KHA1_YEAST - dbPTM
KHA1_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID KHA1_YEAST
UniProt AC P40309
Protein Name K(+)/H(+) antiporter 1
Gene Name KHA1
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 873
Subcellular Localization Membrane
Multi-pass membrane protein .
Protein Description Potassium-proton antiport..
Protein Sequence MANTVGGILSGVNPFHYNSSSPLTLFLFQACLILLVCNLIHIPFSMMRQPKVISEVISGVILGPTIFGQIPNYTNTIFPTSSIPGLNLVANLGIILFMFFLGLEVDIAFIKKHLKKALVIGIVTLAVPFGFGCLLAIPLFHTYANKTEGERHIKFSVFMVFIAVSISVTAFPVLCRILNELRLIKDRAGIVVLAAGIINDIMGWILLALSIILSSAEGSPVNTVYILLITFAWFLIYFFPLKYLLRWVLIRTHELDRSKPSPLATMCILFIMFISAYFTDIIGVHPIFGAFIAGLVVPRDDHYVVKLTERMEDIPNIVFIPIYFAVAGLNVDLTLLNEGRDWGYVFATIGIAIFTKIISGTLTAKLTGLFWREATAAGVLMSCKGIVEIVVLTVGLNAGIISRKIFGMFVLMALVSTFVTTPLTQLVYPDSYRDGVRKSLSTPAEDDGAADGLDSEGVDKTEINTQLNSLADVSKYRIGELTTVINTTEAISPSLKLLNYLSLGVSPKPKNNKHKNETSLSRMTTATDSTLKSNTFKIKKMVHIWSKSVDDVDTNLSVIDEKLTPFEGVGALRAIHLRLLTERTTDLLQSSSLYNDDPHFTANTDSLLQIFDIFSNLSKIPFSSEVIFSTMREKAANIATMKMDSTDLILLPLKGASYEYRGSPVFIDEKYANFDHIYSHLLGLNELSSTFFKSIFQSLKANFAVQISNTYGRLNADRFKRKRFNLLLPKPYLTQSDYLGLYLLLLICYRDGYNNDNASCSIFINSKNIDFAKDLSTAFAEHDWLNESTIKIVDIPFETKVPEEAIEKPSFIETVLDVGLSDTALADIEETTFIIGEDLPDESEPFSEEVRTVIFEGSNRRFDTLIVHHFSSE
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
367PhosphorylationGTLTAKLTGLFWREA
CCHHHHHHCHHHHHH		31.0027017623
455PhosphorylationGAADGLDSEGVDKTE
CCCCCCCCCCCCHHH		41.0921440633
460UbiquitinationLDSEGVDKTEINTQL
CCCCCCCHHHHHHHH		45.7223749301
461PhosphorylationDSEGVDKTEINTQLN
CCCCCCHHHHHHHHH		37.3221440633
519PhosphorylationNKHKNETSLSRMTTA
CCCCCCCCHHHHHHC		20.4025521595
525PhosphorylationTSLSRMTTATDSTLK
CCHHHHHHCCCCCHH		20.4428889911
532UbiquitinationTATDSTLKSNTFKIK
HCCCCCHHHCCEEEE		41.5723749301
548PhosphorylationMVHIWSKSVDDVDTN
EEEEEECCHHHCCCC		25.8427214570
554PhosphorylationKSVDDVDTNLSVIDE
CCHHHCCCCCHHHCC		37.6028152593
557PhosphorylationDDVDTNLSVIDEKLT
HHCCCCCHHHCCCCC		21.0617330950
562UbiquitinationNLSVIDEKLTPFEGV
CCHHHCCCCCCCCCH		54.6423749301
761PhosphorylationNNDNASCSIFINSKN
CCCCCEEEEEEECCC		20.3128889911
773UbiquitinationSKNIDFAKDLSTAFA
CCCCCHHHHHHHHHH		60.2317644757
791UbiquitinationWLNESTIKIVDIPFE
CCCCCCEEEEECCCC		36.4417644757
800UbiquitinationVDIPFETKVPEEAIE
EECCCCCCCCHHHHC		48.9024961812
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 KHA1_YEAST !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of KHA1_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 KHA1_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
NHX1_YEASTNHX1genetic
15659172
TRK1_YEASTTRK1genetic
15659172
TRK2_YEASTTRK2genetic
15659172
ATN1_YEASTENA1genetic
15659172
NAH1_YEASTNHA1genetic
15659172
NHX1_YEASTNHX1genetic
20659170
YPT6_YEASTYPT6genetic
22188384
EXO84_YEASTEXO84genetic
27708008
MCM7_YEASTMCM7genetic
27708008
PDC2_YEASTPDC2genetic
27708008
SEC7_YEASTSEC7genetic
27708008
TFB1_YEASTTFB1genetic
27708008
ACT_YEASTACT1genetic
27708008
PMM_YEASTSEC53genetic
27708008
ATC7_YEASTNEO1genetic
27708008
SEC65_YEASTSEC65genetic
27708008
TYSY_YEASTCDC21genetic
27708008
YBM6_YEASTYBR016Wgenetic
27708008
GAL7_YEASTGAL7genetic
27708008
YBS1_YEASTYBR071Wgenetic
27708008
YMC2_YEASTYMC2genetic
27708008
RMD9L_YEASTYBR238Cgenetic
27708008
IMG2_YEASTIMG2genetic
27708008
VAM7_YEASTVAM7genetic
27708008
RT13_YEASTMRP13genetic
27708008
YM79_YEASTYMR244Wgenetic
27708008
RCF2_YEASTRCF2genetic
27708008
SGT2_YEASTSGT2genetic
27708008
VAM3_YEASTVAM3genetic
27708008
YP162_YEASTYPL162Cgenetic
27708008
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of KHA1_YEAST

loading...

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-455, 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-557, AND MASSSPECTROMETRY.

TOP
© 2024 Institute of Bioinformatics and Systems Biology, NYCU | Designed by : BiOmics Laboratory