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Protein

Ubiquitin-40S ribosomal protein S27a

Gene

ubi3

Organism
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Status
Reviewed-Annotation score: 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
Ribosomal protein S27a is a component of the 40S subunit of the ribosome.

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri121 – 14222C4-typeBy similarityAdd
BLAST

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Ribonucleoprotein, Ribosomal protein

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

ReactomeiR-SPO-110312. Translesion synthesis by REV1.
R-SPO-110314. Recognition of DNA damage by PCNA-containing replication complex.
R-SPO-110320. Translesion Synthesis by POLH.
R-SPO-156827. L13a-mediated translational silencing of Ceruloplasmin expression.
R-SPO-174113. SCF-beta-TrCP mediated degradation of Emi1.
R-SPO-1799339. SRP-dependent cotranslational protein targeting to membrane.
R-SPO-5632684. Hedgehog 'on' state.
R-SPO-5655862. Translesion synthesis by POLK.
R-SPO-5656121. Translesion synthesis by POLI.
R-SPO-5656169. Termination of translesion DNA synthesis.
R-SPO-5696395. Formation of Incision Complex in GG-NER.
R-SPO-5696400. Dual Incision in GG-NER.
R-SPO-6781823. Formation of TC-NER Pre-Incision Complex.
R-SPO-6782135. Dual incision in TC-NER.
R-SPO-6782210. Gap-filling DNA repair synthesis and ligation in TC-NER.
R-SPO-68949. Orc1 removal from chromatin.
R-SPO-69017. CDK-mediated phosphorylation and removal of Cdc6.
R-SPO-69229. Ubiquitin-dependent degradation of Cyclin D1.
R-SPO-69601. Ubiquitin Mediated Degradation of Phosphorylated Cdc25A.
R-SPO-72649. Translation initiation complex formation.
R-SPO-72689. Formation of a pool of free 40S subunits.
R-SPO-72695. Formation of the ternary complex, and subsequently, the 43S complex.
R-SPO-72702. Ribosomal scanning and start codon recognition.
R-SPO-72706. GTP hydrolysis and joining of the 60S ribosomal subunit.
R-SPO-917729. Endosomal Sorting Complex Required For Transport (ESCRT).
R-SPO-975956. Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC).
R-SPO-975957. Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).
R-SPO-983168. Antigen processing: Ubiquitination & Proteasome degradation.

Names & Taxonomyi

Protein namesi
Recommended name:
Ubiquitin-40S ribosomal protein S27a
Cleaved into the following 2 chains:
Gene namesi
Name:ubi3
ORF Names:SPAC6G10.11c
OrganismiSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Taxonomic identifieri284812 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces
Proteomesi
  • UP000002485 Componenti: Chromosome I

Organism-specific databases

EuPathDBiFungiDB:SPAC6G10.11c.
PomBaseiSPAC6G10.11c. ubi3.

Subcellular locationi

Ubiquitin :

GO - Cellular componenti

  • cytoplasm Source: PomBase
  • cytosol Source: PomBase
  • cytosolic small ribosomal subunit Source: PomBase
  • nucleus Source: PomBase
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 7676UbiquitinPRO_0000396486Add
BLAST
Chaini77 – 1507440S ribosomal protein S27aPRO_0000137687Add
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

Proteomic databases

PRIDEiP0C016.

Interactioni

Subunit structurei

Ribosomal protein S27a is part of the 40S ribosomal subunit.By similarity

Protein-protein interaction databases

BioGridi277950. 3 interactions.

Structurei

3D structure databases

ProteinModelPortaliP0C016.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

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

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi77 – 9721Lys-rich (highly basic)Add
BLAST

Sequence similaritiesi

In the N-terminal section; belongs to the ubiquitin family.Curated
In the C-terminal section; belongs to the ribosomal protein S27Ae family.Curated
Contains 1 ubiquitin-like domain.PROSITE-ProRule annotation

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri121 – 14222C4-typeBy similarityAdd
BLAST

Keywords - Domaini

Zinc-finger

Phylogenomic databases

HOGENOMiHOG000233943.
InParanoidiP0C016.
KOiK02977.
OMAiMSILKYY.
OrthoDBiEOG7D5B06.
PhylomeDBiP0C016.

Family and domain databases

InterProiIPR002906. Ribosomal_S27a.
IPR011332. Ribosomal_zn-bd.
IPR019956. Ubiquitin.
IPR029071. Ubiquitin-rel_dom.
IPR019954. Ubiquitin_CS.
IPR000626. Ubiquitin_dom.
[Graphical view]
PfamiPF01599. Ribosomal_S27. 1 hit.
PF00240. ubiquitin. 1 hit.
[Graphical view]
PRINTSiPR00348. UBIQUITIN.
SMARTiSM01402. Ribosomal_S27. 1 hit.
SM00213. UBQ. 1 hit.
[Graphical view]
SUPFAMiSSF54236. SSF54236. 1 hit.
SSF57829. SSF57829. 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.

P0C016-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MQIFVKTLTG KTITLEVESS DTIDNVKSKI QDKEGIPPDQ QRLIFAGKQL
60 70 80 90 100
EDGRTLSDYN IQKESTLHLV LRLRGGGKKR KKKTYTTPKK IKHKHKKVEL
110 120 130 140 150
AVLKYYKVED DGSVKRLRRE CPNCGASTFM ANHKDRLYCG RCHLTLKLEN
Length:150
Mass (Da):17,258
Last modified:August 10, 2010 - v2
Checksum:i5200E01E739CBC97
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CU329670 Genomic DNA. Translation: CAB11297.1.
PIRiT39061.
RefSeqiNP_594108.1. NM_001019532.2.

Genome annotation databases

EnsemblFungiiSPAC6G10.11c.1; SPAC6G10.11c.1:pep; SPAC6G10.11c.
GeneIDi2541445.
KEGGispo:SPAC6G10.11c.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CU329670 Genomic DNA. Translation: CAB11297.1.
PIRiT39061.
RefSeqiNP_594108.1. NM_001019532.2.

3D structure databases

ProteinModelPortaliP0C016.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi277950. 3 interactions.

Proteomic databases

PRIDEiP0C016.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiSPAC6G10.11c.1; SPAC6G10.11c.1:pep; SPAC6G10.11c.
GeneIDi2541445.
KEGGispo:SPAC6G10.11c.

Organism-specific databases

EuPathDBiFungiDB:SPAC6G10.11c.
PomBaseiSPAC6G10.11c. ubi3.

Phylogenomic databases

HOGENOMiHOG000233943.
InParanoidiP0C016.
KOiK02977.
OMAiMSILKYY.
OrthoDBiEOG7D5B06.
PhylomeDBiP0C016.

Enzyme and pathway databases

ReactomeiR-SPO-110312. Translesion synthesis by REV1.
R-SPO-110314. Recognition of DNA damage by PCNA-containing replication complex.
R-SPO-110320. Translesion Synthesis by POLH.
R-SPO-156827. L13a-mediated translational silencing of Ceruloplasmin expression.
R-SPO-174113. SCF-beta-TrCP mediated degradation of Emi1.
R-SPO-1799339. SRP-dependent cotranslational protein targeting to membrane.
R-SPO-5632684. Hedgehog 'on' state.
R-SPO-5655862. Translesion synthesis by POLK.
R-SPO-5656121. Translesion synthesis by POLI.
R-SPO-5656169. Termination of translesion DNA synthesis.
R-SPO-5696395. Formation of Incision Complex in GG-NER.
R-SPO-5696400. Dual Incision in GG-NER.
R-SPO-6781823. Formation of TC-NER Pre-Incision Complex.
R-SPO-6782135. Dual incision in TC-NER.
R-SPO-6782210. Gap-filling DNA repair synthesis and ligation in TC-NER.
R-SPO-68949. Orc1 removal from chromatin.
R-SPO-69017. CDK-mediated phosphorylation and removal of Cdc6.
R-SPO-69229. Ubiquitin-dependent degradation of Cyclin D1.
R-SPO-69601. Ubiquitin Mediated Degradation of Phosphorylated Cdc25A.
R-SPO-72649. Translation initiation complex formation.
R-SPO-72689. Formation of a pool of free 40S subunits.
R-SPO-72695. Formation of the ternary complex, and subsequently, the 43S complex.
R-SPO-72702. Ribosomal scanning and start codon recognition.
R-SPO-72706. GTP hydrolysis and joining of the 60S ribosomal subunit.
R-SPO-917729. Endosomal Sorting Complex Required For Transport (ESCRT).
R-SPO-975956. Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC).
R-SPO-975957. Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC).
R-SPO-983168. Antigen processing: Ubiquitination & Proteasome degradation.

Miscellaneous databases

PROiP0C016.

Family and domain databases

InterProiIPR002906. Ribosomal_S27a.
IPR011332. Ribosomal_zn-bd.
IPR019956. Ubiquitin.
IPR029071. Ubiquitin-rel_dom.
IPR019954. Ubiquitin_CS.
IPR000626. Ubiquitin_dom.
[Graphical view]
PfamiPF01599. Ribosomal_S27. 1 hit.
PF00240. ubiquitin. 1 hit.
[Graphical view]
PRINTSiPR00348. UBIQUITIN.
SMARTiSM01402. Ribosomal_S27. 1 hit.
SM00213. UBQ. 1 hit.
[Graphical view]
SUPFAMiSSF54236. SSF54236. 1 hit.
SSF57829. SSF57829. 1 hit.
PROSITEiPS00299. UBIQUITIN_1. 1 hit.
PS50053. UBIQUITIN_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

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 nameiRS27A_SCHPO
AccessioniPrimary (citable) accession number: P0C016
Secondary accession number(s): O13697
, O14257, P0C014, Q76PD0, Q9HDZ4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 21, 2005
Last sequence update: August 10, 2010
Last modified: June 8, 2016
This is version 71 of the entry and version 2 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

Complete proteome, Reference proteome

Documents

  1. Schizosaccharomyces pombe
    Schizosaccharomyces pombe: entries and gene names
  2. Ribosomal proteins
    Ribosomal proteins families and list of entries
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.