UniProt Accession

 SERC_HUMAN; Q9Y617; Q5T7G5; Q5T7G6; Q96AW2; Q9BQ12 

Genbank Protein ID

 AF113132; AY131232; BT006840; AL353594; AL353594; CH471089; CH471089; BC000971; BC004863; BC016645; BC018129 

Genbank Nucleotide ID

 AAD42052.1; AAN71736.1; AAP35486.1; CAI16882.1; CAI16883.1; EAW62621.1; EAW62617.1; AAH00971.1; AAH04863.1; AAH16645.1; AAH18129.1 

Protein Name

 Phosphoserine aminotransferase 

Protein Synonyms/Alias

 Phosphohydroxythreonine aminotransferase; PSAT 

Gene Name

 PSAT1 

Gene Synonyms/Alias

 PSA 

Created Date

 July 27, 2013 

Organism

 Homo sapiens (Human) 

NCBI Taxa ID

 9606 

Lysine Modification

Position	Peptide	Type	References
16	NFGPGPAKLPHSVLL	ubiquitination	[1, 2, 3, 4]
27	SVLLEIQKELLDYKG	ubiquitination	[1, 2, 3, 4, 5, 6, 7]
33	QKELLDYKGVGISVL	ubiquitination	[3, 4, 7]
51	HRSSDFAKIINNTEN	acetylation	[8]
51	HRSSDFAKIINNTEN	ubiquitination	[1, 2, 3, 4, 5, 6, 7, 9, 10, 11, 12]
94	PLNLIGLKAGRCADY	ubiquitination	[2, 3, 6]
110	VTGAWSAKAAEEAKK	acetylation	[4, 13]
110	VTGAWSAKAAEEAKK	ubiquitination	[3]
117	KAAEEAKKFGTINIV	ubiquitination	[3, 7]
127	TINIVHPKLGSYTKI	acetylation	[4, 8]
127	TINIVHPKLGSYTKI	ubiquitination	[3]
184	MSSNFLSKPVDVSKF	ubiquitination	[2, 3, 4, 6]
190	SKPVDVSKFGVIFAG	ubiquitination	[1, 3]
269	GGAAAMEKLSSIKSQ	acetylation	[8]
269	GGAAAMEKLSSIKSQ	ubiquitination	[2, 3]
274	MEKLSSIKSQTIYEI	ubiquitination	[6]
300	VEPQNRSKMNIPFRI	ubiquitination	[3, 4]
311	PFRIGNAKGDDALEK	acetylation	[4]
311	PFRIGNAKGDDALEK	ubiquitination	[2, 3, 6, 7]
318	KGDDALEKRFLDKAL	acetylation	[4, 8]
318	KGDDALEKRFLDKAL	ubiquitination	[2, 3, 11]
323	LEKRFLDKALELNML	acetylation	[8]
323	LEKRFLDKALELNML	ubiquitination	[1, 2, 3, 4, 5, 6, 7, 9, 10, 11, 12, 14]
333	ELNMLSLKGHRSVGG	acetylation	[4, 8]
333	ELNMLSLKGHRSVGG	ubiquitination	[1, 2, 3, 4, 6, 7, 11]
356	VTIEDVQKLAAFMKK	ubiquitination	[2, 3]
363	KLAAFMKKFLEMHQL	ubiquitination	[1, 2, 3]

Reference

 [1] A proteome-wide, quantitative survey of in vivo ubiquitylation sites reveals widespread regulatory roles.
 Wagner SA, Beli P, Weinert BT, Nielsen ML, Cox J, Mann M, Choudhary C.
 Mol Cell Proteomics. 2011 Oct;10(10):M111.013284. [PMID: 21890473]
 [2] Systematic and quantitative assessment of the ubiquitin-modified proteome.
 Kim W, Bennett EJ, Huttlin EL, Guo A, Li J, Possemato A, Sowa ME, Rad R, Rush J, Comb MJ, Harper JW, Gygi SP.
 Mol Cell. 2011 Oct 21;44(2):325-40. [PMID: 21906983]
 [3] Refined preparation and use of anti-diglycine remnant (K-ε-GG) antibody enables routine quantification of 10,000s of ubiquitination sites in single proteomics experiments.
 Udeshi ND, Svinkina T, Mertins P, Kuhn E, Mani DR, Qiao JW, Carr SA.
 Mol Cell Proteomics. 2013 Mar;12(3):825-31. [PMID: 23266961]
 [4] Integrated proteomic analysis of post-translational modifications by serial enrichment.
 Mertins P, Qiao JW, Patel J, Udeshi ND, Clauser KR, Mani DR, Burgess MW, Gillette MA, Jaffe JD, Carr SA.
 Nat Methods. 2013 Jul;10(7):634-7. [PMID: 23749302]
 [5] Global analysis of lysine ubiquitination by ubiquitin remnant immunoaffinity profiling.
 Xu G, Paige JS, Jaffrey SR.
 Nat Biotechnol. 2010 Aug;28(8):868-73. [PMID: 20639865]
 [6] Global identification of modular cullin-RING ligase substrates.
 Emanuele MJ, Elia AE, Xu Q, Thoma CR, Izhar L, Leng Y, Guo A, Chen YN, Rush J, Hsu PW, Yen HC, Elledge SJ.
 Cell. 2011 Oct 14;147(2):459-74. [PMID: 21963094]
 [7] Landscape of the PARKIN-dependent ubiquitylome in response to mitochondrial depolarization.
 Sarraf SA, Raman M, Guarani-Pereira V, Sowa ME, Huttlin EL, Gygi SP, Harper JW.
 Nature. 2013 Apr 18;496(7445):372-6. [PMID: 23503661]
 [8] Lysine acetylation targets protein complexes and co-regulates major cellular functions.
 Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M.
 Science. 2009 Aug 14;325(5942):834-40. [PMID: 19608861]
 [9] Mass spectrometric analysis of lysine ubiquitylation reveals promiscuity at site level.
 Danielsen JM, Sylvestersen KB, Bekker-Jensen S, Szklarczyk D, Poulsen JW, Horn H, Jensen LJ, Mailand N, Nielsen ML.
 Mol Cell Proteomics. 2011 Mar;10(3):M110.003590. [PMID: 21139048]
 [10] Proteome-wide identification of ubiquitylation sites by conjugation of engineered lysine-less ubiquitin.
 Oshikawa K, Matsumoto M, Oyamada K, Nakayama KI.
 J Proteome Res. 2012 Feb 3;11(2):796-807. [PMID: 22053931]
 [11] Methods for quantification of in vivo changes in protein ubiquitination following proteasome and deubiquitinase inhibition.
 Udeshi ND, Mani DR, Eisenhaure T, Mertins P, Jaffe JD, Clauser KR, Hacohen N, Carr SA.
 Mol Cell Proteomics. 2012 May;11(5):148-59. [PMID: 22505724]
 [12] hCKSAAP_UbSite: improved prediction of human ubiquitination sites by exploiting amino acid pattern and properties.
 Chen Z, Zhou Y, Song J, Zhang Z.
 Biochim Biophys Acta. 2013 Aug;1834(8):1461-7. [PMID: 23603789]
 [13] Proteomic investigations of lysine acetylation identify diverse substrates of mitochondrial deacetylase sirt3.
 Sol EM, Wagner SA, Weinert BT, Kumar A, Kim HS, Deng CX, Choudhary C.
 PLoS One. 2012;7(12):e50545. [PMID: 23236377]
 [14] A data set of human endogenous protein ubiquitination sites.
 Shi Y, Chan DW, Jung SY, Malovannaya A, Wang Y, Qin J.
 Mol Cell Proteomics. 2011 May;10(5):M110.002089. [PMID: 20972266] 

Functional Description

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

Sequence Annotation

 REGION 79 80 Pyridoxal phosphate binding (By
 REGION 241 242 Pyridoxal phosphate binding (By
 BINDING 45 45 L-glutamate (By similarity).
 BINDING 107 107 Pyridoxal phosphate (By similarity).
 BINDING 156 156 Pyridoxal phosphate (By similarity).
 BINDING 176 176 Pyridoxal phosphate (By similarity).
 BINDING 199 199 Pyridoxal phosphate (By similarity).
 MOD_RES 1 1 N-acetylmethionine.
 MOD_RES 51 51 N6-acetyllysine.
 MOD_RES 200 200 N6-(pyridoxal phosphate)lysine (By
 MOD_RES 269 269 N6-acetyllysine.
 MOD_RES 318 318 N6-acetyllysine.
 MOD_RES 323 323 N6-acetyllysine.
 MOD_RES 333 333 N6-acetyllysine.  

Keyword

 3D-structure; Acetylation; Alternative splicing; Amino-acid biosynthesis; Aminotransferase; Complete proteome; Disease mutation; Polymorphism; Pyridoxal phosphate; Reference proteome; Serine biosynthesis; Transferase. 

Sequence Source

 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 

Protein Length

 370 AA 

Protein Sequence

Gene Ontology

 GO:0005829; C:cytosol; TAS:Reactome.
 GO:0004648; F:O-phospho-L-serine:2-oxoglutarate aminotransferase activity; NAS:UniProtKB.
 GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
 GO:0006564; P:L-serine biosynthetic process; NAS:UniProtKB.
 GO:0008615; P:pyridoxine biosynthetic process; NAS:UniProtKB. 

Interpro

 IPR000192; 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. 

Pfam

 PF00266; Aminotran_5 

SMART

  

PROSITE

 PS00595; AA_TRANSFER_CLASS_5 

PRINTS