ZC3H4_HUMAN
ID ZC3H4_HUMAN Reviewed; 1303 AA.
AC Q9UPT8; Q9Y420;
DT 02-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 02-MAY-2006, sequence version 3.
DT 03-AUG-2022, entry version 171.
DE RecName: Full=Zinc finger CCCH domain-containing protein 4 {ECO:0000305};
GN Name=ZC3H4 {ECO:0000303|PubMed:33913806, ECO:0000312|HGNC:HGNC:17808};
GN Synonyms=C19orf7 {ECO:0000312|HGNC:HGNC:17808},
GN KIAA1064 {ECO:0000303|PubMed:10470851};
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 MRNA].
RC TISSUE=Brain;
RX PubMed=10470851; DOI=10.1093/dnares/6.3.197;
RA Kikuno R., Nagase T., Ishikawa K., Hirosawa M., Miyajima N., Tanaka A.,
RA Kotani H., Nomura N., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XIV. The
RT complete sequences of 100 new cDNA clones from brain which code for large
RT proteins in vitro.";
RL DNA Res. 6:197-205(1999).
RN [2]
RP SEQUENCE REVISION.
RX PubMed=12168954; DOI=10.1093/dnares/9.3.99;
RA Nakajima D., Okazaki N., Yamakawa H., Kikuno R., Ohara O., Nagase T.;
RT "Construction of expression-ready cDNA clones for KIAA genes: manual
RT curation of 330 KIAA cDNA clones.";
RL DNA Res. 9:99-106(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 993-1303.
RC TISSUE=Uterus;
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 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-1269 AND SER-1275, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE 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 [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-72, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic kidney;
RX PubMed=17525332; DOI=10.1126/science.1140321;
RA Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E.,
RA Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y.,
RA Gygi S.P., Elledge S.J.;
RT "ATM and ATR substrate analysis reveals extensive protein networks
RT responsive to DNA damage.";
RL Science 316:1160-1166(2007).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1275, AND IDENTIFICATION BY
RP 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 [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-75; SER-76; TYR-155; SER-807;
RP SER-904; SER-908; THR-1106; SER-1108; SER-1114 AND SER-1275, 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 [9]
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 [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-807; SER-808; SER-1104;
RP SER-1114 AND SER-1269, 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 [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-92; SER-94; SER-904 AND
RP SER-1114, AND 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 [12]
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 [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1275, 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 [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-904; SER-1104; SER-1110;
RP SER-1114; SER-1269 AND SER-1275, 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 [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-807; SER-907; SER-1114 AND
RP SER-1275, AND 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 [16]
RP FUNCTION, INTERACTION WITH WDR82, AND SUBCELLULAR LOCATION.
RX PubMed=33913806; DOI=10.7554/elife.67305;
RA Estell C., Davidson L., Steketee P.C., Monier A., West S.;
RT "ZC3H4 restricts non-coding transcription in human cells.";
RL Elife 10:0-0(2021).
RN [17]
RP FUNCTION.
RX PubMed=33767452; DOI=10.1038/s41594-021-00572-y;
RA Austenaa L.M.I., Piccolo V., Russo M., Prosperini E., Polletti S.,
RA Polizzese D., Ghisletti S., Barozzi I., Diaferia G.R., Natoli G.;
RT "A first exon termination checkpoint preferentially suppresses extragenic
RT transcription.";
RL Nat. Struct. Mol. Biol. 28:337-346(2021).
RN [18]
RP STRUCTURE BY NMR OF 417-501 IN COMPLEX WITH ZINC.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of the zinc-finger domain in KIAA1064 protein.";
RL Submitted (NOV-2005) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: RNA-binding protein that suppresses transcription of long
CC non-coding RNAs (lncRNAs) (PubMed:33913806, PubMed:33767452). LncRNAs
CC are defined as transcripts more than 200 nucleotides that are not
CC translated into protein (PubMed:33913806, PubMed:33767452). Together
CC with WDR82, part of a transcription termination checkpoint that
CC promotes transcription termination of lncRNAs and their subsequent
CC degradation by the exosome (PubMed:33913806, PubMed:33767452). The
CC transcription termination checkpoint is activated by the inefficiently
CC spliced first exon of lncRNAs (PubMed:33767452).
CC {ECO:0000269|PubMed:33767452, ECO:0000269|PubMed:33913806}.
CC -!- SUBUNIT: Interacts with WDR82. {ECO:0000269|PubMed:33913806}.
CC -!- SUBCELLULAR LOCATION: Chromosome {ECO:0000269|PubMed:33913806}.
CC Note=Recruited at sites of high RNA polymerase II occupancy.
CC {ECO:0000269|PubMed:33913806}.
CC -!- SIMILARITY: Belongs to the suppressor of sable family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA83016.2; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AB028987; BAA83016.2; ALT_INIT; mRNA.
DR EMBL; AL050155; CAB43296.1; -; mRNA.
DR CCDS; CCDS42582.1; -.
DR PIR; T08781; T08781.
DR RefSeq; NP_055983.1; NM_015168.1.
DR RefSeq; XP_006723176.1; XM_006723113.3.
DR PDB; 2CQE; NMR; -; A=417-501.
DR PDBsum; 2CQE; -.
DR AlphaFoldDB; Q9UPT8; -.
DR SMR; Q9UPT8; -.
DR BioGRID; 116818; 116.
DR IntAct; Q9UPT8; 26.
DR MINT; Q9UPT8; -.
DR STRING; 9606.ENSP00000253048; -.
DR GlyGen; Q9UPT8; 5 sites, 2 O-linked glycans (5 sites).
DR iPTMnet; Q9UPT8; -.
DR PhosphoSitePlus; Q9UPT8; -.
DR SwissPalm; Q9UPT8; -.
DR BioMuta; ZC3H4; -.
DR DMDM; 94707996; -.
DR EPD; Q9UPT8; -.
DR jPOST; Q9UPT8; -.
DR MassIVE; Q9UPT8; -.
DR MaxQB; Q9UPT8; -.
DR PaxDb; Q9UPT8; -.
DR PeptideAtlas; Q9UPT8; -.
DR PRIDE; Q9UPT8; -.
DR ProteomicsDB; 85442; -.
DR Antibodypedia; 45692; 87 antibodies from 24 providers.
DR DNASU; 23211; -.
DR Ensembl; ENST00000253048.10; ENSP00000253048.4; ENSG00000130749.10.
DR GeneID; 23211; -.
DR KEGG; hsa:23211; -.
DR MANE-Select; ENST00000253048.10; ENSP00000253048.4; NM_015168.2; NP_055983.1.
DR UCSC; uc002pga.5; human.
DR CTD; 23211; -.
DR DisGeNET; 23211; -.
DR GeneCards; ZC3H4; -.
DR HGNC; HGNC:17808; ZC3H4.
DR HPA; ENSG00000130749; Low tissue specificity.
DR MIM; 619498; gene.
DR neXtProt; NX_Q9UPT8; -.
DR OpenTargets; ENSG00000130749; -.
DR PharmGKB; PA162409534; -.
DR VEuPathDB; HostDB:ENSG00000130749; -.
DR eggNOG; KOG1040; Eukaryota.
DR GeneTree; ENSGT00940000160011; -.
DR InParanoid; Q9UPT8; -.
DR OMA; MFSHEEL; -.
DR OrthoDB; 145192at2759; -.
DR PhylomeDB; Q9UPT8; -.
DR TreeFam; TF321641; -.
DR PathwayCommons; Q9UPT8; -.
DR SignaLink; Q9UPT8; -.
DR BioGRID-ORCS; 23211; 82 hits in 1081 CRISPR screens.
DR ChiTaRS; ZC3H4; human.
DR EvolutionaryTrace; Q9UPT8; -.
DR GenomeRNAi; 23211; -.
DR Pharos; Q9UPT8; Tbio.
DR PRO; PR:Q9UPT8; -.
DR Proteomes; UP000005640; Chromosome 19.
DR RNAct; Q9UPT8; protein.
DR Bgee; ENSG00000130749; Expressed in sural nerve and 205 other tissues.
DR ExpressionAtlas; Q9UPT8; baseline and differential.
DR Genevisible; Q9UPT8; HS.
DR GO; GO:0005694; C:chromosome; IEA:UniProtKB-SubCell.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:1990841; F:promoter-specific chromatin binding; IDA:UniProtKB.
DR GO; GO:0003723; F:RNA binding; IDA:UniProtKB.
DR GO; GO:0006353; P:DNA-templated transcription, termination; IEA:UniProtKB-KW.
DR GO; GO:0110064; P:lncRNA catabolic process; IDA:UniProtKB.
DR GO; GO:0032785; P:negative regulation of DNA-templated transcription, elongation; IDA:UniProtKB.
DR GO; GO:0140744; P:negative regulation of lncRNA transcription; IDA:UniProtKB.
DR GO; GO:0071027; P:nuclear RNA surveillance; IDA:UniProtKB.
DR InterPro; IPR045124; Su(sable)-like.
DR InterPro; IPR041367; Znf-CCCH_4.
DR InterPro; IPR000571; Znf_CCCH.
DR InterPro; IPR036855; Znf_CCCH_sf.
DR PANTHER; PTHR13119; PTHR13119; 1.
DR Pfam; PF00642; zf-CCCH; 1.
DR Pfam; PF18044; zf-CCCH_4; 1.
DR SMART; SM00356; ZnF_C3H1; 3.
DR SUPFAM; SSF90229; SSF90229; 3.
DR PROSITE; PS50103; ZF_C3H1; 3.
PE 1: Evidence at protein level;
KW 3D-structure; Chromosome; Coiled coil; Metal-binding; Methylation;
KW Phosphoprotein; Reference proteome; Repeat; RNA-binding; Transcription;
KW Transcription regulation; Transcription termination; Zinc; Zinc-finger.
FT CHAIN 1..1303
FT /note="Zinc finger CCCH domain-containing protein 4"
FT /id="PRO_0000234068"
FT ZN_FING 390..417
FT /note="C3H1-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00723"
FT ZN_FING 419..446
FT /note="C3H1-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00723"
FT ZN_FING 447..470
FT /note="C3H1-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00723"
FT REGION 1..388
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 486..571
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 605..685
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 710..955
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 996..1288
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 95..128
FT /evidence="ECO:0000255"
FT COILED 767..800
FT /evidence="ECO:0000255"
FT COMPBIAS 1..37
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 40..54
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 55..73
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 74..100
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 101..128
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 143..159
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 198..216
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 217..239
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 279..303
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 304..325
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 326..342
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 372..388
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 486..502
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 505..562
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 605..628
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 632..648
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 656..685
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 713..738
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 774..802
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 808..837
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 901..920
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 922..936
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1024..1041
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1051..1065
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1235..1249
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1255..1272
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 72
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:17525332"
FT MOD_RES 75
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 76
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 92
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 94
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 155
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 601
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q6ZPZ3"
FT MOD_RES 807
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:24275569"
FT MOD_RES 808
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332"
FT MOD_RES 904
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"
FT MOD_RES 907
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 908
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 1104
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 1106
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 1108
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 1110
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 1114
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT MOD_RES 1118
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q6ZPZ3"
FT MOD_RES 1269
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16964243,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163"
FT MOD_RES 1275
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16964243,
FT ECO:0007744|PubMed:18220336, ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT VARIANT 287
FT /note="E -> K (in dbSNP:rs192824)"
FT /id="VAR_052964"
FT VARIANT 464
FT /note="M -> V (in dbSNP:rs402833)"
FT /id="VAR_052965"
FT VARIANT 1228
FT /note="A -> G (in dbSNP:rs309195)"
FT /id="VAR_052966"
FT TURN 426..430
FT /evidence="ECO:0007829|PDB:2CQE"
FT STRAND 440..447
FT /evidence="ECO:0007829|PDB:2CQE"
FT HELIX 450..453
FT /evidence="ECO:0007829|PDB:2CQE"
FT STRAND 464..466
FT /evidence="ECO:0007829|PDB:2CQE"
FT HELIX 472..487
FT /evidence="ECO:0007829|PDB:2CQE"
SQ SEQUENCE 1303 AA; 140257 MW; A6DAE368F543FF4D CRC64;
MEAAPGTPPP PPSESPPPPS PPPPSTPSPP PCSPDARPAT PHLLHHRLPL PDDREDGELE
EGELEDDGAE ETQDTSGGPE RSRKEKGEKH HSDSDEEKSH RRLKRKRKKE REKEKRRSKK
RRKSKHKRHA SSSDDFSDFS DDSDFSPSEK GHRKYREYSP PYAPSHQQYP PSHATPLPKK
AYSKMDSKSY GMYEDYENEQ YGEYEGDEEE DMGKEDYDDF TKELNQYRRA KEGSSRGRGS
RGRGRGYRGR GSRGGSRGRG MGRGSRGRGR GSMGGDHPED EEDFYEEEMD YGESEEPMGD
DDYDEYSKEL NQYRRSKDSR GRGLSRGRGR GSRGRGKGMG RGRGRGGSRG GMNKGGMNDD
EDFYDEDMGD GGGGSYRSRD HDKPHQQSDK KGKVICKYFV EGRCTWGDHC NFSHDIELPK
KRELCKFYIT GFCARAENCP YMHGDFPCKL YHTTGNCING DDCMFSHDPL TEETRELLDK
MLADDAEAGA EDEKEVEELK KQGINPLPKP PPGVGLLPTP PRPPGPQAPT SPNGRPMQGG
PPPPPPPPPP PPGPPQMPMP VHEPLSPQQL QQQDMYNKKI PSLFEIVVRP TGQLAEKLGV
RFPGPGGPPG PMGPGPNMGP PGPMGGPMHP DMHPDMHPDM HPDMHADMHA DMPMGPGMNP
GPPMGPGGPP MMPYGPGDSP HSGMMPPIPP AQNFYENFYQ QQEGMEMEPG LLGDAEDYGH
YEELPGEPGE HLFPEHPLEP DSFSEGGPPG RPKPGAGVPD FLPSAQRALY LRIQQKQQEE
EERARRLAES SKQDRENEEG DTGNWYSSDE DEGGSSVTSI LKTLRQQTSS RPPASVGELS
SSGLGDPRLQ KGHPTGSRLA DPRLSRDPRL TRHVEASGGS GPGDSGPSDP RLARALPTSK
PEGSLHSSPV GPSSSKGSGP PPTEEEEGER ALREKAVNIP LDPLPGHPLR DPRSQLQQFS
HIKKDVTLSK PSFARTVLWN PEDLIPLPIP KQDAVPPVPA ALQSMPTLDP RLHRAATAGP
PNARQRPGAS TDSSTQGANL PDFELLSRIL KTVNATGSSA APGSSDKPSD PRVRKAPTDP
RLQKPTDSTA SSRAAKPGPA EAPSPTASPS GDASPPATAP YDPRVLAAGG LGQGGGGGQS
SVLSGISLYD PRTPNAGGKA TEPAADTGAQ PKGAEGNGKS SASKAKEPPF VRKSALEQPE
TGKAGADGGT PTDRYNSYNR PRPKAAAAPA ATTATPPPEG APPQPGVHNL PVPTLFGTVK
QTPKTGSGSP FAGNSPAREG EQDAASLKDV FKGFDPTASP FCQ
