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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
 
 
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