IPMK_HUMAN - dbPTM
IPMK_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID IPMK_HUMAN
UniProt AC Q8NFU5
Protein Name Inositol polyphosphate multikinase
Gene Name IPMK
Organism Homo sapiens (Human).
Sequence Length 416
Subcellular Localization Nucleus .
Protein Description Inositol phosphate kinase with a broad substrate specificity. Has a preference for inositol 1,4,5-trisphosphate (Ins(1,4,5)P3) and inositol 1,3,4,6-tetrakisphosphate (Ins(1,3,4,6)P4)..
Protein Sequence MATEPPSPLRVEAPGPPEMRTSPAIESTPEGTPQPAGGRLRFLNGCVPLSHQVAGHMYGKDKVGILQHPDGTVLKQLQPPPRGPRELEFYNMVYAADCFDGVLLELRKYLPKYYGIWSPPTAPNDLYLKLEDVTHKFNKPCIMDVKIGQKSYDPFASSEKIQQQVSKYPLMEEIGFLVLGMRVYHVHSDSYETENQHYGRSLTKETIKDGVSRFFHNGYCLRKDAVAASIQKIEKILQWFENQKQLNFYASSLLFVYEGSSQPTTTKLNDRTLAEKFLSKGQLSDTEVLEYNNNFHVLSSTANGKIESSVGKSLSKMYARHRKIYTKKHHSQTSLKVENLEQDNGWKSMSQEHLNGNVLSQLEKVFYHLPTGCQEIAEVEVRMIDFAHVFPSNTIDEGYVYGLKHLISVLRSILDN
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
2Acetylation------MATEPPSPL
------CCCCCCCCC		22.2219369195
3Phosphorylation-----MATEPPSPLR
-----CCCCCCCCCC		47.9623186163
7Phosphorylation-MATEPPSPLRVEAP
-CCCCCCCCCCCCCC		47.4825159151
21PhosphorylationPGPPEMRTSPAIEST
CCCCCCCCCCCCCCC		37.4418691976
22PhosphorylationGPPEMRTSPAIESTP
CCCCCCCCCCCCCCC		11.2818691976
27PhosphorylationRTSPAIESTPEGTPQ
CCCCCCCCCCCCCCC		43.0517192257
28PhosphorylationTSPAIESTPEGTPQP
CCCCCCCCCCCCCCC		16.7517192257
32PhosphorylationIESTPEGTPQPAGGR
CCCCCCCCCCCCCCC		19.6527732954
72UbiquitinationILQHPDGTVLKQLQP
EEECCCCCCCCCCCC		30.0022817900
113PhosphorylationLRKYLPKYYGIWSPP
HHHHCCHHCCCCCCC		12.65-
114PhosphorylationRKYLPKYYGIWSPPT
HHHCCHHCCCCCCCC		14.30-
118PhosphorylationPKYYGIWSPPTAPND
CHHCCCCCCCCCCCC		21.05-
136UbiquitinationKLEDVTHKFNKPCIM
EHHHCCHHCCCCEEE		41.0729967540
139UbiquitinationDVTHKFNKPCIMDVK
HCCHHCCCCEEEEEE		44.3829967540
150UbiquitinationMDVKIGQKSYDPFAS
EEEEECCCCCCCCCC		45.8529967540
160UbiquitinationDPFASSEKIQQQVSK
CCCCCHHHHHHHHHC		48.0022817900
163UbiquitinationASSEKIQQQVSKYPL
CCHHHHHHHHHCCHH		49.4622817900
208AcetylationSLTKETIKDGVSRFF
CCCHHHHHHHHHHHH		56.7119817419
223UbiquitinationHNGYCLRKDAVAASI
CCCEECCHHHHHHHH		36.7729967540
229PhosphorylationRKDAVAASIQKIEKI
CHHHHHHHHHHHHHH		18.80-
232AcetylationAVAASIQKIEKILQW
HHHHHHHHHHHHHHH		51.6825953088
232UbiquitinationAVAASIQKIEKILQW
HHHHHHHHHHHHHHH		51.6829967540
251PhosphorylationKQLNFYASSLLFVYE
HHHEEEEEEEEEEEC		15.3322468782
252PhosphorylationQLNFYASSLLFVYEG
HHEEEEEEEEEEECC		22.4122468782
257PhosphorylationASSLLFVYEGSSQPT
EEEEEEEECCCCCCC		13.7722468782
266PhosphorylationGSSQPTTTKLNDRTL
CCCCCCCCCCCHHHH		35.69-
312AcetylationKIESSVGKSLSKMYA
EEECCHHHHHHHHHH		46.1725953088
312UbiquitinationKIESSVGKSLSKMYA
EEECCHHHHHHHHHH		46.1729967540
315O-linked_GlycosylationSSVGKSLSKMYARHR
CCHHHHHHHHHHHHH		23.5930379171
318PhosphorylationGKSLSKMYARHRKIY
HHHHHHHHHHHHHHH		12.29-
325PhosphorylationYARHRKIYTKKHHSQ
HHHHHHHHCCCCCCC		18.62-
333PhosphorylationTKKHHSQTSLKVENL
CCCCCCCCEEEEEEC		38.76-
334PhosphorylationKKHHSQTSLKVENLE
CCCCCCCEEEEEECH		20.68-
348PhosphorylationEQDNGWKSMSQEHLN
HHCCCCHHCCHHHHC		19.7019369195
350PhosphorylationDNGWKSMSQEHLNGN
CCCCHHCCHHHHCCC		39.2427050516
360PhosphorylationHLNGNVLSQLEKVFY
HHCCCHHHHHHHHHH		28.56-
367PhosphorylationSQLEKVFYHLPTGCQ
HHHHHHHHHCCCCCH		12.8727642862
412PhosphorylationHLISVLRSILDN---
HHHHHHHHHHCC---		24.2817081983
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_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

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

Oops, there are no PPI records of IPMK_HUMAN !!
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of IPMK_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Large-scale proteomics analysis of the human kinome.";
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,Mann M., Daub H.;
Mol. Cell. Proteomics 8:1751-1764(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-7; THR-21; SER-22;SER-348 AND SER-350, AND MASS SPECTROMETRY.
"Kinase-selective enrichment enables quantitative phosphoproteomics ofthe kinome across the cell cycle.";
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,Greff Z., Keri G., Stemmann O., Mann M.;
Mol. Cell 31:438-448(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-7, AND MASSSPECTROMETRY.

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