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Protein

Ubiquitin-conjugating enzyme E2 4

Gene

ubc4

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

Functioni

Catalyzes the covalent attachment of ubiquitin to other proteins. Mediates the selective degradation of short-lived and abnormal proteins. Mediates ubiquitination of PEX5 (By similarity).PROSITE-ProRule annotation

Catalytic activityi

ATP + ubiquitin + protein lysine = AMP + diphosphate + protein N-ubiquityllysine.PROSITE-ProRule annotation

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei85 – 851Glycyl thioester intermediatePROSITE-ProRule annotation

GO - Molecular functioni

GO - Biological processi

  • mitotic sister chromatid segregation Source: PomBase
  • positive regulation of mitotic metaphase/anaphase transition Source: PomBase
  • protein polyubiquitination Source: UniProtKB
  • protein processing Source: PomBase
  • protein ubiquitination involved in ubiquitin-dependent protein catabolic process Source: PomBase
  • SCF-dependent proteasomal ubiquitin-dependent protein catabolic process Source: PomBase
Complete GO annotation...

Keywords - Molecular functioni

Ligase

Keywords - Biological processi

Ubl conjugation pathway

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

UniPathwayiUPA00143.

Names & Taxonomyi

Protein namesi
Recommended name:
Ubiquitin-conjugating enzyme E2 4 (EC:6.3.2.19)
Alternative name(s):
Ubiquitin carrier protein 4
Ubiquitin-protein ligase 4
Gene namesi
Name:ubc4
ORF Names:SPBC119.02
OrganismiSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Taxonomic identifieri284812 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces
ProteomesiUP000002485 Componenti: Chromosome II

Organism-specific databases

EuPathDBiFungiDB:SPBC119.02.
PomBaseiSPBC119.02.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: PomBase
  • cytosol Source: PomBase
  • nuclear SCF ubiquitin ligase complex Source: PomBase
  • nucleus Source: PomBase
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 147147Ubiquitin-conjugating enzyme E2 4PRO_0000082569Add
BLAST

Proteomic databases

MaxQBiP46595.
PaxDbiP46595.

Interactioni

Protein-protein interaction databases

BioGridi276621. 12 interactions.
IntActiP46595. 1 interaction.
MINTiMINT-4690340.
STRINGi4896.SPBC119.02-1.

Structurei

Secondary structure

1
147
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi2 – 1413Combined sources
Beta strandi20 – 267Combined sources
Beta strandi29 – 3810Combined sources
Turni44 – 474Combined sources
Beta strandi49 – 557Combined sources
Turni58 – 625Combined sources
Beta strandi66 – 694Combined sources
Helixi87 – 893Combined sources
Turni90 – 923Combined sources
Helixi99 – 11113Combined sources
Helixi121 – 1299Combined sources
Helixi131 – 14515Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4II2X-ray2.20C1-147[»]
ProteinModelPortaliP46595.
SMRiP46595. Positions 1-147.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the ubiquitin-conjugating enzyme family.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiCOG5078.
HOGENOMiHOG000233455.
InParanoidiP46595.
KOiK06689.
OMAiMATKRIN.
OrthoDBiEOG7SBP18.
PhylomeDBiP46595.

Family and domain databases

Gene3Di3.10.110.10. 1 hit.
InterProiIPR000608. UBQ-conjugat_E2.
IPR023313. UBQ-conjugating_AS.
IPR016135. UBQ-conjugating_enzyme/RWD.
[Graphical view]
PfamiPF00179. UQ_con. 1 hit.
[Graphical view]
SUPFAMiSSF54495. SSF54495. 1 hit.
PROSITEiPS00183. UBIQUITIN_CONJUGAT_1. 1 hit.
PS50127. UBIQUITIN_CONJUGAT_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P46595-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MALKRINREL ADLGKDPPSS CSAGPVGDDL FHWQATIMGP ADSPYAGGVF
60 70 80 90 100
FLSIHFPTDY PFKPPKVNFT TRIYHPNINS NGSICLDILR DQWSPALTIS
110 120 130 140
KVLLSICSLL TDPNPDDPLV PEIAHVYKTD RSRYELSARE WTRKYAI
Length:147
Mass (Da):16,476
Last modified:November 1, 1995 - v1
Checksum:i3E8BADFF494A91EB
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L37384 mRNA. No translation available.
CU329671 Genomic DNA. Translation: CAA17917.1.
PIRiT39300.
RefSeqiNP_595283.1. NM_001021190.2.

Genome annotation databases

EnsemblFungiiSPBC119.02.1; SPBC119.02.1:pep; SPBC119.02.
GeneIDi2540083.
KEGGispo:SPBC119.02.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L37384 mRNA. No translation available.
CU329671 Genomic DNA. Translation: CAA17917.1.
PIRiT39300.
RefSeqiNP_595283.1. NM_001021190.2.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4II2X-ray2.20C1-147[»]
ProteinModelPortaliP46595.
SMRiP46595. Positions 1-147.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi276621. 12 interactions.
IntActiP46595. 1 interaction.
MINTiMINT-4690340.
STRINGi4896.SPBC119.02-1.

Proteomic databases

MaxQBiP46595.
PaxDbiP46595.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiSPBC119.02.1; SPBC119.02.1:pep; SPBC119.02.
GeneIDi2540083.
KEGGispo:SPBC119.02.

Organism-specific databases

EuPathDBiFungiDB:SPBC119.02.
PomBaseiSPBC119.02.

Phylogenomic databases

eggNOGiCOG5078.
HOGENOMiHOG000233455.
InParanoidiP46595.
KOiK06689.
OMAiMATKRIN.
OrthoDBiEOG7SBP18.
PhylomeDBiP46595.

Enzyme and pathway databases

UniPathwayiUPA00143.

Miscellaneous databases

NextBioi20801220.
PROiP46595.

Family and domain databases

Gene3Di3.10.110.10. 1 hit.
InterProiIPR000608. UBQ-conjugat_E2.
IPR023313. UBQ-conjugating_AS.
IPR016135. UBQ-conjugating_enzyme/RWD.
[Graphical view]
PfamiPF00179. UQ_con. 1 hit.
[Graphical view]
SUPFAMiSSF54495. SSF54495. 1 hit.
PROSITEiPS00183. UBIQUITIN_CONJUGAT_1. 1 hit.
PS50127. UBIQUITIN_CONJUGAT_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Schizosaccharomyces pombe and Candida albicans cDNA homologues of the Saccharomyces cerevisiae UBC4 gene."
    Damagnez V., Rolfe M., Cottarel G.
    Gene 155:137-138(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "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 nameiUBC4_SCHPO
AccessioniPrimary (citable) accession number: P46595
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1995
Last modified: April 29, 2015
This is version 116 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

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

External Data

Dasty 3

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 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.