Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Centromere protein H

Gene

Cenph

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Component of the CENPA-NAC (nucleosome-associated) complex, a complex that plays a central role in assembly of kinetochore proteins, mitotic progression and chromosome segregation. The CENPA-NAC complex recruits the CENPA-CAD (nucleosome distal) complex and may be involved in incorporation of newly synthesized CENPA into centromeres. Required for chromosome congression and efficiently align the chromosomes on a metaphase plate (By similarity).By similarity

GO - Molecular functioni

  • kinetochore binding Source: UniProtKB

GO - Biological processi

  • chromosome segregation Source: MGI
  • kinetochore assembly Source: InterPro
  • kinetochore organization Source: UniProtKB
  • mitotic nuclear division Source: MGI
Complete GO annotation...

Enzyme and pathway databases

ReactomeiREACT_286371. Deposition of new CENPA-containing nucleosomes at the centromere.
REACT_306375. Mitotic Prometaphase.
REACT_321346. Separation of Sister Chromatids.
REACT_329805. Resolution of Sister Chromatid Cohesion.
REACT_358264. RHO GTPases Activate Formins.

Names & Taxonomyi

Protein namesi
Recommended name:
Centromere protein H
Short name:
CENP-H
Gene namesi
Name:CenphImported
Synonyms:EnpImported
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Chromosome 13

Organism-specific databases

MGIiMGI:1349448. Cenph.

Subcellular locationi

  • Nucleus 1 Publication
  • Chromosomecentromerekinetochore 1 Publication

  • Note: Associates with active centromere-kinetochore complexes throughout the cell cycle. Colocalizes with inner kinetochore plate proteins CENPA and CENPC during both interphase and metaphase.

GO - Cellular componenti

  • condensed chromosome kinetochore Source: UniProtKB-SubCell
  • kinetochore Source: MGI
  • nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Centromere, Chromosome, Kinetochore, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 241241Centromere protein HPRO_0000089479Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionineBy similarity

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiQ9QYM8.
PaxDbiQ9QYM8.
PRIDEiQ9QYM8.

PTM databases

PhosphoSiteiQ9QYM8.

Expressioni

Tissue specificityi

Abundantly expressed in thymus, spleen, uterus, ovary, testis and muscle, and weakly expressed in small intestine, lung and stomach. Barely detectable expression in kidney, liver, skin and prostate gland. Not detected in brain, heart or adrenal gland. Also expressed weakly in various hematopoietic cell lines.1 Publication

Developmental stagei

Abundantly expressed between embryonic day 9.5 and 12.5.1 Publication

Gene expression databases

BgeeiQ9QYM8.
CleanExiMM_CENPH.
GenevisibleiQ9QYM8. MM.

Interactioni

Subunit structurei

Self-associates. Component of the CENPA-NAC complex, at least composed of CENPA, CENPC, CENPH, CENPM, CENPN, CENPT and CENPU. The CENPA-NAC complex interacts with the CENPA-CAD complex, composed of CENPI, CENPK, CENPL, CENPO, CENPP, CENPQ, CENPR and CENPS (By similarity). Interacts directly with CENPK (By similarity). Interacts with KIF2C and NDC80 (By similarity). Interacts with TRIM36.By similarity1 Publication

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000074988.

Structurei

3D structure databases

ProteinModelPortaliQ9QYM8.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili28 – 186159Sequence AnalysisAdd
BLAST

Sequence similaritiesi

Belongs to the centromere protein H family.Sequence Analysis

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiNOG10470.
GeneTreeiENSGT00390000009578.
HOGENOMiHOG000013068.
HOVERGENiHBG081083.
InParanoidiQ9QYM8.
KOiK11500.
OMAiLMDNMKH.
OrthoDBiEOG7JQBRQ.
PhylomeDBiQ9QYM8.
TreeFamiTF101134.

Family and domain databases

InterProiIPR008426. CENP-H.
[Graphical view]
PfamiPF05837. CENP-H. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9QYM8-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MEEQPRERSE AGAEACEEKR GLSQAAEERI EDRISLLLRL RAQTKQQLLE
60 70 80 90 100
YKSMIDTNEE KTPEQIMQEK QIEVKIEELE NEIEDVKSNI EMKSLALSRM
110 120 130 140 150
KLSVALRDNM ENMGPENCVL TDDMKHILKL QKLIMKSQEE SSELEKKLLD
160 170 180 190 200
VRKKRLQLKQ ASRSKLLEIQ IEKNKQKEDV DKMENSEMIK TMKKKLQTEI
210 220 230 240
KITTVVQHTF QGLILASKTN WAEDPALRET VLQLEKDLNT L
Length:241
Mass (Da):28,135
Last modified:May 1, 2000 - v1
Checksum:iA56CD10AFE07D0AD
GO

Sequence cautioni

The sequence BAB27505.1 differs from that shown. Reason: Frameshift at position 195. Curated
The sequence BAB27810.1 differs from that shown. Reason: Frameshift at position 195. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti239 – 2391N → T in AAH25084 (PubMed:15489334).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB017634 mRNA. Translation: BAA88520.1.
AK011264 mRNA. Translation: BAB27505.1. Frameshift.
AK011738 mRNA. Translation: BAB27810.1. Frameshift.
BC025084 mRNA. Translation: AAH25084.1.
CCDSiCCDS26738.1.
RefSeqiNP_068686.1. NM_021886.1.
UniGeneiMm.273502.

Genome annotation databases

EnsembliENSMUST00000075550; ENSMUSP00000074988; ENSMUSG00000045273.
GeneIDi26886.
KEGGimmu:26886.
UCSCiuc007rrn.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB017634 mRNA. Translation: BAA88520.1.
AK011264 mRNA. Translation: BAB27505.1. Frameshift.
AK011738 mRNA. Translation: BAB27810.1. Frameshift.
BC025084 mRNA. Translation: AAH25084.1.
CCDSiCCDS26738.1.
RefSeqiNP_068686.1. NM_021886.1.
UniGeneiMm.273502.

3D structure databases

ProteinModelPortaliQ9QYM8.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000074988.

PTM databases

PhosphoSiteiQ9QYM8.

Proteomic databases

MaxQBiQ9QYM8.
PaxDbiQ9QYM8.
PRIDEiQ9QYM8.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000075550; ENSMUSP00000074988; ENSMUSG00000045273.
GeneIDi26886.
KEGGimmu:26886.
UCSCiuc007rrn.1. mouse.

Organism-specific databases

CTDi64946.
MGIiMGI:1349448. Cenph.

Phylogenomic databases

eggNOGiNOG10470.
GeneTreeiENSGT00390000009578.
HOGENOMiHOG000013068.
HOVERGENiHBG081083.
InParanoidiQ9QYM8.
KOiK11500.
OMAiLMDNMKH.
OrthoDBiEOG7JQBRQ.
PhylomeDBiQ9QYM8.
TreeFamiTF101134.

Enzyme and pathway databases

ReactomeiREACT_286371. Deposition of new CENPA-containing nucleosomes at the centromere.
REACT_306375. Mitotic Prometaphase.
REACT_321346. Separation of Sister Chromatids.
REACT_329805. Resolution of Sister Chromatid Cohesion.
REACT_358264. RHO GTPases Activate Formins.

Miscellaneous databases

NextBioi304703.
PROiQ9QYM8.
SOURCEiSearch...

Gene expression databases

BgeeiQ9QYM8.
CleanExiMM_CENPH.
GenevisibleiQ9QYM8. MM.

Family and domain databases

InterProiIPR008426. CENP-H.
[Graphical view]
PfamiPF05837. CENP-H. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Characterization of a novel kinetochore protein, CENP-H."
    Sugata N., Munekata E., Todokoro K.
    J. Biol. Chem. 274:27343-27346(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
  2. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6JImported.
    Tissue: EmbryoImported.
  3. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: Czech IIImported.
    Tissue: Mammary glandImported.
  4. "TRIM36 interacts with the kinetochore protein CENP-H and delays cell cycle progression."
    Miyajima N., Maruyama S., Nonomura K., Hatakeyama S.
    Biochem. Biophys. Res. Commun. 381:383-387(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH TRIM36.

Entry informationi

Entry nameiCENPH_MOUSE
AccessioniPrimary (citable) accession number: Q9QYM8
Secondary accession number(s): Q8R3K9, Q9D079, Q9D0N1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 8, 2005
Last sequence update: May 1, 2000
Last modified: June 24, 2015
This is version 88 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.