Database: UniProt
Entry: P0CH08
LinkDB: P0CH08
Original site: P0CH08 
ID   RL40A_YEAST             Reviewed;         128 AA.
AC   P0CH08; D6VVD9; P04838; P14796; P61864; Q6LA96;
DT   10-AUG-2010, integrated into UniProtKB/Swiss-Prot.
DT   10-AUG-2010, sequence version 1.
DT   29-SEP-2021, entry version 103.
DE   RecName: Full=Ubiquitin-60S ribosomal protein L40;
DE   Contains:
DE     RecName: Full=Ubiquitin;
DE   Contains:
DE     RecName: Full=60S ribosomal protein L40-A {ECO:0000303|PubMed:9559554};
DE     AltName: Full=CEP52;
DE     AltName: Full=Large ribosomal subunit protein eL40-A {ECO:0000303|PubMed:24524803};
DE   Flags: Precursor;
GN   Name=RPL40A {ECO:0000303|PubMed:9559554}; Synonyms=UBI1;
GN   OrderedLocusNames=YIL148W;
OS   Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=559292;
RN   [1]
RX   PubMed=3038523; DOI=10.1002/j.1460-2075.1987.tb02384.x;
RA   Oezkaynak E., Finley D., Solomon M.J., Varshavsky A.;
RT   "The yeast ubiquitin genes: a family of natural gene fusions.";
RL   EMBO J. 6:1429-1439(1987).
RN   [2]
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=9169870;
RA   Churcher C.M., Bowman S., Badcock K., Bankier A.T., Brown D.,
RA   Chillingworth T., Connor R., Devlin K., Gentles S., Hamlin N., Harris D.E.,
RA   Horsnell T., Hunt S., Jagels K., Jones M., Lye G., Moule S., Odell C.,
RA   Pearson D., Rajandream M.A., Rice P., Rowley N., Skelton J., Smith V.,
RA   Walsh S.V., Whitehead S., Barrell B.G.;
RT   "The nucleotide sequence of Saccharomyces cerevisiae chromosome IX.";
RL   Nature 387:84-87(1997).
RN   [3]
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=24374639; DOI=10.1534/g3.113.008995;
RA   Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA   Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA   Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT   "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL   G3 (Bethesda) 4:389-398(2014).
RN   [4]
RX   PubMed=7615550; DOI=10.1074/jbc.270.29.17442;
RA   Johnson E.S., Ma P.C.M., Ota I.M., Varshavsky A.;
RT   "A proteolytic pathway that recognizes ubiquitin as a degradation signal.";
RL   J. Biol. Chem. 270:17442-17456(1995).
RN   [5]
RX   PubMed=7862120; DOI=10.1128/mcb.15.3.1265;
RA   Spence J., Sadis S., Haas A.L., Finley D.;
RT   "A ubiquitin mutant with specific defects in DNA repair and
RT   multiubiquitination.";
RL   Mol. Cell. Biol. 15:1265-1273(1995).
RN   [6]
RX   PubMed=9559554;
RX   DOI=10.1002/(sici)1097-0061(19980330)14:5<471::aid-yea241>;2-u;
RA   Planta R.J., Mager W.H.;
RT   "The list of cytoplasmic ribosomal proteins of Saccharomyces cerevisiae.";
RL   Yeast 14:471-477(1998).
RN   [7]
RX   PubMed=14562095; DOI=10.1038/nature02026;
RA   Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA   Weissman J.S., O'Shea E.K.;
RT   "Global analysis of protein localization in budding yeast.";
RL   Nature 425:686-691(2003).
RN   [8]
RX   PubMed=14562106; DOI=10.1038/nature02046;
RA   Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA   O'Shea E.K., Weissman J.S.;
RT   "Global analysis of protein expression in yeast.";
RL   Nature 425:737-741(2003).
RN   [9]
RX   PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA   Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA   Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA   Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT   "N-terminal acetylome analyses and functional insights of the N-terminal
RT   acetyltransferase NatB.";
RL   Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN   [10]
RX   PubMed=22106047; DOI=10.1002/pmic.201100166;
RA   Starita L.M., Lo R.S., Eng J.K., von Haller P.D., Fields S.;
RT   "Sites of ubiquitin attachment in Saccharomyces cerevisiae.";
RL   Proteomics 12:236-240(2012).
RN   [11]
RX   PubMed=23169626; DOI=10.1073/pnas.1216454109;
RA   Lee A.S., Burdeinick-Kerr R., Whelan S.P.;
RT   "A ribosome-specialized translation initiation pathway is required for cap-
RT   dependent translation of vesicular stomatitis virus mRNAs.";
RL   Proc. Natl. Acad. Sci. U.S.A. 110:324-329(2013).
RN   [12]
RX   PubMed=24524803; DOI=10.1016/;
RA   Ban N., Beckmann R., Cate J.H.D., Dinman J.D., Dragon F., Ellis S.R.,
RA   Lafontaine D.L.J., Lindahl L., Liljas A., Lipton J.M., McAlear M.A.,
RA   Moore P.B., Noller H.F., Ortega J., Panse V.G., Ramakrishnan V.,
RA   Spahn C.M.T., Steitz T.A., Tchorzewski M., Tollervey D., Warren A.J.,
RA   Williamson J.R., Wilson D., Yonath A., Yusupov M.;
RT   "A new system for naming ribosomal proteins.";
RL   Curr. Opin. Struct. Biol. 24:165-169(2014).
RN   [13]
RX   PubMed=21109664; DOI=10.1126/science.1194294;
RA   Ben-Shem A., Jenner L., Yusupova G., Yusupov M.;
RT   "Crystal structure of the eukaryotic ribosome.";
RL   Science 330:1203-1209(2010).
RN   [14]
RX   PubMed=22096102; DOI=10.1126/science.1212642;
RA   Ben-Shem A., Garreau de Loubresse N., Melnikov S., Jenner L., Yusupova G.,
RA   Yusupov M.;
RT   "The structure of the eukaryotic ribosome at 3.0 A resolution.";
RL   Science 334:1524-1529(2011).
RN   [15]
RX   PubMed=23142985; DOI=10.1038/nsmb.2425;
RA   Greber B.J., Boehringer D., Montellese C., Ban N.;
RT   "Cryo-EM structures of Arx1 and maturation factors Rei1 and Jjj1 bound to
RT   the 60S ribosomal subunit.";
RL   Nat. Struct. Mol. Biol. 19:1228-1233(2012).
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: [60S ribosomal protein L40-A]: Component of the ribosome, a
CC       large ribonucleoprotein complex responsible for the synthesis of
CC       proteins in the cell. The small ribosomal subunit (SSU) binds messenger
CC       RNAs (mRNAs) and translates the encoded message by selecting cognate
CC       aminoacyl-transfer RNA (tRNA) molecules. The large subunit (LSU)
CC       contains the ribosomal catalytic site termed the peptidyl transferase
CC       center (PTC), which catalyzes the formation of peptide bonds, thereby
CC       polymerizing the amino acids delivered by tRNAs into a polypeptide
CC       chain. The nascent polypeptides leave the ribosome through a tunnel in
CC       the LSU and interact with protein factors that function in enzymatic
CC       processing, targeting, and the membrane insertion of nascent chains at
CC       the exit of the ribosomal tunnel (PubMed:22096102). eL40 is essential
CC       for translation of a subset of cellular transcripts, including stress
CC       response transcripts, such as DDR2 (PubMed:23169626).
CC       {ECO:0000269|PubMed:23169626, ECO:0000305|PubMed:22096102}.
CC   -!- SUBUNIT: Component of the large ribosomal subunit (LSU). Mature yeast
CC       ribosomes consist of a small (40S) and a large (60S) subunit. The 40S
CC       small subunit contains 1 molecule of ribosomal RNA (18S rRNA) and 33
CC       different proteins (encoded by 57 genes). The large 60S subunit
CC       contains 3 rRNA molecules (25S, 5.8S and 5S rRNA) and 46 different
CC       proteins (encoded by 81 genes) (PubMed:9559554, PubMed:22096102).
CC       {ECO:0000269|PubMed:22096102, ECO:0000305|PubMed:9559554}.
CC   -!- SUBCELLULAR LOCATION: [Ubiquitin]: Cytoplasm {ECO:0000250}. Nucleus
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: [60S ribosomal protein L40-A]: Cytoplasm
CC       {ECO:0000269|PubMed:22096102}.
CC   -!- MISCELLANEOUS: Ubiquitin is encoded by several different genes. UBI1
CC       and UBI2 genes code for a single copy of ubiquitin fused to the
CC       ribosomal proteins eL40. UBI3 is a polyprotein with one copy of
CC       ubiquitin fused to ribosomal protein eS31. UBI4 is a polyprotein
CC       containing 5 exact head to tail repeats of ubiquitin.
CC       {ECO:0000305|PubMed:3038523}.
CC   -!- MISCELLANEOUS: The 60S ribosomal protein L40 is present with 40000
CC       molecules/cell in log phase SD medium. {ECO:0000269|PubMed:14562106}.
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 eL40 family. {ECO:0000305}.
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DR   EMBL; X05728; CAA29195.1; -; Genomic_DNA.
DR   EMBL; X05729; CAA29196.1; -; Genomic_DNA.
DR   EMBL; Z38059; CAA86130.1; -; Genomic_DNA.
DR   EMBL; BK006942; DAA08405.1; -; Genomic_DNA.
DR   PIR; A29456; A29456.
DR   RefSeq; NP_012118.1; NM_001179496.1.
DR   RefSeq; NP_013020.3; NM_001179884.3.
DR   PDB; 3J6X; EM; 6.10 A; 80=1-128.
DR   PDB; 3J6Y; EM; 6.10 A; 80=1-128.
DR   PDB; 3J77; EM; 6.20 A; 90=1-128.
DR   PDB; 3J78; EM; 6.30 A; 90=1-128.
DR   PDB; 4U3M; X-ray; 3.00 A; Q0/q0=77-128.
DR   PDB; 4U3N; X-ray; 3.20 A; Q0/q0=77-128.
DR   PDB; 4U3U; X-ray; 2.90 A; Q0/q0=77-128.
DR   PDB; 4U4N; X-ray; 3.10 A; Q0/q0=77-128.
DR   PDB; 4U4O; X-ray; 3.60 A; Q0/q0=77-128.
DR   PDB; 4U4Q; X-ray; 3.00 A; Q0/q0=77-128.
DR   PDB; 4U4R; X-ray; 2.80 A; Q0/q0=77-128.
DR   PDB; 4U4U; X-ray; 3.00 A; Q0/q0=77-128.
DR   PDB; 4U4Y; X-ray; 3.20 A; Q0/q0=77-128.
DR   PDB; 4U4Z; X-ray; 3.10 A; Q0/q0=77-128.
DR   PDB; 4U50; X-ray; 3.20 A; Q0/q0=77-128.
DR   PDB; 4U51; X-ray; 3.20 A; Q0/q0=77-128.
DR   PDB; 4U52; X-ray; 3.00 A; Q0/q0=77-128.
DR   PDB; 4U53; X-ray; 3.30 A; Q0/q0=77-128.
DR   PDB; 4U55; X-ray; 3.20 A; Q0/q0=77-128.
DR   PDB; 4U56; X-ray; 3.45 A; Q0/q0=77-128.
DR   PDB; 4U6F; X-ray; 3.10 A; Q0/q0=77-128.
DR   PDB; 4V6I; EM; 8.80 A; Bp=77-128.
DR   PDB; 4V88; X-ray; 3.00 A; Bm/Dm=1-128.
DR   PDB; 4V8T; EM; 8.10 A; m=1-128.
DR   PDB; 4V8Y; EM; 4.30 A; Bm=1-128.
DR   PDB; 4V8Z; EM; 6.60 A; Bm=1-128.
DR   PDB; 5APN; EM; 3.91 A; m=1-128.
DR   PDB; 5APO; EM; 3.41 A; m=1-128.
DR   PDB; 5DAT; X-ray; 3.15 A; Q0/q0=77-128.
DR   PDB; 5DC3; X-ray; 3.25 A; Q0/q0=77-128.
DR   PDB; 5DGE; X-ray; 3.45 A; Q0/q0=77-128.
DR   PDB; 5DGF; X-ray; 3.30 A; Q0/q0=77-128.
DR   PDB; 5DGV; X-ray; 3.10 A; Q0/q0=77-128.
DR   PDB; 5FCI; X-ray; 3.40 A; Q0/q0=77-128.
DR   PDB; 5FCJ; X-ray; 3.10 A; Q0/q0=77-128.
DR   PDB; 5GAK; EM; 3.88 A; o=1-128.
DR   PDB; 5I4L; X-ray; 3.10 A; Q0/q0=77-128.
DR   PDB; 5JUO; EM; 4.00 A; RA=1-128.
DR   PDB; 5JUP; EM; 3.50 A; RA=1-128.
DR   PDB; 5JUS; EM; 4.20 A; RA=1-128.
DR   PDB; 5JUT; EM; 4.00 A; RA=1-128.
DR   PDB; 5JUU; EM; 4.00 A; RA=1-128.
DR   PDB; 5LYB; X-ray; 3.25 A; Q0/q0=77-128.
DR   PDB; 5M1J; EM; 3.30 A; m5=77-128.
DR   PDB; 5MC6; EM; 3.80 A; AO=1-128.
DR   PDB; 5MEI; X-ray; 3.50 A; AN/DO=77-128.
DR   PDB; 5NDG; X-ray; 3.70 A; Q0/q0=77-128.
DR   PDB; 5NDV; X-ray; 3.30 A; Q0/q0=77-128.
DR   PDB; 5NDW; X-ray; 3.70 A; Q0/q0=77-128.
DR   PDB; 5OBM; X-ray; 3.40 A; Q0/q0=77-128.
DR   PDB; 5ON6; X-ray; 3.10 A; AN/DO=77-128.
DR   PDB; 5T62; EM; 3.30 A; z=1-128.
DR   PDB; 5T6R; EM; 4.50 A; z=1-128.
DR   PDB; 5TBW; X-ray; 3.00 A; AN/DO=77-128.
DR   PDB; 5TGA; X-ray; 3.30 A; Q0/q0=77-128.
DR   PDB; 5TGM; X-ray; 3.50 A; Q0/q0=77-128.
DR   PDB; 6EF3; EM; 4.17 A; u=1-128.
DR   PDB; 6GQ1; EM; 4.40 A; m=77-128.
DR   PDB; 6GQB; EM; 3.90 A; m=77-128.
DR   PDB; 6GQV; EM; 4.00 A; m=77-128.
DR   PDB; 6HD7; EM; 3.40 A; o=1-128.
DR   PDB; 6HHQ; X-ray; 3.10 A; AN/DO=1-128.
DR   PDB; 6I7O; EM; 5.30 A; AO/XO=77-128.
DR   PDB; 6N8M; EM; 3.50 A; z=1-128.
DR   PDB; 6N8N; EM; 3.80 A; z=1-128.
DR   PDB; 6N8O; EM; 3.50 A; z=1-128.
DR   PDB; 6NYO; X-ray; 1.50 A; E=1-76.
DR   PDB; 6OA9; EM; 3.90 A; H/J/K=1-76.
DR   PDB; 6OAA; EM; 4.10 A; H=1-76.
DR   PDB; 6OIG; EM; 3.80 A; m=77-128.
DR   PDB; 6Q8Y; EM; 3.10 A; AO=77-128.
DR   PDB; 6QIK; EM; 3.10 A; t=1-128.
DR   PDB; 6QT0; EM; 3.40 A; t=1-128.
DR   PDB; 6QTZ; EM; 3.50 A; t=1-128.
DR   PDB; 6R84; EM; 3.60 A; o=77-128.
DR   PDB; 6R86; EM; 3.40 A; o=77-128.
DR   PDB; 6R87; EM; 3.40 A; o=77-128.
DR   PDB; 6RI5; EM; 3.30 A; t=1-128.
DR   PDB; 6S47; EM; 3.28 A; Ao=2-128.
DR   PDB; 6SNT; EM; 2.80 A; ad=1-128.
DR   PDB; 6SV4; EM; 3.30 A; AO/XO/zO=1-128.
DR   PDB; 6T4Q; EM; 2.60 A; Lm=77-128.
DR   PDB; 6T7I; EM; 3.20 A; Lm=1-128.
DR   PDB; 6T7T; EM; 3.10 A; Lm=1-128.
DR   PDB; 6T83; EM; 4.00 A; X/mb=1-128.
DR   PDB; 6TB3; EM; 2.80 A; AO=77-128.
DR   PDB; 6TNU; EM; 3.10 A; AO=77-128.
DR   PDB; 6WOO; EM; 2.90 A; m=78-128.
DR   PDB; 6XIQ; EM; 4.20 A; m=1-128.
DR   PDB; 6Z6J; EM; 3.40 A; Lm=1-128.
DR   PDB; 6Z6K; EM; 3.40 A; Lm=1-128.
DR   PDB; 7AZY; EM; 2.88 A; P=1-128.
DR   PDB; 7B7D; EM; 3.30 A; Li=77-128.
DR   PDB; 7NRC; EM; 3.90 A; Lo=77-128.
DR   PDB; 7NRD; EM; 4.36 A; Lo=77-128.
DR   PDBsum; 3J6X; -.
DR   PDBsum; 3J6Y; -.
DR   PDBsum; 3J77; -.
DR   PDBsum; 3J78; -.
DR   PDBsum; 4U3M; -.
DR   PDBsum; 4U3N; -.
DR   PDBsum; 4U3U; -.
DR   PDBsum; 4U4N; -.
DR   PDBsum; 4U4O; -.
DR   PDBsum; 4U4Q; -.
DR   PDBsum; 4U4R; -.
DR   PDBsum; 4U4U; -.
DR   PDBsum; 4U4Y; -.
DR   PDBsum; 4U4Z; -.
DR   PDBsum; 4U50; -.
DR   PDBsum; 4U51; -.
DR   PDBsum; 4U52; -.
DR   PDBsum; 4U53; -.
DR   PDBsum; 4U55; -.
DR   PDBsum; 4U56; -.
DR   PDBsum; 4U6F; -.
DR   PDBsum; 4V6I; -.
DR   PDBsum; 4V88; -.
DR   PDBsum; 4V8T; -.
DR   PDBsum; 4V8Y; -.
DR   PDBsum; 4V8Z; -.
DR   PDBsum; 5APN; -.
DR   PDBsum; 5APO; -.
DR   PDBsum; 5DAT; -.
DR   PDBsum; 5DC3; -.
DR   PDBsum; 5DGE; -.
DR   PDBsum; 5DGF; -.
DR   PDBsum; 5DGV; -.
DR   PDBsum; 5FCI; -.
DR   PDBsum; 5FCJ; -.
DR   PDBsum; 5GAK; -.
DR   PDBsum; 5I4L; -.
DR   PDBsum; 5JUO; -.
DR   PDBsum; 5JUP; -.
DR   PDBsum; 5JUS; -.
DR   PDBsum; 5JUT; -.
DR   PDBsum; 5JUU; -.
DR   PDBsum; 5LYB; -.
DR   PDBsum; 5M1J; -.
DR   PDBsum; 5MC6; -.
DR   PDBsum; 5MEI; -.
DR   PDBsum; 5NDG; -.
DR   PDBsum; 5NDV; -.
DR   PDBsum; 5NDW; -.
DR   PDBsum; 5OBM; -.
DR   PDBsum; 5ON6; -.
DR   PDBsum; 5T62; -.
DR   PDBsum; 5T6R; -.
DR   PDBsum; 5TBW; -.
DR   PDBsum; 5TGA; -.
DR   PDBsum; 5TGM; -.
DR   PDBsum; 6EF3; -.
DR   PDBsum; 6GQ1; -.
DR   PDBsum; 6GQB; -.
DR   PDBsum; 6GQV; -.
DR   PDBsum; 6HD7; -.
DR   PDBsum; 6HHQ; -.
DR   PDBsum; 6I7O; -.
DR   PDBsum; 6N8M; -.
DR   PDBsum; 6N8N; -.
DR   PDBsum; 6N8O; -.
DR   PDBsum; 6NYO; -.
DR   PDBsum; 6OA9; -.
DR   PDBsum; 6OAA; -.
DR   PDBsum; 6OIG; -.
DR   PDBsum; 6Q8Y; -.
DR   PDBsum; 6QIK; -.
DR   PDBsum; 6QT0; -.
DR   PDBsum; 6QTZ; -.
DR   PDBsum; 6R84; -.
DR   PDBsum; 6R86; -.
DR   PDBsum; 6R87; -.
DR   PDBsum; 6RI5; -.
DR   PDBsum; 6S47; -.
DR   PDBsum; 6SNT; -.
DR   PDBsum; 6SV4; -.
DR   PDBsum; 6T4Q; -.
DR   PDBsum; 6T7I; -.
DR   PDBsum; 6T7T; -.
DR   PDBsum; 6T83; -.
DR   PDBsum; 6TB3; -.
DR   PDBsum; 6TNU; -.
DR   PDBsum; 6WOO; -.
DR   PDBsum; 6XIQ; -.
DR   PDBsum; 6Z6J; -.
DR   PDBsum; 6Z6K; -.
DR   PDBsum; 7AZY; -.
DR   PDBsum; 7B7D; -.
DR   PDBsum; 7NRC; -.
DR   PDBsum; 7NRD; -.
DR   SMR; P0CH08; -.
DR   BioGRID; 34225; 382.
DR   BioGRID; 34844; 193.
DR   IntAct; P0CH08; 1.
DR   STRING; 4932.YKR094C; -.
DR   iPTMnet; P0CH08; -.
DR   SWISS-2DPAGE; P61864; -.
DR   MaxQB; P0CH08; -.
DR   PaxDb; P0CH08; -.
DR   PRIDE; P0CH08; -.
DR   EnsemblFungi; YIL148W_mRNA; YIL148W; YIL148W.
DR   EnsemblFungi; YKR094C_mRNA; YKR094C; YKR094C.
DR   GeneID; 853969; -.
DR   GeneID; 854658; -.
DR   KEGG; sce:YIL148W; -.
DR   KEGG; sce:YKR094C; -.
DR   SGD; S000001410; RPL40A.
DR   VEuPathDB; FungiDB:YIL148W; -.
DR   VEuPathDB; FungiDB:YKR094C; -.
DR   eggNOG; KOG0003; Eukaryota.
DR   HOGENOM; CLU_010412_3_4_1; -.
DR   InParanoid; P0CH08; -.
DR   Reactome; R-SCE-1169408; ISG15 antiviral mechanism.
DR   Reactome; R-SCE-5656169; Termination of translesion DNA synthesis.
DR   PRO; PR:P0CH08; -.
DR   Proteomes; UP000002311; Chromosome IX.
DR   RNAct; P0CH08; protein.
DR   ExpressionAtlas; P0CH08; baseline and differential.
DR   GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR   GO; GO:0005829; C:cytosol; TAS:Reactome.
DR   GO; GO:0022625; C:cytosolic large ribosomal subunit; IDA:SGD.
DR   GO; GO:0005634; C:nucleus; HDA:SGD.
DR   GO; GO:0031386; F:protein tag; ISS:SGD.
DR   GO; GO:0003735; F:structural constituent of ribosome; IC:SGD.
DR   GO; GO:0031625; F:ubiquitin protein ligase binding; IBA:GO_Central.
DR   GO; GO:0002181; P:cytoplasmic translation; IC:SGD.
DR   GO; GO:0019941; P:modification-dependent protein catabolic process; IBA:GO_Central.
DR   GO; GO:0016567; P:protein ubiquitination; IMP:SGD.
DR   GO; GO:0000027; P:ribosomal large subunit assembly; IMP:SGD.
DR   GO; GO:0000055; P:ribosomal large subunit export from nucleus; IMP:SGD.
DR   GO; GO:0042254; P:ribosome biogenesis; IDA:SGD.
DR   Gene3D; 4.10.1060.50; -; 1.
DR   InterPro; IPR038587; L40e_sf.
DR   InterPro; IPR001975; Ribosomal_L40e.
DR   InterPro; IPR000626; Ubiquitin-like_dom.
DR   InterPro; IPR029071; Ubiquitin-like_domsf.
DR   InterPro; IPR019954; Ubiquitin_CS.
DR   InterPro; IPR019956; Ubiquitin_dom.
DR   Pfam; PF01020; Ribosomal_L40e; 1.
DR   Pfam; PF00240; ubiquitin; 1.
DR   SMART; SM01377; Ribosomal_L40e; 1.
DR   SMART; SM00213; UBQ; 1.
DR   SUPFAM; SSF54236; SSF54236; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Cytoplasm; Isopeptide bond; Nucleus; Reference proteome;
KW   Ribonucleoprotein; Ribosomal protein; Ubl conjugation.
FT   CHAIN           1..76
FT                   /note="Ubiquitin"
FT                   /id="PRO_0000396454"
FT   CHAIN           77..128
FT                   /note="60S ribosomal protein L40-A"
FT                   /id="PRO_0000138775"
FT   DOMAIN          1..76
FT                   /note="Ubiquitin-like"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00214"
FT   CROSSLNK        76
FT                   /note="Glycyl lysine isopeptide (Gly-Lys) (interchain with
FT                   K-? in acceptor proteins)"
FT   CROSSLNK        93
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in ubiquitin)"
FT                   /evidence="ECO:0007744|PubMed:22106047"
FT   MUTAGEN         29
FT                   /note="K->R: Deficiency in ubiquitin-protein conjugate
FT                   formation."
FT                   /evidence="ECO:0000269|PubMed:7615550"
FT   MUTAGEN         48
FT                   /note="K->R: Deficiency in ubiquitin-protein conjugate
FT                   formation."
FT                   /evidence="ECO:0000269|PubMed:7615550"
FT   MUTAGEN         63
FT                   /note="K->R: Deficiency in ubiquitin-protein conjugate
FT                   formation. Loss of DNA repair function."
FT                   /evidence="ECO:0000269|PubMed:7615550"
FT   STRAND          1..6
FT                   /evidence="ECO:0007829|PDB:6NYO"
FT   STRAND          12..18
FT                   /evidence="ECO:0007829|PDB:6NYO"
FT   HELIX           23..34
FT                   /evidence="ECO:0007829|PDB:6NYO"
FT   HELIX           38..40
FT                   /evidence="ECO:0007829|PDB:6NYO"
FT   STRAND          41..45
FT                   /evidence="ECO:0007829|PDB:6NYO"
FT   HELIX           57..59
FT                   /evidence="ECO:0007829|PDB:6NYO"
FT   STRAND          66..71
FT                   /evidence="ECO:0007829|PDB:6NYO"
SQ   SEQUENCE   128 AA;  14554 MW;  84BD137A4B1F7797 CRC64;
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