UBP8_MOUSE
ID UBP8_MOUSE Reviewed; 1080 AA.
AC Q80U87; A2AI53; Q80YP2; Q8R0D3; Q9EQU1; Q9WVP5;
DT 01-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2004, sequence version 2.
DT 03-AUG-2022, entry version 164.
DE RecName: Full=Ubiquitin carboxyl-terminal hydrolase 8 {ECO:0000305};
DE EC=3.4.19.12 {ECO:0000269|PubMed:16120644};
DE AltName: Full=Deubiquitinating enzyme 8;
DE AltName: Full=Ubiquitin isopeptidase Y;
DE Short=mUBPy;
DE AltName: Full=Ubiquitin thioesterase 8;
DE AltName: Full=Ubiquitin-specific-processing protease 8;
GN Name=Usp8 {ECO:0000312|MGI:MGI:1934029}; Synonyms=Kiaa0055, Ubpy;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], SH3-BINDING, INTERACTION WITH STAM2, AND
RP MUTAGENESIS OF PRO-405; GLN-406; VAL-407; ASP-408; ARG-409; THR-410;
RP LYS-411; LYS-412 AND PRO-413.
RX PubMed=10982817; DOI=10.1074/jbc.m007251200;
RA Kato M., Miyazawa K., Kitamura N.;
RT "A deubiquitinating enzyme UBPY interacts with the Src homology 3 domain of
RT Hrs-binding protein via a novel binding motif PX(V/I)(D/N)RXXKP.";
RL J. Biol. Chem. 275:37481-37487(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, AND INTERACTION
RP WITH RASGRF1.
RC TISSUE=Embryo;
RX PubMed=11500497; DOI=10.1074/jbc.m103454200;
RA Gnesutta N., Ceriani M., Innocenti M., Mauri I., Zippel R., Sturani E.,
RA Borgonovo B., Berruti G., Martegani E.;
RT "Cloning and characterization of mouse UBPy, a deubiquitinating enzyme that
RT interacts with the ras guanine nucleotide exchange factor CDC25(Mm)/Ras-
RT GRF1.";
RL J. Biol. Chem. 276:39448-39454(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
RX PubMed=12693553; DOI=10.1093/dnares/10.1.35;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Aizawa H., Yuasa S.,
RA Nakajima D., Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: II.
RT The complete nucleotide sequences of 400 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 10:35-48(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Brain, and Kidney;
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 [6]
RP IDENTIFICATION BY MASS SPECTROMETRY, INTERACTION WITH RNF41, FUNCTION, AND
RP MUTAGENESIS OF CYS-748.
RX PubMed=15314180; DOI=10.1128/mcb.24.17.7748-7757.2004;
RA Wu X., Yen L., Irwin L., Sweeney C., Carraway K.L. III;
RT "Stabilization of the E3 ubiquitin ligase Nrdp1 by the deubiquitinating
RT enzyme USP8.";
RL Mol. Cell. Biol. 24:7748-7757(2004).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic brain;
RX PubMed=15345747; DOI=10.1074/mcp.m400085-mcp200;
RA Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.;
RT "Phosphoproteomic analysis of the developing mouse brain.";
RL Mol. Cell. Proteomics 3:1093-1101(2004).
RN [8]
RP INTERACTION WITH OTUB1 AND RNF128, AND MUTAGENESIS OF CYS-748.
RX PubMed=14661020; DOI=10.1038/ni1017;
RA Soares L., Seroogy C., Skrenta H., Anandasabapathy N., Lovelace P.,
RA Chung C.D., Engleman E., Fathman C.G.;
RT "Two isoforms of otubain 1 regulate T cell anergy via GRAIL.";
RL Nat. Immunol. 5:45-54(2004).
RN [9]
RP TISSUE SPECIFICITY, AND INTERACTION WITH DNAJB3.
RX PubMed=15342353; DOI=10.1095/biolreprod.104.030866;
RA Berruti G., Martegani E.;
RT "The deubiquitinating enzyme mUBPy interacts with the sperm-specific
RT molecular chaperone MSJ-1: the relation with the proteasome, acrosome, and
RT centrosome in mouse male germ cells.";
RL Biol. Reprod. 72:14-21(2005).
RN [10]
RP FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, UBIQUITINATION, AND
RP MUTAGENESIS OF CYS-748.
RX PubMed=16120644; DOI=10.1091/mbc.e05-06-0560;
RA Mizuno E., Iura T., Mukai A., Yoshimori T., Kitamura N., Komada M.;
RT "Regulation of epidermal growth factor receptor down-regulation by UBPY-
RT mediated deubiquitination at endosomes.";
RL Mol. Biol. Cell 16:5163-5174(2005).
RN [11]
RP FUNCTION, MUTAGENESIS OF CYS-748, AND INTERACTION WITH ESP15.
RX PubMed=16771824; DOI=10.1111/j.1600-0854.2006.00452.x;
RA Mizuno E., Kobayashi K., Yamamoto A., Kitamura N., Komada M.;
RT "A deubiquitinating enzyme UBPY regulates the level of protein
RT ubiquitination on endosomes.";
RL Traffic 7:1017-1031(2006).
RN [12]
RP PHOSPHORYLATION, INTERACTION WITH EGFR, AND FUNCTION.
RX PubMed=17121848; DOI=10.1074/jbc.m604711200;
RA Alwan H.A., van Leeuwen J.E.;
RT "UBPY-mediated epidermal growth factor receptor (EGFR) de-ubiquitination
RT promotes EGFR degradation.";
RL J. Biol. Chem. 282:1658-1669(2007).
RN [13]
RP PHOSPHORYLATION AT SER-680, INTERACTION WITH YWHAE, MUTAGENESIS OF SER-680,
RP AND SUBCELLULAR LOCATION.
RX PubMed=16944949; DOI=10.1021/pr060206k;
RA Ballif B.A., Cao Z., Schwartz D., Carraway K.L. III, Gygi S.P.;
RT "Identification of 14-3-3epsilon substrates from embryonic murine brain.";
RL J. Proteome Res. 5:2372-2379(2006).
RN [14]
RP FUNCTION, PHOSPHORYLATION AT SER-680, INTERACTION WITH YWHAE; YWHAG AND
RP YWHAZ, MUTAGENESIS OF SER-680, AND SUBCELLULAR LOCATION.
RX PubMed=17720156; DOI=10.1016/j.yexcr.2007.07.028;
RA Mizuno E., Kitamura N., Komada M.;
RT "14-3-3-dependent inhibition of the deubiquitinating activity of UBPY and
RT its cancellation in the M phase.";
RL Exp. Cell Res. 313:3624-3634(2007).
RN [15]
RP FUNCTION, PHOSPHORYLATION AT THR-907, AND MUTAGENESIS OF THR-907.
RX PubMed=17210635; DOI=10.1128/mcb.01245-06;
RA Cao Z., Wu X., Yen L., Sweeney C., Carraway K.L. III;
RT "Neuregulin-induced ErbB3 downregulation is mediated by a protein stability
RT cascade involving the E3 ubiquitin ligase Nrdp1.";
RL Mol. Cell. Biol. 27:2180-2188(2007).
RN [16]
RP FUNCTION.
RX PubMed=17452457; DOI=10.1128/mcb.01566-06;
RA Niendorf S., Oksche A., Kisser A., Lohler J., Prinz M., Schorle H.,
RA Feller S., Lewitzky M., Horak I., Knobeloch K.P.;
RT "Essential role of ubiquitin-specific protease 8 for receptor tyrosine
RT kinase stability and endocytic trafficking in vivo.";
RL Mol. Cell. Biol. 27:5029-5039(2007).
RN [17]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA Thibault P.;
RT "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL Immunity 30:143-154(2009).
RN [18]
RP FUNCTION, ASSOCIATION WITH THE ESCRT-0 COMPLEX, AND MICROTUBULE-BINDING.
RX PubMed=20130268; DOI=10.1095/biolreprod.109.081679;
RA Berruti G., Ripolone M., Ceriani M.;
RT "USP8, a regulator of endosomal sorting, is involved in mouse acrosome
RT biogenesis through interaction with the spermatid ESCRT-0 complex and
RT microtubules.";
RL Biol. Reprod. 82:930-939(2010).
RN [19]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Hydrolase that can remove conjugated ubiquitin from proteins
CC and therefore plays an important regulatory role at the level of
CC protein turnover by preventing degradation. Converts both 'Lys-48' an
CC 'Lys-63'-linked ubiquitin chains. Catalytic activity is enhanced in the
CC M phase. Involved in cell proliferation. Required to enter into S phase
CC in response to serum stimulation. May regulate T-cell anergy mediated
CC by RNF128 via the formation of a complex containing RNF128 and OTUB1.
CC Probably regulates the stability of STAM2 and RASGRF1. Regulates
CC endosomal ubiquitin dynamics, cargo sorting, membrane traffic at early
CC endosomes, and maintenance of ESCRT-0 stability. The level of protein
CC ubiquitination on endosomes is essential for maintaining the morphology
CC of the organelle. Deubiquitinates EPS15 and controles tyrosine kinase
CC stability. Removes conjugated ubiquitin from EGFR thus regulating EGFR
CC degradation and downstream MAPK signaling. Involved in acrosome
CC biogenesis through interaction with the spermatid ESCRT-0 complex and
CC microtubules. Deubiquitinates BIRC6/bruce and KIF23/MKLP1 (By
CC similarity). Deubiquitinates BACE1 which inhibits BACE1 lysosomal
CC degradation and modulates BACE-mediated APP cleavage and amyloid-beta
CC formation (By similarity). {ECO:0000250, ECO:0000250|UniProtKB:P40818,
CC ECO:0000269|PubMed:11500497, ECO:0000269|PubMed:15314180,
CC ECO:0000269|PubMed:16120644, ECO:0000269|PubMed:16771824,
CC ECO:0000269|PubMed:17121848, ECO:0000269|PubMed:17210635,
CC ECO:0000269|PubMed:17452457, ECO:0000269|PubMed:17720156,
CC ECO:0000269|PubMed:20130268}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Thiol-dependent hydrolysis of ester, thioester, amide, peptide
CC and isopeptide bonds formed by the C-terminal Gly of ubiquitin (a 76-
CC residue protein attached to proteins as an intracellular targeting
CC signal).; EC=3.4.19.12; Evidence={ECO:0000269|PubMed:16120644};
CC -!- SUBUNIT: Forms a ternary complex with RNF128 and OTUB1. Interacts (via
CC C-terminal UCH catalytic domain) with OTUB1 isoform 1. Interacts with
CC STAM2 (via SH3 domain). Interacts with DNAJB3, EGFR, EPS15, RASGRF1,
CC RNF41, YWHAE, YWHAG and YWHAZ. Interacts with NBR1, RASGRF1, RNF41 and
CC IST1 (By similarity). Associates with the ESCRT-0 complex and with
CC microtubules. Interacts with BIRC6/bruce and KIF23/MKLP1. {ECO:0000250,
CC ECO:0000269|PubMed:10982817, ECO:0000269|PubMed:11500497,
CC ECO:0000269|PubMed:14661020, ECO:0000269|PubMed:15314180,
CC ECO:0000269|PubMed:15342353, ECO:0000269|PubMed:16771824,
CC ECO:0000269|PubMed:16944949, ECO:0000269|PubMed:17121848,
CC ECO:0000269|PubMed:17720156}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:17720156}. Nucleus
CC {ECO:0000269|PubMed:16944949}. Endosome membrane
CC {ECO:0000269|PubMed:16120644}; Peripheral membrane protein
CC {ECO:0000305}. Cell membrane {ECO:0000250|UniProtKB:P40818}; Peripheral
CC membrane protein {ECO:0000305}.
CC -!- TISSUE SPECIFICITY: Highly expressed in testis. Expressed at
CC intermediate level in brain. {ECO:0000269|PubMed:11500497,
CC ECO:0000269|PubMed:15342353}.
CC -!- DOMAIN: The MIT domain is required for endosomal localization, CHMP1B-
CC binding, maintenance of ESCRT-0 stability and EGFR degradation.
CC {ECO:0000250}.
CC -!- DOMAIN: The rhodanese domain is sufficient for RNF41-binding.
CC -!- PTM: Phosphorylation of Ser-680 is essential for interaction with YWHAE
CC and for cytosol localization. Undergoes dephosphorylation at Ser-680 in
CC the M phase. Tyrosine-phosphorylated in its N-terminal half in an EGFR-
CC dependent manner. {ECO:0000269|PubMed:16944949,
CC ECO:0000269|PubMed:17121848, ECO:0000269|PubMed:17210635,
CC ECO:0000269|PubMed:17720156}.
CC -!- PTM: Ubiquitinated. Inactive form is mostly monoubiquitinated, but
CC polyubiquitination happens too. Ubiquitination is increased in EGF-
CC stimulated cells. Ubiquitination of active form is undetectable,
CC suggesting a possibility that USP8 deubiquitinates itself, thereby
CC regulating its own function. {ECO:0000269|PubMed:16120644}.
CC -!- SIMILARITY: Belongs to the peptidase C19 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC65477.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AB045709; BAB18534.1; -; mRNA.
DR EMBL; AF057146; AAD38869.1; -; mRNA.
DR EMBL; AK122195; BAC65477.1; ALT_INIT; mRNA.
DR EMBL; AL732330; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC027052; AAH27052.1; -; mRNA.
DR EMBL; BC050947; AAH50947.1; -; mRNA.
DR EMBL; BC061465; AAH61465.1; -; mRNA.
DR EMBL; BC066126; AAH66126.1; -; mRNA.
DR CCDS; CCDS16687.1; -.
DR RefSeq; NP_062703.2; NM_019729.3.
DR PDB; 1UJ0; X-ray; 1.70 A; B=699-709.
DR PDBsum; 1UJ0; -.
DR AlphaFoldDB; Q80U87; -.
DR SMR; Q80U87; -.
DR BioGRID; 220000; 22.
DR IntAct; Q80U87; 7.
DR MINT; Q80U87; -.
DR STRING; 10090.ENSMUSP00000106046; -.
DR MEROPS; C19.011; -.
DR iPTMnet; Q80U87; -.
DR PhosphoSitePlus; Q80U87; -.
DR EPD; Q80U87; -.
DR jPOST; Q80U87; -.
DR MaxQB; Q80U87; -.
DR PaxDb; Q80U87; -.
DR PRIDE; Q80U87; -.
DR ProteomicsDB; 297795; -.
DR Antibodypedia; 1385; 278 antibodies from 28 providers.
DR DNASU; 84092; -.
DR Ensembl; ENSMUST00000028841; ENSMUSP00000028841; ENSMUSG00000027363.
DR GeneID; 84092; -.
DR KEGG; mmu:84092; -.
DR UCSC; uc008meb.2; mouse.
DR CTD; 9101; -.
DR MGI; MGI:1934029; Usp8.
DR VEuPathDB; HostDB:ENSMUSG00000027363; -.
DR eggNOG; KOG1868; Eukaryota.
DR GeneTree; ENSGT00940000157542; -.
DR InParanoid; Q80U87; -.
DR OMA; ENKPACY; -.
DR Reactome; R-MMU-1358803; Downregulation of ERBB2:ERBB3 signaling.
DR Reactome; R-MMU-4641263; Regulation of FZD by ubiquitination.
DR Reactome; R-MMU-5689880; Ub-specific processing proteases.
DR Reactome; R-MMU-6807004; Negative regulation of MET activity.
DR BioGRID-ORCS; 84092; 25 hits in 72 CRISPR screens.
DR ChiTaRS; Usp8; mouse.
DR PRO; PR:Q80U87; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; Q80U87; protein.
DR Bgee; ENSMUSG00000027363; Expressed in spermatid and 252 other tissues.
DR ExpressionAtlas; Q80U87; baseline and differential.
DR Genevisible; Q80U87; MM.
DR GO; GO:0002080; C:acrosomal membrane; IDA:MGI.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR GO; GO:0043197; C:dendritic spine; ISO:MGI.
DR GO; GO:0005769; C:early endosome; ISO:MGI.
DR GO; GO:0031313; C:extrinsic component of endosome membrane; IDA:UniProtKB.
DR GO; GO:0019897; C:extrinsic component of plasma membrane; ISO:MGI.
DR GO; GO:0098978; C:glutamatergic synapse; ISO:MGI.
DR GO; GO:0030496; C:midbody; IDA:MGI.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0014069; C:postsynaptic density; ISO:MGI.
DR GO; GO:0004843; F:cysteine-type deubiquitinase activity; IDA:UniProtKB.
DR GO; GO:0017124; F:SH3 domain binding; IEA:UniProtKB-KW.
DR GO; GO:1990090; P:cellular response to nerve growth factor stimulus; ISO:MGI.
DR GO; GO:0007032; P:endosome organization; IMP:UniProtKB.
DR GO; GO:0000281; P:mitotic cytokinesis; ISO:MGI.
DR GO; GO:0090263; P:positive regulation of canonical Wnt signaling pathway; ISO:MGI.
DR GO; GO:0016579; P:protein deubiquitination; IDA:UniProtKB.
DR GO; GO:0071108; P:protein K48-linked deubiquitination; ISO:MGI.
DR GO; GO:0070536; P:protein K63-linked deubiquitination; ISO:MGI.
DR GO; GO:0007265; P:Ras protein signal transduction; IPI:MGI.
DR GO; GO:0099576; P:regulation of protein catabolic process at postsynapse, modulating synaptic transmission; ISO:MGI.
DR GO; GO:0032880; P:regulation of protein localization; ISS:UniProtKB.
DR GO; GO:0031647; P:regulation of protein stability; ISS:UniProtKB.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IEA:InterPro.
DR Gene3D; 3.40.250.10; -; 1.
DR InterPro; IPR038765; Papain-like_cys_pep_sf.
DR InterPro; IPR001394; Peptidase_C19_UCH.
DR InterPro; IPR001763; Rhodanese-like_dom.
DR InterPro; IPR036873; Rhodanese-like_dom_sf.
DR InterPro; IPR015063; USP8_dimer.
DR InterPro; IPR018200; USP_CS.
DR InterPro; IPR028889; USP_dom.
DR Pfam; PF00581; Rhodanese; 1.
DR Pfam; PF00443; UCH; 1.
DR Pfam; PF08969; USP8_dimer; 1.
DR SMART; SM00450; RHOD; 1.
DR SUPFAM; SSF52821; SSF52821; 1.
DR SUPFAM; SSF54001; SSF54001; 1.
DR PROSITE; PS50206; RHODANESE_3; 1.
DR PROSITE; PS00972; USP_1; 1.
DR PROSITE; PS00973; USP_2; 1.
DR PROSITE; PS50235; USP_3; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell cycle; Cell membrane; Cytoplasm; Endosome; Hydrolase;
KW Membrane; Nucleus; Phosphoprotein; Protease; Reference proteome;
KW SH3-binding; Thiol protease; Ubl conjugation; Ubl conjugation pathway.
FT CHAIN 1..1080
FT /note="Ubiquitin carboxyl-terminal hydrolase 8"
FT /id="PRO_0000080628"
FT DOMAIN 33..116
FT /note="MIT"
FT DOMAIN 195..313
FT /note="Rhodanese"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00173"
FT DOMAIN 739..1071
FT /note="USP"
FT REGION 119..176
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 379..455
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 468..605
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 642..710
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 405..413
FT /note="SH3-binding"
FT COMPBIAS 119..168
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 412..428
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 429..447
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 468..537
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 547..561
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 645..659
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 662..677
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 748
FT /note="Nucleophile"
FT ACT_SITE 1029
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10092,
FT ECO:0000255|PROSITE-ProRule:PRU10093"
FT MOD_RES 160
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P40818"
FT MOD_RES 392
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P40818"
FT MOD_RES 446
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P40818"
FT MOD_RES 569
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P40818"
FT MOD_RES 680
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:16944949,
FT ECO:0000269|PubMed:17720156"
FT MOD_RES 681
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P40818"
FT MOD_RES 907
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:17210635"
FT MUTAGEN 405
FT /note="P->A: Abolishes interaction with the SH3 domain of
FT STAM2."
FT /evidence="ECO:0000269|PubMed:10982817"
FT MUTAGEN 406
FT /note="Q->A: Does not affect interaction with the SH3
FT domain of STAM2."
FT /evidence="ECO:0000269|PubMed:10982817"
FT MUTAGEN 407
FT /note="V->A: Reduces interaction with the SH3 domain of
FT STAM2."
FT /evidence="ECO:0000269|PubMed:10982817"
FT MUTAGEN 408
FT /note="D->A: Reduces interaction with the SH3 domain of
FT STAM2."
FT /evidence="ECO:0000269|PubMed:10982817"
FT MUTAGEN 409
FT /note="R->A: Abolishes interaction with the SH3 domain of
FT STAM2."
FT /evidence="ECO:0000269|PubMed:10982817"
FT MUTAGEN 410
FT /note="T->A: Does not affect interaction with the SH3
FT domain of STAM2."
FT /evidence="ECO:0000269|PubMed:10982817"
FT MUTAGEN 411
FT /note="K->A: Does not affect interaction with the SH3
FT domain of STAM2."
FT /evidence="ECO:0000269|PubMed:10982817"
FT MUTAGEN 412
FT /note="K->A: Abolishes interaction with the SH3 domain of
FT STAM2."
FT /evidence="ECO:0000269|PubMed:10982817"
FT MUTAGEN 413
FT /note="P->A: Abolishes interaction with the SH3 domain of
FT STAM2."
FT /evidence="ECO:0000269|PubMed:10982817"
FT MUTAGEN 680
FT /note="S->A: Abolishes the interaction with YWHAE and leads
FT to accumulation in the nucleus."
FT /evidence="ECO:0000269|PubMed:16944949,
FT ECO:0000269|PubMed:17720156"
FT MUTAGEN 748
FT /note="C->A: Impairs deubiquitination of EPS15, RNF128 and
FT RNF41."
FT /evidence="ECO:0000269|PubMed:14661020,
FT ECO:0000269|PubMed:15314180, ECO:0000269|PubMed:16120644,
FT ECO:0000269|PubMed:16771824"
FT MUTAGEN 907
FT /note="T->A: Reduces stabilization activity on RNF41."
FT /evidence="ECO:0000269|PubMed:17210635"
FT CONFLICT 139
FT /note="Q -> P (in Ref. 2; AAD38869)"
FT /evidence="ECO:0000305"
FT CONFLICT 151
FT /note="K -> R (in Ref. 1; BAB18534)"
FT /evidence="ECO:0000305"
FT CONFLICT 349
FT /note="T -> A (in Ref. 1; BAB18534)"
FT /evidence="ECO:0000305"
FT CONFLICT 370
FT /note="E -> G (in Ref. 1; BAB18534)"
FT /evidence="ECO:0000305"
FT CONFLICT 557
FT /note="D -> N (in Ref. 1; BAB18534)"
FT /evidence="ECO:0000305"
FT CONFLICT 576
FT /note="P -> L (in Ref. 1; BAB18534)"
FT /evidence="ECO:0000305"
FT CONFLICT 837
FT /note="F -> S (in Ref. 1; BAB18534)"
FT /evidence="ECO:0000305"
FT CONFLICT 865..873
FT /note="DLQAAEHAW -> EPAGGRARL (in Ref. 1; BAB18534)"
FT /evidence="ECO:0000305"
FT CONFLICT 885..886
FT /note="VA -> RL (in Ref. 1; BAB18534)"
FT /evidence="ECO:0000305"
FT CONFLICT 894
FT /note="S -> A (in Ref. 1; BAB18534)"
FT /evidence="ECO:0000305"
FT HELIX 704..706
FT /evidence="ECO:0007829|PDB:1UJ0"
SQ SEQUENCE 1080 AA; 122611 MW; 7F458E3B1AF0B7FA CRC64;
MPAVASVPKE LYLSSSLKDL NKKTEVKPEK TSTKNYIHSA QKIFKTAEEC RLDRDEERAY
VLYMKYVAVY NLIKKRPDFK QQQDYYLSIL GPANIKKAIE EAERLSESLK LRYEEAEVRK
QLEEKDRREE EQLQQQKRQE MGREDSGAAA KRSVENLLDS KTKTQRINGE KSEGAAAAER
GAITAKELYT MMMDKNTSLI IMDARKIQDY QHSCILDSLS VPEEAISPGV TASWIEANLS
DDSKDTWKKR GSVDYVVLLD WFSSAKDLLL GTTLRSLKDA LFKWESKTVL RHEPLVLEGG
YENWLLCYPQ FTTNAKVTPP PRSRAEEVSV SLDFTYPSLE EPVPSKLPTQ MPPPPIETNE
KALLVTDQDE KLRLSTQPAL AGPGAAPRAE ASPIIQPAPA TKSVPQVDRT KKPSVKLPED
HRIKSENTDQ SGRVLSDRST KPVFPSPTTM LTDEEKARIH QETALLMEKN KQEKELWDKQ
QKEQKEKLRR EEQERKAGKT QDADERDSTE NQHKAKDGQE KKDSKQTKTE DRELSADGAQ
EATGTQRQSK SEHEASDAKV PVEGKRCPTS EAQKRPADVS PASVSGELNA GKAQREPLTR
ARSEEMGRIV PGLPLGWAKF LDPITGTFRY YHSPTNTVHM YPPEMAPSSA PPSTPPTHKV
KPQVPAERDR EPSKLKRSYS SPDITQALQE EEKRRPAVTP MVNRENKPPC YPKAEISRLS
ASQIRNLNPV FGGSGPALTG LRNLGNTCYM NSILQCLCNA PHLADYFNRN CYQDDINRSN
LLGHKGEVAE EFGIIMKALW TGQYRYISPK DFKVTIGKIN DQFAGSSQQD SQELLLFLMD
GLHEDLNKAD NRKRHKEENN EHLDDLQAAE HAWQKHKQLN ESIIVALFQG QFKSTVQCLT
CRRRSRTFEA FMYLSLPLAS TSKCTLQDCL RLFSKEEKLT DNNRFYCSHC RARRDSLKKI
EIWKLPPVLL VHLKRFSYDG RWKQKLQTSV DFPLENLDLS QYVIGPKNSL KKYNLFSVSN
HYGGLDGGHY TAYCKNAARQ RWFKFDDHEV SDISVSSVRS SAAYILFYTS LGPRITDVAT
