STABP_HUMAN
ID STABP_HUMAN Reviewed; 424 AA.
AC O95630; B5M0B6; D6W5H7; Q3MJE7;
DT 19-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 185.
DE RecName: Full=STAM-binding protein;
DE EC=3.4.19.- {ECO:0000269|PubMed:15314065, ECO:0000269|PubMed:23542699, ECO:0000269|PubMed:34425109};
DE AltName: Full=Associated molecule with the SH3 domain of STAM {ECO:0000303|PubMed:10383417};
DE AltName: Full=Endosome-associated ubiquitin isopeptidase {ECO:0000303|PubMed:15314065};
GN Name=STAMBP; Synonyms=AMSH {ECO:0000303|PubMed:10383417};
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, TISSUE SPECIFICITY, AND
RP INTERACTION WITH STAM.
RC TISSUE=Peripheral blood lymphocyte;
RX PubMed=10383417; DOI=10.1074/jbc.274.27.19129;
RA Tanaka N., Kaneko K., Asao H., Kasai H., Endo Y., Fujita T., Takeshita T.,
RA Sugamura K.;
RT "Possible involvement of a novel STAM-associated molecule 'AMSH' in
RT intracellular signal transduction mediated by cytokines.";
RL J. Biol. Chem. 274:19129-19135(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT 4.";
RL Nature 434:724-731(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain, Eye, and Lymph;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 3-346 (ISOFORM 2).
RX PubMed=19906316; DOI=10.1186/1471-2164-10-518;
RA Wang P., Yu P., Gao P., Shi T., Ma D.;
RT "Discovery of novel human transcript variants by analysis of intronic
RT single-block EST with polyadenylation site.";
RL BMC Genomics 10:518-518(2009).
RN [6]
RP FUNCTION, INTERACTION WITH SMAD6 AND SMAD7, SUBCELLULAR LOCATION, AND
RP PHOSPHORYLATION AT SER-2; SER-48; SER-243; SER-245 AND SER-247.
RX PubMed=11483516; DOI=10.1093/emboj/20.15.4132;
RA Itoh F., Asao H., Sugamura K., Heldin C.-H., ten Dijke P., Itoh S.;
RT "Promoting bone morphogenetic protein signaling through negative regulation
RT of inhibitory Smads.";
RL EMBO J. 20:4132-4142(2001).
RN [7]
RP INVOLVEMENT OF GLU-280; HIS-335 AND HIS-337 IN ZINC-BINDING.
RX PubMed=12370088; DOI=10.1186/1471-2091-3-28;
RA Maytal-Kivity V., Reis N., Hofmann K., Glickman M.H.;
RT "MPN+, a putative catalytic motif found in a subset of MPN domain proteins
RT from eukaryotes and prokaryotes, is critical for Rpn11 function.";
RL BMC Biochem. 3:28-28(2002).
RN [8]
RP MUTAGENESIS OF ASP-348, FUNCTION, ACTIVITY REGULATION, SUBCELLULAR
RP LOCATION, AND INTERACTION WITH STAM.
RX PubMed=15314065; DOI=10.1083/jcb.200401141;
RA McCullough J., Clague M.J., Urbe S.;
RT "AMSH is an endosome-associated ubiquitin isopeptidase.";
RL J. Cell Biol. 166:487-492(2004).
RN [9]
RP INTERACTION WITH SMURF2 AND RNF11, AND UBIQUITINATION.
RX PubMed=14755250; DOI=10.1038/sj.onc.1207319;
RA Li H., Seth A.K.;
RT "An RNF11: Smurf2 complex mediates ubiquitination of the AMSH protein.";
RL Oncogene 23:1801-1808(2004).
RN [10]
RP INTERACTION WITH CHMP3.
RX PubMed=17146056; DOI=10.1073/pnas.0603788103;
RA Zamborlini A., Usami Y., Radoshitzky S.R., Popova E., Palu G.,
RA Goettlinger H.;
RT "Release of autoinhibition converts ESCRT-III components into potent
RT inhibitors of HIV-1 budding.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:19140-19145(2006).
RN [11]
RP FUNCTION, INTERACTION WITH CHMP3, AND SUBCELLULAR LOCATION.
RX PubMed=17261583; DOI=10.1074/jbc.m611635200;
RA Ma Y.M., Boucrot E., Villen J., Affar el B., Gygi S.P., Goettlinger H.G.,
RA Kirchhausen T.;
RT "Targeting of AMSH to endosomes is required for epidermal growth factor
RT receptor degradation.";
RL J. Biol. Chem. 282:9805-9812(2007).
RN [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2; SER-243 AND SER-247, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [14]
RP FUNCTION, AND VARIANTS MICCAP PRO-14; CYS-38; GLY-42; CYS-63; TYR-100 AND
RP ILE-313.
RX PubMed=23542699; DOI=10.1038/ng.2602;
RG FORGE Canada Consortium;
RA McDonell L.M., Mirzaa G.M., Alcantara D., Schwartzentruber J., Carter M.T.,
RA Lee L.J., Clericuzio C.L., Graham J.M. Jr., Morris-Rosendahl D.J.,
RA Polster T., Acsadi G., Townshend S., Williams S., Halbert A., Isidor B.,
RA David A., Smyser C.D., Paciorkowski A.R., Willing M., Woulfe J., Das S.,
RA Beaulieu C.L., Marcadier J., Geraghty M.T., Frey B.J., Majewski J.,
RA Bulman D.E., Dobyns W.B., O'Driscoll M., Boycott K.M.;
RT "Mutations in STAMBP, encoding a deubiquitinating enzyme, cause
RT microcephaly-capillary malformation syndrome.";
RL Nat. Genet. 45:556-562(2013).
RN [15]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [16]
RP FUNCTION, AND ACTIVITY REGULATION.
RX PubMed=34425109; DOI=10.1016/j.jbc.2021.101107;
RA Guo Y., Liu Q., Mallette E., Caba C., Hou F., Fux J., LaPlante G., Dong A.,
RA Zhang Q., Zheng H., Tong Y., Zhang W.;
RT "Structural and functional characterization of ubiquitin variant inhibitors
RT for the JAMM-family deubiquitinases STAMBP and STAMBPL1.";
RL J. Biol. Chem. 297:101107-101107(2021).
CC -!- FUNCTION: Zinc metalloprotease that specifically cleaves 'Lys-63'-
CC linked polyubiquitin chains (PubMed:15314065, PubMed:23542699,
CC PubMed:34425109). Does not cleave 'Lys-48'-linked polyubiquitin chains
CC (PubMed:15314065). Plays a role in signal transduction for cell growth
CC and MYC induction mediated by IL-2 and GM-CSF (PubMed:10383417).
CC Potentiates BMP (bone morphogenetic protein) signaling by antagonizing
CC the inhibitory action of SMAD6 and SMAD7 (PubMed:11483516). Has a key
CC role in regulation of cell surface receptor-mediated endocytosis and
CC ubiquitin-dependent sorting of receptors to lysosomes (PubMed:15314065,
CC PubMed:17261583). Endosomal localization of STAMBP is required for
CC efficient EGFR degradation but not for its internalization
CC (PubMed:15314065, PubMed:17261583). Involved in the negative regulation
CC of PI3K-AKT-mTOR and RAS-MAP signaling pathways (PubMed:23542699).
CC {ECO:0000269|PubMed:10383417, ECO:0000269|PubMed:11483516,
CC ECO:0000269|PubMed:15314065, ECO:0000269|PubMed:17261583,
CC ECO:0000269|PubMed:23542699, ECO:0000269|PubMed:34425109}.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000250|UniProtKB:O35864};
CC Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000250|UniProtKB:O35864};
CC -!- ACTIVITY REGULATION: Inhibited by N-ethylmaleimide (PubMed:15314065).
CC Strongly and specifically inhibited by ubiquitin variants UbV(SP.2) and
CC UbV(SP.3) (PubMed:34425109). Also inhibited by UbV(SP.1); an ubiquitin
CC variant that also inhibits STAMBPL1 (PubMed:34425109).
CC {ECO:0000269|PubMed:15314065, ECO:0000269|PubMed:34425109}.
CC -!- SUBUNIT: Interacts with STAM (PubMed:10383417, PubMed:15314065).
CC Interacts with SMAD6 and SMAD7 (PubMed:11483516). Interacts with CHMP3;
CC the interaction appears to relieve the autoinhibition of CHMP3
CC (PubMed:17146056, PubMed:17261583). Interacts with SMURF2 and RNF11;
CC this interaction promotes ubiquitination (PubMed:14755250).
CC {ECO:0000269|PubMed:10383417, ECO:0000269|PubMed:11483516,
CC ECO:0000269|PubMed:14755250, ECO:0000269|PubMed:15314065,
CC ECO:0000269|PubMed:17146056, ECO:0000269|PubMed:17261583}.
CC -!- INTERACTION:
CC O95630; P31941: APOBEC3A; NbExp=3; IntAct=EBI-396676, EBI-13050366;
CC O95630; P54253: ATXN1; NbExp=6; IntAct=EBI-396676, EBI-930964;
CC O95630; P48643: CCT5; NbExp=3; IntAct=EBI-396676, EBI-355710;
CC O95630; Q9HD42: CHMP1A; NbExp=7; IntAct=EBI-396676, EBI-1057156;
CC O95630; Q7LBR1: CHMP1B; NbExp=21; IntAct=EBI-396676, EBI-2118090;
CC O95630; Q9Y3E7: CHMP3; NbExp=26; IntAct=EBI-396676, EBI-2118119;
CC O95630; Q9Y3E7-1: CHMP3; NbExp=6; IntAct=EBI-396676, EBI-15613847;
CC O95630; Q9H444: CHMP4B; NbExp=3; IntAct=EBI-396676, EBI-749627;
CC O95630; Q9NZZ3: CHMP5; NbExp=2; IntAct=EBI-396676, EBI-751303;
CC O95630; O75791: GRAP2; NbExp=4; IntAct=EBI-396676, EBI-740418;
CC O95630; P62993: GRB2; NbExp=9; IntAct=EBI-396676, EBI-401755;
CC O95630; Q8WXH2: JPH3; NbExp=3; IntAct=EBI-396676, EBI-1055254;
CC O95630; O60260-5: PRKN; NbExp=3; IntAct=EBI-396676, EBI-21251460;
CC O95630; Q9Y3C5: RNF11; NbExp=5; IntAct=EBI-396676, EBI-396669;
CC O95630; O43541-2: SMAD6; NbExp=2; IntAct=EBI-396676, EBI-4324970;
CC O95630; Q92783: STAM; NbExp=7; IntAct=EBI-396676, EBI-752333;
CC O95630; O75886: STAM2; NbExp=9; IntAct=EBI-396676, EBI-373258;
CC O95630; Q13148: TARDBP; NbExp=3; IntAct=EBI-396676, EBI-372899;
CC O95630; Q15645: TRIP13; NbExp=4; IntAct=EBI-396676, EBI-358993;
CC O95630; P0CG47: UBB; NbExp=4; IntAct=EBI-396676, EBI-413034;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:17261583,
CC ECO:0000305|PubMed:10383417}. Membrane {ECO:0000269|PubMed:17261583};
CC Peripheral membrane protein {ECO:0000269|PubMed:17261583}. Cytoplasm
CC {ECO:0000269|PubMed:17261583}. Early endosome
CC {ECO:0000269|PubMed:15314065, ECO:0000269|PubMed:17261583}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=O95630-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O95630-2; Sequence=VSP_057197;
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed.
CC {ECO:0000269|PubMed:10383417}.
CC -!- DOMAIN: The JAMM motif is essential for the protease activity.
CC {ECO:0000250|UniProtKB:O35864}.
CC -!- PTM: Phosphorylated after BMP type I receptor activation.
CC {ECO:0000269|PubMed:11483516}.
CC -!- PTM: Ubiquitinated by SMURF2 in the presence of RNF11.
CC {ECO:0000269|PubMed:14755250}.
CC -!- DISEASE: Microcephaly-capillary malformation syndrome (MICCAP)
CC [MIM:614261]: A congenital disorder characterized by severe progressive
CC microcephaly, early-onset refractory epilepsy, profound developmental
CC delay, and multiple small capillary malformations spread diffusely on
CC the body. Additional more variable features include dysmorphic facial
CC features, distal limb abnormalities, and mild heart defects.
CC {ECO:0000269|PubMed:23542699}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- MISCELLANEOUS: X-ray crystallography studies of STAMBPL1, another
CC member of the peptidase M67C family, has shown that Glu-280 binds zinc
CC indirectly via a water molecule. Nevertheless, this residue is
CC essential for catalytic activity. {ECO:0000250|UniProtKB:Q96FJ0}.
CC -!- SIMILARITY: Belongs to the peptidase M67C family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; U73522; AAD05037.1; -; mRNA.
DR EMBL; AC073046; AAX88908.1; -; Genomic_DNA.
DR EMBL; CH471053; EAW99715.1; -; Genomic_DNA.
DR EMBL; CH471053; EAW99716.1; -; Genomic_DNA.
DR EMBL; BC007682; AAH07682.1; -; mRNA.
DR EMBL; BC065574; AAH65574.1; -; mRNA.
DR EMBL; BC101467; AAI01468.1; -; mRNA.
DR EMBL; BC101469; AAI01470.1; -; mRNA.
DR EMBL; EU927390; ACH57452.1; -; mRNA.
DR CCDS; CCDS1929.1; -. [O95630-1]
DR RefSeq; NP_006454.1; NM_006463.4. [O95630-1]
DR RefSeq; NP_964010.1; NM_201647.2. [O95630-1]
DR RefSeq; NP_998787.1; NM_213622.2. [O95630-1]
DR RefSeq; XP_005264145.1; XM_005264088.3.
DR RefSeq; XP_011530785.1; XM_011532483.2. [O95630-1]
DR RefSeq; XP_016858664.1; XM_017003175.1.
DR PDB; 2XZE; X-ray; 1.75 A; A/B=1-146.
DR PDB; 3RZU; X-ray; 2.50 A; A/B/C/D/E/F/G=243-424.
DR PDB; 3RZV; X-ray; 1.67 A; A=219-424.
DR PDB; 5IXF; NMR; -; B=228-241.
DR PDBsum; 2XZE; -.
DR PDBsum; 3RZU; -.
DR PDBsum; 3RZV; -.
DR PDBsum; 5IXF; -.
DR AlphaFoldDB; O95630; -.
DR SMR; O95630; -.
DR BioGRID; 115863; 92.
DR CORUM; O95630; -.
DR DIP; DIP-33062N; -.
DR IntAct; O95630; 59.
DR MINT; O95630; -.
DR STRING; 9606.ENSP00000377633; -.
DR BindingDB; O95630; -.
DR ChEMBL; CHEMBL4105848; -.
DR MEROPS; M67.006; -.
DR GlyGen; O95630; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; O95630; -.
DR MetOSite; O95630; -.
DR PhosphoSitePlus; O95630; -.
DR BioMuta; STAMBP; -.
DR REPRODUCTION-2DPAGE; IPI00007943; -.
DR EPD; O95630; -.
DR jPOST; O95630; -.
DR MassIVE; O95630; -.
DR MaxQB; O95630; -.
DR PaxDb; O95630; -.
DR PeptideAtlas; O95630; -.
DR PRIDE; O95630; -.
DR ProteomicsDB; 50966; -. [O95630-1]
DR Antibodypedia; 31376; 307 antibodies from 35 providers.
DR DNASU; 10617; -.
DR Ensembl; ENST00000339566.7; ENSP00000344742.3; ENSG00000124356.17. [O95630-1]
DR Ensembl; ENST00000394070.7; ENSP00000377633.2; ENSG00000124356.17. [O95630-1]
DR Ensembl; ENST00000394073.6; ENSP00000377636.1; ENSG00000124356.17. [O95630-1]
DR Ensembl; ENST00000409707.6; ENSP00000386548.1; ENSG00000124356.17. [O95630-1]
DR Ensembl; ENST00000432295.7; ENSP00000413874.3; ENSG00000124356.17. [O95630-2]
DR Ensembl; ENST00000682351.1; ENSP00000506833.1; ENSG00000124356.17. [O95630-1]
DR Ensembl; ENST00000682379.1; ENSP00000507081.1; ENSG00000124356.17. [O95630-1]
DR Ensembl; ENST00000682558.1; ENSP00000507014.1; ENSG00000124356.17. [O95630-1]
DR Ensembl; ENST00000682847.1; ENSP00000507864.1; ENSG00000124356.17. [O95630-1]
DR Ensembl; ENST00000683036.1; ENSP00000507639.1; ENSG00000124356.17. [O95630-1]
DR Ensembl; ENST00000683317.1; ENSP00000507092.1; ENSG00000124356.17. [O95630-1]
DR Ensembl; ENST00000683518.1; ENSP00000506865.1; ENSG00000124356.17. [O95630-1]
DR Ensembl; ENST00000683818.1; ENSP00000507658.1; ENSG00000124356.17. [O95630-1]
DR Ensembl; ENST00000684095.1; ENSP00000506845.1; ENSG00000124356.17. [O95630-1]
DR Ensembl; ENST00000684312.1; ENSP00000506958.1; ENSG00000124356.17. [O95630-1]
DR Ensembl; ENST00000684585.1; ENSP00000507054.1; ENSG00000124356.17. [O95630-1]
DR GeneID; 10617; -.
DR KEGG; hsa:10617; -.
DR MANE-Select; ENST00000394070.7; ENSP00000377633.2; NM_213622.4; NP_998787.1.
DR UCSC; uc002sjs.3; human. [O95630-1]
DR CTD; 10617; -.
DR DisGeNET; 10617; -.
DR GeneCards; STAMBP; -.
DR GeneReviews; STAMBP; -.
DR HGNC; HGNC:16950; STAMBP.
DR HPA; ENSG00000124356; Low tissue specificity.
DR MalaCards; STAMBP; -.
DR MIM; 606247; gene.
DR MIM; 614261; phenotype.
DR neXtProt; NX_O95630; -.
DR OpenTargets; ENSG00000124356; -.
DR Orphanet; 294016; Microcephaly-capillary malformation syndrome.
DR PharmGKB; PA134955569; -.
DR VEuPathDB; HostDB:ENSG00000124356; -.
DR eggNOG; KOG2880; Eukaryota.
DR GeneTree; ENSGT00940000153710; -.
DR HOGENOM; CLU_023304_0_1_1; -.
DR InParanoid; O95630; -.
DR OMA; PEYAINT; -.
DR OrthoDB; 411229at2759; -.
DR PhylomeDB; O95630; -.
DR TreeFam; TF323215; -.
DR PathwayCommons; O95630; -.
DR Reactome; R-HSA-5689901; Metalloprotease DUBs.
DR SignaLink; O95630; -.
DR SIGNOR; O95630; -.
DR BioGRID-ORCS; 10617; 125 hits in 1125 CRISPR screens.
DR ChiTaRS; STAMBP; human.
DR GeneWiki; STAMBP; -.
DR GenomeRNAi; 10617; -.
DR Pharos; O95630; Tchem.
DR PRO; PR:O95630; -.
DR Proteomes; UP000005640; Chromosome 2.
DR RNAct; O95630; protein.
DR Bgee; ENSG00000124356; Expressed in C1 segment of cervical spinal cord and 214 other tissues.
DR ExpressionAtlas; O95630; baseline and differential.
DR Genevisible; O95630; HS.
DR GO; GO:0032154; C:cleavage furrow; IDA:MGI.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0005769; C:early endosome; IEA:UniProtKB-SubCell.
DR GO; GO:0005768; C:endosome; IBA:GO_Central.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; TAS:ProtInc.
DR GO; GO:0005886; C:plasma membrane; IDA:HPA.
DR GO; GO:0101005; F:deubiquitinase activity; IDA:MGI.
DR GO; GO:0070122; F:isopeptidase activity; IEA:InterPro.
DR GO; GO:0061578; F:Lys63-specific deubiquitinase activity; IDA:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0140492; F:metal-dependent deubiquitinase activity; IEA:InterPro.
DR GO; GO:0019904; F:protein domain specific binding; IPI:UniProtKB.
DR GO; GO:0110088; P:hippocampal neuron apoptotic process; IEA:Ensembl.
DR GO; GO:0000281; P:mitotic cytokinesis; IMP:MGI.
DR GO; GO:0110091; P:negative regulation of hippocampal neuron apoptotic process; IEA:Ensembl.
DR GO; GO:0014067; P:negative regulation of phosphatidylinositol 3-kinase signaling; IMP:UniProtKB.
DR GO; GO:0046580; P:negative regulation of Ras protein signal transduction; IMP:UniProtKB.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; TAS:ProtInc.
DR GO; GO:0016579; P:protein deubiquitination; IMP:MGI.
DR GO; GO:0070536; P:protein K63-linked deubiquitination; IBA:GO_Central.
DR GO; GO:0007259; P:receptor signaling pathway via JAK-STAT; TAS:ProtInc.
DR CDD; cd08066; MPN_AMSH_like; 1.
DR DisProt; DP01872; -.
DR IDEAL; IID00261; -.
DR InterPro; IPR000555; JAMM/MPN+_dom.
DR InterPro; IPR037518; MPN.
DR InterPro; IPR044098; STAMBP/STALP-like_MPN.
DR InterPro; IPR015063; USP8_dimer.
DR Pfam; PF01398; JAB; 1.
DR Pfam; PF08969; USP8_dimer; 1.
DR SMART; SM00232; JAB_MPN; 1.
DR PROSITE; PS50249; MPN; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cytoplasm; Disease variant; Endosome;
KW Hydrolase; Membrane; Metal-binding; Metalloprotease; Nucleus;
KW Phosphoprotein; Protease; Reference proteome; Ubl conjugation;
KW Ubl conjugation pathway; Zinc.
FT CHAIN 1..424
FT /note="STAM-binding protein"
FT /id="PRO_0000194869"
FT DOMAIN 257..388
FT /note="MPN"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01182"
FT REGION 1..127
FT /note="Interaction with CHMP3"
FT /evidence="ECO:0000269|PubMed:17146056"
FT REGION 227..231
FT /note="Interaction with STAM"
FT /evidence="ECO:0000269|PubMed:10383417"
FT MOTIF 335..348
FT /note="JAMM motif"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01182"
FT BINDING 335
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01182"
FT BINDING 337
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01182"
FT BINDING 348
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01182"
FT BINDING 350
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q96FJ0"
FT BINDING 390
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q96FJ0"
FT BINDING 396
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q96FJ0"
FT BINDING 398
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q96FJ0"
FT SITE 280
FT /note="Indirect zinc-binding"
FT /evidence="ECO:0000250|UniProtKB:Q96FJ0"
FT MOD_RES 2
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:11483516,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 48
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:11483516"
FT MOD_RES 243
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:11483516,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 245
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:11483516"
FT MOD_RES 247
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:11483516,
FT ECO:0007744|PubMed:23186163"
FT VAR_SEQ 336..424
FT /note="THPTQTAFLSSVDLHTHCSYQMMLPESVAIVCSPKFQETGFFKLTDHGLEEI
FT SSCRQKGFHPHSKDPPLFCSCSHVTVVDRAVTITDLR -> VETLWSLKSLHAP (in
FT isoform 2)"
FT /evidence="ECO:0000303|PubMed:19906316"
FT /id="VSP_057197"
FT VARIANT 14
FT /note="R -> P (in MICCAP)"
FT /evidence="ECO:0000269|PubMed:23542699"
FT /id="VAR_069806"
FT VARIANT 38
FT /note="R -> C (in MICCAP; dbSNP:rs143739249)"
FT /evidence="ECO:0000269|PubMed:23542699"
FT /id="VAR_069807"
FT VARIANT 42
FT /note="E -> G (in MICCAP; dbSNP:rs397509387)"
FT /evidence="ECO:0000269|PubMed:23542699"
FT /id="VAR_069808"
FT VARIANT 63
FT /note="Y -> C (in MICCAP; dbSNP:rs781694797)"
FT /evidence="ECO:0000269|PubMed:23542699"
FT /id="VAR_069809"
FT VARIANT 100
FT /note="F -> Y (in MICCAP; dbSNP:rs397514697)"
FT /evidence="ECO:0000269|PubMed:23542699"
FT /id="VAR_069810"
FT VARIANT 313
FT /note="T -> I (in MICCAP; dbSNP:rs202100019)"
FT /evidence="ECO:0000269|PubMed:23542699"
FT /id="VAR_069811"
FT MUTAGEN 348
FT /note="D->A: Promotes accumulation of ubiquitin on
FT endosomes, ablates enzymatic activity toward polyubiquitin
FT substrate and allows ubiquitinated STAM stabilization."
FT /evidence="ECO:0000269|PubMed:15314065"
FT HELIX 11..22
FT /evidence="ECO:0007829|PDB:2XZE"
FT HELIX 33..53
FT /evidence="ECO:0007829|PDB:2XZE"
FT HELIX 56..71
FT /evidence="ECO:0007829|PDB:2XZE"
FT HELIX 74..76
FT /evidence="ECO:0007829|PDB:2XZE"
FT TURN 78..82
FT /evidence="ECO:0007829|PDB:2XZE"
FT HELIX 88..97
FT /evidence="ECO:0007829|PDB:2XZE"
FT HELIX 99..137
FT /evidence="ECO:0007829|PDB:2XZE"
FT STRAND 257..260
FT /evidence="ECO:0007829|PDB:3RZV"
FT HELIX 263..276
FT /evidence="ECO:0007829|PDB:3RZV"
FT STRAND 282..290
FT /evidence="ECO:0007829|PDB:3RZV"
FT STRAND 293..301
FT /evidence="ECO:0007829|PDB:3RZV"
FT STRAND 304..306
FT /evidence="ECO:0007829|PDB:3RZV"
FT STRAND 311..313
FT /evidence="ECO:0007829|PDB:3RZV"
FT HELIX 316..326
FT /evidence="ECO:0007829|PDB:3RZV"
FT STRAND 329..336
FT /evidence="ECO:0007829|PDB:3RZV"
FT STRAND 338..340
FT /evidence="ECO:0007829|PDB:3RZU"
FT HELIX 346..358
FT /evidence="ECO:0007829|PDB:3RZV"
FT STRAND 363..368
FT /evidence="ECO:0007829|PDB:3RZV"
FT TURN 369..372
FT /evidence="ECO:0007829|PDB:3RZV"
FT STRAND 373..379
FT /evidence="ECO:0007829|PDB:3RZV"
FT HELIX 381..389
FT /evidence="ECO:0007829|PDB:3RZV"
FT STRAND 404..407
FT /evidence="ECO:0007829|PDB:3RZV"
FT STRAND 409..414
FT /evidence="ECO:0007829|PDB:3RZV"
FT STRAND 419..422
FT /evidence="ECO:0007829|PDB:3RZV"
SQ SEQUENCE 424 AA; 48077 MW; 7B6E08A245BD9D43 CRC64;
MSDHGDVSLP PEDRVRALSQ LGSAVEVNED IPPRRYFRSG VEIIRMASIY SEEGNIEHAF
ILYNKYITLF IEKLPKHRDY KSAVIPEKKD TVKKLKEIAF PKAEELKAEL LKRYTKEYTE
YNEEKKKEAE ELARNMAIQQ ELEKEKQRVA QQKQQQLEQE QFHAFEEMIR NQELEKERLK
IVQEFGKVDP GLGGPLVPDL EKPSLDVFPT LTVSSIQPSD CHTTVRPAKP PVVDRSLKPG
ALSNSESIPT IDGLRHVVVP GRLCPQFLQL ASANTARGVE TCGILCGKLM RNEFTITHVL
IPKQSAGSDY CNTENEEELF LIQDQQGLIT LGWIHTHPTQ TAFLSSVDLH THCSYQMMLP
ESVAIVCSPK FQETGFFKLT DHGLEEISSC RQKGFHPHSK DPPLFCSCSH VTVVDRAVTI
TDLR
