ZN830_HUMAN
ID ZN830_HUMAN Reviewed; 372 AA.
AC Q96NB3; Q96F60; Q96GZ5; Q9BU38;
DT 06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 30-NOV-2010, sequence version 2.
DT 03-AUG-2022, entry version 160.
DE RecName: Full=Zinc finger protein 830 {ECO:0000312|HGNC:HGNC:28291};
DE AltName: Full=Coiled-coil domain-containing protein 16 {ECO:0000305};
GN Name=ZNF830 {ECO:0000312|HGNC:HGNC:28291};
GN Synonyms=CCDC16 {ECO:0000312|HGNC:HGNC:28291};
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], AND VARIANT GLN-99.
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [2]
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 7-372, AND VARIANTS GLN-99 AND
RP THR-154.
RC TISSUE=Colon, and 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 [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-351, 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 [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-351 AND SER-362, AND
RP IDENTIFICATION BY 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 [6]
RP IDENTIFICATION AS PART OF THE XAB2 COMPLEX, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RX PubMed=17981804; DOI=10.1074/jbc.m706647200;
RA Kuraoka I., Ito S., Wada T., Hayashida M., Lee L., Saijo M., Nakatsu Y.,
RA Matsumoto M., Matsunaga T., Handa H., Qin J., Nakatani Y., Tanaka K.;
RT "Isolation of XAB2 complex involved in pre-mRNA splicing, transcription,
RT and transcription-coupled repair.";
RL J. Biol. Chem. 283:940-950(2008).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-351, AND IDENTIFICATION BY
RP 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 [8]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [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 [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-351, 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 [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-351, AND IDENTIFICATION BY
RP 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-351, 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 [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-225 AND SER-351, AND
RP 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 [13]
RP 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 [14]
RP IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION IN THE IB COMPLEX,
RP SUBUNIT, SUBCELLULAR LOCATION, AND FUNCTION.
RX PubMed=25599396; DOI=10.1038/nsmb.2951;
RA De I., Bessonov S., Hofele R., dos Santos K., Will C.L., Urlaub H.,
RA Luhrmann R., Pena V.;
RT "The RNA helicase Aquarius exhibits structural adaptations mediating its
RT recruitment to spliceosomes.";
RL Nat. Struct. Mol. Biol. 22:138-144(2015).
RN [15]
RP VARIANT [LARGE SCALE ANALYSIS] GLN-99, AND IDENTIFICATION BY MASS
RP 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).
CC -!- FUNCTION: May play a role in pre-mRNA splicing as component of the
CC spliceosome (PubMed:25599396). Acts as an important regulator of the
CC cell cycle that participates in the maintenance of genome integrity.
CC During cell cycle progression in embryonic fibroblast, prevents
CC replication fork collapse, double-strand break formation and cell cycle
CC checkpoint activation. Controls mitotic cell cycle progression and cell
CC survival in rapidly proliferating intestinal epithelium and embryonic
CC stem cells. During the embryo preimplantation, controls different
CC aspects of M phase. During early oocyte growth, plays a role in oocyte
CC survival by preventing chromosomal breaks formation, activation of TP63
CC and reduction of transcription (By similarity).
CC {ECO:0000250|UniProtKB:Q8R1N0, ECO:0000305|PubMed:25599396}.
CC -!- SUBUNIT: Component of the XAB2 complex, a multimeric protein complex
CC composed of XAB2, PRPF19, AQR, ZNF830, ISY1, and PPIE; this complex
CC binds preferentially to RNA. Interacts with XAB2 (PubMed:17981804).
CC Identified in a pentameric intron-binding (IB) complex composed of AQR,
CC XAB2, ISY1, ZNF830 and PPIE that is incorporated into the spliceosome
CC as a preassembled complex (PubMed:25599396). The IB complex does not
CC contain PRPF19 (PubMed:25599396). {ECO:0000269|PubMed:17981804,
CC ECO:0000269|PubMed:25599396}.
CC -!- INTERACTION:
CC Q96NB3; O60306: AQR; NbExp=11; IntAct=EBI-3920997, EBI-2512328;
CC Q96NB3; Q13123: IK; NbExp=2; IntAct=EBI-3920997, EBI-713456;
CC Q96NB3; Q15365: PCBP1; NbExp=2; IntAct=EBI-3920997, EBI-946095;
CC Q96NB3; Q13356: PPIL2; NbExp=2; IntAct=EBI-3920997, EBI-7705988;
CC Q96NB3; Q6P2Q9: PRPF8; NbExp=2; IntAct=EBI-3920997, EBI-538479;
CC Q96NB3; Q86VW0: SESTD1; NbExp=3; IntAct=EBI-3920997, EBI-6117072;
CC Q96NB3; Q13435: SF3B2; NbExp=2; IntAct=EBI-3920997, EBI-749111;
CC Q96NB3; Q13573: SNW1; NbExp=2; IntAct=EBI-3920997, EBI-632715;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:25599396}. Chromosome
CC {ECO:0000250|UniProtKB:Q8R1N0}. Nucleus speckle
CC {ECO:0000250|UniProtKB:Q8R1N0}. Note=Excluded from nucleolus.
CC {ECO:0000250|UniProtKB:Q8R1N0}.
CC -!- PTM: Phosphorylated in response to DNA damage by the cell cycle
CC checkpoint kinases ATR/ATM. {ECO:0000250|UniProtKB:Q8R1N0}.
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DR EMBL; AK055707; BAB70992.1; -; mRNA.
DR EMBL; AC022903; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC002913; AAH02913.2; -; mRNA.
DR EMBL; BC009044; AAH09044.1; -; mRNA.
DR EMBL; BC011584; AAH11584.2; -; mRNA.
DR CCDS; CCDS32618.1; -.
DR RefSeq; NP_443089.3; NM_052857.3.
DR AlphaFoldDB; Q96NB3; -.
DR SMR; Q96NB3; -.
DR BioGRID; 124850; 65.
DR DIP; DIP-61544N; -.
DR IntAct; Q96NB3; 23.
DR MINT; Q96NB3; -.
DR STRING; 9606.ENSP00000354518; -.
DR GlyGen; Q96NB3; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q96NB3; -.
DR PhosphoSitePlus; Q96NB3; -.
DR BioMuta; ZNF830; -.
DR DMDM; 313104066; -.
DR EPD; Q96NB3; -.
DR jPOST; Q96NB3; -.
DR MassIVE; Q96NB3; -.
DR MaxQB; Q96NB3; -.
DR PaxDb; Q96NB3; -.
DR PeptideAtlas; Q96NB3; -.
DR PRIDE; Q96NB3; -.
DR ProteomicsDB; 77499; -.
DR Antibodypedia; 15518; 111 antibodies from 23 providers.
DR DNASU; 91603; -.
DR Ensembl; ENST00000361952.5; ENSP00000354518.3; ENSG00000198783.6.
DR GeneID; 91603; -.
DR KEGG; hsa:91603; -.
DR MANE-Select; ENST00000361952.5; ENSP00000354518.3; NM_052857.4; NP_443089.3.
DR UCSC; uc002hih.5; human.
DR CTD; 91603; -.
DR DisGeNET; 91603; -.
DR GeneCards; ZNF830; -.
DR HGNC; HGNC:28291; ZNF830.
DR HPA; ENSG00000198783; Low tissue specificity.
DR neXtProt; NX_Q96NB3; -.
DR OpenTargets; ENSG00000198783; -.
DR PharmGKB; PA162410767; -.
DR VEuPathDB; HostDB:ENSG00000198783; -.
DR eggNOG; KOG3032; Eukaryota.
DR GeneTree; ENSGT00390000012151; -.
DR HOGENOM; CLU_058140_1_0_1; -.
DR InParanoid; Q96NB3; -.
DR OMA; EQIECYK; -.
DR OrthoDB; 1458826at2759; -.
DR PhylomeDB; Q96NB3; -.
DR TreeFam; TF315895; -.
DR PathwayCommons; Q96NB3; -.
DR Reactome; R-HSA-6781823; Formation of TC-NER Pre-Incision Complex.
DR Reactome; R-HSA-6781827; Transcription-Coupled Nucleotide Excision Repair (TC-NER).
DR Reactome; R-HSA-6782135; Dual incision in TC-NER.
DR Reactome; R-HSA-6782210; Gap-filling DNA repair synthesis and ligation in TC-NER.
DR SignaLink; Q96NB3; -.
DR BioGRID-ORCS; 91603; 658 hits in 1086 CRISPR screens.
DR GenomeRNAi; 91603; -.
DR Pharos; Q96NB3; Tdark.
DR PRO; PR:Q96NB3; -.
DR Proteomes; UP000005640; Chromosome 17.
DR RNAct; Q96NB3; protein.
DR Bgee; ENSG00000198783; Expressed in tendon of biceps brachii and 194 other tissues.
DR ExpressionAtlas; Q96NB3; baseline and differential.
DR Genevisible; Q96NB3; HS.
DR GO; GO:0005694; C:chromosome; IEA:UniProtKB-SubCell.
DR GO; GO:0016607; C:nuclear speck; IEA:UniProtKB-SubCell.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005681; C:spliceosomal complex; IEA:UniProtKB-KW.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0001832; P:blastocyst growth; IEA:Ensembl.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0051276; P:chromosome organization; IEA:Ensembl.
DR GO; GO:0060729; P:intestinal epithelial structure maintenance; IEA:Ensembl.
DR GO; GO:0044773; P:mitotic DNA damage checkpoint signaling; IBA:GO_Central.
DR GO; GO:0033314; P:mitotic DNA replication checkpoint signaling; ISS:UniProtKB.
DR GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR GO; GO:0043066; P:negative regulation of apoptotic process; ISS:UniProtKB.
DR GO; GO:0033260; P:nuclear DNA replication; IBA:GO_Central.
DR GO; GO:0001541; P:ovarian follicle development; ISS:UniProtKB.
DR GO; GO:0001546; P:preantral ovarian follicle growth; ISS:UniProtKB.
DR GO; GO:0048478; P:replication fork protection; ISS:UniProtKB.
DR GO; GO:0008380; P:RNA splicing; IEA:UniProtKB-KW.
DR InterPro; IPR003604; Matrin/U1-like-C_Znf_C2H2.
DR InterPro; IPR040050; ZNF830-like.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR PANTHER; PTHR13278; PTHR13278; 1.
DR SMART; SM00451; ZnF_U1; 1.
DR SUPFAM; SSF57667; SSF57667; 1.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 1.
PE 1: Evidence at protein level;
KW Acetylation; Cell cycle; Cell division; Chromosome; Coiled coil;
KW Developmental protein; Metal-binding; Mitosis; mRNA processing;
KW mRNA splicing; Nucleus; Phosphoprotein; Reference proteome; Spliceosome;
KW Zinc; Zinc-finger.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:19413330"
FT CHAIN 2..372
FT /note="Zinc finger protein 830"
FT /id="PRO_0000076193"
FT ZN_FING 53..75
FT /note="C2H2-type"
FT REGION 78..126
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 143..225
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 312..349
FT /evidence="ECO:0000255"
FT COMPBIAS 102..116
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 157..172
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 188..210
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0007744|PubMed:19413330"
FT MOD_RES 225
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 351
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:17525332, 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 362
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17525332"
FT VARIANT 16
FT /note="I -> V (in dbSNP:rs8073825)"
FT /id="VAR_030940"
FT VARIANT 93
FT /note="S -> P (in dbSNP:rs8078059)"
FT /id="VAR_030941"
FT VARIANT 99
FT /note="H -> Q (in dbSNP:rs931196)"
FT /evidence="ECO:0000269|PubMed:14702039,
FT ECO:0000269|PubMed:15489334, ECO:0007744|PubMed:21269460"
FT /id="VAR_024059"
FT VARIANT 135
FT /note="F -> L (in dbSNP:rs8078217)"
FT /id="VAR_030942"
FT VARIANT 154
FT /note="S -> T (in dbSNP:rs3744355)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_024060"
SQ SEQUENCE 372 AA; 41999 MW; A06403B117672C8C CRC64;
MASSASARTP AGKRVINQEE LRRLMKEKQR LSTSRKRIES PFAKYNRLGQ LSCALCNTPV
KSELLWQTHV LGKQHREKVA ELKGAKEASQ GSSASSAPHS VKRKAPDADD QDVKRAKATL
VPQVQPSTSA WTTNFDKIGK EFIRATPSKP SGLSLLPDYE DEEEEEEEEE GDGERKRGDA
SKPLSDAQGK EHSVSSSREV TSSVLPNDFF STNPPKAPII PHSGSIEKAE IHEKVVERRE
NTAEALPEGF FDDPEVDARV RKVDAPKDQM DKEWDEFQKA MRQVNTISEA IVAEEDEEGR
LDRQIGEIDE QIECYRRVEK LRNRQDEIKN KLKEILTIKE LQKKEEENAD SDDEGELQDL
LSQDWRVKGA LL
