(data stored in ACNUC16935 zone)

SWISSPROT: R27AA_ARATH

ID   R27AA_ARATH             Reviewed;         156 AA.
AC   P59271; O80715; P59263; Q29PZ3; Q38875; Q9LDJ2; Q9LYW1; Q9M0W3;
AC   Q9M1P9; Q9S7X3;
DT   01-FEB-2003, integrated into UniProtKB/Swiss-Prot.
DT   10-AUG-2010, sequence version 2.
DT   30-AUG-2017, entry version 112.
DE   RecName: Full=Ubiquitin-40S ribosomal protein S27a-1;
DE   Contains:
DE     RecName: Full=Ubiquitin;
DE   Contains:
DE     RecName: 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; Magnoliophyta; eudicotyledons; Gunneridae;
OC   Pentapetalae; rosids; malvids; Brassicales; Brassicaceae; Camelineae;
OC   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.,
RA   White O., Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y.,
RA   Buehler E., Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W.,
RA   Chung M.K., Conn L., Conway A.B., Conway A.R., Creasy T.H., Dewar K.,
RA   Dunn P., Etgu P., Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y.,
RA   Gill J.E., Goldsmith A.D., Haas B., Hansen N.F., Hughes B., Huizar L.,
RA   Hunter J.L., Jenkins J., Johnson-Hopson C., Khan S., Khaykin E.,
RA   Kim C.J., Koo H.L., Kremenetskaia I., Kurtz D.B., Kwan A., Lam B.,
RA   Langin-Hooper S., Lee A., Lee J.M., Lenz C.A., Li J.H., Li Y.-P.,
RA   Lin X., Liu S.X., Liu Z.A., Luros J.S., Maiti R., Marziali A.,
RA   Militscher J., Miranda M., Nguyen M., Nierman W.C., Osborne B.I.,
RA   Pai G., Peterson J., Pham P.K., Rizzo M., Rooney T., Rowley D.,
RA   Sakano H., Salzberg S.L., Schwartz J.R., Shinn P., Southwick A.M.,
RA   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.,
RA   Wu D., Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT   "Sequence and analysis of chromosome 1 of the plant Arabidopsis
RT   thaliana.";
RL   Nature 408:816-820(2000).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Columbia;
RG   The Arabidopsis Information Portal (Araport);
RL   Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
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.,
RA   Cooke R., Delseny M., Bailey-Serres J.;
RT   "The organization of cytoplasmic ribosomal protein genes in the
RT   Arabidopsis genome.";
RL   Plant Physiol. 127:398-415(2001).
CC   -!- FUNCTION: Ubiquitin exists either covalently attached to another
CC       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
CC       residues of the ubiquitin (polyubiquitin chains) or a linear
CC       polymer linked via the initiator Met of the ubiquitin (linear
CC       polyubiquitin chains). Polyubiquitin chains, when attached to a
CC       target protein, have different functions depending on the Lys
CC       residue of the ubiquitin that is linked: Lys-11-linked is involved
CC       in ERAD (endoplasmic reticulum-associated degradation) and in
CC       cell-cycle regulation; Lys-29-linked is involved in lysosomal
CC       degradation; Lys-33-linked is involved in kinase modification;
CC       Lys-48-linked is involved in protein degradation via the
CC       proteasome; Lys-63-linked is involved in endocytosis, and DNA-
CC       damage responses. Linear polymer chains formed via attachment by
CC       the initiator Met lead to cell signaling. Ubiquitin is usually
CC       conjugated to Lys residues of target proteins, however, in rare
CC       cases, conjugation to Cys or Ser residues has been observed. When
CC       polyubiquitin is free (unanchored-polyubiquitin), it also has
CC       distinct roles, such as in activation of protein kinases, and in
CC       signaling (By similarity). {ECO:0000250}.
CC   -!- FUNCTION: Ribosomal protein RSP27a-1 is a component of the 40S
CC       subunit of the ribosome.
CC   -!- SUBUNIT: Ribosomal protein RSP27a-1 is part of the 40S ribosomal
CC       subunit. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Ubiquitin: Cytoplasm {ECO:0000250}. Nucleus
CC       {ECO:0000250}.
CC   -!- MISCELLANEOUS: Ubiquitin is encoded by 16 different genes.
CC       Ubiquitin is generally synthesized as a polyubiquitin precursor
CC       with tandem head to tail repeats. Often, there is one to three
CC       additional amino acids after the last repeat, removed in the
CC       mature protein. Alternatively, ubiquitin extension protein is
CC       synthesized as a single copy of ubiquitin fused to a ribosomal
CC       protein (either L40 or S27A) or to a ubiquitin-related protein
CC       (either RUB1 or RUB2). Following translation, extension protein is
CC       cleaved from ubiquitin.
CC   -!- SIMILARITY: In the N-terminal section; belongs to the ubiquitin
CC       family. {ECO:0000305}.
CC   -!- SIMILARITY: In the C-terminal section; belongs to the eukaryotic
CC       ribosomal protein eS31 family. {ECO:0000305}.
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   UniGene; At.41552; -.
DR   ProteinModelPortal; P59271; -.
DR   SMR; P59271; -.
DR   BioGrid; 24188; 7.
DR   IntAct; P59271; 6.
DR   STRING; 3702.AT1G23410.1; -.
DR   iPTMnet; P59271; -.
DR   PaxDb; P59271; -.
DR   PRIDE; P59271; -.
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; locus:2028005; AT1G23410.
DR   eggNOG; ENOG410ITMZ; Eukaryota.
DR   eggNOG; COG1998; LUCA.
DR   InParanoid; P59271; -.
DR   KO; K02977; -.
DR   OMA; YCKVDEN; -.
DR   OrthoDB; EOG09360S3F; -.
DR   Reactome; R-ATH-110312; Translesion synthesis by REV1.
DR   Reactome; R-ATH-110314; Recognition of DNA damage by PCNA-containing replication complex.
DR   Reactome; R-ATH-110320; Translesion Synthesis by POLH.
DR   Reactome; R-ATH-174184; Cdc20:Phospho-APC/C mediated degradation of Cyclin A.
DR   Reactome; R-ATH-349425; Autodegradation of the E3 ubiquitin ligase COP1.
DR   Reactome; R-ATH-382556; ABC-family proteins mediated transport.
DR   Reactome; R-ATH-446652; Interleukin-1 signaling.
DR   Reactome; R-ATH-450302; activated TAK1 mediates p38 MAPK activation.
DR   Reactome; R-ATH-450321; JNK (c-Jun kinases) phosphorylation and activation mediated by activated human TAK1.
DR   Reactome; R-ATH-532668; N-glycan trimming in the ER and Calnexin/Calreticulin cycle.
DR   Reactome; R-ATH-5358346; Hedgehog ligand biogenesis.
DR   Reactome; R-ATH-5632684; Hedgehog 'on' state.
DR   Reactome; R-ATH-5655862; Translesion synthesis by POLK.
DR   Reactome; R-ATH-5656121; Translesion synthesis by POLI.
DR   Reactome; R-ATH-5656169; Termination of translesion DNA synthesis.
DR   Reactome; R-ATH-5687128; MAPK6/MAPK4 signaling.
DR   Reactome; R-ATH-5689603; UCH proteinases.
DR   Reactome; R-ATH-5689877; Josephin domain DUBs.
DR   Reactome; R-ATH-5689880; Ub-specific processing proteases.
DR   Reactome; R-ATH-5689901; Metalloprotease DUBs.
DR   Reactome; R-ATH-5693565; Recruitment and ATM-mediated phosphorylation of repair and signaling proteins at DNA double strand breaks.
DR   Reactome; R-ATH-5696394; DNA Damage Recognition in GG-NER.
DR   Reactome; R-ATH-5696395; Formation of Incision Complex in GG-NER.
DR   Reactome; R-ATH-5696397; Gap-filling DNA repair synthesis and ligation in GG-NER.
DR   Reactome; R-ATH-5696400; Dual Incision in GG-NER.
DR   Reactome; R-ATH-6781823; Formation of TC-NER Pre-Incision Complex.
DR   Reactome; R-ATH-6782135; Dual incision in TC-NER.
DR   Reactome; R-ATH-6782210; Gap-filling DNA repair synthesis and ligation in TC-NER.
DR   Reactome; R-ATH-68949; Orc1 removal from chromatin.
DR   Reactome; R-ATH-69017; CDK-mediated phosphorylation and removal of Cdc6.
DR   Reactome; R-ATH-69229; Ubiquitin-dependent degradation of Cyclin D1.
DR   Reactome; R-ATH-69231; Cyclin D associated events in G1.
DR   Reactome; R-ATH-8854050; FBXL7 down-regulates AURKA during mitotic entry and in early mitosis.
DR   Reactome; R-ATH-8866652; Synthesis of active ubiquitin: roles of E1 and E2 enzymes.
DR   Reactome; R-ATH-8866654; E3 ubiquitin ligases ubiquitinate target proteins.
DR   Reactome; R-ATH-901032; ER Quality Control Compartment (ERQC).
DR   Reactome; R-ATH-917729; Endosomal Sorting Complex Required For Transport (ESCRT).
DR   Reactome; R-ATH-917937; Iron uptake and transport.
DR   Reactome; R-ATH-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR   PRO; PR:P59271; -.
DR   Proteomes; UP000006548; Chromosome 1.
DR   ExpressionAtlas; P59271; baseline and differential.
DR   Genevisible; P59271; AT.
DR   GO; GO:0022627; C:cytosolic small ribosomal subunit; IDA:TAIR.
DR   GO; GO:0005794; C:Golgi apparatus; IDA:TAIR.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0005886; C:plasma membrane; IDA:TAIR.
DR   GO; GO:0009506; C:plasmodesma; IDA:TAIR.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0003735; F:structural constituent of ribosome; IDA:CAFA.
DR   GO; GO:0042256; P:mature ribosome assembly; IC:CAFA.
DR   GO; GO:0006412; P:translation; IEA:InterPro.
DR   InterPro; IPR002906; Ribosomal_S27a.
DR   InterPro; IPR011332; Ribosomal_zn-bd.
DR   InterPro; IPR019956; Ubiquitin.
DR   InterPro; IPR029071; Ubiquitin-rel_dom.
DR   InterPro; IPR019954; Ubiquitin_CS.
DR   InterPro; IPR000626; Ubiquitin_dom.
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; SSF54236; 1.
DR   SUPFAM; SSF57829; SSF57829; 1.
DR   PROSITE; PS00299; UBIQUITIN_1; 1.
DR   PROSITE; PS50053; UBIQUITIN_2; 1.
PE   2: Evidence at transcript level;
DR   PRODOM; Q9M1P9.
DR   SWISS-2DPAGE; Q9M1P9.
KW   Complete proteome; Cytoplasm; Isopeptide bond; Metal-binding; Nucleus;
KW   Reference proteome; Ribonucleoprotein; Ribosomal protein; Zinc;
KW   Zinc-finger.
FT   CHAIN         1     76       Ubiquitin.
FT                                /FTId=PRO_0000396871.
FT   CHAIN        77    156       40S ribosomal protein S27a-1.
FT                                /FTId=PRO_0000137674.
FT   DOMAIN        1     76       Ubiquitin-like. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00214}.
FT   ZN_FING     121    144       C4-type.
FT   COMPBIAS     77     99       Lys-rich (highly basic).
FT   CROSSLNK     76     76       Glycyl lysine isopeptide (Gly-Lys)
FT                                (interchain with K-? in acceptor
FT                                proteins). {ECO:0000255|PROSITE-
FT                                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
//

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