dbPTM

RN139_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	RN139_HUMAN
UniProt AC	Q8WU17
Protein Name	E3 ubiquitin-protein ligase RNF139
Gene Name	RNF139 {ECO:0000312\|HGNC:HGNC:17023}
Organism	Homo sapiens (Human).
Sequence Length	664
Subcellular Localization	Endoplasmic reticulum membrane Multi-pass membrane protein .
Protein Description	E3-ubiquitin ligase; acts as a negative regulator of the cell proliferation through mechanisms involving G2/M arrest and cell death. Required for MHC class I ubiquitination in cells expressing the cytomegalovirus protein US2 before dislocation from the endoplasmic reticulum (ER). Affects SREBP processing by hindering the SREBP/SCAP complex translocation from the ER to the Golgi, thereby reducing SREBF2 target gene expression. Required for INSIG1 ubiquitination. May be required for EIF3 complex ubiquitination. May function as a signaling receptor..
Protein Sequence	MAAVGPPQQQVRMAHQQVWAALEVALRVPCLYIIDAIFNSYPDSSQSRFCIVLQIFLRLFGVFASSIVLILSQRSLFKFYTYSSAFLLAATSVLVNYYASLHIDFYGAYNTSAFGIELLPRKGPSLWMALIVLQLTFGIGYVTLLQIHSIYSQLIILDLLVPVIGLITELPLHIRETLLFTSSLILTLNTVFVLAVKLKWFYYSTRYVYLLVRHMYRIYGLQLLMEDTWKRIRFPDILRVFWLTRVTAQATVLMYILRMANETDSFFISWDDFWDLICNLIISGCDSTLTVLGMSAVISSVAHYLGLGILAFIGSTEEDDRRLGFVAPVLFFILALQTGLSGLRPEERLIRLSRNMCLLLTAVLHFIHGMTDPVLMSLSASHVSSFRRHFPVLFVSACLFILPVLLSYVLWHHYALNTWLFAVTAFCVELCLKVIVSLTVYTLFMIDGYYNVLWEKLDDYVYYVRSTGSIIEFIFGVVMFGNGAYTMMFESGSKIRAFMMCLHAYFNIYLQAKNGWKTFMNRRTAVKKINSLPEIKGSRLQEINDVCAICYHEFTTSARITPCNHYFHALCLRKWLYIQDTCPMCHQKVYIEDDIKDNSNVSNNNGFIPPNETPEEAVREAAAESDRELNEDDSTDCDDDVQRERNGVIQHTGAAAEEFNDDTD

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Acetylation	------MAAVGPPQQ ------CCCCCCHHH	15.74	22814378
72	Phosphorylation	SSIVLILSQRSLFKF HHHHHHHCCCCHHHH	19.29	24719451
75	Phosphorylation	VLILSQRSLFKFYTY HHHHCCCCHHHHHCH	30.44	24719451
228	Phosphorylation	LQLLMEDTWKRIRFP HHHHCCCCHHHCCCC	21.41	-
230	Ubiquitination	LLMEDTWKRIRFPDI HHCCCCHHHCCCCHH	39.79	-
247	Phosphorylation	VFWLTRVTAQATVLM HHHHHHHHHHHHHHH	15.12	20068231
251	Phosphorylation	TRVTAQATVLMYILR HHHHHHHHHHHHHHH	11.33	20068231
255	Phosphorylation	AQATVLMYILRMANE HHHHHHHHHHHHHCC	7.82	20068231
341	Phosphorylation	LALQTGLSGLRPEER HHHHHCCCCCCHHHH	36.81	24719451
449	Phosphorylation	TLFMIDGYYNVLWEK HHHHHCCHHHHHHHH	6.52	-
450	Phosphorylation	LFMIDGYYNVLWEKL HHHHCCHHHHHHHHH	12.34	-
460	Phosphorylation	LWEKLDDYVYYVRST HHHHHCCCEEECCCC	7.04	30576142
466	Phosphorylation	DYVYYVRSTGSIIEF CCEEECCCCCCHHHH	27.38	30576142
469	Phosphorylation	YYVRSTGSIIEFIFG EECCCCCCHHHHHHE	22.08	25332170
485	Phosphorylation	VMFGNGAYTMMFESG EEECCCCEEEEECCC	9.14	25332170
491	Phosphorylation	AYTMMFESGSKIRAF CEEEEECCCHHHHHH	36.78	30576142
528	Ubiquitination	NRRTAVKKINSLPEI CHHHHHHHHHCCCCC	40.29	29967540
531	Phosphorylation	TAVKKINSLPEIKGS HHHHHHHCCCCCCCC	49.10	28450419
625	Phosphorylation	VREAAAESDRELNED HHHHHHHCCHHCCCC	36.92	30278072
634	Phosphorylation	RELNEDDSTDCDDDV HHCCCCCCCCCCHHH	38.17	30278072
635	Phosphorylation	ELNEDDSTDCDDDVQ HCCCCCCCCCCHHHH	47.87	30278072
652	Phosphorylation	RNGVIQHTGAAAEEF HHCCCCCCCHHHHHH	16.49	23403867
663	Phosphorylation	AEEFNDDTD------ HHHHCCCCC------	46.61	20068067

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 RN139_HUMAN !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of RN139_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 RN139_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
INSI1_HUMAN	INSIG1	physical	20068067
EIF3A_HUMAN	EIF3A	physical	20068067
SRBP2_HUMAN	SREBF2	physical	19706601
SCAP_HUMAN	SCAP	physical	19706601
INSI1_HUMAN	INSIG1	physical	22143767
INSI2_HUMAN	INSIG2	physical	22143767
HMDH_HUMAN	HMGCR	physical	22143767
AUP1_HUMAN	AUP1	physical	23223569
UB2G2_HUMAN	UBE2G2	physical	23223569
1C07_HUMAN	HLA-C	physical	19720873
HM13_HUMAN	HM13	physical	19720873

Drug and Disease Associations

Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
144700	Renal cell carcinoma (RCC)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.

Regulatory Network of RN139_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-625; SER-634; THR-635AND THR-663, AND MASS SPECTROMETRY.	18669648 [Abstract]
"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 THR-663, AND MASSSPECTROMETRY.	19690332 [Abstract]
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach."; Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.; Anal. Chem. 81:4493-4501(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-663, AND MASSSPECTROMETRY.	19413330 [Abstract]
"Kinase-selective enrichment enables quantitative phosphoproteomics ofthe kinome across the cell cycle."; Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,Greff Z., Keri G., Stemmann O., Mann M.; Mol. Cell 31:438-448(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-663, AND MASSSPECTROMETRY.	18691976 [Abstract]
"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks."; Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.; Cell 127:635-648(2006). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-663, AND MASSSPECTROMETRY.	17081983 [Abstract]