Reviewed, UniProtKB/Swiss-Prot Q9Y617 (SERC_HUMAN)

Names and origin

Protein names

Recommended name:
    Phosphoserine aminotransferase
    EC=2.6.1.52
Alternative name(s):
    Phosphohydroxythreonine aminotransferase
      Short name=PSAT

Gene names

Name:	PSAT1
Synonyms:	PSA

Organism

Homo sapiens (Human) [Complete proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	370 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence 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.
Catalytic activity	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.
Cofactor	Binds 1 pyridoxal phosphate per subunit By similarity.
Pathway	Amino-acid biosynthesis; L-serine biosynthesis; L-serine from 3-phospho-D-glycerate: step 2/3. Cofactor biosynthesis; pyridoxine 5'-phosphate biosynthesis; pyridoxine 5'-phosphate from D-erythrose 4-phosphate: step 3/5.
Subunit structure	Homodimer By similarity.
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	Defects in PSAT1 are the cause of phosphoserine aminotransferase deficiency (PSATD) [MIM:610992]. PSATD is characterized biochemically by low plasma and cerebrospinal fluid concentrations of serine and glycine and clinically by intractable seizures, acquired microcephaly, hypertonia, and psychomotor retardation. Ref.8
Sequence similarities	Belongs to the class-V pyridoxal-phosphate-dependent aminotransferase family. SerC subfamily.

Ontologies

Keywords
Biological process	Amino-acid biosynthesis Serine biosynthesis
Coding sequence diversity	Alternative splicing Polymorphism
Disease	Disease mutation
Ligand	Pyridoxal phosphate
Molecular function	Aminotransferase Transferase
PTM	Acetylation
Technical term	3D-structure Complete proteome
Gene Ontology (GO)
Biological process	L-serine biosynthetic process Non-traceable author statement. Source: UniProtKB pyridoxine biosynthetic process Non-traceable author statement. Source: UniProtKB
Molecular function	O-phospho-L-serine:2-oxoglutarate aminotransferase activity Non-traceable author statement. Source: UniProtKB pyridoxal phosphate binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

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.

Note: No experimental confirmation available.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 370

370

Phosphoserine aminotransferase

PRO_0000150135

Regions

Region

79 – 80

2

Pyridoxal phosphate binding By similarity

Region

241 – 242

2

Pyridoxal phosphate binding By similarity

Sites

Binding site

45

1

L-glutamate By similarity

Binding site

107

1

Pyridoxal phosphate By similarity

Binding site

156

1

Pyridoxal phosphate By similarity

Binding site

176

1

Pyridoxal phosphate By similarity

Binding site

199

1

Pyridoxal phosphate By similarity

Amino acid modifications

Modified residue

51

1

N6-acetyllysine Ref.7

Modified residue

200

1

N6-(pyridoxal phosphate)lysine By similarity

Modified residue

269

1

N6-acetyllysine Ref.7

Modified residue

318

1

N6-acetyllysine Ref.7

Modified residue

323

1

N6-acetyllysine Ref.7

Modified residue

333

1

N6-acetyllysine Ref.7

Natural variations

Alternative sequence

291 – 336

46

Missing in isoform 2.

VSP_000237

Natural variant

87

1

P → A: dbSNP rs11540974.

VAR_048235

Natural variant

100

1

D → A in PSATD; reduced Vmax. Ref.8

VAR_037252

Experimental info

Sequence conflict

40

1

L → V in AAH16645. Ref.5

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

370

Helix Strand Turn

Details...

Helix

19 – 27

9

Beta strand

29 – 31

3

Turn

39 – 41

3

Helix

47 – 64

18

Beta strand

70 – 75

6

Helix

85 – 90

6

Beta strand

99 – 101

3

Helix

107 – 115

9

Beta strand

121 – 123

3

Helix

137 – 139

3

Beta strand

149 – 154

6

Beta strand

173 – 176

4

Turn

178 – 182

5

Helix

188 – 190

3

Beta strand

194 – 196

3

Turn

199 – 201

3

Beta strand

208 – 213

6

Helix

226 – 228

3

Helix

230 – 233

4

Helix

245 – 250

6

Helix

254 – 260

7

Helix

265 – 283

19

Helix

295 – 297

3

Beta strand

300 – 304

5

Helix

314 – 326

13

Beta strand

329 – 331

3

Beta strand

342 – 344

3

Helix

351 – 368

18

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 (Alpha) [UniParc]. Last modified January 23, 2002. Version 2. Checksum: BAF9A10E71B165B4	FASTA	370	40,423
	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
	Isoform 2 (Beta). Checksum: 4F83811D3593DDA1	FASTA	324	35,189
	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 SVGGIRASLY 310 320 NAVTIEDVQK LAAFMKKFLE MHQL

References

	« Hide 'large scale' referencesShow '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: 12633500] [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. , 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: 15164053] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]	Mural R.J., Istrail S., Sutton 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. , 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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2). Tissue: Lung, Lymph and Placenta.
[6]	Colinge J., Superti-Furga G., Bennett K.L. Submitted (OCT-2008) to UniProtKB Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
[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., Olsen J.V., Mann M. Science 325:834-840(2009) [PubMed: 19608861] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-51; LYS-269; LYS-318; LYS-323 AND LYS-333, MASS SPECTROMETRY.
[8]	"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: 17436247] [Abstract] Cited for: VARIANT PSATD ALA-100, CHARACTERIZATION OF VARIANT PSATD ALA-100.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBLGenBankDDBJ

AF113132 mRNA. Translation: AAD42052.1.
AY131232 mRNA. Translation: AAN71736.1.
BT006840 mRNA. Translation: AAP35486.1.
AL353594 Genomic DNA. Translation: CAI16882.1.
CH471089 Genomic DNA. Translation: EAW62621.1.
BC000971 mRNA. Translation: AAH00971.1.
BC004863 mRNA. Translation: AAH04863.1.
BC016645 mRNA. Translation: AAH16645.1.
BC018129 mRNA. Translation: AAH18129.1.

IPI

IPI00219478.
IPI00930609.

RefSeq

NP_066977.1.
NP_478059.1.

UniGene

Hs.494261
Hs.592595

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
3E77	X-ray	2.50	A/B/C	17-370	[»]

ModBase

Search...

Protein-protein interaction databases

IntAct

Q9Y617. 3 interactions.

STRING

Q9Y617.

PTM databases

PhosphoSite

Q9Y617.

2-D gel databases

REPRODUCTION-2DPAGE

IPI00001734.

Proteomic databases

PeptideAtlas

Q9Y617.

PRIDE

Q9Y617.

Genome annotation databases

Ensembl

ENST00000347159; ENSP00000317606; ENSG00000135069; Homo sapiens. [Genome view]
ENST00000376588; ENSP00000365773; ENSG00000135069; Homo sapiens. [Genome view]
ENST00000421149; ENSP00000388939; ENSG00000135069; Homo sapiens. [Genome view]

GeneID

29968.

KEGG

hsa:29968.

NMPDR

fig|9606.3.peg.31453.

UCSC

uc004ala.1. human.
uc004alb.1. human.

Organism-specific databases

CTD

29968.

GeneCards

GC09P080101.

H-InvDB

HIX0020015.

HGNC

HGNC:19129. PSAT1.

HPA

CAB014882.

MIM

610936. gene.
610992. phenotype.

Orphanet

35705. Neurometabolic disorder due to serine deficiency.

PharmGKB

PA128395782.

GenAtlas

Search...

Phylogenomic databases

HOGENOM

Q9Y617.

HOVERGEN

Q9Y617.

OMA

SMYNTPP.

Enzyme and pathway databases

BRENDA

2.6.1.52. 247.

Gene expression databases

ArrayExpress

Q9Y617.

Bgee

Q9Y617.

CleanEx

HS_PSAT1.

Genevestigator

Q9Y617.

GermOnline

ENSG00000135069. Homo sapiens.

Family and domain databases

InterPro

IPR000192. Aminotrans_V/Cys_dSase.
IPR020578. Aminotrans_V_PyrdxlP_BS.
IPR003248. Pser_amintransf.
IPR015421. PyrdxlP-dep_Trfase_major_sub1.
IPR015422. PyrdxlP-dep_Trfase_major_sub2.
[Graphical view]

Gene3D

G3DSA:3.40.640.10. PyrdxlP-dep_Trfase_major_sub1. 1 hit.
G3DSA:3.90.1150.10. PyrdxlP-dep_Trfase_major_sub2. 1 hit.

Pfam

PF00266. Aminotran_5. 1 hit.
[Graphical view]

ProDom

PD001544. Pser_amintransf. 1 hit.
[Graphical view] [Entries sharing at least one domain]

TIGRFAMs

TIGR01364. serC_1. 1 hit.

PROSITE

PS00595. AA_TRANSFER_CLASS_5. 1 hit.
[Graphical view]

ProtoNet

Search...

Other Resources

DrugBank

DB00142. L-Glutamic Acid.
DB00114. Pyridoxal Phosphate.
DB00165. Pyridoxine.

NextBio

52705.

SOURCE

Search...

Entry information

Entry name

SERC_HUMAN

Accession

Primary (citable) accession number: Q9Y617
Secondary accession number(s): Q5T7G6, Q96AW2, Q9BQ12

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 30, 2000
Last sequence update:	January 23, 2002
Last modified:	November 3, 2009
This is version 102 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

Disclaimer

Any 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.