F1NPG5 (CENPT_CHICK) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Centromere protein T
Short name=CENP-T

Gene names

Name:

CENPT

Organism

Gallus gallus (Chicken) [Reference proteome]

Taxonomic identifier

9031 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Sauropsida › Sauria › Archosauria › Dinosauria › Saurischia › Theropoda › Coelurosauria › Aves › Neognathae › Galliformes › Phasianidae › Phasianinae › Gallus

Protein attributes

Sequence length	639 AA.
Sequence status	Complete.
Protein existence	Evidence at protein 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 By similarity. The CENPA-NAC complex recruits the CENPA-CAD (nucleosome distal) complex and may be involved in incorporation of newly synthesized CENPA into centromeres By similarity. 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. Ref.3 Ref.5
Subunit structure	Component of the CENPA-NAC complex, at least composed of CENPA, CENPC, CENPH, CENPM, CENPN, CENPT and MLF1IP/CENPU By similarity. The CENPA-NAC complex interacts with the CENPA-CAD complex, composed of CENPI, CENPK, CENPL, CENPO, CENPP, CENPQ, CENPR and CENPS By similarity. Part of a centromere complex consisting of CENPA, CENPT and CENPW By similarity. Part of a centromere complex consisting of histone H3, CENPT and CENPW. Component of a heterotetrameric CENP-T-W-S-X complex composed of APITD1/CENPS, STRA13/CENPX, CENPT and CENPW. Interacts directly with CENPW. Interacts (via N-terminus) with the NDC80 complex. Binds DNA. Ref.3 Ref.4 Ref.5
Subcellular location	Nucleus. Chromosome › centromere › kinetochore. 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. Ref.3 Ref.4 Ref.5
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. Ref.4
Miscellaneous	Association with CENPA-containing complexes may be indirect and due to the proximity of centromeric nucleosomes containing histone H3 with those containing CENPA.
Sequence similarities	Belongs to the CENPT family.

Ontologies

Keywords
Biological process	Cell cycle Cell division Mitosis
Cellular component	Centromere Chromosome Kinetochore Nucleus
Ligand	DNA-binding
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	cell division Inferred from electronic annotation. Source: UniProtKB-KW mitosis Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	condensed chromosome kinetochore Inferred from electronic annotation. Source: UniProtKB-SubCell nucleus Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	DNA binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
APITD1	E1BSW7	3	EBI-2132248,EBI-5487792
CENPW	P0DJH6	4	EBI-2132248,EBI-2132287

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 639

639

Centromere protein T

PRO_0000417383

Regions

Region

80 – 500

421

Flexible stalk domain

Secondary structure

1

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.

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639

Helix Strand Turn

Details...

Helix

538 – 549

12

Helix

555 – 582

28

Beta strand

586 – 588

3

Helix

590 – 599

10

Beta strand

602 – 604

3

Beta strand

605 – 607

3

Helix

609 – 616

8

Helix

619 – 625

7

Sequences

	Sequence		Length	Mass (Da)
	F1NPG5 [UniParc]. Last modified May 16, 2012. Version 2. Checksum: 9D314920A56ADC11	FASTA	639	70,670
	10 20 30 40 50 60 MDGRVGLRAS RRAAPTPRVA VRSSPRHRAR VREQEPVVSA MSGSGLGKEN KAGSSTPLRH 70 80 90 100 110 120 RPNAFSELDN ATPRVMLRKI IQNQPQVSPL ALQTVQLEET EDARPEPPSQ RTSSTVELQL 130 140 150 160 170 180 PDLVPEDASV TTFRMTRKRK KLSISEFERA ADKRLPQNQA HSTLDSTLVR SLRMSVGSVM 190 200 210 220 230 240 APDTVEKRGL LRRPQNHKAI DIAAFEGGVE QNMLQIKAQD YLVDLQTSSM TGTTTIRTDA 250 260 270 280 290 300 EVVLNNTELF VEPQLGEQNL LAVEPQLSDS KTSAQRSNTS YPAHEKARLE GLVSRVSTDE 310 320 330 340 350 360 RRTLRFSEKD LITDHEHVDG ITQKTPAKQG EEEQDHSQQN DPMEQFSESE EMAGTTEHHA 370 380 390 400 410 420 DAEYSEHSEK KLSRKAVSQL TAAQDAGVEM EMTPSEGGVA EGTEHQDSPK AELQMAGSPG 430 440 450 460 470 480 GHSPASYSLE KPGAKPLKEA VEQTGEIERG TITGVLDAAE EEATDDESDK EDHESEEISM 490 500 510 520 530 540 KTPMFVHAAA YRPQPVLSPP HPVKSASPEL PPQPVRAKPV PKSSGAAQRK TREPEIASSL 550 560 570 580 590 600 IKQIFSHYVK TPVTRDAYKI VEKCSERYFK QISSDLEAYS QHAGRKTVEM ADVELLMRRQ 610 620 630 GLVTDKMPLH VLVERHLPLE YRKLLIPIAV SGNKVIPCK

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"A comprehensive collection of chicken cDNAs." Boardman P.E., Sanz-Ezquerro J., Overton I.M., Burt D.W., Bosch E., Fong W.T., Tickle C., Brown W.R., Wilson S.A., Hubbard S.J. Curr. Biol. 12:1965-1969(2002) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: White Leghorn Hisex.
[2]	"Sequence and comparative analysis of the chicken genome provide unique perspectives on vertebrate evolution." Hillier L.W., Miller W., Birney E., Warren W., Hardison R.C., Ponting C.P., Bork P., Burt D.W., Groenen M.A.M., Delany M.E., Dodgson J.B., Chinwalla A.T., Cliften P.F., Clifton S.W., Delehaunty K.D., Fronick C., Fulton R.S., Graves T.A. , Kremitzki C., Layman D., Magrini V., McPherson J.D., Miner T.L., Minx P., Nash W.E., Nhan M.N., Nelson J.O., Oddy L.G., Pohl C.S., Randall-Maher J., Smith S.M., Wallis J.W., Yang S.-P., Romanov M.N., Rondelli C.M., Paton B., Smith J., Morrice D., Daniels L., Tempest H.G., Robertson L., Masabanda J.S., Griffin D.K., Vignal A., Fillon V., Jacobbson L., Kerje S., Andersson L., Crooijmans R.P., Aerts J., van der Poel J.J., Ellegren H., Caldwell R.B., Hubbard S.J., Grafham D.V., Kierzek A.M., McLaren S.R., Overton I.M., Arakawa H., Beattie K.J., Bezzubov Y., Boardman P.E., Bonfield J.K., Croning M.D.R., Davies R.M., Francis M.D., Humphray S.J., Scott C.E., Taylor R.G., Tickle C., Brown W.R.A., Rogers J., Buerstedde J.-M., Wilson S.A., Stubbs L., Ovcharenko I., Gordon L., Lucas S., Miller M.M., Inoko H., Shiina T., Kaufman J., Salomonsen J., Skjoedt K., Wong G.K.-S., Wang J., Liu B., Wang J., Yu J., Yang H., Nefedov M., Koriabine M., Dejong P.J., Goodstadt L., Webber C., Dickens N.J., Letunic I., Suyama M., Torrents D., von Mering C., Zdobnov E.M., Makova K., Nekrutenko A., Elnitski L., Eswara P., King D.C., Yang S.-P., Tyekucheva S., Radakrishnan A., Harris R.S., Chiaromonte F., Taylor J., He J., Rijnkels M., Griffiths-Jones S., Ureta-Vidal A., Hoffman M.M., Severin J., Searle S.M.J., Law A.S., Speed D., Waddington D., Cheng Z., Tuzun E., Eichler E., Bao Z., Flicek P., Shteynberg D.D., Brent M.R., Bye J.M., Huckle E.J., Chatterji S., Dewey C., Pachter L., Kouranov A., Mourelatos Z., Hatzigeorgiou A.G., Paterson A.H., Ivarie R., Brandstrom M., Axelsson E., Backstrom N., Berlin S., Webster M.T., Pourquie O., Reymond A., Ucla C., Antonarakis S.E., Long M., Emerson J.J., Betran E., Dupanloup I., Kaessmann H., Hinrichs A.S., Bejerano G., Furey T.S., Harte R.A., Raney B., Siepel A., Kent W.J., Haussler D., Eyras E., Castelo R., Abril J.F., Castellano S., Camara F., Parra G., Guigo R., Bourque G., Tesler G., Pevzner P.A., Smit A., Fulton L.A., Mardis E.R., Wilson R.K. Nature 432:695-716(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Red jungle fowl.
[3]	"CCAN makes multiple contacts with centromeric DNA to provide distinct pathways to the outer kinetochore." Hori T., Amano M., Suzuki A., Backer C.B., Welburn J.P., Dong Y., McEwen B.F., Shang W.-H., Suzuki E., Okawa K., Cheeseman I.M., Fukagawa T. Cell 135:1039-1052(2008) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, SUBUNIT, SUBCELLULAR LOCATION.
[4]	"Spindle microtubules generate tension-dependent changes in the distribution of inner kinetochore proteins." Suzuki A., Hori T., Nishino T., Usukura J., Miyagi A., Morikawa K., Fukagawa T. J. Cell Biol. 193:125-140(2011) [PubMed] [Europe PMC] [Abstract] Cited for: SUBCELLULAR LOCATION, DOMAIN, INTERACTION WITH CENPW.
[5]	"CENP-T-W-S-X forms a unique centromeric chromatin structure with a histone-like fold." Nishino T., Takeuchi K., Gascoigne K.E., Suzuki A., Hori T., Oyama T., Morikawa K., Cheeseman I.M., Fukagawa T. Cell 148:487-501(2012) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) OF 54-162, FUNCTION, SUBUNIT, SUBCELLULAR LOCATION.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AJ452155 mRNA. No translation available.
BU128959 mRNA. No translation available.
BU260128 mRNA. No translation available.
BU381659 mRNA. No translation available.
BU382952 mRNA. No translation available.
BU433983 mRNA. No translation available.
CD734856 mRNA. No translation available.
AADN02051672 Genomic DNA. No translation available.

IPI

IPI00586160.

RefSeq

NP_001263242.1. NM_001276313.1.

UniGene

Gga.2263.
Gga.54685.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
3B0C	X-ray	2.20	T	531-639	[»]
3B0D	X-ray	2.20	B/T	531-639	[»]
3VH5	X-ray	2.40	T	531-637	[»]
3VH6	X-ray	3.35	T	531-637	[»]
3VZA	X-ray	1.90	E/F	63-98	[»]

ModBase

Search...

Protein-protein interaction databases

IntAct

F1NPG5. 4 interactions.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

GeneID

415654.

KEGG

gga:415654.

Organism-specific databases

CTD

80152.

Phylogenomic databases

KO

K11512.

Family and domain databases

Gene3D

1.10.20.10. 1 hit.

InterPro

IPR009072. Histone-fold.
[Graphical view]

SUPFAM

SSF47113. Histone-fold. 1 hit.

ProtoNet

Search...

Entry information

Entry name

CENPT_CHICK

Accession

Primary (citable) accession number: F1NPG5

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 16, 2012
Last sequence update:	May 16, 2012
Last modified:	May 29, 2013
This is version 19 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program