true2008-05-202024-01-24102SH3R1_BOVINNIH - Mammalian Gene Collection (MGC) project2007-04EMBL/GenBank/DDBJNUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]HerefordHypothalamusSH3RF1EukaryotaRHOV GTPase cycleAntigen processing: Ubiquitination & Proteasome degradationExpressed in ruminant reticulum and 102 other cell types or tissuesRING-HC_SH3RF1SH3_SH3RF1_2SH3_SH3RF_CSH3 DomainsZinc/RING finger domain, C3HC4 (zinc finger)SH3-like_dom_sfSH3_domainSH3RF1/SH3RF3_SH3_4SH3RF1_SH3_2Znf_RINGZnf_RING/FYVE/PHDZnf_RING_CSSH3 DOMAIN-CONTAININGUBP4-INTERACTOR SFP47SH3_1SH3_2SH3_9zf-C3HC4_2P67PHOXSH3DOMAINRINGSH3RING/U-boxSH3-domainSH3ZF_RING_1ZF_RING_2E3 ubiquitin-protein ligase SH3RF12.3.2.27Plenty of SH3sProtein POSHRING-type E3 ubiquitin transferase SH3RF1SH3 domain-containing RING finger protein 1SH3RF1POSHPOSH1Has E3 ubiquitin-protein ligase activity. In the absence of an external substrate, it can catalyze self-ubiquitination. Stimulates ubiquitination of potassium channel KCNJ1, enhancing it's dynamin-dependent and clathrin-independent endocytosis. Acts as a scaffold protein that coordinates with MAPK8IP1/JIP1 in organizing different components of the JNK pathway, including RAC1 or RAC2, MAP3K11/MLK3 or MAP3K7/TAK1, MAP2K7/MKK7, MAPK8/JNK1 and/or MAPK9/JNK2 into a functional multiprotein complex to ensure the effective activation of the JNK signaling pathway. Regulates the differentiation of CD4(+) and CD8(+) T-cells and promotes T-helper 1 (Th1) cell differentiation. Regulates the activation of MAPK8/JNK1 and MAPK9/JNK2 in CD4(+) T-cells and the activation of MAPK8/JNK1 in CD8(+) T-cells. Plays a crucial role in the migration of neocortical neurons in the developing brain. Controls proper cortical neuronal migration and the formation of proximal cytoplasmic dilation in the leading process (PCDLP) in migratory neocortical neurons by regulating the proper localization of activated RAC1 and F-actin assembly.Interacts with RAC1; in a GTP-dependent manner. Interacts with MAP3K10/MLK2 and MAP3K11/MLK3. Interacts with MAPK8IP; this interaction leads to the PJAC complex (POSH-JIP or SH3RF1/MAPK8IP apoptotic complex) with a 1:1 ratio. Interacts with SIAH1. Interacts with HERP1. Probably part of a signaling complex that may contain SH3RF1, MAPK8IP, DLK1, MAP2K4/MKK4, MAP2K7/MKK7, MAPK8/JNK1, MAPK9/JNK2, AKT1 and AKT2. Found in a complex with RAC2, MAP3K7/TAK1, MAP2K7/MKK7, MAPK8IP1/JIP1, MAPK8/JNK1 and MAPK9/JNK2. Found in a complex with RAC1, MAP3K11/MLK3, MAP2K7/MKK7, MAPK8IP1/JIP1 and MAPK8/JNK1. Interacts with SH3RF2.Colocalizes, with AKT2, in lamellipodia. Colocalizes, with HERP1, in trans-Golgi network.The RING finger domain is required for ubiquitin ligase activity and autoubiquitination.Phosphorylated at Ser-304 by AKT1 and AKT2. When phosphorylated, it has reduced ability to bind Rac.Autoubiquitinated. Ubiquitinated by SH3RF2, leading to proteasome-mediated degradation.Belongs to the SH3RF family.E3 ubiquitin-protein ligase SH3RF1875921840SH3 1134193SH3 2196259SH3 3439500SH3 4781RING-type1253Disordered105129Disordered267324Interaction with RAC1292362Disordered394442Interaction with AKT2434537Disordered516545Disordered578633Disordered652723Disordered744773Polar residues122Polar residues304Polar residues612Basic and acidic residues680694PhosphoserinePhosphoserine7092007-06-121875924496dc531ab1df44d194102e13b30889MDESALLDLLECPVCLERLDASAKVLPCQHTFCKRCLLGIVGSRNELRCPECRTLVGSGVEQLPSNILLVRLLDGIKQRPWKPGPVGGSGTNGTSALRAQSSAVVTCSPKDGPSSQGGPQPRAQAWSPPVRGIPQLPCAKALYNYEGKEPGDLKFSKGDIIVLRRQVDENWYHGEVGGVHGFFPTNFVQIIKPLPQPPPQCKALYDFEVKDKEADKDCLPFAKDDVLTVIRRVDENWAEGMLADKIGIFPISYVEFNSAAKQLIEWDQPPGPGVAAGEGALATTPSSTTTKQPDGKKNTKKRHSFTSLSMASKASQAAQQRHSMEISPPVLISSSNPAAAARIGELAGLSCSAPSQVHISTTGLIVTPPPSSPVTTGPSFTFPAEAPYPAALATLNPPLPPPPLQAATPTGTAVAAAAGMGPRPTAGPTDQTTHPRPQPRPSVYVAIYPYTPRKEDELELRKGEMFLVFERCQDGWFKGTSMHTSKIGVFPGNYVAPVTRAVTSASQGKVPMLTTGPASRGGVLANPPSTGGPAQKPPGNGVAGGPGVPTAVVSAAHVQTSPQAKVLLHASGQMTVNQARSAARTVSAHSQERPTAAVTPIQVQSTPGQSHHPLVSPQPPAPLGPPAHAAASGLGRVGGPLACATAPASIPAASLEPEPSSRPATLLPGTPTSPDSGSAARPDKDGKKEKKGLLKLLSGASTKRKPRGSPPASPTLDAELGAELSCGPPGPPCACPGPCDGDTMAPGPQRRASSLDSAPVAPPPRQPCSSLGPAASEVRPAVCERHRVVVSYPPQSEAELELKEGDIVFVHKKREDGWFKGTLQRNGKTGLFPGSFVENItruetruetruetruetruetruetruetruetrue