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Q86XE5

- HOGA1_HUMAN

UniProt

Q86XE5 - HOGA1_HUMAN

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Protein

4-hydroxy-2-oxoglutarate aldolase, mitochondrial

Gene

HOGA1

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

Functioni

Catalyzes the final step in the metabolic pathway of hydroxyproline.2 Publications

Catalytic activityi

4-hydroxy-2-oxoglutarate = pyruvate + glyoxylate.1 Publication

Enzyme regulationi

Inhibited by divalent cations.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei168 – 1681Involved in proton transfer during cleavage
Active sitei196 – 1961Schiff-base intermediate with substrate1 Publication
Binding sitei198 – 1981Substrate
Binding sitei222 – 2221Substrate; via carbonyl oxygen

GO - Molecular functioni

  1. 4-hydroxy-2-oxoglutarate aldolase activity Source: UniProtKB
  2. protein homodimerization activity Source: BHF-UCL

GO - Biological processi

  1. 4-hydroxyproline catabolic process Source: BHF-UCL
  2. glyoxylate catabolic process Source: UniProtKB
  3. glyoxylate metabolic process Source: BHF-UCL
  4. oxalate metabolic process Source: BHF-UCL
  5. pyruvate biosynthetic process Source: BHF-UCL
Complete GO annotation...

Keywords - Molecular functioni

Lyase

Keywords - Ligandi

Schiff base

Enzyme and pathway databases

BioCyciMetaCyc:G66-31234-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
4-hydroxy-2-oxoglutarate aldolase, mitochondrial (EC:4.1.3.16)
Alternative name(s):
Dihydrodipicolinate synthase-like
Short name:
DHDPS-like protein
Probable 2-keto-4-hydroxyglutarate aldolase
Short name:
Probable KHG-aldolase
Protein 569272
Gene namesi
Name:HOGA1
Synonyms:C10orf65, DHDPSL
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 10

Organism-specific databases

HGNCiHGNC:25155. HOGA1.

Subcellular locationi

Mitochondrion By similarity

GO - Cellular componenti

  1. extracellular vesicular exosome Source: UniProt
  2. mitochondrion Source: BHF-UCL
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

Pathology & Biotechi

Involvement in diseasei

Hyperoxaluria primary 3 (HP3) [MIM:613616]: A disorder phenotypically similar to hyperoxaluria type 1 and type 2. It is characterized by increase in urinary oxalate excretion and mild glycolic aciduria. Clinical manifestations include calcium oxalate urolithiasis, hematuria, pain, and/or urinary tract infection.1 Publication
Note: The disease is caused by mutations affecting the gene represented in this entry.
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti257 – 2571C → G in HP3. 1 Publication
VAR_064035
Natural varianti287 – 2871G → V in HP3. 1 Publication
VAR_064036
Natural varianti315 – 3151Missing in HP3. 1 Publication
VAR_064037

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi77 – 771S → A: 2-fold decrease in Kcat and a nearly 8-fold increase in KM. 1 Publication
Mutagenesisi77 – 771S → T: Significant loss of activity. 1 Publication
Mutagenesisi78 – 781N → A: 6-fold increase in KM. 1 Publication
Mutagenesisi78 – 781N → Q: 25-fold increase in KM. 1 Publication
Mutagenesisi140 – 1401Y → F: No change in activity. 1 Publication
Mutagenesisi168 – 1681Y → F: No enzymatic activity. 1 Publication
Mutagenesisi196 – 1961K → A: No enzymatic activity. 1 Publication
Mutagenesisi198 – 1981S → A: 2.5-fold decrease in Kcat and 4.2 fold increase in KM. 1 Publication
Mutagenesisi198 – 1981S → T: 7-fold increase in KM. 1 Publication

Keywords - Diseasei

Disease mutation

Organism-specific databases

MIMi613616. phenotype.
Orphaneti93600. Primary hyperoxaluria type 3.
PharmGKBiPA165548441.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 2525MitochondrionBy similarityAdd
BLAST
Chaini26 – 3273024-hydroxy-2-oxoglutarate aldolase, mitochondrialPRO_0000273346Add
BLAST

Proteomic databases

MaxQBiQ86XE5.
PaxDbiQ86XE5.
PRIDEiQ86XE5.

PTM databases

PhosphoSiteiQ86XE5.

Expressioni

Gene expression databases

BgeeiQ86XE5.
CleanExiHS_C10orf65.
GenevestigatoriQ86XE5.

Organism-specific databases

HPAiHPA039466.

Interactioni

Subunit structurei

Homotetramer.By similarity

Protein-protein interaction databases

BioGridi125207. 2 interactions.
IntActiQ86XE5. 1 interaction.

Structurei

Secondary structure

1
327
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi37 – 393
Helixi54 – 6411
Beta strandi70 – 767
Helixi77 – 793
Helixi81 – 833
Helixi86 – 9813
Beta strandi104 – 1096
Helixi115 – 12713
Beta strandi131 – 1366
Helixi142 – 1443
Helixi147 – 16014
Beta strandi165 – 1695
Helixi171 – 1744
Helixi180 – 1878
Beta strandi192 – 1976
Helixi202 – 21110
Turni212 – 2143
Beta strandi218 – 2236
Helixi224 – 2263
Helixi227 – 2337
Beta strandi237 – 2393
Helixi241 – 2444
Helixi247 – 25812
Helixi262 – 27817
Turni279 – 2835
Helixi284 – 29512
Helixi311 – 32212
Turni323 – 3253

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3S5NX-ray2.50A26-327[»]
3S5OX-ray1.97A26-327[»]
ProteinModelPortaliQ86XE5.
SMRiQ86XE5. Positions 33-327.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni77 – 782Substrate binding

Sequence similaritiesi

Belongs to the DapA family.Curated

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiCOG0329.
GeneTreeiENSGT00530000063604.
HOVERGENiHBG081405.
InParanoidiQ86XE5.
KOiK18123.
OMAiLADHENI.
PhylomeDBiQ86XE5.
TreeFamiTF324600.

Family and domain databases

Gene3Di3.20.20.70. 1 hit.
InterProiIPR013785. Aldolase_TIM.
IPR002220. DapA-like.
IPR020625. Dihydrodipicolinate_synth_AS.
[Graphical view]
PANTHERiPTHR12128. PTHR12128. 1 hit.
PfamiPF00701. DHDPS. 1 hit.
[Graphical view]
PIRSFiPIRSF001365. DHDPS. 1 hit.
PRINTSiPR00146. DHPICSNTHASE.
PROSITEiPS00666. DHDPS_2. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

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

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q86XE5) [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
MLGPQVWSSV RQGLSRSLSR NVGVWASGEG KKVDIAGIYP PVTTPFTATA
60 70 80 90 100
EVDYGKLEEN LHKLGTFPFR GFVVQGSNGE FPFLTSSERL EVVSRVRQAM
110 120 130 140 150
PKNRLLLAGS GCESTQATVE MTVSMAQVGA DAAMVVTPCY YRGRMSSAAL
160 170 180 190 200
IHHYTKVADL SPIPVVLYSV PANTGLDLPV DAVVTLSQHP NIVGMKDSGG
210 220 230 240 250
DVTRIGLIVH KTRKQDFQVL AGSAGFLMAS YALGAVGGVC ALANVLGAQV
260 270 280 290 300
CQLERLCCTG QWEDAQKLQH RLIEPNAAVT RRFGIPGLKK IMDWFGYYGG
310 320
PCRAPLQELS PAEEEALRMD FTSNGWL
Length:327
Mass (Da):35,249
Last modified:June 1, 2003 - v1
Checksum:i2DC011E4F9FD32C9
GO
Isoform 2 (identifier: Q86XE5-3) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     71-233: Missing.

Note: No experimental confirmation available.

Show »
Length:164
Mass (Da):17,954
Checksum:i5DC5ADF3B9A891B4
GO

Sequence cautioni

The sequence CAC84901.1 differs from that shown. Reason: Erroneous gene model prediction.
The sequence CAI15457.1 differs from that shown. Reason: Erroneous gene model prediction.

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti257 – 2571C → G in HP3. 1 Publication
VAR_064035
Natural varianti287 – 2871G → V in HP3. 1 Publication
VAR_064036
Natural varianti315 – 3151Missing in HP3. 1 Publication
VAR_064037

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei71 – 233163Missing in isoform 2. 1 PublicationVSP_022515Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AK289440 mRNA. Translation: BAF82129.1.
AL355315 Genomic DNA. Translation: CAI15454.1.
AL355315 Genomic DNA. Translation: CAI15455.1.
AL355315 Genomic DNA. Translation: CAI15457.1. Sequence problems.
CH471066 Genomic DNA. Translation: EAW49912.1.
BC011916 mRNA. Translation: AAH11916.1.
BC045550 mRNA. Translation: AAH45550.1.
BC057821 mRNA. Translation: AAH57821.1.
AJ312051 Genomic DNA. Translation: CAC84901.1. Sequence problems.
CCDSiCCDS44469.1. [Q86XE5-3]
CCDS7467.1. [Q86XE5-1]
RefSeqiNP_001128142.1. NM_001134670.1. [Q86XE5-3]
NP_612422.2. NM_138413.3. [Q86XE5-1]
UniGeneiHs.180346.

Genome annotation databases

EnsembliENST00000370646; ENSP00000359680; ENSG00000241935. [Q86XE5-1]
ENST00000370647; ENSP00000359681; ENSG00000241935. [Q86XE5-3]
GeneIDi112817.
KEGGihsa:112817.
UCSCiuc001kny.3. human. [Q86XE5-1]
uc001knz.3. human. [Q86XE5-3]

Polymorphism databases

DMDMi74750531.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AK289440 mRNA. Translation: BAF82129.1 .
AL355315 Genomic DNA. Translation: CAI15454.1 .
AL355315 Genomic DNA. Translation: CAI15455.1 .
AL355315 Genomic DNA. Translation: CAI15457.1 . Sequence problems.
CH471066 Genomic DNA. Translation: EAW49912.1 .
BC011916 mRNA. Translation: AAH11916.1 .
BC045550 mRNA. Translation: AAH45550.1 .
BC057821 mRNA. Translation: AAH57821.1 .
AJ312051 Genomic DNA. Translation: CAC84901.1 . Sequence problems.
CCDSi CCDS44469.1. [Q86XE5-3 ]
CCDS7467.1. [Q86XE5-1 ]
RefSeqi NP_001128142.1. NM_001134670.1. [Q86XE5-3 ]
NP_612422.2. NM_138413.3. [Q86XE5-1 ]
UniGenei Hs.180346.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
3S5N X-ray 2.50 A 26-327 [» ]
3S5O X-ray 1.97 A 26-327 [» ]
ProteinModelPortali Q86XE5.
SMRi Q86XE5. Positions 33-327.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 125207. 2 interactions.
IntActi Q86XE5. 1 interaction.

Chemistry

BindingDBi Q86XE5.
ChEMBLi CHEMBL5996.

PTM databases

PhosphoSitei Q86XE5.

Polymorphism databases

DMDMi 74750531.

Proteomic databases

MaxQBi Q86XE5.
PaxDbi Q86XE5.
PRIDEi Q86XE5.

Protocols and materials databases

DNASUi 112817.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000370646 ; ENSP00000359680 ; ENSG00000241935 . [Q86XE5-1 ]
ENST00000370647 ; ENSP00000359681 ; ENSG00000241935 . [Q86XE5-3 ]
GeneIDi 112817.
KEGGi hsa:112817.
UCSCi uc001kny.3. human. [Q86XE5-1 ]
uc001knz.3. human. [Q86XE5-3 ]

Organism-specific databases

CTDi 112817.
GeneCardsi GC10P099357.
HGNCi HGNC:25155. HOGA1.
HPAi HPA039466.
MIMi 613597. gene.
613616. phenotype.
neXtProti NX_Q86XE5.
Orphaneti 93600. Primary hyperoxaluria type 3.
PharmGKBi PA165548441.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0329.
GeneTreei ENSGT00530000063604.
HOVERGENi HBG081405.
InParanoidi Q86XE5.
KOi K18123.
OMAi LADHENI.
PhylomeDBi Q86XE5.
TreeFami TF324600.

Enzyme and pathway databases

BioCyci MetaCyc:G66-31234-MONOMER.

Miscellaneous databases

ChiTaRSi HOGA1. human.
GenomeRNAii 112817.
NextBioi 78673.
PROi Q86XE5.
SOURCEi Search...

Gene expression databases

Bgeei Q86XE5.
CleanExi HS_C10orf65.
Genevestigatori Q86XE5.

Family and domain databases

Gene3Di 3.20.20.70. 1 hit.
InterProi IPR013785. Aldolase_TIM.
IPR002220. DapA-like.
IPR020625. Dihydrodipicolinate_synth_AS.
[Graphical view ]
PANTHERi PTHR12128. PTHR12128. 1 hit.
Pfami PF00701. DHDPS. 1 hit.
[Graphical view ]
PIRSFi PIRSF001365. DHDPS. 1 hit.
PRINTSi PR00146. DHPICSNTHASE.
PROSITEi PS00666. DHDPS_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "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] (ISOFORM 1).
    Tissue: Urinary bladder.
  2. "The DNA sequence and comparative analysis of human chromosome 10."
    Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L., Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K., Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L., Taylor A., Battles J.
    , Bird C.P., Ainscough R., Almeida J.P., Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.
    Nature 429:375-381(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  3. 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] (ISOFORMS 1 AND 2).
    Tissue: Hippocampus and Kidney.
  5. "Homo sapiens gene 569272."
    Moschonas N.K.
    Submitted (APR-2001) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-279 (ISOFORM 1).
  6. Cited for: FUNCTION, VARIANTS HP3 GLY-257; VAL-287 AND GLU-315 DEL.
  7. "Structural and biochemical studies of human 4-hydroxy-2-oxoglutarate aldolase: implications for hydroxyproline metabolism in primary hyperoxaluria."
    Riedel T.J., Johnson L.C., Knight J., Hantgan R.R., Holmes R.P., Lowther W.T.
    PLoS ONE 6:E26021-E26021(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.97 ANGSTROMS) OF 26-327 IN COMPLEX WITH PYRUVATE, SUBUNIT, ACTIVE SITE, MUTAGENESIS OF SER-77; ASN-78; TYR-140; TYR-168; LYS-196 AND SER-198, FUNCTION, CATALYTIC ACTIVITY.

Entry informationi

Entry nameiHOGA1_HUMAN
AccessioniPrimary (citable) accession number: Q86XE5
Secondary accession number(s): A8K075
, Q5T680, Q5T684, Q711P0, Q8N9F2, Q96EV5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 23, 2007
Last sequence update: June 1, 2003
Last modified: October 29, 2014
This is version 105 of the entry and version 1 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 10
    Human chromosome 10: 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. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3