Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures
Basic Information
Protein Name :  T-complex protein 1 subunit beta  

UniProtKB / Swiss-Prot ID :  TCPB_HUMAN

Gene Name (Synonyms) : 
CCT2, 99D8.1, CCTB  

Species :  Homo sapiens (Human). 

Subcellular Localization :  Cytoplasm. 

Protein 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. 

Protein Sequence MASLSLAPVNIFKAGADEERAETARLTSFIGAIAIGDLVKSTLGPKGMDKILLSSGRDASLMVTNDGATI...
Predicted Secondary Structure CCHHHCCCHHHHCCCCCEEECHHHHHHHHHHHHHHHHHHHHCCCCCCCEEEEECCCCCCCEEEEECHHHH...
Protein Variant -
- top -

Overview of Protein Modification Sites with Functional and Structural Information
Accessible Surface Area (ASA)
Pred. Secondary
Real Secondary
Disorder Prediction
Protein Domain
&
Experimental PTM Sites
Predicted PTM Sites
- top -

Experimental Post-Translational Modification Sites Download
Locations
Modification
Substrate Sites
&
Secondary Structure
Accessible Surface Area (%)
Resource
Reference
Structural Characterization
Orthologous
Protein Cluster
2N-acetylalanine.---MASLSL
---CCHHHC
21.12UniProtKB
Link-
3Phosphoserine--MASLSLA
--CCHHHCC
19.72HPRD
Link-
3Phosphoserine--MASLSLA
--CCHHHCC
19.72Phosphositeplus
Link-
13Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)VNIFKAGAD
HHHHCCCCC
41.96Phosphositeplus
Link-
13N6-acetyllysineVNIFKAGAD
HHHHCCCCC
41.96HPRD
Link-
13N6-acetyllysineVNIFKAGAD
HHHHCCCCC
41.96Phosphositeplus
Link-
13N6-acetyllysine.VNIFKAGAD
HHHHCCCCC
41.96UniProtKB
Link-
40Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)GDLVKSTLG
HHHHHHCCC
45.05Phosphositeplus
Link-
72Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)ATILKNIGV
HHHHHHCCC
42.54Phosphositeplus
Link-
82Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)NPAAKVLVD
CHHHHHHHH
37.90Phosphositeplus
Link-
115PhosphoserineREAESLIAK
HHHHHHHHC
31.93HPRD
Link-
115PhosphoserineREAESLIAK
HHHHHHHHC
31.93Phosphositeplus
Link-
119Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)SLIAKKIHP
HHHHCCCCH
45.31Phosphositeplus
Link-
120Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)LIAKKIHPQ
HHHCCCCHH
36.91Phosphositeplus
Link-
143PhosphoserineEALLSSAVD
HHHHHHCCC
19.66HPRD
Link-
150PhosphoserineVDHGSDEVK
CCCCCCCCC
27.46HPRD
Link-
150PhosphoserineVDHGSDEVK
CCCCCCCCC
27.46Phosphositeplus
Link-
154Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)SDEVKFRQD
CCCCCCHHH
32.55Phosphositeplus
Link-
154N6-acetyllysineSDEVKFRQD
CCCCCCHHH
32.55HPRD
Link-
154N6-acetyllysineSDEVKFRQD
CCCCCCHHH
32.55Phosphositeplus
Link-
154N6-acetyllysine.SDEVKFRQD
CCCCCCHHH
32.55UniProtKB
Link-
181N6-acetyllysineDHFTKLAVE
HHHHHHHHC
33.24HPRD
Link-
181N6-acetyllysineDHFTKLAVE
HHHHHHHHC
33.24Phosphositeplus
Link-
181N6-acetyllysine.DHFTKLAVE
HHHHHHHHC
33.24UniProtKB
Link-
191Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)VLRLKGSGN
EEEEECCCC
44.59Phosphositeplus
Link-
203Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)IHIIKKLGG
EEEEEECCC
41.14Phosphositeplus
Link-
204Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)HIIKKLGGS
EEEEECCCE
41.79Phosphositeplus
Link-
222Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)FLLDKKIGV
EEECCCCCC
46.38Phosphositeplus
Link-
236Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)IENAKILIA
EECCEEEEE
50.02Phosphositeplus
Link-
248Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)MDTDKIKIF
CCCCCCCCC
48.25Phosphositeplus
Link-
250Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)TDKIKIFGS
CCCCCCCCC
37.41Phosphositeplus
Link-
260PhosphoserineVRVDSTAKV
EEECCHHHH
27.66HPRD
Link-
260PhosphoserineVRVDSTAKV
EEECCHHHH
27.66Phosphositeplus
Link-
260PhosphoserineVRVDSTAKV
EEECCHHHH
27.66SysPTM
Link-
261PhosphothreonineRVDSTAKVA
EECCHHHHH
26.49Phosphositeplus
Link-
263Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)DSTAKVAEI
CCHHHHHHH
41.91Phosphositeplus
Link-
284Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)ERILKHGIN
HHHHHCCCC
37.10Phosphositeplus
Link-
297PhosphotyrosineRQLIYNYPE
CCCHHHHHH
19.75Phosphositeplus
Link-
342Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)PELVKLGSC
CCHHHCCCC
60.81Phosphositeplus
Link-
379PhosphothreonineLRGATQQIL
EECCCHHHH
24.67Phosphositeplus
Link-
402Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)AQTVKDSRT
HHHHHCCCE
54.06Phosphositeplus
Link-
431Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)RTPGKEAVA
CCCHHHHHH
43.64Phosphositeplus
Link-
441Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)ESYAKALRM
HHHHHHHHH
39.46Phosphositeplus
Link-
522Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)DNIIKAAPR
HHHHHCCCC
34.40Phosphositeplus
Link-
- top -

Protein-Protein Interactions
      Interacting Protein      
Interaction type
Source ID
      Resource      
      Pubmed ID      
Domain-Domain Interactions
M3K3_HUMANphysical interactionMINT-48487MINT14743216
ACTB_HUMANin vitro
in vivo
HPRD:06895HPRD10748209
11580269
TCPD_HUMANENSP00000299300STRING
TCPH_HUMANENSP00000299300STRING
TCPE_HUMANENSP00000299300STRING
ACTB_HUMANENSP00000299300STRING
- top -

Disease Reference
Kegg disease
There are no disease associations of PTM sites.
Drug Reference
There are no disease associations of PTM sites.
- top -
Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach.";
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.;
Anal. Chem. 81:4493-4501(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, AND MASS SPECTROMETRY.
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions.";
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.;
Science 325:834-840(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-13; LYS-154 AND LYS-181, ANDMASS SPECTROMETRY.
- top -
Basic Information | Overview of PTM Sites | Experimental PTM Sites | Protein-Protein Interactions | Drug and Disease Associations | Related Literatures