Skip Header

Contribute Send feedback
Read comments (?) or add your own

Q8NFU5 (IPMK_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 72. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Inositol polyphosphate multikinase

EC=2.7.1.151
Alternative name(s):
Inositol 1,3,4,6-tetrakisphosphate 5-kinase
Gene names
Name:IPMK
Synonyms:IMPK
OrganismHomo sapiens (Human)
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length416 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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). Ref.1 Ref.2

Catalytic activity

ATP + 1D-myo-inositol 1,4,5-trisphosphate = ADP + 1D-myo-inositol 1,4,5,6-tetrakisphosphate.

ATP + 1D-myo-inositol 1,4,5,6-tetrakisphosphate = ADP + 1D-myo-inositol 1,3,4,5,6-pentakisphosphate.

Subcellular location

Nucleus Ref.1.

Tissue specificity

Ubiquitous, with the highest expression in skeletal muscle, liver, placenta, lung, peripheral blood leukocytes, kidney, spleen and colon. Ref.2

Sequence similarities

Belongs to the inositol phosphokinase (IPK) family.

Ontologies

Keywords
   Cellular componentNucleus
   Coding sequence diversityPolymorphism
   LigandATP-binding
Nucleotide-binding
   Molecular functionKinase
Transferase
   PTMPhosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Cellular componentnucleus

Inferred from direct assay. Source: HPA

   Molecular functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

inositol-1,4,5-trisphosphate 6-kinase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 416416Inositol polyphosphate multikinase
PRO_0000066870

Regions

Region140 – 1489Substrate binding By similarity
Motif320 – 33011Nuclear localization signal

Amino acid modifications

Modified residue71Phosphoserine Ref.4 Ref.5
Modified residue211Phosphothreonine Ref.5
Modified residue221Phosphoserine Ref.5
Modified residue3481Phosphoserine Ref.5
Modified residue3501Phosphoserine Ref.5

Natural variations

Natural variant3491M → I.
Corresponds to variant rs2275443 [ dbSNP | Ensembl ].
VAR_022112

Experimental info

Mutagenesis322 – 3232RK → QQ: Interferes with nuclear localization. Ref.1
Mutagenesis327 – 3282KK → QQ: Interferes with nuclear localization. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q8NFU5 [UniParc].

Last modified October 1, 2002. Version 1.
Checksum: 622D678696A892F9

FASTA41647,222
        10         20         30         40         50         60 
MATEPPSPLR VEAPGPPEMR TSPAIESTPE GTPQPAGGRL RFLNGCVPLS HQVAGHMYGK 

        70         80         90        100        110        120 
DKVGILQHPD GTVLKQLQPP PRGPRELEFY NMVYAADCFD GVLLELRKYL PKYYGIWSPP 

       130        140        150        160        170        180 
TAPNDLYLKL EDVTHKFNKP CIMDVKIGQK SYDPFASSEK IQQQVSKYPL MEEIGFLVLG 

       190        200        210        220        230        240 
MRVYHVHSDS YETENQHYGR SLTKETIKDG VSRFFHNGYC LRKDAVAASI QKIEKILQWF 

       250        260        270        280        290        300 
ENQKQLNFYA SSLLFVYEGS SQPTTTKLND RTLAEKFLSK GQLSDTEVLE YNNNFHVLSS 

       310        320        330        340        350        360 
TANGKIESSV GKSLSKMYAR HRKIYTKKHH SQTSLKVENL EQDNGWKSMS QEHLNGNVLS 

       370        380        390        400        410 
QLEKVFYHLP TGCQEIAEVE VRMIDFAHVF PSNTIDEGYV YGLKHLISVL RSILDN 

« Hide

References

« Hide 'large scale' references
[1]"The human homologue of yeast ArgRIII protein is an inositol phosphate multikinase with predominantly nuclear localization."
Nalaskowski M.M., Deschermeier C., Fanick W., Mayr G.W.
Biochem. J. 366:549-556(2002) [PubMed: 12027805] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, MUTAGENESIS OF 322-ARG-LYS-323 AND 327-LYS-LYS-328, SUBCELLULAR LOCATION.
[2]"The human homolog of the rat inositol phosphate multikinase is an inositol 1,3,4,6-tetrakisphosphate 5-kinase."
Chang S.-C., Miller A.L., Feng Y., Wente S.R., Majerus P.W.
J. Biol. Chem. 277:43836-43843(2002) [PubMed: 12223481] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY.
[3]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Brain.
[4]"Kinase-selective enrichment enables quantitative phosphoproteomics of the 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) [PubMed: 18691976] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-7, MASS SPECTROMETRY.
Tissue: Cervix carcinoma.
[5]"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) [PubMed: 19369195] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-7; THR-21; SER-22; SER-348 AND SER-350, MASS SPECTROMETRY.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF432853 mRNA. Translation: AAM97838.1.
BK000580 mRNA. Translation: DAA01362.1.
BC065709 mRNA. Translation: AAH65709.1.
IPIIPI00168907.
RefSeqNP_689416.1. NM_152230.4.
UniGeneHs.30280.

3D structure databases

ProteinModelPortalQ8NFU5.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ8NFU5.

PTM databases

PhosphoSiteQ8NFU5.

Polymorphism databases

DMDM50401072.

Proteomic databases

PRIDEQ8NFU5.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000373935; ENSP00000363046; ENSG00000151151.
GeneID253430.
KEGGhsa:253430.
UCSCuc001jkb.1. human.

Organism-specific databases

CTD253430.
GeneCardsGC10M059951.
H-InvDBHIX0008839.
HGNCHGNC:20739. IPMK.
HPAHPA037837.
MIM609851. gene.
neXtProtNX_Q8NFU5.
PharmGKBPA134903369.
GenAtlasSearch...

Phylogenomic databases

eggNOGprNOG08133.
GeneTreeENSGT00390000014381.
HOGENOMHBG564560.
HOVERGENHBG052124.
InParanoidQ8NFU5.
OMAEHLNGNV.
OrthoDBEOG4NVZKR.
PhylomeDBQ8NFU5.

Enzyme and pathway databases

BioCycMetaCyc:ENSG00000151151-MONOMER.
BRENDA2.7.1.151. 2681.

Gene expression databases

ArrayExpressQ8NFU5.
BgeeQ8NFU5.
CleanExHS_IPMK.
GenevestigatorQ8NFU5.
GermOnlineENSG00000151151. Homo sapiens.

Family and domain databases

InterProIPR005522. IPK.
[Graphical view]
KOK00328.
PANTHERPTHR12400. IPK. 1 hit.
PfamPF03770. IPK. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio92097.
SOURCESearch...

Entry information

Entry nameIPMK_HUMAN
AccessionPrimary (citable) accession number: Q8NFU5
Entry history
Integrated into UniProtKB/Swiss-Prot: July 19, 2004
Last sequence update: October 1, 2002
Last modified: January 25, 2012
This is version 72 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

Human chromosome 10

Human chromosome 10: entries, gene names and cross-references to MIM

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

SIMILARITY comments

Index of protein domains and families