Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

P0CH07

- RL402_SCHPO

UniProt

P0CH07 - RL402_SCHPO

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

Ubiquitin-60S ribosomal protein L40

Gene

ubi2

Organism
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli

Functioni

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

GO - Molecular functioni

  1. structural constituent of ribosome Source: PomBase

GO - Biological processi

  1. cytoplasmic translation Source: PomBase
  2. ribosome biogenesis Source: PomBase
  3. translation Source: PomBase
Complete GO annotation...

Keywords - Molecular functioni

Ribonucleoprotein, Ribosomal protein

Enzyme and pathway databases

ReactomeiREACT_188294. SRP-dependent cotranslational protein targeting to membrane.
REACT_188524. Antigen processing: Ubiquitination & Proteasome degradation.
REACT_188542. Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC).
REACT_188549. Endosomal Sorting Complex Required For Transport (ESCRT).
REACT_188560. Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).
REACT_188568. ER-Phagosome pathway.
REACT_206850. Formation of a pool of free 40S subunits.
REACT_208775. SCF-beta-TrCP mediated degradation of Emi1.
REACT_215140. CDK-mediated phosphorylation and removal of Cdc6.
REACT_215320. Orc1 removal from chromatin.
REACT_215930. GTP hydrolysis and joining of the 60S ribosomal subunit.
REACT_218991. Ubiquitin Mediated Degradation of Phosphorylated Cdc25A.
REACT_81558. Regulation of activated PAK-2p34 by proteasome mediated degradation.

Names & Taxonomyi

Protein namesi
Recommended name:
Ubiquitin-60S ribosomal protein L40
Cleaved into the following 2 chains:
Alternative name(s):
CEP52
Gene namesi
Name:ubi2
Synonyms:uep1
ORF Names:SPAC1805.12c
OrganismiSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Taxonomic identifieri284812 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces
ProteomesiUP000002485: Chromosome I

Organism-specific databases

PomBaseiSPAC1805.12c.

Subcellular locationi

Chain Ubiquitin : Cytoplasm By similarity. Nucleus By similarity

GO - Cellular componenti

  1. cytosol Source: PomBase
  2. cytosolic large ribosomal subunit Source: PomBase
  3. nucleolus Source: PomBase
  4. nucleus Source: PomBase
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 7676UbiquitinPRO_0000396452Add
BLAST
Chaini77 – 1285260S ribosomal protein L40PRO_0000396453Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Cross-linki6 – 6Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)
Cross-linki11 – 11Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)
Cross-linki27 – 27Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)
Cross-linki29 – 29Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
Cross-linki33 – 33Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)
Cross-linki48 – 48Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
Cross-linki63 – 63Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
Cross-linki76 – 76Glycyl lysine isopeptide (Gly-Lys) (interchain with K-? in acceptor proteins)PROSITE-ProRule annotation

Keywords - PTMi

Isopeptide bond, Ubl conjugation

Interactioni

Subunit structurei

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

Protein-protein interaction databases

BioGridi278262. 6 interactions.
278890. 14 interactions.

Structurei

Secondary structure

128
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi1 – 77
Beta strandi12 – 187
Helixi23 – 3412
Helixi38 – 403
Beta strandi42 – 454
Helixi56 – 594
Beta strandi66 – 705

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4II2X-ray2.20B1-76[»]
4II3X-ray2.90B/D1-76[»]
ProteinModelPortaliP0CH07.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1 – 7676Ubiquitin-likePROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

In the N-terminal section; belongs to the ubiquitin family.Curated
In the C-terminal section; belongs to the ribosomal protein L40e family.Curated
Contains 1 ubiquitin-like domain.PROSITE-ProRule annotation

Phylogenomic databases

InParanoidiP0CH07.
KOiK02927.
OrthoDBiEOG7D5B06.
PhylomeDBiP0CH07.

Family and domain databases

InterProiIPR001975. Ribosomal_L40e.
IPR019956. Ubiquitin.
IPR000626. Ubiquitin-like.
IPR029071. Ubiquitin-rel_dom.
IPR019954. Ubiquitin_CS.
[Graphical view]
PfamiPF01020. Ribosomal_L40e. 1 hit.
PF00240. ubiquitin. 1 hit.
[Graphical view]
PRINTSiPR00348. UBIQUITIN.
SMARTiSM00213. UBQ. 1 hit.
[Graphical view]
SUPFAMiSSF54236. SSF54236. 1 hit.
PROSITEiPS00299. UBIQUITIN_1. 1 hit.
PS50053. UBIQUITIN_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P0CH07-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MQIFVKTLTG KTITLEVESS DTIDNVKSKI QDKEGIPPDQ QRLIFAGKQL
60 70 80 90 100
EDGRTLSDYN IQKESTLHLV LRLRGGIIEP SLKALASKYN CEKQICRKCY
110 120
ARLPPRATNC RKKKCGHTNQ LRPKKKLK
Length:128
Mass (Da):14,595
Last modified:August 10, 2010 - v1
Checksum:iA35EA817EFD46D38
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CU329670 Genomic DNA. Translation: CAB55853.1.
PIRiT37547.
RefSeqiNP_593923.1. NM_001019352.2.
NP_594398.1. NM_001019821.2.

Genome annotation databases

EnsemblFungiiSPAC11G7.04.1; SPAC11G7.04.1:pep; SPAC11G7.04.
SPAC1805.12c.1; SPAC1805.12c.1:pep; SPAC1805.12c.
GeneIDi2541768.
2542428.
KEGGispo:SPAC11G7.04.
spo:SPAC1805.12c.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CU329670 Genomic DNA. Translation: CAB55853.1 .
PIRi T37547.
RefSeqi NP_593923.1. NM_001019352.2.
NP_594398.1. NM_001019821.2.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
4II2 X-ray 2.20 B 1-76 [» ]
4II3 X-ray 2.90 B/D 1-76 [» ]
ProteinModelPortali P0CH07.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 278262. 6 interactions.
278890. 14 interactions.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblFungii SPAC11G7.04.1 ; SPAC11G7.04.1:pep ; SPAC11G7.04 .
SPAC1805.12c.1 ; SPAC1805.12c.1:pep ; SPAC1805.12c .
GeneIDi 2541768.
2542428.
KEGGi spo:SPAC11G7.04.
spo:SPAC1805.12c.

Organism-specific databases

PomBasei SPAC1805.12c.

Phylogenomic databases

InParanoidi P0CH07.
KOi K02927.
OrthoDBi EOG7D5B06.
PhylomeDBi P0CH07.

Enzyme and pathway databases

Reactomei REACT_188294. SRP-dependent cotranslational protein targeting to membrane.
REACT_188524. Antigen processing: Ubiquitination & Proteasome degradation.
REACT_188542. Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC).
REACT_188549. Endosomal Sorting Complex Required For Transport (ESCRT).
REACT_188560. Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).
REACT_188568. ER-Phagosome pathway.
REACT_206850. Formation of a pool of free 40S subunits.
REACT_208775. SCF-beta-TrCP mediated degradation of Emi1.
REACT_215140. CDK-mediated phosphorylation and removal of Cdc6.
REACT_215320. Orc1 removal from chromatin.
REACT_215930. GTP hydrolysis and joining of the 60S ribosomal subunit.
REACT_218991. Ubiquitin Mediated Degradation of Phosphorylated Cdc25A.
REACT_81558. Regulation of activated PAK-2p34 by proteasome mediated degradation.

Miscellaneous databases

NextBioi 20802859.
PROi P0CH07.

Family and domain databases

InterProi IPR001975. Ribosomal_L40e.
IPR019956. Ubiquitin.
IPR000626. Ubiquitin-like.
IPR029071. Ubiquitin-rel_dom.
IPR019954. Ubiquitin_CS.
[Graphical view ]
Pfami PF01020. Ribosomal_L40e. 1 hit.
PF00240. ubiquitin. 1 hit.
[Graphical view ]
PRINTSi PR00348. UBIQUITIN.
SMARTi SM00213. UBQ. 1 hit.
[Graphical view ]
SUPFAMi SSF54236. SSF54236. 1 hit.
PROSITEi PS00299. UBIQUITIN_1. 1 hit.
PS50053. UBIQUITIN_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  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.
    , 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.

Entry informationi

Entry nameiRL402_SCHPO
AccessioniPrimary (citable) accession number: P0CH07
Secondary accession number(s): O13697
, O14257, P0C014, P0C015, Q76PD0, Q9HDZ4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 10, 2010
Last sequence update: August 10, 2010
Last modified: October 29, 2014
This is version 34 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

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.

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. Schizosaccharomyces pombe
    Schizosaccharomyces pombe: entries and gene names
  3. Ribosomal proteins
    Ribosomal proteins families and list of entries
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3