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Q06830 (PRDX1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 159. 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·Interactions·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Peroxiredoxin-1

EC=1.11.1.15
Alternative name(s):
Natural killer cell-enhancing factor A
Short name=NKEF-A
Proliferation-associated gene protein
Short name=PAG
Thioredoxin peroxidase 2
Thioredoxin-dependent peroxide reductase 2
Gene names
Name:PRDX1
Synonyms:PAGA, PAGB, TDPX2
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length199 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Involved in redox regulation of the cell. Reduces peroxides with reducing equivalents provided through the thioredoxin system but not from glutaredoxin. May play an important role in eliminating peroxides generated during metabolism. Might participate in the signaling cascades of growth factors and tumor necrosis factor-alpha by regulating the intracellular concentrations of H2O2. Reduces an intramolecular disulfide bond in GDPD5 that gates the ability to GDPD5 to drive postmitotic motor neuron differentiation By similarity.

Catalytic activity

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

Subunit structure

Homodimer; disulfide-linked, upon oxidation By similarity. May form heterodimers with AOP2. Interacts with GDPD5; forms a mixed-disulfide with GDPD5 By similarity.

Subcellular location

Cytoplasm. Melanosome. Note: Identified by mass spectrometry in melanosome fractions from stage I to stage IV. Ref.16

Induction

Constitutively expressed in most human cells; is induced to higher levels upon serum stimulation in untransformed and transformed cells.

Post-translational modification

Phosphorylated on Thr-90 during the M-phase, which leads to a more than 80% decrease in enzymatic activity. Ref.12

Miscellaneous

The active site is the redox-active Cys-52 oxidized to Cys-SOH. Cys-SOH rapidly reacts with Cys-173-SH of the other subunit to form an intermolecular disulfide with a concomitant homodimer formation. The enzyme may be subsequently regenerated by reduction of the disulfide by thioredoxin.

Inactivated upon oxidative stress by overoxidation of Cys-52 to Cys-SO2H and Cys-SO3H. Cys-SO2H is retroreduced to Cys-SOH after removal of H2O2, while Cys-SO3H may be irreversibly oxidized.

Sequence similarities

Belongs to the AhpC/TSA family.

Contains 1 thioredoxin domain.

Sequence caution

The sequence CAI13097.1 differs from that shown. Reason: Erroneous gene model prediction.

Ontologies

Keywords
   Cellular componentCytoplasm
   Coding sequence diversityPolymorphism
   DomainRedox-active center
   Molecular functionAntioxidant
Oxidoreductase
Peroxidase
   PTMAcetylation
Disulfide bond
Phosphoprotein
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processcell proliferation

Traceable author statement PubMed 8089076. Source: ProtInc

erythrocyte homeostasis

Inferred from electronic annotation. Source: Ensembl

hydrogen peroxide catabolic process

Inferred from direct assay PubMed 18606987. Source: BHF-UCL

natural killer cell mediated cytotoxicity

Inferred from electronic annotation. Source: Ensembl

regulation of NF-kappaB import into nucleus

Inferred from electronic annotation. Source: Ensembl

regulation of stress-activated MAPK cascade

Inferred from electronic annotation. Source: Ensembl

removal of superoxide radicals

Inferred from electronic annotation. Source: Ensembl

retina homeostasis

Inferred from expression pattern PubMed 23580065. Source: UniProt

skeletal system development

Traceable author statement PubMed 8089076. Source: ProtInc

   Cellular_componentcytoplasm

Inferred from direct assay PubMed 17603937. Source: MGI

cytosol

Traceable author statement. Source: Reactome

extracellular space

Inferred from direct assay PubMed 22664934PubMed 23580065. Source: UniProt

extracellular vesicular exosome

Inferred from direct assay PubMed 19199708PubMed 20458337. Source: UniProt

melanosome

Inferred from electronic annotation. Source: UniProtKB-SubCell

mitochondrial matrix

Inferred from electronic annotation. Source: Ensembl

nuclear euchromatin

Inferred from electronic annotation. Source: Ensembl

nucleolus

Inferred from electronic annotation. Source: Ensembl

nucleus

Inferred from direct assay PubMed 17603937. Source: MGI

peroxisomal matrix

Inferred from electronic annotation. Source: Ensembl

   Molecular_functionheme binding

Inferred from electronic annotation. Source: Ensembl

peroxidase activity

Inferred from direct assay Ref.12. Source: MGI

poly(A) RNA binding

Inferred from direct assay PubMed 22658674PubMed 22681889. Source: UniProtKB

thioredoxin peroxidase activity

Inferred from direct assay PubMed 18606987. Source: BHF-UCL

Complete GO annotation...

Binary interactions

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.17
Chain2 – 199198Peroxiredoxin-1
PRO_0000135076

Regions

Domain6 – 165160Thioredoxin

Sites

Active site521Cysteine sulfenic acid (-SOH) intermediate

Amino acid modifications

Modified residue21N-acetylserine Ref.17
Modified residue71N6-acetyllysine Ref.17
Modified residue161N6-acetyllysine Ref.17
Modified residue271N6-acetyllysine Ref.17
Modified residue351N6-acetyllysine; alternate Ref.17
Modified residue351N6-succinyllysine; alternate By similarity
Modified residue901Phosphothreonine; by CDK1 Ref.12
Modified residue1361N6-acetyllysine By similarity
Disulfide bond52Interchain (with C-173); in linked form
Disulfide bond173Interchain (with C-52); in linked form

Natural variations

Natural variant621R → G. Ref.5
Corresponds to variant rs34034070 [ dbSNP | Ensembl ].
VAR_025050

Experimental info

Mutagenesis901T → A: Abolishes phosphorylation by CDK1; 30% reduction in enzymatic activity. Ref.12
Mutagenesis901T → D: 87% reduction in enzymatic activity. Ref.12
Sequence conflict1471L → P Ref.2
Sequence conflict149 – 1502VG → CC Ref.2
Sequence conflict1891Q → P Ref.2
Sequence conflict1911S → T Ref.2

Secondary structure

.................................. 199
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q06830 [UniParc].

Last modified June 1, 1994. Version 1.
Checksum: 8F68E56D75BF5304

FASTA19922,110
        10         20         30         40         50         60 
MSSGNAKIGH PAPNFKATAV MPDGQFKDIS LSDYKGKYVV FFFYPLDFTF VCPTEIIAFS 

        70         80         90        100        110        120 
DRAEEFKKLN CQVIGASVDS HFCHLAWVNT PKKQGGLGPM NIPLVSDPKR TIAQDYGVLK 

       130        140        150        160        170        180 
ADEGISFRGL FIIDDKGILR QITVNDLPVG RSVDETLRLV QAFQFTDKHG EVCPAGWKPG 

       190 
SDTIKPDVQK SKEYFSKQK 

« Hide

References

« Hide 'large scale' references
[1]"A human cDNA corresponding to a gene overexpressed during cell proliferation encodes a product sharing homology with amoebic and bacterial proteins."
Prosperi M.T., Ferbus D., Karczinski I., Goubin G.
J. Biol. Chem. 268:11050-11056(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"Cloning and sequence analysis of candidate human natural killer-enhancing factor genes."
Shau H., Butterfield L.H., Chiu R., Kim A.
Immunogenetics 40:129-134(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]"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 (OCT-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[4]"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 (MAY-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[5]NIEHS SNPs program
Submitted (NOV-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT GLY-62.
[6]"Human protein factory for converting the transcriptome into an in vitro-expressed proteome."
Goshima N., Kawamura Y., Fukumoto A., Miura A., Honma R., Satoh R., Wakamatsu A., Yamamoto J., Kimura K., Nishikawa T., Andoh T., Iida Y., Ishikawa K., Ito E., Kagawa N., Kaminaga C., Kanehori K., Kawakami B. expand/collapse author list , Kenmochi K., Kimura R., Kobayashi M., Kuroita T., Kuwayama H., Maruyama Y., Matsuo K., Minami K., Mitsubori M., Mori M., Morishita R., Murase A., Nishikawa A., Nishikawa S., Okamoto T., Sakagami N., Sakamoto Y., Sasaki Y., Seki T., Sono S., Sugiyama A., Sumiya T., Takayama T., Takayama Y., Takeda H., Togashi T., Yahata K., Yamada H., Yanagisawa Y., Endo Y., Imamoto F., Kisu Y., Tanaka S., Isogai T., Imai J., Watanabe S., Nomura N.
Nat. Methods 5:1011-1017(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[7]"The DNA sequence and biological annotation of human chromosome 1."
Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K. expand/collapse author list , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[8]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[9]"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].
Tissue: Urinary bladder.
[10]Lubec G., Afjehi-Sadat L., Chen W.-Q., Sun Y.
Submitted (DEC-2008) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 17-35; 93-136; 141-151 AND 159-190, IDENTIFICATION BY MASS SPECTROMETRY.
Tissue: Brain, Cajal-Retzius cell and Fetal brain cortex.
[11]"A method for detection of overoxidation of cysteines: peroxiredoxins are oxidized in vivo at the active-site cysteine during oxidative stress."
Wagner E., Luche S., Penna L., Chevallet M., van Dorsselaer A., Leize-Wagner E., Rabilloud T.
Biochem. J. 366:777-785(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: OVEROXIDATION AT CYS-52.
[12]"Regulation of peroxiredoxin I activity by Cdc2-mediated phosphorylation."
Chang T.-S., Jeong W., Choi S.Y., Yu S., Kang S.W., Rhee S.G.
J. Biol. Chem. 277:25370-25376(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT THR-90, MUTAGENESIS OF THR-90.
[13]"Inactivation of human peroxiredoxin I during catalysis as the result of the oxidation of the catalytic site cysteine to cysteine-sulfinic acid."
Yang K.S., Kang S.W., Woo H.A., Hwang S.C., Chae H.Z., Kim K., Rhee S.G.
J. Biol. Chem. 277:38029-38036(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: OVEROXIDATION AT CYS-52.
[14]"Regeneration of peroxiredoxins during recovery after oxidative stress: only some overoxidized peroxiredoxins can be reduced during recovery after oxidative stress."
Chevallet M., Wagner E., Luche S., van Dorsselaer A., Leize-Wagner E., Rabilloud T.
J. Biol. Chem. 278:37146-37153(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: RETROREDUCTION OF CYS-52, IDENTIFICATION BY MASS SPECTROMETRY.
[15]"Reversing the inactivation of peroxiredoxins caused by cysteine sulfinic acid formation."
Woo H.A., Chae H.Z., Hwang S.C., Yang K.S., Kang S.W., Kim K., Rhee S.G.
Science 300:653-656(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: RETROREDUCTION OF CYS-52, IDENTIFICATION BY MASS SPECTROMETRY.
[16]"Proteomic and bioinformatic characterization of the biogenesis and function of melanosomes."
Chi A., Valencia J.C., Hu Z.-Z., Watabe H., Yamaguchi H., Mangini N.J., Huang H., Canfield V.A., Cheng K.C., Yang F., Abe R., Yamagishi S., Shabanowitz J., Hearing V.J., Wu C., Appella E., Hunt D.F.
J. Proteome Res. 5:3135-3144(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
Tissue: Melanoma.
[17]"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 SER-2; LYS-7; LYS-16; LYS-27 AND LYS-35, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
[18]"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].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X67951 mRNA. Translation: CAA48137.1.
L19184 mRNA. Translation: AAA50464.1.
BT019740 mRNA. Translation: AAV38545.1.
CR407652 mRNA. Translation: CAG28580.1.
DQ297142 Genomic DNA. Translation: ABB84465.1.
AB451262 mRNA. Translation: BAG70076.1.
AB451388 mRNA. Translation: BAG70202.1.
AL451136 Genomic DNA. Translation: CAI13095.1.
AL451136 Genomic DNA. Translation: CAI13096.1.
AL451136 Genomic DNA. Translation: CAI13097.1. Sequence problems.
CH471059 Genomic DNA. Translation: EAX06975.1.
CH471059 Genomic DNA. Translation: EAX06976.1.
CH471059 Genomic DNA. Translation: EAX06978.1.
CH471059 Genomic DNA. Translation: EAX06979.1.
CH471059 Genomic DNA. Translation: EAX06980.1.
CH471059 Genomic DNA. Translation: EAX06981.1.
CH471059 Genomic DNA. Translation: EAX06982.1.
BC007063 mRNA. Translation: AAH07063.1.
BC021683 mRNA. Translation: AAH21683.1.
PIRA46711.
RefSeqNP_001189360.1. NM_001202431.1.
NP_002565.1. NM_002574.3.
NP_859047.1. NM_181696.2.
NP_859048.1. NM_181697.2.
UniGeneHs.180909.
Hs.731900.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2RIIX-ray2.60A/B1-199[»]
3HY2X-ray2.10A/B1-199[»]
ProteinModelPortalQ06830.
SMRQ06830. Positions 3-187.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid111089. 104 interactions.
DIPDIP-33152N.
IntActQ06830. 39 interactions.
MINTMINT-4999060.
STRING9606.ENSP00000262746.

Chemistry

ChEMBLCHEMBL5315.

Protein family/group databases

PeroxiBase4501. Hs2CysPrx01.

PTM databases

PhosphoSiteQ06830.

Polymorphism databases

DMDM548453.

2D gel databases

DOSAC-COBS-2DPAGEQ06830.
OGPQ06830.
SWISS-2DPAGEQ06830.
UCD-2DPAGEQ06830.

Proteomic databases

PaxDbQ06830.
PRIDEQ06830.

Protocols and materials databases

DNASU5052.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000262746; ENSP00000262746; ENSG00000117450.
ENST00000319248; ENSP00000361152; ENSG00000117450.
GeneID5052.
KEGGhsa:5052.
UCSCuc001coa.3. human.

Organism-specific databases

CTD5052.
GeneCardsGC01M045976.
HGNCHGNC:9352. PRDX1.
HPACAB004682.
HPA007730.
MIM176763. gene.
neXtProtNX_Q06830.
PharmGKBPA33722.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0450.
HOVERGENHBG000286.
InParanoidQ06830.
KOK13279.
OMAEFKKINC.
OrthoDBEOG7T1RCD.
PhylomeDBQ06830.
TreeFamTF105181.

Enzyme and pathway databases

ReactomeREACT_120956. Cellular responses to stress.

Gene expression databases

BgeeQ06830.
CleanExHS_PRDX1.
GenevestigatorQ06830.

Family and domain databases

Gene3D3.40.30.10. 1 hit.
InterProIPR000866. AhpC/TSA.
IPR024706. Peroxiredoxin_AhpC-typ.
IPR019479. Peroxiredoxin_C.
IPR012336. Thioredoxin-like_fold.
[Graphical view]
PfamPF10417. 1-cysPrx_C. 1 hit.
PF00578. AhpC-TSA. 1 hit.
[Graphical view]
PIRSFPIRSF000239. AHPC. 1 hit.
SUPFAMSSF52833. SSF52833. 1 hit.
PROSITEPS51352. THIOREDOXIN_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSPRDX1. human.
EvolutionaryTraceQ06830.
GeneWikiPeroxiredoxin_1.
GenomeRNAi5052.
NextBio19468.
PROQ06830.
SOURCESearch...

Entry information

Entry namePRDX1_HUMAN
AccessionPrimary (citable) accession number: Q06830
Secondary accession number(s): B5BU26 expand/collapse secondary AC list , D3DPZ8, P35703, Q2V576, Q5T154, Q5T155
Entry history
Integrated into UniProtKB/Swiss-Prot: June 1, 1994
Last sequence update: June 1, 1994
Last modified: April 16, 2014
This is version 159 of the entry and version 1 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 1

Human chromosome 1: entries, gene names and cross-references to MIM