ELMO2_HUMAN
ID ELMO2_HUMAN Reviewed; 720 AA.
AC Q96JJ3; E1P5T3; Q5JVZ6; Q7Z5G9; Q96CJ2; Q96ME5; Q96PA9; Q9H938; Q9H9L5;
AC Q9HAH0; Q9NQQ6;
DT 16-MAY-2003, integrated into UniProtKB/Swiss-Prot.
DT 16-MAY-2003, sequence version 2.
DT 03-AUG-2022, entry version 180.
DE RecName: Full=Engulfment and cell motility protein 2;
DE AltName: Full=Protein ced-12 homolog A;
DE Short=hCed-12A;
GN Name=ELMO2; Synonyms=CED12A, KIAA1834;
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 1), TISSUE SPECIFICITY, FUNCTION, AND
RP INTERACTION WITH DOCK1.
RX PubMed=11595183; DOI=10.1016/s0092-8674(01)00520-7;
RA Gumienny T.L., Brugnera E., Tosello-Trampont A.-C., Kinchen J.M.,
RA Haney L.B., Nishiwaki K., Walk S.F., Nemergut M.E., Macara I.G.,
RA Francis R., Schedl T., Qin Y., Van Aelst L., Hengartner M.O.,
RA Ravichandran K.S.;
RT "CED-12/ELMO, a novel member of the CrkII/Dock180/Rac pathway, is required
RT for phagocytosis and cell migration.";
RL Cell 107:27-41(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND FUNCTION.
RC TISSUE=Testis;
RX PubMed=11703939; DOI=10.1016/s1534-5807(01)00058-2;
RA Zhou Z., Caron E., Hartwieg E., Hall A., Horvitz H.R.;
RT "The C. elegans PH domain protein CED-12 regulates cytoskeletal
RT reorganization via a Rho/Rac GTPase signaling pathway.";
RL Dev. Cell 1:477-489(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=11347906; DOI=10.1093/dnares/8.2.85;
RA Nagase T., Nakayama M., Nakajima D., Kikuno R., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XX. The
RT complete sequences of 100 new cDNA clones from brain which code for large
RT proteins in vitro.";
RL DNA Res. 8:85-95(2001).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Embryo, Neuroepithelioma, and Teratocarcinoma;
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=11780052; DOI=10.1038/414865a;
RA Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R.,
RA Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L.,
RA Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P.,
RA Bird C.P., Blakey S.E., Bridgeman A.M., Brown A.J., Buck D., Burrill W.D.,
RA Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G.,
RA Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E.,
RA Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D.,
RA Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P.,
RA Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E.,
RA Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J.,
RA Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D.,
RA Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S.,
RA Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D.,
RA Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A.,
RA Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T.,
RA Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I.,
RA Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M.,
RA Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D.,
RA Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M.,
RA Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A.,
RA Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L.,
RA Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L.,
RA Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J.;
RT "The DNA sequence and comparative analysis of human chromosome 20.";
RL Nature 414:865-871(2001).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.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 [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Cervix;
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 [8]
RP FUNCTION, INTERACTION WITH ARHGEF16; DOCK4 AND EPHA2, AND SUBCELLULAR
RP LOCATION.
RX PubMed=20679435; DOI=10.1083/jcb.201005141;
RA Hiramoto-Yamaki N., Takeuchi S., Ueda S., Harada K., Fujimoto S.,
RA Negishi M., Katoh H.;
RT "Ephexin4 and EphA2 mediate cell migration through a RhoG-dependent
RT mechanism.";
RL J. Cell Biol. 190:461-477(2010).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-503, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and 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 INTERACTION WITH ADGRB3.
RX PubMed=24567399; DOI=10.1073/pnas.1313886111;
RA Hamoud N., Tran V., Croteau L.P., Kania A., Cote J.F.;
RT "G-protein coupled receptor BAI3 promotes myoblast fusion in vertebrates.";
RL Proc. Natl. Acad. Sci. U.S.A. 111:3745-3750(2014).
RN [12]
RP FUNCTION, AND INVOLVEMENT IN VMOS.
RX PubMed=27476657; DOI=10.1016/j.ajhg.2016.06.008;
RA Cetinkaya A., Xiong J.R., Vargel I., Koesemehmetoglu K., Canter H.I.,
RA Gerdan O.F., Longo N., Alzahrani A., Camps M.P., Taskiran E.Z.,
RA Laupheimer S., Botto L.D., Paramalingam E., Gormez Z., Uz E., Yuksel B.,
RA Ruacan S., Sagiroglu M.S., Takahashi T., Reversade B., Akarsu N.A.;
RT "Loss-of-function mutations in ELMO2 cause intraosseous vascular
RT malformation by impeding RAC1 signaling.";
RL Am. J. Hum. Genet. 99:299-317(2016).
CC -!- FUNCTION: Involved in cytoskeletal rearrangements required for
CC phagocytosis of apoptotic cells and cell motility. Acts in association
CC with DOCK1 and CRK. Was initially proposed to be required in complex
CC with DOCK1 to activate Rac Rho small GTPases. May enhance the guanine
CC nucleotide exchange factor (GEF) activity of DOCK1.
CC {ECO:0000269|PubMed:11595183, ECO:0000269|PubMed:11703939,
CC ECO:0000269|PubMed:20679435, ECO:0000269|PubMed:27476657}.
CC -!- SUBUNIT: Interacts with the SH3-domain of DOCK1 via its SH3-binding
CC site. Probably part of a complex with DOCK1 and RAC1. Probably part of
CC a complex with DOCK1 and CRK isoform CRK-II. Interacts with ARHGEF16,
CC DOCK4 and EPHA2; mediates activation of RAC1 by EPHA2
CC (PubMed:20679435). Interacts with ADGRB3 (PubMed:24567399). Interacts
CC with AUTS2; the interaction is direct (By similarity).
CC {ECO:0000250|UniProtKB:Q8BHL5, ECO:0000269|PubMed:11595183,
CC ECO:0000269|PubMed:20679435, ECO:0000269|PubMed:24567399}.
CC -!- INTERACTION:
CC Q96JJ3; Q149N5: DOCK4; NbExp=3; IntAct=EBI-3959230, EBI-13336133;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:20679435}.
CC Cytoplasm, cytosol {ECO:0000269|PubMed:20679435}. Membrane
CC {ECO:0000269|PubMed:20679435}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q96JJ3-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q96JJ3-3; Sequence=VSP_055477;
CC -!- TISSUE SPECIFICITY: Widely expressed, with a higher expression in
CC skeletal muscle, kidney and placenta. {ECO:0000269|PubMed:11595183}.
CC -!- DISEASE: Vascular malformation, primary intraosseous (VMOS)
CC [MIM:606893]: A rare malformation characterized by non-neoplastic
CC severe expansions of blood vessels, usually seen in the vertebral
CC column and in the skull. The most commonly affected bones in the skull
CC are the mandible and the maxilla, and life-threatening bleeding after a
CC simple tooth extraction is frequently observed. Inheritance is
CC autosomal recessive. {ECO:0000269|PubMed:27476657}. Note=The disease is
CC caused by variants affecting the gene represented in this entry.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB13879.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAB14210.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAB14405.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAB47463.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AF398886; AAL14467.1; -; Transcribed_RNA.
DR EMBL; AF417861; AAL38512.1; -; mRNA.
DR EMBL; AB058737; BAB47463.1; ALT_INIT; mRNA.
DR EMBL; AK021718; BAB13879.1; ALT_INIT; mRNA.
DR EMBL; AK022731; BAB14210.1; ALT_INIT; mRNA.
DR EMBL; AK023103; BAB14405.1; ALT_INIT; mRNA.
DR EMBL; AK057032; BAB71350.1; -; mRNA.
DR EMBL; AL031686; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL133227; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471077; EAW75739.1; -; Genomic_DNA.
DR EMBL; CH471077; EAW75743.1; -; Genomic_DNA.
DR EMBL; CH471077; EAW75745.1; -; Genomic_DNA.
DR EMBL; CH471077; EAW75746.1; -; Genomic_DNA.
DR EMBL; BC000143; AAH00143.2; -; mRNA.
DR CCDS; CCDS13398.1; -. [Q96JJ3-1]
DR CCDS; CCDS82623.1; -. [Q96JJ3-3]
DR RefSeq; NP_001305182.1; NM_001318253.1. [Q96JJ3-3]
DR RefSeq; NP_573403.1; NM_133171.4. [Q96JJ3-1]
DR RefSeq; NP_877496.1; NM_182764.2. [Q96JJ3-1]
DR RefSeq; XP_005260553.1; XM_005260496.3. [Q96JJ3-1]
DR RefSeq; XP_005260555.1; XM_005260498.3. [Q96JJ3-3]
DR RefSeq; XP_005260556.1; XM_005260499.3. [Q96JJ3-3]
DR RefSeq; XP_005260557.1; XM_005260500.3. [Q96JJ3-3]
DR RefSeq; XP_006723917.1; XM_006723854.3. [Q96JJ3-1]
DR PDB; 6IDX; X-ray; 1.70 A; A=1-520.
DR PDB; 6IE1; X-ray; 2.48 A; A=1-520.
DR PDBsum; 6IDX; -.
DR PDBsum; 6IE1; -.
DR AlphaFoldDB; Q96JJ3; -.
DR SMR; Q96JJ3; -.
DR BioGRID; 121987; 42.
DR IntAct; Q96JJ3; 15.
DR STRING; 9606.ENSP00000290246; -.
DR iPTMnet; Q96JJ3; -.
DR MetOSite; Q96JJ3; -.
DR PhosphoSitePlus; Q96JJ3; -.
DR BioMuta; ELMO2; -.
DR DMDM; 30913107; -.
DR CPTAC; CPTAC-1765; -.
DR EPD; Q96JJ3; -.
DR jPOST; Q96JJ3; -.
DR MassIVE; Q96JJ3; -.
DR MaxQB; Q96JJ3; -.
DR PaxDb; Q96JJ3; -.
DR PeptideAtlas; Q96JJ3; -.
DR PRIDE; Q96JJ3; -.
DR ProteomicsDB; 69288; -.
DR ProteomicsDB; 76970; -. [Q96JJ3-1]
DR Antibodypedia; 13191; 254 antibodies from 32 providers.
DR DNASU; 63916; -.
DR Ensembl; ENST00000290246.11; ENSP00000290246.6; ENSG00000062598.18. [Q96JJ3-1]
DR Ensembl; ENST00000372176.5; ENSP00000361249.1; ENSG00000062598.18. [Q96JJ3-3]
DR Ensembl; ENST00000396391.5; ENSP00000379673.1; ENSG00000062598.18. [Q96JJ3-1]
DR GeneID; 63916; -.
DR KEGG; hsa:63916; -.
DR MANE-Select; ENST00000290246.11; ENSP00000290246.6; NM_133171.5; NP_573403.1.
DR UCSC; uc002xrt.2; human. [Q96JJ3-1]
DR CTD; 63916; -.
DR DisGeNET; 63916; -.
DR GeneCards; ELMO2; -.
DR HGNC; HGNC:17233; ELMO2.
DR HPA; ENSG00000062598; Low tissue specificity.
DR MalaCards; ELMO2; -.
DR MIM; 606421; gene.
DR MIM; 606893; phenotype.
DR neXtProt; NX_Q96JJ3; -.
DR OpenTargets; ENSG00000062598; -.
DR Orphanet; 140436; Primary intraosseous venous malformation.
DR Orphanet; 3019; Ramon syndrome.
DR PharmGKB; PA27755; -.
DR VEuPathDB; HostDB:ENSG00000062598; -.
DR eggNOG; KOG2999; Eukaryota.
DR GeneTree; ENSGT00940000159236; -.
DR HOGENOM; CLU_023887_0_0_1; -.
DR InParanoid; Q96JJ3; -.
DR OMA; XDMANAF; -.
DR OrthoDB; 234725at2759; -.
DR PhylomeDB; Q96JJ3; -.
DR TreeFam; TF312966; -.
DR PathwayCommons; Q96JJ3; -.
DR Reactome; R-HSA-2029482; Regulation of actin dynamics for phagocytic cup formation.
DR Reactome; R-HSA-4420097; VEGFA-VEGFR2 Pathway.
DR Reactome; R-HSA-8849471; PTK6 Regulates RHO GTPases, RAS GTPase and MAP kinases.
DR Reactome; R-HSA-9013408; RHOG GTPase cycle.
DR Reactome; R-HSA-9664422; FCGR3A-mediated phagocytosis.
DR SignaLink; Q96JJ3; -.
DR SIGNOR; Q96JJ3; -.
DR BioGRID-ORCS; 63916; 155 hits in 1086 CRISPR screens.
DR ChiTaRS; ELMO2; human.
DR GeneWiki; ELMO2; -.
DR GenomeRNAi; 63916; -.
DR Pharos; Q96JJ3; Tbio.
DR PRO; PR:Q96JJ3; -.
DR Proteomes; UP000005640; Chromosome 20.
DR RNAct; Q96JJ3; protein.
DR Bgee; ENSG00000062598; Expressed in cerebellar hemisphere and 199 other tissues.
DR ExpressionAtlas; Q96JJ3; baseline and differential.
DR Genevisible; Q96JJ3; HS.
DR GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR GO; GO:0016020; C:membrane; IDA:UniProtKB.
DR GO; GO:0030971; F:receptor tyrosine kinase binding; IPI:UniProtKB.
DR GO; GO:0017124; F:SH3 domain binding; IEA:UniProtKB-KW.
DR GO; GO:0007015; P:actin filament organization; IBA:GO_Central.
DR GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR GO; GO:0060326; P:cell chemotaxis; IMP:UniProtKB.
DR GO; GO:0048870; P:cell motility; IBA:GO_Central.
DR GO; GO:0098609; P:cell-cell adhesion; IEA:InterPro.
DR GO; GO:0006909; P:phagocytosis; IEA:UniProtKB-KW.
DR Gene3D; 1.25.10.10; -; 1.
DR Gene3D; 2.30.29.30; -; 1.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR030713; ELMO2.
DR InterPro; IPR024574; ELMO_ARM.
DR InterPro; IPR006816; ELMO_dom.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR001849; PH_domain.
DR PANTHER; PTHR12771:SF8; PTHR12771:SF8; 1.
DR Pfam; PF11841; DUF3361; 1.
DR Pfam; PF04727; ELMO_CED12; 1.
DR Pfam; PF16457; PH_12; 1.
DR SUPFAM; SSF48371; SSF48371; 1.
DR PROSITE; PS51335; ELMO; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Apoptosis; Cytoplasm; Membrane;
KW Phagocytosis; Phosphoprotein; Reference proteome; SH3-binding.
FT CHAIN 1..720
FT /note="Engulfment and cell motility protein 2"
FT /id="PRO_0000153714"
FT DOMAIN 311..485
FT /note="ELMO"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00664"
FT DOMAIN 553..674
FT /note="PH"
FT MOTIF 700..707
FT /note="SH3-binding"
FT MOD_RES 48
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q8BHL5"
FT MOD_RES 503
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 717
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q8BHL5"
FT VAR_SEQ 1..88
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_055477"
FT VARIANT 695
FT /note="E -> D (in dbSNP:rs34630674)"
FT /id="VAR_048928"
FT CONFLICT 208
FT /note="Y -> C (in Ref. 4; BAB71350)"
FT /evidence="ECO:0000305"
FT CONFLICT 299
FT /note="E -> G (in Ref. 4; BAB13879)"
FT /evidence="ECO:0000305"
FT CONFLICT 509
FT /note="R -> P (in Ref. 4; BAB13879)"
FT /evidence="ECO:0000305"
FT CONFLICT 586
FT /note="D -> N (in Ref. 4; BAB14210)"
FT /evidence="ECO:0000305"
FT STRAND 7..13
FT /evidence="ECO:0007829|PDB:6IDX"
FT STRAND 20..25
FT /evidence="ECO:0007829|PDB:6IDX"
FT HELIX 30..40
FT /evidence="ECO:0007829|PDB:6IDX"
FT HELIX 46..48
FT /evidence="ECO:0007829|PDB:6IDX"
FT STRAND 49..55
FT /evidence="ECO:0007829|PDB:6IDX"
FT HELIX 65..68
FT /evidence="ECO:0007829|PDB:6IDX"
FT STRAND 73..79
FT /evidence="ECO:0007829|PDB:6IDX"
FT HELIX 81..91
FT /evidence="ECO:0007829|PDB:6IDX"
FT HELIX 97..110
FT /evidence="ECO:0007829|PDB:6IDX"
FT HELIX 114..121
FT /evidence="ECO:0007829|PDB:6IDX"
FT TURN 122..124
FT /evidence="ECO:0007829|PDB:6IDX"
FT HELIX 125..135
FT /evidence="ECO:0007829|PDB:6IDX"
FT TURN 139..142
FT /evidence="ECO:0007829|PDB:6IDX"
FT HELIX 144..158
FT /evidence="ECO:0007829|PDB:6IDX"
FT HELIX 165..167
FT /evidence="ECO:0007829|PDB:6IDX"
FT HELIX 170..181
FT /evidence="ECO:0007829|PDB:6IDX"
FT HELIX 187..203
FT /evidence="ECO:0007829|PDB:6IDX"
FT HELIX 205..214
FT /evidence="ECO:0007829|PDB:6IDX"
FT HELIX 217..222
FT /evidence="ECO:0007829|PDB:6IDX"
FT HELIX 223..225
FT /evidence="ECO:0007829|PDB:6IDX"
FT HELIX 229..245
FT /evidence="ECO:0007829|PDB:6IDX"
FT HELIX 248..250
FT /evidence="ECO:0007829|PDB:6IDX"
FT HELIX 251..260
FT /evidence="ECO:0007829|PDB:6IDX"
FT HELIX 263..270
FT /evidence="ECO:0007829|PDB:6IDX"
FT TURN 271..273
FT /evidence="ECO:0007829|PDB:6IDX"
FT STRAND 274..276
FT /evidence="ECO:0007829|PDB:6IDX"
FT HELIX 280..295
FT /evidence="ECO:0007829|PDB:6IDX"
FT HELIX 298..301
FT /evidence="ECO:0007829|PDB:6IDX"
FT HELIX 310..324
FT /evidence="ECO:0007829|PDB:6IDX"
FT HELIX 339..346
FT /evidence="ECO:0007829|PDB:6IDX"
FT TURN 347..349
FT /evidence="ECO:0007829|PDB:6IDX"
FT HELIX 350..352
FT /evidence="ECO:0007829|PDB:6IDX"
FT STRAND 355..358
FT /evidence="ECO:0007829|PDB:6IDX"
FT HELIX 360..365
FT /evidence="ECO:0007829|PDB:6IDX"
FT TURN 367..369
FT /evidence="ECO:0007829|PDB:6IDX"
FT HELIX 370..383
FT /evidence="ECO:0007829|PDB:6IDX"
FT HELIX 385..393
FT /evidence="ECO:0007829|PDB:6IDX"
FT HELIX 406..421
FT /evidence="ECO:0007829|PDB:6IDX"
FT TURN 422..424
FT /evidence="ECO:0007829|PDB:6IDX"
FT HELIX 436..440
FT /evidence="ECO:0007829|PDB:6IDX"
FT HELIX 444..462
FT /evidence="ECO:0007829|PDB:6IDX"
FT HELIX 467..469
FT /evidence="ECO:0007829|PDB:6IDX"
FT HELIX 470..484
FT /evidence="ECO:0007829|PDB:6IDX"
FT HELIX 485..487
FT /evidence="ECO:0007829|PDB:6IDX"
FT HELIX 492..500
FT /evidence="ECO:0007829|PDB:6IDX"
FT HELIX 504..514
FT /evidence="ECO:0007829|PDB:6IDX"
SQ SEQUENCE 720 AA; 82615 MW; A67377E3B26F2937 CRC64;
MPPPSDIVKV AIEWPGANAQ LLEIDQKRPL ASIIKEVCDG WSLPNPEYYT LRYADGPQLY
ITEQTRSDIK NGTILQLAIS PSRAARQLME RTQSSNMETR LDAMKELAKL SADVTFATEF
INMDGIIVLT RLVESGTKLL SHYSEMLAFT LTAFLELMDH GIVSWDMVSI TFIKQIAGYV
SQPMVDVSIL QRSLAILESM VLNSQSLYQK IAEEITVGQL ISHLQVSNQE IQTYAIALIN
ALFLKAPEDK RQDMANAFAQ KHLRSIILNH VIRGNRPIKT EMAHQLYVLQ VLTFNLLEER
MMTKMDPNDQ AQRDIIFELR RIAFDAESDP SNAPGSGTEK RKAMYTKDYK MLGFTNHINP
AMDFTQTPPG MLALDNMLYL AKVHQDTYIR IVLENSSRED KHECPFGRSA IELTKMLCEI
LQVGELPNEG RNDYHPMFFT HDRAFEELFG ICIQLLNKTW KEMRATAEDF NKVMQVVREQ
ITRALPSKPN SLDQFKSKLR SLSYSEILRL RQSERMSQDD FQSPPIVELR EKIQPEILEL
IKQQRLNRLC EGSSFRKIGN RRRQERFWYC RLALNHKVLH YGDLDDNPQG EVTFESLQEK
IPVADIKAIV TGKDCPHMKE KSALKQNKEV LELAFSILYD PDETLNFIAP NKYEYCIWID
GLSALLGKDM SSELTKSDLD TLLSMEMKLR LLDLENIQIP EAPPPIPKEP SSYDFVYHYG
