IPMK_YEAST - dbPTM
IPMK_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID IPMK_YEAST
UniProt AC P07250
Protein Name Inositol polyphosphate multikinase
Gene Name ARG82
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 355
Subcellular Localization Nucleus .
Protein Description Has kinase activity and phosphorylates inositol 1,4,5-trisphosphate (Ins(1,4,5)P3) and inositol 1,3,4,5-tetrakisphosphate (Ins(1,3,4,5)P4). Has low kinase activity towards InsP6. With ARG80, ARG81 and MCM1, coordinates the expression of arginine anabolic and catabolic genes in response to arginine. Recruits ARG80 and MCM21 to stabilize them..
Protein Sequence MDTVNNYRVLEHKAAGHDGTLTDGDGLLIFKPAFPQELEFYKAIQVRDVSRRKSSADGDAPLCSWMPTYLGVLNEGAKIEQSGDAALLKIDERLSDSTDNLDSIPVKSEKSKQYLVLENLLYGFSKPNILDIKLGKTLYDSKASLEKRERMKRVSETTTSGSLGFRICGMKIQKNPSVLNQLSLEYYEEEADSDYIFINKLYGRSRTDQNVSDAIELYFNNPHLSDARKHQLKKTFLKRLQLFYNTMLEEEVRMISSSLLFIYEGDPERWELLNDVDKLMRDDFIDDDDDDDDNDDDDDDDAEGSSEGPKDKKTTGSLSSMSLIDFAHSEITPGKGYDENVIEGVETLLDIFMKF
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
1Acetylation-------MDTVNNYR
-------CCCCCCEE
9.8222814378
54PhosphorylationRDVSRRKSSADGDAP
CCCCCCCCCCCCCCC
29.0119779198
55PhosphorylationDVSRRKSSADGDAPL
CCCCCCCCCCCCCCH
33.1521440633
95PhosphorylationLKIDERLSDSTDNLD
EEHHHHHCCCCCCCC
35.4222369663
97PhosphorylationIDERLSDSTDNLDSI
HHHHHCCCCCCCCCC
33.9922369663
98PhosphorylationDERLSDSTDNLDSIP
HHHHCCCCCCCCCCC
33.6222369663
103PhosphorylationDSTDNLDSIPVKSEK
CCCCCCCCCCCCCHH
31.7722369663
108PhosphorylationLDSIPVKSEKSKQYL
CCCCCCCCHHHHHEE
50.9529136822
177PhosphorylationMKIQKNPSVLNQLSL
EEECCCHHHHHHHHH
48.9428889911
305PhosphorylationDDDDAEGSSEGPKDK
CCCCCCCCCCCCCCC
19.4021440633
306PhosphorylationDDDAEGSSEGPKDKK
CCCCCCCCCCCCCCC
58.3819779198
314PhosphorylationEGPKDKKTTGSLSSM
CCCCCCCCCCCCCHH
41.9721126336
315PhosphorylationGPKDKKTTGSLSSMS
CCCCCCCCCCCCHHC
33.3821126336

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 IPMK_YEAST !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of IPMK_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 IPMK_YEAST !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
ARGR1_YEASTARG80physical
12828642
MCM1_YEASTMCM1physical
12828642
ARGR1_YEASTARG80physical
10632874
MCM1_YEASTMCM1physical
10632874
MCM1_YEASTMCM1genetic
8043104
IPK1_YEASTIPK1genetic
15944147
ARGR1_YEASTARG80physical
18719252
MCM1_YEASTMCM1physical
18719252
PP2C1_YEASTPTC1genetic
21127252
HIR1_YEASTHIR1genetic
21127252
KCS1_YEASTKCS1genetic
21127252
DUN1_YEASTDUN1genetic
21127252
RTG3_YEASTRTG3genetic
21127252
PLC1_YEASTPLC1genetic
22153127
YVC1_YEASTYVC1genetic
22153127
IPMK_YEASTARG82physical
22940862

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of IPMK_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-95; SER-97; THR-98 ANDSER-177, 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-97, AND MASSSPECTROMETRY.

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