AXIN1_RAT - dbPTM
AXIN1_RAT - PTM Information in dbPTM
Basic Information of Protein
UniProt ID AXIN1_RAT
UniProt AC O70239
Protein Name Axin-1
Gene Name Axin1
Organism Rattus norvegicus (Rat).
Sequence Length 827
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 (By similarity).
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 beta-catenin to inhibit the Wnt signaling pathway and ventralize embryos, but also dorsalizes embryos by activating a Wnt-independent JNK signaling pathway (By similarity). Also facilitates the phosphorylation of APC by GSK3B (By similarity). Facilitates the phosphorylation of TP53 by HIPK2 upon ultraviolet irradiation (By similarity). Enhances TGF-beta signaling by recruiting the RNF111 E3 ubiquitin ligase and promoting the degradation of inhibitory SMAD7 (By similarity)..
Protein Sequence MNVQEQGFPLDLGASFTEDAPRPPVPGEEGELVSTDSRPVNHSFCSGKGTSIKSETSTATPRRSDLDLGYEPEGSASPTPPYLRWAESLHSLLDDQDGISLFRTFLKQEGCADLLDFWFACSGFRKLEPCDSNEEKRLKLARAIYRKYILDSNGIVSRQTKPATKSFIKDCVMKQQIDPAMFDQAQTEIQSTMEENTYPSFLKSDIYLEYTRTGSESPKVCSDQSSGSGTGKGMSGYLPTLNEDEEWKCDQDADEDDGRDSVPPSRLTQKLLLETAAPRAPSSRRYNEGRELRYGSWREPVNPYYVNSGYALAPATSANDSEQQSLSSDADTLSLTDSSVDGIPPYRIRKQHRREMQESVQVNGRVPLPHIPRTYRMPKEIRVEPQKFAEELIHRLEAVQRTREAEEKLEERLKRVRMEEEGEDGEMPSGPMASHKLPSVPAWHHFPPRYVDMGCSGLRDAHEENPESILDEHVQRVMRTPGCQSPGPGHRSPDSGHVAKTAVLGGTASGHGKHAPKLGLKLDSAGLHHHRHVHHHVHHNSARPKEQMEAEAARRVQSSFSWGPETHGHAKPRSYSESTGTNPSAGDLAFGGKASAPSKRNTKKAESGKNASAEVPSTTEDAEKNQKIMQWIIEGEKEISRHRKAGHGSSGMRKQQAHESSRPLSIERPGAVHPWVSAQLRNSVQPSHLFIQDPTMPPNPAPNPLTQLEEARRRLEEEEKRANKLPSKQRTKSQRKAGGGSAPPCDSIVVAYYFCGEPIPYRTLVRGRAVTLGQFKELLTKKGSYRYYFKKVSDEFDCGVVFEEVREDEAILPVFEEKIIGKVEKVD
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
43.7528689409
70PhosphorylationRSDLDLGYEPEGSAS
HHHCCCCCCCCCCCC
35.2928689409
75PhosphorylationLGYEPEGSASPTPPY
CCCCCCCCCCCCCCH
24.7422108457
77PhosphorylationYEPEGSASPTPPYLR
CCCCCCCCCCCCHHH
30.8828689409
79PhosphorylationPEGSASPTPPYLRWA
CCCCCCCCCCHHHHH
34.1123984901
82PhosphorylationSASPTPPYLRWAESL
CCCCCCCHHHHHHHH
15.3128689409
160PhosphorylationNGIVSRQTKPATKSF
CCCCCCCCCCCCHHH
37.5721738781
164PhosphorylationSRQTKPATKSFIKDC
CCCCCCCCHHHHHHH
35.4321738781
166PhosphorylationQTKPATKSFIKDCVM
CCCCCCHHHHHHHHH
28.0521738781
217PhosphorylationYTRTGSESPKVCSDQ
EEECCCCCCCEECCC
31.55-
222PhosphorylationSESPKVCSDQSSGSG
CCCCCEECCCCCCCC
41.4925575281
225PhosphorylationPKVCSDQSSGSGTGK
CCEECCCCCCCCCCC
41.4825575281
226PhosphorylationKVCSDQSSGSGTGKG
CEECCCCCCCCCCCC
31.2025575281
228PhosphorylationCSDQSSGSGTGKGMS
ECCCCCCCCCCCCCC
34.8225575281
230PhosphorylationDQSSGSGTGKGMSGY
CCCCCCCCCCCCCCC
37.1025575281
275PhosphorylationTQKLLLETAAPRAPS
HHHHHHHHCCCCCCC
28.2616641100
282PhosphorylationTAAPRAPSSRRYNEG
HCCCCCCCCCCCCCC
35.1816641100
283PhosphorylationAAPRAPSSRRYNEGR
CCCCCCCCCCCCCCC
21.5116641100
317PhosphorylationYALAPATSANDSEQQ
CEECCCCCCCHHHHH
27.47-
321PhosphorylationPATSANDSEQQSLSS
CCCCCCHHHHHHCCC
36.79-
325PhosphorylationANDSEQQSLSSDADT
CCHHHHHHCCCCCCC
29.88-
468PhosphorylationAHEENPESILDEHVQ
HHHHCHHHHHHHHHH
29.70-
480PhosphorylationHVQRVMRTPGCQSPG
HHHHHHCCCCCCCCC
13.1127097102
485PhosphorylationMRTPGCQSPGPGHRS
HCCCCCCCCCCCCCC
35.5827097102
492PhosphorylationSPGPGHRSPDSGHVA
CCCCCCCCCCCCCEE
27.6427097102
495PhosphorylationPGHRSPDSGHVAKTA
CCCCCCCCCCEEEEE
33.8927097102
509PhosphorylationAVLGGTASGHGKHAP
EECCCCCCCCCCCCC
31.03-
578PhosphorylationKPRSYSESTGTNPSA
CCCCCCCCCCCCCCC
26.62-
617PhosphorylationNASAEVPSTTEDAEK
CCCCCCCCCCCHHHH
53.8128689409
618PhosphorylationASAEVPSTTEDAEKN
CCCCCCCCCCHHHHH
28.3028689409
619PhosphorylationSAEVPSTTEDAEKNQ
CCCCCCCCCHHHHHH
35.8828689409
787PhosphorylationTKKGSYRYYFKKVSD
HHCCCEEEEEEEECC
12.67-

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-Uniprot
77SPhosphorylationKinaseCK1-Uniprot
217SPhosphorylationKinaseCK1-Uniprot
468SPhosphorylationKinaseCK1-Uniprot
480TPhosphorylationKinaseGSK3-BETAP18266
Uniprot
485SPhosphorylationKinaseGSK3-BETAP18266
Uniprot

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference
858KSumoylation

-
858Kubiquitylation

-
861KSumoylation

-
861Kubiquitylation

-

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_RAT !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
AXIN1_RATAxin1physical
10330181
DVL3_HUMANDVL3physical
10330181
GSK3B_HUMANGSK3Bphysical
10330181
CTNB1_HUMANCTNNB1physical
10330181
DVL1_HUMANDVL1physical
10330181
APC_HUMANAPCphysical
10330181
DVL1_RATDvl1physical
11113207

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of AXIN1_RAT

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Related Literatures of Post-Translational Modification

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