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

E3 ubiquitin-protein ligase complex slx8-rfp subunit slx8 (EC 2.3.2.27) (RING finger protein slx8) (RING-dependent E3 ubiquitin-protein ligase slx8) (RING-type E3 ubiquitin transferase slx8) (Synthetic lethal of unknown function protein 8)

 SLX8_SCHPO              Reviewed;         269 AA.
P87176; Q9US65;
27-MAR-2002, integrated into UniProtKB/Swiss-Prot.
01-JUL-1997, sequence version 1.
22-NOV-2017, entry version 112.
RecName: Full=E3 ubiquitin-protein ligase complex slx8-rfp subunit slx8;
EC=2.3.2.27;
AltName: Full=RING finger protein slx8;
AltName: Full=RING-dependent E3 ubiquitin-protein ligase slx8;
AltName: Full=RING-type E3 ubiquitin transferase slx8 {ECO:0000305};
AltName: Full=Synthetic lethal of unknown function protein 8;
Name=slx8; ORFNames=SPBC3D6.11c;
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
Schizosaccharomycetes; Schizosaccharomycetales;
Schizosaccharomycetaceae; Schizosaccharomyces.
NCBI_TaxID=284812;
[1]
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).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] OF 1-165, AND
SUBCELLULAR LOCATION.
STRAIN=ATCC 38364 / 968;
PubMed=10759889; DOI=10.1046/j.1365-2443.2000.00317.x;
Ding D.-Q., Tomita Y., Yamamoto A., Chikashige Y., Haraguchi T.,
Hiraoka Y.;
"Large-scale screening of intracellular protein localization in living
fission yeast cells by the use of a GFP-fusion genomic DNA library.";
Genes Cells 5:169-190(2000).
[3]
FUNCTION IN DEGRADATION OF SUMOYLATED PROTEINS, IDENTIFICATION IN A E3
UBIQUITIN-PROTEIN LIGASE COMPLEX WITH RFP1 AND RFP2, INTERACTION WITH
RFP1 AND RFP2, AND SUBCELLULAR LOCATION.
PubMed=17762865; DOI=10.1038/sj.emboj.7601838;
Prudden J., Pebernard S., Raffa G., Slavin D.A., Perry J.J.P.,
Tainer J.A., McGowan C.H., Boddy M.N.;
"SUMO-targeted ubiquitin ligases in genome stability.";
EMBO J. 26:4089-4101(2007).
[4]
FUNCTION IN DEGRADATION OF SUMOYLATED PROTEINS.
PubMed=17762864; DOI=10.1038/sj.emboj.7601839;
Sun H., Leverson J.D., Hunter T.;
"Conserved function of RNF4 family proteins in eukaryotes: targeting a
ubiquitin ligase to SUMOylated proteins.";
EMBO J. 26:4102-4112(2007).
-!- FUNCTION: Mediates ubiquitination and subsequent
desumoylation/degradation of sumoylated proteins and proteins
containing SUMO-like domains. Acts as a critical suppressor of
gross chromosomal rearrangements (GCRs) during normal cell cycle
progression. Involved in stabilizing, restarting or resolving
transiently stalled replication forks. Prevents accumulation of
DNA damage during cell cycle progression (By similarity).
{ECO:0000250, ECO:0000269|PubMed:17762864,
ECO:0000269|PubMed:17762865}.
-!- CATALYTIC ACTIVITY: S-ubiquitinyl-[E2 ubiquitin-conjugating
enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-
conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor
protein]-L-lysine.
-!- PATHWAY: Protein modification; protein ubiquitination.
-!- SUBUNIT: Part of an E3 ubiquitin complex including rfp1, rfp2 and
slx8. Interacts with rfp1 and rfp2. {ECO:0000269|PubMed:17762865}.
-!- INTERACTION:
O13826:rfp1; NbExp=4; IntAct=EBI-7588105, EBI-3647269;
Q9UT72:rfp2; NbExp=3; IntAct=EBI-7588105, EBI-7587772;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:10759889,
ECO:0000269|PubMed:17762865}.
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; CU329671; CAB09120.1; -; Genomic_DNA.
EMBL; AB028016; BAA87320.1; -; Genomic_DNA.
PIR; T40371; T40371.
RefSeq; NP_595523.1; NM_001021432.2.
ProteinModelPortal; P87176; -.
SMR; P87176; -.
BioGrid; 277144; 17.
IntAct; P87176; 3.
MINT; MINT-4784040; -.
STRING; 4896.SPBC3D6.11c.1; -.
MaxQB; P87176; -.
PRIDE; P87176; -.
EnsemblFungi; SPBC3D6.11c.1; SPBC3D6.11c.1:pep; SPBC3D6.11c.
GeneID; 2540618; -.
KEGG; spo:SPBC3D6.11c; -.
EuPathDB; FungiDB:SPBC3D6.11c; -.
PomBase; SPBC3D6.11c; slx8.
InParanoid; P87176; -.
OrthoDB; EOG092C0ORB; -.
PhylomeDB; P87176; -.
UniPathway; UPA00143; -.
PRO; PR:P87176; -.
Proteomes; UP000002485; Chromosome II.
GO; GO:0000790; C:nuclear chromatin; IDA:PomBase.
GO; GO:0005634; C:nucleus; IDA:PomBase.
GO; GO:0033768; C:SUMO-targeted ubiquitin ligase complex; IPI:PomBase.
GO; GO:0061630; F:ubiquitin protein ligase activity; IDA:PomBase.
GO; GO:0008270; F:zinc ion binding; ISM:PomBase.
GO; GO:0006310; P:DNA recombination; IGI:PomBase.
GO; GO:0033234; P:negative regulation of protein sumoylation; IMP:PomBase.
GO; GO:0043161; P:proteasome-mediated ubiquitin-dependent protein catabolic process; IBA:GO_Central.
GO; GO:0042787; P:protein ubiquitination involved in ubiquitin-dependent protein catabolic process; IDA:PomBase.
Gene3D; 3.30.40.10; -; 1.
InterPro; IPR001841; Znf_RING.
InterPro; IPR013083; Znf_RING/FYVE/PHD.
InterPro; IPR017907; Znf_RING_CS.
SMART; SM00184; RING; 1.
PROSITE; PS00518; ZF_RING_1; 1.
PROSITE; PS50089; ZF_RING_2; 1.
1: Evidence at protein level;
Complete proteome; Metal-binding; Nucleus; Reference proteome;
Transferase; Ubl conjugation pathway; Zinc; Zinc-finger.
CHAIN 1 269 E3 ubiquitin-protein ligase complex slx8-
rfp subunit slx8.
/FTId=PRO_0000056331.
ZN_FING 206 247 RING-type. {ECO:0000255|PROSITE-
ProRule:PRU00175}.
SEQUENCE 269 AA; 29656 MW; 310A0F1DB88EEECB CRC64;
MPPAHKRDTN VRNLSAPYNI PSQSARVAAG NAAINRRRSS PVENSPGNGF PVSEDATDYP
SGTTSENESL PLNRAPRSLR EVASELAQEE TLPVETSDLN IDVESEVFDL EDINFQNDAD
DINQRFTYNN HPASVENSLT NVNSIHAQPT TISDMIDLTD ETSYDPRKQK FEQGKNPSTT
NAEIEKEEPS KKQVVPSSQR LADYKCVICL DSPENLSCTP CGHIFCNFCI LSALGTTAAT
QKCPVCRRKV HPNKVICLEM MLGSQKKKS


Related products :

Catalog number Product name Quantity
EIAAB34367 CARP-2,Caspase regulator CARP2,Caspases-8 and -10-associated RING finger protein 2,E3 ubiquitin-protein ligase rififylin,Fring,FYVE-RING finger protein Sakura,Homo sapiens,Human,RFFL,RING finger and F
EIAAB43947 E3 ubiquitin-protein ligase TRIM63,Homo sapiens,Human,IRF,Iris RING finger protein,MuRF1,MURF1,MuRF-1,Muscle-specific RING finger protein 1,RING finger protein 28,RNF28,SMRZ,Striated muscle RING zinc
EIAAB45299 E3 ubiquitin-protein ligase UHRF2,Homo sapiens,Human,NIRF,Np95_ICBP90-like RING finger protein,Np95-like RING finger protein,Nuclear protein 97,Nuclear zinc finger protein Np97,RING finger protein 107
EIAAB35413 E3 ubiquitin-protein ligase RNF138,hNARF,Homo sapiens,HSD4,HSD-4,Human,NARF,Nemo-like kinase-associated RING finger protein,NLK-associated RING finger protein,RING finger protein 138,RNF138
EIAAB35571 CARP-1,Caspase regulator CARP1,Caspases-8 and -10-associated RING finger protein 1,E3 ubiquitin-protein ligase RNF34,FYVE-RING finger protein Momo,Homo sapiens,hRFI,Human,Human RING finger homologous
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
EIAAB45298 E3 ubiquitin-protein ligase UHRF2,Mouse,Mus musculus,NIRF,Nirf,Np95-like ring finger protein,Nuclear protein 97,Nuclear zinc finger protein Np97,Ubiquitin-like PHD and RING finger domain-containing pr
18-003-42501 Ubiquitin ligase protein RING2 - EC 6.3.2.-; RING finger protein 2; RING finger protein 1B; RING1b; RING finger protein BAP-1; DinG protein; Huntingtin-interacting protein 2-interacting protein 3; HIP 0.05 mg Aff Pur
18-003-42502 Ubiquitin ligase protein RING2 - EC 6.3.2.-; RING finger protein 2; RING finger protein 1B; RING1b; RING finger protein BAP-1; DinG protein; Huntingtin-interacting protein 2-interacting protein 3; HIP 0.1 mg Protein A
EIAAB35549 E3 ubiquitin-protein ligase RLIM,Homo sapiens,Human,LIM domain-interacting RING finger protein,Renal carcinoma antigen NY-REN-43,RING finger LIM domain-binding protein,RING finger protein 12,RLIM,R-LI
EIAAB38244 E3 ubiquitin-protein ligase SH3RF1,Homo sapiens,Human,KIAA1494,Plenty of SH3s,POSH,Protein POSH,RING finger protein 142,RNF142,SH3 domain-containing RING finger protein 1,SH3 multiple domains protein
EIAAB38246 Heart protein phosphatase 1-binding protein,HEPP1,Homo sapiens,Human,Putative E3 ubiquitin-protein ligase SH3RF2,RING finger protein 158,RNF158,SH3 domain-containing RING finger protein 2,SH3RF2
EIAAB24906 Homo sapiens,Human,Makorin RING finger protein pseudogene 4,Makorin RING finger protein pseudogene 5,MKRN4,MKRN4P,MKRNP5,Putative E3 ubiquitin-protein ligase makorin-4,RING finger protein 64,RNF64,Zin
EIAAB35482 Dorfin,Double ring-finger protein,E3 ubiquitin-protein ligase RNF19A,Gametogenesis-expressed protein GEG-154,Geg-154,Mouse,Mus musculus,RING finger protein 19A,Rnf19,Rnf19a,UBCM4-interacting protein 1
EIAAB35429 E3 ubiquitin-protein ligase RNF149,Goliath-related E3 ubiquitin-protein ligase 4,Greul4,Mouse,Mus musculus,RING finger protein 149,Rnf149
EIAAB35404 E3 ubiquitin-protein ligase RNF133,Goliath-related E3 ubiquitin-protein ligase 2,Greul2,Mouse,Mus musculus,RING finger protein 133,Rnf133
EIAAB35550 E3 ubiquitin-protein ligase RLIM,LIM domain-interacting RING finger protein,Mouse,Mus musculus,RING finger LIM domain-binding protein,RING finger protein 12,Rlim,R-LIM,Rnf12
EIAAB35402 E3 ubiquitin-protein ligase RNF128,Gene related to anergy in lymphocytes protein,Goliath-related E3 ubiquitin-protein ligase 1,Grail,Greul1,MNCb-3816,Mouse,Mus musculus,RING finger protein 128,Rnf128
EIAAB43998 GERP,Glioblastoma-expressed RING finger protein,Homo sapiens,Human,Probable E3 ubiquitin-protein ligase TRIM8,RING finger protein 27,RNF27,TRIM8,Tripartite motif-containing protein 8
EIAAB34424 Constitutive photomorphogenesis protein 1 homolog,COP1,E3 ubiquitin-protein ligase RFWD2,hCOP1,Homo sapiens,Human,RFWD2,RING finger and WD repeat domain protein 2,RING finger protein 200,RNF200
EIAAB43861 E3 ubiquitin-protein ligase TRIM17,Homo sapiens,Human,RBCC,RING finger protein 16,RNF16,TERF,Testis RING finger protein,TRIM17,Tripartite motif-containing protein 17
EIAAB43999 Gerp,Glioblastoma-expressed RING finger protein,Mouse,Mus musculus,Probable E3 ubiquitin-protein ligase TRIM8,RING finger protein 27,Rnf27,Trim8,Tripartite motif-containing protein 8
EIAAB33374 E3 ubiquitin-protein ligase RNF144B,Homo sapiens,Human,IBR domain-containing protein 2,IBRDC2,p53-inducible RING finger protein,P53RFP,RING finger protein 144B,RNF144B
EIAAB35409 E3 ubiquitin-protein ligase RNF135,Homo sapiens,Human,L13,REUL,RIG-I E3 ubiquitin ligase,RING finger protein 135,Riplet,RNF135
EIAAB43778 E3 ubiquitin-protein ligase TRAF7,Homo sapiens,Human,RFWD1,RING finger and WD repeat-containing protein 1,RING finger protein 119,RNF119,TNF receptor-associated factor 7,TRAF7


 

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