DAK2_YEAST - dbPTM
DAK2_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID DAK2_YEAST
UniProt AC P43550
Protein Name Dihydroxyacetone kinase 2
Gene Name DAK2
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 591
Subcellular Localization
Protein Description Catalyzes both the phosphorylation of dihydroxyacetone and of glyceraldehyde..
Protein Sequence MSHKQFKSDGNIVTPYLLGLARSNPGLTVIKHDRVVFRTASAPNSGNPPKVSLVSGGGSGHEPTHAGFVGEGALDAIAAGAIFASPSTKQIYSAIKAVESPKGTLIIVKNYTGDIIHFGLAAERAKAAGMKVELVAVGDDVSVGKKKGSLVGRRGLGATVLVHKIAGAAASHGLELAEVAEVAQSVVDNSVTIAASLDHCTVPGHKPEAILGENEYEIGMGIHNESGTYKSSPLPSISELVSQMLPLLLDEDEDRSYVKFEPKEDVVLMVNNMGGMSNLELGYAAEVISEQLIDKYQIVPKRTITGAFITALNGPGFGITLMNASKAGGDILKYFDYPTTASGWNQMYHSAKDWEVLAKGQVPTAPSLKTLRNEKGSGVKADYDTFAKILLAGIAKINEVEPKVTWYDTIAGDGDCGTTLVSGGEALEEAIKNHTLRLEDAALGIEDIAYMVEDSMGGTSGGLYSIYLSALAQGVRDSGDKELTAETFKKASNVALDALYKYTRARPGYRTLIDALQPFVEALKAGKGPRAAAQAAYDGAEKTRKMDALVGRASYVAKEELRKLDSEGGLPDPGAVGLAALLDGFVTAAGY
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
23PhosphorylationYLLGLARSNPGLTVI
HHHHHHHCCCCCEEE		41.5928889911
39PhosphorylationHDRVVFRTASAPNSG
ECEEEEEECCCCCCC		17.3127017623
142PhosphorylationVAVGDDVSVGKKKGS
EEECCCCCCCCCCCC		31.9528889911
242PhosphorylationPSISELVSQMLPLLL
CCHHHHHHHHHHHHC		23.6128889911
259AcetylationDEDRSYVKFEPKEDV
CCCCCCCCCCCCCCE		35.4624489116
303PhosphorylationYQIVPKRTITGAFIT
CCCCCCCEECHHHHH		29.0829688323
305PhosphorylationIVPKRTITGAFITAL
CCCCCEECHHHHHHC		23.1129688323
310PhosphorylationTITGAFITALNGPGF
EECHHHHHHCCCCCC		20.7329688323
320PhosphorylationNGPGFGITLMNASKA
CCCCCCEEEEEHHHC		21.9729688323
325PhosphorylationGITLMNASKAGGDIL
CEEEEEHHHCCCCCH		20.3127017623
364PhosphorylationLAKGQVPTAPSLKTL
HHCCCCCCCCCHHHH		52.9621126336
484PhosphorylationDSGDKELTAETFKKA
CCCCCCCCHHHHHHH		24.4428889911
487PhosphorylationDKELTAETFKKASNV
CCCCCHHHHHHHHHH		37.9928889911
492PhosphorylationAETFKKASNVALDAL
HHHHHHHHHHHHHHH		40.4928889911
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 DAK2_YEAST !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of DAK2_YEAST !!
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 DAK2_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
MNN10_YEASTMNN10genetic
19269370
IPYR2_YEASTPPA2genetic
19269370
CG12_YEASTCLN2genetic
19269370
COX9_YEASTCOX9genetic
21623372
DCOR_YEASTSPE1genetic
21623372
THDH_YEASTILV1genetic
21623372
ACON2_YEASTACO2genetic
21623372
ERG2_YEASTERG2genetic
21623372
SCC1_YEASTMCD1genetic
27708008
RU1C_YEASTYHC1genetic
27708008
MCM7_YEASTMCM7genetic
27708008
TCPD_YEASTCCT4genetic
27708008
MAK21_YEASTMAK21genetic
27708008
CDC1_YEASTCDC1genetic
27708008
PRS8_YEASTRPT6genetic
27708008
ARP4_YEASTARP4genetic
27708008
AFG2_YEASTAFG2genetic
27708008
SEC12_YEASTSEC12genetic
27708008
CH10_YEASTHSP10genetic
27708008
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of DAK2_YEAST

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"A multidimensional chromatography technology for in-depthphosphoproteome analysis.";
Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
Mol. Cell. Proteomics 7:1389-1396(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-242, AND MASSSPECTROMETRY.

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