Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Q96GA7

- SDSL_HUMAN

UniProt

Q96GA7 - SDSL_HUMAN

Protein

Serine dehydratase-like

Gene

SDSL

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 97 (01 Oct 2014)
      Sequence version 1 (01 Dec 2001)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

    Has low serine dehydratase and threonine dehydratase activity.

    Catalytic activityi

    L-serine = pyruvate + NH3.1 Publication
    L-threonine = 2-oxobutanoate + NH3.1 Publication

    Cofactori

    Pyridoxal phosphate.

    Kineticsi

    1. KM=30 mM for serine
    2. KM=7 mM for threonine

    GO - Molecular functioni

    1. L-serine ammonia-lyase activity Source: UniProtKB-EC
    2. L-threonine ammonia-lyase activity Source: UniProtKB-EC
    3. pyridoxal phosphate binding Source: InterPro

    GO - Biological processi

    1. cellular amino acid metabolic process Source: InterPro

    Keywords - Molecular functioni

    Lyase

    Keywords - Ligandi

    Pyridoxal phosphate

    Enzyme and pathway databases

    BioCyciMetaCyc:HS06616-MONOMER.
    SABIO-RKQ96GA7.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Serine dehydratase-like
    Alternative name(s):
    L-serine deaminase
    L-serine dehydratase/L-threonine deaminase
    L-threonine dehydratase (EC:4.3.1.19)
    Short name:
    TDH
    Serine dehydratase 2 (EC:4.3.1.17)
    Short name:
    SDH 2
    Gene namesi
    Name:SDSL
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 12

    Organism-specific databases

    HGNCiHGNC:30404. SDSL.

    Subcellular locationi

    GO - Cellular componenti

    1. extracellular vesicular exosome Source: UniProt
    2. mitochondrion Source: Ensembl

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi72 – 721G → A: Strongly increased enzyme activity towards threonine. 1 Publication
    Mutagenesisi309 – 3091C → A: Loss of enzyme activity. 1 Publication

    Organism-specific databases

    PharmGKBiPA134862016.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 329329Serine dehydratase-likePRO_0000264624Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei1 – 11N-acetylmethionine1 Publication
    Modified residuei48 – 481N6-(pyridoxal phosphate)lysine

    Keywords - PTMi

    Acetylation

    Proteomic databases

    MaxQBiQ96GA7.
    PaxDbiQ96GA7.
    PRIDEiQ96GA7.

    PTM databases

    PhosphoSiteiQ96GA7.

    Expressioni

    Gene expression databases

    ArrayExpressiQ96GA7.
    BgeeiQ96GA7.
    CleanExiHS_SDSL.
    GenevestigatoriQ96GA7.

    Organism-specific databases

    HPAiHPA005740.

    Interactioni

    Subunit structurei

    Homodimer.1 Publication

    Protein-protein interaction databases

    BioGridi125255. 3 interactions.
    IntActiQ96GA7. 2 interactions.
    MINTiMINT-1456379.
    STRINGi9606.ENSP00000341117.

    Structurei

    Secondary structure

    1
    329
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi20 – 234
    Helixi24 – 307
    Beta strandi34 – 385
    Helixi39 – 413
    Helixi49 – 6113
    Beta strandi66 – 694
    Helixi74 – 8512
    Beta strandi90 – 945
    Helixi100 – 1089
    Beta strandi112 – 1154
    Helixi120 – 13213
    Beta strandi136 – 1383
    Helixi145 – 16117
    Beta strandi162 – 1643
    Beta strandi167 – 1726
    Beta strandi174 – 1763
    Helixi177 – 18913
    Beta strandi196 – 2016
    Helixi206 – 2138
    Helixi227 – 2293
    Helixi236 – 2449
    Beta strandi247 – 2526
    Helixi254 – 26815
    Helixi274 – 28411
    Helixi287 – 2937
    Beta strandi304 – 3085
    Helixi316 – 32510

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2RKBX-ray2.80A/B/C/D/E11-328[»]
    ProteinModelPortaliQ96GA7.
    SMRiQ96GA7. Positions 11-328.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ96GA7.

    Family & Domainsi

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiCOG1171.
    HOGENOMiHOG000046976.
    HOVERGENiHBG017784.
    InParanoidiQ96GA7.
    KOiK17989.
    OMAiETHGAHC.
    OrthoDBiEOG7VDXQ1.
    PhylomeDBiQ96GA7.
    TreeFamiTF329014.

    Family and domain databases

    InterProiIPR000634. Ser/Thr_deHydtase_PyrdxlP-BS.
    IPR001926. Trp_syn_b_sub_like_PLP_eny_SF.
    [Graphical view]
    PfamiPF00291. PALP. 1 hit.
    [Graphical view]
    SUPFAMiSSF53686. SSF53686. 1 hit.
    PROSITEiPS00165. DEHYDRATASE_SER_THR. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q96GA7-1 [UniParc]FASTAAdd to Basket

    « Hide

    MDGPVAEHAK QEPFHVVTPL LESWALSQVA GMPVFLKCEN VQPSGSFKIR    50
    GIGHFCQEMA KKGCRHLVCS SGGNAGIAAA YAARKLGIPA TIVLPESTSL 100
    QVVQRLQGEG AEVQLTGKVW DEANLRAQEL AKRDGWENVP PFDHPLIWKG 150
    HASLVQELKA VLRTPPGALV LAVGGGGLLA GVVAGLLEVG WQHVPIIAME 200
    THGAHCFNAA ITAGKLVTLP DITSVAKSLG AKTVAARALE CMQVCKIHSE 250
    VVEDTEAVSA VQQLLDDERM LVEPACGAAL AAIYSGLLRR LQAEGCLPPS 300
    LTSVVVIVCG GNNINSRELQ ALKTHLGQV 329
    Length:329
    Mass (Da):34,674
    Last modified:December 1, 2001 - v1
    Checksum:iCEAD30E570A43B7E
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF134473 mRNA. Translation: AAP97250.1.
    BC009849 mRNA. Translation: AAH09849.1.
    BC091479 mRNA. Translation: AAH91479.1.
    CCDSiCCDS9170.1.
    RefSeqiNP_612441.1. NM_138432.2.
    XP_005253887.1. XM_005253830.2.
    XP_005253888.1. XM_005253831.2.
    UniGeneiHs.337594.

    Genome annotation databases

    EnsembliENST00000345635; ENSP00000341117; ENSG00000139410.
    ENST00000403593; ENSP00000385790; ENSG00000139410.
    GeneIDi113675.
    KEGGihsa:113675.
    UCSCiuc001tvi.3. human.

    Polymorphism databases

    DMDMi74731799.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF134473 mRNA. Translation: AAP97250.1 .
    BC009849 mRNA. Translation: AAH09849.1 .
    BC091479 mRNA. Translation: AAH91479.1 .
    CCDSi CCDS9170.1.
    RefSeqi NP_612441.1. NM_138432.2.
    XP_005253887.1. XM_005253830.2.
    XP_005253888.1. XM_005253831.2.
    UniGenei Hs.337594.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2RKB X-ray 2.80 A/B/C/D/E 11-328 [» ]
    ProteinModelPortali Q96GA7.
    SMRi Q96GA7. Positions 11-328.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 125255. 3 interactions.
    IntActi Q96GA7. 2 interactions.
    MINTi MINT-1456379.
    STRINGi 9606.ENSP00000341117.

    Chemistry

    DrugBanki DB00114. Pyridoxal Phosphate.

    PTM databases

    PhosphoSitei Q96GA7.

    Polymorphism databases

    DMDMi 74731799.

    Proteomic databases

    MaxQBi Q96GA7.
    PaxDbi Q96GA7.
    PRIDEi Q96GA7.

    Protocols and materials databases

    DNASUi 113675.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000345635 ; ENSP00000341117 ; ENSG00000139410 .
    ENST00000403593 ; ENSP00000385790 ; ENSG00000139410 .
    GeneIDi 113675.
    KEGGi hsa:113675.
    UCSCi uc001tvi.3. human.

    Organism-specific databases

    CTDi 113675.
    GeneCardsi GC12P113860.
    HGNCi HGNC:30404. SDSL.
    HPAi HPA005740.
    neXtProti NX_Q96GA7.
    PharmGKBi PA134862016.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG1171.
    HOGENOMi HOG000046976.
    HOVERGENi HBG017784.
    InParanoidi Q96GA7.
    KOi K17989.
    OMAi ETHGAHC.
    OrthoDBi EOG7VDXQ1.
    PhylomeDBi Q96GA7.
    TreeFami TF329014.

    Enzyme and pathway databases

    BioCyci MetaCyc:HS06616-MONOMER.
    SABIO-RK Q96GA7.

    Miscellaneous databases

    ChiTaRSi SDSL. human.
    EvolutionaryTracei Q96GA7.
    GenomeRNAii 113675.
    NextBioi 78888.
    PROi Q96GA7.

    Gene expression databases

    ArrayExpressi Q96GA7.
    Bgeei Q96GA7.
    CleanExi HS_SDSL.
    Genevestigatori Q96GA7.

    Family and domain databases

    InterProi IPR000634. Ser/Thr_deHydtase_PyrdxlP-BS.
    IPR001926. Trp_syn_b_sub_like_PLP_eny_SF.
    [Graphical view ]
    Pfami PF00291. PALP. 1 hit.
    [Graphical view ]
    SUPFAMi SSF53686. SSF53686. 1 hit.
    PROSITEi PS00165. DEHYDRATASE_SER_THR. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Cloning of a new human cDNA homologous to Homo sapiens serine dehydratase."
      Gong R.M., Yu L., Zhao S.Y.
      Submitted (MAR-1999) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    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].
      Tissue: Lung and Placenta.
    3. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    4. "Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
      Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
      Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    5. "A catalytic mechanism that explains a low catalytic activity of serine dehydratase like-1 from human cancer cells: crystal structure and site-directed mutagenesis studies."
      Yamada T., Komoto J., Kasuya T., Takata Y., Ogawa H., Mori H., Takusagawa F.
      Biochim. Biophys. Acta 1780:809-818(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 11-328 IN COMPLEX WITH PYRIDOXAL PHOSPHATE, CATALYTIC ACTIVITY, SUBUNIT, MUTAGENESIS OF GLY-72 AND CYS-309.

    Entry informationi

    Entry nameiSDSL_HUMAN
    AccessioniPrimary (citable) accession number: Q96GA7
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 12, 2006
    Last sequence update: December 1, 2001
    Last modified: October 1, 2014
    This is version 97 of the entry and version 1 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 12
      Human chromosome 12: entries, gene names and cross-references to MIM
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3