ATN5_YEAST - dbPTM
ATN5_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ATN5_YEAST
UniProt AC Q12691
Protein Name Sodium transport ATPase 5
Gene Name ENA5
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 1091
Subcellular Localization Cell membrane
Multi-pass membrane protein .
Protein Description This magnesium-dependent enzyme catalyzes the hydrolysis of ATP coupled with the transport of sodium or lithium ions to allow salt tolerance..
Protein Sequence MSEGTVKENNNEEFNAYHTLTTEEAAEFIGTSLTEGLTQDESLRRLKAVGENTLGDDTKIDYKAMVLHQVCNAMIMVLVISMAISFAVRDWITGGVISFVIAVNVLIGLVQEYKATKTMNSLKNLSSPNAHVIRNGKSETINSKDVVPGDICLVKVGDTIPADLRLIETKNFDTDESLLTGESLPVSKDANLVFGKEEETSVGDRLNLAFSSSAVVKGRAKGIVIKTALNSEIGKIAKSLQGDSGLISRDPSKSWLQNTWISTKKVTGAFLGTNVGTPLHRKLSKLAVLLFWIAVLFAIIVMASQKFDVDKRVAIYAICVALSMIPSSLVVVLTITMSVGAAVMVSRNVIVRKLDSLEALGAVNDICSDKTGTLTQGKMLARQIWIPRFGTITISNSDDPFNPNEGNVSLIPRFSPYEYSHNEDGDVGILQNFKDRLYEKDLPEDIDMDLFQKWLETATLANIATVFKDDATDCWKAHGDPTEIAIQVFATKMDLPHNALTGEKSTNQSNENDQSSLSQHNEKPGSAQFEHIAEFPFDSTVKRMSSVYYNNHNETYNIYGKGAFESIISCCSSWYGKDGVKITPLTDCDVETIRKNVYSLSNEGLRVLGFASKSFTKDQVNDDQLKNITSNRATAESDLVFLGLIGIYDPPRNETAGAVKKFHQAGINVHMLTGDFVGTAKAIAQEVGILPTNLYHYSQEIVDSMVMTGSQFDGLSEEEVDDLPVLPLVIARCSPQTKVRMIEALHRRKKFCAMTGDGVNDSPSLKMANVGIAMGINGSDVSKEASDIVLSDDNFASILNAVEEGRRMTDNIQKFVLQLLAENVAQALYLIIGLVFRDENGKSVFPLSPVEVLWIIVVTSCFPAMGLGLEKAAPDLMDRPPNDSEVGIFTWEVIIDTFAYGIIMTGSCMASFTGSLYGINSGRLGHDCDGTYNSSCRDVYRSRSAAFATMTWCALILAWEVVDMRRSFFRMHPDTDSPVKEFFRSIWGNQFLFWSIIFGFVSAFPVVYIPVINDKVFLHKPIGAEWGLAIAFTIAFWIGAELYKCGKRRYFKTQRAHNSENDLERSSKHDPFEAYSTSTTLQSEINISVKH
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
2Phosphorylation------MSEGTVKEN
------CCCCCCCCC		56.9130377154
47UbiquitinationDESLRRLKAVGENTL
CHHHHHHHHHCCCCC		38.9323749301
123UbiquitinationTKTMNSLKNLSSPNA
HHHHHHHCCCCCCCC		56.5123749301
127PhosphorylationNSLKNLSSPNAHVIR
HHHCCCCCCCCEEEE		25.9123749301
137UbiquitinationAHVIRNGKSETINSK
CEEEECCCCCCCCCC		48.9823749301
144UbiquitinationKSETINSKDVVPGDI
CCCCCCCCCCCCCCE		50.4823749301
170UbiquitinationDLRLIETKNFDTDES
CCEEEEECCCCCCCC		42.7123749301
177PhosphorylationKNFDTDESLLTGESL
CCCCCCCCCCCCCCC		31.3328152593
188UbiquitinationGESLPVSKDANLVFG
CCCCCCCCCCCEECC		62.1817644757
196UbiquitinationDANLVFGKEEETSVG
CCCEECCCCCCCCHH		50.9523749301
235UbiquitinationALNSEIGKIAKSLQG
HHHCHHHHHHHHHCC		45.1923749301
238UbiquitinationSEIGKIAKSLQGDSG
CHHHHHHHHHCCCCC		55.9923749301
253UbiquitinationLISRDPSKSWLQNTW
CCCCCCCCHHHHHCE		51.5523749301
264UbiquitinationQNTWISTKKVTGAFL
HHCEEEECCCCCCCC		38.1617644757
265UbiquitinationNTWISTKKVTGAFLG
HCEEEECCCCCCCCC		45.1517644757
353UbiquitinationSRNVIVRKLDSLEAL
CCCEEEEEHHHHHHH		45.8323749301
370UbiquitinationVNDICSDKTGTLTQG
HCHHHCCCCCCCCCC		32.3423749301
378UbiquitinationTGTLTQGKMLARQIW
CCCCCCCHHHHEEEE		22.4123749301
415PhosphorylationVSLIPRFSPYEYSHN
CCEECCCCCCCCCCC		28.0530377154
417PhosphorylationLIPRFSPYEYSHNED
EECCCCCCCCCCCCC		26.7130377154
440UbiquitinationFKDRLYEKDLPEDID
HHHHHHHCCCCCCCC		51.5123749301
468UbiquitinationANIATVFKDDATDCW
HHHHHHHCCCHHHHH		50.8122106047
505PhosphorylationNALTGEKSTNQSNEN
HHCCCCCCCCCCCCC		28.4321440633
506PhosphorylationALTGEKSTNQSNEND
HCCCCCCCCCCCCCC		48.6321440633
509PhosphorylationGEKSTNQSNENDQSS
CCCCCCCCCCCCCHH		48.4529136822
515PhosphorylationQSNENDQSSLSQHNE
CCCCCCCHHHHHCCC		35.7929136822
516PhosphorylationSNENDQSSLSQHNEK
CCCCCCHHHHHCCCC		26.8017287358
518PhosphorylationENDQSSLSQHNEKPG
CCCCHHHHHCCCCCC		31.2029136822
523UbiquitinationSLSQHNEKPGSAQFE
HHHHCCCCCCCCCCE		61.0623749301
526PhosphorylationQHNEKPGSAQFEHIA
HCCCCCCCCCCEEEE		27.6829136822
539PhosphorylationIAEFPFDSTVKRMSS
EEECCCCHHHHHCEE		35.1619823750
540PhosphorylationAEFPFDSTVKRMSSV
EECCCCHHHHHCEEE		31.7119823750
577UbiquitinationCCSSWYGKDGVKITP
HHHHHHCCCCCEEEE		35.3022817900
581UbiquitinationWYGKDGVKITPLTDC
HHCCCCCEEEECCCC		46.5223749301
617UbiquitinationFASKSFTKDQVNDDQ
EECCCCCCCCCCHHH		44.1223749301
626UbiquitinationQVNDDQLKNITSNRA
CCCHHHHHHCCCCCC		40.4423749301
750UbiquitinationEALHRRKKFCAMTGD
HHHHHCCCHHCCCCC		43.8123749301
766UbiquitinationVNDSPSLKMANVGIA
CCCCCCCCCCCEEEE		40.0617644757
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 ATN5_YEAST !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ATN5_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 ATN5_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
ERP4_YEASTERP4physical
16093310
BMH1_YEASTBMH1genetic
22484491
RAD1_YEASTRAD1genetic
27708008
PRS8_YEASTRPT6genetic
27708008
PRP19_YEASTPRP19genetic
27708008
HAP3_YEASTHAP3genetic
27708008
CSG2_YEASTCSG2genetic
27708008
RIM1_YEASTRIM1genetic
27708008
BCS1_YEASTBCS1genetic
27708008
XRN1_YEASTXRN1genetic
27708008
PTH_YEASTPTH1genetic
27708008
AIM18_YEASTAIM18genetic
27708008
FLX1_YEASTFLX1genetic
27708008
TOK1_YEASTTOK1genetic
27708008
MTC1_YEASTMTC1genetic
27708008
MRX5_YEASTYJL147Cgenetic
27708008
PIR5_YEASTYJL160Cgenetic
27708008
GBLP_YEASTASC1genetic
27708008
MED1_YEASTMED1genetic
27708008
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of ATN5_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-177, AND MASSSPECTROMETRY.
Ubiquitylation
ReferencePubMed
"A subset of membrane-associated proteins is ubiquitinated in responseto mutations in the endoplasmic reticulum degradation machinery.";
Hitchcock A.L., Auld K., Gygi S.P., Silver P.A.;
Proc. Natl. Acad. Sci. U.S.A. 100:12735-12740(2003).
Cited for: UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-196, AND MASSSPECTROMETRY.

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