TCPW_HUMAN - dbPTM
TCPW_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID TCPW_HUMAN
UniProt AC Q92526
Protein Name T-complex protein 1 subunit zeta-2
Gene Name CCT6B
Organism Homo sapiens (Human).
Sequence Length 530
Subcellular Localization Cytoplasm.
Protein 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 (By similarity)..
Protein Sequence MAAIKAVNSKAEVARARAALAVNICAARGLQDVLRTNLGPKGTMKMLVSGAGDIKLTKDGNVLLDEMQIQHPTASLIAKVATAQDDVTGDGTTSNVLIIGELLKQADLYISEGLHPRIIAEGFEAAKIKALEVLEEVKVTKEMKRKILLDVARTSLQTKVHAELADVLTEVVVDSVLAVRRPGYPIDLFMVEIMEMKHKLGTDTKLIQGLVLDHGARHPDMKKRVEDAFILICNVSLEYEKTEVNSGFFYKTAEEKEKLVKAERKFIEDRVQKIIDLKDKVCAQSNKGFVVINQKGIDPFSLDSLAKHGIVALRRAKRRNMERLSLACGGMAVNSFEDLTVDCLGHAGLVYEYTLGEEKFTFIEECVNPCSVTLLVKGPNKHTLTQVKDAIRDGLRAIKNAIEDGCMVPGAGAIEVAMAEALVTYKNSIKGRARLGVQAFADALLIIPKVLAQNAGYDPQETLVKVQAEHVESKQLVGVDLNTGEPMVAADAGVWDNYCVKKQLLHSCTVIATNILLVDEIMRAGMSSLK
Overview of Protein Modification Sites with Functional and Structural Information
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure		 ASA (%) Reference Orthologous
Protein Cluster
9PhosphorylationAAIKAVNSKAEVARA
HHHHHHHCHHHHHHH		27.0030622161
35MethylationRGLQDVLRTNLGPKG
HCHHHHHHCCCCCCC		22.78-
38UbiquitinationQDVLRTNLGPKGTMK
HHHHHCCCCCCCCEE		14.2017623298
41UbiquitinationLRTNLGPKGTMKMLV
HHCCCCCCCCEEEEE		66.2827667366
45UbiquitinationLGPKGTMKMLVSGAG
CCCCCCEEEEECCCC		28.9929967540
55UbiquitinationVSGAGDIKLTKDGNV
ECCCCCEEECCCCCE		55.6423000965
58UbiquitinationAGDIKLTKDGNVLLD
CCCEEECCCCCEEEE		74.2521890473
58UbiquitinationAGDIKLTKDGNVLLD
CCCEEECCCCCEEEE		74.2521890473
58UbiquitinationAGDIKLTKDGNVLLD
CCCEEECCCCCEEEE		74.2523000965
73PhosphorylationEMQIQHPTASLIAKV
ECCCCCCCHHHHHHH		27.1030622161
75PhosphorylationQIQHPTASLIAKVAT
CCCCCCHHHHHHHHC		23.8430622161
82UbiquitinationSLIAKVATAQDDVTG
HHHHHHHCCCCCCCC		28.0424816145
104UbiquitinationLIIGELLKQADLYIS
EECHHHHHHCCEECC		56.9429967540
108UbiquitinationELLKQADLYISEGLH
HHHHHCCEECCCCCC		4.6017623298
109PhosphorylationLLKQADLYISEGLHP
HHHHCCEECCCCCCH		11.7121406692
111PhosphorylationKQADLYISEGLHPRI
HHCCEECCCCCCHHH		16.4421406692
116UbiquitinationYISEGLHPRIIAEGF
ECCCCCCHHHHHCCH		33.9222817900
119UbiquitinationEGLHPRIIAEGFEAA
CCCCHHHHHCCHHHH		2.7724816145
144AcetylationVKVTKEMKRKILLDV
CCCCHHHHHHHHHHH		52.197339601
145UbiquitinationKVTKEMKRKILLDVA
CCCHHHHHHHHHHHH		29.9117623298
153UbiquitinationKILLDVARTSLQTKV
HHHHHHHHHHHHHHH		25.3722817900
195UbiquitinationLFMVEIMEMKHKLGT
EEEHHHHHHHHHHCC		51.2224816145
216UbiquitinationGLVLDHGARHPDMKK
HHHHCCCCCCCCHHH		11.8224816145
221UbiquitinationHGARHPDMKKRVEDA
CCCCCCCHHHHHHHE		6.9417623298
224UbiquitinationRHPDMKKRVEDAFIL
CCCCHHHHHHHEEEE		31.3824816145
229UbiquitinationKKRVEDAFILICNVS
HHHHHHEEEEEEEEE		7.8522817900
233UbiquitinationEDAFILICNVSLEYE
HHEEEEEEEEEEEEE		3.5432015554
239PhosphorylationICNVSLEYEKTEVNS
EEEEEEEEECEEECC		28.19-
241UbiquitinationNVSLEYEKTEVNSGF
EEEEEEECEEECCCC		49.4332015554
242UbiquitinationVSLEYEKTEVNSGFF
EEEEEECEEECCCCC		32.9717623298
246PhosphorylationYEKTEVNSGFFYKTA
EECEEECCCCCCCCH		42.0021945579
250NitrationEVNSGFFYKTAEEKE
EECCCCCCCCHHHHH		12.74-
250UbiquitinationEVNSGFFYKTAEEKE
EECCCCCCCCHHHHH		12.7422817900
250PhosphorylationEVNSGFFYKTAEEKE
EECCCCCCCCHHHHH		12.7421945579
250AcetylationEVNSGFFYKTAEEKE
EECCCCCCCCHHHHH		12.7419608861
252PhosphorylationNSGFFYKTAEEKEKL
CCCCCCCCHHHHHHH		28.1127067055
258UbiquitinationKTAEEKEKLVKAERK
CCHHHHHHHHHHHHH		70.4222817900
258AcetylationKTAEEKEKLVKAERK
CCHHHHHHHHHHHHH		70.4219608861
261UbiquitinationEEKEKLVKAERKFIE
HHHHHHHHHHHHHHH		55.7724816145
265UbiquitinationKLVKAERKFIEDRVQ
HHHHHHHHHHHHHHH		42.05-
265AcetylationKLVKAERKFIEDRVQ
HHHHHHHHHHHHHHH		42.057307373
278UbiquitinationVQKIIDLKDKVCAQS
HHHHHHHCHHHHCCC		52.3232015554
287UbiquitinationKVCAQSNKGFVVINQ
HHHCCCCCEEEEEEC		60.0017623298
287AcetylationKVCAQSNKGFVVINQ
HHHCCCCCEEEEEEC		60.0025038526
295AcetylationGFVVINQKGIDPFSL
EEEEEECCCCCCCCH		54.0319608861
295UbiquitinationGFVVINQKGIDPFSL
EEEEEECCCCCCCCH		54.0322817900
301PhosphorylationQKGIDPFSLDSLAKH
CCCCCCCCHHHHHHH		36.3321406692
304PhosphorylationIDPFSLDSLAKHGIV
CCCCCHHHHHHHHHH		35.2021406692
428PhosphorylationALVTYKNSIKGRARL
HHHHCHHCCCCCHHH		22.8622210691
457PhosphorylationVLAQNAGYDPQETLV
HHHHCCCCCHHHHEE		23.2625599653
473PhosphorylationVQAEHVESKQLVGVD
HHHHHCCCCEEECCC		25.3130622161
Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)
Modified Location Modified Residue Modification Type of Upstream Proteins Gene Name of Upstream Proteins UniProt AC of Upstream Proteins Sources

Oops, there are no upstream regulatory protein records of TCPW_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of TCPW_HUMAN !!
Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Modified Location Modification Variant Position
(Distance <= 10) 		Residue Change SAP Related Disease Reference

Oops, there are no SNP-PTM records of TCPW_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
ACADM_HUMANACADMphysical
26344197
ATPG_HUMANATP5C1physical
26344197
TCPB_HUMANCCT2physical
26344197
TCPG_HUMANCCT3physical
26344197
TCPD_HUMANCCT4physical
26344197
TCPZ_HUMANCCT6Aphysical
26344197
TCPH_HUMANCCT7physical
26344197
TCPQ_HUMANCCT8physical
26344197
CLH1_HUMANCLTCphysical
26344197
CP27A_HUMANCYP27A1physical
26344197
DNJA1_HUMANDNAJA1physical
26344197
DNJA4_HUMANDNAJA4physical
26344197
FAS_HUMANFASNphysical
26344197
IDH3A_HUMANIDH3Aphysical
26344197
IMA3_HUMANKPNA4physical
26344197
PRS7_HUMANPSMC2physical
26344197
TCPA_HUMANTCP1physical
26344197
QCR2_HUMANUQCRC2physical
26344197
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of TCPW_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"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-295, AND MASS SPECTROMETRY.

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