IRA1_YEAST - dbPTM
IRA1_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID IRA1_YEAST
UniProt AC P18963
Protein Name Inhibitory regulator protein IRA1
Gene Name IRA1
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 3092
Subcellular Localization Cytoplasm .
Protein Description Inhibitory regulator of the Ras-cyclic AMP pathway in Saccharomyces cerevisiae. Stimulates the GTPase activity of Ras proteins..
Protein Sequence MNQSDPQDKKNFPMEYSLTKHLFFDRLLLVLPIESNLKTYADVEADSVFNSCRSIILNIAITKDLNPIIENTLGLIDLIVQDEEITSDNITDDIAHSILVLLRLLSDVFEYYWDQNNDFKKIRNDNYKPGFSSHRPNFHTSRPKHTRINPALATMLLCKISKLKFNTRTLKVLQNMSHHLSGSATISKSSILPDSQEFLQKRNYPAYTEKIDLTIDYIQRFISASNHVEFTKCVKTKVVAPLLISHTSTELGVVNHLDLFGCEYLTDKNLLAYLDILQHLSSYMKRTIFHSLLLYYASKAFLFWIMARPKEYVKIYNNLISSDYNSPSSSSDNGGSNNSDKTSISQLVSLLFDDVYSTFSVSSLLTNVNNDHHYHLHHSSSSSKTTNTNSPNSISKTSIKQSSVNASGNVSPSQFSTGNDASPTSPMASLSSPLNTNILGYPLSPITSTLGQANTSTSTTAATTKTDADTPSTMNTNNNNNNNNSANLNNIPQRIFSLDDISSFNSSRKSLNLDDSNSLFLWDTSQHSNASMTNTNMHAGVNNSQSQNDQSSLNYMENIMELYSNYTGSELSSHTAILRFLVVLTLLDSEVYDEMNSNSYRKISEPIMNINPKDSNTSSWGSASKNPSIRHLTHGLKKLTLQQGRKRNVKFLTYLIRNLNGGQFVSDVSLIDSIRSILFLMTMTSSISQIDSNIASVIFSKRFYNLLGQNLEVGTNWNSATANTFISHCVERNPLTHRRLQLEFFASGLQLDSDLFLRHLQLEKELNHIDLPKISLYTEGFRVFFHLVSTKKLHEDIAEKTSSVLKRLFCIIADILLKATPYFDDNVTKIIASILDGHILDQFDAARTLSNDDHVSFDAATSVYTEPTEIIHNSSDASLVSSLSQSPLSINSGSNITNTRTWDIQSILPTLSNRSSASDLSLSNILTNPLEAQQNNNANLLAHRLSGVPTTKRYASPNDSERSRQSPYSSPPQLQQSDLPSPLSVLSSSAGFSSNHSITATPTILKNIKSPKPNKTKKIADDKQLKQPSYSRVILSDNDEARKIMMNIFSIFKRMTNWFIRPDANTEFPKTFTDIIKPLFVSILDSNQRLQVTARAFIEIPLSYIATFEDIDNDLDPRVLNDHYLLCTYAVTLFASSLFDLKLENAKREMLLDIIVKFQRVRSYLSNLAEKHNLVQAIITTERLTLPLLVGAVGSGIFISLYCSRGNTPRLIKISCCEFLRSLRFYQKYVGALDQYSIYNIDFIDAMAQDNFTASGSVALQRRLRNNILTYIKGSDSILLDSMDVIYKKWFYFSCSKSVTQEELVDFRSLAGILASMSGILSDMQELEKSKSAPDNEGDSLSFESRNPAYEVHKSLKLELTKKMNFFISKQCQWLNNPNLLTRENSRDILSIELHPLSFNLLFNNLGLKIDELMSIDLSKSHEDSSFVLLEQIIIIIRTILKRDDDEKIMLLFSTDLLDAVDKLIEIVEKISIKSSKYYKGIIQMSKMFRAFEHSEKNLGISNHFHLKNKWLKLVIGWFKLSINKDYDFENLSRPLREMDLQKRDEDFLYIDTSIESAKALAYLTHNVPLEIPPSSSKEDWNRSSTVSFGNHFTILLKGLEKSADLNQFPVSLRHKISILNENVIIALTNLSNANVNVSLKFTLPMGYSPNKDIRIAFLRVFIDIVTNYPVNPEKHEMDKMLAIDDFLKYIIKNPILAFFGSLACSPADVDLYAGGFLNAFDTRNASHILVTELLKQEIKRAARSDDILRRNSCATRALSLYTRSRGNKYLIKTLRPVLQGIVDNKESFEIDKMKPGSENSEKMLDLFEKYMTRLIDAITSSIDDFPIELVDICKTIYNAASVNFPEYAYIAVGSFVFLRFIGPALVSPDSENIIIVTHAHDRKPFITLAKVIQSLANGRENIFKKDILVSKEEFLKTCSDKIFNFLSELCKIPTNNFTVNVREDPTPISFDYSFLHKFFYLNEFTIRKEIINESKLPGEFSFLKNTVMLNDKILGVLGQPSMEIKNEIPPFVVENREKYPSLYEFMSRYAFKKVDMKEEEEDNAPFVHEAMTLDGIQIIVVTFTNCEYNNFVMDSLVYKVLQIYARMWCSKHYVVIDCTTFYGGKANFQKLTTLFFSLIPEQASSNCMGCYYFNVNKSFMDQWASSYTVENPYLVTTIPRCFINSNTDQSLIKSLGLSGRSLEVLKDVRVTLHDITLYDKEKKKFCPVSLKIGNKYFQVLHEIPQLYKVTVSNRTFSIKFNNVYKISNLISVDVSNTTGVSSEFTLSLDNEEKLVFCSPKYLEIVKMFYYAQLKMEEDFGTDFSNDISFSTSSSAVNASYCNVKEVGEIISHLSLVILVGLFNEDDLVKNISYNLLVATQEAFNLDFGTRLHKSPETYVPDDTTTFLALIFKAFSESSTELTPYIWKYMLDGLENDVIPQEHIPTVVCSLSYWVPNLYEHVYLANDEEGPEAISRIIYSLIRLTVKEPNFTTAYLQQIWFLLALDGRLTNVIVEEIVSHALDRDSENRDWMKAVSILTSFPTTEIACQVIEKLINMIKSFLPSLAVEASAHSWSELTILSKISVSIFFESPLLSQMYLPEILFAVSLLIDVGPSEIRVSLYELLMNVCHSLTNNESLPERNRKNLDIVCATFARQKLNFISGFSQEKGRVLPNFAASSFSSKFGTLDLFTKNIMLLMEYGSISEGAQWEAKYKKYLMDAIFGHRSFFSARAMMILGIMSKSHTSLFLCKELLVETMKVFAEPVVDDEQMFIIIAHVFTYSKIVEGLDPSSELMKELFWLATICVESPHPLLFEGGLLFMVNCLKRLYTVHLQLGFDGKSLAKKLMESRNFAATLLAKLESYNGCIWNEDNFPHIILGFIANGLSIPVVKGAALDCLQALFKNTYYERKSNPKSSDYLCYLFLLHLVLSPEQLSTLLLEVGFEDELVPLNNTLKVPLTLINWLSSDSDKSNIVLYQGALLFSCVMSDEPCKFRFALLMRYLLKVNPICVFRFYTLTRKEFRRLSTLEQSSEAVAVSFELIGMLVTHSEFNYLEEFNDEMVELLKKRGLSVVKPLDIFDQEHIEKLKGEGEHQVAIYERKRLATMILARMSCS
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
38UbiquitinationLPIESNLKTYADVEA
EECCCCCCCCCCHHH		43.6817644757
62PhosphorylationIILNIAITKDLNPII
HHHHHHHHCCCHHHH		14.9628889911
207PhosphorylationQKRNYPAYTEKIDLT
HHCCCCHHHCCCCCH		15.7828889911
321PhosphorylationKIYNNLISSDYNSPS
HHHHHHHCCCCCCCC		21.9621551504
322PhosphorylationIYNNLISSDYNSPSS
HHHHHHCCCCCCCCC		36.8021551504
328PhosphorylationSSDYNSPSSSSDNGG
CCCCCCCCCCCCCCC		42.5521440633
331PhosphorylationYNSPSSSSDNGGSNN
CCCCCCCCCCCCCCC		36.7221440633
336PhosphorylationSSSDNGGSNNSDKTS
CCCCCCCCCCCCCCC		33.9521440633
385PhosphorylationHSSSSSKTTNTNSPN
CCCCCCCCCCCCCCC		27.5028889911
390PhosphorylationSKTTNTNSPNSISKT
CCCCCCCCCCCCCCC		24.3423749301
393PhosphorylationTNTNSPNSISKTSIK
CCCCCCCCCCCCCCC		31.4628889911
395PhosphorylationTNSPNSISKTSIKQS
CCCCCCCCCCCCCCC		29.6923749301
397PhosphorylationSPNSISKTSIKQSSV
CCCCCCCCCCCCCCC		28.9721440633
398PhosphorylationPNSISKTSIKQSSVN
CCCCCCCCCCCCCCC		31.3721551504
497PhosphorylationNIPQRIFSLDDISSF
CCCHHHCCHHHHHHC		28.6322369663
502PhosphorylationIFSLDDISSFNSSRK
HCCHHHHHHCCCCCC		35.5530377154
503PhosphorylationFSLDDISSFNSSRKS
CCHHHHHHCCCCCCC		28.8730377154
507PhosphorylationDISSFNSSRKSLNLD
HHHHCCCCCCCCCCC		44.8521551504
615PhosphorylationMNINPKDSNTSSWGS
CCCCCCCCCCCCCCC		48.4028889911
617PhosphorylationINPKDSNTSSWGSAS
CCCCCCCCCCCCCCC		28.2628889911
618PhosphorylationNPKDSNTSSWGSASK
CCCCCCCCCCCCCCC		28.4828889911
619PhosphorylationPKDSNTSSWGSASKN
CCCCCCCCCCCCCCC		33.1628889911
622PhosphorylationSNTSSWGSASKNPSI
CCCCCCCCCCCCCCH		24.1028889911
624PhosphorylationTSSWGSASKNPSIRH
CCCCCCCCCCCCHHH		34.3628889911
628PhosphorylationGSASKNPSIRHLTHG
CCCCCCCCHHHHHHH		41.4723749301
637AcetylationRHLTHGLKKLTLQQG
HHHHHHHHHHHHHHC		50.7825381059
654PhosphorylationRNVKFLTYLIRNLNG
CCHHHHHHHHHHCCC		11.4119779198
676PhosphorylationSLIDSIRSILFLMTM
HHHHHHHHHHHHHHH		23.2127738172
684PhosphorylationILFLMTMTSSISQID
HHHHHHHHCCHHHHC		15.3427738172
688PhosphorylationMTMTSSISQIDSNIA
HHHHCCHHHHCCCHH		24.0327738172
692PhosphorylationSSISQIDSNIASVIF
CCHHHHCCCHHHHHH		31.5927738172
696PhosphorylationQIDSNIASVIFSKRF
HHCCCHHHHHHHHHH		16.3727738172
701UbiquitinationIASVIFSKRFYNLLG
HHHHHHHHHHHHHHC		35.4615699485
892PhosphorylationQSPLSINSGSNITNT
CCCCEECCCCCCCCC		41.7628889911
894PhosphorylationPLSINSGSNITNTRT
CCEECCCCCCCCCCC		25.5328889911
915PhosphorylationLPTLSNRSSASDLSL
HHCCCCCCCCCCCCH		34.2117563356
916PhosphorylationPTLSNRSSASDLSLS
HCCCCCCCCCCCCHH		28.6721440633
918PhosphorylationLSNRSSASDLSLSNI
CCCCCCCCCCCHHHH		40.8219779198
946PhosphorylationNLLAHRLSGVPTTKR
CHHHHHHCCCCCCCC		37.3930377154
956PhosphorylationPTTKRYASPNDSERS
CCCCCCCCCCCCHHH		18.4629136822
966PhosphorylationDSERSRQSPYSSPPQ
CCHHHHCCCCCCCCC		25.3719779198
969PhosphorylationRSRQSPYSSPPQLQQ
HHHCCCCCCCCCCCC		39.4919779198
1332PhosphorylationQELEKSKSAPDNEGD
HHHHHCCCCCCCCCC		52.7221126336
1340PhosphorylationAPDNEGDSLSFESRN
CCCCCCCCCCCCCCC		36.4529136822
1342PhosphorylationDNEGDSLSFESRNPA
CCCCCCCCCCCCCCH		30.8124961812
1345PhosphorylationGDSLSFESRNPAYEV
CCCCCCCCCCCHHHH		35.0329136822
1415PhosphorylationLKIDELMSIDLSKSH
CCHHHHHCCCCCCCC		26.1020377248
1559UbiquitinationDTSIESAKALAYLTH
ECCHHHHHHHHHHHC		53.8917644757
1578UbiquitinationEIPPSSSKEDWNRSS
CCCCCCCCCCCCCCC		62.7317644757
1736UbiquitinationILVTELLKQEIKRAA
HHHHHHHHHHHHHHH		59.5117644757
1753PhosphorylationDDILRRNSCATRALS
CHHHHHCCHHHHHHH		11.87-
1795AcetylationSFEIDKMKPGSENSE
CCCCCCCCCCCCCHH		52.5525381059
1803AcetylationPGSENSEKMLDLFEK
CCCCCHHHHHHHHHH		44.5825381059
2174UbiquitinationNTDQSLIKSLGLSGR
CCCHHHHHHCCCCCC		44.9415699485
2179PhosphorylationLIKSLGLSGRSLEVL
HHHHCCCCCCCHHHH		30.2928889911
3004PhosphorylationRKEFRRLSTLEQSSE
HHHHHHHHCCHHCHH		29.18-
3076PhosphorylationGEHQVAIYERKRLAT
CCHHHEEEHHHHHHH		10.4328889911
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
1753SPhosphorylationKinasePKA-Uniprot
3004SPhosphorylationKinasePKA-Uniprot
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of IRA1_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 IRA1_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
RAS1_YEASTRAS1genetic
2178777
RAS2_YEASTRAS2genetic
2178777
IRA2_YEASTIRA2genetic
2164637
LTE1_YEASTLTE1genetic
7941731
MSI1_YEASTMSI1genetic
2554329
IRA2_YEASTIRA2genetic
9628870
CDC25_YEASTCDC25genetic
10747046
RAEP_YEASTMRS6genetic
8132658
RPI1_YEASTRPI1genetic
12455971
HSP7F_YEASTSSE1genetic
8413180
IRA2_YEASTIRA2genetic
19717739
IRA2_YEASTIRA2genetic
21749328
IRA2_YEASTIRA2genetic
25486365
SYLM_YEASTNAM2genetic
27453043
SYFM_YEASTMSF1genetic
27453043
IRA2_YEASTIRA2genetic
27453043
MTM1_YEASTMTM1genetic
27453043
SNF1_YEASTSNF1genetic
27453043
PHO85_YEASTPHO85genetic
27453043
SCH9_YEASTSCH9genetic
27453043
SSN8_YEASTSSN8genetic
27453043
AAKG_YEASTSNF4genetic
27453043
CDC42_YEASTCDC42genetic
27453043
HFA1_YEASTHFA1genetic
27453043
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of IRA1_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-497; SER-892; SER-1340AND SER-1342, 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-915, AND MASSSPECTROMETRY.

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