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Protein

Ubiquitin-like protein pmt3/smt3

Gene

pmt3

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

Required for chromosome segregation where it may be involved in microtubule assembly. Loss of smt3 leads to an increase in telomere length.1 Publication

GO - Molecular functioni

  • protein tag Source: PomBase

GO - Biological processi

  • chromatin silencing at centromere Source: PomBase
  • chromatin silencing at silent mating-type cassette Source: PomBase
  • mitotic sister chromatid segregation Source: PomBase
  • negative regulation of histone H3-K14 acetylation Source: PomBase
  • negative regulation of histone H3-K4 methylation Source: PomBase
  • negative regulation of histone H3-K9 methylation Source: PomBase
  • protein sumoylation Source: PomBase
  • telomere maintenance Source: PomBase
Complete GO annotation...

Keywords - Biological processi

Ubl conjugation pathway

Enzyme and pathway databases

ReactomeiR-SPO-3065676. SUMO is conjugated to E1 (UBA2:SAE1).
R-SPO-3065678. SUMO is transferred from E1 to E2 (UBE2I, UBC9).
R-SPO-3065679. SUMO is proteolytically processed.
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.

Names & Taxonomyi

Protein namesi
Recommended name:
Ubiquitin-like protein pmt3/smt3
Gene namesi
Name:pmt3
Synonyms:smt3, ubl2
ORF Names:SPBC365.06
OrganismiSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Taxonomic identifieri284812 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces
Proteomesi
  • UP000002485 Componenti: Chromosome II

Organism-specific databases

EuPathDBiFungiDB:SPBC365.06.
PomBaseiSPBC365.06. pmt3.

Subcellular locationi

  • Nucleus 1 Publication

GO - Cellular componenti

  • chromosome, centromeric region Source: GOC
  • linear element Source: PomBase
  • mitotic spindle pole body Source: PomBase
  • nucleus Source: PomBase
  • septin ring Source: GO_Central
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 111111Ubiquitin-like protein pmt3/smt3PRO_0000035961Add
BLAST
Propeptidei112 – 1176Sequence analysisPRO_0000035962

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Cross-linki111 – 111Glycyl lysine isopeptide (Gly-Lys) (interchain with K-? in acceptor proteins)

Keywords - PTMi

Isopeptide bond

Proteomic databases

MaxQBiO13351.

Interactioni

Subunit structurei

Interacts with rfp1.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
rad22P365924EBI-966336,EBI-966242
rfp1O138265EBI-966336,EBI-3647269

Protein-protein interaction databases

BioGridi277443. 54 interactions.
IntActiO13351. 10 interactions.
MINTiMINT-4666598.

Structurei

3D structure databases

ProteinModelPortaliO13351.
SMRiO13351. Positions 35-111.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini35 – 11581Ubiquitin-likePROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the ubiquitin family. SUMO subfamily.Curated
Contains 1 ubiquitin-like domain.PROSITE-ProRule annotation

Phylogenomic databases

HOGENOMiHOG000207495.
InParanoidiO13351.
KOiK12160.
OMAiNRINEDD.
OrthoDBiEOG7SR514.
PhylomeDBiO13351.

Family and domain databases

InterProiIPR022617. Rad60/SUMO-like_dom.
IPR029071. Ubiquitin-rel_dom.
IPR000626. Ubiquitin_dom.
[Graphical view]
PfamiPF11976. Rad60-SLD. 1 hit.
[Graphical view]
SMARTiSM00213. UBQ. 1 hit.
[Graphical view]
SUPFAMiSSF54236. SSF54236. 1 hit.
PROSITEiPS50053. UBIQUITIN_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

O13351-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSESPSANIS DADKSAITPT TGDTSQQDVK PSTEHINLKV VGQDNNEVFF
60 70 80 90 100
KIKKTTEFSK LMKIYCARQG KSMNSLRFLV DGERIRPDQT PAELDMEDGD
110
QIEAVLEQLG GCTHLCL
Length:117
Mass (Da):12,935
Last modified:January 11, 2001 - v2
Checksum:i11C860EBEA172FD2
GO

Sequence cautioni

The sequence AAB71541.1 differs from that shown. Reason: Frameshift at position 29. Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB017187 Genomic DNA. Translation: BAA32595.1.
CU329671 Genomic DNA. Translation: CAB44758.1.
AF019235 mRNA. Translation: AAB71541.1. Frameshift.
PIRiT40313.
T43537.
RefSeqiNP_596035.1. NM_001021945.2.

Genome annotation databases

EnsemblFungiiSPBC365.06.1; SPBC365.06.1:pep; SPBC365.06.
GeneIDi2540927.
KEGGispo:SPBC365.06.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB017187 Genomic DNA. Translation: BAA32595.1.
CU329671 Genomic DNA. Translation: CAB44758.1.
AF019235 mRNA. Translation: AAB71541.1. Frameshift.
PIRiT40313.
T43537.
RefSeqiNP_596035.1. NM_001021945.2.

3D structure databases

ProteinModelPortaliO13351.
SMRiO13351. Positions 35-111.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi277443. 54 interactions.
IntActiO13351. 10 interactions.
MINTiMINT-4666598.

Proteomic databases

MaxQBiO13351.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiSPBC365.06.1; SPBC365.06.1:pep; SPBC365.06.
GeneIDi2540927.
KEGGispo:SPBC365.06.

Organism-specific databases

EuPathDBiFungiDB:SPBC365.06.
PomBaseiSPBC365.06. pmt3.

Phylogenomic databases

HOGENOMiHOG000207495.
InParanoidiO13351.
KOiK12160.
OMAiNRINEDD.
OrthoDBiEOG7SR514.
PhylomeDBiO13351.

Enzyme and pathway databases

ReactomeiR-SPO-3065676. SUMO is conjugated to E1 (UBA2:SAE1).
R-SPO-3065678. SUMO is transferred from E1 to E2 (UBE2I, UBC9).
R-SPO-3065679. SUMO is proteolytically processed.
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

PROiO13351.

Family and domain databases

InterProiIPR022617. Rad60/SUMO-like_dom.
IPR029071. Ubiquitin-rel_dom.
IPR000626. Ubiquitin_dom.
[Graphical view]
PfamiPF11976. Rad60-SLD. 1 hit.
[Graphical view]
SMARTiSM00213. UBQ. 1 hit.
[Graphical view]
SUPFAMiSSF54236. SSF54236. 1 hit.
PROSITEiPS50053. UBIQUITIN_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Characterization of a fission yeast SUMO-1 homologue, pmt3p, required for multiple nuclear events, including the control of telomere length and chromosome segregation."
    Tanaka K., Nishide J., Okazaki K., Kato H., Niwa O., Nakagawa T., Matsuda H., Kawamukai M., Murakami Y.
    Mol. Cell. Biol. 19:8660-8672(1999) [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. "Ubiquitin-like protein (Schizosaccharomyces pombe)."
    Pelletier M.F., Dignard D.
    Submitted (AUG-1997) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 25-117.
    Strain: 358.
  4. "Fission yeast Rnf4 homologs are required for DNA repair."
    Kosoy A., Calonge T.M., Outwin E.A., O'Connell M.J.
    J. Biol. Chem. 282:20388-20394(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH RFP1.

Entry informationi

Entry nameiPMT3_SCHPO
AccessioniPrimary (citable) accession number: O13351
Secondary accession number(s): O74186
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: January 11, 2001
Last modified: July 6, 2016
This is version 133 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Schizosaccharomyces pombe
    Schizosaccharomyces pombe: entries and gene names
  2. 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.