AXIN2_HUMAN - dbPTM
AXIN2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID AXIN2_HUMAN
UniProt AC Q9Y2T1
Protein Name Axin-2
Gene Name AXIN2
Organism Homo sapiens (Human).
Sequence Length 843
Subcellular Localization Cytoplasm.
Protein Description Inhibitor of the Wnt signaling pathway. Down-regulates beta-catenin. Probably facilitate the phosphorylation of beta-catenin and APC by GSK3B (By similarity)..
Protein Sequence MSSAMLVTCLPDPSSSFREDAPRPPVPGEEGETPPCQPGVGKGQVTKPMSVSSNTRRNEDGLGEPEGRASPDSPLTRWTKSLHSLLGDQDGAYLFRTFLEREKCVDTLDFWFACNGFRQMNLKDTKTLRVAKAIYKRYIENNSIVSKQLKPATKTYIRDGIKKQQIDSIMFDQAQTEIQSVMEENAYQMFLTSDIYLEYVRSGGENTAYMSNGGLGSLKVVCGYLPTLNEEEEWTCADFKCKLSPTVVGLSSKTLRATASVRSTETVDSGYRSFKRSDPVNPYHIGSGYVFAPATSANDSEISSDALTDDSMSMTDSSVDGIPPYRVGSKKQLQREMHRSVKANGQVSLPHFPRTHRLPKEMTPVEPATFAAELISRLEKLKLELESRHSLEERLQQIREDEEREGSELTLNSREGAPTQHPLSLLPSGSYEEDPQTILDDHLSRVLKTPGCQSPGVGRYSPRSRSPDHHHHHHSQYHSLLPPGGKLPPAAASPGACPLLGGKGFVTKQTTKHVHHHYIHHHAVPKTKEEIEAEATQRVHCFCPGGSEYYCYSKCKSHSKAPETMPSEQFGGSRGSTLPKRNGKGTEPGLALPAREGGAPGGAGALQLPREEGDRSQDVWQWMLESERQSKPKPHSAQSTKKAYPLESARSSPGERASRHHLWGGNSGHPRTTPRAHLFTQDPAMPPLTPPNTLAQLEEACRRLAEVSKPPKQRCCVASQQRDRNHSATVQTGATPFSNPSLAPEDHKEPKKLAGVHALQASELVVTYFFCGEEIPYRRMLKAQSLTLGHFKEQLSKKGNYRYYFKKASDEFACGAVFEEIWEDETVLPMYEGRILGKVERID
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
2Phosphorylation------MSSAMLVTC
------CCCCEEEEE		27.1424043423
3Phosphorylation-----MSSAMLVTCL
-----CCCCEEEEEC		19.1924043423
8PhosphorylationMSSAMLVTCLPDPSS
CCCCEEEEECCCCCC		12.3624043423
14PhosphorylationVTCLPDPSSSFREDA
EEECCCCCCCCCCCC		46.0924043423
15PhosphorylationTCLPDPSSSFREDAP
EECCCCCCCCCCCCC		38.5924043423
16PhosphorylationCLPDPSSSFREDAPR
ECCCCCCCCCCCCCC		32.4324043423
70PhosphorylationGEPEGRASPDSPLTR
CCCCCCCCCCCCHHH		28.0726657352
73PhosphorylationEGRASPDSPLTRWTK
CCCCCCCCCHHHHHH		25.7821712546
76PhosphorylationASPDSPLTRWTKSLH
CCCCCCHHHHHHHHH		27.7828985074
80UbiquitinationSPLTRWTKSLHSLLG
CCHHHHHHHHHHHHC		44.02-
125PhosphorylationRQMNLKDTKTLRVAK
CCCCCCCHHHHHHHH		25.0923025827
146PhosphorylationIENNSIVSKQLKPAT
HHCCCCCCCCCCCCC		17.02-
244PhosphorylationADFKCKLSPTVVGLS
HCCCCCCCCCEEECC		12.2027422710
246PhosphorylationFKCKLSPTVVGLSSK
CCCCCCCCEEECCCC		25.1728985074
251PhosphorylationSPTVVGLSSKTLRAT
CCCEEECCCCCEEEE		24.7029978859
252PhosphorylationPTVVGLSSKTLRATA
CCEEECCCCCEEEEC		34.4029978859
311PhosphorylationSDALTDDSMSMTDSS
CCCCCCCCCCCCCCC		18.63-
348PhosphorylationVKANGQVSLPHFPRT
HHHCCEECCCCCCCC		28.4429116813
376PhosphorylationTFAAELISRLEKLKL
HHHHHHHHHHHHHHH		43.3624719451
407PhosphorylationEDEEREGSELTLNSR
HHHHHHCCCCEECCC		25.3627422710
413PhosphorylationGSELTLNSREGAPTQ
CCCCEECCCCCCCCC		34.5228985074
428PhosphorylationHPLSLLPSGSYEEDP
CCCCCCCCCCCCCCC		40.1028348404
430PhosphorylationLSLLPSGSYEEDPQT
CCCCCCCCCCCCCCC		33.4429496963
449PhosphorylationHLSRVLKTPGCQSPG
HHHHHHCCCCCCCCC		22.2828188228
454PhosphorylationLKTPGCQSPGVGRYS
HCCCCCCCCCCCCCC		27.9128188228
460PhosphorylationQSPGVGRYSPRSRSP
CCCCCCCCCCCCCCC		19.6625841592
461PhosphorylationSPGVGRYSPRSRSPD
CCCCCCCCCCCCCCC		16.6928188228
493PhosphorylationKLPPAAASPGACPLL
CCCHHHCCCCCCCCC		21.0923312004
528UbiquitinationHHAVPKTKEEIEAEA
CCCCCCCHHHHHHHH		60.52-
549PhosphorylationFCPGGSEYYCYSKCK
ECCCCCEEEEEECCC		10.6722817900
630PhosphorylationMLESERQSKPKPHSA
HHHHHHHCCCCCCCC		58.0917924679
633AcetylationSERQSKPKPHSAQST
HHHHCCCCCCCCCCC		60.137677977
639PhosphorylationPKPHSAQSTKKAYPL
CCCCCCCCCCCCCCH		41.7417924679
640PhosphorylationKPHSAQSTKKAYPLE
CCCCCCCCCCCCCHH		25.2017924679
644PhosphorylationAQSTKKAYPLESARS
CCCCCCCCCHHHHCC		19.7529759185
648PhosphorylationKKAYPLESARSSPGE
CCCCCHHHHCCCCCC		36.3429759185
651PhosphorylationYPLESARSSPGERAS
CCHHHHCCCCCCHHH		40.3726699800
652PhosphorylationPLESARSSPGERASR
CHHHHCCCCCCHHHH		31.2226699800
680PhosphorylationTPRAHLFTQDPAMPP
CCCCEECCCCCCCCC		38.1223663014
689PhosphorylationDPAMPPLTPPNTLAQ
CCCCCCCCCCCHHHH		42.3423663014
693PhosphorylationPPLTPPNTLAQLEEA
CCCCCCCHHHHHHHH		29.2823663014
792AcetylationSLTLGHFKEQLSKKG
HCCCHHHHHHHHHCC		38.5920167786
797AcetylationHFKEQLSKKGNYRYY
HHHHHHHHCCCCEEE		73.6020167786
806AcetylationGNYRYYFKKASDEFA
CCCEEEEEECCCCCC		31.1620167786
838UbiquitinationYEGRILGKVERID--
CCCEEEEEEEECC--		37.1621890473
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
311SPhosphorylationKinasePLK1P53350
PSP
-KUbiquitinationE3 ubiquitin ligaseCDC20Q12834
PMID:22322943
-KUbiquitinationE3 ubiquitin ligaseRNF146Q9NTX7
PMID:21383061
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of AXIN2_HUMAN !!
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 AXIN2_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
APCL_HUMANAPC2physical
10021369
CTNB1_HUMANCTNNB1physical
10966653
APC_HUMANAPCphysical
10966653
GSK3B_HUMANGSK3Bphysical
10966653
ANKR6_HUMANANKRD6physical
12183362
GSK3B_HUMANGSK3Bphysical
12183362
CDC20_HUMANCDC20physical
22322943
RN146_HUMANRNF146physical
21478859
SMAD7_HUMANSMAD7physical
24584437
RNF12_HUMANRLIMphysical
24584437
RN111_HUMANRNF111physical
24584437
M3K2_HUMANMAP3K2physical
26884171
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
114500Colorectal cancer (CRC)
608615Oligodontia-colorectal cancer syndrome (ODCRCS)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of AXIN2_HUMAN

loading...

Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Improved titanium dioxide enrichment of phosphopeptides from HeLacells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra.";
Yu L.-R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.;
J. Proteome Res. 6:4150-4162(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-630; SER-639 ANDTHR-640, AND MASS SPECTROMETRY.

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