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Histone H3-like centromeric protein A (Centromere protein A) (CENP-A)

 CENPA_MOUSE             Reviewed;         134 AA.
O35216; Q545C9;
15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
01-JAN-1998, sequence version 1.
12-SEP-2018, entry version 137.
RecName: Full=Histone H3-like centromeric protein A;
AltName: Full=Centromere protein A;
Short=CENP-A;
Name=Cenpa;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
STRAIN=129/Sv, and C57BL/6J;
PubMed=9465302; DOI=10.1006/geno.1997.5109;
Kalitsis P., Macdonald A.C., Newson A.J., Hudson D.F., Choo K.H.A.;
"Gene structure and sequence analysis of mouse centromere proteins A
and C.";
Genomics 47:108-114(1998).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J, and NOD; TISSUE=Eye, and Thymus;
PubMed=16141072; DOI=10.1126/science.1112014;
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.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=Czech II; TISSUE=Mammary gland;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[4]
POLY-ADP-RIBOSYLATION BY PARP1.
PubMed=12011073; DOI=10.1074/jbc.M200620200;
Saxena A., Saffery R., Wong L.H., Kalitsis P., Choo K.H.;
"Centromere proteins Cenpa, Cenpb, and Bub3 interact with poly(ADP-
ribose) polymerase-1 protein and are poly(ADP-ribosyl)ated.";
J. Biol. Chem. 277:26921-26926(2002).
[5]
FUNCTION.
PubMed=27499292; DOI=10.1016/j.molcel.2016.06.023;
Roulland Y., Ouararhni K., Naidenov M., Ramos L., Shuaib M.,
Syed S.H., Lone I.N., Boopathi R., Fontaine E., Papai G.,
Tachiwana H., Gautier T., Skoufias D., Padmanabhan K., Bednar J.,
Kurumizaka H., Schultz P., Angelov D., Hamiche A., Dimitrov S.;
"The flexible ends of CENP-A nucleosome are required for mitotic
fidelity.";
Mol. Cell 63:674-685(2016).
-!- FUNCTION: Histone H3-like nucleosomal protein that is specifically
found in centromeric nucleosomes. Replaces conventional H3 in the
nucleosome core of centromeric chromatin at the inner plate of the
kinetochore. The presence of CENPA subtly modifies the nucleosome
structure and the way DNA is wrapped around the nucleosome and
gives rise to protruding DNA ends that are less well-ordered and
rigid compared to nucleosomes containing histone H3. May serve as
an epigenetic mark that propagates centromere identity through
replication and cell division (By similarity). Required for
recruitment and assembly of kinetochore proteins, and as a
consequence required for progress through mitosis, chromosome
segregation and cytokinesis (PubMed:27499292).
{ECO:0000250|UniProtKB:P49450, ECO:0000269|PubMed:27499292}.
-!- SUBUNIT: Component of centromeric nucleosomes, where DNA is
wrapped around a histone octamer core. The octamer contains two
molecules each of H2A, H2B, CENPA and H4 assembled in one CENPA-H4
heterotetramer and two H2A-H2B heterodimers. CENPA modulates the
DNA-binding characteristics of nucleosomes so that protruding DNA
ends have higher flexibility than in nucleosomes containing
conventional histone H3. Inhibits binding of histone H1 to
nucleosomes, since histone H1 binds preferentially to rigid DNA
linkers that protrude from nucleosomes. Nucleosomes containing
CENPA also contain histone H2A variants such as macroH2A H2AFY and
H2A.Z/H2AFZ. The CENPA-H4 heterotetramer is more compact and
structurally more rigid than corresponding H3-H4 heterotetramers.
Can assemble into nucleosomes that contain both CENPA and histone
H3.3; these nucleosomes interact with a single CENPC chain.
Heterotrimer composed of HJURP, CENPA and histone H4, where HJURP
interacts with the dimer formed by CENPA and histone H4 and
prevents tetramerization of CENPA and H4. Component of the CENPA-
NAC complex, at least composed of CENPA, CENPC, CENPH, CENPM,
CENPN, CENPT and CENPU. Interacts (via CATD domain) with HJURP;
the interaction is direct and is required for its localization to
centromeres. Interacts with CENPC, CENPN and CENPT; interaction is
direct. Part of a centromere complex consisting of CENPA, CENPT
and CENPW. Identified in centromere complexes containing histones
H2A, H2B and H4, and at least CENPA, CENPB, CENPC, CENPT, CENPN,
HJURP, SUPT16H, SSRP1 and RSF1. Can self-associate. The CENPA-H4
heterotetramer can bind DNA by itself (in vitro). Interacts with
CDK1, PPP1CA and RBBP7. {ECO:0000250|UniProtKB:P49450}.
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P49450}.
Chromosome, centromere, kinetochore
{ECO:0000250|UniProtKB:P49450}. Chromosome, centromere
{ECO:0000250|UniProtKB:P49450}. Note=Localizes exclusively in the
kinetochore domain of centromeres. Occupies a compact domain at
the inner kinetochore plate stretching across 2 thirds of the
length of the constriction but encompassing only one third of the
constriction width and height. Phosphorylation at Ser-62 during
early mitosis abolishes association with chromatin and centromeres
and results in dispersed nuclear location.
{ECO:0000250|UniProtKB:P49450}.
-!- DOMAIN: The CATD (CENPA targeting domain) region is responsible
for the more compact structure of nucleosomes containing CENPA. It
is necessary and sufficient to mediate the localization into
centromeres. {ECO:0000250|UniProtKB:P49450}.
-!- PTM: Poly-ADP-ribosylated by PARP1.
-!- PTM: Trimethylated by NTMT1 at the N-terminal glycine after
cleavage of Met-1. Methylation is low before incorporation into
nucleosomes and increases with cell cycle progression, with the
highest levels in mitotic nucleosomes.
{ECO:0000250|UniProtKB:P49450}.
-!- PTM: Phosphorylated by CDK1 at Ser-62 during early mitosis; this
abolishes association with chromatin and centromeres, prevents
interaction with HJURP and thereby prevents premature assembly of
CENPA into centromeres. Dephosphorylated at Ser-62 by PPP1CA
during late mitosis. {ECO:0000250|UniProtKB:P49450}.
-!- SIMILARITY: Belongs to the histone H3 family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; AF012709; AAC39957.1; -; mRNA.
EMBL; AF012710; AAC39958.1; -; Genomic_DNA.
EMBL; AK010718; BAB27140.1; -; mRNA.
EMBL; AK011399; BAB27591.1; -; mRNA.
EMBL; AK053763; BAC35512.1; -; mRNA.
EMBL; AK089033; BAC40710.1; -; mRNA.
EMBL; BC011038; AAH11038.1; -; mRNA.
CCDS; CCDS19162.1; -.
RefSeq; NP_001289058.1; NM_001302129.1.
RefSeq; NP_001289059.1; NM_001302130.1.
RefSeq; NP_001289060.1; NM_001302131.1.
RefSeq; NP_001289061.1; NM_001302132.1.
RefSeq; NP_031707.1; NM_007681.3.
UniGene; Mm.290563; -.
ProteinModelPortal; O35216; -.
SMR; O35216; -.
IntAct; O35216; 2.
MINT; O35216; -.
STRING; 10090.ENSMUSP00000122831; -.
iPTMnet; O35216; -.
PhosphoSitePlus; O35216; -.
MaxQB; O35216; -.
PaxDb; O35216; -.
PeptideAtlas; O35216; -.
PRIDE; O35216; -.
Ensembl; ENSMUST00000144742; ENSMUSP00000122831; ENSMUSG00000029177.
GeneID; 12615; -.
KEGG; mmu:12615; -.
UCSC; uc008wvt.2; mouse.
CTD; 1058; -.
MGI; MGI:88375; Cenpa.
eggNOG; KOG1745; Eukaryota.
eggNOG; COG2036; LUCA.
GeneTree; ENSGT00910000144321; -.
HOVERGEN; HBG001172; -.
InParanoid; O35216; -.
KO; K11495; -.
OMA; VHLFEDC; -.
OrthoDB; EOG091G13T2; -.
PhylomeDB; O35216; -.
TreeFam; TF354293; -.
Reactome; R-MMU-141444; Amplification of signal from unattached kinetochores via a MAD2 inhibitory signal.
Reactome; R-MMU-2467813; Separation of Sister Chromatids.
Reactome; R-MMU-2500257; Resolution of Sister Chromatid Cohesion.
Reactome; R-MMU-5663220; RHO GTPases Activate Formins.
Reactome; R-MMU-606279; Deposition of new CENPA-containing nucleosomes at the centromere.
Reactome; R-MMU-68877; Mitotic Prometaphase.
PRO; PR:O35216; -.
Proteomes; UP000000589; Chromosome 5.
Bgee; ENSMUSG00000029177; Expressed in 218 organ(s), highest expression level in urogenital fold.
CleanEx; MM_CENPA; -.
ExpressionAtlas; O35216; baseline and differential.
Genevisible; O35216; MM.
GO; GO:0000775; C:chromosome, centromeric region; IDA:MGI.
GO; GO:0000939; C:condensed chromosome inner kinetochore; IDA:MGI.
GO; GO:0000778; C:condensed nuclear chromosome kinetochore; ISO:MGI.
GO; GO:0000780; C:condensed nuclear chromosome, centromeric region; IDA:MGI.
GO; GO:0000788; C:nuclear nucleosome; ISO:MGI.
GO; GO:0031618; C:nuclear pericentric heterochromatin; IDA:MGI.
GO; GO:0005654; C:nucleoplasm; ISO:MGI.
GO; GO:0000786; C:nucleosome; IBA:GO_Central.
GO; GO:0005634; C:nucleus; ISO:MGI.
GO; GO:0031492; F:nucleosomal DNA binding; IBA:GO_Central.
GO; GO:0046982; F:protein heterodimerization activity; IEA:InterPro.
GO; GO:0000132; P:establishment of mitotic spindle orientation; ISO:MGI.
GO; GO:0051382; P:kinetochore assembly; ISO:MGI.
GO; GO:0000281; P:mitotic cytokinesis; ISO:MGI.
GO; GO:0006334; P:nucleosome assembly; IBA:GO_Central.
GO; GO:0071459; P:protein localization to chromosome, centromeric region; ISO:MGI.
Gene3D; 1.10.20.10; -; 1.
InterPro; IPR009072; Histone-fold.
InterPro; IPR007125; Histone_H2A/H2B/H3.
InterPro; IPR000164; Histone_H3/CENP-A.
PANTHER; PTHR11426; PTHR11426; 1.
Pfam; PF00125; Histone; 1.
PRINTS; PR00622; HISTONEH3.
SMART; SM00428; H3; 1.
SUPFAM; SSF47113; SSF47113; 1.
2: Evidence at transcript level;
ADP-ribosylation; Centromere; Chromosome; Complete proteome;
DNA-binding; Kinetochore; Methylation; Nucleosome core; Nucleus;
Phosphoprotein; Reference proteome.
INIT_MET 1 1 Removed. {ECO:0000250|UniProtKB:P49450}.
CHAIN 2 134 Histone H3-like centromeric protein A.
/FTId=PRO_0000221374.
REGION 34 48 Important for flexibility of DNA ends
that protrude from nucleosomes.
{ECO:0000250|UniProtKB:P49450}.
REGION 35 134 H3-like.
REGION 69 110 CATD.
MOD_RES 2 2 N,N,N-trimethylglycine.
{ECO:0000250|UniProtKB:P49450}.
MOD_RES 16 16 Phosphoserine.
{ECO:0000250|UniProtKB:P49450}.
MOD_RES 22 22 Phosphoserine.
{ECO:0000250|UniProtKB:P49450}.
MOD_RES 62 62 Phosphoserine.
{ECO:0000250|UniProtKB:P49450}.
SEQUENCE 134 AA; 15509 MW; 0381FA6492E43C3D CRC64;
MGPRRKPQTP RRRPSSPAPG PSRQSSSVGS QTLRRRQKFM WLKEIKTLQK STDLLFRKKP
FSMVVREICE KFSRGVDFWW QAQALLALQE AAEAFLIHLF EDAYLLSLHA GRVTLFPKDI
QLTRRIRGFE GGLP


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