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) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › 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.16
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.14 Ref.16
Subcellular location	Cytoplasm Ref.16.
Sequence similarities	Belongs to the TCP-1 chaperonin family.

Ontologies

Keywords
Cellular component	Cytoplasm
Coding sequence diversity	Alternative splicing
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	'de novo' posttranslational protein folding Traceable author statement. Source: Reactome chaperone-mediated protein complex assembly Inferred from mutant phenotype Ref.16. Source: MGI
Cellular_component	chaperonin-containing T-complex Inferred from electronic annotation. Source: Compara cytosol Non-traceable author statement PubMed 11532003. Source: UniProtKB microtubule Inferred from direct assay PubMed 21525035. Source: UniProtKB 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 PubMed 11532003. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
BBS7	Q8IWZ6	3	EBI-357407,EBI-1806001

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: P78371-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Isoform 2 (identifier: P78371-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-47: Missing.

Note: No experimental confirmation available.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Initiator methionine	1	1	Removed Ref.11 Ref.12
	Chain	2 – 535	534	T-complex protein 1 subunit beta		PRO_0000128316
Amino acid modifications
	Modified residue	2	1	N-acetylalanine Ref.12 Ref.15 Ref.17 Ref.19
	Modified residue	3	1	Phosphoserine Ref.17 Ref.19
	Modified residue	13	1	N6-acetyllysine Ref.15
	Modified residue	154	1	N6-acetyllysine Ref.15
	Modified residue	181	1	N6-acetyllysine Ref.15
	Modified residue	260	1	Phosphoserine Ref.19
	Modified residue	261	1	Phosphothreonine Ref.19
Natural variations
	Alternative sequence	1 – 47	47	Missing in isoform 2.		VSP_042648
Experimental info
	Sequence conflict	51	1	I → T in BAH11729. Ref.4
	Sequence conflict	126	1	I → T in CAG33352. Ref.5
	Sequence conflict	354	1	I → T in BAF83456. Ref.4
	Sequence conflict	438	1	S → P in BAH13640. Ref.4
	Sequence conflict	444	1	R → K in BAG70037. Ref.6
	Sequence conflict	444	1	R → K in BAG70160. Ref.6
	Sequence conflict	504	1	L → P in CAG33352. Ref.5

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [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
	Isoform 2 [UniParc]. Checksum: 5947D87827A365E3	FASTA	488	52,718
	10 20 30 40 50 60 MDKILLSSGR DASLMVTNDG ATILKNIGVD NPAAKVLVDM SRVQDDEVGD GTTSVTVLAA 70 80 90 100 110 120 ELLREAESLI AKKIHPQTII AGWREATKAA REALLSSAVD HGSDEVKFRQ DLMNIAGTTL 130 140 150 160 170 180 SSKLLTHHKD HFTKLAVEAV LRLKGSGNLE AIHIIKKLGG SLADSYLDEG FLLDKKIGVN 190 200 210 220 230 240 QPKRIENAKI LIANTGMDTD KIKIFGSRVR VDSTAKVAEI EHAEKEKMKE KVERILKHGI 250 260 270 280 290 300 NCFINRQLIY NYPEQLFGAA GVMAIEHADF AGVERLALVT GGEIASTFDH PELVKLGSCK 310 320 330 340 350 360 LIEEVMIGED KLIHFSGVAL GEACTIVLRG ATQQILDEAE RSLHDALCVL AQTVKDSRTV 370 380 390 400 410 420 YGGGCSEMLM AHAVTQLANR TPGKEAVAME SYAKALRMLP TIIADNAGYD SADLVAQLRA 430 440 450 460 470 480 AHSEGNTTAG LDMREGTIGD MAILGITESF QVKRQVLLSA AEAAEVILRV DNIIKAAPRK RVPDHHPC

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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[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] (ISOFORM 1).
[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] (ISOFORM 1).
[4]	"Complete sequencing and characterization of 21,243 full-length human cDNAs." Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S. Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2). Tissue: Amygdala and Testis.
[5]	"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] (ISOFORM 1).
[6]	"Human protein factory for converting the transcriptome into an in vitro-expressed proteome." Goshima N., Kawamura Y., Fukumoto A., Miura A., Honma R., Satoh R., Wakamatsu A., Yamamoto J., Kimura K., Nishikawa T., Andoh T., Iida Y., Ishikawa K., Ito E., Kagawa N., Kaminaga C., Kanehori K., Kawakami B. , Kenmochi K., Kimura R., Kobayashi M., Kuroita T., Kuwayama H., Maruyama Y., Matsuo K., Minami K., Mitsubori M., Mori M., Morishita R., Murase A., Nishikawa A., Nishikawa S., Okamoto T., Sakagami N., Sakamoto Y., Sasaki Y., Seki T., Sono S., Sugiyama A., Sumiya T., Takayama T., Takayama Y., Takeda H., Togashi T., Yahata K., Yamada H., Yanagisawa Y., Endo Y., Imamoto F., Kisu Y., Tanaka S., Isogai T., Imai J., Watanabe S., Nomura N. Nat. Methods 5:1011-1017(2008) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
[7]	"The finished DNA sequence of human chromosome 12." Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R. , Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K., Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D., Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J., Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A., Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M., Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I., Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A., Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G., Gibbs R.A. Nature 440:346-351(2006) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[8]	Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[9]	"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] (ISOFORM 1). Tissue: Brain.
[10]	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.
[11]	"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] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 2-20. Tissue: Platelet.
[12]	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.
[13]	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.
[14]	"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] [Europe PMC] [Abstract] Cited for: INTERACTION WITH PACRG.
[15]	"Lysine acetylation targets protein complexes and co-regulates major cellular functions." Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M. Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2; LYS-13; LYS-154 AND LYS-181, MASS SPECTROMETRY.
[16]	"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] [Europe PMC] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION, IDENTIFICATION IN BBS/CCT COMPLEX.
[17]	"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis." Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M. Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-3, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[18]	"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] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[19]	"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation." Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B. Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-3; SER-260 AND THR-261, MASS SPECTROMETRY.
+	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. AK290767 mRNA. Translation: BAF83456.1. AK294307 mRNA. Translation: BAH11729.1. AK302157 mRNA. Translation: BAH13640.1. AK316397 mRNA. Translation: BAH14768.1. AK316408 mRNA. Translation: BAH14779.1. CR457071 mRNA. Translation: CAG33352.1. AB451223 mRNA. Translation: BAG70037.1. AB451346 mRNA. Translation: BAG70160.1. AC018921 Genomic DNA. No translation available. CH471054 Genomic DNA. Translation: EAW97230.1. BC113514 mRNA. Translation: AAI13515.1. BC113516 mRNA. Translation: AAI13517.1. U91327 Genomic DNA. Translation: AAB67249.1.
IPI	IPI00297779. IPI00981169.
RefSeq	NP_001185771.1. NM_001198842.1. NP_006422.1. NM_006431.2.
UniGene	Hs.189772.
3D structure databases
ProteinModelPortal	P78371.
ModBase	Search...
Protein-protein interaction databases
IntAct	P78371. 44 interactions.
MINT	MINT-1133770.
STRING	9606.ENSP00000299300.
PTM databases
PhosphoSite	P78371.
Polymorphism databases
DMDM	6094436.
2D gel databases
OGP	P78371.
REPRODUCTION-2DPAGE	IPI00297779.
SWISS-2DPAGE	P78371.
UCD-2DPAGE	P78371.
Proteomic databases
PaxDb	P78371.
PeptideAtlas	P78371.
PRIDE	P78371.
Protocols and materials databases
DNASU	10576.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000299300; ENSP00000299300; ENSG00000166226. ENST00000543146; ENSP00000445471; ENSG00000166226.
GeneID	10576.
KEGG	hsa:10576.
UCSC	uc001svb.1. human.
Organism-specific databases
CTD	10576.
GeneCards	GC12P069979.
HGNC	HGNC:1615. CCT2.
HPA	CAB009850. HPA003197. HPA003198.
MIM	605139. gene.
neXtProt	NX_P78371.
PharmGKB	PA26179.
GenAtlas	Search...
Phylogenomic databases
eggNOG	COG0459.
HOGENOM	HOG000226736.
HOVERGEN	HBG001052.
InParanoid	P78371.
KO	K09494.
OMA	NIIRAKP.
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]
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. human.
GenomeRNAi	10576.
NextBio	40141.
SOURCE	Search...

Entry information

Entry name

TCPB_HUMAN

Accession

Primary (citable) accession number: P78371
Secondary accession number(s): A8K402 , B5BTY7, B7Z243, B7Z7K4, B7ZAT2, Q14D36, Q6IAT3

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 15, 1998
Last sequence update:	January 23, 2007
Last modified:	May 1, 2013
This is version 127 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.