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Q9DCQ2

- ASPD_MOUSE

UniProt

Q9DCQ2 - ASPD_MOUSE

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Protein

Putative L-aspartate dehydrogenase

Gene

Aspdh

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

Functioni

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

Catalytic activityi

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

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei131 – 1311NAD; via amide nitrogenBy similarity
Binding sitei196 – 1961NADBy similarity

GO - Molecular functioni

  1. aspartate dehydrogenase activity Source: UniProtKB-EC
  2. NADP binding Source: InterPro

GO - Biological processi

  1. NAD biosynthetic process Source: UniProtKB-UniPathway
  2. NADP catabolic process Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Pyridine nucleotide biosynthesis

Keywords - Ligandi

NAD, NADP

Enzyme and pathway databases

UniPathwayiUPA00253; UER00456.

Names & Taxonomyi

Protein namesi
Recommended name:
Putative L-aspartate dehydrogenase (EC:1.4.1.21)
Alternative name(s):
Aspartate dehydrogenase domain-containing protein
Gene namesi
Name:Aspdh
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 7

Organism-specific databases

MGIiMGI:1915602. Aspdh.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 287287Putative L-aspartate dehydrogenasePRO_0000144901Add
BLAST

Proteomic databases

MaxQBiQ9DCQ2.
PaxDbiQ9DCQ2.
PRIDEiQ9DCQ2.

PTM databases

PhosphoSiteiQ9DCQ2.

Expressioni

Gene expression databases

BgeeiQ9DCQ2.
CleanExiMM_0610012D14RIK.
ExpressionAtlasiQ9DCQ2. baseline and differential.
GenevestigatoriQ9DCQ2.

Interactioni

Protein-protein interaction databases

IntActiQ9DCQ2. 3 interactions.
MINTiMINT-1856535.

Structurei

3D structure databases

ProteinModelPortaliQ9DCQ2.
SMRiQ9DCQ2. Positions 13-231.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the L-aspartate dehydrogenase family.Curated

Phylogenomic databases

eggNOGiCOG1712.
GeneTreeiENSGT00390000004452.
HOGENOMiHOG000007399.
HOVERGENiHBG062283.
InParanoidiQ9DCQ2.
OMAiLAFVWNR.
OrthoDBiEOG773XH5.
PhylomeDBiQ9DCQ2.
TreeFamiTF315092.

Family and domain databases

Gene3Di3.40.50.720. 1 hit.
InterProiIPR005106. Asp/hSer_DH_NAD-bd.
IPR002811. Asp_DH.
IPR011182. L-Asp_DH.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
PfamiPF01958. DUF108. 1 hit.
PF03447. NAD_binding_3. 1 hit.
[Graphical view]
PIRSFiPIRSF005227. Asp_dh_NAD_syn. 1 hit.

Sequencei

Sequence statusi: Complete.

Q9DCQ2-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MATSTLPQVP YKVGVVGYGR LGQSLVSRLL AQGSELGLEL VFVWNRDPGR
60 70 80 90 100
MAGSVPPALQ LQDLTALEER HPDLVVEVAH PKIIHESGAQ ILRHANLLVG
110 120 130 140 150
SPSALADQTT EQQLLEASKR WGHTVFVARG ALWGSEDISR LDAAGGLQSL
160 170 180 190 200
RVTMATHPDG FRLEGPLAAA HSSGPRTVLY EGPVRGLCPL APRNSNTMAA
210 220 230 240 250
AALAAPSLGF DRVIGVLVAD LSLTDMHVVD VELLGPPGPS GRSFAVHTHR
260 270 280
ENPAQPGAVT GSATVTAFWH SLLGCCQLTS RPGIHLC
Length:287
Mass (Da):30,270
Last modified:June 1, 2001 - v1
Checksum:i889D164D943B88DD
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti117 – 1171A → V in AAH19451. (PubMed:15489334)Curated
Sequence conflicti245 – 2451A → S in AAH19451. (PubMed:15489334)Curated

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AK002587 mRNA. Translation: BAB22209.1.
BC019451 mRNA. Translation: AAH19451.1.
CCDSiCCDS21207.1.
RefSeqiNP_080966.1. NM_026690.1.
UniGeneiMm.88478.

Genome annotation databases

EnsembliENSMUST00000035929; ENSMUSP00000039202; ENSMUSG00000038704.
GeneIDi68352.
KEGGimmu:68352.
UCSCiuc009gpk.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AK002587 mRNA. Translation: BAB22209.1 .
BC019451 mRNA. Translation: AAH19451.1 .
CCDSi CCDS21207.1.
RefSeqi NP_080966.1. NM_026690.1.
UniGenei Mm.88478.

3D structure databases

ProteinModelPortali Q9DCQ2.
SMRi Q9DCQ2. Positions 13-231.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

IntActi Q9DCQ2. 3 interactions.
MINTi MINT-1856535.

PTM databases

PhosphoSitei Q9DCQ2.

Proteomic databases

MaxQBi Q9DCQ2.
PaxDbi Q9DCQ2.
PRIDEi Q9DCQ2.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000035929 ; ENSMUSP00000039202 ; ENSMUSG00000038704 .
GeneIDi 68352.
KEGGi mmu:68352.
UCSCi uc009gpk.1. mouse.

Organism-specific databases

CTDi 554235.
MGIi MGI:1915602. Aspdh.

Phylogenomic databases

eggNOGi COG1712.
GeneTreei ENSGT00390000004452.
HOGENOMi HOG000007399.
HOVERGENi HBG062283.
InParanoidi Q9DCQ2.
OMAi LAFVWNR.
OrthoDBi EOG773XH5.
PhylomeDBi Q9DCQ2.
TreeFami TF315092.

Enzyme and pathway databases

UniPathwayi UPA00253 ; UER00456 .

Miscellaneous databases

NextBioi 327053.
PROi Q9DCQ2.
SOURCEi Search...

Gene expression databases

Bgeei Q9DCQ2.
CleanExi MM_0610012D14RIK.
ExpressionAtlasi Q9DCQ2. baseline and differential.
Genevestigatori Q9DCQ2.

Family and domain databases

Gene3Di 3.40.50.720. 1 hit.
InterProi IPR005106. Asp/hSer_DH_NAD-bd.
IPR002811. Asp_DH.
IPR011182. L-Asp_DH.
IPR016040. NAD(P)-bd_dom.
[Graphical view ]
Pfami PF01958. DUF108. 1 hit.
PF03447. NAD_binding_3. 1 hit.
[Graphical view ]
PIRSFi PIRSF005227. Asp_dh_NAD_syn. 1 hit.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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(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.

Entry informationi

Entry nameiASPD_MOUSE
AccessioniPrimary (citable) accession number: Q9DCQ2
Secondary accession number(s): Q8VCQ0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 16, 2005
Last sequence update: June 1, 2001
Last modified: October 29, 2014
This is version 101 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Miscellaneous

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

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

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

External Data

Dasty 3