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Q9DCQ2 (ASPD_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 95. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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:
Putative L-aspartate dehydrogenase

EC=1.4.1.21
Alternative name(s):
Aspartate dehydrogenase domain-containing protein
Gene names
Name:Aspdh
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length287 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Specifically catalyzes the NAD or NADP-dependent dehydrogenation of L-aspartate to iminoaspartate By similarity.

Catalytic activity

L-aspartate + H2O + NAD(P)+ = oxaloacetate + NH3 + NAD(P)H.

Pathway

Cofactor biosynthesis; NAD(+) biosynthesis; iminoaspartate from L-aspartate (dehydrogenase route): step 1/1.

Miscellaneous

The iminoaspartate product is unstable in aqueous solution and can decompose to oxaloacetate and ammonia By similarity.

Sequence similarities

Belongs to the L-aspartate dehydrogenase family.

Ontologies

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 287287Putative L-aspartate dehydrogenase
PRO_0000144901

Sites

Binding site1311NAD; via amide nitrogen By similarity
Binding site1961NAD By similarity

Experimental info

Sequence conflict1171A → V in AAH19451. Ref.2
Sequence conflict2451A → S in AAH19451. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Q9DCQ2 [UniParc].

Last modified June 1, 2001. Version 1.
Checksum: 889D164D943B88DD

FASTA28730,270
        10         20         30         40         50         60 
MATSTLPQVP YKVGVVGYGR LGQSLVSRLL AQGSELGLEL VFVWNRDPGR MAGSVPPALQ 

        70         80         90        100        110        120 
LQDLTALEER HPDLVVEVAH PKIIHESGAQ ILRHANLLVG SPSALADQTT EQQLLEASKR 

       130        140        150        160        170        180 
WGHTVFVARG ALWGSEDISR LDAAGGLQSL RVTMATHPDG FRLEGPLAAA HSSGPRTVLY 

       190        200        210        220        230        240 
EGPVRGLCPL APRNSNTMAA AALAAPSLGF DRVIGVLVAD LSLTDMHVVD VELLGPPGPS 

       250        260        270        280 
GRSFAVHTHR ENPAQPGAVT GSATVTAFWH SLLGCCQLTS RPGIHLC 

« Hide

References

« Hide 'large scale' 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] [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(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: FVB/N.
Tissue: Liver.
[3]Lubec G., Sunyer B., Chen W.-Q.
Submitted (JAN-2009) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 13-20, IDENTIFICATION BY MASS SPECTROMETRY.
Strain: OF1.
Tissue: Hippocampus.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AK002587 mRNA. Translation: BAB22209.1.
BC019451 mRNA. Translation: AAH19451.1.
RefSeqNP_080966.1. NM_026690.1.
UniGeneMm.88478.

3D structure databases

ProteinModelPortalQ9DCQ2.
SMRQ9DCQ2. Positions 10-275.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActQ9DCQ2. 3 interactions.
MINTMINT-1856535.

PTM databases

PhosphoSiteQ9DCQ2.

Proteomic databases

PaxDbQ9DCQ2.
PRIDEQ9DCQ2.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000035929; ENSMUSP00000039202; ENSMUSG00000038704.
GeneID68352.
KEGGmmu:68352.
UCSCuc009gpk.1. mouse.

Organism-specific databases

CTD554235.
MGIMGI:1915602. Aspdh.

Phylogenomic databases

eggNOGCOG1712.
GeneTreeENSGT00390000004452.
HOGENOMHOG000007399.
HOVERGENHBG062283.
InParanoidQ9DCQ2.
OMALELVFVW.
OrthoDBEOG773XH5.
PhylomeDBQ9DCQ2.
TreeFamTF315092.

Enzyme and pathway databases

UniPathwayUPA00253; UER00456.

Gene expression databases

BgeeQ9DCQ2.
CleanExMM_0610012D14RIK.
GenevestigatorQ9DCQ2.

Family and domain databases

Gene3D3.40.50.720. 1 hit.
InterProIPR005106. Asp/hSer_DH_NAD-bd.
IPR002811. Asp_DH.
IPR011182. Asp_DH_NAD_syn.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
PfamPF01958. DUF108. 1 hit.
PF03447. NAD_binding_3. 1 hit.
[Graphical view]
PIRSFPIRSF005227. Asp_dh_NAD_syn. 1 hit.
ProtoNetSearch...

Other

NextBio327053.
PROQ9DCQ2.
SOURCESearch...

Entry information

Entry nameASPD_MOUSE
AccessionPrimary (citable) accession number: Q9DCQ2
Secondary accession number(s): Q8VCQ0
Entry history
Integrated into UniProtKB/Swiss-Prot: August 16, 2005
Last sequence update: June 1, 2001
Last modified: April 16, 2014
This is version 95 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways

MGD cross-references

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