UBQ9_ARATH
ID UBQ9_ARATH Reviewed; 322 AA.
AC Q9FHQ6;
DT 10-AUG-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 25-MAY-2022, entry version 107.
DE RecName: Full=Polyubiquitin 9;
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 Flags: Precursor;
GN Name=UBQ9; OrderedLocusNames=At5g37640; ORFNames=K12B20.90;
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 [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=10470850; DOI=10.1093/dnares/6.3.183;
RA Kaneko T., Katoh T., Sato S., Nakamura Y., Asamizu E., Kotani H.,
RA Miyajima N., Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. IX. Sequence
RT features of the regions of 1,011,550 bp covered by seventeen P1 and TAC
RT clones.";
RL DNA Res. 6:183-195(1999).
RN [2]
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; AB018107; BAB08310.1; -; Genomic_DNA.
DR EMBL; CP002688; AED94213.1; -; Genomic_DNA.
DR PIR; S55244; S55244.
DR RefSeq; NP_568552.1; NM_123123.1.
DR AlphaFoldDB; Q9FHQ6; -.
DR SMR; Q9FHQ6; -.
DR BioGRID; 18993; 5.
DR STRING; 3702.AT5G37640.1; -.
DR PaxDb; Q9FHQ6; -.
DR PRIDE; Q9FHQ6; -.
DR EnsemblPlants; AT5G37640.1; AT5G37640.1; AT5G37640.
DR GeneID; 833742; -.
DR Gramene; AT5G37640.1; AT5G37640.1; AT5G37640.
DR KEGG; ath:AT5G37640; -.
DR Araport; AT5G37640; -.
DR TAIR; locus:2151774; AT5G37640.
DR eggNOG; KOG0001; Eukaryota.
DR HOGENOM; CLU_010412_7_0_1; -.
DR InParanoid; Q9FHQ6; -.
DR OrthoDB; 1536766at2759; -.
DR PhylomeDB; Q9FHQ6; -.
DR PRO; PR:Q9FHQ6; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q9FHQ6; baseline and differential.
DR Genevisible; Q9FHQ6; AT.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005730; C:nucleolus; 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:0009536; C:plastid; HDA:TAIR.
DR GO; GO:0003729; F:mRNA binding; IDA: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; IPR019954; Ubiquitin_CS.
DR InterPro; IPR019956; Ubiquitin_dom.
DR Pfam; PF00240; ubiquitin; 4.
DR PRINTS; PR00348; UBIQUITIN.
DR SMART; SM00213; UBQ; 4.
DR SUPFAM; SSF54236; SSF54236; 4.
DR PROSITE; PS00299; UBIQUITIN_1; 4.
DR PROSITE; PS50053; UBIQUITIN_2; 4.
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_0000396924"
FT CHAIN 79..154
FT /note="Ubiquitin-related 2"
FT /id="PRO_0000396925"
FT CHAIN 155..230
FT /note="Ubiquitin-related 3"
FT /id="PRO_0000396926"
FT CHAIN 231..307
FT /note="Ubiquitin-related 4"
FT /id="PRO_0000396927"
FT PROPEP 308..322
FT /evidence="ECO:0000305"
FT /id="PRO_0000396928"
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..230
FT /note="Ubiquitin-like 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00214"
FT DOMAIN 231..307
FT /note="Ubiquitin-like 4"
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 230
FT /note="Glycyl lysine isopeptide (Gly-Lys) (interchain with
FT K-? in acceptor proteins)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00214"
FT CROSSLNK 307
FT /note="Glycyl lysine isopeptide (Gly-Lys) (interchain with
FT K-? in acceptor proteins)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00214"
SQ SEQUENCE 322 AA; 36257 MW; 8E1D215E50085A99 CRC64;
MSMQIHAKTL TEKTITIDVV SSDTINNVKA KIQDIEGIPL DQQRLIFSGK LLDDGRTLAD
YSIQKDSILH LALRLRGGMQ IFVKTLTGKT ITLEVESSDT IDNVKAKIQD KEGVPPDQQR
LIFAGKQLDD GRTLADYNIQ KESTLHLVLR LRGGMQIFVR TLTRKTIALE VESSDTTDNV
KAKIQDKEGI PPDQQRLIFA GKQLEDGRTL ADYNIQKEST LHLVLRLCGG MQIFVNTLTG
KTITLEVESS DTIDNVKAKI QDKERIQPDQ QRLIFAGEQL EDGYYTLADY NIQKESTLHL
VLRLRGGECF GFIFLFLLCF NS
