dbPTM

UVRAG_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	UVRAG_HUMAN
UniProt AC	Q9P2Y5
Protein Name	UV radiation resistance-associated gene protein
Gene Name	UVRAG
Organism	Homo sapiens (Human).
Sequence Length	699
Subcellular Localization	Late endosome . Lysosome . Early endosome . Endoplasmic reticulum . Midbody . Chromosome, centromere . Colocalizes with RAB9-positive compartments involved in retrograde transport from late endosomes to trans-Golgi network. Colocalization with early
Protein Description	Versatile protein that is involved in regulation of different cellular pathways implicated in membrane trafficking. Involved in regulation of the COPI-dependent retrograde transport from Golgi and the endoplasmic reticulum by associating with the NRZ complex; the function is dependent on its binding to phosphatidylinositol 3-phosphate (PtdIns(3)P). [PubMed: 24056303 During autophagy acts as regulatory subunit of the alternative PI3K complex II (PI3KC3-C2) that mediates formation of phosphatidylinositol 3-phosphate and is believed to be involved in maturation of autophagosomes and endocytosis. Activates lipid kinase activity of PIK3C3. Involved in the regulation of degradative endocytic trafficking and cytokinesis, and in regulation of ATG9A transport from the Golgi to the autophagosome; the functions seems to implicate its association with PI3KC3-C2]
Protein Sequence	MSASASVGGPVPQPPPGPAAALPPGSAARALHVELPSQQRRLRHLRNIAARNIVNRNGHQLLDTYFTLHLCSTEKIYKEFYRSEVIKNSLNPTWRSLDFGIMPDRLDTSVSCFVVKIWGGKENIYQLLIEWKVCLDGLKYLGQQIHARNQNEIIFGLNDGYYGAPFEHKGYSNAQKTILLQVDQNCVRNSYDVFSLLRLHRAQCAIKQTQVTVQKIGKEIEEKLRLTSTSNELKKKSECLQLKILVLQNELERQKKALGREVALLHKQQIALQDKGSAFSAEHLKLQLQKESLNELRKECTAKRELFLKTNAQLTIRCRQLLSELSYIYPIDLNEHKDYFVCGVKLPNSEDFQAKDDGSIAVALGYTAHLVSMISFFLQVPLRYPIIHKGSRSTIKDNINDKLTEKEREFPLYPKGGEKLQFDYGVYLLNKNIAQLRYQHGLGTPDLRQTLPNLKNFMEHGLMVRCDRHHTSSAIPVPKRQSSIFGGADVGFSGGIPSPDKGHRKRASSENERLQYKTPPPSYNSALAQPVTTVPSMGETERKITSLSSSLDTSLDFSKENKKKGEDLVGSLNGGHANVHPSQEQGEALSGHRATVNGTLLPSEQAGSASVQLPGEFHPVSEAELCCTVEQAEEIIGLEATGFASGDQLEAFNCIPVDSAVAVECDEQVLGEFEEFSRRIYALNENVSSFRRPRRSSDK

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
24	Ubiquitination	GPAAALPPGSAARAL CCCCCCCCCCHHHHH	50.66	-
30	Ubiquitination	PPGSAARALHVELPS CCCCHHHHHHCCCCH	9.40	-
83	Phosphorylation	IYKEFYRSEVIKNSL HHHHHHHHHHHHHCC	25.49	22817900
83	Ubiquitination	IYKEFYRSEVIKNSL HHHHHHHHHHHHHCC	25.49	-
87	Ubiquitination	FYRSEVIKNSLNPTW HHHHHHHHHCCCCCH	45.73	-
96	Phosphorylation	SLNPTWRSLDFGIMP CCCCCHHHCCCCCCC	24.69	-
108	Phosphorylation	IMPDRLDTSVSCFVV CCCCCCCCCEEEEEE	35.30	-
109	Phosphorylation	MPDRLDTSVSCFVVK CCCCCCCCEEEEEEE	16.23	-
169	Ubiquitination	YGAPFEHKGYSNAQK CCCCCCCCCCCCCCC	52.96	21963094
176	Ubiquitination	KGYSNAQKTILLQVD CCCCCCCCEEEEEEC	34.81	-
207	Ubiquitination	HRAQCAIKQTQVTVQ HHHHHHHHCCEEEHH	28.86	29967540
212	Phosphorylation	AIKQTQVTVQKIGKE HHHCCEEEHHHHHHH	13.85	-
215	Methylation	QTQVTVQKIGKEIEE CCEEEHHHHHHHHHH	49.44	-
215	Ubiquitination	QTQVTVQKIGKEIEE CCEEEHHHHHHHHHH	49.44	29967540
215	Sumoylation	QTQVTVQKIGKEIEE CCEEEHHHHHHHHHH	49.44	-
215	Sumoylation	QTQVTVQKIGKEIEE CCEEEHHHHHHHHHH	49.44	-
227	Phosphorylation	IEEKLRLTSTSNELK HHHHHHHCCCCHHHH	24.43	22985185
228	Phosphorylation	EEKLRLTSTSNELKK HHHHHHCCCCHHHHH	34.14	22985185
230	Phosphorylation	KLRLTSTSNELKKKS HHHHCCCCHHHHHHH	28.24	22985185
234	Ubiquitination	TSTSNELKKKSECLQ CCCCHHHHHHHHHHH	52.56	29967540
235	Ubiquitination	STSNELKKKSECLQL CCCHHHHHHHHHHHH	74.32	29967540
236	Malonylation	TSNELKKKSECLQLK CCHHHHHHHHHHHHH	50.31	26320211
267	Ubiquitination	REVALLHKQQIALQD HHHHHHHHHHHHHCC	43.82	29967540
285	Ubiquitination	AFSAEHLKLQLQKES CCCHHHHHHHHHHHH	35.77	29967540
290	Ubiquitination	HLKLQLQKESLNELR HHHHHHHHHHHHHHH	58.84	29967540
292	Phosphorylation	KLQLQKESLNELRKE HHHHHHHHHHHHHHH	43.46	24719451
345	Ubiquitination	DYFVCGVKLPNSEDF CEEEEEEECCCCHHH	43.44	29967540
349	Phosphorylation	CGVKLPNSEDFQAKD EEEECCCCHHHCCCC	36.28	26270265
396	Ubiquitination	KGSRSTIKDNINDKL CCCCHHHHCCHHHHC	44.82	29967540
402	Ubiquitination	IKDNINDKLTEKERE HHCCHHHHCCHHHHC	53.47	-
415	Ubiquitination	REFPLYPKGGEKLQF HCCCCCCCCCCCCEE	67.02	29967540
427	Phosphorylation	LQFDYGVYLLNKNIA CEEEEEEEEECCCHH	10.91	25147952
444	Phosphorylation	RYQHGLGTPDLRQTL HHHCCCCCCCHHHHC	20.76	32645325
455	Ubiquitination	RQTLPNLKNFMEHGL HHHCCHHHHHHHCCE	55.57	-
455	Phosphorylation	RQTLPNLKNFMEHGL HHHCCHHHHHHHCCE	55.57	33259812
469	Phosphorylation	LMVRCDRHHTSSAIP EEEEECCCCCCCCCC	18.48	32142685
479	Ubiquitination	SSAIPVPKRQSSIFG CCCCCCCCCCCCCCC	64.40	29967540
482	Phosphorylation	IPVPKRQSSIFGGAD CCCCCCCCCCCCCCC	29.45	23927012
483	Phosphorylation	PVPKRQSSIFGGADV CCCCCCCCCCCCCCC	17.38	25159151
493	Phosphorylation	GGADVGFSGGIPSPD CCCCCCCCCCCCCCC	30.13	23927012
498	Phosphorylation	GFSGGIPSPDKGHRK CCCCCCCCCCCCCCC	43.75	25159151
508	Phosphorylation	KGHRKRASSENERLQ CCCCCCCCCCCCCCC	42.07	25159151
509	Phosphorylation	GHRKRASSENERLQY CCCCCCCCCCCCCCC	43.38	25159151
516	Phosphorylation	SENERLQYKTPPPSY CCCCCCCCCCCCCCC	22.78	22115753
518	Phosphorylation	NERLQYKTPPPSYNS CCCCCCCCCCCCCCC	35.77	25159151
522	Phosphorylation	QYKTPPPSYNSALAQ CCCCCCCCCCCCCCC	42.60	22115753
523	Phosphorylation	YKTPPPSYNSALAQP CCCCCCCCCCCCCCC	20.93	22115753
524	Phosphorylation	KTPPPSYNSALAQPV CCCCCCCCCCCCCCC	25.74	32645325
525	Phosphorylation	TPPPSYNSALAQPVT CCCCCCCCCCCCCCE	19.20	28122231
532	Phosphorylation	SALAQPVTTVPSMGE CCCCCCCEECCCCCC	28.85	26074081
533	Phosphorylation	ALAQPVTTVPSMGET CCCCCCEECCCCCCC	30.56	26074081
535	Phosphorylation	AQPVTTVPSMGETER CCCCEECCCCCCCHH	19.26	33259812
536	Phosphorylation	QPVTTVPSMGETERK CCCEECCCCCCCHHH	34.77	26074081
540	Phosphorylation	TVPSMGETERKITSL ECCCCCCCHHHHHHH	35.05	26074081
545	Phosphorylation	GETERKITSLSSSLD CCCHHHHHHHHHHHC	27.01	25850435
546	Phosphorylation	ETERKITSLSSSLDT CCHHHHHHHHHHHCC	29.72	25850435
548	Phosphorylation	ERKITSLSSSLDTSL HHHHHHHHHHHCCCC	20.04	23401153
549	Phosphorylation	RKITSLSSSLDTSLD HHHHHHHHHHCCCCC	39.97	30266825
550	Phosphorylation	KITSLSSSLDTSLDF HHHHHHHHHCCCCCC	27.21	30266825
553	Phosphorylation	SLSSSLDTSLDFSKE HHHHHHCCCCCCCHH	36.16	29255136
554	Phosphorylation	LSSSLDTSLDFSKEN HHHHHCCCCCCCHHH	26.13	25159151
558	Phosphorylation	LDTSLDFSKENKKKG HCCCCCCCHHHHHCC	38.43	23312004
571	Phosphorylation	KGEDLVGSLNGGHAN CCCCCCCCCCCCCCC	15.92	29255136
582	Phosphorylation	GHANVHPSQEQGEAL CCCCCCCCHHHCCCC	31.32	29523821
590	Phosphorylation	QEQGEALSGHRATVN HHHCCCCCCCEEEEC	39.33	23312004
681	Phosphorylation	EEFSRRIYALNENVS HHHHHHHHHHHCCHH	11.83	21945579
688	Phosphorylation	YALNENVSSFRRPRR HHHHCCHHHCCCCCC	35.03	30108239
689	Phosphorylation	ALNENVSSFRRPRRS HHHCCHHHCCCCCCC	20.63	21945579
696	Phosphorylation	SFRRPRRSSDK---- HCCCCCCCCCC----	44.14	20736484
697	Phosphorylation	FRRPRRSSDK----- CCCCCCCCCC-----	47.83	-

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
493	S	Phosphorylation	Kinase	MTOR	P42345	PSP
498	S	Phosphorylation	Kinase	MTOR	P42345	Uniprot
508	S	Phosphorylation	Kinase	MTOR	P42345	PSP
522	S	Phosphorylation	Kinase	MTOR	P42345	PSP
549	S	Phosphorylation	Kinase	MTOR	P42345	PSP
550	S	Phosphorylation	Kinase	MTOR	P42345	PSP
571	S	Phosphorylation	Kinase	MTOR	P42345	PSP
582	S	Phosphorylation	Kinase	MTOR	P42345	PSP
-	K	Ubiquitination	E3 ubiquitin ligase	SMURF1	Q9HCE7	PMID:30686098

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
498	S	Phosphorylation		18691976
Phosphorylated at Ser-498 by MTOR under basal conditions; increases the interaction with RUBCN implicated in inhibitory effect of RUBCN on PI3KC3 and decreases interaction with RAB7,A and VPS16 and VPS39 (indicative for a class C Vps complex, possibly the HOPS complex).

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 UVRAG_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
VP33A_HUMAN	VPS33A	physical	20562859
VPS18_HUMAN	VPS18	physical	20562859
PI3R4_HUMAN	PIK3R4	physical	20562859
PK3C3_HUMAN	PIK3C3	physical	20562859
PTPRA_HUMAN	PTPRA	physical	20562859
RUBIC_HUMAN	KIAA0226	physical	20562859
BECN1_HUMAN	BECN1	physical	20562859
TGFA1_HUMAN	TGFBRAP1	physical	20562859
VPS16_HUMAN	VPS16	physical	18552835
VPS11_HUMAN	VPS11	physical	18552835
VPS18_HUMAN	VPS18	physical	18552835
VP33A_HUMAN	VPS33A	physical	18552835
VP33B_HUMAN	VPS33B	physical	18552835
VPS39_HUMAN	VPS39	physical	18552835
BECN1_HUMAN	BECN1	physical	19270696
PK3C3_HUMAN	PIK3C3	physical	24980960
BECN1_HUMAN	BECN1	physical	18843052
PK3C3_HUMAN	PIK3C3	physical	18843052
BECN1_HUMAN	BECN1	physical	19050071
UBP18_HUMAN	USP18	physical	25906440
DDB1_HUMAN	DDB1	physical	27203177
DDB2_HUMAN	DDB2	physical	27203177
CUL4A_HUMAN	CUL4A	physical	27203177
RBX1_HUMAN	RBX1	physical	27203177
BECN1_HUMAN	BECN1	physical	27203177

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 UVRAG_HUMAN

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"Large-scale proteomics analysis of the human kinome."; Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,Mann M., Daub H.; Mol. Cell. Proteomics 8:1751-1764(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-482; SER-493; SER-498;SER-508; TYR-516; THR-518; SER-522; THR-545; SER-549; SER-550; SER-571AND SER-689, AND MASS SPECTROMETRY.	19369195 [Abstract]
"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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-689, AND MASSSPECTROMETRY.	19413330 [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-498 AND THR-518, ANDMASS SPECTROMETRY.	18691976 [Abstract]
"Automated phosphoproteome analysis for cultured cancer cells by two-dimensional nanoLC-MS using a calcined titania/C18 biphasic column."; Imami K., Sugiyama N., Kyono Y., Tomita M., Ishihama Y.; Anal. Sci. 24:161-166(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-83, AND MASSSPECTROMETRY.	18187866 [Abstract]
"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 THR-518, AND MASSSPECTROMETRY.	19690332 [Abstract]
"A quantitative atlas of mitotic phosphorylation."; Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.; Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-518, AND MASSSPECTROMETRY.	18669648 [Abstract]

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