ID R27AA_ARATH Reviewed; 156 AA.
AC P59271; O80715; P59263; Q29PZ3; Q38875; Q9LDJ2; Q9LYW1; Q9M0W3; Q9M1P9;
AC Q9S7X3;
DT 01-FEB-2003, integrated into UniProtKB/Swiss-Prot.
DT 10-AUG-2010, sequence version 2.
DT 27-MAR-2024, entry version 145.
DE RecName: Full=Ubiquitin-ribosomal protein eS31z fusion protein {ECO:0000305};
DE Contains:
DE RecName: Full=Ubiquitin;
DE Contains:
DE RecName: Full=Small ribosomal subunit protein eS31z {ECO:0000303|PubMed:36423343};
DE AltName: Full=40S ribosomal protein S27a-1;
DE Flags: Precursor;
GN Name=RPS27AA; Synonyms=UBQ16; OrderedLocusNames=At1g23410;
GN ORFNames=F26F24.28, F28C11.5;
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=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(2000).
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).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RA Shinn P., Chen H., Kim C.J., Ecker J.R.;
RT "Arabidopsis ORF clones.";
RL Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases.
RN [4]
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 [5]
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 [6]
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 eS31z]: Component of the 40S
CC subunit of the ribosome.
CC -!- SUBUNIT: [Small ribosomal subunit protein eS31z]: 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 eS31z]:
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; AC005292; AAF87001.1; -; Genomic_DNA.
DR EMBL; AC007945; AAF79581.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE30384.1; -; Genomic_DNA.
DR EMBL; BT024763; ABD59101.1; -; mRNA.
DR EMBL; AY085389; AAM62617.1; -; mRNA.
DR PIR; H86367; H86367.
DR RefSeq; NP_173755.1; NM_102190.3.
DR AlphaFoldDB; P59271; -.
DR SMR; P59271; -.
DR BioGRID; 24188; 11.
DR IntAct; P59271; 6.
DR STRING; 3702.P59271; -.
DR iPTMnet; P59271; -.
DR MetOSite; P59271; -.
DR PaxDb; 3702-AT1G23410-1; -.
DR ProteomicsDB; 236482; -.
DR EnsemblPlants; AT1G23410.1; AT1G23410.1; AT1G23410.
DR GeneID; 838949; -.
DR Gramene; AT1G23410.1; AT1G23410.1; AT1G23410.
DR KEGG; ath:AT1G23410; -.
DR Araport; AT1G23410; -.
DR TAIR; AT1G23410; -.
DR eggNOG; KOG0004; Eukaryota.
DR HOGENOM; CLU_010412_2_0_1; -.
DR InParanoid; P59271; -.
DR OMA; HYCDKCC; -.
DR OrthoDB; 312211at2759; -.
DR PRO; PR:P59271; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; P59271; differential.
DR Genevisible; P59271; AT.
DR GO; GO:0005829; C:cytosol; HDA:TAIR.
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; HDA:TAIR.
DR GO; GO:0009506; C:plasmodesma; HDA:TAIR.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0003729; F:mRNA binding; IDA:TAIR.
DR GO; GO:0003735; F:structural constituent of ribosome; IDA:CAFA.
DR GO; GO:0006412; P:translation; IEA:InterPro.
DR CDD; cd01803; Ubl_ubiquitin; 1.
DR Gene3D; 6.20.50.150; -; 1.
DR InterPro; IPR002906; Ribosomal_eS31.
DR InterPro; IPR038582; Ribosomal_eS31_euk-type_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 PANTHER; PTHR10666; UBIQUITIN; 1.
DR PANTHER; PTHR10666:SF513; UBIQUITIN-40S RIBOSOMAL PROTEIN S27A-1; 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_0000396871"
FT CHAIN 77..156
FT /note="Small ribosomal subunit protein eS31z"
FT /id="PRO_0000137674"
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 156 AA; 17672 MW; 95FBD9561FD1A25E CRC64;
MQIFVKTLTG KTITLEVESS DTIDNVKAKI QDKEGIPPDQ QRLIFAGKQL EDGRTLADYN
IQKESTLHLV LRLRGGAKKR KKKTYTKPKK IKHTHKKVKL AVLQFYKVDG SGKVQRLKKE
CPSVSCGPGT FMASHFDRHY CGKCGTTYVF KKADEE
//
