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P05089 (ARGI1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 173. 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·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Arginase-1

EC=3.5.3.1
Alternative name(s):
Liver-type arginase
Type I arginase
Gene names
Name:ARG1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length322 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Catalytic activity

L-arginine + H2O = L-ornithine + urea.

Cofactor

Binds 2 manganese ions per subunit.

Pathway

Nitrogen metabolism; urea cycle; L-ornithine and urea from L-arginine: step 1/1.

Subunit structure

Homotrimer. Ref.7 Ref.9 Ref.11

Subcellular location

Cytoplasm Ref.9.

Induction

By arginine or homoarginine.

Involvement in disease

Argininemia (ARGIN) [MIM:207800]: A rare autosomal recessive disorder of the urea cycle. Arginine is elevated in the blood and cerebrospinal fluid, and periodic hyperammonemia occurs. Clinical manifestations include developmental delay, seizures, mental retardation, hypotonia, ataxia and progressive spastic quadriplegia.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.13 Ref.15

Sequence similarities

Belongs to the arginase family.

Ontologies

Keywords
   Biological processArginine metabolism
Urea cycle
   Cellular componentCytoplasm
   Coding sequence diversityAlternative splicing
Polymorphism
   DiseaseDisease mutation
   LigandManganese
Metal-binding
   Molecular functionHydrolase
   PTMPhosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processarginine catabolic process

Traceable author statement Ref.1. Source: ProtInc

cellular nitrogen compound metabolic process

Traceable author statement. Source: Reactome

cellular response to dexamethasone stimulus

Inferred from electronic annotation. Source: Ensembl

cellular response to glucagon stimulus

Inferred from electronic annotation. Source: Ensembl

cellular response to hydrogen peroxide

Inferred from electronic annotation. Source: Ensembl

cellular response to interleukin-4

Inferred from electronic annotation. Source: Ensembl

cellular response to lipopolysaccharide

Inferred from electronic annotation. Source: Ensembl

cellular response to transforming growth factor beta stimulus

Inferred from electronic annotation. Source: Ensembl

collagen biosynthetic process

Inferred from electronic annotation. Source: Ensembl

liver development

Inferred from electronic annotation. Source: Ensembl

lung development

Inferred from electronic annotation. Source: Ensembl

mammary gland involution

Inferred from electronic annotation. Source: Ensembl

maternal process involved in female pregnancy

Inferred from electronic annotation. Source: Ensembl

positive regulation of endothelial cell proliferation

Inferred from electronic annotation. Source: Ensembl

protein homotrimerization

Inferred from electronic annotation. Source: Ensembl

regulation of L-arginine import

Inferred from electronic annotation. Source: Ensembl

response to amine

Inferred from electronic annotation. Source: Ensembl

response to amino acid

Inferred from electronic annotation. Source: Ensembl

response to axon injury

Inferred from electronic annotation. Source: Ensembl

response to cadmium ion

Inferred from electronic annotation. Source: Ensembl

response to drug

Inferred from electronic annotation. Source: Ensembl

response to herbicide

Inferred from electronic annotation. Source: Ensembl

response to manganese ion

Inferred from electronic annotation. Source: Ensembl

response to methylmercury

Inferred from electronic annotation. Source: Ensembl

response to selenium ion

Inferred from electronic annotation. Source: Ensembl

response to vitamin A

Inferred from electronic annotation. Source: Ensembl

response to vitamin E

Inferred from electronic annotation. Source: Ensembl

response to zinc ion

Inferred from electronic annotation. Source: Ensembl

small molecule metabolic process

Traceable author statement. Source: Reactome

urea cycle

Traceable author statement. Source: Reactome

   Cellular_componentcytoplasm

Traceable author statement Ref.1. Source: ProtInc

cytosol

Traceable author statement. Source: Reactome

extracellular space

Inferred from electronic annotation. Source: Ensembl

neuron projection

Inferred from electronic annotation. Source: Ensembl

neuronal cell body

Inferred from electronic annotation. Source: Ensembl

   Molecular_functionarginase activity

Inferred from experiment. Source: Reactome

manganese ion binding

Inferred from electronic annotation. Source: Ensembl

Complete GO annotation...

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P05089-1)

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: P05089-2)

Also known as: Erythroid variant;

The sequence of this isoform differs from the canonical sequence as follows:
     43-43: Q → QVTQNFLIL
Note: May be due to a competing acceptor splice site. No experimental confirmation available.
Isoform 3 (identifier: P05089-3)

The sequence of this isoform differs from the canonical sequence as follows:
     204-289: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 322322Arginase-1
PRO_0000173693

Regions

Region126 – 1305Substrate binding
Region137 – 1393Substrate binding

Sites

Metal binding1011Manganese 1
Metal binding1241Manganese 1
Metal binding1241Manganese 2
Metal binding1261Manganese 2
Metal binding1281Manganese 1
Metal binding2321Manganese 1
Metal binding2321Manganese 2
Metal binding2341Manganese 2
Binding site1831Substrate

Amino acid modifications

Modified residue171N6-succinyllysine By similarity
Modified residue721Phosphoserine By similarity
Modified residue751N6-succinyllysine By similarity

Natural variations

Alternative sequence431Q → QVTQNFLIL in isoform 2.
VSP_009330
Alternative sequence204 – 28986Missing in isoform 3.
VSP_009331
Natural variant111I → T in ARGIN; 12% of wild-type activity. Ref.15
Corresponds to variant rs28941474 [ dbSNP | Ensembl ].
VAR_015594
Natural variant1381G → V in ARGIN. Ref.15
VAR_015595
Natural variant2351G → R in ARGIN. Ref.13
VAR_000674
Natural variant2901T → S. Ref.14
VAR_000675

Experimental info

Sequence conflict481K → E in AAL71547. Ref.3
Sequence conflict861E → Q in AAA51776. Ref.1
Sequence conflict2021E → K in AAL71547. Ref.3

Secondary structure

....................................................... 322
Helix Strand Turn

Details...

Sequences

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

Last modified January 11, 2001. Version 2.
Checksum: 8F3BE2652243F622

FASTA32234,735
        10         20         30         40         50         60 
MSAKSRTIGI IGAPFSKGQP RGGVEEGPTV LRKAGLLEKL KEQECDVKDY GDLPFADIPN 

        70         80         90        100        110        120 
DSPFQIVKNP RSVGKASEQL AGKVAEVKKN GRISLVLGGD HSLAIGSISG HARVHPDLGV 

       130        140        150        160        170        180 
IWVDAHTDIN TPLTTTSGNL HGQPVSFLLK ELKGKIPDVP GFSWVTPCIS AKDIVYIGLR 

       190        200        210        220        230        240 
DVDPGEHYIL KTLGIKYFSM TEVDRLGIGK VMEETLSYLL GRKKRPIHLS FDVDGLDPSF 

       250        260        270        280        290        300 
TPATGTPVVG GLTYREGLYI TEEIYKTGLL SGLDIMEVNP SLGKTPEEVT RTVNTAVAIT 

       310        320 
LACFGLAREG NHKPIDYLNP PK 

« Hide

Isoform 2 (Erythroid variant) [UniParc].

Checksum: 3547D8B6C254179B
Show »

FASTA33035,664
Isoform 3 [UniParc].

Checksum: 79F02C69B700AB67
Show »

FASTA23625,356

References

« Hide 'large scale' references
[1]"Molecular cloning and nucleotide sequence of cDNA for human liver arginase."
Haraguchi Y., Takiguchi M., Amaya Y., Kawamoto S., Matsuda I., Mori M.
Proc. Natl. Acad. Sci. U.S.A. 84:412-415(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Tissue: Liver.
[2]"Human liver-type arginase gene: structure of the gene and analysis of the promoter region."
Takiguchi M., Haraguchi Y., Mori M.
Nucleic Acids Res. 16:8789-8802(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Tissue: Blood.
[3]Lee Y.T., Miller J.L.
Submitted (JAN-2002) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
Tissue: Erythroblast.
[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 (MAY-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
[5]"The DNA sequence and analysis of human chromosome 6."
Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D. expand/collapse author list , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.
Nature 425:805-811(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]"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 3).
Tissue: Liver and Skeletal muscle.
[7]"Expression of human liver arginase in Escherichia coli. Purification and properties of the product."
Ikemoto M., Tabata M., Miyake T., Kono T., Mori M., Totani M., Murachi T.
Biochem. J. 270:697-703(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-13, SUBUNIT.
Tissue: Liver.
[8]"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].
[9]"Crystal structure of human arginase I at 1.29-A resolution and exploration of inhibition in the immune response."
Di Costanzo L., Sabio G., Mora A., Rodriguez P.C., Ochoa A.C., Centeno F., Christianson D.W.
Proc. Natl. Acad. Sci. U.S.A. 102:13058-13063(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.29 ANGSTROMS) IN COMPLEX WITH MANGANESE IONS AND THE SYNTHETIC INHIBITOR 2(S)-AMINO-6-BORONOHEXANOIC ACID, SUBCELLULAR LOCATION, SUBUNIT.
[10]"Expression, purification, assay, and crystal structure of perdeuterated human arginase I."
Di Costanzo L., Moulin M., Haertlein M., Meilleur F., Christianson D.W.
Arch. Biochem. Biophys. 465:82-89(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) IN COMPLEX WITH MANGANESE IONS AND THE SYNTHETIC INHIBITOR 2(S)-AMINO-6-BORONOHEXANOIC ACID, IDENTIFICATION BY MASS SPECTROMETRY.
[11]"Crystal structure of human arginase I complexed with thiosemicarbazide reveals an unusual thiocarbonyl mu-sulfide ligand in the binuclear manganese cluster."
Di Costanzo L., Pique M.E., Christianson D.W.
J. Am. Chem. Soc. 129:6388-6389(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) IN COMPLEX WITH MANGANESE IONS AND THIOSEMICARBAZIDE, SUBUNIT.
[12]"Synthesis of (2S)-2-amino-7,8-epoxyoctanoic acid and structure of its metal-bridging complex with human arginase I."
Zakharian T.Y., Di Costanzo L., Christianson D.W.
Org. Biomol. Chem. 6:3240-3243(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.51 ANGSTROMS) IN COMPLEX WITH MANGANESE IONS AND THE SYNTHETIC INHIBITOR (2S)-2-AMINO-7,8-EPOXYOCTANOIC ACID.
[13]"Three novel mutations in the liver-type arginase gene in three unrelated Japanese patients with argininemia."
Uchino T., Haraguchi Y., Aparicio J.M., Mizutani N., Higashikawa M., Naitoh H., Mori M., Matsuda I.
Am. J. Hum. Genet. 51:1406-1412(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT ARGIN ARG-235.
[14]"Molecular genetic study of human arginase deficiency."
Grody W.W., Klein D., Dodson A.E., Kern R.M., Wissmann P.B., Goodman B.K., Bassand P., Marescau B., Kang S.-S., Leonard J.V., Cederbaum S.D.
Am. J. Hum. Genet. 50:1281-1290(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT SER-290.
[15]"Molecular basis of phenotypic variation in patients with argininemia."
Uchino T., Snyderman S.E., Lambert M., Qureshi I.A., Shapira S.K., Sansaricq C., Smit L.M.E., Jakobs C., Matsuda I.
Hum. Genet. 96:255-260(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS ARGIN THR-11 AND VAL-138.
+Additional computationally mapped references.

Web resources

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M14502 mRNA. Translation: AAA51776.1.
X12662 expand/collapse EMBL AC list , X12663, X12664, X12665, X12666, X12667, X12668, X12669 Genomic DNA. Translation: CAA31188.1.
AY074488 mRNA. Translation: AAL71547.1.
BT006741 mRNA. Translation: AAP35387.1.
AL121575 Genomic DNA. Translation: CAB92071.1.
AL121575 Genomic DNA. Translation: CAI23317.1.
AL121575 Genomic DNA. Translation: CAI23318.1.
BC005321 mRNA. Translation: AAH05321.1.
BC020653 mRNA. Translation: AAH20653.1.
PIRA26370. S02132.
RefSeqNP_000036.2. NM_000045.3.
NP_001231367.1. NM_001244438.1.
UniGeneHs.440934.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1WVAX-ray1.94A/B1-322[»]
1WVBX-ray2.30A/B1-322[»]
2AEBX-ray1.29A/B1-322[»]
2PHAX-ray1.90A/B1-322[»]
2PHOX-ray1.95A/B1-322[»]
2PLLX-ray1.90A/B1-322[»]
2ZAVX-ray1.70A/B1-322[»]
3DJ8X-ray1.51A/B1-322[»]
3E6KX-ray2.10A/B1-322[»]
3E6VX-ray1.72A/B1-322[»]
3F80X-ray1.60A/B1-322[»]
3GMZX-ray1.43A/B1-322[»]
3GN0X-ray1.70A/B1-322[»]
3KV2X-ray1.55A/B1-322[»]
3LP4X-ray1.90A/B1-322[»]
3LP7X-ray2.04A/B1-322[»]
3MFVX-ray1.90A/B1-322[»]
3MFWX-ray1.47A/B1-322[»]
3MJLX-ray1.90A/B1-322[»]
3SJTX-ray1.60A/B1-322[»]
3SKKX-ray1.70A/B1-322[»]
3TF3X-ray1.64A/B1-322[»]
3TH7X-ray2.10A/B1-322[»]
3THEX-ray1.97A/B1-322[»]
3THHX-ray1.85A/B1-322[»]
3THJX-ray1.50A/B1-322[»]
4FCIX-ray1.82A/B1-322[»]
4FCKX-ray1.90A/B1-322[»]
4GSMX-ray1.70A/B1-322[»]
4GSVX-ray1.48A/B1-322[»]
4GSZX-ray2.20A/B1-322[»]
4GWCX-ray1.90A/B1-322[»]
4GWDX-ray1.53A/B1-322[»]
4HWWX-ray1.30A/B5-318[»]
4HXQX-ray1.45A/B5-318[»]
4IE1X-ray2.00A/B5-318[»]
ProteinModelPortalP05089.
SMRP05089. Positions 5-318.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid106878. 7 interactions.
IntActP05089. 8 interactions.
MINTMINT-3974693.
STRING9606.ENSP00000357066.

Chemistry

BindingDBP05089.
ChEMBLCHEMBL1075097.
DrugBankDB00129. L-Ornithine.

PTM databases

PhosphoSiteP05089.

Polymorphism databases

DMDM12230985.

Proteomic databases

PaxDbP05089.
PRIDEP05089.

Protocols and materials databases

DNASU383.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000356962; ENSP00000349446; ENSG00000118520. [P05089-2]
ENST00000368087; ENSP00000357066; ENSG00000118520. [P05089-1]
GeneID383.
KEGGhsa:383.
UCSCuc003qco.2. human. [P05089-1]
uc010kfm.2. human. [P05089-2]

Organism-specific databases

CTD383.
GeneCardsGC06P131936.
HGNCHGNC:663. ARG1.
HPACAB009434.
CAB056159.
HPA003595.
HPA024006.
MIM207800. phenotype.
608313. gene.
neXtProtNX_P05089.
Orphanet90. Argininemia.
PharmGKBPA24947.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0010.
HOGENOMHOG000204319.
HOVERGENHBG003030.
KOK01476.
OMADYGDLPF.
OrthoDBEOG747PJ5.
PhylomeDBP05089.
TreeFamTF300034.

Enzyme and pathway databases

BioCycMetaCyc:HS04231-MONOMER.
ReactomeREACT_111217. Metabolism.
SABIO-RKP05089.
UniPathwayUPA00158; UER00270.

Gene expression databases

BgeeP05089.
CleanExHS_ARG1.
GenevestigatorP05089.

Family and domain databases

Gene3D3.40.800.10. 1 hit.
InterProIPR014033. Arginase.
IPR006035. Ureohydrolase.
IPR023696. Ureohydrolase_domain.
IPR020855. Ureohydrolase_Mn_BS.
[Graphical view]
PANTHERPTHR11358. PTHR11358. 1 hit.
PfamPF00491. Arginase. 1 hit.
[Graphical view]
PIRSFPIRSF036979. Arginase. 1 hit.
PRINTSPR00116. ARGINASE.
TIGRFAMsTIGR01229. rocF_arginase. 1 hit.
PROSITEPS01053. ARGINASE_1. 1 hit.
PS51409. ARGINASE_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP05089.
GenomeRNAi383.
NextBio1603.
PROP05089.
SOURCESearch...

Entry information

Entry nameARGI1_HUMAN
AccessionPrimary (citable) accession number: P05089
Secondary accession number(s): A6NEA0 expand/collapse secondary AC list , Q5JWT5, Q5JWT6, Q8TE72, Q9BS50
Entry history
Integrated into UniProtKB/Swiss-Prot: August 13, 1987
Last sequence update: January 11, 2001
Last modified: April 16, 2014
This is version 173 of the entry and version 2 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 6

Human chromosome 6: entries, gene names and cross-references to MIM