Ubiquitin B

mammalian protein found in Homo sapiens

Protein protein Q21112968

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Ubiquitin B

Summary

Ubiquitin B is a protein^[1].

Key Facts

Ubiquitin B's instance of is recorded as protein^[2].
Ubiquitin B's UniProt protein ID is recorded as P0CG47^[3].
Ubiquitin B's part of is recorded as Ubiquitin-like domain superfamily^[4].
Ubiquitin B's part of is recorded as Ubiquitin domain^[5].
Ubiquitin B's part of is recorded as ubiquitin^[6].
Ubiquitin B's part of is recorded as Ubiquitin-like domain, protein family^[7].
Ubiquitin B's part of is recorded as Ubiquitin conserved site, protein family^[8].
Ubiquitin B's has part is recorded as Ubiquitin domain^[9].
Ubiquitin B's has part is recorded as Ubiquitin conserved site^[10].
Ubiquitin B's RefSeq protein ID is recorded as NP_001268645^[11].
Ubiquitin B's RefSeq protein ID is recorded as NP_001268646^[12].
Ubiquitin B's RefSeq protein ID is recorded as NP_001268647^[13].
Ubiquitin B's RefSeq protein ID is recorded as NP_001268648^[14].
Ubiquitin B's RefSeq protein ID is recorded as NP_001268649^[15].
Ubiquitin B's RefSeq protein ID is recorded as NP_061828^[16].
Ubiquitin B's PDB structure ID is recorded as 2KHW^[17].
Ubiquitin B's PDB structure ID is recorded as 2MBB^[18].
Ubiquitin B's PDB structure ID is recorded as 2MRO^[19].
Ubiquitin B's PDB structure ID is recorded as 2MSG^[20].
Ubiquitin B's PDB structure ID is recorded as 4UEL^[21].
Ubiquitin B's PDB structure ID is recorded as 4UF6^[22].
Ubiquitin B's PDB structure ID is recorded as 4WLR^[23].
Ubiquitin B's PDB structure ID is recorded as 4WUR^[24].
Ubiquitin B's PDB structure ID is recorded as 4ZPZ^[25].
Ubiquitin B's PDB structure ID is recorded as 5CAW^[26].

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Quick Facts

Instance of protein

Part of Ubiquitin-like domain superfamily, Ubiquitin domain, ubiquitin, Ubiquitin-like domain, protein family, Ubiquitin conserved site, protein family

Properties

Biological process DNA damage response, signal transduction by p53 class mediator resulting in cell cycle arrest, negative regulation of epidermal growth factor receptor signaling pathway, interstrand cross-link repair, nucleotide-excision repair, DNA damage recognition, positive regulation of canonical Wnt signaling pathway, tumor necrosis factor-mediated signaling pathway, regulation of type I interferon production, positive regulation of protein monoubiquitination, TRIF-dependent toll-like receptor signaling pathway, Fc-epsilon receptor signaling pathway, endosomal transport, global genome nucleotide-excision repair, NIK/NF-kappaB signaling, G2/M transition of mitotic cell cycle, stress-activated MAPK cascade, transforming growth factor beta receptor signaling pathway, macroautophagy, negative regulation of canonical Wnt signaling pathway, nucleotide-excision repair, DNA gap filling, error-free translesion synthesis, regulation of tumor necrosis factor-mediated signaling pathway, stimulatory C-type lectin receptor signaling pathway, negative regulation of transforming growth factor beta receptor signaling pathway, JNK cascade, regulation of transcription from RNA polymerase II promoter in response to hypoxia, nucleotide-excision repair, DNA incision, I-kappaB kinase/NF-kappaB signaling, innate immune response, Notch signaling pathway, neuron projection morphogenesis, regulation of mRNA stability, protein polyubiquitination, negative regulation of apoptotic process, negative regulation of transcription by RNA polymerase II, virion assembly, positive regulation of intrinsic apoptotic signaling pathway by p53 class mediator, positive regulation of NF-kappaB transcription factor activity, anaphase-promoting complex-dependent catabolic process, negative regulation of type I interferon production, nucleotide-binding oligomerization domain containing signaling pathway, positive regulation of protein ubiquitination, intracellular transport of virus, regulation of proteasomal protein catabolic process, viral life cycle, MyD88-dependent toll-like receptor signaling pathway, error-prone translesion synthesis, MAPK cascade, regulation of mitochondrial membrane potential, fibroblast growth factor receptor signaling pathway, ion transmembrane transport, glycogen biosynthetic process, regulation of neuron death, positive regulation of apoptotic process, positive regulation of I-kappaB kinase/NF-kappaB signaling, translesion synthesis, transcription-coupled nucleotide-excision repair, mitochondrion transport along microtubule, T cell receptor signaling pathway, MyD88-independent toll-like receptor signaling pathway, positive regulation of transcription by RNA polymerase II, regulation of signal transduction by p53 class mediator, positive regulation of epidermal growth factor receptor signaling pathway, Wnt signaling pathway, nucleotide-excision repair, DNA duplex unwinding, nucleotide-excision repair, DNA incision, 5'-to lesion, ERBB2 signaling pathway, Wnt signaling pathway, planar cell polarity pathway, nucleotide-excision repair, preincision complex assembly, proteasome-mediated ubiquitin-dependent protein catabolic process, protein folding, negative regulation of G2/M transition of mitotic cell cycle, protein ubiquitination, protein deubiquitination, SCF-dependent proteasomal ubiquitin-dependent protein catabolic process, entry of bacterium into host cell, transmembrane transport, regulation of necroptotic process, membrane organization, endoplasmic reticulum mannose trimming, cellular iron ion homeostasis, regulation of hematopoietic stem cell differentiation, protein targeting to peroxisome, male meiosis I, female meiosis I, male gonad development, female gonad development, protein ubiquitination, cytokine-mediated signaling pathway, modification-dependent protein catabolic process, hypothalamus gonadotrophin-releasing hormone neuron development, adipose tissue development, fat pad development, interleukin-1-mediated signaling pathway, seminiferous tubule development, energy homeostasis

Cell component cytoplasm, endocytic vesicle membrane, cytosol, mitochondrion, neuron projection, nucleus, extracellular exosome, plasma membrane, nucleoplasm, soma, endosome membrane, extracellular space, mitochondrial outer membrane, endoplasmic reticulum quality control compartment, vesicle, endoplasmic reticulum membrane, host cell, extracellular space, nucleus, cytoplasm, vesicle, extracellular exosome

Encoded by UBB

Found in taxon Homo sapiens

Has part(s) Ubiquitin domain, Ubiquitin conserved site

Imported from wholeness_audit_2026-05-02

Molecular function protein binding, protein tag, ubiquitin protein ligase binding

External References (4)

Ensembl protein id ENSP00000304697, ENSP00000379178, ENSP00000379180, ENSP00000478771, ENSP00000437475, ENSP00000463156, ENSP00000464510, ENSP00000464594

Pdb structure id 2KHW, 2MBB, 2MRO, 2MSG, 4UEL, 4UF6, 4WLR, 4WUR, 4ZPZ, 5CAW, 3OJ3, 5DK8, 5CRA, 4ZFR, 5CVO, 3ZLZ, 4WHV, 4ZFT, 3ZNH, 5D0M, 2Y5B, 2KWV, 5D0K, 5DFL, 5CVM, 4WZP, 5EDV, 5CVN, 2KWU, 4XOF, 5BNB, 2N13, 4ZUX, 5IFR, 5IBK, 5KGF, 5JG6, 5K9P, 5E6J

Refseq protein id NP_001268645, NP_001268646, NP_001268647, NP_001268648, NP_001268649, NP_061828

Uniprot protein id P0CG47

References

Programmatic citations — every numbered marker resolves to a verifiable graph row below.

Direct Wikidata claims

[2] ↑ Ubiquitin B — instance of (P31): protein. Q905695. Retrieved 2019-11-13. wikidata.org.
[3] ↑ Ubiquitin B — UniProt protein ID (P352): P0CG47. Q905695. Retrieved 2019-11-13. wikidata.org.
[4] ↑ Ubiquitin B — part of (P361): Ubiquitin-like domain superfamily. InterPro Release 71.0. ebi.ac.uk. Provenance: wikidata.org.
[5] ↑ Ubiquitin B — part of (P361): Ubiquitin domain. InterPro Release 71.0. ebi.ac.uk. Provenance: wikidata.org.
[6] ↑ Ubiquitin B — part of (P361): ubiquitin. wikidata.org.
[7] ↑ Ubiquitin B — part of (P361): Ubiquitin-like domain, protein family. wikidata.org.
[8] ↑ Ubiquitin B — part of (P361): Ubiquitin conserved site, protein family. wikidata.org.
[9] ↑ Ubiquitin B — has part(s) (P527): Ubiquitin domain. InterPro Release 71.0. ebi.ac.uk. Provenance: wikidata.org.
[10] ↑ Ubiquitin B — has part(s) (P527): Ubiquitin conserved site. InterPro Release 71.0. ebi.ac.uk. Provenance: wikidata.org.
[11] ↑ Ubiquitin B — RefSeq protein ID (P637): NP_001268645. Q20641742. Retrieved 2020-05-30. wikidata.org.
[12] ↑ Ubiquitin B — RefSeq protein ID (P637): NP_001268646. Q20641742. Retrieved 2020-05-30. wikidata.org.
[13] ↑ Ubiquitin B — RefSeq protein ID (P637): NP_001268647. Q20641742. Retrieved 2020-05-30. wikidata.org.
[14] ↑ Ubiquitin B — RefSeq protein ID (P637): NP_001268648. Q20641742. Retrieved 2020-05-30. wikidata.org.
[15] ↑ Ubiquitin B — RefSeq protein ID (P637): NP_001268649. Q20641742. Retrieved 2020-05-30. wikidata.org.
[16] ↑ Ubiquitin B — RefSeq protein ID (P637): NP_061828. Q20641742. Retrieved 2020-05-30. wikidata.org.
[17] ↑ Ubiquitin B — PDB structure ID (P638): 2KHW. Q905695. Retrieved 2016-08-04. wikidata.org.
[18] ↑ Ubiquitin B — PDB structure ID (P638): 2MBB. Q905695. Retrieved 2016-08-04. wikidata.org.
[19] ↑ Ubiquitin B — PDB structure ID (P638): 2MRO. Q905695. Retrieved 2016-08-04. wikidata.org.
[20] ↑ Ubiquitin B — PDB structure ID (P638): 2MSG. Q905695. Retrieved 2016-08-04. wikidata.org.
[21] ↑ Ubiquitin B — PDB structure ID (P638): 4UEL. Q905695. Retrieved 2016-08-04. wikidata.org.
[22] ↑ Ubiquitin B — PDB structure ID (P638): 4UF6. Q905695. Retrieved 2016-08-04. wikidata.org.
[23] ↑ Ubiquitin B — PDB structure ID (P638): 4WLR. Q905695. Retrieved 2016-08-04. wikidata.org.
[24] ↑ Ubiquitin B — PDB structure ID (P638): 4WUR. Q905695. Retrieved 2016-08-04. wikidata.org.
[25] ↑ Ubiquitin B — PDB structure ID (P638): 4ZPZ. Q905695. Retrieved 2016-08-04. wikidata.org.
[26] ↑ Ubiquitin B — PDB structure ID (P638): 5CAW. Q905695. Retrieved 2016-08-04. wikidata.org.

Class ancestry

[1] ↑ Ubiquitin B is an instance of protein (Q8054) [P31, primary]. Wikidata. wikidata.org.

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Use these citations when quoting this entity in research, articles, AI prompts, or wherever provenance matters. We aggregate Wikidata + Wikipedia + authoritative open-data sources; the stitched, scored, cross-referenced view is what 4ort.xyz contributes.

APA 4ort.xyz Knowledge Graph. (2026). Ubiquitin B. Retrieved May 3, 2026, from https://4ort.xyz/entity/ubiquitin-b

MLA “Ubiquitin B.” 4ort.xyz Knowledge Graph, 4ort.xyz, 3 May. 2026, https://4ort.xyz/entity/ubiquitin-b.

BibTeX

@misc{4ortxyz_ubiquitin-b_2026, author = {{4ort.xyz Knowledge Graph}}, title = {{Ubiquitin B}}, year = {2026}, url = {https://4ort.xyz/entity/ubiquitin-b}, note = {Accessed: 2026-05-03}}

LLM prompt

According to 4ort.xyz Knowledge Graph (aggregator of Wikidata, Wikipedia, and authoritative open-data sources): Ubiquitin B — https://4ort.xyz/entity/ubiquitin-b (retrieved 2026-05-03)

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