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Q3TJM4 (CENPT_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 77. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Centromere protein T

Short name=CENP-T
Gene names
Name:Cenpt
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length515 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

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.

Subunit structure

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.

Subcellular location

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.

Domain

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.

Post-translational modification

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

Sequence caution

The sequence BAC40776.1 differs from that shown. Reason: Frameshift at position 303.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 515515Centromere protein T
PRO_0000249516

Regions

Region94 – 375282Flexible stalk domain By similarity

Amino acid modifications

Modified residue861Phosphothreonine By similarity
Modified residue3331Phosphoserine By similarity
Modified residue3451Phosphoserine By similarity
Modified residue3461Phosphoserine By similarity
Modified residue3571Phosphoserine By similarity

Experimental info

Sequence conflict51S → V in BAE25464. Ref.1
Sequence conflict1571K → R in BAE39471. Ref.1
Sequence conflict302 – 3032QS → KG in BAC40776. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q3TJM4 [UniParc].

Last modified October 3, 2006. Version 2.
Checksum: C736E7FA30E6206B

FASTA51556,242
        10         20         30         40         50         60 
MADLSFSDGD PTVRTLLRRV LETADSRTPM RRRSTRINAQ RRRSQTPYSN RQGSQTKTSA 

        70         80         90        100        110        120 
RKQSHGARSV GRSTRVQGRG RLEEQTPRTL LRNILLTAPE SSTVMPDPVV KPAQVPEVAR 

       130        140        150        160        170        180 
SSRRESSRGS LELHLPELEP PSTLAPGLTA PGKRKQKLRL SVFQQEVDQG LPLSQEPRRS 

       190        200        210        220        230        240 
RSADVSSLAS SFNLTFVLPG QPETVERPGL ARRRPIRQLV NAGALLQDLE DNSLASALPG 

       250        260        270        280        290        300 
DSHRTPVAAL PMDVGLEDTQ PFSQSLAAFS LSGKHSLPSP SRPGVEDVER VMGPPSSGTR 

       310        320        330        340        350        360 
LQSRMSRSGP AASPSPFLEP QPPPAEPREA VGSNEAAEPK DQEGSSGYEE TSARPASGEL 

       370        380        390        400        410        420 
SSSTHDSLPA EQPPPSPGVA VLSSEPLESV TAKCPSRTQT AGPRRRQDPH KAGLSPYVKF 

       430        440        450        460        470        480 
FSFCTKMPVE KTALEIVEKC LDKYFQHLCN DLEVFASHAG RKIVKPEDLL LLMRRQGLVT 

       490        500        510 
DQVSQHVLVE RYLPLEYRQQ LIPCAFSGNS VFPAQ 

« Hide

References

[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. expand/collapse author list , 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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS22615.1.
RefSeqNP_796124.1. NM_177150.2.
UniGeneMm.334775.

3D structure databases

ProteinModelPortalQ3TJM4.
SMRQ3TJM4. Positions 419-505.
ModBaseSearch...
MobiDBSearch...

Proteomic databases

PRIDEQ3TJM4.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000040776; ENSMUSP00000038188; ENSMUSG00000036672.
GeneID320394.
KEGGmmu:320394.
UCSCuc009nef.1. mouse.

Organism-specific databases

CTD80152.
MGIMGI:2443939. Cenpt.

Phylogenomic databases

eggNOGNOG26624.
GeneTreeENSGT00390000003044.
HOGENOMHOG000111545.
HOVERGENHBG081089.
InParanoidQ3TJM4.
KOK11512.
OMAFSFYAKM.
OrthoDBEOG7TQV2Z.
PhylomeDBQ3TJM4.
TreeFamTF332946.

Gene expression databases

BgeeQ3TJM4.
CleanExMM_CENPT.
GenevestigatorQ3TJM4.

Family and domain databases

Gene3D1.10.20.10. 1 hit.
InterProIPR028255. CENP-T.
IPR009072. Histone-fold.
[Graphical view]
PANTHERPTHR14857. PTHR14857. 1 hit.
SUPFAMSSF47113. SSF47113. 1 hit.
ProtoNetSearch...

Other

NextBio396642.
PROQ3TJM4.
SOURCESearch...

Entry information

Entry nameCENPT_MOUSE
AccessionPrimary (citable) accession number: Q3TJM4
Secondary accession number(s): Q3TPY6 expand/collapse secondary AC list , Q3UPD2, Q8BTH0, Q8BTP2, Q8R5E9
Entry history
Integrated into UniProtKB/Swiss-Prot: October 3, 2006
Last sequence update: October 3, 2006
Last modified: July 9, 2014
This is version 77 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

MGD cross-references

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