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P30519

- HMOX2_HUMAN

UniProt

P30519 - HMOX2_HUMAN

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Protein

Heme oxygenase 2

Gene

HMOX2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

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. Heme oxygenase 2 could be implicated in the production of carbon monoxide in brain where it could act as a neurotransmitter.

Catalytic activityi

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi45 – 451Iron (heme axial ligand)

GO - Molecular functioni

  1. heme oxygenase (decyclizing) activity Source: UniProtKB
  2. metal ion binding Source: UniProtKB-KW

GO - Biological processi

  1. cellular iron ion homeostasis Source: Reactome
  2. heme catabolic process Source: Reactome
  3. heme oxidation Source: InterPro
  4. porphyrin-containing compound metabolic process Source: Reactome
  5. response to hypoxia Source: UniProtKB
  6. response to oxidative stress Source: Ensembl
  7. small molecule metabolic process Source: Reactome
  8. transmembrane transport Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

Heme, Iron, Metal-binding

Enzyme and pathway databases

ReactomeiREACT_22297. Heme degradation.
REACT_25060. Iron uptake and transport.

Names & Taxonomyi

Protein namesi
Recommended name:
Heme oxygenase 2 (EC:1.14.99.3)
Short name:
HO-2
Gene namesi
Name:HMOX2
Synonyms:HO2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 16

Organism-specific databases

HGNCiHGNC:5014. HMOX2.

Subcellular locationi

GO - Cellular componenti

  1. endoplasmic reticulum membrane Source: Reactome
  2. membrane Source: UniProtKB
  3. plasma membrane Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Microsome

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA29342.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed2 Publications
Chaini2 – 316315Heme oxygenase 2PRO_0000209691Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserine2 Publications

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiP30519.
PaxDbiP30519.
PRIDEiP30519.

PTM databases

PhosphoSiteiP30519.

Miscellaneous databases

PMAP-CutDBP30519.

Expressioni

Inductioni

Heme oxygenase 2 activity is non-inducible.

Gene expression databases

BgeeiP30519.
CleanExiHS_HMOX2.
ExpressionAtlasiP30519. baseline and differential.
GenevestigatoriP30519.

Organism-specific databases

HPAiCAB025464.
HPA040611.

Interactioni

Protein-protein interaction databases

BioGridi109406. 44 interactions.
DIPiDIP-53564N.
IntActiP30519. 34 interactions.
MINTiMINT-1384587.
STRINGi9606.ENSP00000219700.

Structurei

Secondary structure

1
316
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi33 – 408Combined sources
Helixi42 – 498Combined sources
Helixi52 – 587Combined sources
Helixi64 – 8724Combined sources
Turni88 – 903Combined sources
Turni92 – 943Combined sources
Helixi95 – 973Combined sources
Helixi100 – 1034Combined sources
Helixi106 – 11712Combined sources
Helixi121 – 1244Combined sources
Helixi129 – 14416Combined sources
Helixi146 – 1483Combined sources
Helixi149 – 17527Combined sources
Helixi185 – 1873Combined sources
Helixi195 – 20814Combined sources
Helixi213 – 23826Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2Q32X-ray2.40A/B1-264[»]
2QPPX-ray2.61A/B1-264[»]
2RGZX-ray2.61A/B1-264[»]
ProteinModelPortaliP30519.
SMRiP30519. Positions 30-248.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP30519.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati264 – 2696HRM 1
Repeati281 – 2866HRM 2

Sequence similaritiesi

Belongs to the heme oxygenase family.Curated

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiCOG5398.
GeneTreeiENSGT00390000017673.
HOGENOMiHOG000233221.
HOVERGENiHBG005982.
InParanoidiP30519.
KOiK00510.
OMAiMDRNKDH.
PhylomeDBiP30519.
TreeFamiTF314786.

Family and domain databases

Gene3Di1.20.910.10. 1 hit.
InterProiIPR002051. Haem_Oase.
IPR016053. Haem_Oase-like.
IPR016084. Haem_Oase-like_multi-hlx.
IPR018207. Haem_oxygenase_CS.
[Graphical view]
PANTHERiPTHR10720. PTHR10720. 1 hit.
PfamiPF01126. Heme_oxygenase. 1 hit.
[Graphical view]
PIRSFiPIRSF000343. Haem_Oase. 1 hit.
PRINTSiPR00088. HAEMOXYGNASE.
SUPFAMiSSF48613. SSF48613. 1 hit.
PROSITEiPS00593. HEME_OXYGENASE. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: P30519-1) [UniParc]FASTAAdd to Basket

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.

« Hide

        10         20         30         40         50
MSAEVETSEG VDESEKKNSG ALEKENQMRM ADLSELLKEG TKEAHDRAEN
60 70 80 90 100
TQFVKDFLKG NIKKELFKLA TTALYFTYSA LEEEMERNKD HPAFAPLYFP
110 120 130 140 150
MELHRKEALT KDMEYFFGEN WEEQVQCPKA AQKYVERIHY IGQNEPELLV
160 170 180 190 200
AHAYTRYMGD LSGGQVLKKV AQRALKLPST GEGTQFYLFE NVDNAQQFKQ
210 220 230 240 250
LYRARMNALD LNMKTKERIV EEANKAFEYN MQIFNELDQA GSTLARETLE
260 270 280 290 300
DGFPVHDGKG DMRKCPFYAA EQDKGALEGS SCPFRTAMAV LRKPSLQFIL
310
AAGVALAAGL LAWYYM
Length:316
Mass (Da):36,033
Last modified:November 1, 1995 - v2
Checksum:iBF4B6A341F1A81AC
GO
Isoform 2 (identifier: P30519-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-29: Missing.

Show »
Length:287
Mass (Da):32,837
Checksum:iE03CE816D6C72A30
GO

Sequence cautioni

The sequence W38932 differs from that shown. Reason: Frameshift at position 82. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti107 – 1071E → T in W38932. 1 PublicationCurated
Sequence conflicti165 – 1662QV → KC in AAC05297. 1 PublicationCurated
Sequence conflicti222 – 2221Missing in AAB22110. (PubMed:1575508)Curated
Sequence conflicti276 – 2761Missing in AAB22110. (PubMed:1575508)Curated
Sequence conflicti281 – 2888SCPFRTAM → LSLPTSY in AAB22110. (PubMed:1575508)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti137 – 1371R → Q.1 Publication
Corresponds to variant rs17884623 [ dbSNP | Ensembl ].
VAR_021067
Natural varianti146 – 1461P → L.1 Publication
Corresponds to variant rs17880805 [ dbSNP | Ensembl ].
VAR_021068

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 2929Missing in isoform 2. 1 PublicationVSP_055031Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D21243 mRNA. Translation: BAA04789.1.
S34389 mRNA. Translation: AAB22110.2.
BT019788 mRNA. Translation: AAV38591.1.
AY771350 Genomic DNA. Translation: AAV28730.1.
AC007606 Genomic DNA. No translation available.
CH471112 Genomic DNA. Translation: EAW85299.1.
CH471112 Genomic DNA. Translation: EAW85300.1.
BC002396 mRNA. Translation: AAH02396.1.
W38932 mRNA. No translation available.
AF051306 mRNA. Translation: AAC05297.1.
CCDSiCCDS10517.1. [P30519-1]
CCDS66931.1. [P30519-2]
PIRiI60119.
S21700.
RefSeqiNP_001120676.1. NM_001127204.1. [P30519-1]
NP_001120677.1. NM_001127205.1. [P30519-1]
NP_001120678.1. NM_001127206.2. [P30519-1]
NP_001273196.1. NM_001286267.1.
NP_001273197.1. NM_001286268.1. [P30519-1]
NP_001273198.1. NM_001286269.1. [P30519-1]
NP_001273199.1. NM_001286270.1. [P30519-1]
NP_001273200.1. NM_001286271.1. [P30519-2]
NP_002125.3. NM_002134.3. [P30519-1]
UniGeneiHs.284279.

Genome annotation databases

EnsembliENST00000219700; ENSP00000219700; ENSG00000103415. [P30519-1]
ENST00000398595; ENSP00000381595; ENSG00000103415. [P30519-1]
ENST00000406590; ENSP00000385100; ENSG00000103415. [P30519-1]
ENST00000414777; ENSP00000391637; ENSG00000103415. [P30519-1]
ENST00000458134; ENSP00000394103; ENSG00000103415. [P30519-1]
ENST00000570646; ENSP00000459214; ENSG00000103415. [P30519-1]
ENST00000575120; ENSP00000460926; ENSG00000103415. [P30519-2]
ENST00000612525; ENSP00000481295; ENSG00000277424. [P30519-1]
ENST00000615778; ENSP00000484422; ENSG00000277424. [P30519-1]
ENST00000619528; ENSP00000484423; ENSG00000103415. [P30519-1]
ENST00000619913; ENSP00000484467; ENSG00000103415. [P30519-1]
ENST00000620445; ENSP00000478785; ENSG00000277424. [P30519-1]
ENST00000621065; ENSP00000481811; ENSG00000277424. [P30519-1]
ENST00000622146; ENSP00000483319; ENSG00000277424. [P30519-2]
GeneIDi3163.
KEGGihsa:3163.
UCSCiuc002cwq.4. human. [P30519-1]

Polymorphism databases

DMDMi1170328.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Web resourcesi

NIEHS-SNPs

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D21243 mRNA. Translation: BAA04789.1 .
S34389 mRNA. Translation: AAB22110.2 .
BT019788 mRNA. Translation: AAV38591.1 .
AY771350 Genomic DNA. Translation: AAV28730.1 .
AC007606 Genomic DNA. No translation available.
CH471112 Genomic DNA. Translation: EAW85299.1 .
CH471112 Genomic DNA. Translation: EAW85300.1 .
BC002396 mRNA. Translation: AAH02396.1 .
W38932 mRNA. No translation available.
AF051306 mRNA. Translation: AAC05297.1 .
CCDSi CCDS10517.1. [P30519-1 ]
CCDS66931.1. [P30519-2 ]
PIRi I60119.
S21700.
RefSeqi NP_001120676.1. NM_001127204.1. [P30519-1 ]
NP_001120677.1. NM_001127205.1. [P30519-1 ]
NP_001120678.1. NM_001127206.2. [P30519-1 ]
NP_001273196.1. NM_001286267.1.
NP_001273197.1. NM_001286268.1. [P30519-1 ]
NP_001273198.1. NM_001286269.1. [P30519-1 ]
NP_001273199.1. NM_001286270.1. [P30519-1 ]
NP_001273200.1. NM_001286271.1. [P30519-2 ]
NP_002125.3. NM_002134.3. [P30519-1 ]
UniGenei Hs.284279.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2Q32 X-ray 2.40 A/B 1-264 [» ]
2QPP X-ray 2.61 A/B 1-264 [» ]
2RGZ X-ray 2.61 A/B 1-264 [» ]
ProteinModelPortali P30519.
SMRi P30519. Positions 30-248.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 109406. 44 interactions.
DIPi DIP-53564N.
IntActi P30519. 34 interactions.
MINTi MINT-1384587.
STRINGi 9606.ENSP00000219700.

Chemistry

ChEMBLi CHEMBL2546.

PTM databases

PhosphoSitei P30519.

Polymorphism databases

DMDMi 1170328.

Proteomic databases

MaxQBi P30519.
PaxDbi P30519.
PRIDEi P30519.

Protocols and materials databases

DNASUi 3163.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000219700 ; ENSP00000219700 ; ENSG00000103415 . [P30519-1 ]
ENST00000398595 ; ENSP00000381595 ; ENSG00000103415 . [P30519-1 ]
ENST00000406590 ; ENSP00000385100 ; ENSG00000103415 . [P30519-1 ]
ENST00000414777 ; ENSP00000391637 ; ENSG00000103415 . [P30519-1 ]
ENST00000458134 ; ENSP00000394103 ; ENSG00000103415 . [P30519-1 ]
ENST00000570646 ; ENSP00000459214 ; ENSG00000103415 . [P30519-1 ]
ENST00000575120 ; ENSP00000460926 ; ENSG00000103415 . [P30519-2 ]
ENST00000612525 ; ENSP00000481295 ; ENSG00000277424 . [P30519-1 ]
ENST00000615778 ; ENSP00000484422 ; ENSG00000277424 . [P30519-1 ]
ENST00000619528 ; ENSP00000484423 ; ENSG00000103415 . [P30519-1 ]
ENST00000619913 ; ENSP00000484467 ; ENSG00000103415 . [P30519-1 ]
ENST00000620445 ; ENSP00000478785 ; ENSG00000277424 . [P30519-1 ]
ENST00000621065 ; ENSP00000481811 ; ENSG00000277424 . [P30519-1 ]
ENST00000622146 ; ENSP00000483319 ; ENSG00000277424 . [P30519-2 ]
GeneIDi 3163.
KEGGi hsa:3163.
UCSCi uc002cwq.4. human. [P30519-1 ]

Organism-specific databases

CTDi 3163.
GeneCardsi GC16P004524.
HGNCi HGNC:5014. HMOX2.
HPAi CAB025464.
HPA040611.
MIMi 141251. gene.
neXtProti NX_P30519.
PharmGKBi PA29342.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG5398.
GeneTreei ENSGT00390000017673.
HOGENOMi HOG000233221.
HOVERGENi HBG005982.
InParanoidi P30519.
KOi K00510.
OMAi MDRNKDH.
PhylomeDBi P30519.
TreeFami TF314786.

Enzyme and pathway databases

Reactomei REACT_22297. Heme degradation.
REACT_25060. Iron uptake and transport.

Miscellaneous databases

ChiTaRSi HMOX2. human.
EvolutionaryTracei P30519.
GeneWikii HMOX2.
GenomeRNAii 3163.
NextBioi 12542.
PMAP-CutDB P30519.
PROi P30519.
SOURCEi Search...

Gene expression databases

Bgeei P30519.
CleanExi HS_HMOX2.
ExpressionAtlasi P30519. baseline and differential.
Genevestigatori P30519.

Family and domain databases

Gene3Di 1.20.910.10. 1 hit.
InterProi IPR002051. Haem_Oase.
IPR016053. Haem_Oase-like.
IPR016084. Haem_Oase-like_multi-hlx.
IPR018207. Haem_oxygenase_CS.
[Graphical view ]
PANTHERi PTHR10720. PTHR10720. 1 hit.
Pfami PF01126. Heme_oxygenase. 1 hit.
[Graphical view ]
PIRSFi PIRSF000343. Haem_Oase. 1 hit.
PRINTSi PR00088. HAEMOXYGNASE.
SUPFAMi SSF48613. SSF48613. 1 hit.
PROSITEi PS00593. HEME_OXYGENASE. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Heme oxygenase-2. Properties of the heme complex of the purified tryptic fragment of recombinant human heme oxygenase-2."
    Ishikawa K.
    J. Biol. Chem. 270:6345-6350(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    Tissue: Placenta.
  2. "Human heme oxygenase-2: characterization and expression of a full-length cDNA and evidence suggesting that the two HO-2 transcripts may differ by choice of polyadenylation signal."
    McCoubrey W.K. Jr., Ewing J.F., Maines M.D.
    Arch. Biochem. Biophys. 295:13-20(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    Tissue: Kidney.
  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] (ISOFORM 1).
  4. NIEHS SNPs program
    Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS GLN-137 AND LEU-146.
  5. "The sequence and analysis of duplication-rich human chromosome 16."
    Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., Xie G., Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E., Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J.
    , Buckingham J.M., Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C., Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M., Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M., Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D., Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L., Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E., Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H., Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y., Lowry S., Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J., Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D., Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., Rash S., Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A., Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M., Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H., Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A., Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J., DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J., Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M., Myers R.M., Rubin E.M., Pennacchio L.A.
    Nature 432:988-994(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  7. "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] (ISOFORM 1).
    Tissue: Lung.
  8. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-148 (ISOFORM 2).
  9. Bienvenut W.V., Bilsland A.E., Keith W.N.
    Submitted (JAN-2010) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 2-17; 30-38; 48-59; 138-168; 206-214 AND 219-246, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: Colon carcinoma and Ovarian carcinoma.
  10. Follett J., Ahn J.-Y.
    Submitted (FEB-1998) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 10-166.
    Tissue: Intestine.
  11. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
    Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
    Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  12. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  13. "Comparison of apo- and heme-bound crystal structures of a truncated human heme oxygenase-2."
    Bianchetti C.M., Yi L., Ragsdale S.W., Phillips G.N. Jr.
    J. Biol. Chem. 282:37624-37631(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 1-264, HEME-BINDING SITE.

Entry informationi

Entry nameiHMOX2_HUMAN
AccessioniPrimary (citable) accession number: P30519
Secondary accession number(s): A8MT35
, D3DUD5, I3L430, O60605
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1993
Last sequence update: November 1, 1995
Last modified: November 26, 2014
This is version 149 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 16
    Human chromosome 16: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3