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P62987 (RL40_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 95. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Ubiquitin-60S ribosomal protein L40
Alternative name(s):
CEP52
Ubiquitin A-52 residue ribosomal protein fusion product 1

Cleaved into the following 2 chains:

  1. Ubiquitin
  2. 60S ribosomal protein L40
Gene names
Name:UBA52
Synonyms:UBCEP2
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length128 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

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. Ref.8 Ref.12 Ref.15

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. Ref.8 Ref.12 Ref.15

Subunit structure

Ribosomal protein L40 is part of the 60S ribosomal subunit By similarity. Ref.15 Ref.17

Subcellular location

Ubiquitin: Cytoplasm By similarity. Nucleus By similarity.

60S ribosomal protein L40: Cytoplasm By similarity.

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.

For a better understanding, features related to ubiquitin are only indicated for the first chain.

Sequence similarities

In the N-terminal section; belongs to the ubiquitin family.

In the C-terminal section; belongs to the ribosomal protein L40e family.

Contains 1 ubiquitin-like domain.

Sequence caution

The sequence AAK31162.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

Ontologies

Keywords
   Cellular componentCytoplasm
Nucleus
   Molecular functionRibonucleoprotein
Ribosomal protein
   PTMAcetylation
Isopeptide bond
Methylation
Phosphoprotein
Ubl conjugation
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processDNA damage response, signal transduction by p53 class mediator resulting in cell cycle arrest

Traceable author statement. Source: Reactome

DNA repair

Traceable author statement. Source: Reactome

Fc-epsilon receptor signaling pathway

Traceable author statement. Source: Reactome

G1/S transition of mitotic cell cycle

Traceable author statement. Source: Reactome

G2/M transition of mitotic cell cycle

Traceable author statement. Source: Reactome

I-kappaB kinase/NF-kappaB signaling

Traceable author statement. Source: Reactome

JNK cascade

Traceable author statement. Source: Reactome

MyD88-dependent toll-like receptor signaling pathway

Traceable author statement. Source: Reactome

MyD88-independent toll-like receptor signaling pathway

Traceable author statement. Source: Reactome

Notch receptor processing

Traceable author statement. Source: Reactome

Notch signaling pathway

Traceable author statement. Source: Reactome

RNA metabolic process

Traceable author statement. Source: Reactome

SRP-dependent cotranslational protein targeting to membrane

Traceable author statement. Source: Reactome

T cell receptor signaling pathway

Traceable author statement. Source: Reactome

TRIF-dependent toll-like receptor signaling pathway

Traceable author statement. Source: Reactome

activation of MAPK activity

Traceable author statement. Source: Reactome

anaphase-promoting complex-dependent proteasomal ubiquitin-dependent protein catabolic process

Traceable author statement. Source: Reactome

antigen processing and presentation of exogenous peptide antigen via MHC class I

Traceable author statement. Source: Reactome

antigen processing and presentation of exogenous peptide antigen via MHC class I, TAP-dependent

Traceable author statement. Source: Reactome

antigen processing and presentation of peptide antigen via MHC class I

Traceable author statement. Source: Reactome

apoptotic process

Traceable author statement. Source: Reactome

apoptotic signaling pathway

Traceable author statement. Source: Reactome

carbohydrate metabolic process

Traceable author statement. Source: Reactome

cellular protein metabolic process

Traceable author statement. Source: Reactome

cellular protein modification process

Traceable author statement PubMed 2581967. Source: ProtInc

cellular response to hypoxia

Traceable author statement. Source: Reactome

cytokine-mediated signaling pathway

Traceable author statement. Source: Reactome

endosomal transport

Traceable author statement. Source: Reactome

epidermal growth factor receptor signaling pathway

Traceable author statement. Source: Reactome

fibroblast growth factor receptor signaling pathway

Traceable author statement. Source: Reactome

gene expression

Traceable author statement. Source: Reactome

glucose metabolic process

Traceable author statement. Source: Reactome

glycogen biosynthetic process

Traceable author statement. Source: Reactome

innate immune response

Traceable author statement. Source: Reactome

intracellular transport of virus

Traceable author statement. Source: Reactome

ion transmembrane transport

Traceable author statement. Source: Reactome

mRNA metabolic process

Traceable author statement. Source: Reactome

membrane organization

Traceable author statement. Source: Reactome

mitotic cell cycle

Traceable author statement. Source: Reactome

negative regulation of apoptotic process

Traceable author statement. Source: Reactome

negative regulation of epidermal growth factor receptor signaling pathway

Traceable author statement. Source: Reactome

negative regulation of transcription from RNA polymerase II promoter

Traceable author statement. Source: Reactome

negative regulation of transforming growth factor beta receptor signaling pathway

Traceable author statement. Source: Reactome

negative regulation of type I interferon production

Traceable author statement. Source: Reactome

negative regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle

Traceable author statement. Source: Reactome

neurotrophin TRK receptor signaling pathway

Traceable author statement. Source: Reactome

nuclear-transcribed mRNA catabolic process, nonsense-mediated decay

Traceable author statement. Source: Reactome

nucleotide-binding domain, leucine rich repeat containing receptor signaling pathway

Traceable author statement. Source: Reactome

nucleotide-binding oligomerization domain containing signaling pathway

Traceable author statement. Source: Reactome

positive regulation of I-kappaB kinase/NF-kappaB signaling

Traceable author statement. Source: Reactome

positive regulation of NF-kappaB transcription factor activity

Traceable author statement. Source: Reactome

positive regulation of apoptotic process

Traceable author statement. Source: Reactome

positive regulation of transcription from RNA polymerase II promoter

Traceable author statement. Source: Reactome

positive regulation of type I interferon production

Traceable author statement. Source: Reactome

positive regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle

Traceable author statement. Source: Reactome

protein polyubiquitination

Traceable author statement. Source: Reactome

regulation of apoptotic process

Traceable author statement. Source: Reactome

regulation of transcription from RNA polymerase II promoter in response to hypoxia

Traceable author statement. Source: Reactome

regulation of type I interferon production

Traceable author statement. Source: Reactome

regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle

Traceable author statement. Source: Reactome

small molecule metabolic process

Traceable author statement. Source: Reactome

stress-activated MAPK cascade

Traceable author statement. Source: Reactome

toll-like receptor 10 signaling pathway

Traceable author statement. Source: Reactome

toll-like receptor 2 signaling pathway

Traceable author statement. Source: Reactome

toll-like receptor 3 signaling pathway

Traceable author statement. Source: Reactome

toll-like receptor 4 signaling pathway

Traceable author statement. Source: Reactome

toll-like receptor 5 signaling pathway

Traceable author statement. Source: Reactome

toll-like receptor 9 signaling pathway

Traceable author statement. Source: Reactome

toll-like receptor TLR1:TLR2 signaling pathway

Traceable author statement. Source: Reactome

toll-like receptor TLR6:TLR2 signaling pathway

Traceable author statement. Source: Reactome

toll-like receptor signaling pathway

Traceable author statement. Source: Reactome

transcription initiation from RNA polymerase II promoter

Traceable author statement. Source: Reactome

transcription, DNA-templated

Traceable author statement. Source: Reactome

transforming growth factor beta receptor signaling pathway

Traceable author statement. Source: Reactome

translation

Non-traceable author statement PubMed 12962325. Source: UniProtKB

translational elongation

Traceable author statement. Source: Reactome

translational initiation

Traceable author statement. Source: Reactome

translational termination

Traceable author statement. Source: Reactome

transmembrane transport

Traceable author statement. Source: Reactome

viral life cycle

Traceable author statement. Source: Reactome

viral process

Traceable author statement. Source: Reactome

viral protein processing

Traceable author statement. Source: Reactome

viral transcription

Traceable author statement. Source: Reactome

virion assembly

Traceable author statement. Source: Reactome

   Cellular_componentcytosol

Traceable author statement. Source: Reactome

cytosolic large ribosomal subunit

Inferred from direct assay PubMed 12962325. Source: UniProtKB

endocytic vesicle membrane

Traceable author statement. Source: Reactome

endosome membrane

Traceable author statement. Source: Reactome

lysosomal membrane

Inferred from direct assay PubMed 17897319. Source: UniProtKB

nucleoplasm

Traceable author statement. Source: Reactome

plasma membrane

Traceable author statement. Source: Reactome

ribosome

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular_functionstructural constituent of ribosome

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 7676Ubiquitin
PRO_0000396433
Chain77 – 1285260S ribosomal protein L40
PRO_0000396434

Regions

Domain1 – 7676Ubiquitin-like

Sites

Binding site541Activating enzyme
Binding site721Activating enzyme
Site681Essential for function

Amino acid modifications

Modified residue61N6-acetyllysine; alternate By similarity
Modified residue481N6-acetyllysine; alternate By similarity
Modified residue651Phosphoserine By similarity
Modified residue881N6-acetyllysine Ref.13
Modified residue981N6,N6,N6-trimethyllysine By similarity
Cross-link6Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate Ref.6
Cross-link11Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) Ref.6 Ref.8
Cross-link27Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) Probable
Cross-link29Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) Ref.8
Cross-link33Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) By similarity
Cross-link48Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate Ref.6 Ref.8 Ref.10
Cross-link63Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) Ref.8 Ref.11
Cross-link76Glycyl lysine isopeptide (Gly-Lys) (interchain with K-? in acceptor proteins)

Experimental info

Mutagenesis481K → R: No effect on HLTF-mediated polyubiquitination of PCNA. Ref.11
Mutagenesis631K → R: Abolishes HLTF-mediated polyubiquitination of PCNA. Ref.11

Secondary structure

................. 128
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P62987 [UniParc].

Last modified August 10, 2010. Version 2.
Checksum: 7BCB602ABEFAD02A

FASTA12814,728
        10         20         30         40         50         60 
MQIFVKTLTG KTITLEVEPS DTIENVKAKI QDKEGIPPDQ QRLIFAGKQL EDGRTLSDYN 

        70         80         90        100        110        120 
IQKESTLHLV LRLRGGIIEP SLRQLAQKYN CDKMICRKCY ARLHPRAVNC RKKKCGHTNN 


LRPKKKVK 

« Hide

References

« Hide 'large scale' references
[1]"The human ubiquitin-52 amino acid fusion protein gene shares several structural features with mammalian ribosomal protein genes."
Baker R.T., Board P.G.
Nucleic Acids Res. 19:1035-1040(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
Tissue: Adrenal gland, Lymphocyte and Placenta.
[2]"Human ubiquitin A-52 residue ribosomal protein fusion product 1 (UBA52) in salivary epithelial cells."
Wang H., Zhang Y., Okamoto T.
Submitted (FEB-2001) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]"The DNA sequence and biology of human chromosome 19."
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. expand/collapse author list , 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.
Nature 428:529-535(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]"Molecular conservation of 74 amino acid sequence of ubiquitin between cattle and man."
Schlesinger D.H., Goldstein G.
Nature 255:423-424(1975) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 1-74.
[5]Lubec G., Chen W.-Q., Sun Y.
Submitted (DEC-2008) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 1-27; 30-42 AND 55-72, IDENTIFICATION BY MASS SPECTROMETRY.
Tissue: Fetal brain cortex.
[6]"Alzheimer disease-specific conformation of hyperphosphorylated paired helical filament-tau is polyubiquitinated through Lys-48, Lys-11, and Lys-6 ubiquitin conjugation."
Cripps D., Thomas S.N., Jeng Y., Yang F., Davies P., Yang A.J.
J. Biol. Chem. 281:10825-10838(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 1-27 AND 43-54, UBIQUITINATION AT LYS-6; LYS-11 AND LYS-48, IDENTIFICATION BY MASS SPECTROMETRY.
[7]"cDNA encoding a human homolog of yeast ubiquitin 1."
Salvesen G., Lloyd C., Farley D.
Nucleic Acids Res. 15:5485-5485(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 40-128.
[8]"Differential regulation of EGF receptor internalization and degradation by multiubiquitination within the kinase domain."
Huang F., Kirkpatrick D., Jiang X., Gygi S.P., Sorkin A.
Mol. Cell 21:737-748(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, UBIQUITINATION AT LYS-11; LYS-29; LYS-48 AND LYS-63, IDENTIFICATION BY MASS SPECTROMETRY.
[9]"Functional regulation of FEZ1 by the U-box-type ubiquitin ligase E4B contributes to neuritogenesis."
Okumura F., Hatakeyama S., Matsumoto M., Kamura T., Nakayama K.
J. Biol. Chem. 279:53533-53543(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: UBIQUITINATION AT LYS-27.
[10]"The proteomic reactor facilitates the analysis of affinity-purified proteins by mass spectrometry: application for identifying ubiquitinated proteins in human cells."
Vasilescu J., Zweitzig D.R., Denis N.J., Smith J.C., Ethier M., Haines D.S., Figeys D.
J. Proteome Res. 6:298-305(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-48.
Tissue: Lung adenocarcinoma.
[11]"Polyubiquitination of proliferating cell nuclear antigen by HLTF and SHPRH prevents genomic instability from stalled replication forks."
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.
Proc. Natl. Acad. Sci. U.S.A. 105:12411-12416(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: UBIQUITINATION AT LYS-63, MUTAGENESIS OF LYS-48 AND LYS-63.
[12]"The emerging complexity of protein ubiquitination."
Komander D.
Biochem. Soc. Trans. 37:937-953(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: REVIEW, FUNCTION.
[13]"Lysine acetylation targets protein complexes and co-regulates major cellular functions."
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-88, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[14]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[15]"A ribosome-specialized translation initiation pathway is required for cap-dependent translation of vesicular stomatitis virus mRNAs."
Lee A.S., Burdeinick-Kerr R., Whelan S.P.
Proc. Natl. Acad. Sci. U.S.A. 110:324-329(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBUNIT.
[16]"Determination of structural fluctuations of proteins from structure-based calculations of residual dipolar couplings."
Montalvao R.W., De Simone A., Vendruscolo M.
J. Biomol. NMR 53:281-292(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF 1-76.
[17]"Structures of the human and Drosophila 80S ribosome."
Anger A.M., Armache J.P., Berninghausen O., Habeck M., Subklewe M., Wilson D.N., Beckmann R.
Nature 497:80-85(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY ELECTRON MICROSCOPY (5.0 ANGSTROMS) OF 77-128 IN COMPLEX WITHIN THE RIBOSOME, SUBUNIT.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X56998 mRNA. Translation: CAA40313.1.
X56997 Genomic DNA. Translation: CAA40312.1.
X56999 mRNA. Translation: CAA40314.1.
AF348700 mRNA. Translation: AAK31162.1. Different initiation.
AC005253 Genomic DNA. Translation: AAC25582.1.
Y00361 mRNA. Translation: CAA68439.1.
PIRUQHUR. S34428.
RefSeqNP_001029102.1. NM_001033930.1.
NP_003324.1. NM_003333.3.
UniGeneHs.5308.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2LJ5NMR-A1-76[»]
2MBHNMR-A1-76[»]
2RSUNMR-A1-76[»]
3J3Belectron microscopy5.00m77-128[»]
4HJKX-ray1.78A1-76[»]
4JIOX-ray3.60U1-76[»]
ProteinModelPortalP62987.
SMRP62987. Positions 1-128.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid113159. 56 interactions.
IntActP62987. 13 interactions.
MINTMINT-1137632.
STRING9606.ENSP00000388107.

PTM databases

PhosphoSiteP62987.

Polymorphism databases

DMDM302393718.

Proteomic databases

PaxDbP62987.
PRIDEP62987.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000430157; ENSP00000396910; ENSG00000221983.
ENST00000442744; ENSP00000388107; ENSG00000221983.
ENST00000595158; ENSP00000471622; ENSG00000221983.
ENST00000595683; ENSP00000470419; ENSG00000221983.
ENST00000596273; ENSP00000471062; ENSG00000221983.
ENST00000596304; ENSP00000472264; ENSG00000221983.
ENST00000597451; ENSP00000473048; ENSG00000221983.
ENST00000598780; ENSP00000472545; ENSG00000221983.
ENST00000599551; ENSP00000470507; ENSG00000221983.
ENST00000599595; ENSP00000471464; ENSG00000221983.
GeneID7311.
KEGGhsa:7311.
UCSCuc002njr.3. human.

Organism-specific databases

CTD7311.
GeneCardsGC19P018682.
HGNCHGNC:12458. UBA52.
HPAHPA041344.
MIM191321. gene.
neXtProtNX_P62987.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG5272.
HOVERGENHBG079132.
InParanoidP62987.
KOK02927.
OMAQKYNCEK.
OrthoDBEOG7JDR1W.
PhylomeDBP62987.
TreeFamTF352129.

Enzyme and pathway databases

ReactomeREACT_106849. Receptor-ligand binding initiates the second proteolytic cleavage of Notch receptor.
REACT_111102. Signal Transduction.
REACT_111217. Metabolism.
REACT_11123. Membrane Trafficking.
REACT_115566. Cell Cycle.
REACT_116125. Disease.
REACT_120956. Cellular responses to stress.
REACT_13487. Ubiquitination of PAK-2p34.
REACT_13505. Proteasome mediated degradation of PAK-2p34.
REACT_15518. Transmembrane transport of small molecules.
REACT_17015. Metabolism of proteins.
REACT_1762. 3' -UTR-mediated translational regulation.
REACT_188257. Signal Transduction.
REACT_189085. Disease.
REACT_2001. Receptor-ligand binding initiates the second proteolytic cleavage of Notch receptor.
REACT_21257. Metabolism of RNA.
REACT_21300. Mitotic M-M/G1 phases.
REACT_216. DNA Repair.
REACT_24941. Circadian Clock.
REACT_383. DNA Replication.
REACT_578. Apoptosis.
REACT_6782. TRAF6 Mediated Induction of proinflammatory cytokines.
REACT_6850. Cdc20:Phospho-APC/C mediated degradation of Cyclin A.
REACT_6900. Immune System.
REACT_71. Gene Expression.
REACT_8017. APC-Cdc20 mediated degradation of Nek2A.

Gene expression databases

ArrayExpressP62987.
BgeeP62987.
CleanExHS_UBA52.
GenevestigatorP62987.

Family and domain databases

InterProIPR001975. Ribosomal_L40e.
IPR019956. Ubiquitin.
IPR000626. Ubiquitin-like.
IPR019954. Ubiquitin_CS.
[Graphical view]
PfamPF01020. Ribosomal_L40e. 1 hit.
PF00240. ubiquitin. 1 hit.
[Graphical view]
PRINTSPR00348. UBIQUITIN.
SMARTSM00213. UBQ. 1 hit.
[Graphical view]
PROSITEPS00299. UBIQUITIN_1. 1 hit.
PS50053. UBIQUITIN_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSUBA52. human.
GenomeRNAi7311.
NextBio28582.
PROP62987.
SOURCESearch...

Entry information

Entry nameRL40_HUMAN
AccessionPrimary (citable) accession number: P62987
Secondary accession number(s): P02248 expand/collapse secondary AC list , P02249, P02250, P14793, P62988, Q29120, Q6LBL4, Q6LDU5, Q8WYN8, Q91887, Q91888, Q9BWD6, Q9BX98, Q9UEF2, Q9UEG1, Q9UEK8, Q9UPK7
Entry history
Integrated into UniProtKB/Swiss-Prot: August 31, 2004
Last sequence update: August 10, 2010
Last modified: April 16, 2014
This is version 95 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

Ribosomal proteins

Ribosomal proteins families and list of entries

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 19

Human chromosome 19: entries, gene names and cross-references to MIM