dbPTM

RSMB_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	RSMB_HUMAN
UniProt AC	P14678
Protein Name	Small nuclear ribonucleoprotein-associated proteins B and B'
Gene Name	SNRPB
Organism	Homo sapiens (Human).
Sequence Length	240
Subcellular Localization	Cytoplasm, cytosol . Nucleus . SMN-mediated assembly into core snRNPs occurs in the cytosol before SMN-mediated transport to the nucleus to be included in spliceosomes.
Protein Description	Core component of the spliceosomal U1, U2, U4 and U5 small nuclear ribonucleoproteins (snRNPs), the building blocks of the spliceosome. Thereby, plays an important role in the splicing of cellular pre-mRNAs. Most spliceosomal snRNPs contain a common set of Sm proteins SNRPB, SNRPD1, SNRPD2, SNRPD3, SNRPE, SNRPF and SNRPG that assemble in a heptameric protein ring on the Sm site of the small nuclear RNA to form the core snRNP. As part of the U7 snRNP it is involved in histone 3'-end processing..
Protein Sequence	MTVGKSSKMLQHIDYRMRCILQDGRIFIGTFKAFDKHMNLILCDCDEFRKIKPKNSKQAEREEKRVLGLVLLRGENLVSMTVEGPPPKDTGIARVPLAGAAGGPGIGRAAGRGIPAGVPMPQAPAGLAGPVRGVGGPSQQVMTPQGRGTVAAAAAAATASIAGAPTQYPPGRGGPPPPMGRGAPPPGMMGPPPGMRPPMGPPMGIPPGRGTPMGMPPPGMRPPPPGMRGPPPPGMRPPRP

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Phosphorylation	------MTVGKSSKM ------CCCCCHHHH	37.66	20068231
5	Ubiquitination	---MTVGKSSKMLQH ---CCCCCHHHHHHH	47.41	-
5 (in isoform 3)	Ubiquitination	-	47.41	21890473
5 (in isoform 1)	Ubiquitination	-	47.41	21890473
5 (in isoform 2)	Ubiquitination	-	47.41	21890473
6	Phosphorylation	--MTVGKSSKMLQHI --CCCCCHHHHHHHH	29.30	20068231
7	Phosphorylation	-MTVGKSSKMLQHID -CCCCCHHHHHHHHC	26.10	29116813
8 (in isoform 3)	Ubiquitination	-	51.20	21890473
8	Malonylation	MTVGKSSKMLQHIDY CCCCCHHHHHHHHCH	51.20	26320211
8	Acetylation	MTVGKSSKMLQHIDY CCCCCHHHHHHHHCH	51.20	19608861
8 (in isoform 2)	Ubiquitination	-	51.20	21890473
8	Ubiquitination	MTVGKSSKMLQHIDY CCCCCHHHHHHHHCH	51.20	19608861
8 (in isoform 1)	Ubiquitination	-	51.20	21890473
15	Phosphorylation	KMLQHIDYRMRCILQ HHHHHHCHHHHHEEC	13.00	29116813
16	Methylation	MLQHIDYRMRCILQD HHHHHCHHHHHEECC	11.43	-
30	Phosphorylation	DGRIFIGTFKAFDKH CCCEEEEECHHHHHC	19.69	23186163
32 (in isoform 1)	Ubiquitination	-	48.24	21890473
32 (in isoform 2)	Ubiquitination	-	48.24	21890473
32	Ubiquitination	RIFIGTFKAFDKHMN CEEEEECHHHHHCCC	48.24	21890473
32 (in isoform 3)	Ubiquitination	-	48.24	21890473
32	Acetylation	RIFIGTFKAFDKHMN CEEEEECHHHHHCCC	48.24	23954790
36	Ubiquitination	GTFKAFDKHMNLILC EECHHHHHCCCEEEE	38.00	-
36 (in isoform 3)	Ubiquitination	-	38.00	-
36	Acetylation	GTFKAFDKHMNLILC EECHHHHHCCCEEEE	38.00	21466224
57	Ubiquitination	KIKPKNSKQAEREEK CCCCCCCHHHHHHHH	64.02	-
80	Sulfoxidation	RGENLVSMTVEGPPP CCCCEEEEEEECCCC	3.66	21406390
88 (in isoform 1)	Ubiquitination	-	73.94	21890473
88	Acetylation	TVEGPPPKDTGIARV EEECCCCCCCCEEEC	73.94	26051181
88 (in isoform 3)	Ubiquitination	-	73.94	21890473
88 (in isoform 2)	Ubiquitination	-	73.94	21890473
88	Ubiquitination	TVEGPPPKDTGIARV EEECCCCCCCCEEEC	73.94	21890473
94	Methylation	PKDTGIARVPLAGAA CCCCCEEECCCCCCC	28.76	115917385
108	Asymmetric dimethylarginine	AGGPGIGRAAGRGIP CCCCCHHHHCCCCCC	21.24	-
108	Methylation	AGGPGIGRAAGRGIP CCCCCHHHHCCCCCC	21.24	24129315
112	Asymmetric dimethylarginine	GIGRAAGRGIPAGVP CHHHHCCCCCCCCCC	34.83	-
112	Methylation	GIGRAAGRGIPAGVP CHHHHCCCCCCCCCC	34.83	24129315
132	Methylation	AGLAGPVRGVGGPSQ CCCCCCCCCCCCCCC	36.89	81453667
147	Dimethylation	QVMTPQGRGTVAAAA CCCCCCCHHHHHHHH	32.15	-
147	Methylation	QVMTPQGRGTVAAAA CCCCCCCHHHHHHHH	32.15	18600617
166	Phosphorylation	ASIAGAPTQYPPGRG HHHCCCCCCCCCCCC	39.95	24260401
172	Dimethylation	PTQYPPGRGGPPPPM CCCCCCCCCCCCCCC	53.31	-
172	Methylation	PTQYPPGRGGPPPPM CCCCCCCCCCCCCCC	53.31	30761091
181	Dimethylation	GPPPPMGRGAPPPGM CCCCCCCCCCCCCCC	31.67	-
181	Methylation	GPPPPMGRGAPPPGM CCCCCCCCCCCCCCC	31.67	54559501
209	Dimethylation	PMGIPPGRGTPMGMP CCCCCCCCCCCCCCC	52.14	-
209	Methylation	PMGIPPGRGTPMGMP CCCCCCCCCCCCCCC	52.14	137949
221 (in isoform 2)	Dimethylation	-	46.63	-
221	Methylation	GMPPPGMRPPPPGMR CCCCCCCCCCCCCCC	46.63	54851351
228 (in isoform 2)	Dimethylation	-	61.45	-
228	Methylation	RPPPPGMRGPPPPGM CCCCCCCCCCCCCCC	61.45	97770621
236	Dimethylation	GPPPPGMRPPRP--- CCCCCCCCCCCC---	43.94	-
236	Methylation	GPPPPGMRPPRP--- CCCCCCCCCCCC---	43.94	-
239	Methylation	PPGMRPPRP------ CCCCCCCCC------	52.85	-
250 (in isoform 3)	Phosphorylation	-		-

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 RSMB_HUMAN !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification
108	R	Methylation
Arg-108 and Arg-112 are dimethylated, probably to asymmetric dimethylarginine.10).
112	R	Methylation
Arg-108 and Arg-112 are dimethylated, probably to asymmetric dimethylarginine.10).

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 RSMB_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
PRP8_HUMAN	PRPF8	physical	17353931
U520_HUMAN	SNRNP200	physical	17353931
KHK_HUMAN	KHK	physical	17353931
DYHC1_HUMAN	DYNC1H1	physical	17353931
SART3_HUMAN	SART3	physical	17353931
GEMI4_HUMAN	GEMIN4	physical	17353931
U5S1_HUMAN	EFTUD2	physical	17353931
HTSF1_HUMAN	HTATSF1	physical	17353931
ERG28_HUMAN	C14orf1	physical	16169070
PSA3_HUMAN	PSMA3	physical	16169070
COIL_HUMAN	COIL	physical	11641277
HCFC1_HUMAN	HCFC1	physical	12456665
SMD3_HUMAN	SNRPD3	physical	22939629
RUXE_HUMAN	SNRPE	physical	22939629
U520_HUMAN	SNRNP200	physical	22939629
SMD1_HUMAN	SNRPD1	physical	22939629
SMD2_HUMAN	SNRPD2	physical	22939629
RU1C_HUMAN	SNRPC	physical	22939629
RENT1_HUMAN	UPF1	physical	18362360
DSRAD_HUMAN	ADAR	physical	18362360
SMD3_HUMAN	SNRPD3	physical	22365833
LSM2_HUMAN	LSM2	physical	22365833
LSM8_HUMAN	LSM8	physical	22365833
ICLN_HUMAN	CLNS1A	physical	22365833
CD2B2_HUMAN	CD2BP2	physical	15105431
IL7RA_HUMAN	IL7R	physical	23151878
SF3A3_HUMAN	SF3A3	physical	22863883
PNMA1_HUMAN	PNMA1	physical	25416956
CACO2_HUMAN	CALCOCO2	physical	25416956
CD2B2_HUMAN	CD2BP2	physical	25416956
RBPMS_HUMAN	RBPMS	physical	25416956
TFP11_HUMAN	TFIP11	physical	25416956
CREST_HUMAN	SS18L1	physical	25416956
BANP_HUMAN	BANP	physical	25416956
CEP55_HUMAN	CEP55	physical	25416956
LMBL3_HUMAN	L3MBTL3	physical	25416956
K1C40_HUMAN	KRT40	physical	25416956
RFX6_HUMAN	RFX6	physical	25416956

Drug and Disease Associations

Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
117650	Cerebrocostomandibular syndrome (CCMS)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.

Regulatory Network of RSMB_HUMAN

Related Literatures of Post-Translational Modification

Methylation
Reference	PubMed
"Identifying and quantifying in vivo methylation sites by heavy methylSILAC."; Ong S.E., Mittler G., Mann M.; Nat. Methods 1:119-126(2004). Cited for: METHYLATION [LARGE SCALE ANALYSIS] AT ARG-108 AND ARG-112, AND MASSSPECTROMETRY.	15782174 [Abstract]

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