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Ubiquitin-40S ribosomal protein S27a [Cleaved into: Ubiquitin; 40S ribosomal protein S27a]

 RS27A_DROME             Reviewed;         156 AA.
P15357; P68198; Q0E8I1; Q9VKW6; Q9VQX7; Q9VZL4;
01-APR-1990, integrated into UniProtKB/Swiss-Prot.
10-AUG-2010, sequence version 2.
18-JUL-2018, entry version 149.
RecName: Full=Ubiquitin-40S ribosomal protein S27a;
Contains:
RecName: Full=Ubiquitin;
Contains:
RecName: Full=40S ribosomal protein S27a;
Flags: Precursor;
Name=RpS27A; Synonyms=UB3-D, UBI-F80, Ubi-m; ORFNames=CG5271;
Drosophila melanogaster (Fruit fly).
Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta;
Pterygota; Neoptera; Holometabola; Diptera; Brachycera; Muscomorpha;
Ephydroidea; Drosophilidae; Drosophila; Sophophora.
NCBI_TaxID=7227;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=2463465; DOI=10.1128/MCB.8.11.4727;
Lee H., Simon J.A., Lis J.T.;
"Structure and expression of ubiquitin genes of Drosophila
melanogaster.";
Mol. Cell. Biol. 8:4727-4735(1988).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=Canton-S;
PubMed=8068011; DOI=10.1042/bj3020237;
Barrio R., del Arco A., Cabrera H., Arribas C.;
"Structure and expression of the Drosophila ubiquitin-80-amino-acid
fusion-protein gene.";
Biochem. J. 302:237-244(1994).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Berkeley;
PubMed=10731132; DOI=10.1126/science.287.5461.2185;
Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X.,
Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D.,
Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G.,
Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D.,
Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M.,
Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S.,
Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P.,
Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I.,
Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P.,
de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M.,
Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P.,
Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W.,
Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K.,
Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J.,
Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C.,
Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A.,
Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z.,
Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X.,
Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D.,
Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A.,
Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L.,
Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M.,
Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G.,
Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H.,
Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
Spier E., Spradling A.C., Stapleton M., Strong R., Sun E.,
Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X.,
Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J.,
Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A.,
Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L.,
Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X.,
Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.;
"The genome sequence of Drosophila melanogaster.";
Science 287:2185-2195(2000).
[4]
GENOME REANNOTATION.
STRAIN=Berkeley;
PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q.,
Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M.,
Lewis S.E.;
"Annotation of the Drosophila melanogaster euchromatic genome: a
systematic review.";
Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
[5]
STRUCTURE BY ELECTRON MICROSCOPY (6.0 ANGSTROMS) OF THE 80S RIBOSOME.
PubMed=23636399; DOI=10.1038/nature12104;
Anger A.M., Armache J.P., Berninghausen O., Habeck M., Subklewe M.,
Wilson D.N., Beckmann R.;
"Structures of the human and Drosophila 80S ribosome.";
Nature 497:80-85(2013).
-!- FUNCTION: Ubiquitin exists either covalently attached to another
protein, or free (unanchored). When covalently bound, it is
conjugated to target proteins via an isopeptide bond either as a
monomer (monoubiquitin), a polymer linked via different Lys
residues of the ubiquitin (polyubiquitin chains) or a linear
polymer linked via the initiator Met of the ubiquitin (linear
polyubiquitin chains). Polyubiquitin chains, when attached to a
target protein, have different functions depending on the Lys
residue of the ubiquitin that is linked: Lys-48-linked is involved
in protein degradation via the proteasome. Linear polymer chains
formed via attachment by the initiator Met lead to cell signaling.
Ubiquitin is usually conjugated to Lys residues of target
proteins, however, in rare cases, conjugation to Cys or Ser
residues has been observed. When polyubiquitin is free
(unanchored-polyubiquitin), it also has distinct roles, such as in
activation of protein kinases, and in signaling (By similarity).
{ECO:0000250}.
-!- FUNCTION: Ribosomal protein S27a is a component of the 40S subunit
of the ribosome.
-!- SUBUNIT: Ribosomal protein S27a is part of the 40S ribosomal
subunit. {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Ubiquitin: Cytoplasm {ECO:0000250}. Nucleus
{ECO:0000250}.
-!- MISCELLANEOUS: In Drosophila ubiquitin is encoded by 3 different
genes. RpL40 and RpS27A genes code for a single copy of ubiquitin
fused to the ribosomal proteins L40 and S27a, respectively. Ubi-
p63E gene codes for a polyubiquitin precursor with exact head to
tail repeats.
-!- MISCELLANEOUS: For a better understanding, features related to
ubiquitin are only indicated for the first chain.
-!- SIMILARITY: In the N-terminal section; belongs to the ubiquitin
family. {ECO:0000305}.
-!- SIMILARITY: In the C-terminal section; belongs to the eukaryotic
ribosomal protein eS31 family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=CAA48871.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
-----------------------------------------------------------------------
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EMBL; M22536; AAA28998.1; -; mRNA.
EMBL; X69119; CAA48871.1; ALT_SEQ; Genomic_DNA.
EMBL; AE014134; AAF52941.1; -; Genomic_DNA.
RefSeq; NP_476778.1; NM_057430.4.
UniGene; Dm.36737; -.
UniGene; Dm.4835; -.
PDB; 4V6W; EM; 6.00 A; Af=77-156.
PDBsum; 4V6W; -.
ProteinModelPortal; P15357; -.
SMR; P15357; -.
BioGrid; 60502; 95.
IntAct; P15357; 8.
STRING; 7227.FBpp0079606; -.
PaxDb; P15357; -.
PRIDE; P15357; -.
EnsemblMetazoa; FBtr0080016; FBpp0079606; FBgn0003942.
GeneID; 34420; -.
KEGG; dme:Dmel_CG5271; -.
CTD; 6233; -.
FlyBase; FBgn0003942; RpS27A.
eggNOG; KOG0004; Eukaryota.
eggNOG; COG5272; LUCA.
InParanoid; P15357; -.
KO; K02977; -.
OMA; MSILKYY; -.
OrthoDB; EOG091G178I; -.
PhylomeDB; P15357; -.
Reactome; R-DME-110312; Translesion synthesis by REV1.
Reactome; R-DME-110314; Recognition of DNA damage by PCNA-containing replication complex.
Reactome; R-DME-110320; Translesion Synthesis by POLH.
Reactome; R-DME-1169091; Activation of NF-kappaB in B cells.
Reactome; R-DME-1234176; Oxygen-dependent proline hydroxylation of Hypoxia-inducible Factor Alpha.
Reactome; R-DME-1253288; Downregulation of ERBB4 signaling.
Reactome; R-DME-1295596; Spry regulation of FGF signaling.
Reactome; R-DME-1358803; Downregulation of ERBB2:ERBB3 signaling.
Reactome; R-DME-156827; L13a-mediated translational silencing of Ceruloplasmin expression.
Reactome; R-DME-174048; APC/C:Cdc20 mediated degradation of Cyclin B.
Reactome; R-DME-174084; Autodegradation of Cdh1 by Cdh1:APC/C.
Reactome; R-DME-174178; APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1.
Reactome; R-DME-174184; Cdc20:Phospho-APC/C mediated degradation of Cyclin A.
Reactome; R-DME-179409; APC-Cdc20 mediated degradation of Nek2A.
Reactome; R-DME-1799339; SRP-dependent cotranslational protein targeting to membrane.
Reactome; R-DME-182971; EGFR downregulation.
Reactome; R-DME-187577; SCF(Skp2)-mediated degradation of p27/p21.
Reactome; R-DME-195253; Degradation of beta-catenin by the destruction complex.
Reactome; R-DME-201681; TCF dependent signaling in response to WNT.
Reactome; R-DME-209360; Ubiquitination and proteolysis of phosphorylated CI.
Reactome; R-DME-209447; Activation of the IkappaB kinase complex, KEY:IRD5 dimer:KEY.
Reactome; R-DME-209461; Ubiquitination and degradation of phosphorylated ARM.
Reactome; R-DME-209560; NF-kB is activated and signals survival.
Reactome; R-DME-2122948; Activated NOTCH1 Transmits Signal to the Nucleus.
Reactome; R-DME-216167; Nuclear CI is degraded.
Reactome; R-DME-2173788; Downregulation of TGF-beta receptor signaling.
Reactome; R-DME-2173795; Downregulation of SMAD2/3:SMAD4 transcriptional activity.
Reactome; R-DME-2173796; SMAD2/SMAD3:SMAD4 heterotrimer regulates transcription.
Reactome; R-DME-2559582; Senescence-Associated Secretory Phenotype (SASP).
Reactome; R-DME-3769402; Deactivation of the beta-catenin transactivating complex.
Reactome; R-DME-432395; Degradation of TIM.
Reactome; R-DME-432524; Degradation of PER.
Reactome; R-DME-450302; activated TAK1 mediates p38 MAPK activation.
Reactome; R-DME-450321; JNK (c-Jun kinases) phosphorylation and activation mediated by activated human TAK1.
Reactome; R-DME-450408; AUF1 (hnRNP D0) binds and destabilizes mRNA.
Reactome; R-DME-4608870; Asymmetric localization of PCP proteins.
Reactome; R-DME-4641257; Degradation of AXIN.
Reactome; R-DME-4641258; Degradation of DVL.
Reactome; R-DME-5205685; Pink/Parkin Mediated Mitophagy.
Reactome; R-DME-532668; N-glycan trimming in the ER and Calnexin/Calreticulin cycle.
Reactome; R-DME-5358346; Hedgehog ligand biogenesis.
Reactome; R-DME-538864; Degradation of CRY.
Reactome; R-DME-5607761; Dectin-1 mediated noncanonical NF-kB signaling.
Reactome; R-DME-5610785; GLI3 is processed to GLI3R by the proteasome.
Reactome; R-DME-5632684; Hedgehog 'on' state.
Reactome; R-DME-5654726; Negative regulation of FGFR1 signaling.
Reactome; R-DME-5654727; Negative regulation of FGFR2 signaling.
Reactome; R-DME-5654732; Negative regulation of FGFR3 signaling.
Reactome; R-DME-5654733; Negative regulation of FGFR4 signaling.
Reactome; R-DME-5655862; Translesion synthesis by POLK.
Reactome; R-DME-5656121; Translesion synthesis by POLI.
Reactome; R-DME-5656169; Termination of translesion DNA synthesis.
Reactome; R-DME-5675221; Negative regulation of MAPK pathway.
Reactome; R-DME-5675482; Regulation of necroptotic cell death.
Reactome; R-DME-5676590; NIK-->noncanonical NF-kB signaling.
Reactome; R-DME-5689603; UCH proteinases.
Reactome; R-DME-5689877; Josephin domain DUBs.
Reactome; R-DME-5689880; Ub-specific processing proteases.
Reactome; R-DME-5689896; Ovarian tumor domain proteases.
Reactome; R-DME-5689901; Metalloprotease DUBs.
Reactome; R-DME-5693565; Recruitment and ATM-mediated phosphorylation of repair and signaling proteins at DNA double strand breaks.
Reactome; R-DME-5696394; DNA Damage Recognition in GG-NER.
Reactome; R-DME-5696395; Formation of Incision Complex in GG-NER.
Reactome; R-DME-5696400; Dual Incision in GG-NER.
Reactome; R-DME-6781823; Formation of TC-NER Pre-Incision Complex.
Reactome; R-DME-6782135; Dual incision in TC-NER.
Reactome; R-DME-6782210; Gap-filling DNA repair synthesis and ligation in TC-NER.
Reactome; R-DME-6791226; Major pathway of rRNA processing in the nucleolus and cytosol.
Reactome; R-DME-68949; Orc1 removal from chromatin.
Reactome; R-DME-69017; CDK-mediated phosphorylation and removal of Cdc6.
Reactome; R-DME-69229; Ubiquitin-dependent degradation of Cyclin D1.
Reactome; R-DME-69231; Cyclin D associated events in G1.
Reactome; R-DME-69601; Ubiquitin Mediated Degradation of Phosphorylated Cdc25A.
Reactome; R-DME-72649; Translation initiation complex formation.
Reactome; R-DME-72689; Formation of a pool of free 40S subunits.
Reactome; R-DME-72695; Formation of the ternary complex, and subsequently, the 43S complex.
Reactome; R-DME-72702; Ribosomal scanning and start codon recognition.
Reactome; R-DME-72706; GTP hydrolysis and joining of the 60S ribosomal subunit.
Reactome; R-DME-8849469; PTK6 Regulates RTKs and Their Effectors AKT1 and DOK1.
Reactome; R-DME-8854050; FBXL7 down-regulates AURKA during mitotic entry and in early mitosis.
Reactome; R-DME-8856825; Cargo recognition for clathrin-mediated endocytosis.
Reactome; R-DME-8856828; Clathrin-mediated endocytosis.
Reactome; R-DME-8863795; Downregulation of ERBB2 signaling.
Reactome; R-DME-8866652; Synthesis of active ubiquitin: roles of E1 and E2 enzymes.
Reactome; R-DME-8866654; E3 ubiquitin ligases ubiquitinate target proteins.
Reactome; R-DME-8939902; Regulation of RUNX2 expression and activity.
Reactome; R-DME-8941858; Regulation of RUNX3 expression and activity.
Reactome; R-DME-8948747; Regulation of PTEN localization.
Reactome; R-DME-8948751; Regulation of PTEN stability and activity.
Reactome; R-DME-901032; ER Quality Control Compartment (ERQC).
Reactome; R-DME-9010553; Regulation of expression of SLITs and ROBOs.
Reactome; R-DME-9013507; NOTCH3 Activation and Transmission of Signal to the Nucleus.
Reactome; R-DME-9020702; Interleukin-1 signaling.
Reactome; R-DME-9033241; Peroxisomal protein import.
Reactome; R-DME-912631; Regulation of signaling by CBL.
Reactome; R-DME-917729; Endosomal Sorting Complex Required For Transport (ESCRT).
Reactome; R-DME-937039; IRAK1 recruits IKK complex.
Reactome; R-DME-937042; IRAK2 mediated activation of TAK1 complex.
Reactome; R-DME-975110; TRAF6 mediated IRF7 activation in TLR7/8 or 9 signaling.
Reactome; R-DME-975144; IRAK1 recruits IKK complex upon TLR7/8 or 9 stimulation.
Reactome; R-DME-975163; IRAK2 mediated activation of TAK1 complex upon TLR7/8 or 9 stimulation.
Reactome; R-DME-975956; Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC).
Reactome; R-DME-975957; Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).
Reactome; R-DME-983168; Antigen processing: Ubiquitination & Proteasome degradation.
ChiTaRS; RpS27A; fly.
GenomeRNAi; 34420; -.
PRO; PR:P15357; -.
Proteomes; UP000000803; Chromosome 2L.
Bgee; FBgn0003942; -.
ExpressionAtlas; P15357; baseline and differential.
Genevisible; P15357; DM.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0022627; C:cytosolic small ribosomal subunit; TAS:FlyBase.
GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0031386; F:protein tag; ISS:FlyBase.
GO; GO:0003735; F:structural constituent of ribosome; TAS:FlyBase.
GO; GO:0002181; P:cytoplasmic translation; TAS:FlyBase.
GO; GO:0016567; P:protein ubiquitination; ISS:FlyBase.
Gene3D; 2.20.25.660; -; 1.
InterPro; IPR002906; Ribosomal_S27a.
InterPro; IPR011332; Ribosomal_zn-bd.
InterPro; IPR038582; S27a-like_sf.
InterPro; IPR019956; Ubiquitin.
InterPro; IPR029071; Ubiquitin-like_domsf.
InterPro; IPR019954; Ubiquitin_CS.
InterPro; IPR000626; Ubiquitin_dom.
Pfam; PF01599; Ribosomal_S27; 1.
Pfam; PF00240; ubiquitin; 1.
PRINTS; PR00348; UBIQUITIN.
SMART; SM01402; Ribosomal_S27; 1.
SMART; SM00213; UBQ; 1.
SUPFAM; SSF54236; SSF54236; 1.
SUPFAM; SSF57829; SSF57829; 1.
PROSITE; PS00299; UBIQUITIN_1; 1.
PROSITE; PS50053; UBIQUITIN_2; 1.
1: Evidence at protein level;
3D-structure; Complete proteome; Cytoplasm; Isopeptide bond;
Metal-binding; Nucleus; Reference proteome; Ribonucleoprotein;
Ribosomal protein; Ubl conjugation; Zinc; Zinc-finger.
CHAIN 1 76 Ubiquitin.
/FTId=PRO_0000396482.
CHAIN 77 156 40S ribosomal protein S27a.
/FTId=PRO_0000396483.
DOMAIN 1 76 Ubiquitin-like. {ECO:0000255|PROSITE-
ProRule:PRU00214}.
ZN_FING 121 144 C4-type.
COMPBIAS 78 107 Lys-rich.
BINDING 54 54 Activating enzyme.
BINDING 72 72 Activating enzyme.
SITE 68 68 Essential for function.
CROSSLNK 48 48 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin).
CROSSLNK 76 76 Glycyl lysine isopeptide (Gly-Lys)
(interchain with K-? in acceptor
proteins).
SEQUENCE 156 AA; 17940 MW; 4FB9AC25B8E86EF5 CRC64;
MQIFVKTLTG KTITLEVEPS DTIENVKAKI QDKEGIPPDQ QRLIFAGKQL EDGRTLSDYN
IQKESTLHLV LRLRGGAKKR KKKNYSTPKK IKHKRKKVKL AVLKYYKVDE NGKIHRLRRE
CPGENCGAGV FMAAHEDRHY CGKCNLTFVF SKPEEK


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