HEBP1

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

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
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 135,137,522 bp[2] End 135,198,022 bp[2]
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: 135.14 – 135.2 Mb
PubMed search	[3]	[4]
Wikidata
View/Edit Human View/Edit Mouse

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. 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.