Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

T-complex protein 1 subunit zeta

Gene

CCT6A

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Molecular chaperone; assists the folding of proteins upon ATP hydrolysis. Known to play a role, in vitro, in the folding of actin and tubulin.

GO - Molecular functioni

  • ATP binding Source: UniProtKB-KW
  • poly(A) RNA binding Source: UniProtKB
  • protein binding involved in protein folding Source: BHF-UCL
  • unfolded protein binding Source: ProtInc
  • WD40-repeat domain binding Source: BHF-UCL

GO - Biological processi

  • 'de novo' posttranslational protein folding Source: Reactome
  • cellular protein metabolic process Source: Reactome
  • positive regulation of establishment of protein localization to telomere Source: BHF-UCL
  • positive regulation of protein localization to Cajal body Source: BHF-UCL
  • positive regulation of telomerase RNA localization to Cajal body Source: BHF-UCL
  • positive regulation of telomere maintenance via telomerase Source: BHF-UCL
  • protein folding Source: Reactome
  • protein stabilization Source: BHF-UCL
Complete GO annotation...

Keywords - Molecular functioni

Chaperone

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiR-HSA-389957. Prefoldin mediated transfer of substrate to CCT/TriC.
R-HSA-389960. Formation of tubulin folding intermediates by CCT/TriC.
R-HSA-390450. Folding of actin by CCT/TriC.
R-HSA-390471. Association of TriC/CCT with target proteins during biosynthesis.

Names & Taxonomyi

Protein namesi
Recommended name:
T-complex protein 1 subunit zeta
Short name:
TCP-1-zeta
Alternative name(s):
Acute morphine dependence-related protein 2
CCT-zeta-1
HTR3
Tcp20
Gene namesi
Name:CCT6A
Synonyms:CCT6, CCTZ
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 7

Organism-specific databases

HGNCiHGNC:1620. CCT6A.

Subcellular locationi

GO - Cellular componenti

  • chaperonin-containing T-complex Source: UniProtKB
  • cytoplasm Source: HPA
  • cytosol Source: Reactome
  • extracellular exosome Source: UniProtKB
  • microtubule Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA26183.

Polymorphism and mutation databases

BioMutaiCCT6A.
DMDMi730922.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedCombined sources1 Publication
Chaini2 – 531530T-complex protein 1 subunit zetaPRO_0000128355Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanineCombined sources
Modified residuei5 – 51N6-acetyllysineBy similarity
Modified residuei199 – 1991N6-acetyllysineCombined sources
Modified residuei287 – 2871N6-acetyllysineBy similarity
Modified residuei365 – 3651N6-acetyllysineCombined sources
Modified residuei377 – 3771N6-acetyllysineCombined sources
Modified residuei388 – 3881N6-acetyllysineCombined sources

Keywords - PTMi

Acetylation

Proteomic databases

EPDiP40227.
MaxQBiP40227.
PaxDbiP40227.
PeptideAtlasiP40227.
PRIDEiP40227.

2D gel databases

DOSAC-COBS-2DPAGEP40227.
REPRODUCTION-2DPAGEIPI00027626.
P40227.
SWISS-2DPAGEP40227.
UCD-2DPAGEP40227.

PTM databases

iPTMnetiP40227.
PhosphoSiteiP40227.
SwissPalmiP40227.

Expressioni

Gene expression databases

BgeeiP40227.
CleanExiHS_CCT6A.
ExpressionAtlasiP40227. baseline and differential.
GenevisibleiP40227. HS.

Organism-specific databases

HPAiHPA042996.
HPA045576.
HPA049949.

Interactioni

Subunit structurei

Heterooligomeric complex of about 850 to 900 kDa that forms two stacked rings, 12 to 16 nm in diameter. Interacts with PACRG.1 Publication

GO - Molecular functioni

  • protein binding involved in protein folding Source: BHF-UCL
  • unfolded protein binding Source: ProtInc
  • WD40-repeat domain binding Source: BHF-UCL

Protein-protein interaction databases

BioGridi107346. 208 interactions.
DIPiDIP-33558N.
IntActiP40227. 105 interactions.
MINTiMINT-1156875.
STRINGi9606.ENSP00000275603.

Structurei

3D structure databases

ProteinModelPortaliP40227.
SMRiP40227. Positions 4-525.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the TCP-1 chaperonin family.Curated

Phylogenomic databases

eggNOGiKOG0359. Eukaryota.
ENOG410XQ3Q. LUCA.
GeneTreeiENSGT00550000074743.
HOGENOMiHOG000226733.
HOVERGENiHBG103725.
InParanoidiP40227.
KOiK09498.
OMAiEAGVWDN.
OrthoDBiEOG7SN8C9.
PhylomeDBiP40227.
TreeFamiTF106333.

Family and domain databases

Gene3Di1.10.560.10. 2 hits.
3.30.260.10. 2 hits.
3.50.7.10. 1 hit.
InterProiIPR012722. Chap_CCT_zeta.
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]
PfamiPF00118. Cpn60_TCP1. 1 hit.
[Graphical view]
PRINTSiPR00304. TCOMPLEXTCP1.
SUPFAMiSSF52029. SSF52029. 1 hit.
TIGRFAMsiTIGR02347. chap_CCT_zeta. 1 hit.
PROSITEiPS00750. TCP1_1. 1 hit.
PS00751. TCP1_2. 1 hit.
PS00995. TCP1_3. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: P40227-1) [UniParc]FASTAAdd to basket

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.

« Hide

        10         20         30         40         50
MAAVKTLNPK AEVARAQAAL AVNISAARGL QDVLRTNLGP KGTMKMLVSG
60 70 80 90 100
AGDIKLTKDG NVLLHEMQIQ HPTASLIAKV ATAQDDITGD GTTSNVLIIG
110 120 130 140 150
ELLKQADLYI SEGLHPRIIT EGFEAAKEKA LQFLEEVKVS REMDRETLID
160 170 180 190 200
VARTSLRTKV HAELADVLTE AVVDSILAIK KQDEPIDLFM IEIMEMKHKS
210 220 230 240 250
ETDTSLIRGL VLDHGARHPD MKKRVEDAYI LTCNVSLEYE KTEVNSGFFY
260 270 280 290 300
KSAEEREKLV KAERKFIEDR VKKIIELKRK VCGDSDKGFV VINQKGIDPF
310 320 330 340 350
SLDALSKEGI VALRRAKRRN MERLTLACGG VALNSFDDLS PDCLGHAGLV
360 370 380 390 400
YEYTLGEEKF TFIEKCNNPR SVTLLIKGPN KHTLTQIKDA VRDGLRAVKN
410 420 430 440 450
AIDDGCVVPG AGAVEVAMAE ALIKHKPSVK GRAQLGVQAF ADALLIIPKV
460 470 480 490 500
LAQNSGFDLQ ETLVKIQAEH SESGQLVGVD LNTGEPMVAA EVGVWDNYCV
510 520 530
KKQLLHSCTV IATNILLVDE IMRAGMSSLK G
Length:531
Mass (Da):58,024
Last modified:January 23, 2007 - v3
Checksum:i43ABCF548CC82B81
GO
Isoform 2 (identifier: P40227-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     68-112: Missing.

Note: No experimental confirmation available.
Show »
Length:486
Mass (Da):53,289
Checksum:i2B0A27299B03A08A
GO

Sequence cautioni

The sequence AAA58676.1 differs from that shown. Reason: Erroneous initiation. Curated
The sequence BU540578 differs from that shown.Several sequencing errors.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti301 – 3033SLD → PLS in BAB61032 (Ref. 3) Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti229 – 2291Y → C.
Corresponds to variant rs33922584 [ dbSNP | Ensembl ].
VAR_052268

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei68 – 11245Missing in isoform 2. 1 PublicationVSP_044918Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L27706 mRNA. Translation: AAA61061.1.
AF385084 mRNA. Translation: AAK61354.1.
AB063318 mRNA. Translation: BAB61032.1.
AC092101 Genomic DNA. Translation: AAS07451.1.
AC092579 Genomic DNA. No translation available.
BC106942 mRNA. Translation: AAI06943.1.
BU540578 mRNA. No translation available.
M94083 mRNA. Translation: AAA58676.1. Different initiation.
CCDSiCCDS34640.1. [P40227-2]
CCDS5523.1. [P40227-1]
PIRiS48087.
RefSeqiNP_001009186.1. NM_001009186.1. [P40227-2]
NP_001753.1. NM_001762.3. [P40227-1]
UniGeneiHs.82916.

Genome annotation databases

EnsembliENST00000275603; ENSP00000275603; ENSG00000146731. [P40227-1]
ENST00000335503; ENSP00000352019; ENSG00000146731. [P40227-2]
GeneIDi908.
KEGGihsa:908.
UCSCiuc003trl.2. human. [P40227-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L27706 mRNA. Translation: AAA61061.1.
AF385084 mRNA. Translation: AAK61354.1.
AB063318 mRNA. Translation: BAB61032.1.
AC092101 Genomic DNA. Translation: AAS07451.1.
AC092579 Genomic DNA. No translation available.
BC106942 mRNA. Translation: AAI06943.1.
BU540578 mRNA. No translation available.
M94083 mRNA. Translation: AAA58676.1. Different initiation.
CCDSiCCDS34640.1. [P40227-2]
CCDS5523.1. [P40227-1]
PIRiS48087.
RefSeqiNP_001009186.1. NM_001009186.1. [P40227-2]
NP_001753.1. NM_001762.3. [P40227-1]
UniGeneiHs.82916.

3D structure databases

ProteinModelPortaliP40227.
SMRiP40227. Positions 4-525.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi107346. 208 interactions.
DIPiDIP-33558N.
IntActiP40227. 105 interactions.
MINTiMINT-1156875.
STRINGi9606.ENSP00000275603.

PTM databases

iPTMnetiP40227.
PhosphoSiteiP40227.
SwissPalmiP40227.

Polymorphism and mutation databases

BioMutaiCCT6A.
DMDMi730922.

2D gel databases

DOSAC-COBS-2DPAGEP40227.
REPRODUCTION-2DPAGEIPI00027626.
P40227.
SWISS-2DPAGEP40227.
UCD-2DPAGEP40227.

Proteomic databases

EPDiP40227.
MaxQBiP40227.
PaxDbiP40227.
PeptideAtlasiP40227.
PRIDEiP40227.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000275603; ENSP00000275603; ENSG00000146731. [P40227-1]
ENST00000335503; ENSP00000352019; ENSG00000146731. [P40227-2]
GeneIDi908.
KEGGihsa:908.
UCSCiuc003trl.2. human. [P40227-1]

Organism-specific databases

CTDi908.
GeneCardsiCCT6A.
HGNCiHGNC:1620. CCT6A.
HPAiHPA042996.
HPA045576.
HPA049949.
MIMi104613. gene.
neXtProtiNX_P40227.
PharmGKBiPA26183.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG0359. Eukaryota.
ENOG410XQ3Q. LUCA.
GeneTreeiENSGT00550000074743.
HOGENOMiHOG000226733.
HOVERGENiHBG103725.
InParanoidiP40227.
KOiK09498.
OMAiEAGVWDN.
OrthoDBiEOG7SN8C9.
PhylomeDBiP40227.
TreeFamiTF106333.

Enzyme and pathway databases

ReactomeiR-HSA-389957. Prefoldin mediated transfer of substrate to CCT/TriC.
R-HSA-389960. Formation of tubulin folding intermediates by CCT/TriC.
R-HSA-390450. Folding of actin by CCT/TriC.
R-HSA-390471. Association of TriC/CCT with target proteins during biosynthesis.

Miscellaneous databases

GeneWikiiCCT6A.
GenomeRNAii908.
NextBioi3744.
PROiP40227.
SOURCEiSearch...

Gene expression databases

BgeeiP40227.
CleanExiHS_CCT6A.
ExpressionAtlasiP40227. baseline and differential.
GenevisibleiP40227. HS.

Family and domain databases

Gene3Di1.10.560.10. 2 hits.
3.30.260.10. 2 hits.
3.50.7.10. 1 hit.
InterProiIPR012722. Chap_CCT_zeta.
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]
PfamiPF00118. Cpn60_TCP1. 1 hit.
[Graphical view]
PRINTSiPR00304. TCOMPLEXTCP1.
SUPFAMiSSF52029. SSF52029. 1 hit.
TIGRFAMsiTIGR02347. chap_CCT_zeta. 1 hit.
PROSITEiPS00750. TCP1_1. 1 hit.
PS00751. TCP1_2. 1 hit.
PS00995. TCP1_3. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Tcp20, a subunit of the eukaryotic TRiC chaperonin from humans and yeast."
    Li W.-Z., Lin P., Frydman J., Boal T.R., Cardillo T.S., Richard L.M., Toth D., Lichtman M.A., Hartl F.-U., Sherman F., Segel G.B.
    J. Biol. Chem. 269:18616-18622(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PROTEIN SEQUENCE OF 324-339.
  2. "Homo sapiens chaperonin mRNA sequence."
    Lee Y.-K., Yoo Y.-D.
    Submitted (MAY-2001) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  3. "Homo sapiens chaperonin (MoDP) mRNA expressed in SH-SY5Y neuroblastoma cells."
    Wang H., Gao X., Li L., Wang B., Huang Y., Han J.
    Submitted (JUN-2001) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  4. "The DNA sequence of human chromosome 7."
    Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H., Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K., Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A., Delehaunty K.D., Miner T.L.
    , Nash W.E., Cordes M., Du H., Sun H., Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A., Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P., Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M., Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S., Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., Strowmatt C., Latreille P., Miller N., Johnson D., Murray J., Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E., Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E., Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A., Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A., Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R., McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H., Wilson R.K.
    Nature 424:157-164(2003) [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), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-233 (ISOFORM 2).
    Tissue: Lung carcinoma.
  6. "Isolation of a gene encoding a chaperonin-like protein by complementation of yeast amino acid transport mutants with human cDNA."
    Segel G.B., Boal T.R., Cardillo T.S., Murant F.G., Lichtman M.A., Sherman F.
    Proc. Natl. Acad. Sci. U.S.A. 89:6060-6064(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 98-531 (ISOFORM 1).
    Tissue: B-cell.
  7. "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 2-15.
    Tissue: Platelet.
  8. Lubec G., Vishwanath V.
    Submitted (MAR-2007) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 105-117 AND 160-180, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: Brain and Cajal-Retzius cell.
  9. "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.
  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-199; LYS-365; LYS-377 AND LYS-388, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  11. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  12. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS], IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  13. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  14. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiTCPZ_HUMAN
AccessioniPrimary (citable) accession number: P40227
Secondary accession number(s): A6NCD2
, Q3KP28, Q75LP4, Q96S46
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: January 23, 2007
Last modified: May 11, 2016
This is version 160 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 7
    Human chromosome 7: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. SIMILARITY comments
    Index of protein domains and families

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 one 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.