UBXN1_BOVIN
ID UBXN1_BOVIN Reviewed; 297 AA.
AC Q32KW2;
DT 05-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT 06-DEC-2005, sequence version 1.
DT 03-AUG-2022, entry version 101.
DE RecName: Full=UBX domain-containing protein 1;
DE AltName: Full=SAPK substrate protein 1;
GN Name=UBXN1; Synonyms=SAKS1;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Crossbred X Angus; TISSUE=Liver;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (NOV-2005) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Ubiquitin-binding protein that interacts with the BRCA1-BARD1
CC heterodimer, and regulates its activity. Specifically binds 'Lys-6'-
CC linked polyubiquitin chains. Interaction with autoubiquitinated BRCA1,
CC leads to inhibit the E3 ubiquitin-protein ligase activity of the BRCA1-
CC BARD1 heterodimer. Component of a complex required to couple
CC deglycosylation and proteasome-mediated degradation of misfolded
CC proteins in the endoplasmic reticulum that are retrotranslocated in the
CC cytosol (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Component of a complex required to couple retrotranslocation,
CC ubiquitination and deglycosylation composed of NGLY1, SAKS1, AMFR, VCP
CC and RAD23B. Interacts with HOMER2 (By similarity). Interacts directly
CC with VCP. Interacts with BRCA1 and BARD1; interaction takes place when
CC BRCA1 is not autoubiquitinated bur is strongly enhanced in the presence
CC of autoubiquitinated BRCA1 (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- DOMAIN: The UBA domain specifically recognizes and binds 'Lys-6'-linked
CC polyubiquitin chains. {ECO:0000250}.
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DR EMBL; BC109898; AAI09899.1; -; mRNA.
DR RefSeq; NP_001032677.1; NM_001037588.2.
DR AlphaFoldDB; Q32KW2; -.
DR SMR; Q32KW2; -.
DR STRING; 9913.ENSBTAP00000013845; -.
DR PaxDb; Q32KW2; -.
DR PRIDE; Q32KW2; -.
DR Ensembl; ENSBTAT00000013845; ENSBTAP00000013845; ENSBTAG00000010481.
DR GeneID; 506676; -.
DR KEGG; bta:506676; -.
DR CTD; 51035; -.
DR VEuPathDB; HostDB:ENSBTAG00000010481; -.
DR VGNC; VGNC:36622; UBXN1.
DR eggNOG; KOG2689; Eukaryota.
DR GeneTree; ENSGT00940000156457; -.
DR HOGENOM; CLU_047594_1_0_1; -.
DR InParanoid; Q32KW2; -.
DR OMA; AQHFPRK; -.
DR OrthoDB; 1297214at2759; -.
DR TreeFam; TF313944; -.
DR Proteomes; UP000009136; Chromosome 29.
DR Bgee; ENSBTAG00000010481; Expressed in biceps femoris and 107 other tissues.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0034098; C:VCP-NPL4-UFD1 AAA ATPase complex; IEA:Ensembl.
DR GO; GO:0051117; F:ATPase binding; IEA:Ensembl.
DR GO; GO:0036435; F:K48-linked polyubiquitin modification-dependent protein binding; IBA:GO_Central.
DR GO; GO:0071796; F:K6-linked polyubiquitin modification-dependent protein binding; ISS:UniProtKB.
DR GO; GO:1904855; F:proteasome regulatory particle binding; IEA:Ensembl.
DR GO; GO:0043130; F:ubiquitin binding; IEA:Ensembl.
DR GO; GO:0031625; F:ubiquitin protein ligase binding; IEA:Ensembl.
DR GO; GO:1904293; P:negative regulation of ERAD pathway; IEA:Ensembl.
DR GO; GO:0032435; P:negative regulation of proteasomal ubiquitin-dependent protein catabolic process; ISS:UniProtKB.
DR GO; GO:1903094; P:negative regulation of protein K48-linked deubiquitination; IBA:GO_Central.
DR GO; GO:0031397; P:negative regulation of protein ubiquitination; ISS:UniProtKB.
DR GO; GO:2000157; P:negative regulation of ubiquitin-specific protease activity; IEA:Ensembl.
DR CDD; cd14302; UBA_UBXN1; 1.
DR InterPro; IPR015940; UBA.
DR InterPro; IPR009060; UBA-like_sf.
DR InterPro; IPR041923; UBA_UBXN1.
DR InterPro; IPR029071; Ubiquitin-like_domsf.
DR InterPro; IPR001012; UBX_dom.
DR Pfam; PF00627; UBA; 1.
DR Pfam; PF00789; UBX; 1.
DR SMART; SM00165; UBA; 1.
DR SMART; SM00166; UBX; 1.
DR SUPFAM; SSF46934; SSF46934; 1.
DR SUPFAM; SSF54236; SSF54236; 1.
DR PROSITE; PS50030; UBA; 1.
DR PROSITE; PS50033; UBX; 1.
PE 2: Evidence at transcript level;
KW Acetylation; Coiled coil; Cytoplasm; Phosphoprotein; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q04323"
FT CHAIN 2..297
FT /note="UBX domain-containing protein 1"
FT /id="PRO_0000248997"
FT DOMAIN 2..42
FT /note="UBA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00212"
FT DOMAIN 209..291
FT /note="UBX"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00215"
FT REGION 40..210
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 43..297
FT /note="Interaction with BRCA1"
FT /evidence="ECO:0000250"
FT COILED 86..176
FT /evidence="ECO:0000255"
FT COMPBIAS 84..178
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 189..203
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:Q04323"
FT MOD_RES 199
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q04323"
FT MOD_RES 200
FT /note="Phosphoserine; by MAPK12"
FT /evidence="ECO:0000250|UniProtKB:Q04323"
FT MOD_RES 207
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q04323"
FT MOD_RES 229
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q04323"
FT MOD_RES 270
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q04323"
SQ SEQUENCE 297 AA; 33402 MW; EFC33173A0D803F8 CRC64;
MAELTALESL IEMGFPKGRA EKALALTGNQ GIEAAMDWLM EHEDDPDVDE PLATPLGHVL
GREPTPSEQG GPKGPGSAVG EGKPVLTEEE RQEQTKRMLE LVAQKQRERE EREEREALER
ERQRRRQGQE LTAARQRLQE DEMRRAAEER RREKAEELEA RQRVREKIER DKAERAKKYG
GNVGSQPSPP ATEPGPVPSS PSREPPTKRE YDQCRIQVRL PDGTSLTQTF RAREQLAAVR
LYVELHRGEE LGGAQDPVQL LSGFPRRAFS EADMERPLQE LGLVPSAVLI VAKKCPG
