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Protein

Phosphoserine aminotransferase

Gene

Psat1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the reversible conversion of 3-phosphohydroxypyruvate to phosphoserine and of 3-hydroxy-2-oxo-4-phosphonooxybutanoate to phosphohydroxythreonine.By similarity

Catalytic activityi

O-phospho-L-serine + 2-oxoglutarate = 3-phosphonooxypyruvate + L-glutamate.
4-phosphonooxy-L-threonine + 2-oxoglutarate = (3R)-3-hydroxy-2-oxo-4-phosphonooxybutanoate + L-glutamate.

Cofactori

pyridoxal 5'-phosphateBy similarityNote: Binds 1 pyridoxal phosphate per subunit.By similarity

Pathway: L-serine biosynthesis

This protein is involved in step 2 of the subpathway that synthesizes L-serine from 3-phospho-D-glycerate.
Proteins known to be involved in the 3 steps of the subpathway in this organism are:
  1. D-3-phosphoglycerate dehydrogenase (Phgdh)
  2. Phosphoserine aminotransferase (Psat1), Phosphoserine aminotransferase (Psat1), Phosphoserine aminotransferase (Psat1), Phosphoserine aminotransferase (Psat1), Phosphoserine aminotransferase (Psat1)
  3. Phosphoserine phosphatase (Psph)
This subpathway is part of the pathway L-serine biosynthesis, which is itself part of Amino-acid biosynthesis.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes L-serine from 3-phospho-D-glycerate, the pathway L-serine biosynthesis and in Amino-acid biosynthesis.

Pathway: pyridoxine 5'-phosphate biosynthesis

This protein is involved in step 3 of the subpathway that synthesizes pyridoxine 5'-phosphate from D-erythrose 4-phosphate.
Proteins known to be involved in the 5 steps of the subpathway in this organism are:
  1. no protein annotated in this organism
  2. no protein annotated in this organism
  3. Phosphoserine aminotransferase (Psat1)
  4. no protein annotated in this organism
  5. no protein annotated in this organism
This subpathway is part of the pathway pyridoxine 5'-phosphate biosynthesis, which is itself part of Cofactor biosynthesis.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes pyridoxine 5'-phosphate from D-erythrose 4-phosphate, the pathway pyridoxine 5'-phosphate biosynthesis and in Cofactor biosynthesis.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei45 – 451L-glutamateBy similarity
Binding sitei107 – 1071Pyridoxal phosphateBy similarity
Binding sitei156 – 1561Pyridoxal phosphateBy similarity
Binding sitei176 – 1761Pyridoxal phosphateBy similarity
Binding sitei199 – 1991Pyridoxal phosphateBy similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Aminotransferase, Transferase

Keywords - Biological processi

Amino-acid biosynthesis, Serine biosynthesis

Keywords - Ligandi

Pyridoxal phosphate

Enzyme and pathway databases

ReactomeiREACT_306239. Serine biosynthesis.
UniPathwayiUPA00135; UER00197.
UPA00244; UER00311.

Names & Taxonomyi

Protein namesi
Recommended name:
Phosphoserine aminotransferase (EC:2.6.1.52)
Short name:
PSAT
Alternative name(s):
Endometrial progesterone-induced protein
Short name:
EPIP
Phosphohydroxythreonine aminotransferase
Gene namesi
Name:Psat1
Synonyms:Psa, Psat
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Chromosome 19

Organism-specific databases

MGIiMGI:2183441. Psat1.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 370370Phosphoserine aminotransferasePRO_0000150136Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionineBy similarity
Modified residuei51 – 511N6-acetyllysineBy similarity
Modified residuei127 – 1271N6-acetyllysine1 Publication
Modified residuei200 – 2001N6-(pyridoxal phosphate)lysineBy similarity
Modified residuei269 – 2691N6-acetyllysineBy similarity
Modified residuei318 – 3181N6-acetyllysineBy similarity
Modified residuei323 – 3231N6-acetyllysineBy similarity
Modified residuei333 – 3331N6-acetyllysineBy similarity

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiQ99K85.
PaxDbiQ99K85.
PRIDEiQ99K85.

PTM databases

PhosphoSiteiQ99K85.

Expressioni

Gene expression databases

BgeeiQ99K85.
CleanExiMM_PSAT1.
ExpressionAtlasiQ99K85. baseline and differential.
GenevisibleiQ99K85. MM.

Interactioni

Subunit structurei

Homodimer.By similarity

Protein-protein interaction databases

BioGridi223231. 1 interaction.
IntActiQ99K85. 2 interactions.
MINTiMINT-4134236.
STRINGi10090.ENSMUSP00000025542.

Structurei

3D structure databases

ProteinModelPortaliQ99K85.
SMRiQ99K85. Positions 17-370.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni79 – 802Pyridoxal phosphate bindingBy similarity
Regioni241 – 2422Pyridoxal phosphate bindingBy similarity

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG1932.
GeneTreeiENSGT00390000015177.
HOGENOMiHOG000088965.
HOVERGENiHBG001218.
InParanoidiQ99K85.
KOiK00831.
OMAiNNTIFGT.
OrthoDBiEOG7KQ220.
PhylomeDBiQ99K85.
TreeFamiTF312975.

Family and domain databases

Gene3Di3.40.640.10. 1 hit.
3.90.1150.10. 1 hit.
HAMAPiMF_00160. SerC_aminotrans_5.
InterProiIPR000192. Aminotrans_V_dom.
IPR020578. Aminotrans_V_PyrdxlP_BS.
IPR022278. Pser_aminoTfrase.
IPR015424. PyrdxlP-dep_Trfase.
IPR015421. PyrdxlP-dep_Trfase_major_sub1.
IPR015422. PyrdxlP-dep_Trfase_major_sub2.
[Graphical view]
PfamiPF00266. Aminotran_5. 1 hit.
[Graphical view]
PIRSFiPIRSF000525. SerC. 1 hit.
SUPFAMiSSF53383. SSF53383. 1 hit.
TIGRFAMsiTIGR01364. serC_1. 1 hit.
PROSITEiPS00595. AA_TRANSFER_CLASS_5. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q99K85-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MEATKQVVNF GPGPAKLPHS VLLEIQKQLL DYRGLGISVL EMSHRSSDFA
60 70 80 90 100
KIIGNTENLV RELLAVPNNY KVIFVQGGGS GQFSAVPLNL IGLKAGRSAD
110 120 130 140 150
YVVTGAWSAK AAEEAKKFGT VNIVHPKLGS YTKIPDPSTW NLNPDASYVY
160 170 180 190 200
FCANETVHGV EFDFVPDVKG AVLVCDMSSN FLSRPVDVSK FGVIFAGAQK
210 220 230 240 250
NVGSAGVTVV IVRDDLLGFS LRECPSVLDY KVQAGNNSLY NTPPCFSIYV
260 270 280 290 300
MGMVLEWIKN NGGAAAMEKL SSIKSQMIYE IIDNSQGFYV CPVERQNRSR
310 320 330 340 350
MNIPFRIGNA KGDEALEKRF LDKAVELNMI SLKGHRSVGG IRASLYNAVT
360 370
TEDVEKLAAF MKNFLEMHQL
Length:370
Mass (Da):40,473
Last modified:June 1, 2001 - v1
Checksum:i6CF6B80CFDA1974B
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF259674 mRNA. Translation: AAK69389.1.
BC004827 mRNA. Translation: AAH04827.1.
CCDSiCCDS29681.1.
RefSeqiNP_803155.1. NM_177420.2.
UniGeneiMm.289936.

Genome annotation databases

EnsembliENSMUST00000025542; ENSMUSP00000025542; ENSMUSG00000024640.
GeneIDi107272.
KEGGimmu:107272.
UCSCiuc008gwp.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF259674 mRNA. Translation: AAK69389.1.
BC004827 mRNA. Translation: AAH04827.1.
CCDSiCCDS29681.1.
RefSeqiNP_803155.1. NM_177420.2.
UniGeneiMm.289936.

3D structure databases

ProteinModelPortaliQ99K85.
SMRiQ99K85. Positions 17-370.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi223231. 1 interaction.
IntActiQ99K85. 2 interactions.
MINTiMINT-4134236.
STRINGi10090.ENSMUSP00000025542.

PTM databases

PhosphoSiteiQ99K85.

Proteomic databases

MaxQBiQ99K85.
PaxDbiQ99K85.
PRIDEiQ99K85.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000025542; ENSMUSP00000025542; ENSMUSG00000024640.
GeneIDi107272.
KEGGimmu:107272.
UCSCiuc008gwp.2. mouse.

Organism-specific databases

CTDi29968.
MGIiMGI:2183441. Psat1.

Phylogenomic databases

eggNOGiCOG1932.
GeneTreeiENSGT00390000015177.
HOGENOMiHOG000088965.
HOVERGENiHBG001218.
InParanoidiQ99K85.
KOiK00831.
OMAiNNTIFGT.
OrthoDBiEOG7KQ220.
PhylomeDBiQ99K85.
TreeFamiTF312975.

Enzyme and pathway databases

UniPathwayiUPA00135; UER00197.
UPA00244; UER00311.
ReactomeiREACT_306239. Serine biosynthesis.

Miscellaneous databases

ChiTaRSiPsat1. mouse.
NextBioi358656.
PROiQ99K85.
SOURCEiSearch...

Gene expression databases

BgeeiQ99K85.
CleanExiMM_PSAT1.
ExpressionAtlasiQ99K85. baseline and differential.
GenevisibleiQ99K85. MM.

Family and domain databases

Gene3Di3.40.640.10. 1 hit.
3.90.1150.10. 1 hit.
HAMAPiMF_00160. SerC_aminotrans_5.
InterProiIPR000192. Aminotrans_V_dom.
IPR020578. Aminotrans_V_PyrdxlP_BS.
IPR022278. Pser_aminoTfrase.
IPR015424. PyrdxlP-dep_Trfase.
IPR015421. PyrdxlP-dep_Trfase_major_sub1.
IPR015422. PyrdxlP-dep_Trfase_major_sub2.
[Graphical view]
PfamiPF00266. Aminotran_5. 1 hit.
[Graphical view]
PIRSFiPIRSF000525. SerC. 1 hit.
SUPFAMiSSF53383. SSF53383. 1 hit.
TIGRFAMsiTIGR01364. serC_1. 1 hit.
PROSITEiPS00595. AA_TRANSFER_CLASS_5. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Sato M., Oguma T., Tsujimoto K., Tadakuma T.
    Submitted (APR-2000) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: BALB/c.
  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].
  3. Lubec G., Kang S.U., Sunyer B., Chen W.-Q.
    Submitted (JAN-2009) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 17-27; 52-94; 191-200; 223-231 AND 343-356, IDENTIFICATION BY MASS SPECTROMETRY.
    Strain: C57BL/6 and OF1.
    Tissue: Brain and Hippocampus.
  4. "SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
    Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
    Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-127, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic fibroblast.

Entry informationi

Entry nameiSERC_MOUSE
AccessioniPrimary (citable) accession number: Q99K85
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 23, 2002
Last sequence update: June 1, 2001
Last modified: June 24, 2015
This is version 128 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

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.