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P49419

- AL7A1_HUMAN

UniProt

P49419 - AL7A1_HUMAN

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Protein

Alpha-aminoadipic semialdehyde dehydrogenase

Gene

ALDH7A1

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

Functioni

Multifunctional enzyme mediating important protective effects. Metabolizes betaine aldehyde to betaine, an important cellular osmolyte and methyl donor. Protects cells from oxidative stress by metabolizing a number of lipid peroxidation-derived aldehydes. Involved in lysine catabolism.2 Publications

Catalytic activityi

(S)-2-amino-6-oxohexanoate + NAD(P)+ + H2O = L-2-aminoadipate + NAD(P)H.
Betaine aldehyde + NAD+ + H2O = betaine + NADH.
An aldehyde + NAD+ + H2O = a carboxylate + NADH.

Kineticsi

  1. KM=28.5 µM for nonanal1 Publication
  2. KM=5.3 µM for trans-2-nonenal1 Publication
  3. KM=39.1 µM for hexanal1 Publication
  4. KM=17.5 µM for octanal1 Publication
  5. KM=41.1 µM for betaine aldehyde1 Publication
  6. KM=169 µM for L-2-aminoadipate 6-semialdehyde1 Publication
  7. KM=530.2 µM for benzaldehyde1 Publication
  8. KM=647.4 µM for propanal1 Publication
  9. KM=7374.3 µM for glyceraldehyde1 Publication

Vmax=364.9 nmol/min/mg enzyme toward nonanal1 Publication

Vmax=34.9 nmol/min/mg enzyme toward trans-2-nonenal1 Publication

Vmax=243.3 nmol/min/mg enzyme toward hexanal1 Publication

Vmax=72.3 nmol/min/mg enzyme toward octanal1 Publication

Vmax=101.4 nmol/min/mg enzyme toward betaine aldehyde1 Publication

Vmax=276.2 nmol/min/mg enzyme toward L-2-aminoadipate 6-semialdehyde1 Publication

Vmax=125.2 nmol/min/mg enzyme toward benzaldehyde1 Publication

Vmax=69.9 nmol/min/mg enzyme toward propanal1 Publication

Vmax=174 nmol/min/mg enzyme toward glyceraldehyde1 Publication

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei195 – 1951Transition state stabilizerBy similarity
Active sitei296 – 2961Proton acceptorPROSITE-ProRule annotation
Active sitei330 – 3301Nucleophile

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi274 – 2796NADBy similarity

GO - Molecular functioni

  1. aldehyde dehydrogenase (NAD) activity Source: UniProtKB
  2. betaine-aldehyde dehydrogenase activity Source: UniProtKB-EC
  3. L-aminoadipate-semialdehyde dehydrogenase activity Source: Reactome

GO - Biological processi

  1. cellular aldehyde metabolic process Source: UniProtKB
  2. cellular nitrogen compound metabolic process Source: Reactome
  3. glycine betaine biosynthetic process from choline Source: UniProtKB-UniPathway
  4. lysine catabolic process Source: Reactome
  5. sensory perception of sound Source: ProtInc
  6. small molecule metabolic process Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

NAD

Enzyme and pathway databases

BioCyciMetaCyc:HS09157-MONOMER.
ReactomeiREACT_1298. Lysine catabolism.
SABIO-RKP49419.
UniPathwayiUPA00529; UER00386.

Names & Taxonomyi

Protein namesi
Recommended name:
Alpha-aminoadipic semialdehyde dehydrogenase (EC:1.2.1.31)
Short name:
Alpha-AASA dehydrogenase
Alternative name(s):
Aldehyde dehydrogenase family 7 member A1 (EC:1.2.1.3)
Antiquitin-1
Betaine aldehyde dehydrogenase (EC:1.2.1.8)
Delta1-piperideine-6-carboxylate dehydrogenase
Short name:
P6c dehydrogenase
Gene namesi
Name:ALDH7A1
Synonyms:ATQ1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 5

Organism-specific databases

HGNCiHGNC:877. ALDH7A1.

Subcellular locationi

Mitochondrion 1 Publication. Nucleus 1 Publication

GO - Cellular componenti

  1. cytoplasm Source: HPA
  2. extracellular vesicular exosome Source: UniProtKB
  3. mitochondrial matrix Source: Reactome
  4. mitochondrion Source: HPA
  5. nucleus Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Mitochondrion, Nucleus

Pathology & Biotechi

Involvement in diseasei

Pyridoxine-dependent epilepsy (PDE) [MIM:266100]: Characterized by a combination of various seizure types. It usually occurs in the first hours of life and is unresponsive to standard anticonvulsants, responding only to immediate administration of pyridoxine hydrochloride.2 Publications
Note: The disease is caused by mutations affecting the gene represented in this entry.
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti199 – 1991A → V in PDE. 1 Publication
VAR_031718
Natural varianti202 – 2021G → V in PDE. 1 Publication
VAR_069184
Natural varianti291 – 2911G → E in PDE. 1 Publication
VAR_069185
Natural varianti301 – 3011N → I in PDE. 1 Publication
VAR_069186
Natural varianti335 – 3351R → Q in PDE. 1 Publication
VAR_069187
Natural varianti395 – 3951V → G in PDE. 1 Publication
VAR_069188
Natural varianti427 – 4271E → Q in PDE. 2 Publications
Corresponds to variant rs121912707 [ dbSNP | Ensembl ].
VAR_031719
Natural varianti458 – 4581S → N in PDE. 1 Publication
VAR_069189

Keywords - Diseasei

Disease mutation, Epilepsy

Organism-specific databases

MIMi266100. phenotype.
Orphaneti3006. Pyridoxine-dependent epilepsy.
PharmGKBiPA24704.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 2626MitochondrionSequence AnalysisAdd
BLAST
Chaini27 – 539513Alpha-aminoadipic semialdehyde dehydrogenasePRO_0000056490Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei94 – 941N6-acetyllysine; alternateBy similarity
Modified residuei94 – 941N6-succinyllysine; alternateBy similarity
Modified residuei462 – 4621N6-acetyllysineBy similarity
Modified residuei500 – 5001N6-acetyllysineBy similarity
Modified residuei537 – 5371N6-succinyllysineBy similarity

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiP49419.
PaxDbiP49419.
PRIDEiP49419.

2D gel databases

UCD-2DPAGEP49419.

PTM databases

PhosphoSiteiP49419.

Expressioni

Tissue specificityi

Abundant in hepatoma cells and fetal cochlea, ovary, eye, heart, adrenal gland, liver and kidney. Low levels present in adult peripheral blood leukocytes and fetal brain, thymus, spleen, skeletal muscle, lung and tongue.2 Publications

Gene expression databases

BgeeiP49419.
CleanExiHS_ALDH7A1.
ExpressionAtlasiP49419. baseline and differential.
GenevestigatoriP49419.

Organism-specific databases

HPAiHPA023296.

Interactioni

Subunit structurei

Homotetramer.By similarity

Binary interactionsi

WithEntry#Exp.IntActNotes
EPS8Q129292EBI-726842,EBI-375576

Protein-protein interaction databases

BioGridi106990. 27 interactions.
IntActiP49419. 6 interactions.
MINTiMINT-1421491.
STRINGi9606.ENSP00000387123.

Structurei

Secondary structure

1
539
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi33 – 353Combined sources
Helixi37 – 459Combined sources
Beta strandi49 – 524Combined sources
Beta strandi54 – 607Combined sources
Beta strandi65 – 695Combined sources
Turni71 – 733Combined sources
Beta strandi76 – 816Combined sources
Helixi85 – 10218Combined sources
Helixi107 – 12317Combined sources
Helixi125 – 13511Combined sources
Helixi140 – 16021Combined sources
Turni161 – 1633Combined sources
Beta strandi167 – 1693Combined sources
Beta strandi176 – 1849Combined sources
Beta strandi186 – 1916Combined sources
Beta strandi194 – 1963Combined sources
Helixi199 – 21012Combined sources
Beta strandi214 – 2185Combined sources
Helixi221 – 2233Combined sources
Helixi224 – 24017Combined sources
Helixi245 – 2473Combined sources
Beta strandi248 – 2514Combined sources
Helixi255 – 2639Combined sources
Beta strandi268 – 2747Combined sources
Helixi276 – 28813Combined sources
Beta strandi292 – 2965Combined sources
Beta strandi301 – 3055Combined sources
Helixi311 – 32313Combined sources
Helixi324 – 3274Combined sources
Beta strandi333 – 3397Combined sources
Turni340 – 3423Combined sources
Helixi343 – 35513Combined sources
Helixi375 – 39016Combined sources
Beta strandi394 – 3974Combined sources
Beta strandi403 – 4075Combined sources
Beta strandi412 – 4165Combined sources
Helixi422 – 4254Combined sources
Beta strandi429 – 43810Combined sources
Helixi441 – 4499Combined sources
Beta strandi455 – 4606Combined sources
Helixi464 – 4718Combined sources
Beta strandi478 – 4858Combined sources
Beta strandi494 – 4963Combined sources
Helixi500 – 5023Combined sources
Beta strandi507 – 5093Combined sources
Helixi512 – 5165Combined sources
Beta strandi517 – 5259Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2J6LX-ray1.30A/B/C/D/E/F/G/H30-527[»]
ProteinModelPortaliP49419.
SMRiP49419. Positions 30-527.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP49419.

Family & Domainsi

Sequence similaritiesi

Belongs to the aldehyde dehydrogenase family.Curated

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiCOG1012.
GeneTreeiENSGT00760000118999.
HOGENOMiHOG000271511.
HOVERGENiHBG050485.
InParanoidiP49419.
KOiK14085.
OMAiKGIQTIR.
OrthoDBiEOG78D7JV.
PhylomeDBiP49419.
TreeFamiTF300388.

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.
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.
PROSITEiPS00687. ALDEHYDE_DEHYDR_GLU. 1 hit.
[Graphical view]

Sequences (4)i

Sequence statusi: Complete.

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

This entry describes 4 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: P49419-1) [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
MWRLPRALCV HAAKTSKLSG PWSRPAAFMS TLLINQPQYA WLKELGLREE
60 70 80 90 100
NEGVYNGSWG GRGEVITTYC PANNEPIARV RQASVADYEE TVKKAREAWK
110 120 130 140 150
IWADIPAPKR GEIVRQIGDA LREKIQVLGS LVSLEMGKIL VEGVGEVQEY
160 170 180 190 200
VDICDYAVGL SRMIGGPILP SERSGHALIE QWNPVGLVGI ITAFNFPVAV
210 220 230 240 250
YGWNNAIAMI CGNVCLWKGA PTTSLISVAV TKIIAKVLED NKLPGAICSL
260 270 280 290 300
TCGGADIGTA MAKDERVNLL SFTGSTQVGK QVGLMVQERF GRSLLELGGN
310 320 330 340 350
NAIIAFEDAD LSLVVPSALF AAVGTAGQRC TTARRLFIHE SIHDEVVNRL
360 370 380 390 400
KKAYAQIRVG NPWDPNVLYG PLHTKQAVSM FLGAVEEAKK EGGTVVYGGK
410 420 430 440 450
VMDRPGNYVE PTIVTGLGHD ASIAHTETFA PILYVFKFKN EEEVFAWNNE
460 470 480 490 500
VKQGLSSSIF TKDLGRIFRW LGPKGSDCGI VNVNIPTSGA EIGGAFGGEK
510 520 530
HTGGGRESGS DAWKQYMRRS TCTINYSKDL PLAQGIKFQ
Length:539
Mass (Da):58,487
Last modified:April 20, 2010 - v5
Checksum:i05385562F71312B6
GO
Isoform 2 (identifier: P49419-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-28: Missing.

Show »
Length:511
Mass (Da):55,366
Checksum:i08F6F7672C948E2C
GO
Isoform 3 (identifier: P49419-3) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     31-222: Missing.

Note: No experimental confirmation available.

Show »
Length:347
Mass (Da):37,409
Checksum:i257FE6E3EE6C0387
GO
Isoform 4 (identifier: P49419-4) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-1: M → MGSPGRGAGLYFSSSQGLGLIPSPGLSM
     337-400: Missing.

Note: No experimental confirmation available.

Show »
Length:502
Mass (Da):53,987
Checksum:i031B6A8D8BB67F5A
GO

Sequence cautioni

The sequence AAC51935.1 differs from that shown. Reason: Frameshift at positions 233 and 268. Curated
The sequence AAH02515.3 differs from that shown. Reason: Erroneous initiation. Curated
The sequence AAH71712.1 differs from that shown. Reason: Erroneous initiation. Curated
The sequence AAH73174.1 differs from that shown. Reason: Erroneous initiation. Curated
The sequence BAG35366.1 differs from that shown. Reason: Erroneous initiation. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti236 – 2361K → R in BAG59812. (PubMed:14702039)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti199 – 1991A → V in PDE. 1 Publication
VAR_031718
Natural varianti202 – 2021G → V in PDE. 1 Publication
VAR_069184
Natural varianti291 – 2911G → E in PDE. 1 Publication
VAR_069185
Natural varianti301 – 3011N → I in PDE. 1 Publication
VAR_069186
Natural varianti335 – 3351R → Q in PDE. 1 Publication
VAR_069187
Natural varianti395 – 3951V → G in PDE. 1 Publication
VAR_069188
Natural varianti412 – 4121T → A.
Corresponds to variant rs2306618 [ dbSNP | Ensembl ].
VAR_028202
Natural varianti427 – 4271E → Q in PDE. 2 Publications
Corresponds to variant rs121912707 [ dbSNP | Ensembl ].
VAR_031719
Natural varianti439 – 4391K → Q.1 Publication
Corresponds to variant rs12514417 [ dbSNP | Ensembl ].
VAR_028203
Natural varianti458 – 4581S → N in PDE. 1 Publication
VAR_069189

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 2828Missing in isoform 2. 1 PublicationVSP_038987Add
BLAST
Alternative sequencei1 – 11M → MGSPGRGAGLYFSSSQGLGL IPSPGLSM in isoform 4. 1 PublicationVSP_045904
Alternative sequencei31 – 222192Missing in isoform 3. 1 PublicationVSP_038988Add
BLAST
Alternative sequencei337 – 40064Missing in isoform 4. 1 PublicationVSP_045905Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
S74728 mRNA. Translation: AAB31966.1.
AK312459 mRNA. Translation: BAG35366.1. Different initiation.
AK295526 mRNA. Translation: BAG58439.1.
AK297365 mRNA. Translation: BAG59812.1.
AC093535 Genomic DNA. No translation available.
AC099513 Genomic DNA. No translation available.
BC002515 mRNA. Translation: AAH02515.3. Different initiation.
BC071712 mRNA. Translation: AAH71712.1. Different initiation.
BC073174 mRNA. Translation: AAH73174.1. Different initiation.
AF002696 Genomic DNA. Translation: AAC51935.1. Sequence problems.
CCDSiCCDS4137.2. [P49419-1]
CCDS56380.1. [P49419-4]
PIRiA54676.
RefSeqiNP_001173.2. NM_001182.4. [P49419-1]
NP_001188306.1. NM_001201377.1. [P49419-2]
NP_001189333.1. NM_001202404.1. [P49419-4]
UniGeneiHs.483239.

Genome annotation databases

EnsembliENST00000409134; ENSP00000387123; ENSG00000164904. [P49419-1]
ENST00000447989; ENSP00000414132; ENSG00000164904. [P49419-4]
GeneIDi501.
KEGGihsa:501.
UCSCiuc003ktx.3. human. [P49419-1]

Polymorphism databases

DMDMi294862544.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
S74728 mRNA. Translation: AAB31966.1 .
AK312459 mRNA. Translation: BAG35366.1 . Different initiation.
AK295526 mRNA. Translation: BAG58439.1 .
AK297365 mRNA. Translation: BAG59812.1 .
AC093535 Genomic DNA. No translation available.
AC099513 Genomic DNA. No translation available.
BC002515 mRNA. Translation: AAH02515.3 . Different initiation.
BC071712 mRNA. Translation: AAH71712.1 . Different initiation.
BC073174 mRNA. Translation: AAH73174.1 . Different initiation.
AF002696 Genomic DNA. Translation: AAC51935.1 . Sequence problems.
CCDSi CCDS4137.2. [P49419-1 ]
CCDS56380.1. [P49419-4 ]
PIRi A54676.
RefSeqi NP_001173.2. NM_001182.4. [P49419-1 ]
NP_001188306.1. NM_001201377.1. [P49419-2 ]
NP_001189333.1. NM_001202404.1. [P49419-4 ]
UniGenei Hs.483239.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2J6L X-ray 1.30 A/B/C/D/E/F/G/H 30-527 [» ]
ProteinModelPortali P49419.
SMRi P49419. Positions 30-527.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 106990. 27 interactions.
IntActi P49419. 6 interactions.
MINTi MINT-1421491.
STRINGi 9606.ENSP00000387123.

PTM databases

PhosphoSitei P49419.

Polymorphism databases

DMDMi 294862544.

2D gel databases

UCD-2DPAGE P49419.

Proteomic databases

MaxQBi P49419.
PaxDbi P49419.
PRIDEi P49419.

Protocols and materials databases

DNASUi 501.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000409134 ; ENSP00000387123 ; ENSG00000164904 . [P49419-1 ]
ENST00000447989 ; ENSP00000414132 ; ENSG00000164904 . [P49419-4 ]
GeneIDi 501.
KEGGi hsa:501.
UCSCi uc003ktx.3. human. [P49419-1 ]

Organism-specific databases

CTDi 501.
GeneCardsi GC05M125877.
GeneReviewsi ALDH7A1.
HGNCi HGNC:877. ALDH7A1.
HPAi HPA023296.
MIMi 107323. gene.
266100. phenotype.
neXtProti NX_P49419.
Orphaneti 3006. Pyridoxine-dependent epilepsy.
PharmGKBi PA24704.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG1012.
GeneTreei ENSGT00760000118999.
HOGENOMi HOG000271511.
HOVERGENi HBG050485.
InParanoidi P49419.
KOi K14085.
OMAi KGIQTIR.
OrthoDBi EOG78D7JV.
PhylomeDBi P49419.
TreeFami TF300388.

Enzyme and pathway databases

UniPathwayi UPA00529 ; UER00386 .
BioCyci MetaCyc:HS09157-MONOMER.
Reactomei REACT_1298. Lysine catabolism.
SABIO-RK P49419.

Miscellaneous databases

ChiTaRSi ALDH7A1. human.
EvolutionaryTracei P49419.
GeneWikii ALDH7A1.
GenomeRNAii 501.
NextBioi 2097.
PROi P49419.
SOURCEi Search...

Gene expression databases

Bgeei P49419.
CleanExi HS_ALDH7A1.
ExpressionAtlasi P49419. baseline and differential.
Genevestigatori P49419.

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.
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 PS00687. ALDEHYDE_DEHYDR_GLU. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Homology between a human protein and a protein of the green garden pea."
    Lee P., Kuhl W., Gelbart T., Kamimura T., West C., Beutler E.
    Genomics 21:371-378(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), TISSUE SPECIFICITY.
    Tissue: Kidney, Liver and Placenta.
  2. "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; 3 AND 4).
    Tissue: Brain, Caudate nucleus and Hippocampus.
  3. "The DNA sequence and comparative analysis of human chromosome 5."
    Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S., Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M., She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S.
    , Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., Gomez M., Gonzales E., Goodstein D., Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Lopez F., Lou Y., Martinez D., Medina C., Morgan J., Nandkeshwar R., Noonan J.P., Pitluck S., Pollard M., Predki P., Priest J., Ramirez L., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J., Dickson M., Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A., Rokhsar D.S., Richardson P., Lucas S.M., Myers R.M., Rubin E.M.
    Nature 431:268-274(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. "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] (ISOFORM 1), VARIANT GLN-439.
    Tissue: Placenta and Uterus.
  5. "An ancient conserved gene expressed in the human inner ear: identification, expression analysis, and chromosomal mapping of human and mouse antiquitin (ATQ1)."
    Skvorak A.B., Robertson N.G., Yin Y., Weremowicz S., Her H., Bieber F.R., Beisel K.W., Lynch E.D., Beier D.R., Morton C.C.
    Genomics 46:191-199(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 233-268, TISSUE SPECIFICITY.
  6. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
    Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
    Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  7. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  8. "Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
    Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
    Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  9. "Aldehyde dehydrogenase 7A1 (ALDH7A1) is a novel enzyme involved in cellular defense against hyperosmotic stress."
    Brocker C., Lassen N., Estey T., Pappa A., Cantore M., Orlova V.V., Chavakis T., Kavanagh K.L., Oppermann U., Vasiliou V.
    J. Biol. Chem. 285:18452-18463(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.3 ANGSTROMS) OF 30-526, FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, ALTERNATIVE SPLICING, SUBCELLULAR LOCATION.
  10. Cited for: VARIANTS PDE VAL-199 AND GLN-427, FUNCTION.
  11. "Biochemical and molecular characterization of 18 patients with pyridoxine-dependent epilepsy and mutations of the antiquitin (ALDH7A1) gene."
    Plecko B., Paul K., Paschke E., Stoeckler-Ipsiroglu S., Struys E., Jakobs C., Hartmann H., Luecke T., di Capua M., Korenke C., Hikel C., Reutershahn E., Freilinger M., Baumeister F., Bosch F., Erwa W.
    Hum. Mutat. 28:19-26(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS PDE VAL-202; GLU-291; ILE-301; GLN-335; GLY-395; GLN-427 AND ASN-458.

Entry informationi

Entry nameiAL7A1_HUMAN
AccessioniPrimary (citable) accession number: P49419
Secondary accession number(s): B2R669
, B4DIC7, B4DMA0, E7EPT3, O14619, Q6IPU8, Q9BUL4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: April 20, 2010
Last modified: October 29, 2014
This is version 155 of the entry and version 5 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, Reference proteome

Documents

  1. Human chromosome 5
    Human chromosome 5: 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