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P50991 (TCPD_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 138. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
T-complex protein 1 subunit delta

Short name=TCP-1-delta
Alternative name(s):
CCT-delta
Stimulator of TAR RNA-binding
Gene names
Name:CCT4
Synonyms:CCTD, SRB
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length539 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Molecular chaperone; assists the folding of proteins upon ATP hydrolysis. As part of the BBS/CCT complex may play a role in the assembly of BBSome, a complex involved in ciliogenesis regulating transports vesicles to the cilia. Known to play a role, in vitro, in the folding of actin and tubulin. Ref.11

Subunit structure

Heterooligomeric complex of about 850 to 900 kDa that forms two stacked rings, 12 to 16 nm in diameter. Interacts with PACRG. Component of the BBS/CCT complex composed at least of MKKS, BBS10, BBS12, TCP1, CCT2, CCT3, CCT4, CCT5 AND CCT8. Interacts with DYX1C1 By similarity. Ref.8 Ref.11

Subcellular location

Cytoplasm. Melanosome. Cytoplasmcytoskeletonmicrotubule organizing centercentrosome. Note: Identified by mass spectrometry in melanosome fractions from stage I to stage IV. Ref.9 Ref.11

Sequence similarities

Belongs to the TCP-1 chaperonin family.

Ontologies

Keywords
   Cellular componentCytoplasm
Cytoskeleton
   Coding sequence diversityAlternative splicing
Polymorphism
   LigandATP-binding
Nucleotide-binding
   Molecular functionChaperone
   PTMAcetylation
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_process'de novo' posttranslational protein folding

Traceable author statement. Source: Reactome

binding of sperm to zona pellucida

Inferred from electronic annotation. Source: Ensembl

cellular protein metabolic process

Traceable author statement. Source: Reactome

protein folding

Traceable author statement. Source: Reactome

   Cellular_componentcell body

Inferred from electronic annotation. Source: Ensembl

centrosome

Inferred from direct assay Ref.11. Source: MGI

chaperonin-containing T-complex

Inferred from electronic annotation. Source: Ensembl

cytoplasm

Inferred from direct assay. Source: HPA

cytosol

Traceable author statement. Source: Reactome

extracellular vesicular exosome

Inferred from direct assay PubMed 20458337PubMed 23376485. Source: UniProt

melanosome

Inferred from electronic annotation. Source: UniProtKB-SubCell

microtubule

Inferred from direct assay PubMed 21525035. Source: UniProtKB

nucleus

Inferred from direct assay. Source: HPA

zona pellucida receptor complex

Inferred from electronic annotation. Source: Ensembl

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

poly(A) RNA binding

Inferred from direct assay PubMed 22658674. Source: UniProtKB

unfolded protein binding

Traceable author statement Ref.1. Source: ProtInc

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P50991-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: P50991-2)

The sequence of this isoform differs from the canonical sequence as follows:
     60-89: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.6
Chain2 – 539538T-complex protein 1 subunit delta
PRO_0000128332

Amino acid modifications

Modified residue211N6-acetyllysine By similarity
Modified residue2881N6-acetyllysine Ref.10
Modified residue3021N6-acetyllysine Ref.10
Modified residue3191N6-acetyllysine Ref.10
Modified residue3261N6-acetyllysine Ref.10

Natural variations

Alternative sequence60 – 8930Missing in isoform 2.
VSP_045537
Natural variant1121I → V.
Corresponds to variant rs2272428 [ dbSNP | Ensembl ].
VAR_052266

Experimental info

Sequence conflict4351R → A in AAC50384. Ref.1
Sequence conflict5311K → R in BAH13897. Ref.3

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified January 23, 2007. Version 4.
Checksum: 39913C0D0735180D

FASTA53957,924
        10         20         30         40         50         60 
MPENVAPRSG ATAGAAGGRG KGAYQDRDKP AQIRFSNISA AKAVADAIRT SLGPKGMDKM 

        70         80         90        100        110        120 
IQDGKGDVTI TNDGATILKQ MQVLHPAARM LVELSKAQDI EAGDGTTSVV IIAGSLLDSC 

       130        140        150        160        170        180 
TKLLQKGIHP TIISESFQKA LEKGIEILTD MSRPVELSDR ETLLNSATTS LNSKVVSQYS 

       190        200        210        220        230        240 
SLLSPMSVNA VMKVIDPATA TSVDLRDIKI VKKLGGTIDD CELVEGLVLT QKVSNSGITR 

       250        260        270        280        290        300 
VEKAKIGLIQ FCLSAPKTDM DNQIVVSDYA QMDRVLREER AYILNLVKQI KKTGCNVLLI 

       310        320        330        340        350        360 
QKSILRDALS DLALHFLNKM KIMVIKDIER EDIEFICKTI GTKPVAHIDQ FTADMLGSAE 

       370        380        390        400        410        420 
LAEEVNLNGS GKLLKITGCA SPGKTVTIVV RGSNKLVIEE AERSIHDALC VIRCLVKKRA 

       430        440        450        460        470        480 
LIAGGGAPEI ELALRLTEYS RTLSGMESYC VRAFADAMEV IPSTLAENAG LNPISTVTEL 

       490        500        510        520        530 
RNRHAQGEKT AGINVRKGGI SNILEELVVQ PLLVSVSALT LATETVRSIL KIDDVVNTR 

« Hide

Isoform 2 [UniParc].

Checksum: 53EDE4CD2799D28B
Show »

FASTA50954,720

References

« Hide 'large scale' references
[1]"Identification of a group of cellular cofactors that stimulate the binding of RNA polymerase II and TRP-185 to human immunodeficiency virus 1 TAR RNA."
Wu-Baer F., Lane W.S., Gaynor R.B.
J. Biol. Chem. 271:4201-4208(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PARTIAL PROTEIN SEQUENCE.
[2]"Maturation of human cyclin E requires the function of eukaryotic chaperonin CCT."
Won K.-A., Schumacher R.J., Farr G.W., Horwich A.L., Reed S.I.
Mol. Cell. Biol. 18:7584-7589(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[3]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
Tissue: Brain and Thymus.
[4]"Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H. expand/collapse author list , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]"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] (ISOFORM 1).
Tissue: Brain.
[6]"Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides."
Gevaert K., Goethals M., Martens L., Van Damme J., Staes A., Thomas G.R., Vandekerckhove J.
Nat. Biotechnol. 21:566-569(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 2-8.
Tissue: Platelet.
[7]Bienvenut W.V., Barblan J., Quadroni M.
Submitted (MAR-2004) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 420-435, IDENTIFICATION BY MASS SPECTROMETRY.
Tissue: B-cell lymphoma.
[8]"A product of the human gene adjacent to parkin is a component of Lewy bodies and suppresses Pael receptor-induced cell death."
Imai Y., Soda M., Murakami T., Shoji M., Abe K., Takahashi R.
J. Biol. Chem. 278:51901-51910(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH PACRG.
[9]"Proteomic and bioinformatic characterization of the biogenesis and function of melanosomes."
Chi A., Valencia J.C., Hu Z.-Z., Watabe H., Yamaguchi H., Mangini N.J., Huang H., Canfield V.A., Cheng K.C., Yang F., Abe R., Yamagishi S., Shabanowitz J., Hearing V.J., Wu C., Appella E., Hunt D.F.
J. Proteome Res. 5:3135-3144(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
Tissue: Melanoma.
[10]"Lysine acetylation targets protein complexes and co-regulates major cellular functions."
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-288; LYS-302; LYS-319 AND LYS-326, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[11]"BBS6, BBS10, and BBS12 form a complex with CCT/TRiC family chaperonins and mediate BBSome assembly."
Seo S., Baye L.M., Schulz N.P., Beck J.S., Zhang Q., Slusarski D.C., Sheffield V.C.
Proc. Natl. Acad. Sci. U.S.A. 107:1488-1493(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION, IDENTIFICATION IN BBS/CCT COMPLEX.
[12]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[13]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U38846 mRNA. Translation: AAC50384.1.
AF026291 mRNA. Translation: AAC96010.1.
AK303082 mRNA. Translation: BAH13897.1.
AK312586 mRNA. Translation: BAG35480.1.
AC107081 Genomic DNA. Translation: AAY24140.1.
BC014676 mRNA. Translation: AAH14676.1.
BC106934 mRNA. Translation: AAI06935.1.
BC106933 mRNA. Translation: AAI06934.1.
CCDSCCDS33206.1. [P50991-1]
CCDS58711.1. [P50991-2]
RefSeqNP_001243650.1. NM_001256721.1. [P50991-2]
NP_006421.2. NM_006430.3. [P50991-1]
UniGeneHs.421509.

3D structure databases

ProteinModelPortalP50991.
SMRP50991. Positions 18-539.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid115826. 93 interactions.
DIPDIP-32971N.
IntActP50991. 45 interactions.
MINTMINT-1157924.
STRING9606.ENSP00000377958.

PTM databases

PhosphoSiteP50991.

Polymorphism databases

DMDM52001478.

2D gel databases

REPRODUCTION-2DPAGEIPI00302927.
UCD-2DPAGEP50991.

Proteomic databases

MaxQBP50991.
PaxDbP50991.
PeptideAtlasP50991.
PRIDEP50991.

Protocols and materials databases

DNASU10575.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000394440; ENSP00000377958; ENSG00000115484. [P50991-1]
ENST00000544079; ENSP00000443061; ENSG00000115484. [P50991-2]
GeneID10575.
KEGGhsa:10575.
UCSCuc002sbo.4. human. [P50991-1]

Organism-specific databases

CTD10575.
GeneCardsGC02M062095.
HGNCHGNC:1617. CCT4.
HPAHPA029349.
MIM605142. gene.
neXtProtNX_P50991.
PharmGKBPA26181.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0459.
HOGENOMHOG000226735.
HOVERGENHBG106507.
InParanoidP50991.
KOK09496.
OMAPCAKMLV.
OrthoDBEOG722J8B.
PhylomeDBP50991.
TreeFamTF106332.

Enzyme and pathway databases

ReactomeREACT_17015. Metabolism of proteins.

Gene expression databases

ArrayExpressP50991.
BgeeP50991.
CleanExHS_CCT4.
GenevestigatorP50991.

Family and domain databases

Gene3D1.10.560.10. 2 hits.
3.30.260.10. 2 hits.
3.50.7.10. 1 hit.
InterProIPR012717. Chap_CCT_delta.
IPR017998. Chaperone_TCP-1.
IPR002194. Chaperonin_TCP-1_CS.
IPR002423. Cpn60/TCP-1.
IPR027409. GroEL-like_apical_dom.
IPR027413. GROEL-like_equatorial.
IPR027410. TCP-1-like_intermed.
[Graphical view]
PANTHERPTHR11353. PTHR11353. 1 hit.
PfamPF00118. Cpn60_TCP1. 1 hit.
[Graphical view]
PRINTSPR00304. TCOMPLEXTCP1.
SUPFAMSSF48592. SSF48592. 2 hits.
SSF52029. SSF52029. 1 hit.
TIGRFAMsTIGR02342. chap_CCT_delta. 1 hit.
PROSITEPS00750. TCP1_1. 1 hit.
PS00751. TCP1_2. 1 hit.
PS00995. TCP1_3. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSCCT4. human.
GeneWikiCCT4.
GenomeRNAi10575.
NextBio40137.
PMAP-CutDBP50991.
PROP50991.
SOURCESearch...

Entry information

Entry nameTCPD_HUMAN
AccessionPrimary (citable) accession number: P50991
Secondary accession number(s): B2R6I3 expand/collapse secondary AC list , B7Z8B1, F5H5W3, O14870, Q53QP9, Q96C51
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: January 23, 2007
Last modified: July 9, 2014
This is version 138 of the entry and version 4 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 2

Human chromosome 2: entries, gene names and cross-references to MIM