ZKSC4_HUMAN - dbPTM
ZKSC4_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ZKSC4_HUMAN
UniProt AC Q969J2
Protein Name Zinc finger protein with KRAB and SCAN domains 4
Gene Name ZKSCAN4
Organism Homo sapiens (Human).
Sequence Length 545
Subcellular Localization Nucleus .
Protein Description May be involved in the transcriptional activation of MDM2 and EP300 genes..
Protein Sequence MAREPRKNAALDAQSAEDQTGLLTVKVEKEEASALTAEVRAPCSPARGPERSRQRFRGFRYPEAAGPREALSRLRELCGQWLQPEMHSKEQILELLVLEQFLTILPGNLQSWVREQHPESGEEVVVLLEYLERQLDEPAPQVPVGDQGQELLCCKMALLTQTQGSQSSQCQPMKALFKHESLGSQPLHDRVLQVPGLAQGGCCREDAMVASRLTPGSQGLLKMEDVALTLTPGWTQLDSSQVNLYRDEKQENHSSLVSLGGEIQTKSRDLPPVKKLPEKEHGKICHLREDIAQIPTHAEAGEQEGRLQRKQKNAIGSRRHYCHECGKSFAQSSGLTKHRRIHTGEKPYECEDCGKTFIGSSALVIHQRVHTGEKPYECEECGKVFSHSSNLIKHQRTHTGEKPYECDDCGKTFSQSCSLLEHHKIHTGEKPYQCNMCGKAFRRNSHLLRHQRIHGDKNVQNPEHGESWESQGRTESQWENTEAPVSYKCNECERSFTRNRSLIEHQKIHTGEKPYQCDTCGKGFTRTSYLVQHQRSHVGKKTLSQ
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
26SumoylationQTGLLTVKVEKEEAS
CCCCEEEEEEHHHHH		39.17-
26SumoylationQTGLLTVKVEKEEAS
CCCCEEEEEEHHHHH		39.1728112733
29SumoylationLLTVKVEKEEASALT
CEEEEEEHHHHHCCE		64.9328112733
44PhosphorylationAEVRAPCSPARGPER
EEEECCCCCCCCCHH		22.1223401153
61PhosphorylationQRFRGFRYPEAAGPR
HHHHCCCCCHHCCHH		11.8120886841
72PhosphorylationAGPREALSRLRELCG
CCHHHHHHHHHHHHH		36.00-
89MethylationLQPEMHSKEQILELL
HCHHHCCHHHHHHHH		38.6723644510
165PhosphorylationLLTQTQGSQSSQCQP
HHHCCCCCCCCCCCC		19.6417525332
178SumoylationQPMKALFKHESLGSQ
CCHHHHHCCCCCCCC		47.52-
178SumoylationQPMKALFKHESLGSQ
CCHHHHHCCCCCCCC		47.5228112733
181PhosphorylationKALFKHESLGSQPLH
HHHHCCCCCCCCCCC		37.4428555341
214PhosphorylationAMVASRLTPGSQGLL
CHHHCCCCCCCCCCE		25.2121815630
222SumoylationPGSQGLLKMEDVALT
CCCCCCEEHHCEEEE		45.3328112733
265PhosphorylationSLGGEIQTKSRDLPP
HCCHHHEECCCCCCC		36.33-
267PhosphorylationGGEIQTKSRDLPPVK
CHHHEECCCCCCCCC		34.12-
321PhosphorylationAIGSRRHYCHECGKS
HHHCHHHHHHHHHHH		8.1628258704
328PhosphorylationYCHECGKSFAQSSGL
HHHHHHHHHHHHCCC		15.8827134283
337UbiquitinationAQSSGLTKHRRIHTG
HHHCCCCCCCEEECC		39.91-
343PhosphorylationTKHRRIHTGEKPYEC
CCCCEEECCCCCEEC		44.6728111955
348PhosphorylationIHTGEKPYECEDCGK
EECCCCCEECCCCCC		44.2621712546
371PhosphorylationVIHQRVHTGEKPYEC
EEEEEECCCCCCEEC		44.15-
388PhosphorylationCGKVFSHSSNLIKHQ
HCCEEECCCCCHHCC		21.5227251275
397PhosphorylationNLIKHQRTHTGEKPY
CCHHCCCCCCCCCCE		19.74-
399PhosphorylationIKHQRTHTGEKPYEC
HHCCCCCCCCCCEEC		46.56-
404PhosphorylationTHTGEKPYECDDCGK
CCCCCCCEECCCCCC		40.01-
414PhosphorylationDDCGKTFSQSCSLLE
CCCCCCHHHHHHHHH		26.8128555341
418PhosphorylationKTFSQSCSLLEHHKI
CCHHHHHHHHHCCCC		41.0328555341
427PhosphorylationLEHHKIHTGEKPYQC
HHCCCCCCCCCCCCC		50.97-
445PhosphorylationGKAFRRNSHLLRHQR
CHHHHHCHHHHHHCH		17.4430266825
470PhosphorylationEHGESWESQGRTESQ
CCCCCHHHCCCCHHH		31.51-
501PhosphorylationRSFTRNRSLIEHQKI
HHHCCCHHHHEECCC		36.9326055452
510PhosphorylationIEHQKIHTGEKPYQC
HEECCCCCCCCCCCC		50.9721712546
515PhosphorylationIHTGEKPYQCDTCGK
CCCCCCCCCCCCCCC		32.61-
528PhosphorylationGKGFTRTSYLVQHQR
CCCCCCHHHHHHHCH		17.1228555341
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 ZKSC4_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ZKSC4_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 ZKSC4_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
ZKSC4_HUMANZKSCAN4physical
25416956
TYW3_HUMANTYW3physical
28514442
ZKSC3_HUMANZKSCAN3physical
28514442
ZN174_HUMANZNF174physical
28514442
SCND1_HUMANSCAND1physical
28514442
PGBD1_HUMANPGBD1physical
28514442
SCND3_HUMANZBED9physical
28514442
FINC_HUMANFN1physical
28514442
ZSC21_HUMANZSCAN21physical
28514442
ZKSC1_HUMANZKSCAN1physical
28514442
ZN446_HUMANZNF446physical
28514442
ZKSC8_HUMANZKSCAN8physical
28514442
ZNF24_HUMANZNF24physical
28514442
ZN213_HUMANZNF213physical
28514442
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 ZKSC4_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-165, AND MASSSPECTROMETRY.

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