RN138_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: RN138_HUMAN
• UniProt AC: Q8WVD3
• Protein Name: E3 ubiquitin-protein ligase RNF138 {ECO:0000305}
• Gene Name: RNF138 {ECO:0000312|HGNC:HGNC:17765}
• Organism: Homo sapiens (Human).
• Sequence Length: 245
• Subcellular Localization: Chromosome . Recruited at DNA damage sites (PubMed:26502055). Localizes to sites of double-strand break: localization to double-strand break sites is mediated by the zinc fingers (PubMed:26502055, PubMed:26502057).
• Protein Description: E3 ubiquitin-protein ligase involved in DNA damage response by promoting DNA resection and homologous recombination. [PubMed: 26502055]
• Protein Sequence: MAEDLSAATSYTEDDFYCPVCQEVLKTPVRTTACQHVFCRKCFLTAMRESGAHCPLCRGNVTRRERACPERALDLENIMRKFSGSCRCCAKQIKFYRMRHHYKSCKKYQDEYGVSSIIPNFQISQDSVGNSNRSETSTSDNTETYQENTSSSGHPTFKCPLCQESNFTRQRLLDHCNSNHLFQIVPVTCPICVSLPWGDPSQITRNFVSHLNQRHQFDYGEFVNLQLDEETQYQTAVEESFQVNI

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	------MAEDLSAAT ------CCCCHHHCC	21.00	19413330
3	Phosphorylation	-----MAEDLSAATS -----CCCCHHHCCC	59.18	24719451
26	Ubiquitination	PVCQEVLKTPVRTTA HHHHHHHCCCCCCCC	56.83	-
27	Phosphorylation	VCQEVLKTPVRTTAC HHHHHHCCCCCCCCC	23.90	-
41	Acetylation	CQHVFCRKCFLTAMR CHHHHHHHHHHHHHH	30.44	20167786
41	Ubiquitination	CQHVFCRKCFLTAMR CHHHHHHHHHHHHHH	30.44	-
80	Methylation	LDLENIMRKFSGSCR HCHHHHHHHHCCCHH	32.82	115491389
94	Ubiquitination	RCCAKQIKFYRMRHH HHHHHHHHHHHHHHH	33.57	-
107	Ubiquitination	HHYKSCKKYQDEYGV HHHHHHHHHHHHHCC	53.09	-
108	Phosphorylation	HYKSCKKYQDEYGVS HHHHHHHHHHHHCCC	13.49	22817900
112	Phosphorylation	CKKYQDEYGVSSIIP HHHHHHHHCCCCCCC	30.99	22817900
124	Phosphorylation	IIPNFQISQDSVGNS CCCCCEECCCCCCCC	19.70	17525332
127	Phosphorylation	NFQISQDSVGNSNRS CCEECCCCCCCCCCC	25.04	28450419
131	Phosphorylation	SQDSVGNSNRSETST CCCCCCCCCCCCCCC	27.91	29523821
134	Phosphorylation	SVGNSNRSETSTSDN CCCCCCCCCCCCCCC	49.86	23403867
136	Phosphorylation	GNSNRSETSTSDNTE CCCCCCCCCCCCCCC	38.25	30108239
137	Phosphorylation	NSNRSETSTSDNTET CCCCCCCCCCCCCCC	23.12	23401153
138	Phosphorylation	SNRSETSTSDNTETY CCCCCCCCCCCCCCC	47.74	23401153
139	Phosphorylation	NRSETSTSDNTETYQ CCCCCCCCCCCCCCC	28.73	25159151
142	Phosphorylation	ETSTSDNTETYQENT CCCCCCCCCCCCHHC	34.39	26502057
144	Phosphorylation	STSDNTETYQENTSS CCCCCCCCCCHHCCC	28.59	23898821
145	Phosphorylation	TSDNTETYQENTSSS CCCCCCCCCHHCCCC	13.96	23898821
149	Phosphorylation	TETYQENTSSSGHPT CCCCCHHCCCCCCCC	29.27	28450419
150	Phosphorylation	ETYQENTSSSGHPTF CCCCHHCCCCCCCCC	33.80	28450419
151	Phosphorylation	TYQENTSSSGHPTFK CCCHHCCCCCCCCCC	38.00	28450419
152	Phosphorylation	YQENTSSSGHPTFKC CCHHCCCCCCCCCCC	40.67	28450419
156	Phosphorylation	TSSSGHPTFKCPLCQ CCCCCCCCCCCCCCC	30.01	28450419
158	Ubiquitination	SSGHPTFKCPLCQES CCCCCCCCCCCCCCC	37.10	-
161	Phosphorylation	HPTFKCPLCQESNFT CCCCCCCCCCCCCCC	7.07	24719451

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
124	S	Phosphorylation	Kinase	ATM	Q13315	PSP
-	K	Ubiquitination	E3 ubiquitin ligase	RNF138	Q8WVD3	PMID:16714285

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of RN138_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 RN138_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
CF206_HUMAN	C6orf165	physical	16189514
A4_HUMAN	APP	physical	21832049
TRIM8_HUMAN	TRIM8	physical	22493164
LNX2_HUMAN	LNX2	physical	22493164
UBE2K_HUMAN	UBE2K	physical	16714285
LEF1_HUMAN	LEF1	physical	16714285
TF7L2_HUMAN	TCF7L2	physical	16714285
RA51D_HUMAN	RAD51D	physical	27161866
LEF1_HUMAN	LEF1	physical	27195665
LYAR_HUMAN	LYAR	physical	27195665
EF1A1_HUMAN	EEF1A1	physical	27195665
HDAC1_HUMAN	HDAC1	physical	27195665
RA51D_HUMAN	RAD51D	physical	27195665
RBBP4_HUMAN	RBBP4	physical	27195665
UBE2K_HUMAN	UBE2K	physical	27173435

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

Phosphorylation

"ATM and ATR substrate analysis reveals extensive protein networksresponsive to DNA damage.";
Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III,Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.;
Science 316:1160-1166(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-124, AND MASSSPECTROMETRY.
PubMed: 17525332