UBXN1_DANRE
ID UBXN1_DANRE Reviewed; 294 AA.
AC Q6NXA9;
DT 05-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 86.
DE RecName: Full=UBX domain-containing protein 1;
DE AltName: Full=SAPK substrate protein 1;
GN Name=ubxn1; Synonyms=saks1; ORFNames=zgc:77531;
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney;
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (MAR-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Ubiquitin-binding protein that specifically binds 'Lys-6'-
CC linked polyubiquitin chains. 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. Involved in ubiquitin-proteasome systems (By similarity).
CC {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; BC067166; AAH67166.1; -; mRNA.
DR RefSeq; NP_997772.1; NM_212607.1.
DR AlphaFoldDB; Q6NXA9; -.
DR SMR; Q6NXA9; -.
DR STRING; 7955.ENSDARP00000105431; -.
DR PaxDb; Q6NXA9; -.
DR GeneID; 322073; -.
DR KEGG; dre:322073; -.
DR CTD; 51035; -.
DR ZFIN; ZDB-GENE-030131-792; ubxn1.
DR eggNOG; KOG2689; Eukaryota.
DR InParanoid; Q6NXA9; -.
DR OrthoDB; 1297214at2759; -.
DR PhylomeDB; Q6NXA9; -.
DR Reactome; R-DRE-532668; N-glycan trimming in the ER and Calnexin/Calreticulin cycle.
DR PRO; PR:Q6NXA9; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
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: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 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 Coiled coil; Cytoplasm; Reference proteome.
FT CHAIN 1..294
FT /note="UBX domain-containing protein 1"
FT /id="PRO_0000248999"
FT DOMAIN 1..42
FT /note="UBA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00212"
FT DOMAIN 214..291
FT /note="UBX"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00215"
FT REGION 42..215
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 89..159
FT /evidence="ECO:0000255"
FT COMPBIAS 79..181
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 294 AA; 33436 MW; 21D76D43D2EACC64 CRC64;
MADCTTLDSL LEMGFGRNRA EKAVAHTGNQ GIERAMDWLM EHENDPDIDE PYVPPAGNTL
GPAEEQSQSP TEIPESIEDT EEGNARQPMT EEERKEQVKR LEDLMKARQE ERRERERQEG
IEREKQRRKQ GQELLQVRQK LQEDEMKKLA DQRRKEKMED RLAKQRVKDK IARDREERAQ
KFGGGSSSTG LSSPPAEAPA LSPPENQGAP PAKKDYDDCR IQVRLLDGTT LSTVFKAQEP
LAAVRVYVQM NGANGQDFNL ITPYPRRVYT DLDMEKPLRE LGLVPSAVLV VTKK