DACH2_HUMAN - dbPTM
DACH2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID DACH2_HUMAN
UniProt AC Q96NX9
Protein Name Dachshund homolog 2
Gene Name DACH2
Organism Homo sapiens (Human).
Sequence Length 599
Subcellular Localization Nucleus .
Protein Description Transcription factor that is involved in regulation of organogenesis. Seems to be a regulator for SIX1 and SIX6. Seems to act as a corepressor of SIX6 in regulating proliferation by directly repressing cyclin-dependent kinase inhibitors, including the p27Kip1 promoter. Is recruited with SIX6 to the p27Kip1 promoter in embryonal retina. SIX6 corepression seems also to involve NCOR1, TBL1, HDAC1 and HDAC3. May be involved together with PAX3, SIX1, and EYA2 in regulation of myogenesis. In the developing somite, expression of DACH2 and PAX3 is regulated by the overlying ectoderm, and DACH2 and PAX3 positively regulate each other's expression (By similarity). Probably binds to DNA via its DACHbox-N domain..
Protein Sequence MAVSASPVISATSSGAGVPGGLFRAEPLYSTPREPPRLTPNMINSFVVNNHSNSAGGGGRGNTNTNECRMVDMHGMKVASFLMDGQELICLPQVFDLFLKHLVGGLHTVYTKLKRLDISPVVCTVEQVRILRGLGAIQPGVNRCKLITRKDFETLFTDCTNARRKRQMTRKQAVNSSRPGRPPKRSLGVLQENARLLTHAVPGLLSPGLITPTGITAAAMAEAMKLQKMKLMAMNTLQGNGSQNGTESEPDDLNSNTGGSESSWDKDKMQSPFAAPGPQHGIAHAALAGQPGIGGAPTLNPLQQNHLLTNRLDLPFMMMPHPLLPVSLPPASVAMAMNQMNHLNTIANMAAAAQIHSPLSRAGTSVIKERIPESPSPAPSLEENHRPGSQTSSHTSSSVSSSPSQMDHHLERMEEVPVQIPIMKSPLDKIQLTPGQALPAGFPGPFIFADSLSSVETLLTNIQGLLKVALDNARIQEKQIQQEKKELRLELYREREIRENLERQLAVELQSRTTMQKRLKKEKKTKRKLQEALEFESKRREQVEQALKQATTSDSGLRMLKDTGIPDIEIENNGTPHDSAAMQGGNYYCLEMAQQLYSA
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
45PhosphorylationLTPNMINSFVVNNHS
CCHHHCCEEEECCCC
14.4325072903
52PhosphorylationSFVVNNHSNSAGGGG
EEEECCCCCCCCCCC
34.3025072903
54PhosphorylationVVNNHSNSAGGGGRG
EECCCCCCCCCCCCC
31.1625072903
108PhosphorylationHLVGGLHTVYTKLKR
HHHCCHHHHHHHHHC
21.9120049867
110PhosphorylationVGGLHTVYTKLKRLD
HCCHHHHHHHHHCCC
10.1820049867
111PhosphorylationGGLHTVYTKLKRLDI
CCHHHHHHHHHCCCC
26.0920049867
148PhosphorylationVNRCKLITRKDFETL
CCHHEEEEHHHHHHH
41.9428555341
186PhosphorylationPGRPPKRSLGVLQEN
CCCCCCCCHHHHHHH
35.2822210691
236PhosphorylationMKLMAMNTLQGNGSQ
CHHHHHHHCCCCCCC
13.84-
242PhosphorylationNTLQGNGSQNGTESE
HHCCCCCCCCCCCCC
25.19-
327PhosphorylationPHPLLPVSLPPASVA
CCCCCCCCCCHHHHH
32.9722210691
357PhosphorylationAAAAQIHSPLSRAGT
HHHHHCCCCHHHCCC
29.21-
360PhosphorylationAQIHSPLSRAGTSVI
HHCCCCHHHCCCHHH
24.3822210691
433PhosphorylationPLDKIQLTPGQALPA
CCCCCCCCCCCCCCC
14.7022210691
453PhosphorylationFIFADSLSSVETLLT
EEECCCHHHHHHHHH
35.9722210691
454PhosphorylationIFADSLSSVETLLTN
EECCCHHHHHHHHHH
29.3022210691
537PhosphorylationQEALEFESKRREQVE
HHHHHHHHHHHHHHH
36.46-

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

Oops, there are no upstream regulatory protein records of DACH2_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of DACH2_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 DACH2_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
GLYG2_HUMANGYG2physical
28514442
DACH1_HUMANDACH1physical
28514442
TRI26_HUMANTRIM26physical
28514442
CD2AP_HUMANCD2APphysical
28514442

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of DACH2_HUMAN

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Related Literatures of Post-Translational Modification

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