AXIN1_HUMAN - dbPTM
AXIN1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID AXIN1_HUMAN
UniProt AC O15169
Protein Name Axin-1
Gene Name AXIN1
Organism Homo sapiens (Human).
Sequence Length 862
Subcellular Localization Cytoplasm . Nucleus . Membrane . Cell membrane . MACF1 is required for its translocation to cell membrane (By similarity). On UV irradiation, translocates to the nucleus and colocalizes with DAAX (PubMed:17210684).
Protein Description Component of the beta-catenin destruction complex required for regulating CTNNB1 levels through phosphorylation and ubiquitination, and modulating Wnt-signaling. [PubMed: 12192039]
Protein Sequence MNIQEQGFPLDLGASFTEDAPRPPVPGEEGELVSTDPRPASYSFCSGKGVGIKGETSTATPRRSDLDLGYEPEGSASPTPPYLKWAESLHSLLDDQDGISLFRTFLKQEGCADLLDFWFACTGFRKLEPCDSNEEKRLKLARAIYRKYILDNNGIVSRQTKPATKSFIKGCIMKQLIDPAMFDQAQTEIQATMEENTYPSFLKSDIYLEYTRTGSESPKVCSDQSSGSGTGKGISGYLPTLNEDEEWKCDQDMDEDDGRDAAPPGRLPQKLLLETAAPRVSSSRRYSEGREFRYGSWREPVNPYYVNAGYALAPATSANDSEQQSLSSDADTLSLTDSSVDGIPPYRIRKQHRREMQESVQVNGRVPLPHIPRTYRVPKEVRVEPQKFAEELIHRLEAVQRTREAEEKLEERLKRVRMEEEGEDGDPSSGPPGPCHKLPPAPAWHHFPPRCVDMGCAGLRDAHEENPESILDEHVQRVLRTPGRQSPGPGHRSPDSGHVAKMPVALGGAASGHGKHVPKSGAKLDAAGLHHHRHVHHHVHHSTARPKEQVEAEATRRAQSSFAWGLEPHSHGARSRGYSESVGAAPNASDGLAHSGKVGVACKRNAKKAESGKSASTEVPGASEDAEKNQKIMQWIIEGEKEISRHRRTGHGSSGTRKPQPHENSRPLSLEHPWAGPQLRTSVQPSHLFIQDPTMPPHPAPNPLTQLEEARRRLEEEEKRASRAPSKQRYVQEVMRRGRACVRPACAPVLHVVPAVSDMELSETETRSQRKVGGGSAQPCDSIVVAYYFCGEPIPYRTLVRGRAVTLGQFKELLTKKGSYRYYFKKVSDEFDCGVVFEEVREDEAVLPVFEEKIIGKVEKVD
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
42PhosphorylationTDPRPASYSFCSGKG
CCCCCCCEEECCCCC
14.1027642862
58PhosphorylationGIKGETSTATPRRSD
CCCCCCCCCCCCHHH
41.8023312004
60PhosphorylationKGETSTATPRRSDLD
CCCCCCCCCCHHHCC
19.8828985074
64PhosphorylationSTATPRRSDLDLGYE
CCCCCCHHHCCCCCC
43.7523403867
70PhosphorylationRSDLDLGYEPEGSAS
HHHCCCCCCCCCCCC
35.2923403867
75PhosphorylationLGYEPEGSASPTPPY
CCCCCCCCCCCCCCH
24.7425159151
77PhosphorylationYEPEGSASPTPPYLK
CCCCCCCCCCCCHHH
30.8825159151
77 (in isoform 2)Phosphorylation-30.88-
79PhosphorylationPEGSASPTPPYLKWA
CCCCCCCCCCHHHHH
34.1125159151
82PhosphorylationSASPTPPYLKWAESL
CCCCCCCHHHHHHHH
23.3228176443
148PhosphorylationARAIYRKYILDNNGI
HHHHHHHHHHHCCCC
9.5618491316
148 (in isoform 2)Phosphorylation-9.56-
160 (in isoform 2)Phosphorylation-37.57-
160PhosphorylationNGIVSRQTKPATKSF
CCCCCCCCCHHCHHH
37.5718491316
166PhosphorylationQTKPATKSFIKGCIM
CCCHHCHHHHHHHHH
28.0524719451
200PhosphorylationMEENTYPSFLKSDIY
HHHCCCHHHHCCCEE
32.5624719451
213 (in isoform 2)Phosphorylation-36.94-
213PhosphorylationIYLEYTRTGSESPKV
EEEEEEECCCCCCCE
36.9428450419
215PhosphorylationLEYTRTGSESPKVCS
EEEEECCCCCCCEEC
34.0025849741
217 (in isoform 2)Phosphorylation-31.55-
217PhosphorylationYTRTGSESPKVCSDQ
EEECCCCCCCEECCC
31.5523401153
222DephosphorylationSESPKVCSDQSSGSG
CCCCCEECCCCCCCC
41.4917318175
222PhosphorylationSESPKVCSDQSSGSG
CCCCCEECCCCCCCC
41.4923403867
225PhosphorylationPKVCSDQSSGSGTGK
CCEECCCCCCCCCCC
41.4823403867
226PhosphorylationKVCSDQSSGSGTGKG
CEECCCCCCCCCCCC
31.2023403867
228PhosphorylationCSDQSSGSGTGKGIS
ECCCCCCCCCCCCCC
34.8223403867
230PhosphorylationDQSSGSGTGKGISGY
CCCCCCCCCCCCCCC
37.1023403867
281PhosphorylationETAAPRVSSSRRYSE
HHCCCCCCCCCCCCC
24.7126437602
282PhosphorylationTAAPRVSSSRRYSEG
HCCCCCCCCCCCCCC
25.6320068231
283PhosphorylationAAPRVSSSRRYSEGR
CCCCCCCCCCCCCCC
17.1720068231
387UbiquitinationEVRVEPQKFAEELIH
CCCCCHHHHHHHHHH
58.20-
469PhosphorylationAHEENPESILDEHVQ
HHHHCHHHHHHHHHH
29.7020873877
481PhosphorylationHVQRVLRTPGRQSPG
HHHHHHCCCCCCCCC
26.4026055452
486PhosphorylationLRTPGRQSPGPGHRS
HCCCCCCCCCCCCCC
30.3923401153
493 (in isoform 2)Phosphorylation-27.64-
493PhosphorylationSPGPGHRSPDSGHVA
CCCCCCCCCCCCCCC
27.6423401153
496PhosphorylationPGHRSPDSGHVAKMP
CCCCCCCCCCCCCCC
33.8920873877
511PhosphorylationVALGGAASGHGKHVP
EEECCCCCCCCCCCC
30.6825159151
542PhosphorylationVHHHVHHSTARPKEQ
CCCCCCCCCCCHHHH
14.6422798277
560PhosphorylationEATRRAQSSFAWGLE
HHHHHHHHHHHHCCC
26.8328555341
561PhosphorylationATRRAQSSFAWGLEP
HHHHHHHHHHHCCCC
13.6020873877
570PhosphorylationAWGLEPHSHGARSRG
HHCCCCCCCCHHHCC
34.0420873877
575PhosphorylationPHSHGARSRGYSESV
CCCCCHHHCCCCCCC
29.5325159151
576MethylationHSHGARSRGYSESVG
CCCCHHHCCCCCCCC
42.38-
578PhosphorylationHGARSRGYSESVGAA
CCHHHCCCCCCCCCC
14.2529978859
579PhosphorylationGARSRGYSESVGAAP
CHHHCCCCCCCCCCC
26.6429978859
581PhosphorylationRSRGYSESVGAAPNA
HHCCCCCCCCCCCCC
21.6525159151
589PhosphorylationVGAAPNASDGLAHSG
CCCCCCCCCCCCCCC
38.5623312004
595PhosphorylationASDGLAHSGKVGVAC
CCCCCCCCCCHHHHC
34.4023186163
611PhosphorylationRNAKKAESGKSASTE
HCHHHCCCCCCCCCC
57.28-
614 (in isoform 2)Phosphorylation-30.86-
614PhosphorylationKKAESGKSASTEVPG
HHCCCCCCCCCCCCC
30.8610581160
616PhosphorylationAESGKSASTEVPGAS
CCCCCCCCCCCCCCC
31.99-
617PhosphorylationESGKSASTEVPGASE
CCCCCCCCCCCCCCC
40.49-
623PhosphorylationSTEVPGASEDAEKNQ
CCCCCCCCCCHHHHH
41.76-
644PhosphorylationIEGEKEISRHRRTGH
HHCCHHHHCCCCCCC
24.1127251275
665PhosphorylationKPQPHENSRPLSLEH
CCCCCCCCCCCCCCC
32.0825690035
730PhosphorylationRAPSKQRYVQEVMRR
CCCHHHHHHHHHHHH
12.1824043423
787PhosphorylationCDSIVVAYYFCGEPI
CCEEEEEEEECCCCC
5.8622817900
788PhosphorylationDSIVVAYYFCGEPIP
CEEEEEEEECCCCCC
5.2222817900
789 (in isoform 2)Ubiquitination-2.55-
796PhosphorylationFCGEPIPYRTLVRGR
ECCCCCCHHHHCCCC
19.5622817900
806PhosphorylationLVRGRAVTLGQFKEL
HCCCCEEEHHHHHHH
24.9624043423
821 (in isoform 2)Ubiquitination-22.75-
821 (in isoform 2)Sumoylation-22.75-
857SumoylationFEEKIIGKVEKVD--
HHHHHCCEEEECC--
36.4912223491
857SumoylationFEEKIIGKVEKVD--
HHHHHCCEEEECC--
36.49-
860SumoylationKIIGKVEKVD-----
HHCCEEEECC-----
55.4812223491
860SumoylationKIIGKVEKVD-----
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
75SPhosphorylationKinaseCK1-FAMILY-GPS
75SPhosphorylationKinaseCK1-Uniprot
77SPhosphorylationKinaseCK1-FAMILY-GPS
77SPhosphorylationKinaseCK1-Uniprot
217SPhosphorylationKinaseCK1-FAMILY-GPS
217SPhosphorylationKinaseCK1-Uniprot
469SPhosphorylationKinaseCK1-FAMILY-GPS
469SPhosphorylationKinaseCK1-Uniprot
481TPhosphorylationKinaseCDK5Q00535
PSP
481TPhosphorylationKinaseGSK3-BETAP49841
Uniprot
-KUbiquitinationE3 ubiquitin ligaseSMURF2Q9HAU4
PMID:20858899
-KUbiquitinationE3 ubiquitin ligaseSMURF1Q9HCE7
PMID:23959799
-KUbiquitinationE3 ubiquitin ligaseRNF146Q9NTX7
PMID:21478859

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference
48Kubiquitylation

21383061
857KSumoylation

18632848
857Kubiquitylation

18632848
860KSumoylation

18632848
860Kubiquitylation

18632848

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_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
GSK3B_HUMANGSK3Bphysical
9734785
CTNB1_HUMANCTNNB1physical
9734785
APC_HUMANAPCphysical
9734785
CTNB1_HUMANCTNNB1physical
12805222
DVL3_HUMANDVL3physical
12805222
AXIN1_HUMANAXIN1physical
16169070
GAK_HUMANGAKphysical
16169070
UT14A_HUMANUTP14Aphysical
16169070
AN32A_HUMANANP32Aphysical
16169070
DPYL1_HUMANCRMP1physical
16169070
EF1A1_HUMANEEF1A1physical
16169070
LRP5_HUMANLRP5physical
11336703
KC1E_HUMANCSNK1Egenetic
11884395
KC1A_HUMANCSNK1A1genetic
11884395
AXIN1_HUMANAXIN1physical
11884395
GSK3B_HUMANGSK3Bphysical
12511557
TSC1_HUMANTSC1physical
12511557
TSC2_HUMANTSC2physical
12511557
M3K1_HUMANMAP3K1physical
10829020
DVL2_HUMANDVL2physical
10829020
LRP5_HUMANLRP5physical
18632848
DVL1_HUMANDVL1physical
18632848
CTNB1_HUMANCTNNB1physical
16199882
GSK3B_HUMANGSK3Bphysical
16199882
APC_HUMANAPCphysical
16199882
DAXX_HUMANDAXXphysical
17210684
GSK3_CAEELgsk-3physical
17601533
GSK3B_HUMANGSK3Bphysical
17601533
CTNB1_HUMANCTNNB1physical
12421363
AXIN1_HUMANAXIN1physical
18632848
CTNB1_HUMANCTNNB1physical
18632848
GSK3B_HUMANGSK3Bphysical
18632848
FBW1A_HUMANBTRCphysical
10228155
APC_HUMANAPCphysical
10228155
ANM1_HUMANPRMT1physical
21242974
GSK3B_HUMANGSK3Bphysical
21242974
MYC_HUMANMYCphysical
19131971
GSK3A_HUMANGSK3Aphysical
19131971
GSK3B_HUMANGSK3Bphysical
19131971
2A5A_HUMANPPP2R5Aphysical
19131971
PIN1_HUMANPIN1physical
19131971
PP2AA_HUMANPPP2CAphysical
19131971
CTNB1_HUMANCTNNB1physical
19131971
GSK3B_HUMANGSK3Bphysical
21502811
PML_HUMANPMLphysical
21057547
P53_HUMANTP53physical
21057547
HIPK2_HUMANHIPK2physical
21057547
SMUF2_HUMANSMURF2physical
20858899
GSK3B_HUMANGSK3Bphysical
22270359
CTNB1_HUMANCTNNB1physical
22509369
GSK3B_HUMANGSK3Bphysical
22509369
HD_HUMANHTTphysical
20531388
CTNB1_HUMANCTNNB1physical
20531388
APC_HUMANAPCphysical
20128690
CTNB1_HUMANCTNNB1physical
20128690
AMER1_HUMANAMER1physical
20128690
AXIN2_HUMANAXIN2physical
20128690
M3K1_HUMANMAP3K1physical
20128690
GSK3B_HUMANGSK3Bphysical
20128690
LRP6_HUMANLRP6physical
20128690
DVL3_HUMANDVL3physical
20128690
SKI_HUMANSKIphysical
21795712
SKIL_HUMANSKILphysical
21795712
CTNB1_HUMANCTNNB1physical
18593713
GSK3B_HUMANGSK3Bphysical
18593713
NCK2_HUMANNCK2physical
11557983
GSK3B_HUMANGSK3Bphysical
17318175
APC_HUMANAPCphysical
22682247
LRP6_HUMANLRP6physical
22682247
DVL3_HUMANDVL3physical
22682247
GSK3B_HUMANGSK3Bphysical
22682247
CTNB1_HUMANCTNNB1physical
22682247
UBC_HUMANUBCphysical
22682247
FBW1A_HUMANBTRCphysical
22682247
GSK3B_HUMANGSK3Bphysical
19202075
ARRB1_HUMANARRB1physical
19202075
LRP6_HUMANLRP6physical
16890161
CTNB1_HUMANCTNNB1physical
16890161
GSK3B_HUMANGSK3Bphysical
16890161
CAV1_HUMANCAV1physical
16890161
TNAP3_HUMANTNFAIP3physical
23671587
P53_HUMANTP53physical
23826318
CTNB1_HUMANCTNNB1physical
23959799
GSK3A_HUMANGSK3Aphysical
23959799
GSK3B_HUMANGSK3Bphysical
23959799
LRP6_HUMANLRP6physical
23959799
KC1E_HUMANCSNK1Ephysical
21988832
GSK3B_HUMANGSK3Bphysical
21988832
RBTN2_HUMANLMO2physical
21988832
MYOTI_HUMANMYOTphysical
21988832
SMUF1_HUMANSMURF1physical
24700460
GNAS3_HUMANGNASphysical
16293724
GNAS2_HUMANGNASphysical
16293724
ALEX_HUMANGNASphysical
16293724
GNAS1_HUMANGNASphysical
16293724
GSK3B_HUMANGSK3Bphysical
16293724
P53_HUMANTP53genetic
23826318
HIPK2_HUMANHIPK2physical
23826318
APC_HUMANAPCphysical
26496610
KC1A_HUMANCSNK1A1physical
26496610
KC1D_HUMANCSNK1Dphysical
26496610
KC1E_HUMANCSNK1Ephysical
26496610
CTNA1_HUMANCTNNA1physical
26496610
CTNB1_HUMANCTNNB1physical
26496610
GSK3B_HUMANGSK3Bphysical
26496610
PLAK_HUMANJUPphysical
26496610
PUF60_HUMANPUF60physical
26496610
GAPD1_HUMANGAPVD1physical
26496610
RHG21_HUMANARHGAP21physical
26496610
AMER1_HUMANAMER1physical
26496610
M3K2_HUMANMAP3K2physical
26884171
GSK3A_HUMANGSK3Aphysical
26912724
GSK3B_HUMANGSK3Bphysical
26912724
FOXM1_HUMANFOXM1physical
26912724
APC_HUMANAPCphysical
29045831
CTNB1_HUMANCTNNB1physical
29045831
GSK3B_HUMANGSK3Bphysical
29045831
UBP7_HUMANUSP7physical
29045831
FBW1A_HUMANBTRCphysical
29045831

Drug and Disease Associations
Kegg Disease
H00048 Hepatocellular carcinoma
H00934 Caudal duplication anomaly
OMIM Disease
114550Hepatocellular carcinoma (HCC)
607864Caudal duplication anomaly (CADUA)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of AXIN1_HUMAN

loading...

Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Protein phosphatase 1 regulates assembly and function of the beta-catenin degradation complex.";
Luo W., Peterson A., Garcia B.A., Coombs G., Kofahl B., Heinrich R.,Shabanowitz J., Hunt D.F., Yost H.J., Virshup D.M.;
EMBO J. 26:1511-1521(2007).
Cited for: PHOSPHORYLATION AT SER-75; SER-77; SER-217 AND SER-469, MASSSPECTROMETRY, AND INTERACTION WITH GSK3B AND PPP1CA.

TOP