ZN174_HUMAN - dbPTM
ZN174_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ZN174_HUMAN
UniProt AC Q15697
Protein Name Zinc finger protein 174
Gene Name ZNF174
Organism Homo sapiens (Human).
Sequence Length 407
Subcellular Localization Nucleus.
Protein Description Transcriptional repressor..
Protein Sequence MAAKMEITLSSNTEASSKQERHIIAKLEEKRGPPLQKNCPDPELCRQSFRRFCYQEVSGPQEALSQLRQLCRQWLQPELHTKEQILELLVMEQFLTILPPEIQARVRHRCPMSSKEIVTLVEDFHRASKKPKQWVAVCMQGQKVLLEKTGSQLGEQELPDFQPQTPRRDLRESSPAEPSQAGAYDRLSPHHWEKSPLLQEPTPKLAGTEAPRMRSDNKENPQQEGAKGAKPCAVSAGRSKGNGLQNPEPRGANMSEPRLSRRQVSSPNAQKPFAHYQRHCRVEYISSPLKSHPLRELKKSKGGKRSLSNRLQHLGHQPTRSAKKPYKCDDCGKSFTWNSELKRHKRVHTGERPYTCGECGNCFGRQSTLKLHQRIHTGEKPYQCGQCGKSFRQSSNLHQHHRLHHGD
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
16PhosphorylationLSSNTEASSKQERHI
ECCCCCCCHHHHHHH
31.6622817900
17PhosphorylationSSNTEASSKQERHII
CCCCCCCHHHHHHHH
45.4622817900
26UbiquitinationQERHIIAKLEEKRGP
HHHHHHHHHHHHHCC
46.12-
26SumoylationQERHIIAKLEEKRGP
HHHHHHHHHHHHHCC
46.1228112733
149PhosphorylationQKVLLEKTGSQLGEQ
CEEEEEHHCCCCCCC
32.46-
165PhosphorylationLPDFQPQTPRRDLRE
CCCCCCCCCCCCHHH
25.9921815630
173PhosphorylationPRRDLRESSPAEPSQ
CCCCHHHCCCCCHHH
34.8830631047
174PhosphorylationRRDLRESSPAEPSQA
CCCHHHCCCCCHHHC
24.3125159151
179PhosphorylationESSPAEPSQAGAYDR
HCCCCCHHHCCCCCC
24.9430108239
184PhosphorylationEPSQAGAYDRLSPHH
CHHHCCCCCCCCCCH
10.7330108239
188PhosphorylationAGAYDRLSPHHWEKS
CCCCCCCCCCHHCCC
24.0723401153
195 (in isoform 2)Phosphorylation-14.8425056879
195PhosphorylationSPHHWEKSPLLQEPT
CCCHHCCCCCCCCCC
14.8430266825
202PhosphorylationSPLLQEPTPKLAGTE
CCCCCCCCCCCCCCC
32.1025159151
204SumoylationLLQEPTPKLAGTEAP
CCCCCCCCCCCCCCC
54.14-
204SumoylationLLQEPTPKLAGTEAP
CCCCCCCCCCCCCCC
54.1428112733
215PhosphorylationTEAPRMRSDNKENPQ
CCCCCCCCCCCCCHH
35.87-
230SumoylationQEGAKGAKPCAVSAG
HHCCCCCCCCCCCCC
49.6628112733
265PhosphorylationRLSRRQVSSPNAQKP
CCCCCCCCCCCCCCC
31.5730266825
266PhosphorylationLSRRQVSSPNAQKPF
CCCCCCCCCCCCCCC
24.2625849741
271SumoylationVSSPNAQKPFAHYQR
CCCCCCCCCCCHHHH
39.4328112733
284PhosphorylationQRHCRVEYISSPLKS
HHHCCCEECCCCHHH
11.8429214152
286PhosphorylationHCRVEYISSPLKSHP
HCCCEECCCCHHHCC
25.6330266825
287PhosphorylationCRVEYISSPLKSHPL
CCCEECCCCHHHCCH
25.3730266825
291PhosphorylationYISSPLKSHPLRELK
ECCCCHHHCCHHHHH
37.7126074081
349PhosphorylationKRHKRVHTGERPYTC
HHCCCCCCCCCCCCC
37.5721712546
367PhosphorylationGNCFGRQSTLKLHQR
CCCCCCHHHHHHHHH
34.05-
368PhosphorylationNCFGRQSTLKLHQRI
CCCCCHHHHHHHHHH
21.41-
377PhosphorylationKLHQRIHTGEKPYQC
HHHHHHHCCCCCCCC
44.6726055452
382PhosphorylationIHTGEKPYQCGQCGK
HHCCCCCCCCCCCCC
27.7422817900

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 ZN174_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ZN174_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 ZN174_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
ZN174_HUMANZNF174physical
10567577
ZN174_HUMANZNF174physical
11741982
ZNF24_HUMANZNF24physical
10567577
ZKSC8_HUMANZKSCAN8physical
10567577
ZSC32_HUMANZSCAN32physical
20211142

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 ZN174_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Evaluation of the low-specificity protease elastase for large-scalephosphoproteome analysis.";
Wang B., Malik R., Nigg E.A., Korner R.;
Anal. Chem. 80:9526-9533(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-195, AND MASSSPECTROMETRY.
"Immunoaffinity profiling of tyrosine phosphorylation in cancercells.";
Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,Zha X.-M., Polakiewicz R.D., Comb M.J.;
Nat. Biotechnol. 23:94-101(2005).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-382, AND MASSSPECTROMETRY.

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