CENPT_MOUSE
ID CENPT_MOUSE Reviewed; 515 AA.
AC Q3TJM4; Q3TPY6; Q3UPD2; Q8BTH0; Q8BTP2; Q8R5E9;
DT 03-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 03-OCT-2006, sequence version 2.
DT 03-AUG-2022, entry version 127.
DE RecName: Full=Centromere protein T;
DE Short=CENP-T;
GN Name=Cenpt;
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].
RC STRAIN=C57BL/6J; TISSUE=Lung, Placenta, and Spleen;
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].
RC STRAIN=FVB/N; TISSUE=Mammary tumor;
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-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. Part of a
CC nucleosome-associated complex that binds specifically to histone H3-
CC containing nucleosomes at the centromere, as opposed to nucleosomes
CC containing CENPA. Component of the heterotetrameric CENP-T-W-S-X
CC complex that binds and supercoils DNA, and plays an important role in
CC kinetochore assembly. CENPT has a fundamental role in kinetochore
CC assembly and function. It is one of the inner kinetochore proteins,
CC with most further proteins binding downstream. Required for normal
CC chromosome organization and normal progress through mitosis.
CC {ECO:0000250|UniProtKB:Q96BT3}.
CC -!- SUBUNIT: Component of the CENPA-CAD complex, composed of CENPI, CENPK,
CC CENPL, CENPO, CENPP, CENPQ, CENPR and CENPS. The CENPA-CAD complex is
CC probably recruited on centromeres by the CENPA-NAC complex, at least
CC composed of CENPA, CENPC, CENPH, CENPM, CENPN, CENPT and CENPU.
CC Identified in a centromeric complex containing histones H2A, H2B, H3
CC and H4, and at least CENPA, CENPB, CENPC, CENPT, CENPN, HJURP, SUPT16H,
CC SSRP1 and RSF1. Interacts (via N-terminus) with the NDC80 complex.
CC Heterodimer with CENPW; this dimer coassembles with CENPS-CENPX
CC heterodimers at centromeres to form the tetrameric CENP-T-W-S-X
CC complex. {ECO:0000250|UniProtKB:Q96BT3}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q96BT3}.
CC Chromosome, centromere {ECO:0000250|UniProtKB:Q96BT3}. Chromosome,
CC centromere, kinetochore {ECO:0000250|UniProtKB:Q96BT3}.
CC Note=Constitutively localizes to centromeres throughout the cell cycle,
CC and to kinetochores during mitosis. Localizes to the inner kinetochore,
CC and may connect it to the outer kinetochore via its N-terminus.
CC {ECO:0000250|UniProtKB:Q96BT3}.
CC -!- DOMAIN: The largest part of the sequence forms an elongated and
CC flexible stalk structure that is connected to a C-terminal globular
CC domain with a histone-type fold. {ECO:0000250}.
CC -!- PTM: Dynamically phosphorylated during the cell cycle. Phosphorylated
CC during G2 phase, metaphase and anaphase, but not during telophase or G1
CC phase. {ECO:0000250|UniProtKB:Q96BT3}.
CC -!- SIMILARITY: Belongs to the CENP-T/CNN1 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC40776.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AK089172; BAC40776.1; ALT_FRAME; mRNA.
DR EMBL; AK090340; BAC41176.1; -; mRNA.
DR EMBL; AK143613; BAE25464.1; -; mRNA.
DR EMBL; AK164039; BAE37599.1; -; mRNA.
DR EMBL; AK167376; BAE39471.1; -; mRNA.
DR EMBL; BC022690; AAH22690.1; -; mRNA.
DR EMBL; BC121824; AAI21825.1; -; mRNA.
DR CCDS; CCDS22615.1; -.
DR RefSeq; NP_796124.1; NM_177150.2.
DR RefSeq; XP_011246709.1; XM_011248407.1.
DR AlphaFoldDB; Q3TJM4; -.
DR SMR; Q3TJM4; -.
DR ComplexPortal; CPX-5704; Kinetochore CCAN complex.
DR STRING; 10090.ENSMUSP00000038188; -.
DR iPTMnet; Q3TJM4; -.
DR PhosphoSitePlus; Q3TJM4; -.
DR EPD; Q3TJM4; -.
DR jPOST; Q3TJM4; -.
DR MaxQB; Q3TJM4; -.
DR PaxDb; Q3TJM4; -.
DR PeptideAtlas; Q3TJM4; -.
DR PRIDE; Q3TJM4; -.
DR ProteomicsDB; 283882; -.
DR Antibodypedia; 29639; 99 antibodies from 24 providers.
DR DNASU; 320394; -.
DR Ensembl; ENSMUST00000040776; ENSMUSP00000038188; ENSMUSG00000036672.
DR GeneID; 320394; -.
DR KEGG; mmu:320394; -.
DR UCSC; uc009nef.1; mouse.
DR CTD; 80152; -.
DR MGI; MGI:2443939; Cenpt.
DR VEuPathDB; HostDB:ENSMUSG00000036672; -.
DR eggNOG; ENOG502RZH1; Eukaryota.
DR GeneTree; ENSGT00390000003044; -.
DR HOGENOM; CLU_040180_0_0_1; -.
DR InParanoid; Q3TJM4; -.
DR OMA; HHQFPEP; -.
DR OrthoDB; 360139at2759; -.
DR PhylomeDB; Q3TJM4; -.
DR TreeFam; TF332946; -.
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; 320394; 9 hits in 71 CRISPR screens.
DR ChiTaRS; Cenpt; mouse.
DR PRO; PR:Q3TJM4; -.
DR Proteomes; UP000000589; Chromosome 8.
DR RNAct; Q3TJM4; protein.
DR Bgee; ENSMUSG00000036672; Expressed in yolk sac and 227 other tissues.
DR ExpressionAtlas; Q3TJM4; baseline and differential.
DR Genevisible; Q3TJM4; MM.
DR GO; GO:0000775; C:chromosome, centromeric region; ISS:UniProtKB.
DR GO; GO:0000776; C:kinetochore; ISO:MGI.
DR GO; GO:0016604; C:nuclear body; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0046982; F:protein heterodimerization activity; IEA:InterPro.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0051276; P:chromosome organization; ISS:UniProtKB.
DR GO; GO:0007059; P:chromosome segregation; ISS:UniProtKB.
DR GO; GO:0051382; P:kinetochore assembly; ISS:UniProtKB.
DR GO; GO:0000278; P:mitotic cell cycle; ISS:UniProtKB.
DR Gene3D; 1.10.20.10; -; 1.
DR InterPro; IPR028255; CENP-T.
DR InterPro; IPR035425; CENP-T/H4_C.
DR InterPro; IPR032373; CENP-T_N.
DR InterPro; IPR009072; Histone-fold.
DR PANTHER; PTHR46904; PTHR46904; 2.
DR Pfam; PF15511; CENP-T_C; 1.
DR Pfam; PF16171; CENP-T_N; 1.
DR SUPFAM; SSF47113; SSF47113; 1.
PE 2: Evidence at transcript level;
KW Cell cycle; Cell division; Centromere; Chromosome; DNA-binding;
KW Kinetochore; Mitosis; Nucleus; Phosphoprotein; Reference proteome.
FT CHAIN 1..515
FT /note="Centromere protein T"
FT /id="PRO_0000249516"
FT REGION 24..156
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 94..375
FT /note="Flexible stalk domain"
FT /evidence="ECO:0000250"
FT REGION 271..411
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 40..71
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 296..310
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 348..369
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 86
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q96BT3"
FT MOD_RES 313
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q561R1"
FT MOD_RES 333
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96BT3"
FT MOD_RES 345
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96BT3"
FT MOD_RES 346
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96BT3"
FT MOD_RES 357
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96BT3"
FT MOD_RES 376
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q561R1"
FT CONFLICT 5
FT /note="S -> V (in Ref. 1; BAE25464)"
FT /evidence="ECO:0000305"
FT CONFLICT 157
FT /note="K -> R (in Ref. 1; BAE39471)"
FT /evidence="ECO:0000305"
FT CONFLICT 302..303
FT /note="QS -> KG (in Ref. 1; BAC40776)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 515 AA; 56242 MW; C736E7FA30E6206B CRC64;
MADLSFSDGD PTVRTLLRRV LETADSRTPM RRRSTRINAQ RRRSQTPYSN RQGSQTKTSA
RKQSHGARSV GRSTRVQGRG RLEEQTPRTL LRNILLTAPE SSTVMPDPVV KPAQVPEVAR
SSRRESSRGS LELHLPELEP PSTLAPGLTA PGKRKQKLRL SVFQQEVDQG LPLSQEPRRS
RSADVSSLAS SFNLTFVLPG QPETVERPGL ARRRPIRQLV NAGALLQDLE DNSLASALPG
DSHRTPVAAL PMDVGLEDTQ PFSQSLAAFS LSGKHSLPSP SRPGVEDVER VMGPPSSGTR
LQSRMSRSGP AASPSPFLEP QPPPAEPREA VGSNEAAEPK DQEGSSGYEE TSARPASGEL
SSSTHDSLPA EQPPPSPGVA VLSSEPLESV TAKCPSRTQT AGPRRRQDPH KAGLSPYVKF
FSFCTKMPVE KTALEIVEKC LDKYFQHLCN DLEVFASHAG RKIVKPEDLL LLMRRQGLVT
DQVSQHVLVE RYLPLEYRQQ LIPCAFSGNS VFPAQ
