NAH1_YEAST - dbPTM
NAH1_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID NAH1_YEAST
UniProt AC Q99271
Protein Name Na(+)/H(+) antiporter
Gene Name NHA1
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 985
Subcellular Localization Membrane
Multi-pass membrane protein .
Protein Description Sodium export from cell, takes up external protons in exchange for internal sodium ions..
Protein Sequence MAIWEQLEVSKAHVAYACVGVFSSIFSLVSLYVKEKLYIGESTVAGIFGLIVGPVCLNWFNPLKWGNSDSITLEITRIVLCLQIFAVAVELPRKYMLKHWVSVTMLLLPVMTAGWLIIGLFVWILIPGLNFSASLLISACITATDPILAQSVVSGKFAQRVPGHLRNLLSAESGCNDGMAFPFLFLSMNLILHPGNGREIVKDWICVTILYECLFGCLLGCFIGYVGRITIRFAEKKNIIDRESFLAFYVVLAFMCAGFGSILGVDDLLVSFAAGATFAWDGWFSQKTQESNVSTVIDLLLNYAYFIYFGAIIPWSQFNNGEIGTNVWRLIILSIVVIFLRRIPAVMILRPLIPDIKSWREALFVGHFGPIGVGAIFAAILARGELESTFSDEPTPLNVVPSKEESKHWQLIACIWPITCFFIVTSIIVHGSSVAIITLGRHLNTITLTKTFTTHTTNGDNGKSSWMQRLPSLDKAGRSFSLHRMDTQMTLSGDEGEAEEGGGRKGLAGGEDEEGLNNDQIGSVATSGIPARPAGGMPRRRKLSRKEKRLNRRQKLRNKGREIFSSRSKNEMYDDDELNDLGRERLQKEKEARAATFALSTAVNTQRNEEIGMGGDEEEDEYTPEKEYSDNYNNTPSFESSERSSSLRGRTYVPRNRYDGEETESEIESEDEMENESERSMASSEERRIRKMKEEEMKPGTAYLDGNRMIIENKQGEILNQVDIEDRNEARDDEVSVDSTAHSSLTTTMTNLSSSSGGRLKRILTPTSLGKIHSLVDKGKDKNKNSKYHAFKIDNLLIIENEDGDVIKRYKINPHKSDDDKSKNRPRNDSVVSRALTAVGLKSKANSGVPPPVDEEKAIEGPSRKGPGMLKKRTLTPAPPRGVQDSLDLEDEPSSEEDLGDSYNMDDSEDYDDNAYESETEFERQRRLNALGEMTAPADQDDEELPPLPVEAQTGNDGPGTAEGKKKQKSAAVKSALSKTLGLNK
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
388PhosphorylationLARGELESTFSDEPT
HHHCCHHHHCCCCCC
47.5829688323
389PhosphorylationARGELESTFSDEPTP
HHCCHHHHCCCCCCC
20.1329688323
391PhosphorylationGELESTFSDEPTPLN
CCHHHHCCCCCCCCC
40.9529688323
395PhosphorylationSTFSDEPTPLNVVPS
HHCCCCCCCCCCCCC
38.0629688323
402PhosphorylationTPLNVVPSKEESKHW
CCCCCCCCHHHHHHH
40.8829688323
406PhosphorylationVVPSKEESKHWQLIA
CCCCHHHHHHHHHHH
30.8029688323
445PhosphorylationTLGRHLNTITLTKTF
ECCCCCCEEEEEEEE
23.0021440633
447PhosphorylationGRHLNTITLTKTFTT
CCCCCEEEEEEEEEC
26.7417563356
449PhosphorylationHLNTITLTKTFTTHT
CCCEEEEEEEEECCC
21.2719795423
451PhosphorylationNTITLTKTFTTHTTN
CEEEEEEEEECCCCC
22.4528889911
453PhosphorylationITLTKTFTTHTTNGD
EEEEEEEECCCCCCC
23.9321440633
454PhosphorylationTLTKTFTTHTTNGDN
EEEEEEECCCCCCCC
17.0330377154
456PhosphorylationTKTFTTHTTNGDNGK
EEEEECCCCCCCCCC
21.6221440633
457PhosphorylationKTFTTHTTNGDNGKS
EEEECCCCCCCCCCC
29.6021440633
472PhosphorylationSWMQRLPSLDKAGRS
CHHHHCCCCCCCCCC
54.5125533186
475UbiquitinationQRLPSLDKAGRSFSL
HHCCCCCCCCCCEEE
59.0223749301
479PhosphorylationSLDKAGRSFSLHRMD
CCCCCCCCEEEEEEE
20.4728889911
481PhosphorylationDKAGRSFSLHRMDTQ
CCCCCCEEEEEEEEE
25.2228889911
487PhosphorylationFSLHRMDTQMTLSGD
EEEEEEEEEEEEECC
15.7622369663
490PhosphorylationHRMDTQMTLSGDEGE
EEEEEEEEEECCCCC
14.1422369663
492PhosphorylationMDTQMTLSGDEGEAE
EEEEEEEECCCCCCC
34.7222369663
505UbiquitinationAEEGGGRKGLAGGED
CCCCCCCCCCCCCCC
62.6423749301
565PhosphorylationNKGREIFSSRSKNEM
HHHHHHHHCCCCCCC
30.4219823750
566PhosphorylationKGREIFSSRSKNEMY
HHHHHHHCCCCCCCC
29.8019823750
568PhosphorylationREIFSSRSKNEMYDD
HHHHHCCCCCCCCCH
41.6117330950
569UbiquitinationEIFSSRSKNEMYDDD
HHHHCCCCCCCCCHH
56.6823749301
573PhosphorylationSRSKNEMYDDDELND
CCCCCCCCCHHHHHH
15.2717330950
623PhosphorylationDEEEDEYTPEKEYSD
CCCCCCCCCCHHCCC
23.9528889911
628PhosphorylationEYTPEKEYSDNYNNT
CCCCCHHCCCCCCCC
32.1828889911
629PhosphorylationYTPEKEYSDNYNNTP
CCCCHHCCCCCCCCC
22.0728889911
637PhosphorylationDNYNNTPSFESSERS
CCCCCCCCCCCCCCC
39.3428889911
663PhosphorylationNRYDGEETESEIESE
CCCCCCCCHHHHCCH
40.2723749301
665PhosphorylationYDGEETESEIESEDE
CCCCCCHHHHCCHHH
51.8223749301
669PhosphorylationETESEIESEDEMENE
CCHHHHCCHHHHCCH
56.8823749301
680PhosphorylationMENESERSMASSEER
HCCHHHHHHCHHHHH
18.0428889911
683PhosphorylationESERSMASSEERRIR
HHHHHHCHHHHHHHH
29.6419795423
684PhosphorylationSERSMASSEERRIRK
HHHHHCHHHHHHHHH
33.6619795423
698UbiquitinationKMKEEEMKPGTAYLD
HHHHHHCCCCCEEEC
43.5023749301
736PhosphorylationEARDDEVSVDSTAHS
HHCCCCCCCCHHHCH
20.4019795423
739PhosphorylationDDEVSVDSTAHSSLT
CCCCCCCHHHCHHCC
25.9019795423
740PhosphorylationDEVSVDSTAHSSLTT
CCCCCCHHHCHHCCH
24.7519795423
743PhosphorylationSVDSTAHSSLTTTMT
CCCHHHCHHCCHHHH
25.2819795423
744PhosphorylationVDSTAHSSLTTTMTN
CCHHHCHHCCHHHHC
21.6219795423
746PhosphorylationSTAHSSLTTTMTNLS
HHHCHHCCHHHHCCC
23.3619795423
747PhosphorylationTAHSSLTTTMTNLSS
HHCHHCCHHHHCCCC
21.6219795423
748PhosphorylationAHSSLTTTMTNLSSS
HCHHCCHHHHCCCCC
19.4319795423
750PhosphorylationSSLTTTMTNLSSSSG
HHCCHHHHCCCCCCC
30.8019795423
753PhosphorylationTTTMTNLSSSSGGRL
CHHHHCCCCCCCCCE
30.1819795423
754PhosphorylationTTMTNLSSSSGGRLK
HHHHCCCCCCCCCEE
31.5219795423
755PhosphorylationTMTNLSSSSGGRLKR
HHHCCCCCCCCCEEE
29.6219795423
756PhosphorylationMTNLSSSSGGRLKRI
HHCCCCCCCCCEEEE
47.4119795423
765PhosphorylationGRLKRILTPTSLGKI
CCEEEEECCCCHHHH
23.3422369663
767PhosphorylationLKRILTPTSLGKIHS
EEEEECCCCHHHHHH
31.2022369663
768PhosphorylationKRILTPTSLGKIHSL
EEEECCCCHHHHHHH
36.0122369663
774PhosphorylationTSLGKIHSLVDKGKD
CCHHHHHHHHHCCCC
33.2922369663
817PhosphorylationYKINPHKSDDDKSKN
EECCCCCCCCCHHCC
43.1527717283
830PhosphorylationKNRPRNDSVVSRALT
CCCCCCHHHHHHHHH
28.1523749301
833PhosphorylationPRNDSVVSRALTAVG
CCCHHHHHHHHHHHC
15.0724961812
837PhosphorylationSVVSRALTAVGLKSK
HHHHHHHHHHCCHHH
20.5028889911
874PhosphorylationPGMLKKRTLTPAPPR
CCCCCCCCCCCCCCC
43.8119684113
876PhosphorylationMLKKRTLTPAPPRGV
CCCCCCCCCCCCCCC
19.4519684113
918PhosphorylationYDDNAYESETEFERQ
CCCCHHHCHHHHHHH
36.8228889911

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 NAH1_YEAST !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of NAH1_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 NAH1_YEAST !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
HOG1_YEASTHOG1physical
15294160
NAH1_YEASTNHA1physical
16360116
PPZ1_YEASTPPZ1physical
18467557
MNR2_YEASTMNR2physical
16093310
ARL1_YEASTARL1genetic
20659170
KHA1_YEASTKHA1genetic
20659170
NHX1_YEASTNHX1genetic
20659170
VCX1_YEASTVCX1genetic
20709757
SST2_YEASTSST2genetic
20526336
TOR2_YEASTTOR2genetic
20526336
PYC2_YEASTPYC2genetic
21623372
ADE_YEASTAAH1genetic
21623372
6PGD1_YEASTGND1genetic
21623372
IPT1_YEASTIPT1genetic
21623372
ODO2_YEASTKGD2genetic
21623372
THRC_YEASTTHR4genetic
21623372
CEM1_YEASTCEM1genetic
21623372
PDC6_YEASTPDC6genetic
21623372
ARA1_YEASTARA1genetic
21623372
ARGJ_YEASTARG7genetic
21623372
GUP1_YEASTGUP1genetic
21623372
ATPA_YEASTATP1genetic
21623372
GLYM_YEASTSHM1genetic
21623372
ATN1_YEASTENA1genetic
22329368
TOK1_YEASTTOK1genetic
22329368
BMH2_YEASTBMH2physical
22484491
VHC1_YEASTVHC1genetic
23022132
VNX1_YEASTVNX1genetic
23022132
PRY2_YEASTPRY2genetic
27708008
BUD21_YEASTBUD21genetic
27708008
VAM3_YEASTVAM3genetic
27708008
BUD14_YEASTBUD14genetic
27708008
ALG3_YEASTALG3genetic
27708008
PP2C4_YEASTPTC4genetic
27708008
YB9Z_YEASTYBR284Wgenetic
27708008
IMG2_YEASTIMG2genetic
27708008
LSM6_YEASTLSM6genetic
27708008
ATO3_YEASTATO3genetic
27708008
HPRT_YEASTHPT1genetic
27708008
SCS2_YEASTSCS2genetic
27708008
DLDH_YEASTLPD1genetic
27708008
OTU1_YEASTOTU1genetic
27708008
RGD2_YEASTRGD2genetic
27708008
CSK2B_YEASTCKB1genetic
27708008
FKS2_YEASTGSC2genetic
27708008
SMI1_YEASTSMI1genetic
27708008
AP3B_YEASTAPL6genetic
27708008
WSS1_YEASTWSS1genetic
27708008
FMC1_YEASTFMC1genetic
27708008
IF4A_YEASTTIF2genetic
27708008
YJO4_YEASTYJL144Wgenetic
27708008
MOG1_YEASTMOG1genetic
27708008
YJ9J_YEASTYJR142Wgenetic
27708008
IXR1_YEASTIXR1genetic
27708008
RGT1_YEASTRGT1genetic
27708008
PHD1_YEASTPHD1genetic
27708008
MDHM_YEASTMDH1genetic
27708008
TVP38_YEASTTVP38genetic
27708008
SKG1_YEASTSKG1genetic
27708008
HFA1_YEASTHFA1genetic
27708008
SIN3_YEASTSIN3genetic
27708008
OST3_YEASTOST3genetic
27708008
ODC1_YEASTODC1genetic
27708008
ERV14_YEASTERV14physical
26440927
ERV14_YEASTERV14genetic
26440927

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of NAH1_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-447; THR-765; SER-768AND SER-918, AND MASS SPECTROMETRY.
"Proteome-wide identification of in vivo targets of DNA damagecheckpoint kinases.";
Smolka M.B., Albuquerque C.P., Chen S.H., Zhou H.;
Proc. Natl. Acad. Sci. U.S.A. 104:10364-10369(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-447; SER-492 ANDTHR-765, AND MASS SPECTROMETRY.
"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-568, AND MASSSPECTROMETRY.
"Large-scale phosphorylation analysis of alpha-factor-arrestedSaccharomyces cerevisiae.";
Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,Elias J.E., Gygi S.P.;
J. Proteome Res. 6:1190-1197(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-568; THR-765; SER-768AND SER-774, AND MASS SPECTROMETRY.
"Quantitative phosphoproteomics applied to the yeast pheromonesignaling pathway.";
Gruhler A., Olsen J.V., Mohammed S., Mortensen P., Faergeman N.J.,Mann M., Jensen O.N.;
Mol. Cell. Proteomics 4:310-327(2005).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-472, AND MASSSPECTROMETRY.

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