ANR17_MOUSE - dbPTM
ANR17_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ANR17_MOUSE
UniProt AC Q99NH0
Protein Name Ankyrin repeat domain-containing protein 17
Gene Name Ankrd17
Organism Mus musculus (Mouse).
Sequence Length 2603
Subcellular Localization Cytoplasm . Nucleus . Detected around the nucleolus.
Protein Description Could play pivotal roles in cell cycle and DNA regulation. Involved in innate immune defense against viruse by positively regulating the viral dsRNA receptors DDX58 and IFIH1 signaling pathways. Involves in NOD2- and NOD1-mediated responses to bacteria suggesting a role in innate antibacterial immune pathways too. Could play a central role for the formation and/or maintenance of the blood vessels of the circulation system. [PubMed: 19619540]
Protein Sequence MEKATVPAAAEGEGSPPAAAAVAAPPAAAAAEVGGGARPASSPRGMVRVCDLLLKKKPPQQQQQQQPPHHKAKRNRTCRPPSSSESSSDSDNSGGGGGGGGGGGGGTSSNNSEEEEDDDDEEEEVSEVESFILDQDDLENPMLETASKLLLSGTADGADLRTVDPETQARLEALLEAAGIGKLSTADGKAFADPEVLRRLTSSVSCALDEAAAALTRMRAESTANAGQSDNRSLAEACSEGDVNAVRKLLIEGRSVNEHTEEGESLLCLACSAGYYELAQVLLAMHANVEDRGIKGDITPLMAAANGGHVKIVKLLLAHKADVNAQSSTGNTALTYACAGGYVDVVKVLLESGASIEDHNENGHTPLMEAGSAGHVEVARLLLENGAGINTHSNEFKESALTLACYKGHLEMVRFLLEAGADQEHKTDEMHTALMEACMDGHVEVARLLLDSGAQVNMPADSFESPLTLAACGGHVELAALLIERGASLEEVNDEGYTPLMEAAREGHEEMVALLLGQGANINAQTEETQETALTLACCGGFLEVADFLIKAGADIELGCSTPLMEAAQEGHLELVKYLLAAGANVHATTATGDTALTYACENGHTDVADVLLQAGADLEHESEGGRTPLMKAARAGHVCTVQFLISKGANVNRTTANNDHTVLSLACAGGHLAVVELLLAHGADPTHRLKDGSTMLIEAAKGGHTSVVCYLLDYPNNLLAAPPPDVTQLTPPSHDLNRAPRVPVQALPMVVPPQEPDKPPANLAATLPVRSKAASKQKSNSHLPANSQDVQGYITNQSPESIVEEAQGKLTELEQRIKEAIEKNAQLQSLELAHADQLTKEKIEELNKTREEQIQKKQKILEELQKVERELQLKTQQQLKKQYLEVKAQRIQLQQQQQQSCQHLGLFTSVGVGEQLSEGDYARLQQVDPVLLKDEPQQTAAQMGFAPIQPLAMPQALPLATGPLPPGSIANLTELQGVIVGQPVLGQAQLAGLGQGILTETQQGLMVASPAQTLNDTLDDIMAAVSGRASAMSNTPTHSIAASVSQPQTPTPSPIISPSAMLPIYPAIDIDAQTESNHDTALTLACAGGHEELVQTLLERGASIEHRDKKGFTPLILAATAGHVGVVEILLDNGADIEAQSERTKDTPLSLACSGGRQEVVELLLARGANKEHRNVSDYTPLSLAASGGYVNIIKILLNAGAEINSRTGSKLGISPLMLAAMNGHTAAVKLLLDMGSDINAQIETNRNTALTLACFQGRTEVVSLLLDRKANVEHRAKTGLTPLMEAASGGYAEVGRVLLDKGADVNAPPVPSSRDTALTIAADKGHYKFCELLIGKGAHIDVRNKKGNTPLWLAANGGHLDVVQLLVQATADVDAADNRKITPLMAAFRKGHVKVVRYLVKEVNQFPSDSECMRYIATITDKEMLKKCHLCMESIVQAKDRQAAEANKNASILLEELDLEKLREESRRLALAAKREKRKEKRRKKKEEQRRKLEEIEAKNKENFELQAAQEKEKLKVEEEPEVLTEPPSATTTTTIGISATWTTLAGSHGKRNNTITTTSSKRKNRKNKITPENVQIIFDDPLPISYSQPEKVNGESKSSSTSESGDSDNMRISSCSDESSNSNSSRKSNNHASAVVTTTMASKKQPSVLVTFPKEERKSVSGKASIKLSETVNEGTSNSLSTCTKSGPSPLSSPNGKLTVASPKRGPKREEGWKEVVRRSKKVSVPSTVISRVIGRGGCNINAIRECTGAHIDIDKQKDKTGDRIITIRGGTESTRQATQLINALIKDPDKEIDELIPKNRLKSSTANSKIGSSAPTTTAANSSLMGIKMTTVALSSTSQTATALTVPAISSASTHKTIKNPVNNVRPGFPVSLPLAYPPPQFAHALLAAQTFQQIRPPRLPMTHFGGTFPPAQSTWGPFPVRPLSPARATNSPKPHMVPRHSNQNSSGSQVNSAGSLTSSPTTTASSSASAVPGTTSNGSPSSPSVRRQLFVTVVKTSNATTTTVTTTASNNSTAPTNATYPMPTAKEHYPVSSPSSPSPPAQPGGVSRNSPLDCGSASPNKGASASEQEASSPPVVEPANSRPPHSSSSSGSSSGHSTQQQPPGSVPQEPRPPLQQSQVPSPDVRMTVPPTATSSAPVAVPSTAPVTYPMPQTQMGCSQPPKMEAPAIRPPSHATAAPHKTPAPVQSSSASVLNVNHIKRPHSVPSSVQLPSTLSTQSACQNSVHPANKPVAPNFSAPLPFGPFSTLFENNPTNAHAFWGGPVVSSQSTPESMLSGKSSYLPNSDPLHQSDTSKAPGFRPPLQRPAPSPSGIVNMDTPYGSVTPSSTHLGNFASSLSGGQMYGPGAPLGGAPLGGAPTAANFNRQHFSPLSLLTPCSSASNESPAQSVSSGVRAPSPAPSSVPLGSEKPSSVSQDRKVPVPIGTERSARIRQTGTSAPSVIGSNLSTSVGHSGIWSFEGIGGNQDKVDWCNPGMGNPMIHRPMSDPGVFSQHQAMERDSTGIVTPSGTFHQHVPAGYMDFPKVGSMPFSVYGNAMLPPVAPIADGAGGPIFNGPHSAEPSWNSLIKMVSSSTENNGPQTVWTGPWAPHMNSVHMNQLG
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 Orthologous
Protein Cluster
1Acetylation-------MEKATVPA
-------CCCCCCCC
48.78-
5Phosphorylation---MEKATVPAAAEG
---CCCCCCCCHHCC
37.7822942356
15PhosphorylationAAAEGEGSPPAAAAV
CHHCCCCCCCHHHHH
24.3326824392
41PhosphorylationGGGARPASSPRGMVR
CCCCCCCCCCCHHHH
43.4925521595
42PhosphorylationGGARPASSPRGMVRV
CCCCCCCCCCHHHHH
22.2623684622
126PhosphorylationDDEEEEVSEVESFIL
CCHHHHHHHHHHHHC
38.92-
130PhosphorylationEEVSEVESFILDQDD
HHHHHHHHHHCCHHH
23.82-
152PhosphorylationTASKLLLSGTADGAD
HHHHHHHHCCCCCCC
33.7854887109
201PhosphorylationPEVLRRLTSSVSCAL
HHHHHHHHHHHHHHH
19.6923984901
202PhosphorylationEVLRRLTSSVSCALD
HHHHHHHHHHHHHHH
33.0825159016
203PhosphorylationVLRRLTSSVSCALDE
HHHHHHHHHHHHHHH
16.8925159016
205PhosphorylationRRLTSSVSCALDEAA
HHHHHHHHHHHHHHH
8.8125159016
216PhosphorylationDEAAAALTRMRAEST
HHHHHHHHHHHHHHH
20.0725159016
222PhosphorylationLTRMRAESTANAGQS
HHHHHHHHHCCCCCC
31.66118587
223PhosphorylationTRMRAESTANAGQSD
HHHHHHHHCCCCCCC
18.5522345495
488PhosphorylationLLIERGASLEEVNDE
HHHHCCCCHHHHCCC
38.8530635358
728PhosphorylationAAPPPDVTQLTPPSH
CCCCCCCCCCCCCCC
25.8226643407
731PhosphorylationPPDVTQLTPPSHDLN
CCCCCCCCCCCCCCC
24.2826643407
734PhosphorylationVTQLTPPSHDLNRAP
CCCCCCCCCCCCCCC
30.7326643407
780PhosphorylationKAASKQKSNSHLPAN
HHHHCCCCCCCCCCC
40.8626643407
782PhosphorylationASKQKSNSHLPANSQ
HHCCCCCCCCCCCCH
33.2326643407
788PhosphorylationNSHLPANSQDVQGYI
CCCCCCCCHHHCHHH
29.8426643407
794PhosphorylationNSQDVQGYITNQSPE
CCHHHCHHHHCCCHH
6.3626643407
796PhosphorylationQDVQGYITNQSPESI
HHHCHHHHCCCHHHH
20.7926643407
799PhosphorylationQGYITNQSPESIVEE
CHHHHCCCHHHHHHH
32.4826643407
802PhosphorylationITNQSPESIVEEAQG
HHCCCHHHHHHHHCH
35.0126643407
830PhosphorylationEKNAQLQSLELAHAD
HHHHHHHHHHHHHHH
32.19-
1188PhosphorylationTPLSLAASGGYVNII
CCHHHHHCCCCHHHH
27.4351460013
1412PhosphorylationVNQFPSDSECMRYIA
HHCCCCHHHHHHHHH
36.7114463171
1453PhosphorylationAEANKNASILLEELD
HHHHHCHHHHHHHCC
24.1423984901
1557PhosphorylationSHGKRNNTITTTSSK
CCCCCCCCEECCCHH
24.2129550500
1562PhosphorylationNNTITTTSSKRKNRK
CCCEECCCHHCCCCC
31.6029514104
1563PhosphorylationNTITTTSSKRKNRKN
CCEECCCHHCCCCCC
34.0929899451
1566AcetylationTTTSSKRKNRKNKIT
ECCCHHCCCCCCCCC
65.917923351
1573PhosphorylationKNRKNKITPENVQII
CCCCCCCCHHCEEEE
26.59-
1601PhosphorylationKVNGESKSSSTSESG
CCCCCCCCCCCCCCC
38.5129895711
1603PhosphorylationNGESKSSSTSESGDS
CCCCCCCCCCCCCCC
42.9429895711
1604PhosphorylationGESKSSSTSESGDSD
CCCCCCCCCCCCCCC
38.1629895711
1605PhosphorylationESKSSSTSESGDSDN
CCCCCCCCCCCCCCC
31.5429895711
1607PhosphorylationKSSSTSESGDSDNMR
CCCCCCCCCCCCCCE
47.9029895711
1616PhosphorylationDSDNMRISSCSDESS
CCCCCEEECCCCCCC
18.2223684622
1617PhosphorylationSDNMRISSCSDESSN
CCCCEEECCCCCCCC
18.4423684622
1619PhosphorylationNMRISSCSDESSNSN
CCEEECCCCCCCCCC
46.4950565435
1631PhosphorylationNSNSSRKSNNHASAV
CCCCCCCCCCCCCEE
41.5814206459
1636PhosphorylationRKSNNHASAVVTTTM
CCCCCCCCEEEEECC
17.6625619855
1640PhosphorylationNHASAVVTTTMASKK
CCCCEEEEECCCCCC
15.2225619855
1642PhosphorylationASAVVTTTMASKKQP
CCEEEEECCCCCCCC
11.0225619855
1668PhosphorylationKSVSGKASIKLSETV
CCCCCCCEEEEECCC
24.6067054351
1679PhosphorylationSETVNEGTSNSLSTC
ECCCCCCCCCCCCCC
20.68-
1689PhosphorylationSLSTCTKSGPSPLSS
CCCCCCCCCCCCCCC
37.4727087446
1692PhosphorylationTCTKSGPSPLSSPNG
CCCCCCCCCCCCCCC
41.8327087446
1695PhosphorylationKSGPSPLSSPNGKLT
CCCCCCCCCCCCCEE
47.3227087446
1696PhosphorylationSGPSPLSSPNGKLTV
CCCCCCCCCCCCEEE
30.0227087446
1702PhosphorylationSSPNGKLTVASPKRG
CCCCCCEEECCCCCC
19.9422345495
1705PhosphorylationNGKLTVASPKRGPKR
CCCEEECCCCCCCCH
26.9822942356
1734PhosphorylationSVPSTVISRVIGRGG
CCCHHHHHHHHCCCC
19.0319367708
1739MethylationVISRVIGRGGCNINA
HHHHHHCCCCCCHHH
27.49-
1821O-linked_GlycosylationIGSSAPTTTAANSSL
CCCCCCCCHHCCHHH
17.2430059200
1822O-linked_GlycosylationGSSAPTTTAANSSLM
CCCCCCCHHCCHHHC
26.6730059200
1834O-linked_GlycosylationSLMGIKMTTVALSST
HHCCCEEEEEEECCC
17.0830059200
1870Asymmetric dimethylarginineKNPVNNVRPGFPVSL
CCCCCCCCCCCCCCC
27.96-
1870MethylationKNPVNNVRPGFPVSL
CCCCCCCCCCCCCCC
27.9624129315
1934PhosphorylationPLSPARATNSPKPHM
CCCCCCCCCCCCCCC
30.5825266776
1936PhosphorylationSPARATNSPKPHMVP
CCCCCCCCCCCCCCC
29.9135098051
1997O-linked_GlycosylationVRRQLFVTVVKTSNA
HHHEEEEEEEECCCC
16.5530059200
2034PhosphorylationMPTAKEHYPVSSPSS
CCCCHHCCCCCCCCC
13.3525168779
2037PhosphorylationAKEHYPVSSPSSPSP
CHHCCCCCCCCCCCC
31.8427087446
2038PhosphorylationKEHYPVSSPSSPSPP
HHCCCCCCCCCCCCC
29.0927087446
2040PhosphorylationHYPVSSPSSPSPPAQ
CCCCCCCCCCCCCCC
57.7527087446
2041PhosphorylationYPVSSPSSPSPPAQP
CCCCCCCCCCCCCCC
32.5525521595
2043PhosphorylationVSSPSSPSPPAQPGG
CCCCCCCCCCCCCCC
45.5227087446
2052PhosphorylationPAQPGGVSRNSPLDC
CCCCCCCCCCCCCCC
29.0827742792
2055PhosphorylationPGGVSRNSPLDCGSA
CCCCCCCCCCCCCCC
26.2325521595
2061PhosphorylationNSPLDCGSASPNKGA
CCCCCCCCCCCCCCC
31.7221082442
2063PhosphorylationPLDCGSASPNKGASA
CCCCCCCCCCCCCCH
30.6125521595
2186O-linked_GlycosylationATAAPHKTPAPVQSS
CCCCCCCCCCCCCCC
22.9630059200
2193O-linked_GlycosylationTPAPVQSSSASVLNV
CCCCCCCCCCCEECC
16.9155410879
2373PhosphorylationNFNRQHFSPLSLLTP
CCCCCCCCCHHHEEC
23.8661948969
2376PhosphorylationRQHFSPLSLLTPCSS
CCCCCCHHHEECCCC
25.3926643407
2379PhosphorylationFSPLSLLTPCSSASN
CCCHHHEECCCCCCC
27.7826643407
2382O-linked_GlycosylationLSLLTPCSSASNESP
HHHEECCCCCCCCCC
30.0930059200
2382PhosphorylationLSLLTPCSSASNESP
HHHEECCCCCCCCCC
30.0926643407
2383PhosphorylationSLLTPCSSASNESPA
HHEECCCCCCCCCCC
42.2926643407
2388O-linked_GlycosylationCSSASNESPAQSVSS
CCCCCCCCCCCCCCC
29.7730059200
2401PhosphorylationSSGVRAPSPAPSSVP
CCCCCCCCCCCCCCC
32.4811165478
2405PhosphorylationRAPSPAPSSVPLGSE
CCCCCCCCCCCCCCC
46.1825168779
2406PhosphorylationAPSPAPSSVPLGSEK
CCCCCCCCCCCCCCC
27.0527742792
2411PhosphorylationPSSVPLGSEKPSSVS
CCCCCCCCCCCCCCC
50.5625619855
2415PhosphorylationPLGSEKPSSVSQDRK
CCCCCCCCCCCCCCC
55.2125619855
2416PhosphorylationLGSEKPSSVSQDRKV
CCCCCCCCCCCCCCC
34.0225619855
2418PhosphorylationSEKPSSVSQDRKVPV
CCCCCCCCCCCCCCC
28.4525619855
2489PhosphorylationPMIHRPMSDPGVFSQ
CCCCCCCCCCCCCCH
43.2530850165
2509PhosphorylationRDSTGIVTPSGTFHQ
CCCCCEECCCCCCCC
15.1515994051
2527UbiquitinationAGYMDFPKVGSMPFS
CCCCCCCCCCCCCCE
60.26-
2530PhosphorylationMDFPKVGSMPFSVYG
CCCCCCCCCCCEEEC
26.6951460021
2534PhosphorylationKVGSMPFSVYGNAML
CCCCCCCEEECCCCC
14.4625777480
2536PhosphorylationGSMPFSVYGNAMLPP
CCCCCEEECCCCCCC
11.9425777480
2561PhosphorylationPIFNGPHSAEPSWNS
CCCCCCCCCCCCHHH
37.1425777480
2565PhosphorylationGPHSAEPSWNSLIKM
CCCCCCCCHHHHHHH
30.3225777480
2568PhosphorylationSAEPSWNSLIKMVSS
CCCCCHHHHHHHHHC
25.8025777480
2574PhosphorylationNSLIKMVSSSTENNG
HHHHHHHHCCCCCCC
18.3129895711
2575PhosphorylationSLIKMVSSSTENNGP
HHHHHHHCCCCCCCC
29.8429895711
2596PhosphorylationPWAPHMNSVHMNQLG
CCCCCCCCCCHHCCC
13.0629895711

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 ANR17_MOUSE !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ANR17_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 ANR17_MOUSE !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of ANR17_MOUSE !!

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of ANR17_MOUSE

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Large scale localization of protein phosphorylation by use ofelectron capture dissociation mass spectrometry.";
Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
Mol. Cell. Proteomics 8:904-912(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2401, AND MASSSPECTROMETRY.
"The phagosomal proteome in interferon-gamma-activated macrophages.";
Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,Thibault P.;
Immunity 30:143-154(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2040, AND MASSSPECTROMETRY.
"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-1631, AND MASSSPECTROMETRY.
"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-2043, AND MASSSPECTROMETRY.

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