UniProt ID | UCK2_HUMAN | |
---|---|---|
UniProt AC | Q9BZX2 | |
Protein Name | Uridine-cytidine kinase 2 | |
Gene Name | UCK2 | |
Organism | Homo sapiens (Human). | |
Sequence Length | 261 | |
Subcellular Localization | ||
Protein Description | Phosphorylates uridine and cytidine to uridine monophosphate and cytidine monophosphate. Does not phosphorylate deoxyribonucleosides or purine ribonucleosides. Can use ATP or GTP as a phosphate donor. Can also phosphorylate cytidine and uridine nucleoside analogs such as 6-azauridine, 5-fluorouridine, 4-thiouridine, 5-bromouridine, N(4)-acetylcytidine, N(4)-benzoylcytidine, 5-fluorocytidine, 2-thiocytidine, 5-methylcytidine, and N(4)-anisoylcytidine.. | |
Protein Sequence | MAGDSEQTLQNHQQPNGGEPFLIGVSGGTASGKSSVCAKIVQLLGQNEVDYRQKQVVILSQDSFYRVLTSEQKAKALKGQFNFDHPDAFDNELILKTLKEITEGKTVQIPVYDFVSHSRKEETVTVYPADVVLFEGILAFYSQEVRDLFQMKLFVDTDADTRLSRRVLRDISERGRDLEQILSQYITFVKPAFEEFCLPTKKYADVIIPRGADNLVAINLIVQHIQDILNGGPSKRQTNGCLNGYTPSRKRQASESSSRPH | |
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 |
---|---|---|---|---|---|
2 | Acetylation | ------MAGDSEQTL ------CCCCHHHHH | 30.42 | 19413330 | |
8 | Phosphorylation | MAGDSEQTLQNHQQP CCCCHHHHHHHCCCC | 26.68 | 25627689 | |
18 | Ubiquitination | NHQQPNGGEPFLIGV HCCCCCCCCCEEEEE | 46.15 | 22053931 | |
33 | Ubiquitination | SGGTASGKSSVCAKI ECCCCCCCHHHHHHH | 36.74 | 23000965 | |
39 (in isoform 1) | Ubiquitination | - | 37.98 | 21890473 | |
39 | Ubiquitination | GKSSVCAKIVQLLGQ CCHHHHHHHHHHHCC | 37.98 | 21906983 | |
51 | Phosphorylation | LGQNEVDYRQKQVVI HCCCCCCCCCCEEEE | 21.81 | 27642862 | |
52 (in isoform 2) | Ubiquitination | - | 32.53 | 21890473 | |
52 | Ubiquitination | GQNEVDYRQKQVVIL CCCCCCCCCCEEEEE | 32.53 | 23000965 | |
54 | Ubiquitination | NEVDYRQKQVVILSQ CCCCCCCCEEEEEEC | 35.74 | 23000965 | |
54 (in isoform 1) | Ubiquitination | - | 35.74 | 21890473 | |
57 | Ubiquitination | DYRQKQVVILSQDSF CCCCCEEEEEECCHH | 3.18 | 23000965 | |
57 | Neddylation | DYRQKQVVILSQDSF CCCCCEEEEEECCHH | 3.18 | 32015554 | |
60 | Phosphorylation | QKQVVILSQDSFYRV CCEEEEEECCHHHHH | 22.33 | 20873877 | |
63 | Phosphorylation | VVILSQDSFYRVLTS EEEEECCHHHHHCCH | 19.28 | 20873877 | |
73 (in isoform 1) | Ubiquitination | - | 48.04 | 21890473 | |
73 | Ubiquitination | RVLTSEQKAKALKGQ HHCCHHHHHHHHCCC | 48.04 | 23000965 | |
75 (in isoform 1) | Ubiquitination | - | 62.38 | 21890473 | |
75 | Ubiquitination | LTSEQKAKALKGQFN CCHHHHHHHHCCCCC | 62.38 | 23000965 | |
78 | Neddylation | EQKAKALKGQFNFDH HHHHHHHCCCCCCCC | 56.37 | 32015554 | |
78 | Ubiquitination | EQKAKALKGQFNFDH HHHHHHHCCCCCCCC | 56.37 | 23000965 | |
78 (in isoform 1) | Ubiquitination | - | 56.37 | 21890473 | |
84 | Ubiquitination | LKGQFNFDHPDAFDN HCCCCCCCCCCCCCC | 54.22 | 22817900 | |
96 | Ubiquitination | FDNELILKTLKEITE CCCHHHHHHHHHHHC | 44.83 | 22817900 | |
99 | Ubiquitination | ELILKTLKEITEGKT HHHHHHHHHHHCCCC | 52.91 | 21906983 | |
99 (in isoform 1) | Ubiquitination | - | 52.91 | 21890473 | |
105 (in isoform 1) | Ubiquitination | - | 39.01 | 21890473 | |
105 | Ubiquitination | LKEITEGKTVQIPVY HHHHHCCCCEEEEEE | 39.01 | 21906983 | |
106 | O-linked_Glycosylation | KEITEGKTVQIPVYD HHHHCCCCEEEEEEE | 28.62 | 23301498 | |
148 | Ubiquitination | YSQEVRDLFQMKLFV HCHHHHHHHHCEEEE | 1.94 | 23000965 | |
149 | Ubiquitination | SQEVRDLFQMKLFVD CHHHHHHHHCEEEEC | 8.59 | 21890473 | |
157 | Phosphorylation | QMKLFVDTDADTRLS HCEEEECCCHHHHHH | 27.99 | - | |
162 | Methylation | VDTDADTRLSRRVLR ECCCHHHHHHHHHHH | 31.08 | 115919485 | |
180 | Ubiquitination | ERGRDLEQILSQYIT HHCCCHHHHHHHHHH | 49.58 | 23000965 | |
181 | Ubiquitination | RGRDLEQILSQYITF HCCCHHHHHHHHHHH | 2.67 | 21890473 | |
200 | Phosphorylation | FEEFCLPTKKYADVI HHHHCCCCCCCCCEE | 27.50 | 22964224 | |
201 | Ubiquitination | EEFCLPTKKYADVII HHHCCCCCCCCCEEE | 41.67 | 23000965 | |
202 | Ubiquitination | EFCLPTKKYADVIIP HHCCCCCCCCCEEEC | 48.42 | 23000965 | |
202 (in isoform 1) | Ubiquitination | - | 48.42 | 21890473 | |
214 | Ubiquitination | IIPRGADNLVAINLI EECCCCCHHHHHHHH | 35.56 | 33845483 | |
233 | Phosphorylation | QDILNGGPSKRQTNG HHHHCCCCCCCCCCC | 37.77 | 33259812 | |
234 | Phosphorylation | DILNGGPSKRQTNGC HHHCCCCCCCCCCCC | 43.69 | 26074081 | |
235 | Ubiquitination | ILNGGPSKRQTNGCL HHCCCCCCCCCCCCC | 52.22 | 33845483 | |
238 | Phosphorylation | GGPSKRQTNGCLNGY CCCCCCCCCCCCCCC | 37.30 | 26074081 | |
245 | Phosphorylation | TNGCLNGYTPSRKRQ CCCCCCCCCCCHHHH | 17.88 | 26074081 | |
246 | Phosphorylation | NGCLNGYTPSRKRQA CCCCCCCCCCHHHHH | 19.04 | 25159151 | |
248 | Phosphorylation | CLNGYTPSRKRQASE CCCCCCCCHHHHHHC | 42.51 | 28985074 | |
254 | Phosphorylation | PSRKRQASESSSRPH CCHHHHHHCCCCCCC | 29.67 | 25159151 | |
256 | Phosphorylation | RKRQASESSSRPH-- HHHHHHCCCCCCC-- | 30.99 | 21955146 | |
257 | Phosphorylation | KRQASESSSRPH--- HHHHHCCCCCCC--- | 26.72 | 30576142 | |
258 | Phosphorylation | RQASESSSRPH---- HHHHCCCCCCC---- | 60.14 | 22496350 |
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 UCK2_HUMAN !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of UCK2_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 UCK2_HUMAN !! |
Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
---|---|---|---|---|
UPP1_HUMAN | UPP1 | physical | 22939629 | |
UCK1_HUMAN | UCK1 | physical | 28514442 | |
UCKL1_HUMAN | UCKL1 | physical | 28514442 | |
IAH1_HUMAN | IAH1 | physical | 28514442 | |
SYVM_HUMAN | VARS2 | physical | 28514442 |
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 ALA-2, 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 SER-254, AND MASSSPECTROMETRY. |