GIP4_YEAST - dbPTM
GIP4_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID GIP4_YEAST
UniProt AC P39732
Protein Name GLC7-interacting protein 4
Gene Name GIP4
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 760
Subcellular Localization Cytoplasm .
Protein Description GLC7 phosphatase-regulatory protein involved in GLC7 subcellular redistribution and chromosome segregation..
Protein Sequence MVDVQKRKKLLAKAAASASIPAIKGSVPLDSYDIKIIQYKNALYKLNELNRLLNVLVPHLKKKRDNDESYKIIPLVNFILSLCEGPIFNVSPVLAKRYHLLCRFQLIKLSEVQQRLSTNFIDVEGWMFPEEVPLDHYKSCIYNNSLQWKILNSLSCIAQNAIKIYNAKLRQILLERDAYKARSLPFDTSIIEDLLNPVEMTLILDLAVLINDPVRDKSTHSFYKLQWQVMEKLNSCVHSKIFPILRTYYNQLQKFSETRPTSLSNLQKDLPHWEWTLHRIYTFHLRVFSVLCVIISFSRQIFLPNKQHFLDIKTRLSSENVYHYDLIICELMALLSPECDDVTALFELQENLKFWTQTARTDNNSSRTPIFHLQPGLVVELFNNHICKIIPKLRSIMGLLSNWMDCWKYIEKNYKTFDETNDLRENLKEKLERDKALYLEVKNAKSKLKKKPSITKLPASSSPSPSPTSSASPSRQASLESIRTRARAHLASNSSRSPSVSPVRTTFNNKNAETKKSVVSPEKRKLINGRRPRSSSLQSYTNKQQTSYLNSTRHPSIAPPSKLNNQRSNSLQSSTMTLNQKIVQDTVRHLMNKSASTPNPSASSSLAPSPKVSSINNTSSGKSSSTLIANSSDTLAIETLTLDPESNSSELSIKRVRFAGVPPMTEAENPKPTKVGWYKKPAVLHYPPIPASAMIKPLQHKSKYNTLRQEEGFTFRKSLRDGLEWENGESGSETTMMPFGIEIKESTGHRIASKIRSKLR
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
453PhosphorylationSKLKKKPSITKLPAS
HHHCCCCCCCCCCCC		52.3421440633
455PhosphorylationLKKKPSITKLPASSS
HCCCCCCCCCCCCCC		30.7621440633
460PhosphorylationSITKLPASSSPSPSP
CCCCCCCCCCCCCCC		29.4322890988
461PhosphorylationITKLPASSSPSPSPT
CCCCCCCCCCCCCCC		48.6622890988
462PhosphorylationTKLPASSSPSPSPTS
CCCCCCCCCCCCCCC		27.2321082442
464PhosphorylationLPASSSPSPSPTSSA
CCCCCCCCCCCCCCC		39.7021082442
466PhosphorylationASSSPSPSPTSSASP
CCCCCCCCCCCCCCH		45.1822890988
468PhosphorylationSSPSPSPTSSASPSR
CCCCCCCCCCCCHHH		39.3822890988
469PhosphorylationSPSPSPTSSASPSRQ
CCCCCCCCCCCHHHH		27.5622890988
470PhosphorylationPSPSPTSSASPSRQA
CCCCCCCCCCHHHHH		34.9322890988
472PhosphorylationPSPTSSASPSRQASL
CCCCCCCCHHHHHHH		25.9222890988
474PhosphorylationPTSSASPSRQASLES
CCCCCCHHHHHHHHH		34.2322890988
478PhosphorylationASPSRQASLESIRTR
CCHHHHHHHHHHHHH		25.0825752575
481PhosphorylationSRQASLESIRTRARA
HHHHHHHHHHHHHHH		23.7427214570
492PhosphorylationRARAHLASNSSRSPS
HHHHHHHHCCCCCCC		43.5417563356
494PhosphorylationRAHLASNSSRSPSVS
HHHHHHCCCCCCCCC		25.3219684113
495PhosphorylationAHLASNSSRSPSVSP
HHHHHCCCCCCCCCC		40.8219684113
497PhosphorylationLASNSSRSPSVSPVR
HHHCCCCCCCCCCCE		24.3917330950
499PhosphorylationSNSSRSPSVSPVRTT
HCCCCCCCCCCCEEC		36.1519684113
501PhosphorylationSSRSPSVSPVRTTFN
CCCCCCCCCCEECCC		23.2417330950
505PhosphorylationPSVSPVRTTFNNKNA
CCCCCCEECCCCCCC		35.6521440633
520PhosphorylationETKKSVVSPEKRKLI
CCCCCCCCHHHHHHH		25.7823749301
534PhosphorylationINGRRPRSSSLQSYT
HCCCCCCCCCCHHHC		27.2822369663
535PhosphorylationNGRRPRSSSLQSYTN
CCCCCCCCCCHHHCC		36.0322369663
536PhosphorylationGRRPRSSSLQSYTNK
CCCCCCCCCHHHCCC		31.5122369663
568PhosphorylationSKLNNQRSNSLQSST
HHHCCCCCCCCCCCC		22.4722369663
570PhosphorylationLNNQRSNSLQSSTMT
HCCCCCCCCCCCCCC		29.0922369663
573PhosphorylationQRSNSLQSSTMTLNQ
CCCCCCCCCCCCCCH		32.8229734811
574PhosphorylationRSNSLQSSTMTLNQK
CCCCCCCCCCCCCHH		14.8319823750
575PhosphorylationSNSLQSSTMTLNQKI
CCCCCCCCCCCCHHH		21.3019823750
577PhosphorylationSLQSSTMTLNQKIVQ
CCCCCCCCCCHHHHH		23.7319823750
594PhosphorylationVRHLMNKSASTPNPS
HHHHHHCCCCCCCCC		23.5822369663
596PhosphorylationHLMNKSASTPNPSAS
HHHHCCCCCCCCCCC		52.0322369663
597PhosphorylationLMNKSASTPNPSASS
HHHCCCCCCCCCCCC		27.1420377248
601PhosphorylationSASTPNPSASSSLAP
CCCCCCCCCCCCCCC		47.6320377248
603PhosphorylationSTPNPSASSSLAPSP
CCCCCCCCCCCCCCC		25.4620377248
604PhosphorylationTPNPSASSSLAPSPK
CCCCCCCCCCCCCCC		29.1420377248
605PhosphorylationPNPSASSSLAPSPKV
CCCCCCCCCCCCCCC		26.5120377248
609PhosphorylationASSSLAPSPKVSSIN
CCCCCCCCCCCCCCC		31.5722369663
614PhosphorylationAPSPKVSSINNTSSG
CCCCCCCCCCCCCCC		32.1228889911
649PhosphorylationLDPESNSSELSIKRV
ECCCCCCCCCCEEEE		46.9728889911
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 GIP4_YEAST !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of GIP4_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 GIP4_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of GIP4_YEAST !!
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of GIP4_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-462; SER-464; SER-536;SER-570; SER-609 AND SER-649, 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-492; SER-497 ANDSER-501, AND MASS 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-497 AND SER-501, ANDMASS SPECTROMETRY.

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