ATN1_YEAST - dbPTM
ATN1_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ATN1_YEAST
UniProt AC P13587
Protein Name Sodium transport ATPase 1
Gene Name ENA1
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 the sodium or lithium ions to allow salt tolerance. Is negatively modulated by SIS2/HAL3..
Protein Sequence MGEGTTKENNNAEFNAYHTLTAEEAAEFIGTSLTEGLTQDEFVHRLKTVGENTLGDDTKIDYKAMVLHQVCNAMIMVLLISMIISFAMHDWITGGVISFVIAVNVLIGLVQEYKATKTMNSLKNLSSPNAHVIRNGKSETINSKDVVPGDICLVKVGDTIPADLRLIETKNFDTDESLLTGESLPVSKDANLVFGKEEETSVGDRLNLAFSSSAVVKGRAKGIVIKTALNSEIGKIAKSLQGDSGLISRDPSKSWLQNTWISTKKVTGAFLGTNVGTPLHRKLSKLAVLLFWIAVLFAIIVMASQKFDVDKRVAIYAICVALSMIPSSLVVVLTITMSVGAAVMVSRNVIVRKLDSLEALGAVNDICSDKTGTLTQGKMLARQIWIPRFGTITISNSDDPFNPNEGNVSLIPRFSPYEYSHNEDGDVGILQNFKDRLYEKDLPEDIDMDLFQKWLETATLANIATVFKDDATDCWKAHGDPTEIAIQVFATKMDLPHNALTGEKSTNQSNENDQSSLSQHNEKPGSAQFEHIAEFPFDSTVKRMSSVYYNNHNETYNIYGKGAFESIISCCSSWYGKDGVKITPLTDCDVETIRKNVYSLSNEGLRVLGFASKSFTKDQVNDDQLKNITSNRATAESDLVFLGLIGIYDPPRNETAGAVKKFHQAGINVHMLTGDFVGTAKAIAQEVGILPTNLYHYSQEIVDSMVMTGSQFDGLSEEEVDDLPVLPLVIARCSPQTKVRMIEALHRRKKFCTMTGDGVNDSPSLKMANVGIAMGINGSDVSKEASDIVLSDDNFASILNAVEEGRRMTDNIQKFVLQLLAENVAQALYLIIGLVFRDENGKSVFPLSPVEVLWIIVVTSCFPAMGLGLEKAAPDLMDRPPHDSEVGIFTWEVIIDTFAYGIIMTGSCMASFTGSLYGINSGRLGHDCDGTYNSSCRDVYRSRSAAFATMTWCALILAWEVVDMRRSFFRMHPDTDSPVKEFFRSIWGNQFLFWSIIFGFVSAFPVVYIPVINDKVFLHKPIGAEWGLAIAFTIAFWIGAELYKCGKRRYFKTQRAHNPENDLESNNKRDPFEAYSTSTTIHTEVNIGIKQ
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
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
235AcetylationALNSEIGKIAKSLQG
HHHCHHHHHHHHHCC		45.1924489116
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		26.8019823750
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
750UbiquitinationEALHRRKKFCTMTGD
HHHHHCCCCEECCCC		43.8123749301
753PhosphorylationHRRKKFCTMTGDGVN
HHCCCCEECCCCCCC		22.3927017623
762PhosphorylationTGDGVNDSPSLKMAN
CCCCCCCCCCCCCCC		15.9327017623
764PhosphorylationDGVNDSPSLKMANVG
CCCCCCCCCCCCCEE		44.5727017623
779PhosphorylationIAMGINGSDVSKEAS
EEEECCCHHCCHHHH		30.2827017623
1065PhosphorylationNPENDLESNNKRDPF
CCCCCCCCCCCCCCC		53.6625005228
1068UbiquitinationNDLESNNKRDPFEAY
CCCCCCCCCCCCHHH		63.5323749301
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 ATN1_YEAST !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ATN1_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 ATN1_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
HAL4_YEASTSAT4genetic
10207057
HAL5_YEASTHAL5genetic
10207057
PPZ1_YEASTPPZ1genetic
14871941
PPZ2_YEASTPPZ2genetic
14871941
NHX1_YEASTNHX1genetic
17588950
HAL1_YEASTHAL1genetic
9178503
NAH1_YEASTNHA1genetic
19473262
SEN1_YEASTSEN1genetic
11003661
NAH1_YEASTNHA1genetic
20213854
TOK1_YEASTTOK1genetic
20213854
SIS2_YEASTSIS2genetic
11867520
PPZ1_YEASTPPZ1genetic
11867520
PPZ2_YEASTPPZ2genetic
11867520
PMP3_YEASTPMP3genetic
10835350
NAH1_YEASTNHA1genetic
10835350
TPS1_YEASTTPS1genetic
15164360
NAH1_YEASTNHA1genetic
20659170
ARL1_YEASTARL1genetic
20659170
KHA1_YEASTKHA1genetic
20659170
NHX1_YEASTNHX1genetic
20659170
VCX1_YEASTVCX1genetic
20709757
NAH1_YEASTNHA1genetic
21143561
TOK1_YEASTTOK1genetic
22329368
BMH1_YEASTBMH1genetic
22484491
VHC1_YEASTVHC1genetic
23022132
VNX1_YEASTVNX1genetic
23022132
PHO84_YEASTPHO84genetic
25266663
EXO84_YEASTEXO84genetic
27708008
PRS6B_YEASTRPT3genetic
27708008
NU145_YEASTNUP145genetic
27708008
BRL1_YEASTBRL1genetic
27708008
SEC6_YEASTSEC6genetic
27708008
IMB1_YEASTKAP95genetic
27708008
SEC39_YEASTSEC39genetic
27708008
TEM1_YEASTTEM1genetic
27708008
NAT10_YEASTKRE33genetic
27708008
RPC1_YEASTRPO31genetic
27708008
GRPE_YEASTMGE1genetic
27708008
MOT1_YEASTMOT1genetic
27708008
TF2B_YEASTSUA7genetic
27708008
CDC24_YEASTCDC24genetic
27708008
ERD2_YEASTERD2genetic
27708008
MED8_YEASTMED8genetic
27708008
GLE1_YEASTGLE1genetic
27708008
CDC1_YEASTCDC1genetic
27708008
TCPZ_YEASTCCT6genetic
27708008
COG3_YEASTCOG3genetic
27708008
ACT_YEASTACT1genetic
27708008
PSB7_YEASTPRE4genetic
27708008
COAD_YEASTCAB4genetic
27708008
RFC2_YEASTRFC2genetic
27708008
MIF2_YEASTMIF2genetic
27708008
ABF1_YEASTABF1genetic
27708008
NTR2_YEASTNTR2genetic
27708008
PRP19_YEASTPRP19genetic
27708008
SSL1_YEASTSSL1genetic
27708008
NEP1_YEASTEMG1genetic
27708008
SC61A_YEASTSEC61genetic
27708008
ORC1_YEASTORC1genetic
27708008
ARP9_YEASTARP9genetic
27708008
MYO2_YEASTMYO2genetic
27708008
ARP7_YEASTARP7genetic
27708008
SRP54_YEASTSRP54genetic
27708008
PGTB2_YEASTBET2genetic
27708008
CAJ1_YEASTCAJ1genetic
27708008
YFF2_YEASTYFL052Wgenetic
27708008
MRT4_YEASTMRT4genetic
27708008
YL149_YEASTYLR149Cgenetic
27708008
INO4_YEASTINO4genetic
27708008
KTR1_YEASTKTR1genetic
27708008
NCBP2_YEASTCBC2genetic
27708008
BRR1_YEASTBRR1genetic
27708008
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of ATN1_YEAST

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Analysis of phosphorylation sites on proteins from Saccharomycescerevisiae by electron transfer dissociation (ETD) massspectrometry.";
Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L.,Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.;
Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-516, AND MASSSPECTROMETRY.

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