KTHY_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: KTHY_HUMAN
• UniProt AC: P23919
• Protein Name: Thymidylate kinase
• Gene Name: DTYMK
• Organism: Homo sapiens (Human).
• Sequence Length: 212
• Protein Description: Catalyzes the conversion of dTMP to dTDP..
• Protein Sequence: MAARRGALIVLEGVDRAGKSTQSRKLVEALCAAGHRAELLRFPERSTEIGKLLSSYLQKKSDVEDHSVHLLFSANRWEQVPLIKEKLSQGVTLVVDRYAFSGVAFTGAKENFSLDWCKQPDVGLPKPDLVLFLQLQLADAAKRGAFGHERYENGAFQERALRCFHQLMKDTTLNWKMVDASKSIEAVHEDIRVLSEDAIRTATEKPLGELWK

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
2	Acetylation	------MAARRGALI ------CCCCCCCEE	15.07	19413330
25	Ubiquitination	GKSTQSRKLVEALCA CCCHHHHHHHHHHHH	63.23	-
25	Acetylation	GKSTQSRKLVEALCA CCCHHHHHHHHHHHH	63.23	26051181
31	Glutathionylation	RKLVEALCAAGHRAE HHHHHHHHHHCCHHH	2.92	22555962
31	S-nitrosylation	RKLVEALCAAGHRAE HHHHHHHHHHCCHHH	2.92	22178444
31	S-nitrosocysteine	RKLVEALCAAGHRAE HHHHHHHHHHCCHHH	2.92	-
41	Methylation	GHRAELLRFPERSTE CCHHHHCCCCHHHHH	58.67	-
51	Ubiquitination	ERSTEIGKLLSSYLQ HHHHHHHHHHHHHHH	52.49	21890473
51	Acetylation	ERSTEIGKLLSSYLQ HHHHHHHHHHHHHHH	52.49	23236377
51	Ubiquitination	ERSTEIGKLLSSYLQ HHHHHHHHHHHHHHH	52.49	21890473
54	Phosphorylation	TEIGKLLSSYLQKKS HHHHHHHHHHHHHCC	27.63	28152594
55	Phosphorylation	EIGKLLSSYLQKKSD HHHHHHHHHHHHCCC	29.81	21406692
56	Phosphorylation	IGKLLSSYLQKKSDV HHHHHHHHHHHCCCC	15.13	21406692
59	Acetylation	LLSSYLQKKSDVEDH HHHHHHHHCCCCCCC	52.21	25953088
59	Malonylation	LLSSYLQKKSDVEDH HHHHHHHHCCCCCCC	52.21	26320211
59	Ubiquitination	LLSSYLQKKSDVEDH HHHHHHHHCCCCCCC	52.21	-
60	Malonylation	LSSYLQKKSDVEDHS HHHHHHHCCCCCCCC	38.64	26320211
84	Ubiquitination	WEQVPLIKEKLSQGV HHCCCHHHHHHHCCC	57.38	-
88	Phosphorylation	PLIKEKLSQGVTLVV CHHHHHHHCCCEEEE	35.64	22210691
92	Phosphorylation	EKLSQGVTLVVDRYA HHHHCCCEEEEEEEE	22.21	20068231
106	Phosphorylation	AFSGVAFTGAKENFS ECCCEEECCCCCCCC	26.88	22210691
118	Ubiquitination	NFSLDWCKQPDVGLP CCCCCCCCCCCCCCC	61.69	-
143	Methylation	QLADAAKRGAFGHER HHHHHHHHCCCCCHH	36.62	-
151	Phosphorylation	GAFGHERYENGAFQE CCCCCHHHHCCHHHH	15.68	27642862
169	Acetylation	RCFHQLMKDTTLNWK HHHHHHHCCCCCCCE	61.59	19608861
169	Succinylation	RCFHQLMKDTTLNWK HHHHHHHCCCCCCCE	61.59	23954790
176	Ubiquitination	KDTTLNWKMVDASKS CCCCCCCEEECCHHH	28.15	-
176	2-Hydroxyisobutyrylation	KDTTLNWKMVDASKS CCCCCCCEEECCHHH	28.15	-
182	Ubiquitination	WKMVDASKSIEAVHE CEEECCHHHHHHHHH	58.11	-
182	2-Hydroxyisobutyrylation	WKMVDASKSIEAVHE CEEECCHHHHHHHHH	58.11	-
182	Acetylation	WKMVDASKSIEAVHE CEEECCHHHHHHHHH	58.11	25038526
183	Phosphorylation	KMVDASKSIEAVHED EEECCHHHHHHHHHH	24.14	30624053
192	Methylation	EAVHEDIRVLSEDAI HHHHHHHHHHCHHHH	35.33	-
195	Phosphorylation	HEDIRVLSEDAIRTA HHHHHHHCHHHHHHH	30.49	-
201	Phosphorylation	LSEDAIRTATEKPLG HCHHHHHHHCCCCHH	31.64	-
205	Ubiquitination	AIRTATEKPLGELWK HHHHHCCCCHHHHCC	40.98	-
205	Malonylation	AIRTATEKPLGELWK HHHHHCCCCHHHHCC	40.98	30639696
212	Acetylation	KPLGELWK------- CCHHHHCC-------	64.19	30588319

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
88	S	Phosphorylation	Kinase	ATM	Q13315	PSP
-	K	Ubiquitination	E3 ubiquitin ligase	FZR1	Q9UM11	PMID:16103219

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of KTHY_HUMAN !!

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Oops, there are no SNP-PTM records of KTHY_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
DHB7_HUMAN	HSD17B7	physical	21988832

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.

Related Literatures of Post-Translational Modification

Acetylation

"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.
PubMed: 19413330

"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-169, AND MASS SPECTROMETRY.
PubMed: 19608861