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Ubiquitin-like protein pmt3/smt3

 PMT3_SCHPO              Reviewed;         117 AA.
O13351; O74186;
15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
11-JAN-2001, sequence version 2.
05-DEC-2018, entry version 150.
RecName: Full=Ubiquitin-like protein pmt3/smt3;
Flags: Precursor;
Name=pmt3; Synonyms=smt3, ubl2; ORFNames=SPBC365.06;
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
Schizosaccharomycetes; Schizosaccharomycetales;
Schizosaccharomycetaceae; Schizosaccharomyces.
PubMed=10567589; DOI=10.1128/MCB.19.12.8660;
Tanaka K., Nishide J., Okazaki K., Kato H., Niwa O., Nakagawa T.,
Matsuda H., Kawamukai M., Murakami Y.;
"Characterization of a fission yeast SUMO-1 homologue, pmt3p, required
for multiple nuclear events, including the control of telomere length
and chromosome segregation.";
Mol. Cell. Biol. 19:8660-8672(1999).
STRAIN=972 / ATCC 24843;
PubMed=11859360; DOI=10.1038/nature724;
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.;
"The genome sequence of Schizosaccharomyces pombe.";
Nature 415:871-880(2002).
Pelletier M.F., Dignard D.;
"Ubiquitin-like protein (Schizosaccharomyces pombe).";
Submitted (AUG-1997) to the EMBL/GenBank/DDBJ databases.
PubMed=17502373; DOI=10.1074/jbc.M702652200;
Kosoy A., Calonge T.M., Outwin E.A., O'Connell M.J.;
"Fission yeast Rnf4 homologs are required for DNA repair.";
J. Biol. Chem. 282:20388-20394(2007).
-!- FUNCTION: Required for chromosome segregation where it may be
involved in microtubule assembly. Loss of smt3 leads to an
increase in telomere length. {ECO:0000269|PubMed:10567589}.
-!- SUBUNIT: Interacts with rfp1. {ECO:0000269|PubMed:17502373}.
P36592:rad22; NbExp=4; IntAct=EBI-966336, EBI-966242;
O13826:rfp1; NbExp=5; IntAct=EBI-966336, EBI-3647269;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:10567589}.
-!- SIMILARITY: Belongs to the ubiquitin family. SUMO subfamily.
Sequence=AAB71541.1; Type=Frameshift; Positions=29; Evidence={ECO:0000305};
Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
Distributed under the Creative Commons Attribution (CC BY 4.0) License
EMBL; AB017187; BAA32595.1; -; Genomic_DNA.
EMBL; CU329671; CAB44758.1; -; Genomic_DNA.
EMBL; AF019235; AAB71541.1; ALT_FRAME; mRNA.
PIR; T40313; T40313.
PIR; T43537; T43537.
RefSeq; NP_596035.1; NM_001021945.2.
ProteinModelPortal; O13351; -.
SMR; O13351; -.
BioGrid; 277443; 54.
IntAct; O13351; 10.
MINT; O13351; -.
STRING; 4896.SPBC365.06.1; -.
iPTMnet; O13351; -.
MaxQB; O13351; -.
PaxDb; O13351; -.
PRIDE; O13351; -.
EnsemblFungi; SPBC365.06.1; SPBC365.06.1:pep; SPBC365.06.
EuPathDB; FungiDB:SPBC365.06; -.
PomBase; SPBC365.06; pmt3.
HOGENOM; HOG000207495; -.
InParanoid; O13351; -.
OrthoDB; EOG092C5C59; -.
PhylomeDB; O13351; -.
Reactome; R-SPO-3065676; SUMO is conjugated to E1 (UBA2:SAE1).
Reactome; R-SPO-3065678; SUMO is transferred from E1 to E2 (UBE2I, UBC9).
Reactome; R-SPO-3065679; SUMO is proteolytically processed.
Reactome; R-SPO-3108214; SUMOylation of DNA damage response and repair proteins.
Reactome; R-SPO-3899300; SUMOylation of transcription cofactors.
Reactome; R-SPO-4085377; SUMOylation of SUMOylation proteins.
Reactome; R-SPO-4551638; SUMOylation of chromatin organization proteins.
Reactome; R-SPO-4570464; SUMOylation of RNA binding proteins.
Reactome; R-SPO-4615885; SUMOylation of DNA replication proteins.
PRO; PR:O13351; -.
Proteomes; UP000002485; Chromosome II.
GO; GO:0000775; C:chromosome, centromeric region; IEA:GOC.
GO; GO:0030998; C:linear element; IDA:PomBase.
GO; GO:0044732; C:mitotic spindle pole body; IDA:PomBase.
GO; GO:0005634; C:nucleus; IDA:PomBase.
GO; GO:0005940; C:septin ring; IBA:GO_Central.
GO; GO:0031386; F:protein tag; IDA:PomBase.
GO; GO:0030702; P:chromatin silencing at centromere; IMP:PomBase.
GO; GO:0030466; P:chromatin silencing at silent mating-type cassette; IMP:PomBase.
GO; GO:0071441; P:negative regulation of histone H3-K14 acetylation; IMP:PomBase.
GO; GO:0051572; P:negative regulation of histone H3-K4 methylation; IMP:PomBase.
GO; GO:0051573; P:negative regulation of histone H3-K9 methylation; IMP:PomBase.
GO; GO:0016925; P:protein sumoylation; IDA:PomBase.
GO; GO:0000723; P:telomere maintenance; IMP:PomBase.
CDD; cd01763; Sumo; 1.
InterPro; IPR022617; Rad60/SUMO-like_dom.
InterPro; IPR033950; Sumo.
InterPro; IPR029071; Ubiquitin-like_domsf.
InterPro; IPR000626; Ubiquitin_dom.
Pfam; PF11976; Rad60-SLD; 1.
SMART; SM00213; UBQ; 1.
SUPFAM; SSF54236; SSF54236; 1.
1: Evidence at protein level;
Complete proteome; Isopeptide bond; Nucleus; Reference proteome;
Ubl conjugation pathway.
CHAIN 1 111 Ubiquitin-like protein pmt3/smt3.
PROPEP 112 117 {ECO:0000255}.
DOMAIN 35 115 Ubiquitin-like. {ECO:0000255|PROSITE-
CROSSLNK 111 111 Glycyl lysine isopeptide (Gly-Lys)
(interchain with K-? in acceptor
SEQUENCE 117 AA; 12935 MW; 11C860EBEA172FD2 CRC64;

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