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Ubiquitin-60S ribosomal protein L40 (CEP52) (Ubiquitin A-52 residue ribosomal protein fusion product 1) [Cleaved into: Ubiquitin; 60S ribosomal protein L40 (Large ribosomal subunit protein eL40)]

 RL40_HUMAN              Reviewed;         128 AA.
P62987; P02248; P02249; P02250; P14793; P62988; Q29120; Q6LBL4;
Q6LDU5; Q8WYN8; Q91887; Q91888; 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 133.
RecName: Full=Ubiquitin-60S ribosomal protein L40;
AltName: Full=CEP52;
AltName: Full=Ubiquitin A-52 residue ribosomal protein fusion product 1;
Contains:
RecName: Full=Ubiquitin;
Contains:
RecName: Full=60S ribosomal protein L40;
AltName: Full=Large ribosomal subunit protein eL40 {ECO:0000303|PubMed:24524803};
Flags: Precursor;
Name=UBA52; Synonyms=UBCEP2;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
TISSUE=Adrenal gland, Lymphocyte, and Placenta;
PubMed=1850507; DOI=10.1093/nar/19.5.1035;
Baker R.T., Board P.G.;
"The human ubiquitin-52 amino acid fusion protein gene shares several
structural features with mammalian ribosomal protein genes.";
Nucleic Acids Res. 19:1035-1040(1991).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
Wang H., Zhang Y., Okamoto T.;
"Human ubiquitin A-52 residue ribosomal protein fusion product 1
(UBA52) in salivary epithelial cells.";
Submitted (FEB-2001) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15057824; DOI=10.1038/nature02399;
Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J.,
Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M.,
Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E.,
Caenepeel S., Carrano A.V., Caoile C., Chan Y.M., Christensen M.,
Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C.,
Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M.,
Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T.,
Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H.,
Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S.,
Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J.,
Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M.,
Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J.,
Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D.,
Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A.,
Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I.,
Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E.,
Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M.,
Rubin E.M., Lucas S.M.;
"The DNA sequence and biology of human chromosome 19.";
Nature 428:529-535(2004).
[4]
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).
[5]
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.
[6]
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).
[7]
NUCLEOTIDE SEQUENCE [MRNA] OF 40-128.
PubMed=3037496; DOI=10.1093/nar/15.13.5485;
Salvesen G., Lloyd C., Farley D.;
"cDNA encoding a human homolog of yeast ubiquitin 1.";
Nucleic Acids Res. 15:5485-5485(1987).
[8]
INTERACTION WITH UBQLN1.
PubMed=15147878; DOI=10.1016/j.febslet.2004.04.031;
Ko H.S., Uehara T., Tsuruma K., Nomura Y.;
"Ubiquilin interacts with ubiquitylated proteins and proteasome
through its ubiquitin-associated and ubiquitin-like domains.";
FEBS Lett. 566:110-114(2004).
[9]
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).
[10]
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).
[11]
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).
[12]
REVIEW, AND FUNCTION.
PubMed=19754430; DOI=10.1042/BST0370937;
Komander D.;
"The emerging complexity of protein ubiquitination.";
Biochem. Soc. Trans. 37:937-953(2009).
[13]
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).
[14]
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).
[15]
FUNCTION, AND SUBUNIT.
PubMed=23169626; DOI=10.1073/pnas.1216454109;
Lee A.S., Burdeinick-Kerr R., Whelan S.P.;
"A ribosome-specialized translation initiation pathway is required for
cap-dependent translation of vesicular stomatitis virus mRNAs.";
Proc. Natl. Acad. Sci. U.S.A. 110:324-329(2013).
[16]
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).
[17]
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).
[18]
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).
[19]
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).
[20]
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).
[21]
STRUCTURE BY NMR OF 1-76.
PubMed=22729708; DOI=10.1007/s10858-012-9644-3;
Montalvao R.W., De Simone A., Vendruscolo M.;
"Determination of structural fluctuations of proteins from structure-
based calculations of residual dipolar couplings.";
J. Biomol. NMR 53:281-292(2012).
[22]
STRUCTURE BY ELECTRON MICROSCOPY (5.0 ANGSTROMS) OF 77-128 IN COMPLEX
WITHIN THE RIBOSOME, AND SUBUNIT.
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-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: 60S ribosomal protein L40: Component of the 60S subunit
of the ribosome. Ribosomal protein L40 is essential for
translation of a subset of cellular transcripts, and especially
for cap-dependent translation of vesicular stomatitis virus mRNAs.
-!- SUBUNIT: Ribosomal protein L40 is part of the 60S ribosomal
subunit. Interacts with UBQLN1 (via UBA domain).
{ECO:0000269|PubMed:15147878, ECO:0000269|PubMed:23169626}.
-!- INTERACTION:
Q15038:DAZAP2; NbExp=5; IntAct=EBI-357304, EBI-724310;
Q6ICB0:DESI1; NbExp=4; IntAct=EBI-357304, EBI-2806959;
Q86VP1:TAX1BP1; NbExp=4; IntAct=EBI-357304, EBI-529518;
-!- SUBCELLULAR LOCATION: Ubiquitin: Cytoplasm {ECO:0000250}. Nucleus
{ECO:0000250}.
-!- SUBCELLULAR LOCATION: 60S ribosomal protein L40: Cytoplasm
{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 eL40 family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAK31162.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
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EMBL; X56998; CAA40313.1; -; mRNA.
EMBL; X56997; CAA40312.1; -; Genomic_DNA.
EMBL; X56999; CAA40314.1; -; mRNA.
EMBL; AF348700; AAK31162.1; ALT_INIT; mRNA.
EMBL; AC005253; AAC25582.1; -; Genomic_DNA.
EMBL; Y00361; CAA68439.1; -; mRNA.
CCDS; CCDS12382.1; -.
PIR; S34428; UQHUR.
RefSeq; NP_001029102.1; NM_001033930.2.
RefSeq; NP_001307946.1; NM_001321017.1.
RefSeq; NP_001307947.1; NM_001321018.1.
RefSeq; NP_001307948.1; NM_001321019.1.
RefSeq; NP_001307949.1; NM_001321020.1.
RefSeq; NP_003324.1; NM_003333.4.
UniGene; Hs.5308; -.
PDB; 2LJ5; NMR; -; A=1-76.
PDB; 2MBH; NMR; -; A=1-76.
PDB; 2MJB; NMR; -; A=1-76.
PDB; 2MUR; NMR; -; B=1-76.
PDB; 2N3U; NMR; -; B/C=1-76.
PDB; 2N3V; NMR; -; B/C=1-76.
PDB; 2N3W; NMR; -; B/C=1-76.
PDB; 2NBD; NMR; -; A=1-76.
PDB; 2NBE; NMR; -; A=1-76.
PDB; 2RSU; NMR; -; A=1-76.
PDB; 4HJK; X-ray; 1.78 A; A=1-76.
PDB; 4JIO; X-ray; 3.60 A; U=1-76.
PDB; 4P4H; X-ray; 3.40 A; S/T/U/W/X=1-76.
PDB; 4PIG; X-ray; 1.95 A; A/B/C/D=1-76.
PDB; 4PIH; X-ray; 1.50 A; A/B=1-76.
PDB; 4PIJ; X-ray; 1.50 A; A/B=1-75.
PDB; 4RF0; X-ray; 2.80 A; B=1-75.
PDB; 4RF1; X-ray; 2.15 A; B=1-75.
PDB; 4S1Z; X-ray; 3.03 A; A/B/C/D/E=1-76.
PDB; 4UG0; EM; -; Lm=1-128.
PDB; 4V6X; EM; 5.00 A; Cm=77-128.
PDB; 4XKL; X-ray; 2.10 A; A/C=1-76.
PDB; 5AJ0; EM; 3.50 A; Am=1-128.
PDB; 5GO7; X-ray; 1.80 A; B=10-76.
PDB; 5GO8; X-ray; 2.21 A; B=10-76.
PDB; 5GOB; X-ray; 1.15 A; B=10-76.
PDB; 5GOC; X-ray; 1.73 A; D=10-76.
PDB; 5GOD; X-ray; 1.15 A; C/D=10-76.
PDB; 5GOG; X-ray; 1.98 A; B=10-76.
PDB; 5GOH; X-ray; 1.95 A; D=10-76.
PDB; 5GOI; X-ray; 1.59 A; C/D=10-76.
PDB; 5GOJ; X-ray; 1.55 A; B=10-76.
PDB; 5GOK; X-ray; 1.84 A; B=10-76.
PDB; 5HPK; X-ray; 2.43 A; B=7-79.
PDB; 5HPL; X-ray; 2.31 A; C/D=1-77.
PDB; 5HPS; X-ray; 2.05 A; B=1-83.
PDB; 5HPT; X-ray; 2.84 A; B/E/H=5-78.
PDB; 5J26; X-ray; 2.50 A; B=1-75.
PDB; 5J8P; X-ray; 1.55 A; A=1-76, B=10-75.
PDB; 5JBV; X-ray; 2.10 A; A=1-76, B=10-75.
PDB; 5JBY; X-ray; 1.99 A; A/C/E=1-76, B/D/F=10-75.
PDB; 5LKS; EM; 3.60 A; Lm=1-128.
PDB; 5T2C; EM; 3.60 A; g=1-128.
PDBsum; 2LJ5; -.
PDBsum; 2MBH; -.
PDBsum; 2MJB; -.
PDBsum; 2MUR; -.
PDBsum; 2N3U; -.
PDBsum; 2N3V; -.
PDBsum; 2N3W; -.
PDBsum; 2NBD; -.
PDBsum; 2NBE; -.
PDBsum; 2RSU; -.
PDBsum; 4HJK; -.
PDBsum; 4JIO; -.
PDBsum; 4P4H; -.
PDBsum; 4PIG; -.
PDBsum; 4PIH; -.
PDBsum; 4PIJ; -.
PDBsum; 4RF0; -.
PDBsum; 4RF1; -.
PDBsum; 4S1Z; -.
PDBsum; 4UG0; -.
PDBsum; 4V6X; -.
PDBsum; 4XKL; -.
PDBsum; 5AJ0; -.
PDBsum; 5GO7; -.
PDBsum; 5GO8; -.
PDBsum; 5GOB; -.
PDBsum; 5GOC; -.
PDBsum; 5GOD; -.
PDBsum; 5GOG; -.
PDBsum; 5GOH; -.
PDBsum; 5GOI; -.
PDBsum; 5GOJ; -.
PDBsum; 5GOK; -.
PDBsum; 5HPK; -.
PDBsum; 5HPL; -.
PDBsum; 5HPS; -.
PDBsum; 5HPT; -.
PDBsum; 5J26; -.
PDBsum; 5J8P; -.
PDBsum; 5JBV; -.
PDBsum; 5JBY; -.
PDBsum; 5LKS; -.
PDBsum; 5T2C; -.
ProteinModelPortal; P62987; -.
SMR; P62987; -.
BioGrid; 113159; 101.
IntAct; P62987; 31.
MINT; MINT-1137632; -.
STRING; 9606.ENSP00000388107; -.
iPTMnet; P62987; -.
PhosphoSitePlus; P62987; -.
SwissPalm; P62987; -.
BioMuta; UBA52; -.
DMDM; 302393718; -.
EPD; P62987; -.
PaxDb; P62987; -.
PeptideAtlas; P62987; -.
PRIDE; P62987; -.
TopDownProteomics; P62987; -.
Ensembl; ENST00000430157; ENSP00000396910; ENSG00000221983.
Ensembl; ENST00000442744; ENSP00000388107; ENSG00000221983.
Ensembl; ENST00000595158; ENSP00000471622; ENSG00000221983.
Ensembl; ENST00000595683; ENSP00000470419; ENSG00000221983.
Ensembl; ENST00000596273; ENSP00000471062; ENSG00000221983.
Ensembl; ENST00000596304; ENSP00000472264; ENSG00000221983.
Ensembl; ENST00000597451; ENSP00000473048; ENSG00000221983.
Ensembl; ENST00000598780; ENSP00000472545; ENSG00000221983.
Ensembl; ENST00000599551; ENSP00000470507; ENSG00000221983.
Ensembl; ENST00000599595; ENSP00000471464; ENSG00000221983.
GeneID; 7311; -.
KEGG; hsa:7311; -.
CTD; 7311; -.
DisGeNET; 7311; -.
GeneCards; UBA52; -.
HGNC; HGNC:12458; UBA52.
HPA; HPA041344; -.
HPA; HPA049132; -.
HPA; HPA056624; -.
MIM; 191321; gene.
neXtProt; NX_P62987; -.
OpenTargets; ENSG00000221983; -.
eggNOG; KOG0003; Eukaryota.
eggNOG; COG1552; LUCA.
eggNOG; COG5272; LUCA.
GeneTree; ENSGT00870000136502; -.
HOVERGEN; HBG079132; -.
InParanoid; P62987; -.
KO; K02927; -.
OMA; RKTKCGH; -.
PhylomeDB; P62987; -.
TreeFam; TF352129; -.
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-72689; Formation of a pool of free 40S subunits.
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.
SIGNOR; P62987; -.
ChiTaRS; UBA52; human.
GenomeRNAi; 7311; -.
PRO; PR:P62987; -.
Proteomes; UP000005640; Chromosome 19.
Bgee; ENSG00000221983; -.
CleanEx; HS_UBA52; -.
ExpressionAtlas; P62987; baseline and differential.
Genevisible; P62987; HS.
GO; GO:0005829; C:cytosol; IDA:HPA.
GO; GO:0022625; C:cytosolic large ribosomal subunit; IDA:UniProtKB.
GO; GO:0030666; C:endocytic vesicle membrane; TAS:Reactome.
GO; GO:0005783; C:endoplasmic reticulum; IDA:HPA.
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:0005765; C:lysosomal membrane; IDA:UniProtKB.
GO; GO:0005741; C:mitochondrial outer membrane; TAS:Reactome.
GO; GO:0043209; C:myelin sheath; IEA:Ensembl.
GO; GO:0005654; C:nucleoplasm; IDA:HPA.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0005886; C:plasma membrane; IDA:HPA.
GO; GO:0031982; C:vesicle; IDA:UniProtKB.
GO; GO:0003735; F:structural constituent of ribosome; NAS: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:0006464; P:cellular protein modification process; TAS:ProtInc.
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:0017085; P:response to insecticide; IEA:Ensembl.
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; NAS: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; IPR001975; Ribosomal_L40e.
InterPro; IPR019956; Ubiquitin.
InterPro; IPR029071; Ubiquitin-rel_dom.
InterPro; IPR019954; Ubiquitin_CS.
InterPro; IPR000626; Ubiquitin_dom.
Pfam; PF01020; Ribosomal_L40e; 1.
Pfam; PF00240; ubiquitin; 1.
PRINTS; PR00348; UBIQUITIN.
SMART; SM01377; Ribosomal_L40e; 1.
SMART; SM00213; UBQ; 1.
SUPFAM; SSF54236; SSF54236; 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; Methylation; Nucleus; Phosphoprotein;
Reference proteome; Ribonucleoprotein; Ribosomal protein;
Ubl conjugation.
CHAIN 1 76 Ubiquitin.
/FTId=PRO_0000396433.
CHAIN 77 128 60S ribosomal protein L40.
/FTId=PRO_0000396434.
DOMAIN 1 76 Ubiquitin-like. {ECO:0000255|PROSITE-
ProRule:PRU00214}.
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 98 98 N6,N6,N6-trimethyllysine.
{ECO:0000250|UniProtKB:P62986}.
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:24751536,
ECO:0000269|PubMed:24784582}.
MUTAGEN 65 65 S->D: Phosphomimetic mutant that binds
and activates PRKN.
{ECO:0000269|PubMed:24751536}.
STRAND 2 7 {ECO:0000244|PDB:4PIH}.
STRAND 8 10 {ECO:0000244|PDB:4RF1}.
STRAND 12 16 {ECO:0000244|PDB:5GOD}.
STRAND 19 21 {ECO:0000244|PDB:2MBH}.
HELIX 23 34 {ECO:0000244|PDB:5GOD}.
HELIX 38 40 {ECO:0000244|PDB:5GOD}.
STRAND 41 45 {ECO:0000244|PDB:5GOD}.
STRAND 48 50 {ECO:0000244|PDB:5GO7}.
STRAND 54 56 {ECO:0000244|PDB:4RF1}.
HELIX 57 59 {ECO:0000244|PDB:5GOD}.
STRAND 66 71 {ECO:0000244|PDB:5GOD}.
SEQUENCE 128 AA; 14728 MW; 7BCB602ABEFAD02A CRC64;
MQIFVKTLTG KTITLEVEPS DTIENVKAKI QDKEGIPPDQ QRLIFAGKQL EDGRTLSDYN
IQKESTLHLV LRLRGGIIEP SLRQLAQKYN CDKMICRKCY ARLHPRAVNC RKKKCGHTNN
LRPKKKVK


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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
EH3935 Ubiquitin A 52 Residue Ribosomal Protein Fusion Product 1 Elisa Kit 96T
201-20-6174 UBA52{ubiquitin A-52 residue ribosomal protein fusion product 1}rabbit.pAb 0.2ml
E-EL-H2371 Human UBA52 (Ubiquitin A 52 Residue Ribosomal Protein Fusion Product 1) ELISA Kit 96T
I0043 Ubiquitin A 52 Residue Ribosomal Protein Fusion Product 1 (UBA52), Human, ELISA Kit 96T
H9956 UBA52 (Ubiquitin A 52 Residue Ribosomal Protein Fusion Product 1), Human, ELISA Kit 96T
SEE592Hu ELISA Kit for Ubiquitin A 52 Residue Ribosomal Protein Fusion Product 1 (UBA52) Homo sapiens (Human) 96T
CSB-EL025416PI Pig ubiquitin A-52 residue ribosomal protein fusion product 1 (UBA52) ELISA kit, Species Pig, Sample Type serum, plasma 96T
CSB-EL025416RA Rat ubiquitin A-52 residue ribosomal protein fusion product 1 (UBA52) ELISA kit, Species Rat, Sample Type serum, plasma 96T
CSB-EL025416CA Cat ubiquitin A-52 residue ribosomal protein fusion product 1 (UBA52) ELISA kit, Species Cat, Sample Type serum, plasma 96T
CSB-EL025416DO Dog ubiquitin A-52 residue ribosomal protein fusion product 1 (UBA52) ELISA kit, Species Dog, Sample Type serum, plasma 96T
UBA52 UBA52 Gene ubiquitin A-52 residue ribosomal protein fusion product 1
DL-UBA52-Hu Human Ubiquitin A 52 Residue Ribosomal Protein Fusion Product 1 (UBA52) ELISA Kit 96T
CSB-EL025416SH Sheep ubiquitin A-52 residue ribosomal protein fusion product 1 (UBA52) ELISA kit, Species Sheep, Sample Type serum, plasma 96T
CSB-EL025416HU Human ubiquitin A-52 residue ribosomal protein fusion product 1 (UBA52) ELISA kit, Species Human, Sample Type serum, plasma 96T
CSB-EL025416CH Chicken ubiquitin A-52 residue ribosomal protein fusion product 1 (UBA52) ELISA kit, Species Chicken, Sample Type serum, plasma 96T
CSB-EL025416BO Bovine ubiquitin A-52 residue ribosomal protein fusion product 1 (UBA52) ELISA kit, Species Bovine, Sample Type serum, plasma 96T
CSB-EL025416MO Mouse ubiquitin A-52 residue ribosomal protein fusion product 1 (UBA52) ELISA kit, Species Mouse, Sample Type serum, plasma 96T
E11126h Human Ubiquitin A 52 Residue Ribosomal Protein Fus 96T


 

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