Immunogen sequence: EGPHYYTILD SGGIIVAIEH SSRPINVIKF STDEGQCWQT YTFTRDPIYF TGLASEPGAR SMNISIWGFT ESFLTSQWVS YTIDFKDILE RNCEEKDYTI WLAHSTDPED YEDGCILGYK EQFLRLRKSS VCQNGRDYVV TKQPSICLCS LEDFLCDFGY YRPENDSKCV EQPELKGHDL EFCLYGREEH LTTNGYRKIP GDKCQGGVNP VREVKDLKKK CTSNFLSPEK QNSKSNSVPI I; Positive Samples: A-549, Jurkat; Cellular Location: Cell membrane, Endoplasmic reticulum membrane, Endosome membrane, Extracellular side, Golgi apparatus, Golgi stack membrane, Lysosome membrane, Membrane, Nucleus membrane, Single-pass type I membrane protein
Modification of target proteins by ubiquitin participates in a wide array of biological functions. Proteins destined for degradation or processing via the 26 S proteasome are coupled to multiple copies of ubiquitin. However, attachment of ubiquitin or ubiquitin-related molecules may also result in changes in subcellular distribution or modification of protein activity. An additional level of ubiquitin regulation, deubiquitination, is catalyzed by proteases called deubiquitinating enzymes, which fall into four distinct families. Ubiquitin C-terminal hydrolases, ubiquitin-specific processing proteases (USPs), 1 OTU-domain ubiquitin-aldehyde-binding proteins, and Jab1/Pad1/MPN-domain-containing metallo-enzymes. Among these four families, USPs represent the most widespread and represented deubiquitinating enzymes across evolution. USPs tend to release ubiquitin from a conjugated protein. They display similar catalytic domains containing conserved Cys and His boxes but divergent N-terminal and occasionally C-terminal extensions, which are thought to function in substrate recognition, subcellular localization, and protein-protein interactions.
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Protein Aliases: 100 kDa NT receptor; Glycoprotein 110; Glycoprotein 95; Gp110; Gp95; mNTR3; Neurotensin receptor 3; NT3; NTR3; Sortilin
Gene Aliases: 2900053A11Rik; AI852375; Gp95; LDLCQ6; NT3; NTR3; Nts3; Ntsr3; SORT1