MPRIP_HUMAN
ID MPRIP_HUMAN Reviewed; 1025 AA.
AC Q6WCQ1; Q3KQZ5; Q5FB94; Q6DHW2; Q7Z5Y2; Q8N390; Q96G40;
DT 21-FEB-2006, integrated into UniProtKB/Swiss-Prot.
DT 25-NOV-2008, sequence version 3.
DT 03-AUG-2022, entry version 157.
DE RecName: Full=Myosin phosphatase Rho-interacting protein;
DE Short=M-RIP;
DE AltName: Full=Rho-interacting protein 3;
DE Short=RIP3;
DE AltName: Full=p116Rip;
GN Name=MPRIP; Synonyms=KIAA0864, MRIP, RHOIP3 {ECO:0000312|EMBL:BAC78198.1};
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] {ECO:0000305, ECO:0000312|EMBL:AAQ63176.1}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), SUBCELLULAR LOCATION, AND
RP INTERACTION WITH PPP1R12A AND RHOA.
RC TISSUE=Aorta {ECO:0000312|EMBL:AAQ63176.1};
RX PubMed=14506264; DOI=10.1074/jbc.m305622200;
RA Surks H.K., Richards C.T., Mendelsohn M.E.;
RT "Myosin phosphatase-Rho interacting protein. A new member of the myosin
RT phosphatase complex that directly binds RhoA.";
RL J. Biol. Chem. 278:51484-51493(2003).
RN [2] {ECO:0000305, ECO:0000312|EMBL:BAD89507.1}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION, AND INTERACTION WITH
RP PPP1R12A.
RX PubMed=15545284; DOI=10.1074/jbc.m410909200;
RA Koga Y., Ikebe M.;
RT "p116Rip decreases myosin II phosphorylation by activating myosin light
RT chain phosphatase and by inactivating RhoA.";
RL J. Biol. Chem. 280:4983-4991(2005).
RN [3] {ECO:0000305, ECO:0000312|EMBL:BAC78198.1}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), AND VARIANT GLN-327.
RA Inazawa J., Imoto I.;
RT "Cloning of human orthologue RHOIP3 of Mus Rhoip3.";
RL Submitted (DEC-2002) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16625196; DOI=10.1038/nature04689;
RA Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R.,
RA Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A.,
RA Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J.,
RA Chang J.L., Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J.,
RA DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S.,
RA Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E.,
RA Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K.,
RA LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J.,
RA Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A.,
RA Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K.,
RA Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D.,
RA Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A.,
RA Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.;
RT "DNA sequence of human chromosome 17 and analysis of rearrangement in the
RT human lineage.";
RL Nature 440:1045-1049(2006).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 38-1025 (ISOFORM 1), AND VARIANT
RP GLN-327.
RC TISSUE=Melanoma;
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 [6] {ECO:0000305, ECO:0000312|EMBL:AAI05988.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 157-1025 (ISOFORM 3), NUCLEOTIDE
RP SEQUENCE [LARGE SCALE MRNA] OF 194-1025 (ISOFORM 1), AND NUCLEOTIDE
RP SEQUENCE [LARGE SCALE MRNA] OF 377-1025 (ISOFORM 2).
RC TISSUE=Brain {ECO:0000312|EMBL:AAH75847.1},
RC Lymph {ECO:0000312|EMBL:AAI05988.1}, and
RC Muscle {ECO:0000312|EMBL:AAH09982.2};
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] {ECO:0000305}
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH PPP1R12A AND F-ACTIN.
RX PubMed=16257966; DOI=10.1074/jbc.m506863200;
RA Surks H.K., Riddick N., Ohtani K.;
RT "M-RIP targets myosin phosphatase to stress fibers to regulate myosin light
RT chain phosphorylation in vascular smooth muscle cells.";
RL J. Biol. Chem. 280:42543-42551(2005).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-619, AND IDENTIFICATION BY
RP 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 [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of the
RT kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-192; SER-220; SER-224;
RP SER-226; SER-289; SER-292; THR-295; SER-362; SER-365; SER-619; SER-891 AND
RP SER-977, AND 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 [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-289, 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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-220; SER-269; SER-289;
RP SER-362; SER-365; SER-619; SER-891 AND SER-977, AND IDENTIFICATION BY MASS
RP 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 [13]
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 [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-977; SER-993 AND SER-1016,
RP AND 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 [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-224; SER-265; SER-269;
RP SER-326; SER-493; SER-619; THR-646; SER-663; SER-891; SER-977 AND SER-993,
RP 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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-217; SER-220; SER-226;
RP THR-348; SER-362; SER-365; SER-800 AND SER-891, 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).
CC -!- FUNCTION: Targets myosin phosphatase to the actin cytoskeleton.
CC Required for the regulation of the actin cytoskeleton by RhoA and
CC ROCK1. Depletion leads to an increased number of stress fibers in
CC smooth muscle cells through stabilization of actin fibers by
CC phosphorylated myosin. Overexpression of MRIP as well as its F-actin-
CC binding region leads to disassembly of stress fibers in neuronal cells.
CC {ECO:0000250|UniProtKB:P97434, ECO:0000269|PubMed:15545284,
CC ECO:0000269|PubMed:16257966}.
CC -!- SUBUNIT: Binds F-actin through its N-terminus. Interacts with MYZAP (By
CC similarity). Binds RHOA, PPP1R12A/MBS and PPP1R12C/MBS85 through
CC adjacent coiled coil domains. {ECO:0000250,
CC ECO:0000269|PubMed:14506264, ECO:0000269|PubMed:15545284,
CC ECO:0000269|PubMed:16257966}.
CC -!- INTERACTION:
CC Q6WCQ1; P63104: YWHAZ; NbExp=2; IntAct=EBI-1022605, EBI-347088;
CC Q6WCQ1; Q10728: Ppp1r12a; Xeno; NbExp=6; IntAct=EBI-1022605, EBI-918263;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000269|PubMed:14506264, ECO:0000269|PubMed:16257966}.
CC Note=Colocalizes with F-actin.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1 {ECO:0000269|PubMed:15545284};
CC IsoId=Q6WCQ1-1; Sequence=Displayed;
CC Name=2 {ECO:0000269|PubMed:14506264};
CC IsoId=Q6WCQ1-2; Sequence=VSP_051948;
CC Name=3 {ECO:0000305};
CC IsoId=Q6WCQ1-3; Sequence=VSP_051947, VSP_051948;
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DR EMBL; AY296247; AAQ63176.1; -; mRNA.
DR EMBL; AB189741; BAD89507.1; -; mRNA.
DR EMBL; AB098507; BAC78198.1; -; mRNA.
DR EMBL; AC079111; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC055811; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL834513; CAD39169.1; -; mRNA.
DR EMBL; BC009982; AAH09982.2; -; mRNA.
DR EMBL; BC075847; AAH75847.1; -; mRNA.
DR EMBL; BC105987; AAI05988.1; -; mRNA.
DR CCDS; CCDS32578.1; -. [Q6WCQ1-1]
DR CCDS; CCDS42268.1; -. [Q6WCQ1-2]
DR RefSeq; NP_055949.2; NM_015134.3. [Q6WCQ1-2]
DR RefSeq; NP_958431.2; NM_201274.3. [Q6WCQ1-1]
DR AlphaFoldDB; Q6WCQ1; -.
DR SMR; Q6WCQ1; -.
DR BioGRID; 116776; 198.
DR CORUM; Q6WCQ1; -.
DR IntAct; Q6WCQ1; 86.
DR MINT; Q6WCQ1; -.
DR STRING; 9606.ENSP00000379156; -.
DR GlyGen; Q6WCQ1; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q6WCQ1; -.
DR MetOSite; Q6WCQ1; -.
DR PhosphoSitePlus; Q6WCQ1; -.
DR SwissPalm; Q6WCQ1; -.
DR BioMuta; MPRIP; -.
DR DMDM; 215274136; -.
DR EPD; Q6WCQ1; -.
DR jPOST; Q6WCQ1; -.
DR MassIVE; Q6WCQ1; -.
DR MaxQB; Q6WCQ1; -.
DR PaxDb; Q6WCQ1; -.
DR PeptideAtlas; Q6WCQ1; -.
DR PRIDE; Q6WCQ1; -.
DR ProteomicsDB; 67759; -. [Q6WCQ1-1]
DR ProteomicsDB; 67760; -. [Q6WCQ1-2]
DR ProteomicsDB; 67761; -. [Q6WCQ1-3]
DR Antibodypedia; 13293; 221 antibodies from 31 providers.
DR DNASU; 23164; -.
DR Ensembl; ENST00000341712.8; ENSP00000342379.4; ENSG00000133030.22. [Q6WCQ1-1]
DR Ensembl; ENST00000395811.9; ENSP00000379156.4; ENSG00000133030.22. [Q6WCQ1-2]
DR GeneID; 23164; -.
DR KEGG; hsa:23164; -.
DR UCSC; uc002gqu.3; human. [Q6WCQ1-1]
DR CTD; 23164; -.
DR DisGeNET; 23164; -.
DR GeneCards; MPRIP; -.
DR HGNC; HGNC:30321; MPRIP.
DR HPA; ENSG00000133030; Low tissue specificity.
DR MIM; 612935; gene.
DR neXtProt; NX_Q6WCQ1; -.
DR OpenTargets; ENSG00000133030; -.
DR PharmGKB; PA162396092; -.
DR VEuPathDB; HostDB:ENSG00000133030; -.
DR eggNOG; KOG4807; Eukaryota.
DR GeneTree; ENSGT00940000155286; -.
DR HOGENOM; CLU_011327_0_0_1; -.
DR InParanoid; Q6WCQ1; -.
DR OrthoDB; 428862at2759; -.
DR PhylomeDB; Q6WCQ1; -.
DR TreeFam; TF329258; -.
DR PathwayCommons; Q6WCQ1; -.
DR Reactome; R-HSA-6802952; Signaling by BRAF and RAF1 fusions.
DR SignaLink; Q6WCQ1; -.
DR SIGNOR; Q6WCQ1; -.
DR BioGRID-ORCS; 23164; 83 hits in 1082 CRISPR screens.
DR ChiTaRS; MPRIP; human.
DR GeneWiki; M-RIP; -.
DR GenomeRNAi; 23164; -.
DR Pharos; Q6WCQ1; Tbio.
DR PRO; PR:Q6WCQ1; -.
DR Proteomes; UP000005640; Chromosome 17.
DR RNAct; Q6WCQ1; protein.
DR Bgee; ENSG00000133030; Expressed in lower esophagus mucosa and 205 other tissues.
DR ExpressionAtlas; Q6WCQ1; baseline and differential.
DR Genevisible; Q6WCQ1; HS.
DR GO; GO:0015629; C:actin cytoskeleton; IDA:HPA.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0005925; C:focal adhesion; HDA:UniProtKB.
DR GO; GO:0051015; F:actin filament binding; IBA:GO_Central.
DR GO; GO:0045296; F:cadherin binding; HDA:BHF-UCL.
DR GO; GO:0007015; P:actin filament organization; IBA:GO_Central.
DR CDD; cd13275; PH_M-RIP; 1.
DR Gene3D; 2.30.29.30; -; 2.
DR InterPro; IPR039597; M-RIP_PH.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR001849; PH_domain.
DR Pfam; PF00169; PH; 2.
DR SMART; SM00233; PH; 2.
DR PROSITE; PS50003; PH_DOMAIN; 2.
PE 1: Evidence at protein level;
KW Actin-binding; Alternative splicing; Coiled coil; Cytoplasm; Cytoskeleton;
KW Phosphoprotein; Reference proteome; Repeat.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000305"
FT CHAIN 2..1025
FT /note="Myosin phosphatase Rho-interacting protein"
FT /id="PRO_0000223930"
FT DOMAIN 43..150
FT /note="PH 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT DOMAIN 387..483
FT /note="PH 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT REGION 2..383
FT /note="Interaction with F-actin"
FT /evidence="ECO:0000250"
FT REGION 152..302
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 317..383
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 485..545
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 546..824
FT /note="Interaction with RHOA"
FT /evidence="ECO:0000269|PubMed:14506264"
FT REGION 560..591
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 824..879
FT /note="Interaction with PPP1R12A"
FT COILED 673..977
FT /evidence="ECO:0000255"
FT COMPBIAS 173..204
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 214..234
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 239..279
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 332..346
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 486..509
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 511..544
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 570..591
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 192
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 217
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 218
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P97434"
FT MOD_RES 220
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:24275569"
FT MOD_RES 224
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 226
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 265
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 269
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 289
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231"
FT MOD_RES 292
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 295
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 326
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 348
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 362
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:24275569"
FT MOD_RES 365
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:24275569"
FT MOD_RES 493
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 619
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 646
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 663
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 800
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 891
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 977
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 993
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 1014
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P97434"
FT MOD_RES 1016
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT VAR_SEQ 346..383
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_051947"
FT VAR_SEQ 1017..1025
FT /note="VIEQVSWDT -> LKEGLTVQERLKLFESRDLKKD (in isoform 2
FT and isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:15545284, ECO:0000303|Ref.3"
FT /id="VSP_051948"
FT VARIANT 327
FT /note="P -> Q (in dbSNP:rs3744137)"
FT /evidence="ECO:0000269|PubMed:17974005, ECO:0000269|Ref.3"
FT /id="VAR_051203"
FT CONFLICT 31
FT /note="S -> P (in Ref. 1; AAQ63176)"
FT /evidence="ECO:0000305"
FT CONFLICT 184
FT /note="S -> R (in Ref. 2; BAD89507)"
FT /evidence="ECO:0000305"
FT CONFLICT 188..189
FT /note="Missing (in Ref. 2; BAD89507 and 6; AAH09982)"
FT /evidence="ECO:0000305"
FT CONFLICT 189
FT /note="Missing (in Ref. 1; AAQ63176, 3; BAC78198 and 5;
FT CAD39169)"
FT /evidence="ECO:0000305"
FT CONFLICT 235
FT /note="S -> F (in Ref. 2; BAD89507)"
FT /evidence="ECO:0000305"
FT CONFLICT 352
FT /note="P -> S (in Ref. 2; BAD89507)"
FT /evidence="ECO:0000305"
FT CONFLICT 528
FT /note="R -> T (in Ref. 1; AAQ63176)"
FT /evidence="ECO:0000305"
FT CONFLICT 550
FT /note="P -> L (in Ref. 3; BAC78198 and 5; CAD39169)"
FT /evidence="ECO:0000305"
FT CONFLICT 578
FT /note="P -> S (in Ref. 1; AAQ63176)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1025 AA; 116533 MW; 5B7A30CDB3685E4E CRC64;
MSAAKENPCR KFQANIFNKS KCQNCFKPRE SHLLNDEDLT QAKPIYGGWL LLAPDGTDFD
NPVHRSRKWQ RRFFILYEHG LLRYALDEMP TTLPQGTINM NQCTDVVDGE GRTGQKFSLC
ILTPEKEHFI RAETKEIVSG WLEMLMVYPR TNKQNQKKKR KVEPPTPQEP GPAKVAVTSS
SSSSSSSSSI PSAEKVPTTK STLWQEEMRT KDQPDGSSLS PAQSPSQSQP PAASSLREPG
LESKEEESAM SSDRMDCGRK VRVESGYFSL EKTKQDLKAE EQQLPPPLSP PSPSTPNHRR
SQVIEKFEAL DIEKAEHMET NAVGPSPSSD TRQGRSEKRA FPRKRDFTNE APPAPLPDAS
ASPLSPHRRA KSLDRRSTEP SVTPDLLNFK KGWLTKQYED GQWKKHWFVL ADQSLRYYRD
SVAEEAADLD GEIDLSACYD VTEYPVQRNY GFQIHTKEGE FTLSAMTSGI RRNWIQTIMK
HVHPTTAPDV TSSLPEEKNK SSCSFETCPR PTEKQEAELG EPDPEQKRSR ARERRREGRS
KTFDWAEFRP IQQALAQERV GGVGPADTHE PLRPEAEPGE LERERARRRE ERRKRFGMLD
ATDGPGTEDA ALRMEVDRSP GLPMSDLKTH NVHVEIEQRW HQVETTPLRE EKQVPIAPVH
LSSEDGGDRL STHELTSLLE KELEQSQKEA SDLLEQNRLL QDQLRVALGR EQSAREGYVL
QATCERGFAA MEETHQKKIE DLQRQHQREL EKLREEKDRL LAEETAATIS AIEAMKNAHR
EEMERELEKS QRSQISSVNS DVEALRRQYL EELQSVQREL EVLSEQYSQK CLENAHLAQA
LEAERQALRQ CQRENQELNA HNQELNNRLA AEITRLRTLL TGDGGGEATG SPLAQGKDAY
ELEVLLRVKE SEIQYLKQEI SSLKDELQTA LRDKKYASDK YKDIYTELSI AKAKADCDIS
RLKEQLKAAT EALGEKSPDS ATVSGYDIMK SKSNPDFLKK DRSCVTRQLR NIRSKSVIEQ
VSWDT
