GONUTS has been updated to MW1.31 Most things seem to be working but be sure to report problems.

Have any questions? Please email us at ecoliwiki@gmail.com

HUMAN:AL1B1

From GONUTS
Jump to: navigation, search
Species (Taxon ID) Homo sapiens (Human). (9606)
Gene Name(s) ALDH1B1 (synonyms: ALDH5, ALDHX)
Protein Name(s) Aldehyde dehydrogenase X, mitochondrial

Aldehyde dehydrogenase 5 Aldehyde dehydrogenase family 1 member B1

External Links
UniProt P30837
EMBL M63967
BT007418
AK313344
AL135785
BC001619
CCDS CCDS6615.1
PIR A40872
RefSeq NP_000683.3
UniGene Hs.436219
Hs.743532
ProteinModelPortal P30837
SMR P30837
BioGrid 106721
IntAct P30837
STRING 9606.ENSP00000366927
ChEMBL CHEMBL4881
PhosphoSite P30837
DMDM 311033472
REPRODUCTION-2DPAGE IPI00103467
MaxQB P30837
PaxDb P30837
PRIDE P30837
DNASU 219
Ensembl ENST00000377698
GeneID 219
KEGG hsa:219
UCSC uc004aay.3
CTD 219
GeneCards GC09P038392
H-InvDB HIX0008051
HGNC HGNC:407
HPA HPA021037
MIM 100670
neXtProt NX_P30837
PharmGKB PA24695
eggNOG COG1012
HOGENOM HOG000271505
HOVERGEN HBG000097
InParanoid P30837
KO K00128
OrthoDB EOG7PS1F7
PhylomeDB P30837
TreeFam TF300455
SABIO-RK P30837
UniPathway UPA00780
ChiTaRS ALDH1B1
GeneWiki ALDH1B1
GenomeRNAi 219
NextBio 886
PRO PR:P30837
Proteomes UP000005640
Bgee P30837
CleanEx HS_ALDH1B1
ExpressionAtlas P30837
Genevestigator P30837
GO GO:0043231
GO:0005759
GO:0005739
GO:0005634
GO:0004029
GO:0005975
GO:0006068
Gene3D 3.40.309.10
3.40.605.10
InterPro IPR016161
IPR016163
IPR016160
IPR029510
IPR016162
IPR015590
Pfam PF00171
SUPFAM SSF53720
PROSITE PS00070
PS00687

Annotations

Qualifier GO ID GO term name Reference ECO ID ECO term name with/from Aspect Extension Notes Status
GO:0004029

aldehyde dehydrogenase (NAD) activity

PMID:401580[1]

ECO:0000314

F

Table 1: The gels were stained for ALDH activity with an agar overlay containing propionaldehyde or benzaldehyde.

complete
CACAO 8522

enables

GO:0051287

NAD binding

PMID:12693930[2]

ECO:0000250

sequence similarity evidence used in manual assertion

UniProtKB:Q28399

F

Seeded From UniProt

complete

involved_in

GO:0005975

carbohydrate metabolic process

PMID:1306115[3]

ECO:0000303

author statement without traceable support used in manual assertion

P

Seeded From UniProt

complete

enables

GO:0004029

aldehyde dehydrogenase (NAD) activity

PMID:21873635[4]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

FB:FBgn0012036
MGI:MGI:1861722
PANTHER:PTN000192421
RGD:2087
RGD:620252
RGD:68409
RGD:69219
SGD:S000000875
SGD:S000005901
UniProtKB:O75891
UniProtKB:P00352
UniProtKB:P05091
UniProtKB:P08157
UniProtKB:P48644
UniProtKB:P49189
UniProtKB:Q3SY69

F

Seeded From UniProt

complete

part_of

GO:0043231

intracellular membrane-bounded organelle

GO_REF:0000052

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

part_of

GO:0005739

mitochondrion

GO_REF:0000052

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

part_of

GO:0005654

nucleoplasm

GO_REF:0000052

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

enables

GO:0016491

oxidoreductase activity

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR015590
InterPro:IPR016160
InterPro:IPR016161
InterPro:IPR016162
InterPro:IPR016163
InterPro:IPR029510

F

Seeded From UniProt

complete

enables

GO:0016620

oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR016163

F

Seeded From UniProt

complete

involved_in

GO:0055114

oxidation-reduction process

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR015590
InterPro:IPR016160
InterPro:IPR016161
InterPro:IPR016162
InterPro:IPR016163
InterPro:IPR029510

P

Seeded From UniProt

complete

enables

GO:0043878

glyceraldehyde-3-phosphate dehydrogenase (NAD+) (non-phosphorylating) activity

GO_REF:0000003

ECO:0000501

evidence used in automatic assertion

EC:1.2.1.3

F

Seeded From UniProt

complete

enables

GO:0004029

aldehyde dehydrogenase (NAD) activity

GO_REF:0000003

ECO:0000501

evidence used in automatic assertion

EC:1.2.1.3

F

Seeded From UniProt

complete

involved_in

GO:0006069

ethanol oxidation

Reactome:R-HSA-71384

ECO:0000304

author statement supported by traceable reference used in manual assertion

P

Seeded From UniProt

complete

part_of

GO:0005759

mitochondrial matrix

Reactome:R-HSA-5696091

ECO:0000304

author statement supported by traceable reference used in manual assertion

C

Seeded From UniProt

complete

enables

GO:0016491

oxidoreductase activity

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0560

F

Seeded From UniProt

complete

part_of

GO:0005739

mitochondrion

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0496

C

Seeded From UniProt

complete

involved_in

GO:0055114

oxidation-reduction process

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0560

P

Seeded From UniProt

complete

part_of

GO:0005759

mitochondrial matrix

GO_REF:0000039

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-SubCell:SL-0170

C

Seeded From UniProt

complete

involved_in

GO:0006068

ethanol catabolic process

GO_REF:0000041

ECO:0000322

imported manually asserted information used in automatic assertion

UniPathway:UPA00780

P

Seeded From UniProt

complete

Notes

References

See Help:References for how to manage references in GONUTS.

  1. Kassner, EG et al. (1977) Passage of feeding catheters into the pleural space: a radiographic sign of trauma to the pharynx and esophagus in the newborn. AJR Am J Roentgenol 128 19-22 PubMed GONUTS page
  2. Bateman, OA et al. (2003) Crystal structure of eta-crystallin: adaptation of a class 1 aldehyde dehydrogenase for a new role in the eye lens. Biochemistry 42 4349-56 PubMed GONUTS page
  3. Yoshida, A (1992) Molecular genetics of human aldehyde dehydrogenase. Pharmacogenetics 2 139-47 PubMed GONUTS page
  4. Gaudet, P et al. (2011) Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. Brief. Bioinformatics 12 449-62 PubMed GONUTS page