ZN808_HUMAN - dbPTM
ZN808_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ZN808_HUMAN
UniProt AC Q8N4W9
Protein Name Zinc finger protein 808
Gene Name ZNF808
Organism Homo sapiens (Human).
Sequence Length 903
Subcellular Localization Nucleus .
Protein Description May be involved in transcriptional regulation..
Protein Sequence MLREEAAQKRKGKESGMALPQGRLTFRDVAIEFSLAEWKFLNPAQRALYREVMLENYRNLEAVDISSKHMMKEVLSTGQGNREVIHTGTLQRHQSYHIGDFCFQEIEKEIHNIEFQCQEDERNGHEAPTTKIKKLTGSTDQHDHRHAGNKPIKDQLGSSFYSHLPELHIFQIKGEIANQLEKSTSDASSVSTSQRISCRPQIHISNNYGNNPLNSSLLPQKQEVHMREKSFPCNESGKAFNCSSLLRKHQIPHLGDKQYKCDVCGKLFNHKQYLACHRRCHTGEKPYKCKECGKSFSYKSSLTCHHRLHTGVKPYKCNECGKVFRQNSALVIHKAIHTGEKPYKCNECGKAFNQQSHLSRHQRLHTGVKPYKCKICEKAFACHSYLANHTRIHSGEKTYKCNECGKAFNHQSSLARHHILHTGEKPYKCEECDKVFSQKSTLERHKRIHTGEKPYKCKVCDTAFTCNSQLARHRRIHTGEKTYKCNECRKTFSRRSSLLCHRRLHSGEKPYKCNQCGNTFRHRASLVYHRRLHTLEKSYKCTVCNKVFMRNSVLAVHTRIHTAKKPYKCNECGKAFNQQSHLSRHRRLHTGEKPYKCEACDKVFGQKSALESHKRIHTGEKPYRCQVCDTAFTWNSQLARHTRIHTGEKTYKCNECGKTFSYKSSLVWHRRLHGGEKSYKCKVCDKAFVCRSYVAKHTRIHSGMKPYKCNECSKTFSNRSSLVCHRRIHSGEKPYKCSECSKTFSQKATLLCHRRLHSGEKPYKCNDCGNTFRHWSSLVYHRRLHTGEKSYKCTVCDKAFVRNSYLARHIRIHTAEKPYKCNECGKAFNEQSHLSRHHRIHTGEKPYKCEACDKVFSRKSHLKRHRIIHTGEKPYKCNECGKAFSDRSTLIHHQAIHGIGKFD
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
13AcetylationAAQKRKGKESGMALP
HHHHHCCCCCCCCCC		52.3119817397
15PhosphorylationQKRKGKESGMALPQG
HHHCCCCCCCCCCCC		37.0422210691
150UbiquitinationDHRHAGNKPIKDQLG
CCCCCCCCCHHHHCC		47.40-
173SumoylationELHIFQIKGEIANQL
CEEEEEEHHHHHHHH		39.4428112733
184PhosphorylationANQLEKSTSDASSVS
HHHHHHCCCCCCCCC		41.51-
185PhosphorylationNQLEKSTSDASSVST
HHHHHCCCCCCCCCH		37.97-
230PhosphorylationEVHMREKSFPCNESG
CCCCCCCCCCCCCCC		29.6629978859
236PhosphorylationKSFPCNESGKAFNCS
CCCCCCCCCCCCCHH		31.4429978859
244PhosphorylationGKAFNCSSLLRKHQI
CCCCCHHHHHHHCCC		33.3524719451
295PhosphorylationKCKECGKSFSYKSSL
ECCCCCCCCEECCCC		12.52-
300PhosphorylationGKSFSYKSSLTCHHR
CCCCEECCCCCCCCC		23.50-
313SumoylationHRLHTGVKPYKCNEC
CCCCCCCCCEECCCC		43.93-
313SumoylationHRLHTGVKPYKCNEC
CCCCCCCCCEECCCC		43.93-
315PhosphorylationLHTGVKPYKCNECGK
CCCCCCCEECCCCCC		23.58-
316SumoylationHTGVKPYKCNECGKV
CCCCCCEECCCCCCC		38.83-
316SumoylationHTGVKPYKCNECGKV
CCCCCCEECCCCCCC		38.83-
338PhosphorylationVIHKAIHTGEKPYKC
EEEEHHHCCCCCEEC		40.7129496963
341SumoylationKAIHTGEKPYKCNEC
EHHHCCCCCEECCCH		55.80-
341UbiquitinationKAIHTGEKPYKCNEC
EHHHCCCCCEECCCH		55.80-
341SumoylationKAIHTGEKPYKCNEC
EHHHCCCCCEECCCH		55.80-
343PhosphorylationIHTGEKPYKCNECGK
HHCCCCCEECCCHHH		38.9618767875
344SumoylationHTGEKPYKCNECGKA
HCCCCCEECCCHHHH		38.83-
344SumoylationHTGEKPYKCNECGKA
HCCCCCEECCCHHHH		38.83-
356UbiquitinationGKAFNQQSHLSRHQR
HHHHHHHHHHHHHHH		19.3421890473
369SumoylationQRLHTGVKPYKCKIC
HHHHCCCCCCCCCCC		43.93-
369SumoylationQRLHTGVKPYKCKIC
HHHHCCCCCCCCCCC		43.93-
374AcetylationGVKPYKCKICEKAFA
CCCCCCCCCCCCHHH		46.3619827595
397AcetylationTRIHSGEKTYKCNEC
CEECCCCCEEECCCC		61.7619827603
400AcetylationHSGEKTYKCNECGKA
CCCCCEEECCCCHHH		35.5019827611
422PhosphorylationARHHILHTGEKPYKC
HHHCCCCCCCCCCCC		43.5227422710
425SumoylationHILHTGEKPYKCEEC
CCCCCCCCCCCCHHH		55.80-
425UbiquitinationHILHTGEKPYKCEEC
CCCCCCCCCCCCHHH		55.8021890473
425SumoylationHILHTGEKPYKCEEC
CCCCCCCCCCCCHHH		55.80-
428SumoylationHTGEKPYKCEECDKV
CCCCCCCCCHHHHHH		43.63-
428SumoylationHTGEKPYKCEECDKV
CCCCCCCCCHHHHHH		43.63-
450PhosphorylationERHKRIHTGEKPYKC
HHHHCCCCCCCCCCC		44.6729496963
468PhosphorylationDTAFTCNSQLARHRR
CCCEECCHHHHHHCC		28.8124719451
497PhosphorylationKTFSRRSSLLCHRRL
HHHHHCHHHHHHCCC		24.4523312004
506PhosphorylationLCHRRLHSGEKPYKC
HHHCCCCCCCCCEEC		53.9227794612
524UbiquitinationGNTFRHRASLVYHRR
CCCHHHHHHHHHHHH		10.9021890473
568SumoylationHTAKKPYKCNECGKA
CCCCCCEECCCCHHH		38.83-
568SumoylationHTAKKPYKCNECGKA
CCCCCCEECCCCHHH		38.83-
590PhosphorylationSRHRRLHTGEKPYKC
HHHCCCCCCCCCCCC		52.1827422710
593SumoylationRRLHTGEKPYKCEAC
CCCCCCCCCCCCCCC		55.80-
593UbiquitinationRRLHTGEKPYKCEAC
CCCCCCCCCCCCCCC		55.8029967540
593SumoylationRRLHTGEKPYKCEAC
CCCCCCCCCCCCCCC		55.80-
596UbiquitinationHTGEKPYKCEACDKV
CCCCCCCCCCCCHHH		33.84-
612PhosphorylationGQKSALESHKRIHTG
CCHHHHHHCCCCCCC		34.8530576142
618PhosphorylationESHKRIHTGEKPYRC
HHCCCCCCCCCCCCC		44.6729496963
621SumoylationKRIHTGEKPYRCQVC
CCCCCCCCCCCCEEC		49.01-
621SumoylationKRIHTGEKPYRCQVC
CCCCCCCCCCCCEEC		49.01-
621UbiquitinationKRIHTGEKPYRCQVC
CCCCCCCCCCCCEEC		49.01-
636PhosphorylationDTAFTWNSQLARHTR
CCCCCCCHHHHHCCE		20.3823663014
715PhosphorylationKCNECSKTFSNRSSL
ECCCCCCCCCCCCCE		18.9224076635
721PhosphorylationKTFSNRSSLVCHRRI
CCCCCCCCEEEEEEE		22.9124076635
730PhosphorylationVCHRRIHSGEKPYKC
EEEEEECCCCCCEEC		46.4029496963
735PhosphorylationIHSGEKPYKCSECSK
ECCCCCCEECCCCCC		35.38-
758PhosphorylationLCHRRLHSGEKPYKC
HHHCCCCCCCCCEEC		53.9227794612
786PhosphorylationVYHRRLHTGEKSYKC
HHHHCCCCCCCEEEE		52.1821857030
791PhosphorylationLHTGEKSYKCTVCDK
CCCCCCEEEEEECCH		22.5822461510
794PhosphorylationGEKSYKCTVCDKAFV
CCCEEEEEECCHHHH		21.7322461510
804PhosphorylationDKAFVRNSYLARHIR
CHHHHCCHHHHHHCE		15.8024719451
819PhosphorylationIHTAEKPYKCNECGK
EEECCCCCCCCCCHH		38.96-
820SumoylationHTAEKPYKCNECGKA
EECCCCCCCCCCHHH		38.83-
820SumoylationHTAEKPYKCNECGKA
EECCCCCCCCCCHHH		38.83-
842PhosphorylationSRHHRIHTGEKPYKC
HHCCCCCCCCCCCCC		44.6729496963
870PhosphorylationKRHRIIHTGEKPYKC
HHCCEEECCCCCCCC		36.3129496963
873UbiquitinationRIIHTGEKPYKCNEC
CEEECCCCCCCCCCC		55.80-
875PhosphorylationIHTGEKPYKCNECGK
EECCCCCCCCCCCCC		38.9618767875
876SumoylationHTGEKPYKCNECGKA
ECCCCCCCCCCCCCC		38.83-
876SumoylationHTGEKPYKCNECGKA
ECCCCCCCCCCCCCC		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 ZN808_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ZN808_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 ZN808_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of ZN808_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 ZN808_HUMAN

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Related Literatures of Post-Translational Modification

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