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P0CH07 (RL402_SCHPO) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 28. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | 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

Cleaved into the following 2 chains:

  1. Ubiquitin
  2. 60S ribosomal protein L40
    Alternative name(s):
    CEP52
Gene names
Name:ubi2
Synonyms:uep1
ORF Names:SPAC1805.12c
OrganismSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) [Reference proteome]
Taxonomic identifier284812 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces

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, and DNA-damage responses. Linear polymer chains formed via attachment by the initiator Met lead to cell signaling. Ubiquitin is usually conjugated to Lys residues of target proteins, however, in rare cases, conjugation to Cys or Ser residues has been observed. When polyubiquitin is free (unanchored-polyubiquitin), it also has distinct roles, such as in activation of protein kinases, and in signaling By similarity.

60S ribosomal protein L40: component of the 60S subunit of the ribosome.

Subunit structure

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

Subcellular location

Ubiquitin: Cytoplasm By similarity. Nucleus By similarity.

60S ribosomal protein L40: Cytoplasm By similarity.

Miscellaneous

Ubiquitin is encoded by 5 different genes. Ubi1 and ubi2 are synthesized as a polyprotein with one copy of ubiquitin fused to ribosomal protein L40. Ubi3 and ubi5 are polyproteins with one copy of ubiquitin fused to ribosomal proteins S27a and s27b respectively. Ubi4 is a polyprotein containing 5 exact head to tail repeats of ubiquitin.

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 annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 7676Ubiquitin
PRO_0000396452
Chain77 – 1285260S ribosomal protein L40
PRO_0000396453

Regions

Domain1 – 7676Ubiquitin-like

Amino acid modifications

Cross-link6Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)
Cross-link11Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)
Cross-link27Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)
Cross-link29Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) By similarity
Cross-link33Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)
Cross-link48Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) By similarity
Cross-link63Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) By similarity
Cross-link76Glycyl lysine isopeptide (Gly-Lys) (interchain with K-? in acceptor proteins) By similarity

Secondary structure

.............. 128
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P0CH07 [UniParc].

Last modified August 10, 2010. Version 1.
Checksum: A35EA817EFD46D38

FASTA12814,595
        10         20         30         40         50         60 
MQIFVKTLTG KTITLEVESS DTIDNVKSKI QDKEGIPPDQ QRLIFAGKQL EDGRTLSDYN 

        70         80         90        100        110        120 
IQKESTLHLV LRLRGGIIEP SLKALASKYN CEKQICRKCY ARLPPRATNC RKKKCGHTNQ 


LRPKKKLK 

« Hide

References

[1]"The genome sequence of Schizosaccharomyces pombe."
Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A., Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S., Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M. expand/collapse author list , Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G., Nurse P.
Nature 415:871-880(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 972 / ATCC 24843.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CU329670 Genomic DNA. Translation: CAB55853.1.
PIRT37547.
RefSeqNP_593923.1. NM_001019352.2.
NP_594398.1. NM_001019821.2.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
4II2X-ray2.20B1-76[»]
4II3X-ray2.90B/D1-76[»]
ProteinModelPortalP0CH07.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid278262. 3 interactions.
278890. 14 interactions.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiSPAC11G7.04.1; SPAC11G7.04.1:pep; SPAC11G7.04.
SPAC1805.12c.1; SPAC1805.12c.1:pep; SPAC1805.12c.
GeneID2541768.
2542428.
KEGGspo:SPAC11G7.04.
spo:SPAC1805.12c.

Organism-specific databases

PomBaseSPAC11G7.04.
SPAC1805.12c.

Phylogenomic databases

KOK02927.
OrthoDBEOG7D5B06.
PhylomeDBP0CH07.

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

NextBio20802859.
PROP0CH07.

Entry information

Entry nameRL402_SCHPO
AccessionPrimary (citable) accession number: P0CH07
Secondary accession number(s): O13697 expand/collapse secondary AC list , O14257, P0C014, P0C015, Q76PD0, Q9HDZ4
Entry history
Integrated into UniProtKB/Swiss-Prot: August 10, 2010
Last sequence update: August 10, 2010
Last modified: April 16, 2014
This is version 28 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Ribosomal proteins

Ribosomal proteins families and list of entries

Schizosaccharomyces pombe

Schizosaccharomyces pombe: entries and gene names

PDB cross-references

Index of Protein Data Bank (PDB) cross-references