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UniProtKB/Swiss-Prot entry Q8K183


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name PDXK_MOUSE
Primary accession number Q8K183
Secondary accession numbers Q3TM83 Q8BJQ5
Integrated into Swiss-Prot on July 5, 2004
Sequence was last modified on October 1, 2002 (Sequence version 1)
Annotations were last modified on    December 16, 2008 (Entry version 49)
Name and origin of the protein
Protein name Pyridoxal kinase
Synonyms EC 2.7.1.35
Pyridoxine kinase
Gene name
Name: Pdxk
Synonyms: Pkh
From
Mus musculus (Mouse) [TaxID: 10090] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; Muroidea; Muridae; Murinae; Mus.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J;
TISSUE=Brain, Hypothalamus, Lung, and Mammary gland;
DOI=10.1126/science.1112014; PubMed=16141072 [NCBI, ExPASy, EBI, Israel, Japan]
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.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Kidney;
DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan]
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[3]
PROTEIN SEQUENCE OF 140-160, AND MASS SPECTROMETRY.
TISSUE=Hippocampus;
Lubec G., Klug S.;
Submitted (MAR-2007) to UniProtKB.
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
AK039194; BAC30274.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AK080846; BAC38041.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AK145470; BAE26454.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AK166078; BAE38559.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AK166464; BAE38792.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC027745; AAH27745.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq NP_742146.1; -.
UniGene Mm.206159
3D structure databases
HSSP P82197; 1LHP. [HSSP ENTRY / PDB]
SMR Q8K183; 4-312.
ModBase Q8K183.
Organism-specific databases
MGI MGI:1351869; Pdxk.
Gene expression databases
ArrayExpress Q8K183; -.
CleanEx MM_PDXK; -.
GermOnline ENSMUSG00000032788; Mus musculus.
Ontologies
GO
GO:0005737; Cellular component: cytoplasm (inferred from electronic annotation from UniProtKB-KW).
GO:0005524; Molecular function: ATP binding (inferred from electronic annotation from UniProtKB-KW).
GO:0008478; Molecular function: pyridoxal kinase activity (inferred from electronic annotation from InterPro).
GO:0008270; Molecular function: zinc ion binding (inferred from electronic annotation from UniProtKB-KW).
GO:0008615; Biological process: pyridoxine biosynthetic process (inferred from electronic annotation from InterPro).
QuickGo view.
Family and domain databases
InterPro IPR011611; Carb/pur_kinase.
IPR004625; PyrdxlP_synth_PyrdxlKinase.
Graphical view of domain structure.
Pfam PF00294; PfkB; 1.
Pfam graphical view of domain structure.
TIGRFAMs TIGR00687; pyridox_kin; 1.
Proteomics databases
PRIDE Q8K183; -.
Genome annotation databases
Ensembl ENSMUSG00000032788; Mus musculus. [Contig view]
GeneID 216134; -.
KEGG mmu:216134; -.
NMPDR fig|10090.3.peg.13944; -.
Phylogenomic databases
HOGENOM Q8K183; -.
HOVERGEN Q8K183; -.
Other
NextBio 374990; -.
SOURCE Pdxk; Mus musculus.
ProtoNet Q8K183.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Acetylation; ATP-binding; Cytoplasm; Direct protein sequencing; Kinase; Metal-binding; Nucleotide-binding; Phosphoprotein; Transferase; Zinc.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
CHAIN   1   312  312     Pyridoxal kinase. PRO_0000213336
NP_BIND   186   187  2     ATP (By similarity). 
NP_BIND   223   234  12     ATP (By similarity). 
BINDING   12    12        Substrate (By similarity). 
BINDING   47    47        Substrate (By similarity). 
BINDING   127   127        Substrate (By similarity). 
BINDING   235   235        Substrate (By similarity). 
MOD_RES   1     1        N-acetylmethionine (By similarity). 
MOD_RES   213   213        Phosphoserine (By similarity). 
MOD_RES   285   285        Phosphoserine (By similarity). 
CONFLICT   188   188        S -> F (in Ref. 1; BAC38041). 
Sequence information
Length: 312 AA [This is the length of the unprocessed precursor] Molecular weight: 35015 Da [This is the MW of the unprocessed precursor] CRC64: C4F32E8A27E751AF [This is a checksum on the sequence]
        10         20         30         40         50         60 
MEGECRVLSI QSHVVRGYVG NRAAMFPLQV LGFEVDAVNS VQFSNHTGYA HWKGQVLKSQ 

        70         80         90        100        110        120 
ELHELYEGLK VNDVNKYDYV LTGYTRDKSF LAMVVDIVRE LKQQNSRLVY VCDPVMGDKW 

       130        140        150        160        170        180 
NGEGSMYVPQ DLLPVYRDKV VPVADIITPN QFEAELLSGR KIHSQEEAFE VMDMLHCMGP 

       190        200        210        220        230        240 
DTVVITSSDL PSSQGSDYLI ALGSQRMRKP DGSTVTQRIR MEMRKVEAVF VGTGDLFAAM 

       250        260        270        280        290        300 
LLAWTHKHPD NLKVACEKTV SAMQHVLQRT IRCAKAEAGE GQKPSPAQLE LRMVQSKRDI 

       310 
EDPEIVVQAT VL 

Q8K183 in FASTA format

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