ID   CENPK_HUMAN             Reviewed;         269 AA.
AC   Q9BS16; Q9H4L0;
DT   19-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   27-MAR-2024, entry version 158.
DE   RecName: Full=Centromere protein K;
DE            Short=CENP-K;
DE   AltName: Full=Interphase centromere complex protein 37;
DE   AltName: Full=Protein AF-5alpha;
DE   AltName: Full=p33;
GN   Name=CENPK; Synonyms=ICEN37; ORFNames=FKSG14;
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], CHROMOSOMAL TRANSLOCATION WITH KMT2A/MLL1, AND
RP   TISSUE SPECIFICITY.
RX   PubMed=8950979;
RA   Taki T., Hayashi Y., Taniwaki M., Seto M., Ueda R., Hanada R., Suzukawa K.,
RA   Yokota J., Morishita K.;
RT   "Fusion of the MLL gene with two different genes, AF-6 and AF-5alpha, by a
RT   complex translocation involving chromosomes 5, 6, 8 and 11 in infant
RT   leukemia.";
RL   Oncogene 13:2121-2130(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Chang M.S., Yang Y.C.;
RT   "Molecular cloning of human p33.";
RL   Submitted (OCT-2000) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Carcinoma;
RA   Wang Y.-G.;
RT   "Molecular cloning of FKSG14, a novel gene located on chromosome 5.";
RL   Submitted (OCT-2000) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain, and Gall bladder;
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=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   [6]
RP   IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION IN A COMPLEX WITH
RP   CENPH; CENPI; CENPN; CENPO; 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   [7]
RP   IDENTIFICATION BY MASS SPECTROMETRY, AND IDENTIFICATION IN THE CENPA-CAD
RP   COMPLEX WITH CENPI; CENPL; CENPO; 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   [8]
RP   FUNCTION.
RX   PubMed=18045986; DOI=10.1091/mbc.e07-10-1051;
RA   Cheeseman I.M., Hori T., Fukagawa T., Desai A.;
RT   "KNL1 and the CENP-H/I/K complex coordinately direct kinetochore assembly
RT   in vertebrates.";
RL   Mol. Biol. Cell 19:587-594(2008).
RN   [9]
RP   INTERACTION WITH CENPH.
RX   PubMed=19381461; DOI=10.1007/s11427-009-0050-3;
RA   Qiu S., Wang J., Yu C., He D.;
RT   "CENP-K and CENP-H may form coiled-coils in the kinetochores.";
RL   Sci. China, Ser. C, Life Sci. 52:352-359(2009).
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. Acts in
CC       coordination with KNL1 to recruit the NDC80 complex to the outer
CC       kinetochore. {ECO:0000269|PubMed:16622420, ECO:0000269|PubMed:16716197,
CC       ECO:0000269|PubMed:18045986}.
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. Interacts directly with
CC       CENPH. {ECO:0000269|PubMed:16622419, ECO:0000269|PubMed:16622420,
CC       ECO:0000269|PubMed:19381461}.
CC   -!- INTERACTION:
CC       Q9BS16; Q9H3R5: CENPH; NbExp=7; IntAct=EBI-6871750, EBI-1003700;
CC       Q9BS16; Q96HT8: MRFAP1L1; NbExp=3; IntAct=EBI-6871750, EBI-748896;
CC       Q9BS16; O75381: PEX14; NbExp=3; IntAct=EBI-6871750, EBI-594898;
CC       Q9BS16; Q8WWV3: RTN4IP1; NbExp=3; IntAct=EBI-6871750, EBI-743502;
CC       Q9BS16; Q9Y3C0: WASHC3; NbExp=3; IntAct=EBI-6871750, EBI-712969;
CC       Q9BS16; Q86V28; NbExp=3; IntAct=EBI-6871750, EBI-10259496;
CC   -!- SUBCELLULAR LOCATION: Nucleus. Chromosome, centromere. Chromosome,
CC       centromere, kinetochore. Note=Localizes exclusively in the centromeres.
CC       The CENPA-CAD complex is probably recruited on centromeres by the
CC       CENPA-NAC complex.
CC   -!- TISSUE SPECIFICITY: Detected in several fetal organs with highest
CC       levels in fetal liver. In adults, it is weakly expressed in lung and
CC       placenta. {ECO:0000269|PubMed:8950979}.
CC   -!- DISEASE: Note=Chromosomal aberrations involving CENPK are a cause of
CC       acute leukemias. Translocation t(5;11)(q12;q23) with KMT2A/MLL1.
CC       {ECO:0000269|PubMed:8950979}.
CC   -!- SIMILARITY: Belongs to the CENP-K/MCM22 family. {ECO:0000305}.
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DR   EMBL; AY033646; AAK59382.1; -; mRNA.
DR   EMBL; AF315941; AAL26880.1; -; mRNA.
DR   EMBL; AY009151; AAG31004.1; -; mRNA.
DR   EMBL; BC005400; AAH05400.1; -; mRNA.
DR   EMBL; BC008504; AAH08504.1; -; mRNA.
DR   CCDS; CCDS3984.1; -.
DR   RefSeq; NP_001253967.1; NM_001267038.1.
DR   RefSeq; NP_071428.2; NM_022145.4.
DR   RefSeq; XP_011541838.1; XM_011543536.2.
DR   RefSeq; XP_016865179.1; XM_017009690.1.
DR   RefSeq; XP_016865180.1; XM_017009691.1.
DR   RefSeq; XP_016865181.1; XM_017009692.1.
DR   PDB; 7PB4; X-ray; 2.49 A; K=165-269.
DR   PDB; 7PKN; EM; 3.20 A; K=1-269.
DR   PDB; 7QOO; EM; 4.60 A; K=1-269.
DR   PDB; 7R5S; EM; 2.83 A; K=1-269.
DR   PDB; 7R5V; EM; 4.55 A; K=1-269.
DR   PDB; 7XHN; EM; 3.71 A; K=1-269.
DR   PDB; 7XHO; EM; 3.29 A; K=1-269.
DR   PDB; 7YWX; EM; 12.00 A; K=1-269.
DR   PDB; 7YYH; EM; 8.90 A; K=1-269.
DR   PDBsum; 7PB4; -.
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; Q9BS16; -.
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; Q9BS16; -.
DR   BioGRID; 122063; 77.
DR   ComplexPortal; CPX-5646; Kinetochore CCAN complex.
DR   CORUM; Q9BS16; -.
DR   IntAct; Q9BS16; 19.
DR   MINT; Q9BS16; -.
DR   STRING; 9606.ENSP00000379911; -.
DR   GlyGen; Q9BS16; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; Q9BS16; -.
DR   PhosphoSitePlus; Q9BS16; -.
DR   BioMuta; CENPK; -.
DR   DMDM; 74732954; -.
DR   EPD; Q9BS16; -.
DR   jPOST; Q9BS16; -.
DR   MassIVE; Q9BS16; -.
DR   MaxQB; Q9BS16; -.
DR   PaxDb; 9606-ENSP00000379911; -.
DR   PeptideAtlas; Q9BS16; -.
DR   ProteomicsDB; 78857; -.
DR   Pumba; Q9BS16; -.
DR   Antibodypedia; 23756; 216 antibodies from 26 providers.
DR   DNASU; 64105; -.
DR   Ensembl; ENST00000242872.7; ENSP00000242872.3; ENSG00000123219.13.
DR   Ensembl; ENST00000396679.6; ENSP00000379911.1; ENSG00000123219.13.
DR   Ensembl; ENST00000514814.5; ENSP00000422421.1; ENSG00000123219.13.
DR   GeneID; 64105; -.
DR   KEGG; hsa:64105; -.
DR   MANE-Select; ENST00000396679.6; ENSP00000379911.1; NM_022145.5; NP_071428.2.
DR   UCSC; uc003jts.4; human.
DR   AGR; HGNC:29479; -.
DR   CTD; 64105; -.
DR   DisGeNET; 64105; -.
DR   GeneCards; CENPK; -.
DR   HGNC; HGNC:29479; CENPK.
DR   HPA; ENSG00000123219; Tissue enhanced (bone marrow, lymphoid tissue).
DR   MIM; 611502; gene.
DR   neXtProt; NX_Q9BS16; -.
DR   OpenTargets; ENSG00000123219; -.
DR   PharmGKB; PA145149171; -.
DR   VEuPathDB; HostDB:ENSG00000123219; -.
DR   eggNOG; ENOG502QVGW; Eukaryota.
DR   GeneTree; ENSGT00390000006243; -.
DR   InParanoid; Q9BS16; -.
DR   OMA; QNEIILC; -.
DR   OrthoDB; 5399806at2759; -.
DR   PhylomeDB; Q9BS16; -.
DR   TreeFam; TF333264; -.
DR   PathwayCommons; Q9BS16; -.
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; Q9BS16; -.
DR   SIGNOR; Q9BS16; -.
DR   BioGRID-ORCS; 64105; 758 hits in 1154 CRISPR screens.
DR   ChiTaRS; CENPK; human.
DR   GeneWiki; CENPK; -.
DR   GenomeRNAi; 64105; -.
DR   Pharos; Q9BS16; Tbio.
DR   PRO; PR:Q9BS16; -.
DR   Proteomes; UP000005640; Chromosome 5.
DR   RNAct; Q9BS16; Protein.
DR   Bgee; ENSG00000123219; Expressed in oocyte and 130 other cell types or tissues.
DR   ExpressionAtlas; Q9BS16; baseline and differential.
DR   GO; GO:0005829; C:cytosol; TAS:Reactome.
DR   GO; GO:0000939; C:inner kinetochore; IPI:ComplexPortal.
DR   GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR   GO; GO:0005634; C:nucleus; NAS:ComplexPortal.
DR   GO; GO:0007059; P:chromosome segregation; NAS:ComplexPortal.
DR   GO; GO:0051382; P:kinetochore assembly; IEA:InterPro.
DR   GO; GO:0000070; P:mitotic sister chromatid segregation; IBA:GO_Central.
DR   InterPro; IPR020993; Centromere_CenpK.
DR   PANTHER; PTHR14401; CENTROMERE PROTEIN K; 1.
DR   PANTHER; PTHR14401:SF6; CENTROMERE PROTEIN K; 1.
DR   Pfam; PF11802; CENP-K; 1.
DR   Genevisible; Q9BS16; HS.
PE   1: Evidence at protein level;
KW   3D-structure; Centromere; Chromosomal rearrangement; Chromosome;
KW   Coiled coil; Kinetochore; Nucleus; Reference proteome.
FT   CHAIN           1..269
FT                   /note="Centromere protein K"
FT                   /id="PRO_0000249482"
FT   REGION          1..20
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          22..42
FT                   /evidence="ECO:0000255"
FT   COILED          98..151
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        1..18
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   SITE            96..97
FT                   /note="Breakpoint for translocation to form KMT2A/MLL1-
FT                   CENPK oncogene"
FT   CONFLICT        45
FT                   /note="I -> M (in Ref. 3; AAG31004)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        59
FT                   /note="L -> W (in Ref. 3; AAG31004)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        66
FT                   /note="C -> G (in Ref. 3; AAG31004)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        74
FT                   /note="W -> G (in Ref. 3; AAG31004)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        81
FT                   /note="T -> I (in Ref. 3; AAG31004)"
FT                   /evidence="ECO:0000305"
FT   HELIX           20..42
FT                   /evidence="ECO:0007829|PDB:7R5S"
FT   STRAND          52..55
FT                   /evidence="ECO:0007829|PDB:7R5S"
FT   HELIX           56..75
FT                   /evidence="ECO:0007829|PDB:7R5S"
FT   HELIX           87..148
FT                   /evidence="ECO:0007829|PDB:7R5S"
FT   STRAND          150..152
FT                   /evidence="ECO:0007829|PDB:7XHO"
FT   HELIX           166..187
FT                   /evidence="ECO:0007829|PDB:7PB4"
FT   HELIX           212..225
FT                   /evidence="ECO:0007829|PDB:7PB4"
FT   STRAND          236..238
FT                   /evidence="ECO:0007829|PDB:7R5S"
FT   HELIX           240..248
FT                   /evidence="ECO:0007829|PDB:7PB4"
FT   STRAND          251..254
FT                   /evidence="ECO:0007829|PDB:7PB4"
FT   STRAND          261..264
FT                   /evidence="ECO:0007829|PDB:7PB4"
SQ   SEQUENCE   269 AA;  31655 MW;  D59737D32D221A84 CRC64;
     MNQEDLDPDS TTDVGDVTNT EEELIRECEE MWKDMEECQN KLSLIGTETL TDSNAQLSLL
     IMQVKCLTAE LSQWQKKTPE TIPLTEDVLI TLGKEEFQKL RQDLEMVLST KESKNEKLKE
     DLEREQRWLD EQQQIMESLN VLHSELKNKV ETFSESRIFN ELKTKMLNIK EYKEKLLSTL
     GEFLEDHFPL PDRSVKKKKK NIQESSVNLI TLHEMLEILI NRLFDVPHDP YVKISDSFWP
     PYVELLLRNG IALRHPEDPT RIRLEAFHQ
//