UBQ8_ARATH
ID UBQ8_ARATH Reviewed; 631 AA.
AC Q39256;
DT 10-AUG-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 25-MAY-2022, entry version 118.
DE RecName: Full=Polyubiquitin 8;
DE Contains:
DE RecName: Full=Ubiquitin-related 1;
DE Contains:
DE RecName: Full=Ubiquitin-related 2;
DE Contains:
DE RecName: Full=Ubiquitin-related 3;
DE Contains:
DE RecName: Full=Ubiquitin-related 4;
DE Contains:
DE RecName: Full=Ubiquitin-related 5;
DE Contains:
DE RecName: Full=Ubiquitin-related 6;
DE Contains:
DE RecName: Full=Ubiquitin-related 7;
DE Contains:
DE RecName: Full=Ubiquitin-related 8;
DE Flags: Precursor;
GN Name=UBQ8; OrderedLocusNames=At3g09790; ORFNames=F11F8_38, F8A24.16;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=7713442; DOI=10.1093/genetics/139.2.921;
RA Callis J., Carpenter T., Sun C.W., Vierstra R.D.;
RT "Structure and evolution of genes encoding polyubiquitin and ubiquitin-like
RT proteins in Arabidopsis thaliana ecotype Columbia.";
RL Genetics 139:921-939(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130713; DOI=10.1038/35048706;
RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL Nature 408:820-822(2000).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
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-11-linked is involved in ERAD (endoplasmic reticulum-associated
CC degradation) and in cell-cycle regulation; Lys-29-linked is involved in
CC lysosomal degradation; Lys-33-linked is involved in kinase
CC modification; Lys-48-linked is involved in protein degradation via the
CC proteasome; Lys-63-linked is involved in endocytosis, and DNA-damage
CC responses. Linear polymer chains formed via attachment by the initiator
CC Met lead to cell signaling. Ubiquitin is usually conjugated to Lys
CC residues of target proteins, however, in rare cases, conjugation to Cys
CC or Ser residues has been observed. When polyubiquitin is free
CC (unanchored-polyubiquitin), it also has distinct roles, such as in
CC activation of protein kinases, and in signaling (By similarity).
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
CC -!- MISCELLANEOUS: Ubiquitin is encoded by 16 different genes. Ubiquitin is
CC generally synthesized as a polyubiquitin precursor with tandem head to
CC tail repeats. Often, there is one to three additional amino acids after
CC the last repeat, removed in the mature protein. Alternatively,
CC ubiquitin extension protein is synthesized as a single copy of
CC ubiquitin fused to a ribosomal protein (either L40 or S27A) or to a
CC ubiquitin-related protein (either RUB1 or RUB2). Following translation,
CC extension protein is cleaved from ubiquitin.
CC -!- SIMILARITY: Belongs to the ubiquitin family. {ECO:0000305}.
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DR EMBL; L05917; AAA68879.1; -; Genomic_DNA.
DR EMBL; AC015985; AAF23256.1; -; Genomic_DNA.
DR EMBL; AC016661; AAF23307.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE74813.1; -; Genomic_DNA.
DR EMBL; CP002686; ANM63421.1; -; Genomic_DNA.
DR PIR; S55243; S55243.
DR RefSeq; NP_001319513.1; NM_001337841.1.
DR RefSeq; NP_566357.1; NM_111814.2.
DR AlphaFoldDB; Q39256; -.
DR SMR; Q39256; -.
DR BioGRID; 5471; 2.
DR STRING; 3702.AT3G09790.1; -.
DR PaxDb; Q39256; -.
DR PRIDE; Q39256; -.
DR ProteomicsDB; 232996; -.
DR EnsemblPlants; AT3G09790.1; AT3G09790.1; AT3G09790.
DR EnsemblPlants; AT3G09790.2; AT3G09790.2; AT3G09790.
DR GeneID; 820137; -.
DR Gramene; AT3G09790.1; AT3G09790.1; AT3G09790.
DR Gramene; AT3G09790.2; AT3G09790.2; AT3G09790.
DR KEGG; ath:AT3G09790; -.
DR Araport; AT3G09790; -.
DR TAIR; locus:2074909; AT3G09790.
DR eggNOG; KOG0001; Eukaryota.
DR HOGENOM; CLU_010412_1_1_1; -.
DR InParanoid; Q39256; -.
DR OMA; HLTMQIF; -.
DR OrthoDB; 1536766at2759; -.
DR PhylomeDB; Q39256; -.
DR PRO; PR:Q39256; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q39256; baseline and differential.
DR Genevisible; Q39256; AT.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0009505; C:plant-type cell wall; HDA:TAIR.
DR GO; GO:0000325; C:plant-type vacuole; HDA:TAIR.
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 GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; ISS:TAIR.
DR InterPro; IPR000626; Ubiquitin-like_dom.
DR InterPro; IPR029071; Ubiquitin-like_domsf.
DR InterPro; IPR019956; Ubiquitin_dom.
DR Pfam; PF00240; ubiquitin; 8.
DR PRINTS; PR00348; UBIQUITIN.
DR SMART; SM00213; UBQ; 8.
DR SUPFAM; SSF54236; SSF54236; 8.
DR PROSITE; PS50053; UBIQUITIN_2; 8.
PE 3: Inferred from homology;
KW Cytoplasm; Isopeptide bond; Nucleus; Reference proteome; Repeat;
KW Ubl conjugation pathway.
FT CHAIN 1..78
FT /note="Ubiquitin-related 1"
FT /id="PRO_0000396915"
FT CHAIN 79..154
FT /note="Ubiquitin-related 2"
FT /id="PRO_0000396916"
FT CHAIN 155..237
FT /note="Ubiquitin-related 3"
FT /id="PRO_0000396917"
FT CHAIN 238..318
FT /note="Ubiquitin-related 4"
FT /id="PRO_0000396918"
FT CHAIN 319..392
FT /note="Ubiquitin-related 5"
FT /id="PRO_0000396919"
FT CHAIN 393..468
FT /note="Ubiquitin-related 6"
FT /id="PRO_0000396920"
FT CHAIN 469..551
FT /note="Ubiquitin-related 7"
FT /id="PRO_0000396921"
FT CHAIN 552..627
FT /note="Ubiquitin-related 8"
FT /id="PRO_0000396922"
FT PROPEP 628..631
FT /evidence="ECO:0000305"
FT /id="PRO_0000396923"
FT DOMAIN 3..78
FT /note="Ubiquitin-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00214"
FT DOMAIN 79..154
FT /note="Ubiquitin-like 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00214"
FT DOMAIN 155..237
FT /note="Ubiquitin-like 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00214"
FT DOMAIN 238..318
FT /note="Ubiquitin-like 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00214"
FT DOMAIN 319..392
FT /note="Ubiquitin-like 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00214"
FT DOMAIN 393..468
FT /note="Ubiquitin-like 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00214"
FT DOMAIN 469..551
FT /note="Ubiquitin-like 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00214"
FT DOMAIN 552..627
FT /note="Ubiquitin-like 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00214"
FT CROSSLNK 78
FT /note="Glycyl lysine isopeptide (Gly-Lys) (interchain with
FT K-? in acceptor proteins)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00214"
FT CROSSLNK 154
FT /note="Glycyl lysine isopeptide (Gly-Lys) (interchain with
FT K-? in acceptor proteins)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00214"
FT CROSSLNK 551
FT /note="Glycyl lysine isopeptide (Gly-Lys) (interchain with
FT K-? in acceptor proteins)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00214"
SQ SEQUENCE 631 AA; 71769 MW; F9552A7065689D6F CRC64;
MTIQIYAKTL TEKTITLDVE TSDSIHNVKA KIQNKEGIPL DQQRLIFAGK QLEDGLTLAD
YNIQKESTLH LVLRLRGGMQ IFVQTLTGKT ITLEVKSSDT IDNVKAKIQD KEGILPRQQR
LIFAGKQLED GRTLADYNIQ KESTLHLVLR LCGGMQIFVS TFSGKNFTSD TLTLKVESSD
TIENVKAKIQ DREGLRPDHQ RLIFHGEELF TEDNRTLADY GIRNRSTLCL ALRLRGDMYI
FVKNLPYNSF TGENFILEVE SSDTIDNVKA KLQDKERIPM DLHRLIFAGK PLEGGRTLAH
YNIQKGSTLY LVTRFRCGMQ IFVKTLTRKR INLEVESWDT IENVKAMVQD KEGIQPQPNL
QRLIFLGKEL KDGCTLADYS IQKESTLHLV LGMQIFVKLF GGKIITLEVL SSDTIKSVKA
KIQDKVGSPP DQQILLFRGG QLQDGRTLGD YNIRNESTLH LFFHIRHGMQ IFVKTFSFSG
ETPTCKTITL EVESSDTIDN VKVKIQHKVG IPLDRQRLIF GGRVLVGSRT LLDYNIQKGS
TIHQLFLQRG GMQIFIKTLT GKTIILEVES SDTIANVKEK IQVKEGIKPD QQMLIFFGQQ
LEDGVTLGDY DIHKKSTLYL VLRLRQRRYD F
