AXIN1_MOUSE - dbPTM
AXIN1_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID AXIN1_MOUSE
UniProt AC O35625
Protein Name Axin-1
Gene Name Axin1
Organism Mus musculus (Mouse).
Sequence Length 863
Subcellular Localization Cytoplasm . Nucleus . Cell membrane . Membrane . On UV irradiation, translocates to the nucleus and colocalizes with DAAX (By similarity). MACF1 is required for its translocation to cell membrane (PubMed:16815997).
Protein Description Component of the beta-catenin destruction complex required for regulating CTNNB1 levels through phosphorylation and ubiquitination, and modulating Wnt-signaling (By similarity). Controls dorsoventral patterning via two opposing effects; down-regulates CTNNB1 to inhibit the Wnt signaling pathway and ventralize embryos, but also dorsalizes embryos by activating a Wnt-independent JNK signaling pathway. In Wnt signaling, probably facilitates the phosphorylation of CTNNB1 and APC by GSK3B. Likely to function as a tumor suppressor. Facilitates the phosphorylation of TP53 by HIPK2 upon ultraviolet irradiation. Enhances TGF-beta signaling by recruiting the RNF111 E3 ubiquitin ligase and promoting the degradation of inhibitory SMAD7 (By similarity). Also component of the AXIN1-HIPK2-TP53 complex which controls cell growth, apoptosis and development..
Protein Sequence MNVQEQGFPLDLGASFTEDAPRPPVPGEEGELVSTDSRPVNHSFCSGKGTSIKSETSTATPRRSDLDLGYEPEGSASPTPPYLRWAESLHSLLDDQDGISLFRTFLKQEGCADLLDFWFACSGFRKLEPCDSNEEKRLKLARAIYRKYILDSNGIVSRQTKPATKSFIKDCVMKQQIDPAMFDQAQTEIQSTMEENTYPSFLKSDIYLEYTRTGSESPKVCSDQSSGSGTGKGMSGYLPTLNEDEEWKCDQDADEDDGRDPLPPSRLTQKLLLETAAPRAPSSRRYNEGRELRYGSWREPVNPYYVNSGYALAPATSANDSEQQSLSSDADTLSLTDSSVDGIPPYRIRKQHRREMQESIQVNGRVPLPHIPRTYRMPKEIRVEPQKFAEELIHRLEAVQRTREAEEKLEERLKRVRMEEEGEDGEMPSGPMASHKLPSVPAWHHFPPRYVDMGCSGLRDAHEENPESILDEHVQRVMRTPGCQSPGPGHRSPDSGHVAKTAVLGGTASGHGKHVPKLGLKLDTAGLHHHRHVHHHVHHNSARPKEQMEAEVARRVQSSFSWGPETHGHAKPRSYSENAGTTLSAGDLAFGGKTSAPSKRNTKKAESGKNANAEVPSTTEDAEKNQKIMQWIIEGEKEISRHRKAGHGSSGLRKQQAHESSRPLSIERPGAVHPWVSAQLRNSVQPSHLFIQDPTMPPNPAPNPLTQLEEARRRLEEEEKRANKLPSKQRYVQAVMQRGRTCVRPACAPVLSVVPAVSDLELSETETKSQRKAGGGSAPPCDSIVVAYYFCGEPIPYRTLVRGRAVTLGQFKELLTKKGSYRYYFKKVSDEFDCGVVFEEVREDEAVLPVFEEKIIGKVEKVD
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
64PhosphorylationSTATPRRSDLDLGYE
CCCCCCHHHCCCCCC		43.7525619855
70PhosphorylationRSDLDLGYEPEGSAS
HHHCCCCCCCCCCCC		35.2925619855
75PhosphorylationLGYEPEGSASPTPPY
CCCCCCCCCCCCCCH		24.7427149854
77PhosphorylationYEPEGSASPTPPYLR
CCCCCCCCCCCCHHH		30.8825521595
79PhosphorylationPEGSASPTPPYLRWA
CCCCCCCCCCHHHHH		34.1122942356
82PhosphorylationSASPTPPYLRWAESL
CCCCCCCHHHHHHHH		15.3125619855
145PhosphorylationLKLARAIYRKYILDS
HHHHHHHHHHHHHCC		10.4821454597
152PhosphorylationYRKYILDSNGIVSRQ
HHHHHHCCCCCCCCC		33.2525367039
157PhosphorylationLDSNGIVSRQTKPAT
HCCCCCCCCCCCCCC		19.4225367039
160PhosphorylationNGIVSRQTKPATKSF
CCCCCCCCCCCCHHH		37.57-
213PhosphorylationIYLEYTRTGSESPKV
EEEEEEECCCCCCCE		36.9419060867
215PhosphorylationLEYTRTGSESPKVCS
EEEEECCCCCCCEEC		34.0026160508
217PhosphorylationYTRTGSESPKVCSDQ
EEECCCCCCCEECCC		31.5526160508
222PhosphorylationSESPKVCSDQSSGSG
CCCCCEECCCCCCCC		41.4923984901
225PhosphorylationPKVCSDQSSGSGTGK
CCEECCCCCCCCCCC		41.4825777480
282PhosphorylationTAAPRAPSSRRYNEG
HCCCCCCCCCCCCCC		35.1820531401
283PhosphorylationAAPRAPSSRRYNEGR
CCCCCCCCCCCCCCC		21.5120531401
374PhosphorylationPLPHIPRTYRMPKEI
CCCCCCCCCCCCCCE		15.3229895711
375PhosphorylationLPHIPRTYRMPKEIR
CCCCCCCCCCCCCEE		13.2429895711
429PhosphorylationGEDGEMPSGPMASHK
CCCCCCCCCCCCCCC		54.9729899451
468PhosphorylationAHEENPESILDEHVQ
HHHHCHHHHHHHHHH		29.70-
480PhosphorylationHVQRVMRTPGCQSPG
HHHHHHCCCCCCCCC		13.1127087446
485PhosphorylationMRTPGCQSPGPGHRS
HCCCCCCCCCCCCCC		35.5827087446
492PhosphorylationSPGPGHRSPDSGHVA
CCCCCCCCCCCCCEE		27.6427087446
495PhosphorylationPGHRSPDSGHVAKTA
CCCCCCCCCCEEEEE		33.8925159016
509PhosphorylationAVLGGTASGHGKHVP
EECCCCCCCCCCCCC		31.03-
517AcetylationGHGKHVPKLGLKLDT
CCCCCCCCCCCEECC		54.8421728379
777PhosphorylationQRKAGGGSAPPCDSI
HHHCCCCCCCCCCCE		40.66-
783PhosphorylationGSAPPCDSIVVAYYF
CCCCCCCCEEEEEEE		24.81-
797PhosphorylationFCGEPIPYRTLVRGR
ECCCCCCHHHHCCCC		19.56-
858UbiquitinationFEEKIIGKVEKVD--
HHHHHCCEEEECC--		36.49PubMed
858SumoylationFEEKIIGKVEKVD--
HHHHHCCEEEECC--		36.4918632848
858SumoylationFEEKIIGKVEKVD--
HHHHHCCEEEECC--		36.49-
861UbiquitinationKIIGKVEKVD-----
HHCCEEEECC-----		55.48PubMed
861SumoylationKIIGKVEKVD-----
HHCCEEEECC-----		55.4818632848
861SumoylationKIIGKVEKVD-----
HHCCEEEECC-----		55.48-
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
77SPhosphorylationKinaseCK1-Uniprot
157SPhosphorylationKinasePLK1P53350
PSP
468SPhosphorylationKinaseCK1-Uniprot
480TPhosphorylationKinaseCDK5P49615
PSP
480TPhosphorylationKinaseGSK3BQ9WV60
PSP
485SPhosphorylationKinaseGSK3BQ9WV60
PSP
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference
858KSumoylation

12223491
858Kubiquitylation

12223491
861KSumoylation

12223491
861Kubiquitylation

12223491
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 AXIN1_MOUSE !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
CTNB1_HUMANCTNNB1physical
10330403
GSK3B_HUMANGSK3Bphysical
10330403
APCL_HUMANAPC2physical
10330403
APC_XENLAapcphysical
10330403
CADH2_MOUSECdh2physical
19075000
LRP5_MOUSELrp5physical
19075000
RN111_MOUSERnf111physical
16601693
SMAD3_MOUSESmad3physical
16601693
SMAD6_MOUSESmad6physical
16601693
SMAD7_MOUSESmad7physical
16601693
RN111_MOUSERnf111genetic
16601693
CTNB1_MOUSECtnnb1genetic
19204372
DVL1_MOUSEDvl1genetic
14734535
GSK3B_MOUSEGsk3bphysical
14734535
AXIN1_MOUSEAxin1physical
9920888
PP2AA_MOUSEPpp2caphysical
9920888
2AAA_MOUSEPpp2r1aphysical
9920888
GSK3B_MOUSEGsk3bphysical
10318824
M3K4_MOUSEMap3k4physical
12878610
M3K4_MOUSEMap3k4genetic
12878610
AXIN1_MOUSEAxin1physical
15579909
DVL2_MOUSEDvl2physical
15579909
CTNB1_MOUSECtnnb1physical
17053159
KIF3A_MOUSEKif3aphysical
22473005
P53_MOUSETrp53physical
15526030
HIPK2_MOUSEHipk2physical
15526030
GSK3B_MOUSEGsk3bphysical
22682247
CTNB1_MOUSECtnnb1physical
22682247
ANM1_MOUSEPrmt1physical
21242974
GSK3B_MOUSEGsk3bphysical
21242974
CTNB1_MOUSECtnnb1physical
21242974
PIAS1_MOUSEPias1physical
12223491
PIAS2_MOUSEPias2physical
12223491
PIAS4_MOUSEPias4physical
12223491
AXIN1_MOUSEAxin1physical
12223491
AXIN1_MOUSEAxin1physical
18316368
GSK3B_MOUSEGsk3bphysical
18316368
CTNB1_MOUSECtnnb1physical
18316368
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of AXIN1_MOUSE

loading...

Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"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-492, AND MASSSPECTROMETRY.
"A GSK3beta phosphorylation site in axin modulates interaction withbeta-catenin and Tcf-mediated gene expression.";
Jho E., Lomvardas S., Costantini F.;
Biochem. Biophys. Res. Commun. 266:28-35(1999).
Cited for: PHOSPHORYLATION AT THR-480; SER-485 AND SER-492, INTERACTION WITHCTNNB1, AND MUTAGENESIS OF THR-480; SER-485; SER-492 AND SER-495.
Sumoylation
ReferencePubMed
"SUMOylation target sites at the C terminus protect Axin fromubiquitination and confer protein stability.";
Kim M.J., Chia I.V., Costantini F.;
FASEB J. 22:3785-3794(2008).
Cited for: SUMOYLATION AT LYS-858 AND LYS-861, AND MUTAGENESIS OF LYS-858 ANDLYS-861.
"SUMO-1 modification of the C-terminal KVEKVD of Axin is required forJNK activation but has no effect on Wnt signaling.";
Rui H.L., Fan E., Zhou H.M., Xu Z., Zhang Y., Lin S.C.;
J. Biol. Chem. 277:42981-42986(2002).
Cited for: SUMOYLATION AT LYS-858 AND LYS-861, INTERACTION WITH MAP3K1; SUMO1;PIAS1; PIAS2 AND PIAS4, FUNCTION, HOMODIMERIZATION, AND MUTAGENESIS OF858-LYS--ASP-863.

TOP
© 2024 Institute of Bioinformatics and Systems Biology, NYCU | Designed by : BiOmics Laboratory