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Q9Y617 (SERC_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 150. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (7) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Phosphoserine aminotransferase

EC=2.6.1.52
Alternative name(s):
Phosphohydroxythreonine aminotransferase
Short name=PSAT
Gene names
Name:PSAT1
Synonyms:PSA
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length370 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Catalyzes the reversible conversion of 3-phosphohydroxypyruvate to phosphoserine and of 3-hydroxy-2-oxo-4-phosphonooxybutanoate to phosphohydroxythreonine By similarity. HAMAP-Rule MF_00160

Catalytic activity

O-phospho-L-serine + 2-oxoglutarate = 3-phosphonooxypyruvate + L-glutamate. HAMAP-Rule MF_00160

4-phosphonooxy-L-threonine + 2-oxoglutarate = (3R)-3-hydroxy-2-oxo-4-phosphonooxybutanoate + L-glutamate. HAMAP-Rule MF_00160

Cofactor

Binds 1 pyridoxal phosphate per subunit By similarity. HAMAP-Rule MF_00160

Pathway

Amino-acid biosynthesis; L-serine biosynthesis; L-serine from 3-phospho-D-glycerate: step 2/3. HAMAP-Rule MF_00160

Cofactor biosynthesis; pyridoxine 5'-phosphate biosynthesis; pyridoxine 5'-phosphate from D-erythrose 4-phosphate: step 3/5. HAMAP-Rule MF_00160

Subunit structure

Homodimer By similarity. HAMAP-Rule MF_00160

Tissue specificity

Expressed at high levels in the brain, liver, kidney and pancreas, and very weakly expressed in the thymus, prostate, testis and colon.

Involvement in disease

Phosphoserine aminotransferase deficiency (PSATD) [MIM:610992]: Characterized biochemically by low plasma and cerebrospinal fluid concentrations of serine and glycine and clinically by intractable seizures, acquired microcephaly, hypertonia, and psychomotor retardation.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.9

Sequence similarities

Belongs to the class-V pyridoxal-phosphate-dependent aminotransferase family. SerC subfamily.

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q9Y617-1)

Also known as: Alpha;

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: Q9Y617-2)

Also known as: Beta;

The sequence of this isoform differs from the canonical sequence as follows:
     291-336: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 370370Phosphoserine aminotransferase HAMAP-Rule MF_00160
PRO_0000150135

Regions

Region79 – 802Pyridoxal phosphate binding By similarity
Region241 – 2422Pyridoxal phosphate binding By similarity

Sites

Binding site451L-glutamate By similarity
Binding site1071Pyridoxal phosphate By similarity
Binding site1561Pyridoxal phosphate By similarity
Binding site1761Pyridoxal phosphate By similarity
Binding site1991Pyridoxal phosphate By similarity

Amino acid modifications

Modified residue11N-acetylmethionine Ref.6
Modified residue511N6-acetyllysine Ref.7
Modified residue1271N6-acetyllysine By similarity
Modified residue2001N6-(pyridoxal phosphate)lysine By similarity
Modified residue2691N6-acetyllysine Ref.7
Modified residue3181N6-acetyllysine Ref.7
Modified residue3231N6-acetyllysine Ref.7
Modified residue3331N6-acetyllysine Ref.7

Natural variations

Alternative sequence291 – 33646Missing in isoform 2.
VSP_000237
Natural variant871P → A.
Corresponds to variant rs11540974 [ dbSNP | Ensembl ].
VAR_048235
Natural variant1001D → A in PSATD; reduced Vmax. Ref.9
VAR_037252

Experimental info

Sequence conflict401L → V in AAH16645. Ref.5

Secondary structure

................................................................ 370
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 (Alpha) [UniParc].

Last modified January 23, 2002. Version 2.
Checksum: BAF9A10E71B165B4

FASTA37040,423
        10         20         30         40         50         60 
MDAPRQVVNF GPGPAKLPHS VLLEIQKELL DYKGVGISVL EMSHRSSDFA KIINNTENLV 

        70         80         90        100        110        120 
RELLAVPDNY KVIFLQGGGC GQFSAVPLNL IGLKAGRCAD YVVTGAWSAK AAEEAKKFGT 

       130        140        150        160        170        180 
INIVHPKLGS YTKIPDPSTW NLNPDASYVY YCANETVHGV EFDFIPDVKG AVLVCDMSSN 

       190        200        210        220        230        240 
FLSKPVDVSK FGVIFAGAQK NVGSAGVTVV IVRDDLLGFA LRECPSVLEY KVQAGNSSLY 

       250        260        270        280        290        300 
NTPPCFSIYV MGLVLEWIKN NGGAAAMEKL SSIKSQTIYE IIDNSQGFYV CPVEPQNRSK 

       310        320        330        340        350        360 
MNIPFRIGNA KGDDALEKRF LDKALELNML SLKGHRSVGG IRASLYNAVT IEDVQKLAAF 

       370 
MKKFLEMHQL 

« Hide

Isoform 2 (Beta) [UniParc].

Checksum: 4F83811D3593DDA1
Show »

FASTA32435,189

References

« Hide 'large scale' references
[1]"Characterization of human phosphoserine aminotransferase involved in the phosphorylated pathway of L-serine biosynthesis."
Baek J.Y., Jun Y.D., Taub D., Kim Y.H.
Biochem. J. 373:191-200(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
[2]"Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
[3]"DNA sequence and analysis of human chromosome 9."
Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S., Bagguley C.L. expand/collapse author list , Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A., Frankland J.A., French L., Fricker D.G., Garner P., Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S., Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E., Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D., Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E., Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K., Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M., Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J., Dunham I.
Nature 429:369-374(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]"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] (ISOFORMS 1 AND 2).
Tissue: Lung, Lymph and Placenta.
[6]"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[7]"Lysine acetylation targets protein complexes and co-regulates major cellular functions."
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-51; LYS-269; LYS-318; LYS-323 AND LYS-333, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[8]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[9]"Phosphoserine aminotransferase deficiency: a novel disorder of the serine biosynthesis pathway."
Hart C.E., Race V., Achouri Y., Wiame E., Sharrard M., Olpin S.E., Watkinson J., Bonham J.R., Jaeken J., Matthijs G., Van Schaftingen E.
Am. J. Hum. Genet. 80:931-937(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT PSATD ALA-100, CHARACTERIZATION OF VARIANT PSATD ALA-100.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF113132 mRNA. Translation: AAD42052.1.
AY131232 mRNA. Translation: AAN71736.1.
BT006840 mRNA. Translation: AAP35486.1.
AL353594 Genomic DNA. Translation: CAI16882.1.
AL353594 Genomic DNA. Translation: CAI16883.1.
CH471089 Genomic DNA. Translation: EAW62621.1.
CH471089 Genomic DNA. Translation: EAW62617.1.
BC000971 mRNA. Translation: AAH00971.1.
BC004863 mRNA. Translation: AAH04863.1.
BC016645 mRNA. Translation: AAH16645.1.
BC018129 mRNA. Translation: AAH18129.1.
CCDSCCDS6659.1. [Q9Y617-2]
CCDS6660.1. [Q9Y617-1]
RefSeqNP_066977.1. NM_021154.4. [Q9Y617-2]
NP_478059.1. NM_058179.3. [Q9Y617-1]
UniGeneHs.494261.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3E77X-ray2.50A/B/C17-370[»]
ProteinModelPortalQ9Y617.
SMRQ9Y617. Positions 17-370.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid119001. 23 interactions.
IntActQ9Y617. 3 interactions.
MINTMINT-1490243.
STRING9606.ENSP00000365773.

Chemistry

DrugBankDB00142. L-Glutamic Acid.
DB00114. Pyridoxal Phosphate.
DB00165. Pyridoxine.

PTM databases

PhosphoSiteQ9Y617.

Polymorphism databases

DMDM20141815.

2D gel databases

REPRODUCTION-2DPAGEIPI00001734.

Proteomic databases

MaxQBQ9Y617.
PaxDbQ9Y617.
PeptideAtlasQ9Y617.
PRIDEQ9Y617.

Protocols and materials databases

DNASU29968.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000347159; ENSP00000317606; ENSG00000135069. [Q9Y617-2]
ENST00000376588; ENSP00000365773; ENSG00000135069. [Q9Y617-1]
GeneID29968.
KEGGhsa:29968.
UCSCuc004ala.3. human. [Q9Y617-1]
uc004alb.3. human. [Q9Y617-2]

Organism-specific databases

CTD29968.
GeneCardsGC09P080911.
HGNCHGNC:19129. PSAT1.
HPACAB014882.
CAB040567.
MIM610936. gene.
610992. phenotype.
neXtProtNX_Q9Y617.
Orphanet284417. Phosphoserine aminotransferase deficiency.
PharmGKBPA128395782.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG1932.
HOGENOMHOG000088965.
HOVERGENHBG001218.
InParanoidQ9Y617.
KOK00831.
OMAVFFGAQK.
OrthoDBEOG7KQ220.
PhylomeDBQ9Y617.
TreeFamTF312975.

Enzyme and pathway databases

BioCycMetaCyc:HS05946-MONOMER.
ReactomeREACT_111217. Metabolism.
UniPathwayUPA00135; UER00197.
UPA00244; UER00311.

Gene expression databases

ArrayExpressQ9Y617.
BgeeQ9Y617.
CleanExHS_PSAT1.
GenevestigatorQ9Y617.

Family and domain databases

Gene3D3.40.640.10. 1 hit.
3.90.1150.10. 1 hit.
HAMAPMF_00160. SerC_aminotrans_5.
InterProIPR000192. Aminotrans_V/Cys_dSase.
IPR020578. Aminotrans_V_PyrdxlP_BS.
IPR022278. Pser_aminoTfrase.
IPR003248. Pser_aminoTfrase_subgr.
IPR015424. PyrdxlP-dep_Trfase.
IPR015421. PyrdxlP-dep_Trfase_major_sub1.
IPR015422. PyrdxlP-dep_Trfase_major_sub2.
[Graphical view]
PfamPF00266. Aminotran_5. 1 hit.
[Graphical view]
PIRSFPIRSF000525. SerC. 1 hit.
SUPFAMSSF53383. SSF53383. 1 hit.
TIGRFAMsTIGR01364. serC_1. 1 hit.
PROSITEPS00595. AA_TRANSFER_CLASS_5. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSPSAT1. human.
EvolutionaryTraceQ9Y617.
GeneWikiPSAT1.
GenomeRNAi29968.
NextBio52705.
PROQ9Y617.
SOURCESearch...

Entry information

Entry nameSERC_HUMAN
AccessionPrimary (citable) accession number: Q9Y617
Secondary accession number(s): Q5T7G5 expand/collapse secondary AC list , Q5T7G6, Q96AW2, Q9BQ12
Entry history
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: January 23, 2002
Last modified: July 9, 2014
This is version 150 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 9

Human chromosome 9: entries, gene names and cross-references to MIM