Did you know ? If you order before Friday 14h we deliver 90PCT of the the time next Tuesday, GENTAUR another in time delivery

Ubiquitin-40S ribosomal protein S31 [Cleaved into: Ubiquitin; 40S ribosomal protein S31 (CEP76) (S37) (Small ribosomal subunit protein eS31) (YS24)]

 RS31_YEAST              Reviewed;         152 AA.
P05759; D6VYH3; P04838; P14800; P61864; Q6LA96;
01-NOV-1988, integrated into UniProtKB/Swiss-Prot.
10-AUG-2010, sequence version 3.
10-OCT-2018, entry version 178.
RecName: Full=Ubiquitin-40S ribosomal protein S31;
Contains:
RecName: Full=Ubiquitin;
Contains:
RecName: Full=40S ribosomal protein S31 {ECO:0000303|PubMed:9559554};
AltName: Full=CEP76;
AltName: Full=S37;
AltName: Full=Small ribosomal subunit protein eS31 {ECO:0000303|PubMed:24524803};
AltName: Full=YS24;
Flags: Precursor;
Name=RPS31 {ECO:0000303|PubMed:24524803}; Synonyms=RPS37, UBI3;
OrderedLocusNames=YLR167W; ORFNames=L9470.14;
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces.
NCBI_TaxID=559292;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=3038523;
Oezkaynak E., Finley D., Solomon M.J., Varshavsky A.;
"The yeast ubiquitin genes: a family of natural gene fusions.";
EMBO J. 6:1429-1439(1987).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 204508 / S288c;
PubMed=9169871;
Johnston M., Hillier L.W., Riles L., Albermann K., Andre B.,
Ansorge W., Benes V., Brueckner M., Delius H., Dubois E.,
Duesterhoeft A., Entian K.-D., Floeth M., Goffeau A., Hebling U.,
Heumann K., Heuss-Neitzel D., Hilbert H., Hilger F., Kleine K.,
Koetter P., Louis E.J., Messenguy F., Mewes H.-W., Miosga T.,
Moestl D., Mueller-Auer S., Nentwich U., Obermaier B., Piravandi E.,
Pohl T.M., Portetelle D., Purnelle B., Rechmann S., Rieger M.,
Rinke M., Rose M., Scharfe M., Scherens B., Scholler P., Schwager C.,
Schwarz S., Underwood A.P., Urrestarazu L.A., Vandenbol M.,
Verhasselt P., Vierendeels F., Voet M., Volckaert G., Voss H.,
Wambutt R., Wedler E., Wedler H., Zimmermann F.K., Zollner A.,
Hani J., Hoheisel J.D.;
"The nucleotide sequence of Saccharomyces cerevisiae chromosome XII.";
Nature 387:87-90(1997).
[3]
GENOME REANNOTATION.
STRAIN=ATCC 204508 / S288c;
PubMed=24374639; DOI=10.1534/g3.113.008995;
Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M.,
Cherry J.M.;
"The reference genome sequence of Saccharomyces cerevisiae: Then and
now.";
G3 (Bethesda) 4:389-398(2014).
[4]
PARTIAL PROTEIN SEQUENCE OF 77-95.
PubMed=18782943; DOI=10.1007/BF00341461;
Otaka E., Higo K., Itoh T.;
"Yeast ribosomal proteins. VIII. Isolation of two proteins and
sequence characterization of twenty-four proteins from cytoplasmic
ribosomes.";
Mol. Gen. Genet. 195:544-546(1984).
[5]
IDENTIFICATION OF PROTEIN (S31).
PubMed=2538753; DOI=10.1038/338394a0;
Finley D., Bartel B., Varshavsky A.;
"The tails of ubiquitin precursors are ribosomal proteins whose fusion
to ubiquitin facilitates ribosome biogenesis.";
Nature 338:394-401(1989).
[6]
MUTAGENESIS OF LYS-29; LYS-48 AND LYS-63.
PubMed=7615550; DOI=10.1074/jbc.270.29.17442;
Johnson E.S., Ma P.C.M., Ota I.M., Varshavsky A.;
"A proteolytic pathway that recognizes ubiquitin as a degradation
signal.";
J. Biol. Chem. 270:17442-17456(1995).
[7]
MUTAGENESIS OF LYSINE RESIDUES IN UBIQUITIN.
PubMed=7862120; DOI=10.1128/MCB.15.3.1265;
Spence J., Sadis S., Haas A.L., Finley D.;
"A ubiquitin mutant with specific defects in DNA repair and
multiubiquitination.";
Mol. Cell. Biol. 15:1265-1273(1995).
[8]
NOMENCLATURE, AND SUBUNIT (S31).
PubMed=9559554;
DOI=10.1002/(SICI)1097-0061(19980330)14:5<471::AID-YEA241>3.0.CO;2-U;
Planta R.J., Mager W.H.;
"The list of cytoplasmic ribosomal proteins of Saccharomyces
cerevisiae.";
Yeast 14:471-477(1998).
[9]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-122, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=17287358; DOI=10.1073/pnas.0607084104;
Chi A., Huttenhower C., Geer L.Y., Coon J.J., Syka J.E.P., Bai D.L.,
Shabanowitz J., Burke D.J., Troyanskaya O.G., Hunt D.F.;
"Analysis of phosphorylation sites on proteins from Saccharomyces
cerevisiae by electron transfer dissociation (ETD) mass
spectrometry.";
Proc. Natl. Acad. Sci. U.S.A. 104:2193-2198(2007).
[10]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=18407956; DOI=10.1074/mcp.M700468-MCP200;
Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
"A multidimensional chromatography technology for in-depth
phosphoproteome analysis.";
Mol. Cell. Proteomics 7:1389-1396(2008).
[11]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-122, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19779198; DOI=10.1126/science.1172867;
Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
"Global analysis of Cdk1 substrate phosphorylation sites provides
insights into evolution.";
Science 325:1682-1686(2009).
[12]
NOMENCLATURE.
PubMed=24524803; DOI=10.1016/j.sbi.2014.01.002;
Ban N., Beckmann R., Cate J.H.D., Dinman J.D., Dragon F., Ellis S.R.,
Lafontaine D.L.J., Lindahl L., Liljas A., Lipton J.M., McAlear M.A.,
Moore P.B., Noller H.F., Ortega J., Panse V.G., Ramakrishnan V.,
Spahn C.M.T., Steitz T.A., Tchorzewski M., Tollervey D., Warren A.J.,
Williamson J.R., Wilson D., Yonath A., Yusupov M.;
"A new system for naming ribosomal proteins.";
Curr. Opin. Struct. Biol. 24:165-169(2014).
[13]
X-RAY CRYSTALLOGRAPHY (3.00 ANGSTROMS) OF 80S RIBOSOME, SUBUNIT, AND
SUBCELLULAR LOCATION.
PubMed=22096102; DOI=10.1126/science.1212642;
Ben-Shem A., Garreau de Loubresse N., Melnikov S., Jenner L.,
Yusupova G., Yusupov M.;
"The structure of the eukaryotic ribosome at 3.0 A resolution.";
Science 334:1524-1529(2011).
-!- 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-6-linked may be
involved in DNA repair; Lys-11-linked is involved in ERAD
(endoplasmic reticulum-associated degradation) and in cell-cycle
regulation; Lys-29-linked is involved in lysosomal degradation;
Lys-33-linked is involved in kinase modification; Lys-48-linked is
involved in protein degradation via the proteasome; Lys-63-linked
is involved in endocytosis, and DNA-damage responses. 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: 40S ribosomal protein S31: Component of the ribosome, a
large ribonucleoprotein complex responsible for the synthesis of
proteins in the cell. The small ribosomal subunit (SSU) binds
messenger RNAs (mRNAs) and translates the encoded message by
selecting cognate aminoacyl-transfer RNA (tRNA) molecules. The
large subunit (LSU) contains the ribosomal catalytic site termed
the peptidyl transferase center (PTC), which catalyzes the
formation of peptide bonds, thereby polymerizing the amino acids
delivered by tRNAs into a polypeptide chain. The nascent
polypeptides leave the ribosome through a tunnel in the LSU and
interact with protein factors that function in enzymatic
processing, targeting, and the membrane insertion of nascent
chains at the exit of the ribosomal tunnel.
{ECO:0000305|PubMed:22096102}.
-!- SUBUNIT: Component of the small ribosomal subunit (SSU). Mature
yeast ribosomes consist of a small (40S) and a large (60S)
subunit. The 40S small subunit contains 1 molecule of ribosomal
RNA (18S rRNA) and 33 different proteins (encoded by 57 genes).
The large 60S subunit contains 3 rRNA molecules (25S, 5.8S and 5S
rRNA) and 46 different proteins (encoded by 81 genes)
(PubMed:9559554, PubMed:22096102). {ECO:0000269|PubMed:22096102,
ECO:0000305|PubMed:9559554}.
-!- SUBCELLULAR LOCATION: Ubiquitin: Cytoplasm {ECO:0000250}. Nucleus
{ECO:0000250}.
-!- SUBCELLULAR LOCATION: 40S ribosomal protein S31: Cytoplasm
{ECO:0000269|PubMed:22096102}.
-!- MISCELLANEOUS: Ubiquitin is encoded by several different genes.
UBI1 and UBI2 genes code for a single copy of ubiquitin fused to
the ribosomal proteins eL40. UBI3 is a polyprotein with one copy
of ubiquitin fused to ribosomal protein eS31. UBI4 is a
polyprotein containing 5 exact head to tail repeats of ubiquitin.
{ECO:0000305}.
-!- 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}.
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
Distributed under the Creative Commons Attribution (CC BY 4.0) License
-----------------------------------------------------------------------
EMBL; X05730; CAA29197.1; -; Genomic_DNA.
EMBL; U17246; AAB67466.1; -; Genomic_DNA.
EMBL; BK006945; DAA09489.1; -; Genomic_DNA.
PIR; C29456; UQBYR7.
RefSeq; NP_013268.1; NM_001182054.1.
PDB; 3J6X; EM; 6.10 A; 31=1-152.
PDB; 3J6Y; EM; 6.10 A; 31=1-152.
PDB; 3J77; EM; 6.20 A; 31=1-152.
PDB; 3J78; EM; 6.30 A; 31=1-152.
PDB; 4U3M; X-ray; 3.00 A; E1=77-152, e1=78-152.
PDB; 4U3N; X-ray; 3.20 A; E1=77-152, e1=78-152.
PDB; 4U3U; X-ray; 2.90 A; E1=77-152, e1=78-152.
PDB; 4U4N; X-ray; 3.10 A; E1/e1=77-152.
PDB; 4U4O; X-ray; 3.60 A; E1=78-152, e1=77-152.
PDB; 4U4Q; X-ray; 3.00 A; E1/e1=77-152.
PDB; 4U4R; X-ray; 2.80 A; E1/e1=77-152.
PDB; 4U4U; X-ray; 3.00 A; E1/e1=77-152.
PDB; 4U4Y; X-ray; 3.20 A; E1/e1=77-152.
PDB; 4U4Z; X-ray; 3.10 A; E1/e1=77-152.
PDB; 4U50; X-ray; 3.20 A; E1/e1=78-152.
PDB; 4U51; X-ray; 3.20 A; E1/e1=77-152.
PDB; 4U52; X-ray; 3.00 A; E1/e1=77-152.
PDB; 4U53; X-ray; 3.30 A; E1/e1=77-152.
PDB; 4U55; X-ray; 3.20 A; E1/e1=77-152.
PDB; 4U56; X-ray; 3.45 A; E1/e1=77-152.
PDB; 4U6F; X-ray; 3.10 A; E1/e1=77-152.
PDB; 4V88; X-ray; 3.00 A; Af/Cf=1-152.
PDB; 4V8Y; EM; 4.30 A; A5=1-152.
PDB; 4V8Z; EM; 6.60 A; A5=1-152.
PDB; 4V92; EM; 3.70 A; f=101-152.
PDB; 5DAT; X-ray; 3.15 A; E1/e1=77-152.
PDB; 5DC3; X-ray; 3.25 A; E1/e1=78-152.
PDB; 5DGE; X-ray; 3.45 A; E1/e1=77-152.
PDB; 5DGF; X-ray; 3.30 A; E1/e1=77-152.
PDB; 5DGV; X-ray; 3.10 A; E1/e1=77-152.
PDB; 5FCI; X-ray; 3.40 A; E1/e1=77-152.
PDB; 5FCJ; X-ray; 3.10 A; E1/e1=77-152.
PDB; 5I4L; X-ray; 3.10 A; E1/e1=77-152.
PDB; 5JUO; EM; 4.00 A; CC=1-152.
PDB; 5JUP; EM; 3.50 A; CC=1-152.
PDB; 5JUS; EM; 4.20 A; CC=1-152.
PDB; 5JUT; EM; 4.00 A; CC=1-152.
PDB; 5JUU; EM; 4.00 A; CC=1-152.
PDB; 5L6H; X-ray; 2.30 A; B/D/E=1-76.
PDB; 5L6I; X-ray; 2.76 A; B/D/E=1-76.
PDB; 5L6J; X-ray; 2.68 A; B/D=1-76.
PDB; 5LYB; X-ray; 3.25 A; E1/e1=77-152.
PDB; 5M1J; EM; 3.30 A; f2=82-152.
PDB; 5MC6; EM; 3.80 A; N=1-152.
PDB; 5NDG; X-ray; 3.70 A; E1/e1=1-152.
PDB; 5NDW; X-ray; 3.70 A; E1/e1=80-152.
PDB; 5OBM; X-ray; 3.40 A; E1/e1=81-152.
PDB; 5TGA; X-ray; 3.30 A; E1/e1=77-152.
PDB; 5TGM; X-ray; 3.50 A; E1/e1=77-152.
PDB; 5U4P; X-ray; 2.50 A; C=1-76.
PDB; 5WYJ; EM; 8.70 A; Sg=1-152.
PDB; 6EML; EM; 3.60 A; N=1-152.
PDB; 6GQ1; EM; 4.40 A; AW=116-152.
PDB; 6GQB; EM; 3.90 A; AW=116-152.
PDB; 6GQV; EM; 4.00 A; AW=116-152.
PDBsum; 3J6X; -.
PDBsum; 3J6Y; -.
PDBsum; 3J77; -.
PDBsum; 3J78; -.
PDBsum; 4U3M; -.
PDBsum; 4U3N; -.
PDBsum; 4U3U; -.
PDBsum; 4U4N; -.
PDBsum; 4U4O; -.
PDBsum; 4U4Q; -.
PDBsum; 4U4R; -.
PDBsum; 4U4U; -.
PDBsum; 4U4Y; -.
PDBsum; 4U4Z; -.
PDBsum; 4U50; -.
PDBsum; 4U51; -.
PDBsum; 4U52; -.
PDBsum; 4U53; -.
PDBsum; 4U55; -.
PDBsum; 4U56; -.
PDBsum; 4U6F; -.
PDBsum; 4V88; -.
PDBsum; 4V8Y; -.
PDBsum; 4V8Z; -.
PDBsum; 4V92; -.
PDBsum; 5DAT; -.
PDBsum; 5DC3; -.
PDBsum; 5DGE; -.
PDBsum; 5DGF; -.
PDBsum; 5DGV; -.
PDBsum; 5FCI; -.
PDBsum; 5FCJ; -.
PDBsum; 5I4L; -.
PDBsum; 5JUO; -.
PDBsum; 5JUP; -.
PDBsum; 5JUS; -.
PDBsum; 5JUT; -.
PDBsum; 5JUU; -.
PDBsum; 5L6H; -.
PDBsum; 5L6I; -.
PDBsum; 5L6J; -.
PDBsum; 5LYB; -.
PDBsum; 5M1J; -.
PDBsum; 5MC6; -.
PDBsum; 5NDG; -.
PDBsum; 5NDW; -.
PDBsum; 5OBM; -.
PDBsum; 5TGA; -.
PDBsum; 5TGM; -.
PDBsum; 5U4P; -.
PDBsum; 5WYJ; -.
PDBsum; 6EML; -.
PDBsum; 6GQ1; -.
PDBsum; 6GQB; -.
PDBsum; 6GQV; -.
ProteinModelPortal; P05759; -.
SMR; P05759; -.
BioGrid; 31440; 56.
ComplexPortal; CPX-1599; 40S cytosolic small ribosomal subunit.
DIP; DIP-6389N; -.
IntAct; P05759; 19.
MINT; P05759; -.
STRING; 4932.YLR167W; -.
iPTMnet; P05759; -.
SWISS-2DPAGE; P61864; -.
MaxQB; P05759; -.
PaxDb; P05759; -.
PRIDE; P05759; -.
EnsemblFungi; YLR167W; YLR167W; YLR167W.
GeneID; 850864; -.
KEGG; sce:YLR167W; -.
EuPathDB; FungiDB:YLR167W; -.
SGD; S000004157; RPS31.
GeneTree; ENSGT00910000144152; -.
HOGENOM; HOG000224977; -.
InParanoid; P05759; -.
KO; K02977; -.
OMA; MSILKYY; -.
OrthoDB; EOG092C5P9Y; -.
BioCyc; YEAST:G3O-32297-MONOMER; -.
Reactome; R-SCE-110312; Translesion synthesis by REV1.
Reactome; R-SCE-110314; Recognition of DNA damage by PCNA-containing replication complex.
Reactome; R-SCE-110320; Translesion Synthesis by POLH.
Reactome; R-SCE-156827; L13a-mediated translational silencing of Ceruloplasmin expression.
Reactome; R-SCE-174113; SCF-beta-TrCP mediated degradation of Emi1.
Reactome; R-SCE-1799339; SRP-dependent cotranslational protein targeting to membrane.
Reactome; R-SCE-187577; SCF(Skp2)-mediated degradation of p27/p21.
Reactome; R-SCE-382556; ABC-family proteins mediated transport.
Reactome; R-SCE-450408; AUF1 (hnRNP D0) binds and destabilizes mRNA.
Reactome; R-SCE-5655862; Translesion synthesis by POLK.
Reactome; R-SCE-5656121; Translesion synthesis by POLI.
Reactome; R-SCE-5656169; Termination of translesion DNA synthesis.
Reactome; R-SCE-5675221; Negative regulation of MAPK pathway.
Reactome; R-SCE-5687128; MAPK6/MAPK4 signaling.
Reactome; R-SCE-5689603; UCH proteinases.
Reactome; R-SCE-5689880; Ub-specific processing proteases.
Reactome; R-SCE-5689901; Metalloprotease DUBs.
Reactome; R-SCE-5693565; Recruitment and ATM-mediated phosphorylation of repair and signaling proteins at DNA double strand breaks.
Reactome; R-SCE-5696394; DNA Damage Recognition in GG-NER.
Reactome; R-SCE-5696395; Formation of Incision Complex in GG-NER.
Reactome; R-SCE-5696397; Gap-filling DNA repair synthesis and ligation in GG-NER.
Reactome; R-SCE-5696400; Dual Incision in GG-NER.
Reactome; R-SCE-6781823; Formation of TC-NER Pre-Incision Complex.
Reactome; R-SCE-6782135; Dual incision in TC-NER.
Reactome; R-SCE-6782210; Gap-filling DNA repair synthesis and ligation in TC-NER.
Reactome; R-SCE-68949; Orc1 removal from chromatin.
Reactome; R-SCE-69017; CDK-mediated phosphorylation and removal of Cdc6.
Reactome; R-SCE-69229; Ubiquitin-dependent degradation of Cyclin D1.
Reactome; R-SCE-69601; Ubiquitin Mediated Degradation of Phosphorylated Cdc25A.
Reactome; R-SCE-72689; Formation of a pool of free 40S subunits.
Reactome; R-SCE-72695; Formation of the ternary complex, and subsequently, the 43S complex.
Reactome; R-SCE-72702; Ribosomal scanning and start codon recognition.
Reactome; R-SCE-72706; GTP hydrolysis and joining of the 60S ribosomal subunit.
Reactome; R-SCE-8854050; FBXL7 down-regulates AURKA during mitotic entry and in early mitosis.
Reactome; R-SCE-8866652; Synthesis of active ubiquitin: roles of E1 and E2 enzymes.
Reactome; R-SCE-8866654; E3 ubiquitin ligases ubiquitinate target proteins.
Reactome; R-SCE-9033241; Peroxisomal protein import.
Reactome; R-SCE-917937; Iron uptake and transport.
Reactome; R-SCE-975956; Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC).
Reactome; R-SCE-975957; Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).
Reactome; R-SCE-983168; Antigen processing: Ubiquitination & Proteasome degradation.
PRO; PR:P05759; -.
Proteomes; UP000002311; Chromosome XII.
GO; GO:0022627; C:cytosolic small ribosomal subunit; IDA:SGD.
GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0031386; F:protein tag; IMP:SGD.
GO; GO:0003735; F:structural constituent of ribosome; IC:SGD.
GO; GO:0002181; P:cytoplasmic translation; IC:SGD.
GO; GO:0002109; P:maturation of SSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, LSU-rRNA,5S); IMP:SGD.
GO; GO:0000028; P:ribosomal small subunit assembly; IMP:SGD.
GO; GO:0042254; P:ribosome biogenesis; IMP:SGD.
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; Direct protein sequencing;
Isopeptide bond; Metal-binding; Nucleus; Phosphoprotein;
Reference proteome; Ribonucleoprotein; Ribosomal protein; Zinc;
Zinc-finger.
CHAIN 1 76 Ubiquitin.
/FTId=PRO_0000396487.
CHAIN 77 152 40S ribosomal protein S31.
/FTId=PRO_0000137688.
DOMAIN 1 76 Ubiquitin-like. {ECO:0000255|PROSITE-
ProRule:PRU00214}.
ZN_FING 121 144 C4-type.
COMPBIAS 77 99 Lys-rich (highly basic).
MOD_RES 122 122 Phosphoserine.
{ECO:0000244|PubMed:17287358,
ECO:0000244|PubMed:19779198}.
CROSSLNK 76 76 Glycyl lysine isopeptide (Gly-Lys)
(interchain with K-? in acceptor
proteins).
MUTAGEN 29 29 K->R: Deficiency in ubiquitin-protein
conjugate formation.
{ECO:0000269|PubMed:7615550}.
MUTAGEN 48 48 K->R: Deficiency in ubiquitin-protein
conjugate formation.
{ECO:0000269|PubMed:7615550}.
MUTAGEN 63 63 K->R: Deficiency in ubiquitin-protein
conjugate formation. Loss of DNA repair
function. {ECO:0000269|PubMed:7615550}.
STRAND 2 7 {ECO:0000244|PDB:5L6H}.
STRAND 12 16 {ECO:0000244|PDB:5L6H}.
HELIX 23 34 {ECO:0000244|PDB:5L6H}.
HELIX 38 40 {ECO:0000244|PDB:5L6H}.
STRAND 42 45 {ECO:0000244|PDB:5L6H}.
STRAND 47 49 {ECO:0000244|PDB:5L6H}.
HELIX 57 59 {ECO:0000244|PDB:5L6H}.
STRAND 66 70 {ECO:0000244|PDB:5L6H}.
SEQUENCE 152 AA; 17216 MW; 53BF38E2E2F8B38E CRC64;
MQIFVKTLTG KTITLEVESS DTIDNVKSKI QDKEGIPPDQ QRLIFAGKQL EDGRTLSDYN
IQKESTLHLV LRLRGGGKKR KKKVYTTPKK IKHKHKKVKL AVLSYYKVDA EGKVTKLRRE
CSNPTCGAGV FLANHKDRLY CGKCHSVYKV NA


Related products :

Catalog number Product name Quantity
EIAAB35113 CEP52,Homo sapiens,Human,UBA52,UBCEP2,Ubiquitin A-52 residue ribosomal protein fusion product 1,Ubiquitin-60S ribosomal protein L40
EIAAB35115 Bos taurus,Bovine,UBA52,UBCEP2,Ubiquitin A-52 residue ribosomal protein fusion product 1,Ubiquitin-60S ribosomal protein L40
EIAAB35114 Rat,Rattus norvegicus,Uba52,Ubcep2,Ubiquitin A-52 residue ribosomal protein fusion product 1,Ubiquitin-60S ribosomal protein L40
EIAAB35110 CEP52,Pig,Sus scrofa,UBA52,UBCEP2,Ubiquitin A-52 residue ribosomal protein fusion product 1,Ubiquitin-60S ribosomal protein L40
EIAAB35109 Mouse,Mus musculus,Uba52,Ubcep2,Ubiquitin A-52 residue ribosomal protein fusion product 1,Ubiquitin-60S ribosomal protein L40
EIAAB35112 Chicken,Gallus gallus,UBA52,UBCEP2,Ubiquitin A-52 residue ribosomal protein fusion product 1,Ubiquitin-60S ribosomal protein L40
EIAAB35111 B9,Canis familiaris,Canis lupus familiaris,Dog,UBA52,UBCEP2,Ubiquitin A-52 residue ribosomal protein fusion product 1,Ubiquitin-60S ribosomal protein L40
EIAAB36114 Rat,Rattus norvegicus,Rps27a,Uba80,Ubcep1,Ubiquitin carboxyl extension protein 80,Ubiquitin-40S ribosomal protein S27a
EIAAB36113 Bos taurus,Bovine,RPS27A,UBA80,UBCEP1,Ubiquitin carboxyl extension protein 80,Ubiquitin-40S ribosomal protein S27a
EIAAB36116 Mouse,Mus musculus,Rps27a,Uba80,Ubcep1,Ubiquitin carboxyl extension protein 80,Ubiquitin-40S ribosomal protein S27a
EIAAB36115 Homo sapiens,Human,RPS27A,UBA80,UBCEP1,Ubiquitin carboxyl extension protein 80,Ubiquitin-40S ribosomal protein S27a
EIAAB35293 39S ribosomal protein L27 homolog,39S ribosomal protein L41, mitochondrial,Bcl-2-interacting mitochondrial ribosomal protein L41,BMRP,Cell proliferation-inducing gene 3 protein,Homo sapiens,Human,L41m
29-215 RPL9 is a ribosomal protein that is a component of the 60S subunit. RPL9 belongs to the L6P family of ribosomal proteins. It is located in the cytoplasm. As is typical for genes encoding ribosomal pro 0.1 mg
29-214 RPL9 is a ribosomal protein that is a component of the 60S subunit. RPL9 belongs to the L6P family of ribosomal proteins. It is located in the cytoplasm. As is typical for genes encoding ribosomal pro 0.1 mg
EIAAB36117 Chicken,Gallus gallus,RPS27A,UBA80,Ubiquitin carboxyl extension protein 80,Ubiquitin-40S ribosomal protein S27a
EIAAB35298 28S ribosomal protein S32, mitochondrial,39S ribosomal protein L31, mitochondrial,39S ribosomal protein L42, mitochondrial,Homo sapiens,HSPC204,Human,L31mt,L42mt,MRPL31,MRP-L31,MRPL42,MRP-L42,MRPS32,M
EIAAB35296 28S ribosomal protein S32, mitochondrial,39S ribosomal protein L31, mitochondrial,39S ribosomal protein L42, mitochondrial,D10Ertd322e,L31mt,L42mt,Mouse,MRP-L31,Mrpl42,MRP-L42,Mrps32,MRP-S32,Mus muscu
30-186 Mitochondrial ribosomes (mitoribosomes) consist of a small 28S subunit and a large 39S subunit. MRPS12 is the 28S subunit protein that belongs to the ribosomal protein S12P family. The protein is a ke 0.05 mg
29-216 RPL6 is a ribosomal protein that is a component of the 60S subunit. RPL6 belongs to the L6E family of ribosomal proteins. It is located in the cytoplasm. The protein can bind specifically to domain C 0.1 mg
RL40_PIG Pig ELISA Kit FOR Ubiquitin-60S ribosomal protein L40 96T
EIAAB35182 Mouse,Mus musculus,Probable ribosome biogenesis protein RLP24,Ribosomal L24 domain-containing protein 1,Ribosomal protein L24-like,Rsl24d1
EIAAB35181 C15orf15,Homo sapiens,Human,My024,Probable ribosome biogenesis protein RLP24,Ribosomal L24 domain-containing protein 1,Ribosomal protein L24-like,RPL24L,RSL24D1
I0250 Ubiquitin-60S ribosomal protein L40 (UBA52), Dog, ELISA Kit 96T
I0254 Ubiquitin-60S ribosomal protein L40 (UBA52), Rat, ELISA Kit 96T
E0066h Human ELISA Kit FOR Ubiquitin-60S ribosomal protein L40 96T


 

GENTAUR Belgium BVBA BE0473327336
Voortstraat 49, 1910 Kampenhout BELGIUM
Tel 0032 16 58 90 45

Fax 0032 16 50 90 45
info@gentaur.com | Gentaur





GENTAUR Ltd.
Howard Frank Turnberry House
1404-1410 High Road
Whetstone London N20 9BH
Tel 020 3393 8531 Fax 020 8445 9411
uk@gentaur.com | Gentaur

 

 




GENTAUR France SARL
9, rue Lagrange, 75005 Paris
Tel 01 43 25 01 50

Fax 01 43 25 01 60
RCS Paris B 484 237 888

SIRET 48423788800017

BNP PARIBAS PARIS PL MAUBERT BIC BNPAFRPPPRG

france@gentaur.com | Gentaur

GENTAUR GmbH
Marienbongard 20
52062 Aachen Deutschland
Support Karolina Elandt
Tel: 0035929830070
Fax: (+49) 241 56 00 47 88

Logistic :0241 40 08 90 86
Bankleitzahl 39050000
IBAN lautet DE8839050000107569353
Handelsregister Aachen HR B 16058
Umsatzsteuer-Identifikationsnummer *** DE 815175831
Steuernummer 201/5961/3925
de@gentaur.com | Gentaur

GENTAUR U.S.A
Genprice Inc, Logistics
547, Yurok Circle
San Jose, CA 95123
CA 95123
Tel (408) 780-0908,
Fax (408) 780-0908,
sales@genprice.com

Genprice Inc, Invoices and accounting
6017 Snell Ave, Ste 357
San Jose, CA 95123




GENTAUR Nederland BV
NL850396268B01 KVK nummer 52327027
Kuiper 1
5521 DG Eersel Nederland
Tel:  0208-080893  Fax: 0497-517897
nl@gentaur.com | Gentaur
IBAN: NL04 RABO 0156 9854 62   SWIFT RABONL2U






GENTAUR Spain
tel:0911876558
spain@gentaur.com | Gentaur






ГЕНТАУЪР БЪЛГАРИЯ
ID # 201 358 931 /BULSTAT
София 1000, ул. "Граф Игнатиев" 53 вх. В, ет. 2
Tel 0035924682280 Fax 0035924808322
e-mail: Sofia@gentaur.com | Gentaur
IBAN: BG11FINV91501014771636
BIC: FINVBGSF

GENTAUR Poland Sp. z o.o.


ul. Grunwaldzka 88/A m.2
81-771 Sopot, Poland
TEL Gdansk 058 710 33 44 FAX  058 710 33 48              

poland@gentaur.com | Gentaur

Other countries

Österreich +43720880899

Canada Montreal +15149077481

Ceská republika Praha +420246019719

Danmark +4569918806

Finland Helsset +358942419041

Magyarország Budapest +3619980547

Ireland Dublin+35316526556

Luxembourg+35220880274

Norge Oslo+4721031366

Sverige Stockholm+46852503438

Schweiz Züri+41435006251

US New York+17185132983

GENTAUR Italy
SRL IVA IT03841300167
Piazza Giacomo Matteotti, 6
24122 Bergamo Tel 02 36 00 65 93
Fax 02 36 00 65 94
italia@gentaur.com | Gentaur