UCK2_HUMAN - dbPTM
UCK2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
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
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure
ASA (%) Reference Orthologous
Protein Cluster
2Acetylation------MAGDSEQTL
------CCCCHHHHH
30.4219413330
8PhosphorylationMAGDSEQTLQNHQQP
CCCCHHHHHHHCCCC
26.6825627689
18UbiquitinationNHQQPNGGEPFLIGV
HCCCCCCCCCEEEEE
46.1522053931
33UbiquitinationSGGTASGKSSVCAKI
ECCCCCCCHHHHHHH
36.7423000965
39 (in isoform 1)Ubiquitination-37.9821890473
39UbiquitinationGKSSVCAKIVQLLGQ
CCHHHHHHHHHHHCC
37.9821906983
51PhosphorylationLGQNEVDYRQKQVVI
HCCCCCCCCCCEEEE
21.8127642862
52 (in isoform 2)Ubiquitination-32.5321890473
52UbiquitinationGQNEVDYRQKQVVIL
CCCCCCCCCCEEEEE
32.5323000965
54UbiquitinationNEVDYRQKQVVILSQ
CCCCCCCCEEEEEEC
35.7423000965
54 (in isoform 1)Ubiquitination-35.7421890473
57UbiquitinationDYRQKQVVILSQDSF
CCCCCEEEEEECCHH
3.1823000965
57NeddylationDYRQKQVVILSQDSF
CCCCCEEEEEECCHH
3.1832015554
60PhosphorylationQKQVVILSQDSFYRV
CCEEEEEECCHHHHH
22.3320873877
63PhosphorylationVVILSQDSFYRVLTS
EEEEECCHHHHHCCH
19.2820873877
73 (in isoform 1)Ubiquitination-48.0421890473
73UbiquitinationRVLTSEQKAKALKGQ
HHCCHHHHHHHHCCC
48.0423000965
75 (in isoform 1)Ubiquitination-62.3821890473
75UbiquitinationLTSEQKAKALKGQFN
CCHHHHHHHHCCCCC
62.3823000965
78NeddylationEQKAKALKGQFNFDH
HHHHHHHCCCCCCCC
56.3732015554
78UbiquitinationEQKAKALKGQFNFDH
HHHHHHHCCCCCCCC
56.3723000965
78 (in isoform 1)Ubiquitination-56.3721890473
84UbiquitinationLKGQFNFDHPDAFDN
HCCCCCCCCCCCCCC
54.2222817900
96UbiquitinationFDNELILKTLKEITE
CCCHHHHHHHHHHHC
44.8322817900
99UbiquitinationELILKTLKEITEGKT
HHHHHHHHHHHCCCC
52.9121906983
99 (in isoform 1)Ubiquitination-52.9121890473
105 (in isoform 1)Ubiquitination-39.0121890473
105UbiquitinationLKEITEGKTVQIPVY
HHHHHCCCCEEEEEE
39.0121906983
106O-linked_GlycosylationKEITEGKTVQIPVYD
HHHHCCCCEEEEEEE
28.6223301498
148UbiquitinationYSQEVRDLFQMKLFV
HCHHHHHHHHCEEEE
1.9423000965
149UbiquitinationSQEVRDLFQMKLFVD
CHHHHHHHHCEEEEC
8.5921890473
157PhosphorylationQMKLFVDTDADTRLS
HCEEEECCCHHHHHH
27.99-
162MethylationVDTDADTRLSRRVLR
ECCCHHHHHHHHHHH
31.08115919485
180UbiquitinationERGRDLEQILSQYIT
HHCCCHHHHHHHHHH
49.5823000965
181UbiquitinationRGRDLEQILSQYITF
HCCCHHHHHHHHHHH
2.6721890473
200PhosphorylationFEEFCLPTKKYADVI
HHHHCCCCCCCCCEE
27.5022964224
201UbiquitinationEEFCLPTKKYADVII
HHHCCCCCCCCCEEE
41.6723000965
202UbiquitinationEFCLPTKKYADVIIP
HHCCCCCCCCCEEEC
48.4223000965
202 (in isoform 1)Ubiquitination-48.4221890473
214UbiquitinationIIPRGADNLVAINLI
EECCCCCHHHHHHHH
35.5633845483
233PhosphorylationQDILNGGPSKRQTNG
HHHHCCCCCCCCCCC
37.7733259812
234PhosphorylationDILNGGPSKRQTNGC
HHHCCCCCCCCCCCC
43.6926074081
235UbiquitinationILNGGPSKRQTNGCL
HHCCCCCCCCCCCCC
52.2233845483
238PhosphorylationGGPSKRQTNGCLNGY
CCCCCCCCCCCCCCC
37.3026074081
245PhosphorylationTNGCLNGYTPSRKRQ
CCCCCCCCCCCHHHH
17.8826074081
246PhosphorylationNGCLNGYTPSRKRQA
CCCCCCCCCCHHHHH
19.0425159151
248PhosphorylationCLNGYTPSRKRQASE
CCCCCCCCHHHHHHC
42.5128985074
254PhosphorylationPSRKRQASESSSRPH
CCHHHHHHCCCCCCC
29.6725159151
256PhosphorylationRKRQASESSSRPH--
HHHHHHCCCCCCC--
30.9921955146
257PhosphorylationKRQASESSSRPH---
HHHHHCCCCCCC---
26.7230576142
258PhosphorylationRQASESSSRPH----
HHHHCCCCCCC----
60.1422496350

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 UCK2_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of UCK2_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 UCK2_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
UPP1_HUMANUPP1physical
22939629
UCK1_HUMANUCK1physical
28514442
UCKL1_HUMANUCKL1physical
28514442
IAH1_HUMANIAH1physical
28514442
SYVM_HUMANVARS2physical
28514442

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 UCK2_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"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
ReferencePubMed
"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.

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