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P36551 (HEM6_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 153. 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·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Oxygen-dependent coproporphyrinogen-III oxidase, mitochondrial

Short name=COX
Short name=Coprogen oxidase
Short name=Coproporphyrinogenase
EC=1.3.3.3
Gene names
Name:CPOX
Synonyms:CPO, CPX
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length454 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 the heme biosynthesis. Catalyzes the aerobic oxidative decarboxylation of propionate groups of rings A and B of coproporphyrinogen-III to yield the vinyl groups in protoporphyrinogen-IX.

Catalytic activity

Coproporphyrinogen-III + O2 + 2 H+ = protoporphyrinogen-IX + 2 CO2 + 2 H2O.

Pathway

Porphyrin-containing compound metabolism; protoporphyrin-IX biosynthesis; protoporphyrinogen-IX from coproporphyrinogen-III (O2 route): step 1/1.

Subunit structure

Homodimer. Ref.10

Subcellular location

Mitochondrion intermembrane space.

Involvement in disease

Hereditary coproporphyria (HCP) [MIM:121300]: A form of porphyria. Porphyrias are inherited defects in the biosynthesis of heme, resulting in the accumulation and increased excretion of porphyrins or porphyrin precursors. They are classified as erythropoietic or hepatic, depending on whether the enzyme deficiency occurs in red blood cells or in the liver. Hereditary coproporphyria is an acute hepatic porphyria characterized by skin photosensitivity, attacks of abdominal pain, neurological disturbances, and psychiatric symptoms. Most attacks are precipitated by drugs, alcohol, caloric deprivation, infections, or endocrine factors. Hereditary coproporphyria is biochemically characterized by overexcretion of coproporphyrin III in the urine and in the feces.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.11 Ref.12 Ref.13 Ref.14 Ref.15 Ref.16 Ref.17 Ref.18 Ref.19 Ref.20

Sequence similarities

Belongs to the aerobic coproporphyrinogen-III oxidase family.

Sequence caution

The sequence BAA04033.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

Ontologies

Keywords
   Biological processHeme biosynthesis
Porphyrin biosynthesis
   Cellular componentMitochondrion
   Coding sequence diversityPolymorphism
   DiseaseDisease mutation
   DomainTransit peptide
   Molecular functionOxidoreductase
   PTMAcetylation
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processheme biosynthetic process

Traceable author statement. Source: Reactome

porphyrin-containing compound metabolic process

Traceable author statement. Source: Reactome

protoporphyrinogen IX biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-UniPathway

response to arsenic-containing substance

Inferred from electronic annotation. Source: Ensembl

response to insecticide

Inferred from electronic annotation. Source: Ensembl

response to iron ion

Inferred from electronic annotation. Source: Ensembl

response to lead ion

Inferred from electronic annotation. Source: Ensembl

response to methylmercury

Inferred from electronic annotation. Source: Ensembl

small molecule metabolic process

Traceable author statement. Source: Reactome

   Cellular_componentmitochondrial inner membrane

Inferred from electronic annotation. Source: Ensembl

mitochondrial intermembrane space

Traceable author statement. Source: Reactome

mitochondrion

Inferred from direct assay. Source: HPA

   Molecular_functioncoproporphyrinogen oxidase activity

Traceable author statement. Source: Reactome

protein homodimerization activity

Inferred from direct assay Ref.10. Source: UniProtKB

structural constituent of eye lens

Inferred from electronic annotation. Source: Ensembl

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 110110Mitochondrion By similarity
Chain111 – 454344Oxygen-dependent coproporphyrinogen-III oxidase, mitochondrial
PRO_0000006029

Regions

Region193 – 20210Important for dimerization Probable
Region260 – 2623Substrate binding
Region392 – 42837Important for dimerization
Region411 – 4133Substrate binding

Sites

Active site2581Proton donor Ref.10
Binding site2441Substrate Probable
Site3271Important for dimerization

Amino acid modifications

Modified residue4041N6-acetyllysine; alternate By similarity
Modified residue4041N6-succinyllysine; alternate By similarity

Natural variations

Natural variant1351V → A in HCP. Ref.19
VAR_023444
Natural variant162 – 1687Missing in HCP.
VAR_002151
Natural variant1891G → S in HCP; <5% of activity. Ref.12
VAR_002152
Natural variant1971G → W in HCP. Ref.17
VAR_002153
Natural variant2011E → K in HCP. Ref.16
VAR_002154
Natural variant2081S → F in HCP. Ref.18
Corresponds to variant rs28929486 [ dbSNP | Ensembl ].
VAR_019067
Natural variant2141L → R in HCP. Ref.19
VAR_023445
Natural variant2491P → R in HCP. Ref.19
VAR_023446
Natural variant2491P → S in HCP. Ref.16
VAR_002155
Natural variant2721N → H. Ref.7 Ref.12
Corresponds to variant rs1131857 [ dbSNP | Ensembl ].
VAR_002156
Natural variant2791G → R in HCP; a patient carrying also the L-12 mutation in ALAD. Ref.20
VAR_058005
Natural variant2801G → R in HCP. Ref.14
VAR_002157
Natural variant2941V → I. Ref.3 Ref.5 Ref.12
Corresponds to variant rs2228056 [ dbSNP | Ensembl ].
VAR_002158
Natural variant2951H → D in HCP. Ref.15
VAR_002159
Natural variant3281R → C in HCP. Ref.18
Corresponds to variant rs28929487 [ dbSNP | Ensembl ].
VAR_019068
Natural variant3311R → W in HCP. Ref.11 Ref.18
VAR_002160
Natural variant3521R → C.
Corresponds to variant rs11921054 [ dbSNP | Ensembl ].
VAR_048827
Natural variant3901Missing in HCP. Ref.17
VAR_002161
Natural variant4041K → E in HCP; harderoporphyria form. Ref.13
VAR_002162
Natural variant4271W → R in HCP. Ref.17
VAR_002163
Natural variant4471R → C in HCP. Ref.18
Corresponds to variant rs28931603 [ dbSNP | Ensembl ].
VAR_019069

Experimental info

Mutagenesis392 – 41827Missing: Loss for dimerization. Ref.10
Sequence conflict2471I → T in CAA82250. Ref.7

Secondary structure

............................................ 454
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P36551 [UniParc].

Last modified June 7, 2005. Version 3.
Checksum: 6EC3D15FD8FD86B5

FASTA45450,152
        10         20         30         40         50         60 
MALQLGRLSS GPCWLVARGG CGGPRAWSQC GGGGLRAWSQ RSAAGRVCRP PGPAGTEQSR 

        70         80         90        100        110        120 
GLGHGSTSRG GPWVGTGLAA ALAGLVGLAT AAFGHVQRAE MLPKTSGTRA TSLGRPEEEE 

       130        140        150        160        170        180 
DELAHRCSSF MAPPVTDLGE LRRRPGDMKT KMELLILETQ AQVCQALAQV DGGANFSVDR 

       190        200        210        220        230        240 
WERKEGGGGI SCVLQDGCVF EKAGVSISVV HGNLSEEAAK QMRSRGKVLK TKDGKLPFCA 

       250        260        270        280        290        300 
MGVSSVIHPK NPHAPTIHFN YRYFEVEEAD GNKQWWFGGG CDLTPTYLNQ EDAVHFHRTL 

       310        320        330        340        350        360 
KEACDQHGPD LYPKFKKWCD DYFFIAHRGE RRGIGGIFFD DLDSPSKEEV FRFVQSCARA 

       370        380        390        400        410        420 
VVPSYIPLVK KHCDDSFTPQ EKLWQQLRRG RYVEFNLLYD RGTKFGLFTP GSRIESILMS 

       430        440        450 
LPLTARWEYM HSPSENSKEA EILEVLRHPR DWVR 

« Hide

References

« Hide 'large scale' references
[1]"Coproporphyrinogen oxidase: gene organization and description of a mutation leading to exon 6 skipping."
Delfau-Larue M.H., Martasek P., Grandchamp B.
Hum. Mol. Genet. 3:1325-1330(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Tissue: Placenta.
[2]"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. expand/collapse author list , 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].
Tissue: Thalamus.
[3]Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.
Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT ILE-294.
[4]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].
[5]"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], VARIANT ILE-294.
Tissue: Brain, Placenta and Uterus.
[6]"Molecular cloning, sequencing and expression of cDNA encoding human coproporphyrinogen oxidase."
Taketani S., Kohno H., Furukawa T., Yoshinaga T., Tokunaga R.
Biochim. Biophys. Acta 1183:547-549(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 73-454.
Tissue: Placenta.
[7]"Molecular cloning, sequencing, and functional expression of a cDNA encoding human coproporphyrinogen oxidase."
Martasek P., Camadro J.-M., Delfau-Larue M.H., Dumas J.B., Montagne J.J., de Verneuil H., Labbe P., Grandchamp B.
Proc. Natl. Acad. Sci. U.S.A. 91:3024-3028(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 101-454, VARIANT HIS-272.
Tissue: Foreskin.
[8]"The long, but not the short, presequence of human coproporphyrinogen oxidase is essential for its import and sorting to mitochondria."
Susa S., Daimon M., Ono H., Li S., Yoshida T., Kato T.
Tohoku J. Exp. Med. 200:39-45(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEOLYTIC PROCESSING.
[9]"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].
[10]"Structural basis of hereditary coproporphyria."
Lee D.-S., Flachsova E., Bodnarova M., Demeler B., Martasek P., Raman C.S.
Proc. Natl. Acad. Sci. U.S.A. 102:14232-14237(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.58 ANGSTROMS) OF 111-453 IN COMPLEX WITH CITRATE, MUTAGENESIS OF 392-TYR--LEU-418, ACTIVE SITE, SUBUNIT.
[11]"Homozygous hereditary coproporphyria caused by an arginine to tryptophane substitution in coproporphyrinogen oxidase and common intragenic polymorphisms."
Martasek P., Nordmann Y., Grandchamp B.
Hum. Mol. Genet. 3:477-480(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT HCP TRP-331.
[12]"Characterization and expression of cDNA encoding coproporphyrinogen oxidase from a patient with hereditary coproporphyria."
Fujita H., Kondo M., Taketani S., Nomura N., Furuyama K., Akagi R., Nagai T., Terajima M., Galbraith R.A., Sassa S.
Hum. Mol. Genet. 3:1807-1810(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT HCP SER-189, VARIANTS HIS-272 AND ILE-294.
[13]"A molecular defect in coproporphyrinogen oxidase gene causing harderoporphyria, a variant form of hereditary coproporphyria."
Lamoril J., Martasek P., Deybach J.-C., da Silva V., Grandchamp B., Nordmann Y.
Hum. Mol. Genet. 4:275-278(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT HCP GLU-404.
[14]"A novel missense mutation in exon 4 of the human coproporphyrinogen oxidase gene in two patients with hereditary coproporphyria."
Daimon M., Gojyou E., Sugawara M., Yamatani K., Tominaga M., Sasaki H.
Hum. Genet. 99:199-201(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT HCP ARG-280.
[15]"Three novel mutations in the coproporphyrinogen oxidase gene."
Lamoril J., Deybach J.-C., Puy H., Grandchamp B., Nordmann Y.
Hum. Mutat. 9:78-80(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS HCP 162-GLN--ALA-168 DEL AND ASP-295.
[16]"Hereditary coproporphyria: exon screening by heteroduplex analysis detects three novel mutations in the coproporphyrinogen oxidase gene."
Schreiber W.E., Zhang X., Senz J., Jamani A.
Hum. Mutat. 10:196-200(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS HCP LYS-201 AND SER-249.
[17]"Systematic analysis of coproporphyrinogen oxidase gene defects in hereditary coproporphyria and mutation update."
Rosipal R., Lamoril J., Puy H., da Silva V., Gouya L., de Rooij F.W.M., Te Velde K., Nordmann Y., Martasek P., Deybach J.-C.
Hum. Mutat. 13:44-53(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS HCP TRP-197; GLY-390 DEL AND ARG-427.
[18]"Two novel mutations and coexistence of the 991C>T and the 1339C>T mutation on a single allele in the coproporphyrinogen oxidase gene in Swedish patients with hereditary coproporphyria."
Wiman A., Floderus Y., Harper P.
J. Hum. Genet. 47:407-412(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS HCP PHE-208; CYS-328; TRP-331 AND CYS-447.
[19]"Biochemical and genetic characterization of four cases of hereditary coproporphyria in Spain."
To-Figueras J., Badenas C., Enriquez M.T., Segura S., Alvarez C., Mila M., Lecha M., Herrero C.
Mol. Genet. Metab. 85:160-163(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS HCP ALA-135; ARG-214 AND ARG-249.
[20]"Dual gene defects involving delta-aminolaevulinate dehydratase and coproporphyrinogen oxidase in a porphyria patient."
Akagi R., Inoue R., Muranaka S., Tahara T., Taketani S., Anderson K.E., Phillips J.D., Sassa S.
Br. J. Haematol. 132:237-243(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT HCP ARG-279.
[21]Erratum
Akagi R., Inoue R., Muranaka S., Tahara T., Taketani S., Anderson K.E., Phillips J.D., Sassa S.
Br. J. Haematol. 132:662-662(2006)
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
Z34531 expand/collapse EMBL AC list , Z34803, Z34804, Z34805, Z34806, Z34807, Z34808 Genomic DNA. Translation: CAA84292.1.
AK290140 mRNA. Translation: BAF82829.1.
AK223481 mRNA. Translation: BAD97201.1.
CH471052 Genomic DNA. Translation: EAW79854.1.
BC017210 mRNA. Translation: AAH17210.1.
BC023551 mRNA. Translation: AAH23551.1.
BC023554 mRNA. Translation: AAH23554.1.
D16611 mRNA. Translation: BAA04033.1. Different initiation.
Z28409 mRNA. Translation: CAA82250.1.
CCDSCCDS2932.1.
PIRI52444.
RefSeqNP_000088.3. NM_000097.5.
UniGeneHs.476982.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2AEXX-ray1.58A111-454[»]
ProteinModelPortalP36551.
SMRP36551. Positions 119-454.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid107763. 6 interactions.
IntActP36551. 1 interaction.
STRING9606.ENSP00000264193.

Chemistry

ChEMBLCHEMBL1681618.

PTM databases

PhosphoSiteP36551.

Polymorphism databases

DMDM67476671.

Proteomic databases

MaxQBP36551.
PaxDbP36551.
PeptideAtlasP36551.
PRIDEP36551.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000264193; ENSP00000264193; ENSG00000080819.
GeneID1371.
KEGGhsa:1371.
UCSCuc003dsx.3. human.

Organism-specific databases

CTD1371.
GeneCardsGC03M098239.
GeneReviewsCPOX.
HGNCHGNC:2321. CPOX.
HPAHPA015736.
HPA054448.
MIM121300. phenotype.
612732. gene.
neXtProtNX_P36551.
Orphanet79273. Hereditary coproporphyria.
PharmGKBPA134979958.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0408.
HOGENOMHOG000262768.
HOVERGENHBG051897.
InParanoidP36551.
KOK00228.
OMARYFETAN.
PhylomeDBP36551.
TreeFamTF300703.

Enzyme and pathway databases

BioCycMetaCyc:HS01369-MONOMER.
BRENDA1.3.3.3. 2681.
ReactomeREACT_111217. Metabolism.
UniPathwayUPA00251; UER00322.

Gene expression databases

ArrayExpressP36551.
BgeeP36551.
CleanExHS_CPO.
HS_CPOX.
GenevestigatorP36551.

Family and domain databases

Gene3D3.40.1500.10. 1 hit.
InterProIPR001260. Coprogen_oxidase_aer.
IPR018375. Coprogen_oxidase_CS.
[Graphical view]
PANTHERPTHR10755. PTHR10755. 1 hit.
PfamPF01218. Coprogen_oxidas. 1 hit.
[Graphical view]
PRINTSPR00073. COPRGNOXDASE.
SUPFAMSSF102886. SSF102886. 1 hit.
PROSITEPS01021. COPROGEN_OXIDASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP36551.
GeneWikiCoproporphyrinogen_III_oxidase.
GenomeRNAi1371.
NextBio5561.
PROP36551.
SOURCESearch...

Entry information

Entry nameHEM6_HUMAN
AccessionPrimary (citable) accession number: P36551
Secondary accession number(s): A8K275 expand/collapse secondary AC list , Q14060, Q53F08, Q8IZ45, Q96AF3
Entry history
Integrated into UniProtKB/Swiss-Prot: June 1, 1994
Last sequence update: June 7, 2005
Last modified: July 9, 2014
This is version 153 of the entry and version 3 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 3

Human chromosome 3: entries, gene names and cross-references to MIM