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Conserved domains on  [gi|1386876278|ref|NP_001349984|]
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tether containing UBX domain for GLUT4 isoform 4 [Mus musculus]

Protein Classification

MoaD/ThiS family protein; Ubl5/Hub1 family ubiquitin-like protein( domain architecture ID 13006039)

MoaD/ThiS family protein is a ubiquitin-like protein, may be involved in sulfur transfer| Ubl5/Hub1 family ubiquitin-like protein similar to Saccharomyces cerevisiae Hub1 that plays a role in splice-site usage and alternative splicing

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
UBX1_UBXN9 cd17075
Ubiquitin regulatory domain X (UBX) 1 found in UBX domain protein 9 (UBXN9, UBXD9, or ASPSCR1) ...
 90-171 3.71e-34

Ubiquitin regulatory domain X (UBX) 1 found in UBX domain protein 9 (UBXN9, UBXD9, or ASPSCR1) and similar proteins; UBXN9, also termed tether containing UBX domain for GLUT4 (TUG), or alveolar soft part sarcoma chromosomal region candidate gene 1 protein (ASPSCR1), or alveolar soft part sarcoma locus (ASPL), or renal papillary cell carcinoma protein 17 (RCC17), belongs to the UBXD family of proteins that contains two ubiquitin regulatory domains X (UBX) with a beta-grasp ubiquitin-like fold, but without the C-terminal double glycine motif. UBX domain is typically located at the carboxyl terminus of proteins, and participates broadly in the regulation of protein degradation. In addition, UBXN9 contains an N-terminal ubiquitin-like (Ubl) domain. UBXN9 functions as a cofactor of p97 (also known as VCP or Cdc48), which is a homohexameric AAA ATPase (ATPase associated with a variety of activities) involved in a variety of functions ranging from cell-cycle regulation to membrane fusion and protein degradation. UBXN9 is involved in insulin-stimulated redistribution of the glucose transporter GLUT4, assembly of the Golgi apparatus. In addition to GLUT4, UBXN9 also controls vesicle translocation by interacting with insulin-regulated aminopeptidase (IRAP), a transmembrane aminopeptidase. UBXN9 and its budding yeast ortholog, Ubx4p, are multifunctional proteins that share some, but not all functions. Yeast Ubx4p is important for endoplasmic reticulum-associated protein degradation (ERAD) but UBXN9 appears not to share this function.


:

Pssm-ID: 340595  Cd Length: 85  Bit Score: 123.89  E-value: 3.71e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876278  90 NIVRIAFQLDDGSRLQDAFCSRQTLWELLSHFAQTRER---LQQLGEKTPVCVYMRNEVTGRAALQNTTLQSLGLTGGSA 166
Cdd:cd17075     1 SLVTIALQLEDGSRLQKSFPPSTTLWDILEHFEQESNVnlnLTEDGYLEPVCIYMRREISGEEALKKTTLKSLGLTSGSA 80


                  ....*
gi 1386876278 167 TIRFV 171
Cdd:cd17075    81 LIRLV 85
Ubl_ASPSCR1_like cd16105
Ubiquitin-like (Ubl) domain found at the N-terminus of mammalian ASPSCR1 (alveolar soft part ...
 12-80 1.05e-33

Ubiquitin-like (Ubl) domain found at the N-terminus of mammalian ASPSCR1 (alveolar soft part sarcoma chromosomal region candidate gene 1 protein), Saccharomyces cerevisie Ubx4p, and similar proteins; ASPSCR1 (alveolar soft part sarcoma chromosomal region candidate gene 1 protein) is also known as alveolar soft part sarcoma locus protein (ASPL), tether containing UBX domain for GLUT4, TUG, UBX domain protein 9, UBXD9, UBXN9 or renal papillary cell carcinoma protein 17 (RCC17). The majority of members of this family contain two beta-grasp ubiquitin-like fold domains: the N-terminal UBL domain (described in this CD), and a C-terminal UBX domain. This UBL domain lacks the characteristic C-terminal double glycine motif. ASPSCR1 functions as a cofactor of the hexameric AAA (ATPase associated with various activities) ATPase complex, known as p97 or VCP in mammals and Cdc48p in yeast. In mammalian cells, ASPSCR1 is involved in insulin-stimulated redistribution of the glucose transporter GLUT4 and assembly of the Golgi apparatus; ASPSCR1 also plays a role in controlling vesicle translocation by interacting with insulin-regulated aminopeptidase (IRAP), a transmembrane aminopeptidase. Ubx4p and ASPSCR1 have only partially overlapping functions: both interact with p97/Cdc48p; however, Ubx4p is important for the ERAD (endoplasmic reticulum-associated protein degradation) pathway while ASPSCR1 appears not to be.


:

Pssm-ID: 340522  Cd Length: 71  Bit Score: 121.92  E-value: 1.05e-33
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876278  12 VSVLAPNGRRHTVKVTPSTVLLQVLEDTCRRQDFNPSE-YDLKFQRTVLDLSLQWRFANLPNNAKLEMVP 80
Cdd:cd16105     1 LTVLYPNGRRQTVKVTPNTPLSQVLEEACKKFGLDPSSeYSLKHNRKPLDLSLPFRLSNLPNNAKLELVK 70
UBX2_UBXN9 cd16118
Ubiquitin regulatory domain X (UBX) 2 found in UBX domain protein 9 (UBXN9, UBXD9, or ASPSCR1) ...
 387-438 1.26e-21

Ubiquitin regulatory domain X (UBX) 2 found in UBX domain protein 9 (UBXN9, UBXD9, or ASPSCR1) and similar proteins; UBXN9, also termed tether containing UBX domain for GLUT4 (TUG), or alveolar soft part sarcoma chromosomal region candidate gene 1 protein (ASPSCR1), or alveolar soft part sarcoma locus (ASPL), or renal papillary cell carcinoma protein 17 (RCC17), belongs to the UBXD family of proteins that contains two ubiquitin regulatory domains X (UBX) with a beta-grasp ubiquitin-like fold, but without the C-terminal double glycine motif. UBX domain is typically located at the carboxyl terminus of proteins, and participates broadly in the regulation of protein degradation. In addition, UBXN9 contains an N-terminal ubiquitin-like (Ubl) domain. UBXN9 functions as a cofactor of p97 (also known as VCP or Cdc48), which is a homohexameric AAA ATPase (ATPase associated with a variety of activities) involved in a variety of functions ranging from cell-cycle regulation to membrane fusion and protein degradation. However, high-affinity interacting protein ASPL efficiently promotes p97 hexamer disassembly, resulting in the formation of stable p97:ASPL heterotetramers; the extended UBX domain (eUBX) in ASPL is critical for p97 hexamer disassembly and facilitates the assembly of p97:ASPL heterotetramers.UBXN9 is involved in insulin-stimulated redistribution of the glucose transporter GLUT4, assembly of the Golgi apparatus. In addition to GLUT4, UBXN9 also controls vesicle translocation by interacting with insulin-regulated aminopeptidase (IRAP), a transmembrane aminopeptidase. UBXN9 and its budding yeast ortholog, Ubx4p, are multifunctional proteins that share some, but not all functions. Yeast Ubx4p is important for endoplasmic reticulum-associated protein degradation (ERAD) but UBXN9 appears not to share this function.


:

Pssm-ID: 340535  Cd Length: 74  Bit Score: 88.78  E-value: 1.26e-21
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1386876278 387 VALRVLFPDRYILQGFFRPSETV---------------------IAPPKMVLDDHTLTLFQANLFPAALVHFG 438
Cdd:cd16118     1 AVIRVQFPDRLVLQAFFRPLETVralydfvkshladpdlpfylyTTPPKRVLKDKNKTLYQAGLVPAALVYFG 73
 
Name Accession Description Interval E-value
UBX1_UBXN9 cd17075
Ubiquitin regulatory domain X (UBX) 1 found in UBX domain protein 9 (UBXN9, UBXD9, or ASPSCR1) ...
 90-171 3.71e-34

Ubiquitin regulatory domain X (UBX) 1 found in UBX domain protein 9 (UBXN9, UBXD9, or ASPSCR1) and similar proteins; UBXN9, also termed tether containing UBX domain for GLUT4 (TUG), or alveolar soft part sarcoma chromosomal region candidate gene 1 protein (ASPSCR1), or alveolar soft part sarcoma locus (ASPL), or renal papillary cell carcinoma protein 17 (RCC17), belongs to the UBXD family of proteins that contains two ubiquitin regulatory domains X (UBX) with a beta-grasp ubiquitin-like fold, but without the C-terminal double glycine motif. UBX domain is typically located at the carboxyl terminus of proteins, and participates broadly in the regulation of protein degradation. In addition, UBXN9 contains an N-terminal ubiquitin-like (Ubl) domain. UBXN9 functions as a cofactor of p97 (also known as VCP or Cdc48), which is a homohexameric AAA ATPase (ATPase associated with a variety of activities) involved in a variety of functions ranging from cell-cycle regulation to membrane fusion and protein degradation. UBXN9 is involved in insulin-stimulated redistribution of the glucose transporter GLUT4, assembly of the Golgi apparatus. In addition to GLUT4, UBXN9 also controls vesicle translocation by interacting with insulin-regulated aminopeptidase (IRAP), a transmembrane aminopeptidase. UBXN9 and its budding yeast ortholog, Ubx4p, are multifunctional proteins that share some, but not all functions. Yeast Ubx4p is important for endoplasmic reticulum-associated protein degradation (ERAD) but UBXN9 appears not to share this function.


Pssm-ID: 340595  Cd Length: 85  Bit Score: 123.89  E-value: 3.71e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876278  90 NIVRIAFQLDDGSRLQDAFCSRQTLWELLSHFAQTRER---LQQLGEKTPVCVYMRNEVTGRAALQNTTLQSLGLTGGSA 166
Cdd:cd17075     1 SLVTIALQLEDGSRLQKSFPPSTTLWDILEHFEQESNVnlnLTEDGYLEPVCIYMRREISGEEALKKTTLKSLGLTSGSA 80


                  ....*
gi 1386876278 167 TIRFV 171
Cdd:cd17075    81 LIRLV 85
Ubl_ASPSCR1_like cd16105
Ubiquitin-like (Ubl) domain found at the N-terminus of mammalian ASPSCR1 (alveolar soft part ...
 12-80 1.05e-33

Ubiquitin-like (Ubl) domain found at the N-terminus of mammalian ASPSCR1 (alveolar soft part sarcoma chromosomal region candidate gene 1 protein), Saccharomyces cerevisie Ubx4p, and similar proteins; ASPSCR1 (alveolar soft part sarcoma chromosomal region candidate gene 1 protein) is also known as alveolar soft part sarcoma locus protein (ASPL), tether containing UBX domain for GLUT4, TUG, UBX domain protein 9, UBXD9, UBXN9 or renal papillary cell carcinoma protein 17 (RCC17). The majority of members of this family contain two beta-grasp ubiquitin-like fold domains: the N-terminal UBL domain (described in this CD), and a C-terminal UBX domain. This UBL domain lacks the characteristic C-terminal double glycine motif. ASPSCR1 functions as a cofactor of the hexameric AAA (ATPase associated with various activities) ATPase complex, known as p97 or VCP in mammals and Cdc48p in yeast. In mammalian cells, ASPSCR1 is involved in insulin-stimulated redistribution of the glucose transporter GLUT4 and assembly of the Golgi apparatus; ASPSCR1 also plays a role in controlling vesicle translocation by interacting with insulin-regulated aminopeptidase (IRAP), a transmembrane aminopeptidase. Ubx4p and ASPSCR1 have only partially overlapping functions: both interact with p97/Cdc48p; however, Ubx4p is important for the ERAD (endoplasmic reticulum-associated protein degradation) pathway while ASPSCR1 appears not to be.


Pssm-ID: 340522  Cd Length: 71  Bit Score: 121.92  E-value: 1.05e-33
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876278  12 VSVLAPNGRRHTVKVTPSTVLLQVLEDTCRRQDFNPSE-YDLKFQRTVLDLSLQWRFANLPNNAKLEMVP 80
Cdd:cd16105     1 LTVLYPNGRRQTVKVTPNTPLSQVLEEACKKFGLDPSSeYSLKHNRKPLDLSLPFRLSNLPNNAKLELVK 70
TUG-UBL1 pfam11470
TUG ubiquitin-like domain; TUG is a GLUT4 regulating protein and functions to retain membrane ...
 15-78 1.68e-27

TUG ubiquitin-like domain; TUG is a GLUT4 regulating protein and functions to retain membrane vesicles containing GLUT4 intracellularly. TUG releases the GLUT4 containing vesicles to the cellular exocytic machinery in response to insulin stimulation which allows translocation to the plasma membrane. TUG has an N-terminal ubiquitin-like domain (UBL1) which in similar proteins appears to participate in protein-protein interactions. The region does have a area of negative electrostatic potential and increased backbone motility which leads to suggestions of a potential protein-protein interaction site. This domain is also found at the N-terminus of yeast UBX4.


Pssm-ID: 463285  Cd Length: 65  Bit Score: 104.89  E-value: 1.68e-27
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1386876278  15 LAPNGRRHTVKVTPSTVLLQVLEDTCRRQDF-NPSEYDLKFQRTVLDLSLQWRFANLPNNAKLEM 78
Cdd:pfam11470   1 VTYNFRRKKVKVTPNTTLNDVLEEACKKFKLdDSDSYTLKHNNKPLDLSLPFRLSNLPNGAKLEL 65
UBX2_UBXN9 cd16118
Ubiquitin regulatory domain X (UBX) 2 found in UBX domain protein 9 (UBXN9, UBXD9, or ASPSCR1) ...
 387-438 1.26e-21

Ubiquitin regulatory domain X (UBX) 2 found in UBX domain protein 9 (UBXN9, UBXD9, or ASPSCR1) and similar proteins; UBXN9, also termed tether containing UBX domain for GLUT4 (TUG), or alveolar soft part sarcoma chromosomal region candidate gene 1 protein (ASPSCR1), or alveolar soft part sarcoma locus (ASPL), or renal papillary cell carcinoma protein 17 (RCC17), belongs to the UBXD family of proteins that contains two ubiquitin regulatory domains X (UBX) with a beta-grasp ubiquitin-like fold, but without the C-terminal double glycine motif. UBX domain is typically located at the carboxyl terminus of proteins, and participates broadly in the regulation of protein degradation. In addition, UBXN9 contains an N-terminal ubiquitin-like (Ubl) domain. UBXN9 functions as a cofactor of p97 (also known as VCP or Cdc48), which is a homohexameric AAA ATPase (ATPase associated with a variety of activities) involved in a variety of functions ranging from cell-cycle regulation to membrane fusion and protein degradation. However, high-affinity interacting protein ASPL efficiently promotes p97 hexamer disassembly, resulting in the formation of stable p97:ASPL heterotetramers; the extended UBX domain (eUBX) in ASPL is critical for p97 hexamer disassembly and facilitates the assembly of p97:ASPL heterotetramers.UBXN9 is involved in insulin-stimulated redistribution of the glucose transporter GLUT4, assembly of the Golgi apparatus. In addition to GLUT4, UBXN9 also controls vesicle translocation by interacting with insulin-regulated aminopeptidase (IRAP), a transmembrane aminopeptidase. UBXN9 and its budding yeast ortholog, Ubx4p, are multifunctional proteins that share some, but not all functions. Yeast Ubx4p is important for endoplasmic reticulum-associated protein degradation (ERAD) but UBXN9 appears not to share this function.


Pssm-ID: 340535  Cd Length: 74  Bit Score: 88.78  E-value: 1.26e-21
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1386876278 387 VALRVLFPDRYILQGFFRPSETV---------------------IAPPKMVLDDHTLTLFQANLFPAALVHFG 438
Cdd:cd16118     1 AVIRVQFPDRLVLQAFFRPLETVralydfvkshladpdlpfylyTTPPKRVLKDKNKTLYQAGLVPAALVYFG 73
 
Name Accession Description Interval E-value
UBX1_UBXN9 cd17075
Ubiquitin regulatory domain X (UBX) 1 found in UBX domain protein 9 (UBXN9, UBXD9, or ASPSCR1) ...
 90-171 3.71e-34

Ubiquitin regulatory domain X (UBX) 1 found in UBX domain protein 9 (UBXN9, UBXD9, or ASPSCR1) and similar proteins; UBXN9, also termed tether containing UBX domain for GLUT4 (TUG), or alveolar soft part sarcoma chromosomal region candidate gene 1 protein (ASPSCR1), or alveolar soft part sarcoma locus (ASPL), or renal papillary cell carcinoma protein 17 (RCC17), belongs to the UBXD family of proteins that contains two ubiquitin regulatory domains X (UBX) with a beta-grasp ubiquitin-like fold, but without the C-terminal double glycine motif. UBX domain is typically located at the carboxyl terminus of proteins, and participates broadly in the regulation of protein degradation. In addition, UBXN9 contains an N-terminal ubiquitin-like (Ubl) domain. UBXN9 functions as a cofactor of p97 (also known as VCP or Cdc48), which is a homohexameric AAA ATPase (ATPase associated with a variety of activities) involved in a variety of functions ranging from cell-cycle regulation to membrane fusion and protein degradation. UBXN9 is involved in insulin-stimulated redistribution of the glucose transporter GLUT4, assembly of the Golgi apparatus. In addition to GLUT4, UBXN9 also controls vesicle translocation by interacting with insulin-regulated aminopeptidase (IRAP), a transmembrane aminopeptidase. UBXN9 and its budding yeast ortholog, Ubx4p, are multifunctional proteins that share some, but not all functions. Yeast Ubx4p is important for endoplasmic reticulum-associated protein degradation (ERAD) but UBXN9 appears not to share this function.


Pssm-ID: 340595  Cd Length: 85  Bit Score: 123.89  E-value: 3.71e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876278  90 NIVRIAFQLDDGSRLQDAFCSRQTLWELLSHFAQTRER---LQQLGEKTPVCVYMRNEVTGRAALQNTTLQSLGLTGGSA 166
Cdd:cd17075     1 SLVTIALQLEDGSRLQKSFPPSTTLWDILEHFEQESNVnlnLTEDGYLEPVCIYMRREISGEEALKKTTLKSLGLTSGSA 80


                  ....*
gi 1386876278 167 TIRFV 171
Cdd:cd17075    81 LIRLV 85
Ubl_ASPSCR1_like cd16105
Ubiquitin-like (Ubl) domain found at the N-terminus of mammalian ASPSCR1 (alveolar soft part ...
 12-80 1.05e-33

Ubiquitin-like (Ubl) domain found at the N-terminus of mammalian ASPSCR1 (alveolar soft part sarcoma chromosomal region candidate gene 1 protein), Saccharomyces cerevisie Ubx4p, and similar proteins; ASPSCR1 (alveolar soft part sarcoma chromosomal region candidate gene 1 protein) is also known as alveolar soft part sarcoma locus protein (ASPL), tether containing UBX domain for GLUT4, TUG, UBX domain protein 9, UBXD9, UBXN9 or renal papillary cell carcinoma protein 17 (RCC17). The majority of members of this family contain two beta-grasp ubiquitin-like fold domains: the N-terminal UBL domain (described in this CD), and a C-terminal UBX domain. This UBL domain lacks the characteristic C-terminal double glycine motif. ASPSCR1 functions as a cofactor of the hexameric AAA (ATPase associated with various activities) ATPase complex, known as p97 or VCP in mammals and Cdc48p in yeast. In mammalian cells, ASPSCR1 is involved in insulin-stimulated redistribution of the glucose transporter GLUT4 and assembly of the Golgi apparatus; ASPSCR1 also plays a role in controlling vesicle translocation by interacting with insulin-regulated aminopeptidase (IRAP), a transmembrane aminopeptidase. Ubx4p and ASPSCR1 have only partially overlapping functions: both interact with p97/Cdc48p; however, Ubx4p is important for the ERAD (endoplasmic reticulum-associated protein degradation) pathway while ASPSCR1 appears not to be.


Pssm-ID: 340522  Cd Length: 71  Bit Score: 121.92  E-value: 1.05e-33
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1386876278  12 VSVLAPNGRRHTVKVTPSTVLLQVLEDTCRRQDFNPSE-YDLKFQRTVLDLSLQWRFANLPNNAKLEMVP 80
Cdd:cd16105     1 LTVLYPNGRRQTVKVTPNTPLSQVLEEACKKFGLDPSSeYSLKHNRKPLDLSLPFRLSNLPNNAKLELVK 70
TUG-UBL1 pfam11470
TUG ubiquitin-like domain; TUG is a GLUT4 regulating protein and functions to retain membrane ...
 15-78 1.68e-27

TUG ubiquitin-like domain; TUG is a GLUT4 regulating protein and functions to retain membrane vesicles containing GLUT4 intracellularly. TUG releases the GLUT4 containing vesicles to the cellular exocytic machinery in response to insulin stimulation which allows translocation to the plasma membrane. TUG has an N-terminal ubiquitin-like domain (UBL1) which in similar proteins appears to participate in protein-protein interactions. The region does have a area of negative electrostatic potential and increased backbone motility which leads to suggestions of a potential protein-protein interaction site. This domain is also found at the N-terminus of yeast UBX4.


Pssm-ID: 463285  Cd Length: 65  Bit Score: 104.89  E-value: 1.68e-27
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1386876278  15 LAPNGRRHTVKVTPSTVLLQVLEDTCRRQDF-NPSEYDLKFQRTVLDLSLQWRFANLPNNAKLEM 78
Cdd:pfam11470   1 VTYNFRRKKVKVTPNTTLNDVLEEACKKFKLdDSDSYTLKHNNKPLDLSLPFRLSNLPNGAKLEL 65
UBX2_UBXN9 cd16118
Ubiquitin regulatory domain X (UBX) 2 found in UBX domain protein 9 (UBXN9, UBXD9, or ASPSCR1) ...
 387-438 1.26e-21

Ubiquitin regulatory domain X (UBX) 2 found in UBX domain protein 9 (UBXN9, UBXD9, or ASPSCR1) and similar proteins; UBXN9, also termed tether containing UBX domain for GLUT4 (TUG), or alveolar soft part sarcoma chromosomal region candidate gene 1 protein (ASPSCR1), or alveolar soft part sarcoma locus (ASPL), or renal papillary cell carcinoma protein 17 (RCC17), belongs to the UBXD family of proteins that contains two ubiquitin regulatory domains X (UBX) with a beta-grasp ubiquitin-like fold, but without the C-terminal double glycine motif. UBX domain is typically located at the carboxyl terminus of proteins, and participates broadly in the regulation of protein degradation. In addition, UBXN9 contains an N-terminal ubiquitin-like (Ubl) domain. UBXN9 functions as a cofactor of p97 (also known as VCP or Cdc48), which is a homohexameric AAA ATPase (ATPase associated with a variety of activities) involved in a variety of functions ranging from cell-cycle regulation to membrane fusion and protein degradation. However, high-affinity interacting protein ASPL efficiently promotes p97 hexamer disassembly, resulting in the formation of stable p97:ASPL heterotetramers; the extended UBX domain (eUBX) in ASPL is critical for p97 hexamer disassembly and facilitates the assembly of p97:ASPL heterotetramers.UBXN9 is involved in insulin-stimulated redistribution of the glucose transporter GLUT4, assembly of the Golgi apparatus. In addition to GLUT4, UBXN9 also controls vesicle translocation by interacting with insulin-regulated aminopeptidase (IRAP), a transmembrane aminopeptidase. UBXN9 and its budding yeast ortholog, Ubx4p, are multifunctional proteins that share some, but not all functions. Yeast Ubx4p is important for endoplasmic reticulum-associated protein degradation (ERAD) but UBXN9 appears not to share this function.


Pssm-ID: 340535  Cd Length: 74  Bit Score: 88.78  E-value: 1.26e-21
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1386876278 387 VALRVLFPDRYILQGFFRPSETV---------------------IAPPKMVLDDHTLTLFQANLFPAALVHFG 438
Cdd:cd16118     1 AVIRVQFPDRLVLQAFFRPLETVralydfvkshladpdlpfylyTTPPKRVLKDKNKTLYQAGLVPAALVYFG 73
Ubiquitin_like_fold cd00196
Beta-grasp ubiquitin-like fold; Ubiquitin is a protein modifier that is involved in various ...
 12-79 3.23e-15

Beta-grasp ubiquitin-like fold; Ubiquitin is a protein modifier that is involved in various cellular processes including transcriptional regulation, cell cycle control, and DNA repair in eukaryotes. The ubiquitination process comprises a cascade of E1, E2 and E3 enzymes that results in a covalent bond between the C-terminus of ubiquitin and the epsilon-amino group of a substrate lysine. Ubiquitin-like proteins have similar ubiquitin beta-grasp fold and attach to other proteins in a ubiquitin-like manner but with biochemically distinct roles. Ubiquitin and ubiquitin-like proteins conjugate and deconjugate via ligases and peptidases to covalently modify target polypeptides. Some other ubiquitin-like domains have adaptor roles in ubiquitin-signaling by mediating protein-protein interaction. In addition to Ubiquitin-like (Ubl) domain, Ras-associating (RA) domain, F0/F1 sub-domain of FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, TGS (ThrRS, GTPase and SpoT) domain, Ras-binding domain (RBD), Ubiquitin regulatory domain X (UBX), Dublecortin-like domain, and RING finger- and WD40-associated ubiquitin-like (RAWUL) domain have beta-grasp ubiquitin-like folds, and are included in this superfamily.


Pssm-ID: 340450  Cd Length: 68  Bit Score: 70.43  E-value: 3.23e-15
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1386876278  12 VSVLAPNGRRHTVKVTPSTVLLQVLEDTCRRQDFNPSEYDLKFQRTVLDLSLQWRFANLPNNAKLEMV 79
Cdd:cd00196     1 VKVETPSLKKIVVAVPPSTTLRQVLEKVAKRIGLPPDVIRLLFNGQVLDDLMTAKQVGLEPGEELHFV 68
UBX_UBXN6 cd16119
Ubiquitin regulatory domain X (UBX) found in UBX domain protein 6 (UBXN6) and similar proteins; ...
 389-437 7.10e-07

Ubiquitin regulatory domain X (UBX) found in UBX domain protein 6 (UBXN6) and similar proteins; UBXN6, also termed UBX domain-containing protein 1 (UBXD1), and UBXDC2, belongs to the UBXD family of proteins that contains the ubiquitin regulatory domain X (UBX) with a beta-grasp ubiquitin-like fold, but without the C-terminal double glycine motif. UBX domain is typically located at the carboxyl terminus of proteins, and participates broadly in the regulation of protein degradation. UBXN6 acts as a cofactor of p97 (also known as VCP or Cdc48), which is a homohexameric AAA ATPase (ATPase associated with a variety of activities) involved in a variety of functions ranging from cell-cycle regulation to membrane fusion and protein degradation. Unlike other p97 cofactors that binds the N-domain of p97 through their UBX domain, UBXN6 binds p97 in two regions, at the p97 C terminus via a PUB domain and at the p97 N-domain with a short linear interaction motif termed VIM. Its UBX domain is not functional for the binding of p97. The UBXN6-p97 complex regulates the endolysosomal sorting of ubiquitylated plasma membrane protein caveolin-1 (CAV1), as well as the trafficking of ERGIC-53-containing vesicles by controlling the interaction of transport factors with the cytoplasmic tail of ERGIC-53. In addition, UBXN6 is a regulatory component of endoplasmic reticulum-associated degradation (ERAD) that may modulate the adaptor binding to p97.


Pssm-ID: 340536  Cd Length: 73  Bit Score: 46.79  E-value: 7.10e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1386876278 389 LRVLFPDRYILQGFFRPSETVIA--------------------PPKMVLDDHTLTLFQANLFPAALVHF 437
Cdd:cd16119     4 IRVRFPDGVILQGTFYAREKLSAvrefvrealandwlpfelvtPGGQKLTDEDATLAELGLVPAALLNF 72
UBX cd01767
Ubiquitin regulatory domain X (UBX) structurally similar to a beta-grasp ubiquitin-like fold; ...
 93-166 3.42e-03

Ubiquitin regulatory domain X (UBX) structurally similar to a beta-grasp ubiquitin-like fold; The UBXD family of proteins contains the ubiquitin regulatory domain X (UBX) with a beta-grasp ubiquitin-like fold, but without the C-terminal double glycine motif. UBX domain is typically located at the carboxyl terminus of proteins, and participates broadly in the regulation of protein degradation. Members in this family function as cofactors of p97 (also known as VCP or Cdc48), which is a homohexameric AAA ATPase (ATPase associated with a variety of activities) involved in a variety of functions ranging from cell-cycle regulation to membrane fusion and protein degradation. Based on domain composition, UBXD proteins can be divided into two main groups, with and without ubiquitin-associated (UBA) domain.


Pssm-ID: 340466 [Multi-domain]  Cd Length: 74  Bit Score: 36.47  E-value: 3.42e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1386876278  93 RIAFQLDDGSRLQDAFCSRQTLWELLSHFAQTRErlqqlGEKTP---VCVYMRNEVTGraALQNTTLQSLGLTGGSA 166
Cdd:cd01767     1 RIQIRLPDGSRIQRRFSKSDTLQDLYDFVESNLG-----DSPSSfslVTSFPRRVLTD--EDSDKTLEELGLTPNAV 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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