Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

Q9CZS1

- AL1B1_MOUSE

UniProt

Q9CZS1 - AL1B1_MOUSE

(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)

Protein

Aldehyde dehydrogenase X, mitochondrial

Gene

Aldh1b1

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli

Functioni

ALDHs play a major role in the detoxification of alcohol-derived acetaldehyde. They are involved in the metabolism of corticosteroids, biogenic amines, neurotransmitters, and lipid peroxidation (By similarity).By similarity

Catalytic activityi

An aldehyde + NAD+ + H2O = a carboxylate + NADH.

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei188 – 1881Transition state stabilizerBy similarity
Active sitei287 – 2871Proton acceptorPROSITE-ProRule annotation
Active sitei321 – 3211NucleophilePROSITE-ProRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi264 – 2696NADBy similarity

GO - Molecular functioni

  1. aldehyde dehydrogenase (NAD) activity Source: UniProtKB-EC

GO - Biological processi

  1. ethanol catabolic process Source: UniProtKB-UniPathway
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

NAD

Enzyme and pathway databases

UniPathwayiUPA00780; UER00768.

Names & Taxonomyi

Protein namesi
Recommended name:
Aldehyde dehydrogenase X, mitochondrial (EC:1.2.1.3)
Alternative name(s):
Aldehyde dehydrogenase family 1 member B1
Gene namesi
Name:Aldh1b1
Synonyms:Aldhx
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 4

Organism-specific databases

MGIiMGI:1919785. Aldh1b1.

Subcellular locationi

Mitochondrion matrix By similarity

GO - Cellular componenti

  1. mitochondrion Source: MGI
  2. nucleus Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 1919MitochondrionSequence AnalysisAdd
BLAST
Chaini20 – 519500Aldehyde dehydrogenase X, mitochondrialPRO_0000271411Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei53 – 531N6-acetyllysine1 Publication
Modified residuei54 – 541N6-acetyllysine; alternate1 Publication
Modified residuei54 – 541N6-succinyllysine; alternate1 Publication
Modified residuei83 – 831N6-succinyllysine1 Publication
Modified residuei366 – 3661N6-acetyllysine; alternate1 Publication
Modified residuei366 – 3661N6-succinyllysine; alternate1 Publication
Modified residuei385 – 3851N6-acetyllysine; alternate1 Publication
Modified residuei385 – 3851N6-succinyllysine; alternate1 Publication
Modified residuei401 – 4011N6-acetyllysine; alternate1 Publication
Modified residuei401 – 4011N6-succinyllysine; alternate1 Publication
Modified residuei416 – 4161N6-acetyllysine; alternate1 Publication
Modified residuei416 – 4161N6-succinyllysine; alternate1 Publication
Modified residuei428 – 4281N6-acetyllysine; alternate1 Publication
Modified residuei428 – 4281N6-succinyllysine; alternate1 Publication
Modified residuei431 – 4311N6-acetyllysine1 Publication

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiQ9CZS1.
PaxDbiQ9CZS1.
PRIDEiQ9CZS1.

PTM databases

PhosphoSiteiQ9CZS1.

Expressioni

Gene expression databases

BgeeiQ9CZS1.
CleanExiMM_ALDH1B1.
ExpressionAtlasiQ9CZS1. baseline and differential.
GenevestigatoriQ9CZS1.

Interactioni

Subunit structurei

Homotetramer.By similarity

Protein-protein interaction databases

IntActiQ9CZS1. 1 interaction.
MINTiMINT-1869729.
STRINGi10090.ENSMUSP00000041260.

Structurei

3D structure databases

ProteinModelPortaliQ9CZS1.
SMRiQ9CZS1. Positions 34-519.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the aldehyde dehydrogenase family.Curated

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiCOG1012.
GeneTreeiENSGT00760000118999.
HOGENOMiHOG000271505.
HOVERGENiHBG000097.
InParanoidiQ9CZS1.
KOiK00128.
OMAiHEGAEED.
OrthoDBiEOG7PS1F7.
PhylomeDBiQ9CZS1.
TreeFamiTF300455.

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.
[Graphical view]
PfamiPF00171. Aldedh. 1 hit.
[Graphical view]
SUPFAMiSSF53720. SSF53720. 1 hit.
PROSITEiPS00070. ALDEHYDE_DEHYDR_CYS. 1 hit.
PS00687. ALDEHYDE_DEHYDR_GLU. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

Q9CZS1-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MLTARLLLPR LLCLQGRTTS YSTAAALPNP IPNPEICYNK LFINNEWHDA
60 70 80 90 100
VSKKTFPTVN PTTGEVIGHV AEGDRADVDL AVKAAREAFR LGSPWRRMDA
110 120 130 140 150
SERGRLLNRL ADLVERDRVY LASLETLDNG KPFQESYVLD LDEVIKVYRY
160 170 180 190 200
FAGWADKWHG KTIPMDGEHF CFTRHEPVGV CGQIIPWNFP LVMQGWKLAP
210 220 230 240 250
ALATGNTVVM KVAEQTPLSA LYLASLIKEA GFPPGVVNII TGYGPTAGAA
260 270 280 290 300
IAQHMDVDKV AFTGSTEVGH LIQKAAGESN LKRVTLELGG KSPSIVLADA
310 320 330 340 350
DMEHAVDQCH EALFFNMGQC CCAGSRTFVE ESIYREFLER TVEKAKQRKV
360 370 380 390 400
GNPFELDTQQ GPQVDKEQFE RILGYIRLGQ KEGAKLLCGG ERLGERGFFI
410 420 430 440 450
KPTVFGDVQD GMRIAKEEIF GPVQPLFKFK KIEEVIQRAN NTRYGLAAAV
460 470 480 490 500
FTRDLDKAIY FTQALQAGTV WVNTYNIVTC HTPFGGFKES GNGRELGEDG
510
LRAYTEVKTV TIKVPEKNS
Length:519
Mass (Da):57,553
Last modified:June 1, 2001 - v1
Checksum:i69222D7409BFEEF3
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti146 – 1461K → R in BAE30339. (PubMed:16141072)Curated
Sequence conflicti261 – 2611A → T in BAE30339. (PubMed:16141072)Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK012213 mRNA. Translation: BAB28101.1.
AK088396 mRNA. Translation: BAC40326.1.
AK150992 mRNA. Translation: BAE30016.1.
AK151349 mRNA. Translation: BAE30325.1.
AK151364 mRNA. Translation: BAE30339.1.
AK153416 mRNA. Translation: BAE31976.1.
BC020001 mRNA. Translation: AAH20001.1.
BC086768 mRNA. Translation: AAH86768.1.
CCDSiCCDS18139.1.
RefSeqiNP_082546.1. NM_028270.4.
UniGeneiMm.331583.

Genome annotation databases

EnsembliENSMUST00000044384; ENSMUSP00000041260; ENSMUSG00000035561.
GeneIDi72535.
KEGGimmu:72535.
UCSCiuc008ssx.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK012213 mRNA. Translation: BAB28101.1 .
AK088396 mRNA. Translation: BAC40326.1 .
AK150992 mRNA. Translation: BAE30016.1 .
AK151349 mRNA. Translation: BAE30325.1 .
AK151364 mRNA. Translation: BAE30339.1 .
AK153416 mRNA. Translation: BAE31976.1 .
BC020001 mRNA. Translation: AAH20001.1 .
BC086768 mRNA. Translation: AAH86768.1 .
CCDSi CCDS18139.1.
RefSeqi NP_082546.1. NM_028270.4.
UniGenei Mm.331583.

3D structure databases

ProteinModelPortali Q9CZS1.
SMRi Q9CZS1. Positions 34-519.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

IntActi Q9CZS1. 1 interaction.
MINTi MINT-1869729.
STRINGi 10090.ENSMUSP00000041260.

PTM databases

PhosphoSitei Q9CZS1.

Proteomic databases

MaxQBi Q9CZS1.
PaxDbi Q9CZS1.
PRIDEi Q9CZS1.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000044384 ; ENSMUSP00000041260 ; ENSMUSG00000035561 .
GeneIDi 72535.
KEGGi mmu:72535.
UCSCi uc008ssx.1. mouse.

Organism-specific databases

CTDi 219.
MGIi MGI:1919785. Aldh1b1.

Phylogenomic databases

eggNOGi COG1012.
GeneTreei ENSGT00760000118999.
HOGENOMi HOG000271505.
HOVERGENi HBG000097.
InParanoidi Q9CZS1.
KOi K00128.
OMAi HEGAEED.
OrthoDBi EOG7PS1F7.
PhylomeDBi Q9CZS1.
TreeFami TF300455.

Enzyme and pathway databases

UniPathwayi UPA00780 ; UER00768 .

Miscellaneous databases

NextBioi 336439.
PROi Q9CZS1.
SOURCEi Search...

Gene expression databases

Bgeei Q9CZS1.
CleanExi MM_ALDH1B1.
ExpressionAtlasi Q9CZS1. baseline and differential.
Genevestigatori Q9CZS1.

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.
[Graphical view ]
Pfami PF00171. Aldedh. 1 hit.
[Graphical view ]
SUPFAMi SSF53720. SSF53720. 1 hit.
PROSITEi PS00070. ALDEHYDE_DEHYDR_CYS. 1 hit.
PS00687. ALDEHYDE_DEHYDR_GLU. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J and NOD.
    Tissue: Bone marrow, Embryo and Thymus.
  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].
    Strain: C57BL/6 and FVB/N.
    Tissue: Brain and Colon.
  3. "SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
    Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
    Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-54; LYS-83; LYS-366; LYS-385; LYS-401; LYS-416 AND LYS-428, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  4. "Label-free quantitative proteomics of the lysine acetylome in mitochondria identifies substrates of SIRT3 in metabolic pathways."
    Rardin M.J., Newman J.C., Held J.M., Cusack M.P., Sorensen D.J., Li B., Schilling B., Mooney S.D., Kahn C.R., Verdin E., Gibson B.W.
    Proc. Natl. Acad. Sci. U.S.A. 110:6601-6606(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-53; LYS-54; LYS-366; LYS-385; LYS-401; LYS-416; LYS-428 AND LYS-431, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.

Entry informationi

Entry nameiAL1B1_MOUSE
AccessioniPrimary (citable) accession number: Q9CZS1
Secondary accession number(s): Q3UAH5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 9, 2007
Last sequence update: June 1, 2001
Last modified: October 29, 2014
This is version 109 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3