IP6K3_HUMAN - dbPTM
IP6K3_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID IP6K3_HUMAN
UniProt AC Q96PC2
Protein Name Inositol hexakisphosphate kinase 3
Gene Name IP6K3
Organism Homo sapiens (Human).
Sequence Length 410
Subcellular Localization Cytoplasm .
Protein Description Converts inositol hexakisphosphate (InsP6) to diphosphoinositol pentakisphosphate (InsP7/PP-InsP5). Converts 1,3,4,5,6-pentakisphosphate (InsP5) to PP-InsP4..
Protein Sequence MVVQNSADAGDMRAGVQLEPFLHQVGGHMSVMKYDEHTVCKPLVSREQRFYESLPLAMKRFTPQYKGTVTVHLWKDSTGHLSLVANPVKESQEPFKVSTESAAVAIWQTLQQTTGSNGSDCTLAQWPHAQLARSPKESPAKALLRSEPHLNTPAFSLVEDTNGNQVERKSFNPWGLQCHQAHLTRLCSEYPENKRHRFLLLENVVSQYTHPCVLDLKMGTRQHGDDASEEKKARHMRKCAQSTSACLGVRICGMQVYQTDKKYFLCKDKYYGRKLSVEGFRQALYQFLHNGSHLRRELLEPILHQLRALLSVIRSQSSYRFYSSSLLVIYDGQEPPERAPGSPHPHEAPQAAHGSSPGGLTKVDIRMIDFAHTTYKGYWNEHTTYDGPDPGYIFGLENLIRILQDIQEGE
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
34PhosphorylationGHMSVMKYDEHTVCK
CCCEEECCCCCCCCH
14.41-
45PhosphorylationTVCKPLVSREQRFYE
CCCHHCCCHHHHHHH
37.47-
141UbiquitinationSPKESPAKALLRSEP
CCCCCHHHHHHHCCC
42.84-
206PhosphorylationLLLENVVSQYTHPCV
EEHHCHHHHCCCCCE
17.1222210691
208PhosphorylationLENVVSQYTHPCVLD
HHCHHHHCCCCCEEE
10.2622210691
209PhosphorylationENVVSQYTHPCVLDL
HCHHHHCCCCCEEEE
16.2322210691
242PhosphorylationHMRKCAQSTSACLGV
HHHHHHHHHHHHHCH
13.0522817900
243PhosphorylationMRKCAQSTSACLGVR
HHHHHHHHHHHHCHH
14.3022817900
244PhosphorylationRKCAQSTSACLGVRI
HHHHHHHHHHHCHHH
23.4122817900
276PhosphorylationKYYGRKLSVEGFRQA
CCCCEECCHHHHHHH
22.5827499020
315PhosphorylationALLSVIRSQSSYRFY
HHHHHHHCCCCEEEE
24.2428122231
317PhosphorylationLSVIRSQSSYRFYSS
HHHHHCCCCEEEECE
30.5028122231
318PhosphorylationSVIRSQSSYRFYSSS
HHHHCCCCEEEECEE
16.8228122231
319PhosphorylationVIRSQSSYRFYSSSL
HHHCCCCEEEECEEE
15.2528122231
373PhosphorylationRMIDFAHTTYKGYWN
EEEECCCCCCCCCCC
28.5224043423
374PhosphorylationMIDFAHTTYKGYWNE
EEECCCCCCCCCCCC
17.2324043423
375PhosphorylationIDFAHTTYKGYWNEH
EECCCCCCCCCCCCC
11.9924043423

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 IP6K3_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of IP6K3_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 IP6K3_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
M3K3_HUMANMAP3K3physical
26496610
PCCA_HUMANPCCAphysical
26496610
BAG6_HUMANBAG6physical
26496610
UBL4A_HUMANUBL4Aphysical
26496610
TADBP_HUMANTARDBPphysical
26496610
PF21A_HUMANPHF21Aphysical
26496610
SRRT_HUMANSRRTphysical
26496610
ELP3_HUMANELP3physical
26496610
BI2L1_HUMANBAIAP2L1physical
26496610
NU107_HUMANNUP107physical
26496610
PCY1A_HUMANPCYT1Aphysical
28514442
NECA1_HUMANNECAB1physical
28514442
PROZ_HUMANPROZphysical
28514442
ACP7_HUMANPAPLphysical
28514442
T3HPD_HUMANL3HYPDHphysical
28514442

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 IP6K3_HUMAN

loading...

Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Automated phosphoproteome analysis for cultured cancer cells by two-dimensional nanoLC-MS using a calcined titania/C18 biphasic column.";
Imami K., Sugiyama N., Kyono Y., Tomita M., Ishihama Y.;
Anal. Sci. 24:161-166(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-242; THR-243 ANDSER-244, AND MASS SPECTROMETRY.

TOP