FHP_YEAST - dbPTM
FHP_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID FHP_YEAST
UniProt AC P39676
Protein Name Flavohemoprotein
Gene Name YHB1
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 399
Subcellular Localization Cytoplasm.
Protein Description Is involved in NO detoxification in an aerobic process, termed nitric oxide dioxygenase (NOD) reaction that utilizes O(2) and NAD(P)H to convert NO to nitrate, which protects the fungus from various noxious nitrogen compounds. Therefore, plays a central role in the inducible response to nitrosative stress.; In the presence of oxygen and NADH, it has NADH oxidase activity, which leads to the generation of superoxide and H(2)O(2). Under anaerobic conditions, it also exhibits nitric oxide reductase and FAD reductase activities. However, all these reactions are much lower than NOD activity..
Protein Sequence MLAEKTRSIIKATVPVLEQQGTVITRTFYKNMLTEHTELLNIFNRTNQKVGAQPNALATTVLAAAKNIDDLSVLMDHVKQIGHKHRALQIKPEHYPIVGEYLLKAIKEVLGDAATPEIINAWGEAYQAIADIFITVEKKMYEEALWPGWKPFDITAKEYVASDIVEFTVKPKFGSGIELESLPITPGQYITVNTHPIRQENQYDALRHYSLCSASTKNGLRFAVKMEAARENFPAGLVSEYLHKDAKVGDEIKLSAPAGDFAINKELIHQNEVPLVLLSSGVGVTPLLAMLEEQVKCNPNRPIYWIQSSYDEKTQAFKKHVDELLAECANVDKIIVHTDTEPLINAAFLKEKSPAHADVYTCGSLAFMQAMIGHLKELEHRDDMIHYEPFGPKMSTVQV
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
11UbiquitinationEKTRSIIKATVPVLE
HHHHHHHHHHHHHHH		36.0117644757
22PhosphorylationPVLEQQGTVITRTFY
HHHHHCCEEEEHHHH		12.371594608
30AcetylationVITRTFYKNMLTEHT
EEEHHHHHHHHHHCH		31.5224489116
30UbiquitinationVITRTFYKNMLTEHT
EEEHHHHHHHHHHCH		31.5217644757
49AcetylationIFNRTNQKVGAQPNA
HHHHHCCCCCCCCCH		44.7124489116
49UbiquitinationIFNRTNQKVGAQPNA
HHHHHCCCCCCCCCH		44.7124961812
66UbiquitinationTTVLAAAKNIDDLSV
HHHHHHHCCCCHHHH		50.1123749301
79AcetylationSVLMDHVKQIGHKHR
HHHHHHHHHHCHHCC		32.5524489116
79UbiquitinationSVLMDHVKQIGHKHR
HHHHHHHHHHCHHCC		32.5522817900
84UbiquitinationHVKQIGHKHRALQIK
HHHHHCHHCCCCCCC		29.5822817900
91UbiquitinationKHRALQIKPEHYPIV
HCCCCCCCHHHCCCH		31.2417644757
91AcetylationKHRALQIKPEHYPIV
HCCCCCCCHHHCCCH		31.2424489116
104AcetylationIVGEYLLKAIKEVLG
CHHHHHHHHHHHHHC		45.5324489116
104UbiquitinationIVGEYLLKAIKEVLG
CHHHHHHHHHHHHHC		45.5317644757
172UbiquitinationVEFTVKPKFGSGIEL
EEEEECCCCCCCCEE		57.5517644757
210PhosphorylationYDALRHYSLCSASTK
HHHHHHHHCCCCCCC		19.4421440633
213PhosphorylationLRHYSLCSASTKNGL
HHHHHCCCCCCCCCH		30.4623749301
215PhosphorylationHYSLCSASTKNGLRF
HHHCCCCCCCCCHHH		24.5019779198
217UbiquitinationSLCSASTKNGLRFAV
HCCCCCCCCCHHHHH		46.6623749301
225AcetylationNGLRFAVKMEAAREN
CCHHHHHHHHHHHHH		27.8222865919
244UbiquitinationLVSEYLHKDAKVGDE
HHHHHHCCCCCCCCE		57.7117644757
244AcetylationLVSEYLHKDAKVGDE
HHHHHHCCCCCCCCE		57.7124489116
253AcetylationAKVGDEIKLSAPAGD
CCCCCEEEECCCCCC		34.0524489116
319AcetylationEKTQAFKKHVDELLA
HHHHHHHHHHHHHHH		42.2724489116
319UbiquitinationEKTQAFKKHVDELLA
HHHHHHHHHHHHHHH		42.2715699485
333UbiquitinationAECANVDKIIVHTDT
HHHCCCCEEEEECCC		30.0117644757
338PhosphorylationVDKIIVHTDTEPLIN
CCEEEEECCCHHHHC		33.4527017623
340PhosphorylationKIIVHTDTEPLINAA
EEEEECCCHHHHCHH		40.4327017623
350UbiquitinationLINAAFLKEKSPAHA
HHCHHHHCCCCCCCC		57.5523749301
350AcetylationLINAAFLKEKSPAHA
HHCHHHHCCCCCCCC		57.5524489116
352UbiquitinationNAAFLKEKSPAHADV
CHHHHCCCCCCCCCC		61.2222817900
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 FHP_YEAST !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of FHP_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 FHP_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
FRDA_YEASTYFH1physical
15961414
TCPZ_YEASTCCT6physical
16429126
GCN1_YEASTGCN1physical
16429126
GCN20_YEASTGCN20physical
16429126
GFA1_YEASTGFA1physical
16429126
MDN1_YEASTMDN1physical
16429126
RSSA1_YEASTRPS0Aphysical
16429126
TBA1_YEASTTUB1physical
16429126
MPG1_YEASTPSA1physical
16429126
ACON_YEASTACO1physical
16429126
PAA1_YEASTPAA1physical
16429126
RPA2_YEASTRPA135physical
16429126
FADH_YEASTSFA1genetic
19138101
HSP71_YEASTSSA1physical
22940862
HSP72_YEASTSSA2physical
22940862
FHP_YEASTYHB1physical
22940862
TECR_YEASTTSC13genetic
27708008
CHK1_YEASTCHK1genetic
27708008
RTG2_YEASTRTG2genetic
27708008
CDC37_YEASTCDC37genetic
27708008
MED6_YEASTMED6genetic
27708008
SEC22_YEASTSEC22genetic
27708008
CLP1_YEASTCLP1genetic
27708008
VAM6_YEASTVAM6genetic
27708008
IES1_YEASTIES1genetic
27708008
MED5_YEASTNUT1genetic
27708008
ASK10_YEASTASK10genetic
27708008
VMA21_YEASTVMA21genetic
27708008
PIR5_YEASTYJL160Cgenetic
27708008
YAR1_YEASTYAR1genetic
27708008
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of FHP_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 THR-22 AND SER-210, AND MASSSPECTROMETRY.

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