ZKSC5_HUMAN - dbPTM
ZKSC5_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ZKSC5_HUMAN
UniProt AC Q9Y2L8
Protein Name Zinc finger protein with KRAB and SCAN domains 5
Gene Name ZKSCAN5
Organism Homo sapiens (Human).
Sequence Length 839
Subcellular Localization Nucleus .
Protein Description May be involved in transcriptional regulation..
Protein Sequence MIMTESREVIDLDPPAETSQEQEDLFIVKVEEEDCTWMQEYNPPTFETFYQRFRHFQYHEASGPREALSQLRVLCCEWLRPELHTKEQILELLVLEQFLTILPEEFQPWVREHHPESGEEAVAVIENIQRELEERRQQIVACPDVLPRKMATPGAVQESCSPHPLTVDTQPEQAPQKPRLLEENALPVLQVPSLPLKDSQELTASLLSTGSQKLVKIEEVADVAVSFILEEWGHLDQSQKSLYRDDRKENYGSITSMGYESRDNMELIVKQISDDSESHWVAPEHTERSVPQDPDFAEVSDLKGMVQRWQVNPTVGKSRQNPSQKRDLDAITDISPKQSTHGERGHRCSDCGKFFLQASNFIQHRRIHTGEKPFKCGECGKSYNQRVHLTQHQRVHTGEKPYKCQVCGKAFRVSSHLVQHHSVHSGERPYGCNECGKNFGRHSHLIEHLKRHFREKSQRCSDKRSKNTKLSVKKKISEYSEADMELSGKTQRNVSQVQDFGEGCEFQGKLDRKQGIPMKEILGQPSSKRMNYSEVPYVHKKSSTGERPHKCNECGKSFIQSAHLIQHQRIHTGEKPFRCEECGKSYNQRVHLTQHQRVHTGEKPYTCPLCGKAFRVRSHLVQHQSVHSGERPFKCNECGKGFGRRSHLAGHLRLHSREKSHQCRECGEIFFQYVSLIEHQVLHMGQKNEKNGICEEAYSWNLTVIEDKKIELQEQPYQCDICGKAFGYSSDLIQHYRTHTAEKPYQCDICRENVGQCSHTKQHQKIYSSTKSHQCHECGRGFTLKSHLNQHQRIHTGEKPFQCKECGMNFSWSCSLFKHLRSHERTDPINTLSVEGSLL
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
58PhosphorylationQRFRHFQYHEASGPR
HHHHHHCHHHHCCHH		10.73-
85PhosphorylationWLRPELHTKEQILEL
HHCHHCCCHHHHHHH		49.23-
216SumoylationTGSQKLVKIEEVADV
CCCCEEEEHHHHHHH		55.6328112733
248SumoylationSLYRDDRKENYGSIT
HHHCCCCHHCCCCCC		58.2528112733
251PhosphorylationRDDRKENYGSITSMG
CCCCHHCCCCCCCCC		17.2225072903
253PhosphorylationDRKENYGSITSMGYE
CCHHCCCCCCCCCCC		16.6025072903
255PhosphorylationKENYGSITSMGYESR
HHCCCCCCCCCCCCC		17.8525072903
256PhosphorylationENYGSITSMGYESRD
HCCCCCCCCCCCCCC		14.4525072903
259PhosphorylationGSITSMGYESRDNME
CCCCCCCCCCCCCCE		11.3325072903
261PhosphorylationITSMGYESRDNMELI
CCCCCCCCCCCCEEE		36.1324043423
270SumoylationDNMELIVKQISDDSE
CCCEEEEEECCCCCC		34.6128112733
303SumoylationFAEVSDLKGMVQRWQ
HHHHHHHHHHHHHEE		50.3728112733
303UbiquitinationFAEVSDLKGMVQRWQ
HHHHHHHHHHHHHEE		50.37-
317SumoylationQVNPTVGKSRQNPSQ
EECCCCCCCCCCHHH		37.8228112733
332PhosphorylationKRDLDAITDISPKQS
CCCHHHHCCCCCCCC		29.0630108239
335PhosphorylationLDAITDISPKQSTHG
HHHHCCCCCCCCCCC		28.9322617229
339PhosphorylationTDISPKQSTHGERGH
CCCCCCCCCCCCCCC		28.6229396449
340PhosphorylationDISPKQSTHGERGHR
CCCCCCCCCCCCCCC		31.2629396449
369PhosphorylationIQHRRIHTGEKPFKC
HHCCCCCCCCCCEEC		44.6718669648
397PhosphorylationTQHQRVHTGEKPYKC
ECCCCCCCCCCCEEC		44.1529496963
400UbiquitinationQRVHTGEKPYKCQVC
CCCCCCCCCEECCCC		55.80-
400SumoylationQRVHTGEKPYKCQVC
CCCCCCCCCEECCCC		55.80-
400SumoylationQRVHTGEKPYKCQVC
CCCCCCCCCEECCCC		55.80-
414PhosphorylationCGKAFRVSSHLVQHH
CCCEEEECHHHHHCC		14.05-
415PhosphorylationGKAFRVSSHLVQHHS
CCEEEECHHHHHCCC		20.27-
425PhosphorylationVQHHSVHSGERPYGC
HHCCCCCCCCCCCCC		39.95-
487PhosphorylationSEADMELSGKTQRNV
CHHHHHHCCCCCCCH		25.57-
509SumoylationEGCEFQGKLDRKQGI
CCCCCCCCCCCCCCC		36.1128112733
509UbiquitinationEGCEFQGKLDRKQGI
CCCCCCCCCCCCCCC		36.11-
513SumoylationFQGKLDRKQGIPMKE
CCCCCCCCCCCCHHH		53.17-
513SumoylationFQGKLDRKQGIPMKE
CCCCCCCCCCCCHHH		53.1728112733
526PhosphorylationKEILGQPSSKRMNYS
HHHCCCCCCCCCCCC		40.3726434776
527PhosphorylationEILGQPSSKRMNYSE
HHCCCCCCCCCCCCC		30.8526434776
528AcetylationILGQPSSKRMNYSEV
HCCCCCCCCCCCCCC		61.0626822725
557PhosphorylationKCNECGKSFIQSAHL
CCCHHHHHHHHHHHH		16.9328509920
561PhosphorylationCGKSFIQSAHLIQHQ
HHHHHHHHHHHHHCC		16.9128509920
572PhosphorylationIQHQRIHTGEKPFRC
HHCCCCCCCCCCCCC		44.6729496963
600PhosphorylationTQHQRVHTGEKPYTC
CCCCCCCCCCCCCCC		44.15-
605PhosphorylationVHTGEKPYTCPLCGK
CCCCCCCCCCCCCCC		31.85-
628PhosphorylationVQHQSVHSGERPFKC
HCCCCCCCCCCCCCC		39.9528555341
709SumoylationLTVIEDKKIELQEQP
CEEEECCCCEECCCC		54.4528112733
709SumoylationLTVIEDKKIELQEQP
CEEEECCCCEECCCC		54.45-
758PhosphorylationRENVGQCSHTKQHQK
CCCCCCCCCHHHHHH		26.7229978859
760PhosphorylationNVGQCSHTKQHQKIY
CCCCCCCHHHHHHHH		18.9929978859
765UbiquitinationSHTKQHQKIYSSTKS
CCHHHHHHHHHCCCC		41.30-
785UbiquitinationCGRGFTLKSHLNQHQ
CCCCCEEHHHHHHCC		32.54-
785SumoylationCGRGFTLKSHLNQHQ
CCCCCEEHHHHHHCC		32.5428112733
815PhosphorylationMNFSWSCSLFKHLRS
CCEEEHHHHHHHHHH		31.1824719451
837PhosphorylationNTLSVEGSLL-----
CEEEEECCCC-----		17.00-
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 ZKSC5_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ZKSC5_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 ZKSC5_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
ZBTB9_HUMANZBTB9physical
20211142
ZSCA1_HUMANZSCAN1physical
20211142
SUV91_HUMANSUV39H1physical
23455924
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 ZKSC5_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-335, AND MASSSPECTROMETRY.

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