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Protein

T-complex protein 1 subunit beta

Gene

Cct2

Organism
Rattus norvegicus (Rat)
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-RNO-390471. Association of TriC/CCT with target proteins during biosynthesis.
R-RNO-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
Synonyms:Cctb
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 7

Organism-specific databases

RGDi1359143. Cct2.

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_0000271368Add
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

PaxDbiQ5XIM9.
PRIDEiQ5XIM9.

2D gel databases

World-2DPAGE0004:Q5XIM9.

PTM databases

iPTMnetiQ5XIM9.

Expressioni

Gene expression databases

GenevisibleiQ5XIM9. RN.

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

IntActiQ5XIM9. 3 interactions.
MINTiMINT-4577122.
STRINGi10116.ENSRNOP00000029234.

Structurei

3D structure databases

ProteinModelPortaliQ5XIM9.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the TCP-1 chaperonin family.Curated

Phylogenomic databases

eggNOGiKOG0363. Eukaryota.
COG0459. LUCA.
GeneTreeiENSGT00550000074930.
HOGENOMiHOG000226736.
HOVERGENiHBG001052.
InParanoidiQ5XIM9.
KOiK09494.
OMAiSTFEDTS.
OrthoDBiEOG7Q5HD3.
PhylomeDBiQ5XIM9.
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.

Q5XIM9-1 [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 REATKAAREA LLSSAVDHGS
160 170 180 190 200
DEVKFWQDLM 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 AIEHADFAGV ERLALVTGGE IASTFDHPEL VKLGSCKLIE
360 370 380 390 400
EVMIGEDKLI HFSGVALGEA CTIVLRGATQ QILDEAERSL HDALCVLAQT
410 420 430 440 450
VKDPRTVYGG GCSEMLMAHA VTMLASRTPG KEAVAMESFA KALRMLPTII
460 470 480 490 500
ADNAGYDSAD LVAQLRAAHS EGRITAGLDM KEGSIGDMAV LGITESFQVK
510 520 530
RQVLLSAAEA AEVILRVDNI IKAAPRKRVP DHHPC
Length:535
Mass (Da):57,458
Last modified:January 23, 2007 - v3
Checksum:i66BB97367F5FA7FC
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC083650 mRNA. Translation: AAH83650.1.
RefSeqiNP_001005905.1. NM_001005905.1.
UniGeneiRn.2392.

Genome annotation databases

EnsembliENSRNOT00000037946; ENSRNOP00000029234; ENSRNOG00000021317.
GeneIDi299809.
KEGGirno:299809.
UCSCiRGD:1359143. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC083650 mRNA. Translation: AAH83650.1.
RefSeqiNP_001005905.1. NM_001005905.1.
UniGeneiRn.2392.

3D structure databases

ProteinModelPortaliQ5XIM9.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ5XIM9. 3 interactions.
MINTiMINT-4577122.
STRINGi10116.ENSRNOP00000029234.

PTM databases

iPTMnetiQ5XIM9.

2D gel databases

World-2DPAGE0004:Q5XIM9.

Proteomic databases

PaxDbiQ5XIM9.
PRIDEiQ5XIM9.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000037946; ENSRNOP00000029234; ENSRNOG00000021317.
GeneIDi299809.
KEGGirno:299809.
UCSCiRGD:1359143. rat.

Organism-specific databases

CTDi10576.
RGDi1359143. Cct2.

Phylogenomic databases

eggNOGiKOG0363. Eukaryota.
COG0459. LUCA.
GeneTreeiENSGT00550000074930.
HOGENOMiHOG000226736.
HOVERGENiHBG001052.
InParanoidiQ5XIM9.
KOiK09494.
OMAiSTFEDTS.
OrthoDBiEOG7Q5HD3.
PhylomeDBiQ5XIM9.
TreeFamiTF105645.

Enzyme and pathway databases

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

Miscellaneous databases

PROiQ5XIM9.

Gene expression databases

GenevisibleiQ5XIM9. RN.

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

« Hide 'large scale' publications
  1. "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].
    Tissue: Testis.
  2. Lubec G., Afjehi-Sadat L., Chen W.-Q.
    Submitted (APR-2007) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 26-40; 120-131; 205-223; 323-342; 359-376 AND 502-516, IDENTIFICATION BY MASS SPECTROMETRY.
    Strain: Sprague-Dawley.
    Tissue: Hippocampus and Spinal cord.

Entry informationi

Entry nameiTCPB_RAT
AccessioniPrimary (citable) accession number: Q5XIM9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 9, 2007
Last sequence update: January 23, 2007
Last modified: June 8, 2016
This is version 93 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. 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.