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P30038

- AL4A1_HUMAN

UniProt

P30038 - AL4A1_HUMAN

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Protein

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

Gene

ALDH4A1

Organism
Homo sapiens (Human)
Status
Reviewed - 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

Pathwayi

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 – 3481Nucleophile1 PublicationPROSITE-ProRule annotation
Binding sitei447 – 4471NADBy similarity
Binding sitei513 – 5131SubstrateBy similarity

Regions

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

GO - Molecular functioni

  1. 1-pyrroline-5-carboxylate dehydrogenase activity Source: Reactome
  2. aldehyde dehydrogenase (NAD) activity Source: ProtInc
  3. electron carrier activity Source: UniProtKB
  4. identical protein binding Source: IntAct

GO - Biological processi

  1. 4-hydroxyproline catabolic process Source: BHF-UCL
  2. cellular nitrogen compound metabolic process Source: Reactome
  3. glutamate biosynthetic process Source: InterPro
  4. proline biosynthetic process Source: InterPro
  5. proline catabolic process Source: Reactome
  6. proline catabolic process to glutamate Source: UniProtKB-UniPathway
  7. proline metabolic process Source: ProtInc
  8. small molecule metabolic process Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Proline metabolism

Keywords - Ligandi

NAD

Enzyme and pathway databases

BioCyciMetaCyc:HS14757-MONOMER.
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: Chromosome 1

Organism-specific databases

HGNCiHGNC:406. ALDH4A1.

Subcellular locationi

GO - Cellular componenti

  1. mitochondrial matrix Source: Reactome
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

Pathology & Biotechi

Involvement in diseasei

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.1 Publication
Note: The disease is caused by mutations affecting the gene represented in this entry.
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti352 – 3521S → L in HP-2; allele ALDH4A1*3; loss of enzyme activity. 1 Publication
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.

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 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

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.
GenevestigatoriP30038.

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
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.
OMAiLRWKHTS.
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. Align

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. 1 PublicationCurated
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. 1 PublicationCurated
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 HP-2; allele ALDH4A1*3; loss of enzyme activity. 1 Publication
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.

Polymorphism databases

DMDMi62511241.

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 .
CCDSi CCDS188.1. [P30038-1 ]
CCDS53272.1. [P30038-2 ]
RefSeqi NP_001154976.1. NM_001161504.1. [P30038-2 ]
NP_003739.2. NM_003748.3. [P30038-1 ]
NP_733844.1. NM_170726.2. [P30038-1 ]
UniGenei Hs.77448.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
3V9G X-ray 2.50 A/B/C/D 18-563 [» ]
3V9H X-ray 2.40 A/B/C/D 18-563 [» ]
3V9I X-ray 2.85 A/B/C/D 18-563 [» ]
4OE5 X-ray 1.95 A/B/C/D 18-563 [» ]
ProteinModelPortali P30038.
SMRi P30038. Positions 23-563.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 114208. 5 interactions.
IntActi P30038. 1 interaction.
STRINGi 9606.ENSP00000290597.

PTM databases

PhosphoSitei P30038.

Polymorphism databases

DMDMi 62511241.

2D gel databases

OGPi P30038.
SWISS-2DPAGE P30038.

Proteomic databases

MaxQBi P30038.
PaxDbi P30038.
PRIDEi P30038.

Protocols and materials databases

DNASUi 8659.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000290597 ; ENSP00000290597 ; ENSG00000159423 . [P30038-1 ]
ENST00000375341 ; ENSP00000364490 ; ENSG00000159423 . [P30038-1 ]
ENST00000538309 ; ENSP00000442988 ; ENSG00000159423 . [P30038-2 ]
ENST00000538839 ; ENSP00000446071 ; ENSG00000159423 . [P30038-3 ]
GeneIDi 8659.
KEGGi hsa:8659.
UCSCi uc001bbb.3. human. [P30038-1 ]
uc021ohl.1. human.

Organism-specific databases

CTDi 8659.
GeneCardsi GC01M019197.
HGNCi HGNC:406. ALDH4A1.
HPAi CAB004645.
HPA006401.
MIMi 239510. phenotype.
606811. gene.
neXtProti NX_P30038.
Orphaneti 79101. Hyperprolinemia type 2.
PharmGKBi PA24701.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG1012.
GeneTreei ENSGT00560000077335.
HOVERGENi HBG050484.
InParanoidi P30038.
KOi K00294.
OMAi LRWKHTS.
OrthoDBi EOG7T1R9D.
PhylomeDBi P30038.
TreeFami TF300481.

Enzyme and pathway databases

UniPathwayi UPA00261 ; UER00374 .
BioCyci MetaCyc:HS14757-MONOMER.
Reactomei REACT_1002. Proline catabolism.
SABIO-RK P30038.

Miscellaneous databases

ChiTaRSi ALDH4A1. human.
GeneWikii Aldehyde_dehydrogenase_4_family,_member_A1.
GenomeRNAii 8659.
NextBioi 32473.
PROi P30038.
SOURCEi Search...

Gene expression databases

Bgeei P30038.
CleanExi HS_ALDH4A1.
ExpressionAtlasi P30038. baseline and differential.
Genevestigatori P30038.

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.
IPR005931. P5CDH/ALDH4A1.
[Graphical view ]
Pfami PF00171. Aldedh. 1 hit.
[Graphical view ]
SUPFAMi SSF53720. SSF53720. 1 hit.
TIGRFAMsi TIGR01236. D1pyr5carbox1. 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. "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. "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.

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: November 26, 2014
This is version 158 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