ZN770_HUMAN - dbPTM
ZN770_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ZN770_HUMAN
UniProt AC Q6IQ21
Protein Name Zinc finger protein 770
Gene Name ZNF770
Organism Homo sapiens (Human).
Sequence Length 691
Subcellular Localization Nucleus .
Protein Description May be involved in transcriptional regulation..
Protein Sequence MMAENNLKMLKIQQCVVANKLPRNRPYVCNICFKHFETPSKLARHYLIHTGQKPFECDVCHKTFRQLVHLERHQLTHSLPFKCSICQRHFKNLKTFVKHQQLHNETYQNNVKQVRRLLEAKQEKSMYGVYNTFTTEERWALHPCSKSDPMYSMKRRKNIHACTICGKMFPSQSKLDRHVLIHTGQRPFKCVLCTKSFRQSTHLKIHQLTHSEERPFQCCFCQKGFKIQSKLLKHKQIHTRNKAFRALLLKKRRTESRPLPNKLNANQGGFENGEIGESEENNPLDVHSIYIVPFQCPKCEKCFESEQILNEHSCFAARSGKIPSRFKRSYNYKTIVKKILAKLKRARSKKLDNFQSEKKVFKKSFLRNCDLISGEQSSEQTQRTFVGSLGKHGTYKTIGNRKKKTLTLPFSWQNMGKNLKGILTTENILSIDNSVNKKDLSICGSSGEEFFNNCEVLQCGFSVPRENIRTRHKICPCDKCEKVFPSISKLKRHYLIHTGQRPFGCNICGKSFRQSAHLKRHEQTHNEKSPYASLCQVEFGNFNNLSNHSGNNVNYNASQQCQAPGVQKYEVSESDQMSGVKAESQDFIPGSTGQPCLPNVLLESEQSNPFCSYSEHQEKNDVFLYRCSVCAKSFRSPSKLERHYLIHAGQKPFECSVCGKTFRQAPHWKRHQLTHFKERPQGKVVALDSVM
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
11SumoylationENNLKMLKIQQCVVA
HHHHHEEHHHHHHHH
34.6628112733
27PhosphorylationKLPRNRPYVCNICFK
CCCCCCCEEEEEECH
17.8822210691
38PhosphorylationICFKHFETPSKLARH
EECHHCCCHHHHHHH
31.7322210691
50PhosphorylationARHYLIHTGQKPFEC
HHHHHHHCCCCCCCC
34.02-
63PhosphorylationECDVCHKTFRQLVHL
CCCCHHHHHHHHHHH
10.6122210691
76PhosphorylationHLERHQLTHSLPFKC
HHHHHHCCCCCCCCC
11.6622210691
78PhosphorylationERHQLTHSLPFKCSI
HHHHCCCCCCCCCHH
32.2828450419
84PhosphorylationHSLPFKCSICQRHFK
CCCCCCCHHHHHHHC
27.3022210691
112SumoylationETYQNNVKQVRRLLE
HHHHHHHHHHHHHHH
45.2428112733
112UbiquitinationETYQNNVKQVRRLLE
HHHHHHHHHHHHHHH
45.2429967540
121SumoylationVRRLLEAKQEKSMYG
HHHHHHHHHHHHHHC
50.0028112733
121UbiquitinationVRRLLEAKQEKSMYG
HHHHHHHHHHHHHHC
50.0029967540
124UbiquitinationLLEAKQEKSMYGVYN
HHHHHHHHHHHCCCC
37.7229967540
132PhosphorylationSMYGVYNTFTTEERW
HHHCCCCCCCCHHHE
12.50-
146SumoylationWALHPCSKSDPMYSM
EECCCCCCCCCCCCC
66.6428112733
151PhosphorylationCSKSDPMYSMKRRKN
CCCCCCCCCCCCCCC
15.82-
154UbiquitinationSDPMYSMKRRKNIHA
CCCCCCCCCCCCCCE
43.0129967540
226UbiquitinationCFCQKGFKIQSKLLK
CEECCCCCCHHHHHH
48.8029967540
262SumoylationESRPLPNKLNANQGG
CCCCCCCCCCCCCCC
40.9728112733
330PhosphorylationPSRFKRSYNYKTIVK
CCHHCCCCCHHHHHH
26.9222817900
332PhosphorylationRFKRSYNYKTIVKKI
HHCCCCCHHHHHHHH
10.9827762562
333UbiquitinationFKRSYNYKTIVKKIL
HCCCCCHHHHHHHHH
28.3029967540
333SumoylationFKRSYNYKTIVKKIL
HCCCCCHHHHHHHHH
28.30-
333SumoylationFKRSYNYKTIVKKIL
HCCCCCHHHHHHHHH
28.30-
350SumoylationLKRARSKKLDNFQSE
HHHHHHHCCCCHHHH
63.42-
350UbiquitinationLKRARSKKLDNFQSE
HHHHHHHCCCCHHHH
63.4229967540
350SumoylationLKRARSKKLDNFQSE
HHHHHHHCCCCHHHH
63.42-
358AcetylationLDNFQSEKKVFKKSF
CCCHHHHHHHHHHHH
60.5324468157
358UbiquitinationLDNFQSEKKVFKKSF
CCCHHHHHHHHHHHH
60.5329967540
364PhosphorylationEKKVFKKSFLRNCDL
HHHHHHHHHHHCCCC
30.0624719451
373PhosphorylationLRNCDLISGEQSSEQ
HHCCCCCCCCCCCHH
43.50-
377PhosphorylationDLISGEQSSEQTQRT
CCCCCCCCCHHHHHH
31.38-
388PhosphorylationTQRTFVGSLGKHGTY
HHHHCCHHHHCCCEE
28.7524173317
391SumoylationTFVGSLGKHGTYKTI
HCCHHHHCCCEEEEE
44.12-
391UbiquitinationTFVGSLGKHGTYKTI
HCCHHHHCCCEEEEE
44.1229967540
391SumoylationTFVGSLGKHGTYKTI
HCCHHHHCCCEEEEE
44.12-
396UbiquitinationLGKHGTYKTIGNRKK
HHCCCEEEEECCCCC
33.2429967540
407PhosphorylationNRKKKTLTLPFSWQN
CCCCCEEEECCCHHC
37.30-
417UbiquitinationFSWQNMGKNLKGILT
CCHHCCCCCCCCEEE
48.6229967540
420SumoylationQNMGKNLKGILTTEN
HCCCCCCCCEEECCC
53.9828112733
424PhosphorylationKNLKGILTTENILSI
CCCCCEEECCCCHHC
30.09-
425PhosphorylationNLKGILTTENILSID
CCCCEEECCCCHHCC
24.48-
430PhosphorylationLTTENILSIDNSVNK
EECCCCHHCCCCCCC
24.89-
434PhosphorylationNILSIDNSVNKKDLS
CCHHCCCCCCCCCCC
24.2623532336
437UbiquitinationSIDNSVNKKDLSICG
HCCCCCCCCCCCCCC
45.5729967540
437SumoylationSIDNSVNKKDLSICG
HCCCCCCCCCCCCCC
45.5728112733
462PhosphorylationEVLQCGFSVPRENIR
EEEECCCCCCHHHHC
19.25-
489UbiquitinationKVFPSISKLKRHYLI
HHCCCHHHHHHEEEE
57.2529967540
498PhosphorylationKRHYLIHTGQRPFGC
HHEEEEECCCCCCCC
28.19-
511PhosphorylationGCNICGKSFRQSAHL
CCCCCCHHHHHHHHH
15.7924719451
515PhosphorylationCGKSFRQSAHLKRHE
CCHHHHHHHHHHHHH
17.2530622161
519AcetylationFRQSAHLKRHEQTHN
HHHHHHHHHHHHHCC
41.6712431569
569PhosphorylationQAPGVQKYEVSESDQ
CCCCCEEEEECCHHH
12.4128450419
572PhosphorylationGVQKYEVSESDQMSG
CCEEEEECCHHHCCC
21.3128450419
574PhosphorylationQKYEVSESDQMSGVK
EEEEECCHHHCCCCE
26.1528450419
578PhosphorylationVSESDQMSGVKAESQ
ECCHHHCCCCEECCC
34.5028450419
633PhosphorylationRCSVCAKSFRSPSKL
EHHHHHHHCCCHHHH
13.8428102081
636PhosphorylationVCAKSFRSPSKLERH
HHHHHCCCHHHHHHE
31.3629514088
638PhosphorylationAKSFRSPSKLERHYL
HHHCCCHHHHHHEEE
51.6329514088
683SumoylationFKERPQGKVVALDSV
CCCCCCCCEEEEECC
28.4328112733

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 ZN770_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ZN770_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 ZN770_HUMAN !!

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

Oops, there are no PPI records of ZN770_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 ZN770_HUMAN

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Related Literatures of Post-Translational Modification

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