CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-014194
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 T-complex protein 1 subunit beta 
Protein Synonyms/Alias
 TCP-1-beta; CCT-beta 
Gene Name
 Cct2 
Gene Synonyms/Alias
 Cctb 
Created Date
 July 27, 2013 
Organism
 Rattus norvegicus (Rat) 
NCBI Taxa ID
 10116 
Lysine Modification
Position
Peptide
Type
References
13LAPVNIFKAGADEERacetylation[1]
119EAESLIAKKIHPQTIacetylation[1]
176SKLLTHHKDHFTKLAacetylation[1]
203LEAIHVIKKLGGSLAacetylation[1]
222DEGFLLDKKIGVNQPacetylation[1]
248NTGMDTDKIKIFGSRacetylation[1]
272AEIEHAEKEKMKEKVacetylation[1]
Reference
 [1] Proteomic analysis of lysine acetylation sites in rat tissues reveals organ specificity and subcellular patterns.
 Lundby A, Lage K, Weinert BT, Bekker-Jensen DB, Secher A, Skovgaard T, Kelstrup CD, Dmytriyev A, Choudhary C, Lundby C, Olsen JV.
 Cell Rep. 2012 Aug 30;2(2):419-31. [PMID: 22902405] 
Functional Description
 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). 
Sequence Annotation
 MOD_RES 2 2 N-acetylalanine (By similarity).
 MOD_RES 3 3 Phosphoserine (By similarity).
 MOD_RES 13 13 N6-acetyllysine (By similarity).
 MOD_RES 154 154 N6-acetyllysine (By similarity).
 MOD_RES 181 181 N6-acetyllysine (By similarity).
 MOD_RES 260 260 Phosphoserine (By similarity).
 MOD_RES 261 261 Phosphothreonine (By similarity).  
Keyword
 Acetylation; ATP-binding; Chaperone; Complete proteome; Cytoplasm; Direct protein sequencing; Nucleotide-binding; Phosphoprotein; Reference proteome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 535 AA 
Protein Sequence
MASLSLAPVN IFKAGADEER AETARLSSFI GAIAIGDLVK STLGPKGMDK ILLSSGRDAS 60
LMVTNDGATI LKNIGVDNPA AKVLVDMSRV QDDEVGDGTT SVTVLAAELL REAESLIAKK 120
IHPQTIIAGW REATKAAREA LLSSAVDHGS DEVKFWQDLM NIAGTTLSSK LLTHHKDHFT 180
KLAVEAVLRL KGSGNLEAIH VIKKLGGSLA DSYLDEGFLL DKKIGVNQPK RIENAKILIA 240
NTGMDTDKIK IFGSRVRVDS TAKVAEIEHA EKEKMKEKVE RILKHGINCF INRQLIYNYP 300
EQLFGAAGVM AIEHADFAGV ERLALVTGGE IASTFDHPEL VKLGSCKLIE EVMIGEDKLI 360
HFSGVALGEA CTIVLRGATQ QILDEAERSL HDALCVLAQT VKDPRTVYGG GCSEMLMAHA 420
VTMLASRTPG KEAVAMESFA KALRMLPTII ADNAGYDSAD LVAQLRAAHS EGRITAGLDM 480
KEGSIGDMAV LGITESFQVK RQVLLSAAEA AEVILRVDNI IKAAPRKRVP DHHPC 535 
Gene Ontology
 GO:0005832; C:chaperonin-containing T-complex; IEA:Compara.
 GO:0005874; C:microtubule; IEA:Compara.
 GO:0005634; C:nucleus; IEA:Compara.
 GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
 GO:0051131; P:chaperone-mediated protein complex assembly; IEA:Compara.
 GO:0006457; P:protein folding; IEA:InterPro. 
Interpro
 IPR012716; 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. 
Pfam
 PF00118; Cpn60_TCP1 
SMART
  
PROSITE
 PS00750; TCP1_1
 PS00751; TCP1_2
 PS00995; TCP1_3 
PRINTS
 PR00304; TCOMPLEXTCP1.