UBIQF_DICDI
ID UBIQF_DICDI Reviewed; 533 AA.
AC P0CG78; P08618; Q54HH5; Q54L38; Q54SE1; Q54SP3; Q54UW7; Q54WJ3; Q550W7;
AC Q55DZ5; Q86KQ4;
DT 10-AUG-2010, integrated into UniProtKB/Swiss-Prot.
DT 10-AUG-2010, sequence version 1.
DT 03-AUG-2022, entry version 61.
DE RecName: Full=Polyubiquitin-F;
DE Contains:
DE RecName: Full=Ubiquitin;
DE Flags: Precursor;
GN Name=ubqF; ORFNames=DDB_G0289449;
OS Dictyostelium discoideum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=2548604; DOI=10.1021/bi00438a046;
RA Ohmachi T., Giorda R., Shaw D.R., Ennis H.L.;
RT "Molecular organization of developmentally regulated Dictyostelium
RT discoideum ubiquitin cDNAs.";
RL Biochemistry 28:5226-5231(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4;
RX PubMed=15875012; DOI=10.1038/nature03481;
RA Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT "The genome of the social amoeba Dictyostelium discoideum.";
RL Nature 435:43-57(2005).
RN [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=16512674; DOI=10.1021/pr050350q;
RA Reinders Y., Schulz I., Graef R., Sickmann A.;
RT "Identification of novel centrosomal proteins in Dictyostelium discoideum
RT by comparative proteomic approaches.";
RL J. Proteome Res. 5:589-598(2006).
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: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
CC -!- MISCELLANEOUS: Ubiquitin is synthesized as a polyubiquitin precursor
CC with exact head to tail repeats. Some ubiquitin genes contain a single
CC copy of ubiquitin fused to a ribosomal protein. In D.discoideum there
CC are 9 genes: ubqA: 5 copies of Ub and a final Asn; ubqB: 1 copy of Ub
CC and ribosomal protein L40; ubqC: 1 copy of Ub and ribosomal protein
CC S27A; ubqD: 3 copies of Ub and a final Leu; ubqF: 7 copies of Ub and a
CC final Asn; ubqG: 5 copies of Ub and a final Leu; ubqH: 5 copies of Ub
CC and a final Asn; ubqI: 4 copies of Ub and a final Asn; ubqJ: 4 copies
CC of Ub and a final Asn.
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; M23753; AAA33267.1; -; mRNA.
DR EMBL; AAFI02000141; EAL62704.1; -; Genomic_DNA.
DR PIR; A34080; A34080.
DR RefSeq; XP_636210.1; XM_631118.1.
DR AlphaFoldDB; P0CG78; -.
DR SMR; P0CG78; -.
DR STRING; 44689.DDB0201651; -.
DR PaxDb; P0CG78; -.
DR EnsemblProtists; EAL62704; EAL62704; DDB_G0289449.
DR GeneID; 8627148; -.
DR KEGG; ddi:DDB_G0289449; -.
DR dictyBase; DDB_G0289449; ubqF.
DR eggNOG; KOG0001; Eukaryota.
DR HOGENOM; CLU_010412_1_2_1; -.
DR InParanoid; P0CG78; -.
DR OMA; FESAVMQ; -.
DR PhylomeDB; P0CG78; -.
DR Reactome; R-DDI-156827; L13a-mediated translational silencing of Ceruloplasmin expression.
DR Reactome; R-DDI-174048; APC/C:Cdc20 mediated degradation of Cyclin B.
DR Reactome; R-DDI-174084; Autodegradation of Cdh1 by Cdh1:APC/C.
DR Reactome; R-DDI-174113; SCF-beta-TrCP mediated degradation of Emi1.
DR Reactome; R-DDI-174154; APC/C:Cdc20 mediated degradation of Securin.
DR Reactome; R-DDI-174178; APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1.
DR Reactome; R-DDI-174184; Cdc20:Phospho-APC/C mediated degradation of Cyclin A.
DR Reactome; R-DDI-179409; APC-Cdc20 mediated degradation of Nek2A.
DR Reactome; R-DDI-1799339; SRP-dependent cotranslational protein targeting to membrane.
DR Reactome; R-DDI-187577; SCF(Skp2)-mediated degradation of p27/p21.
DR Reactome; R-DDI-2467813; Separation of Sister Chromatids.
DR Reactome; R-DDI-2559582; Senescence-Associated Secretory Phenotype (SASP).
DR Reactome; R-DDI-349425; Autodegradation of the E3 ubiquitin ligase COP1.
DR Reactome; R-DDI-450302; activated TAK1 mediates p38 MAPK activation.
DR Reactome; R-DDI-450321; JNK (c-Jun kinases) phosphorylation and activation mediated by activated human TAK1.
DR Reactome; R-DDI-4641258; Degradation of DVL.
DR Reactome; R-DDI-532668; N-glycan trimming in the ER and Calnexin/Calreticulin cycle.
DR Reactome; R-DDI-5632684; Hedgehog 'on' state.
DR Reactome; R-DDI-5656169; Termination of translesion DNA synthesis.
DR Reactome; R-DDI-5658442; Regulation of RAS by GAPs.
DR Reactome; R-DDI-5675221; Negative regulation of MAPK pathway.
DR Reactome; R-DDI-5687128; MAPK6/MAPK4 signaling.
DR Reactome; R-DDI-5689603; UCH proteinases.
DR Reactome; R-DDI-5689877; Josephin domain DUBs.
DR Reactome; R-DDI-5689880; Ub-specific processing proteases.
DR Reactome; R-DDI-5689901; Metalloprotease DUBs.
DR Reactome; R-DDI-5696394; DNA Damage Recognition in GG-NER.
DR Reactome; R-DDI-5696395; Formation of Incision Complex in GG-NER.
DR Reactome; R-DDI-6781823; Formation of TC-NER Pre-Incision Complex.
DR Reactome; R-DDI-6782135; Dual incision in TC-NER.
DR Reactome; R-DDI-6782210; Gap-filling DNA repair synthesis and ligation in TC-NER.
DR Reactome; R-DDI-6791226; Major pathway of rRNA processing in the nucleolus and cytosol.
DR Reactome; R-DDI-68949; Orc1 removal from chromatin.
DR Reactome; R-DDI-69017; CDK-mediated phosphorylation and removal of Cdc6.
DR Reactome; R-DDI-69231; Cyclin D associated events in G1.
DR Reactome; R-DDI-69601; Ubiquitin Mediated Degradation of Phosphorylated Cdc25A.
DR Reactome; R-DDI-72689; Formation of a pool of free 40S subunits.
DR Reactome; R-DDI-72695; Formation of the ternary complex, and subsequently, the 43S complex.
DR Reactome; R-DDI-72702; Ribosomal scanning and start codon recognition.
DR Reactome; R-DDI-72706; GTP hydrolysis and joining of the 60S ribosomal subunit.
DR Reactome; R-DDI-75815; Ubiquitin-dependent degradation of Cyclin D.
DR Reactome; R-DDI-8854050; FBXL7 down-regulates AURKA during mitotic entry and in early mitosis.
DR Reactome; R-DDI-8866652; Synthesis of active ubiquitin: roles of E1 and E2 enzymes.
DR Reactome; R-DDI-8866654; E3 ubiquitin ligases ubiquitinate target proteins.
DR Reactome; R-DDI-8948747; Regulation of PTEN localization.
DR Reactome; R-DDI-8948751; Regulation of PTEN stability and activity.
DR Reactome; R-DDI-8951664; Neddylation.
DR Reactome; R-DDI-901032; ER Quality Control Compartment (ERQC).
DR Reactome; R-DDI-9020702; Interleukin-1 signaling.
DR Reactome; R-DDI-9033241; Peroxisomal protein import.
DR Reactome; R-DDI-917729; Endosomal Sorting Complex Required For Transport (ESCRT).
DR Reactome; R-DDI-917937; Iron uptake and transport.
DR Reactome; R-DDI-936440; Negative regulators of DDX58/IFIH1 signaling.
DR Reactome; R-DDI-937042; IRAK2 mediated activation of TAK1 complex.
DR Reactome; R-DDI-937072; TRAF6-mediated induction of TAK1 complex within TLR4 complex.
DR Reactome; R-DDI-9646399; Aggrephagy.
DR Reactome; R-DDI-9664873; Pexophagy.
DR Reactome; R-DDI-975163; IRAK2 mediated activation of TAK1 complex upon TLR7/8 or 9 stimulation.
DR Reactome; R-DDI-9755511; KEAP1-NFE2L2 pathway.
DR Reactome; R-DDI-975956; Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC).
DR Reactome; R-DDI-975957; Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).
DR Reactome; R-DDI-9762114; GSK3B and BTRC:CUL1-mediated-degradation of NFE2L2.
DR Reactome; R-DDI-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR PRO; PR:P0CG78; -.
DR Proteomes; UP000002195; Chromosome 5.
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:0016567; P:protein ubiquitination; IBA:GO_Central.
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; 7.
DR PRINTS; PR00348; UBIQUITIN.
DR SMART; SM00213; UBQ; 7.
DR SUPFAM; SSF54236; SSF54236; 7.
DR PROSITE; PS00299; UBIQUITIN_1; 7.
DR PROSITE; PS50053; UBIQUITIN_2; 7.
PE 1: Evidence at protein level;
KW Cytoplasm; Isopeptide bond; Nucleus; Reference proteome; Repeat;
KW Ubl conjugation.
FT CHAIN 1..76
FT /note="Ubiquitin"
FT /id="PRO_0000396321"
FT CHAIN 77..152
FT /note="Ubiquitin"
FT /id="PRO_0000396322"
FT CHAIN 153..228
FT /note="Ubiquitin"
FT /id="PRO_0000396323"
FT CHAIN 229..304
FT /note="Ubiquitin"
FT /id="PRO_0000396324"
FT CHAIN 305..380
FT /note="Ubiquitin"
FT /id="PRO_0000396325"
FT CHAIN 381..456
FT /note="Ubiquitin"
FT /id="PRO_0000396326"
FT CHAIN 457..532
FT /note="Ubiquitin"
FT /id="PRO_0000396327"
FT PROPEP 533
FT /id="PRO_0000396328"
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 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 533 AA; 59770 MW; 86BCCCD5679DAE1F CRC64;
MQIFVKTLTG KTITLEVEGS DNIENVKAKI QDKEGIPPDQ QRLIFAGKQL EDGRTLSDYN
IQKESTLHLV LRLRGGMQIF VKTLTGKTIT LEVEGSDNIE NVKAKIQDKE GIPPDQQRLI
FAGKQLEDGR TLSDYNIQKE STLHLVLRLR GGMQIFVKTL TGKTITLEVE GSDNIENVKA
KIQDKEGIPP DQQRLIFAGK QLEDGRTLSD YNIQKESTLH LVLRLRGGMQ IFVKTLTGKT
ITLEVEGSDN IENVKAKIQD KEGIPPDQQR LIFAGKQLED GRTLSDYNIQ KESTLHLVLR
LRGGMQIFVK TLTGKTITLE VEGSDNIENV KAKIQDKEGI PPDQQRLIFA GKQLEDGRTL
SDYNIQKEST LHLVLRLRGG MQIFVKTLTG KTITLEVEGS DNIENVKAKI QDKEGIPPDQ
QRLIFAGKQL EDGRTLSDYN IQKESTLHLV LRLRGGMQIF VKTLTGKTIT LEVEGSDNIE
NVKAKIQDKE GIPPDQQRLI FAGKQLEDGR TLSDYNIQKE STLHLVLRLR GGN
