RN115_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: RN115_HUMAN
• UniProt AC: Q9Y4L5
• Protein Name: E3 ubiquitin-protein ligase RNF115 {ECO:0000305}
• Gene Name: RNF115 {ECO:0000312|HGNC:HGNC:18154}
• Organism: Homo sapiens (Human).
• Sequence Length: 304
• Subcellular Localization: Cytoplasm, cytosol . The GTP-bound form of RAB7A recruits RNF115 from the cytosol onto late endosomes/lysosomes.
• Protein Description: E3 ubiquitin-protein ligase that mediates E2-dependent, 'Lys-48'- and/or 'Lys-63'-linked polyubiquitination of substrates and may play a role in diverse biological processes. Through their polyubiquitination, may play a role in the endosomal trafficking and degradation of membrane receptors including EGFR, FLT3, MET and CXCR4..
• Protein Sequence: MAEASAAGADSGAAVAAHRFFCHFCKGEVSPKLPEYICPRCESGFIEEVTDDSSFLGGGGSRIDNTTTTHFAELWGHLDHTMFFQDFRPFLSSSPLDQDNRANERGHQTHTDFWGARPPRLPLGRRYRSRGSSRPDRSPAIEGILQHIFAGFFANSAIPGSPHPFSWSGMLHSNPGDYAWGQTGLDAIVTQLLGQLENTGPPPADKEKITSLPTVTVTQEQVDMGLECPVCKEDYTVEEEVRQLPCNHFFHSSCIVPWLELHDTCPVCRKSLNGEDSTRQSQSTEASASNRFSNDSQLHDRWTF

Overview of Protein Modification Sites with Functional and Structural Information

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Acetylation	------MAEASAAGA ------CCCHHHCCC	22.51	19413330
26	"N6,N6-dimethyllysine"	RFFCHFCKGEVSPKL HHHHHHHCCCCCCCC	58.10	-
26	Ubiquitination	RFFCHFCKGEVSPKL HHHHHHHCCCCCCCC	58.10	23000965
26	Methylation	RFFCHFCKGEVSPKL HHHHHHHCCCCCCCC	58.10	-
32	Ubiquitination	CKGEVSPKLPEYICP HCCCCCCCCCHHHCC	69.99	23000965
53	Phosphorylation	IEEVTDDSSFLGGGG EEEECCCCCCCCCCC	26.29	-
61	Phosphorylation	SFLGGGGSRIDNTTT CCCCCCCCCCCCCCC	29.36	-
132	Phosphorylation	RRYRSRGSSRPDRSP HHHHCCCCCCCCCCH	23.28	28787133
138	Phosphorylation	GSSRPDRSPAIEGIL CCCCCCCCHHHHHHH	26.51	28787133
208	Ubiquitination	PPPADKEKITSLPTV CCCCCHHHCCCCCEE	57.96	29967540
214	Phosphorylation	EKITSLPTVTVTQEQ HHCCCCCEEEEEHHH	33.82	24275569
216	Phosphorylation	ITSLPTVTVTQEQVD CCCCCEEEEEHHHHH	21.95	24275569
218	Phosphorylation	SLPTVTVTQEQVDMG CCCEEEEEHHHHHCC	19.61	24275569
281	Phosphorylation	GEDSTRQSQSTEASA CCCCCCHHHHCHHHH	23.86	-
296	Phosphorylation	SNRFSNDSQLHDRWT HHCCCCCCCCCCCCC	38.60	25159151
303	Phosphorylation	SQLHDRWTF------ CCCCCCCCC------	21.99	25159151

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
-	K	Ubiquitination	E3 ubiquitin ligase	RNF115	Q9Y4L5	PMID:17462600

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of RN115_HUMAN !!

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Oops, there are no SNP-PTM records of RN115_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
RD23A_HUMAN	RAD23A	physical	22315970
1433S_HUMAN	SFN	physical	22315970
ATN1_HUMAN	ATN1	physical	22315970
CDK10_HUMAN	CDK10	physical	22315970
CYTC_HUMAN	CST3	physical	22315970
DOCK4_HUMAN	DOCK4	physical	22315970
FOLR3_HUMAN	FOLR3	physical	22315970
MFAP4_HUMAN	MFAP4	physical	22315970
RASH_HUMAN	HRAS	physical	22315970
UBC9_HUMAN	UBE2I	physical	18819927
RL18A_HUMAN	RPL18A	physical	18819927
UBC_HUMAN	UBC	physical	18819927
RN115_HUMAN	RNF115	physical	18819927
RAB7A_HUMAN	RAB7A	physical	12972561
RAB7B_HUMAN	RAB7B	physical	12972561
A4_HUMAN	APP	physical	21832049
UB2D2_HUMAN	UBE2D2	physical	23418353
UBE2N_HUMAN	UBE2N	physical	23418353
RN115_HUMAN	RNF115	physical	23418353
EGFR_HUMAN	EGFR	physical	23418353
MYC_HUMAN	MYC	physical	22844532
TTHY_HUMAN	TTR	physical	22844532
PFD5_HUMAN	PFDN5	physical	22844532
UB2D4_HUMAN	UBE2D4	physical	25416956
UB2D2_HUMAN	UBE2D2	physical	18819927
1433B_HUMAN	YWHAB	physical	22315970
DAZP2_HUMAN	DAZAP2	physical	21516116
TAXB1_HUMAN	TAX1BP1	physical	28514442
H2AX_HUMAN	H2AFX	physical	28536406
RAD51_HUMAN	RAD51	physical	28536406

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.

Related Literatures of Post-Translational Modification

Acetylation

"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: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, AND MASS SPECTROMETRY.
PubMed: 19413330