CSTF3_HUMAN
ID CSTF3_HUMAN Reviewed; 717 AA.
AC Q12996; A8K471; D3DR04; E9PB40; Q32P22; Q96FQ8; Q96QD6; Q96QK4;
DT 19-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 186.
DE RecName: Full=Cleavage stimulation factor subunit 3;
DE AltName: Full=CF-1 77 kDa subunit;
DE AltName: Full=Cleavage stimulation factor 77 kDa subunit;
DE Short=CSTF 77 kDa subunit;
DE Short=CstF-77;
GN Name=CSTF3;
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] (ISOFORM 1).
RC TISSUE=Placenta;
RX PubMed=7984242; DOI=10.1038/372471a0;
RA Takagaki Y., Manley J.L.;
RT "A subunit of the polyadenylation factor CstF is the human homologue of the
RT Drosophila suppressor of forked protein.";
RL Nature 372:471-474(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Liver;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16554811; DOI=10.1038/nature04632;
RA Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K.,
RA Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F., Bloom T.,
RA Bruford E., Chang J.L., Cuomo C.A., Eichler E., FitzGerald M.G.,
RA Jaffe D.B., LaButti K., Nicol R., Park H.-S., Seaman C., Sougnez C.,
RA Yang X., Zimmer A.R., Zody M.C., Birren B.W., Nusbaum C., Fujiyama A.,
RA Hattori M., Rogers J., Lander E.S., Sakaki Y.;
RT "Human chromosome 11 DNA sequence and analysis including novel gene
RT identification.";
RL Nature 440:497-500(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 3).
RC TISSUE=Mammary carcinoma, Placenta, PNS, Prostate, 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 [6]
RP SUBUNIT.
RX PubMed=10669729; DOI=10.1128/mcb.20.5.1515-1525.2000;
RA Takagaki Y., Manley J.L.;
RT "Complex protein interactions within the human polyadenylation machinery
RT identify a novel component.";
RL Mol. Cell. Biol. 20:1515-1525(2000).
RN [7]
RP INTERACTION WITH FIP1L1.
RX PubMed=14749727; DOI=10.1038/sj.emboj.7600070;
RA Kaufmann I., Martin G., Friedlein A., Langen H., Keller W.;
RT "Human Fip1 is a subunit of CPSF that binds to U-rich RNA elements and
RT stimulates poly(A) polymerase.";
RL EMBO J. 23:616-626(2004).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-691, 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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-691, 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 [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-691, AND IDENTIFICATION BY
RP 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 [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-691, 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 [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-691, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=18318008; DOI=10.1002/pmic.200700884;
RA Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D.,
RA Zou H., Gu J.;
RT "Large-scale phosphoproteome analysis of human liver tissue by enrichment
RT and fractionation of phosphopeptides with strong anion exchange
RT chromatography.";
RL Proteomics 8:1346-1361(2008).
RN [13]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-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 [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-691, 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 [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-691, 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 [16]
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 [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-691, 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 [18]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
RN [19]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-691, AND IDENTIFICATION BY
RP 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 [20]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-691, 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: One of the multiple factors required for polyadenylation and
CC 3'-end cleavage of mammalian pre-mRNAs.
CC -!- SUBUNIT: Homodimer. The CSTF complex is composed of CSTF1 (50 kDa
CC subunit), CSTF2 (64 kDa subunit) and CSTF3 (77 kDa subunit). CSTF3
CC directly interacts with CSTF1 and CSTF2. Interacts with FIP1L1.
CC {ECO:0000269|PubMed:10669729, ECO:0000269|PubMed:14749727}.
CC -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q12996-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q12996-2; Sequence=VSP_042731, VSP_042732;
CC Name=3;
CC IsoId=Q12996-3; Sequence=VSP_045675, VSP_045676;
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DR EMBL; U15782; AAA61417.1; -; mRNA.
DR EMBL; AK290836; BAF83525.1; -; mRNA.
DR EMBL; AC131263; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL121926; CAC48252.1; -; Genomic_DNA.
DR EMBL; CH471064; EAW68200.1; -; Genomic_DNA.
DR EMBL; CH471064; EAW68201.1; -; Genomic_DNA.
DR EMBL; CH471064; EAW68202.1; -; Genomic_DNA.
DR EMBL; BC009792; AAH09792.1; -; mRNA.
DR EMBL; BC010533; AAH10533.1; -; mRNA.
DR EMBL; BC059948; AAH59948.1; -; mRNA.
DR EMBL; BC108319; AAI08320.1; -; mRNA.
DR EMBL; BM014288; -; NOT_ANNOTATED_CDS; mRNA.
DR CCDS; CCDS44563.1; -. [Q12996-2]
DR CCDS; CCDS44564.1; -. [Q12996-3]
DR CCDS; CCDS7883.1; -. [Q12996-1]
DR PIR; S50852; S50852.
DR RefSeq; NP_001028677.1; NM_001033505.1. [Q12996-2]
DR RefSeq; NP_001028678.1; NM_001033506.1. [Q12996-3]
DR RefSeq; NP_001317.1; NM_001326.2. [Q12996-1]
DR PDB; 6B3X; X-ray; 2.30 A; B=581-600.
DR PDB; 6URO; EM; 3.60 A; E/F=1-717.
DR PDBsum; 6B3X; -.
DR PDBsum; 6URO; -.
DR AlphaFoldDB; Q12996; -.
DR SMR; Q12996; -.
DR BioGRID; 107861; 124.
DR CORUM; Q12996; -.
DR DIP; DIP-48674N; -.
DR IntAct; Q12996; 31.
DR MINT; Q12996; -.
DR STRING; 9606.ENSP00000315791; -.
DR GlyGen; Q12996; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q12996; -.
DR PhosphoSitePlus; Q12996; -.
DR SwissPalm; Q12996; -.
DR BioMuta; CSTF3; -.
DR DMDM; 71153231; -.
DR EPD; Q12996; -.
DR jPOST; Q12996; -.
DR MassIVE; Q12996; -.
DR MaxQB; Q12996; -.
DR PaxDb; Q12996; -.
DR PeptideAtlas; Q12996; -.
DR PRIDE; Q12996; -.
DR ProteomicsDB; 19137; -.
DR ProteomicsDB; 59086; -. [Q12996-1]
DR ProteomicsDB; 59087; -. [Q12996-2]
DR Antibodypedia; 25689; 222 antibodies from 28 providers.
DR DNASU; 1479; -.
DR Ensembl; ENST00000323959.9; ENSP00000315791.4; ENSG00000176102.13. [Q12996-1]
DR Ensembl; ENST00000431742.2; ENSP00000393064.2; ENSG00000176102.13. [Q12996-3]
DR Ensembl; ENST00000438862.6; ENSP00000388711.2; ENSG00000176102.13. [Q12996-2]
DR GeneID; 1479; -.
DR KEGG; hsa:1479; -.
DR MANE-Select; ENST00000323959.9; ENSP00000315791.4; NM_001326.3; NP_001317.1.
DR UCSC; uc001muh.4; human. [Q12996-1]
DR CTD; 1479; -.
DR DisGeNET; 1479; -.
DR GeneCards; CSTF3; -.
DR HGNC; HGNC:2485; CSTF3.
DR HPA; ENSG00000176102; Low tissue specificity.
DR MIM; 600367; gene.
DR neXtProt; NX_Q12996; -.
DR OpenTargets; ENSG00000176102; -.
DR PharmGKB; PA26987; -.
DR VEuPathDB; HostDB:ENSG00000176102; -.
DR eggNOG; KOG1914; Eukaryota.
DR GeneTree; ENSGT00390000006758; -.
DR HOGENOM; CLU_007630_3_1_1; -.
DR InParanoid; Q12996; -.
DR OMA; LCYIDYL; -.
DR OrthoDB; 331411at2759; -.
DR PhylomeDB; Q12996; -.
DR TreeFam; TF105867; -.
DR PathwayCommons; Q12996; -.
DR Reactome; R-HSA-72163; mRNA Splicing - Major Pathway.
DR Reactome; R-HSA-72187; mRNA 3'-end processing.
DR Reactome; R-HSA-73856; RNA Polymerase II Transcription Termination.
DR Reactome; R-HSA-77595; Processing of Intronless Pre-mRNAs.
DR SignaLink; Q12996; -.
DR SIGNOR; Q12996; -.
DR BioGRID-ORCS; 1479; 766 hits in 1083 CRISPR screens.
DR ChiTaRS; CSTF3; human.
DR GeneWiki; CSTF3; -.
DR GenomeRNAi; 1479; -.
DR Pharos; Q12996; Tbio.
DR PRO; PR:Q12996; -.
DR Proteomes; UP000005640; Chromosome 11.
DR RNAct; Q12996; protein.
DR Bgee; ENSG00000176102; Expressed in adenohypophysis and 203 other tissues.
DR ExpressionAtlas; Q12996; baseline and differential.
DR Genevisible; Q12996; HS.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0003729; F:mRNA binding; IBA:GO_Central.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:0006379; P:mRNA cleavage; TAS:ProtInc.
DR GO; GO:0006378; P:mRNA polyadenylation; TAS:ProtInc.
DR GO; GO:0031123; P:RNA 3'-end processing; IBA:GO_Central.
DR InterPro; IPR003107; HAT.
DR InterPro; IPR045243; Rna14-like.
DR InterPro; IPR008847; Suf.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR PANTHER; PTHR19980; PTHR19980; 1.
DR Pfam; PF05843; Suf; 1.
DR SMART; SM00386; HAT; 10.
DR SUPFAM; SSF48452; SSF48452; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; mRNA processing; Nucleus;
KW Phosphoprotein; Reference proteome; Repeat.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:19413330,
FT ECO:0007744|PubMed:22223895"
FT CHAIN 2..717
FT /note="Cleavage stimulation factor subunit 3"
FT /id="PRO_0000205722"
FT REPEAT 45..77
FT /note="HAT 1"
FT REPEAT 79..110
FT /note="HAT 2"
FT REPEAT 117..152
FT /note="HAT 3"
FT REPEAT 163..196
FT /note="HAT 4"
FT REPEAT 221..261
FT /note="HAT 5"
FT REPEAT 271..303
FT /note="HAT 6"
FT REPEAT 319..352
FT /note="HAT 7"
FT REPEAT 354..387
FT /note="HAT 8"
FT REPEAT 458..494
FT /note="HAT 9"
FT REGION 684..705
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 685..702
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0007744|PubMed:19413330,
FT ECO:0007744|PubMed:22223895"
FT MOD_RES 691
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:18220336, ECO:0007744|PubMed:18318008,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:18691976,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT VAR_SEQ 44
FT /note="N -> V (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_045675"
FT VAR_SEQ 45..717
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_045676"
FT VAR_SEQ 76..103
FT /note="IKAKNYDKVEKLFQRCLMKVLHIDLWKC -> VTILFYFFLYQYCSIHCSDR
FT KQVRNIAN (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_042731"
FT VAR_SEQ 104..717
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_042732"
FT HELIX 586..588
FT /evidence="ECO:0007829|PDB:6B3X"
FT STRAND 589..591
FT /evidence="ECO:0007829|PDB:6B3X"
SQ SEQUENCE 717 AA; 82922 MW; 9ADE7AC86FBB3E93 CRC64;
MSGDGATEQA AEYVPEKVKK AEKKLEENPY DLDAWSILIR EAQNQPIDKA RKTYERLVAQ
FPSSGRFWKL YIEAEIKAKN YDKVEKLFQR CLMKVLHIDL WKCYLSYVRE TKGKLPSYKE
KMAQAYDFAL DKIGMEIMSY QIWVDYINFL KGVEAVGSYA ENQRITAVRR VYQRGCVNPM
INIEQLWRDY NKYEEGINIH LAKKMIEDRS RDYMNARRVA KEYETVMKGL DRNAPSVPPQ
NTPQEAQQVD MWKKYIQWEK SNPLRTEDQT LITKRVMFAY EQCLLVLGHH PDIWYEAAQY
LEQSSKLLAE KGDMNNAKLF SDEAANIYER AISTLLKKNM LLYFAYADYE ESRMKYEKVH
SIYNRLLAIE DIDPTLVYIQ YMKFARRAEG IKSGRMIFKK AREDTRTRHH VYVTAALMEY
YCSKDKSVAF KIFELGLKKY GDIPEYVLAY IDYLSHLNED NNTRVLFERV LTSGSLPPEK
SGEIWARFLA FESNIGDLAS ILKVEKRRFT AFKEEYEGKE TALLVDRYKF MDLYPCSASE
LKALGYKDVS RAKLAAIIPD PVVAPSIVPV LKDEVDRKPE YPKPDTQQMI PFQPRHLAPP
GLHPVPGGVF PVPPAAVVLM KLLPPPICFQ GPFVQVDELM EIFRRCKIPN TVEEAVRIIT
GGAPELAVEG NGPVESNAVL TKAVKRPNED SDEDEEKGAV VPPVHDIYRA RQQKRIR
