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P80317

- TCPZ_MOUSE

UniProt

P80317 - TCPZ_MOUSE

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Protein

T-complex protein 1 subunit zeta

Gene

Cct6a

Organism
Mus musculus (Mouse)
Status
Reviewed - 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

  1. ATP binding Source: UniProtKB-KW

GO - Biological processi

  1. binding of sperm to zona pellucida Source: MGI
  2. protein folding Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Chaperone

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Names & Taxonomyi

Protein namesi
Recommended name:
T-complex protein 1 subunit zeta
Short name:
TCP-1-zeta
Alternative name(s):
CCT-zeta-1
Gene namesi
Name:Cct6a
Synonyms:Cct6, Cctz, Cctz1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Unplaced

Organism-specific databases

MGIiMGI:107943. Cct6a.

Subcellular locationi

GO - Cellular componenti

  1. acrosomal vesicle Source: MGI
  2. cell body Source: MGI
  3. chaperonin-containing T-complex Source: MGI
  4. zona pellucida receptor complex Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11RemovedBy similarity
Chaini2 – 531530T-complex protein 1 subunit zetaPRO_0000128356Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanine1 Publication
Modified residuei5 – 51N6-acetyllysine1 Publication
Modified residuei199 – 1991N6-acetyllysine1 Publication
Modified residuei287 – 2871N6-acetyllysine1 Publication
Modified residuei365 – 3651N6-acetyllysine1 Publication
Modified residuei377 – 3771N6-acetyllysineBy similarity
Modified residuei388 – 3881N6-acetyllysineBy similarity

Post-translational modificationi

The N-terminus is blocked.

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiP80317.
PaxDbiP80317.
PRIDEiP80317.

2D gel databases

REPRODUCTION-2DPAGEIPI00116281.
P80317.
UCD-2DPAGEP80317.

PTM databases

PhosphoSiteiP80317.

Expressioni

Tissue specificityi

Expressed in all tissues examined.

Gene expression databases

CleanExiMM_CCT6A.
GenevestigatoriP80317.

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 By similarity.By similarity

Protein-protein interaction databases

BioGridi198569. 5 interactions.
IntActiP80317. 8 interactions.
MINTiMINT-1870008.

Structurei

3D structure databases

ProteinModelPortaliP80317.
SMRiP80317. Positions 4-525.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the TCP-1 chaperonin family.Curated

Phylogenomic databases

eggNOGiCOG0459.
HOGENOMiHOG000226733.
HOVERGENiHBG103725.
InParanoidiP80317.
KOiK09498.
PhylomeDBiP80317.

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]
PANTHERiPTHR11353. PTHR11353. 1 hit.
PfamiPF00118. Cpn60_TCP1. 1 hit.
[Graphical view]
PRINTSiPR00304. TCOMPLEXTCP1.
SUPFAMiSSF48592. SSF48592. 2 hits.
SSF52029. 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]

Sequencei

Sequence statusi: Complete.

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

P80317-1 [UniParc]FASTAAdd to Basket

« 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 LQFLEQVKVS KEMDRETLID
160 170 180 190 200
VARTSLRTKV HAELADVLTE AVVDSILAIR KKDEPIDLFM VEIMEMKHKS
210 220 230 240 250
ETDTSLIRGL VLDHGARHPD MKKRVENAYI LTCNVSLEYE KTEVNSGFFY
260 270 280 290 300
KSAEEREKLV KAERKFIEDR VKKIIELKKK VCGDSDKGFV VINQKGIDPF
310 320 330 340 350
SLDALAKEGI VALRRAKRRN MERLTLACGG IALNSFDDLN PDCLGHAGLV
360 370 380 390 400
YEYTLGEEKF TFIEKCNNPR SVTLLVKGPN KHTLTQIKDA IRDGLRAVKN
410 420 430 440 450
AIDDGCVVPG AGAVEVALAE ALIKYKPSVK GRAQLGVQAF ADALLIIPKV
460 470 480 490 500
LAQNSGFDLQ ETLVKVQAEH SESGQLVGVD LSTGEPMVAA EMGVWDNYCV
510 520 530
KKQLLHSCTV IATNILLVDE IMRAGMSSLK G
Length:531
Mass (Da):58,004
Last modified:January 23, 2007 - v3
Checksum:iD68C606D67F29642
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
Z31557 mRNA. Translation: CAA83432.1.
AB022159 Genomic DNA. Translation: BAA81877.1.
PIRiS43063.
RefSeqiNP_033968.1. NM_009838.2.
UniGeneiMm.153159.
Mm.360232.

Genome annotation databases

GeneIDi12466.
KEGGimmu:12466.
UCSCiuc029vow.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
Z31557 mRNA. Translation: CAA83432.1 .
AB022159 Genomic DNA. Translation: BAA81877.1 .
PIRi S43063.
RefSeqi NP_033968.1. NM_009838.2.
UniGenei Mm.153159.
Mm.360232.

3D structure databases

ProteinModelPortali P80317.
SMRi P80317. Positions 4-525.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 198569. 5 interactions.
IntActi P80317. 8 interactions.
MINTi MINT-1870008.

PTM databases

PhosphoSitei P80317.

2D gel databases

REPRODUCTION-2DPAGE IPI00116281.
P80317.
UCD-2DPAGE P80317.

Proteomic databases

MaxQBi P80317.
PaxDbi P80317.
PRIDEi P80317.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 12466.
KEGGi mmu:12466.
UCSCi uc029vow.1. mouse.

Organism-specific databases

CTDi 908.
MGIi MGI:107943. Cct6a.

Phylogenomic databases

eggNOGi COG0459.
HOGENOMi HOG000226733.
HOVERGENi HBG103725.
InParanoidi P80317.
KOi K09498.
PhylomeDBi P80317.

Miscellaneous databases

ChiTaRSi CCT6A. mouse.
NextBioi 281338.
PROi P80317.
SOURCEi Search...

Gene expression databases

CleanExi MM_CCT6A.
Genevestigatori P80317.

Family and domain databases

Gene3Di 1.10.560.10. 2 hits.
3.30.260.10. 2 hits.
3.50.7.10. 1 hit.
InterProi IPR012722. 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 ]
PANTHERi PTHR11353. PTHR11353. 1 hit.
Pfami PF00118. Cpn60_TCP1. 1 hit.
[Graphical view ]
PRINTSi PR00304. TCOMPLEXTCP1.
SUPFAMi SSF48592. SSF48592. 2 hits.
SSF52029. SSF52029. 1 hit.
TIGRFAMsi TIGR02347. chap_CCT_zeta. 1 hit.
PROSITEi PS00750. TCP1_1. 1 hit.
PS00751. TCP1_2. 1 hit.
PS00995. TCP1_3. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Identification of six Tcp-1-related genes encoding divergent subunits of the TCP-1-containing chaperonin."
    Kubota H., Hynes G., Carne A., Ashworth A., Willison K.R.
    Curr. Biol. 4:89-99(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE.
    Strain: 129/Sv.
  2. "Structures and co-regulated expression of the genes encoding mouse cytosolic chaperonin CCT subunits."
    Kubota H., Yokota S., Yanagi H., Yura T.
    Eur. J. Biochem. 262:492-500(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: 129/Sv.
  3. Lubec G., Klug S., Kang S.U., Sunyer B., Chen W.-Q.
    Submitted (JAN-2009) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 16-28; 106-127; 130-138; 160-180; 200-208; 242-251 AND 524-530, IDENTIFICATION BY MASS SPECTROMETRY.
    Strain: C57BL/6 and OF1.
    Tissue: Brain and Hippocampus.
  4. "SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
    Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
    Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2; LYS-5; LYS-199; LYS-287 AND LYS-365, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
    Tissue: Embryonic fibroblast.

Entry informationi

Entry nameiTCPZ_MOUSE
AccessioniPrimary (citable) accession number: P80317
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 1, 1994
Last sequence update: January 23, 2007
Last modified: October 29, 2014
This is version 123 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3