CENPT_RAT
ID CENPT_RAT Reviewed; 518 AA.
AC Q561R1;
DT 19-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT 10-MAY-2005, sequence version 1.
DT 03-AUG-2022, entry version 122.
DE RecName: Full=Centromere protein T;
DE Short=CENP-T;
GN Name=Cenpt;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Thymus;
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).
RN [2]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-313; SER-324; SER-345;
RP SER-346 AND SER-382, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
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}.
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DR EMBL; BC093396; AAH93396.1; -; mRNA.
DR RefSeq; NP_001019428.1; NM_001024257.1.
DR AlphaFoldDB; Q561R1; -.
DR SMR; Q561R1; -.
DR STRING; 10116.ENSRNOP00000029297; -.
DR iPTMnet; Q561R1; -.
DR PhosphoSitePlus; Q561R1; -.
DR PaxDb; Q561R1; -.
DR PRIDE; Q561R1; -.
DR Ensembl; ENSRNOT00000036702; ENSRNOP00000029297; ENSRNOG00000024178.
DR GeneID; 307805; -.
DR KEGG; rno:307805; -.
DR UCSC; RGD:1309383; rat.
DR CTD; 80152; -.
DR RGD; 1309383; Cenpt.
DR eggNOG; ENOG502RZH1; Eukaryota.
DR GeneTree; ENSGT00390000003044; -.
DR HOGENOM; CLU_040180_0_0_1; -.
DR InParanoid; Q561R1; -.
DR OMA; HHQFPEP; -.
DR OrthoDB; 360139at2759; -.
DR PhylomeDB; Q561R1; -.
DR TreeFam; TF332946; -.
DR Reactome; R-RNO-141444; Amplification of signal from unattached kinetochores via a MAD2 inhibitory signal.
DR Reactome; R-RNO-2467813; Separation of Sister Chromatids.
DR Reactome; R-RNO-2500257; Resolution of Sister Chromatid Cohesion.
DR Reactome; R-RNO-5663220; RHO GTPases Activate Formins.
DR Reactome; R-RNO-606279; Deposition of new CENPA-containing nucleosomes at the centromere.
DR Reactome; R-RNO-68877; Mitotic Prometaphase.
DR Reactome; R-RNO-9648025; EML4 and NUDC in mitotic spindle formation.
DR PRO; PR:Q561R1; -.
DR Proteomes; UP000002494; Chromosome 19.
DR Bgee; ENSRNOG00000024178; Expressed in testis and 16 other tissues.
DR Genevisible; Q561R1; RN.
DR GO; GO:0000775; C:chromosome, centromeric region; ISS:UniProtKB.
DR GO; GO:0000776; C:kinetochore; ISO:RGD.
DR GO; GO:0016604; C:nuclear body; IEA:Ensembl.
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 1: Evidence at protein level;
KW Cell cycle; Cell division; Centromere; Chromosome; DNA-binding;
KW Kinetochore; Mitosis; Nucleus; Phosphoprotein; Reference proteome.
FT CHAIN 1..518
FT /note="Centromere protein T"
FT /id="PRO_0000249517"
FT REGION 1..71
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 94..381
FT /note="Flexible stalk domain"
FT /evidence="ECO:0000250"
FT REGION 102..156
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 271..362
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 375..412
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 30..54
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 295..309
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 330..347
FT /note="Basic and acidic 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:0007744|PubMed:22673903"
FT MOD_RES 324
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 333
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96BT3"
FT MOD_RES 345
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 346
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 357
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96BT3"
FT MOD_RES 382
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
SQ SEQUENCE 518 AA; 56861 MW; 845AA7B9EED151C9 CRC64;
MADLSSPDGD PTIRTLLRHV LDTADSHTPR RRQSTQTNPQ RRRSQTPYSK RQGSQRKTST
RKHSHGTGSV GRLARVQGHG HLEEQTPRTL LQNILLTAPE SSTVMPNPVV KPAQVPEVAR
PSRRGSSRGS LELQLPELDP PSTLAPGLKA PGKRKQKLRL SVFQQEVNQQ LPLPQEQRGA
ADGSSLASSF NLSFVPSVQP QTVDRPGLAR RRPVRRPVNI GAFLQNLENK SLTSALPGDS
HRTPVAALPT DVVFEDTQPF SQPLAGCSLS VHHSLPNPSQ TEVEDAERVV GPRTPSTGTR
PQSQMSRAGF GASPLPFSEP QPQSPELREA VGSKEAEEPK DLEGSSGDEE TSGMPASREL
SSSAQDLLLA EEPHQLFEPP PSPGVAAVSS ESVPAKLPSR TRTAQPRHHQ DPYKAGLSHY
VKLFSFHTKM PVEKAALEMV EKCLDEYFQR LCNDLEVFAA HAGRKTVKPK DLELLMRRQG
LVTDQVSLHV LVERYLPLEY RQQLIPCAFR GNSVFPAQ
