P78371 (TCPB_HUMAN) Reviewed, UniProtKB/Swiss-Prot

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:	99D8.1, CCTB

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

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. Ref.13
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. Ref.10
Subcellular location	Cytoplasm Ref.13.
Sequence similarities	Belongs to the TCP-1 chaperonin family.

Ontologies

Keywords
Cellular component	Cytoplasm
Ligand	ATP-binding Nucleotide-binding
Molecular function	Chaperone
PTM	Acetylation
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological process	'de novo' posttranslational protein folding Traceable author statement. Source: Reactome
Cellular component	nucleus Inferred from direct assay. Source: HPA
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW unfolded protein binding Non-traceable author statement. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Initiator methionine	1	1	Removed Ref.7 Ref.8
	Chain	2 – 535	534	T-complex protein 1 subunit beta		PRO_0000128316
Amino acid modifications
	Modified residue	2	1	N-acetylalanine Ref.8 Ref.11
	Modified residue	13	1	N6-acetyllysine Ref.12
	Modified residue	154	1	N6-acetyllysine Ref.12
	Modified residue	181	1	N6-acetyllysine Ref.12
Experimental info
	Sequence conflict	126	1	I → T in CAG33352. Ref.4
	Sequence conflict	504	1	L → P in CAG33352. Ref.4

Sequences

	Sequence		Length	Mass (Da)
	P78371 [UniParc]. Last modified January 23, 2007. Version 4. Checksum: 57F9E1720D84A31F	FASTA	535	57,488
	10 20 30 40 50 60 MASLSLAPVN IFKAGADEER AETARLTSFI GAIAIGDLVK STLGPKGMDK ILLSSGRDAS 70 80 90 100 110 120 LMVTNDGATI LKNIGVDNPA AKVLVDMSRV QDDEVGDGTT SVTVLAAELL REAESLIAKK 130 140 150 160 170 180 IHPQTIIAGW REATKAAREA LLSSAVDHGS DEVKFRQDLM NIAGTTLSSK LLTHHKDHFT 190 200 210 220 230 240 KLAVEAVLRL KGSGNLEAIH IIKKLGGSLA 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 VKDSRTVYGG GCSEMLMAHA 430 440 450 460 470 480 VTQLANRTPG KEAVAMESYA KALRMLPTII ADNAGYDSAD LVAQLRAAHS EGNTTAGLDM 490 500 510 520 530 REGTIGDMAI LGITESFQVK RQVLLSAAEA AEVILRVDNI IKAAPRKRVP DHHPC

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Maturation of human cyclin E requires the function of eukaryotic chaperonin CCT." Won K.-A., Schumacher R.J., Farr G.W., Horwich A.L., Reed S.I. Mol. Cell. Biol. 18:7584-7589(1998) [PubMed: 9819444] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	"Isolation and expression of a human novel cDNA homologous to the beta subunit of mouse CCT (chaperonin-containing TCP-1)." Xin Y., Yu L., Bi A., Fan Y., Dai F., Zhang M., Zhang Q., Zhao S. Submitted (SEP-1997) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]	"Cloning of human full-length CDSs in BD Creator(TM) system donor vector." Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A. Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[4]	"Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)." Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B. Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Brain.
[6]	Adams M.D., Loftus B.J., Zhou L., Phillips C., Brandon R., Fuhrmann J., Kim U.J., Kerlavage A.R., Venter J.C. Submitted (MAR-1997) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-217.
[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: 12665801] [Abstract] Cited for: PROTEIN SEQUENCE OF 2-20. Tissue: Platelet.
[8]	Bienvenut W.V., Potts A., Quadroni M. Submitted (MAY-2004) to UniProtKB Cited for: PROTEIN SEQUENCE OF 2-13, ACETYLATION AT ALA-2, MASS SPECTROMETRY. Tissue: B-cell lymphoma.
[9]	Lubec G., Afjehi-Sadat L., Chen W.-Q., Sun Y. Submitted (DEC-2008) to UniProtKB Cited for: PROTEIN SEQUENCE OF 26-40; 58-72; 83-131; 139-154; 157-170; 182-189; 192-203; 205-222; 237-250; 285-342; 348-354; 359-402; 406-427; 432-441; 445-466; 482-500 AND 502-516, MASS SPECTROMETRY. Tissue: Brain, Cajal-Retzius cell and Fetal brain cortex.
[10]	"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: 14532270] [Abstract] Cited for: INTERACTION WITH PACRG.
[11]	"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach." Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S. Anal. Chem. 81:4493-4501(2009) [PubMed: 19413330] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, MASS SPECTROMETRY. Tissue: Embryonic kidney.
[12]	"Lysine acetylation targets protein complexes and co-regulates major cellular functions." Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T., Olsen J.V., Mann M. Science 325:834-840(2009) [PubMed: 19608861] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-13; LYS-154 AND LYS-181, MASS SPECTROMETRY.
[13]	"BBS6, BBS10, and BBS12 form a complex with CCT/TRiC family chaperonins and mediate BBSome assembly." Seo S., Baye L.M., Schulz N.P., Beck J.S., Zhang Q., Slusarski D.C., Sheffield V.C. Proc. Natl. Acad. Sci. U.S.A. 107:1488-1493(2010) [PubMed: 20080638] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION, IDENTIFICATION IN BBS/CCT COMPLEX.
[14]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed: 21269460] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF026293 mRNA. Translation: AAC96012.1. AF026166 mRNA. Translation: AAC98906.1. BT019966 mRNA. Translation: AAV38769.1. CR457071 mRNA. Translation: CAG33352.1. BC113514 mRNA. Translation: AAI13515.1. BC113516 mRNA. Translation: AAI13517.1. U91327 Genomic DNA. Translation: AAB67249.1.
IPI	IPI00297779.
RefSeq	NP_006422.1. NM_006431.2.
UniGene	Hs.189772.
3D structure databases
ProteinModelPortal	P78371.
SMR	P78371. Positions 14-526.
ModBase	Search...
Protein-protein interaction databases
IntAct	P78371. 29 interactions.
MINT	MINT-1133770.
STRING	P78371.
PTM databases
PhosphoSite	P78371.
Polymorphism databases
DMDM	6094436.
2D gel databases
SWISS-2DPAGE	P78371.
OGP	P78371.
REPRODUCTION-2DPAGE	IPI00297779.
UCD-2DPAGE	P78371.
Proteomic databases
PeptideAtlas	P78371.
PRIDE	P78371.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000299300; ENSP00000299300; ENSG00000166226.
GeneID	10576.
KEGG	hsa:10576.
UCSC	uc001svb.1. human.
Organism-specific databases
CTD	10576.
GeneCards	GC12P069979.
H-InvDB	HIX0036680.
HGNC	HGNC:1615. CCT2.
HPA	CAB009850. HPA003197. HPA003198.
MIM	605139. gene.
neXtProt	NX_P78371.
PharmGKB	PA26179.
GenAtlas	Search...
Phylogenomic databases
eggNOG	prNOG11386.
HOGENOM	HBG497503.
HOVERGEN	HBG001052.
InParanoid	P78371.
OMA	PRTVYGG.
OrthoDB	EOG47WNNK.
PhylomeDB	P78371.
Enzyme and pathway databases
Reactome	REACT_17015. Metabolism of proteins.
Gene expression databases
ArrayExpress	P78371.
Bgee	P78371.
CleanEx	HS_CCT2.
Genevestigator	P78371.
GermOnline	ENSG00000166226. Homo sapiens.
Family and domain databases
InterPro	IPR012716. Chap_CCT_beta. IPR017998. Chaperone_TCP-1. IPR002194. Chaperonin_TCP-1_CS. IPR002423. Cpn60/TCP-1. [Graphical view]
KO	K09494.
PANTHER	PTHR11353:SF23. Chap_CCT_beta. 1 hit. PTHR11353. Cpn60/TCP-1. 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
NextBio	40141.
SOURCE	Search...

Entry information

Entry name

TCPB_HUMAN

Accession

Primary (citable) accession number: P78371
Secondary accession number(s): Q14D36, Q6IAT3

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 15, 1998
Last sequence update:	January 23, 2007
Last modified:	January 25, 2012
This is version 113 of the entry and version 4 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.