INP5K_HUMAN - dbPTM
INP5K_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID INP5K_HUMAN
UniProt AC Q9BT40
Protein Name Inositol polyphosphate 5-phosphatase K {ECO:0000305}
Gene Name INPP5K {ECO:0000312|HGNC:HGNC:33882}
Organism Homo sapiens (Human).
Sequence Length 448
Subcellular Localization Endoplasmic reticulum . Following stimulation with EGF, translocates to membrane ruffles.
Protein Description Inositol 5-phosphatase which acts on inositol 1,4,5-trisphosphate, inositol 1,3,4,5-tetrakisphosphate, phosphatidylinositol 4,5-bisphosphate and phosphatidylinositol 3,4,5-trisphosphate. Has 6-fold higher affinity for phosphatidylinositol 4,5-bisphosphate than for inositol 1,4,5-trisphosphate. [PubMed: 10753883 Negatively regulates assembly of the actin cytoskeleton. Controls insulin-dependent glucose uptake among inositol 3,4,5-trisphosphate phosphatases; therefore, is the specific regulator for insulin signaling in skeletal muscle (By similarity]
Protein Sequence MSSRKLSGPKGRRLSIHVVTWNVASAAPPLDLSDLLQLNNRNLNLDIYVIGLQELNSGIISLLSDAAFNDSWSSFLMDVLSPLSFIKVSHVRMQGILLLVFAKYQHLPYIQILSTKSTPTGLFGYWGNKGGVNICLKLYGYYVSIINCHLPPHISNNYQRLEHFDRILEMQNCEGRDIPNILDHDLIIWFGDMNFRIEDFGLHFVRESIKNRCYGGLWEKDQLSIAKKHDPLLREFQEGRLLFPPTYKFDRNSNDYDTSEKKRKPAWTDRILWRLKRQPCAGPDTPIPPASHFSLSLRGYSSHMTYGISDHKPVSGTFDLELKPLVSAPLIVLMPEDLWTVENDMMVSYSSTSDFPSSPWDWIGLYKVGLRDVNDYVSYAWVGDSKVSCSDNLNQVYIDISNIPTTEDEFLLCYYSNSLRSVVGISRPFQIPPGSLREDPLGEAQPQI
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
7Phosphorylation-MSSRKLSGPKGRRL
-CCCCCCCCCCCCCE
56.9629514088
84PhosphorylationMDVLSPLSFIKVSHV
HHHHCHHHHCCCCCE
28.4524719451
114PhosphorylationLPYIQILSTKSTPTG
CCEEEEECCCCCCCC
35.1024719451
172 (in isoform 2)Ubiquitination-25.2121890473
220UbiquitinationCYGGLWEKDQLSIAK
CCCCCCHHHHHHHHH
38.91-
228UbiquitinationDQLSIAKKHDPLLRE
HHHHHHHHHCHHHHH
44.19-
248UbiquitinationLLFPPTYKFDRNSND
CCCCCCCCCCCCCCC
43.1821890473
248 (in isoform 1)Ubiquitination-43.1821890473
294PhosphorylationIPPASHFSLSLRGYS
CCCCHHEEEEECCCC
16.1817081983
296PhosphorylationPASHFSLSLRGYSSH
CCHHEEEEECCCCCC
18.1517081983
388PhosphorylationWVGDSKVSCSDNLNQ
EECCCCEECCCCCCE
16.1922210691
406PhosphorylationDISNIPTTEDEFLLC
ECCCCCCCCCEEEHH
35.7622210691

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 INP5K_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of INP5K_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 INP5K_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
NCOR2_HUMANNCOR2physical
11509665
TANK_HUMANTANKphysical
21988832
FATE1_HUMANFATE1physical
25416956
MD2BP_HUMANMAD2L1BPphysical
28514442
KTNA1_HUMANKATNA1physical
28514442
UBP47_HUMANUSP47physical
28514442
RFX1_HUMANRFX1physical
28514442
UBB_HUMANUBBphysical
28514442
CA131_HUMANC1orf131physical
28514442
PESC_HUMANPES1physical
28514442
PUR2_HUMANGARTphysical
28514442
ABHDA_HUMANABHD10physical
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 INP5K_HUMAN

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Related Literatures of Post-Translational Modification

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