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UBXN6_BOVIN
ID   UBXN6_BOVIN             Reviewed;         441 AA.
AC   Q2KIJ6;
DT   27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT   07-MAR-2006, sequence version 1.
DT   03-AUG-2022, entry version 78.
DE   RecName: Full=UBX domain-containing protein 6 {ECO:0000305};
DE   AltName: Full=UBX domain-containing protein 1 {ECO:0000250|UniProtKB:Q9BZV1};
GN   Name=UBXN6 {ECO:0000250|UniProtKB:Q9BZV1};
GN   Synonyms=UBXD1 {ECO:0000250|UniProtKB:Q9BZV1};
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=Hereford; TISSUE=Testis;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: May negatively regulate the ATPase activity of VCP, an ATP-
CC       driven segregase that associates with different cofactors to control a
CC       wide variety of cellular processes. As a cofactor of VCP, it may play a
CC       role in the transport of CAV1 to lysosomes for degradation. It may also
CC       play a role in endoplasmic reticulum-associated degradation (ERAD) of
CC       misfolded proteins. Together with VCP and other cofactors, it may play
CC       a role in macroautophagy, regulating for instance the clearance of
CC       damaged lysosomes. {ECO:0000250|UniProtKB:Q9BZV1}.
CC   -!- SUBUNIT: Interacts with VCP through the PUB domain (via C-terminus) and
CC       VIM motif (via N-terminus); the interaction is direct. Forms a ternary
CC       complex with CAV1 and VCP. Interacts with SYVN1. Interacts with
CC       HERPUD1. Interacts with VCPKMT. May interact with DERL1. Interacts with
CC       PLAA, VCP and YOD1; may form a complex involved in macroautophagy.
CC       Interacts with LMAN1. {ECO:0000250|UniProtKB:Q9BZV1}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9BZV1}.
CC       Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q9BZV1}. Membrane
CC       {ECO:0000250|UniProtKB:Q9BZV1}; Peripheral membrane protein
CC       {ECO:0000250|UniProtKB:Q9BZV1}. Nucleus {ECO:0000250|UniProtKB:Q9BZV1}.
CC       Cytoplasm, cytoskeleton, microtubule organizing center, centrosome
CC       {ECO:0000250|UniProtKB:Q9BZV1}. Early endosome membrane
CC       {ECO:0000250|UniProtKB:Q9BZV1}; Peripheral membrane protein
CC       {ECO:0000250|UniProtKB:Q9BZV1}. Late endosome membrane
CC       {ECO:0000250|UniProtKB:Q9BZV1}; Peripheral membrane protein
CC       {ECO:0000250|UniProtKB:Q9BZV1}. Lysosome membrane
CC       {ECO:0000250|UniProtKB:Q9BZV1}; Peripheral membrane protein
CC       {ECO:0000250|UniProtKB:Q9BZV1}. Note=Localizes at the centrosome both
CC       in interphase and during mitosis. May be recruited to endosomal and
CC       lysosomal membranes as part of a ternary complex with CAV1 and VCP.
CC       Recruited to damaged lysosomes decorated with K48-linked ubiquitin
CC       chains. {ECO:0000250|UniProtKB:Q9BZV1}.
CC   -!- DOMAIN: The UBX domain lacks key residues critical for VCP binding.
CC       {ECO:0000250|UniProtKB:Q9BZV1}.
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DR   EMBL; BC112614; AAI12615.1; -; mRNA.
DR   RefSeq; NP_001039451.1; NM_001045986.1.
DR   AlphaFoldDB; Q2KIJ6; -.
DR   SMR; Q2KIJ6; -.
DR   STRING; 9913.ENSBTAP00000010767; -.
DR   PaxDb; Q2KIJ6; -.
DR   PRIDE; Q2KIJ6; -.
DR   GeneID; 507936; -.
DR   KEGG; bta:507936; -.
DR   CTD; 80700; -.
DR   eggNOG; KOG2699; Eukaryota.
DR   InParanoid; Q2KIJ6; -.
DR   OrthoDB; 1288120at2759; -.
DR   Proteomes; UP000009136; Unplaced.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR   GO; GO:0031901; C:early endosome membrane; ISS:UniProtKB.
DR   GO; GO:0019898; C:extrinsic component of membrane; ISS:UniProtKB.
DR   GO; GO:0031902; C:late endosome membrane; ISS:UniProtKB.
DR   GO; GO:0005765; C:lysosomal membrane; ISS:UniProtKB.
DR   GO; GO:0005815; C:microtubule organizing center; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0032510; P:endosome to lysosome transport via multivesicular body sorting pathway; ISS:UniProtKB.
DR   GO; GO:0036503; P:ERAD pathway; ISS:UniProtKB.
DR   GO; GO:0016236; P:macroautophagy; ISS:UniProtKB.
DR   CDD; cd10460; PUB_UBXD1; 1.
DR   InterPro; IPR036339; PUB-like_dom_sf.
DR   InterPro; IPR018997; PUB_domain.
DR   InterPro; IPR029071; Ubiquitin-like_domsf.
DR   InterPro; IPR001012; UBX_dom.
DR   InterPro; IPR042774; UBXN6_PUB.
DR   Pfam; PF09409; PUB; 1.
DR   Pfam; PF00789; UBX; 1.
DR   SMART; SM00166; UBX; 1.
DR   SUPFAM; SSF143503; SSF143503; 1.
DR   SUPFAM; SSF54236; SSF54236; 1.
DR   PROSITE; PS50033; UBX; 1.
PE   2: Evidence at transcript level;
KW   Cytoplasm; Cytoskeleton; Endosome; Lysosome; Membrane; Nucleus;
KW   Reference proteome; Ubl conjugation pathway.
FT   CHAIN           1..441
FT                   /note="UBX domain-containing protein 6"
FT                   /id="PRO_0000240351"
FT   DOMAIN          175..244
FT                   /note="PUB"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          332..408
FT                   /note="UBX"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00215"
FT   REGION          1..10
FT                   /note="Mediates interaction with LMAN1"
FT                   /evidence="ECO:0000250|UniProtKB:Q9BZV1"
FT   REGION          12..57
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          51..63
FT                   /note="VCP/p97-interacting motif (VIM)"
FT                   /evidence="ECO:0000250|UniProtKB:Q9BZV1"
FT   REGION          62..81
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          86..113
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   441 AA;  49733 MW;  20C1563B88FF0A3E CRC64;
     MKKFFQEIKA DIKFKSAGPG QKLTESVGEK APKEKPSQPP VRQPRQGPTN EAQMAAAAAL
     ARLEQKQPRA RGPTSQDSIR NQVRKELRAE AAVSGDPEAP GSNTAPEPKE EGSAHLAVPG
     VYFTCPLTGA ILRKDQRDAR IREAILMHFS TDPVAASIMK IHTFNKDRDR VKLGVDTIAK
     YLDNIHLHPE EEKYRKIKVQ NKVFQERIHC LEGTHEFFEA IGFQKVLLPI PDQEGPEEFY
     VLSEAALAQP QSLEWHKEQL LSAEPVRATL ARQRRVFRPS TLASQFDLPA DFFNLTAEEI
     KREQRLRSEA VERLSVLRTK AMREREEQRE MRKYTYTLLR VRLPDGCLLQ GTFYARERVA
     ALYGFVREAL QNDWLPFELL ASGGQKLSED ENLAFNECGL VPSALLTFSL DAAVLEDIRA
     AGTQPDTSIL KPELLSAIEK L
 
 
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