PRAG1_HUMAN
ID PRAG1_HUMAN Reviewed; 1406 AA.
AC Q86YV5; Q8N3N5;
DT 28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2014, sequence version 4.
DT 03-AUG-2022, entry version 156.
DE RecName: Full=Inactive tyrosine-protein kinase PRAG1 {ECO:0000305};
DE AltName: Full=PEAK1-related kinase-activating pseudokinase 1;
DE AltName: Full=Pragmin {ECO:0000303|PubMed:27116701};
DE AltName: Full=Sugen kinase 223 {ECO:0000303|PubMed:29079850};
DE Short=SgK223;
GN Name=PRAG1 {ECO:0000312|HGNC:HGNC:25438}; Synonyms=SGK223;
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 [LARGE SCALE GENOMIC DNA].
RX PubMed=16421571; DOI=10.1038/nature04406;
RA Nusbaum C., Mikkelsen T.S., Zody M.C., Asakawa S., Taudien S., Garber M.,
RA Kodira C.D., Schueler M.G., Shimizu A., Whittaker C.A., Chang J.L.,
RA Cuomo C.A., Dewar K., FitzGerald M.G., Yang X., Allen N.R., Anderson S.,
RA Asakawa T., Blechschmidt K., Bloom T., Borowsky M.L., Butler J., Cook A.,
RA Corum B., DeArellano K., DeCaprio D., Dooley K.T., Dorris L. III,
RA Engels R., Gloeckner G., Hafez N., Hagopian D.S., Hall J.L., Ishikawa S.K.,
RA Jaffe D.B., Kamat A., Kudoh J., Lehmann R., Lokitsang T., Macdonald P.,
RA Major J.E., Matthews C.D., Mauceli E., Menzel U., Mihalev A.H.,
RA Minoshima S., Murayama Y., Naylor J.W., Nicol R., Nguyen C., O'Leary S.B.,
RA O'Neill K., Parker S.C.J., Polley A., Raymond C.K., Reichwald K.,
RA Rodriguez J., Sasaki T., Schilhabel M., Siddiqui R., Smith C.L.,
RA Sneddon T.P., Talamas J.A., Tenzin P., Topham K., Venkataraman V., Wen G.,
RA Yamazaki S., Young S.K., Zeng Q., Zimmer A.R., Rosenthal A., Birren B.W.,
RA Platzer M., Shimizu N., Lander E.S.;
RT "DNA sequence and analysis of human chromosome 8.";
RL Nature 439:331-335(2006).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 24-1406, AND VARIANTS GLN-404; LEU-569;
RP CYS-578 AND THR-1113.
RC TISSUE=Spleen;
RA Jikuya H., Takano J., Nomura N., Kikuno R., Nagase T., Ohara O.;
RT "The nucleotide sequence of a long cDNA clone isolated from human spleen.";
RL Submitted (FEB-2003) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 820-1406, AND VARIANT THR-1113.
RC TISSUE=Amygdala;
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 IDENTIFICATION.
RX PubMed=12471243; DOI=10.1126/science.1075762;
RA Manning G., Whyte D.B., Martinez R., Hunter T., Sudarsanam S.;
RT "The protein kinase complement of the human genome.";
RL Science 298:1912-1934(2002).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-696 AND SER-745, 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 [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-745, 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 [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-826, 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 [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-148; SER-696 AND SER-826, AND
RP IDENTIFICATION BY 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 [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-148 AND SER-782, AND
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 [10]
RP VARIANTS [LARGE SCALE ANALYSIS] ILE-122; GLY-137; ILE-139; GLN-404;
RP LEU-569; CYS-578; ALA-595; THR-662; LEU-814; ARG-851; LEU-1003; MET-1041;
RP THR-1113 AND HIS-1315.
RX PubMed=17344846; DOI=10.1038/nature05610;
RA Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C., Bignell G.,
RA Davies H., Teague J., Butler A., Stevens C., Edkins S., O'Meara S.,
RA Vastrik I., Schmidt E.E., Avis T., Barthorpe S., Bhamra G., Buck G.,
RA Choudhury B., Clements J., Cole J., Dicks E., Forbes S., Gray K.,
RA Halliday K., Harrison R., Hills K., Hinton J., Jenkinson A., Jones D.,
RA Menzies A., Mironenko T., Perry J., Raine K., Richardson D., Shepherd R.,
RA Small A., Tofts C., Varian J., Webb T., West S., Widaa S., Yates A.,
RA Cahill D.P., Louis D.N., Goldstraw P., Nicholson A.G., Brasseur F.,
RA Looijenga L., Weber B.L., Chiew Y.-E., DeFazio A., Greaves M.F.,
RA Green A.R., Campbell P., Birney E., Easton D.F., Chenevix-Trench G.,
RA Tan M.-H., Khoo S.K., Teh B.T., Yuen S.T., Leung S.Y., Wooster R.,
RA Futreal P.A., Stratton M.R.;
RT "Patterns of somatic mutation in human cancer genomes.";
RL Nature 446:153-158(2007).
RN [11]
RP SUBCELLULAR LOCATION.
RX PubMed=27116701; DOI=10.1111/cas.12962;
RA Senda Y., Murata-Kamiya N., Hatakeyama M.;
RT "C-terminal Src kinase-mediated EPIYA phosphorylation of Pragmin creates a
RT feed-forward C-terminal Src kinase activation loop that promotes cell
RT motility.";
RL Cancer Sci. 107:972-980(2016).
RN [12] {ECO:0007744|PDB:5VE6}
RP X-RAY CRYSTALLOGRAPHY (2.95 ANGSTROMS) OF 932-1406, MUTAGENESIS OF LEU-955;
RP LEU-966; ILE-1243; PHE-1271; ARG-1278; TYR-1282; PHE-1366 AND TRP-1382,
RP SUBUNIT, INTERACTION WITH PEAK1, AND DOMAIN.
RX PubMed=29079850; DOI=10.1038/s41467-017-01279-9;
RA Patel O., Griffin M.D.W., Panjikar S., Dai W., Ma X., Chan H., Zheng C.,
RA Kropp A., Murphy J.M., Daly R.J., Lucet I.S.;
RT "Structure of SgK223 pseudokinase reveals novel mechanisms of homotypic and
RT heterotypic association.";
RL Nat. Commun. 8:1157-1157(2017).
CC -!- FUNCTION: Catalytically inactive protein kinase that acts as a scaffold
CC protein. Functions as an effector of the small GTPase RND2, which
CC stimulates RhoA activity and inhibits NGF-induced neurite outgrowth (By
CC similarity). Promotes Src family kinase (SFK) signaling by regulating
CC the subcellular localization of CSK, a negative regulator of these
CC kinases, leading to the regulation of cell morphology and motility by a
CC CSK-dependent mechanism (By similarity). Acts as a critical coactivator
CC of Notch signaling (By similarity). {ECO:0000250|UniProtKB:D3ZMK9,
CC ECO:0000250|UniProtKB:Q571I4}.
CC -!- SUBUNIT: Homodimer (PubMed:29079850). Dimerization leads to the
CC catalytic activation of CSK (By similarity). Interacts (via C-terminus)
CC with RND2 (By similarity). Interacts with CSK (via SH2 domain) in a
CC Tyr-413 phosphorylation-dependent manner; this interaction potentiates
CC kinase activity of CSK (By similarity). Interacts with PEAK1
CC (PubMed:29079850). Interacts with NOTCH1 intracellular domain (N1ICD)
CC (By similarity). Forms a complex with N1ICD and MAML1, in a MAML1-
CC dependent manner (By similarity). {ECO:0000250|UniProtKB:D3ZMK9,
CC ECO:0000250|UniProtKB:Q571I4, ECO:0000269|PubMed:29079850}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:D3ZMK9}. Cell
CC junction, focal adhesion {ECO:0000269|PubMed:27116701}. Nucleus
CC {ECO:0000250|UniProtKB:Q571I4}. Note=Colocalized with NOTCH1 in the
CC nucleus. {ECO:0000250|UniProtKB:Q571I4}.
CC -!- DOMAIN: The dimerization region encompasses helices both from the
CC N- and C-terminal of the protein kinase domain.
CC {ECO:0000269|PubMed:29079850}.
CC -!- PTM: Phosphorylated by CSK on Tyr-253, Tyr-365, and Tyr-413; Tyr-413 is
CC a primary site of phosphorylation. {ECO:0000250|UniProtKB:D3ZMK9}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. {ECO:0000305}.
CC -!- CAUTION: Despite of the presence of a putative ATP-binding motif, this
CC protein does not bind ATP, suggesting that it has no protein kinase
CC activity. {ECO:0000250|UniProtKB:D3ZMK9}.
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DR EMBL; AC068353; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC103957; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AK122582; BAC56923.1; -; mRNA.
DR EMBL; AL833872; CAD38729.1; -; mRNA.
DR CCDS; CCDS43706.1; -.
DR RefSeq; NP_001074295.2; NM_001080826.2.
DR RefSeq; XP_005272426.2; XM_005272369.4.
DR RefSeq; XP_005272427.2; XM_005272370.4.
DR PDB; 5VE6; X-ray; 2.95 A; A=932-1406.
DR PDBsum; 5VE6; -.
DR AlphaFoldDB; Q86YV5; -.
DR SMR; Q86YV5; -.
DR BioGRID; 127591; 21.
DR IntAct; Q86YV5; 12.
DR MINT; Q86YV5; -.
DR STRING; 9606.ENSP00000481109; -.
DR iPTMnet; Q86YV5; -.
DR PhosphoSitePlus; Q86YV5; -.
DR BioMuta; PRAG1; -.
DR DMDM; 327478560; -.
DR EPD; Q86YV5; -.
DR jPOST; Q86YV5; -.
DR MassIVE; Q86YV5; -.
DR PaxDb; Q86YV5; -.
DR PeptideAtlas; Q86YV5; -.
DR PRIDE; Q86YV5; -.
DR ProteomicsDB; 70475; -.
DR Antibodypedia; 73468; 129 antibodies from 28 providers.
DR DNASU; 157285; -.
DR Ensembl; ENST00000615670.5; ENSP00000481109.1; ENSG00000275342.5.
DR Ensembl; ENST00000622241.1; ENSP00000479068.1; ENSG00000275342.5.
DR GeneID; 157285; -.
DR KEGG; hsa:157285; -.
DR MANE-Select; ENST00000615670.5; ENSP00000481109.1; NM_001080826.3; NP_001074295.2.
DR UCSC; uc064kbu.1; human.
DR CTD; 157285; -.
DR DisGeNET; 157285; -.
DR GeneCards; PRAG1; -.
DR HGNC; HGNC:25438; PRAG1.
DR HPA; ENSG00000275342; Tissue enhanced (brain, thyroid gland).
DR MIM; 617344; gene.
DR neXtProt; NX_Q86YV5; -.
DR OpenTargets; ENSG00000275342; -.
DR VEuPathDB; HostDB:ENSG00000275342; -.
DR eggNOG; ENOG502QVUZ; Eukaryota.
DR GeneTree; ENSGT00940000157066; -.
DR HOGENOM; CLU_005467_0_0_1; -.
DR InParanoid; Q86YV5; -.
DR OMA; FKGNGHW; -.
DR OrthoDB; 49921at2759; -.
DR PathwayCommons; Q86YV5; -.
DR Reactome; R-HSA-9696270; RND2 GTPase cycle.
DR SignaLink; Q86YV5; -.
DR BioGRID-ORCS; 157285; 21 hits in 1043 CRISPR screens.
DR ChiTaRS; SGK223; human.
DR GenomeRNAi; 157285; -.
DR Pharos; Q86YV5; Tbio.
DR PRO; PR:Q86YV5; -.
DR Proteomes; UP000005640; Chromosome 8.
DR RNAct; Q86YV5; protein.
DR Bgee; ENSG00000275342; Expressed in cerebellar vermis and 182 other tissues.
DR Genevisible; Q86YV5; HS.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005925; C:focal adhesion; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; IDA:UniProtKB.
DR GO; GO:0004672; F:protein kinase activity; IBA:GO_Central.
DR GO; GO:0016477; P:cell migration; IMP:UniProtKB.
DR GO; GO:0010977; P:negative regulation of neuron projection development; ISS:UniProtKB.
DR GO; GO:0035025; P:positive regulation of Rho protein signal transduction; ISS:UniProtKB.
DR GO; GO:0006468; P:protein phosphorylation; IBA:GO_Central.
DR GO; GO:2000145; P:regulation of cell motility; ISS:UniProtKB.
DR GO; GO:0008360; P:regulation of cell shape; ISS:UniProtKB.
DR GO; GO:0008593; P:regulation of Notch signaling pathway; ISS:UniProtKB.
DR DisProt; DP02420; -.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR008266; Tyr_kinase_AS.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00109; PROTEIN_KINASE_TYR; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell junction; Cytoplasm; Nucleus; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..1406
FT /note="Inactive tyrosine-protein kinase PRAG1"
FT /id="PRO_0000263008"
FT DOMAIN 978..1329
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 184..205
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 217..248
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 372..470
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 484..854
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 933..976
FT /note="Required for homodimerization"
FT /evidence="ECO:0000250|UniProtKB:D3ZMK9"
FT REGION 1163..1206
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1331..1406
FT /note="Required for homodimerization"
FT /evidence="ECO:0000250|UniProtKB:D3ZMK9"
FT COMPBIAS 502..529
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 530..544
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 603..630
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 654..692
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 730..784
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 828..851
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1163..1181
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 148
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 253
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:D3ZMK9"
FT MOD_RES 365
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:D3ZMK9"
FT MOD_RES 413
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:D3ZMK9"
FT MOD_RES 696
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 745
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332"
FT MOD_RES 782
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 826
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT VARIANT 122
FT /note="L -> I (in dbSNP:rs55764617)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_041803"
FT VARIANT 137
FT /note="R -> G (in dbSNP:rs56290960)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_041804"
FT VARIANT 139
FT /note="V -> I (in dbSNP:rs34346032)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_041805"
FT VARIANT 404
FT /note="R -> Q (in dbSNP:rs3896980)"
FT /evidence="ECO:0000269|PubMed:17344846, ECO:0000269|Ref.2"
FT /id="VAR_041806"
FT VARIANT 569
FT /note="P -> L (in dbSNP:rs4840955)"
FT /evidence="ECO:0000269|PubMed:17344846, ECO:0000269|Ref.2"
FT /id="VAR_041807"
FT VARIANT 578
FT /note="S -> C (in dbSNP:rs4840953)"
FT /evidence="ECO:0000269|PubMed:17344846, ECO:0000269|Ref.2"
FT /id="VAR_041808"
FT VARIANT 595
FT /note="P -> A (in dbSNP:rs55994745)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_041809"
FT VARIANT 662
FT /note="P -> T (in dbSNP:rs56351643)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_041810"
FT VARIANT 814
FT /note="P -> L (in dbSNP:rs56207906)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_041811"
FT VARIANT 851
FT /note="H -> R (in dbSNP:rs56215812)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_041812"
FT VARIANT 1003
FT /note="S -> L (in dbSNP:rs56289289)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_041813"
FT VARIANT 1041
FT /note="V -> M (in dbSNP:rs28533138)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_041814"
FT VARIANT 1113
FT /note="A -> T (in dbSNP:rs12549973)"
FT /evidence="ECO:0000269|PubMed:17344846,
FT ECO:0000269|PubMed:17974005, ECO:0000269|Ref.2"
FT /id="VAR_041815"
FT VARIANT 1315
FT /note="R -> H (in dbSNP:rs1314830862)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_041816"
FT MUTAGEN 955
FT /note="L->A: Decreases homodimerization. Abolished
FT interaction with PEAK1. No effect on cell migration."
FT /evidence="ECO:0000269|PubMed:29079850"
FT MUTAGEN 966
FT /note="L->A: Decreases homodimerization. Abolished
FT interaction with PEAK1. Decreases cell migration."
FT /evidence="ECO:0000269|PubMed:29079850"
FT MUTAGEN 1243
FT /note="I->A: No effect on homodimerization. Decreases
FT oligomerization. Decreases interaction with PEAK1."
FT /evidence="ECO:0000269|PubMed:29079850"
FT MUTAGEN 1271
FT /note="F->A: Decreases homodimerization. Decreases
FT interaction with PEAK1."
FT /evidence="ECO:0000269|PubMed:29079850"
FT MUTAGEN 1278
FT /note="R->A: Decreases homodimerization."
FT /evidence="ECO:0000269|PubMed:29079850"
FT MUTAGEN 1282
FT /note="Y->A: No effect on homodimerization. Decreases
FT oligomerization. Decreases interaction with PEAK1. No
FT effect on cell migration."
FT /evidence="ECO:0000269|PubMed:29079850"
FT MUTAGEN 1366
FT /note="F->A: Decreases homodimerization. Abolished
FT interaction with PEAK1. Decreases cell migration."
FT /evidence="ECO:0000269|PubMed:29079850"
FT MUTAGEN 1382
FT /note="W->A: Decreases homodimerization. Abolished
FT interaction with PEAK1. Decreases cell migration."
FT /evidence="ECO:0000269|PubMed:29079850"
FT CONFLICT 1226
FT /note="G -> S (in Ref. 2; BAC56923 and 3; CAD38729)"
FT /evidence="ECO:0000305"
FT HELIX 948..974
FT /evidence="ECO:0007829|PDB:5VE6"
FT HELIX 988..991
FT /evidence="ECO:0007829|PDB:5VE6"
FT STRAND 992..995
FT /evidence="ECO:0007829|PDB:5VE6"
FT STRAND 1000..1002
FT /evidence="ECO:0007829|PDB:5VE6"
FT STRAND 1004..1016
FT /evidence="ECO:0007829|PDB:5VE6"
FT STRAND 1020..1026
FT /evidence="ECO:0007829|PDB:5VE6"
FT STRAND 1050..1059
FT /evidence="ECO:0007829|PDB:5VE6"
FT HELIX 1060..1063
FT /evidence="ECO:0007829|PDB:5VE6"
FT STRAND 1084..1094
FT /evidence="ECO:0007829|PDB:5VE6"
FT STRAND 1096..1099
FT /evidence="ECO:0007829|PDB:5VE6"
FT HELIX 1100..1105
FT /evidence="ECO:0007829|PDB:5VE6"
FT HELIX 1108..1113
FT /evidence="ECO:0007829|PDB:5VE6"
FT HELIX 1115..1138
FT /evidence="ECO:0007829|PDB:5VE6"
FT HELIX 1148..1150
FT /evidence="ECO:0007829|PDB:5VE6"
FT STRAND 1151..1154
FT /evidence="ECO:0007829|PDB:5VE6"
FT STRAND 1211..1214
FT /evidence="ECO:0007829|PDB:5VE6"
FT HELIX 1246..1250
FT /evidence="ECO:0007829|PDB:5VE6"
FT HELIX 1252..1264
FT /evidence="ECO:0007829|PDB:5VE6"
FT HELIX 1270..1272
FT /evidence="ECO:0007829|PDB:5VE6"
FT HELIX 1275..1279
FT /evidence="ECO:0007829|PDB:5VE6"
FT HELIX 1284..1286
FT /evidence="ECO:0007829|PDB:5VE6"
FT HELIX 1296..1307
FT /evidence="ECO:0007829|PDB:5VE6"
FT TURN 1312..1314
FT /evidence="ECO:0007829|PDB:5VE6"
FT HELIX 1318..1329
FT /evidence="ECO:0007829|PDB:5VE6"
FT HELIX 1348..1369
FT /evidence="ECO:0007829|PDB:5VE6"
FT HELIX 1379..1389
FT /evidence="ECO:0007829|PDB:5VE6"
FT HELIX 1393..1402
FT /evidence="ECO:0007829|PDB:5VE6"
SQ SEQUENCE 1406 AA; 149624 MW; 941BCF315B826148 CRC64;
MHQTLCLNPE SLKMSACSDF VEHIWKPGSC KNCFCLRSDH QLVAGPPQPR AGSLPPPPRL
PPRPENCRLE DEGVNSSPYS KPTIAVKPTM MSSEASDVWT EANLSAEVSQ VIWRRAPGKL
PLPKQEDAPV VYLGSFRGVQ KPAGPSTSPD GNSRCPPAYT MVGLHNLEPR GERNIAFHPV
SFPEEKAVHK EKPSFPYQDR PSTQESFRQK LAAFAGTTSG CHQGPGPLRE SLPSEDDSDQ
RCSPSGDSEG GEYCSILDCC PGSPVAKAAS QTAGSRGRHG GRDCSPTCWE QGKCSGPAEQ
EKRGPSFPKE CCSQGPTAHP SCLGPKKLSL TSEAAISSDG LSCGSGSGSG SGASSPFVPH
LESDYCSLMK EPAPEKQQDP GCPGVTPSRC LGLTGEPQPP AHPREATQPE PIYAESTKRK
KAAPVPSKSQ AKIEHAAAAQ GQGQVCTGNA WAQKAASGWG RDSPDPTPQV SATITVMAAH
PEEDHRTIYL SSPDSAVGVQ WPRGPVSQNS EVGEEETSAG QGLSSRESHA HSASESKPKE
RPAIPPKLSK SSPVGSPVSP SAGGPPVSPL ADLSDGSSGG SSIGPQPPSQ GPADPAPSCR
TNGVAISDPS RCPQPAASSA SEQRRPRFQA GTWSRQCRIE EEEEVEQELL SHSWGRETKN
GPTDHSNSTT WHRLHPTDGS SGQNSKVGTG MSKSASFAFE FPKDRSGIET FSPPPPPPKS
RHLLKMNKSS SDLEKVSQGS AESLSPSFRG VHVSFTTGST DSLASDSRTC SDGGPSSELA
HSPTNSGKKL FAPVPFPSGS TEDVSPSGPQ QPPPLPQKKI VSRAASSPDG FFWTQGSPKP
GTASPKLNLS HSETNVHDES HFSYSLSPGN RHHPVFSSSD PLEKAFKGSG HWLPAAGLAG
NRGGCGSPGL QCKGAPSASS SQLSVSSQAS TGSTQLQLHG LLSNISSKEG TYAKLGGLYT
QSLARLVAKC EDLFMGGQKK ELHFNENNWS LFKLTCNKPC CDSGDAIYYC ATCSEDPGST
YAVKICKAPE PKTVSYCSPS VPVHFNIQQD CGHFVASVPS SMLSSPDAPK DPVPALPTHP
PAQEQDCVVV ITREVPHQTA SDFVRDSAAS HQAEPEAYER RVCFLLLQLC NGLEHLKEHG
IIHRDLCLEN LLLVHCTLQA GPGPAPAPAP APAPAAAAPP CSSAAPPAGG TLSPAAGPAS
PEGPREKQLP RLIISNFLKA KQKPGGTPNL QQKKSQARLA PEIVSASQYR KFDEFQTGIL
IYELLHQPNP FEVRAQLRER DYRQEDLPPL PALSLYSPGL QQLAHLLLEA DPIKRIRIGE
AKRVLQCLLW GPRRELVQQP GTSEEALCGT LHNWIDMKRA LMMMKFAEKA VDRRRGVELE
DWLCCQYLAS AEPGALLQSL KLLQLL
