CENPQ_MOUSE
ID CENPQ_MOUSE Reviewed; 267 AA.
AC Q9CPQ5; Q8C2G4; Q8VEF8; Q9CX70;
DT 05-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 02-NOV-2016, sequence version 2.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=Centromere protein Q;
DE Short=CENP-Q;
GN Name=Cenpq;
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 [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J, and NOD; TISSUE=Embryo, Forelimb, and Thymus;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=Czech II; TISSUE=Mammary gland;
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. Plays an
CC important role in chromosome congression and in the recruitment of
CC CENP-O complex (which comprises CENPO, CENPP, CENPQ and CENPU), CENPE
CC and PLK1 to the kinetochores. {ECO:0000250|UniProtKB:Q7L2Z9}.
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.
CC {ECO:0000250|UniProtKB:Q7L2Z9}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q7L2Z9}.
CC Chromosome, centromere {ECO:0000250|UniProtKB:Q7L2Z9}. Note=Localizes
CC exclusively in the centromeres. The CENPA-CAD complex is probably
CC recruited on centromeres by the CENPA-NAC complex.
CC {ECO:0000250|UniProtKB:Q7L2Z9}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9CPQ5-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9CPQ5-2; Sequence=VSP_020451, VSP_020452;
CC -!- PTM: Phosphorylation at Ser-49 is essential for CENPE recruitment to
CC kinetochores and orderly chromosome congression.
CC {ECO:0000250|UniProtKB:Q7L2Z9}.
CC -!- SIMILARITY: Belongs to the CENP-Q/OKP1 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB27968.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAB28080.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAB31976.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAB31976.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=BAC36178.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAC40501.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AK011998; BAB27968.1; ALT_INIT; mRNA.
DR EMBL; AK012179; BAB28080.1; ALT_INIT; mRNA.
DR EMBL; AK020040; BAB31976.1; ALT_SEQ; mRNA.
DR EMBL; AK076094; BAC36178.1; ALT_INIT; mRNA.
DR EMBL; AK088680; BAC40501.1; ALT_INIT; mRNA.
DR EMBL; BC018524; AAH18524.1; -; mRNA.
DR CCDS; CCDS28789.1; -. [Q9CPQ5-1]
DR RefSeq; NP_114069.1; NM_031863.3. [Q9CPQ5-1]
DR AlphaFoldDB; Q9CPQ5; -.
DR SMR; Q9CPQ5; -.
DR BioGRID; 219980; 14.
DR ComplexPortal; CPX-5704; Kinetochore CCAN complex.
DR CORUM; Q9CPQ5; -.
DR IntAct; Q9CPQ5; 9.
DR MINT; Q9CPQ5; -.
DR STRING; 10090.ENSMUSP00000084353; -.
DR PhosphoSitePlus; Q9CPQ5; -.
DR EPD; Q9CPQ5; -.
DR MaxQB; Q9CPQ5; -.
DR PaxDb; Q9CPQ5; -.
DR PeptideAtlas; Q9CPQ5; -.
DR PRIDE; Q9CPQ5; -.
DR ProteomicsDB; 281188; -. [Q9CPQ5-1]
DR ProteomicsDB; 281189; -. [Q9CPQ5-2]
DR Antibodypedia; 30817; 157 antibodies from 25 providers.
DR DNASU; 83815; -.
DR Ensembl; ENSMUST00000087114; ENSMUSP00000084353; ENSMUSG00000023919. [Q9CPQ5-1]
DR GeneID; 83815; -.
DR KEGG; mmu:83815; -.
DR UCSC; uc008con.1; mouse. [Q9CPQ5-1]
DR CTD; 55166; -.
DR MGI; MGI:1933744; Cenpq.
DR VEuPathDB; HostDB:ENSMUSG00000023919; -.
DR eggNOG; ENOG502S34R; Eukaryota.
DR GeneTree; ENSGT00390000005599; -.
DR HOGENOM; CLU_085740_0_0_1; -.
DR InParanoid; Q9CPQ5; -.
DR OMA; VFIEEAY; -.
DR OrthoDB; 1159538at2759; -.
DR TreeFam; TF336238; -.
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; 83815; 8 hits in 72 CRISPR screens.
DR ChiTaRS; Cenpq; mouse.
DR PRO; PR:Q9CPQ5; -.
DR Proteomes; UP000000589; Chromosome 17.
DR RNAct; Q9CPQ5; protein.
DR Bgee; ENSMUSG00000023919; Expressed in primary oocyte and 228 other tissues.
DR ExpressionAtlas; Q9CPQ5; baseline and differential.
DR Genevisible; Q9CPQ5; MM.
DR GO; GO:0015629; C:actin cytoskeleton; ISO:MGI.
DR GO; GO:0031511; C:Mis6-Sim4 complex; IBA:GO_Central.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0051310; P:metaphase plate congression; ISS:UniProtKB.
DR GO; GO:1905342; P:positive regulation of protein localization to kinetochore; ISS:UniProtKB.
DR InterPro; IPR025212; CAD_CENP-Q.
DR PANTHER; PTHR31345; PTHR31345; 1.
DR Pfam; PF13094; CENP-Q; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; Centromere; Chromosome; Coiled coil; Nucleus;
KW Phosphoprotein; Reference proteome.
FT CHAIN 1..267
FT /note="Centromere protein Q"
FT /id="PRO_0000089535"
FT REGION 1..54
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 100..202
FT /evidence="ECO:0000255"
FT COMPBIAS 1..18
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 19..40
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 49
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q7L2Z9"
FT VAR_SEQ 118..126
FT /note="LQQCATLKV -> CIVVIILFR (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_020451"
FT VAR_SEQ 127..267
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_020452"
FT CONFLICT 2
FT /note="S -> EIA (in Ref. 2; AAH18524)"
FT /evidence="ECO:0000305"
FT CONFLICT 105
FT /note="E -> Q (in Ref. 2; AAH18524)"
FT /evidence="ECO:0000305"
FT CONFLICT 159
FT /note="Q -> P (in Ref. 1; BAB31976)"
FT /evidence="ECO:0000305"
FT CONFLICT 163
FT /note="D -> A (in Ref. 1; BAB31976)"
FT /evidence="ECO:0000305"
FT CONFLICT 168..169
FT /note="TT -> AP (in Ref. 1; BAB31976)"
FT /evidence="ECO:0000305"
FT CONFLICT 179
FT /note="L -> V (in Ref. 1; BAB31976)"
FT /evidence="ECO:0000305"
FT CONFLICT 187
FT /note="T -> A (in Ref. 1; BAB31976)"
FT /evidence="ECO:0000305"
FT CONFLICT 219
FT /note="L -> F (in Ref. 1; BAB31976)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 267 AA; 30501 MW; 022A8F262DAFF78E CRC64;
MSGKARASRK KPQQVKRSLK QRANKEADLP ENEVGNTAKR NRSHAKHLSS KVTGQATYVH
LKRVKISSSK RTTWQPLPKD TEEYLQSMME SVILGILFNI KRKEEIQCHL NQLKKRLLQQ
CATLKVPPRK LNYLKDVSKM LKMEKAQERA NEESLASLQE EIDKIVETTE SMTESIQSLK
NKIQILTSEV EEEEQEVKQV FHIDSNKVLA LPELSQKSLK APILQEEILA LIPNQNALLK
DLDVLHDSAP VKNVSAFIEE AYKKLDS
