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

SH3-domain binding protein 4

SH3BP4, SH3-domain binding protein 4, EH-binding protein, Transferrin receptor trafficking protein, EH-binding protein 1
This gene encodes a protein with 3 Asn-Pro-Phe (NPF) motifs, an SH3 domain, a PXXP motif, a bipartite nuclear targeting signal, and a tyrosine phosphorylation site. This protein is involved in cargo-specific control of clathrin-mediated endocytosis, specifically controlling the internalization of a specific protein receptor. [provided by RefSeq, Jul 2008] (from NCBI)
Top mentioned proteins: ACID, CAN, Transferrin, mTORC1, Dynamin I
Papers on SH3BP4
The proline-rich region of glyceraldehyde-3-phosphate dehydrogenase from human sperm may bind SH3 domains, as revealed by a bioinformatic study of low-complexity protein segments.
Grynberg et al., Warsaw, Poland. In Mol Reprod Dev, Jan 2016
The putative binding partners of the proline-rich GAPDHS motif include SH3 domain-binding protein 4 (SH3BP4) and the IL2-inducible T-cell kinase/tyrosine-protein kinase ITK/TSK (ITK).
Whole-exome sequencing in patients with inherited neuropathies: outcome and challenges.
Auer-Grumbach et al., Vienna, Austria. In J Neurol, 2014
In addition, combining data of WES and linkage analysis identified SH3BP4, ITPR3, and KLHL13 as novel IPN candidate genes.
Functional proteomics defines the molecular switch underlying FGF receptor trafficking and cellular outputs.
Olsen et al., Copenhagen, Denmark. In Mol Cell, 2013
By combining mass-spectrometry-based quantitative proteomics with fluorescence microscopy and biochemical methods, we find that FGF-10 specifically induces the rapid phosphorylation of tyrosine (Y) 734 on FGFR2b, which leads to PI3K and SH3BP4 recruitment.
Genome-wide association study in a Chinese population with diabetic retinopathy.
Chen et al., Taiwan. In Hum Mol Genet, 2013
Association analysis with imputed data identified three novel loci: TBC1D4-COMMD6-UCHL3 (rs9565164, P = 1.3 × 10(-7)), LRP2-BBS5 (rs1399634, P = 2.0 × 10(-6)) and ARL4C-SH3BP4 (rs2380261, P = 2.1 × 10(-6)).
dRAGging amino acid-mTORC1 signaling by SH3BP4.
Kim et al., Minneapolis, United States. In Mol Cells, 2013
In particular, this review focuses on SH3 binding protein 4 (SH3BP4), the protein recently identifed as a negative regulator of Rag GTPases.
SH3BP4 is a negative regulator of amino acid-Rag GTPase-mTORC1 signaling.
Kim et al., Minneapolis, United States. In Mol Cell, 2012
SH3BP4 is a negative regulator of the Rag GTPase complex and amino acid-dependent mTORC1 signaling.
MACC1 - more than metastasis? Facts and predictions about a novel gene.
Walther et al., Berlin, Germany. In J Mol Med (berl), 2010
We discuss the MACC1 protein domain structure, posttranslational modifications, its conservation through evolution, and some family ties to SH3BP4.
TTP at Ser245 phosphorylation by AKT is required for binding to 14-3-3.
Abe et al., Japan. In J Biochem, 2009
Transferrin receptor trafficking protein (TTP) is a key molecule for selective internalization of the transferrin receptor (Tf-R) through endocytic protein complexes.
TTP specifically regulates the internalization of the transferrin receptor.
Di Fiore et al., Milano, Italy. In Cell, 2006
Results show that TTP (SH3BP4), a SH3-containing protein, specifically regulates the internalization of the transferrin receptor (TfR).
C-terminal EH-domain-containing proteins: consensus for a role in endocytic trafficking, EH?
Caplan et al., Omaha, United States. In J Cell Sci, 2005
Recent studies have identified an array of novel binding partners for EHD1-EHD4, including NPF-containing proteins, such as the divalent Rab4/5 effector rabenosyn 5, the cell fate determinant Numb, EH-binding protein 1 (EHBP1) and syndapins I and II.
Nuclear and plasma membrane localization of SH3BP4 in retinal pigment epithelial cells.
Dunlevy et al., Grand Forks, United States. In Mol Vis, 2005
PURPOSE: The SH3BP4 protein contains domains belonging to the Eps15-Homology (EH) network family of endocytosis proteins and a C-terminal death domain.
Cloning, chromosomal localization, and characterization of cDNA from a novel gene, SH3BP4, expressed by human corneal fibroblasts.
Hassell et al., Tampa, United States. In Genomics, 2000
This novel gene product, named SH3-domain binding protein 4 (SH3BP4), contains a 5.6-kb message that is present in normal human corneal fibroblasts and all tissues examined, with higher levels in pancreas, placenta, heart, and kidney.
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