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P30044 (PRDX5_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 153. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | 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:
Peroxiredoxin-5, mitochondrial

EC=1.11.1.15
Alternative name(s):
Alu corepressor 1
Antioxidant enzyme B166
Short name=AOEB166
Liver tissue 2D-page spot 71B
PLP
Peroxiredoxin V
Short name=Prx-V
Peroxisomal antioxidant enzyme
TPx type VI
Thioredoxin peroxidase PMP20
Thioredoxin reductase
Gene names
Name:PRDX5
Synonyms:ACR1
ORF Names:SBBI10
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length214 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Reduces hydrogen peroxide and alkyl hydroperoxides with reducing equivalents provided through the thioredoxin system. Involved in intracellular redox signaling.

Catalytic activity

2 R'-SH + ROOH = R'-S-S-R' + H2O + ROH.

Subunit structure

Monomer.

Subcellular location

Isoform Mitochondrial: Mitochondrion Ref.3.

Isoform Cytoplasmic+peroxisomal: Cytoplasm. Peroxisome Ref.3.

Tissue specificity

Widely expressed. Ref.3

Sequence similarities

Belongs to the peroxiredoxin 2 family.

Contains 1 thioredoxin domain.

Sequence caution

The sequence AAF17200.1 differs from that shown. Reason: Frameshift at positions 14 and 30.

Ontologies

Keywords
   Cellular componentCytoplasm
Mitochondrion
Peroxisome
   Coding sequence diversityAlternative initiation
Alternative splicing
Polymorphism
   DomainRedox-active center
Transit peptide
   Molecular functionAntioxidant
Oxidoreductase
Peroxidase
   PTMAcetylation
Disulfide bond
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processNADPH oxidation

Inferred from direct assay Ref.5. Source: UniProtKB

cellular response to reactive oxygen species

Inferred from mutant phenotype PubMed 18262354. Source: UniProtKB

hydrogen peroxide catabolic process

Inferred from direct assay Ref.2. Source: UniProtKB

inflammatory response

Traceable author statement Ref.3. Source: UniProtKB

negative regulation of apoptotic process

Inferred from mutant phenotype PubMed 18262354. Source: UniProtKB

negative regulation of cysteine-type endopeptidase activity involved in apoptotic process

Inferred from mutant phenotype PubMed 18262354. Source: GOC

negative regulation of oxidoreductase activity

Inferred from direct assay PubMed 15280035. Source: UniProtKB

negative regulation of transcription from RNA polymerase III promoter

Inferred from direct assay Ref.1. Source: UniProtKB

positive regulation of collagen biosynthetic process

Inferred from direct assay PubMed 15276323. Source: UniProtKB

reactive nitrogen species metabolic process

Inferred from direct assay PubMed 15280035. Source: UniProtKB

regulation of RNA biosynthetic process

Inferred from direct assay Ref.1. Source: UniProtKB

regulation of apoptosis involved in tissue homeostasis

Inferred from direct assay PubMed 15276323. Source: UniProtKB

response to oxidative stress

Inferred from direct assay Ref.3Ref.2. Source: UniProtKB

   Cellular_componentcytoplasm

Inferred from direct assay PubMed 15785239Ref.2. Source: UniProtKB

cytoplasmic vesicle

Inferred from direct assay Ref.1. Source: UniProtKB

cytosol

Inferred from direct assay PubMed 18262354. Source: UniProtKB

extracellular space

Inferred from direct assay PubMed 23580065. Source: UniProt

extracellular vesicular exosome

Inferred from direct assay PubMed 19056867PubMed 19199708. Source: UniProt

intracellular membrane-bounded organelle

Inferred from direct assay PubMed 15785239. Source: UniProtKB

mitochondrial matrix

Traceable author statement. Source: Reactome

mitochondrion

Inferred from direct assay Ref.3Ref.5PubMed 18262354. Source: UniProtKB

nucleus

Inferred from direct assay Ref.1PubMed 15785239. Source: UniProtKB

perinuclear region of cytoplasm

Inferred from direct assay Ref.1. Source: UniProtKB

peroxisomal matrix

Inferred from direct assay Ref.2. Source: UniProtKB

peroxisome

Inferred from direct assay Ref.3Ref.5. Source: UniProtKB

   Molecular_functionRNA polymerase III regulatory region DNA binding

Inferred from direct assay Ref.1. Source: UniProtKB

antioxidant activity

Inferred from direct assay Ref.2. Source: UniProtKB

cysteine-type endopeptidase inhibitor activity involved in apoptotic process

Inferred from mutant phenotype PubMed 18262354. Source: UniProtKB

peroxidase activity

Inferred from direct assay Ref.3. Source: UniProtKB

peroxiredoxin activity

Inferred from direct assay Ref.5. Source: UniProtKB

peroxynitrite reductase activity

Inferred from direct assay PubMed 15280035. Source: UniProtKB

protein dimerization activity

Inferred from direct assay PubMed 15046979Ref.5. Source: UniProtKB

receptor binding

Inferred from physical interaction PubMed 20178365Ref.2. Source: UniProtKB

Complete GO annotation...

Alternative products

This entry describes 4 isoforms produced by alternative splicing and alternative initiation. [Align] [Select]
Isoform Mitochondrial (identifier: P30044-1)

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 Cytoplasmic+peroxisomal (identifier: P30044-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-52: Missing.
Isoform 3 (identifier: P30044-3)

The sequence of this isoform differs from the canonical sequence as follows:
     102-145: Missing.
Note: No experimental confirmation available.
Isoform 4 (identifier: P30044-4)

The sequence of this isoform differs from the canonical sequence as follows:
     57-145: Missing.
Note: Produced by alternative splicing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 5252Mitochondrion Potential
Chain53 – 214162Peroxiredoxin-5, mitochondrial
PRO_0000023793

Regions

Domain56 – 214159Thioredoxin
Motif212 – 2143Microbody targeting signal By similarity

Sites

Active site1001Cysteine sulfenic acid (-SOH) intermediate Probable

Amino acid modifications

Modified residue751N6-acetyllysine By similarity
Modified residue831N6-acetyllysine; alternate Ref.14
Modified residue831N6-succinyllysine; alternate By similarity
Modified residue1161N6-succinyllysine By similarity
Disulfide bond100 ↔ 204Redox-active Ref.17

Natural variations

Alternative sequence1 – 5252Missing in isoform Cytoplasmic+peroxisomal.
VSP_018829
Alternative sequence57 – 14589Missing in isoform 4.
VSP_046682
Alternative sequence102 – 14544Missing in isoform 3.
VSP_045783
Natural variant331Y → C. Ref.1 Ref.3 Ref.4 Ref.7 Ref.9 Ref.10 Ref.12
Corresponds to variant rs7938623 [ dbSNP | Ensembl ].
VAR_025049
Natural variant1571F → L in a breast cancer sample; somatic mutation. Ref.19
VAR_036406

Experimental info

Mutagenesis1001C → S: Complete loss of activity.
Mutagenesis1251C → S: No change in activity.
Mutagenesis2041C → S: Complete loss of activity.
Sequence conflict1411H → T in AAF04856. Ref.4

Secondary structure

................................... 214
Helix Strand Turn

Details...

Sequences

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

Last modified January 11, 2011. Version 4.
Checksum: DA1DEB21120254EE

FASTA21422,086
        10         20         30         40         50         60 
MGLAGVCALR RSAGYILVGG AGGQSAAAAA RRYSEGEWAS GGVRSFSRAA AAMAPIKVGD 

        70         80         90        100        110        120 
AIPAVEVFEG EPGNKVNLAE LFKGKKGVLF GVPGAFTPGC SKTHLPGFVE QAEALKAKGV 

       130        140        150        160        170        180 
QVVACLSVND AFVTGEWGRA HKAEGKVRLL ADPTGAFGKE TDLLLDDSLV SIFGNRRLKR 

       190        200        210 
FSMVVQDGIV KALNVEPDGT GLTCSLAPNI ISQL 

« Hide

Isoform Cytoplasmic+peroxisomal [UniParc].

Checksum: 370DF621012F880D
Show »

FASTA16217,031
Isoform 3 [UniParc].

Checksum: 29984B81B33F82C1
Show »

FASTA17017,454
Isoform 4 [UniParc].

Checksum: F3A1C1531E4E4A73
Show »

FASTA12512,897

References

« Hide 'large scale' references
[1]"A novel human DNA-binding protein with sequence similarity to a subfamily of redox proteins which is able to repress RNA-polymerase-III-driven transcription of the Alu-family retroposons in vitro."
Kropotov A., Sedova V., Ivanov V., Sazeeva N., Tomilin A., Krutilina R., Oei S.L., Griesenbeck J., Buchlow G., Tomilin N.
Eur. J. Biochem. 260:336-346(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM MITOCHONDRIAL), VARIANT CYS-33.
[2]"Characterization of human and murine PMP20 peroxisomal proteins that exhibit antioxidant activity in vitro."
Yamashita H., Avraham S., Jiang S., London R., Van Veldhoven P.P., Subramani S., Rogers R.A., Avraham H.
J. Biol. Chem. 274:29897-29904(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM CYTOPLASMIC+PEROXISOMAL), CHARACTERIZATION.
[3]"Cloning and characterization of AOEB166, a novel mammalian antioxidant enzyme of the peroxiredoxin family."
Knoops B., Clippe A., Bogard C., Arsalane K., Wattiez R., Hermans C., Duconseille E., Falmagne P., Bernard A.
J. Biol. Chem. 274:30451-30458(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM MITOCHONDRIAL), PROTEIN SEQUENCE OF 54-90, TISSUE SPECIFICITY, SUBCELLULAR LOCATION, CHARACTERIZATION, VARIANT CYS-33.
Tissue: Lung.
[4]"Mouse peroxiredoxin V is a thioredoxin peroxidase that inhibits p53-induced apoptosis."
Zhou Y., Kok K.H., Chun A.C.S., Wong C.M., Wu H.W., Lin M.C.M., Fung P.C.W., Kung H.-F., Jin D.-Y.
Biochem. Biophys. Res. Commun. 268:921-927(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM CYTOPLASMIC+PEROXISOMAL), VARIANT CYS-33.
[5]"Identification of a new type of mammalian peroxiredoxin that forms an intramolecular disulfide as a reaction intermediate."
Seo M.S., Kang S.W., Kim K., Baines I.C., Lee T.H., Rhee S.G.
J. Biol. Chem. 275:20346-20354(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], MUTAGENESIS, CHARACTERIZATION.
[6]"A new type of human thiol peroxidase (Human TPx type VI)."
Kim I.H., Jeong W.
Submitted (SEP-1999) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM CYTOPLASMIC+PEROXISOMAL).
[7]Zhang W., Li N., Wan T., Cao X.
Submitted (MAR-2000) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM MITOCHONDRIAL), VARIANT CYS-33.
[8]"Gene expression profiling in the human hypothalamus-pituitary-adrenal axis and full-length cDNA cloning."
Hu R.-M., Han Z.-G., Song H.-D., Peng Y.-D., Huang Q.-H., Ren S.-X., Gu Y.-J., Huang C.-H., Li Y.-B., Jiang C.-L., Fu G., Zhang Q.-H., Gu B.-W., Dai M., Mao Y.-F., Gao G.-F., Rong R., Ye M. expand/collapse author list , Zhou J., Xu S.-H., Gu J., Shi J.-X., Jin W.-R., Zhang C.-K., Wu T.-M., Huang G.-Y., Chen Z., Chen M.-D., Chen J.-L.
Proc. Natl. Acad. Sci. U.S.A. 97:9543-9548(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM CYTOPLASMIC+PEROXISOMAL).
Tissue: Adrenal gland.
[9]"Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.
Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM MITOCHONDRIAL), VARIANT CYS-33.
[10]NIEHS SNPs program
Submitted (OCT-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT CYS-33.
[11]"Human chromosome 11 DNA sequence and analysis including novel gene identification."
Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K., Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F., Bloom T., Bruford E., Chang J.L., Cuomo C.A., Eichler E., FitzGerald M.G. expand/collapse author list , Jaffe D.B., LaButti K., Nicol R., Park H.-S., Seaman C., Sougnez C., Yang X., Zimmer A.R., Zody M.C., Birren B.W., Nusbaum C., Fujiyama A., Hattori M., Rogers J., Lander E.S., Sakaki Y.
Nature 440:497-500(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[12]"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 MITOCHONDRIAL; 3 AND 4), VARIANT CYS-33.
Tissue: Brain and Medulla oblongata.
[13]"Human liver protein map: a reference database established by microsequencing and gel comparison."
Hochstrasser D.F., Frutiger S., Paquet N., Bairoch A., Ravier F., Pasquali C., Sanchez J.-C., Tissot J.-D., Bjellqvist B., Vargas R., Appel R.D., Hughes G.J.
Electrophoresis 13:992-1001(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 54-63.
Tissue: Liver.
[14]"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(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-83, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[15]"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].
[16]"Crystal structure of human peroxiredoxin 5, a novel type of mammalian peroxiredoxin at 1.5-A resolution."
Declercq J.-P., Evrard C., Clippe A., Stricht D.V., Bernard A., Knoops B.
J. Mol. Biol. 311:751-759(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS).
[17]"The crystal structures of oxidized forms of human peroxiredoxin 5 with an intramolecular disulfide bond confirm the proposed enzymatic mechanism for atypical 2-Cys peroxiredoxins."
Smeets A., Marchand C., Linard D., Knoops B., Declercq J.P.
Arch. Biochem. Biophys. 477:98-104(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.83 ANGSTROMS) OF 54-214, DISULFIDE BOND.
[18]"Structural evidence that peroxiredoxin catalytic power is based on transition-state stabilization."
Hall A., Parsonage D., Poole L.B., Karplus P.A.
J. Mol. Biol. 402:194-209(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.45 ANGSTROMS) OF 54-214 IN COMPLEX WITH DITHIOTHREITOL, ACTIVE SITE.
[19]"The consensus coding sequences of human breast and colorectal cancers."
Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V. expand/collapse author list , Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., Velculescu V.E.
Science 314:268-274(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT [LARGE SCALE ANALYSIS] LEU-157.
+Additional computationally mapped references.

Web resources

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF231705 mRNA. Translation: AAF78899.1.
AF124993 mRNA. Translation: AAF27531.1.
AF110731 mRNA. Translation: AAF03750.1.
AF197952 mRNA. Translation: AAF04856.1.
AJ249483 mRNA. Translation: CAB62210.1.
AF242525 mRNA. Translation: AAF99605.1.
AF112212 mRNA. Translation: AAF17200.1. Frameshift.
CR457203 mRNA. Translation: CAG33484.1.
DQ247769 Genomic DNA. Translation: ABB05181.1.
AP001453 Genomic DNA. No translation available.
AP003774 Genomic DNA. No translation available.
BC110983 mRNA. Translation: AAI10984.1.
BC113723 mRNA. Translation: AAI13724.1.
BC113725 mRNA. Translation: AAI13726.1.
BC143849 mRNA. Translation: AAI43850.1.
BC171733 mRNA. Translation: AAI71733.1.
RefSeqNP_036226.1. NM_012094.4.
NP_857634.1. NM_181651.2.
NP_857635.1. NM_181652.2.
UniGeneHs.502823.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1H4OX-ray1.95A/B/C/D/E/F/G/H54-214[»]
1HD2X-ray1.50A54-214[»]
1OC3X-ray2.00A/B/C54-214[»]
1URMX-ray1.70A54-214[»]
2VL2X-ray1.92A/B/C54-214[»]
2VL3X-ray1.83A/B/C54-214[»]
2VL9X-ray2.70A/B/C/D54-214[»]
3MNGX-ray1.45A54-214[»]
ProteinModelPortalP30044.
SMRP30044. Positions 54-214.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid117352. 33 interactions.
IntActP30044. 5 interactions.
MINTMINT-5002532.
STRING9606.ENSP00000265462.

Chemistry

DrugBankDB00995. Auranofin.

Protein family/group databases

PeroxiBase4448. HsPrxV.

PTM databases

PhosphoSiteP30044.

Polymorphism databases

DMDM317373539.

2D gel databases

OGPP30044.
REPRODUCTION-2DPAGEIPI00759663.
SWISS-2DPAGEP30044.
UCD-2DPAGEP30044.

Proteomic databases

PaxDbP30044.
PRIDEP30044.

Protocols and materials databases

DNASU25824.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000265462; ENSP00000265462; ENSG00000126432. [P30044-1]
ENST00000347941; ENSP00000335363; ENSG00000126432. [P30044-4]
ENST00000352435; ENSP00000335334; ENSG00000126432. [P30044-3]
GeneID25824.
KEGGhsa:25824.
UCSCuc001nzu.3. human. [P30044-1]

Organism-specific databases

CTD25824.
GeneCardsGC11P064085.
HGNCHGNC:9355. PRDX5.
HPACAB008661.
HPA037915.
MIM606583. gene.
neXtProtNX_P30044.
PharmGKBPA33726.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0678.
HOGENOMHOG000255884.
HOVERGENHBG053675.
InParanoidP30044.
KOK11187.
OMAMSAWGKQ.
OrthoDBEOG77Q4XX.
PhylomeDBP30044.
TreeFamTF105182.

Enzyme and pathway databases

ReactomeREACT_120956. Cellular responses to stress.

Gene expression databases

ArrayExpressP30044.
BgeeP30044.
CleanExHS_PRDX5.
GenevestigatorP30044.

Family and domain databases

Gene3D3.40.30.10. 1 hit.
InterProIPR013740. Redoxin.
IPR012336. Thioredoxin-like_fold.
[Graphical view]
PfamPF08534. Redoxin. 1 hit.
[Graphical view]
SUPFAMSSF52833. SSF52833. 1 hit.
PROSITEPS51352. THIOREDOXIN_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSPRDX5. human.
EvolutionaryTraceP30044.
GeneWikiPRDX5.
GenomeRNAi25824.
NextBio35462441.
PROP30044.
SOURCESearch...

Entry information

Entry namePRDX5_HUMAN
AccessionPrimary (citable) accession number: P30044
Secondary accession number(s): A6NC19 expand/collapse secondary AC list , A6NG06, B7ZLJ4, B7ZVW3, Q14CK0, Q6IAF2, Q9UBU5, Q9UJU4, Q9UKX4
Entry history
Integrated into UniProtKB/Swiss-Prot: April 1, 1993
Last sequence update: January 11, 2011
Last modified: April 16, 2014
This is version 153 of the entry and version 4 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

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 11

Human chromosome 11: entries, gene names and cross-references to MIM