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P51649

- SSDH_HUMAN

UniProt

P51649 - SSDH_HUMAN

Protein

Succinate-semialdehyde dehydrogenase, mitochondrial

Gene

ALDH5A1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 145 (01 Oct 2014)
      Sequence version 2 (30 May 2000)
      Previous versions | rss
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    Functioni

    Catalyzes one step in the degradation of the inhibitory neurotransmitter gamma-aminobutyric acid (GABA).1 Publication

    Catalytic activityi

    Succinate semialdehyde + NAD+ + H2O = succinate + NADH.

    Enzyme regulationi

    Redox-regulated. Inhibited under oxydizing conditions. Inhibited by hydrogen peroxide H2O2.1 Publication

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sitei205 – 2051Transition state stabilizerBy similarity
    Binding sitei213 – 2131NAD
    Binding sitei213 – 2131Substrate
    Active sitei306 – 3061Proton acceptorPROSITE-ProRule annotation
    Binding sitei334 – 3341Substrate
    Active sitei340 – 3401NucleophilePROSITE-ProRule annotation
    Binding sitei498 – 4981Substrate

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi228 – 2314NAD
    Nucleotide bindingi284 – 2896NAD

    GO - Molecular functioni

    1. protein homodimerization activity Source: UniProtKB
    2. succinate-semialdehyde dehydrogenase (NAD+) activity Source: UniProtKB
    3. succinate-semialdehyde dehydrogenase [NAD(P)+] activity Source: InterPro

    GO - Biological processi

    1. acetate metabolic process Source: UniProtKB
    2. central nervous system development Source: UniProtKB
    3. galactosylceramide metabolic process Source: UniProtKB
    4. gamma-aminobutyric acid catabolic process Source: UniProtKB
    5. glucose metabolic process Source: UniProtKB
    6. glucosylceramide metabolic process Source: Ensembl
    7. glutamate metabolic process Source: UniProtKB
    8. glutamine metabolic process Source: UniProtKB
    9. glutathione metabolic process Source: UniProtKB
    10. glycerophospholipid metabolic process Source: UniProtKB
    11. neurotransmitter catabolic process Source: UniProtKB
    12. neurotransmitter secretion Source: Reactome
    13. post-embryonic development Source: Ensembl
    14. protein homotetramerization Source: UniProtKB
    15. respiratory electron transport chain Source: UniProtKB
    16. short-chain fatty acid metabolic process Source: UniProtKB
    17. succinate metabolic process Source: UniProtKB
    18. synaptic transmission Source: Reactome

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Ligandi

    NAD

    Enzyme and pathway databases

    BioCyciMetaCyc:HS03550-MONOMER.
    BRENDAi1.2.1.24. 2681.
    ReactomeiREACT_23964. Degradation of GABA.
    SABIO-RKP51649.
    UniPathwayiUPA00733.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Succinate-semialdehyde dehydrogenase, mitochondrial (EC:1.2.1.24)
    Alternative name(s):
    Aldehyde dehydrogenase family 5 member A1
    NAD(+)-dependent succinic semialdehyde dehydrogenase
    Gene namesi
    Name:ALDH5A1
    Synonyms:SSADH
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 6

    Organism-specific databases

    HGNCiHGNC:408. ALDH5A1.

    Subcellular locationi

    GO - Cellular componenti

    1. mitochondrial matrix Source: Reactome
    2. mitochondrion Source: UniProtKB

    Keywords - Cellular componenti

    Mitochondrion

    Pathology & Biotechi

    Involvement in diseasei

    Succinic semialdehyde dehydrogenase deficiency (SSADHD) [MIM:271980]: A rare inborn error of 4-aminobutyric acid (GABA) metabolism, which leads to accumulation of 4-hydroxybutyric acid in physiologic fluids of patients. The disease is clinically characterized by developmental delay, hypotonia, mental retardation, ataxia, seizures, hyperkinetic behavior, aggression, and sleep disturbances.3 Publications
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti93 – 931C → F in SSADHD; 3% of activity. 1 Publication
    VAR_026199
    Natural varianti176 – 1761G → R in SSADHD; <1% of activity. 1 Publication
    VAR_026200
    Natural varianti223 – 2231C → Y in SSADHD; 5% of activity. 1 Publication
    VAR_026201
    Natural varianti233 – 2331T → M in SSADHD; 4% of activity. 1 Publication
    VAR_026202
    Natural varianti255 – 2551N → S in SSADHD; 17% of activity. 1 Publication
    VAR_026203
    Natural varianti268 – 2681G → E in SSADHD; <1% of activity. 2 Publications
    VAR_026204
    Natural varianti335 – 3351N → K in SSADHD; 1% of activity. 1 Publication
    VAR_026205
    Natural varianti382 – 3821P → L in SSADHD; 2% of activity. 1 Publication
    VAR_026206
    Natural varianti382 – 3821P → Q in SSADHD. 1 Publication
    VAR_026207
    Natural varianti409 – 4091G → D in SSADHD; <1% of activity. 2 Publications
    VAR_026208
    Natural varianti487 – 4871V → E in SSADHD. 1 Publication
    VAR_026209
    Natural varianti533 – 5331G → R in SSADHD; <1% of activity. 1 Publication
    VAR_026210

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi213 – 2131R → A: Reduces catalytic activity to less than 15% of wild-type. 1 Publication
    Mutagenesisi334 – 3341R → A: Reduces catalytic activity to less than 15% of wild-type. 1 Publication
    Mutagenesisi342 – 3421C → A: Loss of regulation by redox state. 1 Publication
    Mutagenesisi498 – 4981S → A: Reduces catalytic activity to less than 15% of wild-type. 1 Publication

    Keywords - Diseasei

    Disease mutation

    Organism-specific databases

    MIMi271980. phenotype.
    Orphaneti22. 4-hydroxybutyric aciduria.
    PharmGKBiPA24702.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transit peptidei1 – 4747MitochondrionSequence AnalysisAdd
    BLAST
    Chaini48 – 535488Succinate-semialdehyde dehydrogenase, mitochondrialPRO_0000007184Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei126 – 1261N6-acetyllysine; alternate1 Publication
    Modified residuei126 – 1261N6-succinyllysine; alternateBy similarity
    Modified residuei135 – 1351N6-succinyllysineBy similarity
    Modified residuei184 – 1841N6-succinyllysineBy similarity
    Modified residuei265 – 2651N6-acetyllysine; alternateBy similarity
    Modified residuei265 – 2651N6-succinyllysine; alternateBy similarity
    Disulfide bondi340 ↔ 342In inhibited form1 Publication
    Modified residuei365 – 3651N6-acetyllysineBy similarity
    Modified residuei402 – 4021N6-succinyllysineBy similarity
    Modified residuei411 – 4111N6-acetyllysineBy similarity

    Keywords - PTMi

    Acetylation, Disulfide bond

    Proteomic databases

    MaxQBiP51649.
    PaxDbiP51649.
    PRIDEiP51649.

    PTM databases

    PhosphoSiteiP51649.

    Expressioni

    Tissue specificityi

    Brain, pancreas, heart, liver, skeletal muscle and kidney. Lower in placenta.

    Gene expression databases

    ArrayExpressiP51649.
    BgeeiP51649.
    CleanExiHS_ALDH5A1.
    GenevestigatoriP51649.

    Organism-specific databases

    HPAiHPA029715.
    HPA029716.

    Interactioni

    Subunit structurei

    Homotetramer.2 Publications

    Protein-protein interaction databases

    BioGridi113645. 6 interactions.
    IntActiP51649. 1 interaction.
    MINTiMINT-6950845.
    STRINGi9606.ENSP00000314649.

    Structurei

    Secondary structure

    1
    535
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Turni56 – 583
    Beta strandi62 – 654
    Beta strandi68 – 703
    Beta strandi75 – 795
    Turni81 – 833
    Beta strandi86 – 916
    Helixi95 – 11218
    Helixi117 – 13317
    Helixi135 – 14612
    Helixi150 – 17021
    Helixi171 – 1733
    Beta strandi177 – 1793
    Beta strandi187 – 1948
    Beta strandi197 – 2015
    Beta strandi204 – 2063
    Helixi209 – 22113
    Beta strandi224 – 2285
    Helixi235 – 24713
    Beta strandi253 – 2564
    Helixi261 – 27111
    Beta strandi277 – 2848
    Helixi286 – 29712
    Turni298 – 3003
    Beta strandi302 – 3076
    Beta strandi309 – 3157
    Beta strandi317 – 3193
    Helixi321 – 33212
    Helixi334 – 3374
    Beta strandi341 – 3499
    Helixi350 – 36718
    Beta strandi373 – 3753
    Helixi386 – 40015
    Turni401 – 4033
    Beta strandi405 – 4084
    Beta strandi423 – 4286
    Helixi430 – 4334
    Beta strandi441 – 45010
    Helixi452 – 4598
    Beta strandi466 – 4716
    Helixi475 – 48410
    Beta strandi487 – 4937
    Helixi508 – 5103
    Beta strandi511 – 5133
    Turni517 – 5193
    Helixi520 – 5245
    Beta strandi525 – 5328

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2W8NX-ray2.00A49-535[»]
    2W8OX-ray3.40A49-535[»]
    2W8PX-ray2.30A49-535[»]
    2W8QX-ray2.40A49-535[»]
    2W8RX-ray2.40A49-535[»]
    ProteinModelPortaliP51649.
    SMRiP51649. Positions 56-535.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP51649.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the aldehyde dehydrogenase family.Curated

    Keywords - Domaini

    Transit peptide

    Phylogenomic databases

    eggNOGiCOG1012.
    HOGENOMiHOG000271509.
    HOVERGENiHBG108515.
    KOiK00139.
    OMAiGPLINEM.
    OrthoDBiEOG72G173.
    PhylomeDBiP51649.
    TreeFamiTF352906.

    Family and domain databases

    Gene3Di3.40.309.10. 1 hit.
    3.40.605.10. 1 hit.
    InterProiIPR016161. Ald_DH/histidinol_DH.
    IPR016163. Ald_DH_C.
    IPR016160. Ald_DH_CS_CYS.
    IPR029510. Ald_DH_CS_GLU.
    IPR016162. Ald_DH_N.
    IPR015590. Aldehyde_DH_dom.
    IPR010102. Succ_semiAld_DH.
    [Graphical view]
    PfamiPF00171. Aldedh. 1 hit.
    [Graphical view]
    SUPFAMiSSF53720. SSF53720. 1 hit.
    TIGRFAMsiTIGR01780. SSADH. 1 hit.
    PROSITEiPS00070. ALDEHYDE_DEHYDR_CYS. 1 hit.
    PS00687. ALDEHYDE_DEHYDR_GLU. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: P51649-1) [UniParc]FASTAAdd to Basket

    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

    MATCIWLRSC GARRLGSTFP GCRLRPRAGG LVPASGPAPG PAQLRCYAGR    50
    LAGLSAALLR TDSFVGGRWL PAAATFPVQD PASGAALGMV ADCGVREARA 100
    AVRAAYEAFC RWREVSAKER SSLLRKWYNL MIQNKDDLAR IITAESGKPL 150
    KEAHGEILYS AFFLEWFSEE ARRVYGDIIH TPAKDRRALV LKQPIGVAAV 200
    ITPWNFPSAM ITRKVGAALA AGCTVVVKPA EDTPFSALAL AELASQAGIP 250
    SGVYNVIPCS RKNAKEVGEA ICTDPLVSKI SFTGSTTTGK ILLHHAANSV 300
    KRVSMELGGL APFIVFDSAN VDQAVAGAMA SKFRNTGQTC VCSNQFLVQR 350
    GIHDAFVKAF AEAMKKNLRV GNGFEEGTTQ GPLINEKAVE KVEKQVNDAV 400
    SKGATVVTGG KRHQLGKNFF EPTLLCNVTQ DMLCTHEETF GPLAPVIKFD 450
    TEEEAIAIAN AADVGLAGYF YSQDPAQIWR VAEQLEVGMV GVNEGLISSV 500
    ECPFGGVKQS GLGREGSKYG IDEYLELKYV CYGGL 535
    Length:535
    Mass (Da):57,215
    Last modified:May 30, 2000 - v2
    Checksum:iC63A9431D3FA16C7
    GO
    Isoform 2 (identifier: P51649-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         242-242: E → EVNQGFLLDLDPLL

    Show »
    Length:548
    Mass (Da):58,653
    Checksum:i98C7673CBBF74FC8
    GO

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti36 – 361G → R.1 Publication
    Corresponds to variant rs4646832 [ dbSNP | Ensembl ].
    VAR_026227
    Natural varianti93 – 931C → F in SSADHD; 3% of activity. 1 Publication
    VAR_026199
    Natural varianti176 – 1761G → R in SSADHD; <1% of activity. 1 Publication
    VAR_026200
    Natural varianti180 – 1801H → Y 83% of activity. 2 Publications
    Corresponds to variant rs2760118 [ dbSNP | Ensembl ].
    VAR_016758
    Natural varianti182 – 1821P → L 48% of activity. 1 Publication
    Corresponds to variant rs3765310 [ dbSNP | Ensembl ].
    VAR_016759
    Natural varianti223 – 2231C → Y in SSADHD; 5% of activity. 1 Publication
    VAR_026201
    Natural varianti233 – 2331T → M in SSADHD; 4% of activity. 1 Publication
    VAR_026202
    Natural varianti237 – 2371A → S 65% of activity. 1 Publication
    Corresponds to variant rs62621664 [ dbSNP | Ensembl ].
    VAR_026228
    Natural varianti255 – 2551N → S in SSADHD; 17% of activity. 1 Publication
    VAR_026203
    Natural varianti268 – 2681G → E in SSADHD; <1% of activity. 2 Publications
    VAR_026204
    Natural varianti335 – 3351N → K in SSADHD; 1% of activity. 1 Publication
    VAR_026205
    Natural varianti372 – 3721N → S.1 Publication
    VAR_069047
    Natural varianti382 – 3821P → L in SSADHD; 2% of activity. 1 Publication
    VAR_026206
    Natural varianti382 – 3821P → Q in SSADHD. 1 Publication
    VAR_026207
    Natural varianti406 – 4061V → I.1 Publication
    VAR_026229
    Natural varianti409 – 4091G → D in SSADHD; <1% of activity. 2 Publications
    VAR_026208
    Natural varianti487 – 4871V → E in SSADHD. 1 Publication
    VAR_026209
    Natural varianti533 – 5331G → R in SSADHD; <1% of activity. 1 Publication
    VAR_026210

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei242 – 2421E → EVNQGFLLDLDPLL in isoform 2. 1 PublicationVSP_045231

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Y11192 mRNA. Translation: CAA72076.1.
    AJ427354 mRNA. Translation: CAD20883.2.
    AJ427355 mRNA. Translation: CAD20884.1.
    AK315380 mRNA. Translation: BAG37773.1.
    AL031230 Genomic DNA. Translation: CAA20248.1.
    CH471087 Genomic DNA. Translation: EAW55452.1.
    CH471087 Genomic DNA. Translation: EAW55453.1.
    BC034321 mRNA. Translation: AAH34321.1.
    L34820 mRNA. Translation: AAA67057.1.
    CCDSiCCDS4555.1. [P51649-1]
    CCDS4556.1. [P51649-2]
    PIRiA55773.
    RefSeqiNP_001071.1. NM_001080.3. [P51649-1]
    NP_733936.1. NM_170740.1. [P51649-2]
    UniGeneiHs.371723.

    Genome annotation databases

    EnsembliENST00000348925; ENSP00000314649; ENSG00000112294. [P51649-2]
    ENST00000357578; ENSP00000350191; ENSG00000112294. [P51649-1]
    GeneIDi7915.
    KEGGihsa:7915.
    UCSCiuc003nef.3. human.
    uc003neg.3. human. [P51649-1]

    Polymorphism databases

    DMDMi7531278.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Y11192 mRNA. Translation: CAA72076.1 .
    AJ427354 mRNA. Translation: CAD20883.2 .
    AJ427355 mRNA. Translation: CAD20884.1 .
    AK315380 mRNA. Translation: BAG37773.1 .
    AL031230 Genomic DNA. Translation: CAA20248.1 .
    CH471087 Genomic DNA. Translation: EAW55452.1 .
    CH471087 Genomic DNA. Translation: EAW55453.1 .
    BC034321 mRNA. Translation: AAH34321.1 .
    L34820 mRNA. Translation: AAA67057.1 .
    CCDSi CCDS4555.1. [P51649-1 ]
    CCDS4556.1. [P51649-2 ]
    PIRi A55773.
    RefSeqi NP_001071.1. NM_001080.3. [P51649-1 ]
    NP_733936.1. NM_170740.1. [P51649-2 ]
    UniGenei Hs.371723.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2W8N X-ray 2.00 A 49-535 [» ]
    2W8O X-ray 3.40 A 49-535 [» ]
    2W8P X-ray 2.30 A 49-535 [» ]
    2W8Q X-ray 2.40 A 49-535 [» ]
    2W8R X-ray 2.40 A 49-535 [» ]
    ProteinModelPortali P51649.
    SMRi P51649. Positions 56-535.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 113645. 6 interactions.
    IntActi P51649. 1 interaction.
    MINTi MINT-6950845.
    STRINGi 9606.ENSP00000314649.

    Chemistry

    BindingDBi P51649.
    ChEMBLi CHEMBL1911.
    DrugBanki DB00534. Chlormerodrin.
    DB00157. NADH.
    DB00139. Succinic acid.

    PTM databases

    PhosphoSitei P51649.

    Polymorphism databases

    DMDMi 7531278.

    Proteomic databases

    MaxQBi P51649.
    PaxDbi P51649.
    PRIDEi P51649.

    Protocols and materials databases

    DNASUi 7915.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000348925 ; ENSP00000314649 ; ENSG00000112294 . [P51649-2 ]
    ENST00000357578 ; ENSP00000350191 ; ENSG00000112294 . [P51649-1 ]
    GeneIDi 7915.
    KEGGi hsa:7915.
    UCSCi uc003nef.3. human.
    uc003neg.3. human. [P51649-1 ]

    Organism-specific databases

    CTDi 7915.
    GeneCardsi GC06P024444.
    GeneReviewsi ALDH5A1.
    HGNCi HGNC:408. ALDH5A1.
    HPAi HPA029715.
    HPA029716.
    MIMi 271980. phenotype.
    610045. gene.
    neXtProti NX_P51649.
    Orphaneti 22. 4-hydroxybutyric aciduria.
    PharmGKBi PA24702.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG1012.
    HOGENOMi HOG000271509.
    HOVERGENi HBG108515.
    KOi K00139.
    OMAi GPLINEM.
    OrthoDBi EOG72G173.
    PhylomeDBi P51649.
    TreeFami TF352906.

    Enzyme and pathway databases

    UniPathwayi UPA00733 .
    BioCyci MetaCyc:HS03550-MONOMER.
    BRENDAi 1.2.1.24. 2681.
    Reactomei REACT_23964. Degradation of GABA.
    SABIO-RK P51649.

    Miscellaneous databases

    EvolutionaryTracei P51649.
    GeneWikii Aldehyde_dehydrogenase_5_family,_member_A1.
    GenomeRNAii 7915.
    NextBioi 30381.
    PROi P51649.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P51649.
    Bgeei P51649.
    CleanExi HS_ALDH5A1.
    Genevestigatori P51649.

    Family and domain databases

    Gene3Di 3.40.309.10. 1 hit.
    3.40.605.10. 1 hit.
    InterProi IPR016161. Ald_DH/histidinol_DH.
    IPR016163. Ald_DH_C.
    IPR016160. Ald_DH_CS_CYS.
    IPR029510. Ald_DH_CS_GLU.
    IPR016162. Ald_DH_N.
    IPR015590. Aldehyde_DH_dom.
    IPR010102. Succ_semiAld_DH.
    [Graphical view ]
    Pfami PF00171. Aldedh. 1 hit.
    [Graphical view ]
    SUPFAMi SSF53720. SSF53720. 1 hit.
    TIGRFAMsi TIGR01780. SSADH. 1 hit.
    PROSITEi PS00070. ALDEHYDE_DEHYDR_CYS. 1 hit.
    PS00687. ALDEHYDE_DEHYDR_GLU. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Two exon-skipping mutations as the molecular basis of succinic semialdehyde dehydrogenase deficiency (4-hydroxybutyric aciduria)."
      Chambliss K.L., Hinson D.D., Trettel F., Malaspina P., Novelletto A., Jakobs C., Gibson K.M.
      Am. J. Hum. Genet. 63:399-408(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
      Tissue: Lymphocyte.
    2. "Structure of human succinic semialdehyde dehydrogenase gene: identification of promoter region and alternatively processed isoforms."
      Blasi P., Boyl P.P., Ledda M., Novelletto A., Gibson K.M., Jakobs C., Hogema B., Akaboshi S., Loreni F., Malaspina P.
      Mol. Genet. Metab. 76:348-362(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), NUCLEOTIDE SEQUENCE [MRNA] OF 69-535 (ISOFORM 2), ALTERNATIVE SPLICING, VARIANT SER-372.
      Tissue: B-cell.
    3. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), VARIANT TYR-180.
      Tissue: Brain.
    4. "The DNA sequence and analysis of human chromosome 6."
      Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D.
      , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.
      Nature 425:805-811(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    6. "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] (ISOFORM 1).
      Tissue: Testis.
    7. "Molecular cloning of the mature NAD(+)-dependent succinic semialdehyde dehydrogenase from rat and human. cDNA isolation, evolutionary homology, and tissue expression."
      Chambliss K.L., Caudle D.L., Hinson D.D., Moomaw C.R., Slaughter C.A., Jakobs C., Gibson K.M.
      J. Biol. Chem. 270:461-467(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 213-535 (ISOFORM 1).
      Tissue: Liver.
    8. "Human succinic semialdehyde dehydrogenase. Molecular cloning and chromosomal localization."
      Trettel F., Malaspina P., Jodice C., Novelletto A., Slaughter C.A., Caudle D.L., Hinson D.D., Chambliss K.L., Gibson K.M.
      Adv. Exp. Med. Biol. 414:253-260(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBUNIT.
      Tissue: Brain.
    9. "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-126, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    10. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    11. "Redox-switch modulation of human SSADH by dynamic catalytic loop."
      Kim Y.-G., Lee S., Kwon O.-S., Park S.-Y., Lee S.-J., Park B.-J., Kim K.-J.
      EMBO J. 28:959-968(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 49-535 IN COMPLEX WITH PRODUCT AND ADP, FUNCTION, ENZYME REGULATION, DISULFIDE BOND, MUTAGENESIS OF ARG-213; ARG-334; CYS-342 AND SER-498.
    12. "Prenatal diagnosis of succinic semialdehyde dehydrogenase deficiency: increased accuracy employing DNA, enzyme, and metabolite analyses."
      Hogema B.M., Akaboshi S., Taylor M., Salomons G.S., Jakobs C., Schutgens R.B., Wilcken B., Worthington S., Maropoulos G., Grompe M., Gibson K.M.
      Mol. Genet. Metab. 72:218-222(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS SSADHD GLU-268 AND ASP-409.
    13. "Mutation analysis in a patient with succinic semialdehyde dehydrogenase deficiency: a compound heterozygote with 103-121del and 1460T>A of the ALDH5A1 gene."
      Aoshima T., Kajita M., Sekido Y., Ishiguro Y., Tsuge I., Kimura M., Yamaguchi S., Watanabe K., Shimokata K., Niwa T.
      Hum. Hered. 53:42-44(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT SSADHD GLU-487.
    14. "Mutational spectrum of the succinate semialdehyde dehydrogenase (ALDH5A1) gene and functional analysis of 27 novel disease-causing mutations in patients with SSADH deficiency."
      Akaboshi S., Hogema B.M., Novelletto A., Malaspina P., Salomons G.S., Maropoulos G.D., Jakobs C., Grompe M., Gibson K.M.
      Hum. Mutat. 22:442-450(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS SSADHD PHE-93; ARG-176; TYR-223; MET-233; SER-255; GLU-268; LYS-335; GLN-382; LEU-382; ASP-409 AND ARG-533, VARIANTS ARG-36; TYR-180; LEU-182; SER-237 AND ILE-406, CHARACTERIZATION OF VARIANTS ARG-36; PHE-93; ARG-176; TYR-180; LEU-182; TYR-223; MET-233; SER-237; SER-255; GLU-268; LYS-335; LEU-382; ASP-409 AND ARG-533.

    Entry informationi

    Entry nameiSSDH_HUMAN
    AccessioniPrimary (citable) accession number: P51649
    Secondary accession number(s): B2RD26
    , G5E949, Q546H9, Q8N3W6
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1996
    Last sequence update: May 30, 2000
    Last modified: October 1, 2014
    This is version 145 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 6
      Human chromosome 6: 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