dbPTM

RO60_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	RO60_HUMAN
UniProt AC	P10155
Protein Name	60 kDa SS-A/Ro ribonucleoprotein
Gene Name	TROVE2
Organism	Homo sapiens (Human).
Sequence Length	538
Subcellular Localization	Cytoplasm . Localized in cytoplasmic mRNP granules containing untranslated mRNAs.
Protein Description	RNA-binding protein that binds to misfolded non-coding RNAs, pre-5S rRNA, and several small cytoplasmic RNA molecules known as Y RNAs. May stabilize some of these RNAs and protect them from degradation.; May play roles in cilia formation and/or maintenance..
Protein Sequence	MEESVNQMQPLNEKQIANSQDGYVWQVTDMNRLHRFLCFGSEGGTYYIKEQKLGLENAEALIRLIEDGRGCEVIQEIKSFSQEGRTTKQEPMLFALAICSQCSDISTKQAAFKAVSEVCRIPTHLFTFIQFKKDLKESMKCGMWGRALRKAIADWYNEKGGMALALAVTKYKQRNGWSHKDLLRLSHLKPSSEGLAIVTKYITKGWKEVHELYKEKALSVETEKLLKYLEAVEKVKRTRDELEVIHLIEEHRLVREHLLTNHLKSKEVWKALLQEMPLTALLRNLGKMTANSVLEPGNSEVSLVCEKLCNEKLLKKARIHPFHILIALETYKTGHGLRGKLKWRPDEEILKALDAAFYKTFKTVEPTGKRFLLAVDVSASMNQRVLGSILNASTVAAAMCMVVTRTEKDSYVVAFSDEMVPCPVTTDMTLQQVLMAMSQIPAGGTDCSLPMIWAQKTNTPADVFIVFTDNETFAGGVHPAIALREYRKKMDIPAKLIVCGMTSNGFTIADPDDRGMLDMCGFDTGALDVIRNFTLDMI

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
1	Acetylation	-------MEESVNQM -------CCCCCCCC	13.39	22223895
4	Phosphorylation	----MEESVNQMQPL ----CCCCCCCCCCC	17.04	23186163
19	Phosphorylation	NEKQIANSQDGYVWQ CHHHHCCCCCCCEEE	22.19	22167270
23	Phosphorylation	IANSQDGYVWQVTDM HCCCCCCCEEEEECC	13.55	22167270
41	Phosphorylation	HRFLCFGSEGGTYYI EEEEEEECCCCEEEE	16.90	21406692
45	Phosphorylation	CFGSEGGTYYIKEQK EEECCCCEEEEEEEC	24.82	21406692
46	Phosphorylation	FGSEGGTYYIKEQKL EECCCCEEEEEEECC	13.38	21406692
47	Phosphorylation	GSEGGTYYIKEQKLG ECCCCEEEEEEECCC	12.83	21406692
49 (in isoform 1)	Ubiquitination	-	37.66	21890473
49	Ubiquitination	EGGTYYIKEQKLGLE CCCEEEEEEECCCCC	37.66	21890473
49	Ubiquitination	EGGTYYIKEQKLGLE CCCEEEEEEECCCCC	37.66	21906983
49 (in isoform 2)	Ubiquitination	-	37.66	21906983
52	Ubiquitination	TYYIKEQKLGLENAE EEEEEEECCCCCCHH	45.68	-
69	Methylation	IRLIEDGRGCEVIQE HHHHHCCCCCHHHHH	59.93	115917861
78	Ubiquitination	CEVIQEIKSFSQEGR CHHHHHHHHCCCCCC	44.70	-
79	Phosphorylation	EVIQEIKSFSQEGRT HHHHHHHHCCCCCCC	35.47	-
113	Methylation	STKQAAFKAVSEVCR CHHHHHHHHHHHHHC	43.05	115980489
138	O-linked_Glycosylation	FKKDLKESMKCGMWG HCHHHHHHHCCCHHH	23.19	29351928
140 (in isoform 1)	Ubiquitination	-	36.59	21890473
140	Ubiquitination	KDLKESMKCGMWGRA HHHHHHHCCCHHHHH	36.59	21906983
140 (in isoform 2)	Ubiquitination	-	36.59	21906983
140	Ubiquitination	KDLKESMKCGMWGRA HHHHHHHCCCHHHHH	36.59	21890473
170	Malonylation	ALALAVTKYKQRNGW HHHHHHHHHHHHCCC	43.80	26320211
170	Acetylation	ALALAVTKYKQRNGW HHHHHHHHHHHHCCC	43.80	25953088
170	Methylation	ALALAVTKYKQRNGW HHHHHHHHHHHHCCC	43.80	30592659
180	Ubiquitination	QRNGWSHKDLLRLSH HHCCCCHHHHHHHHC	44.55	-
186	Phosphorylation	HKDLLRLSHLKPSSE HHHHHHHHCCCCCCC	21.97	23312004
189	Ubiquitination	LLRLSHLKPSSEGLA HHHHHCCCCCCCCHH	37.11	21906983
189 (in isoform 1)	Ubiquitination	-	37.11	21890473
189	Ubiquitination	LLRLSHLKPSSEGLA HHHHHCCCCCCCCHH	37.11	21890473
191	Phosphorylation	RLSHLKPSSEGLAIV HHHCCCCCCCCHHHH	39.16	20873877
192	Phosphorylation	LSHLKPSSEGLAIVT HHCCCCCCCCHHHHH	44.18	20873877
199	Phosphorylation	SEGLAIVTKYITKGW CCCHHHHHHHHHCCH	16.41	23312004
201	Phosphorylation	GLAIVTKYITKGWKE CHHHHHHHHHCCHHH	12.40	18491316
203	Phosphorylation	AIVTKYITKGWKEVH HHHHHHHHCCHHHHH	22.03	18491316
207	Ubiquitination	KYITKGWKEVHELYK HHHHCCHHHHHHHHH	59.53	-
213	Phosphorylation	WKEVHELYKEKALSV HHHHHHHHHHHCCCC	17.70	29083192
214	Acetylation	KEVHELYKEKALSVE HHHHHHHHHHCCCCC	66.42	25953088
214	Ubiquitination	KEVHELYKEKALSVE HHHHHHHHHHCCCCC	66.42	-
216	2-Hydroxyisobutyrylation	VHELYKEKALSVETE HHHHHHHHCCCCCHH	50.94	-
219	Phosphorylation	LYKEKALSVETEKLL HHHHHCCCCCHHHHH	23.83	29255136
222	Phosphorylation	EKALSVETEKLLKYL HHCCCCCHHHHHHHH	35.94	-
224 (in isoform 1)	Ubiquitination	-	67.55	21890473
224	Ubiquitination	ALSVETEKLLKYLEA CCCCCHHHHHHHHHH	67.55	21890473
224	Ubiquitination	ALSVETEKLLKYLEA CCCCCHHHHHHHHHH	67.55	21890473
224	Ubiquitination	ALSVETEKLLKYLEA CCCCCHHHHHHHHHH	67.55	21890473
224	Ubiquitination	ALSVETEKLLKYLEA CCCCCHHHHHHHHHH	67.55	21890473
224	Ubiquitination	ALSVETEKLLKYLEA CCCCCHHHHHHHHHH	67.55	21890473
224	Ubiquitination	ALSVETEKLLKYLEA CCCCCHHHHHHHHHH	67.55	21890473
224	Acetylation	ALSVETEKLLKYLEA CCCCCHHHHHHHHHH	67.55	19608861
224	2-Hydroxyisobutyrylation	ALSVETEKLLKYLEA CCCCCHHHHHHHHHH	67.55	-
227	Ubiquitination	VETEKLLKYLEAVEK CCHHHHHHHHHHHHH	59.22	21890473
227	Ubiquitination	VETEKLLKYLEAVEK CCHHHHHHHHHHHHH	59.22	21890473
227 (in isoform 1)	Ubiquitination	-	59.22	21890473
227	Ubiquitination	VETEKLLKYLEAVEK CCHHHHHHHHHHHHH	59.22	21890473
227	Ubiquitination	VETEKLLKYLEAVEK CCHHHHHHHHHHHHH	59.22	21890473
227	Ubiquitination	VETEKLLKYLEAVEK CCHHHHHHHHHHHHH	59.22	21890473
227	Ubiquitination	VETEKLLKYLEAVEK CCHHHHHHHHHHHHH	59.22	21890473
227	Acetylation	VETEKLLKYLEAVEK CCHHHHHHHHHHHHH	59.22	25953088
234	Ubiquitination	KYLEAVEKVKRTRDE HHHHHHHHHHCCHHH	46.59	-
236	Ubiquitination	LEAVEKVKRTRDELE HHHHHHHHCCHHHHH	60.15	-
264	Ubiquitination	HLLTNHLKSKEVWKA HHHHHHHCCHHHHHH	52.51	-
266	Ubiquitination	LTNHLKSKEVWKALL HHHHHCCHHHHHHHH	55.49	-
276	Sulfoxidation	WKALLQEMPLTALLR HHHHHHHCCHHHHHH	1.81	30846556
279	Phosphorylation	LLQEMPLTALLRNLG HHHHCCHHHHHHHHC	14.91	-
287	Ubiquitination	ALLRNLGKMTANSVL HHHHHHCCCCCCCCC	35.92	-
287	Malonylation	ALLRNLGKMTANSVL HHHHHHCCCCCCCCC	35.92	26320211
307	Ubiquitination	EVSLVCEKLCNEKLL HHHHHHHHHHCHHHH	53.89	-
307	Acetylation	EVSLVCEKLCNEKLL HHHHHHHHHHCHHHH	53.89	26051181
312	Malonylation	CEKLCNEKLLKKARI HHHHHCHHHHHHCCC	45.16	26320211
312	Ubiquitination	CEKLCNEKLLKKARI HHHHHCHHHHHHCCC	45.16	-
312	Acetylation	CEKLCNEKLLKKARI HHHHHCHHHHHHCCC	45.16	23749302
342	Ubiquitination	HGLRGKLKWRPDEEI CCCCCCCCCCCCHHH	44.64	21890473
342	Ubiquitination	HGLRGKLKWRPDEEI CCCCCCCCCCCCHHH	44.64	21890473
342 (in isoform 1)	Ubiquitination	-	44.64	21890473
342	Ubiquitination	HGLRGKLKWRPDEEI CCCCCCCCCCCCHHH	44.64	21890473
342	Ubiquitination	HGLRGKLKWRPDEEI CCCCCCCCCCCCHHH	44.64	21890473
342	Ubiquitination	HGLRGKLKWRPDEEI CCCCCCCCCCCCHHH	44.64	21890473
342	Acetylation	HGLRGKLKWRPDEEI CCCCCCCCCCCCHHH	44.64	25953088
342	Ubiquitination	HGLRGKLKWRPDEEI CCCCCCCCCCCCHHH	44.64	21890473
359	Acetylation	ALDAAFYKTFKTVEP HHHHHHHHHCCCCCC	40.82	19608861
359	Ubiquitination	ALDAAFYKTFKTVEP HHHHHHHHHCCCCCC	40.82	21890473
359	Ubiquitination	ALDAAFYKTFKTVEP HHHHHHHHHCCCCCC	40.82	21890473
359	Ubiquitination	ALDAAFYKTFKTVEP HHHHHHHHHCCCCCC	40.82	21890473
359	Ubiquitination	ALDAAFYKTFKTVEP HHHHHHHHHCCCCCC	40.82	21890473
359	Ubiquitination	ALDAAFYKTFKTVEP HHHHHHHHHCCCCCC	40.82	21890473
359 (in isoform 1)	Ubiquitination	-	40.82	21890473
359	Ubiquitination	ALDAAFYKTFKTVEP HHHHHHHHHCCCCCC	40.82	21890473
362	Ubiquitination	AAFYKTFKTVEPTGK HHHHHHCCCCCCCCC	57.82	-
369	2-Hydroxyisobutyrylation	KTVEPTGKRFLLAVD CCCCCCCCEEEEEEE	42.32	-
393	Phosphorylation	LGSILNASTVAAAMC HHHHHCHHHHHHHHH	23.49	18452278
394	Phosphorylation	GSILNASTVAAAMCM HHHHCHHHHHHHHHH	16.26	18452278
503	Phosphorylation	LIVCGMTSNGFTIAD EEEEECCCCCEEECC	26.51	24114839
519 (in isoform 5)	Phosphorylation	-	1.80	20068231
524 (in isoform 5)	Phosphorylation	-	23.30	21406692
537	Sulfoxidation	IRNFTLDMI------ HHHCCCCCC------	4.39	30846556

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 RO60_HUMAN !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of RO60_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 RO60_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
RO52_HUMAN	TRIM21	physical	10785401
LA_HUMAN	SSB	physical	10785401
TEP1_HUMAN	TEP1	physical	22939629
SYCC_HUMAN	CARS	physical	22863883
GFPT1_HUMAN	GFPT1	physical	22863883
HIRP3_HUMAN	HIRIP3	physical	22863883
RL24_HUMAN	RPL24	physical	22863883
SF01_HUMAN	SF1	physical	22863883
XPO7_HUMAN	XPO7	physical	22863883
ATLA3_HUMAN	ATL3	physical	26344197
TCP4_HUMAN	SUB1	physical	26344197
QCR8_HUMAN	UQCRQ	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 RO60_HUMAN

Related Literatures of Post-Translational Modification

Acetylation
Reference	PubMed
"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 MET-1, AND MASS SPECTROMETRY.	19413330 [Abstract]
"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-224 AND LYS-359, AND MASSSPECTROMETRY.	19608861 [Abstract]
Phosphorylation
Reference	PubMed
"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 SER-19, AND MASSSPECTROMETRY.	18669648 [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-19, AND MASSSPECTROMETRY.	18691976 [Abstract]
"ATM and ATR substrate analysis reveals extensive protein networksresponsive to DNA damage."; Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III,Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.; Science 316:1160-1166(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-19, AND MASSSPECTROMETRY.	17525332 [Abstract]