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Protein

Centromere protein T

Gene

Cenpt

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 3 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).By similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Cell cycle, Cell division, Mitosis

Keywords - Ligandi

DNA-binding

Enzyme and pathway databases

ReactomeiREACT_286371. Deposition of new CENPA-containing nucleosomes at the centromere.
REACT_306375. Mitotic Prometaphase.
REACT_321346. Separation of Sister Chromatids.
REACT_329805. Resolution of Sister Chromatid Cohesion.
REACT_358264. RHO GTPases Activate Formins.

Names & Taxonomyi

Protein namesi
Recommended name:
Centromere protein T
Short name:
CENP-T
Gene namesi
Name:Cenpt
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 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).By similarity

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Centromere, Chromosome, Kinetochore, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 515515Centromere protein TPRO_0000249516Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei86 – 861PhosphothreonineBy similarity
Modified residuei333 – 3331PhosphoserineBy similarity
Modified residuei345 – 3451PhosphoserineBy similarity
Modified residuei346 – 3461PhosphoserineBy similarity
Modified residuei357 – 3571PhosphoserineBy similarity

Post-translational modificationi

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

Keywords - PTMi

Phosphoprotein

Proteomic databases

PRIDEiQ3TJM4.

Expressioni

Gene expression databases

BgeeiQ3TJM4.
CleanExiMM_CENPT.
GenevisibleiQ3TJM4. MM.

Interactioni

Subunit structurei

Component of the CENPA-NAC complex, at least composed of CENPA, CENPC, CENPH, CENPM, CENPN, CENPT and CENPU. The CENPA-NAC complex interacts with the CENPA-CAD complex, composed of CENPI, CENPK, CENPL, CENPO, CENPP, CENPQ, CENPR and CENPS. Part of a centromere complex consisting of CENPA, CENPT and CENPW. Part of a centromere complex consisting of histone H3, CENPT and CENPW. Interacts (via N-terminus) with the NDC80 complex (By similarity). Component of a heterotetrameric CENP-T-W-S-X complex composed of APITD1/CENPS, STRA13/CENPX, CENPT and CENPW. Interacts directly with CENPW. Binds DNA (By similarity).By similarity

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000038188.

Structurei

3D structure databases

ProteinModelPortaliQ3TJM4.
SMRiQ3TJM4. Positions 419-505.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni94 – 375282Flexible stalk domainBy similarityAdd
BLAST

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

eggNOGiNOG26624.
GeneTreeiENSGT00390000003044.
HOGENOMiHOG000111545.
HOVERGENiHBG081089.
InParanoidiQ3TJM4.
KOiK11512.
OMAiFSFYAKM.
OrthoDBiEOG7TQV2Z.
PhylomeDBiQ3TJM4.
TreeFamiTF332946.

Family and domain databases

Gene3Di1.10.20.10. 1 hit.
InterProiIPR028255. CENP-T.
IPR009072. Histone-fold.
[Graphical view]
PANTHERiPTHR14857. PTHR14857. 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 BAC40776.1 differs from that shown. Reason: Frameshift at position 303. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti5 – 51S → V in BAE25464 (PubMed:16141072).Curated
Sequence conflicti157 – 1571K → R in BAE39471 (PubMed:16141072).Curated
Sequence conflicti302 – 3032QS → KG in BAC40776 (PubMed:16141072).Curated

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.

Cross-referencesi

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.

3D structure databases

ProteinModelPortaliQ3TJM4.
SMRiQ3TJM4. Positions 419-505.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000038188.

Proteomic databases

PRIDEiQ3TJM4.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi80152.
MGIiMGI:2443939. Cenpt.

Phylogenomic databases

eggNOGiNOG26624.
GeneTreeiENSGT00390000003044.
HOGENOMiHOG000111545.
HOVERGENiHBG081089.
InParanoidiQ3TJM4.
KOiK11512.
OMAiFSFYAKM.
OrthoDBiEOG7TQV2Z.
PhylomeDBiQ3TJM4.
TreeFamiTF332946.

Enzyme and pathway databases

ReactomeiREACT_286371. Deposition of new CENPA-containing nucleosomes at the centromere.
REACT_306375. Mitotic Prometaphase.
REACT_321346. Separation of Sister Chromatids.
REACT_329805. Resolution of Sister Chromatid Cohesion.
REACT_358264. RHO GTPases Activate Formins.

Miscellaneous databases

NextBioi396642.
PROiQ3TJM4.
SOURCEiSearch...

Gene expression databases

BgeeiQ3TJM4.
CleanExiMM_CENPT.
GenevisibleiQ3TJM4. MM.

Family and domain databases

Gene3Di1.10.20.10. 1 hit.
InterProiIPR028255. CENP-T.
IPR009072. Histone-fold.
[Graphical view]
PANTHERiPTHR14857. PTHR14857. 1 hit.
SUPFAMiSSF47113. SSF47113. 1 hit.
ProtoNetiSearch...

Publicationsi

  1. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Lung, Placenta and Spleen.
  2. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: FVB/N.
    Tissue: Mammary tumor.

Entry informationi

Entry nameiCENPT_MOUSE
AccessioniPrimary (citable) accession number: Q3TJM4
Secondary accession number(s): Q3TPY6
, Q3UPD2, Q8BTH0, Q8BTP2, Q8R5E9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 3, 2006
Last sequence update: October 3, 2006
Last modified: July 22, 2015
This is version 88 of the entry and version 2 of the sequence. [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

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.