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Reviewed, UniProtKB/Swiss-Prot Q61753 (SERA_MOUSE)

Last modified June 16, 2009. Version 81. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    D-3-phosphoglycerate dehydrogenase
      Short name=3-PGDH
    EC=1.1.1.95
Alternative name(s):
    A10
Gene names
Name: Phgdh
OrganismMus musculus (Mouse)
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMus

Protein attributes

Sequence length533 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level.

General annotation (Comments)

Catalytic activity

3-phospho-D-glycerate + NAD+ = 3-phosphonooxypyruvate + NADH.

2-hydroxyglutarate + NAD+ = 2-oxoglutarate + NADH.

Pathway

Amino-acid biosynthesis; L-serine biosynthesis; L-serine from 3-phospho-D-glyceric acid: step 1/3.

Subunit structure

Homotetramer By similarity.

Sequence similarities

Belongs to the D-isomer specific 2-hydroxyacid dehydrogenase family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 533532D-3-phosphoglycerate dehydrogenase
PRO_0000076014

Sites

Active site2361 By similarity
Active site2651 By similarity
Active site2831Proton donor By similarity

Amino acid modifications

Modified residue21N-acetylalanine By similarity
Modified residue3711Phosphoserine By similarity

Experimental info

Sequence conflict771G → V in AAB67986. Ref.5
Sequence conflict87 – 882AA → PP in AAB67986. Ref.5
Sequence conflict1241A → T in AAB67986. Ref.5
Sequence conflict3691C → W in AAB67986. Ref.5
Sequence conflict3771G → A in AAB67986. Ref.5
Sequence conflict4471M → K in BAC36494. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Q61753-1 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: 49CBF125AD6A12A5

FASTA53356,586
        10         20         30         40         50         60 
MAFANLRKVL ISDSLDPCCR KILQDGGLQV VEKQNLSKEE LIAELQDCEG LIVRSATKVT 

        70         80         90        100        110        120 
ADVINAAEKL QVVGRAGTGV DNVDLEAATR KGILVMNTPN GNSLSAAELT CGMIMCLARQ 

       130        140        150        160        170        180 
IPQATASMKD GKWDRKKFMG TELNGKTLGI LGLGRIGREV ATRMQSFGMK TVGYDPIISP 

       190        200        210        220        230        240 
EVAASFGVQQ LPLEEIWPLC DFITVHTPLL PSTTGLLNDS TFAQCKKGVR VVNCARGGIV 

       250        260        270        280        290        300 
DEGALLRALQ SGQCAGAALD VFTEEPPRDR ALVDHENVIS CPHLGASTKE AQSRCGEEIA 

       310        320        330        340        350        360 
VQFVDMVKGK SLTGVVNAQA LTSAFSPHTK PWIGLAEAMG TLMHAWAGSP KGTIQVVTQG 

       370        380        390        400        410        420 
TSLKNAGTCL SPAVIVGLLR EASKQADVNL VNAKLLVKEA GLNVTTSHNP GVPGEQGSGE 

       430        440        450        460        470        480 
CLLTVALAGA PYQAVGLVQG TTPMLQMLNG AVFRPEVPLR RGQPLLVFRA QPSDPGMLPT 

       490        500        510        520        530 
MIGLLAEAGV QLLSYQTSMV SDGEPWHVMG LSSLLPSLET WKQHVLEAFQ FCF 

« Hide

References

« Hide 'large scale' references
[1]"Targeted disruption of the mouse 3-phosphoglycerate dehydrogenase gene causes severe neurodevelopmental defects and results in embryonic lethality."
Yoshida K., Furuya S., Osuka S., Mitoma J., Shinoda Y., Watanabe M., Azuma N., Tanaka H., Hashikawa T., Itohara S., Hirabayashi Y.
J. Biol. Chem. 279:3573-3577(2004) [PubMed: 14645240] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: 129/SvJ.
[2]"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: 16141072] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6J and NOD.
Tissue: Testis and Thymus.
[3]"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: 15489334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6.
Tissue: Brain and Olfactory epithelium.
[4]Lubec G., Klug S., Yang J.W., Zigmond M.
Submitted (JUL-2007) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 39-54; 248-268; 365-380 AND 523-533, MASS SPECTROMETRY.
Tissue: Brain and Hippocampus.
[5]"Sequences and expression patterns of murine erythroleukemia cDNAs isolated by subtractive cloning."
Miller I.J., Bieker J.J.
Submitted (SEP-1993) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 49-533.
+Additional computationally mapped references.

Cross-references

Sequence databases

AB128936 Genomic DNA. Translation: BAD08449.1.
AK076815 mRNA. Translation: BAC36494.1.
AK169684 mRNA. Translation: BAE41303.1.
BC086668 mRNA. Translation: AAH86668.1.
BC110673 mRNA. Translation: AAI10674.1.
L21027 mRNA. Translation: AAB67986.1.
IPIIPI00225961.
RefSeqNP_058662.2.
UniGeneMm.16898
Mm.371997

3D structure databases

HSSPHSSP built from PDB template 1HKU based on UniProtKB Q9Z2F5.
SMRQ61753. Positions 6-307.
ModBaseSearch...

PTM databases

PhosphoSiteQ61753.

2-D gel databases

SWISS-2DPAGEQ61753.
REPRODUCTION-2DPAGEQ61753.

Proteomic databases

PRIDEQ61753.

Genome annotation databases

EnsemblENSMUSG00000053398. Mus musculus. [Contig view]
GeneID236539.
KEGGmmu:236539.
NMPDRfig|10090.3.peg.26255.

Organism-specific databases

MGIMGI:1355330. Phgdh.

Phylogenomic databases

HOGENOMQ61753.
HOVERGENQ61753.
OMAQ61753. GTIQVIT.

Enzyme and pathway databases

BRENDA1.1.1.95. 244.

Gene expression databases

ArrayExpressQ61753.
BgeeQ61753.
CleanExMM_PHGDH.
GermOnlineENSMUSG00000053398. Mus musculus.

Family and domain databases

InterProIPR006236. D-3-Phosphoglycerate_DH.
IPR006139. D-isomer_2_OHA_DH.
IPR006140. D-isomer_2_OHA_DH_NAD-bd.
IPR015508. D3PG_DH.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
Gene3DG3DSA:3.40.50.720. NAD(P)-bd. 1 hit.
PANTHERPTHR10996:SF20. D3PG_Deh. 1 hit.
PfamPF00389. 2-Hacid_dh. 1 hit.
PF02826. 2-Hacid_dh_C. 1 hit.
[Graphical view]
TIGRFAMsTIGR01327. PGDH. 1 hit.
PROSITEPS00065. D_2_HYDROXYACID_DH_1. 1 hit.
PS00670. D_2_HYDROXYACID_DH_2. 1 hit.
PS00671. D_2_HYDROXYACID_DH_3. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

NextBio382995.
SOURCESearch...

Entry information

Entry nameSERA_MOUSE
AccessionPrimary (citable) accession number: Q61753
Secondary accession number(s): Q3TEE5, Q75SV9, Q8C603
Entry history
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: January 23, 2007
Last modified: June 16, 2009
This is version 81 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

Relevant documents

MGD cross-references

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

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents