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Protein

SUMO-conjugating enzyme ubc9

Gene

hus5

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-like protein SUMO/Smt3 to other proteins. Required for efficient recovery from DNA damage or S-phase arrest and normal mitosis. This may be as part of a checkpoint independent recovery process.2 Publications

Catalytic activityi

ATP + SUMO + protein lysine = AMP + diphosphate + protein N-SUMOyllysine.

Pathwayi: protein sumoylation

This protein is involved in the pathway protein sumoylation, which is part of Protein modification.
View all proteins of this organism that are known to be involved in the pathway protein sumoylation and in Protein modification.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei93 – 931Glycyl thioester intermediatePROSITE-ProRule annotation

GO - Molecular functioni

GO - Biological processi

  • cellular response to DNA damage stimulus Source: UniProtKB-KW
  • protein sumoylation Source: PomBase
Complete GO annotation...

Keywords - Molecular functioni

Ligase

Keywords - Biological processi

DNA damage, Ubl conjugation pathway

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiR-SPO-3065678. SUMO is transferred from E1 to E2 (UBE2I, UBC9).
R-SPO-3108214. SUMOylation of DNA damage response and repair proteins.
R-SPO-3232118. SUMOylation of transcription factors.
R-SPO-4570464. SUMOylation of RNA binding proteins.
R-SPO-4615885. SUMOylation of DNA replication proteins.
UniPathwayiUPA00886.

Names & Taxonomyi

Protein namesi
Recommended name:
SUMO-conjugating enzyme ubc9 (EC:6.3.2.-)
Alternative name(s):
SUMO protein ligase
Ubiquitin carrier protein 9
Ubiquitin carrier protein hus5
Ubiquitin-conjugating enzyme E2-18 kDa
Ubiquitin-protein ligase hus5
Gene namesi
Name:hus5
Synonyms:ubc9
ORF Names:SPAC30D11.13
OrganismiSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Taxonomic identifieri284812 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces
Proteomesi
  • UP000002485 Componenti: Chromosome I

Organism-specific databases

EuPathDBiFungiDB:SPAC30D11.13.
PomBaseiSPAC30D11.13. hus5.

Subcellular locationi

  • Nucleus 1 Publication

GO - Cellular componenti

  • cytoplasm Source: GO_Central
  • cytosol Source: PomBase
  • nuclear heterochromatin Source: PomBase
  • nucleus Source: PomBase
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 157157SUMO-conjugating enzyme ubc9PRO_0000082568Add
BLAST

Proteomic databases

MaxQBiP40984.

Interactioni

Protein-protein interaction databases

BioGridi278671. 12 interactions.
DIPiDIP-35488N.
IntActiP40984. 3 interactions.
MINTiMINT-4689925.

Structurei

Secondary structure

1
157
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi4 – 1815Combined sources
Beta strandi25 – 306Combined sources
Beta strandi34 – 4613Combined sources
Turni52 – 554Combined sources
Beta strandi57 – 637Combined sources
Turni66 – 705Combined sources
Beta strandi74 – 796Combined sources
Beta strandi90 – 923Combined sources
Helixi95 – 973Combined sources
Turni99 – 1024Combined sources
Helixi109 – 12012Combined sources
Helixi131 – 1399Combined sources
Helixi141 – 15414Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3RCZX-ray1.90B2-157[»]
ProteinModelPortaliP40984.
SMRiP40984. Positions 1-157.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

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

Phylogenomic databases

HOGENOMiHOG000233454.
InParanoidiP40984.
KOiK10577.
OMAiMAFPEEY.
OrthoDBiEOG7SBP18.
PhylomeDBiP40984.

Family and domain databases

Gene3Di3.10.110.10. 1 hit.
InterProiIPR027230. Ubc9.
IPR000608. UBQ-conjugat_E2.
IPR023313. UBQ-conjugating_AS.
IPR016135. UBQ-conjugating_enzyme/RWD.
[Graphical view]
PANTHERiPTHR24067:SF51. PTHR24067:SF51. 1 hit.
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.

P40984-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSSLCKTRLQ EERKQWRRDH PFGFYAKPCK SSDGGLDLMN WKVGIPGKPK
60 70 80 90 100
TSWEGGLYKL TMAFPEEYPT RPPKCRFTPP LFHPNVYPSG TVCLSILNEE
110 120 130 140 150
EGWKPAITIK QILLGIQDLL DDPNIASPAQ TEAYTMFKKD KVEYEKRVRA

QARENAP
Length:157
Mass (Da):17,989
Last modified:February 1, 1995 - v1
Checksum:i4BF3A6389203D27F
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X81846 Genomic DNA. Translation: CAA57438.1.
CU329670 Genomic DNA. Translation: CAA91899.1.
PIRiS62571.
RefSeqiNP_593204.1. NM_001018600.2.

Genome annotation databases

EnsemblFungiiSPAC30D11.13.1; SPAC30D11.13.1:pep; SPAC30D11.13.
GeneIDi2542196.
KEGGispo:SPAC30D11.13.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X81846 Genomic DNA. Translation: CAA57438.1.
CU329670 Genomic DNA. Translation: CAA91899.1.
PIRiS62571.
RefSeqiNP_593204.1. NM_001018600.2.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3RCZX-ray1.90B2-157[»]
ProteinModelPortaliP40984.
SMRiP40984. Positions 1-157.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi278671. 12 interactions.
DIPiDIP-35488N.
IntActiP40984. 3 interactions.
MINTiMINT-4689925.

Proteomic databases

MaxQBiP40984.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiSPAC30D11.13.1; SPAC30D11.13.1:pep; SPAC30D11.13.
GeneIDi2542196.
KEGGispo:SPAC30D11.13.

Organism-specific databases

EuPathDBiFungiDB:SPAC30D11.13.
PomBaseiSPAC30D11.13. hus5.

Phylogenomic databases

HOGENOMiHOG000233454.
InParanoidiP40984.
KOiK10577.
OMAiMAFPEEY.
OrthoDBiEOG7SBP18.
PhylomeDBiP40984.

Enzyme and pathway databases

UniPathwayiUPA00886.
ReactomeiR-SPO-3065678. SUMO is transferred from E1 to E2 (UBE2I, UBC9).
R-SPO-3108214. SUMOylation of DNA damage response and repair proteins.
R-SPO-3232118. SUMOylation of transcription factors.
R-SPO-4570464. SUMOylation of RNA binding proteins.
R-SPO-4615885. SUMOylation of DNA replication proteins.

Miscellaneous databases

PROiP40984.

Family and domain databases

Gene3Di3.10.110.10. 1 hit.
InterProiIPR027230. Ubc9.
IPR000608. UBQ-conjugat_E2.
IPR023313. UBQ-conjugating_AS.
IPR016135. UBQ-conjugating_enzyme/RWD.
[Graphical view]
PANTHERiPTHR24067:SF51. PTHR24067:SF51. 1 hit.
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. "The Schizosaccharomyces pombe hus5 gene encodes a ubiquitin conjugating enzyme required for normal mitosis."
    Al-Khodairy F., Enoch T., Hagman I.M., Carr A.M.
    J. Cell Sci. 108:475-486(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, SUBCELLULAR LOCATION.
  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.
  3. "Characterization of SUMO-conjugating enzyme mutants in Schizosaccharomyces pombe identifies a dominant-negative allele that severely reduces SUMO conjugation."
    Ho J.C., Watts F.Z.
    Biochem. J. 372:97-104(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.

Entry informationi

Entry nameiUBC9_SCHPO
AccessioniPrimary (citable) accession number: P40984
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1995
Last sequence update: February 1, 1995
Last modified: July 6, 2016
This is version 141 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

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.