MNR2_YEAST - dbPTM
MNR2_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID MNR2_YEAST
UniProt AC P35724
Protein Name Manganese resistance protein MNR2
Gene Name MNR2
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 969
Subcellular Localization Membrane
Multi-pass membrane protein.
Protein Description
Protein Sequence MSTDNSQKDEGVPLLSPYSSSPQLRKKKRNQKRRKDKFVGHLKSDSRRPTQLLHDNLQHNHGQITDFDQIDSWGMLHESDSTSNDIIKSEDPSLKGAFIDHRPSMSQPREGPQSVSSTVQPQPIMKFSTPSYKKPAGLRPSDQNRSLVSDLSPSELESWLKRRKSVHKSFVDENSPTDRRQSNANNDVVIDVDALMNHVNNNASTGVNDNSKRRKKKRGSDDSSNKNSKSTSSDSNDEEDEYNSRPSSSLSSNNSSLDDVCLVLDDEGSEVPKAWPDCTVLEEFSKEETERLRSQAIQDAEAFHFQYDEDEEDGTSNEDGILFSKPIVTNIDVPELGNRRVNETENLKNGRLRPKRIAPWHLIQRPMVLGSNSTKDSKSRIQSGLQDNLLVGRNIQYPPHIISNNPEHFRFTYFRVDLDSTVHSPTISGLLQPGQKFQDLFVASIYSQDNSAGHIKTHPNSPTPGIKAETVSQLQGLTAKNPSTLSSMSVANIEDVPPFWLDVSNPTEEEMKILSKAFGIHPLTTEDIFLGEVREKVELFRDYYLICFRSFDIVAEKHVRRRRKEKQESATLDHESISRRKSQAYGATMSNESNANNNNSTSNASRSKWLPSILRARRRSSANRTTNTSSSSYKRRVKSEKKKMEENEKFKRKSGDRHKPREGELEPLNVYIIVFRTGVLTFHFAPTPHPINVRRRARLLKDYLNVTSDWIAYALIDDITDAFAPMIELIEDEVYEIEDAILKMHQSDDSSDSDSSDSDSDSGASDEDAFPFDVYSKKTSYSSAKSSVSSRSMSTSEASFNANLIGWKRKGDMLRRIGECRKRVMSILRLLGSKADVIKGFAKRYNEQWEASPQSEIAMYLGDIQDHIVTMVSSLNHYEKLLSRSHSNYLAQINIDMTKVNNDMNDVLGKITILGTIVLPMNVITGLWGMNVIVPGQYRDSLTWFIGIVLFMCMLACSAYMYTKRRFGF
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------MSTDNSQKD
------CCCCCCCCC		44.4619795423
3Phosphorylation-----MSTDNSQKDE
-----CCCCCCCCCC		37.5919795423
6Phosphorylation--MSTDNSQKDEGVP
--CCCCCCCCCCCCC		41.2219823750
16PhosphorylationDEGVPLLSPYSSSPQ
CCCCCCCCCCCCCHH		29.4929136822
18PhosphorylationGVPLLSPYSSSPQLR
CCCCCCCCCCCHHHH		20.1525521595
19PhosphorylationVPLLSPYSSSPQLRK
CCCCCCCCCCHHHHH		27.9425521595
20PhosphorylationPLLSPYSSSPQLRKK
CCCCCCCCCHHHHHH		39.9529136822
21PhosphorylationLLSPYSSSPQLRKKK
CCCCCCCCHHHHHHH		15.6619823750
89PhosphorylationTSNDIIKSEDPSLKG
CCCCCCCCCCCCCCC		36.5028889911
93PhosphorylationIIKSEDPSLKGAFID
CCCCCCCCCCCCCCC		55.8428889911
104PhosphorylationAFIDHRPSMSQPREG
CCCCCCCCCCCCCCC		30.9025005228
106PhosphorylationIDHRPSMSQPREGPQ
CCCCCCCCCCCCCCC		41.1721440633
114PhosphorylationQPREGPQSVSSTVQP
CCCCCCCCCCCCCCC		27.4017330950
116PhosphorylationREGPQSVSSTVQPQP
CCCCCCCCCCCCCCC		26.0728152593
117PhosphorylationEGPQSVSSTVQPQPI
CCCCCCCCCCCCCCC		30.3717330950
118PhosphorylationGPQSVSSTVQPQPIM
CCCCCCCCCCCCCCE		18.6917330950
129PhosphorylationQPIMKFSTPSYKKPA
CCCEECCCCCCCCCC		21.2728889911
141PhosphorylationKPAGLRPSDQNRSLV
CCCCCCCCHHCCCCC		45.4521440633
146PhosphorylationRPSDQNRSLVSDLSP
CCCHHCCCCCCCCCH		40.4429136822
149PhosphorylationDQNRSLVSDLSPSEL
HHCCCCCCCCCHHHH		37.8229136822
152PhosphorylationRSLVSDLSPSELESW
CCCCCCCCHHHHHHH		31.2222369663
154PhosphorylationLVSDLSPSELESWLK
CCCCCCHHHHHHHHH		51.9820377248
158PhosphorylationLSPSELESWLKRRKS
CCHHHHHHHHHHCHH		50.7829136822
165PhosphorylationSWLKRRKSVHKSFVD
HHHHHCHHHHHHHCC		27.8727017623
169PhosphorylationRRKSVHKSFVDENSP
HCHHHHHHHCCCCCC		18.6722369663
175PhosphorylationKSFVDENSPTDRRQS
HHHCCCCCCCCHHHH		27.4222369663
177PhosphorylationFVDENSPTDRRQSNA
HCCCCCCCCHHHHCC		41.7922369663
182PhosphorylationSPTDRRQSNANNDVV
CCCCHHHHCCCCCEE		35.7819684113
204PhosphorylationNHVNNNASTGVNDNS
HHHCCCCCCCCCCCH		28.0219823750
205PhosphorylationHVNNNASTGVNDNSK
HHCCCCCCCCCCCHH		42.6219823750
211PhosphorylationSTGVNDNSKRRKKKR
CCCCCCCHHHCCHHC		30.3319823750
223PhosphorylationKKRGSDDSSNKNSKS
HHCCCCCCCCCCCCC		40.5828889911
269PhosphorylationLVLDDEGSEVPKAWP
EEECCCCCCCCCCCC		33.1127214570
371PhosphorylationQRPMVLGSNSTKDSK
CCCEECCCCCCCCHH		24.3630377154
374PhosphorylationMVLGSNSTKDSKSRI
EECCCCCCCCHHHHH		43.0230377154
377PhosphorylationGSNSTKDSKSRIQSG
CCCCCCCHHHHHHHH		33.8030377154
383PhosphorylationDSKSRIQSGLQDNLL
CHHHHHHHHCCCCCE		38.8223749301
424PhosphorylationDLDSTVHSPTISGLL
ECCCCCCCCCHHHHC		21.2823749301
447PhosphorylationLFVASIYSQDNSAGH
EEEEEEECCCCCCCC		29.4124961812
451PhosphorylationSIYSQDNSAGHIKTH
EEECCCCCCCCCCCC		43.8724961812
457PhosphorylationNSAGHIKTHPNSPTP
CCCCCCCCCCCCCCC		41.8022890988
461PhosphorylationHIKTHPNSPTPGIKA
CCCCCCCCCCCCCCH		34.3022369663
463PhosphorylationKTHPNSPTPGIKAET
CCCCCCCCCCCCHHH		33.6922369663
470PhosphorylationTPGIKAETVSQLQGL
CCCCCHHHHHHHCCC		30.2528889911
472PhosphorylationGIKAETVSQLQGLTA
CCCHHHHHHHCCCCC		32.3725533186
478PhosphorylationVSQLQGLTAKNPSTL
HHHHCCCCCCCCCCC		42.2729688323
486PhosphorylationAKNPSTLSSMSVANI
CCCCCCCCCCCCCCC		24.8821440633
487PhosphorylationKNPSTLSSMSVANIE
CCCCCCCCCCCCCCC		20.4221440633
516UbiquitinationEEMKILSKAFGIHPL
HHHHHHHHHHCCCCC		44.2717644757
557AcetylationSFDIVAEKHVRRRRK
HHHHHHHHHHHHHHH		37.3524489116
564UbiquitinationKHVRRRRKEKQESAT
HHHHHHHHHHHHHCC		68.4117644757
566UbiquitinationVRRRRKEKQESATLD
HHHHHHHHHHHCCCC		63.5023749301
569PhosphorylationRRKEKQESATLDHES
HHHHHHHHCCCCHHH		24.8622369663
571PhosphorylationKEKQESATLDHESIS
HHHHHHCCCCHHHHH		41.8322369663
576PhosphorylationSATLDHESISRRKSQ
HCCCCHHHHHHHHHH		23.5722369663
578PhosphorylationTLDHESISRRKSQAY
CCCHHHHHHHHHHHH		35.0022369663
581UbiquitinationHESISRRKSQAYGAT
HHHHHHHHHHHHCCC		45.9023749301
582PhosphorylationESISRRKSQAYGATM
HHHHHHHHHHHCCCC		20.4520377248
585PhosphorylationSRRKSQAYGATMSNE
HHHHHHHHCCCCCCC		10.3119779198
588PhosphorylationKSQAYGATMSNESNA
HHHHHCCCCCCCCCC		19.4421440633
590PhosphorylationQAYGATMSNESNANN
HHHCCCCCCCCCCCC		32.8420377248
593PhosphorylationGATMSNESNANNNNS
CCCCCCCCCCCCCCC		45.5520377248
600PhosphorylationSNANNNNSTSNASRS
CCCCCCCCCCCHHHH		35.0220377248
601PhosphorylationNANNNNSTSNASRSK
CCCCCCCCCCHHHHH		28.2921440633
602PhosphorylationANNNNSTSNASRSKW
CCCCCCCCCHHHHHH		30.1620377248
605PhosphorylationNNSTSNASRSKWLPS
CCCCCCHHHHHHHHH		41.1420377248
607PhosphorylationSTSNASRSKWLPSIL
CCCCHHHHHHHHHHH		26.2020377248
612PhosphorylationSRSKWLPSILRARRR
HHHHHHHHHHHHHHH		31.8922890988
626PhosphorylationRSSANRTTNTSSSSY
HHHCCCCCCCCCHHH		33.0128889911
628PhosphorylationSANRTTNTSSSSYKR
HCCCCCCCCCHHHHH		28.0830377154
629PhosphorylationANRTTNTSSSSYKRR
CCCCCCCCCHHHHHH		30.2323749301
630PhosphorylationNRTTNTSSSSYKRRV
CCCCCCCCHHHHHHH		22.6730377154
631PhosphorylationRTTNTSSSSYKRRVK
CCCCCCCHHHHHHHH		37.1423749301
632PhosphorylationTTNTSSSSYKRRVKS
CCCCCCHHHHHHHHH		36.3027214570
783PhosphorylationSKKTSYSSAKSSVSS
CCCCCCCCCCHHCCC		31.3328889911
792PhosphorylationKSSVSSRSMSTSEAS
CHHCCCCCCCCCCHH		21.0227017623
794PhosphorylationSVSSRSMSTSEASFN
HCCCCCCCCCCHHHC		29.9927017623
834UbiquitinationILRLLGSKADVIKGF
HHHHHCCHHHHHHHH		46.9723749301
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 MNR2_YEAST !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of MNR2_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 MNR2_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
ALR1_YEASTALR1genetic
19720860
ALR2_YEASTALR2genetic
19720860
ATG9_YEASTATG9physical
16093310
GLU2A_YEASTROT2physical
22940862
MNR2_YEASTMNR2physical
22940862
SNF5_YEASTSNF5genetic
27708008
HSP78_YEASTHSP78genetic
27708008
CND2_YEASTBRN1genetic
27708008
POP7_YEASTPOP7genetic
27708008
APC11_YEASTAPC11genetic
27708008
CDC1_YEASTCDC1genetic
27708008
RIFK_YEASTFMN1genetic
27708008
TFB1_YEASTTFB1genetic
27708008
SP110_YEASTSPC110genetic
27708008
NCS1_YEASTFRQ1genetic
27708008
SMT3_YEASTSMT3genetic
27708008
RPN11_YEASTRPN11genetic
27708008
SAD1_YEASTSAD1genetic
27708008
PRS8_YEASTRPT6genetic
27708008
NBP35_YEASTNBP35genetic
27708008
PRP18_YEASTPRP18genetic
27708008
CBF3A_YEASTCBF2genetic
27708008
BRL1_YEASTBRL1genetic
27708008
FDFT_YEASTERG9genetic
27708008
CTF8_YEASTCTF8genetic
27708008
NUP85_YEASTNUP85genetic
27708008
FIP1_YEASTFIP1genetic
27708008
VTI1_YEASTVTI1genetic
27708008
PRS10_YEASTRPT4genetic
27708008
TIM50_YEASTTIM50genetic
27708008
ATC3_YEASTDRS2genetic
27708008
SHG1_YEASTSHG1genetic
27708008
YCQ6_YEASTYCR016Wgenetic
27708008
YCY0_YEASTYCR090Cgenetic
27708008
TGL2_YEASTTGL2genetic
27708008
SAC3_YEASTSAC3genetic
27708008
SNX41_YEASTSNX41genetic
27708008
AIM11_YEASTAIM11genetic
27708008
RL8A_YEASTRPL8Agenetic
27708008
ATP18_YEASTATP18genetic
27708008
PML39_YEASTPML39genetic
27708008
PET8_YEASTPET8genetic
27708008
IES4_YEASTIES4genetic
27708008
GGPPS_YEASTBTS1genetic
27708008
RBD2_YEASTRBD2genetic
27708008
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of MNR2_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-21; SER-114; SER-175;SER-472 AND SER-576, 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 SER-175; SER-461 ANDTHR-463, 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 THR-571 AND SER-576, ANDMASS SPECTROMETRY.
"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-114, AND MASSSPECTROMETRY.

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