dbPTM

RU1C_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	RU1C_HUMAN
UniProt AC	P09234
Protein Name	U1 small nuclear ribonucleoprotein C {ECO:0000255\|HAMAP-Rule:MF_03153}
Gene Name	SNRPC {ECO:0000255\|HAMAP-Rule:MF_03153}
Organism	Homo sapiens (Human).
Sequence Length	159
Subcellular Localization	Nucleus .
Protein Description	Component of the spliceosomal U1 snRNP, which is essential for recognition of the pre-mRNA 5' splice-site and the subsequent assembly of the spliceosome. SNRPC/U1-C is directly involved in initial 5' splice-site recognition for both constitutive and regulated alternative splicing. The interaction with the 5' splice-site seems to precede base-pairing between the pre-mRNA and the U1 snRNA. Stimulates commitment or early (E) complex formation by stabilizing the base pairing of the 5' end of the U1 snRNA and the 5' splice-site region..
Protein Sequence	MPKFYCDYCDTYLTHDSPSVRKTHCSGRKHKENVKDYYQKWMEEQAQSLIDKTTAAFQQGKIPPTPFSAPPPAGAMIPPPPSLPGPPRPGMMPAPHMGGPPMMPMMGPPPPGMMPVGPAPGMRPPMGGHMPMMPGPPMMRPPARPMMVPTRPGMTRPDR

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
3	Ubiquitination	-----MPKFYCDYCD -----CCCCCCCCCC	47.90	21890473
3	Acetylation	-----MPKFYCDYCD -----CCCCCCCCCC	47.90	25825284
5	Phosphorylation	---MPKFYCDYCDTY ---CCCCCCCCCCCE	7.19	21945579
8	Phosphorylation	MPKFYCDYCDTYLTH CCCCCCCCCCCEECC	6.67	21945579
9	Glutathionylation	PKFYCDYCDTYLTHD CCCCCCCCCCEECCC	1.69	22555962
11	Phosphorylation	FYCDYCDTYLTHDSP CCCCCCCCEECCCCC	19.50	21945579
12	Phosphorylation	YCDYCDTYLTHDSPS CCCCCCCEECCCCCH	9.06	21945579
14	Phosphorylation	DYCDTYLTHDSPSVR CCCCCEECCCCCHHH	17.14	21945579
17	Phosphorylation	DTYLTHDSPSVRKTH CCEECCCCCHHHHCC	16.09	22167270
19	Phosphorylation	YLTHDSPSVRKTHCS EECCCCCHHHHCCCC	38.21	21945579
35	Ubiquitination	RKHKENVKDYYQKWM CCCHHHHHHHHHHHH	52.15	-
35	Succinylation	RKHKENVKDYYQKWM CCCHHHHHHHHHHHH	52.15	23954790
35	Acetylation	RKHKENVKDYYQKWM CCCHHHHHHHHHHHH	52.15	26051181
37	Phosphorylation	HKENVKDYYQKWMEE CHHHHHHHHHHHHHH	11.32	28796482
38	Phosphorylation	KENVKDYYQKWMEEQ HHHHHHHHHHHHHHH	17.47	28796482
40	Ubiquitination	NVKDYYQKWMEEQAQ HHHHHHHHHHHHHHH	32.18	21890473
48	Phosphorylation	WMEEQAQSLIDKTTA HHHHHHHHHHHHHHH	30.24	19060867
52	2-Hydroxyisobutyrylation	QAQSLIDKTTAAFQQ HHHHHHHHHHHHHHC	40.56	-
52	Ubiquitination	QAQSLIDKTTAAFQQ HHHHHHHHHHHHHHC	40.56	2190698
52	Acetylation	QAQSLIDKTTAAFQQ HHHHHHHHHHHHHHC	40.56	19608861
53	Phosphorylation	AQSLIDKTTAAFQQG HHHHHHHHHHHHHCC	20.23	28102081
54	Phosphorylation	QSLIDKTTAAFQQGK HHHHHHHHHHHHCCC	23.02	28102081
61	Ubiquitination	TAAFQQGKIPPTPFS HHHHHCCCCCCCCCC	47.94	21890473
88	Dimethylation	PSLPGPPRPGMMPAP CCCCCCCCCCCCCCC	43.46	-
88	Methylation	PSLPGPPRPGMMPAP CCCCCCCCCCCCCCC	43.46	52718127

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 RU1C_HUMAN !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of RU1C_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 RU1C_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
EWS_HUMAN	EWSR1	physical	10827180
RUXE_HUMAN	SNRPE	physical	22939629
SRRM2_HUMAN	SRRM2	physical	22939629
RU2A_HUMAN	SNRPA1	physical	22939629
SRPRB_HUMAN	SRPRB	physical	22939629
SLIRP_HUMAN	SLIRP	physical	22939629
WAP53_HUMAN	WRAP53	physical	22939629
STOM_HUMAN	STOM	physical	22939629
SARNP_HUMAN	SARNP	physical	22939629
THY1_HUMAN	THY1	physical	22939629
TOM40_HUMAN	TOMM40	physical	22939629
RBM10_HUMAN	RBM10	physical	22365833
ILF3_HUMAN	ILF3	physical	22365833
WDR83_HUMAN	WDR83	physical	22365833
DDX42_HUMAN	DDX42	physical	22365833
HNRL1_HUMAN	HNRNPUL1	physical	22365833
AGGF1_HUMAN	AGGF1	physical	22365833
RBM4_HUMAN	RBM4	physical	22365833
MEP50_HUMAN	WDR77	physical	22365833
HNRPD_HUMAN	HNRNPD	physical	22365833
HNRPF_HUMAN	HNRNPF	physical	22365833
HNRH2_HUMAN	HNRNPH2	physical	22365833
KHDR3_HUMAN	KHDRBS3	physical	22365833
RFOX2_HUMAN	RBFOX2	physical	22365833
MAGD1_HUMAN	MAGED1	physical	25416956
RBPMS_HUMAN	RBPMS	physical	25416956
WWP2_HUMAN	WWP2	physical	25416956
EXOS8_HUMAN	EXOSC8	physical	25416956
F168A_HUMAN	FAM168A	physical	25416956
CREST_HUMAN	SS18L1	physical	25416956
SPAG8_HUMAN	SPAG8	physical	25416956
CNDH2_HUMAN	NCAPH2	physical	25416956
DHB14_HUMAN	HSD17B14	physical	25416956
RBM11_HUMAN	RBM11	physical	25416956
RNF31_HUMAN	RNF31	physical	25416956
RFX6_HUMAN	RFX6	physical	25416956
CARM1_HUMAN	CARM1	physical	26344197
SF3A3_HUMAN	SF3A3	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 RU1C_HUMAN

Related Literatures of Post-Translational Modification

Acetylation
Reference	PubMed
"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-52, AND MASS SPECTROMETRY.	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-17, AND MASSSPECTROMETRY.	18669648 [Abstract]
"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-8 AND TYR-12, AND MASSSPECTROMETRY.	15592455 [Abstract]