CENPH_MOUSE
ID CENPH_MOUSE Reviewed; 241 AA.
AC Q9QYM8; Q8R3K9; Q9D079; Q9D0N1;
DT 08-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 126.
DE RecName: Full=Centromere protein H;
DE Short=CENP-H;
GN Name=Cenph {ECO:0000312|MGI:MGI:1349448};
GN Synonyms=Enp {ECO:0000312|EMBL:BAA88520.1};
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] {ECO:0000305, ECO:0000312|EMBL:BAA88520.1}
RP NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND
RP DEVELOPMENTAL STAGE.
RX PubMed=10488063; DOI=10.1074/jbc.274.39.27343;
RA Sugata N., Munekata E., Todokoro K.;
RT "Characterization of a novel kinetochore protein, CENP-H.";
RL J. Biol. Chem. 274:27343-27346(1999).
RN [2] {ECO:0000312|EMBL:BAB27505.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J {ECO:0000312|EMBL:BAB27505.1};
RC TISSUE=Embryo {ECO:0000312|EMBL:BAB27505.1};
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] {ECO:0000312|EMBL:AAH25084.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Czech II {ECO:0000312|EMBL:AAH25084.1};
RC TISSUE=Mammary gland {ECO:0000312|EMBL:AAH25084.1};
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 INTERACTION WITH TRIM36.
RX PubMed=19232519; DOI=10.1016/j.bbrc.2009.02.059;
RA Miyajima N., Maruyama S., Nonomura K., Hatakeyama S.;
RT "TRIM36 interacts with the kinetochore protein CENP-H and delays cell cycle
RT progression.";
RL Biochem. Biophys. Res. Commun. 381:383-387(2009).
CC -!- FUNCTION: Component of the CENPA-NAC (nucleosome-associated) complex, a
CC complex that plays a central role in assembly of kinetochore proteins,
CC mitotic progression and chromosome segregation. The CENPA-NAC complex
CC recruits the CENPA-CAD (nucleosome distal) complex and may be involved
CC in incorporation of newly synthesized CENPA into centromeres. Required
CC for chromosome congression and efficiently align the chromosomes on a
CC metaphase plate (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Self-associates. Component of the CENPA-NAC complex, at least
CC composed of CENPA, CENPC, CENPH, CENPM, CENPN, CENPT and CENPU. The
CC CENPA-NAC complex interacts with the CENPA-CAD complex, composed of
CC CENPI, CENPK, CENPL, CENPO, CENPP, CENPQ, CENPR and CENPS (By
CC similarity). Interacts directly with CENPK (By similarity). Interacts
CC with KIF2C and NDC80 (By similarity). Interacts with TRIM36.
CC {ECO:0000250, ECO:0000269|PubMed:19232519}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:10488063}.
CC Chromosome, centromere, kinetochore {ECO:0000269|PubMed:10488063}.
CC Note=Associates with active centromere-kinetochore complexes throughout
CC the cell cycle. Colocalizes with inner kinetochore plate proteins CENPA
CC and CENPC during both interphase and metaphase.
CC -!- TISSUE SPECIFICITY: Abundantly expressed in thymus, spleen, uterus,
CC ovary, testis and muscle, and weakly expressed in small intestine, lung
CC and stomach. Barely detectable expression in kidney, liver, skin and
CC prostate gland. Not detected in brain, heart or adrenal gland. Also
CC expressed weakly in various hematopoietic cell lines.
CC {ECO:0000269|PubMed:10488063}.
CC -!- DEVELOPMENTAL STAGE: Abundantly expressed between embryonic day 9.5 and
CC 12.5. {ECO:0000269|PubMed:10488063}.
CC -!- SIMILARITY: Belongs to the CENP-H/MCM16 family. {ECO:0000255}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB27505.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=BAB27810.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AB017634; BAA88520.1; -; mRNA.
DR EMBL; AK011264; BAB27505.1; ALT_FRAME; mRNA.
DR EMBL; AK011738; BAB27810.1; ALT_FRAME; mRNA.
DR EMBL; BC025084; AAH25084.1; -; mRNA.
DR CCDS; CCDS26738.1; -.
DR RefSeq; NP_068686.1; NM_021886.1.
DR AlphaFoldDB; Q9QYM8; -.
DR SMR; Q9QYM8; -.
DR BioGRID; 205039; 42.
DR ComplexPortal; CPX-5704; Kinetochore CCAN complex.
DR IntAct; Q9QYM8; 25.
DR STRING; 10090.ENSMUSP00000074988; -.
DR PhosphoSitePlus; Q9QYM8; -.
DR EPD; Q9QYM8; -.
DR MaxQB; Q9QYM8; -.
DR PaxDb; Q9QYM8; -.
DR PeptideAtlas; Q9QYM8; -.
DR PRIDE; Q9QYM8; -.
DR ProteomicsDB; 281537; -.
DR Antibodypedia; 23919; 403 antibodies from 30 providers.
DR DNASU; 26886; -.
DR Ensembl; ENSMUST00000075550; ENSMUSP00000074988; ENSMUSG00000045273.
DR GeneID; 26886; -.
DR KEGG; mmu:26886; -.
DR UCSC; uc007rrn.1; mouse.
DR CTD; 64946; -.
DR MGI; MGI:1349448; Cenph.
DR VEuPathDB; HostDB:ENSMUSG00000045273; -.
DR eggNOG; ENOG502S0VG; Eukaryota.
DR GeneTree; ENSGT00390000009578; -.
DR HOGENOM; CLU_097390_0_0_1; -.
DR InParanoid; Q9QYM8; -.
DR OMA; KSHQESW; -.
DR OrthoDB; 1467214at2759; -.
DR PhylomeDB; Q9QYM8; -.
DR TreeFam; TF101134; -.
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; 26886; 20 hits in 71 CRISPR screens.
DR ChiTaRS; Cenph; mouse.
DR PRO; PR:Q9QYM8; -.
DR Proteomes; UP000000589; Chromosome 13.
DR RNAct; Q9QYM8; protein.
DR Bgee; ENSMUSG00000045273; Expressed in dorsal pancreas and 157 other tissues.
DR Genevisible; Q9QYM8; MM.
DR GO; GO:0005694; C:chromosome; ISO:MGI.
DR GO; GO:0000776; C:kinetochore; IDA:MGI.
DR GO; GO:0005730; C:nucleolus; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0043515; F:kinetochore binding; IDA:UniProtKB.
DR GO; GO:0007059; P:chromosome segregation; ISO:MGI.
DR GO; GO:0051382; P:kinetochore assembly; IEA:InterPro.
DR GO; GO:0051383; P:kinetochore organization; TAS:UniProtKB.
DR GO; GO:0000278; P:mitotic cell cycle; ISO:MGI.
DR GO; GO:0007052; P:mitotic spindle organization; IBA:GO_Central.
DR InterPro; IPR040034; CENP-H.
DR InterPro; IPR008426; CENP-H_C.
DR PANTHER; PTHR48122; PTHR48122; 1.
DR Pfam; PF05837; CENP-H; 1.
PE 1: Evidence at protein level;
KW Acetylation; Centromere; Chromosome; Coiled coil; Isopeptide bond;
KW Kinetochore; Nucleus; Phosphoprotein; Reference proteome; Ubl conjugation.
FT CHAIN 1..241
FT /note="Centromere protein H"
FT /id="PRO_0000089479"
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 28..186
FT /evidence="ECO:0000255"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:Q9H3R5"
FT MOD_RES 62
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9H3R5"
FT CROSSLNK 61
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9H3R5"
FT CONFLICT 239
FT /note="N -> T (in Ref. 3; AAH25084)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 241 AA; 28135 MW; A56CD10AFE07D0AD CRC64;
MEEQPRERSE AGAEACEEKR GLSQAAEERI EDRISLLLRL RAQTKQQLLE YKSMIDTNEE
KTPEQIMQEK QIEVKIEELE NEIEDVKSNI EMKSLALSRM KLSVALRDNM ENMGPENCVL
TDDMKHILKL QKLIMKSQEE SSELEKKLLD VRKKRLQLKQ ASRSKLLEIQ IEKNKQKEDV
DKMENSEMIK TMKKKLQTEI KITTVVQHTF QGLILASKTN WAEDPALRET VLQLEKDLNT
L
