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Protein

Xylulose kinase

Gene

Xylb

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at transcript leveli

Functioni

Phosphorylates D-xylulose to produce D-xylulose 5-phosphate, a molecule that may play an important role in the regulation of glucose metabolism and lipogenesis.By similarity

Catalytic activityi

ATP + D-xylulose = ADP + D-xylulose 5-phosphate.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei114 – 1141SubstrateBy similarity
Binding sitei185 – 1851SubstrateBy similarity
Binding sitei295 – 2951SubstrateBy similarity
Binding sitei296 – 2961SubstrateBy similarity
Binding sitei370 – 3701ATPBy similarity
Binding sitei460 – 4601ATPBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi456 – 4572ATPBy similarity

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. xylulokinase activity Source: UniProtKB

GO - Biological processi

  1. carbohydrate phosphorylation Source: MGI
  2. D-xylose metabolic process Source: UniProtKB-KW
  3. xylulose metabolic process Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Transferase

Keywords - Biological processi

Carbohydrate metabolism, Xylose metabolism

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Xylulose kinase (EC:2.7.1.17)
Short name:
Xylulokinase
Gene namesi
Name:Xylb
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Chromosome 9

Organism-specific databases

MGIiMGI:2142985. Xylb.

Subcellular locationi

GO - Cellular componenti

  1. extracellular vesicular exosome Source: MGI
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 551551Xylulose kinasePRO_0000230986Add
BLAST

Proteomic databases

MaxQBiQ3TNA1.
PaxDbiQ3TNA1.
PRIDEiQ3TNA1.

PTM databases

PhosphoSiteiQ3TNA1.

Expressioni

Gene expression databases

BgeeiQ3TNA1.
CleanExiMM_XYLB.
ExpressionAtlasiQ3TNA1. baseline and differential.
GenevestigatoriQ3TNA1.

Interactioni

Subunit structurei

Monomer.By similarity

Protein-protein interaction databases

IntActiQ3TNA1. 1 interaction.
MINTiMINT-4118544.

Structurei

3D structure databases

ProteinModelPortaliQ3TNA1.
SMRiQ3TNA1. Positions 22-544.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the FGGY kinase family.Curated

Phylogenomic databases

eggNOGiCOG1070.
GeneTreeiENSGT00390000010821.
HOGENOMiHOG000174850.
HOVERGENiHBG053124.
InParanoidiQ3TNA1.
KOiK00854.
OMAiGSYSPID.
OrthoDBiEOG751NFS.
PhylomeDBiQ3TNA1.
TreeFamiTF313643.

Family and domain databases

InterProiIPR018485. Carb_kinase_FGGY_C.
IPR018484. Carb_kinase_FGGY_N.
[Graphical view]
PfamiPF02782. FGGY_C. 1 hit.
PF00370. FGGY_N. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q3TNA1-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MDARTHRRAA GTPRALAERA GRRCCLGWDF STQQVKVVAV DAELNVFYED
60 70 80 90 100
SVHFDRDLPE FGTQGGVHVH KDRLTVTSPV LMWVQALDLI LGKMKSSGFD
110 120 130 140 150
FSQVLALSGA GQQHGSVYWK TGASLALSSL SPALPLHQQL QSCFSISDCP
160 170 180 190 200
IWMDSSTTAQ CHQLEAAVGG AQALSCLTGS RAYERFTGNQ IAKLFQKNPE
210 220 230 240 250
AYSHSERISL VSSFAASLFL GGYSPIDYSD GSGMNLLQIQ EKVWSQACLD
260 270 280 290 300
VCAPHLEEKL GSPVPSCSVV GTISSYYVQR YGFPPGCKVV AFSGDNPASL
310 320 330 340 350
AGMRLEEGDI AVSLGTSDTL FLWLQKPMPA LEGHIFCNPV DPQHYMALLC
360 370 380 390 400
FKNGSLMREK IRDESASCSW NKFSKALKST AMGNNGNLGF YFDVMEITPE
410 420 430 440 450
IIGRHRFNAE NMEVSAFPGD VEIRALIEGQ FMAKRIHAEG LGYRVMPKTK
460 470 480 490 500
ILATGGASHN KDILQVLADV FGAPVYVIDT TSSACVGSAY RAFHGLAGGT
510 520 530 540 550
GVAFSEVVKS APQPSLAATP NPGASQVYAA LLPRYSALEQ RILSTAQRPL

E
Length:551
Mass (Da):59,544
Last modified:October 11, 2005 - v1
Checksum:iCED895069FBFD97B
GO

Sequence cautioni

The sequence AAH25442.1 differs from that shown. Reason: Erroneous initiation. Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK143476 mRNA. Translation: BAE25393.1.
AK165440 mRNA. Translation: BAE38188.1.
AK165518 mRNA. Translation: BAE38233.1.
BC025442 mRNA. Translation: AAH25442.1. Different initiation.
BC138244 mRNA. Translation: AAI38245.1.
BC138247 mRNA. Translation: AAI38248.1.
CCDSiCCDS23614.1.
RefSeqiNP_001028381.1. NM_001033209.3.
NP_001186497.1. NM_001199568.1.
UniGeneiMm.219497.

Genome annotation databases

EnsembliENSMUST00000039610; ENSMUSP00000047254; ENSMUSG00000035769.
GeneIDi102448.
KEGGimmu:102448.
UCSCiuc009sat.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK143476 mRNA. Translation: BAE25393.1.
AK165440 mRNA. Translation: BAE38188.1.
AK165518 mRNA. Translation: BAE38233.1.
BC025442 mRNA. Translation: AAH25442.1. Different initiation.
BC138244 mRNA. Translation: AAI38245.1.
BC138247 mRNA. Translation: AAI38248.1.
CCDSiCCDS23614.1.
RefSeqiNP_001028381.1. NM_001033209.3.
NP_001186497.1. NM_001199568.1.
UniGeneiMm.219497.

3D structure databases

ProteinModelPortaliQ3TNA1.
SMRiQ3TNA1. Positions 22-544.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ3TNA1. 1 interaction.
MINTiMINT-4118544.

PTM databases

PhosphoSiteiQ3TNA1.

Proteomic databases

MaxQBiQ3TNA1.
PaxDbiQ3TNA1.
PRIDEiQ3TNA1.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000039610; ENSMUSP00000047254; ENSMUSG00000035769.
GeneIDi102448.
KEGGimmu:102448.
UCSCiuc009sat.2. mouse.

Organism-specific databases

CTDi9942.
MGIiMGI:2142985. Xylb.

Phylogenomic databases

eggNOGiCOG1070.
GeneTreeiENSGT00390000010821.
HOGENOMiHOG000174850.
HOVERGENiHBG053124.
InParanoidiQ3TNA1.
KOiK00854.
OMAiGSYSPID.
OrthoDBiEOG751NFS.
PhylomeDBiQ3TNA1.
TreeFamiTF313643.

Miscellaneous databases

NextBioi355490.
PROiQ3TNA1.
SOURCEiSearch...

Gene expression databases

BgeeiQ3TNA1.
CleanExiMM_XYLB.
ExpressionAtlasiQ3TNA1. baseline and differential.
GenevestigatoriQ3TNA1.

Family and domain databases

InterProiIPR018485. Carb_kinase_FGGY_C.
IPR018484. Carb_kinase_FGGY_N.
[Graphical view]
PfamiPF02782. FGGY_C. 1 hit.
PF00370. FGGY_N. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  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.
    , 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(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Kidney.
  2. "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(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: FVB/N.
    Tissue: Brain and Kidney.

Entry informationi

Entry nameiXYLB_MOUSE
AccessioniPrimary (citable) accession number: Q3TNA1
Secondary accession number(s): B2RR66, Q8R156
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 4, 2006
Last sequence update: October 11, 2005
Last modified: February 4, 2015
This is version 72 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.