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Protein

Delta-1-pyrroline-5-carboxylate dehydrogenase, mitochondrial

Gene

ALDH4A1

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

Functioni

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.1 Publication

Catalytic activityi

L-glutamate 5-semialdehyde + NAD+ + H2O = L-glutamate + NADH.1 Publication

Kineticsi

  1. KM=100 µM for NAD1 Publication
  2. KM=32 µM for L-pyrroline-5-carboxylate1 Publication

    Pathway: L-proline degradation into L-glutamate

    This protein is involved in step 2 of the subpathway that synthesizes L-glutamate from L-proline.1 Publication
    Proteins known to be involved in the 2 steps of the subpathway in this organism are:
    1. Probable proline dehydrogenase 2 (PRODH2), Proline dehydrogenase 1, mitochondrial (PRODH)
    2. Delta-1-pyrroline-5-carboxylate dehydrogenase, mitochondrial (ALDH4A1)
    This subpathway is part of the pathway L-proline degradation into L-glutamate, which is itself part of Amino-acid degradation.
    View all proteins of this organism that are known to be involved in the subpathway that synthesizes L-glutamate from L-proline, the pathway L-proline degradation into L-glutamate and in Amino-acid degradation.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei208 – 2081NADBy similarity
    Sitei211 – 2111Transition state stabilizerBy similarity
    Binding sitei233 – 2331NADBy similarity
    Active sitei314 – 3141Proton acceptorPROSITE-ProRule annotation
    Active sitei348 – 3481NucleophilePROSITE-ProRule annotation1 Publication
    Binding sitei447 – 4471NADBy similarity
    Binding sitei513 – 5131SubstrateBy similarity

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi286 – 2905NADBy similarity

    GO - Molecular functioni

    • 1-pyrroline-5-carboxylate dehydrogenase activity Source: Reactome
    • aldehyde dehydrogenase (NAD) activity Source: CACAO
    • electron carrier activity Source: UniProtKB
    • identical protein binding Source: IntAct

    GO - Biological processi

    Complete GO annotation...

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Biological processi

    Proline metabolism

    Keywords - Ligandi

    NAD

    Enzyme and pathway databases

    BioCyciMetaCyc:HS14757-MONOMER.
    BRENDAi1.2.1.88. 2681.
    ReactomeiREACT_1002. Proline catabolism.
    SABIO-RKP30038.
    UniPathwayiUPA00261; UER00374.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Delta-1-pyrroline-5-carboxylate dehydrogenase, mitochondrial (EC:1.2.1.88)
    Short name:
    P5C dehydrogenase
    Alternative name(s):
    Aldehyde dehydrogenase family 4 member A1
    L-glutamate gamma-semialdehyde dehydrogenase
    Gene namesi
    Name:ALDH4A1
    Synonyms:ALDH4, P5CDH
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640 Componenti: Chromosome 1

    Organism-specific databases

    HGNCiHGNC:406. ALDH4A1.

    Subcellular locationi

    GO - Cellular componenti

    Complete GO annotation...

    Keywords - Cellular componenti

    Mitochondrion

    Pathology & Biotechi

    Involvement in diseasei

    Hyperprolinemia 2 (HYRPRO2)1 Publication

    The disease is caused by mutations affecting the gene represented in this entry.

    Disease descriptionAn inborn error of proline metabolism resulting in elevated plasma levels of proline and delta-1-pyrroline-5-carboxylate (P5C). The condition is considered to be benign, but affected individuals can exhibit neurological manifestations that vary in severity. Clinical signs include seizures, intellectual deficit and mild developmental delay.

    See also OMIM:239510
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti352 – 3521S → L in HYRPRO2; allele ALDH4A1*3; loss of enzyme activity. 2 Publications
    VAR_002260

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi352 – 3521S → A: Reduced affinity for NAD. No effect on enzyme activity. 1 Publication

    Keywords - Diseasei

    Disease mutation

    Organism-specific databases

    MIMi239510. phenotype.
    Orphaneti79101. Hyperprolinemia type 2.
    PharmGKBiPA24701.

    Polymorphism and mutation databases

    BioMutaiALDH4A1.
    DMDMi62511241.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transit peptidei1 – 2424Mitochondrion1 PublicationAdd
    BLAST
    Chaini25 – 563539Delta-1-pyrroline-5-carboxylate dehydrogenase, mitochondrialPRO_0000007173Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei31 – 311N6-succinyllysineBy similarity
    Modified residuei44 – 441Phosphoserine1 Publication
    Modified residuei52 – 521N6-acetyllysineBy similarity
    Modified residuei93 – 931N6-acetyllysine; alternateBy similarity
    Modified residuei93 – 931N6-succinyllysine; alternateBy similarity
    Modified residuei99 – 991N6-acetyllysine; alternateBy similarity
    Modified residuei99 – 991N6-succinyllysine; alternateBy similarity
    Modified residuei114 – 1141N6-acetyllysine; alternateBy similarity
    Modified residuei114 – 1141N6-succinyllysine; alternateBy similarity
    Modified residuei130 – 1301N6-acetyllysine; alternateBy similarity
    Modified residuei130 – 1301N6-succinyllysine; alternateBy similarity
    Modified residuei175 – 1751N6-acetyllysine; alternateBy similarity
    Modified residuei175 – 1751N6-succinyllysine; alternateBy similarity
    Modified residuei318 – 3181N6-acetyllysineBy similarity
    Modified residuei347 – 3471N6-succinyllysineBy similarity
    Modified residuei365 – 3651N6-acetyllysineBy similarity
    Modified residuei376 – 3761N6-acetyllysineBy similarity
    Modified residuei395 – 3951N6-succinyllysineBy similarity
    Modified residuei462 – 4621N6-acetyllysineBy similarity
    Modified residuei509 – 5091N6-acetyllysine; alternateBy similarity
    Modified residuei509 – 5091N6-succinyllysine; alternateBy similarity
    Modified residuei531 – 5311N6-acetyllysineBy similarity
    Modified residuei552 – 5521N6-acetyllysineBy similarity

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiP30038.
    PaxDbiP30038.
    PRIDEiP30038.

    2D gel databases

    OGPiP30038.
    SWISS-2DPAGEP30038.

    PTM databases

    PhosphoSiteiP30038.

    Expressioni

    Tissue specificityi

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

    Gene expression databases

    BgeeiP30038.
    CleanExiHS_ALDH4A1.
    ExpressionAtlasiP30038. baseline and differential.
    GenevisibleiP30038. HS.

    Organism-specific databases

    HPAiCAB004645.
    HPA006401.

    Interactioni

    Subunit structurei

    Homodimer.1 Publication

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    itself2EBI-3926971,EBI-3926971

    Protein-protein interaction databases

    BioGridi114208. 5 interactions.
    IntActiP30038. 1 interaction.
    STRINGi9606.ENSP00000290597.

    Structurei

    Secondary structure

    1
    563
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi24 – 307Combined sources
    Helixi45 – 5713Combined sources
    Beta strandi62 – 643Combined sources
    Beta strandi66 – 683Combined sources
    Beta strandi71 – 733Combined sources
    Beta strandi78 – 836Combined sources
    Beta strandi86 – 9510Combined sources
    Helixi99 – 11820Combined sources
    Helixi121 – 13616Combined sources
    Turni137 – 1393Combined sources
    Helixi140 – 15112Combined sources
    Helixi155 – 16511Combined sources
    Helixi167 – 18014Combined sources
    Beta strandi192 – 1998Combined sources
    Beta strandi201 – 2077Combined sources
    Helixi217 – 2259Combined sources
    Beta strandi229 – 2335Combined sources
    Helixi236 – 2383Combined sources
    Helixi239 – 25113Combined sources
    Beta strandi258 – 2614Combined sources
    Helixi266 – 2749Combined sources
    Beta strandi279 – 2868Combined sources
    Helixi288 – 30013Combined sources
    Helixi301 – 3044Combined sources
    Beta strandi310 – 3156Combined sources
    Beta strandi319 – 3235Combined sources
    Helixi329 – 34113Combined sources
    Helixi342 – 3454Combined sources
    Beta strandi351 – 3577Combined sources
    Turni358 – 3603Combined sources
    Helixi361 – 37212Combined sources
    Turni380 – 3823Combined sources
    Helixi394 – 40916Combined sources
    Beta strandi413 – 4175Combined sources
    Beta strandi424 – 4263Combined sources
    Beta strandi432 – 4376Combined sources
    Helixi442 – 4454Combined sources
    Beta strandi450 – 4589Combined sources
    Helixi460 – 4623Combined sources
    Helixi463 – 47210Combined sources
    Beta strandi475 – 4773Combined sources
    Beta strandi479 – 4835Combined sources
    Helixi487 – 49610Combined sources
    Turni497 – 5004Combined sources
    Beta strandi502 – 5087Combined sources
    Turni515 – 5173Combined sources
    Helixi528 – 5303Combined sources
    Beta strandi534 – 5363Combined sources
    Helixi537 – 5415Combined sources
    Beta strandi542 – 5498Combined sources
    Helixi560 – 5623Combined sources

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    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[»]
    ProteinModelPortaliP30038.
    SMRiP30038. Positions 23-563.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the aldehyde dehydrogenase family.Curated

    Keywords - Domaini

    Transit peptide

    Phylogenomic databases

    eggNOGiCOG1012.
    GeneTreeiENSGT00560000077335.
    HOVERGENiHBG050484.
    InParanoidiP30038.
    KOiK00294.
    OMAiLTDWKYP.
    OrthoDBiEOG7T1R9D.
    PhylomeDBiP30038.
    TreeFamiTF300481.

    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.
    IPR005931. P5CDH/ALDH4A1.
    [Graphical view]
    PfamiPF00171. Aldedh. 1 hit.
    [Graphical view]
    SUPFAMiSSF53720. SSF53720. 1 hit.
    TIGRFAMsiTIGR01236. D1pyr5carbox1. 1 hit.
    PROSITEiPS00070. ALDEHYDE_DEHYDR_CYS. 1 hit.
    PS00687. ALDEHYDE_DEHYDR_GLU. 1 hit.
    [Graphical view]

    Sequences (3)i

    Sequence statusi: Complete.

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

    This entry describes 3 isoformsi produced by alternative splicing. AlignAdd to basket

    Isoform 1 (identifier: P30038-1) [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
    MLLPAPALRR ALLSRPWTGA GLRWKHTSSL KVANEPVLAF TQGSPERDAL
    60 70 80 90 100
    QKALKDLKGR MEAIPCVVGD EEVWTSDVQY QVSPFNHGHK VAKFCYADKS
    110 120 130 140 150
    LLNKAIEAAL AARKEWDLKP IADRAQIFLK AADMLSGPRR AEILAKTMVG
    160 170 180 190 200
    QGKTVIQAEI DAAAELIDFF RFNAKYAVEL EGQQPISVPP STNSTVYRGL
    210 220 230 240 250
    EGFVAAISPF NFTAIGGNLA GAPALMGNVV LWKPSDTAML ASYAVYRILR
    260 270 280 290 300
    EAGLPPNIIQ FVPADGPLFG DTVTSSEHLC GINFTGSVPT FKHLWKQVAQ
    310 320 330 340 350
    NLDRFHTFPR LAGECGGKNF HFVHRSADVE SVVSGTLRSA FEYGGQKCSA
    360 370 380 390 400
    CSRLYVPHSL WPQIKGRLLE EHSRIKVGDP AEDFGTFFSA VIDAKSFARI
    410 420 430 440 450
    KKWLEHARSS PSLTILAGGK CDDSVGYFVE PCIVESKDPQ EPIMKEEIFG
    460 470 480 490 500
    PVLSVYVYPD DKYKETLQLV DSTTSYGLTG AVFSQDKDVV QEATKVLRNA
    510 520 530 540 550
    AGNFYINDKS TGSIVGQQPF GGARASGTND KPGGPHYILR WTSPQVIKET
    560
    HKPLGDWSYA YMQ
    Length:563
    Mass (Da):61,719
    Last modified:February 1, 2005 - v3
    Checksum:i4D964771B7DB5FFD
    GO
    Isoform 2 (identifier: P30038-2) [UniParc]FASTAAdd to basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-60: Missing.

    Show »
    Length:503
    Mass (Da):55,118
    Checksum:i51F7786045941395
    GO
    Isoform 3 (identifier: P30038-3) [UniParc]FASTAAdd to basket

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

    Show »
    Length:512
    Mass (Da):56,043
    Checksum:i1AA9C976895301FE
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti68 – 681V → M in AAC50501 (PubMed:8621661).Curated
    Sequence conflicti68 – 681V → M in AAC50500 (PubMed:8621661).Curated
    Sequence conflicti189 – 1913PPS → LPY AA sequence (PubMed:8493898).Curated
    Sequence conflicti189 – 1891P → L AA sequence (PubMed:1395511).Curated
    Sequence conflicti226 – 2261M → I in BAD96206 (Ref. 4) Curated
    Sequence conflicti271 – 2711D → E AA sequence (PubMed:1395511).Curated
    Sequence conflicti271 – 2711D → E AA sequence (PubMed:8493898).Curated
    Sequence conflicti354 – 3541L → K AA sequence (PubMed:8493898).Curated
    Sequence conflicti376 – 3761K → R in BAD96206 (Ref. 4) Curated
    Sequence conflicti524 – 5263RAS → GSA AA sequence (PubMed:8493898).Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti16 – 161P → L in allele ALDH4A1*4. 1 Publication
    Corresponds to variant rs146450609 [ dbSNP | Ensembl ].
    VAR_002259
    Natural varianti352 – 3521S → L in HYRPRO2; allele ALDH4A1*3; loss of enzyme activity. 2 Publications
    VAR_002260
    Natural varianti470 – 4701V → I.2 Publications
    Corresponds to variant rs2230709 [ dbSNP | Ensembl ].
    VAR_029337
    Natural varianti473 – 4731T → A.
    Corresponds to variant rs6695033 [ dbSNP | Ensembl ].
    VAR_048903

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 6060Missing in isoform 2. 1 PublicationVSP_043785Add
    BLAST
    Alternative sequencei396 – 44651Missing in isoform 3. 1 PublicationVSP_047732Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    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.
    CCDSiCCDS188.1. [P30038-1]
    CCDS53272.1. [P30038-2]
    RefSeqiNP_001154976.1. NM_001161504.1. [P30038-2]
    NP_003739.2. NM_003748.3. [P30038-1]
    NP_733844.1. NM_170726.2. [P30038-1]
    UniGeneiHs.77448.

    Genome annotation databases

    EnsembliENST00000290597; ENSP00000290597; ENSG00000159423. [P30038-1]
    ENST00000375341; ENSP00000364490; ENSG00000159423. [P30038-1]
    ENST00000538309; ENSP00000442988; ENSG00000159423. [P30038-2]
    ENST00000538839; ENSP00000446071; ENSG00000159423. [P30038-3]
    GeneIDi8659.
    KEGGihsa:8659.
    UCSCiuc001bbb.3. human. [P30038-1]
    uc021ohl.1. human.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    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.
    CCDSiCCDS188.1. [P30038-1]
    CCDS53272.1. [P30038-2]
    RefSeqiNP_001154976.1. NM_001161504.1. [P30038-2]
    NP_003739.2. NM_003748.3. [P30038-1]
    NP_733844.1. NM_170726.2. [P30038-1]
    UniGeneiHs.77448.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    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[»]
    ProteinModelPortaliP30038.
    SMRiP30038. Positions 23-563.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    BioGridi114208. 5 interactions.
    IntActiP30038. 1 interaction.
    STRINGi9606.ENSP00000290597.

    PTM databases

    PhosphoSiteiP30038.

    Polymorphism and mutation databases

    BioMutaiALDH4A1.
    DMDMi62511241.

    2D gel databases

    OGPiP30038.
    SWISS-2DPAGEP30038.

    Proteomic databases

    MaxQBiP30038.
    PaxDbiP30038.
    PRIDEiP30038.

    Protocols and materials databases

    DNASUi8659.
    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsembliENST00000290597; ENSP00000290597; ENSG00000159423. [P30038-1]
    ENST00000375341; ENSP00000364490; ENSG00000159423. [P30038-1]
    ENST00000538309; ENSP00000442988; ENSG00000159423. [P30038-2]
    ENST00000538839; ENSP00000446071; ENSG00000159423. [P30038-3]
    GeneIDi8659.
    KEGGihsa:8659.
    UCSCiuc001bbb.3. human. [P30038-1]
    uc021ohl.1. human.

    Organism-specific databases

    CTDi8659.
    GeneCardsiGC01M019197.
    HGNCiHGNC:406. ALDH4A1.
    HPAiCAB004645.
    HPA006401.
    MIMi239510. phenotype.
    606811. gene.
    neXtProtiNX_P30038.
    Orphaneti79101. Hyperprolinemia type 2.
    PharmGKBiPA24701.
    GenAtlasiSearch...

    Phylogenomic databases

    eggNOGiCOG1012.
    GeneTreeiENSGT00560000077335.
    HOVERGENiHBG050484.
    InParanoidiP30038.
    KOiK00294.
    OMAiLTDWKYP.
    OrthoDBiEOG7T1R9D.
    PhylomeDBiP30038.
    TreeFamiTF300481.

    Enzyme and pathway databases

    UniPathwayiUPA00261; UER00374.
    BioCyciMetaCyc:HS14757-MONOMER.
    BRENDAi1.2.1.88. 2681.
    ReactomeiREACT_1002. Proline catabolism.
    SABIO-RKP30038.

    Miscellaneous databases

    ChiTaRSiALDH4A1. human.
    GeneWikiiAldehyde_dehydrogenase_4_family,_member_A1.
    GenomeRNAii8659.
    NextBioi32473.
    PROiP30038.
    SOURCEiSearch...

    Gene expression databases

    BgeeiP30038.
    CleanExiHS_ALDH4A1.
    ExpressionAtlasiP30038. baseline and differential.
    GenevisibleiP30038. HS.

    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.
    IPR005931. P5CDH/ALDH4A1.
    [Graphical view]
    PfamiPF00171. Aldedh. 1 hit.
    [Graphical view]
    SUPFAMiSSF53720. SSF53720. 1 hit.
    TIGRFAMsiTIGR01236. D1pyr5carbox1. 1 hit.
    PROSITEiPS00070. ALDEHYDE_DEHYDR_CYS. 1 hit.
    PS00687. ALDEHYDE_DEHYDR_GLU. 1 hit.
    [Graphical view]
    ProtoNetiSearch...

    Publicationsi

    « Hide 'large scale' publications
    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.
      , 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.
      , 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. 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. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    12. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
      Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
      J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-44, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Liver.
    13. "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 HYRPRO2 LEU-352, CATALYTIC ACTIVITY, FUNCTION, PATHWAY, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, ACTIVE SITE, CHARACTERIZATION OF VARIANT HYRPRO2 LEU-352, MUTAGENESIS OF SER-352.
    14. "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 HYRPRO2 LEU-352, VARIANT LEU-16.

    Entry informationi

    Entry nameiAL4A1_HUMAN
    AccessioniPrimary (citable) accession number: P30038
    Secondary accession number(s): A8K1Q7
    , B4DGE4, D2D4A3, Q16882, Q53HU4, Q5JNV6, Q8IZ38, Q96IF0, Q9UDI6
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 1, 1993
    Last sequence update: February 1, 2005
    Last modified: June 24, 2015
    This is version 164 of the entry and version 3 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, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 1
      Human chromosome 1: 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

    Similar proteinsi

    Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
    100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
    90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
    50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.