Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Retinal dehydrogenase 1

Gene

ALDH1A1

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

Functioni

Binds free retinal and cellular retinol-binding protein-bound retinal. Can convert/oxidize retinaldehyde to retinoic acid (By similarity).By similarity

Catalytic activityi

Retinal + NAD+ + H2O = retinoate + NADH.

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei170 – 1701Transition state stabilizerBy similarity
Active sitei269 – 2691Proton acceptorPROSITE-ProRule annotation1 Publication
Active sitei303 – 3031NucleophilePROSITE-ProRule annotation1 Publication
Binding sitei456 – 4561NAD

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi246 – 2516NADBy similarity

GO - Molecular functioni

  1. 3-chloroallyl aldehyde dehydrogenase activity Source: GO_Central
  2. aldehyde dehydrogenase (NAD) activity Source: Reactome
  3. androgen binding Source: ProtInc
  4. benzaldehyde dehydrogenase (NAD+) activity Source: GO_Central
  5. Ras GTPase activator activity Source: UniProtKB
  6. retinal dehydrogenase activity Source: GO_Central

GO - Biological processi

  1. cellular aldehyde metabolic process Source: ProtInc
  2. ethanol oxidation Source: Reactome
  3. positive regulation of Ras GTPase activity Source: GOC
  4. retinol metabolic process Source: UniProtKB-UniPathway
  5. small molecule metabolic process Source: Reactome
  6. xenobiotic metabolic process Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

NAD

Enzyme and pathway databases

BioCyciMetaCyc:HS09183-MONOMER.
ReactomeiREACT_268561. RA biosynthesis pathway.
REACT_34. Ethanol oxidation.
SABIO-RKP00352.
UniPathwayiUPA00912.

Names & Taxonomyi

Protein namesi
Recommended name:
Retinal dehydrogenase 1 (EC:1.2.1.36)
Short name:
RALDH 1
Short name:
RalDH1
Alternative name(s):
ALDH-E1
ALHDII
Aldehyde dehydrogenase family 1 member A1
Aldehyde dehydrogenase, cytosolic
Gene namesi
Name:ALDH1A1
Synonyms:ALDC, ALDH1, PUMB1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 9

Organism-specific databases

HGNCiHGNC:402. ALDH1A1.

Subcellular locationi

GO - Cellular componenti

  1. cytoplasm Source: ProtInc
  2. cytosol Source: Reactome
  3. extracellular vesicular exosome Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA24692.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed2 Publications
Chaini2 – 501500Retinal dehydrogenase 1PRO_0000056415Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserine2 Publications
Modified residuei91 – 911N6-acetyllysine1 Publication
Modified residuei128 – 1281N6-acetyllysine1 Publication
Modified residuei252 – 2521N6-acetyllysine1 Publication
Modified residuei337 – 3371Phosphothreonine1 Publication
Modified residuei353 – 3531N6-acetyllysine1 Publication
Modified residuei367 – 3671N6-acetyllysine1 Publication
Modified residuei410 – 4101N6-acetyllysine1 Publication
Modified residuei413 – 4131Phosphoserine1 Publication
Modified residuei419 – 4191N6-acetyllysine1 Publication
Modified residuei435 – 4351N6-acetyllysine1 Publication
Modified residuei495 – 4951N6-acetyllysine1 Publication

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiP00352.
PaxDbiP00352.
PeptideAtlasiP00352.
PRIDEiP00352.

2D gel databases

DOSAC-COBS-2DPAGEP00352.
REPRODUCTION-2DPAGEIPI00218914.
P00352.
SWISS-2DPAGEP00352.
UCD-2DPAGEP00352.

PTM databases

PhosphoSiteiP00352.

Expressioni

Gene expression databases

BgeeiP00352.
CleanExiHS_ALDH1A1.
ExpressionAtlasiP00352. baseline and differential.
GenevestigatoriP00352.

Organism-specific databases

HPAiCAB020690.
HPA002123.

Interactioni

Subunit structurei

Homotetramer.

Protein-protein interaction databases

BioGridi106718. 8 interactions.
IntActiP00352. 6 interactions.
MINTiMINT-4999613.
STRINGi9606.ENSP00000297785.

Structurei

Secondary structure

1
501
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi22 – 254Combined sources
Beta strandi28 – 303Combined sources
Beta strandi37 – 415Combined sources
Turni43 – 453Combined sources
Beta strandi48 – 536Combined sources
Helixi57 – 7115Combined sources
Helixi76 – 794Combined sources
Helixi82 – 9817Combined sources
Helixi100 – 11112Combined sources
Helixi115 – 1206Combined sources
Helixi122 – 13615Combined sources
Helixi137 – 1393Combined sources
Beta strandi148 – 15912Combined sources
Beta strandi162 – 1665Combined sources
Beta strandi169 – 1713Combined sources
Helixi172 – 18514Combined sources
Beta strandi189 – 1935Combined sources
Helixi200 – 21213Combined sources
Beta strandi218 – 2214Combined sources
Turni226 – 2283Combined sources
Helixi229 – 2357Combined sources
Beta strandi241 – 2466Combined sources
Helixi248 – 26013Combined sources
Beta strandi265 – 2695Combined sources
Beta strandi275 – 2784Combined sources
Helixi284 – 29613Combined sources
Helixi297 – 3004Combined sources
Beta strandi308 – 3125Combined sources
Helixi313 – 32715Combined sources
Helixi348 – 36316Combined sources
Beta strandi367 – 3704Combined sources
Beta strandi373 – 3797Combined sources
Beta strandi385 – 3895Combined sources
Helixi395 – 3984Combined sources
Beta strandi403 – 41210Combined sources
Helixi414 – 4229Combined sources
Beta strandi428 – 4336Combined sources
Helixi437 – 44610Combined sources
Beta strandi450 – 4556Combined sources
Helixi470 – 4723Combined sources
Beta strandi473 – 4753Combined sources
Helixi479 – 4835Combined sources
Helixi484 – 4863Combined sources
Beta strandi487 – 4959Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4WB9X-ray2.07A1-501[»]
4WJ9X-ray1.74A1-501[»]
ProteinModelPortaliP00352.
SMRiP00352. Positions 8-501.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the aldehyde dehydrogenase family.Curated

Phylogenomic databases

eggNOGiCOG1012.
HOGENOMiHOG000271505.
HOVERGENiHBG000097.
InParanoidiP00352.
KOiK07249.
OMAiVEFAHIG.
OrthoDBiEOG7PS1F7.
PhylomeDBiP00352.
TreeFamiTF300455.

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.
[Graphical view]
PfamiPF00171. Aldedh. 1 hit.
[Graphical view]
SUPFAMiSSF53720. SSF53720. 1 hit.
PROSITEiPS00070. ALDEHYDE_DEHYDR_CYS. 1 hit.
PS00687. ALDEHYDE_DEHYDR_GLU. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P00352-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSSSGTPDLP VLLTDLKIQY TKIFINNEWH DSVSGKKFPV FNPATEEELC
60 70 80 90 100
QVEEGDKEDV DKAVKAARQA FQIGSPWRTM DASERGRLLY KLADLIERDR
110 120 130 140 150
LLLATMESMN GGKLYSNAYL NDLAGCIKTL RYCAGWADKI QGRTIPIDGN
160 170 180 190 200
FFTYTRHEPI GVCGQIIPWN FPLVMLIWKI GPALSCGNTV VVKPAEQTPL
210 220 230 240 250
TALHVASLIK EAGFPPGVVN IVPGYGPTAG AAISSHMDID KVAFTGSTEV
260 270 280 290 300
GKLIKEAAGK SNLKRVTLEL GGKSPCIVLA DADLDNAVEF AHHGVFYHQG
310 320 330 340 350
QCCIAASRIF VEESIYDEFV RRSVERAKKY ILGNPLTPGV TQGPQIDKEQ
360 370 380 390 400
YDKILDLIES GKKEGAKLEC GGGPWGNKGY FVQPTVFSNV TDEMRIAKEE
410 420 430 440 450
IFGPVQQIMK FKSLDDVIKR ANNTFYGLSA GVFTKDIDKA ITISSALQAG
460 470 480 490 500
TVWVNCYGVV SAQCPFGGFK MSGNGRELGE YGFHEYTEVK TVTVKISQKN

S
Length:501
Mass (Da):54,862
Last modified:January 22, 2007 - v2
Checksum:iB26464DC7168348E
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti162 – 1621V → I in AAA35518 (PubMed:4015823).Curated
Sequence conflicti162 – 1621V → I in AAA51695 (PubMed:2987944).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti121 – 1211N → S.1 Publication
Corresponds to variant rs1049981 [ dbSNP | Ensembl ].
VAR_048901
Natural varianti125 – 1251G → R.
Corresponds to variant rs11554423 [ dbSNP | Ensembl ].
VAR_048902
Natural varianti177 – 1771I → F.1 Publication
Corresponds to variant rs8187929 [ dbSNP | Ensembl ].
VAR_017778

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M31994
, M31982, M31983, M31984, M31985, M31986, M31987, M31988, M31989, M31990, M31991, M31992 Genomic DNA. Translation: AAA51692.1.
AF003341 mRNA. Translation: AAC51652.1.
AY390731 mRNA. Translation: AAR92229.1.
BT006921 mRNA. Translation: AAP35567.1.
AY338497 Genomic DNA. Translation: AAP88039.1.
AL591031 Genomic DNA. Translation: CAI12257.1.
CH471089 Genomic DNA. Translation: EAW62543.1.
BC001505 mRNA. Translation: AAH01505.1.
S61235 Genomic DNA. Translation: AAD13925.1.
M26761 mRNA. Translation: AAA35518.1.
K03000 mRNA. Translation: AAA51695.1.
CCDSiCCDS6644.1.
PIRiA33371. DEHUE1.
RefSeqiNP_000680.2. NM_000689.4.
UniGeneiHs.76392.

Genome annotation databases

EnsembliENST00000297785; ENSP00000297785; ENSG00000165092.
GeneIDi216.
KEGGihsa:216.
UCSCiuc004ajd.3. human.

Polymorphism databases

DMDMi118495.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Web resourcesi

NIEHS-SNPs

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M31994
, M31982, M31983, M31984, M31985, M31986, M31987, M31988, M31989, M31990, M31991, M31992 Genomic DNA. Translation: AAA51692.1.
AF003341 mRNA. Translation: AAC51652.1.
AY390731 mRNA. Translation: AAR92229.1.
BT006921 mRNA. Translation: AAP35567.1.
AY338497 Genomic DNA. Translation: AAP88039.1.
AL591031 Genomic DNA. Translation: CAI12257.1.
CH471089 Genomic DNA. Translation: EAW62543.1.
BC001505 mRNA. Translation: AAH01505.1.
S61235 Genomic DNA. Translation: AAD13925.1.
M26761 mRNA. Translation: AAA35518.1.
K03000 mRNA. Translation: AAA51695.1.
CCDSiCCDS6644.1.
PIRiA33371. DEHUE1.
RefSeqiNP_000680.2. NM_000689.4.
UniGeneiHs.76392.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4WB9X-ray2.07A1-501[»]
4WJ9X-ray1.74A1-501[»]
ProteinModelPortaliP00352.
SMRiP00352. Positions 8-501.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi106718. 8 interactions.
IntActiP00352. 6 interactions.
MINTiMINT-4999613.
STRINGi9606.ENSP00000297785.

Chemistry

BindingDBiP00352.
ChEMBLiCHEMBL3577.
DrugBankiDB00755. Tretinoin.
DB00162. Vitamin A.

PTM databases

PhosphoSiteiP00352.

Polymorphism databases

DMDMi118495.

2D gel databases

DOSAC-COBS-2DPAGEP00352.
REPRODUCTION-2DPAGEIPI00218914.
P00352.
SWISS-2DPAGEP00352.
UCD-2DPAGEP00352.

Proteomic databases

MaxQBiP00352.
PaxDbiP00352.
PeptideAtlasiP00352.
PRIDEiP00352.

Protocols and materials databases

DNASUi216.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000297785; ENSP00000297785; ENSG00000165092.
GeneIDi216.
KEGGihsa:216.
UCSCiuc004ajd.3. human.

Organism-specific databases

CTDi216.
GeneCardsiGC09M075515.
HGNCiHGNC:402. ALDH1A1.
HPAiCAB020690.
HPA002123.
MIMi100640. gene.
neXtProtiNX_P00352.
PharmGKBiPA24692.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG1012.
HOGENOMiHOG000271505.
HOVERGENiHBG000097.
InParanoidiP00352.
KOiK07249.
OMAiVEFAHIG.
OrthoDBiEOG7PS1F7.
PhylomeDBiP00352.
TreeFamiTF300455.

Enzyme and pathway databases

UniPathwayiUPA00912.
BioCyciMetaCyc:HS09183-MONOMER.
ReactomeiREACT_268561. RA biosynthesis pathway.
REACT_34. Ethanol oxidation.
SABIO-RKP00352.

Miscellaneous databases

ChiTaRSiALDH1A1. human.
GeneWikiiALDH1A1.
GenomeRNAii216.
NextBioi874.
PROiP00352.
SOURCEiSearch...

Gene expression databases

BgeeiP00352.
CleanExiHS_ALDH1A1.
ExpressionAtlasiP00352. baseline and differential.
GenevestigatoriP00352.

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.
[Graphical view]
PfamiPF00171. Aldedh. 1 hit.
[Graphical view]
SUPFAMiSSF53720. SSF53720. 1 hit.
PROSITEiPS00070. ALDEHYDE_DEHYDR_CYS. 1 hit.
PS00687. ALDEHYDE_DEHYDR_GLU. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Genomic structure of the human cytosolic aldehyde dehydrogenase gene."
    Hsu L.C., Chang W.-C., Yoshida A.
    Genomics 5:857-865(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "Cloning and expression of the full-length cDNAs encoding human liver class 1 and class 2 aldehyde dehydrogenase."
    Zheng C.F., Wang T.T., Weiner H.
    Alcohol. Clin. Exp. Res. 17:828-831(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT SER-121.
    Tissue: Liver.
  3. "Cloning and expression of aldehyde dehydrogenase 1 (ALDH1A1) from human lens cDNA library."
    Ramana K.V., Xiao T., Ansari N.H.
    Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Lens.
  4. "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
    Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
    Submitted (APR-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  5. NIEHS SNPs program
    Submitted (JUN-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT PHE-177.
  6. "DNA sequence and analysis of human chromosome 9."
    Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S., Bagguley C.L.
    , Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A., Frankland J.A., French L., Fricker D.G., Garner P., Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S., Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E., Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D., Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E., Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K., Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M., Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J., Dunham I.
    Nature 429:369-374(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  7. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  8. "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(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Colon.
  9. "Biological role of human cytosolic aldehyde dehydrogenase 1: hormonal response, retinal oxidation and implication in testicular feminization."
    Yoshida A., Hsu L.C., Yanagawa Y.
    Adv. Exp. Med. Biol. 328:37-44(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-6.
  10. "Aldehyde dehydrogenase from human liver. Primary structure of the cytoplasmic isoenzyme."
    Hempel J., von Bahr-Lindstroem H., Joernvall H.
    Eur. J. Biochem. 141:21-35(1983) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 2-501, ACETYLATION AT SER-2.
    Tissue: Liver.
  11. "Molecular abnormality and cDNA cloning of human aldehyde dehydrogenases."
    Yoshida A., Ikawa M., Hsu L.C., Tani K.
    Alcohol 2:103-106(1984) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 162-501.
  12. Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 162-501.
    Tissue: Liver.
  13. Cited for: PROTEIN SEQUENCE OF 266-273, ACTIVE SITES GLU-269 AND CYS-303, NAD-BINDING SITE CYS-456.
  14. "Aldehyde dehydrogenase from human erythrocytes: structural relationship to the liver cytosolic isozyme."
    Agarwal D.P., Cohn P., Goedde H.W., Hempel J.
    Enzyme 42:47-52(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: PARTIAL PROTEIN SEQUENCE.
    Tissue: Erythrocyte.
  15. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
    Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
    Science 325:834-840(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-91; LYS-128; LYS-252; LYS-353; LYS-367; LYS-410; LYS-419; LYS-435 AND LYS-495, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  16. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  17. "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(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
  18. "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(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-337 AND SER-413, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.

Entry informationi

Entry nameiAL1A1_HUMAN
AccessioniPrimary (citable) accession number: P00352
Secondary accession number(s): O00768, Q5SYR1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 20, 1986
Last sequence update: January 22, 2007
Last modified: March 31, 2015
This is version 164 of the entry and version 2 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 9
    Human chromosome 9: 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.