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UBQL1_PONAB
ID   UBQL1_PONAB             Reviewed;         589 AA.
AC   Q5R684;
DT   12-JUN-2007, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 1.
DT   25-MAY-2022, entry version 96.
DE   RecName: Full=Ubiquilin-1;
GN   Name=UBQLN1;
OS   Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pongo.
OX   NCBI_TaxID=9601;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain cortex;
RG   The German cDNA consortium;
RL   Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Plays an important role in the regulation of different
CC       protein degradation mechanisms and pathways including ubiquitin-
CC       proteasome system (UPS), autophagy and endoplasmic reticulum-associated
CC       protein degradation (ERAD) pathway. Mediates the proteasomal targeting
CC       of misfolded or accumulated proteins for degradation by binding (via
CC       UBA domain) to their polyubiquitin chains and by interacting (via
CC       ubiquitin-like domain) with the subunits of the proteasome. Plays a
CC       role in the ERAD pathway via its interaction with ER-localized proteins
CC       UBXN4, VCP and HERPUD1 and may form a link between the
CC       polyubiquitinated ERAD substrates and the proteasome. Plays a role in
CC       unfolded protein response (UPR) by attenuating the induction of UPR-
CC       inducible genes, DDTI3/CHOP, HSPA5 and PDIA2 during ER stress. Involved
CC       in the regulation of macroautophagy and autophagosome formation;
CC       required for maturation of autophagy-related protein LC3 from the
CC       cytosolic form LC3-I to the membrane-bound form LC3-II and may assist
CC       in the maturation of autophagosomes to autolysosomes by mediating
CC       autophagosome-lysosome fusion. Negatively regulates the TICAM1/TRIF-
CC       dependent toll-like receptor signaling pathway by decreasing the
CC       abundance of TICAM1 via the autophagic pathway. Promotes the
CC       ubiquitination and lysosomal degradation of ORAI1, consequently down-
CC       regulating the ORAI1-mediated Ca2+ mobilization. Suppresses the
CC       maturation and proteasomal degradation of amyloid beta A4 protein (A4)
CC       by stimulating the lysine 63 (K63)-linked polyubiquitination. Delays
CC       the maturation of A4 by sequestering it in the Golgi apparatus and
CC       preventing its transport to the cell surface for subsequent processing.
CC       Ubiquitinates BCL2L10 and thereby stabilizes protein abundance (By
CC       similarity). {ECO:0000250|UniProtKB:Q9JJP9,
CC       ECO:0000250|UniProtKB:Q9UMX0}.
CC   -!- SUBUNIT: Monomer and homodimer. Heterodimer with UBQLN2. Binds CD47,
CC       NBL1, GABRA1, GABRA2, GABRA3, GABRA6, GABRB1, GABRB2 and GABRB3. Binds
CC       UBE3A, BTRC, P4HB and MTOR. Interacts with the proteasome 19S subunit.
CC       Interacts (via ubiquitin-like domain) with TREX1; the interaction is
CC       direct and may control TREX1 subcellular location. Forms a complex with
CC       UBXN4 and VCP. Interacts (via UBA domain) with UBQLN4 (via ubiquitin-
CC       like domain). Found in a complex with UBQLN2 and MAP1LC3A/B/C. The
CC       monomeric form interacts with PSEN1 and PSEN2. Interacts with ORAI1.
CC       Interacts (via UBA domain) with TICAM1. Interacts with EPS15. Interacts
CC       (via UBA domain) with UBA52 and (via ubiquitin-like domain) with PSMD3
CC       and PSMD4. Interacts with HERPUD1. Interacts with MAP1LC3A/B/C in the
CC       presence of UBQLN4. Interacts (via ubiquitin-like domain) with EPS15
CC       (via UIM domains) and both the ubiquitinated and non-ubiquitinated
CC       forms can interact with EPS15. Interacts (via ubiquitin-like domain)
CC       with EPS15L1, HGS (via UIM domain) and STAM2 (via UIM domain) (By
CC       similarity). Interacts with BCL2L10/BCL-B; in the cytoplasm (By
CC       similarity). {ECO:0000250|UniProtKB:Q8R317,
CC       ECO:0000250|UniProtKB:Q9JJP9, ECO:0000250|UniProtKB:Q9UMX0}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9UMX0}. Cytoplasm
CC       {ECO:0000250|UniProtKB:Q9UMX0}. Endoplasmic reticulum
CC       {ECO:0000250|UniProtKB:Q9UMX0}. Cytoplasmic vesicle, autophagosome
CC       {ECO:0000250|UniProtKB:Q9UMX0}. Cell membrane
CC       {ECO:0000250|UniProtKB:Q9UMX0}. Note=Detected in neuronal processes and
CC       at synapses. Recruited to the ER during ER-associated protein
CC       degradation (ERAD). Colocalizes with PSEN1 in the cell membrane and in
CC       cytoplasmic juxtanuclear structures called aggresomes. Colocalizes with
CC       ORAI1 and TICAM1 in the autophagosome. Colocalizes with EPS15 and HGS
CC       in ubiquitin-rich cytoplasmic aggregates that are not endocytic
CC       compartments and with EPS15 also in aggresomes.
CC       {ECO:0000250|UniProtKB:Q9JJP9, ECO:0000250|UniProtKB:Q9UMX0}.
CC   -!- DOMAIN: The UBA domain mediates binding to PSEN1 and PSEN2. It also
CC       binds ubiquitin with micromolar affinity, independently of
CC       polyubiquitin linkage type. Essential for its association with
CC       microtubule-associated protein 1 light chain 3 (MAP1LC3).
CC       {ECO:0000250|UniProtKB:Q9UMX0}.
CC   -!- DOMAIN: The ubiquitin-like domain mediates its association with the
CC       subunits of the proteasome. {ECO:0000250|UniProtKB:Q9UMX0}.
CC   -!- DOMAIN: Dimerization is dependent upon the central region of the
CC       protein containing the STI1 domains and is independent of its
CC       ubiquitin-like and UBA domains. {ECO:0000250|UniProtKB:Q9UMX0}.
CC   -!- PTM: Degraded during both macroautophagy and during chaperone-mediated
CC       autophagy (CMA). {ECO:0000250|UniProtKB:Q9UMX0}.
CC   -!- PTM: Phosphorylated. {ECO:0000250|UniProtKB:Q9UMX0}.
CC   -!- PTM: Ubiquitinated. {ECO:0000250|UniProtKB:Q9UMX0}.
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DR   EMBL; CR860611; CAH92732.1; -; mRNA.
DR   RefSeq; NP_001127579.1; NM_001134107.1.
DR   AlphaFoldDB; Q5R684; -.
DR   BMRB; Q5R684; -.
DR   SMR; Q5R684; -.
DR   STRING; 9601.ENSPPYP00000021651; -.
DR   GeneID; 100174657; -.
DR   KEGG; pon:100174657; -.
DR   CTD; 29979; -.
DR   eggNOG; KOG0010; Eukaryota.
DR   InParanoid; Q5R684; -.
DR   OrthoDB; 1553668at2759; -.
DR   Proteomes; UP000001595; Unplaced.
DR   GO; GO:0016235; C:aggresome; ISS:UniProtKB.
DR   GO; GO:0005776; C:autophagosome; ISS:UniProtKB.
DR   GO; GO:0031410; C:cytoplasmic vesicle; IEA:UniProtKB-KW.
DR   GO; GO:0005783; C:endoplasmic reticulum; ISS:UniProtKB.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR   GO; GO:0000502; C:proteasome complex; IEA:UniProtKB-KW.
DR   GO; GO:0031593; F:polyubiquitin modification-dependent protein binding; ISS:UniProtKB.
DR   GO; GO:0035973; P:aggrephagy; ISS:UniProtKB.
DR   GO; GO:1901340; P:negative regulation of store-operated calcium channel activity; ISS:UniProtKB.
DR   GO; GO:1903071; P:positive regulation of ER-associated ubiquitin-dependent protein catabolic process; ISS:UniProtKB.
DR   GO; GO:0031398; P:positive regulation of protein ubiquitination; ISS:UniProtKB.
DR   GO; GO:0030433; P:ubiquitin-dependent ERAD pathway; ISS:UniProtKB.
DR   InterPro; IPR006636; STI1_HS-bd.
DR   InterPro; IPR015940; UBA.
DR   InterPro; IPR009060; UBA-like_sf.
DR   InterPro; IPR028430; Ubiquilin-1/2.
DR   InterPro; IPR000626; Ubiquitin-like_dom.
DR   InterPro; IPR029071; Ubiquitin-like_domsf.
DR   PANTHER; PTHR10677:SF5; PTHR10677:SF5; 2.
DR   Pfam; PF00240; ubiquitin; 1.
DR   SMART; SM00727; STI1; 4.
DR   SMART; SM00165; UBA; 1.
DR   SMART; SM00213; UBQ; 1.
DR   SUPFAM; SSF46934; SSF46934; 1.
DR   SUPFAM; SSF54236; SSF54236; 1.
DR   PROSITE; PS50030; UBA; 1.
DR   PROSITE; PS50053; UBIQUITIN_2; 1.
PE   2: Evidence at transcript level;
KW   Acetylation; Autophagy; Cell membrane; Cytoplasm; Cytoplasmic vesicle;
KW   Endoplasmic reticulum; Membrane; Nucleus; Phosphoprotein; Proteasome;
KW   Reference proteome; Ubl conjugation.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250|UniProtKB:Q9UMX0"
FT   CHAIN           2..589
FT                   /note="Ubiquilin-1"
FT                   /id="PRO_0000290337"
FT   DOMAIN          37..111
FT                   /note="Ubiquitin-like"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00214"
FT   DOMAIN          182..210
FT                   /note="STI1 1"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          212..251
FT                   /note="STI1 2"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          387..434
FT                   /note="STI1 3"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          438..470
FT                   /note="STI1 4"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          546..586
FT                   /note="UBA"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00212"
FT   REGION          1..35
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          110..145
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          178..428
FT                   /note="Interaction with UBXN4"
FT                   /evidence="ECO:0000250|UniProtKB:Q9UMX0"
FT   REGION          295..371
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          488..520
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        295..364
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        491..520
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         2
FT                   /note="N-acetylalanine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9UMX0"
SQ   SEQUENCE   589 AA;  62503 MW;  8B4756A7542F3025 CRC64;
     MAESGESGGP PGSQDSAAGA EGAGAPAAAA SAEPKIMKVT VKTPKEKEEF AVPENSSVQQ
     FKEEISKRFK SHTDQLVLIF AGKILKDQDT LSQHGIHDGL TVHLVIKTQN RPQDHSAQQT
     NTAGSNVTTS STPNSNSTSG SATSNPFGLG GLGGLAGLSS LGLNTTNFSE LQSQMQRQLL
     SNPEMMVQIM ENPFVQSMLS NPDLMRQLIM ANPQMQQLIQ RNPEISHMLN NPDIMRQTLE
     LARNPAMMQE MMRNQDRALS NLESIPGGYN ALRRMYTDIQ EPMLSAAQEQ FGGNPFASLV
     SNTSSGEGSQ PSRTENRDPL PNPWAPQTSQ SSSASSGTAS TVGGTTGSTA SGTSGQSTTA
     PNLVPGVGAS MFNTPGMQSL LQQITENPQL MQNMLSAPYM RSMMQSLSQN PDLAAQMMLN
     NPLFAGNPQL QEQMRQQLPT FLQQMQNPDT LSAMSNPRAM QALLQIQQGL QTLATEAPGL
     IPGFTPGLGA LGSTGGSSGT NGSNATPSEN TSPTAGTTEP GHQQFIQQML QALAGVNPQL
     QNPEVRFQQQ LEQPSAMGFL NREANLQALI ATGGDINAAI ERLLGSQPS
 
 
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