Did you know ? If you order before Friday 14h we deliver 90PCT of the the time next Tuesday, GENTAUR another in time delivery

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.
22-NOV-2017, entry version 145.
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.
NCBI_TaxID=284812;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND SUBCELLULAR LOCATION.
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).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
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).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 25-117.
STRAIN=358;
Pelletier M.F., Dignard D.;
"Ubiquitin-like protein (Schizosaccharomyces pombe).";
Submitted (AUG-1997) to the EMBL/GenBank/DDBJ databases.
[4]
INTERACTION WITH RFP1.
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}.
-!- INTERACTION:
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.
{ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAB71541.1; Type=Frameshift; Positions=29; Evidence={ECO:0000305};
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs 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; MINT-4666598; -.
STRING; 4896.SPBC365.06.1; -.
iPTMnet; O13351; -.
MaxQB; O13351; -.
PRIDE; O13351; -.
EnsemblFungi; SPBC365.06.1; SPBC365.06.1:pep; SPBC365.06.
KEGG; spo:SPBC365.06; -.
EuPathDB; FungiDB:SPBC365.06; -.
PomBase; SPBC365.06; pmt3.
HOGENOM; HOG000207495; -.
InParanoid; O13351; -.
KO; K12160; -.
OMA; NDTIDVM; -.
OrthoDB; EOG092C5C59; -.
PhylomeDB; O13351; -.
Reactome; R-SPO-3065676; SUMO is conjugated to E1 (UBA2:SAE1).
Reactome; R-SPO-3065679; SUMO is proteolytically processed.
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.
PROSITE; PS50053; UBIQUITIN_2; 1.
1: Evidence at protein level;
Complete proteome; Isopeptide bond; Nucleus; Reference proteome;
Ubl conjugation pathway.
CHAIN 1 111 Ubiquitin-like protein pmt3/smt3.
/FTId=PRO_0000035961.
PROPEP 112 117 {ECO:0000255}.
/FTId=PRO_0000035962.
DOMAIN 35 115 Ubiquitin-like. {ECO:0000255|PROSITE-
ProRule:PRU00214}.
CROSSLNK 111 111 Glycyl lysine isopeptide (Gly-Lys)
(interchain with K-? in acceptor
proteins).
SEQUENCE 117 AA; 12935 MW; 11C860EBEA172FD2 CRC64;
MSESPSANIS DADKSAITPT TGDTSQQDVK PSTEHINLKV VGQDNNEVFF KIKKTTEFSK
LMKIYCARQG KSMNSLRFLV DGERIRPDQT PAELDMEDGD QIEAVLEQLG GCTHLCL


Related products :

Catalog number Product name Quantity
18-783-75567 RABBIT ANTI SUMO-1 (N-TERMINAL) - SMALL UBIQUITIN-RELATED MODIFIER-1; SUMO-1; Sentrin; Ubiquitin-like protein SMT3C; SMT3 homolog 3; Ubiquitin-homology domain protein PIC1; Ubiquitin-like protein UBL1 0.1 mg
10-663-45613 SUMO-I_Sentrin-I Human - SUMO-1; Ubiquitin-like protein SMT3C; SMT3 homolog 3; Ubiquitin-homology domain protein PIC1; Ubiquitin-like protein UBL1; GAP-modifying protein 1; GMP1; Sentrin N_A 1 mg
10-663-45613 SUMO-I_Sentrin-I Human - SUMO-1; Ubiquitin-like protein SMT3C; SMT3 homolog 3; Ubiquitin-homology domain protein PIC1; Ubiquitin-like protein UBL1; GAP-modifying protein 1; GMP1; Sentrin N_A 0.05 mg
10-663-45613 SUMO-I_Sentrin-I Human - SUMO-1; Ubiquitin-like protein SMT3C; SMT3 homolog 3; Ubiquitin-homology domain protein PIC1; Ubiquitin-like protein UBL1; GAP-modifying protein 1; GMP1; Sentrin N_A 0.01 mg
EIAAB40559 GAP-modifying protein 1,GMP1,Homo sapiens,Human,OK_SW-cl.43,Sentrin,Small ubiquitin-related modifier 1,SMT3 homolog 3,Smt3C,SMT3C,SMT3H3,SUMO1,SUMO-1,Ubiquitin-homology domain protein PIC1,Ubiquitin-l
EIAAB40561 Mouse,Mus musculus,Small ubiquitin-related modifier 1,SMT3 homolog 3,Smt3C,Smt3c,Smt3h3,Sumo1,SUMO-1,Ubiquitin-homology domain protein PIC1,Ubiquitin-like protein SMT3C,Ubl1
EIAAB40574 Mouse,Mus musculus,Small ubiquitin-related modifier 3,SMT3 homolog 1,Smt3B,Smt3b,Smt3h1,Sumo3,SUMO-3,Ubiquitin-like protein SMT3B
EIAAB40566 Bos taurus,Bovine,Sentrin-2,Small ubiquitin-related modifier 2,SMT3 homolog 2,Smt3A,SMT3A,SMT3H2,SUMO2,SUMO-2,Ubiquitin-like protein SMT3A
EIAAB40568 Mouse,Mus musculus,Sentrin-2,Small ubiquitin-related modifier 2,SMT3 homolog 2,Smt3A,Smt3a,Smt3h2,Sumo2,SUMO-2,Ubiquitin-like protein SMT3A
EIAAB40570 Rat,Rattus norvegicus,Sentrin-2,Small ubiquitin-related modifier 2,SMT3 homolog 2,Smt3A,Smt3a,Smt3h2,Sumo2,SUMO-2,Ubiquitin-like protein SMT3A
EIAAB40565 MIF2 suppressor,Pig,Sentrin-2,Small ubiquitin-related modifier 2,SMT3 homolog 2,Smt3A,SMT3A,SMT3H2,SUMO2,SUMO-2,Sus scrofa,Ubiquitin-like protein SMT3A
EIAAB40572 Homo sapiens,Human,Small ubiquitin-related modifier 3,SMT3 homolog 1,Smt3B,SMT3B,SMT3H1,SUMO-2,SUMO3,SUMO-3,Ubiquitin-like protein SMT3B
EIAAB40569 Homo sapiens,HSMT3,Human,Sentrin-2,Small ubiquitin-related modifier 2,SMT3 homolog 2,Smt3A,SMT3A,SMT3H2,SUMO2,SUMO-2,SUMO-3,Ubiquitin-like protein SMT3A
25-863 RNF217 is an E3 ubiquitin-protein ligase which accepts ubiquitin from E2 ubiquitin-conjugating enzymes in the form of a thioester and then directly transfers the ubiquitin to targeted substrates. 0.05 mg
EIAAB45296 Ac2-121,E3 ubiquitin-protein ligase UHRF1,Liver regeneration-related protein LRRG126,Rat,Rattus norvegicus,Ubiquitin-like PHD and RING finger domain-containing protein 1,Ubiquitin-like-containing PHD
29-847 KIAA1333 is a probable E3 ubiquitin-protein ligase which accepts ubiquitin from an E2 ubiquitin-conjugating enzyme in the form of a thioester and then directly transfers the ubiquitin to targeted subs 0.05 mg
25-866 HECTD2 is a probable E3 ubiquitin-protein ligase which accepts ubiquitin from an E2 ubiquitin-conjugating enzyme in the form of a thioester and then directly transfers the ubiquitin to targeted substr 0.05 mg
25-847 MARCH7 is an E3 ubiquitin-protein ligase which may specifically enhance the E2 activity of HIP2. E3 ubiquitin ligases accept ubiquitin from an E2 ubiquitin-conjugating enzyme in the form of a thioeste 0.05 mg
EIAAB44730 Deubiquitinating enzyme 17-like protein 5,Homo sapiens,Human,Ubiquitin carboxyl-terminal hydrolase 17-like protein 5,Ubiquitin thiolesterase 17-like protein 5,Ubiquitin-specific-processing protease 17
EIAAB44731 Deubiquitinating enzyme 17-like protein 6,Homo sapiens,Human,Ubiquitin carboxyl-terminal hydrolase 17-like protein 6,Ubiquitin thiolesterase 17-like protein 6,Ubiquitin-specific-processing protease 17
EIAAB44818 Homo sapiens,Human,NICE5,PRO3094,Protein NICE-5,UBE2Q,UBE2Q1,Ubiquitin carrier protein Q1,Ubiquitin-conjugating enzyme E2 Q1,Ubiquitin-protein ligase Q1
EIAAB44728 Deubiquitinating enzyme 17-like protein 3,Homo sapiens,Human,Ubiquitin carboxyl-terminal hydrolase 17-like protein 3,Ubiquitin thiolesterase 17-like protein 3,Ubiquitin-specific-processing protease 17
EIAAB44725 Deubiquitinating enzyme 17-like protein 1,Homo sapiens,Human,Putative ubiquitin carboxyl-terminal hydrolase 17-like protein 1,Ubiquitin thiolesterase 17-like protein 1,Ubiquitin-specific-processing pr
EIAAB44754 Homo sapiens,Human,Putative ubiquitin-conjugating enzyme E2 D2-like protein,UBE2D2L,UBE2DNL,Ubiquitin carrier protein D2-like,Ubiquitin-conjugating enzyme E2D N-terminal-like,Ubiquitin-protein ligase
EIAAB44908 Cell proliferation-inducing gene 50 protein,Homo sapiens,HSPC150,Human,PIG50,UBE2T,Ubiquitin carrier protein T,Ubiquitin-conjugating enzyme E2 T,Ubiquitin-protein ligase T


 

GENTAUR Belgium BVBA BE0473327336
Voortstraat 49, 1910 Kampenhout BELGIUM
Tel 0032 16 58 90 45

Fax 0032 16 50 90 45
info@gentaur.com | Gentaur





GENTAUR Ltd.
Howard Frank Turnberry House
1404-1410 High Road
Whetstone London N20 9BH
Tel 020 3393 8531 Fax 020 8445 9411
uk@gentaur.com | Gentaur

 

 




GENTAUR France SARL
9, rue Lagrange, 75005 Paris
Tel 01 43 25 01 50

Fax 01 43 25 01 60
RCS Paris B 484 237 888

SIRET 48423788800017

BNP PARIBAS PARIS PL MAUBERT BIC BNPAFRPPPRG

france@gentaur.com | Gentaur

GENTAUR GmbH
Marienbongard 20
52062 Aachen Deutschland
Support Karolina Elandt
Tel: 0035929830070
Fax: (+49) 241 56 00 47 88

Logistic :0241 40 08 90 86
Bankleitzahl 39050000
IBAN lautet DE8839050000107569353
Handelsregister Aachen HR B 16058
Umsatzsteuer-Identifikationsnummer *** DE 815175831
Steuernummer 201/5961/3925
de@gentaur.com | Gentaur

GENTAUR U.S.A
Genprice Inc, Logistics
547, Yurok Circle
San Jose, CA 95123
CA 95123
Tel (408) 780-0908,
Fax (408) 780-0908,
sales@genprice.com

Genprice Inc, Invoices and accounting
6017 Snell Ave, Ste 357
San Jose, CA 95123




GENTAUR Nederland BV
NL850396268B01 KVK nummer 52327027
Kuiper 1
5521 DG Eersel Nederland
Tel:  0208-080893  Fax: 0497-517897
nl@gentaur.com | Gentaur
IBAN: NL04 RABO 0156 9854 62   SWIFT RABONL2U






GENTAUR Spain
tel:0911876558
spain@gentaur.com | Gentaur






ГЕНТАУЪР БЪЛГАРИЯ
ID # 201 358 931 /BULSTAT
София 1000, ул. "Граф Игнатиев" 53 вх. В, ет. 2
Tel 0035924682280 Fax 0035924808322
e-mail: Sofia@gentaur.com | Gentaur
IBAN: BG11FINV91501014771636
BIC: FINVBGSF

GENTAUR Poland Sp. z o.o.


ul. Grunwaldzka 88/A m.2
81-771 Sopot, Poland
TEL Gdansk 058 710 33 44 FAX  058 710 33 48              

poland@gentaur.com | Gentaur

Other countries

Österreich +43720880899

Canada Montreal +15149077481

Ceská republika Praha +420246019719

Danmark +4569918806

Finland Helsset +358942419041

Magyarország Budapest +3619980547

Ireland Dublin+35316526556

Luxembourg+35220880274

Norge Oslo+4721031366

Sverige Stockholm+46852503438

Schweiz Züri+41435006251

US New York+17185132983

GENTAUR Italy
SRL IVA IT03841300167
Piazza Giacomo Matteotti, 6
24122 Bergamo Tel 02 36 00 65 93
Fax 02 36 00 65 94
italia@gentaur.com | Gentaur