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P51649 (SSDH_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 143. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (7) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:ALDH5A1
Synonyms:SSADH
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length535 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Catalyzes one step in the degradation of the inhibitory neurotransmitter gamma-aminobutyric acid (GABA). Ref.11

Catalytic activity

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

Enzyme regulation

Redox-regulated. Inhibited under oxydizing conditions. Inhibited by hydrogen peroxide H2O2. Ref.11

Pathway

Amino-acid degradation; 4-aminobutanoate degradation.

Subunit structure

Homotetramer. Ref.8

Subcellular location

Mitochondrion.

Tissue specificity

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

Involvement in disease

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.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.12 Ref.13 Ref.14

Sequence similarities

Belongs to the aldehyde dehydrogenase family.

Ontologies

Keywords
   Cellular componentMitochondrion
   Coding sequence diversityAlternative splicing
Polymorphism
   DiseaseDisease mutation
   DomainTransit peptide
   LigandNAD
   Molecular functionOxidoreductase
   PTMAcetylation
Disulfide bond
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processacetate metabolic process

Inferred from sequence or structural similarity. Source: UniProtKB

central nervous system development

Inferred from mutant phenotype Ref.1. Source: UniProtKB

galactosylceramide metabolic process

Inferred from sequence or structural similarity. Source: UniProtKB

gamma-aminobutyric acid catabolic process

Inferred from direct assay Ref.1. Source: UniProtKB

glucose metabolic process

Inferred from sequence or structural similarity. Source: UniProtKB

glucosylceramide metabolic process

Inferred from electronic annotation. Source: Ensembl

glutamate metabolic process

Inferred from sequence or structural similarity. Source: UniProtKB

glutamine metabolic process

Inferred from sequence or structural similarity. Source: UniProtKB

glutathione metabolic process

Inferred from sequence or structural similarity. Source: UniProtKB

glycerophospholipid metabolic process

Inferred from sequence or structural similarity. Source: UniProtKB

neurotransmitter catabolic process

Inferred from sequence or structural similarity. Source: UniProtKB

neurotransmitter secretion

Traceable author statement. Source: Reactome

post-embryonic development

Inferred from electronic annotation. Source: Ensembl

protein homotetramerization

Inferred from direct assay PubMed 16199352. Source: UniProtKB

respiratory electron transport chain

Inferred from sequence or structural similarity. Source: UniProtKB

short-chain fatty acid metabolic process

Inferred from sequence or structural similarity. Source: UniProtKB

succinate metabolic process

Inferred from sequence or structural similarity. Source: UniProtKB

synaptic transmission

Traceable author statement. Source: Reactome

   Cellular_componentmitochondrial matrix

Traceable author statement. Source: Reactome

mitochondrion

Inferred from sequence or structural similarity. Source: UniProtKB

   Molecular_functionprotein homodimerization activity

Inferred by curator PubMed 16199352. Source: UniProtKB

succinate-semialdehyde dehydrogenase (NAD+) activity

Inferred from direct assay Ref.1. Source: UniProtKB

succinate-semialdehyde dehydrogenase [NAD(P)+] activity

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: P51649-1)

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: P51649-2)

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 4747Mitochondrion Potential
Chain48 – 535488Succinate-semialdehyde dehydrogenase, mitochondrial
PRO_0000007184

Regions

Nucleotide binding228 – 2314NAD
Nucleotide binding284 – 2896NAD

Sites

Active site3061Proton acceptor By similarity
Active site3401Nucleophile By similarity
Binding site2131NAD
Binding site2131Substrate
Binding site3341Substrate
Binding site4981Substrate
Site2051Transition state stabilizer By similarity

Amino acid modifications

Modified residue1261N6-acetyllysine; alternate Ref.9
Modified residue1261N6-succinyllysine; alternate By similarity
Modified residue1351N6-succinyllysine By similarity
Modified residue1841N6-succinyllysine By similarity
Modified residue2651N6-acetyllysine; alternate By similarity
Modified residue2651N6-succinyllysine; alternate By similarity
Modified residue3651N6-acetyllysine By similarity
Modified residue4021N6-succinyllysine By similarity
Modified residue4111N6-acetyllysine By similarity
Disulfide bond340 ↔ 342In inhibited form Ref.11

Natural variations

Alternative sequence2421E → EVNQGFLLDLDPLL in isoform 2.
VSP_045231
Natural variant361G → R. Ref.14
Corresponds to variant rs4646832 [ dbSNP | Ensembl ].
VAR_026227
Natural variant931C → F in SSADHD; 3% of activity. Ref.14
VAR_026199
Natural variant1761G → R in SSADHD; <1% of activity. Ref.14
VAR_026200
Natural variant1801H → Y 83% of activity. Ref.3 Ref.14
Corresponds to variant rs2760118 [ dbSNP | Ensembl ].
VAR_016758
Natural variant1821P → L 48% of activity. Ref.14
Corresponds to variant rs3765310 [ dbSNP | Ensembl ].
VAR_016759
Natural variant2231C → Y in SSADHD; 5% of activity. Ref.14
VAR_026201
Natural variant2331T → M in SSADHD; 4% of activity. Ref.14
VAR_026202
Natural variant2371A → S 65% of activity. Ref.14
Corresponds to variant rs62621664 [ dbSNP | Ensembl ].
VAR_026228
Natural variant2551N → S in SSADHD; 17% of activity. Ref.14
VAR_026203
Natural variant2681G → E in SSADHD; <1% of activity. Ref.12 Ref.14
VAR_026204
Natural variant3351N → K in SSADHD; 1% of activity. Ref.14
VAR_026205
Natural variant3721N → S. Ref.2
VAR_069047
Natural variant3821P → L in SSADHD; 2% of activity. Ref.14
VAR_026206
Natural variant3821P → Q in SSADHD. Ref.14
VAR_026207
Natural variant4061V → I. Ref.14
VAR_026229
Natural variant4091G → D in SSADHD; <1% of activity. Ref.12 Ref.14
VAR_026208
Natural variant4871V → E in SSADHD. Ref.13
VAR_026209
Natural variant5331G → R in SSADHD; <1% of activity. Ref.14
VAR_026210

Experimental info

Mutagenesis2131R → A: Reduces catalytic activity to less than 15% of wild-type. Ref.11
Mutagenesis3341R → A: Reduces catalytic activity to less than 15% of wild-type. Ref.11
Mutagenesis3421C → A: Loss of regulation by redox state. Ref.11
Mutagenesis4981S → A: Reduces catalytic activity to less than 15% of wild-type. Ref.11

Secondary structure

...................................................................................... 535
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified May 30, 2000. Version 2.
Checksum: C63A9431D3FA16C7

FASTA53557,215
        10         20         30         40         50         60 
MATCIWLRSC GARRLGSTFP GCRLRPRAGG LVPASGPAPG PAQLRCYAGR LAGLSAALLR 

        70         80         90        100        110        120 
TDSFVGGRWL PAAATFPVQD PASGAALGMV ADCGVREARA AVRAAYEAFC RWREVSAKER 

       130        140        150        160        170        180 
SSLLRKWYNL MIQNKDDLAR IITAESGKPL KEAHGEILYS AFFLEWFSEE ARRVYGDIIH 

       190        200        210        220        230        240 
TPAKDRRALV LKQPIGVAAV ITPWNFPSAM ITRKVGAALA AGCTVVVKPA EDTPFSALAL 

       250        260        270        280        290        300 
AELASQAGIP SGVYNVIPCS RKNAKEVGEA ICTDPLVSKI SFTGSTTTGK ILLHHAANSV 

       310        320        330        340        350        360 
KRVSMELGGL APFIVFDSAN VDQAVAGAMA SKFRNTGQTC VCSNQFLVQR GIHDAFVKAF 

       370        380        390        400        410        420 
AEAMKKNLRV GNGFEEGTTQ GPLINEKAVE KVEKQVNDAV SKGATVVTGG KRHQLGKNFF 

       430        440        450        460        470        480 
EPTLLCNVTQ DMLCTHEETF GPLAPVIKFD TEEEAIAIAN AADVGLAGYF YSQDPAQIWR 

       490        500        510        520        530 
VAEQLEVGMV GVNEGLISSV ECPFGGVKQS GLGREGSKYG IDEYLELKYV CYGGL 

« Hide

Isoform 2 [UniParc].

Checksum: 98C7673CBBF74FC8
Show »

FASTA54858,653

References

« Hide 'large scale' references
[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. expand/collapse author list , 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. expand/collapse author list , 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]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. expand/collapse author list , 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].
[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]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS4555.1. [P51649-1]
CCDS4556.1. [P51649-2]
PIRA55773.
RefSeqNP_001071.1. NM_001080.3. [P51649-1]
NP_733936.1. NM_170740.1. [P51649-2]
UniGeneHs.371723.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2W8NX-ray2.00A49-535[»]
2W8OX-ray3.40A49-535[»]
2W8PX-ray2.30A49-535[»]
2W8QX-ray2.40A49-535[»]
2W8RX-ray2.40A49-535[»]
ProteinModelPortalP51649.
SMRP51649. Positions 56-535.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid113645. 6 interactions.
IntActP51649. 1 interaction.
MINTMINT-6950845.
STRING9606.ENSP00000314649.

Chemistry

BindingDBP51649.
ChEMBLCHEMBL1911.
DrugBankDB00534. Chlormerodrin.
DB00157. NADH.
DB00139. Succinic acid.

PTM databases

PhosphoSiteP51649.

Polymorphism databases

DMDM7531278.

Proteomic databases

MaxQBP51649.
PaxDbP51649.
PRIDEP51649.

Protocols and materials databases

DNASU7915.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000348925; ENSP00000314649; ENSG00000112294. [P51649-2]
ENST00000357578; ENSP00000350191; ENSG00000112294. [P51649-1]
GeneID7915.
KEGGhsa:7915.
UCSCuc003nef.3. human.
uc003neg.3. human. [P51649-1]

Organism-specific databases

CTD7915.
GeneCardsGC06P024444.
GeneReviewsALDH5A1.
HGNCHGNC:408. ALDH5A1.
HPAHPA029715.
HPA029716.
MIM271980. phenotype.
610045. gene.
neXtProtNX_P51649.
Orphanet22. 4-hydroxybutyric aciduria.
PharmGKBPA24702.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG1012.
HOGENOMHOG000271509.
HOVERGENHBG108515.
KOK00139.
OMAGPLINEM.
OrthoDBEOG72G173.
PhylomeDBP51649.
TreeFamTF352906.

Enzyme and pathway databases

BioCycMetaCyc:HS03550-MONOMER.
BRENDA1.2.1.24. 2681.
ReactomeREACT_13685. Neuronal System.
SABIO-RKP51649.
UniPathwayUPA00733.

Gene expression databases

ArrayExpressP51649.
BgeeP51649.
CleanExHS_ALDH5A1.
GenevestigatorP51649.

Family and domain databases

Gene3D3.40.309.10. 1 hit.
3.40.605.10. 1 hit.
InterProIPR016161. 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]
PfamPF00171. Aldedh. 1 hit.
[Graphical view]
SUPFAMSSF53720. SSF53720. 1 hit.
TIGRFAMsTIGR01780. SSADH. 1 hit.
PROSITEPS00070. ALDEHYDE_DEHYDR_CYS. 1 hit.
PS00687. ALDEHYDE_DEHYDR_GLU. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP51649.
GeneWikiAldehyde_dehydrogenase_5_family,_member_A1.
GenomeRNAi7915.
NextBio30381.
PROP51649.
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Entry information

Entry nameSSDH_HUMAN
AccessionPrimary (citable) accession number: P51649
Secondary accession number(s): B2RD26 expand/collapse secondary AC list , G5E949, Q546H9, Q8N3W6
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: May 30, 2000
Last modified: July 9, 2014
This is version 143 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 6

Human chromosome 6: entries, gene names and cross-references to MIM