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GoPubMed Proteins lists recent and important papers and reviews for proteins. Page last changed on 19 Dec 2016.

Heme binding protein 1

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. [provided by RefSeq, Jul 2008] (from NCBI)
Top mentioned proteins: Stam, Ubiquitin, HRs, V1a, CAN
Papers on STAM2
Revealing genome-wide mRNA and microRNA expression patterns in leukemic cells highlighted "hsa-miR-2278" as a tumor suppressor for regain of chemotherapeutic imatinib response due to targeting STAT5A.
Can et al., İzmir, Turkey. In Tumour Biol, Sep 2015
Functional analyses indicated that AKT2, STAM2, and STAT5A mRNAs were functional targets for miR-2278 as mimic transfection decreased their expressions both at transcriptional and translational level, thus highlighting miR-2278 as a tumor suppressor.
STAM2, a member of the endosome-associated complex ESCRT-0 is highly expressed in neurons.
Gajović et al., Zagreb, Croatia. In Mol Cell Neurosci, Jul 2015
STAM2 (signal transducing adaptor molecule 2), a subunit of the ESCRT-0 complex, is an endosomal protein acting as a regulator of receptor signaling and trafficking.
Realization of a p-n junction in a single layer boron-phosphide.
Peeters et al., Antwerp, Belgium. In Phys Chem Chem Phys, Jun 2015
On the basis of first-principles calculations based on density functional theory, we first investigate the electronic and mechanical properties of single layer boron phosphide (h-BP).
RHEX, a novel regulator of human erythroid progenitor cell expansion and erythroblast development.
Wojchowski et al., Danvers, United States. In J Exp Med, 2014
Molecular adaptors comprised one major set including growth factor receptor-bound protein 2 (GRB2)-associated binding proteins 1-3 (GAB1-3), insulin receptor substrate 2 (IRS2), docking protein 1 (DOK1), Src homology 2 domain containing transforming protein 1 (SHC1), and sprouty homologue 1 (SPRY1) as validating targets, and SPRY2, SH2 domain containing 2A (SH2D2A), and signal transducing adaptor molecule 2 (STAM2) as novel candidate adaptors together with an ORF factor designated as regulator of human erythroid cell expansion (RHEX).
Immunohistochemical expression of STAM2 in gastrointestinal stromal tumors.
Krušlin et al., Zagreb, Croatia. In Anticancer Res, 2014
Recent studies incidentally found the expression in interstitial cells of Cajal of the signal-transducing adaptor molecule-2 (STAM2), which is an endosomal protein acting as a regulator of receptor signaling and trafficking.
SARA and RNF11 interact with each other and ESCRT-0 core proteins and regulate degradative EGFR trafficking.
Murphy et al., Ioánnina, Greece. In Oncogene, 2013
RNF11 and SARA interact with the ESCRT-0 subunits STAM2 and Eps15b, but only RNF11 associates with the core subunit Hrs.
Recruitment of UBPY and ESCRT exchange drive HD-PTP-dependent sorting of EGFR to the MVB.
Woodman et al., Manchester, United Kingdom. In Curr Biol, 2013
HD-PTP binds ESCRT-0 via two interactions with the STAM2 subunit.
Molecular cloning, polymorphisms, and association analysis of the promoter region of the STAM2 gene in Wuchuan Black cattle.
Xie et al., Guiyang, China. In Genet Mol Res, 2012
We selected the STAM2 gene as a candidate gene that could be linked to growth performance in analysis of a Chinese cattle breed (Wuchuan Black cattle).
Competitive binding of UBPY and ubiquitin to the STAM2 SH3 domain revealed by NMR.
Walker et al., Villeurbanne, France. In Febs Lett, 2012
To date, the signal transducing adaptor molecule 2 (STAM2) was shown to harbour two ubiquitin binding domains (UBDs) known as the VHS and UIM domains, while the SH3 domain of STAM2 was reported to interact with deubiquitinating enzymes (DUBs) like UBPY and AMSH.
Evidence for cooperative and domain-specific binding of the signal transducing adaptor molecule 2 (STAM2) to Lys63-linked diubiquitin.
Walker et al., Villeurbanne, France. In J Biol Chem, 2012
report the interactions of the UIM domain and VHS-UIM construct of STAM2 with monoubiquitin (Ub), Lys(48)- and Lys(63)-linked diubiquitins.
Neurons and a subset of interstitial cells of Cajal in the enteric nervous system highly express Stam2 gene.
Gajovic et al., Zagreb, Croatia. In Anat Rec (hoboken), 2012
Mice carrying a gene trap insertion in the Stam2 transgene do not reveal phenotype changes; therefore, STAM2 function in the digestive tube remains elusive.
Stam2 expression pattern during embryo development.
Gajović et al., Zagreb, Croatia. In Gene Expr Patterns, 2012
Stam2 is expressed in the nervous tissue, heart, digestive and endocrine system during embryo development.
Processing of HEBP1 by cathepsin D gives rise to F2L, the agonist of formyl peptide receptor 3.
Parmentier et al., Brussels, Belgium. In J Immunol, 2011
The functional activity of purified full-length HEBP1 has been evaluated on human formyl peptide receptor (FPR)3-expressing CHO-K1 cells
Identification and expression of soul/p22HBP genes in zebrafish.
Sordino et al., Napoli, Italy. In Gene Expr Patterns, 2011
The SOUL/p22HBP family is an evolutionarily ancient group of heme binding proteins with a main function as cytosolic buffer against tetrapyrrole accumulation.
NMR reveals a different mode of binding of the Stam2 VHS domain to ubiquitin and diubiquitin.
Walker et al., Villeurbanne, France. In Biochemistry, 2011
The VHS domain of the Stam2 protein is a ubiquitin binding domain involved in the recognition of ubiquitinated proteins committed to lysosomal degradation.
Tetrapyrrole binding affinity of the murine and human p22HBP heme-binding proteins.
Félix et al., Aveiro, Portugal. In J Mol Graph Model, 2010
Results present a systematic molecular modeling study of the binding properties of murine and human p22HBP protein (heme-binding protein) with four tetrapyrrole ring systems belonging to the heme biosynthetic pathway.
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