dbPTM

RNF4_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	RNF4_HUMAN
UniProt AC	P78317
Protein Name	E3 ubiquitin-protein ligase RNF4
Gene Name	RNF4
Organism	Homo sapiens (Human).
Sequence Length	190
Subcellular Localization	Cytoplasm. Nucleus. Nucleus, PML body. Nucleus, nucleoplasm.
Protein Description	E3 ubiquitin-protein ligase which binds polysumoylated chains covalently attached to proteins and mediates 'Lys-6'-, 'Lys-11'-, 'Lys-48'- and 'Lys-63'-linked polyubiquitination of those substrates and their subsequent targeting to the proteasome for degradation. Regulates the degradation of several proteins including PML and the transcriptional activator PEA3. Involved in chromosome alignment and spindle assembly, it regulates the kinetochore CENPH-CENPI-CENPK complex by targeting polysumoylated CENPI to proteasomal degradation. Regulates the cellular responses to hypoxia and heat shock through degradation of respectively EPAS1 and PARP1. Alternatively, it may also bind DNA/nucleosomes and have a more direct role in the regulation of transcription for instance enhancing basal transcription and steroid receptor-mediated transcriptional activation..
Protein Sequence	MSTRKRRGGAINSRQAQKRTREATSTPEISLEAEPIELVETAGDEIVDLTCESLEPVVVDLTHNDSVVIVDERRRPRRNARRLPQDHADSCVVSSDDEELSRDRDVYVTTHTPRNARDEGATGLRPSGTVSCPICMDGYSEIVQNGRLIVSTECGHVFCSQCLRDSLKNANTCPTCRKKINHKRYHPIYI

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
7	Methylation	-MSTRKRRGGAINSR -CCCCCCCCCCCCHH	51.43	115386031
26	Phosphorylation	RTREATSTPEISLEA HHHHCCCCCCCCEEE	22.15	-
90	Phosphorylation	LPQDHADSCVVSSDD CCCCCCCCCEECCCH	15.03	23927012
94	Phosphorylation	HADSCVVSSDDEELS CCCCCEECCCHHHHH	13.98	29255136
95	Phosphorylation	ADSCVVSSDDEELSR CCCCEECCCHHHHHC	37.15	29255136
101	Phosphorylation	SSDDEELSRDRDVYV CCCHHHHHCCCCEEE	35.10	23401153
107	Phosphorylation	LSRDRDVYVTTHTPR HHCCCCEEEECCCCC	9.07	28796482
109	Phosphorylation	RDRDVYVTTHTPRNA CCCCEEEECCCCCCC	8.65	28796482
110	Phosphorylation	DRDVYVTTHTPRNAR CCCEEEECCCCCCCC	17.44	28796482
112	Phosphorylation	DVYVTTHTPRNARDE CEEEECCCCCCCCCC	23.11	28796482
129	Phosphorylation	TGLRPSGTVSCPICM CCCCCCCEEECCEEC	17.37	22468782
131	Phosphorylation	LRPSGTVSCPICMDG CCCCCEEECCEECCC	17.64	22210691
152	Phosphorylation	NGRLIVSTECGHVFC CCEEEEEECCCCEEH	25.13	22210691
160	Phosphorylation	ECGHVFCSQCLRDSL CCCCEEHHHHHHHHH	16.68	27251275
166	Phosphorylation	CSQCLRDSLKNANTC HHHHHHHHHHHCCCC	34.51	27251275
168	Ubiquitination	QCLRDSLKNANTCPT HHHHHHHHHCCCCCC	58.95	23000965
189	Phosphorylation	HKRYHPIYI------ CCCCCCCCC------	12.67	-

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
26	T	Phosphorylation	Kinase	CDK2	P24941	PSP
112	T	Phosphorylation	Kinase	CDK2	P24941	PSP
-	K	Ubiquitination	E3 ubiquitin ligase	RNF4	P78317	PMID:14987998

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of RNF4_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 RNF4_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
PATZ1_HUMAN	PATZ1	physical	10713105
ESR1_HUMAN	ESR1	physical	9710597
PRGR_HUMAN	PGR	physical	9710597
ANDR_HUMAN	AR	physical	9710597
TBP_HUMAN	TBP	physical	9710597
PATZ1_HUMAN	PATZ1	physical	11719514
ANDR_HUMAN	AR	physical	11719514
SP1_HUMAN	SP1	physical	10617653
ANDR_HUMAN	AR	physical	10617653
NEMO_HUMAN	IKBKG	physical	20211142
RNF4_HUMAN	RNF4	physical	21857666
UB2D1_HUMAN	UBE2D1	physical	21857666
SUMO2_HUMAN	SUMO2	physical	20943951
SP1_HUMAN	SP1	physical	21983342
SUMO2_HUMAN	SUMO2	physical	21252943
TIF1B_HUMAN	TRIM28	physical	21252943
PML_HUMAN	PML	physical	21252943
SNUT1_HUMAN	SART1	physical	21252943
UHRF1_HUMAN	UHRF1	physical	21252943
MDC1_HUMAN	MDC1	physical	22661230
RFA1_HUMAN	RPA1	physical	22661229
RNF4_HUMAN	RNF4	physical	15707587
PML_HUMAN	PML	physical	15707587
TDG_HUMAN	TDG	physical	20696907
APEX1_HUMAN	APEX1	physical	20696907
SUMO2_HUMAN	SUMO2	physical	18408734
PML_HUMAN	PML	physical	18408734
TRPS1_HUMAN	TRPS1	physical	12885770
PML_HUMAN	PML	physical	23028697
UB2D1_HUMAN	UBE2D1	physical	18408734
SUMO2_HUMAN	SUMO2	physical	23086935
SUMO1_HUMAN	SUMO1	physical	23086935
NF2L2_HUMAN	NFE2L2	physical	23543742
SUMO2_HUMAN	SUMO2	physical	23560854
UB2D1_HUMAN	UBE2D1	physical	23560854
UB2D2_HUMAN	UBE2D2	physical	23560854
UB2D3_HUMAN	UBE2D3	physical	23560854
UB2D4_HUMAN	UBE2D4	physical	23560854
UBE2W_HUMAN	UBE2W	physical	23560854
RTA_EBVB9	BRLF1	physical	23504328
UB2D1_HUMAN	UBE2D1	physical	23504328
SUMO2_HUMAN	SUMO2	physical	23530056
UB2D2_HUMAN	UBE2D2	physical	23530056
UB2D3_HUMAN	UBE2D3	physical	23530056
TRAIP_HUMAN	TRAIP	physical	22493164
HNF4A_HUMAN	HNF4A	physical	22505616
SUMO1_HUMAN	SUMO1	physical	24151981
SUMO2_HUMAN	SUMO2	physical	24151981
PML_HUMAN	PML	physical	22388745
UBC_HUMAN	UBC	physical	24714598
UB2D1_HUMAN	UBE2D1	physical	24714598
H32_HUMAN	HIST2H3C	physical	24714598
RNF4_HUMAN	RNF4	physical	24656128
UB2D1_HUMAN	UBE2D1	physical	24656128
SUMO2_HUMAN	SUMO2	physical	24844634
SUMO1_HUMAN	SUMO1	physical	24844634
ATX1_HUMAN	ATXN1	physical	24882209
TADBP_HUMAN	TARDBP	physical	24882209
RNF4_HUMAN	RNF4	physical	24882209
UB2D1_HUMAN	UBE2D1	physical	24882209
SUMO2_HUMAN	SUMO2	physical	24969970
TIF1B_HUMAN	TRIM28	physical	24907272
PML_HUMAN	PML	physical	24907272
MECP2_HUMAN	MECP2	physical	25355316
PML_HUMAN	PML	physical	18708055
SUMO2_HUMAN	SUMO2	physical	22661230
UB2D1_HUMAN	UBE2D1	physical	24969970
NCOA1_HUMAN	NCOA1	genetic	11696545
TBP_HUMAN	TBP	genetic	11696545
TERF2_HUMAN	TERF2	physical	26450775
FANCA_HUMAN	FANCA	physical	25751062
UBE2N_HUMAN	UBE2N	physical	26148049
UBC_HUMAN	UBC	physical	26148049
M3K7_HUMAN	MAP3K7	physical	26299341
UBP11_HUMAN	USP11	physical	25969536
SP1_HUMAN	SP1	physical	26511642
SUMO2_HUMAN	SUMO2	physical	26950370
UB2D1_HUMAN	UBE2D1	physical	26950370
UB2D2_HUMAN	UBE2D2	physical	25960396
UB2E1_HUMAN	UBE2E1	physical	25960396
RNF4_HUMAN	RNF4	physical	25960396
UB2E2_HUMAN	UBE2E2	physical	25960396
UB2E3_HUMAN	UBE2E3	physical	25960396
MYC_HUMAN	MYC	physical	27653698
CTNB1_HUMAN	CTNNB1	physical	27653698
M18BP_HUMAN	MIS18BP1	physical	28951443
UB2D2_HUMAN	UBE2D2	physical	27678051
UB2D1_HUMAN	UBE2D1	physical	27678051
UB2D3_HUMAN	UBE2D3	physical	27678051
UBE2A_HUMAN	UBE2A	physical	27678051
UBE2B_HUMAN	UBE2B	physical	27678051
RNF4_HUMAN	RNF4	physical	27678051

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 RNF4_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-94 AND SER-95, AND MASSSPECTROMETRY.	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-94 AND SER-95, AND MASSSPECTROMETRY.	18669648 [Abstract]