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Protein

Putative L-aspartate dehydrogenase

Gene

Aspdh

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: 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

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei24 – 241PhosphoserineBy similarity
Modified residuei172 – 1721PhosphoserineBy similarity

Keywords - PTMi

Phosphoprotein

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.
OMAiLELVFVW.
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:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
Links Updated
AK002587 mRNA. Translation: BAB22209.1.
BC019451 mRNA. Translation: AAH19451.1.
CCDSiCCDS21207.1.
RefSeqiNP_080966.1. NM_026690.1.
UniGeneiMm.88478.

3D structure databases

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

Protein-protein interaction databases

IntActiQ9DCQ2. 3 interactions.
MINTiMINT-1856535.

PTM databases

PhosphoSiteiQ9DCQ2.

Proteomic databases

MaxQBiQ9DCQ2.
PaxDbiQ9DCQ2.
PRIDEiQ9DCQ2.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi554235.
MGIiMGI:1915602. Aspdh.

Phylogenomic databases

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

Enzyme and pathway databases

UniPathwayiUPA00253; UER00456.

Miscellaneous databases

NextBioi327053.
PROiQ9DCQ2.
SOURCEiSearch...

Gene expression databases

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

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.
ProtoNetiSearch...

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: March 4, 2015
This is version 103 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

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.