dbPTM

UCKL1_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	UCKL1_HUMAN
UniProt AC	Q9NWZ5
Protein Name	Uridine-cytidine kinase-like 1
Gene Name	UCKL1
Organism	Homo sapiens (Human).
Sequence Length	548
Subcellular Localization	Cytoplasm . Nucleus . EBNA3 induces isoform 1 translocation to the nucleus, whereas it does change isoform 3 location.
Protein Description	May contribute to UTP accumulation needed for blast transformation and proliferation..
Protein Sequence	MAAPPARADADPSPTSPPTARDTPGRQAEKSETACEDRSNAESLDRLLPPVGTGRSPRKRTTSQCKSEPPLLRTSKRTIYTAGRPPWYNEHGTQSKEAFAIGLGGGSASGKTTVARMIIEALDVPWVVLLSMDSFYKVLTEQQQEQAAHNNFNFDHPDAFDFDLIISTLKKLKQGKSVKVPIYDFTTHSRKKDWKTLYGANVIIFEGIMAFADKTLLELLDMKIFVDTDSDIRLVRRLRRDISERGRDIEGVIKQYNKFVKPSFDQYIQPTMRLADIVVPRGSGNTVAIDLIVQHVHSQLEERELSVRAALASAHQCHPLPRTLSVLKSTPQVRGMHTIIRDKETSRDEFIFYSKRLMRLLIEHALSFLPFQDCVVQTPQGQDYAGKCYAGKQITGVSILRAGETMEPALRAVCKDVRIGTILIQTNQLTGEPELHYLRLPKDISDDHVILMDCTVSTGAAAMMAVRVLLDHDVPEDKIFLLSLLMAEMGVHSVAYAFPRVRIITTAVDKRVNDLFRIIPGIGNFGDRYFGTDAVPDGSDEEEVAYTG

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
13	Phosphorylation	ARADADPSPTSPPTA CCCCCCCCCCCCCCC	41.16	30266825
15	Phosphorylation	ADADPSPTSPPTARD CCCCCCCCCCCCCCC	59.19	30266825
16	Phosphorylation	DADPSPTSPPTARDT CCCCCCCCCCCCCCC	32.06	29255136
19	Phosphorylation	PSPTSPPTARDTPGR CCCCCCCCCCCCCCC	37.40	29255136
23	Phosphorylation	SPPTARDTPGRQAEK CCCCCCCCCCCCCCC	23.30	20068231
39	Phosphorylation	ETACEDRSNAESLDR CCCCCCCCCHHHHHH	53.35	21712546
43	Phosphorylation	EDRSNAESLDRLLPP CCCCCHHHHHHHCCC	32.91	21712546
53	Phosphorylation	RLLPPVGTGRSPRKR HHCCCCCCCCCCCCC	29.65	30266825
56	Phosphorylation	PPVGTGRSPRKRTTS CCCCCCCCCCCCCHH	30.33	29255136
61	Phosphorylation	GRSPRKRTTSQCKSE CCCCCCCCHHHCCCC	33.56	25106551
62	Phosphorylation	RSPRKRTTSQCKSEP CCCCCCCHHHCCCCC	22.34	25106551
63	Phosphorylation	SPRKRTTSQCKSEPP CCCCCCHHHCCCCCC	32.73	23927012
66	Ubiquitination	KRTTSQCKSEPPLLR CCCHHHCCCCCCCEE	50.66	-
67	Phosphorylation	RTTSQCKSEPPLLRT CCHHHCCCCCCCEEC	64.06	23927012
74	Phosphorylation	SEPPLLRTSKRTIYT CCCCCEECCCCEEEE	38.27	26074081
75	Phosphorylation	EPPLLRTSKRTIYTA CCCCEECCCCEEEEC	17.44	26074081
78	Phosphorylation	LLRTSKRTIYTAGRP CEECCCCEEEECCCC	23.28	25404012
80	Phosphorylation	RTSKRTIYTAGRPPW ECCCCEEEECCCCCC	7.02	25404012
81	Phosphorylation	TSKRTIYTAGRPPWY CCCCEEEECCCCCCC	20.84	25404012
88	Phosphorylation	TAGRPPWYNEHGTQS ECCCCCCCCCCCCCC	19.22	25404012
93	Phosphorylation	PWYNEHGTQSKEAFA CCCCCCCCCCCEEEE	31.41	25404012
95	Phosphorylation	YNEHGTQSKEAFAIG CCCCCCCCCEEEEEE	32.09	25404012
107	Phosphorylation	AIGLGGGSASGKTTV EEECCCCCCCCHHHH	23.65	21082442
111	Ubiquitination	GGGSASGKTTVARMI CCCCCCCHHHHHHHH	38.23	-
179	Acetylation	LKQGKSVKVPIYDFT HHCCCCEEEEEEECC	49.76	25953088
179	Ubiquitination	LKQGKSVKVPIYDFT HHCCCCEEEEEEECC	49.76	-
196	Phosphorylation	SRKKDWKTLYGANVI CCCCCHHHHHCCCEE	22.43	30622161
198	Phosphorylation	KKDWKTLYGANVIIF CCCHHHHHCCCEEEE	21.30	30622161
215	Phosphorylation	IMAFADKTLLELLDM HHHHCCHHHHHHCCC	36.80	-
228	Phosphorylation	DMKIFVDTDSDIRLV CCEEEECCHHHHHHH	31.91	-
230	Phosphorylation	KIFVDTDSDIRLVRR EEEECCHHHHHHHHH	36.71	-
254	Ubiquitination	RDIEGVIKQYNKFVK CCHHHHHHHHHHHHC	44.30	-
261	Ubiquitination	KQYNKFVKPSFDQYI HHHHHHHCCCHHHHC	37.77	21906983
261 (in isoform 1)	Ubiquitination	-	37.77	21906983
261 (in isoform 2)	Ubiquitination	-	37.77	21906983
261 (in isoform 3)	Ubiquitination	-	37.77	21906983
313	Phosphorylation	SVRAALASAHQCHPL HHHHHHHHHHHCCCC	27.43	28555341
317	S-nitrosylation	ALASAHQCHPLPRTL HHHHHHHCCCCCCHH	2.27	22178444
328 (in isoform 3)	Ubiquitination	-	50.56	21906983
328	Ubiquitination	PRTLSVLKSTPQVRG CCHHHHHHCCCCCCC	50.56	21906983
328 (in isoform 1)	Ubiquitination	-	50.56	21906983
343	Ubiquitination	MHTIIRDKETSRDEF CEEEECCCCCCHHHH	53.71	-
387	Ubiquitination	QGQDYAGKCYAGKQI CCCCCCCCCCCCCEE	18.85	-
392	Ubiquitination	AGKCYAGKQITGVSI CCCCCCCCEECEEEE	30.29	-
505	Phosphorylation	FPRVRIITTAVDKRV CCCEEEEEHHHHHHH	13.31	23403867
506	Phosphorylation	PRVRIITTAVDKRVN CCEEEEEHHHHHHHH	17.80	23403867
510	Malonylation	IITTAVDKRVNDLFR EEEHHHHHHHHHHHH	52.20	26320211
510	Ubiquitination	IITTAVDKRVNDLFR EEEHHHHHHHHHHHH	52.20	-
510 (in isoform 1)	Ubiquitination	-	52.20	21906983
510	Acetylation	IITTAVDKRVNDLFR EEEHHHHHHHHHHHH	52.20	23749302
529	Phosphorylation	IGNFGDRYFGTDAVP CCCCCCCCCCCCCCC	15.88	30108239
532	Phosphorylation	FGDRYFGTDAVPDGS CCCCCCCCCCCCCCC	15.75	30108239
539	Phosphorylation	TDAVPDGSDEEEVAY CCCCCCCCCHHHHCC	49.59	12199906
546	Phosphorylation	SDEEEVAYTG----- CCHHHHCCCC-----	19.71	30108239
547	Phosphorylation	DEEEVAYTG------ CHHHHCCCC------	27.03	30108239

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
-	K	Ubiquitination	E3 ubiquitin ligase	RNF19B	Q6ZMZ0	PMID:16709802

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of UCKL1_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 UCKL1_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference	Domain-Domain Interactions
BCS1_HUMAN	BCS1L	physical	26344197

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 UCKL1_HUMAN

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions."; Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.; Sci. Signal. 2:RA46-RA46(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-16 AND SER-539, AND MASSSPECTROMETRY.	19690332 [Abstract]
"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-56, AND MASSSPECTROMETRY.	18691976 [Abstract]
"A probability-based approach for high-throughput proteinphosphorylation analysis and site localization."; Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.; Nat. Biotechnol. 24:1285-1292(2006). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-16, AND MASSSPECTROMETRY.	16964243 [Abstract]