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Protein

Heme-binding protein 1

Gene

Hebp1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

May bind free porphyrinogens that may be present in the cell and thus facilitate removal of these potentially toxic compound. Binds with a high affinity to one molecule of heme or porphyrins. It binds metalloporphyrins, free porphyrins and N-methylprotoporphyrin with similar affinities.2 Publications

GO - Molecular functioni

  • heme binding Source: UniProtKB

GO - Biological processi

  • heme metabolic process Source: MGI
Complete GO annotation...

Names & Taxonomyi

Protein namesi
Recommended name:
Heme-binding protein 1
Alternative name(s):
p22HBP
Gene namesi
Name:Hebp1
Synonyms:Hbp
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Unplaced

Organism-specific databases

MGIiMGI:1333880. Hebp1.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: MGI
  • cytosol Source: MGI
  • extracellular exosome Source: MGI
  • mitochondrion Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 190190Heme-binding protein 1PRO_0000116898Add
BLAST

Proteomic databases

EPDiQ9R257.
MaxQBiQ9R257.
PaxDbiQ9R257.
PRIDEiQ9R257.

PTM databases

iPTMnetiQ9R257.
PhosphoSiteiQ9R257.
SwissPalmiQ9R257.

Expressioni

Tissue specificityi

Ubiquitously expressed. Extremely abundant in liver.1 Publication

Gene expression databases

BgeeiQ9R257.
CleanExiMM_HEBP1.

Interactioni

Subunit structurei

Monomer.3 Publications

Protein-protein interaction databases

BioGridi200269. 1 interaction.
IntActiQ9R257. 5 interactions.
MINTiMINT-1845080.
STRINGi10090.ENSMUSP00000042232.

Structurei

Secondary structure

1
190
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi10 – 123Combined sources
Beta strandi19 – 235Combined sources
Beta strandi27 – 293Combined sources
Beta strandi31 – 355Combined sources
Beta strandi40 – 4910Combined sources
Helixi51 – 6717Combined sources
Beta strandi70 – 723Combined sources
Beta strandi82 – 887Combined sources
Beta strandi94 – 1029Combined sources
Helixi106 – 1105Combined sources
Beta strandi117 – 1193Combined sources
Beta strandi121 – 1244Combined sources
Beta strandi129 – 1379Combined sources
Helixi141 – 15414Combined sources
Turni155 – 1573Combined sources
Beta strandi162 – 17312Combined sources
Beta strandi176 – 1794Combined sources
Beta strandi182 – 1898Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2GOVNMR-A7-190[»]
2HVANMR-A1-190[»]
4A1MNMR-A7-190[»]
ProteinModelPortaliQ9R257.
SMRiQ9R257. Positions 1-190.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9R257.

Family & Domainsi

Domaini

Forms a distorted beta-barrel structure, with two helices that are packed against the outer surface of the barrel. Porphyrins are expected to bind to a hydrophobic patch on the outer surface of the beta-barrel structure.2 Publications

Sequence similaritiesi

Belongs to the HEBP family.Curated

Phylogenomic databases

eggNOGiENOG410IKQ6. Eukaryota.
ENOG4111HGX. LUCA.
HOGENOMiHOG000237638.
HOVERGENiHBG053223.
InParanoidiQ9R257.
OrthoDBiEOG7B5WZC.
TreeFamiTF328887.

Family and domain databases

InterProiIPR011256. Reg_factor_effector_dom.
IPR006917. SOUL_haem-bd.
[Graphical view]
PANTHERiPTHR11220. PTHR11220. 1 hit.
PfamiPF04832. SOUL. 1 hit.
[Graphical view]
SUPFAMiSSF55136. SSF55136. 1 hit.

Sequencei

Sequence statusi: Complete.

Q9R257-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLGMIRNSLF GSVETWPWQV LSTGGKEDVS YEERACEGGK FATVEVTDKP
60 70 80 90 100
VDEALREAMP KIMKYVGGTN DKGVGMGMTV PVSFALFPNE DGSLQKKLKV
110 120 130 140 150
WFRIPNQFQG SPPAPSDESV KIEEREGITV YSTQFGGYAK EADYVAHATQ
160 170 180 190
LRTTLEGTPA TYQGDVYYCA GYDPPMKPYG RRNEVWLVKA
Length:190
Mass (Da):21,067
Last modified:October 3, 2012 - v2
Checksum:iC1EA42E1798931DB
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti86 – 861L → V in BAA33770 (PubMed:9813049).Curated
Sequence conflicti86 – 861L → V in AAD32096 (PubMed:10640688).Curated
Sequence conflicti86 – 861L → V in CAJ18470 (Ref. 4) Curated
Sequence conflicti86 – 861L → V in AAH12654 (PubMed:15489334).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB013095 mRNA. Translation: BAA33770.1.
AF117613 mRNA. Translation: AAD32096.1.
CT010262 mRNA. Translation: CAJ18470.1.
AC131718 Genomic DNA. No translation available.
BC012654 mRNA. Translation: AAH12654.1.
CCDSiCCDS20645.1.
RefSeqiNP_038574.3. NM_013546.3.
UniGeneiMm.378937.

Genome annotation databases

GeneIDi15199.
KEGGimmu:15199.
UCSCiuc009elh.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB013095 mRNA. Translation: BAA33770.1.
AF117613 mRNA. Translation: AAD32096.1.
CT010262 mRNA. Translation: CAJ18470.1.
AC131718 Genomic DNA. No translation available.
BC012654 mRNA. Translation: AAH12654.1.
CCDSiCCDS20645.1.
RefSeqiNP_038574.3. NM_013546.3.
UniGeneiMm.378937.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2GOVNMR-A7-190[»]
2HVANMR-A1-190[»]
4A1MNMR-A7-190[»]
ProteinModelPortaliQ9R257.
SMRiQ9R257. Positions 1-190.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi200269. 1 interaction.
IntActiQ9R257. 5 interactions.
MINTiMINT-1845080.
STRINGi10090.ENSMUSP00000042232.

PTM databases

iPTMnetiQ9R257.
PhosphoSiteiQ9R257.
SwissPalmiQ9R257.

Proteomic databases

EPDiQ9R257.
MaxQBiQ9R257.
PaxDbiQ9R257.
PRIDEiQ9R257.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi15199.
KEGGimmu:15199.
UCSCiuc009elh.1. mouse.

Organism-specific databases

CTDi50865.
MGIiMGI:1333880. Hebp1.

Phylogenomic databases

eggNOGiENOG410IKQ6. Eukaryota.
ENOG4111HGX. LUCA.
HOGENOMiHOG000237638.
HOVERGENiHBG053223.
InParanoidiQ9R257.
OrthoDBiEOG7B5WZC.
TreeFamiTF328887.

Miscellaneous databases

EvolutionaryTraceiQ9R257.
PROiQ9R257.
SOURCEiSearch...

Gene expression databases

BgeeiQ9R257.
CleanExiMM_HEBP1.

Family and domain databases

InterProiIPR011256. Reg_factor_effector_dom.
IPR006917. SOUL_haem-bd.
[Graphical view]
PANTHERiPTHR11220. PTHR11220. 1 hit.
PfamiPF04832. SOUL. 1 hit.
[Graphical view]
SUPFAMiSSF55136. SSF55136. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Molecular characterizatin of a newly identified heme-binding protein induced during differentiation of Murine erythroleukemia cells."
    Taketani S., Adachi Y., Kohno H., Ikehara S., Tokunaga R., Ishii T.
    J. Biol. Chem. 273:31388-31394(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
  2. "Discovery of a putative heme-binding protein family (SOUL/HBP) by two-tissue suppression subtractive hybridization and database searches."
    Zylka M.J., Reppert S.M.
    Brain Res. Mol. Brain Res. 74:175-181(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  3. "Characterization of a human and mouse tetrapyrrole-binding protein."
    Jacob Blackmon B., Dailey T.A., Lianchun X., Dailey H.A.
    Arch. Biochem. Biophys. 407:196-201(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, SUBUNIT.
    Tissue: Liver.
  4. "Cloning of mouse full open reading frames in Gateway(R) system entry vector (pDONR201)."
    Ebert L., Muenstermann E., Schatten R., Henze S., Bohn E., Mollenhauer J., Wiemann S., Schick M., Korn B.
    Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6J.
  6. "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].
    Strain: FVB/N.
    Tissue: Colon.
  7. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas, Spleen and Testis.
  8. "The first structure from the SOUL/HBP family of heme-binding proteins, murine P22HBP."
    Dias J.S., Macedo A.L., Ferreira G.C., Peterson F.C., Volkman B.F., Goodfellow B.J.
    J. Biol. Chem. 281:31553-31561(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 7-190, FUNCTION AS HEME-BINDING PROTEIN, SUBUNIT, DOMAIN.
  9. "A novel haem-binding interface in the 22 kDa haem-binding protein p22HBP."
    Gell D.A., Westman B.J., Gorman D., Liew C., Welch J.J., Weiss M.J., Mackay J.P.
    J. Mol. Biol. 362:287-297(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR, SUBUNIT, DOMAIN.

Entry informationi

Entry nameiHEBP1_MOUSE
AccessioniPrimary (citable) accession number: Q9R257
Secondary accession number(s): O88814
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 24, 2006
Last sequence update: October 3, 2012
Last modified: March 16, 2016
This is version 105 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.