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P09601 (HMOX1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 154. 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·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Heme oxygenase 1

Short name=HO-1
EC=1.14.99.3
Gene names
Name:HMOX1
Synonyms:HO, HO1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length288 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Heme oxygenase cleaves the heme ring at the alpha methene bridge to form biliverdin. Biliverdin is subsequently converted to bilirubin by biliverdin reductase. Under physiological conditions, the activity of heme oxygenase is highest in the spleen, where senescent erythrocytes are sequestrated and destroyed. Exhibits cytoprotective effects since excess of free heme sensitizes cells to undergo apoptosis.

Catalytic activity

Protoheme + 3 AH2 + 3 O2 = biliverdin + Fe2+ + CO + 3 A + 3 H2O.

Subcellular location

Microsome. Endoplasmic reticulum membrane; Peripheral membrane protein; Cytoplasmic side Ref.13.

Tissue specificity

Expressed at higher levels in renal cancer tissue than in normal tissue (at protein level). Ref.10

Induction

Heme oxygenase 1 activity is highly inducible by its substrate heme and by various non-heme substances such as heavy metals, bromobenzene, endotoxin, oxidizing agents and UVA.

Involvement in disease

Heme oxygenase 1 deficiency (HMOX1D) [MIM:614034]: A disease characterized by impaired stress hematopoiesis, resulting in marked erythrocyte fragmentation and intravascular hemolysis, coagulation abnormalities, endothelial damage, and iron deposition in renal and hepatic tissues. Clinical features include persistent hemolytic anemia, asplenia, nephritis, generalized erythematous rash, growth retardation and hepatomegaly.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.7

Sequence similarities

Belongs to the heme oxygenase family.

Ontologies

Keywords
   Biological processApoptosis
   Cellular componentEndoplasmic reticulum
Membrane
Microsome
   Coding sequence diversityPolymorphism
   LigandHeme
Iron
Metal-binding
   Molecular functionOxidoreductase
   PTMPhosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processangiogenesis

Traceable author statement PubMed 12239590. Source: BHF-UCL

cell death

Inferred from sequence or structural similarity. Source: BHF-UCL

cellular iron ion homeostasis

Traceable author statement. Source: Reactome

cellular response to arsenic-containing substance

Inferred from electronic annotation. Source: Ensembl

cellular response to cadmium ion

Inferred from electronic annotation. Source: Ensembl

cellular response to hypoxia

Inferred from expression pattern PubMed 12511571. Source: UniProtKB

cellular response to nutrient

Inferred from electronic annotation. Source: Ensembl

endothelial cell proliferation

Traceable author statement PubMed 12239590. Source: BHF-UCL

erythrocyte homeostasis

Inferred from mutant phenotype Ref.7. Source: BHF-UCL

excretion

Inferred by curator PubMed 17915953. Source: BHF-UCL

heme catabolic process

Inferred from direct assay PubMed 17915953. Source: BHF-UCL

heme oxidation

Inferred from direct assay PubMed 17915953. Source: BHF-UCL

intracellular signal transduction

Traceable author statement PubMed 17652371. Source: BHF-UCL

intrinsic apoptotic signaling pathway in response to DNA damage

Inferred from electronic annotation. Source: Ensembl

iron ion homeostasis

Inferred from direct assay PubMed 17915953. Source: BHF-UCL

low-density lipoprotein particle clearance

Traceable author statement Ref.7. Source: BHF-UCL

negative regulation of DNA binding

Inferred from electronic annotation. Source: Ensembl

negative regulation of extrinsic apoptotic signaling pathway via death domain receptors

Inferred from mutant phenotype PubMed 18202225. Source: BHF-UCL

negative regulation of leukocyte migration

Traceable author statement PubMed 14525760. Source: BHF-UCL

negative regulation of mast cell cytokine production

Inferred from electronic annotation. Source: Ensembl

negative regulation of mast cell degranulation

Inferred from electronic annotation. Source: Ensembl

negative regulation of muscle cell apoptotic process

Inferred from electronic annotation. Source: Ensembl

negative regulation of neuron apoptotic process

Inferred from electronic annotation. Source: Ensembl

negative regulation of sequence-specific DNA binding transcription factor activity

Inferred from electronic annotation. Source: Ensembl

negative regulation of smooth muscle cell proliferation

Inferred from direct assay PubMed 17600318. Source: UniProtKB

porphyrin-containing compound metabolic process

Traceable author statement. Source: Reactome

positive regulation of I-kappaB kinase/NF-kappaB signaling

Inferred from mutant phenotype PubMed 12761501. Source: UniProtKB

positive regulation of angiogenesis

Inferred from electronic annotation. Source: Ensembl

positive regulation of chemokine biosynthetic process

Traceable author statement PubMed 17652371. Source: BHF-UCL

positive regulation of smooth muscle cell proliferation

Inferred from direct assay PubMed 17600318. Source: UniProtKB

positive regulation of vasodilation

Inferred by curator PubMed 17915953. Source: BHF-UCL

protein homooligomerization

Inferred from direct assay PubMed 19556236. Source: UniProtKB

regulation of angiogenesis

Traceable author statement PubMed 17652371. Source: BHF-UCL

regulation of blood pressure

Inferred from electronic annotation. Source: Ensembl

regulation of sequence-specific DNA binding transcription factor activity

Inferred from sequence or structural similarity. Source: BHF-UCL

regulation of transcription from RNA polymerase II promoter in response to oxidative stress

Inferred from sequence or structural similarity. Source: BHF-UCL

response to estrogen

Inferred from electronic annotation. Source: Ensembl

response to hydrogen peroxide

Inferred from sequence or structural similarity. Source: BHF-UCL

response to nicotine

Inferred from direct assay PubMed 18205746. Source: BHF-UCL

response to oxidative stress

Inferred from mutant phenotype Ref.7. Source: BHF-UCL

small GTPase mediated signal transduction

Inferred from electronic annotation. Source: Ensembl

small molecule metabolic process

Traceable author statement. Source: Reactome

smooth muscle hyperplasia

Traceable author statement PubMed 18289072. Source: BHF-UCL

transmembrane transport

Traceable author statement. Source: Reactome

wound healing involved in inflammatory response

Inferred from mutant phenotype Ref.7. Source: BHF-UCL

   Cellular_componentcaveola

Inferred from electronic annotation. Source: Ensembl

cytosol

Inferred from electronic annotation. Source: Ensembl

endoplasmic reticulum

Inferred from direct assay PubMed 19556236. Source: UniProtKB

endoplasmic reticulum membrane

Traceable author statement. Source: Reactome

extracellular space

Traceable author statement PubMed 18307065. Source: BHF-UCL

membrane

Traceable author statement Ref.1. Source: ProtInc

nucleolus

Inferred from electronic annotation. Source: Ensembl

nucleus

Inferred from sequence or structural similarity. Source: BHF-UCL

   Molecular_functionenzyme binding

Inferred from sequence or structural similarity PubMed 15516695. Source: BHF-UCL

heme binding

Inferred from direct assay PubMed 17915953. Source: BHF-UCL

heme oxygenase (decyclizing) activity

Inferred from mutant phenotype PubMed 19556236. Source: UniProtKB

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

phospholipase D activity

Inferred from electronic annotation. Source: Ensembl

protein homodimerization activity

Inferred from direct assay PubMed 19556236. Source: UniProtKB

signal transducer activity

Inferred from mutant phenotype PubMed 12761501. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 288288Heme oxygenase 1
PRO_0000209687

Sites

Metal binding251Iron (heme axial ligand)
Binding site181Heme
Binding site1341Heme
Binding site1831Heme

Amino acid modifications

Modified residue2291Phosphoserine Ref.11

Natural variations

Natural variant71D → H. Ref.3
Corresponds to variant rs2071747 [ dbSNP | Ensembl ].
VAR_019165
Natural variant1061P → L.
Corresponds to variant rs9282702 [ dbSNP | Ensembl ].
VAR_022156

Experimental info

Mutagenesis1401D → A: Inactive as a heme oxygenase but active as a peroxidase. Ref.15

Secondary structure

............................... 288
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P09601 [UniParc].

Last modified July 1, 1989. Version 1.
Checksum: AB47827778694064

FASTA28832,819
        10         20         30         40         50         60 
MERPQPDSMP QDLSEALKEA TKEVHTQAEN AEFMRNFQKG QVTRDGFKLV MASLYHIYVA 

        70         80         90        100        110        120 
LEEEIERNKE SPVFAPVYFP EELHRKAALE QDLAFWYGPR WQEVIPYTPA MQRYVKRLHE 

       130        140        150        160        170        180 
VGRTEPELLV AHAYTRYLGD LSGGQVLKKI AQKALDLPSS GEGLAFFTFP NIASATKFKQ 

       190        200        210        220        230        240 
LYRSRMNSLE MTPAVRQRVI EEAKTAFLLN IQLFEELQEL LTHDTKDQSP SRAPGLRQRA 

       250        260        270        280 
SNKVQDSAPV ETPRGKPPLN TRSQAPLLRW VLTLSFLVAT VAVGLYAM 

« Hide

References

« Hide 'large scale' references
[1]"Human heme oxygenase cDNA and induction of its mRNA by hemin."
Yoshida T., Biro P., Cohen T., Mueller R.M., Shibahara S.
Eur. J. Biochem. 171:457-461(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"A genome annotation-driven approach to cloning the human ORFeome."
Collins J.E., Wright C.L., Edwards C.A., Davis M.P., Grinham J.A., Cole C.G., Goward M.E., Aguado B., Mallya M., Mokrab Y., Huckle E.J., Beare D.M., Dunham I.
Genome Biol. 5:R84.1-R84.11(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[3]SeattleSNPs variation discovery resource
Submitted (NOV-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT HIS-7.
[4]"The DNA sequence of human chromosome 22."
Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M., Clamp M., Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., Bagguley C., Bailey J., Barlow K.F., Bates K.N., Beasley O.P., Bird C.P., Blakey S.E., Bridgeman A.M. expand/collapse author list , Buck D., Burgess J., Burrill W.D., Burton J., Carder C., Carter N.P., Chen Y., Clark G., Clegg S.M., Cobley V.E., Cole C.G., Collier R.E., Connor R., Conroy D., Corby N.R., Coville G.J., Cox A.V., Davis J., Dawson E., Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M., Ellington A.G., Evans K.L., Fey J.M., Fleming K., French L., Garner A.A., Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C., Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S., Hunt S.E., Jones M.C., Kershaw J., Kimberley A.M., King A., Laird G.K., Langford C.F., Leversha M.A., Lloyd C., Lloyd D.M., Martyn I.D., Mashreghi-Mohammadi M., Matthews L.H., Mccann O.T., Mcclay J., Mclaren S., McMurray A.A., Milne S.A., Mortimore B.J., Odell C.N., Pavitt R., Pearce A.V., Pearson D., Phillimore B.J.C.T., Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y., Rogers L., Ross M.T., Scott C.E., Sehra H.K., Skuce C.D., Smalley S., Smith M.L., Soderlund C., Spragon L., Steward C.A., Sulston J.E., Swann R.M., Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L., Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L., Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N., Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J., Shintani A., Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., Roe B.A., Chen F., Chu L., Crabtree J., Deschamps S., Do A., Do T., Dorman A., Fang F., Fu Y., Hu P., Hua A., Kenton S., Lai H., Lao H.I., Lewis J., Lewis S., Lin S.-P., Loh P., Malaj E., Nguyen T., Pan H., Phan S., Qi S., Qian Y., Ray L., Ren Q., Shaull S., Sloan D., Song L., Wang Q., Wang Y., Wang Z., White J., Willingham D., Wu H., Yao Z., Zhan M., Zhang G., Chissoe S., Murray J., Miller N., Minx P., Fulton R., Johnson D., Bemis G., Bentley D., Bradshaw H., Bourne S., Cordes M., Du Z., Fulton L., Goela D., Graves T., Hawkins J., Hinds K., Kemp K., Latreille P., Layman D., Ozersky P., Rohlfing T., Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K., Nelson J., Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R., Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., Budarf M.L., McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., Edelmann L., Kim U.J., Shizuya H., Simon M.I., Dumanski J.P., Peyrard M., Kedra D., Seroussi E., Fransson I., Tapia I., Bruder C.E., O'Brien K.P., Wilkinson P., Bodenteich A., Hartman K., Hu X., Khan A.S., Lane L., Tilahun Y., Wright H.
Nature 402:489-495(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]"Heme oxygenase is the major 32-kDa stress protein induced in human skin fibroblasts by UVA radiation, hydrogen peroxide, and sodium arsenite."
Keyse S.M., Tyrrell R.M.
Proc. Natl. Acad. Sci. U.S.A. 86:99-103(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-103.
Tissue: Foreskin.
[6]"Structural organization of the human heme oxygenase gene and the function of its promoter."
Shibahara S., Sato M., Muller R.M., Yoshida T.
Eur. J. Biochem. 179:557-563(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-7.
[7]"Oxidative stress causes enhanced endothelial cell injury in human heme oxygenase-1 deficiency."
Yachie A., Niida Y., Wada T., Igarashi N., Kaneda H., Toma T., Ohta K., Kasahara Y., Koizumi S.
J. Clin. Invest. 103:129-135(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: INVOLVEMENT IN HMOX1D.
[8]"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[9]"Mechanisms of cell protection by heme oxygenase-1."
Gozzelino R., Jeney V., Soares M.P.
Annu. Rev. Pharmacol. Toxicol. 50:323-354(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: REVIEW ON ANTIAPOPTOTIC FUNCTION.
[10]"CXCR3-B can mediate growth-inhibitory signals in human renal cancer cells by down-regulating the expression of heme oxygenase-1."
Datta D., Banerjee P., Gasser M., Waaga-Gasser A.M., Pal S.
J. Biol. Chem. 285:36842-36848(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: TISSUE SPECIFICITY.
[11]"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-229, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[12]"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].
[13]"Endoplasmic reticulum anchored heme-oxygenase 1 faces the cytosol."
Gottlieb Y., Truman M., Cohen L.A., Leichtmann-Bardoogo Y., Meyron-Holtz E.G.
Haematologica 97:1489-1493(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION.
[14]"Crystal structure of human heme oxygenase-1."
Schuller D.J., Wilks A., Ortiz de Montellano P.R., Poulos T.L.
Nat. Struct. Biol. 6:860-867(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.08 ANGSTROMS).
[15]"Crystal structures of the ferric, ferrous, and ferrous-NO forms of the Asp140Ala mutant of human heme oxygenase-1: catalytic implications."
Lad L., Wang J., Li H., Friedman J., Bhaskar B., Ortiz de Montellano P.R., Poulos T.L.
J. Mol. Biol. 330:527-538(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.55 ANGSTROMS) OF 1-233 OF MUTANT ALA-140, HEME-BINDING SITES, MUTAGENESIS OF ASP-140.
+Additional computationally mapped references.

Web resources

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X06985 mRNA. Translation: CAA30045.1.
CR456505 mRNA. Translation: CAG30391.1.
AY460337 Genomic DNA. Translation: AAR23262.1.
Z82244 Genomic DNA. Translation: CAB05109.1.
M23041 mRNA. Translation: AAA50403.1.
X14782 Genomic DNA. Translation: CAA32886.1.
PIRS00325.
RefSeqNP_002124.1. NM_002133.2.
UniGeneHs.517581.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1N3UX-ray2.58A/B1-233[»]
1N45X-ray1.50A/B1-233[»]
1NI6X-ray2.10A/B/C/D1-224[»]
1OYKX-ray2.59A/B1-233[»]
1OYLX-ray1.59A/B1-233[»]
1OZEX-ray2.19A/B1-233[»]
1OZLX-ray1.58A/B1-233[»]
1OZRX-ray1.74A/B1-233[»]
1OZWX-ray1.55A/B1-233[»]
1S13X-ray2.29A/B1-233[»]
1S8CX-ray2.19A/B/C/D1-233[»]
1T5PX-ray2.11A/B1-233[»]
1TWNX-ray2.20A/B1-233[»]
1TWRX-ray2.10A/B1-233[»]
1XJZX-ray1.88A/B1-233[»]
1XK0X-ray2.18A/B1-233[»]
1XK1X-ray2.08A/B1-233[»]
1XK2X-ray2.20A/B1-233[»]
1XK3X-ray2.08A/B1-233[»]
3CZYX-ray1.54A/B1-233[»]
3HOKX-ray2.19A/B1-233[»]
3K4FX-ray2.17A/B1-233[»]
3TGMX-ray2.85A/B1-233[»]
ProteinModelPortalP09601.
SMRP09601. Positions 10-223.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid109405. 11 interactions.
IntActP09601. 8 interactions.
STRING9606.ENSP00000216117.

Chemistry

BindingDBP09601.
ChEMBLCHEMBL2823.
DrugBankDB00157. NADH.

PTM databases

PhosphoSiteP09601.

Polymorphism databases

DMDM123446.

Proteomic databases

PaxDbP09601.
PRIDEP09601.

Protocols and materials databases

DNASU3162.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000216117; ENSP00000216117; ENSG00000100292.
GeneID3162.
KEGGhsa:3162.
UCSCuc003ant.2. human.

Organism-specific databases

CTD3162.
GeneCardsGC22P035776.
HGNCHGNC:5013. HMOX1.
HPACAB017444.
HPA000635.
MIM141250. gene.
614034. phenotype.
neXtProtNX_P09601.
PharmGKBPA29341.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG5398.
HOGENOMHOG000233221.
HOVERGENHBG005982.
InParanoidP09601.
KOK00510.
OMAYAPLYFP.
PhylomeDBP09601.
TreeFamTF314786.

Enzyme and pathway databases

BioCycMetaCyc:HS02027-MONOMER.
ReactomeREACT_111217. Metabolism.
REACT_15518. Transmembrane transport of small molecules.

Gene expression databases

ArrayExpressP09601.
BgeeP09601.
CleanExHS_HMOX1.
GenevestigatorP09601.

Family and domain databases

Gene3D1.20.910.10. 1 hit.
InterProIPR002051. Haem_Oase.
IPR016053. Haem_Oase-like.
IPR016084. Haem_Oase-like_multi-hlx.
IPR018207. Haem_oxygenase_CS.
[Graphical view]
PANTHERPTHR10720. PTHR10720. 1 hit.
PfamPF01126. Heme_oxygenase. 1 hit.
[Graphical view]
PIRSFPIRSF000343. Haem_Oase. 1 hit.
PRINTSPR00088. HAEMOXYGNASE.
SUPFAMSSF48613. SSF48613. 1 hit.
PROSITEPS00593. HEME_OXYGENASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP09601.
GeneWikiHMOX1.
GenomeRNAi3162.
NextBio12538.
PROP09601.
SOURCESearch...

Entry information

Entry nameHMOX1_HUMAN
AccessionPrimary (citable) accession number: P09601
Entry history
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: July 1, 1989
Last modified: April 16, 2014
This is version 154 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 22

Human chromosome 22: entries, gene names and cross-references to MIM