PRR12_HUMAN
ID PRR12_HUMAN Reviewed; 2036 AA.
AC Q9ULL5; E9PB06; Q8N4J6;
DT 27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 13-FEB-2019, sequence version 3.
DT 03-AUG-2022, entry version 147.
DE RecName: Full=Proline-rich protein 12;
GN Name=PRR12 {ECO:0000312|HGNC:HGNC:29217}; Synonyms=KIAA1205;
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=15057824; DOI=10.1038/nature02399;
RA Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E.,
RA Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A.,
RA Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S.,
RA Carrano A.V., Caoile C., Chan Y.M., Christensen M., Cleland C.A.,
RA Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J.,
RA Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M.,
RA Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W.,
RA Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V.,
RA Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D.,
RA McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I.,
RA Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L.,
RA Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A.,
RA She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M.,
RA Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J.,
RA Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E.,
RA Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M.,
RA Rubin E.M., Lucas S.M.;
RT "The DNA sequence and biology of human chromosome 19.";
RL Nature 428:529-535(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 838-2036 (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=10574462; DOI=10.1093/dnares/6.5.337;
RA Nagase T., Ishikawa K., Kikuno R., Hirosawa M., Nomura N., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XV. The
RT complete sequences of 100 new cDNA clones from brain which code for large
RT proteins in vitro.";
RL DNA Res. 6:337-345(1999).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1365-2036 (ISOFORM 2).
RC TISSUE=Pancreas;
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 [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1308; THR-1561 AND SER-1568,
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 [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-865 AND SER-1925, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18220336; DOI=10.1021/pr0705441;
RA Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III;
RT "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient
RT phosphoproteomic analysis.";
RL J. Proteome Res. 7:1346-1351(2008).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1077; THR-1304; SER-1308;
RP SER-1381; SER-1382; THR-1561 AND SER-1568, AND IDENTIFICATION BY MASS
RP 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 [7]
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 [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1381 AND SER-1382, AND
RP IDENTIFICATION BY 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 [9]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-1223, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-651; THR-738; SER-865;
RP THR-1304; SER-1308; SER-1381; SER-1382; SER-1387 AND SER-1925, AND
RP IDENTIFICATION BY MASS 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 [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-651; SER-1381; SER-1382 AND
RP SER-1387, 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 [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-865; SER-1077; SER-1308;
RP SER-1381; SER-1382 AND THR-1705, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [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 [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1308, 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).
RN [14]
RP INVOLVEMENT IN NOC, AND VARIANT NOC 640-GLU--GLY-2036 DEL.
RX PubMed=29556724; DOI=10.1007/s00439-018-1877-0;
RA Leduc M.S., Mcguire M., Madan-Khetarpal S., Ortiz D., Hayflick S.,
RA Keller K., Eng C.M., Yang Y., Bi W.;
RT "De novo apparent loss-of-function mutations in PRR12 in three patients
RT with intellectual disability and iris abnormalities.";
RL Hum. Genet. 137:257-264(2018).
RN [15]
RP INVOLVEMENT IN NOC.
RX PubMed=33314030; DOI=10.1111/cge.13897;
RA Reis L.M., Costakos D., Wheeler P.G., Bardakjian T., Schneider A.,
RA Fung S.S.M., Semina E.V.;
RT "Dominant variants in PRR12 result in unilateral or bilateral complex
RT microphthalmia.";
RL Clin. Genet. 99:437-442(2021).
RN [16]
RP INVOLVEMENT IN NOC, AND VARIANTS NOC 264-GLN--GLY-2036 DEL;
RP 411-SER--GLY-2036 DEL; 507-TYR--GLY-2036 DEL; 640-GLU--GLY-2036 DEL;
RP 919-GLN--GLY-2036 DEL; TRP-1169; 1320-ARG--GLY-2036 DEL AND PRO-1970.
RX PubMed=33824499; DOI=10.1038/s41436-021-01129-6;
RA Chowdhury F., Wang L., Al-Raqad M., Amor D.J., Baxova A., Bendova S.,
RA Biamino E., Brusco A., Caluseriu O., Cox N.J., Froukh T., Gunay-Aygun M.,
RA Hancarova M., Haynes D., Heide S., Hoganson G., Kaname T., Keren B.,
RA Kosaki K., Kubota K., Lemons J.M., Magrina M.A., Mark P.R., McDonald M.T.,
RA Montgomery S., Morley G.M., Ohnishi H., Okamoto N., Rodriguez-Buritica D.,
RA Rump P., Sedlacek Z., Schatz K., Streff H., Uehara T., Walia J.S.,
RA Wheeler P.G., Wiesener A., Zweier C., Kawakami K., Wentzensen I.M.,
RA Lalani S.R., Siu V.M., Bi W., Balci T.B.;
RT "Haploinsufficiency of PRR12 causes a spectrum of neurodevelopmental, eye,
RT and multisystem abnormalities.";
RL Genet. Med. 23:1234-1245(2021).
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:E9PYL2}.
CC Postsynaptic density {ECO:0000250|UniProtKB:E9PYL2}. Synapse,
CC synaptosome {ECO:0000250|UniProtKB:E9PYL2}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9ULL5-3; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9ULL5-2; Sequence=VSP_019503;
CC -!- DISEASE: Neuroocular syndrome (NOC) [MIM:619539]: An autosomal dominant
CC syndrome characterized by developmental delay, impaired intellectual
CC development, and variable eye abnormalities including anophthalmia,
CC microphthalmia, and coloboma. Other common systemic features include
CC congenital heart and kidney defects, hypotonia, failure to thrive, and
CC microcephaly. {ECO:0000269|PubMed:29556724,
CC ECO:0000269|PubMed:33314030, ECO:0000269|PubMed:33824499}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA86519.1; Type=Miscellaneous discrepancy; Note=Aberrant splicing.; Evidence={ECO:0000305};
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DR EMBL; AB033031; BAA86519.1; ALT_SEQ; mRNA.
DR EMBL; AC010619; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC011495; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC034003; AAH34003.1; -; mRNA.
DR CCDS; CCDS46143.1; -. [Q9ULL5-3]
DR RefSeq; NP_065770.1; NM_020719.2. [Q9ULL5-3]
DR AlphaFoldDB; Q9ULL5; -.
DR BioGRID; 121549; 72.
DR IntAct; Q9ULL5; 54.
DR MINT; Q9ULL5; -.
DR STRING; 9606.ENSP00000394510; -.
DR GlyGen; Q9ULL5; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q9ULL5; -.
DR PhosphoSitePlus; Q9ULL5; -.
DR BioMuta; PRR12; -.
DR DMDM; 109892840; -.
DR EPD; Q9ULL5; -.
DR jPOST; Q9ULL5; -.
DR MassIVE; Q9ULL5; -.
DR MaxQB; Q9ULL5; -.
DR PaxDb; Q9ULL5; -.
DR PeptideAtlas; Q9ULL5; -.
DR PRIDE; Q9ULL5; -.
DR ProteomicsDB; 85071; -. [Q9ULL5-2]
DR ProteomicsDB; 85072; -. [Q9ULL5-3]
DR Antibodypedia; 32065; 14 antibodies from 8 providers.
DR Ensembl; ENST00000418929.7; ENSP00000394510.1; ENSG00000126464.15. [Q9ULL5-3]
DR GeneID; 57479; -.
DR KEGG; hsa:57479; -.
DR MANE-Select; ENST00000418929.7; ENSP00000394510.1; NM_020719.3; NP_065770.1.
DR UCSC; uc002poo.5; human. [Q9ULL5-3]
DR CTD; 57479; -.
DR DisGeNET; 57479; -.
DR GeneCards; PRR12; -.
DR HGNC; HGNC:29217; PRR12.
DR HPA; ENSG00000126464; Low tissue specificity.
DR MalaCards; PRR12; -.
DR MIM; 616633; gene.
DR MIM; 619539; phenotype.
DR neXtProt; NX_Q9ULL5; -.
DR OpenTargets; ENSG00000126464; -.
DR PharmGKB; PA134903328; -.
DR VEuPathDB; HostDB:ENSG00000126464; -.
DR eggNOG; KOG4805; Eukaryota.
DR GeneTree; ENSGT00440000037417; -.
DR HOGENOM; CLU_000708_0_0_1; -.
DR InParanoid; Q9ULL5; -.
DR OMA; FPEMEDM; -.
DR OrthoDB; 52008at2759; -.
DR PhylomeDB; Q9ULL5; -.
DR TreeFam; TF333141; -.
DR PathwayCommons; Q9ULL5; -.
DR SignaLink; Q9ULL5; -.
DR BioGRID-ORCS; 57479; 46 hits in 1081 CRISPR screens.
DR ChiTaRS; PRR12; human.
DR GenomeRNAi; 57479; -.
DR Pharos; Q9ULL5; Tdark.
DR PRO; PR:Q9ULL5; -.
DR Proteomes; UP000005640; Chromosome 19.
DR RNAct; Q9ULL5; protein.
DR Bgee; ENSG00000126464; Expressed in cardia of stomach and 149 other tissues.
DR ExpressionAtlas; Q9ULL5; baseline and differential.
DR Genevisible; Q9ULL5; HS.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0043005; C:neuron projection; IEA:UniProtKB-KW.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0014069; C:postsynaptic density; IEA:UniProtKB-SubCell.
DR InterPro; IPR025451; DUF4211.
DR Pfam; PF13926; DUF4211; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Disease variant;
KW Intellectual disability; Nucleus; Phosphoprotein; Reference proteome;
KW Synapse; Synaptosome.
FT CHAIN 1..2036
FT /note="Proline-rich protein 12"
FT /id="PRO_0000243945"
FT REGION 210..283
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 331..587
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 649..697
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 758..850
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 859..878
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 886..925
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 952..1068
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1120..1260
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1294..1347
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1376..1573
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1668..1840
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 222..242
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 244..268
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 476..493
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 523..539
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 790..805
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 830..849
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 974..991
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1035..1055
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1198..1219
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1302..1337
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1415..1441
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1451..1539
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1690..1705
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1719..1733
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1734..1764
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1785..1804
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 332
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:E9PYL2"
FT MOD_RES 340
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:E9PYL2"
FT MOD_RES 651
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT MOD_RES 738
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT MOD_RES 865
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18220336,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"
FT MOD_RES 1077
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 1135
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:E9PYL2"
FT MOD_RES 1223
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 1304
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231"
FT MOD_RES 1308
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT MOD_RES 1381
FT /note="Phosphoserine"
FT /evidence="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 1382
FT /note="Phosphoserine"
FT /evidence="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 1387
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692"
FT MOD_RES 1561
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:18669648"
FT MOD_RES 1568
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:18669648"
FT MOD_RES 1705
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 1925
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18220336,
FT ECO:0007744|PubMed:20068231"
FT VAR_SEQ 1875..1946
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_019503"
FT VARIANT 264..2036
FT /note="Missing (in NOC)"
FT /evidence="ECO:0000269|PubMed:33824499"
FT /id="VAR_086258"
FT VARIANT 411..2036
FT /note="Missing (in NOC)"
FT /evidence="ECO:0000269|PubMed:33824499"
FT /id="VAR_086259"
FT VARIANT 507..2036
FT /note="Missing (in NOC)"
FT /evidence="ECO:0000269|PubMed:33824499"
FT /id="VAR_086260"
FT VARIANT 640..2036
FT /note="Missing (in NOC; dbSNP:rs1555740650)"
FT /evidence="ECO:0000269|PubMed:29556724,
FT ECO:0000269|PubMed:33824499"
FT /id="VAR_086261"
FT VARIANT 919..2036
FT /note="Missing (in NOC)"
FT /evidence="ECO:0000269|PubMed:33824499"
FT /id="VAR_086262"
FT VARIANT 1169
FT /note="R -> W (in NOC)"
FT /evidence="ECO:0000269|PubMed:33824499"
FT /id="VAR_086263"
FT VARIANT 1320..2036
FT /note="Missing (in NOC)"
FT /evidence="ECO:0000269|PubMed:33824499"
FT /id="VAR_086264"
FT VARIANT 1970
FT /note="L -> P (in NOC)"
FT /evidence="ECO:0000269|PubMed:33824499"
FT /id="VAR_086265"
SQ SEQUENCE 2036 AA; 211044 MW; 11D30279770ECFF0 CRC64;
MDRNYPSAGF GDPLGAGAGW SYERSAKASL VYGSSRTSHP ETDILHRQAY AAPHPLQSYA
TNHHPAGLSG LFDTGLHHAG SAGPDASVMN LISALESRGP QPGPSASSLL SQFRSPSWQT
AMHTPGPTEL FISGALPGSS TFPSSSALSA YQHPASFGSR PFPVPSSLSL QDPPFSPPAN
GLLSPHDVLH LKPSQAPTVP SSLGFERLAG GGVLGPAGLG PAQTPPYRPG PPDPPPPPRH
LPTQFNLLAS SSAAAAAAEQ SSPQLYNFSG AAPGPPPPER ALPRQDTVIK HYQRPASAQP
PPPPPPAHAL QHYLSCGGSY PSMGHRANLA CSPLGGGEPS PGAGEPSKAG PSGATAGASG
RATGPEAAGG GGAGGGGGGY RPIIQSPGYK TGKGGYGAAA GGATRPPPPR STATPKCQSL
GGPAAAYATG KASGAGGAGG QAYSPGQPQG LLGPQAYGQG FGGGQAQDLS KAPSYSGGPP
QPPSGPPPPG LATCQSYSPD QLQGQLYGVQ GEPYPGPAAH SQGLPTASPS LSYSTGHSPA
LSGHGGGWGP SSLGGGGEAS PSHIIRPLQS PPATGRPPGV GSPGAPGKYL SSVLASAPFL
APPGAGSYAA GAGGYKGKGD GSELLAGPGG PPAERTEDEE FLIQHLLQAP SPPRTSGADG
LVGEDGAADA SKGLGGSGGA GGPPGTPYEL AKEDPQRYHL QSVIRTSASL DEGATAALEL
GLGRLKEKKK GPERGGETPE GLATSVVHYG AGAKELGAFL QKSPPPPPPT AQSTQPTPHG
LLLEAGGPDL PLVLPPPPPQ LLPSVLSHAP SPSPSASKVG VHLLEPATRD GAPQPPPPPP
PPPPPMPLQL EAHLRSHGLE PAAPSPRLRP EESLDPPGAM QELLGALEPL PPAPGDTGVG
PPNSEGKDPA GAYRSPSPQG TKAPRFVPLT SICFPDSLLQ DEERSFFPTM EEMFGGGAAD
DYGKAGPPED EGDPKAGAGP PPGPPAYDPY GPYCPGRASG AGPETPGLGL DPNKPPELPS
TVNAEPLGLI QSGPHQAAPP PPPPPPPPPA PASEPKGGLT SPIFCSTKPK KLLKTSSFHL
LRRRDPPFQT PKKLYAQEYE FEADEDKADV PADIRLNPRR LPDLVSSCRS RPALSPLGDI
DFCPPNPGPD GPRRRGRKPT KAKRDGPPRP RGRPRIRPLE VPTTAGPASA STPTDGAKKP
RGRGRGRGRK AEEAGGTRLE PLKPLKIKLS VPKAGEGLGT SSGDAISGTD HNSLDSSLTR
EKIEAKIKEV EEKQPEMKSG FMASFLDFLK SGKRHPPLYQ AGLTPPLSPP KSVPPSVPAR
GLQPQPPATP AVPHPPPSGA FGLGGALEAA ESEGLGLGCP SPCKRLDEEL KRNLETLPSF
SSDEEDSVAK NRDLQESISS AISALDDPPL AGPKDTSTPD GPPLAPAAAV PGPPPLPGLP
SANSNGTPEP PLLEEKPPPT PPPAPTPQPQ PPPPPPPPQP ALPSPPPLVA PTPSSPPPPP
LPPPPPPAMP SPPPPPPPAA APLAAPPEEP AAPSPEDPEL PDTRPLHLAK KQETAAVCGE
TDEEAGESGG EGIFRERDEF VIRAEDIPSL KLALQTGREP PPIWRVQKAL LQKFTPEIKD
GQRQFCATSN YLGYFGDAKN RYQRLYVKFL ENVNKKDYVR VCARKPWHRP PVPVRRSGQA
KNPVSAGGSS APPPKAPAPP PKPETPEKTT SEKPPEQTPE TAMPEPPAPE KPSLLRPVEK
EKEKEKVTRG ERPLRGERAT SGRQTRPERS LATGQPATSR LPKARPTKVK AEPPPKKRKK
WLKEAGGNAT AGGGPPGSSS DSESSPGAPS EDERAVPGRL LKTRAMREMY RSYVEMLVST
ALDPDMIQAL EDTHDELYLP PMRKIDGLLN EHKKKVLKRL SLSPALQDAL HTFPQLQVEQ
SGEGSPEEGA VRLRPAGEPY NRKTLSKLKR SVVRAQEFKV ELEKSGYYTL YHSLHHYKYH
TFLRCRDQTL AIEGGAEDLG QEEVVQQCMR NQPWLEQLFD SFSDLLAQAQ AHSRCG