ZN182_HUMAN - dbPTM
ZN182_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ZN182_HUMAN
UniProt AC P17025
Protein Name Zinc finger protein 182
Gene Name ZNF182
Organism Homo sapiens (Human).
Sequence Length 639
Subcellular Localization Nucleus .
Protein Description May be involved in transcriptional regulation..
Protein Sequence MTPASASGEDSGSFYSWQKAKREQGLVTFEDVAVDFTQEEWQYLNPPQRTLYRDVMLETYSNLVFVGQQVTKPNLILKLEVEECPAEGKIPFWNFPEVCQVDEQIERQHQDDQDKCLLMQVGFSDKKTIITKSARDCHEFGNILHLSTNLVASIQRPDKHESFGNNMVDNLDLFSRSSAENKYDNGCAKLFFHTEYEKTNPGMKPYGYKECGKGLRRKKGLSLHQRIKNGEKPFECTACRKTFSKKSHLIVHWRTHTGEKPFGCTECGKAFSQKSQLIIHLRTHTGERPFECPECGKAFREKSTVIIHYRTHTGEKPYECNECGKAFTQKSNLIVHQKTHTGEKTYECTKCGESFIQKLDLIIHHSTHTGKKPHECNECKKTFSDKSTLIIHQRTHTGEKPHKCTECGKSFNEKSTLIVHQRTHTGEKPYECDVCGKTFTQKSNLGVHQRTHSGEKPFECNECEKAFSQKSYLMLHQRGHTGEKPYECNECEKAFSQKSYLIIHQRTHTEEKPYKCNECGKAFREKSKLIIHQRIHTGEKPYECPVCWKAFSQKSQLIIHQRTHTGEKPYACTECGKAFREKSTFTVHQRTHTGEKPYKCTECGKAFTQKSNLIVHQRTHAGKKAHGRGHTRKSKFMAH
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
13PhosphorylationASGEDSGSFYSWQKA
CCCCCCCCCCCCHHC
25.5922210691
70UbiquitinationLVFVGQQVTKPNLIL
EEEEECCCCCCCEEE
5.9729967540
89UbiquitinationEECPAEGKIPFWNFP
EECCCCCCCCCCCCH
38.4229967540
124PhosphorylationLLMQVGFSDKKTIIT
EEEEECCCCCCEEEE
42.4629507054
128PhosphorylationVGFSDKKTIITKSAR
ECCCCCCEEEECCHH
24.29-
131PhosphorylationSDKKTIITKSARDCH
CCCCEEEECCHHHHH
18.33-
133PhosphorylationKKTIITKSARDCHEF
CCEEEECCHHHHHHH
21.64-
153PhosphorylationLSTNLVASIQRPDKH
HHCCHHHHCCCCCCC
16.2724719451
200UbiquitinationHTEYEKTNPGMKPYG
ECEEHHCCCCCCCCC
42.0429967540
219UbiquitinationGKGLRRKKGLSLHQR
CCCHHHCCCCCHHHH
64.3729967540
222PhosphorylationLRRKKGLSLHQRIKN
HHHCCCCCHHHHHHC
32.26-
228AcetylationLSLHQRIKNGEKPFE
CCHHHHHHCCCCCEE
62.1720167786
232AcetylationQRIKNGEKPFECTAC
HHHHCCCCCEECEEE
57.3020167786
241AcetylationFECTACRKTFSKKSH
EECEEEECCCCCCCE
54.5320167786
255PhosphorylationHLIVHWRTHTGEKPF
EEEEEEECCCCCCCC
20.71-
257PhosphorylationIVHWRTHTGEKPFGC
EEEEECCCCCCCCCC
46.56-
285PhosphorylationIIHLRTHTGERPFEC
EEEEEECCCCCCCCC
39.8719664995
303PhosphorylationGKAFREKSTVIIHYR
CHHHHHCCEEEEEEE
24.1319664995
304PhosphorylationKAFREKSTVIIHYRT
HHHHHCCEEEEEEEE
27.1319664995
309PhosphorylationKSTVIIHYRTHTGEK
CCEEEEEEEECCCCC
13.5419664995
311UbiquitinationTVIIHYRTHTGEKPY
EEEEEEEECCCCCCE
19.3429967540
311PhosphorylationTVIIHYRTHTGEKPY
EEEEEEEECCCCCCE
19.3428348404
313PhosphorylationIIHYRTHTGEKPYEC
EEEEEECCCCCCEEC
46.5629496963
316UbiquitinationYRTHTGEKPYECNEC
EEECCCCCCEECCCC
55.00-
319UbiquitinationHTGEKPYECNECGKA
CCCCCCEECCCCCCC
39.1229967540
330UbiquitinationCGKAFTQKSNLIVHQ
CCCCCCCCCCEEEEE
37.9529967540
338UbiquitinationSNLIVHQKTHTGEKT
CCEEEEECCCCCCCE
27.6529967540
339PhosphorylationNLIVHQKTHTGEKTY
CEEEEECCCCCCCEE
20.3529978859
341PhosphorylationIVHQKTHTGEKTYEC
EEEECCCCCCCEEEE
52.8729978859
366PhosphorylationLDLIIHHSTHTGKKP
HCEEEECCCCCCCCC
14.02-
388PhosphorylationKTFSDKSTLIIHQRT
CCCCCCCEEEEEEEC
27.93-
395PhosphorylationTLIIHQRTHTGEKPH
EEEEEEECCCCCCCC
19.74-
397PhosphorylationIIHQRTHTGEKPHKC
EEEEECCCCCCCCCC
46.56-
423PhosphorylationTLIVHQRTHTGEKPY
EEEEEECCCCCCCCE
19.74-
423UbiquitinationTLIVHQRTHTGEKPY
EEEEEECCCCCCCCE
19.7429967540
425PhosphorylationIVHQRTHTGEKPYEC
EEEECCCCCCCCEEE
46.5628555341
442UbiquitinationCGKTFTQKSNLGVHQ
CCCEEECCCCCCCCC
37.9529967540
443PhosphorylationGKTFTQKSNLGVHQR
CCEEECCCCCCCCCC
27.7230576142
453PhosphorylationGVHQRTHSGEKPFEC
CCCCCCCCCCCCCCC
48.2930576142
472PhosphorylationKAFSQKSYLMLHQRG
HHHHCCCEEEECCCC
11.81-
499PhosphorylationEKAFSQKSYLIIHQR
HHHHCCCCEEEEECC
19.9630622161
500PhosphorylationKAFSQKSYLIIHQRT
HHHCCCCEEEEECCC
14.6830622161
507PhosphorylationYLIIHQRTHTEEKPY
EEEEECCCCCCCCCC
26.9530622161
509PhosphorylationIIHQRTHTEEKPYKC
EEECCCCCCCCCCCC
45.2730622161
515SumoylationHTEEKPYKCNECGKA
CCCCCCCCCCCCHHH
38.83-
515SumoylationHTEEKPYKCNECGKA
CCCCCCCCCCCCHHH
38.83-
537PhosphorylationIIHQRIHTGEKPYEC
EEEEEEECCCCCCCC
44.6728111955
554SumoylationCWKAFSQKSQLIIHQ
CHHHHCCCCEEEEEE
38.68-
554SumoylationCWKAFSQKSQLIIHQ
CHHHHCCCCEEEEEE
38.68-
563PhosphorylationQLIIHQRTHTGEKPY
EEEEEECCCCCCCCE
19.74-
565PhosphorylationIIHQRTHTGEKPYAC
EEEECCCCCCCCEEE
46.56-
570PhosphorylationTHTGEKPYACTECGK
CCCCCCCEEECHHHH
25.94-
577UbiquitinationYACTECGKAFREKST
EEECHHHHHHHHCCC
56.88-
591PhosphorylationTFTVHQRTHTGEKPY
CEEEEECCCCCCCCE
19.7428348404
593PhosphorylationTVHQRTHTGEKPYKC
EEEECCCCCCCCEEE
46.5626270265
596UbiquitinationQRTHTGEKPYKCTEC
ECCCCCCCCEEECCC
55.80-
610UbiquitinationCGKAFTQKSNLIVHQ
CCCCCCCCCCEEEEE
37.95-

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 ZN182_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ZN182_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 ZN182_HUMAN !!

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

Oops, there are no PPI records of ZN182_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 ZN182_HUMAN

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Related Literatures of Post-Translational Modification

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