dbPTM

RBM7_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	RBM7_HUMAN
UniProt AC	Q9Y580
Protein Name	RNA-binding protein 7
Gene Name	RBM7
Organism	Homo sapiens (Human).
Sequence Length	266
Subcellular Localization	Nucleus . Excluded from the nucleolus.
Protein Description	Subunit of the trimeric nuclear exosome targeting (NEXT) complex, a complex that directs a subset of non-coding short-lived RNAs for exosomal degradation. The RNA exosome is fundamental for the degradation of RNA in eukaryotic nuclei. Substrate targeting is facilitated by its cofactor MTREX, which links to RNA-binding protein adapters. [PubMed: 27871484 Possible involved in germ cell RNA processing and meiosis (Probable]
Protein Sequence	MGAAAAEADRTLFVGNLETKVTEELLFELFHQAGPVIKVKIPKDKDGKPKQFAFVNFKHEVSVPYAMNLLNGIKLYGRPIKIQFRSGSSHAPQDVSLSYPQHHVGNSSPTSTSPSRYERTMDNMTSSAQIIQRSFSSPENFQRQAVMNSALRQMSYGGKFGSSPLDQSGFSPSVQSHSHSFNQSSSSQWRQGTPSSQRKVRMNSYPYLADRHYSREQRYTDHGSDHHYRGKRDDFFYEDRNHDDWSHDYDNRRDSSRDGKWRSSRH

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Acetylation	------MGAAAAEAD ------CCHHHHHCC	24.75	25489052
11	Phosphorylation	AAAEADRTLFVGNLE HHHHCCCEEEECCCC	25.70	20068231
19	Phosphorylation	LFVGNLETKVTEELL EEECCCCCHHCHHHH	33.70	20068231
45	"N6,N6-dimethyllysine"	KVKIPKDKDGKPKQF EEECCCCCCCCCCEE	74.61	-
45	Methylation	KVKIPKDKDGKPKQF EEECCCCCCCCCCEE	74.61	-
48	Acetylation	IPKDKDGKPKQFAFV CCCCCCCCCCEEEEE	60.21	7662453
50	Acetylation	KDKDGKPKQFAFVNF CCCCCCCCEEEEEEE	62.63	7662465
58	Acetylation	QFAFVNFKHEVSVPY EEEEEEEEEEECHHH	33.38	7662477
65	Phosphorylation	KHEVSVPYAMNLLNG EEEECHHHHHHHHCC	19.14	20860994
81	Ubiquitination	KLYGRPIKIQFRSGS EEECEEEEEEECCCC	32.89	-
86	Phosphorylation	PIKIQFRSGSSHAPQ EEEEEECCCCCCCCC	44.29	27080861
88	Phosphorylation	KIQFRSGSSHAPQDV EEEECCCCCCCCCEE	21.87	27080861
89	Phosphorylation	IQFRSGSSHAPQDVS EEECCCCCCCCCEEE	27.48	27080861
96	Phosphorylation	SHAPQDVSLSYPQHH CCCCCEEEECCCCCC	21.64	27732954
98	Phosphorylation	APQDVSLSYPQHHVG CCCEEEECCCCCCCC	27.53	29978859
99	Phosphorylation	PQDVSLSYPQHHVGN CCEEEECCCCCCCCC	16.53	29978859
107	Phosphorylation	PQHHVGNSSPTSTSP CCCCCCCCCCCCCCH	31.59	23401153
108	Phosphorylation	QHHVGNSSPTSTSPS CCCCCCCCCCCCCHH	35.88	21712546
110	Phosphorylation	HVGNSSPTSTSPSRY CCCCCCCCCCCHHHH	46.73	21712546
111	Phosphorylation	VGNSSPTSTSPSRYE CCCCCCCCCCHHHHH	30.21	23663014
112	Phosphorylation	GNSSPTSTSPSRYER CCCCCCCCCHHHHHH	47.32	21712546
113	Phosphorylation	NSSPTSTSPSRYERT CCCCCCCCHHHHHHH	22.20	21712546
115	Phosphorylation	SPTSTSPSRYERTMD CCCCCCHHHHHHHHC	47.46	21712546
117	Phosphorylation	TSTSPSRYERTMDNM CCCCHHHHHHHHCCC	17.69	29449344
120	Phosphorylation	SPSRYERTMDNMTSS CHHHHHHHHCCCCCH	19.55	22199227
121	Sulfoxidation	PSRYERTMDNMTSSA HHHHHHHHCCCCCHH	4.37	21406390
125	Phosphorylation	ERTMDNMTSSAQIIQ HHHHCCCCCHHHHHH	26.28	22199227
126	O-linked_Glycosylation	RTMDNMTSSAQIIQR HHHCCCCCHHHHHHH	16.95	31492838
126	Phosphorylation	RTMDNMTSSAQIIQR HHHCCCCCHHHHHHH	16.95	22199227
127	Phosphorylation	TMDNMTSSAQIIQRS HHCCCCCHHHHHHHH	18.28	22199227
134	Phosphorylation	SAQIIQRSFSSPENF HHHHHHHHCCCHHHH	17.07	30266825
135	Phosphorylation	AQIIQRSFSSPENFQ HHHHHHHCCCHHHHH	10.25	20058876
136	Phosphorylation	QIIQRSFSSPENFQR HHHHHHCCCHHHHHH	46.35	25159151
137	Phosphorylation	IIQRSFSSPENFQRQ HHHHHCCCHHHHHHH	33.93	19664994
138	Phosphorylation	IQRSFSSPENFQRQA HHHHCCCHHHHHHHH	39.08	19664994
143	Methylation	SSPENFQRQAVMNSA CCHHHHHHHHHHHHH	23.45	115490823
144	Methylation	SPENFQRQAVMNSAL CHHHHHHHHHHHHHH	27.76	-
149	Phosphorylation	QRQAVMNSALRQMSY HHHHHHHHHHHHHHC	15.58	21815630
150	Phosphorylation	RQAVMNSALRQMSYG HHHHHHHHHHHHHCC	11.19	-
152	Methylation	AVMNSALRQMSYGGK HHHHHHHHHHHCCCC	29.85	24129315
153	Methylation	VMNSALRQMSYGGKF HHHHHHHHHHCCCCC	26.48	-
155	Phosphorylation	NSALRQMSYGGKFGS HHHHHHHHCCCCCCC	16.58	28857561
156	Phosphorylation	SALRQMSYGGKFGSS HHHHHHHCCCCCCCC	25.26	23312004
159	Acetylation	RQMSYGGKFGSSPLD HHHHCCCCCCCCCCC	42.04	25953088
162	Phosphorylation	SYGGKFGSSPLDQSG HCCCCCCCCCCCCCC	31.73	22199227
163	Phosphorylation	YGGKFGSSPLDQSGF CCCCCCCCCCCCCCC	29.84	22199227
164	Phosphorylation	GGKFGSSPLDQSGFS CCCCCCCCCCCCCCC	41.47	-
168	Phosphorylation	GSSPLDQSGFSPSVQ CCCCCCCCCCCCCHH	41.28	22199227
169	Phosphorylation	SSPLDQSGFSPSVQS CCCCCCCCCCCCHHC	22.78	-
171	Phosphorylation	PLDQSGFSPSVQSHS CCCCCCCCCCHHCCC	21.57	22199227
172	Phosphorylation	LDQSGFSPSVQSHSH CCCCCCCCCHHCCCC	35.94	-
173	Phosphorylation	DQSGFSPSVQSHSHS CCCCCCCCHHCCCCC	31.43	29523821
176	Phosphorylation	GFSPSVQSHSHSFNQ CCCCCHHCCCCCCCC	25.46	22199227
178	Phosphorylation	SPSVQSHSHSFNQSS CCCHHCCCCCCCCCC	26.52	22199227
179	Phosphorylation	PSVQSHSHSFNQSSS CCHHCCCCCCCCCCC	30.87	-
180	Phosphorylation	SVQSHSHSFNQSSSS CHHCCCCCCCCCCCC	28.98	22199227
181	Phosphorylation	VQSHSHSFNQSSSSQ HHCCCCCCCCCCCCC	8.91	-
184	Phosphorylation	HSHSFNQSSSSQWRQ CCCCCCCCCCCCCCC	33.04	22199227
185	Phosphorylation	SHSFNQSSSSQWRQG CCCCCCCCCCCCCCC	25.01	22199227
186	Phosphorylation	HSFNQSSSSQWRQGT CCCCCCCCCCCCCCC	31.62	22199227
187	Phosphorylation	SFNQSSSSQWRQGTP CCCCCCCCCCCCCCC	35.39	22199227
190	Dimethylation	QSSSSQWRQGTPSSQ CCCCCCCCCCCCCHH	19.88	-
190	Methylation	QSSSSQWRQGTPSSQ CCCCCCCCCCCCCHH	19.88	80702625
191	Methylation	SSSSQWRQGTPSSQR CCCCCCCCCCCCHHH	58.09	-
193	Phosphorylation	SSQWRQGTPSSQRKV CCCCCCCCCCHHHHH	16.20	21406692
195	Phosphorylation	QWRQGTPSSQRKVRM CCCCCCCCHHHHHCC	38.65	21406692
196	Phosphorylation	WRQGTPSSQRKVRMN CCCCCCCHHHHHCCC	34.90	21406692
198	Methylation	QGTPSSQRKVRMNSY CCCCCHHHHHCCCCC	41.19	24412129
198	Dimethylation	QGTPSSQRKVRMNSY CCCCCHHHHHCCCCC	41.19	-
199	Methylation	GTPSSQRKVRMNSYP CCCCHHHHHCCCCCH	26.93	115490807
200	Methylation	TPSSQRKVRMNSYPY CCCHHHHHCCCCCHH	8.38	-
201	Methylation	PSSQRKVRMNSYPYL CCHHHHHCCCCCHHH	22.92	54558675
202	Methylation	SSQRKVRMNSYPYLA CHHHHHCCCCCHHHH	4.35	-
204	Phosphorylation	QRKVRMNSYPYLADR HHHHCCCCCHHHHHC	20.38	23401153
205	Phosphorylation	RKVRMNSYPYLADRH HHHCCCCCHHHHHCC	7.29	25159151
206	Phosphorylation	KVRMNSYPYLADRHY HHCCCCCHHHHHCCC	19.92	-
207	Phosphorylation	VRMNSYPYLADRHYS HCCCCCHHHHHCCCC	13.29	23312004
211	Methylation	SYPYLADRHYSREQR CCHHHHHCCCCCCHH	25.65	115490815
212	Methylation	YPYLADRHYSREQRY CHHHHHCCCCCCHHH	26.01	-
246	Phosphorylation	DRNHDDWSHDYDNRR CCCCCCCCCCCCCCC	17.30	20873877
260	Acetylation	RDSSRDGKWRSSRH- CCCCCCCCCCCCCC-	43.66	30591829

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
136	S	Phosphorylation	Kinase	MAPKAPK2	P49137	PSP
204	S	Phosphorylation	Kinase	MAPKAPK2	P49137	PSP

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
136	S	Phosphorylation		25189701
Phosphorylated at Ser-136 by MAPK14/p38-alpha-activated MAPKAPK2/MK2; this phosphorylation is stress-dependent; this phosphorylation decreases its RNA-binding capacity therefore affecting RNA nuclear exosome-mediated degradation.

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 RBM7_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
CC85B_HUMAN	CCDC85B	physical	16189514
RBMX_HUMAN	RBMX	physical	16189514
KHDR3_HUMAN	KHDRBS3	physical	16189514
HM20A_HUMAN	HMG20A	physical	16189514
SF3B2_HUMAN	SF3B2	physical	12634307
SRSF3_HUMAN	SRSF3	physical	12634307
SF3B2_HUMAN	SF3B2	physical	22365833
CHERP_HUMAN	CHERP	physical	22365833
SF01_HUMAN	SF1	physical	22365833
DHX8_HUMAN	DHX8	physical	22365833
RBM4_HUMAN	RBM4	physical	22365833
KHDR1_HUMAN	KHDRBS1	physical	22365833
KHDR3_HUMAN	KHDRBS3	physical	19447967
SF3B1_HUMAN	SF3B1	physical	26186194
SF3B2_HUMAN	SF3B2	physical	26186194
HTSF1_HUMAN	HTATSF1	physical	26186194
SK2L2_HUMAN	SKIV2L2	physical	26186194
NADAP_HUMAN	SLC4A1AP	physical	26186194
ZCHC8_HUMAN	ZCCHC8	physical	26186194
SF3A1_HUMAN	SF3A1	physical	26186194
SF3A3_HUMAN	SF3A3	physical	26186194
EXOS7_HUMAN	EXOSC7	physical	26186194
NCBP1_HUMAN	NCBP1	physical	26496610
EXOS9_HUMAN	EXOSC9	physical	26496610
EXOSX_HUMAN	EXOSC10	physical	26496610
M3K7_HUMAN	MAP3K7	physical	26496610
1433G_HUMAN	YWHAG	physical	26496610
1433F_HUMAN	YWHAH	physical	26496610
NCBP2_HUMAN	NCBP2	physical	26496610
KIF1B_HUMAN	KIF1B	physical	26496610
SK2L2_HUMAN	SKIV2L2	physical	26496610
EXOS3_HUMAN	EXOSC3	physical	26496610
EXOS1_HUMAN	EXOSC1	physical	26496610
SRRT_HUMAN	SRRT	physical	26496610
M18BP_HUMAN	MIS18BP1	physical	26496610
ZCHC8_HUMAN	ZCCHC8	physical	26496610
EXOS5_HUMAN	EXOSC5	physical	26496610
ELMO3_HUMAN	ELMO3	physical	26496610
UBP45_HUMAN	USP45	physical	26496610
EXOS6_HUMAN	EXOSC6	physical	26496610
ZCH18_HUMAN	ZC3H18	physical	26496610
ZCHC8_HUMAN	ZCCHC8	physical	28514442
EXOS7_HUMAN	EXOSC7	physical	28514442
NADAP_HUMAN	SLC4A1AP	physical	28514442
SK2L2_HUMAN	SKIV2L2	physical	28514442
HNRPF_HUMAN	HNRNPF	physical	28514442
HTSF1_HUMAN	HTATSF1	physical	28514442
SF3B2_HUMAN	SF3B2	physical	28514442
SF3A3_HUMAN	SF3A3	physical	28514442
SF3B1_HUMAN	SF3B1	physical	28514442

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 RBM7_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-136; SER-137 ANDSER-204, AND MASS SPECTROMETRY.	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 SER-134; SER-136 ANDSER-137, AND MASS SPECTROMETRY.	18669648 [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-136 AND SER-137, ANDMASS SPECTROMETRY.	16964243 [Abstract]
"Large-scale characterization of HeLa cell nuclear phosphoproteins."; Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J.,Li J., Cohn M.A., Cantley L.C., Gygi S.P.; Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-136, AND MASSSPECTROMETRY.	15302935 [Abstract]

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