| UniProt ID | ZNHI2_HUMAN | |
|---|---|---|
| UniProt AC | Q9UHR6 | |
| Protein Name | Zinc finger HIT domain-containing protein 2 | |
| Gene Name | ZNHIT2 | |
| Organism | Homo sapiens (Human). | |
| Sequence Length | 403 | |
| Subcellular Localization | ||
| Protein Description | ||
| Protein Sequence | MEPAGPCGFCPAGEVQPARYTCPRCNAPYCSLRCYRTHGTCAENFYRDQVLGELRGCSAPPSRLASALRRLRQQRETEDEPGEAGLSSGPAPGGLSGLWERLAPGEKAAFERLLSRGEAGRLLPPWRPWWWNRGAGPQLLEELDNAPGSDAAELELAPARTPPDSVKDASAAEPAAAERVLGDVPGACTPVVPTRIPAIVSLSRGPVSPLVRFQLPNVLFAYAHTLALYHGGDDALLSDFCATLLGVSGALGAQQVFASAEEALQAAAHVLEAGEHPPGPLGTRGAMHEVARILLGEGPTNQKGYTLAALGDLAQTLGRARKQAVAREERDHLYRARKKCQFLLAWTNENEAALTPLALDCARAHQAHAVVAEEVAALTGELERLWGGPVPPAPRTLIEELPS | |
| Overview of Protein Modification Sites with Functional and Structural Information | ||
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* ASA = Accessible Surface Area
| Locations | Modification | Substrate Peptides & Secondary Structure |
ASA (%) | Reference | Orthologous Protein Cluster |
|---|---|---|---|---|---|
| 1 | Acetylation | -------MEPAGPCG -------CCCCCCCC | 14.54 | 22814378 | |
| 60 | Phosphorylation | ELRGCSAPPSRLASA HHCCCCCCHHHHHHH | 15.88 | 32645325 | |
| 62 | Phosphorylation | RGCSAPPSRLASALR CCCCCCHHHHHHHHH | 38.58 | - | |
| 66 | Phosphorylation | APPSRLASALRRLRQ CCHHHHHHHHHHHHH | 32.21 | 28674151 | |
| 96 | Phosphorylation | GPAPGGLSGLWERLA CCCCCCCCHHHHHHC | 34.80 | 24667141 | |
| 107 | Ubiquitination | ERLAPGEKAAFERLL HHHCCCCHHHHHHHH | 51.43 | - | |
| 115 | Phosphorylation | AAFERLLSRGEAGRL HHHHHHHHCCCCCCC | 42.71 | 26462736 | |
| 149 | Phosphorylation | ELDNAPGSDAAELEL HHHCCCCCCHHHHHC | 24.02 | 21955146 | |
| 161 | Phosphorylation | LELAPARTPPDSVKD HHCCCCCCCCCCCCC | 41.08 | 30278072 | |
| 165 | Phosphorylation | PARTPPDSVKDASAA CCCCCCCCCCCCHHC | 36.52 | 21955146 | |
| 167 | Ubiquitination | RTPPDSVKDASAAEP CCCCCCCCCCHHCCH | 52.08 | 21906983 | |
| 170 | Phosphorylation | PDSVKDASAAEPAAA CCCCCCCHHCCHHHH | 37.84 | 26434776 | |
| 189 | Phosphorylation | GDVPGACTPVVPTRI CCCCCCCCCCCCCCC | 20.70 | 21712546 | |
| 194 | Phosphorylation | ACTPVVPTRIPAIVS CCCCCCCCCCCEEEE | 29.62 | 27251275 | |
| 201 | Phosphorylation | TRIPAIVSLSRGPVS CCCCEEEECCCCCCC | 17.95 | 28555341 | |
| 203 | Phosphorylation | IPAIVSLSRGPVSPL CCEEEECCCCCCCCC | 27.90 | 24719451 | |
| 208 | Phosphorylation | SLSRGPVSPLVRFQL ECCCCCCCCCHHCCC | 18.69 | 26270265 | |
| 300 | Phosphorylation | ILLGEGPTNQKGYTL HHHCCCCCCCCCCHH | 62.23 | 20860994 | |
| 303 | Ubiquitination | GEGPTNQKGYTLAAL CCCCCCCCCCHHHHH | 56.82 | 21906983 | |
| 306 | Phosphorylation | PTNQKGYTLAALGDL CCCCCCCHHHHHHHH | 20.70 | 29496907 | |
| 316 | Phosphorylation | ALGDLAQTLGRARKQ HHHHHHHHHHHHHHH | 26.10 | - | |
| 319 | Methylation | DLAQTLGRARKQAVA HHHHHHHHHHHHHHH | 34.04 | 115920681 | |
| 322 | Acetylation | QTLGRARKQAVAREE HHHHHHHHHHHHHHH | 41.44 | 7297999 | |
| 338 | Ubiquitination | DHLYRARKKCQFLLA HHHHHHHHHCCEEEE | 57.84 | - | |
| 339 | Ubiquitination | HLYRARKKCQFLLAW HHHHHHHHCCEEEEE | 27.93 | - | |
| 403 | Phosphorylation | TLIEELPS------- HHHHHCCC------- | 66.53 | 27251275 |
| 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 ZNHI2_HUMAN !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of ZNHI2_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 ZNHI2_HUMAN !! | ||||||
| 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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| Acetylation | |
| Reference | PubMed |
| "Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach."; Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.; Anal. Chem. 81:4493-4501(2009). Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND MASS SPECTROMETRY. | |
| Phosphorylation | |
| Reference | PubMed |
| "Kinase-selective enrichment enables quantitative phosphoproteomics ofthe kinome across the cell cycle."; Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,Greff Z., Keri G., Stemmann O., Mann M.; Mol. Cell 31:438-448(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-161, AND MASSSPECTROMETRY. | |