HEBP1

HEBP1
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 2GOV, 2HVA, 4A1M
Identifiers
Aliases	HEBP1 , HBP, HEBP, heme binding protein 1
External IDs	OMIM: 605826; MGI: 1333880; HomoloGene: 8407; GeneCards: HEBP1; OMA:HEBP1 - orthologs
Gene location (Human) Chr. Chromosome 12 (human) [1] Band 12p13.1 Start 12,974,870 bp [1] End 13,000,265 bp [1]
Gene location (Mouse) Chr. Chromosome 6 (mouse) [2] Band 6|6 G1 Start 135,114,520 bp [2] End 135,175,020 bp [2]
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in jejunal mucosa duodenum mucosa of ileum right adrenal gland right adrenal cortex left adrenal gland trabecular bone parotid gland left adrenal cortex left lobe of thyroid gland Top expressed in fetal liver hematopoietic progenitor cell left lobe of liver yolk sac tibiofemoral joint spleen white adipose tissue subcutaneous adipose tissue gastrula migratory enteric neural crest cell efferent ductule More reference expression data BioGPS n/a
Gene ontology Molecular function heme binding Cellular component cytoplasm extracellular region extracellular exosome cytosol Biological process circadian rhythm G protein-coupled receptor signaling pathway Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 50865 15199 Ensembl ENSG00000013583 ENSMUSG00000042770 UniProt Q9NRV9 Q9R257 RefSeq (mRNA) NM_015987 NM_013546 RefSeq (protein) NP_057071 NP_038574 Location (UCSC) Chr 12: 12.97 – 13 Mb Chr 6: 135.11 – 135.18 Mb PubMed search [3] [4]
Wikidata
View/Edit Human View/Edit Mouse

Heme binding protein 1 is a protein that in humans is encoded by the HEBP1 gene. ^[5]

Function

The full-length protein encoded by this gene is an intracellular tetrapyrrole-binding protein. This protein includes a natural chemoattractant peptide of 21 amino acids at the N-terminus, which is a natural ligand for formyl peptide receptor-like receptor 2 (FPRL2) and promotes calcium mobilization and chemotaxis in monocytes and dendritic cells. ^[5]

References

1. GRCh38: Ensembl release 89: ENSG00000013583 – Ensembl, May 2017
2. GRCm38: Ensembl release 89: ENSMUSG00000042770 – Ensembl, May 2017
3. "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
4. "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
5. "Entrez Gene: Heme binding protein 1".

Further reading

• Jacob Blackmon B, Dailey TA, Lianchun X, Dailey HA (Nov 2002). "Characterization of a human and mouse tetrapyrrole-binding protein". Archives of Biochemistry and Biophysics. 407 (2): 196–201. doi:10.1016/s0003-9861(02)00471-x. PMID   12413491.
• Gao JL, Guillabert A, Hu J, Le Y, Urizar E, Seligman E, Fang KJ, Yuan X, Imbault V, Communi D, Wang JM, Parmentier M, Murphy PM, Migeotte I (Feb 2007). "F2L, a peptide derived from heme-binding protein, chemoattracts mouse neutrophils by specifically activating Fpr2, the low-affinity N-formylpeptide receptor". Journal of Immunology. 178 (3): 1450–6. doi: 10.4049/jimmunol.178.3.1450 . PMID   17237393.
• Micaelo NM, Macedo AL, Goodfellow BJ, Félix V (Nov 2010). "Tetrapyrrole binding affinity of the murine and human p22HBP heme-binding proteins". Journal of Molecular Graphics & Modelling. 29 (3): 396–405. doi:10.1016/j.jmgm.2010.07.008. PMID   20800521.
• Migeotte I, Riboldi E, Franssen JD, Grégoire F, Loison C, Wittamer V, Detheux M, Robberecht P, Costagliola S, Vassart G, Sozzani S, Parmentier M, Communi D (Jan 2005). "Identification and characterization of an endogenous chemotactic ligand specific for FPRL2". The Journal of Experimental Medicine. 201 (1): 83–93. doi:10.1084/jem.20041277. PMC   2212760 . PMID   15623572.
• Devosse T, Dutoit R, Migeotte I, De Nadai P, Imbault V, Communi D, Salmon I, Parmentier M (Aug 2011). "Processing of HEBP1 by cathepsin D gives rise to F2L, the agonist of formyl peptide receptor 3". Journal of Immunology. 187 (3): 1475–85. doi: 10.4049/jimmunol.1003545 . hdl: 2013/ULB-DIPOT:oai:dipot.ulb.ac.be:2013/114502 . PMID   21709160.
• Zylka MJ, Reppert SM (Dec 1999). "Discovery of a putative heme-binding protein family (SOUL/HBP) by two-tissue suppression subtractive hybridization and database searches". Brain Research. Molecular Brain Research. 74 (1–2): 175–81. doi:10.1016/s0169-328x(99)00277-6. PMID   10640688.

This article incorporates text from the United States National Library of Medicine, which is in the public domain.