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Ubiquitin-40S ribosomal protein S27a (Ubiquitin carboxyl extension protein 80) [Cleaved into: Ubiquitin; 40S ribosomal protein S27a (Small ribosomal subunit protein eS31)]

 RS27A_HUMAN             Reviewed;         156 AA.
P62979; P02248; P02249; P02250; P14798; P62988; Q29120; Q6LBL4;
Q6LDU5; Q8WYN8; Q91887; Q91888; Q9BQ77; Q9BWD6; Q9BX98; Q9UEF2;
Q9UEG1; Q9UEK8; Q9UPK7;
31-AUG-2004, integrated into UniProtKB/Swiss-Prot.
10-AUG-2010, sequence version 2.
30-AUG-2017, entry version 139.
RecName: Full=Ubiquitin-40S ribosomal protein S27a;
AltName: Full=Ubiquitin carboxyl extension protein 80;
Contains:
RecName: Full=Ubiquitin;
Contains:
RecName: Full=40S ribosomal protein S27a;
AltName: Full=Small ribosomal subunit protein eS31 {ECO:0000303|PubMed:24524803};
Flags: Precursor;
Name=RPS27A; Synonyms=UBA80, UBCEP1;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=1657614; DOI=10.1002/eji.1830211113;
Pancre V., Pierce R.J., Fournier F., Mehtali M., Delanoye A.,
Capron A., Auriault C.;
"Effect of ubiquitin on platelet functions: possible identity with
platelet activity suppressive lymphokine (PASL).";
Eur. J. Immunol. 21:2735-2741(1991).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=1370760; DOI=10.1038/bjc.1992.12;
Adams S.M., Sharp M.G., Walker R.A., Brammar W.J., Varley J.M.;
"Differential expression of translation-associated genes in benign and
malignant human breast tumours.";
Br. J. Cancer 65:65-71(1992).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15815621; DOI=10.1038/nature03466;
Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H.,
Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M.,
Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E.,
Kremitzki C., Oddy L., Du H., Sun H., Bradshaw-Cordum H., Ali J.,
Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C.,
Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J.,
Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A.,
Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K.,
Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M.,
Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N.,
Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M.,
Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E.,
Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P.,
Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A.,
Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A.,
Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T.,
Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D.,
Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X.,
McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
Miller W., Eichler E.E., Bork P., Suyama M., Torrents D.,
Waterston R.H., Wilson R.K.;
"Generation and annotation of the DNA sequences of human chromosomes 2
and 4.";
Nature 434:724-731(2005).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Placenta, and Skin;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[5]
PROTEIN SEQUENCE OF 1-98.
TISSUE=Placenta;
PubMed=8706699; DOI=10.1111/j.1432-1033.1996.0144u.x;
Vladimirov S.N., Ivanov A.V., Karpova G.G., Musolyamov A.K.,
Egorov T.A., Thiede B., Wittmann-Liebold B., Otto A.;
"Characterization of the human small-ribosomal-subunit proteins by N-
terminal and internal sequencing, and mass spectrometry.";
Eur. J. Biochem. 239:144-149(1996).
[6]
PROTEIN SEQUENCE OF 1-74.
PubMed=1128706; DOI=10.1038/255423a0;
Schlesinger D.H., Goldstein G.;
"Molecular conservation of 74 amino acid sequence of ubiquitin between
cattle and man.";
Nature 255:423-424(1975).
[7]
PROTEIN SEQUENCE OF 1-27; 30-42 AND 55-72, AND IDENTIFICATION BY MASS
SPECTROMETRY.
TISSUE=Fetal brain cortex;
Lubec G., Chen W.-Q., Sun Y.;
Submitted (DEC-2008) to UniProtKB.
[8]
PROTEIN SEQUENCE OF 1-27 AND 43-54, UBIQUITINATION AT LYS-6; LYS-11
AND LYS-48, AND IDENTIFICATION BY MASS SPECTROMETRY.
PubMed=16443603; DOI=10.1074/jbc.M512786200;
Cripps D., Thomas S.N., Jeng Y., Yang F., Davies P., Yang A.J.;
"Alzheimer disease-specific conformation of hyperphosphorylated paired
helical filament-tau is polyubiquitinated through Lys-48, Lys-11, and
Lys-6 ubiquitin conjugation.";
J. Biol. Chem. 281:10825-10838(2006).
[9]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-34.
PubMed=11875025; DOI=10.1101/gr.214202;
Yoshihama M., Uechi T., Asakawa S., Kawasaki K., Kato S., Higa S.,
Maeda N., Minoshima S., Tanaka T., Shimizu N., Kenmochi N.;
"The human ribosomal protein genes: sequencing and comparative
analysis of 73 genes.";
Genome Res. 12:379-390(2002).
[10]
NUCLEOTIDE SEQUENCE [MRNA] OF 5-156.
PubMed=2581967;
Lund P.K., Moats-Staats B.M., Simmons J.G., Hoyt E., D'Ercole A.J.,
Martin F., van Wyk J.J.;
"Nucleotide sequence analysis of a cDNA encoding human ubiquitin
reveals that ubiquitin is synthesized as a precursor.";
J. Biol. Chem. 260:7609-7613(1985).
[11]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 98-148.
PubMed=9582194;
Kenmochi N., Kawaguchi T., Rozen S., Davis E., Goodman N.,
Hudson T.J., Tanaka T., Page D.C.;
"A map of 75 human ribosomal protein genes.";
Genome Res. 8:509-523(1998).
[12]
FUNCTION, UBIQUITINATION AT LYS-11; LYS-29; LYS-48 AND LYS-63, AND
IDENTIFICATION BY MASS SPECTROMETRY.
PubMed=16543144; DOI=10.1016/j.molcel.2006.02.018;
Huang F., Kirkpatrick D., Jiang X., Gygi S.P., Sorkin A.;
"Differential regulation of EGF receptor internalization and
degradation by multiubiquitination within the kinase domain.";
Mol. Cell 21:737-748(2006).
[13]
UBIQUITINATION AT LYS-27.
PubMed=15466860; DOI=10.1074/jbc.M402916200;
Okumura F., Hatakeyama S., Matsumoto M., Kamura T., Nakayama K.;
"Functional regulation of FEZ1 by the U-box-type ubiquitin ligase E4B
contributes to neuritogenesis.";
J. Biol. Chem. 279:53533-53543(2004).
[14]
UBIQUITINATION AT LYS-63, AND MUTAGENESIS OF LYS-48 AND LYS-63.
PubMed=18719106; DOI=10.1073/pnas.0805685105;
Motegi A., Liaw H.-J., Lee K.-Y., Roest H.P., Maas A., Wu X.,
Moinova H., Markowitz S.D., Ding H., Hoeijmakers J.H.J., Myung K.;
"Polyubiquitination of proliferating cell nuclear antigen by HLTF and
SHPRH prevents genomic instability from stalled replication forks.";
Proc. Natl. Acad. Sci. U.S.A. 105:12411-12416(2008).
[15]
REVIEW, AND FUNCTION.
PubMed=19754430; DOI=10.1042/BST0370937;
Komander D.;
"The emerging complexity of protein ubiquitination.";
Biochem. Soc. Trans. 37:937-953(2009).
[16]
ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-104 AND LYS-113, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19608861; DOI=10.1126/science.1175371;
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
Walther T.C., Olsen J.V., Mann M.;
"Lysine acetylation targets protein complexes and co-regulates major
cellular functions.";
Science 325:834-840(2009).
[17]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[18]
PHOSPHORYLATION AT SER-65, AND MUTAGENESIS OF SER-65.
PubMed=24660806; DOI=10.1042/BJ20140334;
Kazlauskaite A., Kondapalli C., Gourlay R., Campbell D.G.,
Ritorto M.S., Hofmann K., Alessi D.R., Knebel A., Trost M.,
Muqit M.M.;
"Parkin is activated by PINK1-dependent phosphorylation of ubiquitin
at Ser65.";
Biochem. J. 460:127-139(2014).
[19]
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).
[20]
PHOSPHORYLATION AT SER-65, AND MUTAGENESIS OF SER-65.
PubMed=24751536; DOI=10.1083/jcb.201402104;
Kane L.A., Lazarou M., Fogel A.I., Li Y., Yamano K., Sarraf S.A.,
Banerjee S., Youle R.J.;
"PINK1 phosphorylates ubiquitin to activate Parkin E3 ubiquitin ligase
activity.";
J. Cell Biol. 205:143-153(2014).
[21]
PHOSPHORYLATION AT SER-65, AND MUTAGENESIS OF SER-65.
PubMed=24784582; DOI=10.1038/nature13392;
Koyano F., Okatsu K., Kosako H., Tamura Y., Go E., Kimura M.,
Kimura Y., Tsuchiya H., Yoshihara H., Hirokawa T., Endo T., Fon E.A.,
Trempe J.F., Saeki Y., Tanaka K., Matsuda N.;
"Ubiquitin is phosphorylated by PINK1 to activate parkin.";
Nature 510:162-166(2014).
[22]
PHOSPHORYLATION AT SER-65.
PubMed=25527291; DOI=10.15252/embj.201489847;
Wauer T., Swatek K.N., Wagstaff J.L., Gladkova C., Pruneda J.N.,
Michel M.A., Gersch M., Johnson C.M., Freund S.M., Komander D.;
"Ubiquitin Ser65 phosphorylation affects ubiquitin structure, chain
assembly and hydrolysis.";
EMBO J. 34:307-325(2015).
[23]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25944712; DOI=10.1002/pmic.201400617;
Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M.,
Ayoub D., Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
"N-terminome analysis of the human mitochondrial proteome.";
Proteomics 15:2519-2524(2015).
-!- 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, DNA-damage responses as well as in
signaling processes leading to activation of the transcription
factor NF-kappa-B. 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.
-!- FUNCTION: 40S Ribosomal protein S27a: Component of the 40S subunit
of the ribosome.
-!- SUBUNIT: Ribosomal protein S27a is part of the 40S ribosomal
subunit. {ECO:0000250}.
-!- INTERACTION:
Q13137:CALCOCO2; NbExp=3; IntAct=EBI-357375, EBI-739580;
Q15038:DAZAP2; NbExp=8; IntAct=EBI-357375, EBI-724310;
Q9UMX0:UBQLN1; NbExp=4; IntAct=EBI-357375, EBI-741480;
-!- SUBCELLULAR LOCATION: Ubiquitin: Cytoplasm {ECO:0000250}. Nucleus
{ECO:0000250}.
-!- PTM: Ubiquitin: Phosphorylated at Ser-65 by PINK1 during
mitophagy. Phosphorylated ubiquitin specifically binds and
activates parkin (PRKN), triggering mitophagy (PubMed:24660806,
PubMed:24751536, PubMed:24784582, PubMed:25527291).
Phosphorylation does not affect E1-mediated E2 charging of
ubiquitin but affects discharging of E2 enzymes to form
polyubiquitin chains. It also affects deubiquitination by
deubiquitinase enzymes such as USP30 (PubMed:25527291).
{ECO:0000269|PubMed:24660806, ECO:0000269|PubMed:24751536,
ECO:0000269|PubMed:24784582, ECO:0000269|PubMed:25527291}.
-!- MISCELLANEOUS: Ubiquitin is encoded by 4 different genes. UBA52
and RPS27A genes code for a single copy of ubiquitin fused to the
ribosomal proteins L40 and S27a, respectively. UBB and UBC genes
code for a polyubiquitin precursor with exact head to tail
repeats, the number of repeats differ between species and strains.
-!- 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}.
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EMBL; X63237; CAA44911.1; -; mRNA.
EMBL; S79522; AAB21188.1; -; mRNA.
EMBL; AC012358; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC001392; AAH01392.1; -; mRNA.
EMBL; BC066293; AAH66293.1; -; mRNA.
EMBL; AB062071; BAB79490.1; -; Genomic_DNA.
EMBL; M10939; AAA36788.1; -; mRNA.
EMBL; AB007163; BAA25826.1; -; Genomic_DNA.
CCDS; CCDS33202.1; -.
RefSeq; NP_001129064.1; NM_001135592.2.
RefSeq; NP_001170884.1; NM_001177413.1.
RefSeq; NP_002945.1; NM_002954.5.
UniGene; Hs.311640; -.
UniGene; Hs.546292; -.
UniGene; Hs.743392; -.
PDB; 2KHW; NMR; -; B=1-76.
PDB; 2KOX; NMR; -; A=1-76.
PDB; 2KTF; NMR; -; A=1-76.
PDB; 2KWU; NMR; -; B=1-76.
PDB; 2KWV; NMR; -; B=1-76.
PDB; 2L0F; NMR; -; A=1-76.
PDB; 2L0T; NMR; -; A=1-76.
PDB; 2XK5; X-ray; 3.00 A; A/B=1-76.
PDB; 3AXC; X-ray; 2.19 A; A=1-76.
PDB; 3I3T; X-ray; 2.59 A; B/D/F/H=1-75.
PDB; 3K9P; X-ray; 2.80 A; B=1-76.
PDB; 3N30; X-ray; 3.00 A; A/B=1-76.
PDB; 3N32; X-ray; 1.80 A; A=1-76.
PDB; 3NHE; X-ray; 1.26 A; B=1-76.
PDB; 3NOB; X-ray; 2.19 A; A/B/C/D/E/F/G/H=1-76.
PDB; 3NS8; X-ray; 1.71 A; A/B=1-76.
PDB; 3PHD; X-ray; 3.00 A; E/F/G/H=1-76.
PDB; 3PHW; X-ray; 2.00 A; B/D/F/H=1-75.
PDB; 3TBL; X-ray; 2.90 A; D/E=1-76.
PDB; 3VDZ; X-ray; 2.40 A; A/B=1-76.
PDB; 4R62; X-ray; 2.28 A; B=1-76.
PDB; 4UG0; EM; -; Sf=1-156.
PDB; 4V6X; EM; 5.00 A; Af=77-156.
PDB; 5A2Q; EM; 3.90 A; f=78-149.
PDB; 5AJ0; EM; 3.50 A; Bf=1-156.
PDB; 5FLX; EM; 3.90 A; f=1-156.
PDB; 5LKS; EM; 3.60 A; Sf=1-156.
PDB; 5T2C; EM; 3.60 A; AH=1-156.
PDBsum; 2KHW; -.
PDBsum; 2KOX; -.
PDBsum; 2KTF; -.
PDBsum; 2KWU; -.
PDBsum; 2KWV; -.
PDBsum; 2L0F; -.
PDBsum; 2L0T; -.
PDBsum; 2XK5; -.
PDBsum; 3AXC; -.
PDBsum; 3I3T; -.
PDBsum; 3K9P; -.
PDBsum; 3N30; -.
PDBsum; 3N32; -.
PDBsum; 3NHE; -.
PDBsum; 3NOB; -.
PDBsum; 3NS8; -.
PDBsum; 3PHD; -.
PDBsum; 3PHW; -.
PDBsum; 3TBL; -.
PDBsum; 3VDZ; -.
PDBsum; 4R62; -.
PDBsum; 4UG0; -.
PDBsum; 4V6X; -.
PDBsum; 5A2Q; -.
PDBsum; 5AJ0; -.
PDBsum; 5FLX; -.
PDBsum; 5LKS; -.
PDBsum; 5T2C; -.
ProteinModelPortal; P62979; -.
SMR; P62979; -.
BioGrid; 112147; 127.
IntAct; P62979; 29.
MINT; MINT-1138719; -.
STRING; 9606.ENSP00000272317; -.
iPTMnet; P62979; -.
PhosphoSitePlus; P62979; -.
SwissPalm; P62979; -.
BioMuta; RPS27A; -.
DMDM; 302393745; -.
EPD; P62979; -.
MaxQB; P62979; -.
PaxDb; P62979; -.
PeptideAtlas; P62979; -.
PRIDE; P62979; -.
TopDownProteomics; P62979; -.
DNASU; 6233; -.
Ensembl; ENST00000272317; ENSP00000272317; ENSG00000143947.
Ensembl; ENST00000402285; ENSP00000383981; ENSG00000143947.
Ensembl; ENST00000404735; ENSP00000385659; ENSG00000143947.
GeneID; 6233; -.
KEGG; hsa:6233; -.
UCSC; uc002ryk.4; human.
CTD; 6233; -.
DisGeNET; 6233; -.
GeneCards; RPS27A; -.
H-InvDB; HIX0161861; -.
HGNC; HGNC:10417; RPS27A.
HPA; CAB033319; -.
HPA; HPA041344; -.
HPA; HPA049132; -.
HPA; HPA054087; -.
MIM; 191343; gene.
neXtProt; NX_P62979; -.
OpenTargets; ENSG00000143947; -.
PharmGKB; PA34821; -.
eggNOG; KOG0004; Eukaryota.
eggNOG; COG5272; LUCA.
GeneTree; ENSGT00880000137943; -.
HOVERGEN; HBG079148; -.
InParanoid; P62979; -.
KO; K02977; -.
OMA; MSILKYY; -.
OrthoDB; EOG091G178I; -.
PhylomeDB; P62979; -.
TreeFam; TF300036; -.
Reactome; R-HSA-110312; Translesion synthesis by REV1.
Reactome; R-HSA-110314; Recognition of DNA damage by PCNA-containing replication complex.
Reactome; R-HSA-110320; Translesion Synthesis by POLH.
Reactome; R-HSA-1169091; Activation of NF-kappaB in B cells.
Reactome; R-HSA-1169408; ISG15 antiviral mechanism.
Reactome; R-HSA-1234176; Oxygen-dependent proline hydroxylation of Hypoxia-inducible Factor Alpha.
Reactome; R-HSA-1236382; Constitutive Signaling by Ligand-Responsive EGFR Cancer Variants.
Reactome; R-HSA-1236974; ER-Phagosome pathway.
Reactome; R-HSA-1253288; Downregulation of ERBB4 signaling.
Reactome; R-HSA-1295596; Spry regulation of FGF signaling.
Reactome; R-HSA-1358803; Downregulation of ERBB2:ERBB3 signaling.
Reactome; R-HSA-156827; L13a-mediated translational silencing of Ceruloplasmin expression.
Reactome; R-HSA-156902; Peptide chain elongation.
Reactome; R-HSA-162588; Budding and maturation of HIV virion.
Reactome; R-HSA-168638; NOD1/2 Signaling Pathway.
Reactome; R-HSA-168928; RIG-I/MDA5 mediated induction of IFN-alpha/beta pathways.
Reactome; R-HSA-174048; APC/C:Cdc20 mediated degradation of Cyclin B.
Reactome; R-HSA-174084; Autodegradation of Cdh1 by Cdh1:APC/C.
Reactome; R-HSA-174113; SCF-beta-TrCP mediated degradation of Emi1.
Reactome; R-HSA-174154; APC/C:Cdc20 mediated degradation of Securin.
Reactome; R-HSA-174178; APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1.
Reactome; R-HSA-174184; Cdc20:Phospho-APC/C mediated degradation of Cyclin A.
Reactome; R-HSA-174490; Membrane binding and targetting of GAG proteins.
Reactome; R-HSA-175474; Assembly Of The HIV Virion.
Reactome; R-HSA-179409; APC-Cdc20 mediated degradation of Nek2A.
Reactome; R-HSA-1799339; SRP-dependent cotranslational protein targeting to membrane.
Reactome; R-HSA-180534; Vpu mediated degradation of CD4.
Reactome; R-HSA-180585; Vif-mediated degradation of APOBEC3G.
Reactome; R-HSA-182971; EGFR downregulation.
Reactome; R-HSA-187577; SCF(Skp2)-mediated degradation of p27/p21.
Reactome; R-HSA-192823; Viral mRNA Translation.
Reactome; R-HSA-195253; Degradation of beta-catenin by the destruction complex.
Reactome; R-HSA-201681; TCF dependent signaling in response to WNT.
Reactome; R-HSA-202424; Downstream TCR signaling.
Reactome; R-HSA-205043; NRIF signals cell death from the nucleus.
Reactome; R-HSA-209543; p75NTR recruits signalling complexes.
Reactome; R-HSA-209560; NF-kB is activated and signals survival.
Reactome; R-HSA-211733; Regulation of activated PAK-2p34 by proteasome mediated degradation.
Reactome; R-HSA-2122947; NOTCH1 Intracellular Domain Regulates Transcription.
Reactome; R-HSA-2122948; Activated NOTCH1 Transmits Signal to the Nucleus.
Reactome; R-HSA-2173788; Downregulation of TGF-beta receptor signaling.
Reactome; R-HSA-2173791; TGF-beta receptor signaling in EMT (epithelial to mesenchymal transition).
Reactome; R-HSA-2173795; Downregulation of SMAD2/3:SMAD4 transcriptional activity.
Reactome; R-HSA-2173796; SMAD2/SMAD3:SMAD4 heterotrimer regulates transcription.
Reactome; R-HSA-2408557; Selenocysteine synthesis.
Reactome; R-HSA-2467813; Separation of Sister Chromatids.
Reactome; R-HSA-2559580; Oxidative Stress Induced Senescence.
Reactome; R-HSA-2559582; Senescence-Associated Secretory Phenotype (SASP).
Reactome; R-HSA-2559585; Oncogene Induced Senescence.
Reactome; R-HSA-2565942; Regulation of PLK1 Activity at G2/M Transition.
Reactome; R-HSA-2644606; Constitutive Signaling by NOTCH1 PEST Domain Mutants.
Reactome; R-HSA-2672351; Stimuli-sensing channels.
Reactome; R-HSA-2691232; Constitutive Signaling by NOTCH1 HD Domain Mutants.
Reactome; R-HSA-2871837; FCERI mediated NF-kB activation.
Reactome; R-HSA-2894862; Constitutive Signaling by NOTCH1 HD+PEST Domain Mutants.
Reactome; R-HSA-2979096; NOTCH2 Activation and Transmission of Signal to the Nucleus.
Reactome; R-HSA-3134975; Regulation of innate immune responses to cytosolic DNA.
Reactome; R-HSA-3322077; Glycogen synthesis.
Reactome; R-HSA-349425; Autodegradation of the E3 ubiquitin ligase COP1.
Reactome; R-HSA-3769402; Deactivation of the beta-catenin transactivating complex.
Reactome; R-HSA-3785653; Myoclonic epilepsy of Lafora.
Reactome; R-HSA-382556; ABC-family proteins mediated transport.
Reactome; R-HSA-400253; Circadian Clock.
Reactome; R-HSA-445989; TAK1 activates NFkB by phosphorylation and activation of IKKs complex.
Reactome; R-HSA-446652; Interleukin-1 signaling.
Reactome; R-HSA-450302; activated TAK1 mediates p38 MAPK activation.
Reactome; R-HSA-450321; JNK (c-Jun kinases) phosphorylation and activation mediated by activated human TAK1.
Reactome; R-HSA-450408; AUF1 (hnRNP D0) binds and destabilizes mRNA.
Reactome; R-HSA-4608870; Asymmetric localization of PCP proteins.
Reactome; R-HSA-4641257; Degradation of AXIN.
Reactome; R-HSA-4641258; Degradation of DVL.
Reactome; R-HSA-4641263; Regulation of FZD by ubiquitination.
Reactome; R-HSA-5205685; Pink/Parkin Mediated Mitophagy.
Reactome; R-HSA-532668; N-glycan trimming in the ER and Calnexin/Calreticulin cycle.
Reactome; R-HSA-5357905; Regulation of TNFR1 signaling.
Reactome; R-HSA-5357956; TNFR1-induced NFkappaB signaling pathway.
Reactome; R-HSA-5358346; Hedgehog ligand biogenesis.
Reactome; R-HSA-5362768; Hh mutants that don't undergo autocatalytic processing are degraded by ERAD.
Reactome; R-HSA-5607761; Dectin-1 mediated noncanonical NF-kB signaling.
Reactome; R-HSA-5607764; CLEC7A (Dectin-1) signaling.
Reactome; R-HSA-5610780; Degradation of GLI1 by the proteasome.
Reactome; R-HSA-5610783; Degradation of GLI2 by the proteasome.
Reactome; R-HSA-5610785; GLI3 is processed to GLI3R by the proteasome.
Reactome; R-HSA-5632684; Hedgehog 'on' state.
Reactome; R-HSA-5654726; Negative regulation of FGFR1 signaling.
Reactome; R-HSA-5654727; Negative regulation of FGFR2 signaling.
Reactome; R-HSA-5654732; Negative regulation of FGFR3 signaling.
Reactome; R-HSA-5654733; Negative regulation of FGFR4 signaling.
Reactome; R-HSA-5655862; Translesion synthesis by POLK.
Reactome; R-HSA-5656121; Translesion synthesis by POLI.
Reactome; R-HSA-5656169; Termination of translesion DNA synthesis.
Reactome; R-HSA-5658442; Regulation of RAS by GAPs.
Reactome; R-HSA-5668541; TNFR2 non-canonical NF-kB pathway.
Reactome; R-HSA-5675221; Negative regulation of MAPK pathway.
Reactome; R-HSA-5675482; Regulation of necroptotic cell death.
Reactome; R-HSA-5676590; NIK-->noncanonical NF-kB signaling.
Reactome; R-HSA-5678895; Defective CFTR causes cystic fibrosis.
Reactome; R-HSA-5684264; MAP3K8 (TPL2)-dependent MAPK1/3 activation.
Reactome; R-HSA-5685942; HDR through Homologous Recombination (HRR).
Reactome; R-HSA-5687128; MAPK6/MAPK4 signaling.
Reactome; R-HSA-5689603; UCH proteinases.
Reactome; R-HSA-5689877; Josephin domain DUBs.
Reactome; R-HSA-5689880; Ub-specific processing proteases.
Reactome; R-HSA-5689896; Ovarian tumor domain proteases.
Reactome; R-HSA-5689901; Metalloprotease DUBs.
Reactome; R-HSA-5693565; Recruitment and ATM-mediated phosphorylation of repair and signaling proteins at DNA double strand breaks.
Reactome; R-HSA-5693607; Processing of DNA double-strand break ends.
Reactome; R-HSA-5696394; DNA Damage Recognition in GG-NER.
Reactome; R-HSA-5696395; Formation of Incision Complex in GG-NER.
Reactome; R-HSA-5696397; Gap-filling DNA repair synthesis and ligation in GG-NER.
Reactome; R-HSA-5696400; Dual Incision in GG-NER.
Reactome; R-HSA-6781823; Formation of TC-NER Pre-Incision Complex.
Reactome; R-HSA-6781827; Transcription-Coupled Nucleotide Excision Repair (TC-NER).
Reactome; R-HSA-6782135; Dual incision in TC-NER.
Reactome; R-HSA-6782210; Gap-filling DNA repair synthesis and ligation in TC-NER.
Reactome; R-HSA-6783310; Fanconi Anemia Pathway.
Reactome; R-HSA-6791226; Major pathway of rRNA processing in the nucleolus and cytosol.
Reactome; R-HSA-6804756; Regulation of TP53 Activity through Phosphorylation.
Reactome; R-HSA-6804757; Regulation of TP53 Degradation.
Reactome; R-HSA-6804760; Regulation of TP53 Activity through Methylation.
Reactome; R-HSA-6807004; Negative regulation of MET activity.
Reactome; R-HSA-68827; CDT1 association with the CDC6:ORC:origin complex.
Reactome; R-HSA-68949; Orc1 removal from chromatin.
Reactome; R-HSA-69017; CDK-mediated phosphorylation and removal of Cdc6.
Reactome; R-HSA-69229; Ubiquitin-dependent degradation of Cyclin D1.
Reactome; R-HSA-69231; Cyclin D associated events in G1.
Reactome; R-HSA-69298; Association of licensing factors with the pre-replicative complex.
Reactome; R-HSA-69481; G2/M Checkpoints.
Reactome; R-HSA-69541; Stabilization of p53.
Reactome; R-HSA-69601; Ubiquitin Mediated Degradation of Phosphorylated Cdc25A.
Reactome; R-HSA-72649; Translation initiation complex formation.
Reactome; R-HSA-72689; Formation of a pool of free 40S subunits.
Reactome; R-HSA-72695; Formation of the ternary complex, and subsequently, the 43S complex.
Reactome; R-HSA-72702; Ribosomal scanning and start codon recognition.
Reactome; R-HSA-72706; GTP hydrolysis and joining of the 60S ribosomal subunit.
Reactome; R-HSA-72764; Eukaryotic Translation Termination.
Reactome; R-HSA-8849469; PTK6 Regulates RTKs and Their Effectors AKT1 and DOK1.
Reactome; R-HSA-8852276; The role of GTSE1 in G2/M progression after G2 checkpoint.
Reactome; R-HSA-8854050; FBXL7 down-regulates AURKA during mitotic entry and in early mitosis.
Reactome; R-HSA-8856825; Cargo recognition for clathrin-mediated endocytosis.
Reactome; R-HSA-8856828; Clathrin-mediated endocytosis.
Reactome; R-HSA-8863795; Downregulation of ERBB2 signaling.
Reactome; R-HSA-8866652; Synthesis of active ubiquitin: roles of E1 and E2 enzymes.
Reactome; R-HSA-8866654; E3 ubiquitin ligases ubiquitinate target proteins.
Reactome; R-HSA-8875360; InlB-mediated entry of Listeria monocytogenes into host cell.
Reactome; R-HSA-8876493; InlA-mediated entry of Listeria monocytogenes into host cells.
Reactome; R-HSA-8941858; Regulation of RUNX3 expression and activity.
Reactome; R-HSA-8951664; Neddylation.
Reactome; R-HSA-901032; ER Quality Control Compartment (ERQC).
Reactome; R-HSA-912631; Regulation of signaling by CBL.
Reactome; R-HSA-917729; Endosomal Sorting Complex Required For Transport (ESCRT).
Reactome; R-HSA-917937; Iron uptake and transport.
Reactome; R-HSA-936440; Negative regulators of RIG-I/MDA5 signaling.
Reactome; R-HSA-936964; Activation of IRF3/IRF7 mediated by TBK1/IKK epsilon.
Reactome; R-HSA-937039; IRAK1 recruits IKK complex.
Reactome; R-HSA-937041; IKK complex recruitment mediated by RIP1.
Reactome; R-HSA-937042; IRAK2 mediated activation of TAK1 complex.
Reactome; R-HSA-937072; TRAF6 mediated induction of TAK1 complex.
Reactome; R-HSA-975110; TRAF6 mediated IRF7 activation in TLR7/8 or 9 signaling.
Reactome; R-HSA-975144; IRAK1 recruits IKK complex upon TLR7/8 or 9 stimulation.
Reactome; R-HSA-975163; IRAK2 mediated activation of TAK1 complex upon TLR7/8 or 9 stimulation.
Reactome; R-HSA-975956; Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC).
Reactome; R-HSA-975957; Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).
Reactome; R-HSA-977225; Amyloid fiber formation.
Reactome; R-HSA-983168; Antigen processing: Ubiquitination & Proteasome degradation.
ChiTaRS; RPS27A; human.
EvolutionaryTrace; P62979; -.
GeneWiki; RPS27A; -.
GenomeRNAi; 6233; -.
PRO; PR:P62979; -.
Proteomes; UP000005640; Chromosome 2.
Bgee; ENSG00000143947; -.
CleanEx; HS_RPS27A; -.
ExpressionAtlas; P62979; baseline and differential.
Genevisible; P62979; HS.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0022627; C:cytosolic small ribosomal subunit; IDA:UniProtKB.
GO; GO:0030666; C:endocytic vesicle membrane; TAS:Reactome.
GO; GO:0005789; C:endoplasmic reticulum membrane; TAS:Reactome.
GO; GO:0044322; C:endoplasmic reticulum quality control compartment; IEA:GOC.
GO; GO:0010008; C:endosome membrane; TAS:Reactome.
GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
GO; GO:0005615; C:extracellular space; IDA:UniProtKB.
GO; GO:0043657; C:host cell; IEA:GOC.
GO; GO:0016020; C:membrane; IDA:UniProtKB.
GO; GO:0005741; C:mitochondrial outer membrane; TAS:Reactome.
GO; GO:0043209; C:myelin sheath; IEA:Ensembl.
GO; GO:0005730; C:nucleolus; IDA:UniProtKB.
GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0005886; C:plasma membrane; TAS:Reactome.
GO; GO:0015935; C:small ribosomal subunit; IDA:UniProtKB.
GO; GO:0031982; C:vesicle; IDA:UniProtKB.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0003723; F:RNA binding; IDA:UniProtKB.
GO; GO:0003735; F:structural constituent of ribosome; IDA:UniProtKB.
GO; GO:0000187; P:activation of MAPK activity; TAS:Reactome.
GO; GO:0031145; P:anaphase-promoting complex-dependent catabolic process; TAS:Reactome.
GO; GO:0006879; P:cellular iron ion homeostasis; TAS:Reactome.
GO; GO:0044267; P:cellular protein metabolic process; TAS:Reactome.
GO; GO:0042769; P:DNA damage response, detection of DNA damage; TAS:Reactome.
GO; GO:0006977; P:DNA damage response, signal transduction by p53 class mediator resulting in cell cycle arrest; TAS:Reactome.
GO; GO:1904380; P:endoplasmic reticulum mannose trimming; TAS:Reactome.
GO; GO:0016197; P:endosomal transport; TAS:Reactome.
GO; GO:0035635; P:entry of bacterium into host cell; TAS:Reactome.
GO; GO:0038128; P:ERBB2 signaling pathway; TAS:Reactome.
GO; GO:0070987; P:error-free translesion synthesis; TAS:Reactome.
GO; GO:0042276; P:error-prone translesion synthesis; TAS:Reactome.
GO; GO:0038095; P:Fc-epsilon receptor signaling pathway; TAS:Reactome.
GO; GO:0008543; P:fibroblast growth factor receptor signaling pathway; TAS:Reactome.
GO; GO:0000086; P:G2/M transition of mitotic cell cycle; TAS:Reactome.
GO; GO:0070911; P:global genome nucleotide-excision repair; TAS:Reactome.
GO; GO:0005978; P:glycogen biosynthetic process; TAS:Reactome.
GO; GO:0007249; P:I-kappaB kinase/NF-kappaB signaling; TAS:Reactome.
GO; GO:0045087; P:innate immune response; TAS:Reactome.
GO; GO:0036297; P:interstrand cross-link repair; TAS:Reactome.
GO; GO:0075733; P:intracellular transport of virus; TAS:Reactome.
GO; GO:0034220; P:ion transmembrane transport; TAS:Reactome.
GO; GO:0007254; P:JNK cascade; TAS:Reactome.
GO; GO:0016236; P:macroautophagy; TAS:Reactome.
GO; GO:0000165; P:MAPK cascade; TAS:Reactome.
GO; GO:0061024; P:membrane organization; TAS:Reactome.
GO; GO:0002755; P:MyD88-dependent toll-like receptor signaling pathway; TAS:Reactome.
GO; GO:0002756; P:MyD88-independent toll-like receptor signaling pathway; TAS:Reactome.
GO; GO:0043066; P:negative regulation of apoptotic process; TAS:Reactome.
GO; GO:0090090; P:negative regulation of canonical Wnt signaling pathway; TAS:Reactome.
GO; GO:0042059; P:negative regulation of epidermal growth factor receptor signaling pathway; TAS:Reactome.
GO; GO:0010972; P:negative regulation of G2/M transition of mitotic cell cycle; TAS:Reactome.
GO; GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; TAS:Reactome.
GO; GO:0030512; P:negative regulation of transforming growth factor beta receptor signaling pathway; TAS:Reactome.
GO; GO:0032480; P:negative regulation of type I interferon production; TAS:Reactome.
GO; GO:0051436; P:negative regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle; TAS:Reactome.
GO; GO:0038061; P:NIK/NF-kappaB signaling; TAS:Reactome.
GO; GO:0007219; P:Notch signaling pathway; TAS:Reactome.
GO; GO:0000184; P:nuclear-transcribed mRNA catabolic process, nonsense-mediated decay; TAS:Reactome.
GO; GO:0070423; P:nucleotide-binding oligomerization domain containing signaling pathway; TAS:Reactome.
GO; GO:0000715; P:nucleotide-excision repair, DNA damage recognition; TAS:Reactome.
GO; GO:0000717; P:nucleotide-excision repair, DNA duplex unwinding; TAS:Reactome.
GO; GO:0006297; P:nucleotide-excision repair, DNA gap filling; TAS:Reactome.
GO; GO:0033683; P:nucleotide-excision repair, DNA incision; TAS:Reactome.
GO; GO:0006296; P:nucleotide-excision repair, DNA incision, 5'-to lesion; TAS:Reactome.
GO; GO:0006294; P:nucleotide-excision repair, preincision complex assembly; TAS:Reactome.
GO; GO:0043065; P:positive regulation of apoptotic process; TAS:Reactome.
GO; GO:0090263; P:positive regulation of canonical Wnt signaling pathway; TAS:Reactome.
GO; GO:0045742; P:positive regulation of epidermal growth factor receptor signaling pathway; TAS:Reactome.
GO; GO:0043123; P:positive regulation of I-kappaB kinase/NF-kappaB signaling; TAS:Reactome.
GO; GO:0051092; P:positive regulation of NF-kappaB transcription factor activity; TAS:Reactome.
GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; TAS:Reactome.
GO; GO:0051437; P:positive regulation of ubiquitin-protein ligase activity involved in regulation of mitotic cell cycle transition; TAS:Reactome.
GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; TAS:Reactome.
GO; GO:0016579; P:protein deubiquitination; TAS:Reactome.
GO; GO:0006457; P:protein folding; TAS:Reactome.
GO; GO:0000209; P:protein polyubiquitination; TAS:Reactome.
GO; GO:0016567; P:protein ubiquitination; TAS:Reactome.
GO; GO:0042787; P:protein ubiquitination involved in ubiquitin-dependent protein catabolic process; TAS:Reactome.
GO; GO:0043488; P:regulation of mRNA stability; TAS:Reactome.
GO; GO:0060544; P:regulation of necroptotic process; TAS:Reactome.
GO; GO:1901796; P:regulation of signal transduction by p53 class mediator; TAS:Reactome.
GO; GO:0061418; P:regulation of transcription from RNA polymerase II promoter in response to hypoxia; TAS:Reactome.
GO; GO:0010803; P:regulation of tumor necrosis factor-mediated signaling pathway; TAS:Reactome.
GO; GO:0032479; P:regulation of type I interferon production; TAS:Reactome.
GO; GO:0006364; P:rRNA processing; TAS:Reactome.
GO; GO:0031146; P:SCF-dependent proteasomal ubiquitin-dependent protein catabolic process; TAS:Reactome.
GO; GO:0006614; P:SRP-dependent cotranslational protein targeting to membrane; TAS:Reactome.
GO; GO:0002223; P:stimulatory C-type lectin receptor signaling pathway; TAS:Reactome.
GO; GO:0051403; P:stress-activated MAPK cascade; TAS:Reactome.
GO; GO:0050852; P:T cell receptor signaling pathway; TAS:Reactome.
GO; GO:0006283; P:transcription-coupled nucleotide-excision repair; TAS:Reactome.
GO; GO:0007179; P:transforming growth factor beta receptor signaling pathway; TAS:Reactome.
GO; GO:0006412; P:translation; IC:UniProtKB.
GO; GO:0006413; P:translational initiation; TAS:Reactome.
GO; GO:0019985; P:translesion synthesis; TAS:Reactome.
GO; GO:0055085; P:transmembrane transport; TAS:Reactome.
GO; GO:0035666; P:TRIF-dependent toll-like receptor signaling pathway; TAS:Reactome.
GO; GO:0033209; P:tumor necrosis factor-mediated signaling pathway; TAS:Reactome.
GO; GO:0019058; P:viral life cycle; TAS:Reactome.
GO; GO:0019083; P:viral transcription; TAS:Reactome.
GO; GO:0019068; P:virion assembly; TAS:Reactome.
GO; GO:0016055; P:Wnt signaling pathway; TAS:Reactome.
GO; GO:0060071; P:Wnt signaling pathway, planar cell polarity pathway; TAS:Reactome.
InterPro; IPR002906; Ribosomal_S27a.
InterPro; IPR011332; Ribosomal_zn-bd.
InterPro; IPR019956; Ubiquitin.
InterPro; IPR029071; Ubiquitin-rel_dom.
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; Acetylation; Complete proteome; Cytoplasm;
Direct protein sequencing; Isopeptide bond; Metal-binding; Nucleus;
Phosphoprotein; Reference proteome; Ribonucleoprotein;
Ribosomal protein; Ubl conjugation; Zinc; Zinc-finger.
CHAIN 1 76 Ubiquitin.
/FTId=PRO_0000396477.
CHAIN 77 156 40S ribosomal protein S27a.
/FTId=PRO_0000396478.
DOMAIN 1 76 Ubiquitin-like. {ECO:0000255|PROSITE-
ProRule:PRU00214}.
ZN_FING 121 144 C4-type.
COMPBIAS 77 99 Lys-rich (highly basic).
BINDING 54 54 Activating enzyme.
BINDING 72 72 Activating enzyme.
SITE 68 68 Essential for function.
MOD_RES 65 65 Phosphoserine; by PINK1.
{ECO:0000269|PubMed:24660806,
ECO:0000269|PubMed:24751536,
ECO:0000269|PubMed:24784582,
ECO:0000269|PubMed:25527291}.
MOD_RES 104 104 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
MOD_RES 113 113 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
MOD_RES 152 152 N6-acetyllysine.
{ECO:0000250|UniProtKB:P62983}.
CROSSLNK 6 6 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin).
{ECO:0000269|PubMed:16443603}.
CROSSLNK 11 11 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin).
{ECO:0000269|PubMed:16443603,
ECO:0000269|PubMed:16543144}.
CROSSLNK 27 27 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin).
{ECO:0000305|PubMed:15466860}.
CROSSLNK 29 29 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin).
{ECO:0000269|PubMed:16543144}.
CROSSLNK 48 48 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin).
{ECO:0000269|PubMed:16443603,
ECO:0000269|PubMed:16543144}.
CROSSLNK 63 63 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin).
{ECO:0000269|PubMed:16543144,
ECO:0000269|PubMed:18719106}.
CROSSLNK 76 76 Glycyl lysine isopeptide (Gly-Lys)
(interchain with K-? in acceptor
proteins).
MUTAGEN 48 48 K->R: No effect on HLTF-mediated
polyubiquitination of PCNA.
{ECO:0000269|PubMed:18719106}.
MUTAGEN 63 63 K->R: Abolishes HLTF-mediated
polyubiquitination of PCNA.
{ECO:0000269|PubMed:18719106}.
MUTAGEN 65 65 S->A: Prevents phosphorylation in case of
mitophagy. {ECO:0000269|PubMed:24660806,
ECO:0000269|PubMed:24784582}.
MUTAGEN 65 65 S->D: Phosphomimetic mutant that binds
and activates PRKN.
{ECO:0000269|PubMed:24751536}.
STRAND 2 6 {ECO:0000244|PDB:3NHE}.
STRAND 8 10 {ECO:0000244|PDB:3NHE}.
STRAND 12 16 {ECO:0000244|PDB:3NHE}.
HELIX 23 34 {ECO:0000244|PDB:3NHE}.
HELIX 38 40 {ECO:0000244|PDB:3NHE}.
STRAND 42 45 {ECO:0000244|PDB:3NHE}.
HELIX 57 59 {ECO:0000244|PDB:3NHE}.
STRAND 66 70 {ECO:0000244|PDB:3NHE}.
SEQUENCE 156 AA; 17965 MW; 617BC63DF3A904F7 CRC64;
MQIFVKTLTG KTITLEVEPS DTIENVKAKI QDKEGIPPDQ QRLIFAGKQL EDGRTLSDYN
IQKESTLHLV LRLRGGAKKR KKKSYTTPKK NKHKRKKVKL AVLKYYKVDE NGKISRLRRE
CPSDECGAGV FMASHFDRHY CGKCCLTYCF NKPEDK


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CSB-EL020420RA Rat Ubiquitin-40S ribosomal protein S27a(RPS27A) ELISA kit SpeciesRat 96T
I0241 Ubiquitin-40S ribosomal protein S27a (RPS27A), Bovine, ELISA Kit 96T
CSB-EL020420HU Human Ubiquitin-40S ribosomal protein S27a(RPS27A) ELISA kit 96T
CSB-EL020420BO Bovine Ubiquitin-40S ribosomal protein S27a(RPS27A) ELISA kit 96T
I0245 Ubiquitin-40S ribosomal protein S27a (RPS27A), Mouse, ELISA Kit 96T
CSB-EL020420CH Chicken Ubiquitin-40S ribosomal protein S27a(RPS27A) ELISA kit SpeciesChicken 96T
CSB-EL020420HU Human Ubiquitin-40S ribosomal protein S27a(RPS27A) ELISA kit SpeciesHuman 96T
CSB-EL020420MO Mouse Ubiquitin-40S ribosomal protein S27a(RPS27A) ELISA kit SpeciesMouse 96T
CSB-EL020420BO Bovine Ubiquitin-40S ribosomal protein S27a(RPS27A) ELISA kit SpeciesBovine 96T
RS27A_RAT ELISA Kit FOR Ubiquitin-40S ribosomal protein S27a; organism: Rat; gene name: Rps27a 96T
CSB-EL020420GU Guinea pig Ubiquitin-40S ribosomal protein S27a(RPS27A) ELISA kit SpeciesGuinea pig 96T
EIAAB35113 CEP52,Homo sapiens,Human,UBA52,UBCEP2,Ubiquitin A-52 residue ribosomal protein fusion product 1,Ubiquitin-60S ribosomal protein L40


 

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