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Protein

T-complex protein 1 subunit beta

Gene

CCT2

Organism
Bos taurus (Bovine)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

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 (By similarity).By similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Chaperone

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiR-BTA-390471. Association of TriC/CCT with target proteins during biosynthesis.
R-BTA-6814122. Cooperation of PDCL (PhLP1) and TRiC/CCT in G-protein beta folding.

Names & Taxonomyi

Protein namesi
Recommended name:
T-complex protein 1 subunit beta
Short name:
TCP-1-beta
Alternative name(s):
CCT-beta
Gene namesi
Name:CCT2
OrganismiBos taurus (Bovine)
Taxonomic identifieri9913 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
Proteomesi
  • UP000009136 Componenti: Chromosome 5

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedBy similarity
Chaini2 – 535534T-complex protein 1 subunit betaPRO_0000236259Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanineBy similarity
Modified residuei3 – 31PhosphoserineBy similarity
Modified residuei13 – 131N6-acetyllysineBy similarity
Modified residuei154 – 1541N6-acetyllysineBy similarity
Modified residuei181 – 1811N6-acetyllysineBy similarity
Modified residuei260 – 2601PhosphoserineBy similarity
Modified residuei261 – 2611PhosphothreonineBy similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

PaxDbiQ3ZBH0.
PRIDEiQ3ZBH0.

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. Component of the BBS/CCT complex composed at least of MKKS, BBS10, BBS12, TCP1, CCT2, CCT3, CCT4, CCT5 AND CCT8 (By similarity).By similarity

Protein-protein interaction databases

DIPiDIP-58618N.
IntActiQ3ZBH0. 1 interaction.
STRINGi9913.ENSBTAP00000025496.

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3IYGelectron microscopy-B14-526[»]
3KTTelectron microscopy-B14-526[»]
4A0Oelectron microscopy10.50A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P14-526[»]
4A0Velectron microscopy10.70A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P14-526[»]
4A0Welectron microscopy13.90A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P14-526[»]
4A13electron microscopy11.30A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P14-526[»]
4B2TX-ray5.50B/b1-535[»]
ProteinModelPortaliQ3ZBH0.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the TCP-1 chaperonin family.Curated

Phylogenomic databases

eggNOGiKOG0363. Eukaryota.
COG0459. LUCA.
GeneTreeiENSGT00550000074930.
HOGENOMiHOG000226736.
HOVERGENiHBG001052.
InParanoidiQ3ZBH0.
KOiK09494.
OMAiAHYEGKS.
OrthoDBiEOG7Q5HD3.
TreeFamiTF105645.

Family and domain databases

Gene3Di1.10.560.10. 2 hits.
3.30.260.10. 2 hits.
3.50.7.10. 1 hit.
InterProiIPR012716. Chap_CCT_beta.
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.
TIGRFAMsiTIGR02341. chap_CCT_beta. 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.

Q3ZBH0-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MASLSLAPVN IFKAGADEER AETARLSSFI GAIAIGDLVK STLGPKGMDK
60 70 80 90 100
ILLSSGRDAS LMVTNDGATI LKNIGVDNPA AKVLVDMSRV QDDEVGDGTT
110 120 130 140 150
SVTVLAAELL REAESLIAKK IHPQTIIAGW REATKAARQA LLNSAVDHGS
160 170 180 190 200
DEVKFRQDLM NIAGTTLSSK LLTHHKDHFT KLAVEAVLRL KGSGNLEAIH
210 220 230 240 250
VIKKLGGSLA DSYLDEGFLL DKKIGVNQPK RIENAKILIA NTGMDTDKIK
260 270 280 290 300
IFGSRVRVDS TAKVAEIEHA EKEKMKEKVE RILKHGINCF INRQLIYNYP
310 320 330 340 350
EQLFGAAGVM AIEHADFVGV ERLALVTGGE IASTFDHPEL VKLGSCKLIE
360 370 380 390 400
EVMIGEDKLI HFSGVALGEA CTIVLRGATQ QILDEAERSL HDALCVLAQT
410 420 430 440 450
VKDSRTVYGG GCSEMLMAHA VTQLASRTPG KEAVAMESYA KALRMLPTII
460 470 480 490 500
ADNAGYDSAD LVAQLRAAHS EGKTTAGLDM KEGTIGDMSV LGITESFQVK
510 520 530
RQVLLSAAEA AEVILRVDNI IKAAPRKRVP DHHPC
Length:535
Mass (Da):57,475
Last modified:January 23, 2007 - v3
Checksum:iB21ED675C5EA4C7A
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC103298 mRNA. Translation: AAI03299.1.
RefSeqiNP_001029411.1. NM_001034239.1.
UniGeneiBt.49413.

Genome annotation databases

EnsembliENSBTAT00000025496; ENSBTAP00000025496; ENSBTAG00000019156.
GeneIDi505313.
KEGGibta:505313.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC103298 mRNA. Translation: AAI03299.1.
RefSeqiNP_001029411.1. NM_001034239.1.
UniGeneiBt.49413.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3IYGelectron microscopy-B14-526[»]
3KTTelectron microscopy-B14-526[»]
4A0Oelectron microscopy10.50A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P14-526[»]
4A0Velectron microscopy10.70A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P14-526[»]
4A0Welectron microscopy13.90A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P14-526[»]
4A13electron microscopy11.30A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P14-526[»]
4B2TX-ray5.50B/b1-535[»]
ProteinModelPortaliQ3ZBH0.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-58618N.
IntActiQ3ZBH0. 1 interaction.
STRINGi9913.ENSBTAP00000025496.

Proteomic databases

PaxDbiQ3ZBH0.
PRIDEiQ3ZBH0.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSBTAT00000025496; ENSBTAP00000025496; ENSBTAG00000019156.
GeneIDi505313.
KEGGibta:505313.

Organism-specific databases

CTDi10576.

Phylogenomic databases

eggNOGiKOG0363. Eukaryota.
COG0459. LUCA.
GeneTreeiENSGT00550000074930.
HOGENOMiHOG000226736.
HOVERGENiHBG001052.
InParanoidiQ3ZBH0.
KOiK09494.
OMAiAHYEGKS.
OrthoDBiEOG7Q5HD3.
TreeFamiTF105645.

Enzyme and pathway databases

ReactomeiR-BTA-390471. Association of TriC/CCT with target proteins during biosynthesis.
R-BTA-6814122. Cooperation of PDCL (PhLP1) and TRiC/CCT in G-protein beta folding.

Family and domain databases

Gene3Di1.10.560.10. 2 hits.
3.30.260.10. 2 hits.
3.50.7.10. 1 hit.
InterProiIPR012716. Chap_CCT_beta.
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.
TIGRFAMsiTIGR02341. chap_CCT_beta. 1 hit.
PROSITEiPS00750. TCP1_1. 1 hit.
PS00751. TCP1_2. 1 hit.
PS00995. TCP1_3. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. NIH - Mammalian Gene Collection (MGC) project
    Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: Hereford.
    Tissue: Uterus.

Entry informationi

Entry nameiTCPB_BOVIN
AccessioniPrimary (citable) accession number: Q3ZBH0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 30, 2006
Last sequence update: January 23, 2007
Last modified: June 8, 2016
This is version 80 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

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. 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.