CENPK_MOUSE
ID CENPK_MOUSE Reviewed; 271 AA.
AC Q9ESN5; Q3UXA9; Q569Q3; Q8C469;
DT 19-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT 19-SEP-2006, sequence version 2.
DT 03-AUG-2022, entry version 125.
DE RecName: Full=Centromere protein K;
DE Short=CENP-K;
DE AltName: Full=SoxLZ/Sox6 leucine zipper-binding protein in testis;
GN Name=Cenpk; Synonyms=Solt;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, AND POSSIBLE INTERACTION WITH SOX6.
RX PubMed=10996314; DOI=10.1016/s0014-5793(00)01987-6;
RA Yamashita A., Ito M., Takamatsu N., Shiba T.;
RT "Characterization of Solt, a novel SoxLZ/Sox6 binding protein expressed in
RT adult mouse testis.";
RL FEBS Lett. 481:147-151(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3).
RC STRAIN=C57BL/6J; TISSUE=Egg, and Spinal cord;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-120.
RC STRAIN=NMRI; TISSUE=Mammary tumor;
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).
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 (By similarity). {ECO:0000250}.
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. May interact with Sox6.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Chromosome, centromere
CC {ECO:0000250}. Chromosome, centromere, kinetochore {ECO:0000250}.
CC Note=Localizes exclusively in the centromeres. The CENPA-CAD complex is
CC probably recruited on centromeres by the CENPA-NAC complex (By
CC similarity). {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q9ESN5-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9ESN5-2; Sequence=VSP_020438;
CC Name=3;
CC IsoId=Q9ESN5-3; Sequence=VSP_020437, VSP_020439;
CC -!- TISSUE SPECIFICITY: Highly expressed in testis.
CC {ECO:0000269|PubMed:10996314}.
CC -!- SIMILARITY: Belongs to the CENP-K/MCM22 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH92351.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305};
CC Sequence=BAB16367.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AB043687; BAB16367.1; ALT_INIT; mRNA.
DR EMBL; AK082939; BAC38702.1; -; mRNA.
DR EMBL; AK135773; BAE22654.1; -; mRNA.
DR EMBL; BC092351; AAH92351.1; ALT_SEQ; mRNA.
DR CCDS; CCDS26750.1; -. [Q9ESN5-2]
DR RefSeq; NP_068562.1; NM_021790.2.
DR RefSeq; NP_851406.1; NM_181061.5. [Q9ESN5-2]
DR RefSeq; XP_017171041.1; XM_017315552.1.
DR RefSeq; XP_017171042.1; XM_017315553.1.
DR AlphaFoldDB; Q9ESN5; -.
DR SMR; Q9ESN5; -.
DR BioGRID; 208561; 20.
DR ComplexPortal; CPX-5704; Kinetochore CCAN complex.
DR IntAct; Q9ESN5; 1.
DR MINT; Q9ESN5; -.
DR STRING; 10090.ENSMUSP00000022227; -.
DR iPTMnet; Q9ESN5; -.
DR PhosphoSitePlus; Q9ESN5; -.
DR MaxQB; Q9ESN5; -.
DR PaxDb; Q9ESN5; -.
DR PeptideAtlas; Q9ESN5; -.
DR PRIDE; Q9ESN5; -.
DR ProteomicsDB; 280060; -. [Q9ESN5-1]
DR ProteomicsDB; 280061; -. [Q9ESN5-2]
DR ProteomicsDB; 280062; -. [Q9ESN5-3]
DR Antibodypedia; 23756; 194 antibodies from 26 providers.
DR DNASU; 60411; -.
DR Ensembl; ENSMUST00000070761; ENSMUSP00000070910; ENSMUSG00000021714. [Q9ESN5-2]
DR GeneID; 60411; -.
DR KEGG; mmu:60411; -.
DR UCSC; uc007rtc.2; mouse. [Q9ESN5-2]
DR UCSC; uc007rtd.2; mouse. [Q9ESN5-1]
DR UCSC; uc007rtf.1; mouse. [Q9ESN5-3]
DR CTD; 64105; -.
DR MGI; MGI:1926210; Cenpk.
DR VEuPathDB; HostDB:ENSMUSG00000021714; -.
DR eggNOG; ENOG502QVGW; Eukaryota.
DR GeneTree; ENSGT00390000006243; -.
DR InParanoid; Q9ESN5; -.
DR OrthoDB; 1051530at2759; -.
DR PhylomeDB; Q9ESN5; -.
DR TreeFam; TF333264; -.
DR Reactome; R-MMU-141444; Amplification of signal from unattached kinetochores via a MAD2 inhibitory signal.
DR Reactome; R-MMU-2467813; Separation of Sister Chromatids.
DR Reactome; R-MMU-2500257; Resolution of Sister Chromatid Cohesion.
DR Reactome; R-MMU-5663220; RHO GTPases Activate Formins.
DR Reactome; R-MMU-606279; Deposition of new CENPA-containing nucleosomes at the centromere.
DR Reactome; R-MMU-68877; Mitotic Prometaphase.
DR Reactome; R-MMU-9648025; EML4 and NUDC in mitotic spindle formation.
DR BioGRID-ORCS; 60411; 21 hits in 73 CRISPR screens.
DR PRO; PR:Q9ESN5; -.
DR Proteomes; UP000000589; Chromosome 13.
DR RNAct; Q9ESN5; protein.
DR Bgee; ENSMUSG00000021714; Expressed in ureter smooth muscle and 175 other tissues.
DR ExpressionAtlas; Q9ESN5; baseline and differential.
DR GO; GO:0000776; C:kinetochore; IEA:UniProtKB-KW.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0051382; P:kinetochore assembly; IEA:InterPro.
DR GO; GO:0000070; P:mitotic sister chromatid segregation; IBA:GO_Central.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:MGI.
DR InterPro; IPR020993; Centromere_CenpK.
DR PANTHER; PTHR14401; PTHR14401; 1.
DR Pfam; PF11802; CENP-K; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Centromere; Chromosomal rearrangement; Chromosome;
KW Coiled coil; Kinetochore; Nucleus; Reference proteome.
FT CHAIN 1..271
FT /note="Centromere protein K"
FT /id="PRO_0000249483"
FT COILED 11..44
FT /evidence="ECO:0000255"
FT COILED 102..151
FT /evidence="ECO:0000255"
FT VAR_SEQ 1..107
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_020437"
FT VAR_SEQ 220..271
FT /note="MLINRMFDVPHDPYVKIRDSFWPPYIELLLRYGIALRHPEDPSQIRLEAFHQ
FT -> VPLRAMGSTLESCWFPRETLLEEAAFSLASASVG (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_020438"
FT VAR_SEQ 266..271
FT /note="LEAFHQ -> TSCMVGACGDQKSHH (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_020439"
FT CONFLICT 115
FT /note="S -> T (in Ref. 3; AAH92351)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 271 AA; 31686 MW; 0805A7930078B014 CRC64;
MSENKQEVHP DTITDVEAVI DTEEELIKEC EEMWKDMEDC QNKLSLIGTE TLTNADAQLS
LLIMQMKCLT AELGQWKKRK PEIIPLNEDV LLTLGKEEFQ KLRCDLEMVL STIQSKNEKL
KEDLEREQQW LDEQQQILDT LNVLNSDVEN QVVTLTESRI FNELTTKIRG IKEFKEKLLL
TLGAFLDNHF PLPEASTPKK RKNIQDSNAQ LITLNEILEM LINRMFDVPH DPYVKIRDSF
WPPYIELLLR YGIALRHPED PSQIRLEAFH Q
