UBS3A_HUMAN
ID UBS3A_HUMAN Reviewed; 661 AA.
AC P57075; G5E9E4; Q6HA34; Q6HA35; Q6ISI6; Q6ISK3; Q6ISS9;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2000, sequence version 1.
DT 03-AUG-2022, entry version 179.
DE RecName: Full=Ubiquitin-associated and SH3 domain-containing protein A;
DE AltName: Full=Cbl-interacting protein 4;
DE Short=CLIP4;
DE AltName: Full=Suppressor of T-cell receptor signaling 2;
DE Short=STS-2;
DE AltName: Full=T-cell ubiquitin ligand 1;
DE Short=TULA-1;
GN Name=UBASH3A; Synonyms=STS2;
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] (ISOFORMS 1 AND 2), AND TISSUE SPECIFICITY.
RC TISSUE=Placenta;
RX PubMed=11281453; DOI=10.1007/s004390000453;
RA Wattenhofer M., Shibuya K., Kudoh J., Lyle R., Michaud J., Rossier C.,
RA Kawasaki K., Asakawa S., Minoshima S., Berry A., Bonne-Tamir B.,
RA Shimizu N., Antonarakis S.E., Scott H.S.;
RT "Isolation and characterization of the UBASH3A gene on 21q22.3 encoding a
RT potential nuclear protein with a novel combination of domains.";
RL Hum. Genet. 108:140-147(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), IDENTIFICATION BY MASS
RP SPECTROMETRY, INTERACTION WITH CBL AND UBIQUITIN, SUBCELLULAR LOCATION, AND
RP TISSUE SPECIFICITY.
RC TISSUE=Leukemia;
RX PubMed=15107835; DOI=10.1038/sj.onc.1207627;
RA Feshchenko E.A., Smirnova E.V., Swaminathan G., Teckchandani A.M.,
RA Agrawal R., Band H., Zhang X., Annan R.S., Carr S.A., Tsygankov A.Y.;
RT "TULA: an SH3- and UBA-containing protein that binds to c-Cbl and
RT ubiquitin.";
RL Oncogene 23:4690-4706(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=10830953; DOI=10.1038/35012518;
RA Hattori M., Fujiyama A., Taylor T.D., Watanabe H., Yada T., Park H.-S.,
RA Toyoda A., Ishii K., Totoki Y., Choi D.-K., Groner Y., Soeda E., Ohki M.,
RA Takagi T., Sakaki Y., Taudien S., Blechschmidt K., Polley A., Menzel U.,
RA Delabar J., Kumpf K., Lehmann R., Patterson D., Reichwald K., Rump A.,
RA Schillhabel M., Schudy A., Zimmermann W., Rosenthal A., Kudoh J.,
RA Shibuya K., Kawasaki K., Asakawa S., Shintani A., Sasaki T., Nagamine K.,
RA Mitsuyama S., Antonarakis S.E., Minoshima S., Shimizu N., Nordsiek G.,
RA Hornischer K., Brandt P., Scharfe M., Schoen O., Desario A., Reichelt J.,
RA Kauer G., Bloecker H., Ramser J., Beck A., Klages S., Hennig S.,
RA Riesselmann L., Dagand E., Wehrmeyer S., Borzym K., Gardiner K.,
RA Nizetic D., Francis F., Lehrach H., Reinhardt R., Yaspo M.-L.;
RT "The DNA sequence of human chromosome 21.";
RL Nature 405:311-319(2000).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton 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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 3), AND VARIANTS
RP GLY-18 AND PHE-28.
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 FUNCTION, MUTAGENESIS OF TRP-317, SUBUNIT, INTERACTION WITH CBL AND
RP UBIQUITIN, IDENTIFICATION IN A COMPLEX WITH EGFR, AND SUBCELLULAR LOCATION.
RX PubMed=15159412; DOI=10.1074/jbc.m403759200;
RA Kowanetz K., Crosetto N., Haglund K., Schmidt M.H., Heldin C.-H., Dikic I.;
RT "Suppressors of T-cell receptor signaling Sts-1 and Sts-2 bind to Cbl and
RT inhibit endocytosis of receptor tyrosine kinases.";
RL J. Biol. Chem. 279:32786-32795(2004).
RN [7]
RP FUNCTION, INTERACTION WITH DYNAMIN, AND MUTAGENESIS OF TRP-317.
RX PubMed=17382318; DOI=10.1016/j.yexcr.2007.02.017;
RA Bertelsen V., Breen K., Sandvig K., Stang E., Madshus I.H.;
RT "The Cbl-interacting protein TULA inhibits dynamin-dependent endocytosis.";
RL Exp. Cell Res. 313:1696-1709(2007).
RN [8]
RP FUNCTION, AND LACK OF PROTEIN PHOSPHATASE ACTIVITY.
RX PubMed=18189269; DOI=10.1002/jcb.21678;
RA Agrawal R., Carpino N., Tsygankov A.;
RT "TULA proteins regulate activity of the protein tyrosine kinase Syk.";
RL J. Cell. Biochem. 104:953-964(2008).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [10]
RP STRUCTURE BY NMR OF 20-70.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of the UBA domain of human UBASH3A protein.";
RL Submitted (NOV-2005) to the PDB data bank.
CC -!- FUNCTION: Interferes with CBL-mediated down-regulation and degradation
CC of receptor-type tyrosine kinases. Promotes accumulation of activated
CC target receptors, such as T-cell receptors, EGFR and PDGFRB, on the
CC cell surface. Exhibits negligigle protein tyrosine phosphatase activity
CC at neutral pH. May act as a dominant-negative regulator of UBASH3B-
CC dependent dephosphorylation. May inhibit dynamin-dependent endocytic
CC pathways by functionally sequestering dynamin via its SH3 domain.
CC {ECO:0000269|PubMed:15159412, ECO:0000269|PubMed:17382318,
CC ECO:0000269|PubMed:18189269}.
CC -!- SUBUNIT: Homodimer or homooligomer. Interacts with CBL. Part of a
CC complex containing CBL and activated EGFR. Interacts with ubiquitin and
CC with mono-ubiquitinated proteins. Interacts with dynamin.
CC {ECO:0000269|PubMed:15107835, ECO:0000269|PubMed:15159412,
CC ECO:0000269|PubMed:17382318}.
CC -!- INTERACTION:
CC P57075; P35520: CBS; NbExp=4; IntAct=EBI-2105393, EBI-740135;
CC P57075; Q15038: DAZAP2; NbExp=4; IntAct=EBI-2105393, EBI-724310;
CC P57075; Q6FHJ6: KCNE1; NbExp=3; IntAct=EBI-2105393, EBI-10215868;
CC P57075; Q6A162: KRT40; NbExp=3; IntAct=EBI-2105393, EBI-10171697;
CC P57075; Q04864: REL; NbExp=3; IntAct=EBI-2105393, EBI-307352;
CC P57075; Q15427: SF3B4; NbExp=3; IntAct=EBI-2105393, EBI-348469;
CC P57075; O43597: SPRY2; NbExp=4; IntAct=EBI-2105393, EBI-742487;
CC P57075; Q13625-3: TP53BP2; NbExp=3; IntAct=EBI-2105393, EBI-10175039;
CC P57075; O94972: TRIM37; NbExp=3; IntAct=EBI-2105393, EBI-741602;
CC P57075-2; Q8N5I2: ARRDC1; NbExp=3; IntAct=EBI-7353612, EBI-2339564;
CC P57075-2; Q96B67: ARRDC3; NbExp=3; IntAct=EBI-7353612, EBI-2875665;
CC P57075-2; O75815: BCAR3; NbExp=3; IntAct=EBI-7353612, EBI-702336;
CC P57075-2; Q13191: CBLB; NbExp=3; IntAct=EBI-7353612, EBI-744027;
CC P57075-2; Q8WXC6-1: COPS9; NbExp=3; IntAct=EBI-7353612, EBI-17466401;
CC P57075-2; Q15038: DAZAP2; NbExp=3; IntAct=EBI-7353612, EBI-724310;
CC P57075-2; Q14203-5: DCTN1; NbExp=3; IntAct=EBI-7353612, EBI-25840379;
CC P57075-2; Q96D03: DDIT4L; NbExp=3; IntAct=EBI-7353612, EBI-742054;
CC P57075-2; Q9NRI5-2: DISC1; NbExp=3; IntAct=EBI-7353612, EBI-11988027;
CC P57075-2; Q9Y2H0-1: DLGAP4; NbExp=3; IntAct=EBI-7353612, EBI-12000556;
CC P57075-2; P50570: DNM2; NbExp=3; IntAct=EBI-7353612, EBI-346547;
CC P57075-2; Q8N9I9: DTX3; NbExp=3; IntAct=EBI-7353612, EBI-2340258;
CC P57075-2; Q8N9I5: FADS6; NbExp=3; IntAct=EBI-7353612, EBI-3943864;
CC P57075-2; Q86UY5: FAM83A; NbExp=3; IntAct=EBI-7353612, EBI-1384254;
CC P57075-2; Q9NVK5-3: FGFR1OP2; NbExp=3; IntAct=EBI-7353612, EBI-12377025;
CC P57075-2; P14136: GFAP; NbExp=3; IntAct=EBI-7353612, EBI-744302;
CC P57075-2; A6NEM1: GOLGA6L9; NbExp=3; IntAct=EBI-7353612, EBI-5916454;
CC P57075-2; Q9ULR0-1: ISY1; NbExp=3; IntAct=EBI-7353612, EBI-18398632;
CC P57075-2; Q719H9: KCTD1; NbExp=3; IntAct=EBI-7353612, EBI-9027502;
CC P57075-2; Q6ZU52: KIAA0408; NbExp=3; IntAct=EBI-7353612, EBI-739493;
CC P57075-2; Q5T749: KPRP; NbExp=5; IntAct=EBI-7353612, EBI-10981970;
CC P57075-2; P02533: KRT14; NbExp=3; IntAct=EBI-7353612, EBI-702178;
CC P57075-2; Q15323: KRT31; NbExp=3; IntAct=EBI-7353612, EBI-948001;
CC P57075-2; Q14532: KRT32; NbExp=3; IntAct=EBI-7353612, EBI-1044146;
CC P57075-2; Q92764: KRT35; NbExp=3; IntAct=EBI-7353612, EBI-1058674;
CC P57075-2; Q6A163: KRT39; NbExp=5; IntAct=EBI-7353612, EBI-11958242;
CC P57075-2; P80188: LCN2; NbExp=3; IntAct=EBI-7353612, EBI-11911016;
CC P57075-2; Q8TBB1: LNX1; NbExp=3; IntAct=EBI-7353612, EBI-739832;
CC P57075-2; Q9Y250: LZTS1; NbExp=3; IntAct=EBI-7353612, EBI-1216080;
CC P57075-2; Q9BRK4: LZTS2; NbExp=3; IntAct=EBI-7353612, EBI-741037;
CC P57075-2; Q9UHC7: MKRN1; NbExp=3; IntAct=EBI-7353612, EBI-373524;
CC P57075-2; O15049: N4BP3; NbExp=3; IntAct=EBI-7353612, EBI-2512055;
CC P57075-2; Q6X4W1-2: NSMF; NbExp=3; IntAct=EBI-7353612, EBI-12028784;
CC P57075-2; Q96CS7: PLEKHB2; NbExp=3; IntAct=EBI-7353612, EBI-373552;
CC P57075-2; Q969W9-2: PMEPA1; NbExp=3; IntAct=EBI-7353612, EBI-13318883;
CC P57075-2; Q96PV4: PNMA5; NbExp=3; IntAct=EBI-7353612, EBI-10171633;
CC P57075-2; Q9NQX0: PRDM6; NbExp=3; IntAct=EBI-7353612, EBI-11320284;
CC P57075-2; O60260-5: PRKN; NbExp=6; IntAct=EBI-7353612, EBI-21251460;
CC P57075-2; Q9Y3C5: RNF11; NbExp=3; IntAct=EBI-7353612, EBI-396669;
CC P57075-2; Q9NWF9: RNF216; NbExp=3; IntAct=EBI-7353612, EBI-723313;
CC P57075-2; Q6ZSJ9: SHISA6; NbExp=3; IntAct=EBI-7353612, EBI-12037847;
CC P57075-2; Q9H6Q3: SLA2; NbExp=3; IntAct=EBI-7353612, EBI-1222854;
CC P57075-2; Q8NCR6: SMRP1; NbExp=3; IntAct=EBI-7353612, EBI-10269322;
CC P57075-2; Q6IEG0: SNRNP48; NbExp=3; IntAct=EBI-7353612, EBI-2876632;
CC P57075-2; Q07889: SOS1; NbExp=3; IntAct=EBI-7353612, EBI-297487;
CC P57075-2; O43609: SPRY1; NbExp=3; IntAct=EBI-7353612, EBI-3866665;
CC P57075-2; O75558: STX11; NbExp=3; IntAct=EBI-7353612, EBI-714135;
CC P57075-2; Q86VP1: TAX1BP1; NbExp=3; IntAct=EBI-7353612, EBI-529518;
CC P57075-2; Q969V4: TEKT1; NbExp=3; IntAct=EBI-7353612, EBI-10180409;
CC P57075-2; Q8WW24: TEKT4; NbExp=3; IntAct=EBI-7353612, EBI-750487;
CC P57075-2; O43615: TIMM44; NbExp=3; IntAct=EBI-7353612, EBI-861737;
CC P57075-2; Q7Z6W1: TMCO2; NbExp=3; IntAct=EBI-7353612, EBI-12807858;
CC P57075-2; Q8WW34-2: TMEM239; NbExp=3; IntAct=EBI-7353612, EBI-11528917;
CC P57075-2; Q05BL1: TP53BP2; NbExp=3; IntAct=EBI-7353612, EBI-11952721;
CC P57075-2; Q9H3D4: TP63; NbExp=3; IntAct=EBI-7353612, EBI-2337775;
CC P57075-2; P14373: TRIM27; NbExp=3; IntAct=EBI-7353612, EBI-719493;
CC P57075-2; Q9C035-3: TRIM5; NbExp=3; IntAct=EBI-7353612, EBI-12840050;
CC P57075-2; Q86XT4: TRIM50; NbExp=3; IntAct=EBI-7353612, EBI-9867283;
CC P57075-2; Q9BZR9: TRIM8; NbExp=5; IntAct=EBI-7353612, EBI-2340370;
CC P57075-2; Q9H9H4: VPS37B; NbExp=3; IntAct=EBI-7353612, EBI-4400866;
CC P57075-2; P42768: WAS; NbExp=3; IntAct=EBI-7353612, EBI-346375;
CC P57075-2; O00401: WASL; NbExp=3; IntAct=EBI-7353612, EBI-957615;
CC P57075-2; Q9Y2W2: WBP11; NbExp=3; IntAct=EBI-7353612, EBI-714455;
CC P57075-2; B2RXF5: ZBTB42; NbExp=3; IntAct=EBI-7353612, EBI-12287587;
CC P57075-2; Q53FD0-2: ZC2HC1C; NbExp=3; IntAct=EBI-7353612, EBI-14104088;
CC P57075-2; Q9P2Y4: ZNF219; NbExp=3; IntAct=EBI-7353612, EBI-3937106;
CC P57075-2; Q6S9Z5: ZNF474; NbExp=3; IntAct=EBI-7353612, EBI-17269964;
CC P57075-2; Q9UGI0: ZRANB1; NbExp=3; IntAct=EBI-7353612, EBI-527853;
CC P57075-2; Q7Z783; NbExp=3; IntAct=EBI-7353612, EBI-9088990;
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1; Synonyms=Long;
CC IsoId=P57075-1; Sequence=Displayed;
CC Name=2; Synonyms=Short;
CC IsoId=P57075-2; Sequence=VSP_006703;
CC Name=3;
CC IsoId=P57075-3; Sequence=VSP_006703, VSP_045549, VSP_045550;
CC -!- TISSUE SPECIFICITY: Highest expression of UBASH3A in tissues belonging
CC to the immune system, including spleen, peripheral blood leukocytes,
CC thymus and bone marrow. {ECO:0000269|PubMed:11281453,
CC ECO:0000269|PubMed:15107835}.
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DR EMBL; AJ277750; CAB91543.1; -; mRNA.
DR EMBL; AF520809; AAP80731.1; -; mRNA.
DR EMBL; AF521702; AAP80738.1; -; mRNA.
DR EMBL; AP001746; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471079; EAX09560.1; -; Genomic_DNA.
DR EMBL; BC069357; AAH69357.1; -; mRNA.
DR EMBL; BC069483; AAH69483.1; -; mRNA.
DR EMBL; BC069511; AAH69511.1; -; mRNA.
DR EMBL; BC069577; -; NOT_ANNOTATED_CDS; mRNA.
DR CCDS; CCDS13687.1; -. [P57075-1]
DR CCDS; CCDS33566.1; -. [P57075-2]
DR CCDS; CCDS58791.1; -. [P57075-3]
DR RefSeq; NP_001001895.1; NM_001001895.2. [P57075-2]
DR RefSeq; NP_001230396.1; NM_001243467.1. [P57075-3]
DR RefSeq; NP_061834.1; NM_018961.3. [P57075-1]
DR PDB; 2CRN; NMR; -; A=20-70.
DR PDB; 5WDI; X-ray; 2.43 A; A/B=394-658.
DR PDBsum; 2CRN; -.
DR PDBsum; 5WDI; -.
DR AlphaFoldDB; P57075; -.
DR SMR; P57075; -.
DR BioGRID; 119748; 107.
DR IntAct; P57075; 81.
DR MINT; P57075; -.
DR STRING; 9606.ENSP00000317327; -.
DR DEPOD; UBASH3A; -.
DR iPTMnet; P57075; -.
DR PhosphoSitePlus; P57075; -.
DR BioMuta; UBASH3A; -.
DR DMDM; 10720330; -.
DR jPOST; P57075; -.
DR MassIVE; P57075; -.
DR MaxQB; P57075; -.
DR PaxDb; P57075; -.
DR PeptideAtlas; P57075; -.
DR PRIDE; P57075; -.
DR ProteomicsDB; 33914; -.
DR ProteomicsDB; 56982; -. [P57075-1]
DR ProteomicsDB; 56983; -. [P57075-2]
DR Antibodypedia; 23818; 334 antibodies from 35 providers.
DR DNASU; 53347; -.
DR Ensembl; ENST00000291535.11; ENSP00000291535.6; ENSG00000160185.15. [P57075-2]
DR Ensembl; ENST00000319294.11; ENSP00000317327.6; ENSG00000160185.15. [P57075-1]
DR Ensembl; ENST00000398367.1; ENSP00000381408.1; ENSG00000160185.15. [P57075-3]
DR GeneID; 53347; -.
DR KEGG; hsa:53347; -.
DR MANE-Select; ENST00000319294.11; ENSP00000317327.6; NM_018961.4; NP_061834.1.
DR UCSC; uc002zbe.4; human. [P57075-1]
DR CTD; 53347; -.
DR DisGeNET; 53347; -.
DR GeneCards; UBASH3A; -.
DR HGNC; HGNC:12462; UBASH3A.
DR HPA; ENSG00000160185; Tissue enriched (lymphoid).
DR MIM; 605736; gene.
DR neXtProt; NX_P57075; -.
DR OpenTargets; ENSG00000160185; -.
DR PharmGKB; PA37112; -.
DR VEuPathDB; HostDB:ENSG00000160185; -.
DR eggNOG; KOG3734; Eukaryota.
DR GeneTree; ENSGT00940000160841; -.
DR HOGENOM; CLU_016516_0_0_1; -.
DR InParanoid; P57075; -.
DR OMA; MCFCEEL; -.
DR OrthoDB; 243749at2759; -.
DR PhylomeDB; P57075; -.
DR TreeFam; TF313334; -.
DR PathwayCommons; P57075; -.
DR SignaLink; P57075; -.
DR BioGRID-ORCS; 53347; 25 hits in 1074 CRISPR screens.
DR ChiTaRS; UBASH3A; human.
DR EvolutionaryTrace; P57075; -.
DR GeneWiki; UBASH3A; -.
DR GenomeRNAi; 53347; -.
DR Pharos; P57075; Tbio.
DR PRO; PR:P57075; -.
DR Proteomes; UP000005640; Chromosome 21.
DR RNAct; P57075; protein.
DR Bgee; ENSG00000160185; Expressed in granulocyte and 85 other tissues.
DR ExpressionAtlas; P57075; baseline and differential.
DR Genevisible; P57075; HS.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; HDA:UniProtKB.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0005794; C:Golgi apparatus; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0050860; P:negative regulation of T cell receptor signaling pathway; IBA:GO_Central.
DR GO; GO:0001817; P:regulation of cytokine production; IEA:Ensembl.
DR CDD; cd07067; HP_PGM_like; 1.
DR CDD; cd11937; SH3_UBASH3A; 1.
DR Gene3D; 3.40.50.1240; -; 1.
DR InterPro; IPR013078; His_Pase_superF_clade-1.
DR InterPro; IPR029033; His_PPase_superfam.
DR InterPro; IPR036028; SH3-like_dom_sf.
DR InterPro; IPR001452; SH3_domain.
DR InterPro; IPR015940; UBA.
DR InterPro; IPR009060; UBA-like_sf.
DR InterPro; IPR035634; UBASH3A_SH3.
DR Pfam; PF00300; His_Phos_1; 1.
DR Pfam; PF14604; SH3_9; 1.
DR SMART; SM00326; SH3; 1.
DR SUPFAM; SSF46934; SSF46934; 1.
DR SUPFAM; SSF50044; SSF50044; 1.
DR SUPFAM; SSF53254; SSF53254; 1.
DR PROSITE; PS50002; SH3; 1.
DR PROSITE; PS50030; UBA; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cytoplasm; Nucleus; Reference proteome;
KW SH3 domain.
FT CHAIN 1..661
FT /note="Ubiquitin-associated and SH3 domain-containing
FT protein A"
FT /id="PRO_0000210994"
FT DOMAIN 15..60
FT /note="UBA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00212"
FT DOMAIN 276..341
FT /note="SH3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT REGION 395..661
FT /note="Phosphatase-like"
FT VAR_SEQ 185..223
FT /note="GTSVSRFWIFSQVPGHGPNLRLSNLTRASFVSHYILQKY -> D (in
FT isoform 2 and isoform 3)"
FT /evidence="ECO:0000303|PubMed:11281453,
FT ECO:0000303|PubMed:15107835, ECO:0000303|PubMed:15489334"
FT /id="VSP_006703"
FT VAR_SEQ 545..564
FT /note="PAFPLSALMPAESYQEYMDR -> SLPWACASVKKIKRKENGSW (in
FT isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_045549"
FT VAR_SEQ 565..661
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_045550"
FT VARIANT 18
FT /note="S -> G (in dbSNP:rs2277798)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_026971"
FT VARIANT 28
FT /note="L -> F (in dbSNP:rs2277800)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_026972"
FT VARIANT 286
FT /note="Q -> R (in dbSNP:rs775952011)"
FT /id="VAR_026973"
FT VARIANT 324
FT /note="R -> L (in dbSNP:rs13048049)"
FT /id="VAR_061921"
FT VARIANT 324
FT /note="R -> Q (in dbSNP:rs13048049)"
FT /id="VAR_061922"
FT VARIANT 466
FT /note="D -> E (in dbSNP:rs17114930)"
FT /id="VAR_052675"
FT MUTAGEN 317
FT /note="W->A: Loss of interaction with CBL."
FT /evidence="ECO:0000269|PubMed:15159412,
FT ECO:0000269|PubMed:17382318"
FT MUTAGEN 317
FT /note="W->L: Abolishes binding to dynamin."
FT /evidence="ECO:0000269|PubMed:15159412,
FT ECO:0000269|PubMed:17382318"
FT CONFLICT 64
FT /note="P -> H (in Ref. 5; AAH69511)"
FT /evidence="ECO:0000305"
FT CONFLICT 129
FT /note="E -> K (in Ref. 5; BC069577)"
FT /evidence="ECO:0000305"
FT CONFLICT 229
FT /note="C -> Y (in Ref. 5; AAH69511)"
FT /evidence="ECO:0000305"
FT CONFLICT 283
FT /note="A -> V (in Ref. 5; AAH69483)"
FT /evidence="ECO:0000305"
FT CONFLICT 393
FT /note="V -> I (in Ref. 5; AAH69511)"
FT /evidence="ECO:0000305"
FT CONFLICT 651
FT /note="A -> V (in Ref. 5; AAH69511)"
FT /evidence="ECO:0000305"
FT HELIX 25..30
FT /evidence="ECO:0007829|PDB:2CRN"
FT HELIX 35..45
FT /evidence="ECO:0007829|PDB:2CRN"
FT HELIX 50..60
FT /evidence="ECO:0007829|PDB:2CRN"
FT STRAND 61..63
FT /evidence="ECO:0007829|PDB:2CRN"
FT STRAND 397..402
FT /evidence="ECO:0007829|PDB:5WDI"
FT HELIX 407..411
FT /evidence="ECO:0007829|PDB:5WDI"
FT HELIX 415..418
FT /evidence="ECO:0007829|PDB:5WDI"
FT HELIX 445..447
FT /evidence="ECO:0007829|PDB:5WDI"
FT HELIX 455..471
FT /evidence="ECO:0007829|PDB:5WDI"
FT STRAND 475..480
FT /evidence="ECO:0007829|PDB:5WDI"
FT HELIX 484..497
FT /evidence="ECO:0007829|PDB:5WDI"
FT TURN 500..502
FT /evidence="ECO:0007829|PDB:5WDI"
FT STRAND 505..507
FT /evidence="ECO:0007829|PDB:5WDI"
FT HELIX 509..511
FT /evidence="ECO:0007829|PDB:5WDI"
FT HELIX 515..517
FT /evidence="ECO:0007829|PDB:5WDI"
FT HELIX 529..534
FT /evidence="ECO:0007829|PDB:5WDI"
FT HELIX 549..551
FT /evidence="ECO:0007829|PDB:5WDI"
FT HELIX 558..574
FT /evidence="ECO:0007829|PDB:5WDI"
FT STRAND 581..587
FT /evidence="ECO:0007829|PDB:5WDI"
FT HELIX 591..594
FT /evidence="ECO:0007829|PDB:5WDI"
FT HELIX 597..600
FT /evidence="ECO:0007829|PDB:5WDI"
FT HELIX 607..615
FT /evidence="ECO:0007829|PDB:5WDI"
FT STRAND 622..628
FT /evidence="ECO:0007829|PDB:5WDI"
FT TURN 629..632
FT /evidence="ECO:0007829|PDB:5WDI"
FT STRAND 633..637
FT /evidence="ECO:0007829|PDB:5WDI"
FT HELIX 654..657
FT /evidence="ECO:0007829|PDB:5WDI"
SQ SEQUENCE 661 AA; 74123 MW; 60DA2E0B8CE4ABFC CRC64;
MAAGETQLYA KVSNKLKSRS SPSLLEPLLA MGFPVHTALK ALAATGRKTA EEALAWLHDH
CNDPSLDDPI PQEYALFLCP TGPLLEKLQE FWRESKRQCA KNRAHEVFPH VTLCDFFTCE
DQKVECLYEA LKRAGDRLLG SFPTAVPLAL HSSISYLGFF VSGSPADVIR EFAMTFATEA
SLLAGTSVSR FWIFSQVPGH GPNLRLSNLT RASFVSHYIL QKYCSVKPCT KQLHLTLAHK
FYPHHQRTLE QLARAIPLGH SCQWTAALYS RDMRFVHYQT LRALFQYKPQ NVDELTLSPG
DYIFVDPTQQ DEASEGWVIG ISQRTGCRGF LPENYTDRAS ESDTWVKHRM YTFSLATDLN
SRKDGEASSR CSGEFLPQTA RSLSSLQALQ ATVARKSVLV VRHGERVDQI FGKAWLQQCS
TPDGKYYRPD LNFPCSLPRR SRGIKDFEND PPLSSCGIFQ SRIAGDALLD SGIRISSVFA
SPALRCVQTA KLILEELKLE KKIKIRVEPG IFEWTKWEAG KTTPTLMSLE ELKEANFNID
TDYRPAFPLS ALMPAESYQE YMDRCTASMV QIVNTCPQDT GVILIVSHGS TLDSCTRPLL
GLPPRECGDF AQLVRKIPSL GMCFCEENKE EGKWELVNPP VKTLTHGANA AFNWRNWISG
N
