ZW10_HUMAN
ID ZW10_HUMAN Reviewed; 779 AA.
AC O43264; A1A528;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 184.
DE RecName: Full=Centromere/kinetochore protein zw10 homolog;
GN Name=ZW10;
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=Cervix carcinoma;
RX PubMed=9298984; DOI=10.1083/jcb.138.6.1289;
RA Starr D.A., Williams B.C., Li Z., Etemad-Moghadam B., Dawe R.K.,
RA Goldberg M.L.;
RT "Conservation of the centromere/kinetochore protein ZW10.";
RL J. Cell Biol. 138:1289-1301(1997).
RN [2]
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
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 PROTEIN SEQUENCE OF 2-14.
RC TISSUE=Platelet;
RX PubMed=12665801; DOI=10.1038/nbt810;
RA Gevaert K., Goethals M., Martens L., Van Damme J., Staes A., Thomas G.R.,
RA Vandekerckhove J.;
RT "Exploring proteomes and analyzing protein processing by mass spectrometric
RT identification of sorted N-terminal peptides.";
RL Nat. Biotechnol. 21:566-569(2003).
RN [5]
RP PROTEIN SEQUENCE OF 2-14 AND 161-170, CLEAVAGE OF INITIATOR METHIONINE,
RP ACETYLATION AT ALA-2, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Hepatoma;
RA Bienvenut W.V., Boldt K., von Kriegsheim A.F., Kolch W.;
RL Submitted (JUL-2007) to UniProtKB.
RN [6]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH KNTC1.
RX PubMed=11590237; DOI=10.1242/jcs.114.17.3103;
RA Scaeerou F., Starr D.A., Piano F., Papoulas O., Karess R.E., Goldberg M.L.;
RT "The ZW10 and Rough Deal checkpoint proteins function together in a large,
RT evolutionarily conserved complex targeted to the kinetochore.";
RL J. Cell Sci. 114:3103-3114(2001).
RN [7]
RP INTERACTION WITH ZWILCH AND ZW10.
RX PubMed=12686595; DOI=10.1091/mbc.e02-09-0624;
RA Williams B.C., Li Z., Liu S., Williams E.V., Leung G., Yen T.J.,
RA Goldberg M.L.;
RT "Zwilch, a new component of the ZW10/ROD complex required for kinetochore
RT functions.";
RL Mol. Biol. Cell 14:1379-1391(2003).
RN [8]
RP FUNCTION, SUBCELLULAR LOCATION, IDENTIFICATION BY MASS SPECTROMETRY,
RP IDENTIFICATION IN A COMPLEX WITH STX18; USE1L; SEC22B AND RINT1, AND
RP INTERACTION WITH RINT1.
RX PubMed=15029241; DOI=10.1038/sj.emboj.7600135;
RA Hirose H., Arasaki K., Dohmae N., Takio K., Hatsuzawa K., Nagahama M.,
RA Tani K., Yamamoto A., Tohyama M., Tagaya M.;
RT "Implication of ZW10 in membrane trafficking between the endoplasmic
RT reticulum and Golgi.";
RL EMBO J. 23:1267-1278(2004).
RN [9]
RP INTERACTION WITH BNIP1 THROUGH RINT1.
RX PubMed=15272311; DOI=10.1038/sj.emboj.7600333;
RA Nakajima K., Hirose H., Taniguchi M., Kurashina H., Arasaki K.,
RA Nagahama M., Tani K., Yamamoto A., Tagaya M.;
RT "Involvement of BNIP1 in apoptosis and endoplasmic reticulum membrane
RT fusion.";
RL EMBO J. 23:3216-3226(2004).
RN [10]
RP FUNCTION.
RX PubMed=15094189; DOI=10.1016/j.gene.2004.01.028;
RA Musio A., Mariani T., Montagna C., Zambroni D., Ascoli C., Ried T.,
RA Vezzoni P.;
RT "Recapitulation of the Roberts syndrome cellular phenotype by inhibition of
RT INCENP, ZWINT-1 and ZW10 genes.";
RL Gene 331:33-40(2004).
RN [11]
RP FUNCTION, INTERACTION WITH ZWINT, AND SUBCELLULAR LOCATION.
RX PubMed=15485811; DOI=10.1074/jbc.m407588200;
RA Wang H., Hu X., Ding X., Dou Z., Yang Z., Shaw A.W., Teng M.,
RA Cleveland D.W., Goldberg M.L., Niu L., Yao X.;
RT "Human Zwint-1 specifies localization of Zeste White 10 to kinetochores and
RT is essential for mitotic checkpoint signaling.";
RL J. Biol. Chem. 279:54590-54598(2004).
RN [12]
RP FUNCTION, IDENTIFICATION BY MASS SPECTROMETRY, INTERACTION WITH C19ORF25;
RP KNTC1; RINT1; ZWILCH AND ZWINT, AND SUBCELLULAR LOCATION.
RX PubMed=15824131; DOI=10.1083/jcb.200411118;
RA Kops G.J.P.L., Kim Y., Weaver B.A.A., Mao Y., McLeod I., Yates J.R. III,
RA Tagaya M., Cleveland D.W.;
RT "ZW10 links mitotic checkpoint signaling to the structural kinetochore.";
RL J. Cell Biol. 169:49-60(2005).
RN [13]
RP INTERACTION WITH ZWINT, AND SUBCELLULAR LOCATION.
RX PubMed=16732327; DOI=10.1038/sj.onc.1209687;
RA Lin Y.-T., Chen Y., Wu G., Lee W.-H.;
RT "Hec1 sequentially recruits Zwint-1 and ZW10 to kinetochores for faithful
RT chromosome segregation and spindle checkpoint control.";
RL Oncogene 25:6901-6914(2006).
RN [14]
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 [15]
RP SUBUNIT.
RX PubMed=19369418; DOI=10.1091/mbc.e08-11-1104;
RA Aoki T., Ichimura S., Itoh A., Kuramoto M., Shinkawa T., Isobe T.,
RA Tagaya M.;
RT "Identification of the neuroblastoma-amplified gene product as a component
RT of the syntaxin 18 complex implicated in Golgi-to-endoplasmic reticulum
RT retrograde transport.";
RL Mol. Biol. Cell 20:2639-2649(2009).
RN [16]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-777, 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 [17]
RP INTERACTION WITH NBAS, IDENTIFICATION IN THE RRZ COMPLEX, AND
RP IDENTIFICATION IN THE NRZ COMPLEX.
RX PubMed=20462495; DOI=10.1016/j.str.2010.02.014;
RA Civril F., Wehenkel A., Giorgi F.M., Santaguida S., Di Fonzo A.,
RA Grigorean G., Ciccarelli F.D., Musacchio A.;
RT "Structural analysis of the RZZ complex reveals common ancestry with
RT multisubunit vesicle tethering machinery.";
RL Structure 18:616-626(2010).
RN [18]
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 [19]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-3 AND SER-12, 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 [20]
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=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
RN [21]
RP INTERACTION WITH ZFYVE1 AND RAB18, AND SUBCELLULAR LOCATION.
RX PubMed=30970241; DOI=10.1016/j.celrep.2019.03.025;
RA Li D., Zhao Y.G., Li D., Zhao H., Huang J., Miao G., Feng D., Liu P.,
RA Li D., Zhang H.;
RT "The ER-Localized Protein DFCP1 Modulates ER-Lipid Droplet Contact
RT Formation.";
RL Cell Rep. 27:343-358(2019).
CC -!- FUNCTION: Essential component of the mitotic checkpoint, which prevents
CC cells from prematurely exiting mitosis. Required for the assembly of
CC the dynein-dynactin and MAD1-MAD2 complexes onto kinetochores. Its
CC function related to the spindle assembly machinery is proposed to
CC depend on its association in the mitotic RZZ complex (PubMed:11590237,
CC PubMed:15485811, PubMed:15824131). Involved in regulation of membrane
CC traffic between the Golgi and the endoplasmic reticulum (ER); the
CC function is proposed to depend on its association in the interphase NRZ
CC complex which is believed to play a role in SNARE assembly at the ER
CC (PubMed:15029241). {ECO:0000269|PubMed:11590237,
CC ECO:0000269|PubMed:15029241, ECO:0000269|PubMed:15094189,
CC ECO:0000269|PubMed:15485811, ECO:0000269|PubMed:15824131, ECO:0000305}.
CC -!- SUBUNIT: Interacts with NBAS and KNTC1/ROD; the interactions are
CC mutually exclusive and indicative for its association in two different
CC vesicle tethering complexes (PubMed:11590237, PubMed:15824131,
CC PubMed:20462495). Component of the RZZ complex composed of KNTC1/ROD,
CC ZW10 and ZWILCH (PubMed:12686595, PubMed:20462495). Component of the
CC NRZ complex composed of NBAS, ZW10 and RINT1/TIP20L; NRZ associates
CC with SNAREs STX18, USE1L, BNIP1/SEC20L and SEC22B (the assembly has
CC been described as syntaxin 18 complex). Interacts directly with
CC RINT1/TIP20L bound to BNIP1/SEC20L (PubMed:15029241, PubMed:15272311,
CC PubMed:20462495, PubMed:19369418). Interacts with C19orf25 and ZWINT
CC (PubMed:15485811, PubMed:15824131., PubMed:16732327). Interacts with
CC ZFYVE1 (PubMed:30970241). Interacts with RAB18 and this interaction is
CC enhanced in the presence of ZFYVE1 (PubMed:30970241).
CC {ECO:0000269|PubMed:12686595, ECO:0000269|PubMed:15029241,
CC ECO:0000269|PubMed:15272311, ECO:0000269|PubMed:15485811,
CC ECO:0000269|PubMed:15824131, ECO:0000269|PubMed:16732327,
CC ECO:0000269|PubMed:20462495, ECO:0000269|PubMed:30970241,
CC ECO:0000305|PubMed:20462495}.
CC -!- INTERACTION:
CC O43264; Q6NUQ1: RINT1; NbExp=16; IntAct=EBI-1001217, EBI-726876;
CC O43264; O95229: ZWINT; NbExp=6; IntAct=EBI-1001217, EBI-1001132;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:15029241}.
CC Endoplasmic reticulum membrane {ECO:0000269|PubMed:15029241};
CC Peripheral membrane protein {ECO:0000269|PubMed:15029241}. Chromosome,
CC centromere, kinetochore {ECO:0000269|PubMed:11590237,
CC ECO:0000269|PubMed:15485811, ECO:0000269|PubMed:15824131}. Cytoplasm,
CC cytoskeleton, spindle {ECO:0000269|PubMed:11590237}. Lipid droplet
CC {ECO:0000269|PubMed:30970241}. Note=Dynamic pattern of localization
CC during the cell cycle. In most cells at interphase, present diffusely
CC in the cytoplasm (PubMed:15029241). In prometaphase, associated with
CC the kinetochore. At metaphase, detected both at the kinetochores and,
CC most prominently, at the spindle, particularly at the spindle poles. In
CC very early anaphase, detected on segregating kinetochores. In late
CC anaphase and telophase, accumulates at the spindle midzone
CC (PubMed:11590237). {ECO:0000269|PubMed:11590237,
CC ECO:0000269|PubMed:15029241}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=O43264-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O43264-2; Sequence=VSP_056006;
CC -!- TISSUE SPECIFICITY: Widely expressed.
CC -!- DEVELOPMENTAL STAGE: No significant variation in expression during cell
CC cycle.
CC -!- MISCELLANEOUS: Overexpression as well as silencing of ZW10 disrupts the
CC morphology of the ER-Golgi intermediate compartment as well as the
CC Golgi apparatus and slows down ER-Golgi transport.
CC -!- SIMILARITY: Belongs to the ZW10 family. {ECO:0000305}.
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DR EMBL; U54996; AAB88237.1; -; mRNA.
DR EMBL; AP002436; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AP003170; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC128264; AAI28265.1; -; mRNA.
DR CCDS; CCDS8363.1; -. [O43264-1]
DR RefSeq; NP_004715.1; NM_004724.3. [O43264-1]
DR PDB; 7QPG; EM; 3.90 A; W/X=1-779.
DR PDBsum; 7QPG; -.
DR AlphaFoldDB; O43264; -.
DR BioGRID; 114620; 136.
DR ComplexPortal; CPX-6017; RZZ complex.
DR ComplexPortal; CPX-6201; NRZ tethering complex.
DR CORUM; O43264; -.
DR DIP; DIP-36471N; -.
DR IntAct; O43264; 48.
DR MINT; O43264; -.
DR STRING; 9606.ENSP00000200135; -.
DR GlyGen; O43264; 1 site, 2 O-linked glycans (1 site).
DR iPTMnet; O43264; -.
DR MetOSite; O43264; -.
DR PhosphoSitePlus; O43264; -.
DR BioMuta; ZW10; -.
DR EPD; O43264; -.
DR jPOST; O43264; -.
DR MassIVE; O43264; -.
DR MaxQB; O43264; -.
DR PaxDb; O43264; -.
DR PeptideAtlas; O43264; -.
DR PRIDE; O43264; -.
DR ProteomicsDB; 104; -.
DR ProteomicsDB; 48842; -. [O43264-1]
DR Antibodypedia; 3162; 171 antibodies from 25 providers.
DR DNASU; 9183; -.
DR Ensembl; ENST00000200135.8; ENSP00000200135.3; ENSG00000086827.9. [O43264-1]
DR Ensembl; ENST00000535142.5; ENSP00000440879.1; ENSG00000086827.9. [O43264-2]
DR GeneID; 9183; -.
DR KEGG; hsa:9183; -.
DR MANE-Select; ENST00000200135.8; ENSP00000200135.3; NM_004724.4; NP_004715.1.
DR UCSC; uc001poe.4; human. [O43264-1]
DR CTD; 9183; -.
DR DisGeNET; 9183; -.
DR GeneCards; ZW10; -.
DR HGNC; HGNC:13194; ZW10.
DR HPA; ENSG00000086827; Low tissue specificity.
DR MIM; 603954; gene.
DR neXtProt; NX_O43264; -.
DR OpenTargets; ENSG00000086827; -.
DR PharmGKB; PA37759; -.
DR VEuPathDB; HostDB:ENSG00000086827; -.
DR eggNOG; KOG2163; Eukaryota.
DR GeneTree; ENSGT00390000016427; -.
DR HOGENOM; CLU_012948_0_0_1; -.
DR InParanoid; O43264; -.
DR OMA; LMMILQA; -.
DR OrthoDB; 422807at2759; -.
DR PhylomeDB; O43264; -.
DR TreeFam; TF105966; -.
DR PathwayCommons; O43264; -.
DR Reactome; R-HSA-141444; Amplification of signal from unattached kinetochores via a MAD2 inhibitory signal.
DR Reactome; R-HSA-2467813; Separation of Sister Chromatids.
DR Reactome; R-HSA-2500257; Resolution of Sister Chromatid Cohesion.
DR Reactome; R-HSA-5663220; RHO GTPases Activate Formins.
DR Reactome; R-HSA-6811434; COPI-dependent Golgi-to-ER retrograde traffic.
DR Reactome; R-HSA-68877; Mitotic Prometaphase.
DR Reactome; R-HSA-9648025; EML4 and NUDC in mitotic spindle formation.
DR SignaLink; O43264; -.
DR SIGNOR; O43264; -.
DR BioGRID-ORCS; 9183; 239 hits in 1078 CRISPR screens.
DR ChiTaRS; ZW10; human.
DR GeneWiki; ZW10; -.
DR GenomeRNAi; 9183; -.
DR Pharos; O43264; Tbio.
DR PRO; PR:O43264; -.
DR Proteomes; UP000005640; Chromosome 11.
DR RNAct; O43264; protein.
DR Bgee; ENSG00000086827; Expressed in tibialis anterior and 150 other tissues.
DR ExpressionAtlas; O43264; baseline and differential.
DR Genevisible; O43264; HS.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0070939; C:Dsl1/NZR complex; IDA:UniProtKB.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:HGNC-UCL.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0000776; C:kinetochore; IDA:UniProtKB.
DR GO; GO:0005828; C:kinetochore microtubule; IDA:UniProtKB.
DR GO; GO:0005811; C:lipid droplet; IDA:UniProtKB.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:HGNC-UCL.
DR GO; GO:1990423; C:RZZ complex; IDA:UniProtKB.
DR GO; GO:0000922; C:spindle pole; IDA:UniProtKB.
DR GO; GO:0019237; F:centromeric DNA binding; TAS:ProtInc.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0006888; P:endoplasmic reticulum to Golgi vesicle-mediated transport; IMP:HGNC-UCL.
DR GO; GO:0000132; P:establishment of mitotic spindle orientation; IMP:UniProtKB.
DR GO; GO:0007030; P:Golgi organization; IMP:UniProtKB.
DR GO; GO:0051321; P:meiotic cell cycle; TAS:ProtInc.
DR GO; GO:0007080; P:mitotic metaphase plate congression; IMP:UniProtKB.
DR GO; GO:0000070; P:mitotic sister chromatid segregation; IDA:HGNC-UCL.
DR GO; GO:0007094; P:mitotic spindle assembly checkpoint signaling; IDA:UniProtKB.
DR GO; GO:0034501; P:protein localization to kinetochore; IMP:UniProtKB.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR GO; GO:0065003; P:protein-containing complex assembly; IDA:HGNC-UCL.
DR GO; GO:0007096; P:regulation of exit from mitosis; IDA:HGNC-UCL.
DR GO; GO:0006890; P:retrograde vesicle-mediated transport, Golgi to endoplasmic reticulum; IC:ComplexPortal.
DR Gene3D; 1.10.357.150; -; 1.
DR InterPro; IPR009361; RZZ-complex_Zw10.
DR InterPro; IPR046362; Zw10/DSL1_C_sf.
DR Pfam; PF06248; Zw10; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Cell cycle; Cell division;
KW Centromere; Chromosome; Coiled coil; Cytoplasm; Cytoskeleton;
KW Direct protein sequencing; Endoplasmic reticulum; ER-Golgi transport;
KW Kinetochore; Lipid droplet; Membrane; Mitosis; Phosphoprotein;
KW Protein transport; Reference proteome; Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:12665801, ECO:0000269|Ref.5,
FT ECO:0007744|PubMed:19413330, ECO:0007744|PubMed:25944712"
FT CHAIN 2..779
FT /note="Centromere/kinetochore protein zw10 homolog"
FT /id="PRO_0000184957"
FT REGION 2..317
FT /note="Interaction with RINT1"
FT REGION 2..81
FT /note="Interaction with ZWINT"
FT COILED 14..130
FT /evidence="ECO:0000255"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000269|Ref.5, ECO:0007744|PubMed:19413330,
FT ECO:0007744|PubMed:25944712"
FT MOD_RES 3
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 12
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 777
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT VAR_SEQ 673..779
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_056006"
FT VARIANT 77
FT /note="I -> M (in dbSNP:rs2271796)"
FT /id="VAR_053537"
SQ SEQUENCE 779 AA; 88829 MW; 9C38186153886481 CRC64;
MASFVTEVLA HSGRLEKEDL GTRISRLTRR VEEIKGEVCN MISKKYSEFL PSMQSAQGLI
TQVDKLSEDI DLLKSRIESE VRRDLHVSTG EFTDLKQQLE RDSVVLSLLK QLQEFSTAIE
EYNCALTEKK YVTGAQRLEE AQKCLKLLKS RKCFDLKILK SLSMELTIQK QNILYHLGEE
WQKLIVWKFP PSKDTSSLES YLQTELHLYT EQSHKEEKTP MPPISSVLLA FSVLGELHSK
LKSFGQMLLK YILRPLASCP SLHAVIESQP NIVIIRFESI MTNLEYPSPS EVFTKIRLVL
EVLQKQLLDL PLDTDLENEK TSTVPLAEML GDMIWEDLSE CLIKNCLVYS IPTNSSKLQQ
YEEIIQSTEE FENALKEMRF LKGDTTDLLK YARNINSHFA NKKCQDVIVA ARNLMTSEIH
NTVKIIPDSK INVPELPTPD EDNKLEVQKV SNTQYHEVMN LEPENTLDQH SFSLPTCRIS
ESVKKLMELA YQTLLEATTS SDQCAVQLFY SVRNIFHLFH DVVPTYHKEN LQKLPQLAAI
HHNNCMYIAH HLLTLGHQFR LRLAPILCDG TATFVDLVPG FRRLGTECFL AQMRAQKGEL
LERLSSARNF SNMDDEENYS AASKAVRQVL HQLKRLGIVW QDVLPVNIYC KAMGTLLNTA
ISEVIGKITA LEDISTEDGD RLYSLCKTVM DEGPQVFAPL SEESKNKKYQ EEVPVYVPKW
MPFKELMMML QASLQEIGDR WADGKGPLAA AFSSSEVKAL IRALFQNTER RAAALAKIK
