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P49419 (AL7A1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 152. 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:
Alpha-aminoadipic semialdehyde dehydrogenase

Short name=Alpha-AASA dehydrogenase
EC=1.2.1.31
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 names
Name:ALDH7A1
Synonyms:ATQ1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length539 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.9 Ref.10

Catalytic activity

(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.

Pathway

Amine and polyamine biosynthesis; betaine biosynthesis via choline pathway; betaine from betaine aldehyde: step 1/1.

Subunit structure

Homotetramer By similarity.

Subcellular location

Mitochondrion. Nucleus Ref.9.

Isoform 2: Cytoplasmcytosol Ref.9.

Tissue specificity

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. Ref.1 Ref.5

Involvement in disease

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.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.10 Ref.11

Sequence similarities

Belongs to the aldehyde dehydrogenase family.

Biophysicochemical properties

Kinetic parameters:

KM=28.5 µM for nonanal Ref.9

KM=5.3 µM for trans-2-nonenal

KM=39.1 µM for hexanal

KM=17.5 µM for octanal

KM=41.1 µM for betaine aldehyde

KM=169 µM for L-2-aminoadipate 6-semialdehyde

KM=530.2 µM for benzaldehyde

KM=647.4 µM for propanal

KM=7374.3 µM for glyceraldehyde

Vmax=364.9 nmol/min/mg enzyme toward nonanal

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

Vmax=243.3 nmol/min/mg enzyme toward hexanal

Vmax=72.3 nmol/min/mg enzyme toward octanal

Vmax=101.4 nmol/min/mg enzyme toward betaine aldehyde

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

Vmax=125.2 nmol/min/mg enzyme toward benzaldehyde

Vmax=69.9 nmol/min/mg enzyme toward propanal

Vmax=174 nmol/min/mg enzyme toward glyceraldehyde

Sequence caution

The sequence AAC51935.1 differs from that shown. Reason: Frameshift at positions 233 and 268.

The sequence AAH02515.3 differs from that shown. Reason: Erroneous initiation.

The sequence AAH71712.1 differs from that shown. Reason: Erroneous initiation.

The sequence AAH73174.1 differs from that shown. Reason: Erroneous initiation.

The sequence BAG35366.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
   Cellular componentCytoplasm
Mitochondrion
Nucleus
   Coding sequence diversityAlternative splicing
Polymorphism
   DiseaseDisease mutation
Epilepsy
   DomainTransit peptide
   LigandNAD
   Molecular functionOxidoreductase
   PTMAcetylation
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcellular aldehyde metabolic process

Inferred from sequence or structural similarity. Source: UniProtKB

cellular nitrogen compound metabolic process

Traceable author statement. Source: Reactome

glycine betaine biosynthetic process from choline

Inferred from electronic annotation. Source: UniProtKB-UniPathway

lysine catabolic process

Traceable author statement. Source: Reactome

sensory perception of sound

Traceable author statement Ref.5. Source: ProtInc

small molecule metabolic process

Traceable author statement. Source: Reactome

   Cellular_componentcytoplasm

Inferred from direct assay. Source: HPA

cytosol

Inferred from electronic annotation. Source: UniProtKB-SubCell

mitochondrial matrix

Traceable author statement. Source: Reactome

mitochondrion

Inferred from direct assay. Source: HPA

nucleus

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionL-aminoadipate-semialdehyde dehydrogenase activity

Inferred from experiment. Source: Reactome

aldehyde dehydrogenase (NAD) activity

Inferred from sequence or structural similarity. Source: UniProtKB

betaine-aldehyde dehydrogenase activity

Inferred from electronic annotation. Source: UniProtKB-EC

protein binding

Inferred from physical interaction PubMed 21988832. Source: IntAct

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

EPS8Q129292EBI-726842,EBI-375576

Alternative products

This entry describes 4 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P49419-1)

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: P49419-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-28: Missing.
Isoform 3 (identifier: P49419-3)

The sequence of this isoform differs from the canonical sequence as follows:
     31-222: Missing.
Note: No experimental confirmation available.
Isoform 4 (identifier: P49419-4)

The sequence of this isoform differs from the canonical sequence as follows:
     1-1: M → MGSPGRGAGLYFSSSQGLGLIPSPGLSM
     337-400: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 2626Mitochondrion Potential
Chain27 – 539513Alpha-aminoadipic semialdehyde dehydrogenase
PRO_0000056490

Regions

Nucleotide binding274 – 2796NAD By similarity

Sites

Active site2961Proton acceptor By similarity
Active site3301Nucleophile
Site1951Transition state stabilizer By similarity

Amino acid modifications

Modified residue941N6-acetyllysine; alternate By similarity
Modified residue941N6-succinyllysine; alternate By similarity
Modified residue4621N6-acetyllysine By similarity
Modified residue5001N6-acetyllysine By similarity
Modified residue5371N6-succinyllysine By similarity

Natural variations

Alternative sequence1 – 2828Missing in isoform 2.
VSP_038987
Alternative sequence11M → MGSPGRGAGLYFSSSQGLGL IPSPGLSM in isoform 4.
VSP_045904
Alternative sequence31 – 222192Missing in isoform 3.
VSP_038988
Alternative sequence337 – 40064Missing in isoform 4.
VSP_045905
Natural variant1991A → V in PDE. Ref.10
VAR_031718
Natural variant2021G → V in PDE. Ref.11
VAR_069184
Natural variant2911G → E in PDE. Ref.11
VAR_069185
Natural variant3011N → I in PDE. Ref.11
VAR_069186
Natural variant3351R → Q in PDE. Ref.11
VAR_069187
Natural variant3951V → G in PDE. Ref.11
VAR_069188
Natural variant4121T → A.
Corresponds to variant rs2306618 [ dbSNP | Ensembl ].
VAR_028202
Natural variant4271E → Q in PDE. Ref.10 Ref.11
Corresponds to variant rs121912707 [ dbSNP | Ensembl ].
VAR_031719
Natural variant4391K → Q. Ref.4
Corresponds to variant rs12514417 [ dbSNP | Ensembl ].
VAR_028203
Natural variant4581S → N in PDE. Ref.11
VAR_069189

Experimental info

Sequence conflict2361K → R in BAG59812. Ref.2

Secondary structure

........................................................................................ 539
Helix Strand Turn

Details...

Sequences

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

Last modified April 20, 2010. Version 5.
Checksum: 05385562F71312B6

FASTA53958,487
        10         20         30         40         50         60 
MWRLPRALCV HAAKTSKLSG PWSRPAAFMS TLLINQPQYA WLKELGLREE NEGVYNGSWG 

        70         80         90        100        110        120 
GRGEVITTYC PANNEPIARV RQASVADYEE TVKKAREAWK IWADIPAPKR GEIVRQIGDA 

       130        140        150        160        170        180 
LREKIQVLGS LVSLEMGKIL VEGVGEVQEY VDICDYAVGL SRMIGGPILP SERSGHALIE 

       190        200        210        220        230        240 
QWNPVGLVGI ITAFNFPVAV YGWNNAIAMI CGNVCLWKGA PTTSLISVAV TKIIAKVLED 

       250        260        270        280        290        300 
NKLPGAICSL TCGGADIGTA MAKDERVNLL SFTGSTQVGK QVGLMVQERF GRSLLELGGN 

       310        320        330        340        350        360 
NAIIAFEDAD LSLVVPSALF AAVGTAGQRC TTARRLFIHE SIHDEVVNRL KKAYAQIRVG 

       370        380        390        400        410        420 
NPWDPNVLYG PLHTKQAVSM FLGAVEEAKK EGGTVVYGGK VMDRPGNYVE PTIVTGLGHD 

       430        440        450        460        470        480 
ASIAHTETFA PILYVFKFKN EEEVFAWNNE VKQGLSSSIF TKDLGRIFRW LGPKGSDCGI 

       490        500        510        520        530 
VNVNIPTSGA EIGGAFGGEK HTGGGRESGS DAWKQYMRRS TCTINYSKDL PLAQGIKFQ 

« Hide

Isoform 2 [UniParc].

Checksum: 08F6F7672C948E2C
Show »

FASTA51155,366
Isoform 3 [UniParc].

Checksum: 257FE6E3EE6C0387
Show »

FASTA34737,409
Isoform 4 [UniParc].

Checksum: 031B6A8D8BB67F5A
Show »

FASTA50253,987

References

« Hide 'large scale' references
[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. 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; 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. expand/collapse author list , 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]"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].
[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]"Mutations in antiquitin in individuals with pyridoxine-dependent seizures."
Mills P.B., Struys E., Jakobs C., Plecko B., Baxter P., Baumgartner M., Willemsen M.A.A.P., Omran H., Tacke U., Uhlenberg B., Weschke B., Clayton P.T.
Nat. Med. 12:307-309(2006) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS4137.2. [P49419-1]
CCDS56380.1. [P49419-4]
PIRA54676.
RefSeqNP_001173.2. NM_001182.4. [P49419-1]
NP_001188306.1. NM_001201377.1. [P49419-2]
NP_001189333.1. NM_001202404.1. [P49419-4]
UniGeneHs.483239.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2J6LX-ray1.30A/B/C/D/E/F/G/H30-527[»]
ProteinModelPortalP49419.
SMRP49419. Positions 30-527.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid106990. 24 interactions.
IntActP49419. 6 interactions.
MINTMINT-1421491.
STRING9606.ENSP00000387123.

Chemistry

DrugBankDB00157. NADH.
DB00165. Pyridoxine.

PTM databases

PhosphoSiteP49419.

Polymorphism databases

DMDM294862544.

2D gel databases

UCD-2DPAGEP49419.

Proteomic databases

MaxQBP49419.
PaxDbP49419.
PRIDEP49419.

Protocols and materials databases

DNASU501.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000409134; ENSP00000387123; ENSG00000164904. [P49419-1]
ENST00000447989; ENSP00000414132; ENSG00000164904. [P49419-4]
GeneID501.
KEGGhsa:501.
UCSCuc003ktx.3. human. [P49419-1]

Organism-specific databases

CTD501.
GeneCardsGC05M125877.
GeneReviewsALDH7A1.
HGNCHGNC:877. ALDH7A1.
HPAHPA023296.
MIM107323. gene.
266100. phenotype.
neXtProtNX_P49419.
Orphanet3006. Pyridoxine-dependent epilepsy.
PharmGKBPA24704.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG1012.
HOGENOMHOG000271511.
HOVERGENHBG050485.
InParanoidP49419.
KOK14085.
OMAKGIQTIR.
OrthoDBEOG78D7JV.
PhylomeDBP49419.
TreeFamTF300388.

Enzyme and pathway databases

BioCycMetaCyc:HS09157-MONOMER.
ReactomeREACT_111217. Metabolism.
SABIO-RKP49419.
UniPathwayUPA00529; UER00386.

Gene expression databases

ArrayExpressP49419.
BgeeP49419.
CleanExHS_ALDH7A1.
GenevestigatorP49419.

Family and domain databases

Gene3D3.40.309.10. 1 hit.
3.40.605.10. 1 hit.
InterProIPR016161. Ald_DH/histidinol_DH.
IPR016163. Ald_DH_C.
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.
PROSITEPS00687. ALDEHYDE_DEHYDR_GLU. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSALDH7A1. human.
EvolutionaryTraceP49419.
GeneWikiALDH7A1.
GenomeRNAi501.
NextBio2097.
PROP49419.
SOURCESearch...

Entry information

Entry nameAL7A1_HUMAN
AccessionPrimary (citable) accession number: P49419
Secondary accession number(s): B2R669 expand/collapse secondary AC list , B4DIC7, B4DMA0, E7EPT3, O14619, Q6IPU8, Q9BUL4
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: April 20, 2010
Last modified: July 9, 2014
This is version 152 of the entry and version 5 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 5

Human chromosome 5: entries, gene names and cross-references to MIM