dbPTM

ZNRF2_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	ZNRF2_HUMAN
UniProt AC	Q8NHG8
Protein Name	E3 ubiquitin-protein ligase ZNRF2
Gene Name	ZNRF2
Organism	Homo sapiens (Human).
Sequence Length	242
Subcellular Localization	Endosome membrane Peripheral membrane protein . Lysosome membrane Peripheral membrane protein . Cell junction, synapse, presynaptic cell membrane Peripheral membrane protein . Present in presynaptic plasma membranes in neurons.
Protein Description	May play a role in the establishment and maintenance of neuronal transmission and plasticity via its ubiquitin ligase activity. E3 ubiquitin ligases accept ubiquitin from an E2 ubiquitin-conjugating enzyme in the form of a thioester and then directly transfer the ubiquitin to targeted substrates..
Protein Sequence	MGAKQSGPAAANGRTRAYSGSDLPSSSSGGANGTAGGGGGARAAAAGRFPAQVPSAHQPSASGGAAAAAAAPAAPAAPRSRSLGGAVGSVASGARAAQSPFSIPNSSSGPYGSQDSVHSSPEDGGGGRDRPVGGSPGGPRLVIGSLPAHLSPHMFGGFKCPVCSKFVSSDEMDLHLVMCLTKPRITYNEDVLSKDAGECAICLEELQQGDTIARLPCLCIYHKGCIDEWFEVNRSCPEHPSD

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Myristoylation	------MGAKQSGPA ------CCCCCCCCC	41.29	14561866
6	Phosphorylation	--MGAKQSGPAAANG --CCCCCCCCCCCCC	46.14	-
15	Phosphorylation	PAAANGRTRAYSGSD CCCCCCCCCCCCCCC	22.50	23401153
18	Phosphorylation	ANGRTRAYSGSDLPS CCCCCCCCCCCCCCC	15.41	30278072
19	Phosphorylation	NGRTRAYSGSDLPSS CCCCCCCCCCCCCCC	30.73	19664994
21	Phosphorylation	RTRAYSGSDLPSSSS CCCCCCCCCCCCCCC	29.99	22167270
25	Phosphorylation	YSGSDLPSSSSGGAN CCCCCCCCCCCCCCC	50.58	30278072
26	Phosphorylation	SGSDLPSSSSGGANG CCCCCCCCCCCCCCC	26.95	29978859
27	Phosphorylation	GSDLPSSSSGGANGT CCCCCCCCCCCCCCC	37.02	23927012
28	Phosphorylation	SDLPSSSSGGANGTA CCCCCCCCCCCCCCC	43.10	23927012
34	Phosphorylation	SSGGANGTAGGGGGA CCCCCCCCCCCCHHH	23.18	23927012
60	Phosphorylation	VPSAHQPSASGGAAA CCCCCCCCCCCHHHH	28.61	-
80	Phosphorylation	AAPAAPRSRSLGGAV CCCCCCCCCCCCCHH	25.76	23401153
82	Phosphorylation	PAAPRSRSLGGAVGS CCCCCCCCCCCHHHH	32.39	29255136
89	Phosphorylation	SLGGAVGSVASGARA CCCCHHHHHHHHCCC	14.12	23927012
92	Phosphorylation	GAVGSVASGARAAQS CHHHHHHHHCCCCCC	30.72	23927012
99	Phosphorylation	SGARAAQSPFSIPNS HHCCCCCCCCCCCCC	24.16	26055452
102	Phosphorylation	RAAQSPFSIPNSSSG CCCCCCCCCCCCCCC	40.29	30576142
106	Phosphorylation	SPFSIPNSSSGPYGS CCCCCCCCCCCCCCC	22.11	23401153
107	Phosphorylation	PFSIPNSSSGPYGSQ CCCCCCCCCCCCCCC	46.05	23401153
108	Phosphorylation	FSIPNSSSGPYGSQD CCCCCCCCCCCCCCC	43.54	28348404
111	Phosphorylation	PNSSSGPYGSQDSVH CCCCCCCCCCCCCCC	32.69	22617229
113	Phosphorylation	SSSGPYGSQDSVHSS CCCCCCCCCCCCCCC	25.60	23401153
116	Phosphorylation	GPYGSQDSVHSSPED CCCCCCCCCCCCCCC	17.69	17525332
119	Phosphorylation	GSQDSVHSSPEDGGG CCCCCCCCCCCCCCC	45.49	17525332
120	Phosphorylation	SQDSVHSSPEDGGGG CCCCCCCCCCCCCCC	19.89	26055452
135	Phosphorylation	RDRPVGGSPGGPRLV CCCCCCCCCCCCCEE	17.91	29255136
145	Phosphorylation	GPRLVIGSLPAHLSP CCCEEEECCCCCCCH	21.76	29255136
151	Phosphorylation	GSLPAHLSPHMFGGF ECCCCCCCHHHCCCC	11.68	29255136
165	Ubiquitination	FKCPVCSKFVSSDEM CCCCCCCCCCCCCCC	44.66	-
168	Phosphorylation	PVCSKFVSSDEMDLH CCCCCCCCCCCCEEE	34.89	24719451
169	Phosphorylation	VCSKFVSSDEMDLHL CCCCCCCCCCCEEEE	32.08	28348404
186	Phosphorylation	CLTKPRITYNEDVLS HHCCCCCCCCHHHHC	22.90	27690223
187	Phosphorylation	LTKPRITYNEDVLSK HCCCCCCCCHHHHCC	17.74	27690223
193	Phosphorylation	TYNEDVLSKDAGECA CCCHHHHCCCCCCCE	28.47	30576142

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
145	S	Phosphorylation	Kinase	MTOR	P42345	PSP

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of ZNRF2_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 ZNRF2_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
1433T_HUMAN	YWHAQ	physical	22797923
AT1A2_HUMAN	ATP1A2	physical	22797923
UBE2N_HUMAN	UBE2N	physical	22797923
ZNRF1_HUMAN	ZNRF1	physical	22797923
UBE2N_HUMAN	UBE2N	physical	18615712
UB2E1_HUMAN	UBE2E1	physical	18615712
AT1A1_HUMAN	ATP1A1	physical	22797923
UBC_HUMAN	UBC	physical	22797923
MTOR_HUMAN	MTOR	physical	27244671
RPTOR_HUMAN	RPTOR	physical	27244671
LST8_HUMAN	MLST8	physical	27244671
PPP6_HUMAN	PPP6C	physical	27244671
ANR28_HUMAN	ANKRD28	physical	27244671
PP6R3_HUMAN	PPP6R3	physical	27244671
VPP2_HUMAN	ATP6V0A2	physical	27244671
LTOR1_HUMAN	LAMTOR1	physical	27244671

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 ZNRF2_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-82; SER-113 AND SER-116,AND MASS SPECTROMETRY.	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 SER-19, 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-82 AND SER-151, AND MASSSPECTROMETRY.	18669648 [Abstract]
"Combining protein-based IMAC, peptide-based IMAC, and MudPIT forefficient phosphoproteomic analysis."; Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D.,Yates J.R. III; J. Proteome Res. 7:1346-1351(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-18 AND SER-82, AND MASSSPECTROMETRY.	18220336 [Abstract]
"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-113; SER-116 ANDSER-119, AND MASS SPECTROMETRY.	17525332 [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 SER-135, AND MASSSPECTROMETRY.	17081983 [Abstract]