ID   R27AB_ARATH             Reviewed;         157 AA.
AC   P59232; O80715; P19233; P59263; Q38875; Q9LDJ2; Q9LYW1; Q9M0W3; Q9M1P9;
AC   Q9S7X3;
DT   01-FEB-2003, integrated into UniProtKB/Swiss-Prot.
DT   10-AUG-2010, sequence version 2.
DT   02-SEP-2026, entry version 157.
DE   RecName: Full=Ubiquitin-ribosomal protein eS31y fusion protein {ECO:0000305};
DE   Contains:
DE     RecName: Full=Ubiquitin;
DE   Contains:
DE     RecName: Full=Small ribosomal subunit protein eS31y {ECO:0000303|PubMed:36423343};
DE     AltName: Full=40S ribosomal protein S27a-2;
DE   Flags: Precursor;
GN   Name=RPS27AB; Synonyms=UBQ6; OrderedLocusNames=At2g47110;
GN   ORFNames=F14M4.6;
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=2165066; DOI=10.1016/s0021-9258(19)38372-3;
RA   Callis J., Raasch J.A., Vierstra R.D.;
RT   "Ubiquitin extension proteins of Arabidopsis thaliana. Structure,
RT   localization, and expression of their promoters in transgenic tobacco.";
RL   J. Biol. Chem. 265:12486-12493(1990).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=10617197; DOI=10.1038/45471;
RA   Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA   Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA   Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA   Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA   Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA   Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA   Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT   "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL   Nature 402:761-768(1999).
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).
RN   [4]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Columbia;
RG   The Arabidopsis Information Resource (TAIR);
RT   "Community-consensus reference genome of Arabidopsis thaliana Col-0.";
RL   Submitted (FEB-2026) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=14593172; DOI=10.1126/science.1088305;
RA   Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA   Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA   Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA   Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA   Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA   Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA   Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA   Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA   Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA   Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA   Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA   Ecker J.R.;
RT   "Empirical analysis of transcriptional activity in the Arabidopsis
RT   genome.";
RL   Science 302:842-846(2003).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA   Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA   Feldmann K.A.;
RT   "Full-length cDNA from Arabidopsis thaliana.";
RL   Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN   [7]
RP   GENE FAMILY ORGANIZATION, AND NOMENCLATURE.
RX   PubMed=11598216; DOI=10.1104/pp.127.2.398;
RA   Barakat A., Szick-Miranda K., Chang I.-F., Guyot R., Blanc G., Cooke R.,
RA   Delseny M., Bailey-Serres J.;
RT   "The organization of cytoplasmic ribosomal protein genes in the Arabidopsis
RT   genome.";
RL   Plant Physiol. 127:398-415(2001).
RN   [8]
RP   NOMENCLATURE.
RX   PubMed=36423343; DOI=10.1093/plcell/koac333;
RA   Scarpin M.R., Busche M., Martinez R.E., Harper L.C., Reiser L.,
RA   Szakonyi D., Merchante C., Lan T., Xiong W., Mo B., Tang G., Chen X.,
RA   Bailey-Serres J., Browning K.S., Brunkard J.O.;
RT   "An updated nomenclature for plant ribosomal protein genes.";
RL   Plant Cell 35:640-643(2023).
CC   -!- FUNCTION: [Ubiquitin]: Ubiquitin exists either covalently attached to
CC       another protein, or free (unanchored). When covalently bound, it is
CC       conjugated to target proteins via an isopeptide bond either as a
CC       monomer (monoubiquitin), a polymer linked via different Lys residues of
CC       the 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   -!- FUNCTION: [Small ribosomal subunit protein eS31y]: Component of the 40S
CC       subunit of the ribosome.
CC   -!- SUBUNIT: [Small ribosomal subunit protein eS31y]: Part of the 40S
CC       ribosomal subunit. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: [Ubiquitin]: Cytoplasm {ECO:0000250}. Nucleus
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: [Small ribosomal subunit protein eS31y]:
CC       Cytoplasm {ECO:0000305}.
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 are one to three additional amino acids
CC       after 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 eL40 or eS31) or to a
CC       ubiquitin-related protein (either RUB1 or RUB2). Following translation,
CC       extension protein is cleaved from ubiquitin.
CC   -!- SIMILARITY: In the N-terminal section; belongs to the ubiquitin family.
CC       {ECO:0000305}.
CC   -!- SIMILARITY: In the C-terminal section; belongs to the eukaryotic
CC       ribosomal protein eS31 family. {ECO:0000305}.
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DR   EMBL; J05540; AAA32907.1; -; Genomic_DNA.
DR   EMBL; AC004411; AAC34235.1; -; Genomic_DNA.
DR   EMBL; CP002685; AEC10801.1; -; Genomic_DNA.
DR   EMBL; CP002685; AEC10802.1; -; Genomic_DNA.
DR   EMBL; OZ408684; CAO7039047.1; -; Genomic_DNA.
DR   EMBL; AF375416; AAK53000.1; -; mRNA.
DR   EMBL; AY142033; AAM98297.1; -; mRNA.
DR   EMBL; AY143810; AAN28749.1; -; mRNA.
DR   EMBL; AY088370; AAM65909.1; -; mRNA.
DR   PIR; D36571; D36571.
DR   RefSeq; NP_001189768.1; NM_001202839.1.
DR   RefSeq; NP_566095.1; NM_130278.3.
DR   AlphaFoldDB; P59232; -.
DR   SMR; P59232; -.
DR   BioGRID; 4658; 6.
DR   FunCoup; P59232; 1050.
DR   IntAct; P59232; 2.
DR   STRING; 3702.P59232; -.
DR   iPTMnet; P59232; -.
DR   PaxDb; 3702-P59232; -.
DR   ProteomicsDB; 226095; -.
DR   GeneID; 819323; -.
DR   KEGG; ath:AT2G47110; -.
DR   Araport; AT2G47110; -.
DR   TAIR; AT2G47110; UBQ6.
DR   eggNOG; KOG0004; Eukaryota.
DR   HOGENOM; CLU_010412_2_0_1; -.
DR   InParanoid; P59232; -.
DR   OMA; GVFMAFH; -.
DR   OrthoDB; 1082030at2759; -.
DR   PRO; PR:P59232; -.
DR   Proteomes; UP000006548; Chromosome 2.
DR   ExpressionAtlas; P59232; baseline and differential.
DR   GO; GO:0005829; C:cytosol; HDA:TAIR.
DR   GO; GO:0022626; C:cytosolic ribosome; IBA:GO_Central.
DR   GO; GO:0022627; C:cytosolic small ribosomal subunit; HDA:TAIR.
DR   GO; GO:0005794; C:Golgi apparatus; HDA:TAIR.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0003729; F:mRNA binding; IDA:TAIR.
DR   GO; GO:0031386; F:protein tag activity; IBA:GO_Central.
DR   GO; GO:0003735; F:structural constituent of ribosome; IDA:CAFA.
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:0006412; P:translation; IEA:InterPro.
DR   GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; ISS:TAIR.
DR   CDD; cd01803; Ubl_ubiquitin; 1.
DR   FunFam; 3.10.20.90:FF:000008; Ubiquitin-40S ribosomal protein S27a; 1.
DR   Gene3D; 6.20.50.150; -; 1.
DR   Gene3D; 3.10.20.90; Phosphatidylinositol 3-kinase Catalytic Subunit, Chain A, domain 1; 1.
DR   InterPro; IPR002906; Ribosomal_eS31.
DR   InterPro; IPR038582; Ribosomal_eS31_euk_sf.
DR   InterPro; IPR011332; Ribosomal_zn-bd.
DR   InterPro; IPR000626; Ubiquitin-like_dom.
DR   InterPro; IPR029071; Ubiquitin-like_domsf.
DR   InterPro; IPR019954; Ubiquitin_CS.
DR   InterPro; IPR019956; Ubiquitin_dom.
DR   InterPro; IPR050158; Ubiquitin_ubiquitin-like.
DR   PANTHER; PTHR10666; UBIQUITIN; 1.
DR   Pfam; PF01599; Ribosomal_S27; 1.
DR   Pfam; PF00240; ubiquitin; 1.
DR   PRINTS; PR00348; UBIQUITIN.
DR   SMART; SM01402; Ribosomal_S27; 1.
DR   SMART; SM00213; UBQ; 1.
DR   SUPFAM; SSF54236; Ubiquitin-like; 1.
DR   SUPFAM; SSF57829; Zn-binding ribosomal proteins; 1.
DR   PROSITE; PS00299; UBIQUITIN_1; 1.
DR   PROSITE; PS50053; UBIQUITIN_2; 1.
PE   2: Evidence at transcript level;
KW   Cytoplasm; Isopeptide bond; Metal-binding; Nucleus; Reference proteome;
KW   Ribonucleoprotein; Ribosomal protein; Zinc; Zinc-finger.
FT   CHAIN           1..76
FT                   /note="Ubiquitin"
FT                   /id="PRO_0000396872"
FT   CHAIN           77..157
FT                   /note="Small ribosomal subunit protein eS31y"
FT                   /id="PRO_0000137675"
FT   DOMAIN          1..76
FT                   /note="Ubiquitin-like"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00214"
FT   ZN_FING         121..144
FT                   /note="C4-type"
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   157 AA;  17812 MW;  AE3B7797763FD558 CRC64;
     MQIFVKTLTG KTITLEVESS DTIDNVKAKI QDKEGIPPDQ QRLIFAGKQL EDGRTLADYN
     IQKESTLHLV LRLRGGAKKR KKKTYTKPKK IKHKHKKVKL AVLQFYKVDG SGKVQRLRKE
     CPNATCGAGT FMASHFDRHY CGKCGLTYVY QKEGAQE
//