KCY_HUMAN - dbPTM
KCY_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID KCY_HUMAN
UniProt AC P30085
Protein Name UMP-CMP kinase {ECO:0000255|HAMAP-Rule:MF_03172}
Gene Name CMPK1 {ECO:0000255|HAMAP-Rule:MF_03172}
Organism Homo sapiens (Human).
Sequence Length 196
Subcellular Localization Nucleus . Cytoplasm . Predominantly cytoplasmic, less than 15% nuclear.
Protein Description Catalyzes the phosphorylation of pyrimidine nucleoside monophosphates at the expense of ATP. Plays an important role in de novo pyrimidine nucleotide biosynthesis. Has preference for UMP and CMP as phosphate acceptors. Also displays broad nucleoside diphosphate kinase activity..
Protein Sequence MKPLVVFVLGGPGAGKGTQCARIVEKYGYTHLSAGELLRDERKNPDSQYGELIEKYIKEGKIVPVEITISLLKREMDQTMAANAQKNKFLIDGFPRNQDNLQGWNKTMDGKADVSFVLFFDCNNEICIERCLERGKSSGRSDDNRESLEKRIQTYLQSTKPIIDLYEEMGKVKKIDASKSVDEVFDEVVQIFDKEG
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
1Sulfoxidation-------MKPLVVFV
-------CCCEEEEE		10.2128183972
26UbiquitinationQCARIVEKYGYTHLS
HHHHHHHHHCCCEEC		32.8421890473
26AcetylationQCARIVEKYGYTHLS
HHHHHHHHHCCCEEC		32.8425953088
29PhosphorylationRIVEKYGYTHLSAGE
HHHHHHCCCEECHHH		6.4624719451
30PhosphorylationIVEKYGYTHLSAGEL
HHHHHCCCEECHHHH		16.3924719451
30 (in isoform 2)Phosphorylation-16.39-
33PhosphorylationKYGYTHLSAGELLRD
HHCCCEECHHHHHHC		26.9923312004
43MalonylationELLRDERKNPDSQYG
HHHHCHHHCCCCHHH		71.4426320211
43AcetylationELLRDERKNPDSQYG
HHHHCHHHCCCCHHH		71.4423954790
43UbiquitinationELLRDERKNPDSQYG
HHHHCHHHCCCCHHH		71.4421906983
47PhosphorylationDERKNPDSQYGELIE
CHHHCCCCHHHHHHH		26.9328152594
49PhosphorylationRKNPDSQYGELIEKY
HHCCCCHHHHHHHHH		19.2728152594
55AcetylationQYGELIEKYIKEGKI
HHHHHHHHHHHCCCE		45.3319608861
55UbiquitinationQYGELIEKYIKEGKI
HHHHHHHHHHHCCCE		45.3321890473
56PhosphorylationYGELIEKYIKEGKIV
HHHHHHHHHHCCCEE		12.3919835603
58UbiquitinationELIEKYIKEGKIVPV
HHHHHHHHCCCEEEE		58.27-
58UbiquitinationELIEKYIKEGKIVPV
HHHHHHHHCCCEEEE		58.2721890473
65PhosphorylationKEGKIVPVEITISLL
HCCCEEEEEHHHHHH		6.0227251275
68PhosphorylationKIVPVEITISLLKRE
CEEEEEHHHHHHHHH		7.3319835603
70PhosphorylationVPVEITISLLKREMD
EEEEHHHHHHHHHHH		20.9919835603
71UbiquitinationPVEITISLLKREMDQ
EEEHHHHHHHHHHHH		6.0521890473
73SumoylationEITISLLKREMDQTM
EHHHHHHHHHHHHHH		52.1628112733
73AcetylationEITISLLKREMDQTM
EHHHHHHHHHHHHHH		52.1626051181
75UbiquitinationTISLLKREMDQTMAA
HHHHHHHHHHHHHHH		45.5921890473
75UbiquitinationTISLLKREMDQTMAA
HHHHHHHHHHHHHHH		45.59-
75AcetylationTISLLKREMDQTMAA
HHHHHHHHHHHHHHH		45.59-
76SulfoxidationISLLKREMDQTMAAN
HHHHHHHHHHHHHHH		5.5530846556
79PhosphorylationLKREMDQTMAANAQK
HHHHHHHHHHHHHHC		12.4320068231
80SulfoxidationKREMDQTMAANAQKN
HHHHHHHHHHHHHCC		2.4930846556
81PhosphorylationREMDQTMAANAQKNK
HHHHHHHHHHHHCCC		10.84-
86UbiquitinationTMAANAQKNKFLIDG
HHHHHHHCCCEEECC		60.75-
87UbiquitinationMAANAQKNKFLIDGF
HHHHHHCCCEEECCC		28.3821890473
87UbiquitinationMAANAQKNKFLIDGF
HHHHHHCCCEEECCC		28.3819608861
87AcetylationMAANAQKNKFLIDGF
HHHHHHCCCEEECCC		28.3819608861
88PhosphorylationAANAQKNKFLIDGFP
HHHHHCCCEEECCCC		48.89-
88AcetylationAANAQKNKFLIDGFP
HHHHHCCCEEECCCC		48.8926051181
882-HydroxyisobutyrylationAANAQKNKFLIDGFP
HHHHHCCCEEECCCC		48.89-
88UbiquitinationAANAQKNKFLIDGFP
HHHHHCCCEEECCCC		48.8921890473
89UbiquitinationANAQKNKFLIDGFPR
HHHHCCCEEECCCCC		11.4721890473
100PhosphorylationGFPRNQDNLQGWNKT
CCCCCCCCCCCCCCC		25.21-
102PhosphorylationPRNQDNLQGWNKTMD
CCCCCCCCCCCCCCC		62.20-
106SuccinylationDNLQGWNKTMDGKAD
CCCCCCCCCCCCCCC		38.4221906983
106AcetylationDNLQGWNKTMDGKAD
CCCCCCCCCCCCCCC		38.4227452117
106UbiquitinationDNLQGWNKTMDGKAD
CCCCCCCCCCCCCCC		38.4221890473
106SuccinylationDNLQGWNKTMDGKAD
CCCCCCCCCCCCCCC		38.42-
106MethylationDNLQGWNKTMDGKAD
CCCCCCCCCCCCCCC		38.42-
107PhosphorylationNLQGWNKTMDGKADV
CCCCCCCCCCCCCCE		19.79-
120UbiquitinationDVSFVLFFDCNNEIC
CEEEEEEEECCCEEH		10.27-
120UbiquitinationDVSFVLFFDCNNEIC
CEEEEEEEECCCEEH		10.272189047
137PhosphorylationRCLERGKSSGRSDDN
HHHHHCCCCCCCCCC		40.6328348404
138UbiquitinationCLERGKSSGRSDDNR
HHHHCCCCCCCCCCH		41.5321906983
138MethylationCLERGKSSGRSDDNR
HHHHCCCCCCCCCCH		41.53-
138UbiquitinationCLERGKSSGRSDDNR
HHHHCCCCCCCCCCH		41.53-
141PhosphorylationRGKSSGRSDDNRESL
HCCCCCCCCCCHHHH		53.4929214152
147PhosphorylationRSDDNRESLEKRIQT
CCCCCHHHHHHHHHH		38.2920068231
150SuccinylationDNRESLEKRIQTYLQ
CCHHHHHHHHHHHHH		61.1623954790
150AcetylationDNRESLEKRIQTYLQ
CCHHHHHHHHHHHHH		61.1625953088
150UbiquitinationDNRESLEKRIQTYLQ
CCHHHHHHHHHHHHH		61.16-
154PhosphorylationSLEKRIQTYLQSTKP
HHHHHHHHHHHCCCC		24.6720068231
155PhosphorylationLEKRIQTYLQSTKPI
HHHHHHHHHHCCCCC		6.0820068231
158PhosphorylationRIQTYLQSTKPIIDL
HHHHHHHCCCCCHHH		35.4820068231
159PhosphorylationIQTYLQSTKPIIDLY
HHHHHHCCCCCHHHH		28.0720068231
160AcetylationQTYLQSTKPIIDLYE
HHHHHCCCCCHHHHH		39.1926051181
166PhosphorylationTKPIIDLYEEMGKVK
CCCCHHHHHHHCCCE		13.1927259358
178PhosphorylationKVKKIDASKSVDEVF
CCEECCCCCCHHHHH		23.0128258704
179PhosphorylationVKKIDASKSVDEVFD
CEECCCCCCHHHHHH		57.1020068231
180PhosphorylationKKIDASKSVDEVFDE
EECCCCCCHHHHHHH		32.1028192239
186PhosphorylationKSVDEVFDEVVQIFD
CCHHHHHHHHHHHHC		53.6220068231
187PhosphorylationSVDEVFDEVVQIFDK
CHHHHHHHHHHHHCC		32.8820068231
198PhosphorylationIFDKEG---------
HHCCCC---------		20068231
212Phosphorylation-----------------------
-----------------------		27251275
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 KCY_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of KCY_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 KCY_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
TTC19_HUMANTTC19physical
26186194
NIT2_HUMANNIT2physical
26344197
TATD1_HUMANTATDN1physical
26344197
TTC19_HUMANTTC19physical
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
DB00441Gemcitabine
DB00709Lamivudine
Regulatory Network of KCY_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions.";
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.;
Science 325:834-840(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-55, AND MASS SPECTROMETRY.

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