CENPX_MOUSE
ID CENPX_MOUSE Reviewed; 78 AA.
AC Q8C4X1; A2AC08; O08693; O08694; O08695; Q8BPD7;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 136.
DE RecName: Full=Centromere protein X;
DE Short=CENP-X;
DE AltName: Full=FANCM-interacting histone fold protein 2;
DE AltName: Full=Fanconi anemia-associated polypeptide of 10 kDa;
DE AltName: Full=Immediate-early-response protein D9;
DE AltName: Full=Retinoic acid-inducible gene D9 protein;
DE AltName: Full=Stimulated by retinoic acid gene 13 protein homolog;
GN Name=Cenpx; Synonyms=Faap10, Mhf2, Stra13;
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] (ISOFORMS 1; 2 AND 3), AND INDUCTION.
RC STRAIN=MDF1;
RX PubMed=8839844;
RA Scott L.M., Mueller L., Collins S.J.;
RT "E3, a hematopoietic-specific transcript directly regulated by the retinoic
RT acid receptor alpha.";
RL Blood 88:2517-2530(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 4).
RC STRAIN=C57BL/6J, and NOD; TISSUE=Cerebellum;
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 GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
CC -!- FUNCTION: DNA-binding component of the Fanconi anemia (FA) core
CC complex. Required for the normal activation of the FA pathway, leading
CC to monoubiquitination of the FANCI-FANCD2 complex in response to DNA
CC damage, cellular resistance to DNA cross-linking drugs, and prevention
CC of chromosomal breakage. In complex with CENPS (MHF heterodimer),
CC crucial cofactor for FANCM in both binding and ATP-dependent remodeling
CC of DNA. Stabilizes FANCM. In complex with CENPS and FANCM (but not
CC other FANC proteins), rapidly recruited to blocked forks and promotes
CC gene conversion at blocked replication forks. In complex with CENPS,
CC CENPT and CENPW (CENP-T-W-S-X heterotetramer), involved in the
CC formation of a functional kinetochore outer plate, which is essential
CC for kinetochore-microtubule attachment and faithful mitotic
CC progression. As a component of MHF and CENP-T-W-S-X complexes, binds
CC DNA and bends it to form a nucleosome-like structure. DNA-binding
CC function is fulfilled in the presence of CENPS, with the following
CC preference for DNA substates: Holliday junction > double-stranded >
CC splay arm > single-stranded. Does not bind DNA on its own.
CC {ECO:0000250|UniProtKB:A8MT69}.
CC -!- SUBUNIT: Heterodimer with CENPX, sometimes called MHF; this interaction
CC stabilizes both partners. MHF heterodimers can assemble to form
CC tetrameric structures. MHF also coassemble with CENPT-CENPW
CC heterodimers at centromeres to form the tetrameric CENP-T-W-S-X
CC complex. Forms a discrete complex with FANCM and CENPX, called FANCM-
CC MHF; this interaction, probably mediated by direct binding between
CC CENPS and FANCM, leads to synergistic activation of double-stranded DNA
CC binding and strongly stimulates FANCM-mediated DNA remodeling.
CC Recruited by FANCM to the Fanconi anemia (FA) core complex, which
CC consists of CENPS, CENPX, FANCA, FANCB, FANCC, FANCE, FANCF, FANCG,
CC FANCL, FANCM, FAAP24 and FAAP100. The FA core complex associates with
CC Bloom syndrome (BLM) complex, which consists of at least BLM, DNA
CC topoisomerase 3-alpha (TOP3A), RMI1/BLAP75, RPA1/RPA70 and RPA2/RPA32.
CC The super complex between FA and BLM is called BRAFT.
CC {ECO:0000250|UniProtKB:A8MT69}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:A8MT69}.
CC Chromosome, centromere {ECO:0000250|UniProtKB:A8MT69}. Chromosome,
CC centromere, kinetochore {ECO:0000250|UniProtKB:A8MT69}. Note=Assembly
CC of CENPS and CENPX and its partner subunits CENPT and CENPW at
CC centromeres occurs through a dynamic exchange mechanism. Although
CC exchange is continuous in the cell cycle, de novo assembly starts
CC principally during mid-late S phase and is complete by G2. CENPX being
CC less stably bound at the kinetochore than CENPS.
CC {ECO:0000250|UniProtKB:A8MT69}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1; Synonyms=Variant 2;
CC IsoId=Q8C4X1-1; Sequence=Displayed;
CC Name=2; Synonyms=Variant 3;
CC IsoId=Q8C4X1-2; Sequence=VSP_033950;
CC Name=3; Synonyms=Variant 1;
CC IsoId=Q8C4X1-3; Sequence=VSP_033951;
CC Name=4;
CC IsoId=Q8C4X1-4; Sequence=VSP_033952;
CC -!- INDUCTION: By retinoic acid. {ECO:0000269|PubMed:8839844}.
CC -!- SIMILARITY: Belongs to the CENP-X/MHF2 family. {ECO:0000305}.
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DR EMBL; U95003; AAB53635.1; -; mRNA.
DR EMBL; U95004; AAB53636.1; -; mRNA.
DR EMBL; U95005; AAB53637.1; -; mRNA.
DR EMBL; AK076181; BAC36237.1; -; mRNA.
DR EMBL; AK080500; BAC37933.1; -; mRNA.
DR EMBL; AK170126; BAE41581.1; -; mRNA.
DR EMBL; AL663030; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS49009.1; -. [Q8C4X1-1]
DR CCDS; CCDS83948.1; -. [Q8C4X1-4]
DR RefSeq; NP_001334540.1; NM_001347611.1. [Q8C4X1-4]
DR RefSeq; NP_057874.2; NM_016665.2. [Q8C4X1-1]
DR AlphaFoldDB; Q8C4X1; -.
DR SMR; Q8C4X1; -.
DR BioGRID; 203553; 1.
DR ComplexPortal; CPX-5704; Kinetochore CCAN complex.
DR STRING; 10090.ENSMUSP00000050335; -.
DR PhosphoSitePlus; Q8C4X1; -.
DR MaxQB; Q8C4X1; -.
DR PaxDb; Q8C4X1; -.
DR PeptideAtlas; Q8C4X1; -.
DR PRIDE; Q8C4X1; -.
DR ProteomicsDB; 281585; -. [Q8C4X1-1]
DR ProteomicsDB; 281586; -. [Q8C4X1-2]
DR ProteomicsDB; 281587; -. [Q8C4X1-3]
DR ProteomicsDB; 281588; -. [Q8C4X1-4]
DR DNASU; 20892; -.
DR Ensembl; ENSMUST00000026137; ENSMUSP00000026137; ENSMUSG00000025144. [Q8C4X1-4]
DR Ensembl; ENSMUST00000055424; ENSMUSP00000050335; ENSMUSG00000025144. [Q8C4X1-1]
DR GeneID; 20892; -.
DR KEGG; mmu:20892; -.
DR UCSC; uc007muc.1; mouse. [Q8C4X1-1]
DR UCSC; uc029rqh.1; mouse. [Q8C4X1-4]
DR CTD; 201254; -.
DR MGI; MGI:894324; Cenpx.
DR VEuPathDB; HostDB:ENSMUSG00000025144; -.
DR eggNOG; ENOG502S98G; Eukaryota.
DR GeneTree; ENSGT00960000191026; -.
DR HOGENOM; CLU_175684_0_0_1; -.
DR InParanoid; Q8C4X1; -.
DR OMA; AESEDCN; -.
DR OrthoDB; 1560521at2759; -.
DR TreeFam; TF330764; -.
DR Reactome; R-MMU-606279; Deposition of new CENPA-containing nucleosomes at the centromere.
DR Reactome; R-MMU-6783310; Fanconi Anemia Pathway.
DR BioGRID-ORCS; 20892; 2 hits in 71 CRISPR screens.
DR ChiTaRS; Stra13; mouse.
DR PRO; PR:Q8C4X1; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; Q8C4X1; protein.
DR Bgee; ENSMUSG00000025144; Expressed in animal zygote and 242 other tissues.
DR ExpressionAtlas; Q8C4X1; baseline and differential.
DR Genevisible; Q8C4X1; MM.
DR GO; GO:0000785; C:chromatin; ISO:MGI.
DR GO; GO:0071821; C:FANCM-MHF complex; ISS:UniProtKB.
DR GO; GO:0043240; C:Fanconi anaemia nuclear complex; ISS:UniProtKB.
DR GO; GO:0000776; C:kinetochore; IEA:UniProtKB-KW.
DR GO; GO:0003677; F:DNA binding; ISS:UniProtKB.
DR GO; GO:0003690; F:double-stranded DNA binding; ISO:MGI.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0036297; P:interstrand cross-link repair; ISO:MGI.
DR GO; GO:0051382; P:kinetochore assembly; IEA:InterPro.
DR GO; GO:0031297; P:replication fork processing; ISS:UniProtKB.
DR GO; GO:0000712; P:resolution of meiotic recombination intermediates; ISS:UniProtKB.
DR InterPro; IPR018552; CENP-X.
DR PANTHER; PTHR28680; PTHR28680; 1.
DR Pfam; PF09415; CENP-X; 1.
PE 2: Evidence at transcript level;
KW Acetylation; Alternative splicing; Cell cycle; Cell division; Centromere;
KW Chromosome; DNA damage; DNA repair; DNA-binding; Kinetochore; Mitosis;
KW Nucleus; Reference proteome.
FT CHAIN 1..78
FT /note="Centromere protein X"
FT /id="PRO_0000337181"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:A8MT69"
FT VAR_SEQ 9
FT /note="K -> KAIHFEGRGCLSLPTFCLSLVVPHSVLDYANLSGLGFTHCTDARGLL
FT MAHLWCSHGIPRPLDSPSHLHLTNYHQPFSSQAIPDAWPICRHHL (in isoform
FT 2)"
FT /evidence="ECO:0000303|PubMed:8839844"
FT /id="VSP_033950"
FT VAR_SEQ 9
FT /note="K -> KALDSPSHLHLTNYHQPFSSQAIPDAWSICRHHL (in isoform
FT 3)"
FT /evidence="ECO:0000303|PubMed:8839844"
FT /id="VSP_033951"
FT VAR_SEQ 26
FT /note="K -> KGLGHQWGGEYVGHREGGCPMTPPPSPFPP (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_033952"
FT CONFLICT 19
FT /note="H -> N (in Ref. 1; AAB53636)"
FT /evidence="ECO:0000305"
FT CONFLICT 43
FT /note="V -> G (in Ref. 1; AAB53636)"
FT /evidence="ECO:0000305"
FT CONFLICT 56
FT /note="A -> V (in Ref. 1; AAB53636)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 78 AA; 8926 MW; 4FF0546DDC3F3856 CRC64;
MEGNSGFRKE LVSRLLHLHF RDCKTKVSGD ALQLMAEFLR IFVLEAAVRG VWQAQAEDLD
VVEVDQLEKV LPQLLLDF
