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P30038 (AL4A1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 154. 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·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Delta-1-pyrroline-5-carboxylate dehydrogenase, mitochondrial

Short name=P5C dehydrogenase
EC=1.2.1.88
Alternative name(s):
Aldehyde dehydrogenase family 4 member A1
L-glutamate gamma-semialdehyde dehydrogenase
Gene names
Name:ALDH4A1
Synonyms:ALDH4, P5CDH
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length563 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Irreversible conversion of delta-1-pyrroline-5-carboxylate (P5C), derived either from proline or ornithine, to glutamate. This is a necessary step in the pathway interconnecting the urea and tricarboxylic acid cycles. The preferred substrate is glutamic gamma-semialdehyde, other substrates include succinic, glutaric and adipic semialdehydes. Ref.12

Catalytic activity

L-glutamate 5-semialdehyde + NAD+ + H2O = L-glutamate + NADH. Ref.12

Pathway

Amino-acid degradation; L-proline degradation into L-glutamate; L-glutamate from L-proline: step 2/2. Ref.12

Subunit structure

Homodimer. Ref.12

Subcellular location

Mitochondrion matrix.

Tissue specificity

Highest expression is found in liver followed by skeletal muscle, kidney, heart, brain, placenta, lung and pancreas.

Involvement in disease

Hyperprolinemia 2 (HP-2) [MIM:239510]: Characterized by the accumulation of delta-1-pyrroline-5-carboxylate (P5C) and proline. The disorder may be causally related to neurologic manifestations, including seizures and mental retardation.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.12 Ref.13

Sequence similarities

Belongs to the aldehyde dehydrogenase family.

Biophysicochemical properties

Kinetic parameters:

KM=100 µM for NAD Ref.12

KM=32 µM for L-pyrroline-5-carboxylate

Binary interactions

With

Entry

#Exp.

IntAct

Notes

itself2EBI-3926971,EBI-3926971

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P30038-1)

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: P30038-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-60: Missing.
Isoform 3 (identifier: P30038-3)

The sequence of this isoform differs from the canonical sequence as follows:
     396-446: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 2424Mitochondrion Ref.9
Chain25 – 563539Delta-1-pyrroline-5-carboxylate dehydrogenase, mitochondrial
PRO_0000007173

Regions

Nucleotide binding286 – 2905NAD By similarity

Sites

Active site3141Proton acceptor By similarity
Active site3481Nucleophile Ref.12
Binding site2081NAD By similarity
Binding site2331NAD By similarity
Binding site4471NAD By similarity
Binding site5131Substrate By similarity
Site2111Transition state stabilizer By similarity

Amino acid modifications

Modified residue311N6-succinyllysine By similarity
Modified residue521N6-acetyllysine By similarity
Modified residue931N6-acetyllysine; alternate By similarity
Modified residue931N6-succinyllysine; alternate By similarity
Modified residue991N6-acetyllysine; alternate By similarity
Modified residue991N6-succinyllysine; alternate By similarity
Modified residue1141N6-acetyllysine; alternate By similarity
Modified residue1141N6-succinyllysine; alternate By similarity
Modified residue1301N6-acetyllysine; alternate By similarity
Modified residue1301N6-succinyllysine; alternate By similarity
Modified residue1751N6-acetyllysine; alternate By similarity
Modified residue1751N6-succinyllysine; alternate By similarity
Modified residue3181N6-acetyllysine By similarity
Modified residue3471N6-succinyllysine By similarity
Modified residue3651N6-acetyllysine By similarity
Modified residue3761N6-acetyllysine By similarity
Modified residue3951N6-succinyllysine By similarity
Modified residue4621N6-acetyllysine By similarity
Modified residue5091N6-acetyllysine; alternate By similarity
Modified residue5091N6-succinyllysine; alternate By similarity
Modified residue5311N6-acetyllysine By similarity
Modified residue5521N6-acetyllysine By similarity

Natural variations

Alternative sequence1 – 6060Missing in isoform 2.
VSP_043785
Alternative sequence396 – 44651Missing in isoform 3.
VSP_047732
Natural variant161P → L in allele ALDH4A1*4. Ref.13
Corresponds to variant rs146450609 [ dbSNP | Ensembl ].
VAR_002259
Natural variant3521S → L in HP-2; allele ALDH4A1*3; loss of enzyme activity. Ref.12 Ref.13
VAR_002260
Natural variant4701V → I. Ref.3 Ref.7
Corresponds to variant rs2230709 [ dbSNP | Ensembl ].
VAR_029337
Natural variant4731T → A.
Corresponds to variant rs6695033 [ dbSNP | Ensembl ].
VAR_048903

Experimental info

Mutagenesis3521S → A: Reduced affinity for NAD. No effect on enzyme activity. Ref.12
Sequence conflict681V → M in AAC50501. Ref.1
Sequence conflict681V → M in AAC50500. Ref.1
Sequence conflict189 – 1913PPS → LPY AA sequence Ref.10
Sequence conflict1891P → L AA sequence Ref.8
Sequence conflict2261M → I in BAD96206. Ref.4
Sequence conflict2711D → E AA sequence Ref.8
Sequence conflict2711D → E AA sequence Ref.10
Sequence conflict3541L → K AA sequence Ref.10
Sequence conflict3761K → R in BAD96206. Ref.4
Sequence conflict524 – 5263RAS → GSA AA sequence Ref.10

Secondary structure

.......................................................................................... 563
Helix Strand Turn

Details...

Sequences

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

Last modified February 1, 2005. Version 3.
Checksum: 4D964771B7DB5FFD

FASTA56361,719
        10         20         30         40         50         60 
MLLPAPALRR ALLSRPWTGA GLRWKHTSSL KVANEPVLAF TQGSPERDAL QKALKDLKGR 

        70         80         90        100        110        120 
MEAIPCVVGD EEVWTSDVQY QVSPFNHGHK VAKFCYADKS LLNKAIEAAL AARKEWDLKP 

       130        140        150        160        170        180 
IADRAQIFLK AADMLSGPRR AEILAKTMVG QGKTVIQAEI DAAAELIDFF RFNAKYAVEL 

       190        200        210        220        230        240 
EGQQPISVPP STNSTVYRGL EGFVAAISPF NFTAIGGNLA GAPALMGNVV LWKPSDTAML 

       250        260        270        280        290        300 
ASYAVYRILR EAGLPPNIIQ FVPADGPLFG DTVTSSEHLC GINFTGSVPT FKHLWKQVAQ 

       310        320        330        340        350        360 
NLDRFHTFPR LAGECGGKNF HFVHRSADVE SVVSGTLRSA FEYGGQKCSA CSRLYVPHSL 

       370        380        390        400        410        420 
WPQIKGRLLE EHSRIKVGDP AEDFGTFFSA VIDAKSFARI KKWLEHARSS PSLTILAGGK 

       430        440        450        460        470        480 
CDDSVGYFVE PCIVESKDPQ EPIMKEEIFG PVLSVYVYPD DKYKETLQLV DSTTSYGLTG 

       490        500        510        520        530        540 
AVFSQDKDVV QEATKVLRNA AGNFYINDKS TGSIVGQQPF GGARASGTND KPGGPHYILR 

       550        560 
WTSPQVIKET HKPLGDWSYA YMQ 

« Hide

Isoform 2 [UniParc].

Checksum: 51F7786045941395
Show »

FASTA50355,118
Isoform 3 [UniParc].

Checksum: 1AA9C976895301FE
Show »

FASTA51256,043

References

« Hide 'large scale' references
[1]"Cloning, characterization, and expression of cDNAs encoding human delta 1-pyrroline-5-carboxylate dehydrogenase."
Hu C.-A., Lin W.-W., Valle D.
J. Biol. Chem. 271:9795-9800(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Tissue: Kidney and Retina.
[2]"A novel transcript variant of human ALDH4A1 gene."
Stagos D., Vasiliou V.
Submitted (NOV-2008) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
[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] (ISOFORMS 1 AND 2), VARIANT ILE-470.
Tissue: Amygdala and Hippocampus.
[4]Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.
Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Tissue: Adipose tissue.
[5]"The DNA sequence and biological annotation of human chromosome 1."
Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K. expand/collapse author list , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]Mural R.J., Istrail S., Sutton G.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].
[7]"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], VARIANT ILE-470.
Tissue: Lung and Placenta.
[8]"Human liver glutamic gamma-semialdehyde dehydrogenase: structural relationship to the yeast enzyme."
Hempel J., Eckey R., Berie D., Romovacek H., Agarwal D.P., Goedde H.W.
Comp. Biochem. Physiol. 102B:791-793(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: PARTIAL PROTEIN SEQUENCE.
Tissue: Liver.
[9]"Human liver protein map: a reference database established by microsequencing and gel comparison."
Hochstrasser D.F., Frutiger S., Paquet N., Bairoch A., Ravier F., Pasquali C., Sanchez J.-C., Tissot J.-D., Bjellqvist B., Vargas R., Appel R.D., Hughes G.J.
Electrophoresis 13:992-1001(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 25-35.
Tissue: Liver.
[10]"Human liver high Km aldehyde dehydrogenase (ALDH4): properties and structural relationship to the glutamic gamma-semialdehyde dehydrogenase."
Agarwal D.P., Eckey R., Hempel J., Goedde H.W.
Adv. Exp. Med. Biol. 328:191-197(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 94-99; 105-113; 125-139; 176-191; 251-273; 339-347; 354-365 AND 510-526.
Tissue: Liver.
[11]"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].
[12]"The three-dimensional structural basis of type II hyperprolinemia."
Srivastava D., Singh R.K., Moxley M.A., Henzl M.T., Becker D.F., Tanner J.J.
J. Mol. Biol. 420:176-189(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.40 ANGSTROMS) OF 18-563 OF WILD-TYPE; MUTANT ALA-352 AND VARIANT HP-2 LEU-352, CATALYTIC ACTIVITY, FUNCTION, PATHWAY, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, ACTIVE SITE, CHARACTERIZATION OF VARIANT HP-2 LEU-352, MUTAGENESIS OF SER-352.
[13]"Mutations in the Delta1-pyrroline 5-carboxylate dehydrogenase gene cause type II hyperprolinemia."
Geraghty M.T., Vaughn D., Nicholson A.J., Lin W.-W., Jimenez-Sanchez G., Obie C., Flynn M.P., Valle D., Hu C.-A.A.
Hum. Mol. Genet. 7:1411-1415(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT HP-2 LEU-352, VARIANT LEU-16.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U24267 mRNA. Translation: AAC50501.1.
U24266 mRNA. Translation: AAC50500.1.
FJ462711 mRNA. Translation: ACN89883.1.
AK289972 mRNA. Translation: BAF82661.1.
AK294552 mRNA. Translation: BAG57755.1.
AK222486 mRNA. Translation: BAD96206.1.
AL080251, AL954340 Genomic DNA. Translation: CAI23417.1.
AL954340, AL080251 Genomic DNA. Translation: CAI39493.1.
BX537160 Genomic DNA. No translation available.
CH471134 Genomic DNA. Translation: EAW94858.1.
BC007581 mRNA. Translation: AAH07581.1.
BC023600 mRNA. Translation: AAH23600.1.
CCDSCCDS188.1. [P30038-1]
CCDS53272.1. [P30038-2]
RefSeqNP_001154976.1. NM_001161504.1. [P30038-2]
NP_003739.2. NM_003748.3. [P30038-1]
NP_733844.1. NM_170726.2. [P30038-1]
UniGeneHs.77448.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3V9GX-ray2.50A/B/C/D18-563[»]
3V9HX-ray2.40A/B/C/D18-563[»]
3V9IX-ray2.85A/B/C/D18-563[»]
4OE5X-ray1.95A/B/C/D18-563[»]
ProteinModelPortalP30038.
SMRP30038. Positions 23-563.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid114208. 4 interactions.
IntActP30038. 1 interaction.
STRING9606.ENSP00000290597.

Chemistry

DrugBankDB00157. NADH.

PTM databases

PhosphoSiteP30038.

Polymorphism databases

DMDM62511241.

2D gel databases

OGPP30038.
SWISS-2DPAGEP30038.

Proteomic databases

MaxQBP30038.
PaxDbP30038.
PRIDEP30038.

Protocols and materials databases

DNASU8659.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000290597; ENSP00000290597; ENSG00000159423. [P30038-1]
ENST00000375341; ENSP00000364490; ENSG00000159423. [P30038-1]
ENST00000538309; ENSP00000442988; ENSG00000159423. [P30038-2]
ENST00000538839; ENSP00000446071; ENSG00000159423. [P30038-3]
GeneID8659.
KEGGhsa:8659.
UCSCuc001bbb.3. human. [P30038-1]

Organism-specific databases

CTD8659.
GeneCardsGC01M019197.
HGNCHGNC:406. ALDH4A1.
HPACAB004645.
HPA006401.
MIM239510. phenotype.
606811. gene.
neXtProtNX_P30038.
Orphanet79101. Hyperprolinemia type 2.
PharmGKBPA24701.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG1012.
HOVERGENHBG050484.
InParanoidP30038.
KOK00294.
OMALRWKHTS.
OrthoDBEOG7T1R9D.
PhylomeDBP30038.
TreeFamTF300481.

Enzyme and pathway databases

BioCycMetaCyc:HS14757-MONOMER.
ReactomeREACT_111217. Metabolism.
SABIO-RKP30038.
UniPathwayUPA00261; UER00374.

Gene expression databases

ArrayExpressP30038.
BgeeP30038.
CleanExHS_ALDH4A1.
GenevestigatorP30038.

Family and domain databases

Gene3D3.40.309.10. 1 hit.
3.40.605.10. 1 hit.
InterProIPR005931. 1-pyrroline-5-COlate_DH.
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]
PfamPF00171. Aldedh. 1 hit.
[Graphical view]
SUPFAMSSF53720. SSF53720. 1 hit.
TIGRFAMsTIGR01236. D1pyr5carbox1. 1 hit.
PROSITEPS00070. ALDEHYDE_DEHYDR_CYS. 1 hit.
PS00687. ALDEHYDE_DEHYDR_GLU. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GeneWikiAldehyde_dehydrogenase_4_family,_member_A1.
GenomeRNAi8659.
NextBio32473.
PROP30038.
SOURCESearch...

Entry information

Entry nameAL4A1_HUMAN
AccessionPrimary (citable) accession number: P30038
Secondary accession number(s): A8K1Q7 expand/collapse secondary AC list , B4DGE4, D2D4A3, Q16882, Q53HU4, Q5JNV6, Q8IZ38, Q96IF0, Q9UDI6
Entry history
Integrated into UniProtKB/Swiss-Prot: April 1, 1993
Last sequence update: February 1, 2005
Last modified: July 9, 2014
This is version 154 of the entry and version 3 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 1

Human chromosome 1: entries, gene names and cross-references to MIM