ID CENPO_HUMAN Reviewed; 300 AA. AC Q9BU64; B2RDC0; D6W536; Q53T55; Q96JV3; DT 19-SEP-2006, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-2001, sequence version 1. DT 05-FEB-2025, entry version 169. DE RecName: Full=Centromere protein O; DE Short=CENP-O; DE AltName: Full=Interphase centromere complex protein 36; GN Name=CENPO; Synonyms=ICEN36, MCM21R; 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] (ISOFORMS 1 AND 2), AND VARIANT RP ARG-34. RC TISSUE=Placenta; 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=15815621; DOI=10.1038/nature03466; RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., RA Wilson R.K.; RT "Generation and annotation of the DNA sequences of human chromosomes 2 and RT 4."; RL Nature 434:724-731(2005). RN [3] 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 [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Lung; 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 [5] RP FUNCTION, AND SUBCELLULAR LOCATION. RX PubMed=16932742; DOI=10.1038/sj.emboj.7601293; RA McAinsh A.D., Meraldi P., Draviam V.M., Toso A., Sorger P.K.; RT "The human kinetochore proteins Nnf1R and Mcm21R are required for accurate RT chromosome segregation."; RL EMBO J. 25:4033-4049(2006). RN [6] RP FUNCTION, AND SUBCELLULAR LOCATION. RX PubMed=16716197; DOI=10.1111/j.1365-2443.2006.00969.x; RA Izuta H., Ikeno M., Suzuki N., Tomonaga T., Nozaki N., Obuse C., Kisu Y., RA Goshima N., Nomura F., Nomura N., Yoda K.; RT "Comprehensive analysis of the ICEN (Interphase Centromere Complex) RT components enriched in the CENP-A chromatin of human cells."; RL Genes Cells 11:673-684(2006). RN [7] RP IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION IN A COMPLEX WITH RP CENPH; CENPI; CENPK; CENPN; CENPP; CENPQ; CENPR AND CENPU, FUNCTION, AND RP SUBCELLULAR LOCATION. RX PubMed=16622420; DOI=10.1038/ncb1396; RA Okada M., Cheeseman I.M., Hori T., Okawa K., McLeod I.X., Yates J.R. III, RA Desai A., Fukagawa T.; RT "The CENP-H-I complex is required for the efficient incorporation of newly RT synthesized CENP-A into centromeres."; RL Nat. Cell Biol. 8:446-457(2006). RN [8] RP IDENTIFICATION BY MASS SPECTROMETRY, AND IDENTIFICATION IN THE CENPA-CAD RP COMPLEX WITH CENPI; CENPK; CENPL; CENPP; CENPQ; CENPR AND CENPS. RX PubMed=16622419; DOI=10.1038/ncb1397; RA Foltz D.R., Jansen L.E.T., Black B.E., Bailey A.O., Yates J.R. III, RA Cleveland D.W.; RT "The human CENP-A centromeric nucleosome-associated complex."; RL Nat. Cell Biol. 8:458-469(2006). RN [9] RP FUNCTION, AND SUBCELLULAR LOCATION. RX PubMed=18007590; DOI=10.1038/sj.emboj.7601927; RA McClelland S.E., Borusu S., Amaro A.C., Winter J.R., Belwal M., RA McAinsh A.D., Meraldi P.; RT "The CENP-A NAC/CAD kinetochore complex controls chromosome congression and RT spindle bipolarity."; RL EMBO J. 26:5033-5047(2007). RN [10] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-35, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=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). CC -!- FUNCTION: Component of the CENPA-CAD (nucleosome distal) complex, a CC complex recruited to centromeres which is involved in assembly of CC kinetochore proteins, mitotic progression and chromosome segregation. CC May be involved in incorporation of newly synthesized CENPA into CC centromeres via its interaction with the CENPA-NAC complex. Modulates CC the kinetochore-bound levels of NDC80 complex. CC {ECO:0000269|PubMed:16622420, ECO:0000269|PubMed:16716197, CC ECO:0000269|PubMed:16932742, ECO:0000269|PubMed:18007590}. CC -!- SUBUNIT: Component of the CENPA-CAD complex, composed of CENPI, CENPK, CC CENPL, CENPO, CENPP, CENPQ, CENPR and CENPS. The CENPA-CAD complex CC interacts with the CENPA-NAC complex, at least composed of CENPA, CC CENPC, CENPH, CENPM, CENPN, CENPT and CENPU. CC {ECO:0000269|PubMed:16622419, ECO:0000269|PubMed:16622420}. CC -!- INTERACTION: CC Q9BU64; Q6IPU0: CENPP; NbExp=13; IntAct=EBI-745954, EBI-10250303; CC Q9BU64; Q96L14: CEP170P1; NbExp=5; IntAct=EBI-745954, EBI-743488; CC Q9BU64; Q9UHG0: DCDC2; NbExp=3; IntAct=EBI-745954, EBI-10303987; CC Q9BU64; Q6FG41: FOS; NbExp=3; IntAct=EBI-745954, EBI-10198738; CC Q9BU64; P53539: FOSB; NbExp=3; IntAct=EBI-745954, EBI-2806743; CC Q9BU64; Q7Z6G3-2: NECAB2; NbExp=3; IntAct=EBI-745954, EBI-10172876; CC -!- SUBCELLULAR LOCATION: Nucleus. Chromosome, centromere. Chromosome, CC centromere, kinetochore. Note=The CENPA-CAD complex is probably CC recruited on centromeres by the CENPA-NAC complex. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=Q9BU64-1; Sequence=Displayed; CC Name=2; CC IsoId=Q9BU64-2; Sequence=VSP_020446; CC -!- SIMILARITY: Belongs to the CENP-O/MCM21 family. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AK027859; BAB55414.1; -; mRNA. DR EMBL; AK315483; BAG37867.1; -; mRNA. DR EMBL; AC012073; AAY14786.1; -; Genomic_DNA. DR EMBL; AC013459; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471053; EAX00742.1; -; Genomic_DNA. DR EMBL; CH471053; EAX00743.1; -; Genomic_DNA. DR EMBL; BC002870; AAH02870.1; -; mRNA. DR CCDS; CCDS1714.1; -. [Q9BU64-1] DR CCDS; CCDS56113.1; -. [Q9BU64-2] DR RefSeq; NP_001186732.1; NM_001199803.2. [Q9BU64-2] DR RefSeq; NP_001309030.1; NM_001322101.1. [Q9BU64-1] DR RefSeq; NP_077298.1; NM_024322.3. [Q9BU64-1] DR PDB; 7PB8; X-ray; 3.68 A; O=1-300. DR PDB; 7PKN; EM; 3.20 A; O=1-300. DR PDB; 7QOO; EM; 4.60 A; O=1-300. DR PDB; 7R5S; EM; 2.83 A; O=1-300. DR PDB; 7R5V; EM; 4.55 A; O=1-300. DR PDB; 7XHN; EM; 3.71 A; O/o=1-300. DR PDB; 7XHO; EM; 3.29 A; O=1-300. DR PDB; 7YWX; EM; 12.00 A; O=1-300. DR PDB; 7YYH; EM; 8.90 A; O=1-300. DR PDBsum; 7PB8; -. DR PDBsum; 7PKN; -. DR PDBsum; 7QOO; -. DR PDBsum; 7R5S; -. DR PDBsum; 7R5V; -. DR PDBsum; 7XHN; -. DR PDBsum; 7XHO; -. DR PDBsum; 7YWX; -. DR PDBsum; 7YYH; -. DR AlphaFoldDB; Q9BU64; -. DR EMDB; EMD-13473; -. DR EMDB; EMD-14098; -. DR EMDB; EMD-14336; -. DR EMDB; EMD-14341; -. DR EMDB; EMD-14351; -. DR EMDB; EMD-14375; -. DR EMDB; EMD-33196; -. DR EMDB; EMD-33197; -. DR SMR; Q9BU64; -. DR BioGRID; 122589; 49. DR ComplexPortal; CPX-5646; Kinetochore CCAN complex. DR CORUM; Q9BU64; -. DR IntAct; Q9BU64; 41. DR MINT; Q9BU64; -. DR STRING; 9606.ENSP00000370214; -. DR iPTMnet; Q9BU64; -. DR PhosphoSitePlus; Q9BU64; -. DR BioMuta; CENPO; -. DR DMDM; 74733185; -. DR jPOST; Q9BU64; -. DR MassIVE; Q9BU64; -. DR PaxDb; 9606-ENSP00000370214; -. DR PeptideAtlas; Q9BU64; -. DR ProteomicsDB; 79055; -. [Q9BU64-1] DR ProteomicsDB; 79056; -. [Q9BU64-2] DR Pumba; Q9BU64; -. DR Antibodypedia; 27556; 207 antibodies from 30 providers. DR DNASU; 79172; -. DR Ensembl; ENST00000260662.2; ENSP00000260662.1; ENSG00000138092.11. [Q9BU64-1] DR Ensembl; ENST00000380834.7; ENSP00000370214.2; ENSG00000138092.11. [Q9BU64-1] DR Ensembl; ENST00000473706.5; ENSP00000417787.1; ENSG00000138092.11. [Q9BU64-2] DR GeneID; 79172; -. DR KEGG; hsa:79172; -. DR MANE-Select; ENST00000380834.7; ENSP00000370214.2; NM_001322101.2; NP_001309030.1. DR UCSC; uc002rfp.3; human. [Q9BU64-1] DR AGR; HGNC:28152; -. DR CTD; 79172; -. DR DisGeNET; 79172; -. DR GeneCards; CENPO; -. DR HGNC; HGNC:28152; CENPO. DR HPA; ENSG00000138092; Low tissue specificity. DR MIM; 611504; gene. DR neXtProt; NX_Q9BU64; -. DR OpenTargets; ENSG00000138092; -. DR PharmGKB; PA145149197; -. DR VEuPathDB; HostDB:ENSG00000138092; -. DR eggNOG; ENOG502RY72; Eukaryota. DR GeneTree; ENSGT00390000016702; -. DR HOGENOM; CLU_079531_0_0_1; -. DR InParanoid; Q9BU64; -. DR OMA; MEWANDG; -. DR OrthoDB; 10050372at2759; -. DR PhylomeDB; Q9BU64; -. DR TreeFam; TF335524; -. DR PathwayCommons; Q9BU64; -. 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-606279; Deposition of new CENPA-containing nucleosomes at the centromere. DR Reactome; R-HSA-68877; Mitotic Prometaphase. DR Reactome; R-HSA-9648025; EML4 and NUDC in mitotic spindle formation. DR SignaLink; Q9BU64; -. DR SIGNOR; Q9BU64; -. DR BioGRID-ORCS; 79172; 121 hits in 1162 CRISPR screens. DR ChiTaRS; CENPO; human. DR GeneWiki; CENPO; -. DR GenomeRNAi; 79172; -. DR Pharos; Q9BU64; Tbio. DR PRO; PR:Q9BU64; -. DR Proteomes; UP000005640; Chromosome 2. DR RNAct; Q9BU64; protein. DR Bgee; ENSG00000138092; Expressed in ventricular zone and 122 other cell types or tissues. DR GO; GO:0005829; C:cytosol; TAS:Reactome. DR GO; GO:0000939; C:inner kinetochore; IPI:ComplexPortal. DR GO; GO:0031511; C:Mis6-Sim4 complex; IBA:GO_Central. DR GO; GO:0016604; C:nuclear body; IDA:HPA. DR GO; GO:0005654; C:nucleoplasm; IDA:HPA. DR GO; GO:0005634; C:nucleus; NAS:ComplexPortal. DR GO; GO:0034508; P:centromere complex assembly; IEA:InterPro. DR GO; GO:0007059; P:chromosome segregation; NAS:ComplexPortal. DR InterPro; IPR018464; CENP-O. DR PANTHER; PTHR14582:SF1; CENTROMERE PROTEIN O; 1. DR PANTHER; PTHR14582; INNER KINETOCHORE SUBUNIT MAL2; 1. DR Pfam; PF09496; CENP-O; 1. PE 1: Evidence at protein level; KW 3D-structure; Alternative splicing; Centromere; Chromosome; Coiled coil; KW Kinetochore; Nucleus; Phosphoprotein; Proteomics identification; KW Reference proteome. FT CHAIN 1..300 FT /note="Centromere protein O" FT /id="PRO_0000249502" FT COILED 18..42 FT /evidence="ECO:0000255" FT COILED 83..109 FT /evidence="ECO:0000255" FT MOD_RES 35 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT VAR_SEQ 1..15 FT /note="MEQANPLRPDGESKG -> MAGILASGL (in isoform 2)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_020446" FT VARIANT 34 FT /note="Q -> R (in dbSNP:rs1550116)" FT /evidence="ECO:0000269|PubMed:14702039" FT /id="VAR_027420" FT CONFLICT 235 FT /note="A -> V (in Ref. 1; BAB55414)" FT /evidence="ECO:0000305" FT CONFLICT 269 FT /note="A -> V (in Ref. 1; BAB55414)" FT /evidence="ECO:0000305" FT HELIX 17..26 FT /evidence="ECO:0007829|PDB:7R5S" FT HELIX 90..108 FT /evidence="ECO:0007829|PDB:7R5S" FT HELIX 109..111 FT /evidence="ECO:0007829|PDB:7R5S" FT STRAND 112..117 FT /evidence="ECO:0007829|PDB:7R5S" FT STRAND 119..130 FT /evidence="ECO:0007829|PDB:7R5S" FT STRAND 133..143 FT /evidence="ECO:0007829|PDB:7R5S" FT STRAND 145..147 FT /evidence="ECO:0007829|PDB:7R5S" FT STRAND 149..153 FT /evidence="ECO:0007829|PDB:7R5S" FT STRAND 157..159 FT /evidence="ECO:0007829|PDB:7XHO" FT HELIX 161..168 FT /evidence="ECO:0007829|PDB:7R5S" FT STRAND 169..171 FT /evidence="ECO:0007829|PDB:7R5S" FT HELIX 173..199 FT /evidence="ECO:0007829|PDB:7R5S" FT STRAND 203..205 FT /evidence="ECO:0007829|PDB:7R5S" FT HELIX 213..215 FT /evidence="ECO:0007829|PDB:7XHO" FT STRAND 217..224 FT /evidence="ECO:0007829|PDB:7R5S" FT STRAND 226..228 FT /evidence="ECO:0007829|PDB:7XHO" FT STRAND 231..238 FT /evidence="ECO:0007829|PDB:7R5S" FT STRAND 248..253 FT /evidence="ECO:0007829|PDB:7R5S" FT HELIX 262..277 FT /evidence="ECO:0007829|PDB:7R5S" FT HELIX 280..287 FT /evidence="ECO:0007829|PDB:7R5S" FT HELIX 292..294 FT /evidence="ECO:0007829|PDB:7XHO" SQ SEQUENCE 300 AA; 33786 MW; 05A89E12C6847D81 CRC64; MEQANPLRPD GESKGGVLAH LERLETQVSR SRKQSEELQS VQAQEGALGT KIHKLRRLRD ELRAVVRHRR ASVKACIANV EPNQTVEINE QEALEEKLEN VKAILQAYHF TGLSGKLTSR GVCVCISTAF EGNLLDSYFV DLVIQKPLRI HHHSVPVFIP LEEIAAKYLQ TNIQHFLFSL CEYLNAYSGR KYQADRLQSD FAALLTGPLQ RNPLCNLLSF TYKLDPGGQS FPFCARLLYK DLTATLPTDV TVTCQGVEVL STSWEEQRAS HETLFCTKPL HQVFASFTRK GEKLDMSLVS //