T-complex protein 1 subunit beta - Mus musculus (Mouse)

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P80314 (TCPB_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 119. History...

Clusters with 100%, 90%, 50% identity |

Documents (2) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
T-complex protein 1 subunit beta
Short name=TCP-1-beta

Alternative name(s):
CCT-beta

Gene names

Name:	Cct2
Synonyms:	Cctb

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	535 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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 By similarity.
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 By similarity.
Subcellular location	Cytoplasm.
Post-translational modification	The N-terminus is blocked.
Sequence similarities	Belongs to the TCP-1 chaperonin family.

Ontologies

Keywords
Cellular component	Cytoplasm
Ligand	ATP-binding Nucleotide-binding
Molecular function	Chaperone
PTM	Acetylation Phosphoprotein
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	binding of sperm to zona pellucida Inferred from direct assay PubMed 21880732. Source: MGI chaperone-mediated protein complex assembly Inferred from electronic annotation. Source: Compara protein folding Inferred from electronic annotation. Source: InterPro
Cellular_component	chaperonin-containing T-complex Inferred from direct assay PubMed 7828721 Ref.1. Source: MGI microtubule Inferred from electronic annotation. Source: Compara nucleus Inferred from electronic annotation. Source: Compara sperm part Inferred from direct assay PubMed 21880732. Source: MGI zona pellucida receptor complex Inferred from direct assay PubMed 21880732. Source: MGI
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

Removed By similarity

Chain

2 – 535

534

T-complex protein 1 subunit beta

PRO_0000128317

Amino acid modifications

Modified residue

N-acetylalanine By similarity

Modified residue

Phosphoserine By similarity

Modified residue

N6-acetyllysine By similarity

Modified residue

181

N6-acetyllysine By similarity

Modified residue

260

Phosphoserine By similarity

Modified residue

261

Phosphothreonine By similarity

Experimental info

Sequence conflict

T → I in CAA83428. Ref.1

Sequence conflict

187

V → G in CAA83428. Ref.1

Sequences

Sequence

Length

Mass (Da)

Tools

P80314 [UniParc].

Last modified January 23, 2007. Version 4.
Checksum: 605744DF068BB192
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FASTA

535

57,477

        10         20         30         40         50         60 
MASLSLAPVN IFKAGADEER AETARLSSFI GAIAIGDLVK STLGPKGMDK ILLSSGRDAA 

        70         80         90        100        110        120 
LMVTNDGATI LKNIGVDNPA AKVLVDMSRV QDDEVGDGTT SVTVLAAELL REAESLIAKK 

       130        140        150        160        170        180 
IHPQTIISGW REATKAAREA LLSSAVDHGS DEARFWQDLM NIAGTTLSSK LLTHHKDHFT 

       190        200        210        220        230        240 
KLAVEAVLRL KGSGNLEAIH VIKKLGGSLA DSYLDEGFLL DKKIGVNQPK RIENAKILIA 

       250        260        270        280        290        300 
NTGMDTDKIK IFGSRVRVDS TAKVAEIEHA EKEKMKEKVE RILKHGINCF INRQLIYNYP 

       310        320        330        340        350        360 
EQLFGAAGVM AIEHADFAGV ERLALVTGGE IASTFDHPEL VKLGSCKLIE EVMIGEDKLI 

       370        380        390        400        410        420 
HFSGVALGEA CTIVLRGATQ QILDEAERSL HDALCVLAQT VKDPRTVYGG GCSEMLMAHA 

       430        440        450        460        470        480 
VTQLANRTPG KEAVAMESFA KALRMLPTII ADNAGYDSAD LVAQLRAAHS EGHITAGLDM 

       490        500        510        520        530 
KEGTIGDMAV LGITESFQVK RQVLLSAAEA AEVILRVDNI IKAAPRKRVP DHHPC

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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]	"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: Eye.
[4]	Lubec G., Klug S., Yang J.W., Zigmond M., Sunyer B., Chen W.-Q. Submitted (JAN-2009) to UniProtKB Cited for: PROTEIN SEQUENCE OF 26-40; 51-82; 90-131; 139-170; 182-189; 192-203; 205-223; 224-230; 237-248; 264-272; 285-293; 323-342; 348-402; 406-427; 432-441; 445-500 AND 502-516, MASS SPECTROMETRY. Strain: OF1. Tissue: Brain and Hippocampus.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	Z31553 mRNA. Translation: CAA83428.1. AB022156 Genomic DNA. Translation: BAA81874.1. BC007470 mRNA. Translation: AAH07470.1. BC026918 mRNA. Translation: AAH26918.1.
IPI	IPI00320217.
PIR	S43059.
RefSeq	NP_031662.2. NM_007636.2.
UniGene	Mm.247788. Mm.473578.
3D structure databases
ProteinModelPortal	P80314.
SMR	P80314. Positions 14-526.
ModBase	Search...
Protein-protein interaction databases
IntAct	P80314. 9 interactions.
PTM databases
PhosphoSite	P80314.
2D gel databases
REPRODUCTION-2DPAGE	P80314.
Proteomic databases
PaxDb	P80314.
PRIDE	P80314.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000047672; ENSMUSP00000036288; ENSMUSG00000034024.
GeneID	12461.
KEGG	mmu:12461.
Organism-specific databases
CTD	10576.
MGI	MGI:107186. Cct2.
Phylogenomic databases
eggNOG	COG0459.
HOGENOM	HOG000226736.
HOVERGEN	HBG001052.
InParanoid	P80314.
KO	K09494.
OMA	NIIRAKP.
OrthoDB	EOG47WNNK.
Gene expression databases
ArrayExpress	P80314.
Bgee	P80314.
CleanEx	MM_CCT2.
Genevestigator	P80314.
GermOnline	ENSMUSG00000034024. Mus musculus.
Family and domain databases
InterPro	IPR012716. Chap_CCT_beta. IPR017998. Chaperone_TCP-1. IPR002194. Chaperonin_TCP-1_CS. IPR002423. Cpn60/TCP-1. [Graphical view]
PANTHER	PTHR11353. PTHR11353. 1 hit. PTHR11353:SF23. PTHR11353:SF23. 1 hit.
Pfam	PF00118. Cpn60_TCP1. 1 hit. [Graphical view]
PRINTS	PR00304. TCOMPLEXTCP1.
SUPFAM	SSF48592. GroEL-ATPase. 1 hit.
TIGRFAMs	TIGR02341. chap_CCT_beta. 1 hit.
PROSITE	PS00750. TCP1_1. 1 hit. PS00751. TCP1_2. 1 hit. PS00995. TCP1_3. 1 hit. [Graphical view]
ProtoNet	Search...
Other
ChiTaRS	CCT2. mouse.
NextBio	281320.
SOURCE	Search...

Entry information

Entry name

TCPB_MOUSE

Accession

Primary (citable) accession number: P80314
Secondary accession number(s): Q9R1U0

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 1, 1994
Last sequence update:	January 23, 2007
Last modified:	April 3, 2013
This is version 119 of the entry and version 4 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Relevant documents

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Amino acid modifications

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

PTM databases

2D gel databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents