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   27-MAR-2024, entry version 165.
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   -!- INTERACTION:
CC       Q86YV5; P31947: SFN; NbExp=2; IntAct=EBI-719420, EBI-476295;
CC       Q86YV5; P62258: YWHAE; NbExp=2; IntAct=EBI-719420, EBI-356498;
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   PDB; 8DGN; X-ray; 3.16 A; B=812-831.
DR   PDBsum; 5VE6; -.
DR   PDBsum; 8DGN; -.
DR   AlphaFoldDB; Q86YV5; -.
DR   SMR; Q86YV5; -.
DR   BioGRID; 127591; 29.
DR   IntAct; Q86YV5; 13.
DR   MINT; Q86YV5; -.
DR   STRING; 9606.ENSP00000481109; -.
DR   iPTMnet; Q86YV5; -.
DR   PhosphoSitePlus; Q86YV5; -.
DR   BioMuta; PRAG1; -.
DR   DMDM; 327478560; -.
DR   CPTAC; non-CPTAC-5650; -.
DR   CPTAC; non-CPTAC-5651; -.
DR   EPD; Q86YV5; -.
DR   jPOST; Q86YV5; -.
DR   MassIVE; Q86YV5; -.
DR   PaxDb; 9606-ENSP00000481109; -.
DR   PeptideAtlas; Q86YV5; -.
DR   ProteomicsDB; 70475; -.
DR   Pumba; Q86YV5; -.
DR   Antibodypedia; 73468; 150 antibodies from 28 providers.
DR   DNASU; 157285; -.
DR   Ensembl; ENST00000615670.5; ENSP00000481109.1; ENSG00000275342.6.
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   AGR; HGNC:25438; -.
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; DLKMSAC; -.
DR   OrthoDB; 2914135at2759; -.
DR   PathwayCommons; Q86YV5; -.
DR   Reactome; R-HSA-9696270; RND2 GTPase cycle.
DR   SignaLink; Q86YV5; -.
DR   BioGRID-ORCS; 157285; 22 hits in 1121 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 184 other cell types or tissues.
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: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   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR   InterPro; IPR008266; Tyr_kinase_AS.
DR   PANTHER; PTHR22972:SF3; INACTIVE TYROSINE-PROTEIN KINASE PRAG1; 1.
DR   PANTHER; PTHR22972; SERINE/THREONINE PROTEIN KINASE; 1.
DR   Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00109; PROTEIN_KINASE_TYR; 1.
DR   Genevisible; Q86YV5; HS.
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
//