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Conserved domains on  [gi|209862889|ref|NP_001129516|]
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transmembrane and ubiquitin-like domain-containing protein 1 [Homo sapiens]

Protein Classification

Ubl_TMUB1 domain-containing protein( domain architecture ID 13019431)

Ubl_TMUB1 domain-containing protein

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Ubl_TMUB1 cd17131
ubiquitin-like (Ubl) domain found in transmembrane and ubiquitin-like domain-containing ...
102-172 4.97e-47

ubiquitin-like (Ubl) domain found in transmembrane and ubiquitin-like domain-containing protein 1 (TMUB1); TMUB1, also termed dendritic cell-derived ubiquitin-like protein (DULP), or hepatocyte odd protein shuttling protein, or ubiquitin-like protein SB144, or HOPS, is highly expressed in the nervous system. It is involved in the termination of liver regeneration and plays a negative role in interleukin-6-induced hepatocyte proliferation. The overexpression of Tmub1 has been shown to play a role in the inhibition of cell proliferation. TMUB1 has also been implicated in the regulation of locomotor activity and wakefulness in mice, perhaps acting through its interaction with CAMLG. It also facilitates the recycling of AMPA receptors into synaptic membrane in cultured primary neurons. TMUB1 contains transmembrane domains and a ubiquitin-like (Ubl) domain with a beta-grasp Ubl fold.


:

Pssm-ID: 340651  Cd Length: 71  Bit Score: 150.36  E-value: 4.97e-47
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 209862889 102 PLVLRLKFLNDSEQVARAWPHDTIGSLKRTQFPGREQQVRLIYQGQLLGDDTQTLGSLHLPPNCVLHCHVS 172
Cdd:cd17131    1 PIVLRLKFLNDTERLARVKPEDTIGSLKRTYFPGQEHQVRLIYQGQLLGDDSQTLASLHLTDNCVLHCHIS 71
 
Name Accession Description Interval E-value
Ubl_TMUB1 cd17131
ubiquitin-like (Ubl) domain found in transmembrane and ubiquitin-like domain-containing ...
102-172 4.97e-47

ubiquitin-like (Ubl) domain found in transmembrane and ubiquitin-like domain-containing protein 1 (TMUB1); TMUB1, also termed dendritic cell-derived ubiquitin-like protein (DULP), or hepatocyte odd protein shuttling protein, or ubiquitin-like protein SB144, or HOPS, is highly expressed in the nervous system. It is involved in the termination of liver regeneration and plays a negative role in interleukin-6-induced hepatocyte proliferation. The overexpression of Tmub1 has been shown to play a role in the inhibition of cell proliferation. TMUB1 has also been implicated in the regulation of locomotor activity and wakefulness in mice, perhaps acting through its interaction with CAMLG. It also facilitates the recycling of AMPA receptors into synaptic membrane in cultured primary neurons. TMUB1 contains transmembrane domains and a ubiquitin-like (Ubl) domain with a beta-grasp Ubl fold.


Pssm-ID: 340651  Cd Length: 71  Bit Score: 150.36  E-value: 4.97e-47
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 209862889 102 PLVLRLKFLNDSEQVARAWPHDTIGSLKRTQFPGREQQVRLIYQGQLLGDDTQTLGSLHLPPNCVLHCHVS 172
Cdd:cd17131    1 PIVLRLKFLNDTERLARVKPEDTIGSLKRTYFPGQEHQVRLIYQGQLLGDDSQTLASLHLTDNCVLHCHIS 71
ubiquitin pfam00240
Ubiquitin family; This family contains a number of ubiquitin-like proteins: SUMO (smt3 homolog) ...
105-174 1.63e-08

Ubiquitin family; This family contains a number of ubiquitin-like proteins: SUMO (smt3 homolog), Nedd8, Elongin B, Rub1, and Parkin. A number of them are thought to carry a distinctive five-residue motif termed the proteasome-interacting motif (PIM), which may have a biologically significant role in protein delivery to proteasomes and recruitment of proteasomes to transcription sites.


Pssm-ID: 459726 [Multi-domain]  Cd Length: 72  Bit Score: 50.25  E-value: 1.63e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 209862889  105 LRLKFLNDSEQVARAWPHDTIGSLK-----RTQFPGREQqvRLIYQGQLLGDDtQTLGSLHLPPNCVLHCHVSTR 174
Cdd:pfam00240   1 ITVKTLDGKKITLEVDPTDTVLELKekiaeKEGVPPEQQ--RLIYSGKVLEDD-QTLGEYGIEDGSTIHLVLRQR 72
UBQ smart00213
Ubiquitin homologues; Ubiquitin-mediated proteolysis is involved in the regulated turnover of ...
105-172 4.24e-07

Ubiquitin homologues; Ubiquitin-mediated proteolysis is involved in the regulated turnover of proteins required for controlling cell cycle progression


Pssm-ID: 214563 [Multi-domain]  Cd Length: 72  Bit Score: 46.10  E-value: 4.24e-07
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 209862889   105 LRLKFLNDSEQVARAWPHDTIGSLK-----RTQFPgREQQvRLIYQGQLLGDDtQTLGSLHLPPNCVLHCHVS 172
Cdd:smart00213   3 LTVKTLDGKTITLEVKPSDTVSELKekiaeLTGIP-PEQQ-RLIYKGKVLEDD-RTLADYGIQDGSTIHLVLR 72
 
Name Accession Description Interval E-value
Ubl_TMUB1 cd17131
ubiquitin-like (Ubl) domain found in transmembrane and ubiquitin-like domain-containing ...
102-172 4.97e-47

ubiquitin-like (Ubl) domain found in transmembrane and ubiquitin-like domain-containing protein 1 (TMUB1); TMUB1, also termed dendritic cell-derived ubiquitin-like protein (DULP), or hepatocyte odd protein shuttling protein, or ubiquitin-like protein SB144, or HOPS, is highly expressed in the nervous system. It is involved in the termination of liver regeneration and plays a negative role in interleukin-6-induced hepatocyte proliferation. The overexpression of Tmub1 has been shown to play a role in the inhibition of cell proliferation. TMUB1 has also been implicated in the regulation of locomotor activity and wakefulness in mice, perhaps acting through its interaction with CAMLG. It also facilitates the recycling of AMPA receptors into synaptic membrane in cultured primary neurons. TMUB1 contains transmembrane domains and a ubiquitin-like (Ubl) domain with a beta-grasp Ubl fold.


Pssm-ID: 340651  Cd Length: 71  Bit Score: 150.36  E-value: 4.97e-47
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 209862889 102 PLVLRLKFLNDSEQVARAWPHDTIGSLKRTQFPGREQQVRLIYQGQLLGDDTQTLGSLHLPPNCVLHCHVS 172
Cdd:cd17131    1 PIVLRLKFLNDTERLARVKPEDTIGSLKRTYFPGQEHQVRLIYQGQLLGDDSQTLASLHLTDNCVLHCHIS 71
Ubl_TMUB1_like cd17057
ubiquitin-like (Ubl) domain found in transmembrane and ubiquitin-like domain-containing ...
103-172 1.05e-32

ubiquitin-like (Ubl) domain found in transmembrane and ubiquitin-like domain-containing proteins TMUB1, TMUB2, and similar proteins; TMUB1, also termed dendritic cell-derived ubiquitin-like protein (DULP), or hepatocyte odd protein shuttling protein, or ubiquitin-like protein SB144, or HOPS, is highly expressed in the nervous system. It is involved in the termination of liver regeneration and plays a negative role in interleukin-6-induced hepatocyte proliferation. The overexpression of Tmub1 has been shown to play a role in the inhibition of cell proliferation. TMUB1 has been implicated in the regulation of locomotor activity and wakefulness in mice, perhaps acting through its interaction with CAMLG. It also facilitates the recycling of AMPA receptors into synaptic membrane in cultured primary neurons. TMUB1 contains transmembrane domains and a ubiquitin-like (Ubl) domain with a beta-grasp Ubl fold. TMUB2 is an uncharacterized transmembrane domain and Ubl domain-containing protein that shows high sequence similarity to TMUB1.


Pssm-ID: 340577  Cd Length: 74  Bit Score: 113.86  E-value: 1.05e-32
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 209862889 103 LVLRLKFLNDSEQVARAWPHDTIGSLKRTQFPG---REQQVRLIYQGQLLGDDTQTLGSLHLPPNCVLHCHVS 172
Cdd:cd17057    2 ITIRLKFLNETERVVYARPEDTVGDFKRRHFPDelaQGKRVRLIYQGQLLRDDSRTLSSYGIQDGSVIHCHIS 74
Ubl_TMUB2 cd17132
ubiquitin-like (Ubl) domain found in transmembrane and ubiquitin-like domain-containing ...
105-172 3.01e-31

ubiquitin-like (Ubl) domain found in transmembrane and ubiquitin-like domain-containing protein 2 (TMUB2); TMUB2 is composed of an uncharacterized transmembrane domain and a ubiquitin-like (Ubl) domain-containing protein that shows high sequence similarity to TMUB1; the latter is highly expressed in the nervous system and is involved in the termination of liver regeneration.


Pssm-ID: 340652  Cd Length: 71  Bit Score: 109.92  E-value: 3.01e-31
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 209862889 105 LRLKFLNDSEQVARAWPHDTIGSLKRTQFPGREQQVRLIYQGQLLGDDTQTLGSLHLPPNCVLHCHVS 172
Cdd:cd17132    4 VRLKFLNDTEEVAVVRPEDTIGFLKSKYFPGQEQQMKLIYQGQLLQDPARTLRSLNITDNCVIHCHRS 71
ubiquitin pfam00240
Ubiquitin family; This family contains a number of ubiquitin-like proteins: SUMO (smt3 homolog) ...
105-174 1.63e-08

Ubiquitin family; This family contains a number of ubiquitin-like proteins: SUMO (smt3 homolog), Nedd8, Elongin B, Rub1, and Parkin. A number of them are thought to carry a distinctive five-residue motif termed the proteasome-interacting motif (PIM), which may have a biologically significant role in protein delivery to proteasomes and recruitment of proteasomes to transcription sites.


Pssm-ID: 459726 [Multi-domain]  Cd Length: 72  Bit Score: 50.25  E-value: 1.63e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 209862889  105 LRLKFLNDSEQVARAWPHDTIGSLK-----RTQFPGREQqvRLIYQGQLLGDDtQTLGSLHLPPNCVLHCHVSTR 174
Cdd:pfam00240   1 ITVKTLDGKKITLEVDPTDTVLELKekiaeKEGVPPEQQ--RLIYSGKVLEDD-QTLGEYGIEDGSTIHLVLRQR 72
UBQ smart00213
Ubiquitin homologues; Ubiquitin-mediated proteolysis is involved in the regulated turnover of ...
105-172 4.24e-07

Ubiquitin homologues; Ubiquitin-mediated proteolysis is involved in the regulated turnover of proteins required for controlling cell cycle progression


Pssm-ID: 214563 [Multi-domain]  Cd Length: 72  Bit Score: 46.10  E-value: 4.24e-07
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 209862889   105 LRLKFLNDSEQVARAWPHDTIGSLK-----RTQFPgREQQvRLIYQGQLLGDDtQTLGSLHLPPNCVLHCHVS 172
Cdd:smart00213   3 LTVKTLDGKTITLEVKPSDTVSELKekiaeLTGIP-PEQQ-RLIYKGKVLEDD-RTLADYGIQDGSTIHLVLR 72
Ubl_ubiquitin_like cd17039
ubiquitin-like (Ubl) domain found in ubiquitin and ubiquitin-like Ubl proteins; Ubiquitin-like ...
121-170 2.76e-06

ubiquitin-like (Ubl) domain found in ubiquitin and ubiquitin-like Ubl proteins; Ubiquitin-like (Ubl) proteins have a similar ubiquitin (Ub) beta-grasp fold and attach to other proteins in a Ubl manner but with biochemically distinct roles. Ub and Ubl proteins conjugate and deconjugate via ligases and peptidases to covalently modify target polypeptides. Some Ubl domains have adaptor roles in Ub-signaling by mediating protein-protein interaction. Prokaryotic sulfur carrier proteins are Ub-related proteins that can be activated in an ATP-dependent manner. Polyubiquitination signals for a diverse set of cellular events via different isopeptide linkages formed between the C terminus of one ubiquitin (Ub) and the epsilon-amine of K6, K11, K27, K29, K33, K48, or K63 of a second Ub. One of these seven lysine residues (K27, Ub numbering) is conserved in this Ubl_ubiquitin_like family. K27-linked Ub chains are versatile and can be recognized by several downstream receptor proteins. K27 has roles beyond chain linkage, such as in Ubl NEDD8 (which contains many of the same lysines (K6, K11, K27, K33, K48) as Ub) where K27 has a role (other than conjugation) in the mechanism of protein neddylation.


Pssm-ID: 340559 [Multi-domain]  Cd Length: 68  Bit Score: 43.74  E-value: 2.76e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 209862889 121 PHDTIGSLK-----RTQFPGREQqvRLIYQGQLLgDDTQTLGSLHLPPNCVLHCH 170
Cdd:cd17039   17 PDDTVADLKekieeKTGIPVEQQ--RLIYNGKEL-KDDKTLSDYGIKDGSTIHLV 68
Ubl_USP48 cd01795
ubiquitin-like (Ubl) domain found in ubiquitin-specific-processing protease 48 (USP48) and ...
122-173 1.82e-04

ubiquitin-like (Ubl) domain found in ubiquitin-specific-processing protease 48 (USP48) and similar proteins; USP48, also termed USP31, or deubiquitinating enzyme 48, or ubiquitin thioesterase 48, or ubiquitin carboxyl-terminal hydrolase 48, belongs to the ubiquitin specific protease (USP) family that is one of at least seven deubiquitylating enzyme (DUB) families capable of deconjugating ubiquitin (Ub)and ubiquitin-like (Ubl) adducts. While the USP proteins have a conserved catalytic core domain, USP48 differs in its domain architecture. It contains an N-terminal USP domain, three DUSP (domain present in ubiquitin-specific protease) domains, and a C-terminal Ubl domain with a beta-grasp Ubl fold, a common structure involved in protein-protein interactions. USP48 is a deubiquitinating enzyme that interacts with TNF receptor-associated factor 2 (TRAF2) and has been implicated in activation of nuclear factor-kappaB (NF-kappaB). Moreover, as a nuclear deubiquitinase regulated by casein kinase 2 (CK2), USP48 controls the ubiquitin/proteasome-system (UPS)-dependent turnover of activated NF-kappaB/RelA in the nucleus together with the COP9 signalosome, suggesting a role of USP48 in a timely control of immune responses.


Pssm-ID: 340493 [Multi-domain]  Cd Length: 99  Bit Score: 39.58  E-value: 1.82e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 209862889 122 HDTIGSLKRT---QF---PgrEQQvRLIYQGQLLGDDTQTLGSLHLPPNCVLHCHVST 173
Cdd:cd01795   15 TTTLKELKLQimeKFsvaP--FDQ-HLYFNGRELTDDSATLADLGILPGDVLYLKVDE 69
Ubiquitin_like_fold cd00196
Beta-grasp ubiquitin-like fold; Ubiquitin is a protein modifier that is involved in various ...
105-169 1.97e-04

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: 38.84  E-value: 1.97e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 209862889 105 LRLKFLNDSEQVARAWPHDTIGSLK----RTQFPgREQQVRLIYQGQLLgDDTQTLGSLHLPPNCVLHC 169
Cdd:cd00196    1 VKVETPSLKKIVVAVPPSTTLRQVLekvaKRIGL-PPDVIRLLFNGQVL-DDLMTAKQVGLEPGEELHF 67
Rad60-SLD_2 pfam13881
Ubiquitin-2 like Rad60 SUMO-like;
114-174 3.06e-03

Ubiquitin-2 like Rad60 SUMO-like;


Pssm-ID: 372780  Cd Length: 111  Bit Score: 36.52  E-value: 3.06e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 209862889  114 EQVARAWPHDtigslkRTQFPGREQQVRLIYQGQLLgDDTQTLGSLHLP----PNCVLHCHVSTR 174
Cdd:pfam13881  31 EKVIAQWPKD------KENGPKTVNDVKLINAGKIL-ENNKTLGECRLPvgetPGGVTTMHVVVR 88
 
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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