ZN813_HUMAN - dbPTM
ZN813_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ZN813_HUMAN
UniProt AC Q6ZN06
Protein Name Zinc finger protein 813
Gene Name ZNF813
Organism Homo sapiens (Human).
Sequence Length 617
Subcellular Localization Nucleus .
Protein Description May be involved in transcriptional regulation..
Protein Sequence MALPQGLLTFRDVAIEFSQEEWKCLDPAQRTLYRDVMLENYRNLVSLDISSKCMMKEFSSTAQGNREVIHTGTLQRHESHHTGDFRFQEIDKDIHNLEFQWQEDERNSHEAPMTEIKKLTGSADRYDQRHAGNKPIKDQLGSSFHSHLPELHMFQTQGKIGNQVEKSINDASSISTSQRISCRPKTHISNNYGNNFRNSSLLTQKQEVHMREKSFQCNESGKAFNYSSLLRKHQIIHLGEKQYKCDVCGKVFNRKRNLVCHRRCHTGEKPYRCNECGKTFSQTYSLTCHRRLHTGEKPYKCEECDKAFSFKSNLKRHRRIHAGEKPYKCNECGKTFSQTSSLTCHRRLHTGEKPFKCNECGKTFSRKSSLTCHHRLHTGEKPYKCNECGKTFSQELTLKCHRRLHTGEKPYKCNECGKVFNKKANLARHHRLHSGEKPYKCTECVKTFSRNSALVIHKAIHIGEKRYKCNECGKTFSRISALVIHTAIHTGEKPYKCNECGKGFNRKTHLACHHRLHTGEKPYKCNECGKVFNRKTHLAHHHRLHTGDKPYKCNECGKVFNQKAHLARHHRLHTGEKPYKCNECGKVFNQKANLARHHRLHTGEKPYKFNECGKAFN
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
18PhosphorylationRDVAIEFSQEEWKCL
HHHHHCCCHHHHHHC
24.7227251275
23UbiquitinationEFSQEEWKCLDPAQR
CCCHHHHHHCCHHHH
28.35-
41PhosphorylationRDVMLENYRNLVSLD
HHHHHHHHHHHEECC
7.4822210691
46PhosphorylationENYRNLVSLDISSKC
HHHHHHEECCCCCCH
24.4022210691
56UbiquitinationISSKCMMKEFSSTAQ
CCCCHHHHHHHHHHC
28.82-
60PhosphorylationCMMKEFSSTAQGNRE
HHHHHHHHHHCCCCE
32.8430631047
134UbiquitinationDQRHAGNKPIKDQLG
HHCCCCCCCHHHHHH
47.40-
175PhosphorylationINDASSISTSQRISC
HHCCHHCCHHHCCCC
24.77-
176PhosphorylationNDASSISTSQRISCR
HCCHHCCHHHCCCCC
27.49-
177PhosphorylationDASSISTSQRISCRP
CCHHCCHHHCCCCCC
15.63-
227PhosphorylationSGKAFNYSSLLRKHQ
CCCCCCHHHHHHHHC
18.6626434776
228PhosphorylationGKAFNYSSLLRKHQI
CCCCCHHHHHHHHCE
22.5124719451
287PhosphorylationFSQTYSLTCHRRLHT
HHEEEEEEEECCCCC
10.58-
294PhosphorylationTCHRRLHTGEKPYKC
EEECCCCCCCCCCCC
52.1827422710
297SumoylationRRLHTGEKPYKCEEC
CCCCCCCCCCCCCCC
55.80-
297UbiquitinationRRLHTGEKPYKCEEC
CCCCCCCCCCCCCCC
55.8021890473
297SumoylationRRLHTGEKPYKCEEC
CCCCCCCCCCCCCCC
55.80-
300SumoylationHTGEKPYKCEECDKA
CCCCCCCCCCCCCCC
43.63-
300SumoylationHTGEKPYKCEECDKA
CCCCCCCCCCCCCCC
43.63-
309PhosphorylationEECDKAFSFKSNLKR
CCCCCCCCCHHHHHH
36.3024719451
328SumoylationHAGEKPYKCNECGKT
CCCCCCEECCCCCCC
38.83-
328SumoylationHAGEKPYKCNECGKT
CCCCCCEECCCCCCC
38.83-
335PhosphorylationKCNECGKTFSQTSSL
ECCCCCCCCCCCCCC
17.50-
339PhosphorylationCGKTFSQTSSLTCHR
CCCCCCCCCCCEECC
21.05-
340PhosphorylationGKTFSQTSSLTCHRR
CCCCCCCCCCEECCE
18.7327251275
341PhosphorylationKTFSQTSSLTCHRRL
CCCCCCCCCEECCEE
30.9627251275
343PhosphorylationFSQTSSLTCHRRLHT
CCCCCCCEECCEECC
14.28-
350PhosphorylationTCHRRLHTGEKPFKC
EECCEECCCCCCEEC
52.1818669648
353SumoylationRRLHTGEKPFKCNEC
CEECCCCCCEECCCC
58.04-
353SumoylationRRLHTGEKPFKCNEC
CEECCCCCCEECCCC
58.04-
362UbiquitinationFKCNECGKTFSRKSS
EECCCCCCCCCCCCC
59.04-
378PhosphorylationTCHHRLHTGEKPYKC
EECCCCCCCCCCEEC
52.1827422710
381SumoylationHRLHTGEKPYKCNEC
CCCCCCCCCEECCCC
55.80-
381UbiquitinationHRLHTGEKPYKCNEC
CCCCCCCCCEECCCC
55.8021890473
381SumoylationHRLHTGEKPYKCNEC
CCCCCCCCCEECCCC
55.80-
383PhosphorylationLHTGEKPYKCNECGK
CCCCCCCEECCCCCC
38.96-
384SumoylationHTGEKPYKCNECGKT
CCCCCCEECCCCCCC
38.83-
384SumoylationHTGEKPYKCNECGKT
CCCCCCEECCCCCCC
38.83-
384UbiquitinationHTGEKPYKCNECGKT
CCCCCCEECCCCCCC
38.83-
406PhosphorylationKCHRRLHTGEKPYKC
HHHHCCCCCCCCEEC
52.1827422710
409SumoylationRRLHTGEKPYKCNEC
HCCCCCCCCEECCCC
55.80-
409UbiquitinationRRLHTGEKPYKCNEC
HCCCCCCCCEECCCC
55.8021890473
409SumoylationRRLHTGEKPYKCNEC
HCCCCCCCCEECCCC
55.80-
411PhosphorylationLHTGEKPYKCNECGK
CCCCCCCEECCCCHH
38.96-
412SumoylationHTGEKPYKCNECGKV
CCCCCCEECCCCHHC
38.83-
412UbiquitinationHTGEKPYKCNECGKV
CCCCCCEECCCCHHC
38.83-
412SumoylationHTGEKPYKCNECGKV
CCCCCCEECCCCHHC
38.83-
422AcetylationECGKVFNKKANLARH
CCHHCCCHHHHHHHH
41.6220167786
434PhosphorylationARHHRLHSGEKPYKC
HHHHCCCCCCCCCCC
53.9226425664
465AcetylationKAIHIGEKRYKCNEC
EEEHHCCCCEECCCC
56.6813467601
474UbiquitinationYKCNECGKTFSRISA
EECCCCCCCHHHHHH
59.04-
490PhosphorylationVIHTAIHTGEKPYKC
HHHHHHHCCCCCEEC
40.7129496963
493UbiquitinationTAIHTGEKPYKCNEC
HHHHCCCCCEECCCC
55.80-
493SumoylationTAIHTGEKPYKCNEC
HHHHCCCCCEECCCC
55.80-
493SumoylationTAIHTGEKPYKCNEC
HHHHCCCCCEECCCC
55.80-
495PhosphorylationIHTGEKPYKCNECGK
HHCCCCCEECCCCCC
38.9618767875
496SumoylationHTGEKPYKCNECGKG
HCCCCCEECCCCCCC
38.83-
496SumoylationHTGEKPYKCNECGKG
HCCCCCEECCCCCCC
38.83-
518PhosphorylationACHHRLHTGEKPYKC
HHCCCCCCCCCCEEC
52.1827422710
521SumoylationHRLHTGEKPYKCNEC
CCCCCCCCCEECCCC
55.80-
521UbiquitinationHRLHTGEKPYKCNEC
CCCCCCCCCEECCCC
55.8021890473
521SumoylationHRLHTGEKPYKCNEC
CCCCCCCCCEECCCC
55.80-
523PhosphorylationLHTGEKPYKCNECGK
CCCCCCCEECCCCCC
38.96-
524SumoylationHTGEKPYKCNECGKV
CCCCCCEECCCCCCC
38.83-
524UbiquitinationHTGEKPYKCNECGKV
CCCCCCEECCCCCCC
38.83-
524SumoylationHTGEKPYKCNECGKV
CCCCCCEECCCCCCC
38.83-
546PhosphorylationAHHHRLHTGDKPYKC
HHCCCCCCCCCCEEC
52.2324719451
549AcetylationHRLHTGDKPYKCNEC
CCCCCCCCCEECCCH
52.1425953088
552SumoylationHTGDKPYKCNECGKV
CCCCCCEECCCHHHH
38.83-
552SumoylationHTGDKPYKCNECGKV
CCCCCCEECCCHHHH
38.83-
574PhosphorylationARHHRLHTGEKPYKC
HHHCCCCCCCCCEEC
52.1827422710
577SumoylationHRLHTGEKPYKCNEC
CCCCCCCCCEECCCC
55.80-
577UbiquitinationHRLHTGEKPYKCNEC
CCCCCCCCCEECCCC
55.8021890473
577SumoylationHRLHTGEKPYKCNEC
CCCCCCCCCEECCCC
55.80-
579PhosphorylationLHTGEKPYKCNECGK
CCCCCCCEECCCCHH
38.96-
580SumoylationHTGEKPYKCNECGKV
CCCCCCEECCCCHHH
38.83-
580UbiquitinationHTGEKPYKCNECGKV
CCCCCCEECCCCHHH
38.83-
580SumoylationHTGEKPYKCNECGKV
CCCCCCEECCCCHHH
38.83-
602PhosphorylationARHHRLHTGEKPYKF
HHHCCCCCCCCCCCC
52.1827422710
605SumoylationHRLHTGEKPYKFNEC
CCCCCCCCCCCCCCC
55.80-
605UbiquitinationHRLHTGEKPYKFNEC
CCCCCCCCCCCCCCC
55.8021890473
605SumoylationHRLHTGEKPYKFNEC
CCCCCCCCCCCCCCC
55.80-

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 ZN813_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ZN813_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 ZN813_HUMAN !!

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

Oops, there are no PPI records of ZN813_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 ZN813_HUMAN

loading...

Related Literatures of Post-Translational Modification

TOP