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P02790

- HEMO_HUMAN

UniProt

P02790 - HEMO_HUMAN

Protein

Hemopexin

Gene

HPX

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 151 (01 Oct 2014)
      Sequence version 2 (01 Oct 1996)
      Previous versions | rss
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    Functioni

    Binds heme and transports it to the liver for breakdown and iron recovery, after which the free hemopexin returns to the circulation.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi79 – 791Iron (heme 1 axial ligand)By similarity
    Metal bindingi150 – 1501Iron (heme 1 axial ligand)By similarity
    Metal bindingi236 – 2361Iron (heme 2 axial ligand)By similarity
    Metal bindingi293 – 2931Iron (heme 2 axial ligand)By similarity

    GO - Molecular functioni

    1. heme transporter activity Source: ProtInc
    2. metal ion binding Source: UniProtKB-KW
    3. protein binding Source: UniProtKB

    GO - Biological processi

    1. cellular iron ion homeostasis Source: ProtInc
    2. heme metabolic process Source: Ensembl
    3. heme transport Source: ProtInc
    4. hemoglobin metabolic process Source: Ensembl
    5. positive regulation of humoral immune response mediated by circulating immunoglobulin Source: Ensembl
    6. positive regulation of immunoglobulin production Source: Ensembl
    7. positive regulation of interferon-gamma-mediated signaling pathway Source: Ensembl
    8. positive regulation of tyrosine phosphorylation of Stat1 protein Source: Ensembl
    9. viral process Source: UniProtKB-KW

    Keywords - Biological processi

    Host-virus interaction, Transport

    Keywords - Ligandi

    Heme, Iron, Metal-binding

    Enzyme and pathway databases

    ReactomeiREACT_160163. Scavenging of heme from plasma.

    Protein family/group databases

    TCDBi1.C.39.8.3. the membrane attack complex/perforin (macpf) family.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Hemopexin
    Alternative name(s):
    Beta-1B-glycoprotein
    Gene namesi
    Name:HPX
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 11

    Organism-specific databases

    HGNCiHGNC:5171. HPX.

    Subcellular locationi

    GO - Cellular componenti

    1. blood microparticle Source: UniProt
    2. endocytic vesicle lumen Source: Reactome
    3. extracellular region Source: UniProtKB
    4. extracellular space Source: UniProt
    5. extracellular vesicular exosome Source: UniProt

    Keywords - Cellular componenti

    Secreted

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA29441.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 23232 PublicationsAdd
    BLAST
    Chaini24 – 462439Hemopexin1 PublicationPRO_0000021406Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi24 – 241O-linked (GalNAc...)3 Publications
    Glycosylationi29 – 291O-linked (GalNAc...)1 Publication
    Disulfide bondi50 ↔ 2311 Publication
    Glycosylationi64 – 641N-linked (GlcNAc...) (complex)3 Publications
    Disulfide bondi149 ↔ 1541 Publication
    Glycosylationi187 – 1871N-linked (GlcNAc...) (complex)8 Publications
    Disulfide bondi188 ↔ 2001 Publication
    Glycosylationi240 – 2401N-linked (GlcNAc...)3 Publications
    Glycosylationi246 – 2461N-linked (GlcNAc...)3 Publications
    Disulfide bondi257 ↔ 4601 Publication
    Disulfide bondi366 ↔ 4081 Publication
    Disulfide bondi418 ↔ 4351 Publication
    Glycosylationi453 – 4531N-linked (GlcNAc...) (complex)6 Publications

    Post-translational modificationi

    N- and O-glycosylated. O-glycosylated with core 1 or possibly core 8 glycans. O-glycosylation in the 30-40 region is minor compared to glycosylation at Thr-24 and Thr-29.9 Publications

    Keywords - PTMi

    Disulfide bond, Glycoprotein

    Proteomic databases

    PaxDbiP02790.
    PeptideAtlasiP02790.
    PRIDEiP02790.

    2D gel databases

    DOSAC-COBS-2DPAGEP02790.
    REPRODUCTION-2DPAGEIPI00022488.
    SWISS-2DPAGEP02790.

    PTM databases

    PhosphoSiteiP02790.

    Expressioni

    Tissue specificityi

    Expressed by the liver and secreted in plasma.

    Gene expression databases

    BgeeiP02790.
    CleanExiHS_HPX.
    GenevestigatoriP02790.

    Organism-specific databases

    HPAiCAB016725.

    Interactioni

    Subunit structurei

    Interacts with HEV ORF3 protein. Interacts with FLVCR1.2 Publications

    Protein-protein interaction databases

    BioGridi109500. 3 interactions.
    DIPiDIP-38339N.
    IntActiP02790. 3 interactions.
    STRINGi9606.ENSP00000265983.

    Structurei

    3D structure databases

    ProteinModelPortaliP02790.
    SMRiP02790. Positions 48-462.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Repeati53 – 9341Hemopexin 1Add
    BLAST
    Repeati94 – 13946Hemopexin 2Add
    BLAST
    Repeati140 – 18445Hemopexin 3Add
    BLAST
    Repeati185 – 23147Hemopexin 4Add
    BLAST
    Repeati259 – 30446Hemopexin 5Add
    BLAST
    Repeati305 – 35248Hemopexin 6Add
    BLAST
    Repeati357 – 39640Hemopexin 7Add
    BLAST
    Repeati400 – 45051Hemopexin 8Add
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni30 – 4011O-glycosylated at one siteAdd
    BLAST

    Sequence similaritiesi

    Belongs to the hemopexin family.Curated
    Contains 8 hemopexin repeats.Curated

    Keywords - Domaini

    Repeat, Signal

    Phylogenomic databases

    eggNOGiNOG251805.
    HOGENOMiHOG000112887.
    HOVERGENiHBG005956.
    InParanoidiP02790.
    OMAiAVECHRG.
    OrthoDBiEOG7Q8CN5.
    PhylomeDBiP02790.
    TreeFamiTF331201.

    Family and domain databases

    Gene3Di2.110.10.10. 2 hits.
    InterProiIPR000585. Hemopexin-like_dom.
    IPR018487. Hemopexin-like_repeat.
    IPR016358. Hemopexin_chordata.
    IPR018486. Hemopexin_CS.
    [Graphical view]
    PfamiPF00045. Hemopexin. 5 hits.
    [Graphical view]
    PIRSFiPIRSF002551. Hemopexin_chordata. 1 hit.
    SMARTiSM00120. HX. 5 hits.
    [Graphical view]
    SUPFAMiSSF50923. SSF50923. 2 hits.
    PROSITEiPS00024. HEMOPEXIN. 2 hits.
    PS51642. HEMOPEXIN_2. 8 hits.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    P02790-1 [UniParc]FASTAAdd to Basket

    « Hide

    MARVLGAPVA LGLWSLCWSL AIATPLPPTS AHGNVAEGET KPDPDVTERC    50
    SDGWSFDATT LDDNGTMLFF KGEFVWKSHK WDRELISERW KNFPSPVDAA 100
    FRQGHNSVFL IKGDKVWVYP PEKKEKGYPK LLQDEFPGIP SPLDAAVECH 150
    RGECQAEGVL FFQGDREWFW DLATGTMKER SWPAVGNCSS ALRWLGRYYC 200
    FQGNQFLRFD PVRGEVPPRY PRDVRDYFMP CPGRGHGHRN GTGHGNSTHH 250
    GPEYMRCSPH LVLSALTSDN HGATYAFSGT HYWRLDTSRD GWHSWPIAHQ 300
    WPQGPSAVDA AFSWEEKLYL VQGTQVYVFL TKGGYTLVSG YPKRLEKEVG 350
    TPHGIILDSV DAAFICPGSS RLHIMAGRRL WWLDLKSGAQ ATWTELPWPH 400
    EKVDGALCME KSLGPNSCSA NGPGLYLIHG PNLYCYSDVE KLNAAKALPQ 450
    PQNVTSLLGC TH 462
    Length:462
    Mass (Da):51,676
    Last modified:October 1, 1996 - v2
    Checksum:i054B44D0603763B8
    GO

    Sequence cautioni

    The sequence CAA26382.1 differs from that shown. Reason: Erroneous initiation.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti411 – 4111K → R in BAG36404. (PubMed:14702039)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti52 – 521D → N.
    Corresponds to variant rs10839564 [ dbSNP | Ensembl ].
    VAR_047137
    Natural varianti83 – 831R → W.
    Corresponds to variant rs12117 [ dbSNP | Ensembl ].
    VAR_033990

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M36803
    , M36796, M36799, M36800, M36801, M36802 Genomic DNA. Translation: AAA58678.1.
    AK313648 mRNA. Translation: BAG36404.1.
    J03048 mRNA. Translation: AAA52704.1.
    X02537 mRNA. Translation: CAA26382.1. Different initiation.
    CCDSiCCDS7763.1.
    PIRiI56456. OQHU.
    RefSeqiNP_000604.1. NM_000613.2.
    XP_005252940.1. XM_005252883.1.
    UniGeneiHs.426485.

    Genome annotation databases

    EnsembliENST00000265983; ENSP00000265983; ENSG00000110169.
    GeneIDi3263.
    KEGGihsa:3263.
    UCSCiuc001mdg.2. human.

    Polymorphism databases

    DMDMi1708182.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M36803
    , M36796 , M36799 , M36800 , M36801 , M36802 Genomic DNA. Translation: AAA58678.1 .
    AK313648 mRNA. Translation: BAG36404.1 .
    J03048 mRNA. Translation: AAA52704.1 .
    X02537 mRNA. Translation: CAA26382.1 . Different initiation.
    CCDSi CCDS7763.1.
    PIRi I56456. OQHU.
    RefSeqi NP_000604.1. NM_000613.2.
    XP_005252940.1. XM_005252883.1.
    UniGenei Hs.426485.

    3D structure databases

    ProteinModelPortali P02790.
    SMRi P02790. Positions 48-462.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 109500. 3 interactions.
    DIPi DIP-38339N.
    IntActi P02790. 3 interactions.
    STRINGi 9606.ENSP00000265983.

    Protein family/group databases

    TCDBi 1.C.39.8.3. the membrane attack complex/perforin (macpf) family.

    PTM databases

    PhosphoSitei P02790.

    Polymorphism databases

    DMDMi 1708182.

    2D gel databases

    DOSAC-COBS-2DPAGE P02790.
    REPRODUCTION-2DPAGE IPI00022488.
    SWISS-2DPAGE P02790.

    Proteomic databases

    PaxDbi P02790.
    PeptideAtlasi P02790.
    PRIDEi P02790.

    Protocols and materials databases

    DNASUi 3263.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000265983 ; ENSP00000265983 ; ENSG00000110169 .
    GeneIDi 3263.
    KEGGi hsa:3263.
    UCSCi uc001mdg.2. human.

    Organism-specific databases

    CTDi 3263.
    GeneCardsi GC11M006452.
    HGNCi HGNC:5171. HPX.
    HPAi CAB016725.
    MIMi 142290. gene.
    neXtProti NX_P02790.
    PharmGKBi PA29441.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG251805.
    HOGENOMi HOG000112887.
    HOVERGENi HBG005956.
    InParanoidi P02790.
    OMAi AVECHRG.
    OrthoDBi EOG7Q8CN5.
    PhylomeDBi P02790.
    TreeFami TF331201.

    Enzyme and pathway databases

    Reactomei REACT_160163. Scavenging of heme from plasma.

    Miscellaneous databases

    ChiTaRSi HPX. human.
    GeneWikii Hemopexin.
    GenomeRNAii 3263.
    NextBioi 12957.
    PROi P02790.
    SOURCEi Search...

    Gene expression databases

    Bgeei P02790.
    CleanExi HS_HPX.
    Genevestigatori P02790.

    Family and domain databases

    Gene3Di 2.110.10.10. 2 hits.
    InterProi IPR000585. Hemopexin-like_dom.
    IPR018487. Hemopexin-like_repeat.
    IPR016358. Hemopexin_chordata.
    IPR018486. Hemopexin_CS.
    [Graphical view ]
    Pfami PF00045. Hemopexin. 5 hits.
    [Graphical view ]
    PIRSFi PIRSF002551. Hemopexin_chordata. 1 hit.
    SMARTi SM00120. HX. 5 hits.
    [Graphical view ]
    SUPFAMi SSF50923. SSF50923. 2 hits.
    PROSITEi PS00024. HEMOPEXIN. 2 hits.
    PS51642. HEMOPEXIN_2. 8 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Structure of the human hemopexin gene and evidence for intron-mediated evolution."
      Altruda F., Poli V., Restagno G., Silengo L.
      J. Mol. Evol. 27:102-108(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    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.
      , 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: Mammary gland.
    3. "The hemopexin gene maps to the same location as the beta-globin gene cluster on human chromosome 11."
      Law M.L., Cai G.Y., Hartz J.A., Jones C., Kao F.T.
      Genomics 3:48-52(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 2-462.
    4. "The primary structure of human hemopexin deduced from cDNA sequence: evidence for internal, repeating homology."
      Altruda F., Poli V., Restagno G., Argos P., Cortese R., Silengo L.
      Nucleic Acids Res. 13:3841-3859(1985) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 22-462.
    5. "Complete amino acid sequence of human hemopexin, the heme-binding protein of serum."
      Takahashi N., Takahashi Y., Putnam F.W.
      Proc. Natl. Acad. Sci. U.S.A. 82:73-77(1985) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF ACTIVE PROTEIN.
    6. "Amino acid sequence of the N-terminal region of human hemopexin."
      Frantikova V., Borvak J., Kluh I., Moravek L.
      FEBS Lett. 178:213-216(1984) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 24-255.
    7. "Structure of human hemopexin: O-glycosyl and N-glycosyl sites and unusual clustering of tryptophan residues."
      Takahashi N., Takahashi Y., Putnam F.W.
      Proc. Natl. Acad. Sci. U.S.A. 81:2021-2025(1984) [PubMed] [Europe PMC] [Abstract]
      Cited for: PARTIAL PROTEIN SEQUENCE, GLYCOSYLATION AT THR-24; ASN-64; ASN-64; ASN-187; ASN-240; ASN-246 AND ASN-453.
    8. Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-187 AND ASN-453.
      Tissue: Bile.
    9. "Screening for N-glycosylated proteins by liquid chromatography mass spectrometry."
      Bunkenborg J., Pilch B.J., Podtelejnikov A.V., Wisniewski J.R.
      Proteomics 4:454-465(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-187; ASN-240 AND ASN-246.
      Tissue: Plasma.
    10. "Human plasma N-glycoproteome analysis by immunoaffinity subtraction, hydrazide chemistry, and mass spectrometry."
      Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E., Moore R.J., Smith R.D.
      J. Proteome Res. 4:2070-2080(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-64 AND ASN-187.
      Tissue: Plasma.
    11. "Identification of N-linked glycoproteins in human saliva by glycoprotein capture and mass spectrometry."
      Ramachandran P., Boontheung P., Xie Y., Sondej M., Wong D.T., Loo J.A.
      J. Proteome Res. 5:1493-1503(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-187 AND ASN-453.
      Tissue: Saliva.
    12. "The ORF3 protein of hepatitis E virus interacts with hemopexin by means of its 26 amino acid N-terminal hydrophobic domain II."
      Ratra R., Kar-Roy A., Lal S.K.
      Biochemistry 47:1957-1969(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH HEV ORF3 PROTEIN.
    13. "Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry."
      Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.
      J. Proteome Res. 8:651-661(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-187 AND ASN-453.
      Tissue: Liver.
    14. Cited for: GLYCOSYLATION AT ASN-187 AND ASN-453.
    15. "Enrichment of glycopeptides for glycan structure and attachment site identification."
      Nilsson J., Rueetschi U., Halim A., Hesse C., Carlsohn E., Brinkmalm G., Larson G.
      Nat. Methods 6:809-811(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT THR-24; ASN-64; ASN-187 AND ASN-453, STRUCTURE OF CARBOHYDRATES.
      Tissue: Cerebrospinal fluid.
    16. "Kinetics and specificity of feline leukemia virus subgroup C receptor (FLVCR) export function and its dependence on hemopexin."
      Yang Z., Philips J.D., Doty R.T., Giraudi P., Ostrow J.D., Tiribelli C., Smith A., Abkowitz J.L.
      J. Biol. Chem. 285:28874-28882(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH FLVCR1.
    17. "LC-MS/MS characterization of O-glycosylation sites and glycan structures of human cerebrospinal fluid glycoproteins."
      Halim A., Ruetschi U., Larson G., Nilsson J.
      J. Proteome Res. 12:573-584(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: GLYCOSYLATION AT THR-29, IDENTIFICATION BY MASS SPECTROMETRY.

    Entry informationi

    Entry nameiHEMO_HUMAN
    AccessioniPrimary (citable) accession number: P02790
    Secondary accession number(s): B2R957
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 21, 1986
    Last sequence update: October 1, 1996
    Last modified: October 1, 2014
    This is version 151 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

    Miscellaneous

    The isolated N-terminal domain binds one heme. The full-length protein also binds one heme, but at a different site. The physiological significance of this is not clear By similarity.By similarity

    Keywords - Technical termi

    Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 11
      Human chromosome 11: 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. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3