ZBTB5_HUMAN - dbPTM
ZBTB5_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ZBTB5_HUMAN
UniProt AC O15062
Protein Name Zinc finger and BTB domain-containing protein 5
Gene Name ZBTB5
Organism Homo sapiens (Human).
Sequence Length 677
Subcellular Localization Nucleus .
Protein Description May be involved in transcriptional regulation..
Protein Sequence MDFPGHFEQIFQQLNYQRLHGQLCDCVIVVGNRHFKAHRSVLAACSTHFRALFSVAEGDQTMNMIQLDSEVVTAEAFAALIDMMYTSTLMLGESNVMDVLLAASHLHLNSVVKACKHYLTTRTLPMSPPSERVQEQSARMQRSFMLQQLGLSIVSSALNSSQNGEEQPAPMSSSMRSNLDQRTPFPMRRLHKRKQSAEERARQRLRPSIDESAISDVTPENGPSGVHSREEFFSPDSLKIVDNPKADGMTDNQEDSAIMFDQSFGTQEDAQVPSQSDNSAGNMAQLSMASRATQVETSFDQEAAPEKSSFQCENPEVGLGEKEHMRVVVKSEPLSSPEPQDEVSDVTSQAEGSESVEVEGVVVSAEKIDLSPESSDRSFSDPQSSTDRVGDIHILEVTNNLEHKSTFSISNFLNKSRGNNFTANQNNDDNIPNTTSDCRLESEAPYLLSPEAGPAGGPSSAPGSHVENPFSEPADSHFVRPMQEVMGLPCVQTSGYQGGEQFGMDFSRSGLGLHSSFSRVMIGSPRGGASNFPYYRRIAPKMPVVTSVRSSQIPENSTSSQLMMNGATSSFENGHPSQPGPPQLTRASADVLSKCKKALSEHNVLVVEGARKYACKICCKTFLTLTDCKKHIRVHTGEKPYACLKCGKRFSQSSHLYKHSKTTCLRWQSSNLPSTLL
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
118PhosphorylationVVKACKHYLTTRTLP
HHHHHHHHHHHCCCC
7.40-
123PhosphorylationKHYLTTRTLPMSPPS
HHHHHHCCCCCCCCH
32.8723403867
127PhosphorylationTTRTLPMSPPSERVQ
HHCCCCCCCCHHHHH
31.5520044836
130PhosphorylationTLPMSPPSERVQEQS
CCCCCCCHHHHHHHH
41.2323403867
143PhosphorylationQSARMQRSFMLQQLG
HHHHHHHHHHHHHHH
9.7122210691
155PhosphorylationQLGLSIVSSALNSSQ
HHHHHHHHHHHHCCC
14.2822210691
173PhosphorylationEQPAPMSSSMRSNLD
CCCCCCCHHHHCCCC
23.1522210691
183PhosphorylationRSNLDQRTPFPMRRL
HCCCCCCCCCCHHHH
24.5328555341
208PhosphorylationARQRLRPSIDESAIS
HHHHHCCCCCHHHHC
35.9228450419
212PhosphorylationLRPSIDESAISDVTP
HCCCCCHHHHCCCCC
27.4425394399
215PhosphorylationSIDESAISDVTPENG
CCCHHHHCCCCCCCC
26.2420873877
218PhosphorylationESAISDVTPENGPSG
HHHHCCCCCCCCCCC
29.8520873877
224PhosphorylationVTPENGPSGVHSREE
CCCCCCCCCCCCCCC
55.6420873877
228PhosphorylationNGPSGVHSREEFFSP
CCCCCCCCCCCCCCC
38.6920873877
234PhosphorylationHSREEFFSPDSLKIV
CCCCCCCCCCCCEEC
32.8730266825
237PhosphorylationEEFFSPDSLKIVDNP
CCCCCCCCCEECCCC
34.6430266825
239SumoylationFFSPDSLKIVDNPKA
CCCCCCCEECCCCCC
44.6428112733
239UbiquitinationFFSPDSLKIVDNPKA
CCCCCCCEECCCCCC
44.6421906983
245SumoylationLKIVDNPKADGMTDN
CEECCCCCCCCCCCC
66.42-
297PhosphorylationSRATQVETSFDQEAA
HHHHCCCCCCCCCCC
35.5229978859
298PhosphorylationRATQVETSFDQEAAP
HHHCCCCCCCCCCCC
17.2021815630
307UbiquitinationDQEAAPEKSSFQCEN
CCCCCCCCCCCCCCC
50.79-
308PhosphorylationQEAAPEKSSFQCENP
CCCCCCCCCCCCCCC
34.4225627689
309PhosphorylationEAAPEKSSFQCENPE
CCCCCCCCCCCCCCC
30.3325627689
322SumoylationPEVGLGEKEHMRVVV
CCCCCCCCCCEEEEE
51.6328112733
322UbiquitinationPEVGLGEKEHMRVVV
CCCCCCCCCCEEEEE
51.63-
330SumoylationEHMRVVVKSEPLSSP
CCEEEEEECCCCCCC
37.1828112733
335PhosphorylationVVKSEPLSSPEPQDE
EEECCCCCCCCCCCC
55.34-
371PhosphorylationSAEKIDLSPESSDRS
EEEEEECCCCCCCCC
23.9123401153
374PhosphorylationKIDLSPESSDRSFSD
EEECCCCCCCCCCCC
40.7120873877
375PhosphorylationIDLSPESSDRSFSDP
EECCCCCCCCCCCCC
35.0720873877
378PhosphorylationSPESSDRSFSDPQSS
CCCCCCCCCCCCCCC
33.8121815630
380PhosphorylationESSDRSFSDPQSSTD
CCCCCCCCCCCCCCC
50.0227732954
384PhosphorylationRSFSDPQSSTDRVGD
CCCCCCCCCCCCCCC
40.3627732954
385PhosphorylationSFSDPQSSTDRVGDI
CCCCCCCCCCCCCCE
29.1327732954
386PhosphorylationFSDPQSSTDRVGDIH
CCCCCCCCCCCCCEE
32.8327732954
404SumoylationVTNNLEHKSTFSISN
EECCCCCCCCEEHHH
41.6428112733
408PhosphorylationLEHKSTFSISNFLNK
CCCCCCEEHHHHHHH
25.7928555341
415UbiquitinationSISNFLNKSRGNNFT
EHHHHHHHCCCCCCC
43.61-
415SumoylationSISNFLNKSRGNNFT
EHHHHHHHCCCCCCC
43.6128112733
493PhosphorylationMGLPCVQTSGYQGGE
HCCCEEECCCCCCCH
12.0624043423
494PhosphorylationGLPCVQTSGYQGGEQ
CCCEEECCCCCCCHH
20.5724043423
496PhosphorylationPCVQTSGYQGGEQFG
CEEECCCCCCCHHCC
12.0724043423
507PhosphorylationEQFGMDFSRSGLGLH
HHCCCCCCCCCCCCC
22.6724043423
509PhosphorylationFGMDFSRSGLGLHSS
CCCCCCCCCCCCCCC
36.8523186163
515PhosphorylationRSGLGLHSSFSRVMI
CCCCCCCCCCEEEEE
37.8128450419
516PhosphorylationSGLGLHSSFSRVMIG
CCCCCCCCCEEEEEC
19.2523403867
518PhosphorylationLGLHSSFSRVMIGSP
CCCCCCCEEEEECCC
26.3923186163
524PhosphorylationFSRVMIGSPRGGASN
CEEEEECCCCCCCCC
10.6628985074
526MethylationRVMIGSPRGGASNFP
EEEECCCCCCCCCCC
58.8554560775
541SumoylationYYRRIAPKMPVVTSV
HHHHCCCCCCEEEEE
46.98-
541SumoylationYYRRIAPKMPVVTSV
HHHHCCCCCCEEEEE
46.9828112733
594SumoylationASADVLSKCKKALSE
HHHHHHHHHHHHHHH
46.0128112733
594UbiquitinationASADVLSKCKKALSE
HHHHHHHHHHHHHHH
46.01-
597UbiquitinationDVLSKCKKALSEHNV
HHHHHHHHHHHHCCE
65.12-
597SumoylationDVLSKCKKALSEHNV
HHHHHHHHHHHHCCE
65.1228112733
636PhosphorylationKKHIRVHTGEKPYAC
HHHEEEECCCCCEEE
44.1529214152
641PhosphorylationVHTGEKPYACLKCGK
EECCCCCEEEECCCC
22.4821253578
645SumoylationEKPYACLKCGKRFSQ
CCCEEEECCCCCCCC
40.6028112733
645SumoylationEKPYACLKCGKRFSQ
CCCEEEECCCCCCCC
40.60-
658SumoylationSQSSHLYKHSKTTCL
CCCHHHHHCCCCCHH
48.0028112733

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 ZBTB5_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ZBTB5_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 ZBTB5_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
CC85B_HUMANCCDC85Bphysical
16189514
JADE2_HUMANJADE2physical
20211142
SWP70_HUMANSWAP70physical
25416956
ZBT7B_HUMANZBTB7Bphysical
25416956

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 ZBTB5_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions.";
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.;
Sci. Signal. 2:RA46-RA46(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-371, AND MASSSPECTROMETRY.

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