FARP1_HUMAN
ID FARP1_HUMAN Reviewed; 1045 AA.
AC Q9Y4F1; Q5JVI9; Q6IQ29;
DT 18-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 179.
DE RecName: Full=FERM, ARHGEF and pleckstrin domain-containing protein 1;
DE AltName: Full=Chondrocyte-derived ezrin-like protein;
DE AltName: Full=FERM, RhoGEF and pleckstrin domain-containing protein 1;
DE AltName: Full=Pleckstrin homology domain-containing family C member 2;
DE Short=PH domain-containing family C member 2;
GN Name=FARP1; Synonyms=CDEP, PLEKHC2;
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), INDUCTION, AND TISSUE SPECIFICITY.
RC TISSUE=Cartilage;
RX PubMed=9425278; DOI=10.1006/bbrc.1997.7826;
RA Koyano Y., Kawamoto T., Shen M., Yan W., Noshiro M., Fujii K., Kato Y.;
RT "Molecular cloning and characterization of CDEP, a novel human protein
RT containing the ezrin-like domain of the band 4.1 superfamily and the Dbl
RT homology domain of rho guanine nucleotide exchange factors.";
RL Biochem. Biophys. Res. Commun. 241:369-375(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15057823; DOI=10.1038/nature02379;
RA Dunham A., Matthews L.H., Burton J., Ashurst J.L., Howe K.L.,
RA Ashcroft K.J., Beare D.M., Burford D.C., Hunt S.E., Griffiths-Jones S.,
RA Jones M.C., Keenan S.J., Oliver K., Scott C.E., Ainscough R., Almeida J.P.,
RA Ambrose K.D., Andrews D.T., Ashwell R.I.S., Babbage A.K., Bagguley C.L.,
RA Bailey J., Bannerjee R., Barlow K.F., Bates K., Beasley H., Bird C.P.,
RA Bray-Allen S., Brown A.J., Brown J.Y., Burrill W., Carder C., Carter N.P.,
RA Chapman J.C., Clamp M.E., Clark S.Y., Clarke G., Clee C.M., Clegg S.C.,
RA Cobley V., Collins J.E., Corby N., Coville G.J., Deloukas P., Dhami P.,
RA Dunham I., Dunn M., Earthrowl M.E., Ellington A.G., Faulkner L.,
RA Frankish A.G., Frankland J., French L., Garner P., Garnett J.,
RA Gilbert J.G.R., Gilson C.J., Ghori J., Grafham D.V., Gribble S.M.,
RA Griffiths C., Hall R.E., Hammond S., Harley J.L., Hart E.A., Heath P.D.,
RA Howden P.J., Huckle E.J., Hunt P.J., Hunt A.R., Johnson C., Johnson D.,
RA Kay M., Kimberley A.M., King A., Laird G.K., Langford C.J., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Lloyd C., Loveland J.E., Lovell J.,
RA Martin S., Mashreghi-Mohammadi M., McLaren S.J., McMurray A., Milne S.,
RA Moore M.J.F., Nickerson T., Palmer S.A., Pearce A.V., Peck A.I., Pelan S.,
RA Phillimore B., Porter K.M., Rice C.M., Searle S., Sehra H.K., Shownkeen R.,
RA Skuce C.D., Smith M., Steward C.A., Sycamore N., Tester J., Thomas D.W.,
RA Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P.,
RA Whitehead S.L., Willey D.L., Wilming L., Wray P.W., Wright M.W., Young L.,
RA Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Beck S., Bentley D.R.,
RA Rogers J., Ross M.T.;
RT "The DNA sequence and analysis of human chromosome 13.";
RL Nature 428:522-528(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 3).
RC TISSUE=Brain, Placenta, and 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 [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-427, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17924679; DOI=10.1021/pr070152u;
RA Yu L.R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.;
RT "Improved titanium dioxide enrichment of phosphopeptides from HeLa cells
RT and high confident phosphopeptide identification by cross-validation of
RT MS/MS and MS/MS/MS spectra.";
RL J. Proteome Res. 6:4150-4162(2007).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-427, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18220336; DOI=10.1021/pr0705441;
RA Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III;
RT "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient
RT phosphoproteomic analysis.";
RL J. Proteome Res. 7:1346-1351(2008).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-24 AND SER-340, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-889, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=18318008; DOI=10.1002/pmic.200700884;
RA Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D.,
RA Zou H., Gu J.;
RT "Large-scale phosphoproteome analysis of human liver tissue by enrichment
RT and fractionation of phosphopeptides with strong anion exchange
RT chromatography.";
RL Proteomics 8:1346-1361(2008).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-24; SER-427; SER-510 AND
RP SER-514, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [11]
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 [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-872 AND SER-889, AND
RP IDENTIFICATION BY 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 [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-24, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
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 [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-373; SER-403; SER-418;
RP SER-427; SER-833; SER-872; THR-883 AND SER-889, AND IDENTIFICATION BY MASS
RP 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 [15]
RP X-RAY CRYSTALLOGRAPHY (4.09 ANGSTROMS) OF 539-1035, AND DOMAIN.
RX PubMed=23375260; DOI=10.1016/j.str.2013.01.001;
RA He X., Kuo Y.C., Rosche T.J., Zhang X.;
RT "Structural basis for autoinhibition of the guanine nucleotide exchange
RT factor FARP2.";
RL Structure 21:355-364(2013).
RN [16]
RP VARIANT [LARGE SCALE ANALYSIS] LEU-714.
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 guanine nucleotide exchange factor for RAC1. May
CC play a role in semaphorin signaling. Plays a role in the assembly and
CC disassembly of dendritic filopodia, the formation of dendritic spines,
CC regulation of dendrite length and ultimately the formation of synapses
CC (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Interacts with CADM1. Interacts with RAC1 (By similarity).
CC {ECO:0000250}.
CC -!- INTERACTION:
CC Q9Y4F1; Q9NWS0: PIH1D1; NbExp=3; IntAct=EBI-5235630, EBI-357318;
CC -!- SUBCELLULAR LOCATION: Cell membrane; Peripheral membrane protein;
CC Cytoplasmic side. Synapse. Synapse, synaptosome {ECO:0000250}.
CC Cytoplasm, cytosol {ECO:0000250}. Cell projection, filopodium
CC {ECO:0000250}. Cell projection, dendrite {ECO:0000250}. Cell
CC projection, dendritic spine {ECO:0000250}. Note=Recruited to the cell
CC membrane via interaction with CADM1. {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q9Y4F1-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9Y4F1-2; Sequence=VSP_017976;
CC Name=3;
CC IsoId=Q9Y4F1-3; Sequence=VSP_040989, VSP_040990;
CC -!- TISSUE SPECIFICITY: Detected in cAMP-treated chondrocytes, but not in
CC untreated chondrocytes. Detected in fetal brain, heart and spleen, and
CC in adult testis, kidney and lung. {ECO:0000269|PubMed:9425278}.
CC -!- INDUCTION: Up-regulated in response to cAMP in cultured embryonic
CC chondrocytes. {ECO:0000269|PubMed:9425278}.
CC -!- DOMAIN: Intramolecular interaction between the DH domain and the PH
CC domains can stabilize the protein in an autoinhibited conformation.
CC {ECO:0000269|PubMed:23375260}.
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DR EMBL; AB008430; BAA24267.1; -; mRNA.
DR EMBL; AL136300; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL137249; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL161896; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL445223; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC041595; AAH41595.1; -; mRNA.
DR EMBL; BC065020; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; BC071592; AAH71592.1; -; mRNA.
DR CCDS; CCDS32000.1; -. [Q9Y4F1-3]
DR CCDS; CCDS66572.1; -. [Q9Y4F1-2]
DR CCDS; CCDS9487.1; -. [Q9Y4F1-1]
DR PIR; JC5795; JC5795.
DR RefSeq; NP_001001715.2; NM_001001715.3. [Q9Y4F1-3]
DR RefSeq; NP_001273768.1; NM_001286839.1.
DR RefSeq; NP_005757.1; NM_005766.3. [Q9Y4F1-1]
DR RefSeq; XP_016875801.1; XM_017020312.1. [Q9Y4F1-1]
DR PDB; 4H6Y; X-ray; 4.09 A; A/B=539-1035.
DR PDBsum; 4H6Y; -.
DR AlphaFoldDB; Q9Y4F1; -.
DR SMR; Q9Y4F1; -.
DR BioGRID; 115462; 127.
DR IntAct; Q9Y4F1; 54.
DR MINT; Q9Y4F1; -.
DR STRING; 9606.ENSP00000471242; -.
DR CarbonylDB; Q9Y4F1; -.
DR iPTMnet; Q9Y4F1; -.
DR PhosphoSitePlus; Q9Y4F1; -.
DR BioMuta; FARP1; -.
DR DMDM; 74762059; -.
DR EPD; Q9Y4F1; -.
DR jPOST; Q9Y4F1; -.
DR MassIVE; Q9Y4F1; -.
DR MaxQB; Q9Y4F1; -.
DR PaxDb; Q9Y4F1; -.
DR PeptideAtlas; Q9Y4F1; -.
DR PRIDE; Q9Y4F1; -.
DR ProteomicsDB; 86186; -. [Q9Y4F1-1]
DR ProteomicsDB; 86187; -. [Q9Y4F1-2]
DR ProteomicsDB; 86188; -. [Q9Y4F1-3]
DR Antibodypedia; 619; 217 antibodies from 20 providers.
DR DNASU; 10160; -.
DR Ensembl; ENST00000319562.11; ENSP00000322926.6; ENSG00000152767.17. [Q9Y4F1-1]
DR Ensembl; ENST00000376581.9; ENSP00000365765.4; ENSG00000152767.17. [Q9Y4F1-3]
DR GeneID; 10160; -.
DR KEGG; hsa:10160; -.
DR MANE-Select; ENST00000319562.11; ENSP00000322926.6; NM_005766.4; NP_005757.1.
DR UCSC; uc001vni.5; human. [Q9Y4F1-1]
DR CTD; 10160; -.
DR DisGeNET; 10160; -.
DR GeneCards; FARP1; -.
DR HGNC; HGNC:3591; FARP1.
DR HPA; ENSG00000152767; Low tissue specificity.
DR MIM; 602654; gene.
DR neXtProt; NX_Q9Y4F1; -.
DR OpenTargets; ENSG00000152767; -.
DR PharmGKB; PA28004; -.
DR VEuPathDB; HostDB:ENSG00000152767; -.
DR eggNOG; KOG3531; Eukaryota.
DR GeneTree; ENSGT00940000155318; -.
DR HOGENOM; CLU_012301_0_0_1; -.
DR InParanoid; Q9Y4F1; -.
DR OrthoDB; 476668at2759; -.
DR PhylomeDB; Q9Y4F1; -.
DR TreeFam; TF351276; -.
DR PathwayCommons; Q9Y4F1; -.
DR Reactome; R-HSA-8980692; RHOA GTPase cycle.
DR Reactome; R-HSA-9013148; CDC42 GTPase cycle.
DR Reactome; R-HSA-9013149; RAC1 GTPase cycle.
DR Reactome; R-HSA-9035034; RHOF GTPase cycle.
DR SignaLink; Q9Y4F1; -.
DR BioGRID-ORCS; 10160; 14 hits in 1069 CRISPR screens.
DR ChiTaRS; FARP1; human.
DR GeneWiki; FARP1; -.
DR GenomeRNAi; 10160; -.
DR Pharos; Q9Y4F1; Tbio.
DR PRO; PR:Q9Y4F1; -.
DR Proteomes; UP000005640; Chromosome 13.
DR RNAct; Q9Y4F1; protein.
DR Bgee; ENSG00000152767; Expressed in renal medulla and 202 other tissues.
DR ExpressionAtlas; Q9Y4F1; baseline and differential.
DR Genevisible; Q9Y4F1; HS.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0005856; C:cytoskeleton; TAS:ProtInc.
DR GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR GO; GO:0030425; C:dendrite; ISS:UniProtKB.
DR GO; GO:0043197; C:dendritic spine; IEA:UniProtKB-SubCell.
DR GO; GO:0031234; C:extrinsic component of cytoplasmic side of plasma membrane; ISS:UniProtKB.
DR GO; GO:0098890; C:extrinsic component of postsynaptic membrane; IEA:Ensembl.
DR GO; GO:0030175; C:filopodium; IEA:UniProtKB-SubCell.
DR GO; GO:0098978; C:glutamatergic synapse; IEA:Ensembl.
DR GO; GO:0008092; F:cytoskeletal protein binding; IEA:InterPro.
DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; ISS:UniProtKB.
DR GO; GO:0031267; F:small GTPase binding; IEA:Ensembl.
DR GO; GO:0048813; P:dendrite morphogenesis; ISS:UniProtKB.
DR GO; GO:0098974; P:postsynaptic actin cytoskeleton organization; IEA:Ensembl.
DR GO; GO:1905606; P:regulation of presynapse assembly; IEA:Ensembl.
DR GO; GO:0098942; P:retrograde trans-synaptic signaling by trans-synaptic protein complex; IEA:Ensembl.
DR GO; GO:0007416; P:synapse assembly; ISS:UniProtKB.
DR CDD; cd14473; FERM_B-lobe; 1.
DR CDD; cd13193; FERM_C_FARP1-like; 1.
DR CDD; cd00160; RhoGEF; 1.
DR DisProt; DP02833; -.
DR Gene3D; 1.20.80.10; -; 1.
DR Gene3D; 1.20.900.10; -; 1.
DR Gene3D; 2.30.29.30; -; 3.
DR InterPro; IPR019749; Band_41_domain.
DR InterPro; IPR035899; DBL_dom_sf.
DR InterPro; IPR000219; DH-domain.
DR InterPro; IPR000798; Ez/rad/moesin-like.
DR InterPro; IPR041788; FARP1/FARP2/FRMD7_FERM_C.
DR InterPro; IPR014847; FERM-adjacent.
DR InterPro; IPR014352; FERM/acyl-CoA-bd_prot_sf.
DR InterPro; IPR035963; FERM_2.
DR InterPro; IPR019748; FERM_central.
DR InterPro; IPR019747; FERM_CS.
DR InterPro; IPR000299; FERM_domain.
DR InterPro; IPR018979; FERM_N.
DR InterPro; IPR018980; FERM_PH-like_C.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR001849; PH_domain.
DR InterPro; IPR029071; Ubiquitin-like_domsf.
DR Pfam; PF08736; FA; 1.
DR Pfam; PF09380; FERM_C; 1.
DR Pfam; PF00373; FERM_M; 1.
DR Pfam; PF09379; FERM_N; 1.
DR Pfam; PF00169; PH; 2.
DR Pfam; PF00621; RhoGEF; 1.
DR PRINTS; PR00935; BAND41.
DR PRINTS; PR00661; ERMFAMILY.
DR SMART; SM00295; B41; 1.
DR SMART; SM01195; FA; 1.
DR SMART; SM01196; FERM_C; 1.
DR SMART; SM00233; PH; 2.
DR SMART; SM00325; RhoGEF; 1.
DR SUPFAM; SSF47031; SSF47031; 1.
DR SUPFAM; SSF48065; SSF48065; 1.
DR SUPFAM; SSF54236; SSF54236; 1.
DR PROSITE; PS50010; DH_2; 1.
DR PROSITE; PS00660; FERM_1; 1.
DR PROSITE; PS50057; FERM_3; 1.
DR PROSITE; PS50003; PH_DOMAIN; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cell membrane; Cell projection;
KW Cytoplasm; Developmental protein; Guanine-nucleotide releasing factor;
KW Membrane; Phosphoprotein; Reference proteome; Repeat; Synapse; Synaptosome.
FT CHAIN 1..1045
FT /note="FERM, ARHGEF and pleckstrin domain-containing
FT protein 1"
FT /id="PRO_0000232753"
FT DOMAIN 40..320
FT /note="FERM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00084"
FT DOMAIN 540..730
FT /note="DH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00062"
FT DOMAIN 759..856
FT /note="PH 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT DOMAIN 932..1029
FT /note="PH 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT REGION 1..37
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 361..534
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 864..903
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 16..30
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 371..401
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 460..515
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 20
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:F8VPU2"
FT MOD_RES 23
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:F8VPU2"
FT MOD_RES 24
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"
FT MOD_RES 340
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 373
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 389
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:F8VPU2"
FT MOD_RES 403
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 418
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 427
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17924679,
FT ECO:0007744|PubMed:18220336, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 433
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:F8VPU2"
FT MOD_RES 510
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 514
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 833
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 872
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 878
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:F8VPU2"
FT MOD_RES 883
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 889
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18318008,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:24275569"
FT MOD_RES 896
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:F8VPU2"
FT MOD_RES 899
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:F8VPU2"
FT VAR_SEQ 58..129
FT /note="QRAPGKVLLDAVCNHLNLVEGDYFGLEFPDHKKITVWLDLLKPIVKQIRRPK
FT HVVVKFVVKFFPPDHTQLQE -> MVSSSSFLKATGSSWTGWVLRCSMKPKHHSHLIEK
FT FGEDRILTHLTGSISYTNWAGSRSLAVTVTEELLNLF (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_040989"
FT VAR_SEQ 130..1045
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_040990"
FT VAR_SEQ 758
FT /note="R -> RPGSFSLMRTPHLGQARRIPCAPERRPLLLVK (in isoform
FT 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_017976"
FT VARIANT 8
FT /note="P -> L (in dbSNP:rs9300466)"
FT /id="VAR_048362"
FT VARIANT 714
FT /note="R -> L (in a breast cancer sample; somatic mutation;
FT dbSNP:rs1458028855)"
FT /evidence="ECO:0000269|PubMed:16959974"
FT /id="VAR_035851"
FT CONFLICT 644
FT /note="H -> Y (in Ref. 3; AAH71592)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1045 AA; 118633 MW; 0E8B2D61C0F58417 CRC64;
MGEIEQRPTP GSRLGAPENS GISTLERGQK PPPTPSGKLV SIKIQMLDDT QEAFEVPQRA
PGKVLLDAVC NHLNLVEGDY FGLEFPDHKK ITVWLDLLKP IVKQIRRPKH VVVKFVVKFF
PPDHTQLQEE LTRYLFALQV KQDLAQGRLT CNDTSAALLI SHIVQSEIGD FDEALDREHL
AKNKYIPQQD ALEDKIVEFH HNHIGQTPAE SDFQLLEIAR RLEMYGIRLH PAKDREGTKI
NLAVANTGIL VFQGFTKINA FNWAKVRKLS FKRKRFLIKL RPDANSAYQD TLEFLMASRD
FCKSFWKICV EHHAFFRLFE EPKPKPKPVL FSRGSSFRFS GRTQKQVLDY VKEGGHKKVQ
FERKHSKIHS IRSLASQPTE LNSEVLEQSQ QSTSLTFGEG AESPGGQSCR RGKEPKVSAG
EPGSHPSPAP RRSPAGNKQA DGAASAPTEE EEEVVKDRTQ QSKPQPPQPS TGSLTGSPHL
SELSVNSQGG VAPANVTLSP NLSPDTKQAS PLISPLLNDQ ACPRTDDEDE GRRKRFPTDK
AYFIAKEVST TERTYLKDLE VITSWFQSTV SKEDAMPEAL KSLIFPNFEP LHKFHTNFLK
EIEQRLALWE GRSNAQIRDY QRIGDVMLKN IQGMKHLAAH LWKHSEALEA LENGIKSSRR
LENFCRDFEL QKVCYLPLNT FLLRPLHRLM HYKQVLERLC KHHPPSHADF RDCRAALAEI
TEMVAQLHGT MIKMENFQKL HELKKDLIGI DNLVVPGREF IRLGSLSKLS GKGLQQRMFF
LFNDVLLYTS RGLTASNQFK VHGQLPLYGM TIEESEDEWG VPHCLTLRGQ RQSIIVAASS
RSEMEKWVED IQMAIDLAEK SSSPAPEFLA SSPPDNKSPD EATAADQESE DDLSASRTSL
ERQAPHRGNT MVHVCWHRNT SVSMVDFSIA VENQLSGNLL RKFKNSNGWQ KLWVVFTNFC
LFFYKSHQDN HPLASLPLLG YSLTIPSESE NIQKDYVFKL HFKSHVYYFR AESEYTFERW
MEVIRSATSS ASRPHVLSHK ESLVY
