dbPTM

RU2B_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	RU2B_HUMAN
UniProt AC	P08579
Protein Name	U2 small nuclear ribonucleoprotein B''
Gene Name	SNRPB2
Organism	Homo sapiens (Human).
Sequence Length	225
Subcellular Localization	Nucleus .
Protein Description	Involved in pre-mRNA splicing as component of the spliceosome. [PubMed: 11991638]
Protein Sequence	MDIRPNHTIYINNMNDKIKKEELKRSLYALFSQFGHVVDIVALKTMKMRGQAFVIFKELGSSTNALRQLQGFPFYGKPMRIQYAKTDSDIISKMRGTFADKEKKKEKKKAKTVEQTATTTNKKPGQGTPNSANTQGNSTPNPQVPDYPPNYILFLNNLPEETNEMMLSMLFNQFPGFKEVRLVPGRHDIAFVEFENDGQAGAARDALQGFKITPSHAMKITYAKK

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
17	Ubiquitination	YINNMNDKIKKEELK EECCCCHHHCHHHHH	51.96	-
20	Ubiquitination	NMNDKIKKEELKRSL CCCHHHCHHHHHHHH	60.95	24816145
57	Acetylation	GQAFVIFKELGSSTN CCEEEEEECCCCCHH	40.69	26051181
57	Ubiquitination	GQAFVIFKELGSSTN CCEEEEEECCCCCHH	40.69	23000965
77	Ubiquitination	QGFPFYGKPMRIQYA CCCCCCCCCCEEEEE	25.02	23000965
85	Acetylation	PMRIQYAKTDSDIIS CCEEEEEECCHHHHH	48.18	25953088
85	Ubiquitination	PMRIQYAKTDSDIIS CCEEEEEECCHHHHH	48.18	21906983
86	O-linked_Glycosylation	MRIQYAKTDSDIISK CEEEEEECCHHHHHH	32.34	29351928
93	Ubiquitination	TDSDIISKMRGTFAD CCHHHHHHHHCCCCC	23.39	27667366
93	Acetylation	TDSDIISKMRGTFAD CCHHHHHHHHCCCCC	23.39	25953088
101	Acetylation	MRGTFADKEKKKEKK HHCCCCCHHHHHHHH	68.92	26051181
111	Ubiquitination	KKEKKKAKTVEQTAT HHHHHHCCCCEECCC	63.08	33845483
111	Sumoylation	KKEKKKAKTVEQTAT HHHHHHCCCCEECCC	63.08	28112733
111	Acetylation	KKEKKKAKTVEQTAT HHHHHHCCCCEECCC	63.08	-
112	Phosphorylation	KEKKKAKTVEQTATT HHHHHCCCCEECCCC	33.85	23312004
116	Phosphorylation	KAKTVEQTATTTNKK HCCCCEECCCCCCCC	16.68	28102081
118	Phosphorylation	KTVEQTATTTNKKPG CCCEECCCCCCCCCC	37.22	28102081
119	Phosphorylation	TVEQTATTTNKKPGQ CCEECCCCCCCCCCC	26.38	28102081
120	Phosphorylation	VEQTATTTNKKPGQG CEECCCCCCCCCCCC	40.46	28102081
122	Ubiquitination	QTATTTNKKPGQGTP ECCCCCCCCCCCCCC	59.25	27667366
128	Phosphorylation	NKKPGQGTPNSANTQ CCCCCCCCCCCCCCC	16.06	-
151	Phosphorylation	VPDYPPNYILFLNNL CCCCCCCEEEEECCC	12.55	28112733
211	Ubiquitination	RDALQGFKITPSHAM HHHHCCCCCCHHHCC	53.12	32015554
211	Acetylation	RDALQGFKITPSHAM HHHHCCCCCCHHHCC	53.12	25953088
213	Phosphorylation	ALQGFKITPSHAMKI HHCCCCCCHHHCCEE	21.23	20068231
215	Phosphorylation	QGFKITPSHAMKITY CCCCCCHHHCCEEEE	18.41	23186163
219	Ubiquitination	ITPSHAMKITYAKK- CCHHHCCEEEEECC-	32.45	23000965
219	Malonylation	ITPSHAMKITYAKK- CCHHHCCEEEEECC-	32.45	26320211
219	Acetylation	ITPSHAMKITYAKK- CCHHHCCEEEEECC-	32.45	25953088
221	Phosphorylation	PSHAMKITYAKK--- HHHCCEEEEECC---	16.35	29083192
222	Phosphorylation	SHAMKITYAKK---- HHCCEEEEECC----	21.64	29083192
224	Ubiquitination	AMKITYAKK------ CCEEEEECC------	48.91	23000965
225	Ubiquitination	MKITYAKK------- CEEEEECC-------	58.35	23000965

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 RU2B_HUMAN !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of RU2B_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 RU2B_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
RU2A_HUMAN	SNRPA1	physical	9716128
SF3A1_HUMAN	SF3A1	physical	22939629
SF3B1_HUMAN	SF3B1	physical	22939629
SF3B3_HUMAN	SF3B3	physical	22939629
SF3B2_HUMAN	SF3B2	physical	22939629
SF3B4_HUMAN	SF3B4	physical	22939629
SF3A3_HUMAN	SF3A3	physical	22939629
U520_HUMAN	SNRNP200	physical	22939629
SRRM2_HUMAN	SRRM2	physical	22939629
WBP11_HUMAN	WBP11	physical	22939629
SKP2_HUMAN	SKP2	physical	22939629
RU2A_HUMAN	SNRPA1	physical	22365833
SUGP1_HUMAN	SUGP1	physical	22365833
HNRL1_HUMAN	HNRNPUL1	physical	22365833
ZBT14_HUMAN	ZBTB14	physical	25416956
PNMA1_HUMAN	PNMA1	physical	25416956
MTUS2_HUMAN	MTUS2	physical	25416956
HOMEZ_HUMAN	HOMEZ	physical	25416956
HMBX1_HUMAN	HMBOX1	physical	25416956
SF3A3_HUMAN	SF3A3	physical	26344197
SF3B1_HUMAN	SF3B1	physical	26344197
LA_HUMAN	SSB	physical	26344197
PA2G4_HUMAN	PA2G4	physical	27173435
TRAP1_HUMAN	TRAP1	physical	27173435
SND1_HUMAN	SND1	physical	27173435
SF3A1_HUMAN	SF3A1	physical	27173435
ANXA5_HUMAN	ANXA5	physical	27173435
IF2P_HUMAN	EIF5B	physical	27173435
G6PI_HUMAN	GPI	physical	27173435
IDHP_HUMAN	IDH2	physical	27173435
PDIA3_HUMAN	PDIA3	physical	27173435
UBE2N_HUMAN	UBE2N	physical	27173435
RM12_HUMAN	MRPL12	physical	27173435
CRNN_HUMAN	CRNN	physical	27173435
ZN207_HUMAN	ZNF207	physical	27173435
CPNE3_HUMAN	CPNE3	physical	27173435
CISY_HUMAN	CS	physical	27173435
PYGL_HUMAN	PYGL	physical	27173435
SF3A3_HUMAN	SF3A3	physical	27173435
DNJC8_HUMAN	DNAJC8	physical	27173435
PLST_HUMAN	PLS3	physical	27173435
CPSF6_HUMAN	CPSF6	physical	27173435

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 RU2B_HUMAN

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"Immunoaffinity profiling of tyrosine phosphorylation in cancercells."; Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,Zha X.-M., Polakiewicz R.D., Comb M.J.; Nat. Biotechnol. 23:94-101(2005). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-151, AND MASSSPECTROMETRY.	15592455 [Abstract]