UBS3A_MOUSE
ID UBS3A_MOUSE Reviewed; 624 AA.
AC Q3V3E1; Q3TED7;
DT 25-JAN-2012, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2005, sequence version 1.
DT 03-AUG-2022, entry version 125.
DE RecName: Full=Ubiquitin-associated and SH3 domain-containing protein A;
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; ORFNames=Sts2;
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 [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J, and NOD; TISSUE=Thymus;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
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 [3]
RP LACK OF PROTEIN PHOSPHATASE ACTIVITY.
RX PubMed=20670933; DOI=10.1074/jbc.m110.114181;
RA Chen X., Ren L., Kim S., Carpino N., Daniel J.L., Kunapuli S.P.,
RA Tsygankov A.Y., Pei D.;
RT "Determination of the substrate specificity of protein-tyrosine phosphatase
RT TULA-2 and identification of Syk as a TULA-2 substrate.";
RL J. Biol. Chem. 285:31268-31276(2010).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) OF 354-622, FUNCTION, AND VERY LOW
RP PHOSPHATASE ACTIVITY AT PH 5.
RX PubMed=19196006; DOI=10.1021/bi802219n;
RA Chen Y., Jakoncic J., Carpino N., Nassar N.;
RT "Structural and functional characterization of the 2H-phosphatase domain of
RT Sts-2 reveals an acid-dependent phosphatase activity.";
RL Biochemistry 48:1681-1690(2009).
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. May inhibit dynamin-dependent endocytic pathways by
CC functionally sequestering dynamin via its SH3 domain (By similarity).
CC Exhibits negligigle protein tyrosine phosphatase activity at neutral
CC pH. May act as a dominant-negative regulator of UBASH3B-dependent
CC dephosphorylation. {ECO:0000250, ECO:0000269|PubMed:19196006}.
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 (By
CC similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
CC -!- MISCELLANEOUS: Has very nearly lost all enzyme activity. Has very low,
CC but measurable tyrosine phosphatase activity at pH 5.0.
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; AK041690; BAE20600.1; -; mRNA.
DR EMBL; AK169696; BAE41311.1; -; mRNA.
DR EMBL; AC154652; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC167247; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CU024900; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS50054.1; -.
DR RefSeq; NP_808491.2; NM_177823.4.
DR PDB; 3D4I; X-ray; 1.95 A; A/B/C/D=354-622.
DR PDB; 3D6A; X-ray; 2.25 A; A/B/C/D=354-622.
DR PDB; 3DB1; X-ray; 2.77 A; A/B/C/D=354-622.
DR PDBsum; 3D4I; -.
DR PDBsum; 3D6A; -.
DR PDBsum; 3DB1; -.
DR AlphaFoldDB; Q3V3E1; -.
DR SMR; Q3V3E1; -.
DR IntAct; Q3V3E1; 6.
DR STRING; 10090.ENSMUSP00000045890; -.
DR iPTMnet; Q3V3E1; -.
DR PhosphoSitePlus; Q3V3E1; -.
DR EPD; Q3V3E1; -.
DR jPOST; Q3V3E1; -.
DR MaxQB; Q3V3E1; -.
DR PaxDb; Q3V3E1; -.
DR PRIDE; Q3V3E1; -.
DR ProteomicsDB; 297798; -.
DR Antibodypedia; 23818; 334 antibodies from 35 providers.
DR DNASU; 328795; -.
DR Ensembl; ENSMUST00000236745; ENSMUSP00000158544; ENSMUSG00000042345.
DR GeneID; 328795; -.
DR KEGG; mmu:328795; -.
DR UCSC; uc008bus.2; mouse.
DR CTD; 53347; -.
DR MGI; MGI:1926074; Ubash3a.
DR VEuPathDB; HostDB:ENSMUSG00000042345; -.
DR eggNOG; KOG3734; Eukaryota.
DR GeneTree; ENSGT00940000160841; -.
DR HOGENOM; CLU_016516_0_0_1; -.
DR InParanoid; Q3V3E1; -.
DR OMA; MCFCEEL; -.
DR OrthoDB; 243749at2759; -.
DR PhylomeDB; Q3V3E1; -.
DR TreeFam; TF313334; -.
DR BioGRID-ORCS; 328795; 2 hits in 73 CRISPR screens.
DR ChiTaRS; Ubash3a; mouse.
DR EvolutionaryTrace; Q3V3E1; -.
DR PRO; PR:Q3V3E1; -.
DR Proteomes; UP000000589; Chromosome 17.
DR RNAct; Q3V3E1; protein.
DR Bgee; ENSMUSG00000042345; Expressed in thymus and 56 other tissues.
DR ExpressionAtlas; Q3V3E1; baseline and differential.
DR Genevisible; Q3V3E1; MM.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005794; C:Golgi apparatus; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0050860; P:negative regulation of T cell receptor signaling pathway; IGI:MGI.
DR GO; GO:0001817; P:regulation of cytokine production; IGI:MGI.
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 Pfam; PF00627; UBA; 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; Cytoplasm; Nucleus; Reference proteome; SH3 domain.
FT CHAIN 1..624
FT /note="Ubiquitin-associated and SH3 domain-containing
FT protein A"
FT /id="PRO_0000415372"
FT DOMAIN 19..60
FT /note="UBA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00212"
FT DOMAIN 238..303
FT /note="SH3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT REGION 358..624
FT /note="Phosphatase-like"
FT CONFLICT 75
FT /note="A -> V (in Ref. 1; BAE41311)"
FT /evidence="ECO:0000305"
FT CONFLICT 331
FT /note="C -> S (in Ref. 1; BAE41311)"
FT /evidence="ECO:0000305"
FT CONFLICT 337
FT /note="P -> S (in Ref. 1; BAE41311)"
FT /evidence="ECO:0000305"
FT CONFLICT 444
FT /note="S -> F (in Ref. 1; BAE41311)"
FT /evidence="ECO:0000305"
FT CONFLICT 463
FT /note="E -> D (in Ref. 1; BAE41311)"
FT /evidence="ECO:0000305"
FT STRAND 360..365
FT /evidence="ECO:0007829|PDB:3D4I"
FT HELIX 370..374
FT /evidence="ECO:0007829|PDB:3D4I"
FT HELIX 378..381
FT /evidence="ECO:0007829|PDB:3D4I"
FT STRAND 385..387
FT /evidence="ECO:0007829|PDB:3DB1"
FT HELIX 406..412
FT /evidence="ECO:0007829|PDB:3D4I"
FT HELIX 418..434
FT /evidence="ECO:0007829|PDB:3D4I"
FT STRAND 438..443
FT /evidence="ECO:0007829|PDB:3D4I"
FT HELIX 447..459
FT /evidence="ECO:0007829|PDB:3D4I"
FT TURN 463..465
FT /evidence="ECO:0007829|PDB:3D4I"
FT STRAND 468..470
FT /evidence="ECO:0007829|PDB:3D4I"
FT HELIX 472..474
FT /evidence="ECO:0007829|PDB:3D4I"
FT HELIX 478..480
FT /evidence="ECO:0007829|PDB:3D4I"
FT HELIX 485..488
FT /evidence="ECO:0007829|PDB:3D4I"
FT HELIX 492..497
FT /evidence="ECO:0007829|PDB:3D4I"
FT HELIX 512..514
FT /evidence="ECO:0007829|PDB:3D4I"
FT HELIX 521..536
FT /evidence="ECO:0007829|PDB:3D4I"
FT STRAND 544..550
FT /evidence="ECO:0007829|PDB:3D4I"
FT HELIX 554..557
FT /evidence="ECO:0007829|PDB:3D4I"
FT HELIX 560..563
FT /evidence="ECO:0007829|PDB:3D4I"
FT HELIX 570..578
FT /evidence="ECO:0007829|PDB:3D4I"
FT STRAND 585..590
FT /evidence="ECO:0007829|PDB:3D4I"
FT TURN 592..594
FT /evidence="ECO:0007829|PDB:3D4I"
FT STRAND 597..600
FT /evidence="ECO:0007829|PDB:3D4I"
FT HELIX 617..620
FT /evidence="ECO:0007829|PDB:3D4I"
SQ SEQUENCE 624 AA; 70145 MW; E40AFB541AC84538 CRC64;
MAAGETQLYA KVSNKLKGRS TPSLLDPLLA MGFPTHTALK ALAATGRKTA EAAADWLHGH
CNDPSLDDPI PQEYALFLCP TGPLLEKLQE FWRESRRQCA KNRAHEVFPH VTLCDFFTCE
DQKVECLYEA LRRAGDRILG SFPTLVPLVL HSSISYLGFF INDSPADAIR EFAMAFATEA
AVLADCTIKP CTKQLHLTLA HKFYPHHQRT LEQLAKAIQP SHSCQWTAAL YSRDMRFVHY
QTLKALFQYK PQNADELMLS AGDYIFVDPT QQEEASEGWA IGISHRTGCR GFLPENYTER
ANEADTWVKH RTYTFNLAMD LNSRKDFEAS CRGNGEPHTP SMSKSVSSIQ ALQATISRRG
ILVVRHGERV DQVFGKSWLQ QCTTADGKYY RPDLNFPRSL PRRSNGIKDF ENDPPLSSCG
IFQARLAGEA LLDSGVRVTA VFASPALRCV QTAKHILEEL KLEKKLKIRV EPGIFEWMKW
EASKATLTFL TLEELKEANF NVDLDYRPAL PRCSLMPAES YDQYVERCAV SMGQIINTCP
QDMGITLIVS HSSALDSCTR PLLGLPPREC GDFAQLVRKI PSLGMCFCEE NREDGKWDLV
NPPVKTLTHG ANSVFNWRNW ISSN
