ZBTB2_HUMAN - dbPTM
ZBTB2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ZBTB2_HUMAN
UniProt AC Q8N680
Protein Name Zinc finger and BTB domain-containing protein 2
Gene Name ZBTB2
Organism Homo sapiens (Human).
Sequence Length 514
Subcellular Localization Nucleus .
Protein Description May be involved in transcriptional regulation..
Protein Sequence MDLANHGLILLQQLNAQREFGFLCDCTVAIGDVYFKAHKSVLASFSNYFKMLFVHQTSECVRLKPTDIQPDIFSYLLHLMYTGKMAPQLIDPVRLEQGIKFLHAYPLIQEASLASQGAFSHPDQVFPLASSLYGIQIADHQLRQATKIASAPEKLGRDPRPQTSRISQEQVPEASQLSQLTSNLAQVNRTNMTPSDPLQTSLSPELVSTPVPPPPPGEETNLEASSSDEQPASLTIAHVKPSIMKRNGSFPKYYACHLCGRRFTLRSSLREHLQIHTGVPFTSSQQGESRVPLTLCSNAADLGKDAMEVPEAGMISDSELQHISDSPIIDGQQQSETPPPSDIADIDNLEQADQEREVKRRKYECTICGRKFIQKSHWREHMYIHTGKPFKCSTCDKSFCRANQAARHVCLNQSIDTYTMVDKQTLELCTFEEGSQMDNMLVQTNKPYKCNLCDKTFSTPNEVVKHSCQNQNSDVFALDEGRSILLGSGDSEVTEPDHPVLASIKKEQETVLLD
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
115PhosphorylationIQEASLASQGAFSHP
HHHHHHHHCCCCCCH		34.1517478428
147SumoylationHQLRQATKIASAPEK
HHHHHHHHHHHCHHH		39.0128112733
154SumoylationKIASAPEKLGRDPRP
HHHHCHHHHCCCCCC		56.0028112733
167PhosphorylationRPQTSRISQEQVPEA
CCCCCCCCHHHCCCH		26.9330108239
175PhosphorylationQEQVPEASQLSQLTS
HHHCCCHHHHHHHHH		29.9623401153
178PhosphorylationVPEASQLSQLTSNLA
CCCHHHHHHHHHCHH		18.5930108239
181PhosphorylationASQLSQLTSNLAQVN
HHHHHHHHHCHHHHC		14.1327251275
182PhosphorylationSQLSQLTSNLAQVNR
HHHHHHHHCHHHHCC		38.1427251275
193PhosphorylationQVNRTNMTPSDPLQT
HHCCCCCCCCCCCCC		23.01-
203PhosphorylationDPLQTSLSPELVSTP
CCCCCCCCHHHHCCC		18.98-
264PhosphorylationHLCGRRFTLRSSLRE
HHCCCCEEHHHHHHH		21.3224719451
267PhosphorylationGRRFTLRSSLREHLQ
CCCEEHHHHHHHHHH		36.5221406692
268PhosphorylationRRFTLRSSLREHLQI
CCEEHHHHHHHHHHH		25.6320068231
277PhosphorylationREHLQIHTGVPFTSS
HHHHHHCCCCCCCCC		41.3128555341
282PhosphorylationIHTGVPFTSSQQGES
HCCCCCCCCCCCCCC		22.7723312004
283PhosphorylationHTGVPFTSSQQGESR
CCCCCCCCCCCCCCC		26.9129523821
284PhosphorylationTGVPFTSSQQGESRV
CCCCCCCCCCCCCCC		24.3829523821
289PhosphorylationTSSQQGESRVPLTLC
CCCCCCCCCCCEEEE		45.4629523821
297PhosphorylationRVPLTLCSNAADLGK
CCCEEEECCHHHHCC		32.3928555341
335PhosphorylationIIDGQQQSETPPPSD
CCCCCCCCCCCCCCH		38.8228348404
337PhosphorylationDGQQQSETPPPSDIA
CCCCCCCCCCCCHHC		46.4728348404
341PhosphorylationQSETPPPSDIADIDN
CCCCCCCCHHCCCCC		47.6328112733
362SumoylationEREVKRRKYECTICG
HHHHHHHHHEEEECC		49.8128112733
362SumoylationEREVKRRKYECTICG
HHHHHHHHHEEEECC		49.81-
388AcetylationHMYIHTGKPFKCSTC
CEEEECCCCEECCCC		48.7323236377
388SumoylationHMYIHTGKPFKCSTC
CEEEECCCCEECCCC		48.73-
388SumoylationHMYIHTGKPFKCSTC
CEEEECCCCEECCCC		48.73-
391MethylationIHTGKPFKCSTCDKS
EECCCCEECCCCCHH		35.48115978397
398PhosphorylationKCSTCDKSFCRANQA
ECCCCCHHHHHHHHH		19.1424719451
414PhosphorylationRHVCLNQSIDTYTMV
HHHHHCCCCCEEECC		22.7430108239
417PhosphorylationCLNQSIDTYTMVDKQ
HHCCCCCEEECCCCC		21.1530108239
418PhosphorylationLNQSIDTYTMVDKQT
HCCCCCEEECCCCCE		6.7830108239
419PhosphorylationNQSIDTYTMVDKQTL
CCCCCEEECCCCCEE		16.8930108239
435PhosphorylationLCTFEEGSQMDNMLV
EEEECCCCCCCCEEE		26.1317525332
456PhosphorylationKCNLCDKTFSTPNEV
CCCCCCCCCCCHHHH		15.0122199227
458PhosphorylationNLCDKTFSTPNEVVK
CCCCCCCCCHHHHHH		48.4622199227
459PhosphorylationLCDKTFSTPNEVVKH
CCCCCCCCHHHHHHH		26.4122199227
465SumoylationSTPNEVVKHSCQNQN
CCHHHHHHHHHCCCC		34.6728112733
483PhosphorylationFALDEGRSILLGSGD
EEECCCCEEEECCCC		28.5728450419
488PhosphorylationGRSILLGSGDSEVTE
CCEEEECCCCCCCCC		39.1225159151
491PhosphorylationILLGSGDSEVTEPDH
EEECCCCCCCCCCCC		37.1825159151
494PhosphorylationGSGDSEVTEPDHPVL
CCCCCCCCCCCCCCH		37.4423663014
503PhosphorylationPDHPVLASIKKEQET
CCCCCHHCCCCHHCC		30.6822115753
505SumoylationHPVLASIKKEQETVL
CCCHHCCCCHHCCEE		48.0028112733
505SumoylationHPVLASIKKEQETVL
CCCHHCCCCHHCCEE		48.00-
506SumoylationPVLASIKKEQETVLL
CCHHCCCCHHCCEEC		64.0628112733
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
115SPhosphorylationKinaseATMQ13315
PSP
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ZBTB2_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 ZBTB2_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
P53_HUMANTP53physical
19380588
SP1_HUMANSP1physical
25609694
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 ZBTB2_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"ATM and ATR substrate analysis reveals extensive protein networksresponsive to DNA damage.";
Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III,Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.;
Science 316:1160-1166(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-435, AND MASSSPECTROMETRY.

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