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 | ||
* ASA = Accessible Surface Area
Locations | Modification | Substrate Peptides & Secondary Structure |
ASA (%) | Reference | Orthologous Protein Cluster |
---|---|---|---|---|---|
16 | Phosphorylation | LSSNTEASSKQERHI ECCCCCCCHHHHHHH | 31.66 | 22817900 | |
17 | Phosphorylation | SSNTEASSKQERHII CCCCCCCHHHHHHHH | 45.46 | 22817900 | |
26 | Ubiquitination | QERHIIAKLEEKRGP HHHHHHHHHHHHHCC | 46.12 | - | |
26 | Sumoylation | QERHIIAKLEEKRGP HHHHHHHHHHHHHCC | 46.12 | 28112733 | |
149 | Phosphorylation | QKVLLEKTGSQLGEQ CEEEEEHHCCCCCCC | 32.46 | - | |
165 | Phosphorylation | LPDFQPQTPRRDLRE CCCCCCCCCCCCHHH | 25.99 | 21815630 | |
173 | Phosphorylation | PRRDLRESSPAEPSQ CCCCHHHCCCCCHHH | 34.88 | 30631047 | |
174 | Phosphorylation | RRDLRESSPAEPSQA CCCHHHCCCCCHHHC | 24.31 | 25159151 | |
179 | Phosphorylation | ESSPAEPSQAGAYDR HCCCCCHHHCCCCCC | 24.94 | 30108239 | |
184 | Phosphorylation | EPSQAGAYDRLSPHH CHHHCCCCCCCCCCH | 10.73 | 30108239 | |
188 | Phosphorylation | AGAYDRLSPHHWEKS CCCCCCCCCCHHCCC | 24.07 | 23401153 | |
195 (in isoform 2) | Phosphorylation | - | 14.84 | 25056879 | |
195 | Phosphorylation | SPHHWEKSPLLQEPT CCCHHCCCCCCCCCC | 14.84 | 30266825 | |
202 | Phosphorylation | SPLLQEPTPKLAGTE CCCCCCCCCCCCCCC | 32.10 | 25159151 | |
204 | Sumoylation | LLQEPTPKLAGTEAP CCCCCCCCCCCCCCC | 54.14 | - | |
204 | Sumoylation | LLQEPTPKLAGTEAP CCCCCCCCCCCCCCC | 54.14 | 28112733 | |
215 | Phosphorylation | TEAPRMRSDNKENPQ CCCCCCCCCCCCCHH | 35.87 | - | |
230 | Sumoylation | QEGAKGAKPCAVSAG HHCCCCCCCCCCCCC | 49.66 | 28112733 | |
265 | Phosphorylation | RLSRRQVSSPNAQKP CCCCCCCCCCCCCCC | 31.57 | 30266825 | |
266 | Phosphorylation | LSRRQVSSPNAQKPF CCCCCCCCCCCCCCC | 24.26 | 25849741 | |
271 | Sumoylation | VSSPNAQKPFAHYQR CCCCCCCCCCCHHHH | 39.43 | 28112733 | |
284 | Phosphorylation | QRHCRVEYISSPLKS HHHCCCEECCCCHHH | 11.84 | 29214152 | |
286 | Phosphorylation | HCRVEYISSPLKSHP HCCCEECCCCHHHCC | 25.63 | 30266825 | |
287 | Phosphorylation | CRVEYISSPLKSHPL CCCEECCCCHHHCCH | 25.37 | 30266825 | |
291 | Phosphorylation | YISSPLKSHPLRELK ECCCCHHHCCHHHHH | 37.71 | 26074081 | |
349 | Phosphorylation | KRHKRVHTGERPYTC HHCCCCCCCCCCCCC | 37.57 | 21712546 | |
367 | Phosphorylation | GNCFGRQSTLKLHQR CCCCCCHHHHHHHHH | 34.05 | - | |
368 | Phosphorylation | NCFGRQSTLKLHQRI CCCCCHHHHHHHHHH | 21.41 | - | |
377 | Phosphorylation | KLHQRIHTGEKPYQC HHHHHHHCCCCCCCC | 44.67 | 26055452 | |
382 | Phosphorylation | IHTGEKPYQCGQCGK HHCCCCCCCCCCCCC | 27.74 | 22817900 |
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 !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of ZN174_HUMAN !! |
* 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 !! |
Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
---|---|---|---|---|
ZN174_HUMAN | ZNF174 | physical | 10567577 | |
ZN174_HUMAN | ZNF174 | physical | 11741982 | |
ZNF24_HUMAN | ZNF24 | physical | 10567577 | |
ZKSC8_HUMAN | ZKSCAN8 | physical | 10567577 | |
ZSC32_HUMAN | ZSCAN32 | physical | 20211142 |
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. |
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Phosphorylation | |
Reference | PubMed |
"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. |