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E3 ubiquitin-protein ligase TOM1 (EC 2.3.2.26) (HECT-type E3 ubiquitin transferase TOM1) (Suppressor of snRNA protein 2) (Temperature-dependent organization in mitotic nucleus protein 1)

 TOM1_YEAST              Reviewed;        3268 AA.
Q03280; D6VT81; Q7LIK7;
19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
01-NOV-1996, sequence version 1.
18-JUL-2018, entry version 173.
RecName: Full=E3 ubiquitin-protein ligase TOM1;
EC=2.3.2.26;
AltName: Full=HECT-type E3 ubiquitin transferase TOM1;
AltName: Full=Suppressor of snRNA protein 2;
AltName: Full=Temperature-dependent organization in mitotic nucleus protein 1;
Name=TOM1; Synonyms=SSR2; OrderedLocusNames=YDR457W; ORFNames=D8035.1;
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces.
NCBI_TaxID=559292;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 204508 / S288c;
PubMed=9169867;
Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G.,
Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C.,
Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F.,
Delaveau T., del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M.,
Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T.,
Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C.,
Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S.,
Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N.,
Paulin L., Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M.,
Prydz H., Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L.,
Rieger M., Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M.,
Scharfe M., Schmidt E.R., Schneider C., Scholler P., Schwarz S.,
Soler-Mira A., Urrestarazu L.A., Verhasselt P., Vissers S., Voet M.,
Volckaert G., Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S.,
Harris D.E., Bowman S., Brown D., Churcher C.M., Connor R., Dedman K.,
Gentles S., Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D.,
Niblett D., Odell C., Oliver K., Rajandream M.A., Richards C.,
Shore L., Walsh S.V., Barrell B.G., Dietrich F.S., Mulligan J.T.,
Allen E., Araujo R., Aviles E., Berno A., Carpenter J., Chen E.,
Cherry J.M., Chung E., Duncan M., Hunicke-Smith S., Hyman R.W.,
Komp C., Lashkari D., Lew H., Lin D., Mosedale D., Nakahara K.,
Namath A., Oefner P., Oh C., Petel F.X., Roberts D., Schramm S.,
Schroeder M., Shogren T., Shroff N., Winant A., Yelton M.A.,
Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R.,
Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S.,
Greco T., Hallsworth K., Hawkins J., Hillier L.W., Jier M.,
Johnson D., Johnston L., Kirsten J., Kucaba T., Langston Y.,
Latreille P., Le T., Mardis E., Menezes S., Miller N., Nhan M.,
Pauley A., Peluso D., Rifkin L., Riles L., Taich A., Trevaskis E.,
Vignati D., Wilcox L., Wohldman P., Vaudin M., Wilson R.,
Waterston R., Albermann K., Hani J., Heumann K., Kleine K.,
Mewes H.-W., Zollner A., Zaccaria P.;
"The nucleotide sequence of Saccharomyces cerevisiae chromosome IV.";
Nature 387:75-78(1997).
[2]
GENOME REANNOTATION.
STRAIN=ATCC 204508 / S288c;
PubMed=24374639; DOI=10.1534/g3.113.008995;
Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M.,
Cherry J.M.;
"The reference genome sequence of Saccharomyces cerevisiae: Then and
now.";
G3 (Bethesda) 4:389-398(2014).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 2156-3268, FUNCTION, AND
MUTAGENESIS OF CYS-3235.
PubMed=10395901; DOI=10.1016/S0378-1119(99)00197-3;
Utsugi T., Hirata A., Sekiguchi Y., Sasaki T., Toh-e A., Kikuchi Y.;
"Yeast tom1 mutant exhibits pleiotropic defects in nuclear division,
maintenance of nuclear structure and nucleocytoplasmic transport at
high temperatures.";
Gene 234:285-295(1999).
[4]
FUNCTION, INTERACTION WITH ADA3, AND MUTAGENESIS OF CYS-3235.
PubMed=9753545; DOI=10.1006/jmbi.1998.2036;
Saleh A., Collart M., Martens J.A., Genereaux J., Allard S., Cote J.,
Brandl C.J.;
"TOM1p, a yeast hect-domain protein which mediates transcriptional
regulation through the ADA/SAGA coactivator complexes.";
J. Mol. Biol. 282:933-946(1998).
[5]
FUNCTION.
PubMed=10660055; DOI=10.1007/PL00008662;
Sasaki T., Toh-e A., Kikuchi Y.;
"Extragenic suppressors that rescue defects in the heat stress
response of the budding yeast mutant tom1.";
Mol. Gen. Genet. 262:940-948(2000).
[6]
FUNCTION, SUBCELLULAR LOCATION, AND MUTAGENESIS OF CYS-3235.
PubMed=10873801; DOI=10.1016/S0960-9822(00)00527-3;
Duncan K., Umen J.G., Guthrie C.;
"A putative ubiquitin ligase required for efficient mRNA export
differentially affects hnRNP transport.";
Curr. Biol. 10:687-696(2000).
[7]
INTERACTION WITH KRR1.
PubMed=11027267; DOI=10.1128/MCB.20.21.7971-7979.2000;
Sasaki T., Toh-e A., Kikuchi Y.;
"Yeast Krr1p physically and functionally interacts with a novel
essential Kri1p, and both proteins are required for 40S ribosome
biogenesis in the nucleolus.";
Mol. Cell. Biol. 20:7971-7979(2000).
[8]
FUNCTION.
PubMed=11238398;
Tabb A.L., Utsugi T., Wooten-Kee C.R., Sasaki T., Edling S.A.,
Gump W., Kikuchi Y., Ellis S.R.;
"Genes encoding ribosomal proteins Rps0A/B of Saccharomyces cerevisiae
interact with TOM1 mutants defective in ribosome synthesis.";
Genetics 157:1107-1116(2001).
[9]
SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
PubMed=14562095; DOI=10.1038/nature02026;
Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
Weissman J.S., O'Shea E.K.;
"Global analysis of protein localization in budding yeast.";
Nature 425:686-691(2003).
[10]
LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
PubMed=14562106; DOI=10.1038/nature02046;
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A.,
Dephoure N., O'Shea E.K., Weissman J.S.;
"Global analysis of protein expression in yeast.";
Nature 425:737-741(2003).
[11]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1890 AND SER-2418, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
STRAIN=ADR376;
PubMed=17330950; DOI=10.1021/pr060559j;
Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,
Elias J.E., Gygi S.P.;
"Large-scale phosphorylation analysis of alpha-factor-arrested
Saccharomyces cerevisiae.";
J. Proteome Res. 6:1190-1197(2007).
[12]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1890; SER-2376 AND
SER-2418, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
PubMed=18407956; DOI=10.1074/mcp.M700468-MCP200;
Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
"A multidimensional chromatography technology for in-depth
phosphoproteome analysis.";
Mol. Cell. Proteomics 7:1389-1396(2008).
[13]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1890; THR-2096;
SER-2119; SER-2376; SER-2406 AND SER-2418, AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19779198; DOI=10.1126/science.1172867;
Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
"Global analysis of Cdk1 substrate phosphorylation sites provides
insights into evolution.";
Science 325:1682-1686(2009).
-!- FUNCTION: Probable ubiquitin ligase protein involved in many
cellular processes, such as transcription regulation, maintenance
of nuclear structure, cell cycle, mRNA export and rRNA maturation.
E3 ubiquitin ligase proteins mediate ubiquitination and subsequent
proteasomal degradation of target proteins. Involved in
transcription regulation by interacting, and probably mediating,
ubiquitination of some subunit of the SAGA complex. Required for
SPT7 ubiquitination. Participates in mRNA export from the nucleus
by regulating the transport of hnRNP proteins. Required for the
shuttling of hnRNP protein NAB2, probably by mediating
ubiquitination of a protein associated with NAB2. Also required
for full induction of the general stress and heat-shock responses.
Involved in 18S rRNA maturation by affecting several early steps
in the rRNA processing pathway. {ECO:0000269|PubMed:10395901,
ECO:0000269|PubMed:10660055, ECO:0000269|PubMed:10873801,
ECO:0000269|PubMed:11238398, ECO:0000269|PubMed:9753545}.
-!- 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: Interacts with the ADA3/NGG1 subunit of the SAGA complex.
Interacts with KRR1. {ECO:0000269|PubMed:11027267,
ECO:0000269|PubMed:9753545}.
-!- INTERACTION:
P15108:HSC82; NbExp=4; IntAct=EBI-36817, EBI-8666;
P19524:MYO2; NbExp=7; IntAct=EBI-36817, EBI-11659;
P32492:MYO4; NbExp=2; IntAct=EBI-36817, EBI-11681;
P23201:SPA2; NbExp=5; IntAct=EBI-36817, EBI-17803;
P38788:SSZ1; NbExp=2; IntAct=EBI-36817, EBI-24570;
P0CG63:UBI4; NbExp=3; IntAct=EBI-36817, EBI-7000452;
P16521:YEF3; NbExp=2; IntAct=EBI-36817, EBI-6338;
P32527:ZUO1; NbExp=3; IntAct=EBI-36817, EBI-29684;
-!- SUBCELLULAR LOCATION: Nucleus, nucleolus
{ECO:0000269|PubMed:10873801, ECO:0000269|PubMed:14562095}.
-!- MISCELLANEOUS: Present with 350 molecules/cell in log phase SD
medium. {ECO:0000269|PubMed:14562106}.
-!- SIMILARITY: Belongs to the UPL family. TOM1/PTR1 subfamily.
{ECO:0000305}.
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EMBL; U33050; AAB64910.1; -; Genomic_DNA.
EMBL; D63905; BAA21482.1; -; Genomic_DNA.
EMBL; BK006938; DAA12291.1; -; Genomic_DNA.
PIR; S69625; S69625.
RefSeq; NP_010745.3; NM_001180765.3.
ProteinModelPortal; Q03280; -.
SMR; Q03280; -.
BioGrid; 32511; 705.
DIP; DIP-5927N; -.
IntAct; Q03280; 30.
MINT; Q03280; -.
STRING; 4932.YDR457W; -.
iPTMnet; Q03280; -.
MaxQB; Q03280; -.
PaxDb; Q03280; -.
PRIDE; Q03280; -.
EnsemblFungi; YDR457W; YDR457W; YDR457W.
GeneID; 852068; -.
KEGG; sce:YDR457W; -.
EuPathDB; FungiDB:YDR457W; -.
SGD; S000002865; TOM1.
GeneTree; ENSGT00850000132302; -.
HOGENOM; HOG000093627; -.
InParanoid; Q03280; -.
KO; K10592; -.
OMA; LLNCPNF; -.
OrthoDB; EOG092C016J; -.
BioCyc; YEAST:G3O-29985-MONOMER; -.
Reactome; R-SCE-6798695; Neutrophil degranulation.
Reactome; R-SCE-983168; Antigen processing: Ubiquitination & Proteasome degradation.
UniPathway; UPA00143; -.
PRO; PR:Q03280; -.
Proteomes; UP000002311; Chromosome IV.
GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
GO; GO:0061630; F:ubiquitin protein ligase activity; IBA:GO_Central.
GO; GO:0004842; F:ubiquitin-protein transferase activity; IDA:SGD.
GO; GO:0000448; P:cleavage in ITS2 between 5.8S rRNA and LSU-rRNA of tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA); IMP:SGD.
GO; GO:0000480; P:endonucleolytic cleavage in 5'-ETS of tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA); IMP:SGD.
GO; GO:0000447; P:endonucleolytic cleavage in ITS1 to separate SSU-rRNA from 5.8S rRNA and LSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA); IMP:SGD.
GO; GO:0000472; P:endonucleolytic cleavage to generate mature 5'-end of SSU-rRNA from (SSU-rRNA, 5.8S rRNA, LSU-rRNA); IMP:SGD.
GO; GO:0000278; P:mitotic cell cycle; IMP:SGD.
GO; GO:0051028; P:mRNA transport; IEA:UniProtKB-KW.
GO; GO:0006913; P:nucleocytoplasmic transport; IMP:SGD.
GO; GO:0006997; P:nucleus organization; IMP:SGD.
GO; GO:0016567; P:protein ubiquitination; IDA:SGD.
GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:UniProtKB-KW.
GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IMP:SGD.
CDD; cd00078; HECTc; 1.
Gene3D; 1.25.10.10; -; 1.
InterPro; IPR011989; ARM-like.
InterPro; IPR016024; ARM-type_fold.
InterPro; IPR025527; DUF4414.
InterPro; IPR010309; E3_Ub_ligase_DUF908.
InterPro; IPR010314; E3_Ub_ligase_DUF913.
InterPro; IPR000569; HECT_dom.
InterPro; IPR035983; Hect_E3_ubiquitin_ligase.
Pfam; PF14377; DUF4414; 1.
Pfam; PF06012; DUF908; 1.
Pfam; PF06025; DUF913; 1.
Pfam; PF00632; HECT; 1.
SMART; SM00119; HECTc; 1.
SUPFAM; SSF48371; SSF48371; 2.
SUPFAM; SSF56204; SSF56204; 1.
PROSITE; PS50237; HECT; 1.
1: Evidence at protein level;
Cell cycle; Complete proteome; mRNA transport; Nucleus;
Phosphoprotein; Reference proteome; rRNA processing; Transcription;
Transcription regulation; Transferase; Transport;
Ubl conjugation pathway.
CHAIN 1 3268 E3 ubiquitin-protein ligase TOM1.
/FTId=PRO_0000120348.
DOMAIN 2932 3268 HECT. {ECO:0000255|PROSITE-
ProRule:PRU00104}.
COMPBIAS 1879 2054 Asp-rich.
ACT_SITE 3235 3235 Glycyl thioester intermediate.
{ECO:0000255|PROSITE-ProRule:PRU00104}.
MOD_RES 1890 1890 Phosphoserine.
{ECO:0000244|PubMed:17330950,
ECO:0000244|PubMed:18407956,
ECO:0000244|PubMed:19779198}.
MOD_RES 2096 2096 Phosphothreonine.
{ECO:0000244|PubMed:19779198}.
MOD_RES 2119 2119 Phosphoserine.
{ECO:0000244|PubMed:19779198}.
MOD_RES 2376 2376 Phosphoserine.
{ECO:0000244|PubMed:18407956,
ECO:0000244|PubMed:19779198}.
MOD_RES 2406 2406 Phosphoserine.
{ECO:0000244|PubMed:19779198}.
MOD_RES 2418 2418 Phosphoserine.
{ECO:0000244|PubMed:17330950,
ECO:0000244|PubMed:18407956,
ECO:0000244|PubMed:19779198}.
MUTAGEN 3235 3235 C->A: Loss of function. Induces a
decrease in transcription activation.
{ECO:0000269|PubMed:10395901,
ECO:0000269|PubMed:10873801,
ECO:0000269|PubMed:9753545}.
SEQUENCE 3268 AA; 374185 MW; 8F71F3493D70A6C9 CRC64;
MVLFTRCEKA RKEKLAAGYK PLVDYLIDCD TPTFLERIEA IQEWDRSRDD LYVWIPILDR
MDGLLLKVAE KYKYKQDPKK ECEVKLVEME AHDVDYCLKM LKFTRRLLLN TENRFVYSSG
DVLMYLLNCP NFTIKLAVMR ILAILGERFV IAREKIVAHN IFGDHNLRKK TLKLALSLSS
SVMDEDGEHF SLVDLYFDKK KVPQKWRKLR FTHYTSNDFK KSSQQKNNIN ETQTSIKKVT
MTTQELCEHS LQQIFDKGMA LLPAESWFDF SIKASVAKAF SDDSGENIDL RNIIIETKLN
AIAFVNTIFS PPQVSSKLFE LDPYAFNSLT DLISLSETKI PKELRTDALF TLECISLKHV
WCSDIIRNLG GNISHGLLFQ ILRYIAKTLR EATDEIDEEY NVRFFYLISN LADVKPLHES
LFAAGLIPTL LEIVSIRNCP YKRTLASATH LLETFIDNSE TTTEFIENDG FTMLITSVAN
EIDFTLAHPE TWQPPKYSVV YYSISFRELA YIRSLLKLVL KLLSTDSGDR IRNLIDSPIL
VSLKKILENK LVFGLTLITY TLDVVQKVIN SEPTIYPVLV EAGLIPYVID NFPKLIGPSA
ELLSLLPDVV SAICLNPEGL KQVKEKGLIN NLFDFLLDAD HARILTGGDR STEYGTDIDE
LARHYPDLKA NIVEALCNVI RKMPSTFRNE REFLFTSPKD QKYFFHRKNE EILTDKEEHE
PAYWELLDKG TMLDTFTSVL FGMSLGNGSF SQVPQHLEAR DFLAIIFMEN PPYEYFTSVA
ISNVTEVLQY LDEKYEDYAF MDVMKVLNDQ LENLNDFLNS PNDRSFFLER DGENSVRSCH
SKLCRLAAIL NIVTNVYIDL TTLSCKRIMQ IYSYFDKRGF SLIKNLKLLF QKCALEEMYI
RQHMPDSVIT ETMPLPIVDV SGDGPPLQIY IDDPKKGDQK GKITSVKTRN TLQMRTILYT
LQSNTAILFR CFLRLSHSRN MDLEHKDLTT EVHIFENVVE NVIEMLKATE LEGHLPYILV
LLNFNTFVFT IPKASPNSTE ILQTIPAYIF YQKGGYLLYL HIIRDLFTRM TKIKDLSSLD
NINYIDESNG ILTLSCLINA LTFYNKSMQT ETMENVQSIG KYYVSIDDDY NIMKALTVPI
KVMALAMILD LDKSDSLFKT QSRNVPYSVF KQLLSMLKNI FTNVNIYTKE LYELHWDLIF
PPIKKISLFE QVGIPGDVAA NYLTDTGDDL PADNSIGLFS PEQWEKYKKL IGEDKSIYYP
QPMQAQYYKG CSSKELDELR DTFFNDGLPS RIFTVLPFYP KLVNAFAKTL LQIFTKYDEP
TEVFAGRILD RILETDLDDP ATLSSLIHLF GIFLNEKYIY QKASHLMQRF IEYLEKSLKP
EHVNTPWFSK ALYVYEIILA KSELPHLEEL SKDVLLRYPL LSMAKVFRIP DPMKQKLFDI
LIRVSDISNF YSALATSRIL IFYSRDELYA NNIARSGILS RLLKVIGSFQ KLDKINFLES
SFLLLTRRCF ETTENVDALI RAEINRSFTA RPLGGGDDAV RELTTILEEK AHVVMRSPSQ
FIDVLCETAR FHEFDDQGAL VDYSLKRFLG EKDKNTQASS TEKSDIYERT GIMHLLLSQL
MAASEKDWLS EPANSSDLPE NKKAQLDPSR NPVCAYMIFL LKLLVELVSS YNQCKFEFLT
FSRRNTYAER PRPRTTAINF FLYRLLDKPV GTDHDKHEAK RREVIGMLAR SVIIGFLATV
QDDRTTKTDV KLADPHMNFI RKFAIEAIIK AIRNATSSSK LLESNHLKLD MWFRIITSMV
YVQAPYLRQL LDSNKVEADQ YQLCKLVIDL GLPSVITEAM ASIDLNYPFS KKIFNVAVEA
LNTISSTRNN FSEHFKIEDH DEVEDEVDES DKEEIPDMFK NSALGMYDVE DIEEDDDDDT
SLIGDDDAMA FVDSDNGFEV VFSDEDDDMG EEDADDARSD SEENELSSEM QSSTADGTDV
DYEVDDADGL IINIDQPSGD DEEMADYDAN ISHSSHSENE DDASMDVIEV YDDELSSGYD
VDLSDYDVDE SDWDSGLSSL SISDEDSESS EDEPINSTRM GDSRRRWLIA EGVELTDDSQ
GESEEDDRGV FRGIEHIFSN ENEPLFRVHD EMRHRNHHRS INRTHFHSAM SAPSLSLLNR
GRRNQSNLIN PLGPTGLEQV ENDISDQVTV AGSGSRPRSH HLHFSEVLVS GSFFDEPVLD
GIILKSTVSR WKDIFDMFYD SKTYANCIIP TVINRLYKVS LALQKDLENK REQEKLKNKN
LLFNEAKVES HNSSDAISVE QDDIQESNVT HDDHEPVYVT IQGSEVDIGG TDIDPEFMNA
LPDDIRADVF AQHVRERRAE ARLNSDHNVH SREIDSDFLE AIPEDIREGI LDTEAEEQRM
FGRIGSSADV IRADDDVSNN DEEVENGLDH GNSNDRNNAD PEKKKPARIY FAPLIDRAGI
ASLMKSVFIS KPYIQREIYH ELFYRLCSSK QNRNDLMNTF LFILSEGIID QHSLEKVYNI
ISSRAMGHAK TTTVRQLPSD CTPLTVANQT IEILQSLIDA DSRLKYFLIA EHDNLIVNKA
NNKSRKEALP DKKLRWPLWH LFSLLDRKLI TDESVLMDLL TRILQVCTKT LAVLSTSSNG
KENLSKKFHL PSFDEDDLMK ILSIIMLDSC TTRVFQQTLN IIYNLSKLQG CMSIFTKHLV
SLAISIMSKL KSALDGLSRE VGTITTGMEI NSELLQKFTL PSSDQAKLLK ILTTVDFLYT
HKRKEEERNV KDLQSLYDKM NGGPVWSSLS ECLSQFEKSQ AINTSATILL PLIESLMVVC
RRSDLSQNRN TAVKYEDAKL LDFSKTRVEN LFFPFTDAHK KLLNQMIRSN PKLMSGPFAL
LVKNPKVLDF DNKRYFFNAK LKSDNQERPK LPITVRREQV FLDSYRALFF KTNDEIKNSK
LEITFKGESG VDAGGVTREW YQVLSRQMFN PDYALFLPVP SDKTTFHPNR TSGINPEHLS
FFKFIGMIIG KAIRDQCFLD CHFSREVYKN ILGRPVSLKD MESLDPDYYK SLVWILENDI
TDIIEETFSV ETDDYGEHKV INLIEGGKDI IVTEANKQDY VKKVVEYKLQ TSVKEQMDNF
LVGFYALISK DLITIFDEQE LELLISGLPD IDVDDWKNNT TYVNYTATCK EVSYFWRAVR
SFDAEERAKL LQFVTGTSKV PLNGFKELSG VNGVCKFSIH RDFGSSERLP SSHTCFNQLN
LPPYESYETL RGSLLLAINE GHEGFGLA


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EIAAB45117 E3 ubiquitin-protein ligase UBR3,Kiaa2024,Mouse,Mus musculus,N-recognin-3,Ubiquitin-protein ligase E3-alpha-3,Ubiquitin-protein ligase E3-alpha-III,Ubr3,Zfp650,Zinc finger protein 650,Znf650
EIAAB45116 E3 ubiquitin-protein ligase UBR3,Homo sapiens,Human,KIAA2024,N-recognin-3,Ubiquitin-protein ligase E3-alpha-3,Ubiquitin-protein ligase E3-alpha-III,UBR3,Zinc finger protein 650,ZNF650
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
EIAAB44818 Homo sapiens,Human,NICE5,PRO3094,Protein NICE-5,UBE2Q,UBE2Q1,Ubiquitin carrier protein Q1,Ubiquitin-conjugating enzyme E2 Q1,Ubiquitin-protein ligase Q1
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
18-003-44311 Ubiquitin-conjugating enzyme E2-25 kDa - EC 6.3.2.19; Ubiquitin-protein ligase; Ubiquitin carrier protein; E2(25K); Huntingtin-interacting protein 2; HIP-2 Polyclonal 0.1 mg Protein A
EIAAB45115 C6orf133,E3 ubiquitin-protein ligase UBR2,Homo sapiens,Human,KIAA0349,N-recognin-2,Ubiquitin-protein ligase E3-alpha-2,Ubiquitin-protein ligase E3-alpha-II,UBR2
10-663-45300 ubiquitin-conjugating enzyme (UBC9) Human - EC 6.3.2.19; SUMO-1-protein ligase; Ubiquitin-conjugating enzyme E2 I; Ubiquitin-protein ligase I; Ubiquitin carrier protein I; Ubiquitin carrier protein 9; 0.05 mg
10-663-45300 ubiquitin-conjugating enzyme (UBC9) Human - EC 6.3.2.19; SUMO-1-protein ligase; Ubiquitin-conjugating enzyme E2 I; Ubiquitin-protein ligase I; Ubiquitin carrier protein I; Ubiquitin carrier protein 9; 1 mg
10-663-45300 ubiquitin-conjugating enzyme (UBC9) Human - EC 6.3.2.19; SUMO-1-protein ligase; Ubiquitin-conjugating enzyme E2 I; Ubiquitin-protein ligase I; Ubiquitin carrier protein I; Ubiquitin carrier protein 9; 0.01 mg
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
EIAAB25831 C1orf166,E3 ubiquitin-protein ligase MUL1,GIDE,Growth inhibition and death E3 ligase,Homo sapiens,Human,MAPL,Mitochondrial ubiquitin ligase activator of NFKB 1,Mitochondrial-anchored protein ligase,MU
EIAAB44781 Pig,Sus scrofa,UBC4,UBCH4,UBCH5B,UBE2D2,Ubiquitin carrier protein D2,Ubiquitin-conjugating enzyme E2 D2,Ubiquitin-protein ligase D2
EIAAB44811 Mouse,Mus musculus,Ubce7,UbcM4,Ube2l3,Ubiquitin carrier protein L3,Ubiquitin-conjugating enzyme E2 L3,Ubiquitin-protein ligase L3
EIAAB44911 Homo sapiens,Human,Probable ubiquitin-conjugating enzyme E2 W,UBE2W,Ubiquitin carrier protein W,Ubiquitin-protein ligase W
EIAAB44802 E217K,Mouse,Mus musculus,UBC7,Ube2g,Ube2g1,Ubiquitin carrier protein G1,Ubiquitin-conjugating enzyme E2 G1,Ubiquitin-protein ligase G1
EIAAB44790 HBUCE1,Homo sapiens,Human,UBCH5D,UBE2D4,Ubiquitin carrier protein D4,Ubiquitin-conjugating enzyme E2 D4,Ubiquitin-protein ligase D4
EIAAB44785 Bos taurus,Bovine,UBC4,UBCH4,UBCH5B,UBE2D2,Ubiquitin carrier protein D2,Ubiquitin-conjugating enzyme E2 D2,Ubiquitin-protein ligase D2
EIAAB44801 E217K,Homo sapiens,Human,UBC7,UBE2G,UBE2G1,Ubiquitin carrier protein G1,Ubiquitin-conjugating enzyme E2 G1,Ubiquitin-protein ligase G1
EIAAB44822 Homo sapiens,Human,UBE2Q2,Ubiquitin carrier protein Q2,Ubiquitin-conjugating enzyme E2 Q2,Ubiquitin-protein ligase Q2
EIAAB44819 Mouse,Mus musculus,Ube2q,Ube2q1,Ubiquitin carrier protein Q1,Ubiquitin-conjugating enzyme E2 Q1,Ubiquitin-protein ligase Q1


 

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