YNX4_YEAST - dbPTM
YNX4_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID YNX4_YEAST
UniProt AC P53857
Protein Name Uncharacterized globin-like protein YNL234W
Gene Name YNL234W
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 426
Subcellular Localization
Protein Description
Protein Sequence MTGEKILHSQLLTNSDMSSGNVHHTKPMMYNVTLPSYNSSSIGPVDNLKINERPGSHDHSMRSEMSSKNSGSDFMPQSISRSEGSVYQVKIDRGDSPNTEGFDFKVNARDLLLLRMSWDILLREYLTPKELKVFQALLYSNKHITSTERPYLNTAPDGMISKTIDPTARPRKTKQRDNDNKVDTALFCSQFYDNLIAMDPLLEEYFPSLKHQAVSFCKVLDSAIDNLENVHVLDDYIVKLGKRHSRILGIKTVGFEVMGKAFMTTLQDRFGSFLTLELKNLWGQLYSYLANCMITAGKDPMEKIQPDFSYNGDSVVLNFSIPKLAMHDISTVNKLQMVKTKNATIPHNITQVPTNKIPTEILLDNSSTPIKSDRESTPPISPKGSGSTKPSIGSSTVVESNTKKNNYDEKIHLLQKTAQQKNCSIM
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
67PhosphorylationSMRSEMSSKNSGSDF
HHHHHHHCCCCCCCC		34.2521551504
78PhosphorylationGSDFMPQSISRSEGS
CCCCCCCEEECCCCC		19.3621440633
80PhosphorylationDFMPQSISRSEGSVY
CCCCCEEECCCCCEE		34.6921440633
82PhosphorylationMPQSISRSEGSVYQV
CCCEEECCCCCEEEE		39.2528889911
85PhosphorylationSISRSEGSVYQVKID
EEECCCCCEEEEEEE		17.3821440633
87PhosphorylationSRSEGSVYQVKIDRG
ECCCCCEEEEEEECC		14.8624930733
96PhosphorylationVKIDRGDSPNTEGFD
EEEECCCCCCCCCCC		23.9122369663
99PhosphorylationDRGDSPNTEGFDFKV
ECCCCCCCCCCCEEE		40.6522369663
139PhosphorylationKVFQALLYSNKHITS
HHHHHHHHCCCCCCC		15.8525533186
162AcetylationAPDGMISKTIDPTAR
CCCCCCCCCCCCCCC		38.2825381059
366PhosphorylationTEILLDNSSTPIKSD
CEEECCCCCCCCCCC		34.9421440633
367PhosphorylationEILLDNSSTPIKSDR
EEECCCCCCCCCCCC		44.4428889911
368PhosphorylationILLDNSSTPIKSDRE
EECCCCCCCCCCCCC		28.9321551504
372PhosphorylationNSSTPIKSDRESTPP
CCCCCCCCCCCCCCC		42.4925521595
376PhosphorylationPIKSDRESTPPISPK
CCCCCCCCCCCCCCC		47.2921440633
377PhosphorylationIKSDRESTPPISPKG
CCCCCCCCCCCCCCC		28.4725752575
381PhosphorylationRESTPPISPKGSGST
CCCCCCCCCCCCCCC		26.7427214570
388PhosphorylationSPKGSGSTKPSIGSS
CCCCCCCCCCCCCCC		50.9625521595
395PhosphorylationTKPSIGSSTVVESNT
CCCCCCCCEEEECCC		21.7325521595
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 YNX4_YEAST !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of YNX4_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 YNX4_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
CLU_YEASTCLU1physical
16554755
TAPT1_YEASTEMP65genetic
27708008
LSB3_YEASTLSB3genetic
27708008
STF2_YEASTSTF2genetic
27708008
TNA1_YEASTTNA1genetic
27708008
THIK_YEASTPOT1genetic
27708008
YJ24_YEASTKCH1genetic
27708008
YL032_YEASTYLL032Cgenetic
27708008
YL149_YEASTYLR149Cgenetic
27708008
EIF3J_YEASTHCR1genetic
27708008
SOK2_YEASTSOK2genetic
27708008
YMS4_YEASTYMR034Cgenetic
27708008
YM01_YEASTYMR111Cgenetic
27708008
SCS7_YEASTSCS7genetic
27708008
KTR1_YEASTKTR1genetic
27708008
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of YNX4_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-96 AND SER-367, AND MASSSPECTROMETRY.

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