CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-007101
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
 BIN3; TCP2; YIL142W 
Created Date
 July 27, 2013 
Organism
 Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) 
NCBI Taxa ID
 559292 
Lysine Modification
Position
Peptide
Type
References
44LGPKGMDKLLQSASSubiquitination[1]
65NDGATILKSIPLDNPubiquitination[1]
242NTTLDTDKVKIFGTKacetylation[2]
249KVKIFGTKFKVDSTAacetylation[2]
263AKLAQLEKAEREKMKacetylation[2]
278NKIAKISKFGINTFIacetylation[2]
396SVLSQTTKETRTVLGubiquitination[1]
413CAEMVMSKAVDTEAQubiquitination[1]
425EAQNIDGKKSLAVEAubiquitination[1]
Reference
 [1] Global analysis of phosphorylation and ubiquitylation cross-talk in protein degradation.
 Swaney DL, Beltrao P, Starita L, Guo A, Rush J, Fields S, Krogan NJ, Villén J.
 Nat Methods. 2013 Jul;10(7):676-82. [PMID: 23749301]
 [2] Proteome-wide analysis of lysine acetylation suggests its broad regulatory scope in Saccharomyces cerevisiae.
 Henriksen P, Wagner SA, Weinert BT, Sharma S, Bacinskaja G, Rehman M, Juffer AH, Walther TC, Lisby M, Choudhary C.
 Mol Cell Proteomics. 2012 Nov;11(11):1510-22. [PMID: 22865919] 
Functional Description
 Molecular chaperone; assists the folding of proteins upon ATP hydrolysis. Known to play a role, in vitro, in the folding of actin and tubulin. In yeast may play a role in mitotic spindle formation. 
Sequence Annotation
  
Keyword
 3D-structure; ATP-binding; Chaperone; Complete proteome; Cytoplasm; Nucleotide-binding; Reference proteome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 527 AA 
Protein Sequence
MSVQIFGDQV TEERAENARL SAFVGAIAVG DLVKSTLGPK GMDKLLQSAS SNTCMVTNDG 60
ATILKSIPLD NPAAKVLVNI SKVQDDEVGD GTTSVTVLSA ELLREAEKLI DQSKIHPQTI 120
IEGYRLASAA ALDALTKAAV DNSHDKTMFR EDLIHIAKTT LSSKILSQDK DHFAELATNA 180
ILRLKGSTNL EHIQIIKILG GKLSDSFLDE GFILAKKFGN NQPKRIENAK ILIANTTLDT 240
DKVKIFGTKF KVDSTAKLAQ LEKAEREKMK NKIAKISKFG INTFINRQLI YDYPEQLFTD 300
LGINSIEHAD FEGVERLALV TGGEVVSTFD EPSKCKLGEC DVIEEIMLGE QPFLKFSGCK 360
AGEACTIVLR GATDQTLDEA ERSLHDALSV LSQTTKETRT VLGGGCAEMV MSKAVDTEAQ 420
NIDGKKSLAV EAFARALRQL PTILADNAGF DSSELVSKLR SSIYNGISTS GLDLNNGTIA 480
DMRQLGIVES YKLKRAVVSS ASEAAEVLLR VDNIIRARPR TANRQHM 527 
Gene Ontology
 GO:0005832; C:chaperonin-containing T-complex; IDA:SGD.
 GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
 GO:0051082; F:unfolded protein binding; IDA:SGD.
 GO:0006457; P:protein folding; IDA:SGD. 
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.