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Protein

Centromere protein T

Gene

Cenpt

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at transcript leveli

Functioni

Component of the CENPA-NAC (nucleosome-associated) complex, a complex that plays a central role in assembly of kinetochore proteins, mitotic progression and chromosome segregation. The CENPA-NAC complex recruits the CENPA-CAD (nucleosome distal) complex and may be involved in incorporation of newly synthesized CENPA into centromeres. Part of a nucleosome-associated complex that binds specifically to histone H3-containing nucleosomes at the centromere, as opposed to nucleosomes containing CENPA. Component of the heterotetrameric CENP-T-W-S-X complex that binds and supercoils DNA, and plays an important role in kinetochore assembly. CENPT has a fundamental role in kinetochore assembly and function. It is one of the inner kinetochore proteins, with most further proteins binding downstream. Required for normal chromosome organization and normal progress through mitosis.By similarity

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionDNA-binding
Biological processCell cycle, Cell division, Mitosis

Enzyme and pathway databases

ReactomeiR-MMU-2467813. Separation of Sister Chromatids.
R-MMU-2500257. Resolution of Sister Chromatid Cohesion.
R-MMU-5663220. RHO GTPases Activate Formins.
R-MMU-606279. Deposition of new CENPA-containing nucleosomes at the centromere.
R-MMU-68877. Mitotic Prometaphase.

Names & Taxonomyi

Protein namesi
Recommended name:
Centromere protein T
Short name:
CENP-T
Gene namesi
Name:Cenpt
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 8

Organism-specific databases

MGIiMGI:2443939. Cenpt.

Subcellular locationi

  • Nucleus By similarity
  • Chromosomecentromere By similarity
  • Chromosomecentromerekinetochore By similarity

  • Note: Constitutively localizes to centromeres throughout the cell cycle, and to kinetochores during mitosis. Localizes to the inner kinetochore, and may connect it to the outer kinetochore via its N-terminus.By similarity

GO - Cellular componenti

Keywords - Cellular componenti

Centromere, Chromosome, Kinetochore, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002495161 – 515Centromere protein TAdd BLAST515

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei86PhosphothreonineBy similarity1
Modified residuei313PhosphoserineBy similarity1
Modified residuei333PhosphoserineBy similarity1
Modified residuei345PhosphoserineBy similarity1
Modified residuei346PhosphoserineBy similarity1
Modified residuei357PhosphoserineBy similarity1
Modified residuei376PhosphoserineBy similarity1

Post-translational modificationi

Dynamically phosphorylated during the cell cycle. Phosphorylated during G2 phase, metaphase and anaphase, but not during telophase or G1 phase.By similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiQ3TJM4.
MaxQBiQ3TJM4.
PaxDbiQ3TJM4.
PeptideAtlasiQ3TJM4.
PRIDEiQ3TJM4.

PTM databases

iPTMnetiQ3TJM4.
PhosphoSitePlusiQ3TJM4.

Expressioni

Gene expression databases

BgeeiENSMUSG00000036672.
CleanExiMM_CENPT.
ExpressionAtlasiQ3TJM4. baseline and differential.
GenevisibleiQ3TJM4. MM.

Interactioni

Subunit structurei

Component of the CENPA-CAD complex, composed of CENPI, CENPK, CENPL, CENPO, CENPP, CENPQ, CENPR and CENPS. The CENPA-CAD complex is probably recruited on centromeres by the CENPA-NAC complex, at least composed of CENPA, CENPC, CENPH, CENPM, CENPN, CENPT and CENPU. Identified in a centromeric complex containing histones H2A, H2B, H3 and H4, and at least CENPA, CENPB, CENPC, CENPT, CENPN, HJURP, SUPT16H, SSRP1 and RSF1. Interacts (via N-terminus) with the NDC80 complex. Heterodimer with CENPW; this dimer coassembles with CENPS-CENPX heterodimers at centromeres to form the tetrameric CENP-T-W-S-X complex.By similarity

GO - Molecular functioni

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000038188.

Structurei

3D structure databases

ProteinModelPortaliQ3TJM4.
SMRiQ3TJM4.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni94 – 375Flexible stalk domainBy similarityAdd BLAST282

Domaini

The largest part of the sequence forms an elongated and flexible stalk structure that is connected to a C-terminal globular domain with a histone-type fold.By similarity

Phylogenomic databases

eggNOGiENOG410IFJ0. Eukaryota.
ENOG4111ZWH. LUCA.
GeneTreeiENSGT00390000003044.
HOGENOMiHOG000111545.
HOVERGENiHBG081089.
InParanoidiQ3TJM4.
KOiK11512.
OMAiFSFYAKM.
OrthoDBiEOG091G05OQ.
PhylomeDBiQ3TJM4.
TreeFamiTF332946.

Family and domain databases

InterProiView protein in InterPro
IPR028255. CENP-T.
IPR035425. CENP-T/H4_C.
IPR032373. CENP-T_N.
IPR009072. Histone-fold.
PANTHERiPTHR10484:SF117. PTHR10484:SF117. 1 hit.
PfamiView protein in Pfam
PF15511. CENP-T_C. 1 hit.
PF16171. CENP-T_N. 1 hit.
SUPFAMiSSF47113. SSF47113. 1 hit.

Sequencei

Sequence statusi: Complete.

Q3TJM4-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MADLSFSDGD PTVRTLLRRV LETADSRTPM RRRSTRINAQ RRRSQTPYSN
60 70 80 90 100
RQGSQTKTSA RKQSHGARSV GRSTRVQGRG RLEEQTPRTL LRNILLTAPE
110 120 130 140 150
SSTVMPDPVV KPAQVPEVAR SSRRESSRGS LELHLPELEP PSTLAPGLTA
160 170 180 190 200
PGKRKQKLRL SVFQQEVDQG LPLSQEPRRS RSADVSSLAS SFNLTFVLPG
210 220 230 240 250
QPETVERPGL ARRRPIRQLV NAGALLQDLE DNSLASALPG DSHRTPVAAL
260 270 280 290 300
PMDVGLEDTQ PFSQSLAAFS LSGKHSLPSP SRPGVEDVER VMGPPSSGTR
310 320 330 340 350
LQSRMSRSGP AASPSPFLEP QPPPAEPREA VGSNEAAEPK DQEGSSGYEE
360 370 380 390 400
TSARPASGEL SSSTHDSLPA EQPPPSPGVA VLSSEPLESV TAKCPSRTQT
410 420 430 440 450
AGPRRRQDPH KAGLSPYVKF FSFCTKMPVE KTALEIVEKC LDKYFQHLCN
460 470 480 490 500
DLEVFASHAG RKIVKPEDLL LLMRRQGLVT DQVSQHVLVE RYLPLEYRQQ
510
LIPCAFSGNS VFPAQ
Length:515
Mass (Da):56,242
Last modified:October 3, 2006 - v2
Checksum:iC736E7FA30E6206B
GO

Sequence cautioni

The sequence BAC40776 differs from that shown. Reason: Frameshift at position 303.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti5S → V in BAE25464 (PubMed:16141072).Curated1
Sequence conflicti157K → R in BAE39471 (PubMed:16141072).Curated1
Sequence conflicti302 – 303QS → KG in BAC40776 (PubMed:16141072).Curated2

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK089172 mRNA. Translation: BAC40776.1. Frameshift.
AK090340 mRNA. Translation: BAC41176.1.
AK143613 mRNA. Translation: BAE25464.1.
AK164039 mRNA. Translation: BAE37599.1.
AK167376 mRNA. Translation: BAE39471.1.
BC022690 mRNA. Translation: AAH22690.1.
BC121824 mRNA. Translation: AAI21825.1.
CCDSiCCDS22615.1.
RefSeqiNP_796124.1. NM_177150.2.
XP_011246709.1. XM_011248407.1.
UniGeneiMm.334775.

Genome annotation databases

EnsembliENSMUST00000040776; ENSMUSP00000038188; ENSMUSG00000036672.
GeneIDi320394.
KEGGimmu:320394.
UCSCiuc009nef.1. mouse.

Entry informationi

Entry nameiCENPT_MOUSE
AccessioniPrimary (citable) accession number: Q3TJM4
Secondary accession number(s): Q3TPY6
, Q3UPD2, Q8BTH0, Q8BTP2, Q8R5E9
Entry historyiIntegrated into UniProtKB/Swiss-Prot: October 3, 2006
Last sequence update: October 3, 2006
Last modified: August 30, 2017
This is version 104 of the entry and version 2 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot