ubiquitin-like protein 5 [Homo sapiens]
Protein Classification
Ubl5/Hub1 family ubiquitin-like protein( domain architecture ID 10110356)
Ubl5/Hub1 family ubiquitin-like protein similar to Saccharomyces cerevisiae Hub1 that plays a role in splice-site usage and alternative splicing
List of domain hits
| Name | Accession | Description | Interval | E-value | ||
| Ubl_UBL5 | cd01791 | ubiquitin-like (Ubl) domain found in ubiquitin-like protein 5 (UBL5) and similar proteins; ... |
1-71 | 4.21e-49 | ||
ubiquitin-like (Ubl) domain found in ubiquitin-like protein 5 (UBL5) and similar proteins; UBL5, known as Hub1 in yeast, is an atypical ubiquitin-like (Ubl) post-translational modifier that contains a conserved Ubl domain with a beta-grasp Ubl fold. At the C-terminal end of its Ubl fold is a di-tyrosine motif followed by a single variable residue instead of the characteristic di-glycine found in all other Ubl modifiers, and thus UBL5 does not form covalent conjugates with cellular proteins. The yeast Hub1p binds non-covalently to the HIND element of spliceosomal protein Snu66p (Snu66p is termed SART1 in mammals) and modifies the spliceosome by this unconventional Ubl modifier. In higher eukaryotes, UBL5/Hub1 plays a role in modulating pre-mRNA splicing. It also is required for signaling in the mitochondrial unfolded protein response, through interaction with the transcription factor DVE-1 and upregulation of chaperone genes in response to mitochondrial stress. Moreover, UBL5 functions as a factor that directly binds to and stabilizes FANCI, and promotes the functionality of the Fanconi anemia (FA) DNA repair pathway. : Pssm-ID: 340489 Cd Length: 71 Bit Score: 148.62 E-value: 4.21e-49
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| Name | Accession | Description | Interval | E-value | ||
| Ubl_UBL5 | cd01791 | ubiquitin-like (Ubl) domain found in ubiquitin-like protein 5 (UBL5) and similar proteins; ... |
1-71 | 4.21e-49 | ||
ubiquitin-like (Ubl) domain found in ubiquitin-like protein 5 (UBL5) and similar proteins; UBL5, known as Hub1 in yeast, is an atypical ubiquitin-like (Ubl) post-translational modifier that contains a conserved Ubl domain with a beta-grasp Ubl fold. At the C-terminal end of its Ubl fold is a di-tyrosine motif followed by a single variable residue instead of the characteristic di-glycine found in all other Ubl modifiers, and thus UBL5 does not form covalent conjugates with cellular proteins. The yeast Hub1p binds non-covalently to the HIND element of spliceosomal protein Snu66p (Snu66p is termed SART1 in mammals) and modifies the spliceosome by this unconventional Ubl modifier. In higher eukaryotes, UBL5/Hub1 plays a role in modulating pre-mRNA splicing. It also is required for signaling in the mitochondrial unfolded protein response, through interaction with the transcription factor DVE-1 and upregulation of chaperone genes in response to mitochondrial stress. Moreover, UBL5 functions as a factor that directly binds to and stabilizes FANCI, and promotes the functionality of the Fanconi anemia (FA) DNA repair pathway. Pssm-ID: 340489 Cd Length: 71 Bit Score: 148.62 E-value: 4.21e-49
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| ubiquitin | pfam00240 | Ubiquitin family; This family contains a number of ubiquitin-like proteins: SUMO (smt3 homolog) ... |
11-71 | 8.63e-05 | ||
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: 36.38 E-value: 8.63e-05
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| UBQ | smart00213 | Ubiquitin homologues; Ubiquitin-mediated proteolysis is involved in the regulated turnover of ... |
11-71 | 1.20e-03 | ||
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: 33.77 E-value: 1.20e-03
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| Name | Accession | Description | Interval | E-value | ||
| Ubl_UBL5 | cd01791 | ubiquitin-like (Ubl) domain found in ubiquitin-like protein 5 (UBL5) and similar proteins; ... |
1-71 | 4.21e-49 | ||
ubiquitin-like (Ubl) domain found in ubiquitin-like protein 5 (UBL5) and similar proteins; UBL5, known as Hub1 in yeast, is an atypical ubiquitin-like (Ubl) post-translational modifier that contains a conserved Ubl domain with a beta-grasp Ubl fold. At the C-terminal end of its Ubl fold is a di-tyrosine motif followed by a single variable residue instead of the characteristic di-glycine found in all other Ubl modifiers, and thus UBL5 does not form covalent conjugates with cellular proteins. The yeast Hub1p binds non-covalently to the HIND element of spliceosomal protein Snu66p (Snu66p is termed SART1 in mammals) and modifies the spliceosome by this unconventional Ubl modifier. In higher eukaryotes, UBL5/Hub1 plays a role in modulating pre-mRNA splicing. It also is required for signaling in the mitochondrial unfolded protein response, through interaction with the transcription factor DVE-1 and upregulation of chaperone genes in response to mitochondrial stress. Moreover, UBL5 functions as a factor that directly binds to and stabilizes FANCI, and promotes the functionality of the Fanconi anemia (FA) DNA repair pathway. Pssm-ID: 340489 Cd Length: 71 Bit Score: 148.62 E-value: 4.21e-49
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| Ubl_ubiquitin_like | cd17039 | ubiquitin-like (Ubl) domain found in ubiquitin and ubiquitin-like Ubl proteins; Ubiquitin-like ... |
4-71 | 5.28e-09 | ||
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: 47.21 E-value: 5.28e-09
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| ubiquitin | pfam00240 | Ubiquitin family; This family contains a number of ubiquitin-like proteins: SUMO (smt3 homolog) ... |
11-71 | 8.63e-05 | ||
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: 36.38 E-value: 8.63e-05
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| Ubl2_OASL | cd16103 | ubiquitin-like (Ubl) domain 2 found in 2'-5'-oligoadenylate synthase-like protein (OASL) and ... |
19-70 | 4.33e-04 | ||
ubiquitin-like (Ubl) domain 2 found in 2'-5'-oligoadenylate synthase-like protein (OASL) and similar proteins; OASL, also termed 2'-5'-OAS-related protein (2'-5'-OAS-RP), or 59 kDa 2'-5'-oligoadenylate synthase-like protein, or thyroid receptor-interacting protein 14, or TR-interacting protein 14 (TRIP-14), or p59 OASL (p59OASL), is an interferon (IFN)-induced antiviral protein that plays an important role in the IFNs-mediated antiviral signaling pathway. It inhibits respiratory syncytial virus replication and is targeted by the viral nonstructural protein 1 (NS1). It also displays antiviral activity against encephalomyocarditis virus (EMCV) and hepatitis C virus (HCV) via an alternative antiviral pathway independent of RNase L. Moreover, OASL does not have 2'-5'-OAS activity, but can bind double-stranded RNA (dsRNA) to enhance RIG-I signaling. OASL belongs to the 2'-5' oligoadenylate synthase (OAS) family. While each member of this family has a conserved N-terminal OAS catalytic domain, only OASL has two tandem C-terminal ubiquitin-like (Ubl) repeats, which are required for its antiviral activity. This family corresponds to the second Ubl domain. Pssm-ID: 340520 [Multi-domain] Cd Length: 72 Bit Score: 34.96 E-value: 4.33e-04
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| Ubl_SF3a120 | cd01800 | ubiquitin-like (Ubl) domain found in splicing factor 3A 120kDa subunit (SF3a120) and similar ... |
22-70 | 7.77e-04 | ||
ubiquitin-like (Ubl) domain found in splicing factor 3A 120kDa subunit (SF3a120) and similar proteins; Mammalian splicing factor SF3a consists of three subunits of 60, 66, and 120 kDa and functions early during pre-mRNA splicing by converting the U2 snRNP to its active form. The 120kDa subunit SF3a120, also termed splicing factor 3A subunit 1 (SF3A1), or spliceosome-associated protein 114 (SAP114), is the U2 snRNP-specific protein that is critical for spliceosome assembly and normal splicing events. During splicing, SF3a120, together with the U2 snRNP and other proteins, are recruited to the 3' splicing site to generate the splicing complex A after the recognition of the 3' splicing site. SF3a120 contains two N-terminal SWAP (suppressor-of-white-apricot) domains, referred to collectively as the SURP module, as well as a C-terminal ubiquitin-like (Ubl) domain with a beta-grasp Ubl fold, a common structure involved in protein-protein interactions. Pssm-ID: 340498 Cd Length: 84 Bit Score: 34.47 E-value: 7.77e-04
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| UBQ | smart00213 | Ubiquitin homologues; Ubiquitin-mediated proteolysis is involved in the regulated turnover of ... |
11-71 | 1.20e-03 | ||
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: 33.77 E-value: 1.20e-03
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| Ubl_Dsk2p_like | cd16106 | ubiquitin-like (Ubl) domain found in Saccharomyces cerevisiae proteasome interacting protein ... |
13-65 | 5.46e-03 | ||
ubiquitin-like (Ubl) domain found in Saccharomyces cerevisiae proteasome interacting protein Dsk2p and similar proteins; The family contains several fungal multiubiquitin receptors, including Saccharomyces cerevisiae Dsk2p and Schizosaccharomyces pombe Dph1p, both of which have been characterized as shuttle proteins transporting ubiquitinated substrates destined for degradation from the E3 ligase to the 26S proteasome. They interact with the proteasome through their N-terminal ubiquitin-like domain (Ubl) and with ubiquitin (Ub) through their C-terminal Ub-associated domain (UBA). S. cerevisiae Dsk2p is a nuclear-enriched protein that may involve in the ubiquitin-proteasome proteolytic pathway through interacting with K48-linked polyubiquitin and the proteasome. Moreover, it has been implicated in spindle pole duplication through assisting in Cdc31 assembly into the new spindle pole body (SPB). S. pombe Dph1p is an ubiquitin (Ub0 receptor working in concert with the class V myosin, Myo52, to target the degradation of the S. pombe CLIP-170 homolog, Tip1. It also can protect Ub chains against disassembly by deubiquitinating enzymes. Pssm-ID: 340523 [Multi-domain] Cd Length: 73 Bit Score: 31.84 E-value: 5.46e-03
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