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STAM-binding protein (EC 3.4.19.-) (Associated molecule with the SH3 domain of STAM) (Endosome-associated ubiquitin isopeptidase)

 STABP_HUMAN             Reviewed;         424 AA.
O95630; B5M0B6; D6W5H7; Q3MJE7;
19-JUL-2005, integrated into UniProtKB/Swiss-Prot.
01-MAY-1999, sequence version 1.
20-DEC-2017, entry version 154.
RecName: Full=STAM-binding protein;
EC=3.4.19.-;
AltName: Full=Associated molecule with the SH3 domain of STAM;
AltName: Full=Endosome-associated ubiquitin isopeptidase;
Name=STAMBP; Synonyms=AMSH;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, AND INTERACTION WITH
STAM.
TISSUE=Peripheral blood lymphocyte;
PubMed=10383417; DOI=10.1074/jbc.274.27.19129;
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].
PubMed=15815621; DOI=10.1038/nature03466;
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 GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Brain, Eye, and Lymph;
PubMed=15489334; DOI=10.1101/gr.2596504;
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).
[5]
NUCLEOTIDE SEQUENCE [MRNA] OF 3-346 (ISOFORM 2).
PubMed=19906316; DOI=10.1186/1471-2164-10-518;
Wang P., Yu P., Gao P., Shi T., Ma D.;
"Discovery of novel human transcript variants by analysis of intronic
single-block EST with polyadenylation site.";
BMC Genomics 10:518-518(2009).
[6]
FUNCTION, INTERACTION WITH SMAD6 AND SMAD7, SUBCELLULAR LOCATION, AND
PHOSPHORYLATION AT SER-2; SER-48; SER-243; SER-245 AND SER-247.
PubMed=11483516; DOI=10.1093/emboj/20.15.4132;
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).
[7]
INVOLVEMENT OF GLU-280; HIS-335 AND HIS-337 IN ZINC-BINDING.
PubMed=12370088; DOI=10.1186/1471-2091-3-28;
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).
[8]
MUTAGENESIS OF ASP-348, FUNCTION, SUBCELLULAR LOCATION, AND
INTERACTION WITH STAM.
PubMed=15314065; DOI=10.1083/jcb.200401141;
McCullough J., Clague M.J., Urbe S.;
"AMSH is an endosome-associated ubiquitin isopeptidase.";
J. Cell Biol. 166:487-492(2004).
[9]
INTERACTION WITH SMURF2 AND RNF11, AND UBIQUITINATION.
PubMed=14755250; DOI=10.1038/sj.onc.1207319;
Li H., Seth A.K.;
"An RNF11: Smurf2 complex mediates ubiquitination of the AMSH
protein.";
Oncogene 23:1801-1808(2004).
[10]
INTERACTION WITH CHMP3.
PubMed=17146056; DOI=10.1073/pnas.0603788103;
Zamborlini A., Usami Y., Radoshitzky S.R., Popova E., Palu G.,
Goettlinger H.;
"Release of autoinhibition converts ESCRT-III components into potent
inhibitors of HIV-1 budding.";
Proc. Natl. Acad. Sci. U.S.A. 103:19140-19145(2006).
[11]
FUNCTION, INTERACTION WITH CHMP3, AND SUBCELLULAR LOCATION.
PubMed=17261583; DOI=10.1074/jbc.M611635200;
Ma Y.M., Boucrot E., Villen J., Affar el B., Gygi S.P.,
Goettlinger H.G., Kirchhausen T.;
"Targeting of AMSH to endosomes is required for epidermal growth
factor receptor degradation.";
J. Biol. Chem. 282:9805-9812(2007).
[12]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[13]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2; SER-243 AND SER-247,
AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[14]
FUNCTION, AND VARIANTS MICCAP PRO-14; CYS-38; GLY-42; CYS-63; TYR-100
AND ILE-313.
PubMed=23542699; DOI=10.1038/ng.2602;
FORGE Canada Consortium;
McDonell L.M., Mirzaa G.M., Alcantara D., Schwartzentruber J.,
Carter M.T., Lee L.J., Clericuzio C.L., Graham J.M. Jr.,
Morris-Rosendahl D.J., Polster T., Acsadi G., Townshend S.,
Williams S., Halbert A., Isidor B., David A., Smyser C.D.,
Paciorkowski A.R., Willing M., Woulfe J., Das S., Beaulieu C.L.,
Marcadier J., Geraghty M.T., Frey B.J., Majewski J., Bulman D.E.,
Dobyns W.B., O'Driscoll M., Boycott K.M.;
"Mutations in STAMBP, encoding a deubiquitinating enzyme, cause
microcephaly-capillary malformation syndrome.";
Nat. Genet. 45:556-562(2013).
[15]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
-!- FUNCTION: Zinc metalloprotease that specifically cleaves 'Lys-63'-
linked polyubiquitin chains. Does not cleave 'Lys-48'-linked
polyubiquitin chains (By similarity). Plays a role in signal
transduction for cell growth and MYC induction mediated by IL-2
and GM-CSF. Potentiates BMP (bone morphogenetic protein) signaling
by antagonizing the inhibitory action of SMAD6 and SMAD7. Has a
key role in regulation of cell surface receptor-mediated
endocytosis and ubiquitin-dependent sorting of receptors to
lysosomes. Endosomal localization of STAMBP is required for
efficient EGFR degradation but not for its internalization (By
similarity). Involved in the negative regulation of PI3K-AKT-mTOR
and RAS-MAP signaling pathways. {ECO:0000250,
ECO:0000269|PubMed:10383417, ECO:0000269|PubMed:11483516,
ECO:0000269|PubMed:15314065, ECO:0000269|PubMed:17261583,
ECO:0000269|PubMed:23542699}.
-!- COFACTOR:
Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000250};
-!- ENZYME REGULATION: Inhibited by N-ethylmaleimide.
-!- SUBUNIT: Interacts with STAM. Interacts with SMAD6 and SMAD7.
Interacts with CHMP3; the interaction appears to relieve the
autoinhibition of CHMP3. Interacts with SMURF2 and RNF11; this
interaction promotes ubiquitination. {ECO:0000269|PubMed:10383417,
ECO:0000269|PubMed:11483516, ECO:0000269|PubMed:14755250,
ECO:0000269|PubMed:15314065, ECO:0000269|PubMed:17146056,
ECO:0000269|PubMed:17261583}.
-!- INTERACTION:
P31941:APOBEC3A; NbExp=4; IntAct=EBI-396676, EBI-13050366;
Q9HD42:CHMP1A; NbExp=6; IntAct=EBI-396676, EBI-1057156;
Q7LBR1:CHMP1B; NbExp=19; IntAct=EBI-396676, EBI-2118090;
Q9Y3E7:CHMP3; NbExp=19; IntAct=EBI-396676, EBI-2118119;
Q9Y3E7-1:CHMP3; NbExp=6; IntAct=EBI-396676, EBI-15613847;
Q9H444:CHMP4B; NbExp=3; IntAct=EBI-396676, EBI-749627;
Q9NZZ3:CHMP5; NbExp=2; IntAct=EBI-396676, EBI-751303;
P62993:GRB2; NbExp=9; IntAct=EBI-396676, EBI-401755;
Q9Y3C5:RNF11; NbExp=2; IntAct=EBI-396676, EBI-396669;
O43541-2:SMAD6; NbExp=2; IntAct=EBI-396676, EBI-4324970;
Q92783:STAM; NbExp=7; IntAct=EBI-396676, EBI-752333;
O75886:STAM2; NbExp=4; IntAct=EBI-396676, EBI-373258;
-!- SUBCELLULAR LOCATION: Nucleus. Membrane; Peripheral membrane
protein. Cytoplasm. Early endosome.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=O95630-1; Sequence=Displayed;
Name=2;
IsoId=O95630-2; Sequence=VSP_057197;
-!- TISSUE SPECIFICITY: Ubiquitously expressed.
-!- DOMAIN: The JAMM motif is essential for the protease activity.
{ECO:0000250}.
-!- PTM: Phosphorylated after BMP type I receptor activation.
{ECO:0000269|PubMed:11483516}.
-!- PTM: Ubiquitinated by SMURF2 in the presence of RNF11.
{ECO:0000269|PubMed:14755250}.
-!- DISEASE: Microcephaly-capillary malformation syndrome (MICCAP)
[MIM:614261]: A congenital disorder characterized by severe
progressive microcephaly, early-onset refractory epilepsy,
profound developmental delay, and multiple small capillary
malformations spread diffusely on the body. Additional more
variable features include dysmorphic facial features, distal limb
abnormalities, and mild heart defects.
{ECO:0000269|PubMed:23542699}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- MISCELLANEOUS: X-ray crystallography studies of STAMBPL1, another
member of the peptidase M67C family, has shown that Glu-280 binds
zinc indirectly via a water molecule. Nevertheless, this residue
is essential for catalytic activity.
-!- SIMILARITY: Belongs to the peptidase M67C family. {ECO:0000305}.
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EMBL; U73522; AAD05037.1; -; mRNA.
EMBL; AC073046; AAX88908.1; -; Genomic_DNA.
EMBL; CH471053; EAW99715.1; -; Genomic_DNA.
EMBL; CH471053; EAW99716.1; -; Genomic_DNA.
EMBL; BC007682; AAH07682.1; -; mRNA.
EMBL; BC065574; AAH65574.1; -; mRNA.
EMBL; BC101467; AAI01468.1; -; mRNA.
EMBL; BC101469; AAI01470.1; -; mRNA.
EMBL; EU927390; ACH57452.1; -; mRNA.
CCDS; CCDS1929.1; -. [O95630-1]
RefSeq; NP_006454.1; NM_006463.4. [O95630-1]
RefSeq; NP_964010.1; NM_201647.2. [O95630-1]
RefSeq; NP_998787.1; NM_213622.2. [O95630-1]
RefSeq; XP_005264145.1; XM_005264088.3.
RefSeq; XP_011530785.1; XM_011532483.2. [O95630-1]
RefSeq; XP_016858664.1; XM_017003175.1.
UniGene; Hs.469018; -.
PDB; 2XZE; X-ray; 1.75 A; A/B=1-146.
PDB; 3RZU; X-ray; 2.50 A; A/B/C/D/E/F/G=243-424.
PDB; 3RZV; X-ray; 1.67 A; A=219-424.
PDB; 5IXF; NMR; -; B=228-241.
PDBsum; 2XZE; -.
PDBsum; 3RZU; -.
PDBsum; 3RZV; -.
PDBsum; 5IXF; -.
ProteinModelPortal; O95630; -.
SMR; O95630; -.
BioGrid; 115863; 67.
CORUM; O95630; -.
DIP; DIP-33062N; -.
IntAct; O95630; 41.
MINT; MINT-96921; -.
STRING; 9606.ENSP00000344742; -.
BindingDB; O95630; -.
MEROPS; M67.006; -.
iPTMnet; O95630; -.
PhosphoSitePlus; O95630; -.
BioMuta; STAMBP; -.
REPRODUCTION-2DPAGE; IPI00007943; -.
EPD; O95630; -.
MaxQB; O95630; -.
PaxDb; O95630; -.
PeptideAtlas; O95630; -.
PRIDE; O95630; -.
DNASU; 10617; -.
Ensembl; ENST00000339566; ENSP00000344742; ENSG00000124356. [O95630-1]
Ensembl; ENST00000394070; ENSP00000377633; ENSG00000124356. [O95630-1]
Ensembl; ENST00000394073; ENSP00000377636; ENSG00000124356. [O95630-1]
Ensembl; ENST00000409707; ENSP00000386548; ENSG00000124356. [O95630-1]
GeneID; 10617; -.
KEGG; hsa:10617; -.
UCSC; uc002sjs.3; human. [O95630-1]
CTD; 10617; -.
DisGeNET; 10617; -.
EuPathDB; HostDB:ENSG00000124356.15; -.
GeneCards; STAMBP; -.
GeneReviews; STAMBP; -.
HGNC; HGNC:16950; STAMBP.
HPA; HPA035800; -.
MalaCards; STAMBP; -.
MIM; 606247; gene.
MIM; 614261; phenotype.
neXtProt; NX_O95630; -.
OpenTargets; ENSG00000124356; -.
Orphanet; 294016; Microcephaly-capillary malformation syndrome.
PharmGKB; PA134955569; -.
eggNOG; KOG2880; Eukaryota.
eggNOG; COG1310; LUCA.
GeneTree; ENSGT00390000015439; -.
HOGENOM; HOG000195792; -.
HOVERGEN; HBG058519; -.
InParanoid; O95630; -.
KO; K11866; -.
OMA; CNTMHEE; -.
OrthoDB; EOG091G06CJ; -.
PhylomeDB; O95630; -.
TreeFam; TF323215; -.
Reactome; R-HSA-5689901; Metalloprotease DUBs.
SignaLink; O95630; -.
SIGNOR; O95630; -.
ChiTaRS; STAMBP; human.
GeneWiki; STAMBP; -.
GenomeRNAi; 10617; -.
PRO; PR:O95630; -.
Proteomes; UP000005640; Chromosome 2.
Bgee; ENSG00000124356; -.
CleanEx; HS_STAMBP; -.
ExpressionAtlas; O95630; baseline and differential.
Genevisible; O95630; HS.
GO; GO:0032154; C:cleavage furrow; IDA:MGI.
GO; GO:0005829; C:cytosol; IDA:HPA.
GO; GO:0005769; C:early endosome; IEA:UniProtKB-SubCell.
GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
GO; GO:0005654; C:nucleoplasm; IDA:HPA.
GO; GO:0005634; C:nucleus; TAS:ProtInc.
GO; GO:0005886; C:plasma membrane; IDA:HPA.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0008237; F:metallopeptidase activity; IEA:UniProtKB-KW.
GO; GO:0019904; F:protein domain specific binding; IPI:UniProtKB.
GO; GO:0004843; F:thiol-dependent ubiquitin-specific protease activity; IDA:MGI.
GO; GO:0007259; P:JAK-STAT cascade; TAS:ProtInc.
GO; GO:0000281; P:mitotic cytokinesis; IMP:MGI.
GO; GO:0043524; P:negative regulation of neuron apoptotic process; IEA:Ensembl.
GO; GO:0014067; P:negative regulation of phosphatidylinositol 3-kinase signaling; IMP:UniProtKB.
GO; GO:0046580; P:negative regulation of Ras protein signal transduction; IMP:UniProtKB.
GO; GO:0008284; P:positive regulation of cell proliferation; TAS:ProtInc.
GO; GO:0016579; P:protein deubiquitination; IMP:MGI.
Gene3D; 2.130.10.10; -; 1.
InterPro; IPR000555; JAMM/MPN+_dom.
InterPro; IPR037518; MPN.
InterPro; IPR015063; USP8_dimer.
InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
Pfam; PF01398; JAB; 1.
Pfam; PF08969; USP8_dimer; 1.
SMART; SM00232; JAB_MPN; 1.
PROSITE; PS50249; MPN; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; Complete proteome; Cytoplasm;
Disease mutation; Endosome; Hydrolase; Membrane; Metal-binding;
Metalloprotease; Nucleus; Phosphoprotein; Protease;
Reference proteome; Ubl conjugation; Ubl conjugation pathway; Zinc.
CHAIN 1 424 STAM-binding protein.
/FTId=PRO_0000194869.
DOMAIN 257 388 MPN. {ECO:0000255|PROSITE-
ProRule:PRU01182}.
REGION 1 127 Interaction with CHMP3.
REGION 227 231 Interaction with STAM.
MOTIF 335 348 JAMM motif. {ECO:0000255|PROSITE-
ProRule:PRU01182}.
COMPBIAS 104 177 Glu-rich.
METAL 335 335 Zinc 1; catalytic. {ECO:0000255|PROSITE-
ProRule:PRU01182}.
METAL 337 337 Zinc 1; catalytic. {ECO:0000255|PROSITE-
ProRule:PRU01182}.
METAL 348 348 Zinc 1; catalytic. {ECO:0000255|PROSITE-
ProRule:PRU01182}.
METAL 350 350 Zinc 2. {ECO:0000250}.
METAL 390 390 Zinc 2. {ECO:0000250}.
METAL 396 396 Zinc 2. {ECO:0000250}.
METAL 398 398 Zinc 2. {ECO:0000250}.
SITE 280 280 Indirect zinc-binding. {ECO:0000250}.
MOD_RES 2 2 Phosphoserine.
{ECO:0000244|PubMed:23186163,
ECO:0000269|PubMed:11483516}.
MOD_RES 48 48 Phosphoserine.
{ECO:0000269|PubMed:11483516}.
MOD_RES 243 243 Phosphoserine.
{ECO:0000244|PubMed:23186163,
ECO:0000269|PubMed:11483516}.
MOD_RES 245 245 Phosphoserine.
{ECO:0000269|PubMed:11483516}.
MOD_RES 247 247 Phosphoserine.
{ECO:0000244|PubMed:23186163,
ECO:0000269|PubMed:11483516}.
VAR_SEQ 336 424 THPTQTAFLSSVDLHTHCSYQMMLPESVAIVCSPKFQETGF
FKLTDHGLEEISSCRQKGFHPHSKDPPLFCSCSHVTVVDRA
VTITDLR -> VETLWSLKSLHAP (in isoform 2).
{ECO:0000303|PubMed:19906316}.
/FTId=VSP_057197.
VARIANT 14 14 R -> P (in MICCAP).
{ECO:0000269|PubMed:23542699}.
/FTId=VAR_069806.
VARIANT 38 38 R -> C (in MICCAP; dbSNP:rs143739249).
{ECO:0000269|PubMed:23542699}.
/FTId=VAR_069807.
VARIANT 42 42 E -> G (in MICCAP; dbSNP:rs397509387).
{ECO:0000269|PubMed:23542699}.
/FTId=VAR_069808.
VARIANT 63 63 Y -> C (in MICCAP; dbSNP:rs781694797).
{ECO:0000269|PubMed:23542699}.
/FTId=VAR_069809.
VARIANT 100 100 F -> Y (in MICCAP; dbSNP:rs397514697).
{ECO:0000269|PubMed:23542699}.
/FTId=VAR_069810.
VARIANT 313 313 T -> I (in MICCAP; dbSNP:rs202100019).
{ECO:0000269|PubMed:23542699}.
/FTId=VAR_069811.
MUTAGEN 348 348 D->A: Promotes accumulation of ubiquitin
on endosomes, ablates enzymatic activity
toward polyubiquitin substrate and allows
ubiquitinated STAM stabilization.
{ECO:0000269|PubMed:15314065}.
HELIX 11 22 {ECO:0000244|PDB:2XZE}.
HELIX 33 53 {ECO:0000244|PDB:2XZE}.
HELIX 56 71 {ECO:0000244|PDB:2XZE}.
HELIX 74 76 {ECO:0000244|PDB:2XZE}.
TURN 78 82 {ECO:0000244|PDB:2XZE}.
HELIX 88 97 {ECO:0000244|PDB:2XZE}.
HELIX 99 137 {ECO:0000244|PDB:2XZE}.
STRAND 257 260 {ECO:0000244|PDB:3RZV}.
HELIX 263 276 {ECO:0000244|PDB:3RZV}.
STRAND 282 290 {ECO:0000244|PDB:3RZV}.
STRAND 293 301 {ECO:0000244|PDB:3RZV}.
STRAND 304 306 {ECO:0000244|PDB:3RZV}.
STRAND 311 313 {ECO:0000244|PDB:3RZV}.
HELIX 316 326 {ECO:0000244|PDB:3RZV}.
STRAND 329 336 {ECO:0000244|PDB:3RZV}.
STRAND 338 340 {ECO:0000244|PDB:3RZU}.
HELIX 346 358 {ECO:0000244|PDB:3RZV}.
STRAND 363 368 {ECO:0000244|PDB:3RZV}.
TURN 369 372 {ECO:0000244|PDB:3RZV}.
STRAND 373 379 {ECO:0000244|PDB:3RZV}.
HELIX 381 389 {ECO:0000244|PDB:3RZV}.
STRAND 404 407 {ECO:0000244|PDB:3RZV}.
STRAND 409 414 {ECO:0000244|PDB:3RZV}.
STRAND 419 422 {ECO:0000244|PDB:3RZV}.
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


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