DACT1_HUMAN - dbPTM
DACT1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID DACT1_HUMAN
UniProt AC Q9NYF0
Protein Name Dapper homolog 1
Gene Name DACT1
Organism Homo sapiens (Human).
Sequence Length 836
Subcellular Localization Cytoplasm. Nucleus. Cell junction, synapse. Shuttles between the nucleus and the cytoplasm. Seems to be nuclear in the absence of Wnt signaling and to translocate to the cytoplasm in its presence.
Protein Description Involved in regulation of intracellular signaling pathways during development. Specifically thought to play a role in canonical and/or non-canonical Wnt signaling pathways through interaction with DSH (Dishevelled) family proteins. The activation/inhibition of Wnt signaling may depend on the phosphorylation status. Proposed to regulate the degradation of CTNNB1/beta-catenin, thereby modulating the transcriptional activation of target genes of the Wnt signaling pathway. Its function in stabilizing CTNNB1 may involve inhibition of GSK3B activity. Promotes the membrane localization of CTNNB1. The cytoplasmic form can induce DVL2 degradation via a lysosome-dependent mechanism; the function is inhibited by PKA-induced binding to 14-3-3 proteins, such as YWHAB. Seems to be involved in morphogenesis at the primitive streak by regulating VANGL2 and DVL2; the function seems to be independent of canonical Wnt signaling and rather involves the non-canonical Wnt/planar cell polarity (PCP) pathway (By similarity). The nuclear form may prevent the formation of LEF1:CTNNB1 complex and recruit HDAC1 to LEF1 at target gene promoters to repress transcription thus antagonizing Wnt signaling. May be involved in positive regulation of fat cell differentiation. During neuronal differentiation may be involved in excitatory synapse organization, and dendrite formation and establishment of spines..
Protein Sequence MKPSPAGTAKELEPPAPARGEQRTAEPEGRWREKGEADTERQRTRERQEATLAGLAELEYLRQRQELLVRGALRGAGGAGAAAPRAGELLGEAAQRSRLEEKFLEENILLLRKQLNCLRRRDAGLLNQLQELDKQISDLRLDVEKTSEEHLETDSRPSSGFYELSDGASGSLSNSSNSVFSECLSSCHSSTCFCSPLEATLSLSDGCPKSADLIGLLEYKEGHCEDQASGAVCRSLSTPQFNSLDVIADVNPKYQCDLVSKNGNDVYRYPSPLHAVAVQSPMFLLCLTGNPLREEDRLGNHASDICGGSELDAVKTDSSLPSPSSLWSASHPSSSKKMDGYILSLVQKKTHPVRTNKPRTSVNADPTKGLLRNGSVCVRAPGGVSQGNSVNLKNSKQACLPSGGIPSLNNGTFSPPKQWSKESKAEQAESKRVPLPEGCPSGAASDLQSKHLPKTAKPASQEHARCSAIGTGESPKESAQLSGASPKESPSRGPAPPQENKVVQPLKKMSQKNSLQGVPPATPPLLSTAFPVEERPALDFKSEGSSQSLEEAHLVKAQFIPGQQPSVRLHRGHRNMGVVKNSSLKHRGPALQGLENGLPTVREKTRAGSKKCRFPDDLDTNKKLKKASSKGRKSGGGPEAGVPGRPAGGGHRAGSRAHGHGREAVVAKPKHKRTDYRRWKSSAEISYEEALRRARRGRRENVGLYPAPVPLPYASPYAYVASDSEYSAECESLFHSTVVDTSEDEQSNYTTNCFGDSESSVSEGEFVGESTTTSDSEESGGLIWSQFVQTLPIQTVTAPDLHNHPAKTFVKIKASHNLKKKILRFRSGSLKLMTTV
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
51PhosphorylationTRERQEATLAGLAEL
HHHHHHHHHHHHHHH
19.1823403867
60PhosphorylationAGLAELEYLRQRQEL
HHHHHHHHHHHHHHH
21.5823403867
70MethylationQRQELLVRGALRGAG
HHHHHHHHHHHCCCC
25.33-
137PhosphorylationQELDKQISDLRLDVE
HHHHHHHHHHCCCHH
28.2624719451
235PhosphorylationASGAVCRSLSTPQFN
HCCCHHHCCCCCCCC
22.8827251275
237PhosphorylationGAVCRSLSTPQFNSL
CCHHHCCCCCCCCCC
39.0121262972
238PhosphorylationAVCRSLSTPQFNSLD
CHHHCCCCCCCCCCE
26.8027251275
325PhosphorylationSSLPSPSSLWSASHP
CCCCCHHHHHCCCCC
36.92-
360PhosphorylationVRTNKPRTSVNADPT
CCCCCCCCCCCCCCC
45.6223312004
361PhosphorylationRTNKPRTSVNADPTK
CCCCCCCCCCCCCCC
18.0423312004
367PhosphorylationTSVNADPTKGLLRNG
CCCCCCCCCCCCCCC
37.99-
420PhosphorylationFSPPKQWSKESKAEQ
CCCCCCCCHHHHHHH
24.85-
423PhosphorylationPKQWSKESKAEQAES
CCCCCHHHHHHHHHH
40.68-
430PhosphorylationSKAEQAESKRVPLPE
HHHHHHHHCCCCCCC
28.86-
478PhosphorylationTGESPKESAQLSGAS
CCCCHHHHHHHCCCC
27.6924706070
482PhosphorylationPKESAQLSGASPKES
HHHHHHHCCCCCCCC
21.8922985185
485PhosphorylationSAQLSGASPKESPSR
HHHHCCCCCCCCCCC
39.7822985185
514PhosphorylationKKMSQKNSLQGVPPA
HHHHHCCCCCCCCCC
29.1629255136
522PhosphorylationLQGVPPATPPLLSTA
CCCCCCCCCCCCCCC
31.0829255136
527PhosphorylationPATPPLLSTAFPVEE
CCCCCCCCCCCCCCC
25.9329255136
528PhosphorylationATPPLLSTAFPVEER
CCCCCCCCCCCCCCC
32.0829255136
545PhosphorylationLDFKSEGSSQSLEEA
CCCCCCCCCCCHHHH
22.5823312004
546PhosphorylationDFKSEGSSQSLEEAH
CCCCCCCCCCHHHHH
34.3523312004
548PhosphorylationKSEGSSQSLEEAHLV
CCCCCCCCHHHHHEE
39.4328857561
566PhosphorylationFIPGQQPSVRLHRGH
ECCCCCCCEEEECCC
18.6128857561
582PhosphorylationNMGVVKNSSLKHRGP
CCCCCCCCCCCCCCH
31.18-
583PhosphorylationMGVVKNSSLKHRGPA
CCCCCCCCCCCCCHH
51.32-
628PhosphorylationNKKLKKASSKGRKSG
CHHHHHHHHHCCCCC
41.2729457462
629PhosphorylationKKLKKASSKGRKSGG
HHHHHHHHHCCCCCC
43.9529457462
634PhosphorylationASSKGRKSGGGPEAG
HHHHCCCCCCCCCCC
41.1128555341
655PhosphorylationGGGHRAGSRAHGHGR
CCCCCCCCCCCCCCC
25.88-
681PhosphorylationTDYRRWKSSAEISYE
CCHHHHHHHHCCCHH
28.0227251275
686PhosphorylationWKSSAEISYEEALRR
HHHHHCCCHHHHHHH
20.2826330541
687PhosphorylationKSSAEISYEEALRRA
HHHHCCCHHHHHHHH
24.3726330541
827PhosphorylationKKILRFRSGSLKLMT
HHHHHCCCCCCEEEE
29.9821262972
829PhosphorylationILRFRSGSLKLMTTV
HHHCCCCCCEEEEEC
24.4729514088

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
237SPhosphorylationKinasePRKACAP17612
GPS
237SPhosphorylationKinasePKA-Uniprot
827SPhosphorylationKinasePRKACAP17612
GPS
827SPhosphorylationKinasePKA-Uniprot

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of DACT1_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 DACT1_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
LEF1_HUMANLEF1physical
18936100
HDAC1_HUMANHDAC1physical
18936100
BECN1_HUMANBECN1physical
24980960
PK3C3_HUMANPIK3C3physical
24980960
BAKOR_HUMANATG14physical
24980960
ZBT17_HUMANZBTB17physical
25558878
VHL_HUMANVHLphysical
25825496
1433B_HUMANYWHABphysical
21262972
KAPCA_HUMANPRKACAphysical
21262972
DVL2_HUMANDVL2physical
21262972

Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
182940Neural tube defects (NTD)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of DACT1_HUMAN

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Related Literatures of Post-Translational Modification

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