RPGF1_HUMAN
ID RPGF1_HUMAN Reviewed; 1077 AA.
AC Q13905; Q5JUE4; Q68DL3; Q8IV73;
DT 15-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT 03-APR-2007, sequence version 3.
DT 03-AUG-2022, entry version 199.
DE RecName: Full=Rap guanine nucleotide exchange factor 1;
DE AltName: Full=CRK SH3-binding GNRP;
DE AltName: Full=Guanine nucleotide-releasing factor 2;
DE AltName: Full=Protein C3G;
GN Name=RAPGEF1; Synonyms=GRF2;
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 LONG), AND CHARACTERIZATION.
RC TISSUE=Placenta, and Spleen;
RX PubMed=7512734; DOI=10.1073/pnas.91.8.3443;
RA Tanaka S., Morishita T., Hashimoto Y., Hattori S., Nakamura S., Shibuya M.,
RA Matuoka K., Takenawa T., Kurata T., Nagashima K., Matsuda M.;
RT "C3G, a guanine nucleotide-releasing protein expressed ubiquitously, binds
RT to the Src homology 3 domains of CRK and GRB2/ASH proteins.";
RL Proc. Natl. Acad. Sci. U.S.A. 91:3443-3447(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND ALTERNATIVE SPLICING.
RX PubMed=7806500; DOI=10.1016/s0021-9258(20)30059-4;
RA Knudsen B., Feller S., Hanafusa H.;
RT "Four proline-rich sequences of the guanine-nucleotide exchange factor C3G
RT bind with unique specificity to the first Src homology 3 domain of Crk.";
RL J. Biol. Chem. 269:32781-32787(1994).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
RC TISSUE=Testis;
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 [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC TISSUE=Skin;
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 INTERACTION WITH CRK.
RX PubMed=8662907; DOI=10.1074/jbc.271.24.14468;
RA Matsuda M., Ota S., Tanimura R., Nakamura H., Matuoka K., Takenawa T.,
RA Nagashima K., Kurata T.;
RT "Interaction between the amino-terminal SH3 domain of CRK and its natural
RT target proteins.";
RL J. Biol. Chem. 271:14468-14472(1996).
RN [7]
RP FUNCTION.
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 HCK, MUTAGENESIS OF TYR-504, AND PHOSPHORYLATION AT
RP TYR-504.
RX PubMed=14551197; DOI=10.1074/jbc.m310656200;
RA Shivakrupa R., Radha V., Sudhakar C., Swarup G.;
RT "Physical and functional interaction between Hck tyrosine kinase and
RT guanine nucleotide exchange factor C3G results in apoptosis, which is
RT independent of C3G catalytic domain.";
RL J. Biol. Chem. 278:52188-52194(2003).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=15144186; DOI=10.1021/ac035352d;
RA Brill L.M., Salomon A.R., Ficarro S.B., Mukherji M., Stettler-Gill M.,
RA Peters E.C.;
RT "Robust phosphoproteomic profiling of tyrosine phosphorylation sites from
RT human T cells using immobilized metal affinity chromatography and tandem
RT mass spectrometry.";
RL Anal. Chem. 76:2763-2772(2004).
RN [10]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=17724123; DOI=10.1083/jcb.200610073;
RA Hisata S., Sakisaka T., Baba T., Yamada T., Aoki K., Matsuda M., Takai Y.;
RT "Rap1-PDZ-GEF1 interacts with a neurotrophin receptor at late endosomes,
RT leading to sustained activation of Rap1 and ERK and neurite outgrowth.";
RL J. Cell Biol. 178:843-860(2007).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-360, AND IDENTIFICATION BY
RP 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 [12]
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 [13]
RP FUNCTION.
RX PubMed=21840392; DOI=10.1016/j.cellsig.2011.07.022;
RA Pannekoek W.J., van Dijk J.J., Chan O.Y., Huveneers S., Linnemann J.R.,
RA Spanjaard E., Brouwer P.M., van der Meer A.J., Zwartkruis F.J., Rehmann H.,
RA de Rooij J., Bos J.L.;
RT "Epac1 and PDZ-GEF cooperate in Rap1 mediated endothelial junction
RT control.";
RL Cell. Signal. 23:2056-2064(2011).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-293, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-281; SER-314; SER-335 AND
RP SER-360, AND IDENTIFICATION BY 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 [16]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [17]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-57 (ISOFORM SHORT), AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25218447; DOI=10.1038/nsmb.2890;
RA Hendriks I.A., D'Souza R.C., Yang B., Verlaan-de Vries M., Mann M.,
RA Vertegaal A.C.;
RT "Uncovering global SUMOylation signaling networks in a site-specific
RT manner.";
RL Nat. Struct. Mol. Biol. 21:927-936(2014).
RN [18]
RP VARIANT GLN-1012.
RX PubMed=23033978; DOI=10.1056/nejmoa1206524;
RA de Ligt J., Willemsen M.H., van Bon B.W., Kleefstra T., Yntema H.G.,
RA Kroes T., Vulto-van Silfhout A.T., Koolen D.A., de Vries P., Gilissen C.,
RA del Rosario M., Hoischen A., Scheffer H., de Vries B.B., Brunner H.G.,
RA Veltman J.A., Vissers L.E.;
RT "Diagnostic exome sequencing in persons with severe intellectual
RT disability.";
RL N. Engl. J. Med. 367:1921-1929(2012).
CC -!- FUNCTION: Guanine nucleotide-releasing protein that binds to SH3 domain
CC of CRK and GRB2/ASH. Transduces signals from CRK to activate RAS.
CC Involved in cell branching and adhesion mediated by BCAR1-CRK-RAPGEF1
CC signaling and activation of RAP1 (PubMed:12432078). Plays a role in the
CC establishment of basal endothelial barrier function. Plays a role in
CC nerve growth factor (NGF)-induced sustained activation of Rap1 and
CC neurite outgrowth. {ECO:0000269|PubMed:12432078,
CC ECO:0000269|PubMed:17724123, ECO:0000269|PubMed:21840392,
CC ECO:0000269|PubMed:7806500}.
CC -!- SUBUNIT: Interacts with HCK (via SH3-binding sites) (PubMed:14551197).
CC Interacts with CRK (via SH3-binding sites) (PubMed:8662907).
CC {ECO:0000269|PubMed:14551197, ECO:0000269|PubMed:8662907}.
CC -!- INTERACTION:
CC Q13905; P00519: ABL1; NbExp=4; IntAct=EBI-976876, EBI-375543;
CC Q13905; P46108: CRK; NbExp=5; IntAct=EBI-976876, EBI-886;
CC Q13905; P46108-1: CRK; NbExp=3; IntAct=EBI-976876, EBI-287556;
CC Q13905; P46109: CRKL; NbExp=3; IntAct=EBI-976876, EBI-910;
CC Q13905; P06241: FYN; NbExp=2; IntAct=EBI-976876, EBI-515315;
CC Q13905; P16333: NCK1; NbExp=2; IntAct=EBI-976876, EBI-389883;
CC Q13905; P27986: PIK3R1; NbExp=2; IntAct=EBI-976876, EBI-79464;
CC Q13905; P12931: SRC; NbExp=2; IntAct=EBI-976876, EBI-621482;
CC -!- SUBCELLULAR LOCATION: Early endosome {ECO:0000269|PubMed:17724123}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=Long;
CC IsoId=Q13905-1; Sequence=Displayed;
CC Name=Short;
CC IsoId=Q13905-2; Sequence=VSP_001822;
CC Name=3;
CC IsoId=Q13905-3; Sequence=VSP_042052;
CC Name=4;
CC IsoId=Q13905-4; Sequence=VSP_057416;
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed in adult and fetus.
CC Expression is high in adult skeletal muscle and placenta and in fetal
CC brain and heart. Low levels of expression in adult and fetal liver.
CC -!- PTM: Phosphorylation at Tyr-504 enhances activity as Rap guanine
CC nucleotide exchange factor. {ECO:0000269|PubMed:14551197}.
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/RAPGEF1ID42045ch9q34.html";
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DR EMBL; D21239; BAA04770.1; -; mRNA.
DR EMBL; CR749354; CAH18207.1; -; mRNA.
DR EMBL; AL160271; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL160276; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC041710; AAH41710.1; -; mRNA.
DR CCDS; CCDS48047.1; -. [Q13905-1]
DR CCDS; CCDS48048.1; -. [Q13905-3]
DR CCDS; CCDS78450.1; -. [Q13905-4]
DR RefSeq; NP_001291204.1; NM_001304275.1. [Q13905-4]
DR RefSeq; NP_005303.2; NM_005312.3. [Q13905-1]
DR RefSeq; NP_941372.1; NM_198679.1. [Q13905-3]
DR PDB; 5L23; X-ray; 1.77 A; B=279-293.
DR PDBsum; 5L23; -.
DR AlphaFoldDB; Q13905; -.
DR SMR; Q13905; -.
DR BioGRID; 109146; 31.
DR CORUM; Q13905; -.
DR DIP; DIP-29392N; -.
DR ELM; Q13905; -.
DR IntAct; Q13905; 17.
DR MINT; Q13905; -.
DR STRING; 9606.ENSP00000361263; -.
DR iPTMnet; Q13905; -.
DR PhosphoSitePlus; Q13905; -.
DR BioMuta; RAPGEF1; -.
DR DMDM; 143811452; -.
DR EPD; Q13905; -.
DR jPOST; Q13905; -.
DR MassIVE; Q13905; -.
DR MaxQB; Q13905; -.
DR PaxDb; Q13905; -.
DR PeptideAtlas; Q13905; -.
DR PRIDE; Q13905; -.
DR ProteomicsDB; 59720; -. [Q13905-1]
DR ProteomicsDB; 59721; -. [Q13905-2]
DR ProteomicsDB; 59722; -. [Q13905-3]
DR ProteomicsDB; 66090; -.
DR Antibodypedia; 1488; 296 antibodies from 27 providers.
DR DNASU; 2889; -.
DR Ensembl; ENST00000372189.7; ENSP00000361263.2; ENSG00000107263.19. [Q13905-1]
DR Ensembl; ENST00000372190.7; ENSP00000361264.3; ENSG00000107263.19. [Q13905-3]
DR Ensembl; ENST00000372195.5; ENSP00000361269.1; ENSG00000107263.19. [Q13905-4]
DR GeneID; 2889; -.
DR KEGG; hsa:2889; -.
DR UCSC; uc064wrk.1; human. [Q13905-1]
DR UCSC; uc064wrl.1; human.
DR CTD; 2889; -.
DR DisGeNET; 2889; -.
DR GeneCards; RAPGEF1; -.
DR HGNC; HGNC:4568; RAPGEF1.
DR HPA; ENSG00000107263; Tissue enhanced (skeletal).
DR MIM; 600303; gene.
DR neXtProt; NX_Q13905; -.
DR OpenTargets; ENSG00000107263; -.
DR PharmGKB; PA28964; -.
DR VEuPathDB; HostDB:ENSG00000107263; -.
DR eggNOG; KOG3417; Eukaryota.
DR GeneTree; ENSGT00940000156235; -.
DR HOGENOM; CLU_003982_1_0_1; -.
DR InParanoid; Q13905; -.
DR OMA; QQVHYEI; -.
DR OrthoDB; 231215at2759; -.
DR PhylomeDB; Q13905; -.
DR TreeFam; TF317296; -.
DR PathwayCommons; Q13905; -.
DR Reactome; R-HSA-170968; Frs2-mediated activation.
DR Reactome; R-HSA-186763; Downstream signal transduction.
DR Reactome; R-HSA-8875555; MET activates RAP1 and RAC1.
DR Reactome; R-HSA-9013423; RAC3 GTPase cycle.
DR Reactome; R-HSA-9027284; Erythropoietin activates RAS.
DR Reactome; R-HSA-912631; Regulation of signaling by CBL.
DR SignaLink; Q13905; -.
DR SIGNOR; Q13905; -.
DR BioGRID-ORCS; 2889; 63 hits in 1081 CRISPR screens.
DR ChiTaRS; RAPGEF1; human.
DR GeneWiki; RAPGEF1; -.
DR GenomeRNAi; 2889; -.
DR Pharos; Q13905; Tbio.
DR PRO; PR:Q13905; -.
DR Proteomes; UP000005640; Chromosome 9.
DR RNAct; Q13905; protein.
DR Bgee; ENSG00000107263; Expressed in gastrocnemius and 169 other tissues.
DR ExpressionAtlas; Q13905; baseline and differential.
DR Genevisible; Q13905; HS.
DR GO; GO:0005737; C:cytoplasm; IDA:CAFA.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005769; C:early endosome; IDA:UniProtKB.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IDA:UniProtKB.
DR GO; GO:0017124; F:SH3 domain binding; IEA:UniProtKB-KW.
DR GO; GO:0071320; P:cellular response to cAMP; IDA:UniProtKB.
DR GO; GO:1990090; P:cellular response to nerve growth factor stimulus; IDA:UniProtKB.
DR GO; GO:0061028; P:establishment of endothelial barrier; IMP:UniProtKB.
DR GO; GO:0038180; P:nerve growth factor signaling pathway; IDA:UniProtKB.
DR GO; GO:0007399; P:nervous system development; IEA:UniProtKB-KW.
DR GO; GO:0043547; P:positive regulation of GTPase activity; IDA:UniProtKB.
DR GO; GO:0010976; P:positive regulation of neuron projection development; IMP:UniProtKB.
DR GO; GO:0032486; P:Rap protein signal transduction; IMP:UniProtKB.
DR GO; GO:0007265; P:Ras protein signal transduction; IBA:GO_Central.
DR GO; GO:1901888; P:regulation of cell junction assembly; IMP:UniProtKB.
DR GO; GO:0007165; P:signal transduction; NAS:ProtInc.
DR GO; GO:0007169; P:transmembrane receptor protein tyrosine kinase signaling pathway; TAS:ProtInc.
DR CDD; cd00155; RasGEF; 1.
DR CDD; cd06224; REM; 1.
DR Gene3D; 1.10.840.10; -; 1.
DR InterPro; IPR008937; Ras-like_GEF.
DR InterPro; IPR000651; Ras-like_Gua-exchang_fac_N.
DR InterPro; IPR019804; Ras_G-nucl-exch_fac_CS.
DR InterPro; IPR023578; Ras_GEF_dom_sf.
DR InterPro; IPR001895; RASGEF_cat_dom.
DR InterPro; IPR036964; RASGEF_cat_dom_sf.
DR PANTHER; PTHR23113; PTHR23113; 1.
DR Pfam; PF00617; RasGEF; 1.
DR Pfam; PF00618; RasGEF_N; 1.
DR SMART; SM00147; RasGEF; 1.
DR SMART; SM00229; RasGEFN; 1.
DR SUPFAM; SSF48366; SSF48366; 1.
DR PROSITE; PS00720; RASGEF; 1.
DR PROSITE; PS50009; RASGEF_CAT; 1.
DR PROSITE; PS50212; RASGEF_NTER; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Endosome;
KW Guanine-nucleotide releasing factor; Isopeptide bond; Neurogenesis;
KW Phosphoprotein; Reference proteome; SH3-binding; Ubl conjugation.
FT CHAIN 1..1077
FT /note="Rap guanine nucleotide exchange factor 1"
FT /id="PRO_0000068864"
FT DOMAIN 688..810
FT /note="N-terminal Ras-GEF"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00135"
FT DOMAIN 840..1064
FT /note="Ras-GEF"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00168"
FT REGION 207..235
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 248..300
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 336..376
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 411..494
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 600..670
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 281..292
FT /note="SH3-binding"
FT MOTIF 451..462
FT /note="SH3-binding"
FT MOTIF 538..549
FT /note="SH3-binding"
FT MOTIF 606..617
FT /note="SH3-binding"
FT COMPBIAS 264..291
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 345..376
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 281
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 293
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT MOD_RES 314
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 335
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 360
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 504
FT /note="Phosphotyrosine; by HCK"
FT /evidence="ECO:0000269|PubMed:14551197"
FT VAR_SEQ 1..3
FT /note="MDT -> MGNAIEKQKPLKRSHLYPWKQ (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_042052"
FT VAR_SEQ 1..3
FT /note="MDT -> MSGGLGLRRSPEMSGKIEKA (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:17974005"
FT /id="VSP_057416"
FT VAR_SEQ 50..88
FT /note="Missing (in isoform Short)"
FT /evidence="ECO:0000305"
FT /id="VSP_001822"
FT VARIANT 1012
FT /note="R -> Q (found in a patient with intellectual
FT disability, frontal epilepsy and mild facial dysmorphism)"
FT /evidence="ECO:0000269|PubMed:23033978"
FT /id="VAR_069375"
FT MUTAGEN 504
FT /note="Y->F: Abolishes phosphorylation by HCK."
FT /evidence="ECO:0000269|PubMed:14551197"
FT CONFLICT 137
FT /note="P -> R (in Ref. 2)"
FT /evidence="ECO:0000305"
FT CONFLICT 183
FT /note="E -> G (in Ref. 2)"
FT /evidence="ECO:0000305"
FT CONFLICT 217
FT /note="S -> C (in Ref. 2)"
FT /evidence="ECO:0000305"
FT CONFLICT 254
FT /note="T -> S (in Ref. 2)"
FT /evidence="ECO:0000305"
FT CONFLICT 287
FT /note="P -> T (in Ref. 1; BAA04770)"
FT /evidence="ECO:0000305"
FT CONFLICT 355
FT /note="G -> D (in Ref. 1; BAA04770)"
FT /evidence="ECO:0000305"
FT CONFLICT 636
FT /note="G -> V (in Ref. 2)"
FT /evidence="ECO:0000305"
FT CONFLICT 698
FT /note="D -> N (in Ref. 2)"
FT /evidence="ECO:0000305"
FT CONFLICT 846..847
FT /note="EQ -> DE (in Ref. 2)"
FT /evidence="ECO:0000305"
FT CROSSLNK Q13905-2:57
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25218447"
SQ SEQUENCE 1077 AA; 120548 MW; E700631A0EE76CA1 CRC64;
MDTDSQRSHL SSFTMKLMDK FHSPKIKRTP SKKGKPAEVS VKIPEKPVNK EATDRFLPEG
YPLPLDLEQQ AVEFMSTSAV ASRSQRQKNL SWLEEKEKEV VSALRYFKTI VDKMAIDKKV
LEMLPGSASK VLEAILPLVQ NDPRIQHSSA LSSCYSRVYQ SLANLIRWSD QVMLEGVNSE
DKEMVTTVKG VIKAVLDGVK ELVRLTIEKQ GRPSPTSPVK PSSPASKPDG PAELPLTDRE
VEILNKTTGM SQSTELLPDA TDEEVAPPKP PLPGIRVVDN SPPPALPPKK RQSAPSPTRV
AVVAPMSRAT SGSSLPVGIN RQDFDVDCYA QRRLSGGSHS YGGESPRLSP CSSIGKLSKS
DEQLSSLDRD SGQCSRNTSC ETLDHYDPDY EFLQQDLSNA DQIPQQTAWN LSPLPESLGE
SGSPFLGPPF QLPLGGHPQP DGPLAPGQQT DTPPALPEKK RRSAASQTAD GSGCRVSYER
HPSQYDNISG EDLQSTAPIP SVPYAPFAAI LPFQHGGSSA PVEFVGDFTA PESTGDPEKP
PPLPEKKNKH MLAYMQLLED YSEPQPSMFY QTPQNEHIYQ QKNKLLMEVY GFSDSFSGVD
SVQELAPPPA LPPKQRQLEP PAGKDGHPRD PSAVSGVPGK DSRDGSERAP KSPDALESAQ
SEEEVDELSL IDHNEIMSRL TLKQEGDDGP DVRGGSGDIL LVHATETDRK DLVLYCEAFL
TTYRTFISPE ELIKKLQYRY EKFSPFADTF KKRVSKNTFF VLVRVVDELC LVELTEEILK
LLMELVFRLV CNGELSLARV LRKNILDKVD QKKLLRCATS SQPLAARGVA ARPGTLHDFH
SHEIAEQLTL LDAELFYKIE IPEVLLWAKE QNEEKSPNLT QFTEHFNNMS YWVRSIIMLQ
EKAQDRERLL LKFIKIMKHL RKLNNFNSYL AILSALDSAP IRRLEWQKQT SEGLAEYCTL
IDSSSSFRAY RAALSEVEPP CIPYLGLILQ DLTFVHLGNP DYIDGKVNFS KRWQQFNILD
SMRCFQQAHY DMRRNDDIIN FFNDFSDHLA EEALWELSLK IKPRNITRRK TDREEKT
