GNDS_HUMAN
ID GNDS_HUMAN Reviewed; 914 AA.
AC Q12967; B7Z753; E7ER93; E7ERZ0; Q5T7V4; Q6KH11; Q6PCE1; Q6ZSD5; Q9HAX7;
AC Q9HAY1; Q9HCT1; Q9P2N8;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 20-JUN-2001, sequence version 2.
DT 03-AUG-2022, entry version 198.
DE RecName: Full=Ral guanine nucleotide dissociation stimulator;
DE Short=RalGDS;
DE AltName: Full=Ral guanine nucleotide exchange factor;
DE Short=RalGEF;
GN Name=RALGDS; Synonyms=KIAA1308, RGF;
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 [GENOMIC DNA / MRNA] (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=9365783; DOI=10.1046/j.1469-1809.1997.6140299.x;
RA Humphrey D., Kwiatkowska J., Henske E.P., Haines J.L., Halley D.,
RA van Slegtenhorst M., Kwiatkowski D.J.;
RT "Cloning and evaluation of RALGDS as a candidate for the tuberous sclerosis
RT gene TSC1.";
RL Ann. Hum. Genet. 61:299-305(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
RA Yu L., Zhao S.Y.;
RL Submitted (SEP-1997) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 4 AND 5).
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 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 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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 6).
RC TISSUE=Placenta;
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 205-912 (ISOFORM 2).
RC TISSUE=Brain;
RX PubMed=10718198; DOI=10.1093/dnares/7.1.65;
RA Nagase T., Kikuno R., Ishikawa K., Hirosawa M., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XVI. The
RT complete sequences of 150 new cDNA clones from brain which code for large
RT proteins in vitro.";
RL DNA Res. 7:65-73(2000).
RN [8]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 587-914 (ISOFORM 1).
RX PubMed=7972015; DOI=10.1073/pnas.91.23.11089;
RA Hofer F., Fields S., Schneider C., Martin G.S.;
RT "Activated Ras interacts with the Ral guanine nucleotide dissociation
RT stimulator.";
RL Proc. Natl. Acad. Sci. U.S.A. 91:11089-11093(1994).
RN [9]
RP FUNCTION, AND INTERACTION WITH TRAF3.
RX PubMed=27438768; DOI=10.1016/j.immuni.2016.06.023;
RA Miao Y., Wu J., Abraham S.N.;
RT "Ubiquitination of Innate Immune Regulator TRAF3 Orchestrates Expulsion of
RT Intracellular Bacteria by Exocyst Complex.";
RL Immunity 45:94-105(2016).
RN [10]
RP STRUCTURE BY NMR OF 788-884.
RX PubMed=9302994; DOI=10.1038/nsb0997-694;
RA Geyer M., Herrmann C., Wohlgemuth S., Wittinghofer A., Kalbitzer H.R.;
RT "Structure of the Ras-binding domain of RalGEF and implications for Ras
RT binding and signalling.";
RL Nat. Struct. Biol. 4:694-699(1997).
RN [11]
RP STRUCTURE BY NMR OF 771-886.
RA Mueller T.D., Handel L., Schmieder P., Oschkinat H.;
RT "High-resolution structure of the RA-domain of human RalGDS and a dynamics
RT study of its binding loop to Ras.";
RL Submitted (MAR-1999) to the PDB data bank.
RN [12]
RP VARIANT [LARGE SCALE ANALYSIS] LEU-496.
RX PubMed=16959974; DOI=10.1126/science.1133427;
RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P.,
RA Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V.,
RA Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H.,
RA Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W.,
RA Velculescu V.E.;
RT "The consensus coding sequences of human breast and colorectal cancers.";
RL Science 314:268-274(2006).
CC -!- FUNCTION: Functions as a guanine nucleotide exchange factor (GEF)
CC activating either RalA or RalB GTPases and plays an important role in
CC intracellular transport. Interacts and acts as an effector molecule for
CC R-Ras, H-Ras, K-Ras, and Rap (By similarity). During bacterial
CC clearance, recognizes 'Lys-33'-linked polyubiquitinated TRAF3 and
CC subsequently mediates assembly of the exocyst complex
CC (PubMed:27438768). {ECO:0000250|UniProtKB:Q03385,
CC ECO:0000269|PubMed:27438768}.
CC -!- SUBUNIT: Interacts with RIT1 and RIT2 (By similarity). Interacts with
CC OOG1 (By similarity). Interacts with TRAF3 (PubMed:27438768). Interacts
CC with HRAS (By similarity). {ECO:0000250|UniProtKB:Q03385,
CC ECO:0000269|PubMed:27438768}.
CC -!- INTERACTION:
CC Q12967; P01112: HRAS; NbExp=3; IntAct=EBI-365861, EBI-350145;
CC Q12967; P61224: RAP1B; NbExp=2; IntAct=EBI-365861, EBI-358143;
CC Q12967-6; A8MQ03: CYSRT1; NbExp=3; IntAct=EBI-12005546, EBI-3867333;
CC Q12967-6; P49639: HOXA1; NbExp=3; IntAct=EBI-12005546, EBI-740785;
CC Q12967-6; P60410: KRTAP10-8; NbExp=3; IntAct=EBI-12005546, EBI-10171774;
CC Q12967-6; P61224: RAP1B; NbExp=3; IntAct=EBI-12005546, EBI-358143;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q03385}. Nucleus
CC {ECO:0000250|UniProtKB:Q03385}. Note=Localizes mainly in the peripheral
CC region of the cytoplasmic membrane in oocytes and in preimplantation
CC embryos until the 8-cell stage. Between the late 1-cell and the early
CC 2-cell stages, nuclear localization becomes stronger. After the 4-cell
CC stage, not detected in the nucleus. {ECO:0000250|UniProtKB:Q03385}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=6;
CC Name=1;
CC IsoId=Q12967-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q12967-2; Sequence=VSP_035301;
CC Name=3;
CC IsoId=Q12967-3; Sequence=VSP_043659;
CC Name=4;
CC IsoId=Q12967-4; Sequence=VSP_055215, VSP_055217;
CC Name=5;
CC IsoId=Q12967-5; Sequence=VSP_055216;
CC Name=6;
CC IsoId=Q12967-6; Sequence=VSP_055217;
CC -!- DOMAIN: The Ras-associating domain interacts with Ras.
CC -!- PTM: Phosphorylation of Tyr-814 by MET blocks HRAS binding.
CC {ECO:0000250|UniProtKB:Q03385}.
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DR EMBL; AF295773; AAG02122.1; -; mRNA.
DR EMBL; AK127524; BAC87018.1; -; mRNA.
DR EMBL; AK301470; BAH13489.1; -; mRNA.
DR EMBL; AF295775; AAG10221.1; -; Genomic_DNA.
DR EMBL; AF295778; AAG10221.1; JOINED; Genomic_DNA.
DR EMBL; AF295780; AAG10225.1; -; Genomic_DNA.
DR EMBL; AF027169; AAQ13414.1; -; mRNA.
DR EMBL; AL162417; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471090; EAW88040.1; -; Genomic_DNA.
DR EMBL; CH471090; EAW88042.1; -; Genomic_DNA.
DR EMBL; BC059362; AAH59362.1; -; mRNA.
DR EMBL; AB037729; BAA92546.1; -; mRNA.
DR EMBL; U14417; AAA52360.1; -; mRNA.
DR CCDS; CCDS43897.1; -. [Q12967-3]
DR CCDS; CCDS65172.1; -. [Q12967-6]
DR CCDS; CCDS65173.1; -. [Q12967-5]
DR CCDS; CCDS65174.1; -. [Q12967-4]
DR CCDS; CCDS6959.1; -. [Q12967-1]
DR PIR; I38853; I38853.
DR RefSeq; NP_001035827.1; NM_001042368.2. [Q12967-3]
DR RefSeq; NP_001258703.1; NM_001271774.1. [Q12967-4]
DR RefSeq; NP_001258704.1; NM_001271775.1. [Q12967-5]
DR RefSeq; NP_001258705.1; NM_001271776.1. [Q12967-6]
DR RefSeq; NP_006257.1; NM_006266.3. [Q12967-1]
DR PDB; 1RAX; NMR; -; A=775-886.
DR PDB; 2B3A; NMR; -; A=798-884.
DR PDB; 2RGF; NMR; -; A=788-884.
DR PDB; 3KH0; X-ray; 2.10 A; A/B=793-914.
DR PDBsum; 1RAX; -.
DR PDBsum; 2B3A; -.
DR PDBsum; 2RGF; -.
DR PDBsum; 3KH0; -.
DR AlphaFoldDB; Q12967; -.
DR SMR; Q12967; -.
DR BioGRID; 111836; 29.
DR DIP; DIP-31375N; -.
DR IntAct; Q12967; 23.
DR MINT; Q12967; -.
DR STRING; 9606.ENSP00000361120; -.
DR GlyGen; Q12967; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q12967; -.
DR PhosphoSitePlus; Q12967; -.
DR BioMuta; RALGDS; -.
DR DMDM; 14549162; -.
DR EPD; Q12967; -.
DR jPOST; Q12967; -.
DR MassIVE; Q12967; -.
DR MaxQB; Q12967; -.
DR PaxDb; Q12967; -.
DR PeptideAtlas; Q12967; -.
DR PRIDE; Q12967; -.
DR ProteomicsDB; 17741; -.
DR ProteomicsDB; 17880; -.
DR ProteomicsDB; 59058; -. [Q12967-1]
DR ProteomicsDB; 59059; -. [Q12967-2]
DR ProteomicsDB; 59060; -. [Q12967-3]
DR ProteomicsDB; 67063; -.
DR Antibodypedia; 31763; 125 antibodies from 27 providers.
DR DNASU; 5900; -.
DR Ensembl; ENST00000372047.7; ENSP00000361117.3; ENSG00000160271.16. [Q12967-6]
DR Ensembl; ENST00000372050.8; ENSP00000361120.3; ENSG00000160271.16. [Q12967-1]
DR Ensembl; ENST00000372062.8; ENSP00000361132.3; ENSG00000160271.16. [Q12967-4]
DR Ensembl; ENST00000393157.8; ENSP00000376864.3; ENSG00000160271.16. [Q12967-5]
DR Ensembl; ENST00000393160.7; ENSP00000376867.3; ENSG00000160271.16. [Q12967-3]
DR GeneID; 5900; -.
DR KEGG; hsa:5900; -.
DR MANE-Select; ENST00000372050.8; ENSP00000361120.3; NM_006266.4; NP_006257.1.
DR UCSC; uc004cco.5; human. [Q12967-1]
DR CTD; 5900; -.
DR DisGeNET; 5900; -.
DR GeneCards; RALGDS; -.
DR HGNC; HGNC:9842; RALGDS.
DR HPA; ENSG00000160271; Low tissue specificity.
DR MIM; 601619; gene.
DR neXtProt; NX_Q12967; -.
DR OpenTargets; ENSG00000160271; -.
DR PharmGKB; PA34200; -.
DR VEuPathDB; HostDB:ENSG00000160271; -.
DR eggNOG; KOG3629; Eukaryota.
DR GeneTree; ENSGT00940000153181; -.
DR HOGENOM; CLU_010252_0_1_1; -.
DR InParanoid; Q12967; -.
DR OMA; DAHFREW; -.
DR PhylomeDB; Q12967; -.
DR TreeFam; TF315204; -.
DR PathwayCommons; Q12967; -.
DR Reactome; R-HSA-171007; p38MAPK events.
DR Reactome; R-HSA-5673001; RAF/MAP kinase cascade.
DR SignaLink; Q12967; -.
DR SIGNOR; Q12967; -.
DR BioGRID-ORCS; 5900; 17 hits in 1077 CRISPR screens.
DR ChiTaRS; RALGDS; human.
DR EvolutionaryTrace; Q12967; -.
DR GeneWiki; RALGDS; -.
DR GenomeRNAi; 5900; -.
DR Pharos; Q12967; Tbio.
DR PRO; PR:Q12967; -.
DR Proteomes; UP000005640; Chromosome 9.
DR RNAct; Q12967; protein.
DR Bgee; ENSG00000160271; Expressed in right hemisphere of cerebellum and 95 other tissues.
DR ExpressionAtlas; Q12967; baseline and differential.
DR Genevisible; Q12967; HS.
DR GO; GO:0005903; C:brush border; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0030695; F:GTPase regulator activity; IDA:UniProtKB.
DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IBA:GO_Central.
DR GO; GO:0043547; P:positive regulation of GTPase activity; IBA:GO_Central.
DR GO; GO:0007265; P:Ras protein signal transduction; IBA:GO_Central.
DR CDD; cd00155; RasGEF; 1.
DR CDD; cd06224; REM; 1.
DR Gene3D; 1.10.840.10; -; 1.
DR InterPro; IPR000159; RA_dom.
DR InterPro; IPR015758; RalGDS.
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 InterPro; IPR029071; Ubiquitin-like_domsf.
DR PANTHER; PTHR23113; PTHR23113; 1.
DR PANTHER; PTHR23113:SF35; PTHR23113:SF35; 1.
DR Pfam; PF00788; RA; 1.
DR Pfam; PF00617; RasGEF; 1.
DR Pfam; PF00618; RasGEF_N; 1.
DR SMART; SM00314; RA; 1.
DR SMART; SM00147; RasGEF; 1.
DR SMART; SM00229; RasGEFN; 1.
DR SUPFAM; SSF48366; SSF48366; 1.
DR SUPFAM; SSF54236; SSF54236; 1.
DR PROSITE; PS50200; RA; 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; Cytoplasm;
KW Guanine-nucleotide releasing factor; Nucleus; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..914
FT /note="Ral guanine nucleotide dissociation stimulator"
FT /id="PRO_0000068877"
FT DOMAIN 112..249
FT /note="N-terminal Ras-GEF"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00135"
FT DOMAIN 386..648
FT /note="Ras-GEF"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00168"
FT DOMAIN 798..885
FT /note="Ras-associating"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00166"
FT REGION 280..365
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 666..689
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 728..776
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 282..306
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 350..364
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 737..776
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 814
FT /note="Phosphotyrosine; by MET"
FT /evidence="ECO:0000250|UniProtKB:Q03385"
FT VAR_SEQ 1..61
FT /note="MVQRMWAEAAGPAGGAEPLFPGSRRSRSVWDAVRLEVGVPDSCPVVLHSFTQ
FT LDPDLPRPE -> MMVDCQ (in isoform 3)"
FT /evidence="ECO:0000303|Ref.2"
FT /id="VSP_043659"
FT VAR_SEQ 1..61
FT /note="MVQRMWAEAAGPAGGAEPLFPGSRRSRSVWDAVRLEVGVPDSCPVVLHSFTQ
FT LDPDLPRPE -> MCLWGHSTAPAHTLSSPPLLFCSLPCALHLQPGTGHPPGQVPRK
FT (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_055215"
FT VAR_SEQ 1..60
FT /note="MVQRMWAEAAGPAGGAEPLFPGSRRSRSVWDAVRLEVGVPDSCPVVLHSFTQ
FT LDPDLPRP -> MAREAGQVCARPAVPRGRKGSVFFACVSVVTARRRAVARRAALQSPT
FT PWLAPLPAPATT (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_055216"
FT VAR_SEQ 163..174
FT /note="Missing (in isoform 4 and isoform 6)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_055217"
FT VAR_SEQ 738..912
FT /note="FWESASQSSPETSGISSASSSTSSSSASTTPVAATRTHKRSVSGLCNSSSAL
FT PLYNQQVGDCCIIRVSLDVDNGNMYKSILVTSQDKAPAVIRKAMDKHNLEEEEPEDYEL
FT LQILSDDRKLKIPENANVFYAMNSTANYDFVLKKRTFTKGVKVKHGASSTLPRMKQKGL
FT KIAKG -> VTACPSPQYPFPSPHSKSMHGARKPWILNTASRRFPIWQLAWGAPTGQWD
FT LLILPSPSVLGISLTVIPGDLRHQLSLQQHLVLLSLHHARGCHTHPQALCLRALQLQLR
FT AAALQPAGGRLLYHPRQPGRGQWQHVQEHPGKPAGVAWVPPSTGGKCTLNTVHHPCPPG
FT VYLVVGGEGQMSARYRNEEGSDQGQGWPEGRGGGKEQPCKAPRS (in isoform
FT 2)"
FT /evidence="ECO:0000303|PubMed:10718198"
FT /id="VSP_035301"
FT VARIANT 496
FT /note="R -> L (in a colorectal cancer sample; somatic
FT mutation)"
FT /evidence="ECO:0000269|PubMed:16959974"
FT /id="VAR_035822"
FT CONFLICT 97
FT /note="L -> F (in Ref. 3; BAC87018)"
FT /evidence="ECO:0000305"
FT CONFLICT 869
FT /note="A -> T (in Ref. 3; BAH13489)"
FT /evidence="ECO:0000305"
FT STRAND 791..793
FT /evidence="ECO:0007829|PDB:2RGF"
FT STRAND 795..797
FT /evidence="ECO:0007829|PDB:3KH0"
FT STRAND 799..807
FT /evidence="ECO:0007829|PDB:3KH0"
FT STRAND 809..820
FT /evidence="ECO:0007829|PDB:3KH0"
FT HELIX 825..835
FT /evidence="ECO:0007829|PDB:3KH0"
FT TURN 836..839
FT /evidence="ECO:0007829|PDB:2RGF"
FT HELIX 843..845
FT /evidence="ECO:0007829|PDB:3KH0"
FT STRAND 846..853
FT /evidence="ECO:0007829|PDB:3KH0"
FT STRAND 856..859
FT /evidence="ECO:0007829|PDB:3KH0"
FT STRAND 862..864
FT /evidence="ECO:0007829|PDB:2B3A"
FT HELIX 866..869
FT /evidence="ECO:0007829|PDB:3KH0"
FT STRAND 877..882
FT /evidence="ECO:0007829|PDB:3KH0"
FT CONFLICT Q12967-5:3
FT /note="R -> W (in Ref. 3; BAC87018)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 914 AA; 100607 MW; EA5A5CF25AF3D523 CRC64;
MVQRMWAEAA GPAGGAEPLF PGSRRSRSVW DAVRLEVGVP DSCPVVLHSF TQLDPDLPRP
ESSTQEIGEE LINGVIYSIS LRKVQLHHGG NKGQRWLGYE NESALNLYET CKVRTVKAGT
LEKLVEHLVP AFQGSDLSYV TIFLCTYRAF TTTQQVLDLL FKRYGRCDAL TASSRYGCIL
PYSDEDGGPQ DQLKNAISSI LGTWLDQYSE DFCQPPDFPC LKQLVAYVQL NMPGSDLERR
AHLLLAQLEH SEPIEAEPEA LSPVPALKPT PELELALTPA RAPSPVPAPA PEPEPAPTPA
PGSELEVAPA PAPELQQAPE PAVGLESAPA PALELEPAPE QDPAPSQTLE LEPAPAPVPS
LQPSWPSPVV AENGLSEEKP HLLVFPPDLV AEQFTLMDAE LFKKVVPYHC LGSIWSQRDK
KGKEHLAPTI RATVTQFNSV ANCVITTCLG NRSTKAPDRA RVVEHWIEVA RECRILKNFS
SLYAILSALQ SNSIHRLKKT WEDVSRDSFR IFQKLSEIFS DENNYSLSRE LLIKEGTSKF
ATLEMNPKRA QKRPKETGII QGTVPYLGTF LTDLVMLDTA MKDYLYGRLI NFEKRRKEFE
VIAQIKLLQS ACNNYSIAPD EQFGAWFRAV ERLSETESYN LSCELEPPSE SASNTLRTKK
NTAIVKRWSD RQAPSTELST SGSSHSKSCD QLRCGPYLSS GDIADALSVH SAGSSSSDVE
EINISFVPES PDGQEKKFWE SASQSSPETS GISSASSSTS SSSASTTPVA ATRTHKRSVS
GLCNSSSALP LYNQQVGDCC IIRVSLDVDN GNMYKSILVT SQDKAPAVIR KAMDKHNLEE
EEPEDYELLQ ILSDDRKLKI PENANVFYAM NSTANYDFVL KKRTFTKGVK VKHGASSTLP
RMKQKGLKIA KGIF
