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Database: UniProt
Entry: Q8N5H7
LinkDB: Q8N5H7
Original site: Q8N5H7 
ID   SH2D3_HUMAN             Reviewed;         860 AA.
AC   Q8N5H7; A8K5S8; E9PG48; Q5HYE5; Q5JU31; Q6UY42; Q8N6X3; Q9Y2X5;
DT   21-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   12-AUG-2020, entry version 154.
DE   RecName: Full=SH2 domain-containing protein 3C;
DE   AltName: Full=Cas/HEF1-associated signal transducer {ECO:0000303|PubMed:17174122};
DE            Short=Chat-H {ECO:0000303|PubMed:17174122};
DE   AltName: Full=Novel SH2-containing protein 3;
DE   AltName: Full=SH2 domain-containing Eph receptor-binding protein 1;
DE            Short=SHEP1;
GN   Name=SH2D3C; Synonyms=NSP3; ORFNames=UNQ272/PRO309/PRO34088;
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] (ISOFORM 2), AND TISSUE SPECIFICITY.
RC   TISSUE=Placenta;
RX   PubMed=10187783; DOI=10.1074/jbc.274.15.10047;
RA   Lu Y., Brush J., Stewart T.A.;
RT   "NSP1 defines a novel family of adaptor proteins linking integrin and
RT   tyrosine kinase receptors to the c-Jun N-terminal kinase/stress-activated
RT   protein kinase signaling pathway.";
RL   J. Biol. Chem. 274:10047-10052(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3).
RX   PubMed=12975309; DOI=10.1101/gr.1293003;
RA   Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J.,
RA   Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P.,
RA   Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E., Heldens S., Huang A.,
RA   Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., Lewis L., Liao D.,
RA   Mark M.R., Robbie E., Sanchez C., Schoenfeld J., Seshagiri S., Simmons L.,
RA   Singh J., Smith V., Stinson J., Vagts A., Vandlen R.L., Watanabe C.,
RA   Wieand D., Woods K., Xie M.-H., Yansura D.G., Yi S., Yu G., Yuan J.,
RA   Zhang M., Zhang Z., Goddard A.D., Wood W.I., Godowski P.J., Gray A.M.;
RT   "The secreted protein discovery initiative (SPDI), a large-scale effort to
RT   identify novel human secreted and transmembrane proteins: a bioinformatics
RT   assessment.";
RL   Genome Res. 13:2265-2270(2003).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 5 AND 6).
RC   TISSUE=Brain;
RX   PubMed=14702039; DOI=10.1038/ng1285;
RA   Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA   Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA   Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA   Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA   Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA   Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA   Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA   Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA   Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA   Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA   Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA   Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA   Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA   Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA   Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA   Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA   Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA   Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA   Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA   Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA   Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA   Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA   Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA   Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA   Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA   Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA   Isogai T., Sugano S.;
RT   "Complete sequencing and characterization of 21,243 full-length human
RT   cDNAs.";
RL   Nat. Genet. 36:40-45(2004).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
RC   TISSUE=Cervix;
RX   PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA   Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA   Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA   Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA   Wiemann S., Schupp I.;
RT   "The full-ORF clone resource of the German cDNA consortium.";
RL   BMC Genomics 8:399-399(2007).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15164053; DOI=10.1038/nature02465;
RA   Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L.,
RA   Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R.,
RA   Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S.,
RA   Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K.,
RA   Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y.,
RA   Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C.,
RA   Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E.,
RA   Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M.,
RA   Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J.,
RA   Frankish A., Frankland J.A., French L., Fricker D.G., Garner P.,
RA   Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S.,
RA   Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E.,
RA   Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D.,
RA   Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E.,
RA   Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K.,
RA   Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S.,
RA   Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J.,
RA   Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E.,
RA   McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V.,
RA   Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S.,
RA   Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K.,
RA   Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J.,
RA   Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M.,
RA   West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L.,
RA   Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M.,
RA   Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J.,
RA   Dunham I.;
RT   "DNA sequence and analysis of human chromosome 9.";
RL   Nature 429:369-374(2004).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC   TISSUE=Pancreas, and Testis;
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   [7]
RP   FUNCTION, IDENTIFICATION IN A COMPLEX WITH BCAR1 AND CRK, AND SUBCELLULAR
RP   LOCATION.
RX   PubMed=12432078; DOI=10.1242/jcs.00207;
RA   Sakakibara A., Ohba Y., Kurokawa K., Matsuda M., Hattori S.;
RT   "Novel function of Chat in controlling cell adhesion via Cas-Crk-C3G-
RT   pathway-mediated Rap1 activation.";
RL   J. Cell Sci. 115:4915-4924(2002).
RN   [8]
RP   INTERACTION WITH BCAR1, AND SUBCELLULAR LOCATION.
RX   PubMed=17174122; DOI=10.1016/j.immuni.2006.09.014;
RA   Regelmann A.G., Danzl N.M., Wanjalla C., Alexandropoulos K.;
RT   "The hematopoietic isoform of Cas-Hef1-associated signal transducer
RT   regulates chemokine-induced inside-out signaling and T cell trafficking.";
RL   Immunity 25:907-918(2006).
RN   [9]
RP   FUNCTION, AND INTERACTION WITH IGF1.
RX   PubMed=20881139; DOI=10.1523/jneurosci.3289-10.2010;
RA   Wang L., Vervoort V., Wallez Y., Core N., Cremer H., Pasquale E.B.;
RT   "The SRC homology 2 domain protein Shep1 plays an important role in the
RT   penetration of olfactory sensory axons into the forebrain.";
RL   J. Neurosci. 30:13201-13210(2010).
RN   [10]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-440, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Erythroleukemia;
RX   PubMed=23186163; DOI=10.1021/pr300630k;
RA   Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA   Mohammed S.;
RT   "Toward a comprehensive characterization of a human cancer cell
RT   phosphoproteome.";
RL   J. Proteome Res. 12:260-271(2013).
RN   [11]
RP   X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 539-860 IN COMPLEX WITH BCAR1.
RX   PubMed=22081014; DOI=10.1038/nsmb.2152;
RA   Mace P.D., Wallez Y., Dobaczewska M.K., Lee J.J., Robinson H.,
RA   Pasquale E.B., Riedl S.J.;
RT   "NSP-Cas protein structures reveal a promiscuous interaction module in cell
RT   signaling.";
RL   Nat. Struct. Mol. Biol. 18:1381-1387(2011).
CC   -!- FUNCTION: Acts as an adapter protein that mediates cell signaling
CC       pathways involved in cellular functions such as cell adhesion and
CC       migration, tissue organization, and the regulation of the immune
CC       response (PubMed:12432078, PubMed:20881139). Plays a role in integrin-
CC       mediated cell adhesion through BCAR1-CRK-RAPGEF1 signaling and
CC       activation of the small GTPase RAP1 (PubMed:12432078). Promotes cell
CC       migration and invasion through the extracellular matrix
CC       (PubMed:20881139). Required for marginal zone B-cell development and
CC       thymus-independent type 2 immune responses (By similarity). Mediates
CC       migration and adhesion of B cells in the splenic marginal zone via
CC       promoting hyperphosphorylation of NEDD9/CASL (By similarity). Plays a
CC       role in CXCL13-induced chemotaxis of B-cells (By similarity). Plays a
CC       role in the migration of olfactory sensory neurons (OSNs) into the
CC       forebrain and the innervation of the olfactory bulb by the OSN axons
CC       during development (By similarity). Required for the efficient tyrosine
CC       phosphorylation of BCAR1 in OSN axons (By similarity).
CC       {ECO:0000250|UniProtKB:Q9QZS8, ECO:0000269|PubMed:12432078,
CC       ECO:0000269|PubMed:20881139}.
CC   -!- FUNCTION: [Isoform 1]: Important regulator of chemokine-induced,
CC       integrin-mediated T lymphocyte adhesion and migration, acting upstream
CC       of RAP1 (By similarity). Required for tissue-specific adhesion of T
CC       lymphocytes to peripheral tissues (By similarity). Required for basal
CC       and CXCL2 stimulated serine-threonine phosphorylation of NEDD9 (By
CC       similarity). May be involved in the regulation of T-cell receptor-
CC       mediated IL2 production through the activation of the JNK pathway in T-
CC       cells (By similarity). {ECO:0000250|UniProtKB:Q9QZS8}.
CC   -!- FUNCTION: [Isoform 2]: May be involved in the BCAR1/CAS-mediated JNK
CC       activation pathway. {ECO:0000250|UniProtKB:Q9QZS8}.
CC   -!- SUBUNIT: Component of a complex comprised of SH2D3C, BCAR1/CAS, and CRK
CC       (PubMed:12432078). Within the complex, interacts with CRK and (via C-
CC       terminus) with BCAR1/CAS (via C-terminus) (PubMed:12432078,
CC       PubMed:17174122, PubMed:22081014). Interacts with NEDD9/HEF1 (By
CC       similarity). Interacts with EPHB2 (By similarity).
CC       {ECO:0000250|UniProtKB:Q9QZS8, ECO:0000269|PubMed:12432078,
CC       ECO:0000269|PubMed:17174122, ECO:0000269|PubMed:22081014}.
CC   -!- SUBUNIT: [Isoform 1]: Interacts with NEDD9/HEF1 (By similarity).
CC       Interacts with BCAR1/CAS (By similarity). Interacts with PTK2B (By
CC       similarity). {ECO:0000250|UniProtKB:Q9QZS8}.
CC   -!- SUBUNIT: [Isoform 2]: Interacts (via C-terminus) with BCAR1/CAS (via C-
CC       terminus) (By similarity). Interacts with IGF1 (PubMed:20881139).
CC       {ECO:0000250|UniProtKB:Q9QZS8, ECO:0000269|PubMed:20881139}.
CC   -!- INTERACTION:
CC       Q8N5H7; P10721: KIT; NbExp=4; IntAct=EBI-745980, EBI-1379503;
CC       Q8N5H7; P08581: MET; NbExp=4; IntAct=EBI-745980, EBI-1039152;
CC       Q8N5H7-2; P56945: BCAR1; NbExp=8; IntAct=EBI-15952996, EBI-702093;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:12432078,
CC       ECO:0000269|PubMed:17174122}. Cell membrane
CC       {ECO:0000269|PubMed:12432078}; Peripheral membrane protein
CC       {ECO:0000250|UniProtKB:Q9QZS8}. Cell projection, axon
CC       {ECO:0000250|UniProtKB:Q9QZS8}. Cell projection, ruffle membrane
CC       {ECO:0000250|UniProtKB:Q9QZS8}. Note=Associated with the membrane when
CC       EGF-stimulated (By similarity). Expressed at the cortical actin ring in
CC       B cells (By similarity). {ECO:0000250|UniProtKB:Q9QZS8}.
CC   -!- SUBCELLULAR LOCATION: [Isoform 1]: Cell membrane
CC       {ECO:0000269|PubMed:17174122}; Peripheral membrane protein
CC       {ECO:0000269|PubMed:17174122}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=6;
CC       Name=1; Synonyms=Chat-H {ECO:0000303|PubMed:17174122};
CC         IsoId=Q8N5H7-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q8N5H7-2; Sequence=VSP_017707;
CC       Name=3;
CC         IsoId=Q8N5H7-3; Sequence=VSP_017706;
CC       Name=4;
CC         IsoId=Q8N5H7-4; Sequence=VSP_017708;
CC       Name=5;
CC         IsoId=Q8N5H7-5; Sequence=VSP_044581, VSP_044582;
CC       Name=6;
CC         IsoId=Q8N5H7-6; Sequence=VSP_044581;
CC   -!- TISSUE SPECIFICITY: [Isoform 1]: Ubiquitously expressed.
CC       {ECO:0000269|PubMed:10187783}.
CC   -!- DOMAIN: The C-terminal Cdc25-homology/Ras-GEF domain adopts a closed
CC       conformation rendering it incapable of carrying out canonical exchange
CC       factor function, this closed conformation is required for interaction
CC       with BCAR1.
CC   -!- PTM: [Isoform 1]: Phosphorylated by MAPK/ERK upon T-cell receptor
CC       stimulation in T-cells. {ECO:0000250|UniProtKB:Q9QZS8}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAQ88456.1; Type=Erroneous initiation; Evidence={ECO:0000305};
DR   EMBL; AF124251; AAD28246.1; -; mRNA.
DR   EMBL; AY358089; AAQ88456.1; ALT_INIT; Transcribed_RNA.
DR   EMBL; AY358440; AAQ89948.1; -; mRNA.
DR   EMBL; AK056068; BAG51614.1; -; mRNA.
DR   EMBL; AK291393; BAF84082.1; -; mRNA.
DR   EMBL; BX647905; CAI46101.1; -; mRNA.
DR   EMBL; AL162586; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AL162426; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC027962; AAH27962.1; -; mRNA.
DR   EMBL; BC032365; AAH32365.1; -; mRNA.
DR   CCDS; CCDS48026.1; -. [Q8N5H7-5]
DR   CCDS; CCDS48027.1; -. [Q8N5H7-6]
DR   CCDS; CCDS48028.1; -. [Q8N5H7-3]
DR   CCDS; CCDS59145.1; -. [Q8N5H7-4]
DR   CCDS; CCDS6877.1; -. [Q8N5H7-1]
DR   CCDS; CCDS6878.1; -. [Q8N5H7-2]
DR   RefSeq; NP_001136004.1; NM_001142532.1. [Q8N5H7-3]
DR   RefSeq; NP_001136005.1; NM_001142533.1. [Q8N5H7-5]
DR   RefSeq; NP_001136006.1; NM_001142534.1. [Q8N5H7-6]
DR   RefSeq; NP_001239263.1; NM_001252334.1. [Q8N5H7-4]
DR   RefSeq; NP_005480.2; NM_005489.3. [Q8N5H7-2]
DR   RefSeq; NP_733745.1; NM_170600.2. [Q8N5H7-1]
DR   RefSeq; XP_005251696.1; XM_005251639.1.
DR   RefSeq; XP_011516419.1; XM_011518117.2.
DR   RefSeq; XP_016869663.1; XM_017014174.1.
DR   PDB; 3T6G; X-ray; 2.50 A; A/C=539-860.
DR   PDBsum; 3T6G; -.
DR   SMR; Q8N5H7; -.
DR   BioGRID; 115355; 6.
DR   DIP; DIP-59443N; -.
DR   IntAct; Q8N5H7; 161.
DR   MINT; Q8N5H7; -.
DR   STRING; 9606.ENSP00000317817; -.
DR   iPTMnet; Q8N5H7; -.
DR   PhosphoSitePlus; Q8N5H7; -.
DR   BioMuta; SH2D3C; -.
DR   DMDM; 74751027; -.
DR   EPD; Q8N5H7; -.
DR   jPOST; Q8N5H7; -.
DR   MassIVE; Q8N5H7; -.
DR   MaxQB; Q8N5H7; -.
DR   PaxDb; Q8N5H7; -.
DR   PeptideAtlas; Q8N5H7; -.
DR   PRIDE; Q8N5H7; -.
DR   ProteomicsDB; 20244; -.
DR   ProteomicsDB; 72054; -. [Q8N5H7-1]
DR   ProteomicsDB; 72055; -. [Q8N5H7-2]
DR   ProteomicsDB; 72056; -. [Q8N5H7-3]
DR   ProteomicsDB; 72057; -. [Q8N5H7-4]
DR   ProteomicsDB; 72058; -. [Q8N5H7-5]
DR   Antibodypedia; 30796; 268 antibodies.
DR   DNASU; 10044; -.
DR   Ensembl; ENST00000314830; ENSP00000317817; ENSG00000095370. [Q8N5H7-1]
DR   Ensembl; ENST00000373276; ENSP00000362373; ENSG00000095370. [Q8N5H7-4]
DR   Ensembl; ENST00000373277; ENSP00000362374; ENSG00000095370. [Q8N5H7-2]
DR   Ensembl; ENST00000420366; ENSP00000388536; ENSG00000095370. [Q8N5H7-5]
DR   Ensembl; ENST00000429553; ENSP00000394632; ENSG00000095370. [Q8N5H7-3]
DR   Ensembl; ENST00000629203; ENSP00000485866; ENSG00000095370. [Q8N5H7-6]
DR   GeneID; 10044; -.
DR   KEGG; hsa:10044; -.
DR   UCSC; uc004bry.4; human. [Q8N5H7-1]
DR   CTD; 10044; -.
DR   DisGeNET; 10044; -.
DR   EuPathDB; HostDB:ENSG00000095370.19; -.
DR   GeneCards; SH2D3C; -.
DR   HGNC; HGNC:16884; SH2D3C.
DR   HPA; ENSG00000095370; Low tissue specificity.
DR   MIM; 604722; gene.
DR   neXtProt; NX_Q8N5H7; -.
DR   OpenTargets; ENSG00000095370; -.
DR   PharmGKB; PA38191; -.
DR   eggNOG; ENOG502QPX3; Eukaryota.
DR   GeneTree; ENSGT00940000154130; -.
DR   HOGENOM; CLU_015281_0_0_1; -.
DR   InParanoid; Q8N5H7; -.
DR   KO; K23690; -.
DR   OMA; LWNFRYP; -.
DR   OrthoDB; 138275at2759; -.
DR   PhylomeDB; Q8N5H7; -.
DR   TreeFam; TF323756; -.
DR   PathwayCommons; Q8N5H7; -.
DR   SignaLink; Q8N5H7; -.
DR   BioGRID-ORCS; 10044; 4 hits in 870 CRISPR screens.
DR   ChiTaRS; SH2D3C; human.
DR   GeneWiki; SH2D3C; -.
DR   GenomeRNAi; 10044; -.
DR   Pharos; Q8N5H7; Tbio.
DR   PRO; PR:Q8N5H7; -.
DR   Proteomes; UP000005640; Chromosome 9.
DR   RNAct; Q8N5H7; protein.
DR   Bgee; ENSG00000095370; Expressed in right lung and 182 other tissues.
DR   ExpressionAtlas; Q8N5H7; baseline and differential.
DR   Genevisible; Q8N5H7; HS.
DR   GO; GO:0030424; C:axon; IEA:UniProtKB-SubCell.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0032587; C:ruffle membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IEA:InterPro.
DR   GO; GO:0007254; P:JNK cascade; TAS:ProtInc.
DR   GO; GO:0033138; P:positive regulation of peptidyl-serine phosphorylation; IBA:GO_Central.
DR   GO; GO:0007264; P:small GTPase mediated signal transduction; IEA:InterPro.
DR   Gene3D; 1.10.840.10; -; 1.
DR   Gene3D; 3.30.505.10; -; 1.
DR   InterPro; IPR023578; Ras_GEF_dom_sf.
DR   InterPro; IPR001895; RASGEF_cat_dom.
DR   InterPro; IPR036964; RASGEF_cat_dom_sf.
DR   InterPro; IPR000980; SH2.
DR   InterPro; IPR036860; SH2_dom_sf.
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   3D-structure; Alternative splicing; Cell membrane; Cell projection;
KW   Cytoplasm; Membrane; Phosphoprotein; Polymorphism; Reference proteome;
KW   SH2 domain.
FT   CHAIN           1..860
FT                   /note="SH2 domain-containing protein 3C"
FT                   /id="PRO_0000228833"
FT   DOMAIN          220..319
FT                   /note="SH2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00191"
FT   DOMAIN          586..854
FT                   /note="Ras-GEF"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00168"
FT   MOD_RES         22
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9QZS8"
FT   MOD_RES         278
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9QZS8"
FT   MOD_RES         283
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9QZS8"
FT   MOD_RES         359
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9QZS8"
FT   MOD_RES         440
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000244|PubMed:23186163"
FT   MOD_RES         793
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9QZS8"
FT   VAR_SEQ         1..354
FT                   /note="Missing (in isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:12975309"
FT                   /id="VSP_017706"
FT   VAR_SEQ         1..185
FT                   /note="MTEGTKKTSKKFKFFKFKGFGSLSNLPRSFTLRRSSASISRQSHLEPDTFEA
FT                   TQDDMVTVPKSPPAYARSSDMYSHMGTMPRPSIKKAQNSQAARQAQEAGPKPNLVPGGV
FT                   PDPPGLEAAKEVMVKATGPLEDTPAMEPNPSAVEVDPIRKPEVPTGDVEEERPPRDVHS
FT                   ERAAGEPEAGSDYVK -> MTERCSLWSALSAAACCFYRGSFVQ (in isoform 5
FT                   and isoform 6)"
FT                   /evidence="ECO:0000303|PubMed:14702039"
FT                   /id="VSP_044581"
FT   VAR_SEQ         1..172
FT                   /note="MTEGTKKTSKKFKFFKFKGFGSLSNLPRSFTLRRSSASISRQSHLEPDTFEA
FT                   TQDDMVTVPKSPPAYARSSDMYSHMGTMPRPSIKKAQNSQAARQAQEAGPKPNLVPGGV
FT                   PDPPGLEAAKEVMVKATGPLEDTPAMEPNPSAVEVDPIRKPEVPTGDVEEERPPRDVHS
FT                   ER -> MTAVGRRCPALGSRG (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:10187783,
FT                   ECO:0000303|PubMed:12975309, ECO:0000303|PubMed:15489334"
FT                   /id="VSP_017707"
FT   VAR_SEQ         1..172
FT                   /note="MTEGTKKTSKKFKFFKFKGFGSLSNLPRSFTLRRSSASISRQSHLEPDTFEA
FT                   TQDDMVTVPKSPPAYARSSDMYSHMGTMPRPSIKKAQNSQAARQAQEAGPKPNLVPGGV
FT                   PDPPGLEAAKEVMVKATGPLEDTPAMEPNPSAVEVDPIRKPEVPTGDVEEERPPRDVHS
FT                   ER -> MAPALPSPHKAVARPELLLDTAAHSGKLRAPDGGEGAECAGHNGGPSWGVGQG
FT                   QSQEPSRQGIPQAPWLVSWQRRGFPPSSFCPGPLRTEKLRAGRCPLLLCGG (in
FT                   isoform 4)"
FT                   /evidence="ECO:0000303|PubMed:17974005"
FT                   /id="VSP_017708"
FT   VAR_SEQ         186
FT                   /note="F -> VQF (in isoform 5)"
FT                   /evidence="ECO:0000303|PubMed:14702039"
FT                   /id="VSP_044582"
FT   VARIANT         23
FT                   /note="L -> F (in dbSNP:rs10760500)"
FT                   /id="VAR_051352"
FT   CONFLICT        445
FT                   /note="R -> C (in Ref. 1; AAD28246 and 2; AAQ89948)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        723
FT                   /note="K -> E (in Ref. 3; BAF84082)"
FT                   /evidence="ECO:0000305"
FT   HELIX           555..557
FT                   /evidence="ECO:0000244|PDB:3T6G"
FT   STRAND          561..563
FT                   /evidence="ECO:0000244|PDB:3T6G"
FT   HELIX           572..583
FT                   /evidence="ECO:0000244|PDB:3T6G"
FT   HELIX           587..601
FT                   /evidence="ECO:0000244|PDB:3T6G"
FT   STRAND          604..606
FT                   /evidence="ECO:0000244|PDB:3T6G"
FT   HELIX           609..615
FT                   /evidence="ECO:0000244|PDB:3T6G"
FT   STRAND          616..618
FT                   /evidence="ECO:0000244|PDB:3T6G"
FT   HELIX           620..623
FT                   /evidence="ECO:0000244|PDB:3T6G"
FT   HELIX           627..629
FT                   /evidence="ECO:0000244|PDB:3T6G"
FT   HELIX           630..652
FT                   /evidence="ECO:0000244|PDB:3T6G"
FT   HELIX           658..677
FT                   /evidence="ECO:0000244|PDB:3T6G"
FT   HELIX           682..692
FT                   /evidence="ECO:0000244|PDB:3T6G"
FT   HELIX           695..698
FT                   /evidence="ECO:0000244|PDB:3T6G"
FT   HELIX           701..710
FT                   /evidence="ECO:0000244|PDB:3T6G"
FT   HELIX           712..720
FT                   /evidence="ECO:0000244|PDB:3T6G"
FT   HELIX           722..730
FT                   /evidence="ECO:0000244|PDB:3T6G"
FT   HELIX           738..740
FT                   /evidence="ECO:0000244|PDB:3T6G"
FT   HELIX           747..752
FT                   /evidence="ECO:0000244|PDB:3T6G"
FT   HELIX           773..787
FT                   /evidence="ECO:0000244|PDB:3T6G"
FT   HELIX           790..800
FT                   /evidence="ECO:0000244|PDB:3T6G"
FT   TURN            801..803
FT                   /evidence="ECO:0000244|PDB:3T6G"
FT   HELIX           808..813
FT                   /evidence="ECO:0000244|PDB:3T6G"
FT   HELIX           816..824
FT                   /evidence="ECO:0000244|PDB:3T6G"
FT   HELIX           828..830
FT                   /evidence="ECO:0000244|PDB:3T6G"
FT   HELIX           833..851
FT                   /evidence="ECO:0000244|PDB:3T6G"
FT   CONFLICT        Q8N5H7-3:29
FT                   /note="L -> T (in Ref. 4; CAI46101)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   860 AA;  94411 MW;  62598F2F643147C5 CRC64;
     MTEGTKKTSK KFKFFKFKGF GSLSNLPRSF TLRRSSASIS RQSHLEPDTF EATQDDMVTV
     PKSPPAYARS SDMYSHMGTM PRPSIKKAQN SQAARQAQEA GPKPNLVPGG VPDPPGLEAA
     KEVMVKATGP LEDTPAMEPN PSAVEVDPIR KPEVPTGDVE EERPPRDVHS ERAAGEPEAG
     SDYVKFSKEK YILDSSPEKL HKELEEELKL SSTDLRSHAW YHGRIPREVS ETLVQRNGDF
     LIRDSLTSLG DYVLTCRWRN QALHFKINKV VVKAGESYTH IQYLFEQESF DHVPALVRYH
     VGSRKAVSEQ SGAIIYCPVN RTFPLRYLEA SYGLGQGSSK PASPVSPSGP KGSHMKRRSV
     TMTDGLTADK VTRSDGCPTS TSLPRPRDSI RSCALSMDQI PDLHSPMSPI SESPSSPAYS
     TVTRVHAAPA APSATALPAS PVARRSSEPQ LCPGSAPKTH GESDKGPHTS PSHTLGKASP
     SPSLSSYSDP DSGHYCQLQP PVRGSREWAA TETSSQQARS YGERLKELSE NGAPEGDWGK
     TFTVPIVEVT SSFNPATFQS LLIPRDNRPL EVGLLRKVKE LLAEVDARTL ARHVTKVDCL
     VARILGVTKE MQTLMGVRWG MELLTLPHGR QLRLDLLERF HTMSIMLAVD ILGCTGSAEE
     RAALLHKTIQ LAAELRGTMG NMFSFAAVMG ALDMAQISRL EQTWVTLRQR HTEGAILYEK
     KLKPFLKSLN EGKEGPPLSN TTFPHVLPLI TLLECDSAPP EGPEPWGSTE HGVEVVLAHL
     EAARTVAHHG GLYHTNAEVK LQGFQARPEL LEVFSTEFQM RLLWGSQGAS SSQARRYEKF
     DKVLTALSHK LEPAVRSSEL
//
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