UBIQ1_CAEEL
ID UBIQ1_CAEEL Reviewed; 838 AA.
AC P0CG71; P14792; Q9U1P3;
DT 10-AUG-2010, integrated into UniProtKB/Swiss-Prot.
DT 10-AUG-2010, sequence version 1.
DT 03-AUG-2022, entry version 85.
DE RecName: Full=Polyubiquitin-A;
DE Contains:
DE RecName: Full=Ubiquitin;
DE Contains:
DE RecName: Full=Ubiquitin-related;
DE Flags: Precursor;
GN Name=ubq-1; Synonyms=ubia; ORFNames=F25B5.4;
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2538720; DOI=10.1128/mcb.9.1.268-277.1989;
RA Graham R.W., Jones D., Candidio E.P.M.;
RT "UbiA, the major polyubiquitin locus in Caenorhabditis elegans, has unusual
RT structural features and is constitutively expressed.";
RL Mol. Cell. Biol. 9:268-277(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-37.
RX PubMed=2839490; DOI=10.1016/s0021-9258(19)81532-6;
RA Graham R.W., van Doren K., Bektesh S., Candido E.P.M.;
RT "Maturation of the major ubiquitin gene transcript in Caenorhabditis
RT elegans involves the acquisition of a trans-spliced leader.";
RL J. Biol. Chem. 263:10415-10419(1988).
CC -!- FUNCTION: Ubiquitin exists either covalently attached to another
CC protein, or free (unanchored). When covalently bound, it is conjugated
CC to target proteins via an isopeptide bond either as a monomer
CC (monoubiquitin), a polymer linked via different Lys residues of the
CC ubiquitin (polyubiquitin chains) or a linear polymer linked via the
CC initiator Met of the ubiquitin (linear polyubiquitin chains).
CC Polyubiquitin chains, when attached to a target protein, have different
CC functions depending on the Lys residue of the ubiquitin that is linked:
CC Lys-48-linked is involved in protein degradation via the proteasome.
CC Linear polymer chains formed via attachment by the initiator Met lead
CC to cell signaling. Ubiquitin is usually conjugated to Lys residues of
CC target proteins, however, in rare cases, conjugation to Cys or Ser
CC residues has been observed. When polyubiquitin is free (unanchored-
CC polyubiquitin), it also has distinct roles, such as in activation of
CC protein kinases, and in signaling (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: [Ubiquitin]: Cytoplasm {ECO:0000250}. Nucleus
CC {ECO:0000250}.
CC -!- MISCELLANEOUS: In C.elegans ubiquitin is encoded by 2 different genes.
CC ubq-2 gene codes for a single copy of ubiquitin fused to the ribosomal
CC proteins L40. ubq-1 gene codes for a polyubiquitin precursor with exact
CC head to tail repeats.
CC -!- MISCELLANEOUS: For the sake of clarity sequence features are annotated
CC only for the first chain, and are not repeated for each of the
CC following chains.
CC -!- SIMILARITY: Belongs to the ubiquitin family. {ECO:0000305}.
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DR EMBL; M23433; AAA28154.1; -; Genomic_DNA.
DR EMBL; FO081045; CCD68779.1; -; Genomic_DNA.
DR EMBL; M21321; AAA28153.1; -; Genomic_DNA.
DR PIR; A30126; A30126.
DR PIR; T16144; T16144.
DR RefSeq; NP_741157.1; NM_171139.4.
DR AlphaFoldDB; P0CG71; -.
DR SMR; P0CG71; -.
DR BioGRID; 41061; 20.
DR IntAct; P0CG71; 1.
DR STRING; 6239.F25B5.4a.2; -.
DR EPD; P0CG71; -.
DR PaxDb; P0CG71; -.
DR EnsemblMetazoa; F25B5.4.1; F25B5.4.1; WBGene00006727.
DR EnsemblMetazoa; F25B5.4.2; F25B5.4.2; WBGene00006727.
DR GeneID; 175840; -.
DR KEGG; cel:CELE_F25B5.4; -.
DR CTD; 175840; -.
DR WormBase; F25B5.4; CE01921; WBGene00006727; ubq-1.
DR eggNOG; KOG0001; Eukaryota.
DR GeneTree; ENSGT00940000163900; -.
DR HOGENOM; CLU_010412_1_0_1; -.
DR InParanoid; P0CG71; -.
DR OMA; HLTMQIF; -.
DR OrthoDB; 1536766at2759; -.
DR PhylomeDB; P0CG71; -.
DR Reactome; R-CEL-110312; Translesion synthesis by REV1.
DR Reactome; R-CEL-110314; Recognition of DNA damage by PCNA-containing replication complex.
DR Reactome; R-CEL-110320; Translesion Synthesis by POLH.
DR Reactome; R-CEL-1234176; Oxygen-dependent proline hydroxylation of Hypoxia-inducible Factor Alpha.
DR Reactome; R-CEL-1253288; Downregulation of ERBB4 signaling.
DR Reactome; R-CEL-156827; L13a-mediated translational silencing of Ceruloplasmin expression.
DR Reactome; R-CEL-1799339; SRP-dependent cotranslational protein targeting to membrane.
DR Reactome; R-CEL-182971; EGFR downregulation.
DR Reactome; R-CEL-187577; SCF(Skp2)-mediated degradation of p27/p21.
DR Reactome; R-CEL-195253; Degradation of beta-catenin by the destruction complex.
DR Reactome; R-CEL-2173788; Downregulation of TGF-beta receptor signaling.
DR Reactome; R-CEL-2173795; Downregulation of SMAD2/3:SMAD4 transcriptional activity.
DR Reactome; R-CEL-2173796; SMAD2/SMAD3:SMAD4 heterotrimer regulates transcription.
DR Reactome; R-CEL-2672351; Stimuli-sensing channels.
DR Reactome; R-CEL-349425; Autodegradation of the E3 ubiquitin ligase COP1.
DR Reactome; R-CEL-382556; ABC-family proteins mediated transport.
DR Reactome; R-CEL-4641258; Degradation of DVL.
DR Reactome; R-CEL-532668; N-glycan trimming in the ER and Calnexin/Calreticulin cycle.
DR Reactome; R-CEL-5358346; Hedgehog ligand biogenesis.
DR Reactome; R-CEL-5632684; Hedgehog 'on' state.
DR Reactome; R-CEL-5655862; Translesion synthesis by POLK.
DR Reactome; R-CEL-5675221; Negative regulation of MAPK pathway.
DR Reactome; R-CEL-5689603; UCH proteinases.
DR Reactome; R-CEL-5689877; Josephin domain DUBs.
DR Reactome; R-CEL-5689880; Ub-specific processing proteases.
DR Reactome; R-CEL-5689896; Ovarian tumor domain proteases.
DR Reactome; R-CEL-5689901; Metalloprotease DUBs.
DR Reactome; R-CEL-5696394; DNA Damage Recognition in GG-NER.
DR Reactome; R-CEL-5696395; Formation of Incision Complex in GG-NER.
DR Reactome; R-CEL-5696397; Gap-filling DNA repair synthesis and ligation in GG-NER.
DR Reactome; R-CEL-5696400; Dual Incision in GG-NER.
DR Reactome; R-CEL-6781823; Formation of TC-NER Pre-Incision Complex.
DR Reactome; R-CEL-6782135; Dual incision in TC-NER.
DR Reactome; R-CEL-6782210; Gap-filling DNA repair synthesis and ligation in TC-NER.
DR Reactome; R-CEL-6791226; Major pathway of rRNA processing in the nucleolus and cytosol.
DR Reactome; R-CEL-6807004; Negative regulation of MET activity.
DR Reactome; R-CEL-68949; Orc1 removal from chromatin.
DR Reactome; R-CEL-69017; CDK-mediated phosphorylation and removal of Cdc6.
DR Reactome; R-CEL-69231; Cyclin D associated events in G1.
DR Reactome; R-CEL-72689; Formation of a pool of free 40S subunits.
DR Reactome; R-CEL-72706; GTP hydrolysis and joining of the 60S ribosomal subunit.
DR Reactome; R-CEL-8849469; PTK6 Regulates RTKs and Their Effectors AKT1 and DOK1.
DR Reactome; R-CEL-8854050; FBXL7 down-regulates AURKA during mitotic entry and in early mitosis.
DR Reactome; R-CEL-8856825; Cargo recognition for clathrin-mediated endocytosis.
DR Reactome; R-CEL-8856828; Clathrin-mediated endocytosis.
DR Reactome; R-CEL-8863795; Downregulation of ERBB2 signaling.
DR Reactome; R-CEL-8866652; Synthesis of active ubiquitin: roles of E1 and E2 enzymes.
DR Reactome; R-CEL-8866654; E3 ubiquitin ligases ubiquitinate target proteins.
DR Reactome; R-CEL-8939902; Regulation of RUNX2 expression and activity.
DR Reactome; R-CEL-8941858; Regulation of RUNX3 expression and activity.
DR Reactome; R-CEL-8948747; Regulation of PTEN localization.
DR Reactome; R-CEL-8948751; Regulation of PTEN stability and activity.
DR Reactome; R-CEL-8951664; Neddylation.
DR Reactome; R-CEL-901032; ER Quality Control Compartment (ERQC).
DR Reactome; R-CEL-9020702; Interleukin-1 signaling.
DR Reactome; R-CEL-9033241; Peroxisomal protein import.
DR Reactome; R-CEL-912631; Regulation of signaling by CBL.
DR Reactome; R-CEL-917729; Endosomal Sorting Complex Required For Transport (ESCRT).
DR Reactome; R-CEL-917937; Iron uptake and transport.
DR Reactome; R-CEL-936440; Negative regulators of DDX58/IFIH1 signaling.
DR Reactome; R-CEL-9646399; Aggrephagy.
DR Reactome; R-CEL-9664873; Pexophagy.
DR Reactome; R-CEL-9755511; KEAP1-NFE2L2 pathway.
DR Reactome; R-CEL-975956; Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC).
DR Reactome; R-CEL-975957; Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).
DR Reactome; R-CEL-9762114; GSK3B and BTRC:CUL1-mediated-degradation of NFE2L2.
DR Reactome; R-CEL-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR SignaLink; P0CG71; -.
DR PRO; PR:P0CG71; -.
DR Proteomes; UP000001940; Chromosome III.
DR Bgee; WBGene00006727; Expressed in germ line (C elegans) and 4 other tissues.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0031386; F:protein tag; IBA:GO_Central.
DR GO; GO:0031625; F:ubiquitin protein ligase binding; IBA:GO_Central.
DR GO; GO:0019941; P:modification-dependent protein catabolic process; IBA:GO_Central.
DR GO; GO:0010623; P:programmed cell death involved in cell development; IMP:UniProtKB.
DR GO; GO:0016567; P:protein ubiquitination; IBA:GO_Central.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IMP:UniProtKB.
DR InterPro; IPR000626; Ubiquitin-like_dom.
DR InterPro; IPR029071; Ubiquitin-like_domsf.
DR InterPro; IPR019954; Ubiquitin_CS.
DR InterPro; IPR019956; Ubiquitin_dom.
DR Pfam; PF00240; ubiquitin; 11.
DR PRINTS; PR00348; UBIQUITIN.
DR SMART; SM00213; UBQ; 11.
DR SUPFAM; SSF54236; SSF54236; 11.
DR PROSITE; PS00299; UBIQUITIN_1; 11.
DR PROSITE; PS50053; UBIQUITIN_2; 11.
PE 3: Inferred from homology;
KW Cytoplasm; Isopeptide bond; Nucleus; Reference proteome; Repeat;
KW Ubl conjugation.
FT CHAIN 1..76
FT /note="Ubiquitin"
FT /id="PRO_0000114817"
FT CHAIN 77..152
FT /note="Ubiquitin"
FT /id="PRO_0000396270"
FT CHAIN 153..228
FT /note="Ubiquitin"
FT /id="PRO_0000396271"
FT CHAIN 229..304
FT /note="Ubiquitin"
FT /id="PRO_0000396272"
FT CHAIN 305..380
FT /note="Ubiquitin"
FT /id="PRO_0000396273"
FT CHAIN 381..456
FT /note="Ubiquitin-related"
FT /id="PRO_0000396274"
FT CHAIN 457..532
FT /note="Ubiquitin"
FT /id="PRO_0000396275"
FT CHAIN 533..608
FT /note="Ubiquitin"
FT /id="PRO_0000396276"
FT CHAIN 609..684
FT /note="Ubiquitin"
FT /id="PRO_0000396277"
FT CHAIN 685..760
FT /note="Ubiquitin"
FT /id="PRO_0000396278"
FT CHAIN 761..836
FT /note="Ubiquitin"
FT /id="PRO_0000396279"
FT PROPEP 837..838
FT /id="PRO_0000396280"
FT DOMAIN 1..76
FT /note="Ubiquitin-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00214"
FT DOMAIN 77..152
FT /note="Ubiquitin-like 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00214"
FT DOMAIN 153..228
FT /note="Ubiquitin-like 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00214"
FT DOMAIN 229..304
FT /note="Ubiquitin-like 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00214"
FT DOMAIN 305..380
FT /note="Ubiquitin-like 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00214"
FT DOMAIN 381..456
FT /note="Ubiquitin-like 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00214"
FT DOMAIN 457..532
FT /note="Ubiquitin-like 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00214"
FT DOMAIN 533..608
FT /note="Ubiquitin-like 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00214"
FT DOMAIN 609..684
FT /note="Ubiquitin-like 9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00214"
FT DOMAIN 685..760
FT /note="Ubiquitin-like 10"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00214"
FT DOMAIN 761..836
FT /note="Ubiquitin-like 11"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00214"
FT CROSSLNK 48
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250"
FT CROSSLNK 76
FT /note="Glycyl lysine isopeptide (Gly-Lys) (interchain with
FT K-? in acceptor proteins)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00214"
SQ SEQUENCE 838 AA; 93987 MW; 4CF0B1369DC312E6 CRC64;
MQIFVKTLTG KTITLEVEAS DTIENVKAKI QDKEGIPPDQ QRLIFAGKQL EDGRTLSDYN
IQKESTLHLV LRLRGGMQIF VKTLTGKTIT LEVEASDTIE NVKAKIQDKE GIPPDQQRLI
FAGKQLEDGR TLSDYNIQKE STLHLVLRLR GGMQIFVKTL TGKTITLEVE ASDTIENVKA
KIQDKEGIPP DQQRLIFAGK QLEDGRTLSD YNIQKESTLH LVLRLRGGMQ IFVKTLTGKT
ITLEVEASDT IENVKAKIQD KEGIPPDQQR LIFAGKQLED GRTLSDYNIQ KESTLHLVLR
LRGGMQIFVK TLTGKTITLE VEASDTIENV KAKIQDKEGI PPDQQRLIFA GKQLEDGRTL
SDYNIQKEST LHLVLRLRGG MQIFVKTLIG KTITLEVEAS DTIENVKAKI QDKEGIPPDQ
QRLIFAGKQL EDGRTLSDYN IQKESTLHLV LRLRGGMQIF VKTLTGKTIT LEVEASDTIE
NVKAKIQDKE GIPPDQQRLI FAGKQLEDGR TLSDYNIQKE STLHLVLRLR GGMQIFVKTL
TGKTITLEVE ASDTIENVKA KIQDKEGIPP DQQRLIFAGK QLEDGRTLSD YNIQKESTLH
LVLRLRGGMQ IFVKTLTGKT ITLEVEASDT IENVKAKIQD KEGIPPDQQR LIFAGKQLED
GRTLSDYNIQ KESTLHLVLR LRGGMQIFVK TLTGKTITLE VEASDTIENV KAKIQDKEGI
PPDQQRLIFA GKQLEDGRTL SDYNIQKEST LHLVLRLRGG MQIFVKTLTG KTITLEVEAS
DTIENVKAKI QDKEGIPPDQ QRLIFAGKQL EDGRTLSDYN IQKESTLHLV LRLRGGDI
