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Protein

Retinal dehydrogenase 2

Gene

ALDH1A2

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

Functioni

Recognizes as substrates free retinal and cellular retinol-binding protein-bound retinal. Does metabolize octanal and decanal but does not metabolize citral, benzaldehyde, acetaldehyde and propanal efficiently (By similarity).By similarity

Catalytic activityi

Retinal + NAD+ + H2O = retinoate + NADH.

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei187 – 1871Transition state stabilizerBy similarity
Active sitei286 – 2861Proton acceptorPROSITE-ProRule annotation
Active sitei320 – 3201NucleophilePROSITE-ProRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi263 – 2686NADBy similarity

GO - Molecular functioni

  1. 3-chloroallyl aldehyde dehydrogenase activity Source: UniProtKB
  2. aldehyde dehydrogenase (NAD) activity Source: GO_Central
  3. retinal binding Source: UniProtKB
  4. retinal dehydrogenase activity Source: UniProtKB

GO - Biological processi

  1. 9-cis-retinoic acid biosynthetic process Source: Ensembl
  2. anterior/posterior pattern specification Source: Ensembl
  3. blood vessel development Source: Ensembl
  4. cardiac muscle tissue development Source: Ensembl
  5. cellular response to retinoic acid Source: Ensembl
  6. determination of bilateral symmetry Source: Ensembl
  7. embryonic camera-type eye development Source: Ensembl
  8. embryonic digestive tract development Source: Ensembl
  9. embryonic forelimb morphogenesis Source: Ensembl
  10. face development Source: Ensembl
  11. heart morphogenesis Source: Ensembl
  12. hindbrain development Source: Ensembl
  13. kidney development Source: Ensembl
  14. liver development Source: Ensembl
  15. lung development Source: Ensembl
  16. midgut development Source: Ensembl
  17. morphogenesis of embryonic epithelium Source: Ensembl
  18. negative regulation of cell proliferation Source: UniProtKB
  19. neural crest cell development Source: Ensembl
  20. neural tube development Source: UniProtKB
  21. neuron differentiation Source: Ensembl
  22. pancreas development Source: Ensembl
  23. pituitary gland development Source: Ensembl
  24. positive regulation of apoptotic process Source: Ensembl
  25. positive regulation of cell proliferation Source: Ensembl
  26. positive regulation of gene expression Source: Ensembl
  27. proximal/distal pattern formation Source: Ensembl
  28. regulation of endothelial cell proliferation Source: Ensembl
  29. response to cytokine Source: UniProtKB
  30. response to estradiol Source: Ensembl
  31. response to vitamin A Source: Ensembl
  32. retinal metabolic process Source: Ensembl
  33. retinoic acid metabolic process Source: UniProtKB
  34. retinoic acid receptor signaling pathway Source: Ensembl
  35. retinol metabolic process Source: UniProtKB-UniPathway
  36. ureter maturation Source: Ensembl
  37. vitamin A metabolic process Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

NAD

Enzyme and pathway databases

BioCyciMetaCyc:HS05232-MONOMER.
UniPathwayiUPA00912.

Names & Taxonomyi

Protein namesi
Recommended name:
Retinal dehydrogenase 2 (EC:1.2.1.36)
Short name:
RALDH 2
Short name:
RalDH2
Alternative name(s):
Aldehyde dehydrogenase family 1 member A2
Retinaldehyde-specific dehydrogenase type 2
Short name:
RALDH(II)
Gene namesi
Name:ALDH1A2
Synonyms:RALDH2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 15

Organism-specific databases

HGNCiHGNC:15472. ALDH1A2.

Subcellular locationi

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB
  2. cytosol Source: Reactome
  3. perinuclear region of cytoplasm Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA24693.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 518518Retinal dehydrogenase 2PRO_0000056422Add
BLAST

Proteomic databases

MaxQBiO94788.
PaxDbiO94788.
PRIDEiO94788.

PTM databases

PhosphoSiteiO94788.

Expressioni

Gene expression databases

BgeeiO94788.
CleanExiHS_ALDH1A2.
ExpressionAtlasiO94788. baseline and differential.
GenevestigatoriO94788.

Organism-specific databases

HPAiHPA010022.

Interactioni

Subunit structurei

Homotetramer.By similarity

Protein-protein interaction databases

BioGridi114379. 3 interactions.
IntActiO94788. 1 interaction.
STRINGi9606.ENSP00000249750.

Structurei

3D structure databases

ProteinModelPortaliO94788.
SMRiO94788. Positions 20-518.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the aldehyde dehydrogenase family.Curated

Phylogenomic databases

eggNOGiCOG1012.
GeneTreeiENSGT00760000118999.
HOGENOMiHOG000271505.
HOVERGENiHBG000097.
InParanoidiO94788.
KOiK07249.
OMAiICEIQEA.
OrthoDBiEOG7PS1F7.
PhylomeDBiO94788.
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]

Sequences (4)i

Sequence statusi: Complete.

This entry describes 4 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: O94788-1) [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
MTSSKIEMPG EVKADPAALM ASLHLLPSPT PNLEIKYTKI FINNEWQNSE
60 70 80 90 100
SGRVFPVYNP ATGEQVCEVQ EADKADIDKA VQAARLAFSL GSVWRRMDAS
110 120 130 140 150
ERGRLLDKLA DLVERDRAVL ATMESLNGGK PFLQAFYVDL QGVIKTFRYY
160 170 180 190 200
AGWADKIHGM TIPVDGDYFT FTRHEPIGVC GQIIPWNFPL LMFAWKIAPA
210 220 230 240 250
LCCGNTVVIK PAEQTPLSAL YMGALIKEAG FPPGVINILP GYGPTAGAAI
260 270 280 290 300
ASHIGIDKIA FTGSTEVGKL IQEAAGRSNL KRVTLELGGK SPNIIFADAD
310 320 330 340 350
LDYAVEQAHQ GVFFNQGQCC TAGSRIFVEE SIYEEFVRRS VERAKRRVVG
360 370 380 390 400
SPFDPTTEQG PQIDKKQYNK ILELIQSGVA EGAKLECGGK GLGRKGFFIE
410 420 430 440 450
PTVFSNVTDD MRIAKEEIFG PVQEILRFKT MDEVIERANN SDFGLVAAVF
460 470 480 490 500
TNDINKALTV SSAMQAGTVW INCYNALNAQ SPFGGFKMSG NGREMGEFGL
510
REYSEVKTVT VKIPQKNS
Length:518
Mass (Da):56,724
Last modified:March 7, 2006 - v3
Checksum:iAAEE7A886951373F
GO
Isoform 2 (identifier: O94788-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     229-266: Missing.

Note: No experimental confirmation available.

Show »
Length:480
Mass (Da):53,060
Checksum:i5AC931BE5ED26AA4
GO
Isoform 3 (identifier: O94788-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-39: MTSSKIEMPGEVKADPAALMASLHLLPSPTPNLEIKYTK → MKNQCETVWLKSPIKLKL

Note: No experimental confirmation available.

Show »
Length:497
Mass (Da):54,673
Checksum:i27E8A8307A680BB7
GO
Isoform 4 (identifier: O94788-4) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-96: Missing.

Show »
Length:422
Mass (Da):46,137
Checksum:i4927D07BDD3BAC5D
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti231 – 2311F → L in BAG64174 (PubMed:14702039).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti50 – 501E → G.1 Publication
Corresponds to variant rs34266719 [ dbSNP | Ensembl ].
VAR_025439
Natural varianti110 – 1101A → V.1 Publication
Corresponds to variant rs35365164 [ dbSNP | Ensembl ].
VAR_025440
Natural varianti348 – 3481V → I.4 Publications
Corresponds to variant rs4646626 [ dbSNP | Ensembl ].
VAR_025441
Natural varianti436 – 4361E → K.1 Publication
Corresponds to variant rs34744827 [ dbSNP | Ensembl ].
VAR_025442

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 9696Missing in isoform 4. 1 PublicationVSP_047259Add
BLAST
Alternative sequencei1 – 3939MTSSK…IKYTK → MKNQCETVWLKSPIKLKL in isoform 3. 1 PublicationVSP_044496Add
BLAST
Alternative sequencei229 – 26638Missing in isoform 2. 1 PublicationVSP_017363Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB015226 mRNA. Translation: BAA34785.1.
AB015227 mRNA. Translation: BAA34786.1.
AB015228 mRNA. Translation: BAA34787.1.
AK128709 mRNA. Translation: BAG54714.1.
AK303057 mRNA. Translation: BAG64174.1.
DQ322171 Genomic DNA. Translation: ABC40749.1.
AC012653 Genomic DNA. No translation available.
AC018904 Genomic DNA. No translation available.
AC025431 Genomic DNA. No translation available.
AC066616 Genomic DNA. No translation available.
AC084781 Genomic DNA. No translation available.
BC030589 mRNA. Translation: AAH30589.1.
AL110299 mRNA. Translation: CAB53740.2.
CCDSiCCDS10163.1. [O94788-1]
CCDS10164.1. [O94788-2]
CCDS45266.1. [O94788-4]
CCDS55968.1. [O94788-3]
PIRiT14799.
RefSeqiNP_001193826.1. NM_001206897.1. [O94788-3]
NP_003879.2. NM_003888.3. [O94788-1]
NP_733797.1. NM_170696.2. [O94788-2]
NP_733798.1. NM_170697.2. [O94788-4]
UniGeneiHs.643455.

Genome annotation databases

EnsembliENST00000249750; ENSP00000249750; ENSG00000128918. [O94788-1]
ENST00000347587; ENSP00000309623; ENSG00000128918. [O94788-2]
ENST00000537372; ENSP00000438296; ENSG00000128918. [O94788-3]
ENST00000559517; ENSP00000453408; ENSG00000128918. [O94788-4]
GeneIDi8854.
KEGGihsa:8854.
UCSCiuc002aew.3. human. [O94788-1]
uc002aey.3. human. [O94788-2]
uc010ugv.2. human. [O94788-3]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Web resourcesi

NIEHS-SNPs

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB015226 mRNA. Translation: BAA34785.1.
AB015227 mRNA. Translation: BAA34786.1.
AB015228 mRNA. Translation: BAA34787.1.
AK128709 mRNA. Translation: BAG54714.1.
AK303057 mRNA. Translation: BAG64174.1.
DQ322171 Genomic DNA. Translation: ABC40749.1.
AC012653 Genomic DNA. No translation available.
AC018904 Genomic DNA. No translation available.
AC025431 Genomic DNA. No translation available.
AC066616 Genomic DNA. No translation available.
AC084781 Genomic DNA. No translation available.
BC030589 mRNA. Translation: AAH30589.1.
AL110299 mRNA. Translation: CAB53740.2.
CCDSiCCDS10163.1. [O94788-1]
CCDS10164.1. [O94788-2]
CCDS45266.1. [O94788-4]
CCDS55968.1. [O94788-3]
PIRiT14799.
RefSeqiNP_001193826.1. NM_001206897.1. [O94788-3]
NP_003879.2. NM_003888.3. [O94788-1]
NP_733797.1. NM_170696.2. [O94788-2]
NP_733798.1. NM_170697.2. [O94788-4]
UniGeneiHs.643455.

3D structure databases

ProteinModelPortaliO94788.
SMRiO94788. Positions 20-518.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi114379. 3 interactions.
IntActiO94788. 1 interaction.
STRINGi9606.ENSP00000249750.

Chemistry

ChEMBLiCHEMBL3112384.
DrugBankiDB00755. Tretinoin.
DB00162. Vitamin A.

PTM databases

PhosphoSiteiO94788.

Proteomic databases

MaxQBiO94788.
PaxDbiO94788.
PRIDEiO94788.

Protocols and materials databases

DNASUi8854.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000249750; ENSP00000249750; ENSG00000128918. [O94788-1]
ENST00000347587; ENSP00000309623; ENSG00000128918. [O94788-2]
ENST00000537372; ENSP00000438296; ENSG00000128918. [O94788-3]
ENST00000559517; ENSP00000453408; ENSG00000128918. [O94788-4]
GeneIDi8854.
KEGGihsa:8854.
UCSCiuc002aew.3. human. [O94788-1]
uc002aey.3. human. [O94788-2]
uc010ugv.2. human. [O94788-3]

Organism-specific databases

CTDi8854.
GeneCardsiGC15M058245.
H-InvDBHIX0038341.
HGNCiHGNC:15472. ALDH1A2.
HPAiHPA010022.
MIMi603687. gene.
neXtProtiNX_O94788.
PharmGKBiPA24693.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG1012.
GeneTreeiENSGT00760000118999.
HOGENOMiHOG000271505.
HOVERGENiHBG000097.
InParanoidiO94788.
KOiK07249.
OMAiICEIQEA.
OrthoDBiEOG7PS1F7.
PhylomeDBiO94788.
TreeFamiTF300455.

Enzyme and pathway databases

UniPathwayiUPA00912.
BioCyciMetaCyc:HS05232-MONOMER.

Miscellaneous databases

ChiTaRSiALDH1A2. human.
GeneWikiiALDH1A2.
GenomeRNAii8854.
NextBioi33241.
PROiO94788.
SOURCEiSearch...

Gene expression databases

BgeeiO94788.
CleanExiHS_ALDH1A2.
ExpressionAtlasiO94788. baseline and differential.
GenevestigatoriO94788.

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. "TAL1 and LIM-only proteins synergistically induce retinaldehyde dehydrogenase 2 expression in T-cell acute lymphoblastic leukemia by acting as cofactors for GATA3."
    Ono Y., Fukuhara N., Yoshie O.
    Mol. Cell. Biol. 18:6939-6950(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 4), VARIANT ILE-348.
  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 AND 3), VARIANT ILE-348.
    Tissue: Testis and Uterus.
  3. NIEHS SNPs program
    Submitted (DEC-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS GLY-50; VAL-110; ILE-348 AND LYS-436.
  4. "Analysis of the DNA sequence and duplication history of human chromosome 15."
    Zody M.C., Garber M., Sharpe T., Young S.K., Rowen L., O'Neill K., Whittaker C.A., Kamal M., Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Kodira C.D., Madan A., Qin S., Yang X., Abbasi N., Abouelleil A.
    , Arachchi H.M., Baradarani L., Birditt B., Bloom S., Bloom T., Borowsky M.L., Burke J., Butler J., Cook A., DeArellano K., DeCaprio D., Dorris L. III, Dors M., Eichler E.E., Engels R., Fahey J., Fleetwood P., Friedman C., Gearin G., Hall J.L., Hensley G., Johnson E., Jones C., Kamat A., Kaur A., Locke D.P., Madan A., Munson G., Jaffe D.B., Lui A., Macdonald P., Mauceli E., Naylor J.W., Nesbitt R., Nicol R., O'Leary S.B., Ratcliffe A., Rounsley S., She X., Sneddon K.M.B., Stewart S., Sougnez C., Stone S.M., Topham K., Vincent D., Wang S., Zimmer A.R., Birren B.W., Hood L., Lander E.S., Nusbaum C.
    Nature 440:671-675(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. "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 2).
    Tissue: Testis.
  6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 302-518 (ISOFORMS 1/2), VARIANT ILE-348.
    Tissue: Testis.
  7. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiAL1A2_HUMAN
AccessioniPrimary (citable) accession number: O94788
Secondary accession number(s): B3KY52
, B4DZR2, F5H2Y9, H0YM00, Q2PJS6, Q8NHQ4, Q9UBR8, Q9UFY0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1999
Last sequence update: March 7, 2006
Last modified: March 4, 2015
This is version 142 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

Complete proteome, Reference proteome

Documents

  1. Human chromosome 15
    Human chromosome 15: 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. 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.