ZN600_HUMAN - dbPTM
ZN600_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ZN600_HUMAN
UniProt AC Q6ZNG1
Protein Name Zinc finger protein 600
Gene Name ZNF600
Organism Homo sapiens (Human).
Sequence Length 722
Subcellular Localization Nucleus .
Protein Description May be involved in transcriptional regulation..
Protein Sequence MMKEVLSTGQGNTEVIHTGTLQRYQSYHIGDFCFQEIEKEIHDIEFQCQEDERNGHEAPMTKIKKLTGSTDQHDHRHAGNKPIKDQLGSSFYSHLPELHIIQIKGKIGNQFEKSTSDAPSVSTSQRISPRPQIHISNNYGNNSPNSSLLPQKQEVYMREKSFQCNESGKAFNCSSLLRKHQIPHLGDKQYKCDVCGKLFNHKQYLTCHCRCHTGEKPYKCNECGKSFSQVSSLTCHRRLHTAVKSHKCNECGKIFGQNSALVIHKAIHTGEKPYKCNECDKAFNQQSNLARHRRIHTGEKPYKCEECDKVFSRKSTLESHKRIHTGEKPYKCKVCDTAFTWNSQLARHKRIHTGEKTYKCNECGKTFSHKSSLVCHHRLHGGEKSYKCKVCDKAFAWNSHLVRHTRIHSGGKPYKCNECGKTFGQNSDLLIHKSIHTGEQPYKYEECEKVFSCGSTLETHKIIHTGEKPYKCKVCDKAFACHSYLAKHTRIHSGEKPYKCNECSKTFRLRSYLASHRRVHSGEKPYKCNECSKTFSQRSYLHCHRRLHSGEKPYKCNECGKTFSHKPSLVHHRRLHTGEKSYKCTVCDKAFVRNSYLARHTRIHTAEKPYKCNECGKAFNQQSQLSLHHRIHAGEKLYKCETCDKVFSRKSHLKRHRRIHPGKKPYKCKVCDKTFGSDSHLKQHTGLHTGEKPYKCNECGKAFSKQSTLIHHQAVHGVGKLD
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
62UbiquitinationGHEAPMTKIKKLTGS
CCCCCCHHHHHHHCC		46.40-
67PhosphorylationMTKIKKLTGSTDQHD
CHHHHHHHCCCCCCC		37.66-
81UbiquitinationDHRHAGNKPIKDQLG
CCCCCCCCCHHHHCC		47.40-
116PhosphorylationNQFEKSTSDAPSVST
CCCCCCCCCCCCCCC		38.5817525332
124PhosphorylationDAPSVSTSQRISPRP
CCCCCCCCCCCCCCC		15.2317525332
128PhosphorylationVSTSQRISPRPQIHI
CCCCCCCCCCCEEEC		19.6230631047
169AcetylationFQCNESGKAFNCSSL
EECCCCCCCCCHHHH		60.117216845
175PhosphorylationGKAFNCSSLLRKHQI
CCCCCHHHHHHHCCC		33.3524719451
219SumoylationHTGEKPYKCNECGKS
CCCCCCEECCCCCCC		38.83-
219SumoylationHTGEKPYKCNECGKS
CCCCCCEECCCCCCC		38.83-
226PhosphorylationKCNECGKSFSQVSSL
ECCCCCCCHHHHHHH		18.53-
269PhosphorylationVIHKAIHTGEKPYKC
EEEEHHHCCCCCCCC		40.7129496963
272SumoylationKAIHTGEKPYKCNEC
EHHHCCCCCCCCCHH		55.80-
272UbiquitinationKAIHTGEKPYKCNEC
EHHHCCCCCCCCCHH		55.80-
272SumoylationKAIHTGEKPYKCNEC
EHHHCCCCCCCCCHH		55.80-
297PhosphorylationARHRRIHTGEKPYKC
HHHCCCCCCCCCCCC		44.6729496963
303SumoylationHTGEKPYKCEECDKV
CCCCCCCCCHHCCCE		43.63-
303SumoylationHTGEKPYKCEECDKV
CCCCCCCCCHHCCCE		43.63-
325PhosphorylationESHKRIHTGEKPYKC
HHCCCCCCCCCCEEC		44.6729496963
343PhosphorylationDTAFTWNSQLARHKR
CCCCCCCHHHHHCCC		20.3823663014
353PhosphorylationARHKRIHTGEKTYKC
HHCCCCCCCCCEEEC		44.6722210691
357PhosphorylationRIHTGEKTYKCNECG
CCCCCCCEEECCCCC		24.7422210691
358PhosphorylationIHTGEKTYKCNECGK
CCCCCCEEECCCCCC		25.3122210691
415SumoylationHSGGKPYKCNECGKT
CCCCCEEECCCCCCC		38.83-
415SumoylationHSGGKPYKCNECGKT
CCCCCEEECCCCCCC		38.83-
437PhosphorylationLIHKSIHTGEQPYKY
EEEEEECCCCCCCCH		40.5225159151
461UbiquitinationGSTLETHKIIHTGEK
CCCEEECCEEECCCC		51.26-
465PhosphorylationETHKIIHTGEKPYKC
EECCEEECCCCCCCC		36.3129496963
468UbiquitinationKIIHTGEKPYKCKVC
CEEECCCCCCCCCCC		55.80-
470PhosphorylationIHTGEKPYKCKVCDK
EECCCCCCCCCCCCC		39.83-
493PhosphorylationAKHTRIHSGEKPYKC
HHCCCCCCCCCCCCC		46.4029496963
526PhosphorylationVHSGEKPYKCNECSK
CCCCCCCCCCCCCCC		38.9618785766
549PhosphorylationHCHRRLHSGEKPYKC
HHHCCCCCCCCCEEC		53.9227794612
555SumoylationHSGEKPYKCNECGKT
CCCCCCEECCCCCCC		38.83-
555SumoylationHSGEKPYKCNECGKT
CCCCCCEECCCCCCC		38.83-
577PhosphorylationVHHRRLHTGEKSYKC
EEECCCCCCCCEEEE		52.1821857030
582PhosphorylationLHTGEKSYKCTVCDK
CCCCCCEEEEEECCH		22.5822461510
585PhosphorylationGEKSYKCTVCDKAFV
CCCEEEEEECCHHHH		21.7322461510
610PhosphorylationIHTAEKPYKCNECGK
EECCCCCEECCCCHH		38.96-
611SumoylationHTAEKPYKCNECGKA
ECCCCCEECCCCHHH		38.83-
611SumoylationHTAEKPYKCNECGKA
ECCCCCEECCCCHHH		38.83-
623PhosphorylationGKAFNQQSQLSLHHR
HHHHCCCHHHHHHCH		24.2719690332
689PhosphorylationKQHTGLHTGEKPYKC
HHHCCCCCCCCCEEC		52.6727422710
692SumoylationTGLHTGEKPYKCNEC
CCCCCCCCCEECCCC		55.80-
692UbiquitinationTGLHTGEKPYKCNEC
CCCCCCCCCEECCCC		55.80-
692SumoylationTGLHTGEKPYKCNEC
CCCCCCCCCEECCCC		55.80-
694PhosphorylationLHTGEKPYKCNECGK
CCCCCCCEECCCCCC		38.96-
695SumoylationHTGEKPYKCNECGKA
CCCCCCEECCCCCCC		38.83-
695UbiquitinationHTGEKPYKCNECGKA
CCCCCCEECCCCCCC		38.83-
695SumoylationHTGEKPYKCNECGKA
CCCCCCEECCCCCCC		38.83-
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 ZN600_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ZN600_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 ZN600_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of ZN600_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 ZN600_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-116 AND SER-124, ANDMASS SPECTROMETRY.

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