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Database: UniProt
Entry: Q9QZS8
LinkDB: Q9QZS8
Original site: Q9QZS8 
ID   SH2D3_MOUSE             Reviewed;         854 AA.
AC   Q9QZS8; A2AK84; Q9JME1;
DT   21-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   29-OCT-2014, entry version 109.
DE   RecName: Full=SH2 domain-containing protein 3C;
DE   AltName: Full=Cas/HEF1-associated signal transducer;
DE   AltName: Full=SH2 domain-containing Eph receptor-binding protein 1;
GN   Name=Sh2d3c; Synonyms=Chat, Shep1;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, AND
RP   PHOSPHORYLATION.
RX   PubMed=10542222; DOI=10.1074/jbc.274.45.31941;
RA   Dodelet V.C., Pazzagli C., Zisch A.H., Hauser C.A., Pasquale E.B.;
RT   "A novel signaling intermediate, SHEP1, directly couples Eph receptors
RT   to R-Ras and Rap1A.";
RL   J. Biol. Chem. 274:31941-31946(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), INTERACTION WITH BCAR1 AND
RP   NEDD9, TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION.
RX   PubMed=10692442; DOI=10.1074/jbc.275.9.6404;
RA   Sakakibara A., Hattori S.;
RT   "Chat, a Cas/HEF1-associated adaptor protein that integrates multiple
RT   signaling pathways.";
RL   J. Biol. Chem. 275:6404-6410(2000).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), INTERACTION WITH BCAR1; NEDD9
RP   AND PTK2B, TISSUE SPECIFICITY, AND PHOSPHORYLATION.
RC   TISSUE=Spleen;
RX   PubMed=12486027; DOI=10.1074/jbc.M207942200;
RA   Sakakibara A., Hattori S., Nakamura S., Katagiri T.;
RT   "A novel hematopoietic adaptor protein, Chat-H, positively regulates T
RT   cell receptor-mediated interleukin-2 production by Jurkat cells.";
RL   J. Biol. Chem. 278:6012-6017(2003).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC   STRAIN=C57BL/6J, and NOD; TISSUE=Cerebellum;
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.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   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.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [5]
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.,
RA   She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
RA   Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
RA   Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
RA   Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
RA   Lindblad-Toh K., Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of
RT   the mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [7]
RP   PHOSPHORYLATION AT TYR-273; TYR-278 AND TYR-787, IDENTIFICATION BY
RP   MASS SPECTROMETRY, AND MUTAGENESIS OF TYR-787.
RX   PubMed=15272013; DOI=10.1074/jbc.M402929200;
RA   Dail M., Kalo M.S., Seddon J.A., Cote J.-F., Vuori K., Pasquale E.B.;
RT   "SHEP1 function in cell migration is impaired by a single amino acid
RT   mutation that disrupts association with the scaffolding protein cas
RT   but not with Ras GTPases.";
RL   J. Biol. Chem. 279:41892-41902(2004).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-435, AND IDENTIFICATION
RP   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).
CC   -!- FUNCTION: Eph receptor-binding protein which may be a positive
CC       regulator of TCR signaling. Binding to BCAR1 is required to induce
CC       membrane ruffling and promote EGF-dependent cell migration.
CC   -!- SUBUNIT: Interacts (via C-terminus) with BCAR1/CAS (By
CC       similarity). Interacts with PTK2B. Isoform 2 interacts with
CC       NEDD9/HEF1. {ECO:0000250, ECO:0000269|PubMed:10692442,
CC       ECO:0000269|PubMed:12486027}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10692442}.
CC       Membrane {ECO:0000269|PubMed:10692442}; Peripheral membrane
CC       protein {ECO:0000269|PubMed:10692442}. Note=Associated with the
CC       membrane when EGF-stimulated. Found at ruffling membranes.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1; Synonyms=Chat-H;
CC         IsoId=Q9QZS8-1; Sequence=Displayed;
CC       Name=2; Synonyms=Chat;
CC         IsoId=Q9QZS8-2; Sequence=VSP_017709;
CC   -!- TISSUE SPECIFICITY: Isoform 2 is ubiquitously expressed. Isoform 1
CC       is expressed in hematopoietic cells from spleen, lymph node and
CC       thymus. {ECO:0000269|PubMed:10542222, ECO:0000269|PubMed:10692442,
CC       ECO:0000269|PubMed:12486027}.
CC   -!- DOMAIN: The C-terminal Cdc25-homology/Ras-GEF domain adopts a
CC       closed conformation rendering it incapable of carrying out
CC       canonical exchange factor function, this closed conformation is
CC       required for interaction with BCAR1. {ECO:0000250}.
CC   -!- SIMILARITY: Contains 1 Ras-GEF domain. {ECO:0000255|PROSITE-
CC       ProRule:PRU00168}.
CC   -!- SIMILARITY: Contains 1 SH2 domain. {ECO:0000255|PROSITE-
CC       ProRule:PRU00191}.
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DR   EMBL; AF168364; AAF13305.1; -; mRNA.
DR   EMBL; AB030442; BAA90557.1; -; mRNA.
DR   EMBL; AB043953; BAA96361.1; -; mRNA.
DR   EMBL; AK042709; BAC31340.1; -; mRNA.
DR   EMBL; AK155165; BAE33088.1; -; mRNA.
DR   EMBL; AL772271; CAM16622.1; -; Genomic_DNA.
DR   EMBL; BC113203; AAI13204.1; -; mRNA.
DR   CCDS; CCDS15928.1; -. [Q9QZS8-1]
DR   CCDS; CCDS57168.1; -. [Q9QZS8-2]
DR   RefSeq; NP_001239476.1; NM_001252547.1. [Q9QZS8-2]
DR   RefSeq; NP_038809.1; NM_013781.3. [Q9QZS8-1]
DR   UniGene; Mm.474256; -.
DR   UniGene; Mm.9593; -.
DR   ProteinModelPortal; Q9QZS8; -.
DR   SMR; Q9QZS8; 209-295, 537-849.
DR   DIP; DIP-42657N; -.
DR   IntAct; Q9QZS8; 1.
DR   MINT; MINT-1503279; -.
DR   STRING; 10090.ENSMUSP00000073866; -.
DR   PhosphoSite; Q9QZS8; -.
DR   MaxQB; Q9QZS8; -.
DR   PaxDb; Q9QZS8; -.
DR   PRIDE; Q9QZS8; -.
DR   Ensembl; ENSMUST00000074248; ENSMUSP00000073866; ENSMUSG00000059013. [Q9QZS8-1]
DR   Ensembl; ENSMUST00000113242; ENSMUSP00000108868; ENSMUSG00000059013. [Q9QZS8-2]
DR   GeneID; 27387; -.
DR   KEGG; mmu:27387; -.
DR   UCSC; uc008jgp.2; mouse. [Q9QZS8-1]
DR   UCSC; uc008jgr.2; mouse. [Q9QZS8-2]
DR   CTD; 10044; -.
DR   MGI; MGI:1351631; Sh2d3c.
DR   eggNOG; NOG149796; -.
DR   GeneTree; ENSGT00390000008976; -.
DR   HOGENOM; HOG000231595; -.
DR   HOVERGEN; HBG053174; -.
DR   InParanoid; Q9QZS8; -.
DR   OMA; YCPINRT; -.
DR   OrthoDB; EOG77126R; -.
DR   PhylomeDB; Q9QZS8; -.
DR   TreeFam; TF323756; -.
DR   NextBio; 305340; -.
DR   PRO; PR:Q9QZS8; -.
DR   Bgee; Q9QZS8; -.
DR   CleanEx; MM_CHAT; -.
DR   CleanEx; MM_SH2D3C; -.
DR   ExpressionAtlas; Q9QZS8; baseline and differential.
DR   Genevestigator; Q9QZS8; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IEA:InterPro.
DR   GO; GO:0005068; F:transmembrane receptor protein tyrosine kinase adaptor activity; TAS:MGI.
DR   GO; GO:0007165; P:signal transduction; TAS:MGI.
DR   GO; GO:0007264; P:small GTPase mediated signal transduction; IEA:InterPro.
DR   GO; GO:0007169; P:transmembrane receptor protein tyrosine kinase signaling pathway; TAS:GOC.
DR   Gene3D; 1.10.840.10; -; 1.
DR   Gene3D; 3.30.505.10; -; 1.
DR   InterPro; IPR023578; Ras_GEF_dom.
DR   InterPro; IPR001895; RASGEF_cat_dom.
DR   InterPro; IPR000980; SH2.
DR   Pfam; PF00617; RasGEF; 1.
DR   Pfam; PF00017; SH2; 1.
DR   SMART; SM00147; RasGEF; 1.
DR   SMART; SM00252; SH2; 1.
DR   SUPFAM; SSF48366; SSF48366; 1.
DR   SUPFAM; SSF55550; SSF55550; 1.
DR   PROSITE; PS50009; RASGEF_CAT; 1.
DR   PROSITE; PS50001; SH2; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Complete proteome; Cytoplasm; Membrane;
KW   Phosphoprotein; Reference proteome; SH2 domain.
FT   CHAIN         1    854       SH2 domain-containing protein 3C.
FT                                /FTId=PRO_0000228834.
FT   DOMAIN      215    314       SH2. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00191}.
FT   DOMAIN      580    848       Ras-GEF. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00168}.
FT   MOD_RES     273    273       Phosphotyrosine.
FT                                {ECO:0000269|PubMed:15272013}.
FT   MOD_RES     278    278       Phosphotyrosine.
FT                                {ECO:0000269|PubMed:15272013}.
FT   MOD_RES     435    435       Phosphoserine.
FT                                {ECO:0000269|PubMed:19144319}.
FT   MOD_RES     787    787       Phosphotyrosine.
FT                                {ECO:0000269|PubMed:15272013}.
FT   VAR_SEQ       1    166       MTEMPKKTGRKFKFFKFKGLGSLSNLPRSFSLRRSSASASI
FT                                RSCPEPDTFEATQDDMVTLPKSPPAYARSSDMYSHMGTMPR
FT                                PNIKKAQKQQAVQKAQEVSRESHLVSRRLPEPPDLEAAKEA
FT                                GEGTEALLEDTAPSAVEVDPMRELEDLTVDTEKEQVPGDVS
FT                                PE -> MTAVGRRCSALEPR (in isoform 2).
FT                                {ECO:0000303|PubMed:10692442,
FT                                ECO:0000303|PubMed:16141072}.
FT                                /FTId=VSP_017709.
FT   MUTAGEN     787    787       Y->E: Disrupts binding to BCAR1 and
FT                                inhibits EGF-induced tyrosine
FT                                phosphorylation.
FT                                {ECO:0000269|PubMed:15272013}.
SQ   SEQUENCE   854 AA;  94323 MW;  FA8FC2FDEAE32FF5 CRC64;
     MTEMPKKTGR KFKFFKFKGL GSLSNLPRSF SLRRSSASAS IRSCPEPDTF EATQDDMVTL
     PKSPPAYARS SDMYSHMGTM PRPNIKKAQK QQAVQKAQEV SRESHLVSRR LPEPPDLEAA
     KEAGEGTEAL LEDTAPSAVE VDPMRELEDL TVDTEKEQVP GDVSPERTAA ELEAAGDYVK
     FSKEKYILDS SPEKLHKELE EELKLSSTDL RSHAWYHGRI PREVSETLVQ RNGDFLIRDS
     LTSLGDYVLT CRWHNQALHF KINKVVVKAG ESYTHIRYLF EQESFDHVPA LVRYHVGSRK
     AVSEQSGAII YCPVNRTFPL RYLEASYGLS QGSSKTASPA SPSGSKGSHM KRRSITMTDG
     LTTDKVTRSD GCPNSTSLPH PRDSIRNCAL SMDQIPDLHS PLSPISESPS SPAYSTVTRV
     HAPSATPSTS AQPASPVARR SSEPQLCPGN TPKPPGESDR APHASPSHTL CKASPSPSLS
     SYSDPDSGHY CQLQPPVRGS REQAAGETPR KARGSGERQK ELLENGVSDG EWGKTFTVPV
     VEATSSFNLA TFQSQLIPKE NRPLEVALLR KVKELLSEVD ARTLARHVTK VDCLVARILG
     VTKEMQTLMG VRWGMELLTL PHGRQLRLDL LERFHTMSIM LAVDILGCTG SAEERAALLH
     KTIQLAAELR GTMGNMFSFA AVMGALEMAQ ISRLEQTWMT LRQRHTEGAI LYEKKLKPFL
     KSLNEGKEGP PLSNTTFPHV LPFITLLECD SAPAEGPEPW GSTEHGVEVV LAHLEAARTV
     AHHGGLYHTN AEVKLQGFQA RPELLEVFST EFQMRLLWGS QGANSSQAWR YEKFDKVLTA
     LSHKLEPAIR SSEL
//
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