RS27A_BOVIN
ID RS27A_BOVIN Reviewed; 156 AA.
AC P62992; O97577; P02248; P02249; P02250; P0CG52; P62990; P80169; Q01235;
AC Q24K23; Q28169; Q28170; Q29120; Q3T0V5; Q3ZCE3; Q862C1; Q862F4; Q862M4;
AC Q862T5; Q862X8; Q91887; Q91888;
DT 31-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 10-AUG-2010, sequence version 2.
DT 03-AUG-2022, entry version 124.
DE RecName: Full=Ubiquitin-40S ribosomal protein S27a;
DE AltName: Full=Ubiquitin carboxyl extension protein 80;
DE Contains:
DE RecName: Full=Ubiquitin;
DE Contains:
DE RecName: Full=40S ribosomal protein S27a;
DE Flags: Precursor;
GN Name=RPS27A; Synonyms=UBA80, UBCEP1;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=9765411; DOI=10.1128/jvi.72.11.8697-8704.1998;
RA Becher P., Orlich M., Thiel H.J.;
RT "Ribosomal S27a coding sequences upstream of ubiquitin coding sequences in
RT the genome of a pestivirus.";
RL J. Virol. 72:8697-8704(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=12658628; DOI=10.1002/mrd.10292;
RA Ishiwata H., Katsuma S., Kizaki K., Patel O.V., Nakano H., Takahashi T.,
RA Imai K., Hirasawa A., Shiojima S., Ikawa H., Suzuki Y., Tsujimoto G.,
RA Izaike Y., Todoroki J., Hashizume K.;
RT "Characterization of gene expression profiles in early bovine pregnancy
RT using a custom cDNA microarray.";
RL Mol. Reprod. Dev. 65:9-18(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Crossbred X Angus; TISSUE=Ileum, and Liver;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP PROTEIN SEQUENCE OF 1-74.
RX PubMed=1170880; DOI=10.1021/bi00681a026;
RA Schlesinger D.H., Goldstein G., Niall H.D.;
RT "The complete amino acid sequence of ubiquitin, an adenylate cyclase
RT stimulating polypeptide probably universal in living cells.";
RL Biochemistry 14:2214-2218(1975).
RN [5]
RP PROTEIN SEQUENCE OF 1-50.
RX PubMed=6254502; DOI=10.1016/0006-291x(80)91188-2;
RA Hamilton J.W., Rouse J.B.;
RT "The biosynthesis of ubiquitin by parathyroid gland.";
RL Biochem. Biophys. Res. Commun. 96:114-120(1980).
RN [6]
RP PROTEIN SEQUENCE OF 1-20.
RC TISSUE=Brain;
RX PubMed=1333954; DOI=10.1111/j.1432-1033.1992.tb17446.x;
RA Zdebska E., Antoniewicz J., Nilsson B., Sandhoff K., Fuerst W., Janik P.,
RA Koscielak J.;
RT "Ganglioside binding proteins of calf brain with ubiquitin-like N-
RT terminals.";
RL Eur. J. Biochem. 210:483-489(1992).
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 proteotoxic stress
CC response and cell cycle; 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, DNA-damage
CC responses as well as in signaling processes leading to activation of
CC the transcription factor NF-kappa-B. Linear polymer chains formed via
CC attachment by the initiator Met lead to cell signaling. Ubiquitin is
CC usually 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 distinct
CC roles, such as in activation of protein kinases, and in signaling (By
CC similarity). {ECO:0000250}.
CC -!- FUNCTION: [40S ribosomal protein S27a]: 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 -!- INTERACTION:
CC PRO_0000396474; PRO_0000338257 [P0C6U8]: 1a; Xeno; NbExp=2; IntAct=EBI-25820711, EBI-25635190;
CC -!- SUBCELLULAR LOCATION: [Ubiquitin]: Cytoplasm {ECO:0000250}. Nucleus
CC {ECO:0000250}.
CC -!- PTM: [Ubiquitin]: Phosphorylated at Ser-65 by PINK1 during mitophagy.
CC Phosphorylated ubiquitin specifically binds and activates parkin
CC (PRKN), triggering mitophagy. Phosphorylation does not affect E1-
CC mediated E2 charging of ubiquitin but affects discharging of E2 enzymes
CC to form polyubiquitin chains. It also affects deubiquitination by
CC deubiquitinase enzymes such as USP30. {ECO:0000250|UniProtKB:P62979}.
CC -!- PTM: [Ubiquitin]: Mono-ADP-ribosylated at the C-terminus by PARP9, a
CC component of the PPAR9-DTX3L complex. ADP-ribosylation requires
CC processing by E1 and E2 enzymes and prevents ubiquitin conjugation to
CC substrates such as histones. {ECO:0000250|UniProtKB:P62979}.
CC -!- MISCELLANEOUS: Ubiquitin is encoded by 4 different genes. Uba52 and
CC Rps27a genes code for a single copy of ubiquitin fused to the ribosomal
CC proteins L40 and S27a, respectively. UBB and UBC genes code for a
CC polyubiquitin precursor with exact head to tail repeats, the number of
CC repeats differ between species and strains.
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; AF058700; AAC77907.1; -; mRNA.
DR EMBL; AB098891; BAC56381.1; -; mRNA.
DR EMBL; BC102491; AAI02492.2; -; mRNA.
DR PIR; A28144; A28144.
DR RefSeq; NP_777203.1; NM_174778.1.
DR RefSeq; XP_005212615.1; XM_005212558.2.
DR PDB; 4M0W; X-ray; 1.40 A; B=1-76.
DR PDB; 4Y1H; X-ray; 1.40 A; A=1-76.
DR PDB; 4Z9S; X-ray; 2.30 A; A/B/C/D=1-76.
DR PDB; 5BZ0; X-ray; 2.10 A; B=1-76.
DR PDB; 5FER; X-ray; 2.34 A; C/F=1-76.
DR PDB; 5JQS; X-ray; 2.65 A; D=1-76.
DR PDB; 5MN9; X-ray; 2.05 A; A/B=1-76.
DR PDB; 5XU8; X-ray; 1.81 A; B=1-76.
DR PDB; 5XVE; X-ray; 1.24 A; B=1-76.
DR PDB; 6DJW; X-ray; 3.80 A; B=1-74.
DR PDB; 6DJX; X-ray; 4.80 A; B=1-76.
DR PDB; 6E2B; X-ray; 1.45 A; A/C/E/G/I/P=1-76.
DR PDB; 6Q01; X-ray; 0.85 A; A/B=1-76.
DR PDB; 7F0U; X-ray; 2.20 A; C/D=1-76.
DR PDB; 7NWH; EM; 4.10 A; ff=83-150.
DR PDBsum; 4M0W; -.
DR PDBsum; 4Y1H; -.
DR PDBsum; 4Z9S; -.
DR PDBsum; 5BZ0; -.
DR PDBsum; 5FER; -.
DR PDBsum; 5JQS; -.
DR PDBsum; 5MN9; -.
DR PDBsum; 5XU8; -.
DR PDBsum; 5XVE; -.
DR PDBsum; 6DJW; -.
DR PDBsum; 6DJX; -.
DR PDBsum; 6E2B; -.
DR PDBsum; 6Q01; -.
DR PDBsum; 7F0U; -.
DR PDBsum; 7NWH; -.
DR AlphaFoldDB; P62992; -.
DR SMR; P62992; -.
DR BioGRID; 159949; 3.
DR IntAct; P62992; 1.
DR STRING; 9913.ENSBTAP00000033015; -.
DR PaxDb; P62992; -.
DR PRIDE; P62992; -.
DR Ensembl; ENSBTAT00000033091; ENSBTAP00000033015; ENSBTAG00000015473.
DR GeneID; 286839; -.
DR KEGG; bta:286839; -.
DR CTD; 6233; -.
DR VEuPathDB; HostDB:ENSBTAG00000015473; -.
DR VGNC; VGNC:34135; RPS27A.
DR eggNOG; KOG0004; Eukaryota.
DR GeneTree; ENSGT00940000165870; -.
DR HOGENOM; CLU_010412_2_0_1; -.
DR InParanoid; P62992; -.
DR OMA; FMAQHAN; -.
DR OrthoDB; 1536766at2759; -.
DR TreeFam; TF300036; -.
DR Proteomes; UP000009136; Chromosome 11.
DR ExpressionAtlas; P62992; baseline and differential.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0022627; C:cytosolic small ribosomal subunit; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0031386; F:protein tag; IBA:GO_Central.
DR GO; GO:0003735; F:structural constituent of ribosome; 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:0006412; P:translation; IEA:InterPro.
DR Gene3D; 6.20.50.150; -; 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; Acetylation; ADP-ribosylation; Cytoplasm;
KW Direct protein sequencing; Isopeptide bond; Metal-binding; Nucleus;
KW Phosphoprotein; Reference proteome; Repeat; Ribonucleoprotein;
KW Ribosomal protein; Ubl conjugation; Zinc; Zinc-finger.
FT CHAIN 1..76
FT /note="Ubiquitin"
FT /id="PRO_0000396474"
FT CHAIN 77..156
FT /note="40S ribosomal protein S27a"
FT /id="PRO_0000137660"
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 REGION 76..95
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 54
FT /note="Interacts with activating enzyme"
FT SITE 68
FT /note="Essential for function"
FT SITE 72
FT /note="Interacts with activating enzyme"
FT MOD_RES 65
FT /note="Phosphoserine; by PINK1"
FT /evidence="ECO:0000250|UniProtKB:P62979"
FT MOD_RES 76
FT /note="ADP-ribosylglycine"
FT /evidence="ECO:0000250|UniProtKB:P62979"
FT MOD_RES 104
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P62979"
FT MOD_RES 113
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P62979"
FT MOD_RES 152
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P62983"
FT CROSSLNK 6
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:P62979"
FT CROSSLNK 11
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:P62979"
FT CROSSLNK 27
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:P62979"
FT CROSSLNK 29
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:P62979"
FT CROSSLNK 33
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:P62979"
FT CROSSLNK 48
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:P62979"
FT CROSSLNK 63
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:P62979"
FT CROSSLNK 76
FT /note="Glycyl lysine isopeptide (Gly-Lys) (interchain with
FT K-? in acceptor proteins)"
FT CONFLICT 141..156
FT /note="CGKCCLTYCFNKPEDK -> VANVV (in Ref. 2; BAC56381)"
FT /evidence="ECO:0000305"
FT STRAND 2..7
FT /evidence="ECO:0007829|PDB:6Q01"
FT STRAND 8..10
FT /evidence="ECO:0007829|PDB:5XVE"
FT STRAND 12..16
FT /evidence="ECO:0007829|PDB:6Q01"
FT HELIX 23..34
FT /evidence="ECO:0007829|PDB:6Q01"
FT HELIX 38..40
FT /evidence="ECO:0007829|PDB:6Q01"
FT STRAND 41..45
FT /evidence="ECO:0007829|PDB:6Q01"
FT HELIX 57..59
FT /evidence="ECO:0007829|PDB:6Q01"
FT STRAND 66..71
FT /evidence="ECO:0007829|PDB:6Q01"
FT STRAND 73..75
FT /evidence="ECO:0007829|PDB:5JQS"
SQ SEQUENCE 156 AA; 17965 MW; 617BC63DF3A904F7 CRC64;
MQIFVKTLTG KTITLEVEPS DTIENVKAKI QDKEGIPPDQ QRLIFAGKQL EDGRTLSDYN
IQKESTLHLV LRLRGGAKKR KKKSYTTPKK NKHKRKKVKL AVLKYYKVDE NGKISRLRRE
CPSDECGAGV FMASHFDRHY CGKCCLTYCF NKPEDK
