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   27-MAR-2024, entry version 166.
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;
GN   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}, Lymph
RC   {ECO:0000312|EMBL:AAI05988.1}, and Muscle
RC   {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; P31947: SFN; NbExp=3; IntAct=EBI-1022605, EBI-476295;
CC       Q6WCQ1; P27348: YWHAQ; NbExp=4; IntAct=EBI-1022605, EBI-359854;
CC       Q6WCQ1; P63104: YWHAZ; NbExp=3; 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; 233.
DR   CORUM; Q6WCQ1; -.
DR   IntAct; Q6WCQ1; 100.
DR   MINT; Q6WCQ1; -.
DR   STRING; 9606.ENSP00000379156; -.
DR   GlyCosmos; Q6WCQ1; 1 site, 1 glycan.
DR   GlyGen; Q6WCQ1; 4 sites, 1 O-linked glycan (4 sites).
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; 9606-ENSP00000379156; -.
DR   PeptideAtlas; Q6WCQ1; -.
DR   ProteomicsDB; 67759; -. [Q6WCQ1-1]
DR   ProteomicsDB; 67760; -. [Q6WCQ1-2]
DR   ProteomicsDB; 67761; -. [Q6WCQ1-3]
DR   Pumba; Q6WCQ1; -.
DR   Antibodypedia; 13293; 261 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   AGR; HGNC:30321; -.
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; 2961037at2759; -.
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; 92 hits in 1161 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 207 other cell types or tissues.
DR   ExpressionAtlas; Q6WCQ1; baseline and differential.
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   CDD; cd13275; PH_M-RIP; 1.
DR   CDD; cd01236; PH_RIP; 1.
DR   Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 2.
DR   InterPro; IPR039597; M-RIP_PH.
DR   InterPro; IPR011993; PH-like_dom_sf.
DR   InterPro; IPR001849; PH_domain.
DR   PANTHER; PTHR17271:SF9; MYOSIN PHOSPHATASE RHO-INTERACTING PROTEIN; 1.
DR   PANTHER; PTHR17271; PLECKSTRIN HOMOLOGY PH DOMAIN-CONTAINING PROTEIN; 1.
DR   Pfam; PF00169; PH; 2.
DR   SMART; SM00233; PH; 2.
DR   SUPFAM; SSF50729; PH domain-like; 2.
DR   PROSITE; PS50003; PH_DOMAIN; 2.
DR   Genevisible; Q6WCQ1; HS.
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
//