dbPTM

RPR1B_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	RPR1B_HUMAN
UniProt AC	Q9NQG5
Protein Name	Regulation of nuclear pre-mRNA domain-containing protein 1B
Gene Name	RPRD1B
Organism	Homo sapiens (Human).
Sequence Length	326
Subcellular Localization	Nucleus .
Protein Description	Interacts with phosphorylated C-terminal heptapeptide repeat domain (CTD) of the largest RNA polymerase II subunit POLR2A, and participates in dephosphorylation of the CTD by RPAP2. Transcriptional regulator which enhances expression of CCND1. Promotes binding of RNA polymerase II to the CCDN1 promoter and to the termination region before the poly-A site but decreases its binding after the poly-A site. Prevents RNA polymerase II from reading through the 3' end termination site and may allow it to be recruited back to the promoter through promotion of the formation of a chromatin loop. Also enhances the transcription of a number of other cell cycle-related genes including CDK2, CDK4, CDK6 and cyclin-E but not CDKN1A, CDKN1B or cyclin-A. Promotes cell proliferation..
Protein Sequence	MSSFSESALEKKLSELSNSQQSVQTLSLWLIHHRKHAGPIVSVWHRELRKAKSNRKLTFLYLANDVIQNSKRKGPEFTREFESVLVDAFSHVAREADEGCKKPLERLLNIWQERSVYGGEFIQQLKLSMEDSKSPPPKATEEKKSLKRTFQQIQEEEDDDYPGSYSPQDPSAGPLLTEELIKALQDLENAASGDATVRQKIASLPQEVQDVSLLEKITDKEAAERLSKTVDEACLLLAEYNGRLAAELEDRRQLARMLVEYTQNQKDVLSEKEKKLEEYKQKLARVTQVRKELKSHIQSLPDLSLLPNVTGGLAPLPSAGDLFSTD

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Acetylation	------MSSFSESAL ------CCCCCHHHH	39.84	22223895
2	Phosphorylation	------MSSFSESAL ------CCCCCHHHH	39.84	23186163
3	Phosphorylation	-----MSSFSESALE -----CCCCCHHHHH	31.34	25159151
7	Phosphorylation	-MSSFSESALEKKLS -CCCCCHHHHHHHHH	36.63	21964256
11	2-Hydroxyisobutyrylation	FSESALEKKLSELSN CCHHHHHHHHHHHCC	60.92	-
11	Acetylation	FSESALEKKLSELSN CCHHHHHHHHHHHCC	60.92	25953088
11	Ubiquitination	FSESALEKKLSELSN CCHHHHHHHHHHHCC	60.92	-
12	Ubiquitination	SESALEKKLSELSNS CHHHHHHHHHHHCCC	48.12	-
12	Sumoylation	SESALEKKLSELSNS CHHHHHHHHHHHCCC	48.12	-
12	Sumoylation	SESALEKKLSELSNS CHHHHHHHHHHHCCC	48.12	-
17	Phosphorylation	EKKLSELSNSQQSVQ HHHHHHHCCCHHHHH	30.31	-
27	Phosphorylation	QQSVQTLSLWLIHHR HHHHHHHHHHHHHCH	22.38	-
35	Malonylation	LWLIHHRKHAGPIVS HHHHHCHHCCCCCHH	33.19	32601280
56	Ubiquitination	RKAKSNRKLTFLYLA HHHHHCCCCEEHHHH	57.01	-
67	Ubiquitination	LYLANDVIQNSKRKG HHHHHHHHHHCHHCC	3.42	24816145
71	Ubiquitination	NDVIQNSKRKGPEFT HHHHHHCHHCCCHHH	66.72	-
92	Ubiquitination	LVDAFSHVAREADEG HHHHHHHHHHHCCCC	5.35	24816145
101	Ubiquitination	READEGCKKPLERLL HHCCCCCCHHHHHHH	69.18	24816145
117	Phosphorylation	IWQERSVYGGEFIQQ HHHHCCCCCHHHHHH	22.21	28152594
128	Phosphorylation	FIQQLKLSMEDSKSP HHHHHCCCCCCCCCC	20.66	23927012
132	Phosphorylation	LKLSMEDSKSPPPKA HCCCCCCCCCCCCCC	23.02	29255136
134	Phosphorylation	LSMEDSKSPPPKATE CCCCCCCCCCCCCHH	46.74	29255136
140	Phosphorylation	KSPPPKATEEKKSLK CCCCCCCHHHHHHHH	51.29	23927012
145	Phosphorylation	KATEEKKSLKRTFQQ CCHHHHHHHHHHHHH	50.63	-
149	Phosphorylation	EKKSLKRTFQQIQEE HHHHHHHHHHHHHHH	24.98	28176443
161	Phosphorylation	QEEEDDDYPGSYSPQ HHHCCCCCCCCCCCC	19.25	28176443
164	Phosphorylation	EDDDYPGSYSPQDPS CCCCCCCCCCCCCCC	20.24	25159151
165	Phosphorylation	DDDYPGSYSPQDPSA CCCCCCCCCCCCCCC	30.22	28176443
166	Phosphorylation	DDYPGSYSPQDPSAG CCCCCCCCCCCCCCC	20.13	25159151
171	Phosphorylation	SYSPQDPSAGPLLTE CCCCCCCCCCCCCHH	54.90	28176443
177	Phosphorylation	PSAGPLLTEELIKAL CCCCCCCHHHHHHHH	34.79	28176443
200	Ubiquitination	GDATVRQKIASLPQE CCHHHHHHHHCCCHH	29.67	24816145
212	Phosphorylation	PQEVQDVSLLEKITD CHHHHHHHHHHHCCC	35.21	25159151
216	Ubiquitination	QDVSLLEKITDKEAA HHHHHHHHCCCHHHH	51.37	32015554
251	Methylation	LAAELEDRRQLARML HHHHHHHHHHHHHHH	20.90	115492387
257	Sulfoxidation	DRRQLARMLVEYTQN HHHHHHHHHHHHHHH	4.01	28183972
262	Phosphorylation	ARMLVEYTQNQKDVL HHHHHHHHHHHHHHC	13.92	23401153
272	Ubiquitination	QKDVLSEKEKKLEEY HHHHCCHHHHHHHHH	72.03	33845483
272	2-Hydroxyisobutyrylation	QKDVLSEKEKKLEEY HHHHCCHHHHHHHHH	72.03	-
294	Ubiquitination	TQVRKELKSHIQSLP HHHHHHHHHHHHHCC	40.87	33845483
299	Phosphorylation	ELKSHIQSLPDLSLL HHHHHHHHCCCHHCC	41.07	28348404
325	Phosphorylation	SAGDLFSTD------ CHHHCCCCC------	38.09	25627689

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
145	S	Phosphorylation	Kinase	AURB	Q96GD4	PSP
166	S	Phosphorylation	Kinase	MTOR	P42345	PSP

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of RPR1B_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 RPR1B_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
AASD1_HUMAN	AARSD1	physical	22863883
ARPC4_HUMAN	ARPC4	physical	22863883
BAG1_HUMAN	BAG1	physical	22863883
FUBP1_HUMAN	FUBP1	physical	22863883
GRPE1_HUMAN	GRPEL1	physical	22863883
LPP_HUMAN	LPP	physical	22863883
NIF3L_HUMAN	NIF3L1	physical	22863883
NPL4_HUMAN	NPLOC4	physical	22863883
OGT1_HUMAN	OGT	physical	22863883
OSGEP_HUMAN	OSGEP	physical	22863883
PFD5_HUMAN	PFDN5	physical	22863883
MYPT1_HUMAN	PPP1R12A	physical	22863883
RAGP1_HUMAN	RANGAP1	physical	22863883
RFA1_HUMAN	RPA1	physical	22863883
SAE1_HUMAN	SAE1	physical	22863883
STA5B_HUMAN	STAT5B	physical	22863883
PRPK_HUMAN	TP53RK	physical	22863883
TTL12_HUMAN	TTLL12	physical	22863883
RPAB1_HUMAN	POLR2E	physical	26186194
RPB7_HUMAN	POLR2G	physical	26186194
CTDP1_HUMAN	CTDP1	physical	26186194
RPAP2_HUMAN	RPAP2	physical	26186194
RPB1_HUMAN	POLR2A	physical	26186194
MYZAP_HUMAN	POLR2M	physical	26186194
GRL1A_HUMAN	POLR2M	physical	26186194
GL1AD_HUMAN	POLR2M	physical	26186194
RPR1A_HUMAN	RPRD1A	physical	26186194
RPB4_HUMAN	POLR2D	physical	26186194
RPRD2_HUMAN	RPRD2	physical	26186194
RECQ5_HUMAN	RECQL5	physical	26186194
RPB2_HUMAN	POLR2B	physical	26186194
RPB11_HUMAN	POLR2J	physical	26186194
SPT6H_HUMAN	SUPT6H	physical	26186194
RPB9_HUMAN	POLR2I	physical	26186194
RPB3_HUMAN	POLR2C	physical	26186194
GPN3_HUMAN	GPN3	physical	26186194
RPAB5_HUMAN	POLR2L	physical	26186194
RPAB2_HUMAN	POLR2F	physical	26186194
VATB2_HUMAN	ATP6V1B2	physical	26344197
IMB1_HUMAN	KPNB1	physical	26344197
SPEE_HUMAN	SRM	physical	26344197
RPR1A_HUMAN	RPRD1A	physical	28514442
MYZAP_HUMAN	POLR2M	physical	28514442
GRL1A_HUMAN	POLR2M	physical	28514442
GL1AD_HUMAN	POLR2M	physical	28514442
RPRD2_HUMAN	RPRD2	physical	28514442
RPB7_HUMAN	POLR2G	physical	28514442
CTDP1_HUMAN	CTDP1	physical	28514442
RECQ5_HUMAN	RECQL5	physical	28514442
RPAP2_HUMAN	RPAP2	physical	28514442
RPB11_HUMAN	POLR2J	physical	28514442
RPB1_HUMAN	POLR2A	physical	28514442
RPB9_HUMAN	POLR2I	physical	28514442
GPN3_HUMAN	GPN3	physical	28514442
RPAB5_HUMAN	POLR2L	physical	28514442
SPT6H_HUMAN	SUPT6H	physical	28514442
RPAB1_HUMAN	POLR2E	physical	28514442
RPB2_HUMAN	POLR2B	physical	28514442
RPB3_HUMAN	POLR2C	physical	28514442
GPN1_HUMAN	GPN1	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 RPR1B_HUMAN

Related Literatures of Post-Translational Modification

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-166, AND MASSSPECTROMETRY.	18669648 [Abstract]
"Global proteomic profiling of phosphopeptides using electron transferdissociation tandem mass spectrometry."; Molina H., Horn D.M., Tang N., Mathivanan S., Pandey A.; Proc. Natl. Acad. Sci. U.S.A. 104:2199-2204(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-134, AND MASSSPECTROMETRY.	17287340 [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-166, AND MASSSPECTROMETRY.	15302935 [Abstract]