| UniProt ID | ZCHC3_HUMAN | |
|---|---|---|
| UniProt AC | Q9NUD5 | |
| Protein Name | Zinc finger CCHC domain-containing protein 3 | |
| Gene Name | ZCCHC3 | |
| Organism | Homo sapiens (Human). | |
| Sequence Length | 404 | |
| Subcellular Localization | ||
| Protein Description | ||
| Protein Sequence | MATGGGAEEERKRGRPQLLPPARPAARGEEADGGREKMGWAQVVKNLAEKKGEFREPRPPRREEESGGGGGSAGLGGPAGLAAPDLGDFPPAGRGDPKGRRRDPAGEAVDPRKKKGAAEAGRRKKAEAAAAAMATPARPGEAEDAAERPLQDEPAAAAAGPGKGRFLVRICFQGDEGACPTRDFVVGALILRSIGMDPSDIYAVIQIPGSREFDVSFRSAEKLALFLRVYEEKREQEDCWENFVVLGRSKSSLKTLFILFRNETVDVEDIVTWLKRHCDVLAVPVKVTDRFGIWTGEYKCEIELRQGEGGVRHLPGAFFLGAERGYSWYKGQPKTCFKCGSRTHMSGSCTQDRCFRCGEEGHLSPYCRKGIVCNLCGKRGHAFAQCPKAVHNSVAAQLTGVAGH | |
| 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 |
|---|---|---|---|---|---|
| 45 | Ubiquitination | MGWAQVVKNLAEKKG CCHHHHHHHHHHHCC | 47.60 | 22817900 | |
| 45 | Ubiquitination | MGWAQVVKNLAEKKG CCHHHHHHHHHHHCC | 47.60 | - | |
| 50 | Ubiquitination | VVKNLAEKKGEFREP HHHHHHHHCCCCCCC | 61.54 | 22817900 | |
| 94 | Methylation | GDFPPAGRGDPKGRR CCCCCCCCCCCCCCC | 48.74 | 80702665 | |
| 124 | Acetylation | AAEAGRRKKAEAAAA HHHHHHHHHHHHHHH | 55.78 | 70875 | |
| 125 | Acetylation | AEAGRRKKAEAAAAA HHHHHHHHHHHHHHH | 50.04 | 70879 | |
| 201 | Phosphorylation | IGMDPSDIYAVIQIP CCCCHHHCEEEEECC | 2.53 | 15592455 | |
| 202 | Phosphorylation | GMDPSDIYAVIQIPG CCCHHHCEEEEECCC | 10.37 | 25147952 | |
| 222 | Ubiquitination | VSFRSAEKLALFLRV EECHHHHHHHHHHHH | 38.48 | - | |
| 275 | Ubiquitination | EDIVTWLKRHCDVLA HHHHHHHHHHCCEEE | 31.49 | - | |
| 285 | Ubiquitination | CDVLAVPVKVTDRFG CCEEEEEEEEECCCC | 6.64 | 24816145 | |
| 286 | Ubiquitination | DVLAVPVKVTDRFGI CEEEEEEEEECCCCC | 33.09 | - | |
| 329 | Ubiquitination | AERGYSWYKGQPKTC CCCCCCCCCCCCCEE | 10.17 | 32015554 | |
| 329 | Neddylation | AERGYSWYKGQPKTC CCCCCCCCCCCCCEE | 10.17 | 32015554 | |
| 330 | Ubiquitination | ERGYSWYKGQPKTCF CCCCCCCCCCCCEEE | 44.82 | - | |
| 350 | Phosphorylation | THMSGSCTQDRCFRC CCCCCCCCCCCEECC | 34.89 | - | |
| 353 | Methylation | SGSCTQDRCFRCGEE CCCCCCCCEECCCCC | 16.20 | 115920341 | |
| 363 | Phosphorylation | RCGEEGHLSPYCRKG CCCCCCCCCCCCCCC | 8.96 | 24719451 | |
| 364 | Phosphorylation | CGEEGHLSPYCRKGI CCCCCCCCCCCCCCE | 14.24 | 25159151 | |
| 366 | Phosphorylation | EEGHLSPYCRKGIVC CCCCCCCCCCCCEEE | 11.08 | 29396449 | |
| 369 | Ubiquitination | HLSPYCRKGIVCNLC CCCCCCCCCEEECCC | 49.80 | - | |
| 377 | Ubiquitination | GIVCNLCGKRGHAFA CEEECCCCCCCCCHH | 26.34 | 32015554 | |
| 387 | Ubiquitination | GHAFAQCPKAVHNSV CCCHHHCCHHHHHHH | 18.63 | 32015554 |
| 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 ZCHC3_HUMAN !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of ZCHC3_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 ZCHC3_HUMAN !! | ||||||
| Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
|---|---|---|---|---|
Oops, there are no PPI records of ZCHC3_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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| Phosphorylation | |
| Reference | PubMed |
| "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-202, AND MASSSPECTROMETRY. | |
| Ubiquitylation | |
| Reference | PubMed |
| "Tryptic digestion of ubiquitin standards reveals an improved strategyfor identifying ubiquitinated proteins by mass spectrometry."; Denis N.J., Vasilescu J., Lambert J.-P., Smith J.C., Figeys D.; Proteomics 7:868-874(2007). Cited for: UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-45, AND MASSSPECTROMETRY. | |