ZN536_HUMAN - dbPTM
ZN536_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ZN536_HUMAN
UniProt AC O15090
Protein Name Zinc finger protein 536
Gene Name ZNF536
Organism Homo sapiens (Human).
Sequence Length 1300
Subcellular Localization Nucleus .
Protein Description May be involved in transcriptional regulation. Recognizes and binds 2 copies of the core DNA sequence 5'-CCCCCA-3'..
Protein Sequence MEEASLCLGVSSAEPEAEPHLSGPVLNGQYAMSQKLHQITSQLSHAFPELHPRPNPEEKPPASLEEKAHVPMSGQPMGSQMALLANQLGREVDTSLNGRVDLQQFLNGQNLGIMSQMSDIEDDARKNRKYPCPLCGKRFRFNSILSLHMRTHTGEKPFKCPYCDHRAAQKGNLKIHLRTHKLGNLGKGRGRVREENRLLHELEERAILRDKQLKGSLLQPRPDLKPPPHAQQAPLAACTLALQANHSVPDVAHPVPSPKPASVQEDAVAPAAGFRCTFCKGKFKKREELDRHIRILHKPYKCTLCDFAASQEEELISHVEKAHITAESAQGQGPNGGGEQSANEFRCEVCGQVFSQAWFLKGHMRKHKDSFEHCCQICGRRFKEPWFLKNHMKVHLNKLSVKNKSPSDPEVPVPMGGMSQEAHANLYSRYLSCLQSGFMTPDKAGLSEPSQLYGKGELPMKEKEALGKLLSPISSMAHGVPEGDKHSLLGCLNLVPPLKSSCIERLQAAAKAAEMDPVNSYQAWQLMARGMAMEHGFLSKEHPLQRNHEDTLANAGVLFDKEKREYVLVGADGSKQKMPADLVHSTKVGSQRDLPSKLDPLESSRDFLSHGLNQTLEYNLQGPGNMKEKPTECPDCGRVFRTYHQVVVHSRVHKRDRKGEEDGLHVGLDERRGSGSDQESQSVSRSTTPGSSNVTEESGVGGGLSQTGSAQEDSPHPSSPSSSDIGEEAGRSAGVQQPALLRDRSLGSAMKDCPYCGKTFRTSHHLKVHLRIHTGEKPYKCPHCDYAGTQSASLKYHLERHHRERQNGAGPLSGQPPNQDHKDEMSSKASLFIRPDILRGAFKGLPGIDFRGGPASQQWTSGVLSSGDHSGQATGMSSEVPSDALKGTDLPSKSTHFSEIGRAYQSIVSNGVNFQGSLQAFMDSFVLSSLKKEKDMKDKALADPPSMKVHGVDGGEEKPSGKSSQRKSEKSQYEPLDLSVRPDAASLPGSSVTVQDSIAWHGCLFCAFTTSSMELMALHLQANHLGKAKRKDNTIGVTVNCKDQAREASKMALLPSLQSNKDLGLSNMISSLDSASEKMAQGQLKETLGEQKSGAWTGHVDPAFCNFPSDFYKQFGVYPGMVGSGASSSCPNKEPDGKAHSEEDVPILIPETTSKNTTDDLSDIASSEDMDSSKGENNDEEDVETEPEMMTKPLSALSKDSSSDGGDSLQPTGTSQPVQGLVSPLSQAPEKQWHSQGLLQAQDPLAGLPKPERGPQSLDKPMNMLSVLRAYSSDGLAAFNGLASSTANSGCIKRPDLCGK
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
5Phosphorylation---MEEASLCLGVSS
---CCCCCEEECCCC
23.93-
151PhosphorylationILSLHMRTHTGEKPF
CEEEEECCCCCCCCC
19.0623312004
153PhosphorylationSLHMRTHTGEKPFKC
EEEECCCCCCCCCCC
46.5629496963
211UbiquitinationERAILRDKQLKGSLL
HHHHHCCCCCCCCCC
51.6129967540
257PhosphorylationDVAHPVPSPKPASVQ
CCCCCCCCCCCCCCC
45.8724719451
405PhosphorylationKLSVKNKSPSDPEVP
HCCCCCCCCCCCCCC
38.7423403867
407PhosphorylationSVKNKSPSDPEVPVP
CCCCCCCCCCCCCCC
73.2623403867
419PhosphorylationPVPMGGMSQEAHANL
CCCCCCCCHHHHHHH
28.3029978859
427PhosphorylationQEAHANLYSRYLSCL
HHHHHHHHHHHHHHH
7.3023403867
428PhosphorylationEAHANLYSRYLSCLQ
HHHHHHHHHHHHHHH
20.0224719451
436PhosphorylationRYLSCLQSGFMTPDK
HHHHHHHHCCCCCCC
22.5027732954
440PhosphorylationCLQSGFMTPDKAGLS
HHHHCCCCCCCCCCC
26.5227732954
596PhosphorylationGSQRDLPSKLDPLES
CCCCCCCCCCCCCHH
53.8224719451
631PhosphorylationGNMKEKPTECPDCGR
CCCCCCCCCCCCHHH
62.3828787133
674PhosphorylationGLDERRGSGSDQESQ
CCCCCCCCCCCCCCC
33.0622496350
676PhosphorylationDERRGSGSDQESQSV
CCCCCCCCCCCCCCC
37.5120363803
680PhosphorylationGSGSDQESQSVSRST
CCCCCCCCCCCCCCC
23.32-
682PhosphorylationGSDQESQSVSRSTTP
CCCCCCCCCCCCCCC
31.1927732954
684PhosphorylationDQESQSVSRSTTPGS
CCCCCCCCCCCCCCC
26.2627732954
774PhosphorylationKVHLRIHTGEKPYKC
EEEEEEECCCCCCCC
44.6729496963
826PhosphorylationQDHKDEMSSKASLFI
CCCCHHHHHHHHEEC
27.0022817900
827PhosphorylationDHKDEMSSKASLFIR
CCCHHHHHHHHEECC
30.8222817900
874PhosphorylationGDHSGQATGMSSEVP
CCCCCCCCCCCCCCC
26.06-
892PhosphorylationLKGTDLPSKSTHFSE
HCCCCCCCCCCCHHH
46.6824719451
928PhosphorylationFMDSFVLSSLKKEKD
HHHHHHHHHHHHHHH
28.4624719451
967AcetylationSGKSSQRKSEKSQYE
CCCCCCCCCCCCCCC
56.167365035
973PhosphorylationRKSEKSQYEPLDLSV
CCCCCCCCCCCCCCC
26.97-
1042UbiquitinationIGVTVNCKDQAREAS
EEEEEECHHHHHHHH
47.90-
1093PhosphorylationETLGEQKSGAWTGHV
HHHCCCCCCCCCCCC
33.1822468782
1097PhosphorylationEQKSGAWTGHVDPAF
CCCCCCCCCCCCHHH
19.5122468782
1109PhosphorylationPAFCNFPSDFYKQFG
HHHCCCCHHHHHHHC
35.8922468782
1141PhosphorylationEPDGKAHSEEDVPIL
CCCCCCCCCCCCCEE
47.7629255136
1162PhosphorylationKNTTDDLSDIASSED
CCCCCCHHHHHCCCC
33.6825921289
1166PhosphorylationDDLSDIASSEDMDSS
CCHHHHHCCCCCCCC
34.3025921289
1167PhosphorylationDLSDIASSEDMDSSK
CHHHHHCCCCCCCCC
28.7025921289
1172PhosphorylationASSEDMDSSKGENND
HCCCCCCCCCCCCCC
27.5825921289
1201PhosphorylationLSALSKDSSSDGGDS
HHHHCCCCCCCCCCC
35.1627732954
1202PhosphorylationSALSKDSSSDGGDSL
HHHCCCCCCCCCCCC
42.4527732954
1203PhosphorylationALSKDSSSDGGDSLQ
HHCCCCCCCCCCCCC
44.2027732954
1208PhosphorylationSSSDGGDSLQPTGTS
CCCCCCCCCCCCCCC
31.9827732954
1223PhosphorylationQPVQGLVSPLSQAPE
CCCCHHCCCHHHCCH
25.7627732954
1226PhosphorylationQGLVSPLSQAPEKQW
CHHCCCHHHCCHHHH
27.9027732954
1266PhosphorylationDKPMNMLSVLRAYSS
CCCCHHHHHHHHHCC
14.3424719451
1266O-linked_GlycosylationDKPMNMLSVLRAYSS
CCCCHHHHHHHHHCC
14.3430379171

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 ZN536_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ZN536_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 ZN536_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of ZN536_HUMAN !!

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 ZN536_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-826 AND SER-827, ANDMASS SPECTROMETRY.

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