SMAD2_MOUSE - dbPTM
SMAD2_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID SMAD2_MOUSE
UniProt AC Q62432
Protein Name Mothers against decapentaplegic homolog 2
Gene Name Smad2
Organism Mus musculus (Mouse).
Sequence Length 467
Subcellular Localization Cytoplasm . Nucleus . Cytoplasmic and nuclear in the absence of TGF-beta. On TGF-beta stimulation, migrates to the nucleus when complexed with SMAD4. On dephosphorylation by phosphatase PPM1A, released from the SMAD2/SMAD4 complex, and exported out o
Protein Description Receptor-regulated SMAD (R-SMAD) that is an intracellular signal transducer and transcriptional modulator activated by TGF-beta (transforming growth factor) and activin type 1 receptor kinases. Binds the TRE element in the promoter region of many genes that are regulated by TGF-beta and, on formation of the SMAD2/SMAD4 complex, activates transcription. May act as a tumor suppressor in colorectal carcinoma. Positively regulates PDPK1 kinase activity by stimulating its dissociation from the 14-3-3 protein YWHAQ which acts as a negative regulator (By similarity)..
Protein Sequence MSSILPFTPPVVKRLLGWKKSAGGSGGAGGGEQNGQEEKWCEKAVKSLVKKLKKTGRLDELEKAITTQNCNTKCVTIPSTCSEIWGLSTANTVDQWDTTGLYSFSEQTRSLDGRLQVSHRKGLPHVIYCRLWRWPDLHSHHELKAIENCEYAFNLKKDEVCVNPYHYQRVETPVLPPVLVPRHTEILTELPPLDDYTHSIPENTNFPAGIEPQSNYIPETPPPGYISEDGETSDQQLNQSMDTGSPAELSPTTLSPVNHSLDLQPVTYSEPAFWCSIAYYELNQRVGETFHASQPSLTVDGFTDPSNSERFCLGLLSNVNRNATVEMTRRHIGRGVRLYYIGGEVFAECLSDSAIFVQSPNCNQRYGWHPATVCKIPPGCNLKIFNNQEFAALLAQSVNQGFEAVYQLTRMCTIRMSFVKGWGAEYRRQTVTSTPCWIELHLNGPLQWLDKVLTQMGSPSVRCSSMS
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------MSSILPFTP
------CCCCCCCCH		26.5325619855
2Acetylation------MSSILPFTP
------CCCCCCCCH		26.53-
3Phosphorylation-----MSSILPFTPP
-----CCCCCCCCHH		27.1825619855
8PhosphorylationMSSILPFTPPVVKRL
CCCCCCCCHHHHHHH		25.4123527152
19AcetylationVKRLLGWKKSAGGSG
HHHHHCCCCCCCCCC		34.74-
21PhosphorylationRLLGWKKSAGGSGGA
HHHCCCCCCCCCCCC		28.5529514104
43MalonylationQEEKWCEKAVKSLVK
CHHHHHHHHHHHHHH		56.1726320211
47PhosphorylationWCEKAVKSLVKKLKK
HHHHHHHHHHHHHHH		31.62-
102PhosphorylationQWDTTGLYSFSEQTR
CCCCCCCEECCHHHC		14.71-
118PhosphorylationLDGRLQVSHRKGLPH
CCCCEEEECCCCCCE		12.4725338131
128PhosphorylationKGLPHVIYCRLWRWP
CCCCEEEEEEECCCC		3.1429514104
172PhosphorylationYHYQRVETPVLPPVL
CCCCCCCCCCCCCCC		18.8127180971
220PhosphorylationQSNYIPETPPPGYIS
CCCCCCCCCCCCCCC		35.42-
240PhosphorylationSDQQLNQSMDTGSPA
CHHHHHHHCCCCCCC		19.97-
245PhosphorylationNQSMDTGSPAELSPT
HHHCCCCCCCCCCCC		24.03-
250PhosphorylationTGSPAELSPTTLSPV
CCCCCCCCCCCCCCC		16.23-
255PhosphorylationELSPTTLSPVNHSLD
CCCCCCCCCCCCCCC		25.39-
324PhosphorylationSNVNRNATVEMTRRH
HCCCCCCCHHHHHHH		22.13-
351PhosphorylationEVFAECLSDSAIFVQ
HHHHHHHCCCEEEEE		40.9717991884
366PhosphorylationSPNCNQRYGWHPATV
CCCCCCCCCCCCCCE		18.1429514104
417PhosphorylationRMCTIRMSFVKGWGA
HHHHHHHHHHCCCCC		19.6222871156
420AcetylationTIRMSFVKGWGAEYR
HHHHHHHCCCCCCHH		47.1123806337
420MalonylationTIRMSFVKGWGAEYR
HHHHHHHCCCCCCHH		47.1126320211
426PhosphorylationVKGWGAEYRRQTVTS
HCCCCCCHHCEECCC		15.5722871156
430PhosphorylationGAEYRRQTVTSTPCW
CCCHHCEECCCCCEE		24.7617991884
433PhosphorylationYRRQTVTSTPCWIEL
HHCEECCCCCEEEEE		26.4722817900
458PhosphorylationKVLTQMGSPSVRCSS
HHHHHCCCCCCCCCC		14.5222006019
460PhosphorylationLTQMGSPSVRCSSMS
HHHCCCCCCCCCCCC		24.7228066266
464PhosphorylationGSPSVRCSSMS----
CCCCCCCCCCC----		20.6426643407
465PhosphorylationSPSVRCSSMS-----
CCCCCCCCCC-----		27.0318255094
467PhosphorylationSVRCSSMS-------
CCCCCCCC-------		38.7318255094
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
240SPhosphorylationKinaseCAMK2-Uniprot
324TPhosphorylationKinaseMINKQ8N4C8
PSP
465SPhosphorylationKinaseTGFBR1Q64729
Uniprot
467SPhosphorylationKinaseTGFBR1Q64729
Uniprot
-KUbiquitinationE3 ubiquitin ligaseItchQ8C863
PMID:22199232
-KUbiquitinationE3 ubiquitin ligaseNedd4lQ8CFI0
PMID:22199232
-KUbiquitinationE3 ubiquitin ligaseWwp2Q9DBH0
PMID:31399586
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference
19KAcetylation

-
240SPhosphorylation

12672795
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 SMAD2_MOUSE !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
ZEB2_MOUSEZeb2physical
20211142
EVI1_MOUSEMecomphysical
15849193
RN111_MOUSERnf111physical
17341133
ITCH_MOUSEItchphysical
15350225
SMAD4_MOUSESmad4physical
17452626
LEF1_MOUSELef1physical
17452626
MYOD1_MOUSEMyod1physical
11711431
PEX6_MOUSEPex6physical
14651998
4ET_MOUSEEif4enif1physical
14651998
ZMYM2_MOUSEZmym2physical
14651998
PBX1_MOUSEPbx1physical
14764653
PKNX1_MOUSEPknox1physical
14764653
SMAD4_MOUSESmad4physical
14764653
FOXH1_MOUSEFoxh1physical
9702197
PRD16_MOUSEPrdm16physical
17467076
SMAD4_MOUSESmad4physical
21145499
YAP1_MOUSEYap1physical
21145499
SMAD4_MOUSESmad4physical
23973329
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of SMAD2_MOUSE

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Related Literatures of Post-Translational Modification

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