dbPTM

WRIP1_MOUSE - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	WRIP1_MOUSE
UniProt AC	Q91XU0
Protein Name	ATPase WRNIP1
Gene Name	Wrnip1 {ECO:0000312\|MGI:MGI:1926153}
Organism	Mus musculus (Mouse).
Sequence Length	660
Subcellular Localization	Nucleus . Cytoplasm . Colocalizes with WRN in granular structures in the nucleus.
Protein Description	Functions as a modulator of initiation or reinitiation events during DNA polymerase delta-mediated DNA synthesis. In the presence of ATP, stimulation of DNA polymerase delta-mediated DNA synthesis is decreased. Plays also a role in the innate immune defense against viruses. Stabilizes the RIG-I/DDX58 dsRNA interaction and promotes RIG-I/DDX58 'Lys-63'-linked polyubiquitination. In turn, RIG-I/DDX58 transmits the signal through mitochondrial MAVS..
Protein Sequence	MEVSGPEDDPFLSQLHQVQCPVCQQMMPAAHINSHLDRCLLLHPAGHAEPAAGSHRAGERAKGPSPPGAKRRRLSESSALKQPATPTAAESSEGEGEEGDDGGETESRESYDAPPTPSGARLIPDFPVARSSSPARKGMGKRPAAAAAAGSASPRSWDEAEAQEEEEAGVDGDGDADVDGEDDPGHWDADAADASFGVSAGRAHPRALAAEEIRQMLEGKPLADKMRPDTLQDYIGQSRAVGQETLLRSLLEANEIPSLILWGPPGCGKTTLAHIIANNSKKHSIRFVTLSATNAKTNDVRDVIKQAQNEKSFFKRKTILFIDEIHRFNKSQQDTFLPHVECGTITLIGATTENPSFQVNAALLSRCRVIVLEKLPVEAMVTILMRAINSLGIHVLDSSRPTDPLSHSSNCSSEPSVFIEDKAVDTLAYLSDGDARTGLNGLQLAVLARLSSRKVFCKKSGQTYSPSRVLITENDVKEGLQRSHILYDRAGEEHYNCISALHKAMRGSDQNASLYWLARMLEGGEDPLYVARRLVRFASEDIGLADPSALAQAVAAYQGCHFIGMPECEVLLAQCVVYFARAPKSIEVYSAYNNVKACLRSHQGPLPPVPLHLRNAPTRLMKDLGYGKGYKYNPMYSEPVDQDYLPEELRGVDFFKQRRC

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
65	Phosphorylation	GERAKGPSPPGAKRR HHHCCCCCCCCHHHH	53.01	25521595
75	Phosphorylation	GAKRRRLSESSALKQ CHHHHCCCCCCCCCC	33.35	25521595
77	Phosphorylation	KRRRLSESSALKQPA HHHCCCCCCCCCCCC	19.96	21082442
78	Phosphorylation	RRRLSESSALKQPAT HHCCCCCCCCCCCCC	33.30	25168779
81	Ubiquitination	LSESSALKQPATPTA CCCCCCCCCCCCCCC	54.69	-
85	Phosphorylation	SALKQPATPTAAESS CCCCCCCCCCCCCCC	28.05	23684622
87	Phosphorylation	LKQPATPTAAESSEG CCCCCCCCCCCCCCC	33.86	27087446
91	Phosphorylation	ATPTAAESSEGEGEE CCCCCCCCCCCCCCC	29.03	27087446
92	Phosphorylation	TPTAAESSEGEGEEG CCCCCCCCCCCCCCC	40.92	25521595
105	Phosphorylation	EGDDGGETESRESYD CCCCCCCCCCCCCCC	42.40	25293948
107	Phosphorylation	DDGGETESRESYDAP CCCCCCCCCCCCCCC	49.09	25293948
110	Phosphorylation	GETESRESYDAPPTP CCCCCCCCCCCCCCC	27.48	25619855
111	Phosphorylation	ETESRESYDAPPTPS CCCCCCCCCCCCCCC	16.03	28285833
116	Phosphorylation	ESYDAPPTPSGARLI CCCCCCCCCCCCCCC	29.09	25521595
118	Phosphorylation	YDAPPTPSGARLIPD CCCCCCCCCCCCCCC	47.79	25619855
131	Phosphorylation	PDFPVARSSSPARKG CCCCCCCCCCCCCCC	25.98	29514104
132	Phosphorylation	DFPVARSSSPARKGM CCCCCCCCCCCCCCC	34.48	29514104
133	Phosphorylation	FPVARSSSPARKGMG CCCCCCCCCCCCCCC	24.67	29514104
141	Ubiquitination	PARKGMGKRPAAAAA CCCCCCCCCHHHHHH	46.44	27667366
151	Phosphorylation	AAAAAAGSASPRSWD HHHHHCCCCCCCCHH	22.35	23684622
153	Phosphorylation	AAAAGSASPRSWDEA HHHCCCCCCCCHHHH	23.65	27087446
220	Ubiquitination	IRQMLEGKPLADKMR HHHHHCCCCCHHHCC	27.73	22790023
267	S-palmitoylation	ILWGPPGCGKTTLAH EEECCCCCCHHHHHH	6.61	28526873
281	Ubiquitination	HIIANNSKKHSIRFV HHHHCCCCCCEEEEE	57.54	22790023
296	Ubiquitination	TLSATNAKTNDVRDV EEECCCCCCCCHHHH	50.35	22790023
305	Ubiquitination	NDVRDVIKQAQNEKS CCHHHHHHHHHCCCC	39.15	-
451	Phosphorylation	LAVLARLSSRKVFCK HHHHHHHHCCCEEEC	23.65	23140645
452	Phosphorylation	AVLARLSSRKVFCKK HHHHHHHCCCEEECC	40.49	23140645
458	Acetylation	SSRKVFCKKSGQTYS HCCCEEECCCCCEEC	38.21	7719777
459	Ubiquitination	SRKVFCKKSGQTYSP CCCEEECCCCCEECC	62.08	-
460	Phosphorylation	RKVFCKKSGQTYSPS CCEEECCCCCEECCC	22.94	23984901
463	Phosphorylation	FCKKSGQTYSPSRVL EECCCCCEECCCEEE	29.50	23984901
464	Phosphorylation	CKKSGQTYSPSRVLI ECCCCCEECCCEEEE	15.65	23984901
465	Phosphorylation	KKSGQTYSPSRVLIT CCCCCEECCCEEEEE	21.56	25266776
467	Phosphorylation	SGQTYSPSRVLITEN CCCEECCCEEEEECC	29.13	23984901
472	Phosphorylation	SPSRVLITENDVKEG CCCEEEEECCHHHHH	25.28	25521595
477	Ubiquitination	LITENDVKEGLQRSH EEECCHHHHHHHHHC	49.26	22790023
495	Phosphorylation	DRAGEEHYNCISALH CCCCHHHHHHHHHHH	18.27	-
503	Ubiquitination	NCISALHKAMRGSDQ HHHHHHHHHHCCCCH	44.73	22790023
529	Phosphorylation	EGGEDPLYVARRLVR HCCCCHHHHHHHHHH	9.46	22817900
557	Phosphorylation	LAQAVAAYQGCHFIG HHHHHHHHCCCCCCC	8.83	-
590	Phosphorylation	PKSIEVYSAYNNVKA CCCEEHHHHHCCHHH	29.47	28418008
596	Ubiquitination	YSAYNNVKACLRSHQ HHHHCCHHHHHHHCC	35.19	22790023
622	Ubiquitination	NAPTRLMKDLGYGKG CCCCHHHHHHCCCCC	55.16	22790023
628	Acetylation	MKDLGYGKGYKYNPM HHHHCCCCCCCCCCC	51.05	23806337
628	Ubiquitination	MKDLGYGKGYKYNPM HHHHCCCCCCCCCCC	51.05	22790023
631	Ubiquitination	LGYGKGYKYNPMYSE HCCCCCCCCCCCCCC	47.41	22790023
656	Ubiquitination	LRGVDFFKQRRC--- HCCCCCHHHCCC---	42.78	22790023

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 WRIP1_MOUSE !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of WRIP1_MOUSE !!

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 WRIP1_MOUSE !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference	Domain-Domain Interactions
WRIP1_MOUSE	Wrnip1	physical	18842586

Drug and Disease Associations

Kegg Drug
DrugBank
There are no disease associations of PTM sites.

Regulatory Network of WRIP1_MOUSE

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"Solid tumor proteome and phosphoproteome analysis by high resolutionmass spectrometry."; Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,Faessler R., Mann M.; J. Proteome Res. 7:5314-5326(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-153, AND MASSSPECTROMETRY.	19367708 [Abstract]
"Large-scale phosphorylation analysis of mouse liver."; Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.; Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-92, AND MASSSPECTROMETRY.	17242355 [Abstract]
"Large-scale identification and evolution indexing of tyrosinephosphorylation sites from murine brain."; Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.; J. Proteome Res. 7:311-318(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-529, AND MASSSPECTROMETRY.	18034455 [Abstract]