CENPV_HUMAN
ID CENPV_HUMAN Reviewed; 275 AA.
AC Q7Z7K6; B2RPK2; Q3L8N5; Q8NFH6;
DT 27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 03-AUG-2022, entry version 147.
DE RecName: Full=Centromere protein V;
DE Short=CENP-V;
DE AltName: Full=Nuclear protein p30;
DE AltName: Full=Proline-rich protein 6;
GN Name=CENPV; Synonyms=PRR6;
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 2).
RA Zheng H., Xie Y., Mao Y.;
RT "Cloning and characterization of a novel splice variant of nuclear protein
RT p30.";
RL Submitted (SEP-2003) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
RC TISSUE=Blood;
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 [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 2-275 (ISOFORM 3), AND SUBCELLULAR LOCATION.
RX PubMed=12196509; DOI=10.1083/jcb.200206106;
RA Cronshaw J.M., Krutchinsky A.N., Zhang W., Chait B.T., Matunis M.J.;
RT "Proteomic analysis of the mammalian nuclear pore complex.";
RL J. Cell Biol. 158:915-927(2002).
RN [4]
RP FUNCTION, SUBCELLULAR LOCATION, AND MUTAGENESIS OF CYS-172; CYS-174 AND
RP CYS-177.
RX PubMed=18772885; DOI=10.1038/emboj.2008.175;
RA Tadeu A.M.B., Ribeiro S., Johnston J., Goldberg I., Gerloff D.,
RA Earnshaw W.C.;
RT "CENP-V is required for centromere organization, chromosome alignment and
RT cytokinesis.";
RL EMBO J. 27:2510-2522(2008).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-21, 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 [6]
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 [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-21, 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 [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-18, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
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 [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-98; THR-101 AND THR-103, AND
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).
CC -!- FUNCTION: Required for distribution of pericentromeric heterochromatin
CC in interphase nuclei and for centromere formation and organization,
CC chromosome alignment and cytokinesis. {ECO:0000269|PubMed:18772885}.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU01239};
CC Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000255|PROSITE-
CC ProRule:PRU01239};
CC -!- INTERACTION:
CC Q7Z7K6; P54253: ATXN1; NbExp=6; IntAct=EBI-1210604, EBI-930964;
CC Q7Z7K6; Q9UBB4: ATXN10; NbExp=3; IntAct=EBI-1210604, EBI-702390;
CC Q7Z7K6; P46379-2: BAG6; NbExp=3; IntAct=EBI-1210604, EBI-10988864;
CC Q7Z7K6; G5E9A7: DMWD; NbExp=3; IntAct=EBI-1210604, EBI-10976677;
CC Q7Z7K6; O14645: DNALI1; NbExp=3; IntAct=EBI-1210604, EBI-395638;
CC Q7Z7K6; Q5SUL5: HLA-A; NbExp=3; IntAct=EBI-1210604, EBI-8561769;
CC Q7Z7K6; O43464: HTRA2; NbExp=3; IntAct=EBI-1210604, EBI-517086;
CC Q7Z7K6; P42858: HTT; NbExp=15; IntAct=EBI-1210604, EBI-466029;
CC Q7Z7K6; Q8WXH2: JPH3; NbExp=3; IntAct=EBI-1210604, EBI-1055254;
CC Q7Z7K6; Q92993: KAT5; NbExp=3; IntAct=EBI-1210604, EBI-399080;
CC Q7Z7K6; O14901: KLF11; NbExp=3; IntAct=EBI-1210604, EBI-948266;
CC Q7Z7K6; Q8TAP4-4: LMO3; NbExp=3; IntAct=EBI-1210604, EBI-11742507;
CC Q7Z7K6; Q13449: LSAMP; NbExp=3; IntAct=EBI-1210604, EBI-4314821;
CC Q7Z7K6; P23284: PPIB; NbExp=3; IntAct=EBI-1210604, EBI-359252;
CC Q7Z7K6; P41219: PRPH; NbExp=3; IntAct=EBI-1210604, EBI-752074;
CC Q7Z7K6; Q15047-2: SETDB1; NbExp=3; IntAct=EBI-1210604, EBI-9090795;
CC Q7Z7K6; P37840: SNCA; NbExp=4; IntAct=EBI-1210604, EBI-985879;
CC Q7Z7K6; Q7Z699: SPRED1; NbExp=3; IntAct=EBI-1210604, EBI-5235340;
CC Q7Z7K6; P61981: YWHAG; NbExp=3; IntAct=EBI-1210604, EBI-359832;
CC -!- SUBCELLULAR LOCATION: Chromosome, centromere, kinetochore
CC {ECO:0000269|PubMed:18772885}. Nucleus {ECO:0000269|PubMed:12196509}.
CC Cytoplasm, cytoskeleton, spindle {ECO:0000269|PubMed:18772885}.
CC Note=Enriched at the nuclear periphery and around the nucleolus
CC (PubMed:12196509). In mitotic cells, localizes to kinetochores from
CC prometaphase to metaphase (PubMed:18772885). At anaphase onset,
CC transfers to the spindle midzone and then to the mid-body in telophase
CC and cytokinesis (PubMed:18772885).
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q7Z7K6-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q7Z7K6-2; Sequence=VSP_019549;
CC Name=3;
CC IsoId=Q7Z7K6-3; Sequence=VSP_019550;
CC -!- SIMILARITY: Belongs to the Gfa family. {ECO:0000305}.
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DR EMBL; AY382899; AAR24368.1; -; mRNA.
DR EMBL; BC052604; AAH52604.1; -; mRNA.
DR EMBL; BC137486; AAI37487.1; -; mRNA.
DR EMBL; BC137487; AAI37488.1; -; mRNA.
DR EMBL; AF514992; AAM76703.1; -; mRNA.
DR CCDS; CCDS32575.1; -. [Q7Z7K6-3]
DR RefSeq; NP_859067.2; NM_181716.2. [Q7Z7K6-3]
DR AlphaFoldDB; Q7Z7K6; -.
DR SMR; Q7Z7K6; -.
DR BioGRID; 128365; 100.
DR IntAct; Q7Z7K6; 56.
DR MINT; Q7Z7K6; -.
DR STRING; 9606.ENSP00000299736; -.
DR GlyGen; Q7Z7K6; 5 sites, 2 O-linked glycans (5 sites).
DR iPTMnet; Q7Z7K6; -.
DR PhosphoSitePlus; Q7Z7K6; -.
DR SwissPalm; Q7Z7K6; -.
DR BioMuta; CENPV; -.
DR DMDM; 74750244; -.
DR EPD; Q7Z7K6; -.
DR jPOST; Q7Z7K6; -.
DR MassIVE; Q7Z7K6; -.
DR MaxQB; Q7Z7K6; -.
DR PaxDb; Q7Z7K6; -.
DR PeptideAtlas; Q7Z7K6; -.
DR PRIDE; Q7Z7K6; -.
DR ProteomicsDB; 69557; -. [Q7Z7K6-1]
DR ProteomicsDB; 69558; -. [Q7Z7K6-2]
DR ProteomicsDB; 69559; -. [Q7Z7K6-3]
DR Antibodypedia; 25303; 80 antibodies from 22 providers.
DR DNASU; 201161; -.
DR Ensembl; ENST00000299736.5; ENSP00000299736.4; ENSG00000166582.11. [Q7Z7K6-3]
DR GeneID; 201161; -.
DR KEGG; hsa:201161; -.
DR MANE-Select; ENST00000299736.5; ENSP00000299736.4; NM_181716.3; NP_859067.2. [Q7Z7K6-3]
DR UCSC; uc002gpw.4; human. [Q7Z7K6-1]
DR CTD; 201161; -.
DR DisGeNET; 201161; -.
DR GeneCards; CENPV; -.
DR HGNC; HGNC:29920; CENPV.
DR HPA; ENSG00000166582; Low tissue specificity.
DR MIM; 608139; gene.
DR neXtProt; NX_Q7Z7K6; -.
DR OpenTargets; ENSG00000166582; -.
DR PharmGKB; PA164717842; -.
DR VEuPathDB; HostDB:ENSG00000166582; -.
DR eggNOG; KOG4192; Eukaryota.
DR GeneTree; ENSGT00390000003183; -.
DR HOGENOM; CLU_087799_0_0_1; -.
DR InParanoid; Q7Z7K6; -.
DR OMA; HRLSCEE; -.
DR OrthoDB; 1326510at2759; -.
DR PhylomeDB; Q7Z7K6; -.
DR TreeFam; TF313636; -.
DR PathwayCommons; Q7Z7K6; -.
DR SignaLink; Q7Z7K6; -.
DR BioGRID-ORCS; 201161; 21 hits in 1081 CRISPR screens.
DR ChiTaRS; CENPV; human.
DR GenomeRNAi; 201161; -.
DR Pharos; Q7Z7K6; Tbio.
DR PRO; PR:Q7Z7K6; -.
DR Proteomes; UP000005640; Chromosome 17.
DR RNAct; Q7Z7K6; protein.
DR Bgee; ENSG00000166582; Expressed in ganglionic eminence and 159 other tissues.
DR ExpressionAtlas; Q7Z7K6; baseline and differential.
DR Genevisible; Q7Z7K6; HS.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0000776; C:kinetochore; IDA:UniProtKB.
DR GO; GO:0015630; C:microtubule cytoskeleton; IDA:MGI.
DR GO; GO:0030496; C:midbody; IDA:HPA.
DR GO; GO:0031965; C:nuclear membrane; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0051233; C:spindle midzone; IDA:UniProtKB.
DR GO; GO:0016846; F:carbon-sulfur lyase activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0001667; P:ameboidal-type cell migration; IDA:MGI.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0034508; P:centromere complex assembly; IMP:UniProtKB.
DR GO; GO:0031508; P:pericentric heterochromatin assembly; IMP:UniProtKB.
DR GO; GO:0032467; P:positive regulation of cytokinesis; IMP:UniProtKB.
DR GO; GO:0033044; P:regulation of chromosome organization; IMP:UniProtKB.
DR InterPro; IPR006913; CENP-V/GFA.
DR InterPro; IPR011057; Mss4-like_sf.
DR Pfam; PF04828; GFA; 1.
DR SUPFAM; SSF51316; SSF51316; 1.
DR PROSITE; PS51891; CENP_V_GFA; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell cycle; Cell division; Centromere; Chromosome;
KW Cytoplasm; Cytoskeleton; Kinetochore; Metal-binding; Methylation; Mitosis;
KW Nucleus; Phosphoprotein; Reference proteome; Zinc.
FT CHAIN 1..275
FT /note="Centromere protein V"
FT /id="PRO_0000244359"
FT DOMAIN 148..260
FT /note="CENP-V/GFA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01239"
FT REGION 1..109
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 40..55
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 58..74
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 76..102
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 152
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="structural"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01239"
FT BINDING 154
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="structural"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01239"
FT BINDING 172
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01239"
FT BINDING 174
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01239"
FT BINDING 177
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01239"
FT BINDING 216
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="structural"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01239"
FT BINDING 219
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="structural"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01239"
FT MOD_RES 18
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 21
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231"
FT MOD_RES 43
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q9CXS4"
FT MOD_RES 98
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 101
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 103
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 257
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9CXS4"
FT VAR_SEQ 1..173
FT /note="MRRSRSSAAAKLRGQKRSGASGASAAPAASAAAALAPSATRTRRSASQAGSK
FT SQAVEKPPSEKPRLRRSSPRAQEEGPGEPPPPELALLPPPPPPPPTPATPTSSASNLDL
FT GEQRERWETFQKRQKLTSEGAAKLLLDTFEYQGLVKHTGGCHCGAVRFEVWASADLHIF
FT DCN -> MQVAAHNLEFALSFCS (in isoform 2)"
FT /evidence="ECO:0000303|Ref.1"
FT /id="VSP_019549"
FT VAR_SEQ 18..20
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:12196509,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_019550"
FT MUTAGEN 172
FT /note="C->A: Abolishes chromatin hypercondensation
FT phenotype induced by overexpression of wild-type protein;
FT when associated with A-177."
FT /evidence="ECO:0000269|PubMed:18772885"
FT MUTAGEN 174
FT /note="C->A: Abolishes chromatin hypercondensation
FT phenotype induced by overexpression of wild-type protein."
FT /evidence="ECO:0000269|PubMed:18772885"
FT MUTAGEN 177
FT /note="C->A: Abolishes chromatin hypercondensation
FT phenotype induced by overexpression of wild-type protein;
FT when associated with A-172."
FT /evidence="ECO:0000269|PubMed:18772885"
SQ SEQUENCE 275 AA; 29946 MW; E9A69F1F9BA746D8 CRC64;
MRRSRSSAAA KLRGQKRSGA SGASAAPAAS AAAALAPSAT RTRRSASQAG SKSQAVEKPP
SEKPRLRRSS PRAQEEGPGE PPPPELALLP PPPPPPPTPA TPTSSASNLD LGEQRERWET
FQKRQKLTSE GAAKLLLDTF EYQGLVKHTG GCHCGAVRFE VWASADLHIF DCNCSICKKK
QNRHFIVPAS RFKLLKGAEH ITTYTFNTHK AQHTFCKRCG VQSFYTPRSN PGGFGIAPHC
LDEGTVRSMV TEEFNGSDWE KAMKEHKTIK NMSKE
