HIRP3_HUMAN
ID HIRP3_HUMAN Reviewed; 556 AA.
AC Q9BW71; H3BSR3; O75707; O75708;
DT 20-JUN-2002, integrated into UniProtKB/Swiss-Prot.
DT 17-OCT-2006, sequence version 3.
DT 03-AUG-2022, entry version 162.
DE RecName: Full=HIRA-interacting protein 3;
GN Name=HIRIP3;
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] (ISOFORMS 1 AND 2), FUNCTION, INTERACTION WITH
RP HIRA, AND TISSUE SPECIFICITY.
RC TISSUE=Cervix carcinoma;
RX PubMed=9710638; DOI=10.1128/mcb.18.9.5546;
RA Lorain S., Quivy J.-P., Monier-Gavelle F., Scamps C., Lecluse Y.,
RA Almouzni G., Lipinski M.;
RT "Core histones and HIRIP3, a novel histone-binding protein, directly
RT interact with WD repeat protein HIRA.";
RL Mol. Cell. Biol. 18:5546-5556(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), INTERACTION WITH CK2, SUBCELLULAR
RP LOCATION, AND PHOSPHORYLATION.
RX PubMed=17391060; DOI=10.1515/bc.2007.045;
RA Assrir N., Filhol O., Galisson F., Lipinski M.;
RT "HIRIP3 is a nuclear phosphoprotein interacting with and phosphorylated by
RT the serine-threonine kinase CK2.";
RL Biol. Chem. 388:391-398(2007).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC TISSUE=Neuroblastoma;
RA Li W.B., Gruber C., Jessee J., Polayes D.;
RT "Full-length cDNA libraries and normalization.";
RL Submitted (APR-2003) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15616553; DOI=10.1038/nature03187;
RA Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., Xie G.,
RA Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E.,
RA Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J., Buckingham J.M.,
RA Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C.,
RA Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M.,
RA Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M.,
RA Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D.,
RA Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L.,
RA Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E.,
RA Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H.,
RA Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y.,
RA Lowry S., Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J.,
RA Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D.,
RA Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., Rash S.,
RA Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A.,
RA Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M.,
RA Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H.,
RA Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A.,
RA Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J.,
RA DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J.,
RA Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M.,
RA Myers R.M., Rubin E.M., Pennacchio L.A.;
RT "The sequence and analysis of duplication-rich human chromosome 16.";
RL Nature 432:988-994(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=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 [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-125; SER-142; SER-143;
RP SER-159; SER-160; SER-196; SER-199; SER-223; SER-227; SER-289 AND SER-291,
RP AND 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 [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-84; SER-87; SER-196; SER-227
RP AND SER-370, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=16964243; DOI=10.1038/nbt1240;
RA Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
RT "A probability-based approach for high-throughput protein phosphorylation
RT analysis and site localization.";
RL Nat. Biotechnol. 24:1285-1292(2006).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=T-cell;
RX PubMed=19367720; DOI=10.1021/pr800500r;
RA Carrascal M., Ovelleiro D., Casas V., Gay M., Abian J.;
RT "Phosphorylation analysis of primary human T lymphocytes using sequential
RT IMAC and titanium oxide enrichment.";
RL J. Proteome Res. 7:5167-5176(2008).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-98; SER-100; SER-159;
RP SER-160; SER-223; SER-227; SER-330; SER-332; SER-333; SER-357; THR-358;
RP SER-359; SER-363 AND SER-372, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [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 [10]
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 [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-27; SER-125; SER-196; SER-223
RP AND SER-227, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP 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-125; SER-159; SER-160;
RP SER-196; SER-199; SER-227; SER-289; SER-291; SER-330; SER-332; SER-333;
RP SER-550; SER-551 AND SER-555, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [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-125; SER-142; SER-143;
RP SER-159; SER-160; SER-196; SER-199; SER-223; SER-227; SER-289; SER-291;
RP SER-330; SER-332; SER-333; SER-357; THR-358; SER-359; SER-363 AND SER-370,
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-27; SER-125; SER-159;
RP SER-160; SER-196; SER-199; SER-223; SER-227; SER-289; SER-291; SER-330;
RP SER-332; SER-333; SER-370; THR-471 AND SER-530, AND IDENTIFICATION BY MASS
RP 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-555, AND IDENTIFICATION BY
RP 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).
CC -!- FUNCTION: May play a role in chromatin function and histone metabolism
CC via its interaction with HIRA and histones.
CC {ECO:0000269|PubMed:9710638}.
CC -!- SUBUNIT: Interacts with HIRA. Weak interaction with histones H2B and
CC H3. Interacts with CK2. {ECO:0000269|PubMed:17391060,
CC ECO:0000269|PubMed:9710638}.
CC -!- INTERACTION:
CC Q9BW71; P42858: HTT; NbExp=6; IntAct=EBI-723624, EBI-466029;
CC Q9BW71; Q9HBY8-2: SGK2; NbExp=5; IntAct=EBI-723624, EBI-12143041;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:17391060}.
CC Note=Nuclear throughout the cell cycle and is excluded from condensed
CC chromatin during mitosis.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q9BW71-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9BW71-2; Sequence=VSP_003877;
CC Name=3;
CC IsoId=Q9BW71-3; Sequence=VSP_046024, VSP_046025;
CC -!- TISSUE SPECIFICITY: Widely expressed. Isoform 1 is predominant in
CC skeletal muscle. Isoform 2 is predominant in liver and heart.
CC {ECO:0000269|PubMed:9710638}.
CC -!- PTM: Phosphorylated by CK2. {ECO:0000269|PubMed:17391060}.
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DR EMBL; AJ223349; CAA11273.1; -; mRNA.
DR EMBL; AJ223350; CAA11274.1; -; mRNA.
DR EMBL; AJ223351; CAA11275.2; -; mRNA.
DR EMBL; BX393533; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AC093512; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC000588; AAH00588.1; -; mRNA.
DR CCDS; CCDS10664.1; -. [Q9BW71-1]
DR CCDS; CCDS58449.1; -. [Q9BW71-3]
DR RefSeq; NP_001184252.1; NM_001197323.1. [Q9BW71-3]
DR RefSeq; NP_003600.2; NM_003609.4. [Q9BW71-1]
DR AlphaFoldDB; Q9BW71; -.
DR SMR; Q9BW71; -.
DR BioGRID; 114053; 60.
DR IntAct; Q9BW71; 27.
DR MINT; Q9BW71; -.
DR STRING; 9606.ENSP00000279392; -.
DR iPTMnet; Q9BW71; -.
DR MetOSite; Q9BW71; -.
DR PhosphoSitePlus; Q9BW71; -.
DR BioMuta; HIRIP3; -.
DR DMDM; 116242511; -.
DR EPD; Q9BW71; -.
DR jPOST; Q9BW71; -.
DR MassIVE; Q9BW71; -.
DR MaxQB; Q9BW71; -.
DR PaxDb; Q9BW71; -.
DR PeptideAtlas; Q9BW71; -.
DR PRIDE; Q9BW71; -.
DR ProteomicsDB; 42429; -.
DR ProteomicsDB; 79258; -. [Q9BW71-1]
DR ProteomicsDB; 79259; -. [Q9BW71-2]
DR Antibodypedia; 26925; 195 antibodies from 28 providers.
DR DNASU; 8479; -.
DR Ensembl; ENST00000279392.8; ENSP00000279392.3; ENSG00000149929.16. [Q9BW71-1]
DR Ensembl; ENST00000564026.1; ENSP00000456824.1; ENSG00000149929.16. [Q9BW71-3]
DR GeneID; 8479; -.
DR KEGG; hsa:8479; -.
DR MANE-Select; ENST00000279392.8; ENSP00000279392.3; NM_003609.5; NP_003600.2.
DR UCSC; uc002dve.4; human. [Q9BW71-1]
DR CTD; 8479; -.
DR GeneCards; HIRIP3; -.
DR HGNC; HGNC:4917; HIRIP3.
DR HPA; ENSG00000149929; Low tissue specificity.
DR MIM; 603365; gene.
DR neXtProt; NX_Q9BW71; -.
DR OpenTargets; ENSG00000149929; -.
DR PharmGKB; PA29294; -.
DR VEuPathDB; HostDB:ENSG00000149929; -.
DR eggNOG; ENOG502S0AG; Eukaryota.
DR GeneTree; ENSGT00390000014062; -.
DR HOGENOM; CLU_038583_0_0_1; -.
DR InParanoid; Q9BW71; -.
DR OMA; QAPPDWS; -.
DR OrthoDB; 879744at2759; -.
DR PhylomeDB; Q9BW71; -.
DR TreeFam; TF331753; -.
DR PathwayCommons; Q9BW71; -.
DR SignaLink; Q9BW71; -.
DR BioGRID-ORCS; 8479; 9 hits in 1086 CRISPR screens.
DR ChiTaRS; HIRIP3; human.
DR GeneWiki; HIRIP3; -.
DR GenomeRNAi; 8479; -.
DR Pharos; Q9BW71; Tdark.
DR PRO; PR:Q9BW71; -.
DR Proteomes; UP000005640; Chromosome 16.
DR RNAct; Q9BW71; protein.
DR Bgee; ENSG00000149929; Expressed in oocyte and 199 other tissues.
DR Genevisible; Q9BW71; HS.
DR GO; GO:0005730; C:nucleolus; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0006325; P:chromatin organization; TAS:ProtInc.
DR InterPro; IPR037647; HIRIP3.
DR InterPro; IPR019098; Histone_chaperone_domain_CHZ.
DR PANTHER; PTHR15410; PTHR15410; 1.
DR Pfam; PF09649; CHZ; 1.
DR SMART; SM01082; CHZ; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Nucleus; Phosphoprotein; Reference proteome.
FT CHAIN 1..556
FT /note="HIRA-interacting protein 3"
FT /id="PRO_0000083989"
FT REGION 64..426
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 502..556
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 64..99
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 127..170
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 188..242
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 253..348
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 525..540
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 27
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 84
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:16964243"
FT MOD_RES 87
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16964243"
FT MOD_RES 98
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 100
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 125
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
FT MOD_RES 142
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:21406692"
FT MOD_RES 143
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:21406692"
FT MOD_RES 159
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
FT MOD_RES 160
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
FT MOD_RES 196
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16964243,
FT ECO:0007744|PubMed:17081983, ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 199
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 223
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
FT MOD_RES 227
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16964243,
FT ECO:0007744|PubMed:17081983, ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
FT MOD_RES 289
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 291
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 330
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 332
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 333
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 357
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:21406692"
FT MOD_RES 358
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:21406692"
FT MOD_RES 359
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:21406692"
FT MOD_RES 363
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:21406692"
FT MOD_RES 370
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16964243,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
FT MOD_RES 372
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 471
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 530
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 550
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 551
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 555
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:24275569"
FT VAR_SEQ 101..413
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:9710638"
FT /id="VSP_003877"
FT VAR_SEQ 101..175
FT /note="ESGSEASSPDYFGPPAKNGVAAEVSPAKEENPRRASKAVEESSDEERQRDLP
FT AQRGEESSEEEEKGYKGKTRKKP -> GWLRSPWRGPPGCDEAEALHSGLWCPSKLQEA
FT VGLLLLTQGAPEYPPGRTGSARHEGYPFPREVSGPEGAEGGGS (in isoform 3)"
FT /evidence="ECO:0000303|Ref.3"
FT /id="VSP_046024"
FT VAR_SEQ 176..556
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|Ref.3"
FT /id="VSP_046025"
FT VARIANT 496
FT /note="A -> V (in dbSNP:rs35431046)"
FT /id="VAR_051033"
FT VARIANT 521
FT /note="G -> W (in dbSNP:rs11643314)"
FT /id="VAR_028115"
FT CONFLICT 58
FT /note="L -> P (in Ref. 1; CAA11273/CAA11274/CAA11275 and
FT 2)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 556 AA; 61957 MW; ACABE2E0032B8C13 CRC64;
MAREKEMQEF TRSFFRGRPD LSTLTHSIVR RRYLAHSGRS HLEPEEKQAL KRLVEEELLK
MQVDEAASRE DKLDLTKKGK RPPTPCSDPE RKRFRFNSES ESGSEASSPD YFGPPAKNGV
AAEVSPAKEE NPRRASKAVE ESSDEERQRD LPAQRGEESS EEEEKGYKGK TRKKPVVKKQ
APGKASVSRK QAREESEESE AEPVQRTAKK VEGNKGTKSL KESEQESEEE ILAQKKEQRE
EEVEEEEKEE DEEKGDWKPR TRSNGRRKSA REERSCKQKS QAKRLLGDSD SEEEQKEAAS
SGDDSGRDRE PPVQRKSEDR TQLKGGKRLS GSSEDEEDSG KGEPTAKGSR KMARLGSTSG
EESDLEREVS DSEAGGGPQG ERKNRSSKKS SRKGRTRSSS SSSDGSPEAK GGKAGSGRRG
EDHPAVMRLK RYIRACGAHR NYKKLLGSCC SHKERLSILR AELEALGMKG TPSLGKCRAL
KEQREEAAEV ASLDVANIIS GSGRPRRRTA WNPLGEAAPP GELYRRTLDS DEERPRPAPP
DWSHMRGIIS SDGESN
