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UBXN1_XENTR
ID   UBXN1_XENTR             Reviewed;         287 AA.
AC   Q6GL77;
DT   05-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 89.
DE   RecName: Full=UBX domain-containing protein 1;
DE   AltName: Full=SAPK substrate protein 1;
GN   Name=ubxn1; Synonyms=saks1;
OS   Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX   NCBI_TaxID=8364;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Embryo;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Component of a complex required to couple deglycosylation and
CC       proteasome-mediated degradation of misfolded proteins in the
CC       endoplasmic reticulum that are retrotranslocated in the cytosol.
CC       Involved in ubiquitin-proteasome systems (By similarity).
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
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DR   EMBL; BC074627; AAH74627.1; -; mRNA.
DR   EMBL; BC075456; AAH75456.1; -; mRNA.
DR   RefSeq; NP_001004957.1; NM_001004957.1.
DR   RefSeq; XP_012809780.1; XM_012954326.2.
DR   AlphaFoldDB; Q6GL77; -.
DR   SMR; Q6GL77; -.
DR   STRING; 8364.ENSXETP00000012041; -.
DR   PaxDb; Q6GL77; -.
DR   DNASU; 448372; -.
DR   Ensembl; ENSXETT00000012041; ENSXETP00000012041; ENSXETG00000005477.
DR   GeneID; 448372; -.
DR   KEGG; xtr:448372; -.
DR   CTD; 51035; -.
DR   Xenbase; XB-GENE-979857; ubxn1.
DR   eggNOG; KOG2689; Eukaryota.
DR   HOGENOM; CLU_047594_1_0_1; -.
DR   InParanoid; Q6GL77; -.
DR   OMA; TNHANGV; -.
DR   OrthoDB; 1297214at2759; -.
DR   PhylomeDB; Q6GL77; -.
DR   TreeFam; TF313944; -.
DR   Proteomes; UP000008143; Chromosome 4.
DR   Proteomes; UP000790000; Unplaced.
DR   Bgee; ENSXETG00000005477; Expressed in heart and 14 other tissues.
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:0032435; P:negative regulation of proteasomal ubiquitin-dependent protein catabolic process; IBA:GO_Central.
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; IBA:GO_Central.
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..287
FT                   /note="UBX domain-containing protein 1"
FT                   /id="PRO_0000249002"
FT   DOMAIN          1..42
FT                   /note="UBA"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00212"
FT   DOMAIN          205..284
FT                   /note="UBX"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00215"
FT   REGION          44..207
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          72..164
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        74..123
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        133..171
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   287 AA;  32566 MW;  7D64EC26CB677338 CRC64;
     MAECSTLESL IEMGFSPSRA EKALAATGNQ GIEPAMDWLV EHEDDPDIDE PSVVVPEDSD
     SGTTDTQGMD TCEERLPLTE EEKEKQTKRM MELIAQKQKE REEREKRERI EQEKQRRKQG
     QELSAVKQKI QEQEMQKAVE DRRREKQEEK LARDRVREKI ARDKAERARR FGGAGSEPIS
     PPAEASIPAT TPSPSSPVQE PPTKKEYDQC RIQVRLLDGS ALSQTFRARE QLAAVRLYVE
     LNWPGGAPGP FNLLTSFPRR VFTEEDMEKP LQELGLVPSA VLIVARK
 
 
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