dbPTM

UGPA_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	UGPA_HUMAN
UniProt AC	Q16851
Protein Name	UTP--glucose-1-phosphate uridylyltransferase
Gene Name	UGP2
Organism	Homo sapiens (Human).
Sequence Length	508
Subcellular Localization	Cytoplasm .
Protein Description	Plays a central role as a glucosyl donor in cellular metabolic pathways..
Protein Sequence	MSRFVQDLSKAMSQDGASQFQEVIRQELELSVKKELEKILTTASSHEFEHTKKDLDGFRKLFHRFLQEKGPSVDWGKIQRPPEDSIQPYEKIKARGLPDNISSVLNKLVVVKLNGGLGTSMGCKGPKSLIGVRNENTFLDLTVQQIEHLNKTYNTDVPLVLMNSFNTDEDTKKILQKYNHCRVKIYTFNQSRYPRINKESLLPVAKDVSYSGENTEAWYPPGHGDIYASFYNSGLLDTFIGEGKEYIFVSNIDNLGATVDLYILNHLMNPPNGKRCEFVMEVTNKTRADVKGGTLTQYEGKLRLVEIAQVPKAHVDEFKSVSKFKIFNTNNLWISLAAVKRLQEQNAIDMEIIVNAKTLDGGLNVIQLETAVGAAIKSFENSLGINVPRSRFLPVKTTSDLLLVMSNLYSLNAGSLTMSEKREFPTVPLVKLGSSFTKVQDYLRRFESIPDMLELDHLTVSGDVTFGKNVSLKGTVIIIANHGDRIDIPPGAVLENKIVSGNLRILDH

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2 (in isoform 2)	Phosphorylation	-	34.13	25849741
2	Phosphorylation	------MSRFVQDLS ------CCHHHHHHH	34.13	20068231
2 (in isoform 2)	Acetylation	-	34.13	21406692
3	Methylation	-----MSRFVQDLSK -----CCHHHHHHHH	34.16	115386709
9	Phosphorylation	SRFVQDLSKAMSQDG CHHHHHHHHHHCCCC	27.02	28258704
10	Ubiquitination	RFVQDLSKAMSQDGA HHHHHHHHHHCCCCH	56.24	-
12	Sulfoxidation	VQDLSKAMSQDGASQ HHHHHHHHCCCCHHH	4.20	30846556
13	Phosphorylation	QDLSKAMSQDGASQF HHHHHHHCCCCHHHH	29.94	26846344
18	Phosphorylation	AMSQDGASQFQEVIR HHCCCCHHHHHHHHH	36.74	29396449
33	Acetylation	QELELSVKKELEKIL HHHHHHHHHHHHHHH	36.83	25953088
33	2-Hydroxyisobutyrylation	QELELSVKKELEKIL HHHHHHHHHHHHHHH	36.83	-
33	Ubiquitination	QELELSVKKELEKIL HHHHHHHHHHHHHHH	36.83	-
41	Phosphorylation	KELEKILTTASSHEF HHHHHHHHHHCCCCC	24.64	23312004
42	Phosphorylation	ELEKILTTASSHEFE HHHHHHHHHCCCCCC	22.54	23312004
44	Phosphorylation	EKILTTASSHEFEHT HHHHHHHCCCCCCCC	30.09	24275569
45	Phosphorylation	KILTTASSHEFEHTK HHHHHHCCCCCCCCC	25.27	26437602
51	Phosphorylation	SSHEFEHTKKDLDGF CCCCCCCCCCCHHHH	32.37	23312004
52	2-Hydroxyisobutyrylation	SHEFEHTKKDLDGFR CCCCCCCCCCHHHHH	46.31	-
52	Ubiquitination	SHEFEHTKKDLDGFR CCCCCCCCCCHHHHH	46.31	-
69	Ubiquitination	FHRFLQEKGPSVDWG HHHHHHHHCCCCCCC	64.26	-
69	2-Hydroxyisobutyrylation	FHRFLQEKGPSVDWG HHHHHHHHCCCCCCC	64.26	-
69	Malonylation	FHRFLQEKGPSVDWG HHHHHHHHCCCCCCC	64.26	26320211
69	Acetylation	FHRFLQEKGPSVDWG HHHHHHHHCCCCCCC	64.26	23954790
69	Succinylation	FHRFLQEKGPSVDWG HHHHHHHHCCCCCCC	64.26	23954790
72	Phosphorylation	FLQEKGPSVDWGKIQ HHHHHCCCCCCCCCC	41.18	21406692
77	Ubiquitination	GPSVDWGKIQRPPED CCCCCCCCCCCCCCC	31.26	-
77	2-Hydroxyisobutyrylation	GPSVDWGKIQRPPED CCCCCCCCCCCCCCC	31.26	-
77	Acetylation	GPSVDWGKIQRPPED CCCCCCCCCCCCCCC	31.26	26051181
85	Phosphorylation	IQRPPEDSIQPYEKI CCCCCCCCCCCHHHH	22.82	24275569
89	Phosphorylation	PEDSIQPYEKIKARG CCCCCCCHHHHHHCC	17.30	-
91	Acetylation	DSIQPYEKIKARGLP CCCCCHHHHHHCCCC	43.60	23236377
91	Malonylation	DSIQPYEKIKARGLP CCCCCHHHHHHCCCC	43.60	26320211
91	Ubiquitination	DSIQPYEKIKARGLP CCCCCHHHHHHCCCC	43.60	-
92 (in isoform 2)	Phosphorylation	-	2.56	24719451
102	Phosphorylation	RGLPDNISSVLNKLV CCCCCCHHHHHHHEE	22.20	25850435
103	Phosphorylation	GLPDNISSVLNKLVV CCCCCHHHHHHHEEE	27.16	28258704
109 (in isoform 2)	Phosphorylation	-	5.06	24719451
119	Phosphorylation	KLNGGLGTSMGCKGP EECCCCCCCCCCCCC	22.15	29396449
120	Phosphorylation	LNGGLGTSMGCKGPK ECCCCCCCCCCCCCH	16.04	29396449
124	Acetylation	LGTSMGCKGPKSLIG CCCCCCCCCCHHHEE	72.95	24885337
137	Phosphorylation	IGVRNENTFLDLTVQ EEECCCCCEEEEEHH	21.28	27174698
142	Phosphorylation	ENTFLDLTVQQIEHL CCCEEEEEHHHHHHH	18.88	27174698
172	Acetylation	FNTDEDTKKILQKYN CCCCHHHHHHHHHHC	50.57	155719
177	Ubiquitination	DTKKILQKYNHCRVK HHHHHHHHHCCCEEE	44.57	-
177	2-Hydroxyisobutyrylation	DTKKILQKYNHCRVK HHHHHHHHHCCCEEE	44.57	-
177	Acetylation	DTKKILQKYNHCRVK HHHHHHHHHCCCEEE	44.57	26051181
184	2-Hydroxyisobutyrylation	KYNHCRVKIYTFNQS HHCCCEEEEEEECCC	15.62	-
184	Acetylation	KYNHCRVKIYTFNQS HHCCCEEEEEEECCC	15.62	26051181
186	Phosphorylation	NHCRVKIYTFNQSRY CCCEEEEEEECCCCC	10.28	21253578
198	Ubiquitination	SRYPRINKESLLPVA CCCCCCCHHHCCCCC	46.43	-
198	Acetylation	SRYPRINKESLLPVA CCCCCCCHHHCCCCC	46.43	25038526
280 (in isoform 2)	Ubiquitination	-	4.10	21890473
291	2-Hydroxyisobutyrylation	NKTRADVKGGTLTQY CCCCCCCCCCEEEEE	52.77	-
291	Ubiquitination	NKTRADVKGGTLTQY CCCCCCCCCCEEEEE	52.77	2190698
291	Malonylation	NKTRADVKGGTLTQY CCCCCCCCCCEEEEE	52.77	26320211
291	Acetylation	NKTRADVKGGTLTQY CCCCCCCCCCEEEEE	52.77	26051181
291 (in isoform 1)	Ubiquitination	-	52.77	21890473
294	Phosphorylation	RADVKGGTLTQYEGK CCCCCCCEEEEEECE	34.99	21406692
296	Phosphorylation	DVKGGTLTQYEGKLR CCCCCEEEEEECEEE	29.01	28152594
298	Phosphorylation	KGGTLTQYEGKLRLV CCCEEEEEECEEEEE	22.78	28152594
301	Ubiquitination	TLTQYEGKLRLVEIA EEEEEECEEEEEEEE	20.63	-
312	Ubiquitination	VEIAQVPKAHVDEFK EEEECCCHHHHHHCC	52.87	-
312	2-Hydroxyisobutyrylation	VEIAQVPKAHVDEFK EEEECCCHHHHHHCC	52.87	-
312	Acetylation	VEIAQVPKAHVDEFK EEEECCCHHHHHHCC	52.87	26051181
319	Acetylation	KAHVDEFKSVSKFKI HHHHHHCCCCCEEEE	48.15	23236377
319	Ubiquitination	KAHVDEFKSVSKFKI HHHHHHCCCCCEEEE	48.15	-
320	Phosphorylation	AHVDEFKSVSKFKIF HHHHHCCCCCEEEEE	36.62	26437602
329	Phosphorylation	SKFKIFNTNNLWISL CEEEEEECCCEEEEH	18.09	-
378	Phosphorylation	AVGAAIKSFENSLGI HHHHHHHHHHHHCCC	31.51	-
397	Phosphorylation	SRFLPVKTTSDLLLV HHCCCCCCHHHHHHH	31.59	21406692
398	Phosphorylation	RFLPVKTTSDLLLVM HCCCCCCHHHHHHHH	17.96	21406692
399	Phosphorylation	FLPVKTTSDLLLVMS CCCCCCHHHHHHHHH	31.34	21406692
406	Phosphorylation	SDLLLVMSNLYSLNA HHHHHHHHHCCCCCC	19.06	21406692
409	Phosphorylation	LLVMSNLYSLNAGSL HHHHHHCCCCCCCCC	18.50	21406692
410	Phosphorylation	LVMSNLYSLNAGSLT HHHHHCCCCCCCCCC	20.50	21406692
415	Phosphorylation	LYSLNAGSLTMSEKR CCCCCCCCCCCCCCC	20.46	21406692
417	Phosphorylation	SLNAGSLTMSEKREF CCCCCCCCCCCCCCC	21.98	21406692
419	Phosphorylation	NAGSLTMSEKREFPT CCCCCCCCCCCCCCC	34.43	21406692
421	Ubiquitination	GSLTMSEKREFPTVP CCCCCCCCCCCCCCC	50.34	-
423 (in isoform 2)	Phosphorylation	-	68.02	24719451
424 (in isoform 2)	Phosphorylation	-	7.74	24719451
426	Phosphorylation	SEKREFPTVPLVKLG CCCCCCCCCCEEECC	39.82	27362937
427 (in isoform 2)	Acetylation	-	3.34	-
434	Phosphorylation	VPLVKLGSSFTKVQD CCEEECCCCCHHHHH	32.49	19764811
435	Phosphorylation	PLVKLGSSFTKVQDY CEEECCCCCHHHHHH	34.83	27362937
437	Phosphorylation	VKLGSSFTKVQDYLR EECCCCCHHHHHHHH	32.05	27362937
437 (in isoform 2)	Phosphorylation	-	32.05	24719451
438	Malonylation	KLGSSFTKVQDYLRR ECCCCCHHHHHHHHH	35.57	26320211
438	Acetylation	KLGSSFTKVQDYLRR ECCCCCHHHHHHHHH	35.57	19608861
442	Phosphorylation	SFTKVQDYLRRFESI CCHHHHHHHHHHHCC	5.75	26852163
448	Phosphorylation	DYLRRFESIPDMLEL HHHHHHHCCCCHHCC	36.39	28192239
459	Phosphorylation	MLELDHLTVSGDVTF HHCCCEEEEECCEEE	14.81	21406692
461	Phosphorylation	ELDHLTVSGDVTFGK CCCEEEEECCEEECC	24.84	8612650
465	Phosphorylation	LTVSGDVTFGKNVSL EEEECCEEECCCCEE	31.26	21406692
471	Phosphorylation	VTFGKNVSLKGTVII EEECCCCEECCEEEE	33.48	21406692
475	Phosphorylation	KNVSLKGTVIIIANH CCCEECCEEEEEECC	13.62	22210691
500	Phosphorylation	VLENKIVSGNLRILD EECCEEEECCCEECC	25.99	22210691

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 UGPA_HUMAN !!

Functions of PTM Sites

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

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
ARI2_HUMAN	ARIH2	physical	16189514
UGPA_HUMAN	UGP2	physical	16189514
MRO2B_HUMAN	MROH2B	physical	22939629
UGPA_HUMAN	UGP2	physical	21988832
CUL1_HUMAN	CUL1	physical	22863883
SYFB_HUMAN	FARSB	physical	22863883
PUR2_HUMAN	GART	physical	22863883
HIRP3_HUMAN	HIRIP3	physical	22863883
HS105_HUMAN	HSPH1	physical	22863883
ILK_HUMAN	ILK	physical	22863883
NUDC_HUMAN	NUDC	physical	22863883
NUSAP_HUMAN	NUSAP1	physical	22863883
PACN2_HUMAN	PACSIN2	physical	22863883
PAPOA_HUMAN	PAPOLA	physical	22863883
PARVA_HUMAN	PARVA	physical	22863883
PLOD2_HUMAN	PLOD2	physical	22863883
PPM1G_HUMAN	PPM1G	physical	22863883
2A5G_HUMAN	PPP2R5C	physical	22863883
PUF60_HUMAN	PUF60	physical	22863883
RANB3_HUMAN	RANBP3	physical	22863883
SET_HUMAN	SET	physical	22863883
SYTC_HUMAN	TARS	physical	22863883
RO60_HUMAN	TROVE2	physical	22863883
VASN_HUMAN	VASN	physical	22863883
ZYX_HUMAN	ZYX	physical	22863883
UGPA_HUMAN	UGP2	physical	25416956
ARI2_HUMAN	ARIH2	physical	25416956
GLRX3_HUMAN	GLRX3	physical	25416956
A16A1_HUMAN	ALDH16A1	physical	26344197
GLPK2_HUMAN	GK2	physical	26344197
CH10_HUMAN	HSPE1	physical	26344197
KHK_HUMAN	KHK	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 UGPA_HUMAN

Related Literatures of Post-Translational Modification

Acetylation
Reference	PubMed
"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-438, AND MASS SPECTROMETRY.	19608861 [Abstract]