databases
PeptideAtlas O95630; -.
Genome annotation databases
Ensembl ENSG00000124356; Homo sapiens. [Contig view]
GeneID 10617; -.
KEGG hsa:10617; -.
Phylogenomic databases
HOGENOM O95630; -.
HOVERGEN O95630; -.
Other
LinkHub O95630; -.
NextBio 40340; -.
SOURCE STAMBP; Homo sapiens.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Cytoplasm; Hydrolase; Membrane; Metal-binding; Metalloprotease; Nucleus; Phosphoprotein; Protease; Ubl conjugation pathway; Zinc.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
CHAIN   1   424  424     STAM-binding protein. PRO_0000194869
DOMAIN   252   361  110     MPN. 
REGION   227   231  5     Interaction with STAM1. 
COMPBIAS   104   177  74     Glu-rich. 
METAL   280   280        Zinc (By similarity). 
METAL   335   335        Zinc (By similarity). 
METAL   337   337        Zinc (By similarity). 
METAL   348   348        Zinc; catalytic. 
MOD_RES   2     2        Phosphoserine. 
MOD_RES   48    48        Phosphoserine. 
MOD_RES   243   243        Phosphoserine. 
MOD_RES   245   245        Phosphoserine. 
MOD_RES   247   247        Phosphoserine. 
MUTAGEN   348   348        D->A: Promotes accumulation of ubiquitin on endosomes, ablates enzymatic activity toward polyubiquitin substrate and allows ubiquitinated STAM stabilization. 
Sequence information
Length: 424 AA [This is the length of the unprocessed precursor] Molecular weight: 48077 Da [This is the MW of the unprocessed precursor] CRC64: 7B6E08A245BD9D43 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MSDHGDVSLP PEDRVRALSQ LGSAVEVNED IPPRRYFRSG VEIIRMASIY SEEGNIEHAF 

        70         80         90        100        110        120 
ILYNKYITLF IEKLPKHRDY KSAVIPEKKD TVKKLKEIAF PKAEELKAEL LKRYTKEYTE 

       130        140        150        160        170        180 
YNEEKKKEAE ELARNMAIQQ ELEKEKQRVA QQKQQQLEQE QFHAFEEMIR NQELEKERLK 

       190        200        210        220        230        240 
IVQEFGKVDP GLGGPLVPDL EKPSLDVFPT LTVSSIQPSD CHTTVRPAKP PVVDRSLKPG 

       250        260        270        280        290        300 
ALSNSESIPT IDGLRHVVVP GRLCPQFLQL ASANTARGVE TCGILCGKLM RNEFTITHVL 

       310        320        330        340        350        360 
IPKQSAGSDY CNTENEEELF LIQDQQGLIT LGWIHTHPTQ TAFLSSVDLH THCSYQMMLP 

       370        380        390        400        410        420 
ESVAIVCSPK FQETGFFKLT DHGLEEISSC RQKGFHPHSK DPPLFCSCSH VTVVDRAVTI 


TDLR 

O95630 in FASTA format

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