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Conserved domains on  [gi|1952076956|ref|NP_001376485|]
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UBX domain-containing protein 11 isoform 2 [Homo sapiens]

Protein Classification

UBX domain-containing protein 11( domain architecture ID 13742898)

UBX domain-containing protein 11 (UBXN11) may function 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; also contains a SEP domain

Gene Symbol:  UBXN11
PubMed:  11243799

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
UBX_UBXN11 cd17077
Ubiquitin regulatory domain X (UBX) found in UBX domain protein 11 (UBXN11) and similar ...
 395-464 5.42e-30

Ubiquitin regulatory domain X (UBX) found in UBX domain protein 11 (UBXN11) and similar proteins; UBXN11, also termed colorectal tumor-associated antigen COA-1, or socius, or UBX domain-containing protein 5 (UBXD5), 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. UBXN11 may function 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. UBXN11 also acts as a novel interacting partner of Rnd proteins (Rnd1, Rnd2, and Rnd3/RhoE), new members of Rho family of small GTPases. It directly binds to Rnd GTPases through its C-terminal region, and further participates in disassembly of actin stress fibers. UBXN11 also binds directly to Galpha12 and Galpha13 through its N-terminal region. As a novel activator of the Galpha12 family, UBXN11 promotes the Galpha12-induced RhoA activation.


:

Pssm-ID: 340597  Cd Length: 76  Bit Score: 111.93  E-value: 5.42e-30
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952076956 395 PLSMLRIKSENGEQAFLLMMQPDNTIGDVRALLAQARVMDASAFEIFSTFPPTLYQDDTLTLQAAGLVPK 464
Cdd:cd17077     1 DVTTLRIKSENGEQTYILKMRFSDTIGDLRRYLDKHRSKDAASYEIVTTFPNKVYDDDSATLEELGLVPN 70
SEP pfam08059
SEP domain; The SEP domain is named after Saccharomyces cerevisiae Shp1, Drosophila ...
 235-306 5.79e-21

SEP domain; The SEP domain is named after Saccharomyces cerevisiae Shp1, Drosophila melanogaster eyes closed gene (eyc), and vertebrate p47. In p47, the SEP domain has been shown to bind to and inhibit the cysteine protease cathepsin L. Most SEP domains are succeeded closely by a UBX domain.


:

Pssm-ID: 462348  Cd Length: 75  Bit Score: 86.76  E-value: 5.79e-21
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1952076956 235 LKLYRNGIMMFDGPFQPFYDPSTQRCLRDILDGFFPSELQRLYPN-GVPFKVSDLRNQVYLED--GLDPFPGEGR 306
Cdd:pfam08059   1 LTFWRNGFSVDDGPLRRYDDPANAEFLEAINRGEAPLELLNVAPGqGVDVNLEDRRDEDYVPPkkKYKPFSGSGR 75
bchH super family cl36246
magnesium chelatase subunit H; Provisional
 119-256 2.83e-03

magnesium chelatase subunit H; Provisional


The actual alignment was detected with superfamily member PRK13405:

Pssm-ID: 237377 [Multi-domain]  Cd Length: 1209  Bit Score: 40.42  E-value: 2.83e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952076956  119 AEATLQRQEELETMCVQLQRQVREMERFLSDYGLQWVGEPMDQEdsesktvsehgER-DWMTAKkfwkpGDSLAPPEVDF 197
Cdd:PRK13405   712 APAEPAWEEEAGARIAKLWAALLELEYTLIPHGLHVVGEPPSEE-----------ERvDLLLAM-----AEASHGKRAEI 775

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952076956  198 DRLLASLQDLSELVVEGDTQ-VTPVPGGARLRTLEPIPLKlyRNgIMMFDgpfqPFYDPS 256
Cdd:PRK13405   776 DRLLAEDHELPALLRALDGRfIRPVPGGDLLRTPAILPTG--RN-LHGFD----PFRIPS 828
 
Name Accession Description Interval E-value
UBX_UBXN11 cd17077
Ubiquitin regulatory domain X (UBX) found in UBX domain protein 11 (UBXN11) and similar ...
 395-464 5.42e-30

Ubiquitin regulatory domain X (UBX) found in UBX domain protein 11 (UBXN11) and similar proteins; UBXN11, also termed colorectal tumor-associated antigen COA-1, or socius, or UBX domain-containing protein 5 (UBXD5), 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. UBXN11 may function 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. UBXN11 also acts as a novel interacting partner of Rnd proteins (Rnd1, Rnd2, and Rnd3/RhoE), new members of Rho family of small GTPases. It directly binds to Rnd GTPases through its C-terminal region, and further participates in disassembly of actin stress fibers. UBXN11 also binds directly to Galpha12 and Galpha13 through its N-terminal region. As a novel activator of the Galpha12 family, UBXN11 promotes the Galpha12-induced RhoA activation.


Pssm-ID: 340597  Cd Length: 76  Bit Score: 111.93  E-value: 5.42e-30
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952076956 395 PLSMLRIKSENGEQAFLLMMQPDNTIGDVRALLAQARVMDASAFEIFSTFPPTLYQDDTLTLQAAGLVPK 464
Cdd:cd17077     1 DVTTLRIKSENGEQTYILKMRFSDTIGDLRRYLDKHRSKDAASYEIVTTFPNKVYDDDSATLEELGLVPN 70
SEP pfam08059
SEP domain; The SEP domain is named after Saccharomyces cerevisiae Shp1, Drosophila ...
 235-306 5.79e-21

SEP domain; The SEP domain is named after Saccharomyces cerevisiae Shp1, Drosophila melanogaster eyes closed gene (eyc), and vertebrate p47. In p47, the SEP domain has been shown to bind to and inhibit the cysteine protease cathepsin L. Most SEP domains are succeeded closely by a UBX domain.


Pssm-ID: 462348  Cd Length: 75  Bit Score: 86.76  E-value: 5.79e-21
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1952076956 235 LKLYRNGIMMFDGPFQPFYDPSTQRCLRDILDGFFPSELQRLYPN-GVPFKVSDLRNQVYLED--GLDPFPGEGR 306
Cdd:pfam08059   1 LTFWRNGFSVDDGPLRRYDDPANAEFLEAINRGEAPLELLNVAPGqGVDVNLEDRRDEDYVPPkkKYKPFSGSGR 75
SEP smart00553
Domain present in Saccharomyces cerevisiae Shp1, Drosophila melanogaster eyes closed gene (eyc) ...
 235-309 3.63e-06

Domain present in Saccharomyces cerevisiae Shp1, Drosophila melanogaster eyes closed gene (eyc), and vertebrate p47;


Pssm-ID: 197786  Cd Length: 93  Bit Score: 45.47  E-value: 3.63e-06
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1952076956  235 LKLYRNGIMMFDGPFQPFYDPSTQRCLRDILDGFFPSELQRLYPNG-VPFKVSDLRNQVY--LEDGLDPFPGEGRVVG 309
Cdd:smart00553   7 LTFWSNGFSVDDGPLRTYDDPENAEFLESIRRGEAPLELLRVAKGQpVNVDVEDHRDEDYvaPPGAFKPFSGSGQKLG 84
bchH PRK13405
magnesium chelatase subunit H; Provisional
 119-256 2.83e-03

magnesium chelatase subunit H; Provisional


Pssm-ID: 237377 [Multi-domain]  Cd Length: 1209  Bit Score: 40.42  E-value: 2.83e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952076956  119 AEATLQRQEELETMCVQLQRQVREMERFLSDYGLQWVGEPMDQEdsesktvsehgER-DWMTAKkfwkpGDSLAPPEVDF 197
Cdd:PRK13405   712 APAEPAWEEEAGARIAKLWAALLELEYTLIPHGLHVVGEPPSEE-----------ERvDLLLAM-----AEASHGKRAEI 775

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952076956  198 DRLLASLQDLSELVVEGDTQ-VTPVPGGARLRTLEPIPLKlyRNgIMMFDgpfqPFYDPS 256
Cdd:PRK13405   776 DRLLAEDHELPALLRALDGRfIRPVPGGDLLRTPAILPTG--RN-LHGFD----PFRIPS 828
 
Name Accession Description Interval E-value
UBX_UBXN11 cd17077
Ubiquitin regulatory domain X (UBX) found in UBX domain protein 11 (UBXN11) and similar ...
 395-464 5.42e-30

Ubiquitin regulatory domain X (UBX) found in UBX domain protein 11 (UBXN11) and similar proteins; UBXN11, also termed colorectal tumor-associated antigen COA-1, or socius, or UBX domain-containing protein 5 (UBXD5), 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. UBXN11 may function 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. UBXN11 also acts as a novel interacting partner of Rnd proteins (Rnd1, Rnd2, and Rnd3/RhoE), new members of Rho family of small GTPases. It directly binds to Rnd GTPases through its C-terminal region, and further participates in disassembly of actin stress fibers. UBXN11 also binds directly to Galpha12 and Galpha13 through its N-terminal region. As a novel activator of the Galpha12 family, UBXN11 promotes the Galpha12-induced RhoA activation.


Pssm-ID: 340597  Cd Length: 76  Bit Score: 111.93  E-value: 5.42e-30
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952076956 395 PLSMLRIKSENGEQAFLLMMQPDNTIGDVRALLAQARVMDASAFEIFSTFPPTLYQDDTLTLQAAGLVPK 464
Cdd:cd17077     1 DVTTLRIKSENGEQTYILKMRFSDTIGDLRRYLDKHRSKDAASYEIVTTFPNKVYDDDSATLEELGLVPN 70
SEP pfam08059
SEP domain; The SEP domain is named after Saccharomyces cerevisiae Shp1, Drosophila ...
 235-306 5.79e-21

SEP domain; The SEP domain is named after Saccharomyces cerevisiae Shp1, Drosophila melanogaster eyes closed gene (eyc), and vertebrate p47. In p47, the SEP domain has been shown to bind to and inhibit the cysteine protease cathepsin L. Most SEP domains are succeeded closely by a UBX domain.


Pssm-ID: 462348  Cd Length: 75  Bit Score: 86.76  E-value: 5.79e-21
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1952076956 235 LKLYRNGIMMFDGPFQPFYDPSTQRCLRDILDGFFPSELQRLYPN-GVPFKVSDLRNQVYLED--GLDPFPGEGR 306
Cdd:pfam08059   1 LTFWRNGFSVDDGPLRRYDDPANAEFLEAINRGEAPLELLNVAPGqGVDVNLEDRRDEDYVPPkkKYKPFSGSGR 75
UBX cd01767
Ubiquitin regulatory domain X (UBX) structurally similar to a beta-grasp ubiquitin-like fold; ...
 398-464 5.95e-08

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: 49.95  E-value: 5.95e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1952076956 398 MLRIKSENGEQAFLLMMqPDNTIGDVRALLAQARVMDASAFEIFSTFPPTLY--QDDTLTLQAAGLVPK 464
Cdd:cd01767     1 RIQIRLPDGSRIQRRFS-KSDTLQDLYDFVESNLGDSPSSFSLVTSFPRRVLtdEDSDKTLEELGLTPN 68
UBX_UBXN2 cd01770
Ubiquitin regulatory domain X (UBX) found in UBX domain-containing proteins UBXN2A, UBXN2B, ...
 417-461 2.39e-06

Ubiquitin regulatory domain X (UBX) found in UBX domain-containing proteins UBXN2A, UBXN2B, NSFL1C/UBXN2C, and similar proteins; This family includes UBX domain-containing proteins UBXN2A, UBXN2B, and NSFL1C/UBXN2C, which contain a SEP (Saccharomyces cerevisiae Shp1, Drosophila melanogaster eyes closed gene (eyc), and vertebrate p47) domain, and a ubiquitin regulatory domain X (UBX) with a beta-grasp ubiquitin-like fold at the C-terminus. UBX domain participates broadly in the regulation of protein degradation. UBXN2A, UBXN2B, and UBXN2C function as the adaptor proteins 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.


Pssm-ID: 340468  Cd Length: 71  Bit Score: 45.25  E-value: 2.39e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 1952076956 417 DNTIGDVRALLAQARVMDASAFEIFSTFPPTLYQDDTLTLQAAGL 461
Cdd:cd01770    19 THTVGDIRQFIDSARPGYSRPFVLMTGFPPKELTDESQTLEEAGL 63
SEP smart00553
Domain present in Saccharomyces cerevisiae Shp1, Drosophila melanogaster eyes closed gene (eyc) ...
 235-309 3.63e-06

Domain present in Saccharomyces cerevisiae Shp1, Drosophila melanogaster eyes closed gene (eyc), and vertebrate p47;


Pssm-ID: 197786  Cd Length: 93  Bit Score: 45.47  E-value: 3.63e-06
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1952076956  235 LKLYRNGIMMFDGPFQPFYDPSTQRCLRDILDGFFPSELQRLYPNG-VPFKVSDLRNQVY--LEDGLDPFPGEGRVVG 309
Cdd:smart00553   7 LTFWSNGFSVDDGPLRTYDDPENAEFLESIRRGEAPLELLRVAKGQpVNVDVEDHRDEDYvaPPGAFKPFSGSGQKLG 84
bchH PRK13405
magnesium chelatase subunit H; Provisional
 119-256 2.83e-03

magnesium chelatase subunit H; Provisional


Pssm-ID: 237377 [Multi-domain]  Cd Length: 1209  Bit Score: 40.42  E-value: 2.83e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952076956  119 AEATLQRQEELETMCVQLQRQVREMERFLSDYGLQWVGEPMDQEdsesktvsehgER-DWMTAKkfwkpGDSLAPPEVDF 197
Cdd:PRK13405   712 APAEPAWEEEAGARIAKLWAALLELEYTLIPHGLHVVGEPPSEE-----------ERvDLLLAM-----AEASHGKRAEI 775

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1952076956  198 DRLLASLQDLSELVVEGDTQ-VTPVPGGARLRTLEPIPLKlyRNgIMMFDgpfqPFYDPS 256
Cdd:PRK13405   776 DRLLAEDHELPALLRALDGRfIRPVPGGDLLRTPAILPTG--RN-LHGFD----PFRIPS 828
fabG PRK05786
3-ketoacyl-(acyl-carrier-protein) reductase; Provisional
 174-228 4.76e-03

3-ketoacyl-(acyl-carrier-protein) reductase; Provisional


Pssm-ID: 235608 [Multi-domain]  Cd Length: 238  Bit Score: 38.97  E-value: 4.76e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1952076956 174 ERDWmtaKKFWKPGDSLAPPEvDFDRLLASL-QDLSELVvegDTQVTPVPGGARLR 228
Cdd:PRK05786  190 ERNW---KKLRKLGDDMAPPE-DFAKVIIWLlTDEADWV---DGVVIPVDGGARLK 238
UBX2_UBXN9 cd16118
Ubiquitin regulatory domain X (UBX) 2 found in UBX domain protein 9 (UBXN9, UBXD9, or ASPSCR1) ...
 408-463 9.04e-03

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: 35.24  E-value: 9.04e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1952076956 408 QAFLLmmqPDNTIGDVRALLAQARVMDASAFEIFSTFPPTLYQDDTLTLQAAGLVP 463
Cdd:cd16118    14 QAFFR---PLETVRALYDFVKSHLADPDLPFYLYTTPPKRVLKDKNKTLYQAGLVP 66
 
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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