dbPTM

U3IP2_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	U3IP2_HUMAN
UniProt AC	O43818
Protein Name	U3 small nucleolar RNA-interacting protein 2
Gene Name	RRP9
Organism	Homo sapiens (Human).
Sequence Length	475
Subcellular Localization	Nucleus, nucleolus .
Protein Description	Component of a nucleolar small nuclear ribonucleoprotein particle (snoRNP) thought to participate in the processing and modification of pre-ribosomal RNA..
Protein Sequence	MSATAAARKRGKPASGAGAGAGAGKRRRKADSAGDRGKSKGGGKMNEEISSDSESESLAPRKPEEEEEEELEETAQEKKLRLAKLYLEQLRQQEEEKAEARAFEEDQVAGRLKEDVLEQRGRLQKLVAKEIQAPASADIRVLRGHQLSITCLVVTPDDSAIFSAAKDCSIIKWSVESGRKLHVIPRAKKGAEGKPPGHSSHVLCMAISSDGKYLASGDRSKLILIWEAQSCQHLYTFTGHRDAVSGLAFRRGTHQLYSTSHDRSVKVWNVAENSYVETLFGHQDAVAALDALSRECCVTAGGRDGTVRVWKIPEESQLVFYGHQGSIDCIHLINEEHMVSGADDGSVALWGLSKKRPLALQREAHGLRGEPGLEQPFWISSVAALLNTDLVATGSHSSCVRLWQCGEGFRQLDLLCDIPLVGFINSLKFSSSGDFLVAGVGQEHRLGRWWRIKEARNSVCIIPLRRVPVPPAAGS

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Phosphorylation	------MSATAAARK ------CCHHHHHHH	34.03	20068231
4	Phosphorylation	----MSATAAARKRG ----CCHHHHHHHHC	14.99	20068231
9	Ubiquitination	SATAAARKRGKPASG CHHHHHHHHCCCCCC	61.86	22817900
10	Methylation	ATAAARKRGKPASGA HHHHHHHHCCCCCCC	53.46	24129315
12	Acetylation	AAARKRGKPASGAGA HHHHHHCCCCCCCCC	41.25	26051181
12	Ubiquitination	AAARKRGKPASGAGA HHHHHHCCCCCCCCC	41.25	21906983
15	Phosphorylation	RKRGKPASGAGAGAG HHHCCCCCCCCCCCC	37.39	23879269
25	Acetylation	GAGAGAGKRRRKADS CCCCCCCHHCCCCCC	42.04	25953088
25	2-Hydroxyisobutyrylation	GAGAGAGKRRRKADS CCCCCCCHHCCCCCC	42.04	-
32	Phosphorylation	KRRRKADSAGDRGKS HHCCCCCCCCCCCCC	38.72	-
39	Phosphorylation	SAGDRGKSKGGGKMN CCCCCCCCCCCCCCC	39.08	-
40	Acetylation	AGDRGKSKGGGKMNE CCCCCCCCCCCCCCC	66.13	25953088
50	Phosphorylation	GKMNEEISSDSESES CCCCCCCCCCCCCCC	31.22	29255136
51	Phosphorylation	KMNEEISSDSESESL CCCCCCCCCCCCCCC	51.31	29255136
53	Phosphorylation	NEEISSDSESESLAP CCCCCCCCCCCCCCC	44.99	29255136
55	Phosphorylation	EISSDSESESLAPRK CCCCCCCCCCCCCCC	36.12	22167270
57	Phosphorylation	SSDSESESLAPRKPE CCCCCCCCCCCCCCH	38.83	22167270
62	Ubiquitination	SESLAPRKPEEEEEE CCCCCCCCCHHHHHH	56.58	-
62	Acetylation	SESLAPRKPEEEEEE CCCCCCCCCHHHHHH	56.58	26051181
74	Phosphorylation	EEEELEETAQEKKLR HHHHHHHHHHHHHHH	25.02	30108239
78	Acetylation	LEETAQEKKLRLAKL HHHHHHHHHHHHHHH	45.06	26051181
84	Ubiquitination	EKKLRLAKLYLEQLR HHHHHHHHHHHHHHH	42.11	-
84	Acetylation	EKKLRLAKLYLEQLR HHHHHHHHHHHHHHH	42.11	25953088
86	Phosphorylation	KLRLAKLYLEQLRQQ HHHHHHHHHHHHHHH	13.90	28152594
113	Acetylation	DQVAGRLKEDVLEQR HHHHHHHHHHHHHHC	50.97	21339330
113	Sumoylation	DQVAGRLKEDVLEQR HHHHHHHHHHHHHHC	50.97	28112733
113	Ubiquitination	DQVAGRLKEDVLEQR HHHHHHHHHHHHHHC	50.97	33845483
125	Ubiquitination	EQRGRLQKLVAKEIQ HHCHHHHHHHHHHCC	49.90	23000965
129	Acetylation	RLQKLVAKEIQAPAS HHHHHHHHHCCCCCC	48.12	26051181
129	Ubiquitination	RLQKLVAKEIQAPAS HHHHHHHHHCCCCCC	48.12	21890473
129	Ubiquitination	RLQKLVAKEIQAPAS HHHHHHHHHCCCCCC	48.12	23000965
148	Phosphorylation	VLRGHQLSITCLVVT EECCCCCEEEEEEEC	14.85	27251275
150	Phosphorylation	RGHQLSITCLVVTPD CCCCCEEEEEEECCC	9.08	27251275
155	Phosphorylation	SITCLVVTPDDSAIF EEEEEEECCCCHHHH	17.33	27251275
159	Phosphorylation	LVVTPDDSAIFSAAK EEECCCCHHHHHHHC	30.55	27251275
163	Phosphorylation	PDDSAIFSAAKDCSI CCCHHHHHHHCCCCE	22.62	27251275
169	Phosphorylation	FSAAKDCSIIKWSVE HHHHCCCCEEEEEEC	37.17	24719451
172	Acetylation	AKDCSIIKWSVESGR HCCCCEEEEEECCCC	31.57	26051181
180	Ubiquitination	WSVESGRKLHVIPRA EEECCCCCEEEECCC	46.61	-
245	Phosphorylation	TGHRDAVSGLAFRRG CCCHHHHCCEEECCC	29.79	20068231
306	Phosphorylation	TAGGRDGTVRVWKIP EECCCCCEEEEEECC	14.93	26074081
316	Phosphorylation	VWKIPEESQLVFYGH EEECCCHHCEEEEEC	27.44	22210691
321	Phosphorylation	EESQLVFYGHQGSID CHHCEEEEECCCCEE	13.25	26074081
326	Phosphorylation	VFYGHQGSIDCIHLI EEEECCCCEEEEEEE	14.53	26074081
346	Phosphorylation	VSGADDGSVALWGLS CCCCCCCCEEEEECC	15.94	22210691
353	Phosphorylation	SVALWGLSKKRPLAL CEEEEECCCCCCCHH	31.99	22210691
355	Ubiquitination	ALWGLSKKRPLALQR EEEECCCCCCCHHHH	56.74	-
458	Phosphorylation	RIKEARNSVCIIPLR ECHHCCCEEEEEECC	16.89	28509920
475	Phosphorylation	PVPPAAGS------- CCCCCCCC-------	32.11	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
Oops, there are no upstream regulatory protein records of U3IP2_HUMAN !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Reference
12	K	Acetylation	26867678
Acetylation at Lys-12 and Lys-25 by KAT2B/PCAF under stress impairs pre-rRNA processing.
25	K	Acetylation	26867678
Acetylation at Lys-12 and Lys-25 by KAT2B/PCAF under stress impairs pre-rRNA processing.

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 U3IP2_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
WDR36_HUMAN	WDR36	physical	22939629
UTRO_HUMAN	UTRN	physical	22939629
VIME_HUMAN	VIM	physical	22939629
DCA13_HUMAN	DCAF13	physical	26344197
HMGN5_HUMAN	HMGN5	physical	26344197
IMP3_HUMAN	IMP3	physical	26344197
NOL6_HUMAN	NOL6	physical	26344197
PWP2_HUMAN	PWP2	physical	26344197
TBL3_HUMAN	TBL3	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 U3IP2_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-50; SER-51; SER-53 ANDSER-57, AND MASS SPECTROMETRY.	19690332 [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-50; SER-51 AND SER-53,AND MASS SPECTROMETRY.	19413330 [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 SER-50; SER-51; SER-53 ANDSER-57, AND MASS SPECTROMETRY.	18669648 [Abstract]
"Evaluation of the low-specificity protease elastase for large-scalephosphoproteome analysis."; Wang B., Malik R., Nigg E.A., Korner R.; Anal. Chem. 80:9526-9533(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-475, AND MASSSPECTROMETRY.	19007248 [Abstract]
"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks."; Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.; Cell 127:635-648(2006). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-50; SER-51 AND SER-53,AND MASS SPECTROMETRY.	17081983 [Abstract]

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