ZN436_HUMAN - dbPTM
ZN436_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ZN436_HUMAN
UniProt AC Q9C0F3
Protein Name Zinc finger protein 436
Gene Name ZNF436
Organism Homo sapiens (Human).
Sequence Length 470
Subcellular Localization Nucleus .
Protein Description May be a transcriptional repressor..
Protein Sequence MAATLLMAGSQAPVTFEDMAMYLTREEWRPLDAAQRDLYRDVMQENYGNVVSLDFEIRSENEVNPKQEISEDVQFGTTSERPAENAEENPESEEGFESGDRSERQWGDLTAEEWVSYPLQPVTDLLVHKEVHTGIRYHICSHCGKAFSQISDLNRHQKTHTGDRPYKCYECGKGFSRSSHLIQHQRTHTGERPYDCNECGKSFGRSSHLIQHQTIHTGEKPHKCNECGKSFCRLSHLIQHQRTHSGEKPYECEECGKSFSRSSHLAQHQRTHTGEKPYECNECGRGFSERSDLIKHYRVHTGERPYKCDECGKNFSQNSDLVRHRRAHTGEKPYHCNECGENFSRISHLVQHQRTHTGEKPYECNACGKSFSRSSHLITHQKIHTGEKPYECNECWRSFGERSDLIKHQRTHTGEKPYECVQCGKGFTQSSNLITHQRVHTGEKPYECTECEKSFSRSSALIKHKRVHTD
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
4Phosphorylation----MAATLLMAGSQ
----CCCCHHCCCCC
15.7523532336
10PhosphorylationATLLMAGSQAPVTFE
CCHHCCCCCCCCCHH
17.4023663014
15PhosphorylationAGSQAPVTFEDMAMY
CCCCCCCCHHHHHHH
21.9023663014
22PhosphorylationTFEDMAMYLTREEWR
CHHHHHHHHHHHHHC
8.7223663014
24PhosphorylationEDMAMYLTREEWRPL
HHHHHHHHHHHHCCC
20.6723663014
66SumoylationSENEVNPKQEISEDV
CCCCCCCCHHHCCCC
56.1928112733
92PhosphorylationNAEENPESEEGFESG
CCCCCCCCCCCCCCC
42.0528985074
167SumoylationHTGDRPYKCYECGKG
CCCCCCEEEEECCCC
32.78-
167SumoylationHTGDRPYKCYECGKG
CCCCCCEEEEECCCC
32.78-
243PhosphorylationHLIQHQRTHSGEKPY
HHHHHCCCCCCCCCC
17.52-
245PhosphorylationIQHQRTHSGEKPYEC
HHHCCCCCCCCCCCC
48.29-
260PhosphorylationEECGKSFSRSSHLAQ
HHHCCCCCCHHHHHH
38.0417081983
271PhosphorylationHLAQHQRTHTGEKPY
HHHHHCCCCCCCCCC
19.74-
273PhosphorylationAQHQRTHTGEKPYEC
HHHCCCCCCCCCCCC
46.56-
301PhosphorylationIKHYRVHTGERPYKC
HHHCEECCCCCCCCC
37.5727251275
355PhosphorylationHLVQHQRTHTGEKPY
HHHHHCCCCCCCCCC
19.74-
357PhosphorylationVQHQRTHTGEKPYEC
HHHCCCCCCCCCCCC
46.56-
372PhosphorylationNACGKSFSRSSHLIT
CCCCCCCCCCCCCCE
38.0417081983
385PhosphorylationITHQKIHTGEKPYEC
CEECEEECCCCCCCC
50.9728655764
411PhosphorylationDLIKHQRTHTGEKPY
HHHHHCCCCCCCCCE
19.74-
413PhosphorylationIKHQRTHTGEKPYEC
HHHCCCCCCCCCEEE
46.5621712546
418PhosphorylationTHTGEKPYECVQCGK
CCCCCCCEEEEECCC
32.78-
425SumoylationYECVQCGKGFTQSSN
EEEEECCCCCCCCCC
59.48-
425SumoylationYECVQCGKGFTQSSN
EEEEECCCCCCCCCC
59.48-
441PhosphorylationITHQRVHTGEKPYEC
EECCEEECCCCCCCC
44.15-
449PhosphorylationGEKPYECTECEKSFS
CCCCCCCCCCCCCCC
31.5628985074
456PhosphorylationTECEKSFSRSSALIK
CCCCCCCCCCCHHHH
38.0417081983
465MethylationSSALIKHKRVHTD--
CCHHHHCCCCCCC--
51.63116253735

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 ZN436_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ZN436_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 ZN436_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
SUV91_HUMANSUV39H1physical
23455924
KDM1A_HUMANKDM1Aphysical
23455924
ANM5_HUMANPRMT5physical
23455924
ANM6_HUMANPRMT6physical
23455924

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 ZN436_HUMAN

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Related Literatures of Post-Translational Modification

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