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Conserved domains on  [gi|767939602|ref|XP_011512743|]
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E3 ubiquitin-protein ligase UBR2 isoform X6 [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PRT6_C pfam18995
Proteolysis_6 C-terminal; This is the C-terminal domain mainly found in E3 ubiquitin ligases. ...
 794-1212 1.83e-122

Proteolysis_6 C-terminal; This is the C-terminal domain mainly found in E3 ubiquitin ligases. Proteolysis 6 (PRT6) encodes a ubiquitin E3 ligase belonging to the N-end rule pathway of targeted protein degradation, which is a specialized subset of the ubiquitin proteasome system. In Arabidopsis, at least two N-recognins (E3 ubiquitin ligases) with different substrate specificities exist, namely PROTEOLYSIS1 (PRT1) and PRT6.


:

Pssm-ID: 465944  Cd Length: 444  Bit Score: 385.85  E-value: 1.83e-122
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767939602   794 TATYKVGLKV---HPNEEDPRVPI-MCWGSCAYTIQSIERILSDEDKP---LFGPLPCRLDDCLRSLTRFAAAHWTV--- 863
Cdd:pfam18995    3 DTTRPNGLQSrhpSDPSSDDLVSSdLLWDSLAYTISSIEIAQRGVGKPggtLLGKLPEQQLTLLRILSETVSSYASVgfl 82

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767939602   864 -------ASVSVVQGHFCKLFASLVPNDSH--EELPCILDIDMFHLLVGLVLAFPALQCQDFSgislgtgdlHIFHLVTM 934
Cdd:pfam18995   83 rsggtneEGRELIRRGILRLLLQLFPRISSlgEASPPLLLRDPFGLLVELALCLPSLFLEDIL---------HLLRLCYL 153

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767939602   935 AHIIQILLTSCTEENGMDQENPP---CEEESAVLALYKTLHQYTGSALKEIP----------SGWHLWRSVRAGIMPFLK 1001
Cdd:pfam18995  154 AEIVQVVLTLSRNLSKTLRWAEGletRSPSDESEDALRDFREFVGSVLRHSGvfadldndgfDDERLYKLVRKYALPFLR 233

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767939602  1002 CSALFFHYLNGVPSPPDI-QVPGTSHFEHLCSYLSLPNnLICLFQENSEIMNSLIESWCRNSEVKRYLEGERDA----IR 1076
Cdd:pfam18995  234 KAAILLHVLYGVPFPSPLsSDPEGDELERLCKYLRLPS-LDELCQSNQDTLRSLVSGWCRHPAVFGHLSASPLNpsilLS 312

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767939602  1077 YPReSNKLINLPEDYSSLINQASNFSCPKSGGDkSRAPTLCLVCGSLLCSQSYCCQTElegEDVGACTAHTYSCGSGVGI 1156
Cdd:pfam18995  313 HPG-IFELVGLPKDYDTLIEEASKRRCPTCGTD-PTDPALCLFCGTILCSQSYCCQEE---LNVGECNQHMRKCGGGVGI 387

                          410       420       430       440       450
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 767939602  1157 FLRVRECQVLFLAGKTkGCFYSPPYLDDYGETDQGLRRGNPLHLCKERFKKIQKLW 1212
Cdd:pfam18995  388 FLLIRKCTILLLHGGN-GSFWPAPYLDAHGETDPGLRRGRPLYLNQKRYDELRRLW 442
RING-H2_UBR2 cd16686
RING finger, H2 subclass, found in ubiquitin-protein ligase E3-alpha-2 (UBR2) and similar ...
 591-706 7.64e-84

RING finger, H2 subclass, found in ubiquitin-protein ligase E3-alpha-2 (UBR2) and similar proteins; UBR2, also known as N-recognin-2 or E3alpha-II, is an E3 ubiquitin-protein ligase that plays an important role in maintaining genome integrity and in homologous recombination repair. It regulates the level of the transcription factor Rpn4 (also known as Son1 and Ufd5) through ubiquitylation. The ubiquitin-conjugating enzyme Rad6, another binding partner of URB2, and an additional factor Mub1, are required for the ubiquitin-dependent degradation of Rpn4. UBR2 associates with Mub1 to form a Mub1/Ubr2 complex that regulates the conserved Dsn1 kinetochore protein levels, which is a part of a quality control system that monitors kinetochore integrity, thus ensuring genomic stability. As the recognition component of a major cellular proteolytic system, UBR2 is associated with chromatin and controls chromatin dynamics and gene expression in both spermatocytes and somatic cells. UBR2 also mediates transcriptional silencing during spermatogenesis via histone ubiquitination. It functions as a scaffold E3 promoting HR6B/UbcH2-dependent ubiquitylation of H2A and H2B, but not H3 and H4. It also binds to Tex19.1, also known as Tex19, a germ cell-specific protein, and metabolically stabilizes it during spermatogenesis. Furthermore, UBR2 is involved in skeletal muscle (SKM) atrophy. Its expression can be modulated by the mouse ether-a-gogo-related gene 1a (MERG1a) potassium channel. In addition, UBR2 up-regulation in cachectic muscle is mediated by the p38beta-CCAAT/enhancer binding protein (C/EBP)-beta signaling pathway responsible for the bulk of tumor-induced muscle proteolysis. UBR2 contains an N-terminal ubiquitin-recognin (UBR) box involved in binding type-1 (basic) N-end rule substrate, an N-domain (also known as ClpS domain) required for type-2 (bulky hydrophobic) N-end rule substrate recognition, a C3H2C3-type RING-H2 finger, and a C-terminal UBR-specific autoinhibitory (UAIN) domain.


:

Pssm-ID: 438347  Cd Length: 116  Bit Score: 268.42  E-value: 7.64e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767939602  591 TCILCQEEQEVKVESRAMVLAAFVQRSTVLSKNRSKFIQDPEKYDPLFMHPDLSCGTHTSSCGHIMHAHCWQRYFDSVQA 670
Cdd:cd16686     1 TCILCQEEQEIKVDNKAMVLAAFVQRSTVMSKNRSRVIHDPEKYDPLFMHPDLSCGTHTGSCGHIMHAHCWQRYFDAVQA 80

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 767939602  671 KEQRRQQRLRLHTSYDVENGEFLCPLCECLSNTVIP 706
Cdd:cd16686    81 KEQRRQQRLRVHTSYDVENGEFLCPLCECLSNTVIP 116
 
Name Accession Description Interval E-value
PRT6_C pfam18995
Proteolysis_6 C-terminal; This is the C-terminal domain mainly found in E3 ubiquitin ligases. ...
 794-1212 1.83e-122

Proteolysis_6 C-terminal; This is the C-terminal domain mainly found in E3 ubiquitin ligases. Proteolysis 6 (PRT6) encodes a ubiquitin E3 ligase belonging to the N-end rule pathway of targeted protein degradation, which is a specialized subset of the ubiquitin proteasome system. In Arabidopsis, at least two N-recognins (E3 ubiquitin ligases) with different substrate specificities exist, namely PROTEOLYSIS1 (PRT1) and PRT6.


Pssm-ID: 465944  Cd Length: 444  Bit Score: 385.85  E-value: 1.83e-122
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767939602   794 TATYKVGLKV---HPNEEDPRVPI-MCWGSCAYTIQSIERILSDEDKP---LFGPLPCRLDDCLRSLTRFAAAHWTV--- 863
Cdd:pfam18995    3 DTTRPNGLQSrhpSDPSSDDLVSSdLLWDSLAYTISSIEIAQRGVGKPggtLLGKLPEQQLTLLRILSETVSSYASVgfl 82

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767939602   864 -------ASVSVVQGHFCKLFASLVPNDSH--EELPCILDIDMFHLLVGLVLAFPALQCQDFSgislgtgdlHIFHLVTM 934
Cdd:pfam18995   83 rsggtneEGRELIRRGILRLLLQLFPRISSlgEASPPLLLRDPFGLLVELALCLPSLFLEDIL---------HLLRLCYL 153

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767939602   935 AHIIQILLTSCTEENGMDQENPP---CEEESAVLALYKTLHQYTGSALKEIP----------SGWHLWRSVRAGIMPFLK 1001
Cdd:pfam18995  154 AEIVQVVLTLSRNLSKTLRWAEGletRSPSDESEDALRDFREFVGSVLRHSGvfadldndgfDDERLYKLVRKYALPFLR 233

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767939602  1002 CSALFFHYLNGVPSPPDI-QVPGTSHFEHLCSYLSLPNnLICLFQENSEIMNSLIESWCRNSEVKRYLEGERDA----IR 1076
Cdd:pfam18995  234 KAAILLHVLYGVPFPSPLsSDPEGDELERLCKYLRLPS-LDELCQSNQDTLRSLVSGWCRHPAVFGHLSASPLNpsilLS 312

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767939602  1077 YPReSNKLINLPEDYSSLINQASNFSCPKSGGDkSRAPTLCLVCGSLLCSQSYCCQTElegEDVGACTAHTYSCGSGVGI 1156
Cdd:pfam18995  313 HPG-IFELVGLPKDYDTLIEEASKRRCPTCGTD-PTDPALCLFCGTILCSQSYCCQEE---LNVGECNQHMRKCGGGVGI 387

                          410       420       430       440       450
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 767939602  1157 FLRVRECQVLFLAGKTkGCFYSPPYLDDYGETDQGLRRGNPLHLCKERFKKIQKLW 1212
Cdd:pfam18995  388 FLLIRKCTILLLHGGN-GSFWPAPYLDAHGETDPGLRRGRPLYLNQKRYDELRRLW 442
RING-H2_UBR2 cd16686
RING finger, H2 subclass, found in ubiquitin-protein ligase E3-alpha-2 (UBR2) and similar ...
 591-706 7.64e-84

RING finger, H2 subclass, found in ubiquitin-protein ligase E3-alpha-2 (UBR2) and similar proteins; UBR2, also known as N-recognin-2 or E3alpha-II, is an E3 ubiquitin-protein ligase that plays an important role in maintaining genome integrity and in homologous recombination repair. It regulates the level of the transcription factor Rpn4 (also known as Son1 and Ufd5) through ubiquitylation. The ubiquitin-conjugating enzyme Rad6, another binding partner of URB2, and an additional factor Mub1, are required for the ubiquitin-dependent degradation of Rpn4. UBR2 associates with Mub1 to form a Mub1/Ubr2 complex that regulates the conserved Dsn1 kinetochore protein levels, which is a part of a quality control system that monitors kinetochore integrity, thus ensuring genomic stability. As the recognition component of a major cellular proteolytic system, UBR2 is associated with chromatin and controls chromatin dynamics and gene expression in both spermatocytes and somatic cells. UBR2 also mediates transcriptional silencing during spermatogenesis via histone ubiquitination. It functions as a scaffold E3 promoting HR6B/UbcH2-dependent ubiquitylation of H2A and H2B, but not H3 and H4. It also binds to Tex19.1, also known as Tex19, a germ cell-specific protein, and metabolically stabilizes it during spermatogenesis. Furthermore, UBR2 is involved in skeletal muscle (SKM) atrophy. Its expression can be modulated by the mouse ether-a-gogo-related gene 1a (MERG1a) potassium channel. In addition, UBR2 up-regulation in cachectic muscle is mediated by the p38beta-CCAAT/enhancer binding protein (C/EBP)-beta signaling pathway responsible for the bulk of tumor-induced muscle proteolysis. UBR2 contains an N-terminal ubiquitin-recognin (UBR) box involved in binding type-1 (basic) N-end rule substrate, an N-domain (also known as ClpS domain) required for type-2 (bulky hydrophobic) N-end rule substrate recognition, a C3H2C3-type RING-H2 finger, and a C-terminal UBR-specific autoinhibitory (UAIN) domain.


Pssm-ID: 438347  Cd Length: 116  Bit Score: 268.42  E-value: 7.64e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767939602  591 TCILCQEEQEVKVESRAMVLAAFVQRSTVLSKNRSKFIQDPEKYDPLFMHPDLSCGTHTSSCGHIMHAHCWQRYFDSVQA 670
Cdd:cd16686     1 TCILCQEEQEIKVDNKAMVLAAFVQRSTVMSKNRSRVIHDPEKYDPLFMHPDLSCGTHTGSCGHIMHAHCWQRYFDAVQA 80

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 767939602  671 KEQRRQQRLRLHTSYDVENGEFLCPLCECLSNTVIP 706
Cdd:cd16686    81 KEQRRQQRLRVHTSYDVENGEFLCPLCECLSNTVIP 116
 
Name Accession Description Interval E-value
PRT6_C pfam18995
Proteolysis_6 C-terminal; This is the C-terminal domain mainly found in E3 ubiquitin ligases. ...
 794-1212 1.83e-122

Proteolysis_6 C-terminal; This is the C-terminal domain mainly found in E3 ubiquitin ligases. Proteolysis 6 (PRT6) encodes a ubiquitin E3 ligase belonging to the N-end rule pathway of targeted protein degradation, which is a specialized subset of the ubiquitin proteasome system. In Arabidopsis, at least two N-recognins (E3 ubiquitin ligases) with different substrate specificities exist, namely PROTEOLYSIS1 (PRT1) and PRT6.


Pssm-ID: 465944  Cd Length: 444  Bit Score: 385.85  E-value: 1.83e-122
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767939602   794 TATYKVGLKV---HPNEEDPRVPI-MCWGSCAYTIQSIERILSDEDKP---LFGPLPCRLDDCLRSLTRFAAAHWTV--- 863
Cdd:pfam18995    3 DTTRPNGLQSrhpSDPSSDDLVSSdLLWDSLAYTISSIEIAQRGVGKPggtLLGKLPEQQLTLLRILSETVSSYASVgfl 82

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767939602   864 -------ASVSVVQGHFCKLFASLVPNDSH--EELPCILDIDMFHLLVGLVLAFPALQCQDFSgislgtgdlHIFHLVTM 934
Cdd:pfam18995   83 rsggtneEGRELIRRGILRLLLQLFPRISSlgEASPPLLLRDPFGLLVELALCLPSLFLEDIL---------HLLRLCYL 153

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767939602   935 AHIIQILLTSCTEENGMDQENPP---CEEESAVLALYKTLHQYTGSALKEIP----------SGWHLWRSVRAGIMPFLK 1001
Cdd:pfam18995  154 AEIVQVVLTLSRNLSKTLRWAEGletRSPSDESEDALRDFREFVGSVLRHSGvfadldndgfDDERLYKLVRKYALPFLR 233

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767939602  1002 CSALFFHYLNGVPSPPDI-QVPGTSHFEHLCSYLSLPNnLICLFQENSEIMNSLIESWCRNSEVKRYLEGERDA----IR 1076
Cdd:pfam18995  234 KAAILLHVLYGVPFPSPLsSDPEGDELERLCKYLRLPS-LDELCQSNQDTLRSLVSGWCRHPAVFGHLSASPLNpsilLS 312

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767939602  1077 YPReSNKLINLPEDYSSLINQASNFSCPKSGGDkSRAPTLCLVCGSLLCSQSYCCQTElegEDVGACTAHTYSCGSGVGI 1156
Cdd:pfam18995  313 HPG-IFELVGLPKDYDTLIEEASKRRCPTCGTD-PTDPALCLFCGTILCSQSYCCQEE---LNVGECNQHMRKCGGGVGI 387

                          410       420       430       440       450
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 767939602  1157 FLRVRECQVLFLAGKTkGCFYSPPYLDDYGETDQGLRRGNPLHLCKERFKKIQKLW 1212
Cdd:pfam18995  388 FLLIRKCTILLLHGGN-GSFWPAPYLDAHGETDPGLRRGRPLYLNQKRYDELRRLW 442
RING-H2_UBR2 cd16686
RING finger, H2 subclass, found in ubiquitin-protein ligase E3-alpha-2 (UBR2) and similar ...
 591-706 7.64e-84

RING finger, H2 subclass, found in ubiquitin-protein ligase E3-alpha-2 (UBR2) and similar proteins; UBR2, also known as N-recognin-2 or E3alpha-II, is an E3 ubiquitin-protein ligase that plays an important role in maintaining genome integrity and in homologous recombination repair. It regulates the level of the transcription factor Rpn4 (also known as Son1 and Ufd5) through ubiquitylation. The ubiquitin-conjugating enzyme Rad6, another binding partner of URB2, and an additional factor Mub1, are required for the ubiquitin-dependent degradation of Rpn4. UBR2 associates with Mub1 to form a Mub1/Ubr2 complex that regulates the conserved Dsn1 kinetochore protein levels, which is a part of a quality control system that monitors kinetochore integrity, thus ensuring genomic stability. As the recognition component of a major cellular proteolytic system, UBR2 is associated with chromatin and controls chromatin dynamics and gene expression in both spermatocytes and somatic cells. UBR2 also mediates transcriptional silencing during spermatogenesis via histone ubiquitination. It functions as a scaffold E3 promoting HR6B/UbcH2-dependent ubiquitylation of H2A and H2B, but not H3 and H4. It also binds to Tex19.1, also known as Tex19, a germ cell-specific protein, and metabolically stabilizes it during spermatogenesis. Furthermore, UBR2 is involved in skeletal muscle (SKM) atrophy. Its expression can be modulated by the mouse ether-a-gogo-related gene 1a (MERG1a) potassium channel. In addition, UBR2 up-regulation in cachectic muscle is mediated by the p38beta-CCAAT/enhancer binding protein (C/EBP)-beta signaling pathway responsible for the bulk of tumor-induced muscle proteolysis. UBR2 contains an N-terminal ubiquitin-recognin (UBR) box involved in binding type-1 (basic) N-end rule substrate, an N-domain (also known as ClpS domain) required for type-2 (bulky hydrophobic) N-end rule substrate recognition, a C3H2C3-type RING-H2 finger, and a C-terminal UBR-specific autoinhibitory (UAIN) domain.


Pssm-ID: 438347  Cd Length: 116  Bit Score: 268.42  E-value: 7.64e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767939602  591 TCILCQEEQEVKVESRAMVLAAFVQRSTVLSKNRSKFIQDPEKYDPLFMHPDLSCGTHTSSCGHIMHAHCWQRYFDSVQA 670
Cdd:cd16686     1 TCILCQEEQEIKVDNKAMVLAAFVQRSTVMSKNRSRVIHDPEKYDPLFMHPDLSCGTHTGSCGHIMHAHCWQRYFDAVQA 80

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 767939602  671 KEQRRQQRLRLHTSYDVENGEFLCPLCECLSNTVIP 706
Cdd:cd16686    81 KEQRRQQRLRVHTSYDVENGEFLCPLCECLSNTVIP 116
RING-H2_UBR1 cd16685
RING finger, H2 subclass, found in ubiquitin-protein ligase E3-alpha-1 (UBR1) and similar ...
 590-708 4.49e-51

RING finger, H2 subclass, found in ubiquitin-protein ligase E3-alpha-1 (UBR1) and similar proteins; UBR1, also known as N-recognin-1 or E3alpha-I, is an E3 ubiquitin-protein ligase component of the N-end rule pathway. It also promotes degradation of proteins via distinct mechanism that detects a misfolded conformation. UBR1 associates with the RAD6-encoded E2 enzyme to form an E2-E3 complex that catalyzes the synthesis of a substrate-linked multi-ubiquitin chain and may also mediate the delivery of substrates to the 26S proteasome. Moreover, UBR1 promotes the degradation of misfolded proteins in the cytosol. It promotes protein kinase quality control and sensitizes cells to heat shock protein 90 (Hsp90) inhibition. Furthermore, UBR1 functions as a polyubiquitylation-enhancing component of the UBR1-UFD4 complex in its targeting of ubiquitin-fusion degradation (UFD) substrates. UBR1 harbors at least three distinct substrate-binding sites and functions in association with Ubc2/Rad6 and also Ubc4. It contains an N-terminal ubiquitin-recognin (UBR) box involved in binding type-1 (basic) N-end rule substrate, an N-domain (also known as ClpS domain) required for type-2 (bulky hydrophobic) N-end rule substrate recognition, a C3H2C3-type RING-H2 finger, and a C-terminal UBR-specific autoinhibitory (UAIN) domain. A missense mutation in UBR1 is responsible for Johanson-Blizzard syndrome leads to UBR box unfolding and loss of function.


Pssm-ID: 438346  Cd Length: 120  Bit Score: 175.44  E-value: 4.49e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767939602  590 VTCILCQEEQEVKVESRAMVLAAFVQRSTVLSKNRSKFIQ-DPEKYDPLFMHPDLSCGTHTSSCGHIMHAHCWQRYFDSV 668
Cdd:cd16685     3 LTCILCQEEQEVKLDKMAMVLTACVQKSTALTQNRGKVVElTGENFDPLFMNPDLAYGTHTGSCGHVMHAVCWQKYFEAV 82

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 767939602  669 QakeQRRQQRLRLHTSYDVENGEFLCPLCECLSNTVIPLL 708
Cdd:cd16685    83 Q---NSTRQRLHVELIFDLENGEYLCPLCKSLCNTVIPII 119
RING-H2_UBR1-like cd16482
RING finger, H2 subclass, found in ubiquitin-protein ligase E3-alpha-1 (UBR1), E3-alpha-2 ...
 646-706 1.18e-28

RING finger, H2 subclass, found in ubiquitin-protein ligase E3-alpha-1 (UBR1), E3-alpha-2 (UBR2), and similar proteins; Two UBR family members, UBR1 and UBR2, are major N-recognin ubiquitin ligases that both function in the N-end rule degradation pathway. They can recognize substrate proteins with type-1 (basic) and type-2 (bulky hydrophobic) N-terminal residues as part of N-degrons and an internal lysine residue for ubiquitin conjugation. They also function in a quality control pathway for degradation of unfolded cytosolic proteins. Their action is stimulated by Hsp70. Moreover, UBR1 and UBR2 are negative regulators of the leucine-mTOR signaling pathway. Leucine might activate this pathway in part through inhibition of their ubiquitin ligase activity. In yeast, only one E3, encoded by UBR1, mediates the recognition of substrates by the N-end rule pathway. Saccharomyces cerevisiae UBR1 also functions as an additional E3 ligase in the endoplasmic reticulum-associated protein degradation (ERAD). It can provide ubiquitin ligation activity for the ERAD substrate mutated Ste6 (sterile). Schizosaccharomyces pombe UBR1 is a critical regulator that influences the oxidative stress response via degradation of active Pap1 basic leucine zipper (bZIP) transcription factor in the nucleus. Both UBR1 and UBR2 contain an N-terminal ubiquitin-recognin (UBR) box involved in binding type-1 (basic) N-end rule substrate, an N-domain (also known as ClpS domain) required for type-2 (bulky hydrophobic) N-end rule substrate recognition, a C3H2C3-type RING-H2 finger, and a C-terminal UBR-specific autoinhibitory (UAIN) domain.


Pssm-ID: 438145  Cd Length: 67  Bit Score: 109.74  E-value: 1.18e-28
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767939602  646 GTHTSSCGHIMHAHCWQRYFDSVQAKEQRRQQRLRLHtSYDVENGEFLCPLCECLSNTVIP 706
Cdd:cd16482     8 GLHISSCGHVMHYDCWQRYFDSVRLREQRRPAFRRHH-SEDVSKGEFLCPLCKSLSNTVLP 67
RING-H2_UBR3 cd16483
RING finger, H2 subclass, found in ubiquitin-protein ligase E3-alpha-3 (UBR3) and similar ...
 645-706 2.06e-12

RING finger, H2 subclass, found in ubiquitin-protein ligase E3-alpha-3 (UBR3) and similar proteins; UBR3, also known as N-recognin-3, E3alpha-III, or zinc finger protein 650, is an E3 ubiquitin-protein ligase targeting the essential DNA repair protein APE1, also known as Ref-1, for ubiquitylation. It regulates cellular levels of APE1 and is required for genome stability. It also plays a regulatory role in sensory pathways, including olfaction. In Drosophila, UBR3 also regulates apoptosis by controlling the activity of Drosophila inhibitor of apoptosis protein 1 (DIAP1), which is required to prevent caspase activation. UBR3 contains an N-terminal ubiquitin-recognin (UBR) box, a C3H2C3-type RING-H2 finger, and a C-terminal UBR-specific autoinhibitory (UAIN) domain.


Pssm-ID: 438146  Cd Length: 63  Bit Score: 63.18  E-value: 2.06e-12
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767939602  645 CGTHTSSCGHIMHAHCWQRYFDSVQAKEQRRQqrlrlhtSYDVENGEFLCPLCECLSNTVIP 706
Cdd:cd16483     9 SGVHVQTCGHYIHIDCHKSYLESLRQDQVGLQ-------LLSVRRGEFTCPLCRQLSNSVLP 63
RING-H2_RNF25 cd16470
RING finger, H2 subclass, found in RING finger protein 25 (RNF25) and similar proteins; RNF25, ...
 650-697 6.03e-03

RING finger, H2 subclass, found in RING finger protein 25 (RNF25) and similar proteins; RNF25, also known as AO7, is a putative E3 ubiquitin-protein ligase that was initially identified as an interacting protein of the E2 ubiquitin-conjugating enzyme, Ubc5B. It is ubiquitously expressed in various tissues and predominantly localized in the nucleus. RNF25 activates the nuclear factor (NF)-kappaB-dependent gene expression upon stimulation with Interleukin-1 beta (IL-1beta), or tumor necrosis factor (TNF), or overexpression of NF-kappaB-inducing kinase. It interacts with the p65 transactivation domain (TAD) and modulates its transcriptional activity. RNF25 contains an N-terminal RWD domain, a C3H2C3-type RING-H2 finger, and a C-terminal Pro-rich region. Both the RING-H2 finger and the C-terminal regions of RNF25 are necessary for transcriptional activation.


Pssm-ID: 438133 [Multi-domain]  Cd Length: 74  Bit Score: 36.61  E-value: 6.03e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 767939602  650 SSCGHIMHAHCWQRYFDSVQA--KEQRRQQRLRLHTSYDVENGEFLCPLC 697
Cdd:cd16470    21 TPCYHYFHSHCLARYIQHMEEnlKEEQEEQEERPRAQTEQEQFQVLCPVC 70
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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