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Q9Y617

- SERC_HUMAN

UniProt

Q9Y617 - SERC_HUMAN

Protein

Phosphoserine aminotransferase

Gene

PSAT1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 152 (01 Oct 2014)
      Sequence version 2 (23 Jan 2002)
      Previous versions | rss
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    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

    Binds 1 pyridoxal phosphate per subunit.By similarity

    Pathwayi

    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

    1. O-phospho-L-serine:2-oxoglutarate aminotransferase activity Source: UniProtKB
    2. pyridoxal phosphate binding Source: InterPro

    GO - Biological processi

    1. cellular amino acid biosynthetic process Source: Reactome
    2. cellular nitrogen compound metabolic process Source: Reactome
    3. L-serine biosynthetic process Source: UniProtKB
    4. pyridoxine biosynthetic process Source: UniProtKB
    5. small molecule metabolic process Source: Reactome

    Keywords - Molecular functioni

    Aminotransferase, Transferase

    Keywords - Biological processi

    Amino-acid biosynthesis, Serine biosynthesis

    Keywords - Ligandi

    Pyridoxal phosphate

    Enzyme and pathway databases

    BioCyciMetaCyc:HS05946-MONOMER.
    ReactomeiREACT_115789. Serine biosynthesis.
    UniPathwayiUPA00135; UER00197.
    UPA00244; UER00311.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Phosphoserine aminotransferase (EC:2.6.1.52)
    Alternative name(s):
    Phosphohydroxythreonine aminotransferase
    Short name:
    PSAT
    Gene namesi
    Name:PSAT1
    Synonyms:PSA
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 9

    Organism-specific databases

    HGNCiHGNC:19129. PSAT1.

    Subcellular locationi

    GO - Cellular componenti

    1. cytosol Source: Reactome
    2. extracellular vesicular exosome Source: UniProt

    Pathology & Biotechi

    Involvement in diseasei

    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.1 Publication
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti100 – 1001D → A in PSATD; reduced Vmax. 1 Publication
    VAR_037252

    Keywords - Diseasei

    Disease mutation

    Organism-specific databases

    MIMi610992. phenotype.
    Orphaneti284417. Phosphoserine aminotransferase deficiency.
    PharmGKBiPA128395782.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 370370Phosphoserine aminotransferasePRO_0000150135Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei1 – 11N-acetylmethionine1 Publication
    Modified residuei51 – 511N6-acetyllysine1 Publication
    Modified residuei127 – 1271N6-acetyllysineBy similarity
    Modified residuei200 – 2001N6-(pyridoxal phosphate)lysineBy similarity
    Modified residuei269 – 2691N6-acetyllysine1 Publication
    Modified residuei318 – 3181N6-acetyllysine1 Publication
    Modified residuei323 – 3231N6-acetyllysine1 Publication
    Modified residuei333 – 3331N6-acetyllysine1 Publication

    Keywords - PTMi

    Acetylation

    Proteomic databases

    MaxQBiQ9Y617.
    PaxDbiQ9Y617.
    PeptideAtlasiQ9Y617.
    PRIDEiQ9Y617.

    2D gel databases

    REPRODUCTION-2DPAGEIPI00001734.

    PTM databases

    PhosphoSiteiQ9Y617.

    Expressioni

    Tissue specificityi

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

    Gene expression databases

    ArrayExpressiQ9Y617.
    BgeeiQ9Y617.
    CleanExiHS_PSAT1.
    GenevestigatoriQ9Y617.

    Organism-specific databases

    HPAiCAB014882.
    CAB040567.

    Interactioni

    Subunit structurei

    Homodimer.By similarity

    Protein-protein interaction databases

    BioGridi119001. 24 interactions.
    IntActiQ9Y617. 3 interactions.
    MINTiMINT-1490243.
    STRINGi9606.ENSP00000365773.

    Structurei

    Secondary structure

    1
    370
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi19 – 279
    Beta strandi29 – 313
    Helixi32 – 343
    Beta strandi35 – 373
    Turni39 – 413
    Helixi47 – 6418
    Beta strandi70 – 778
    Helixi78 – 9013
    Helixi91 – 933
    Beta strandi98 – 1014
    Helixi106 – 11510
    Turni116 – 1183
    Beta strandi119 – 1235
    Beta strandi129 – 1313
    Helixi137 – 1393
    Beta strandi149 – 1557
    Turni156 – 1594
    Beta strandi173 – 1764
    Turni178 – 1825
    Helixi188 – 1903
    Beta strandi192 – 1976
    Turni198 – 2025
    Beta strandi208 – 2136
    Helixi226 – 2283
    Helixi230 – 2345
    Turni235 – 2384
    Helixi245 – 26016
    Helixi263 – 28321
    Beta strandi288 – 2903
    Helixi295 – 2973
    Beta strandi300 – 30910
    Helixi314 – 32613
    Beta strandi329 – 3313
    Turni336 – 3383
    Beta strandi340 – 3445
    Helixi351 – 36818

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3E77X-ray2.50A/B/C17-370[»]
    ProteinModelPortaliQ9Y617.
    SMRiQ9Y617. Positions 17-370.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ9Y617.

    Family & Domainsi

    Region

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

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiCOG1932.
    HOGENOMiHOG000088965.
    HOVERGENiHBG001218.
    InParanoidiQ9Y617.
    KOiK00831.
    OMAiVFFGAQK.
    OrthoDBiEOG7KQ220.
    PhylomeDBiQ9Y617.
    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/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]
    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]

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q9Y617-1) [UniParc]FASTAAdd to Basket

    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.

    « Hide

    MDAPRQVVNF GPGPAKLPHS VLLEIQKELL DYKGVGISVL EMSHRSSDFA    50
    KIINNTENLV RELLAVPDNY KVIFLQGGGC GQFSAVPLNL IGLKAGRCAD 100
    YVVTGAWSAK AAEEAKKFGT INIVHPKLGS YTKIPDPSTW NLNPDASYVY 150
    YCANETVHGV EFDFIPDVKG AVLVCDMSSN FLSKPVDVSK FGVIFAGAQK 200
    NVGSAGVTVV IVRDDLLGFA LRECPSVLEY KVQAGNSSLY NTPPCFSIYV 250
    MGLVLEWIKN NGGAAAMEKL SSIKSQTIYE IIDNSQGFYV CPVEPQNRSK 300
    MNIPFRIGNA KGDDALEKRF LDKALELNML SLKGHRSVGG IRASLYNAVT 350
    IEDVQKLAAF MKKFLEMHQL 370
    Length:370
    Mass (Da):40,423
    Last modified:January 23, 2002 - v2
    Checksum:iBAF9A10E71B165B4
    GO
    Isoform 2 (identifier: Q9Y617-2) [UniParc]FASTAAdd to Basket

    Also known as: Beta

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

    Show »
    Length:324
    Mass (Da):35,189
    Checksum:i4F83811D3593DDA1
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti40 – 401L → V in AAH16645. (PubMed:15489334)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti87 – 871P → A.
    Corresponds to variant rs11540974 [ dbSNP | Ensembl ].
    VAR_048235
    Natural varianti100 – 1001D → A in PSATD; reduced Vmax. 1 Publication
    VAR_037252

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei291 – 33646Missing in isoform 2. 2 PublicationsVSP_000237Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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.
    CCDSiCCDS6659.1. [Q9Y617-2]
    CCDS6660.1. [Q9Y617-1]
    RefSeqiNP_066977.1. NM_021154.4. [Q9Y617-2]
    NP_478059.1. NM_058179.3. [Q9Y617-1]
    UniGeneiHs.494261.

    Genome annotation databases

    EnsembliENST00000347159; ENSP00000317606; ENSG00000135069. [Q9Y617-2]
    ENST00000376588; ENSP00000365773; ENSG00000135069. [Q9Y617-1]
    GeneIDi29968.
    KEGGihsa:29968.
    UCSCiuc004ala.3. human. [Q9Y617-1]
    uc004alb.3. human. [Q9Y617-2]

    Polymorphism databases

    DMDMi20141815.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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 .
    CCDSi CCDS6659.1. [Q9Y617-2 ]
    CCDS6660.1. [Q9Y617-1 ]
    RefSeqi NP_066977.1. NM_021154.4. [Q9Y617-2 ]
    NP_478059.1. NM_058179.3. [Q9Y617-1 ]
    UniGenei Hs.494261.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    3E77 X-ray 2.50 A/B/C 17-370 [» ]
    ProteinModelPortali Q9Y617.
    SMRi Q9Y617. Positions 17-370.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 119001. 24 interactions.
    IntActi Q9Y617. 3 interactions.
    MINTi MINT-1490243.
    STRINGi 9606.ENSP00000365773.

    PTM databases

    PhosphoSitei Q9Y617.

    Polymorphism databases

    DMDMi 20141815.

    2D gel databases

    REPRODUCTION-2DPAGE IPI00001734.

    Proteomic databases

    MaxQBi Q9Y617.
    PaxDbi Q9Y617.
    PeptideAtlasi Q9Y617.
    PRIDEi Q9Y617.

    Protocols and materials databases

    DNASUi 29968.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000347159 ; ENSP00000317606 ; ENSG00000135069 . [Q9Y617-2 ]
    ENST00000376588 ; ENSP00000365773 ; ENSG00000135069 . [Q9Y617-1 ]
    GeneIDi 29968.
    KEGGi hsa:29968.
    UCSCi uc004ala.3. human. [Q9Y617-1 ]
    uc004alb.3. human. [Q9Y617-2 ]

    Organism-specific databases

    CTDi 29968.
    GeneCardsi GC09P080911.
    HGNCi HGNC:19129. PSAT1.
    HPAi CAB014882.
    CAB040567.
    MIMi 610936. gene.
    610992. phenotype.
    neXtProti NX_Q9Y617.
    Orphaneti 284417. Phosphoserine aminotransferase deficiency.
    PharmGKBi PA128395782.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG1932.
    HOGENOMi HOG000088965.
    HOVERGENi HBG001218.
    InParanoidi Q9Y617.
    KOi K00831.
    OMAi VFFGAQK.
    OrthoDBi EOG7KQ220.
    PhylomeDBi Q9Y617.
    TreeFami TF312975.

    Enzyme and pathway databases

    UniPathwayi UPA00135 ; UER00197 .
    UPA00244 ; UER00311 .
    BioCyci MetaCyc:HS05946-MONOMER.
    Reactomei REACT_115789. Serine biosynthesis.

    Miscellaneous databases

    ChiTaRSi PSAT1. human.
    EvolutionaryTracei Q9Y617.
    GeneWikii PSAT1.
    GenomeRNAii 29968.
    NextBioi 52705.
    PROi Q9Y617.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9Y617.
    Bgeei Q9Y617.
    CleanExi HS_PSAT1.
    Genevestigatori Q9Y617.

    Family and domain databases

    Gene3Di 3.40.640.10. 1 hit.
    3.90.1150.10. 1 hit.
    HAMAPi MF_00160. SerC_aminotrans_5.
    InterProi 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.
    [Graphical view ]
    Pfami PF00266. Aminotran_5. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF000525. SerC. 1 hit.
    SUPFAMi SSF53383. SSF53383. 1 hit.
    TIGRFAMsi TIGR01364. serC_1. 1 hit.
    PROSITEi PS00595. AA_TRANSFER_CLASS_5. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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.
      , 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. 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. 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.

    Entry informationi

    Entry nameiSERC_HUMAN
    AccessioniPrimary (citable) accession number: Q9Y617
    Secondary accession number(s): Q5T7G5
    , Q5T7G6, Q96AW2, Q9BQ12
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 30, 2000
    Last sequence update: January 23, 2002
    Last modified: October 1, 2014
    This is version 152 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (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.

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 9
      Human chromosome 9: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    6. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    7. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3