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P02790

- HEMO_HUMAN

UniProt

P02790 - HEMO_HUMAN

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

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
Complete GO annotation...

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
Complete GO annotation...

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA29441.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 23231 Publication
Add
BLAST
Chaini24 – 462439Hemopexin1 Publication
PRO_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-29.3 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.

Family & Domainsi

Domains and Repeats

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

Region

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

Sequence similaritiesi

Belongs to the hemopexin family.
Contains 8 hemopexin repeats.

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.

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 conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti411 – 4111K → R in BAG36404. 1 Publication

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

« Hide 'large scale' publications
  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: September 3, 2014
This is version 150 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.

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

Similar proteinsi