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Reviewed, UniProtKB/Swiss-Prot Q3TRM8 (HXK3_MOUSE)

Last modified January 19, 2010. Version 39. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Hexokinase-3
    EC=2.7.1.1
Alternative name(s):
    Hexokinase type III
      Short name=HK III
Gene names
Name: Hk3
OrganismMus musculus (Mouse)
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMus

Protein attributes

Sequence length922 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level.

General annotation (Comments)

Catalytic activity

ATP + D-hexose = ADP + D-hexose 6-phosphate.

Enzyme regulation

Hexokinase is an allosteric enzyme inhibited by its product Glc-6-P By similarity.

Pathway

Carbohydrate metabolism; hexose metabolism.

Subunit structure

Monomer By similarity.

Domain

The N- and C-terminal halves of this hexokinase show extensive sequence similarity to each other. The catalytic activity is associated with the C-terminus while regulatory function is associated with the N-terminus.

Miscellaneous

In vertebrates there are four major glucose-phosphorylating isoenzymes, designated hexokinase I, II, III and IV (glucokinase).

Sequence similarities

Belongs to the hexokinase family.

Ontologies

Keywords
   Biological processGlycolysis
   DomainRepeat
   LigandATP-binding
Nucleotide-binding
   Molecular functionKinase
Transferase
   PTMPhosphoprotein
   Technical termAllosteric enzyme
Gene Ontology (GO)
   Biological processglycolysis

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentmitochondrion

Inferred from direct assay. Source: MGI

   Molecular functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

hexokinase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 922922Hexokinase-3
PRO_0000197591

Regions

Nucleotide binding93 – 986ATP Potential
Nucleotide binding540 – 5456ATP Potential
Region1 – 486486Regulatory
Region160 – 18627Glucose-binding Potential
Region487 – 922436Catalytic
Region602 – 62827Glucose-binding Potential

Amino acid modifications

Modified residue7321Phosphothreonine Ref.2

Experimental info

Sequence conflict2031A → S in BAE37000. Ref.1
Sequence conflict3841Y → C in BAE29220. Ref.1
Sequence conflict4391K → E in BAE29220. Ref.1
Sequence conflict4421V → I in BAE29007. Ref.1
Sequence conflict5091G → E in BAE29007. Ref.1
Sequence conflict8601T → A in BAE29007. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q3TRM8-1 [UniParc].

Last modified December 6, 2005. Version 2.
Checksum: 38F4E024630C45E5

FASTA922100,101
        10         20         30         40         50         60 
MATIGPSGLH PGERASVCPH EGVPRPSGSL ELECLQQFKV TRTQLQQIQA SLLCSMEQAL 

        70         80         90        100        110        120 
KGQDSPAPSV RMLPTYVRST PHGTEQGDFL VLELGATGAS LRVLWVTLTG TKECRVEPRS 

       130        140        150        160        170        180 
REFVIPQEVI LGAGQQLFDF AARCLSEFLD AYPVENQGLK LGFNFSFPCH QTGLDRSTLI 

       190        200        210        220        230        240 
SWTKGFRCSG VEGQDVVQLL RDAIQRQGTY RIDVVAMVND TVGTMMGCEL GTRPCEVGLI 

       250        260        270        280        290        300 
VDTGTNACYM EEARHVAALD EDRGRTCVSI EWGSFYDEDA LGPVLTTFDS ALDRESLTPG 

       310        320        330        340        350        360 
AQRFEKMIGG LYLGELVRLV LVHLTQHGVL FDGCASPALL SQGCILLDHV AEMEDTATGT 

       370        380        390        400        410        420 
ARVHTILQDL GLSPRASDAE LVQYVCVAVC TRAAQLCAAA LAAVLSRLQH SREQQTLQVA 

       430        440        450        460        470        480 
VATGGRVFER HPRFLRILKE TVTLLAPNCD VSFIPSVDGG GRGVAMVTAV AARLAAHRRI 

       490        500        510        520        530        540 
LEETLAPFQL TLEQMTVVQA QMREAMIRGL QGEASSLRML PTYVRATPDG SERGDFLALD 

       550        560        570        580        590        600 
LGGTNFRVLL VRVAEGSVQI INQVYSIPEC RAQGSGQKLF DHIVDCIVDF QKRQGLSGQS 

       610        620        630        640        650        660 
LPLGFTFSFP CKQLGLDQGI LLNWTKGFNA SGCEGQDVVY LLREAIRRRQ AVELNVVAIV 

       670        680        690        700        710        720 
NDTVGTMMSC GYDDPRCEMG LIVGTGTNAC YMEELRNVAS VPGDSGLMCI NMEWGAFGDD 

       730        740        750        760        770        780 
GSLGTLSTRF DTSVDQASIN PGKQRFEKMI SGMYLGEIVR HILLHLTNLG VLFRGQKTQC 

       790        800        810        820        830        840 
LQARDIFKTK FLSEIESDSL ALRQVRAILE DLGLTLTSDD ALMVLEVCQA VSRRAAQLCG 

       850        860        870        880        890        900 
AGVAAVVEKI RENRGLQELT VSVGVDGTLY KLHPHFSKLV SATVRKLAPQ CTVTFLQSED 

       910        920 
GSGKGAALVT AVACRLTQMA HV 

« Hide

References

[1]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed: 16141072] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6J and NOD.
Tissue: Bone and Bone marrow.
[2]"Protein phosphorylation and expression profiling by Yin-yang multidimensional liquid chromatography (Yin-yang MDLC) mass spectrometry."
Dai J., Jin W.-H., Sheng Q.-H., Shieh C.-H., Wu J.-R., Zeng R.
J. Proteome Res. 6:250-262(2007) [PubMed: 17203969] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-732, MASS SPECTROMETRY.
Tissue: Liver.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AK149651 mRNA. Translation: BAE29007.1.
AK149992 mRNA. Translation: BAE29220.1.
AK154603 mRNA. Translation: BAE32706.1.
AK162637 mRNA. Translation: BAE37000.1.
AK171580 mRNA. Translation: BAE42538.1.
IPIIPI00751595.
RefSeqNP_001028417.1.
UniGeneMm.267479

3D structure databases

SMRQ3TRM8. Positions 33-916.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ3TRM8.

PTM databases

PhosphoSiteQ3TRM8.

Proteomic databases

PRIDEQ3TRM8.

Genome annotation databases

EnsemblENSMUST00000052949; ENSMUSP00000051215; ENSMUSG00000025877; Mus musculus. [Genome view]
GeneID212032.
KEGGmmu:212032.
UCSCuc007qpr.1. mouse.

Organism-specific databases

CTD212032.
MGIMGI:2670962. Hk3.

Phylogenomic databases

HOGENOMHBG446386.
HOVERGENQ3TRM8.
InParanoidQ3TRM8.
OMATLISWTK.
OrthoDBEOG989760.
PhylomeDBQ3TRM8.

Enzyme and pathway databases

BRENDA2.7.1.1. 244.

Gene expression databases

ArrayExpressQ3TRM8.
BgeeQ3TRM8.
CleanExMM_HK3.
GenevestigatorQ3TRM8.
GermOnlineENSMUSG00000025877. Mus musculus.

Family and domain databases

InterProIPR001312. Hexokinase.
IPR019807. Hexokinase_CS.
[Graphical view]
PANTHERPTHR19443. Hexokinase. 1 hit.
PfamPF00349. Hexokinase_1. 2 hits.
PF03727. Hexokinase_2. 2 hits.
[Graphical view]
PRINTSPR00475. HEXOKINASE.
PROSITEPS00378. HEXOKINASES. 2 hits.
[Graphical view]
ProtoNetSearch...

Other Resources

NextBio373427.
SOURCESearch...

Entry information

Entry nameHXK3_MOUSE
AccessionPrimary (citable) accession number: Q3TRM8
Secondary accession number(s): Q3TAX6, Q3UDP1, Q3UEA4
Entry history
Integrated into UniProtKB/Swiss-Prot: December 6, 2005
Last sequence update: December 6, 2005
Last modified: January 19, 2010
This is version 39 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

Relevant documents

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents