GenomeNet

Database: UniProt
Entry: P69061
LinkDB: P69061
Original site: P69061 
ID   RS27A_KLULA             Reviewed;         150 AA.
AC   P69061; Q6CQ09; Q6CQB8; Q9Y848; Q9Y852;
DT   01-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT   10-AUG-2010, sequence version 2.
DT   07-APR-2021, entry version 85.
DE   RecName: Full=Ubiquitin-40S ribosomal protein S27a;
DE   Contains:
DE     RecName: Full=Ubiquitin;
DE   Contains:
DE     RecName: Full=40S ribosomal protein S27a;
DE   Flags: Precursor;
GN   Name=ubi3; OrderedLocusNames=KLLA0D18304g;
OS   Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 /
OS   NRRL Y-1140 / WM37) (Yeast) (Candida sphaerica).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Kluyveromyces.
OX   NCBI_TaxID=284590;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCCC 76492 / CBS 2359/152 / CLIB 210;
RX   PubMed=10669872;
RX   DOI=10.1002/1097-0061(20000315)16:4<343::aid-yea534>3.0.co;2-f;
RA   Bao W.-G., Fukuhara H.;
RT   "The ubiquitin-encoding genes of Kluyveromyces lactis.";
RL   Yeast 16:343-351(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37;
RX   PubMed=15229592; DOI=10.1038/nature02579;
RA   Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA   de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA   Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA   Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA   Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA   Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA   Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA   Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA   Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA   Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA   Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA   Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA   Weissenbach J., Wincker P., Souciet J.-L.;
RT   "Genome evolution in yeasts.";
RL   Nature 430:35-44(2004).
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-6-linked may be involved in DNA repair; Lys-11-linked is involved
CC       in ERAD (endoplasmic reticulum-associated degradation) and in cell-
CC       cycle regulation; Lys-29-linked is involved in lysosomal degradation;
CC       Lys-33-linked is involved in kinase modification; Lys-48-linked is
CC       involved in protein degradation via the proteasome; Lys-63-linked is
CC       involved in endocytosis, and DNA-damage responses. Linear polymer
CC       chains formed via attachment by the initiator Met lead to cell
CC       signaling. Ubiquitin is usually conjugated to Lys residues of target
CC       proteins, however, in rare cases, conjugation to Cys or Ser residues
CC       has been observed. When polyubiquitin is free (unanchored-
CC       polyubiquitin), it also has distinct roles, such as in activation of
CC       protein kinases, and in signaling (By similarity). {ECO:0000250}.
CC   -!- FUNCTION: Ribosomal protein S27a is a component of the 40S subunit of
CC       the ribosome.
CC   -!- SUBUNIT: Ribosomal protein S27a is part of the 40S ribosomal subunit.
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: [Ubiquitin]: Cytoplasm {ECO:0000250}. Nucleus
CC       {ECO:0000250}.
CC   -!- MISCELLANEOUS: Ubiquitin is encoded by several different genes. Ubi3
CC       genes code for a single copy of ubiquitin fused to the ribosomal
CC       proteins S27a. Ubi4 is synthesized as a polyubiquitin precursor with 5
CC       exact head to tail repeats.
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AJ243802; CAB50894.1; -; Genomic_DNA.
DR   EMBL; CR382124; CAH00967.1; -; Genomic_DNA.
DR   RefSeq; XP_453871.1; XM_453871.1.
DR   PDB; 3J80; EM; 3.75 A; f=1-150.
DR   PDB; 3J81; EM; 4.00 A; f=1-150.
DR   PDB; 3JAM; EM; 3.46 A; f=1-150.
DR   PDB; 3JAP; EM; 4.90 A; f=1-150.
DR   PDB; 3JAQ; EM; 6.00 A; f=1-150.
DR   PDB; 5IT7; EM; 3.60 A; f=82-150.
DR   PDB; 5IT9; EM; 3.80 A; f=82-150.
DR   PDB; 6FYX; EM; 3.05 A; f=1-150.
DR   PDB; 6FYY; EM; 3.05 A; f=1-150.
DR   PDB; 6GSM; EM; 5.15 A; f=82-150.
DR   PDB; 6GSN; EM; 5.75 A; f=82-150.
DR   PDB; 6UZ7; EM; 3.60 A; f=1-150.
DR   PDBsum; 3J80; -.
DR   PDBsum; 3J81; -.
DR   PDBsum; 3JAM; -.
DR   PDBsum; 3JAP; -.
DR   PDBsum; 3JAQ; -.
DR   PDBsum; 5IT7; -.
DR   PDBsum; 5IT9; -.
DR   PDBsum; 6FYX; -.
DR   PDBsum; 6FYY; -.
DR   PDBsum; 6GSM; -.
DR   PDBsum; 6GSN; -.
DR   PDBsum; 6UZ7; -.
DR   SMR; P69061; -.
DR   STRING; 28985.XP_453871.1; -.
DR   EnsemblFungi; CAH00967; CAH00967; KLLA0_D18304g.
DR   GeneID; 2893475; -.
DR   KEGG; kla:KLLA0_D18304g; -.
DR   eggNOG; KOG0004; Eukaryota.
DR   HOGENOM; CLU_010412_2_0_1; -.
DR   InParanoid; P69061; -.
DR   OMA; FMAQHAN; -.
DR   Proteomes; UP000000598; Chromosome D.
DR   GO; GO:0022627; C:cytosolic small ribosomal subunit; IEA:EnsemblFungi.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0031386; F:protein tag; IEA:EnsemblFungi.
DR   GO; GO:0003735; F:structural constituent of ribosome; IEA:InterPro.
DR   GO; GO:0002109; P:maturation of SSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, LSU-rRNA,5S); IEA:EnsemblFungi.
DR   GO; GO:0000028; P:ribosomal small subunit assembly; IEA:EnsemblFungi.
DR   GO; GO:0006412; P:translation; IEA:InterPro.
DR   Gene3D; 2.20.25.660; -; 1.
DR   InterPro; IPR002906; Ribosomal_S27a.
DR   InterPro; IPR011332; Ribosomal_zn-bd.
DR   InterPro; IPR038582; S27a-like_sf.
DR   InterPro; IPR000626; Ubiquitin-like_dom.
DR   InterPro; IPR029071; Ubiquitin-like_domsf.
DR   InterPro; IPR019954; Ubiquitin_CS.
DR   InterPro; IPR019956; 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   1: Evidence at protein level;
KW   3D-structure; Cytoplasm; Isopeptide bond; Metal-binding; Nucleus;
KW   Reference proteome; Ribonucleoprotein; Ribosomal protein; Ubl conjugation;
KW   Zinc; Zinc-finger.
FT   CHAIN           1..76
FT                   /note="Ubiquitin"
FT                   /id="PRO_0000114857"
FT   CHAIN           77..150
FT                   /note="40S ribosomal protein S27a"
FT                   /id="PRO_0000137685"
FT   DOMAIN          1..76
FT                   /note="Ubiquitin-like"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00214"
FT   ZN_FING         121..142
FT                   /note="C4-type"
FT   COMPBIAS        77..99
FT                   /note="Lys-rich (highly basic)"
FT   CROSSLNK        6
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in ubiquitin)"
FT   CROSSLNK        11
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in ubiquitin)"
FT   CROSSLNK        27
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in ubiquitin)"
FT   CROSSLNK        29
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in ubiquitin)"
FT   CROSSLNK        33
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in ubiquitin)"
FT   CROSSLNK        48
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in ubiquitin)"
FT                   /evidence="ECO:0000250"
FT   CROSSLNK        63
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in ubiquitin)"
FT   CROSSLNK        76
FT                   /note="Glycyl lysine isopeptide (Gly-Lys) (interchain with
FT                   K-? in acceptor proteins)"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00214"
FT   STRAND          105..107
FT                   /evidence="ECO:0007744|PDB:3JAM"
FT   STRAND          110..112
FT                   /evidence="ECO:0007744|PDB:3JAM"
FT   STRAND          122..124
FT                   /evidence="ECO:0007744|PDB:3JAM"
FT   STRAND          133..135
FT                   /evidence="ECO:0007744|PDB:3JAM"
FT   STRAND          140..142
FT                   /evidence="ECO:0007744|PDB:3JAM"
SQ   SEQUENCE   150 AA;  17074 MW;  4D7C82E923721474 CRC64;
     MQIFVKTLTG KTITLEVESS DTIDNVKSKI QDKEGIPPDQ QRLIFAGKQL EDGRTLSDYN
     IQKESTLHLV LRLRGGGKKR KKKVYTTPKK IRHKHKKVKL AVLNYYKVDD EGKVAKLRKE
     CPNCGPGIFL ANHGDRFYCG KCHSTFATQK
//
DBGET integrated database retrieval system