UBQL2_MOUSE
ID UBQL2_MOUSE Reviewed; 638 AA.
AC Q9QZM0; B1AY62; Q7TSJ8; Q8VDH9;
DT 29-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 157.
DE RecName: Full=Ubiquilin-2;
DE AltName: Full=Chap1;
DE AltName: Full=DSK2 homolog;
DE AltName: Full=Protein linking IAP with cytoskeleton 2;
DE Short=PLIC-2;
DE AltName: Full=Ubiquitin-like product Chap1/Dsk2;
GN Name=Ubqln2; Synonyms=Plic2;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, AND INTERACTION WITH CD47.
RC STRAIN=Swiss Webster / NIH; TISSUE=Embryo;
RX PubMed=10549293; DOI=10.1016/s1097-2765(00)80212-9;
RA Wu A.-L., Wang J., Zheleznyak A., Brown E.J.;
RT "Ubiquitin-related proteins regulate interaction of vimentin intermediate
RT filaments with the plasma membrane.";
RL Mol. Cell 4:619-625(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Brain;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-25, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic brain;
RX PubMed=15345747; DOI=10.1074/mcp.m400085-mcp200;
RA Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.;
RT "Phosphoproteomic analysis of the developing mouse brain.";
RL Mol. Cell. Proteomics 3:1093-1101(2004).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
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 the endoplasmic reticulum-
CC associated protein degradation (ERAD) pathway. Mediates the proteasomal
CC targeting of misfolded or accumulated proteins for degradation by
CC binding (via UBA domain) to their polyubiquitin chains and by
CC interacting (via ubiquitin-like domain) with the subunits of the
CC proteasome. Plays a role in the ERAD pathway via its interaction with
CC ER-localized proteins FAF2/UBXD8 and HERPUD1 and may form a link
CC between the polyubiquitinated ERAD substrates and the proteasome.
CC Involved in the regulation of macroautophagy and autophagosome
CC formation; required for maturation of autophagy-related protein LC3
CC from the cytosolic form LC3-I to the membrane-bound form LC3-II and may
CC assist in the maturation of autophagosomes to autolysosomes by
CC mediating autophagosome-lysosome fusion. Negatively regulates the
CC endocytosis of GPCR receptors: AVPR2 and ADRB2, by specifically
CC reducing the rate at which receptor-arrestin complexes concentrate in
CC clathrin-coated pits (CCPs) (By similarity). Links CD47 to vimentin-
CC containing intermediate filaments of the cytoskeleton
CC (PubMed:10549293). {ECO:0000250|UniProtKB:Q9UHD9,
CC ECO:0000269|PubMed:10549293}.
CC -!- SUBUNIT: Homodimer. Forms heterodimer with UBQLN1. Binds UBE3A and
CC BTRC. Interacts with the 19S proteasome subunit. Interacts with C9orf72
CC (By similarity). Binds CD47 (PubMed:10549293). Interacts with HNRNPA1
CC and HNRNPU. Found in a complex with UBQLN1 and MAP1LC3A/B/C. Interacts
CC with EPS15, EPN1 and EPN2. Interacts with HERPUD1. Interacts with
CC RAD23A. Interacts with TARDBP. Interacts (via C-terminus) with FAF2
CC (via N-terminus). Interacts with UBQLN4 (By similarity).
CC {ECO:0000250|UniProtKB:Q9UHD9, ECO:0000269|PubMed:10549293}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10549293}. Nucleus
CC {ECO:0000269|PubMed:10549293}. Membrane {ECO:0000269|PubMed:10549293}.
CC Cytoplasmic vesicle, autophagosome {ECO:0000250|UniProtKB:Q9UHD9}.
CC Note=Colocalizes with a subset of proteasomes, namely those that are
CC cytoskeleton associated or free in the cytosol. Associated with fibers
CC in mitotic cells. {ECO:0000250|UniProtKB:Q9UHD9}.
CC -!- TISSUE SPECIFICITY: Highly expressed in smooth muscle. Expression in
CC other tissues is very low. {ECO:0000269|PubMed:10549293}.
CC -!- DOMAIN: The ubiquitin-like domain is essential for its inhibitory
CC effect on GPCR endocytosis. Mediates its association with the subunits
CC of the proteasome. {ECO:0000250|UniProtKB:Q9UHD9}.
CC -!- DOMAIN: The UBA domain is essential for its association with
CC microtubule-associated protein 1 light chain 3 (MAP1LC3). Mediates its
CC association with ubiquitinated substrates.
CC {ECO:0000250|UniProtKB:Q9UHD9}.
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:Q9UHD9}.
CC -!- PTM: Degraded during macroautophagy. {ECO:0000250|UniProtKB:Q9UHD9}.
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DR EMBL; AF177346; AAF01366.1; -; mRNA.
DR EMBL; AL844583; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH466653; EDL31351.1; -; Genomic_DNA.
DR EMBL; BC021824; AAH21824.1; -; mRNA.
DR EMBL; BC053022; AAH53022.1; -; mRNA.
DR CCDS; CCDS30482.1; -.
DR RefSeq; NP_061268.2; NM_018798.2.
DR AlphaFoldDB; Q9QZM0; -.
DR SMR; Q9QZM0; -.
DR BioGRID; 207684; 49.
DR STRING; 10090.ENSMUSP00000056888; -.
DR iPTMnet; Q9QZM0; -.
DR PhosphoSitePlus; Q9QZM0; -.
DR EPD; Q9QZM0; -.
DR MaxQB; Q9QZM0; -.
DR PaxDb; Q9QZM0; -.
DR PeptideAtlas; Q9QZM0; -.
DR PRIDE; Q9QZM0; -.
DR ProteomicsDB; 300071; -.
DR Antibodypedia; 570; 303 antibodies from 34 providers.
DR DNASU; 54609; -.
DR Ensembl; ENSMUST00000060714; ENSMUSP00000056888; ENSMUSG00000050148.
DR GeneID; 54609; -.
DR KEGG; mmu:54609; -.
DR UCSC; uc009uqw.1; mouse.
DR CTD; 29978; -.
DR MGI; MGI:1860283; Ubqln2.
DR VEuPathDB; HostDB:ENSMUSG00000050148; -.
DR eggNOG; KOG0010; Eukaryota.
DR GeneTree; ENSGT00940000162603; -.
DR HOGENOM; CLU_024293_4_0_1; -.
DR InParanoid; Q9QZM0; -.
DR OMA; QMMNNPD; -.
DR OrthoDB; 1553668at2759; -.
DR PhylomeDB; Q9QZM0; -.
DR TreeFam; TF314412; -.
DR Reactome; R-MMU-8856825; Cargo recognition for clathrin-mediated endocytosis.
DR BioGRID-ORCS; 54609; 0 hits in 73 CRISPR screens.
DR ChiTaRS; Ubqln2; mouse.
DR PRO; PR:Q9QZM0; -.
DR Proteomes; UP000000589; Chromosome X.
DR RNAct; Q9QZM0; protein.
DR Bgee; ENSMUSG00000050148; Expressed in habenula and 253 other tissues.
DR Genevisible; Q9QZM0; MM.
DR GO; GO:0005776; C:autophagosome; IEA:UniProtKB-SubCell.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0031410; C:cytoplasmic vesicle; IEA:UniProtKB-KW.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0031593; F:polyubiquitin modification-dependent protein binding; IBA:GO_Central.
DR GO; GO:0000045; P:autophagosome assembly; IBA:GO_Central.
DR GO; GO:1900186; P:negative regulation of clathrin-dependent endocytosis; ISS:UniProtKB.
DR GO; GO:1904021; P:negative regulation of G protein-coupled receptor internalization; ISS:UniProtKB.
DR GO; GO:1903071; P:positive regulation of ER-associated ubiquitin-dependent protein catabolic process; ISS:UniProtKB.
DR GO; GO:2000785; P:regulation of autophagosome assembly; ISS:UniProtKB.
DR GO; GO:0016241; P:regulation of macroautophagy; ISS:UniProtKB.
DR GO; GO:0030433; P:ubiquitin-dependent ERAD pathway; ISS:UniProtKB.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IBA:GO_Central.
DR InterPro; IPR016024; ARM-type_fold.
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; 1.
DR Pfam; PF00627; UBA; 1.
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; SSF48371; SSF48371; 1.
DR SUPFAM; SSF54236; SSF54236; 1.
DR PROSITE; PS50030; UBA; 1.
DR PROSITE; PS50053; UBIQUITIN_2; 1.
PE 1: Evidence at protein level;
KW Acetylation; Autophagy; Cytoplasm; Cytoplasmic vesicle; Membrane; Nucleus;
KW Phosphoprotein; Reference proteome; Repeat.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q9UHD9"
FT CHAIN 2..638
FT /note="Ubiquilin-2"
FT /id="PRO_0000211012"
FT DOMAIN 33..107
FT /note="Ubiquitin-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00214"
FT DOMAIN 189..217
FT /note="STI1 1"
FT /evidence="ECO:0000255"
FT DOMAIN 219..258
FT /note="STI1 2"
FT /evidence="ECO:0000255"
FT DOMAIN 393..440
FT /note="STI1 3"
FT /evidence="ECO:0000255"
FT DOMAIN 444..476
FT /note="STI1 4"
FT /evidence="ECO:0000255"
FT REPEAT 505..507
FT /note="1"
FT REPEAT 508..510
FT /note="2"
FT REPEAT 511..513
FT /note="3"
FT REPEAT 514..516
FT /note="4"
FT REPEAT 517..519
FT /note="5"
FT REPEAT 520..522
FT /note="6"
FT REPEAT 523..525
FT /note="7"
FT REPEAT 526..528
FT /note="8"
FT REPEAT 529..531
FT /note="9"
FT REPEAT 532..533
FT /note="10"
FT REPEAT 535..537
FT /note="11"
FT DOMAIN 589..635
FT /note="UBA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00212"
FT REGION 1..31
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 107..158
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 298..364
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 505..537
FT /note="11 X 3 AA tandem repeats P-X-X"
FT REGION 528..570
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 298..324
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 336..364
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 535..570
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:Q9UHD9"
FT MOD_RES 25
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:15345747"
FT CONFLICT 179
FT /note="Q -> R (in Ref. 1; AAF01366)"
FT /evidence="ECO:0000305"
FT CONFLICT 362
FT /note="Missing (in Ref. 4; AAH21824)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 638 AA; 67351 MW; A9E7350F978B8E2A CRC64;
MAENGESSGP PRPSRGPAAA PGAASPPAEP KIIKVTVKTP KEKEEFAVPE NSTVQQFKEA
ISKRFKSQTD QLVLIFAGKI LKDQDTLMQH GIHDGLTVHL VIKSQNRPQG QATTQPSTTA
GTSTTTTTTT TAAAPAATTS SAPRSSSTPT TTNSSSFGLG SLSSLSNLGL NSPNFTELQN
QMQQQLLASP EMMIQIMENP FVQSMLSNPD LMRQLIMANP QMQQLIQRNP EISHLLNNPD
IMRQTLEIAR NPAMMQEMMR NQDLALSNLE SIPGGYNALR RMYTDIQEPM LNAAQEQFGG
NPFATVGSSS TSGEGTQPSR TENRDPLPNP WAPPPTTQTA ATTTTTTTTS SGSGSGSSSS
STTAGNTMAA ANYVASIFST PGMQSLLQQI TENPQLIQNM LSAPYMRSMM QSLSQNPDMA
AQMMLSSPLF TSNPQLQEQM RPQLPNFLQQ MQNPETIAAM SNPRAMQALM QIQQGLQTLA
TEAPGLIPSF APGVGMGVLG TAITPVGPVT PIGPIGPIVP FTPIGPIGPI GPTGPASSPG
STGTGIPPAT TVSSSAPTET ISPTSESGPN QQFIQQMVQA LTGGSPPQPP NPEVRFQQQL
EQLNAMGFLN REANLQALIA TGGDINAAIE RLLGSQPS
