dbPTM

RN220_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	RN220_HUMAN
UniProt AC	Q5VTB9
Protein Name	E3 ubiquitin-protein ligase RNF220
Gene Name	RNF220
Organism	Homo sapiens (Human).
Sequence Length	566
Subcellular Localization	Cytoplasm .
Protein Description	E3 ubiquitin-protein ligase that promotes the ubiquitination and proteasomal degradation of SIN3B (By similarity). Independently of its E3 ligase activity, acts as a CTNNB1 stabilizer through USP7-mediated deubiquitination of CTNNB1 promoting Wnt signaling. [PubMed: 25266658]
Protein Sequence	MDLHRAAFKMENSSYLPNPLASPALMVLASTAEASRDASIPCQQPRPFGVPVSVDKDVHIPFTNGSYTFASMYHRQGGVPGTFANRDFPPSLLHLHPQFAPPNLDCTPISMLNHSGVGAFRPFASTEDRESYQSAFTPAKRLKNCHDTESPHLRFSDADGKEYDFGTQLPSSSPGSLKVDDTGKKIFAVSGLISDREASSSPEDRNDRCKKKAAALFDSQAPICPICQVLLRPSELQEHMEQELEQLAQLPSSKNSLLKDAMAPGTPKSLLLSASIKREGESPTASPHSSATDDLHHSDRYQTFLRVRANRQTRLNARIGKMKRRKQDEGQREGSCMAEDDAVDIEHENNNRFEEYEWCGQKRIRATTLLEGGFRGSGFIMCSGKENPDSDADLDVDGDDTLEYGKPQYTEADVIPCTGEEPGEAKEREALRGAVLNGGPPSTRITPEFSKWASDEMPSTSNGESSKQEAMQKTCKNSDIEKITEDSAVTTFEALKARVRELERQLSRGDRYKCLICMDSYSMPLTSIQCWHVHCEECWLRTLGAKKLCPQCNTITAPGDLRRIYL

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
14	Phosphorylation	AFKMENSSYLPNPLA HHHCCCCCCCCCCCC	42.12	28165663
15	Phosphorylation	FKMENSSYLPNPLAS HHCCCCCCCCCCCCC	26.46	24719451
22	Phosphorylation	YLPNPLASPALMVLA CCCCCCCCHHHHHHH	20.56	24719451
30	Phosphorylation	PALMVLASTAEASRD HHHHHHHHHHHHHCC	24.80	24719451
35	Phosphorylation	LASTAEASRDASIPC HHHHHHHHCCCCCCC	23.38	28165663
53	O-linked_Glycosylation	RPFGVPVSVDKDVHI CCCCCCEEECCCEEC	20.66	28657654
101	Ubiquitination	HLHPQFAPPNLDCTP HCCCCCCCCCCCCCC	21.43	21890473
104	Ubiquitination	PQFAPPNLDCTPISM CCCCCCCCCCCCHHH	7.64	23000965
123	Ubiquitination	GVGAFRPFASTEDRE CCCCCCCCCCCCCHH	7.96	21890473
132	Phosphorylation	STEDRESYQSAFTPA CCCCHHHHHHCCCHH	11.18	32142685
140	Acetylation	QSAFTPAKRLKNCHD HHCCCHHHHHCCCCC	60.51	30591971
149	Ubiquitination	LKNCHDTESPHLRFS HCCCCCCCCCCCEEE	69.22	23000965
149	Ubiquitination	LKNCHDTESPHLRFS HCCCCCCCCCCCEEE	69.22	21890473
150	Phosphorylation	KNCHDTESPHLRFSD CCCCCCCCCCCEEEC	21.51	25159151
167	Phosphorylation	GKEYDFGTQLPSSSP CCEEECCCCCCCCCC	27.25	27050516
168	Ubiquitination	KEYDFGTQLPSSSPG CEEECCCCCCCCCCC	52.32	33845483
171	Phosphorylation	DFGTQLPSSSPGSLK ECCCCCCCCCCCCEE	52.63	29978859
172	Phosphorylation	FGTQLPSSSPGSLKV CCCCCCCCCCCCEEE	38.32	25159151
173	Phosphorylation	GTQLPSSSPGSLKVD CCCCCCCCCCCEEEC	37.30	29978859
176	Phosphorylation	LPSSSPGSLKVDDTG CCCCCCCCEEECCCC	28.53	29978859
177	Phosphorylation	PSSSPGSLKVDDTGK CCCCCCCEEECCCCC	8.53	32142685
190	Ubiquitination	GKKIFAVSGLISDRE CCEEEEEEEEECCHH	25.18	23000965
190	Phosphorylation	GKKIFAVSGLISDRE CCEEEEEEEEECCHH	25.18	30301811
193	Ubiquitination	IFAVSGLISDREASS EEEEEEEECCHHHCC	4.61	23000965
194	Phosphorylation	FAVSGLISDREASSS EEEEEEECCHHHCCC	35.34	30301811
196	Dimethylation	VSGLISDREASSSPE EEEEECCHHHCCCCC	34.29	-
196	Methylation	VSGLISDREASSSPE EEEEECCHHHCCCCC	34.29	24379857
200	Phosphorylation	ISDREASSSPEDRND ECCHHHCCCCCHHCH	57.89	21712546
201	Phosphorylation	SDREASSSPEDRNDR CCHHHCCCCCHHCHH	29.79	21712546
209	Ubiquitination	PEDRNDRCKKKAAAL CCHHCHHHHHHHHHH	9.39	32015554
212	Ubiquitination	RNDRCKKKAAALFDS HCHHHHHHHHHHHCC	28.84	23000965
213	Ubiquitination	NDRCKKKAAALFDSQ CHHHHHHHHHHHCCC	13.57	33845483
238	Ubiquitination	LRPSELQEHMEQELE HCHHHHHHHHHHHHH	58.80	21890473
238	Ubiquitination	LRPSELQEHMEQELE HCHHHHHHHHHHHHH	58.80	23000965
254	Ubiquitination	LAQLPSSKNSLLKDA HHCCCCCCCHHHHHH	55.69	32015554
256	Phosphorylation	QLPSSKNSLLKDAMA CCCCCCCHHHHHHCC	38.52	24719451
266	Phosphorylation	KDAMAPGTPKSLLLS HHHCCCCCCHHHHHH	26.87	23401153
269	Phosphorylation	MAPGTPKSLLLSASI CCCCCCHHHHHHHHE	26.00	21406692
273	Phosphorylation	TPKSLLLSASIKREG CCHHHHHHHHEECCC	21.68	21406692
275	Phosphorylation	KSLLLSASIKREGES HHHHHHHHEECCCCC	25.85	21406692
277	Sumoylation	LLLSASIKREGESPT HHHHHHEECCCCCCC	41.73	25218447
277	Sumoylation	LLLSASIKREGESPT HHHHHHEECCCCCCC	41.73	-
282	Phosphorylation	SIKREGESPTASPHS HEECCCCCCCCCCCC	38.11	23401153
283	Ubiquitination	IKREGESPTASPHSS EECCCCCCCCCCCCC	27.90	29967540
284	Phosphorylation	KREGESPTASPHSSA ECCCCCCCCCCCCCC	49.39	29116813
286	Phosphorylation	EGESPTASPHSSATD CCCCCCCCCCCCCCC	26.14	23401153
289	Phosphorylation	SPTASPHSSATDDLH CCCCCCCCCCCCCCC	25.67	20873877
290	Phosphorylation	PTASPHSSATDDLHH CCCCCCCCCCCCCCC	31.96	20873877
292	Phosphorylation	ASPHSSATDDLHHSD CCCCCCCCCCCCCCH	31.81	20873877
335	Phosphorylation	DEGQREGSCMAEDDA CCCCCCCCCCCCCCC	8.93	20873877
356	Phosphorylation	NNNRFEEYEWCGQKR CCCCCCCEEECCCCC	13.92	27642862
362	Acetylation	EYEWCGQKRIRATTL CEEECCCCCCEEEEE	34.77	26051181
362 (in isoform 1)	Ubiquitination	-	34.77	21890473
362	Ubiquitination	EYEWCGQKRIRATTL CEEECCCCCCEEEEE	34.77	21890473
362	Ubiquitination	EYEWCGQKRIRATTL CEEECCCCCCEEEEE	34.77	23000965
367	Phosphorylation	GQKRIRATTLLEGGF CCCCCEEEEEECCCC	14.23	21406692
368	Phosphorylation	QKRIRATTLLEGGFR CCCCEEEEEECCCCC	28.50	21406692
388	Ubiquitination	MCSGKENPDSDADLD EECCCCCCCCCCCCC	43.50	23000965
390	Phosphorylation	SGKENPDSDADLDVD CCCCCCCCCCCCCCC	35.64	25159151
401	Phosphorylation	LDVDGDDTLEYGKPQ CCCCCCCCCCCCCCC	26.65	30576142
404	Phosphorylation	DGDDTLEYGKPQYTE CCCCCCCCCCCCCCC	33.30	29978859
409	Phosphorylation	LEYGKPQYTEADVIP CCCCCCCCCCCCEEE	18.31	25002506
410	Phosphorylation	EYGKPQYTEADVIPC CCCCCCCCCCCEEEC	21.32	25002506
416	Phosphorylation	YTEADVIPCTGEEPG CCCCCEEECCCCCCC	14.95	32142685
418	Phosphorylation	EADVIPCTGEEPGEA CCCEEECCCCCCCCH	42.12	28111955
426	Ubiquitination	GEEPGEAKEREALRG CCCCCCHHHHHHHHH	53.66	33845483
442	Phosphorylation	VLNGGPPSTRITPEF HHCCCCCCCCCCHHH	33.19	26270265
443	Phosphorylation	LNGGPPSTRITPEFS HCCCCCCCCCCHHHH	31.68	26270265
446	Phosphorylation	GPPSTRITPEFSKWA CCCCCCCCHHHHHHC	17.30	26657352
450	Phosphorylation	TRITPEFSKWASDEM CCCCHHHHHHCCCCC	26.14	26270265
451 (in isoform 1)	Ubiquitination	-	52.69	21890473
451	Ubiquitination	RITPEFSKWASDEMP CCCHHHHHHCCCCCC	52.69	21890473
451	Ubiquitination	RITPEFSKWASDEMP CCCHHHHHHCCCCCC	52.69	23000965
452	Ubiquitination	ITPEFSKWASDEMPS CCHHHHHHCCCCCCC	10.37	33845483
459	Phosphorylation	WASDEMPSTSNGESS HCCCCCCCCCCCHHH	43.06	28450419
460	Phosphorylation	ASDEMPSTSNGESSK CCCCCCCCCCCHHHH	21.97	28450419
461	Phosphorylation	SDEMPSTSNGESSKQ CCCCCCCCCCHHHHH	47.37	28450419
465	Phosphorylation	PSTSNGESSKQEAMQ CCCCCCHHHHHHHHH	44.21	28450419
466	Phosphorylation	STSNGESSKQEAMQK CCCCCHHHHHHHHHH	33.77	28450419
467	Ubiquitination	TSNGESSKQEAMQKT CCCCHHHHHHHHHHH	62.53	32015554
467	Acetylation	TSNGESSKQEAMQKT CCCCHHHHHHHHHHH	62.53	26051181
477	Ubiquitination	AMQKTCKNSDIEKIT HHHHHHCCCCHHHHC	47.24	23000965
493	Ubiquitination	DSAVTTFEALKARVR CCHHHHHHHHHHHHH	51.50	32015554
496	Ubiquitination	VTTFEALKARVRELE HHHHHHHHHHHHHHH	40.99	29967540

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	RNF220	Q5VTB9	PMID:22199232

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of RN220_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 RN220_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
SIN3B_HUMAN	SIN3B	physical	20170641
UB2D3_HUMAN	UBE2D3	physical	20170641
CTNB1_HUMAN	CTNNB1	physical	25266658
UBP7_HUMAN	USP7	physical	25266658
GSK3B_HUMAN	GSK3B	physical	25266658
GOPC_HUMAN	GOPC	physical	25416956

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 RN220_HUMAN

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"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 SER-173, AND MASSSPECTROMETRY.	19413330 [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-390, AND MASSSPECTROMETRY.	18669648 [Abstract]