B0KWT6

PR
Gene name
UBL4A
Protein name
Ubiquitin-like protein 4A
Names
Species
Callithrix jacchus (White-tufted-ear marmoset)
KEGG Pathway
cjc:100387252
EC number
Protein Class

Descriptions

The autoinhibited protein was predicted that may have potential autoinhibitory elements via cis-regPred.

Autoinhibitory domains (AIDs)

50-135 (Predicted disordered autoinhibitory region) PR

Target domain

Relief mechanism

Assay

cis-regPred

Accessory elements

No accessory elements

References

Autoinhibited structure

Activated structure

1 structures for B0KWT6

Entry ID Method Resolution Chain Position Source
AF-B0KWT6-F1 Predicted AlphaFoldDB

No variants for B0KWT6

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for B0KWT6

No associated diseases with B0KWT6

7 regional properties for B0KWT6

Type Name Position InterPro Accession
domain Ubiquitin-like domain 1 - 73 IPR000626
conserved_site Ubiquitin conserved site 27 - 52 IPR019954
domain Ubiquitin domain 11 - 31 IPR019956-1
domain Ubiquitin domain 32 - 52 IPR019956-2
domain Ubiquitin domain 53 - 74 IPR019956-3
domain Ubl4, C-terminal TUGS domain 96 - 142 IPR041421
domain UBL4A-like, ubiquitin-like domain 1 - 72 IPR044724

Functions

Description
EC Number
Subcellular Localization
  • Cytoplasm, cytosol
  • Nucleus
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

4 GO annotations of cellular component

Name Definition
BAT3 complex A protein complex found in mammals that transfers tail-anchored (TA) proteins from SGTA to GET3 (ASNA1/TRC4) for targeting to the endoplasmic reticulum membrane. Also chaperones polypeptides from the endoplasmic reticulum retrotranslocation machinery to the proteasome, maintaining the solubility of substrates to improve ER-associated protein degradation (ERAD). Consists of BAG6 (BAT3) and its cofactors GET4 (TRC35) and UBL4A.
cytosol The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes.
membrane A lipid bilayer along with all the proteins and protein complexes embedded in it an attached to it.
nucleoplasm That part of the nuclear content other than the chromosomes or the nucleolus.

1 GO annotations of molecular function

Name Definition
chaperone binding Binding to a chaperone protein, a class of proteins that bind to nascent or unfolded polypeptides and ensure correct folding or transport.

4 GO annotations of biological process

Name Definition
post-translational protein targeting to endoplasmic reticulum membrane The targeting of proteins to a membrane that occurs after their translation. Some secretory proteins exhibit posttranslational transport into the endoplasmic reticulum (ER) lumen: they are synthesized in their entirety on free cytosolic ribosomes and then released into the cytosol, where they are bound by chaperones which keep them in an unfolded state, and subsequently are translocated across the ER membrane.
regulation of protein stability Any process that affects the structure and integrity of a protein, altering the likelihood of its degradation or aggregation.
tail-anchored membrane protein insertion into ER membrane A process of protein insertion into the endoplasmic reticulum (ER) membrane in which a tail-anchored (TA) transmembrane protein is incorporated into an endoplasmic reticulum (ER) membrane. TA transmembrane protein, also named type II transmembrane proteins, contain a single C- terminal transmembrane region.
ubiquitin-dependent protein catabolic process The chemical reactions and pathways resulting in the breakdown of a protein or peptide by hydrolysis of its peptide bonds, initiated by the covalent attachment of a ubiquitin group, or multiple ubiquitin groups, to the protein.

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MQLTVKALQG RDCSLQVPED ELVSTLKQLV SEKLNVPVRQ QRLLFKGKAL ADGKRLSDYS
70 80 90 100 110 120
IGPNSKLNLV VKPLEKVLLE EGTGRRLADS PPPQVWQLIS KVLARHFSAA DASRVLEQLQ
130 140 150
RDYERSLSRL TLDDIERLAG RFLHPEVTET MEKGFSK