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P51649

- SSDH_HUMAN

UniProt

P51649 - SSDH_HUMAN

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Protein

Succinate-semialdehyde dehydrogenase, mitochondrial

Gene

ALDH5A1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

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
Complete GO annotation...

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
Complete GO annotation...

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

BgeeiP51649.
CleanExiHS_ALDH5A1.
ExpressionAtlasiP51649. baseline and differential.
GenevestigatoriP51649.

Organism-specific databases

HPAiHPA029715.
HPA029716.

Interactioni

Subunit structurei

Homotetramer.2 Publications

Protein-protein interaction databases

BioGridi113645. 9 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 – 583Combined sources
Beta strandi62 – 654Combined sources
Beta strandi68 – 703Combined sources
Beta strandi75 – 795Combined sources
Turni81 – 833Combined sources
Beta strandi86 – 916Combined sources
Helixi95 – 11218Combined sources
Helixi117 – 13317Combined sources
Helixi135 – 14612Combined sources
Helixi150 – 17021Combined sources
Helixi171 – 1733Combined sources
Beta strandi177 – 1793Combined sources
Beta strandi187 – 1948Combined sources
Beta strandi197 – 2015Combined sources
Beta strandi204 – 2063Combined sources
Helixi209 – 22113Combined sources
Beta strandi224 – 2285Combined sources
Helixi235 – 24713Combined sources
Beta strandi253 – 2564Combined sources
Helixi261 – 27111Combined sources
Beta strandi277 – 2848Combined sources
Helixi286 – 29712Combined sources
Turni298 – 3003Combined sources
Beta strandi302 – 3076Combined sources
Beta strandi309 – 3157Combined sources
Beta strandi317 – 3193Combined sources
Helixi321 – 33212Combined sources
Helixi334 – 3374Combined sources
Beta strandi341 – 3499Combined sources
Helixi350 – 36718Combined sources
Beta strandi373 – 3753Combined sources
Helixi386 – 40015Combined sources
Turni401 – 4033Combined sources
Beta strandi405 – 4084Combined sources
Beta strandi423 – 4286Combined sources
Helixi430 – 4334Combined sources
Beta strandi441 – 45010Combined sources
Helixi452 – 4598Combined sources
Beta strandi466 – 4716Combined sources
Helixi475 – 48410Combined sources
Beta strandi487 – 4937Combined sources
Helixi508 – 5103Combined sources
Beta strandi511 – 5133Combined sources
Turni517 – 5193Combined sources
Helixi520 – 5245Combined sources
Beta strandi525 – 5328Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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.
InParanoidiP51649.
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

        10         20         30         40         50
MATCIWLRSC GARRLGSTFP GCRLRPRAGG LVPASGPAPG PAQLRCYAGR
60 70 80 90 100
LAGLSAALLR TDSFVGGRWL PAAATFPVQD PASGAALGMV ADCGVREARA
110 120 130 140 150
AVRAAYEAFC RWREVSAKER SSLLRKWYNL MIQNKDDLAR IITAESGKPL
160 170 180 190 200
KEAHGEILYS AFFLEWFSEE ARRVYGDIIH TPAKDRRALV LKQPIGVAAV
210 220 230 240 250
ITPWNFPSAM ITRKVGAALA AGCTVVVKPA EDTPFSALAL AELASQAGIP
260 270 280 290 300
SGVYNVIPCS RKNAKEVGEA ICTDPLVSKI SFTGSTTTGK ILLHHAANSV
310 320 330 340 350
KRVSMELGGL APFIVFDSAN VDQAVAGAMA SKFRNTGQTC VCSNQFLVQR
360 370 380 390 400
GIHDAFVKAF AEAMKKNLRV GNGFEEGTTQ GPLINEKAVE KVEKQVNDAV
410 420 430 440 450
SKGATVVTGG KRHQLGKNFF EPTLLCNVTQ DMLCTHEETF GPLAPVIKFD
460 470 480 490 500
TEEEAIAIAN AADVGLAGYF YSQDPAQIWR VAEQLEVGMV GVNEGLISSV
510 520 530
ECPFGGVKQS GLGREGSKYG IDEYLELKYV CYGGL
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:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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:
PDBei
RCSB PDBi
PDBji
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. 9 interactions.
IntActi P51649. 1 interaction.
MINTi MINT-6950845.
STRINGi 9606.ENSP00000314649.

Chemistry

BindingDBi P51649.
ChEMBLi CHEMBL1911.
DrugBanki DB00534. Chlormerodrin.
DB00139. Succinic acid.
DB00313. Valproic 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.
InParanoidi P51649.
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

Bgeei P51649.
CleanExi HS_ALDH5A1.
ExpressionAtlasi P51649. baseline and differential.
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

« Hide 'large scale' publications
  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 29, 2014
This is version 146 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