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Ubiquitin-conjugating enzyme E2 E1 (EC 2.3.2.23) ((E3-independent) E2 ubiquitin-conjugating enzyme E1) (EC 2.3.2.24) (E2 ubiquitin-conjugating enzyme E1) (UbcH6) (Ubiquitin carrier protein E1) (Ubiquitin-protein ligase E1)

 UB2E1_HUMAN             Reviewed;         193 AA.
P51965; B2RBX4; C9J8K2; K4DI90;
01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
01-OCT-1996, sequence version 1.
23-MAY-2018, entry version 182.
RecName: Full=Ubiquitin-conjugating enzyme E2 E1;
EC=2.3.2.23 {ECO:0000269|PubMed:20061386};
AltName: Full=(E3-independent) E2 ubiquitin-conjugating enzyme E1;
EC=2.3.2.24 {ECO:0000269|PubMed:17588522};
AltName: Full=E2 ubiquitin-conjugating enzyme E1;
AltName: Full=UbcH6;
AltName: Full=Ubiquitin carrier protein E1;
AltName: Full=Ubiquitin-protein ligase E1;
Name=UBE2E1; Synonyms=UBCH6;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
PubMed=8576257; DOI=10.1074/jbc.271.5.2795;
Nuber U., Schwarz S., Kaiser P., Schneider R., Scheffner M.;
"Cloning of human ubiquitin-conjugating enzymes UbcH6 and UbcH7 (E2-
F1) and characterization of their interaction with E6-AP and RSP5.";
J. Biol. Chem. 271:2795-2800(1996).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Amygdala;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16641997; DOI=10.1038/nature04728;
Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R.,
Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R.,
Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V.,
Hume J., Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R.,
Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Morgan M.B.,
Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Wei S.,
Wheeler D.A., Wright M.W., Worley K.C., Yuan Y., Zhang Z., Adams C.Q.,
Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z.,
Clendenning J., Clerc-Blankenburg K.P., Chen R., Chen Z., Davis C.,
Delgado O., Dinh H.H., Dong W., Draper H., Ernst S., Fu G.,
Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., Hao B.,
Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., Jackson L.R.,
Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., Liu J.,
Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Palmeiri A.,
Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B.,
Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H.,
Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J.,
Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J.,
Zhang X., Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H.,
Reinhardt R., Naylor S.L., Yang H., Olson M., Weinstock G.,
Gibbs R.A.;
"The DNA sequence, annotation and analysis of human chromosome 3.";
Nature 440:1194-1198(2006).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 3).
TISSUE=Cervix carcinoma, Colon, and Hypothalamus;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[6]
FUNCTION, AND ISGYLATION AT LYS-136.
PubMed=16428300; DOI=10.1093/jb/mvi172;
Takeuchi T., Iwahara S., Saeki Y., Sasajima H., Yokosawa H.;
"Link between the ubiquitin conjugation system and the ISG15
conjugation system: ISG15 conjugation to the UbcH6 ubiquitin E2
enzyme.";
J. Biochem. 138:711-719(2005).
[7]
CATALYTIC ACTIVITY AS E3-INDEPENDENT E2 UBIQUITIN-CONJUGATING ENZYME.
PubMed=17588522; DOI=10.1016/j.molcel.2007.05.014;
Hoeller D., Hecker C.M., Wagner S., Rogov V., Doetsch V., Dikic I.;
"E3-independent monoubiquitination of ubiquitin-binding proteins.";
Mol. Cell 26:891-898(2007).
[8]
SUBCELLULAR LOCATION.
PubMed=18845142; DOI=10.1016/j.yexcr.2008.09.011;
Espinosa A., Oke V., Elfving A., Nyberg F., Covacu R.,
Wahren-Herlenius M.;
"The autoantigen Ro52 is an E3 ligase resident in the cytoplasm but
enters the nucleus upon cellular exposure to nitric oxide.";
Exp. Cell Res. 314:3605-3613(2008).
[9]
ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19413330; DOI=10.1021/ac9004309;
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
Mohammed S.;
"Lys-N and trypsin cover complementary parts of the phosphoproteome in
a refined SCX-based approach.";
Anal. Chem. 81:4493-4501(2009).
[10]
FUNCTION, AND CATALYTIC ACTIVITY.
PubMed=20061386; DOI=10.1074/jbc.M109.089003;
David Y., Ziv T., Admon A., Navon A.;
"The E2 ubiquitin-conjugating enzymes direct polyubiquitination to
preferred lysines.";
J. Biol. Chem. 285:8595-8604(2010).
[11]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[12]
ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21406692; DOI=10.1126/scisignal.2001570;
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
Blagoev B.;
"System-wide temporal characterization of the proteome and
phosphoproteome of human embryonic stem cell differentiation.";
Sci. Signal. 4:RS3-RS3(2011).
[13] {ECO:0000244|PDB:3BZH}
X-RAY CRYSTALLOGRAPHY (1.60 ANGSTROMS), AND AUTOUBIQUITINATION.
PubMed=22496338; DOI=10.1074/mcp.O111.013706;
Sheng Y., Hong J.H., Doherty R., Srikumar T., Shloush J.,
Avvakumov G.V., Walker J.R., Xue S., Neculai D., Wan J.W., Kim S.K.,
Arrowsmith C.H., Raught B., Dhe-Paganon S.;
"A human ubiquitin conjugating enzyme (E2)-HECT E3 ligase structure-
function screen.";
Mol. Cell. Proteomics 11:329-341(2012).
-!- FUNCTION: Accepts ubiquitin from the E1 complex and catalyzes its
covalent attachment to other proteins. Catalyzes the covalent
attachment of ISG15 to other proteins. Mediates the selective
degradation of short-lived and abnormal proteins. In vitro also
catalyzes 'Lys-48'-linked polyubiquitination.
{ECO:0000269|PubMed:16428300, ECO:0000269|PubMed:20061386}.
-!- CATALYTIC ACTIVITY: S-ubiquitinyl-[E1 ubiquitin-activating
enzyme]-L-cysteine + [E2 ubiquitin-conjugating enzyme]-L-cysteine
= [E1 ubiquitin-activating enzyme]-L-cysteine + S-ubiquitinyl-[E2
ubiquitin-conjugating enzyme]-L-cysteine. {ECO:0000255|PROSITE-
ProRule:PRU00388, ECO:0000255|PROSITE-ProRule:PRU10133,
ECO:0000269|PubMed:20061386}.
-!- CATALYTIC ACTIVITY: S-ubiquitinyl-[E1 ubiquitin-activating
enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E1 ubiquitin-
activating enzyme]-L-cysteine + N(6)-monoubiquitinyl-[acceptor
protein]-L-lysine. {ECO:0000269|PubMed:17588522}.
-!- PATHWAY: Protein modification; protein ubiquitination.
{ECO:0000255|PROSITE-ProRule:PRU00388}.
-!- SUBUNIT: Interacts with RNF14.
-!- INTERACTION:
Q99PZ6:ospG (xeno); NbExp=3; IntAct=EBI-348546, EBI-9316527;
Q96FW1:OTUB1; NbExp=3; IntAct=EBI-348546, EBI-1058491;
Q8N7H5:PAF1; NbExp=2; IntAct=EBI-348546, EBI-2607770;
Q9Y3C5:RNF11; NbExp=2; IntAct=EBI-348546, EBI-396669;
Q5VTR2:RNF20; NbExp=2; IntAct=EBI-348546, EBI-2372238;
Q8ND25:ZNRF1; NbExp=3; IntAct=EBI-348546, EBI-2129250;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:18845142}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=1;
IsoId=P51965-1; Sequence=Displayed;
Name=2;
IsoId=P51965-2; Sequence=VSP_045884;
Note=No experimental confirmation available.;
Name=3;
IsoId=P51965-3; Sequence=VSP_047200;
Note=No experimental confirmation available.;
-!- PTM: ISGylation suppresses ubiquitin E2 enzyme activity.
{ECO:0000269|PubMed:16428300}.
-!- PTM: Autoubiquitinated in vitro. {ECO:0000269|PubMed:22496338}.
-!- SIMILARITY: Belongs to the ubiquitin-conjugating enzyme family.
{ECO:0000255|PROSITE-ProRule:PRU00388}.
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EMBL; X92963; CAA63539.1; -; mRNA.
EMBL; AK314854; BAG37371.1; -; mRNA.
EMBL; AC020626; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC124914; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471055; EAW64329.1; -; Genomic_DNA.
EMBL; CH471055; EAW64331.1; -; Genomic_DNA.
EMBL; CH471055; EAW64332.1; -; Genomic_DNA.
EMBL; BC009139; AAH09139.1; -; mRNA.
EMBL; BI223271; -; NOT_ANNOTATED_CDS; mRNA.
EMBL; BI666638; -; NOT_ANNOTATED_CDS; mRNA.
CCDS; CCDS2638.1; -. [P51965-1]
CCDS; CCDS2639.1; -. [P51965-3]
CCDS; CCDS56244.1; -. [P51965-2]
RefSeq; NP_001189405.1; NM_001202476.1. [P51965-2]
RefSeq; NP_003332.1; NM_003341.4. [P51965-1]
RefSeq; NP_872607.1; NM_182666.2. [P51965-3]
UniGene; Hs.164853; -.
PDB; 1XR9; X-ray; 1.79 A; C=83-91.
PDB; 3BZH; X-ray; 1.60 A; A=1-193.
PDB; 4JJQ; X-ray; 1.95 A; B=5-14.
PDB; 5LBN; X-ray; 1.42 A; A=37-193.
PDBsum; 1XR9; -.
PDBsum; 3BZH; -.
PDBsum; 4JJQ; -.
PDBsum; 5LBN; -.
ProteinModelPortal; P51965; -.
SMR; P51965; -.
BioGrid; 113172; 132.
CORUM; P51965; -.
IntAct; P51965; 68.
MINT; P51965; -.
STRING; 9606.ENSP00000303709; -.
iPTMnet; P51965; -.
PhosphoSitePlus; P51965; -.
BioMuta; UBE2E1; -.
DMDM; 1717857; -.
EPD; P51965; -.
MaxQB; P51965; -.
PaxDb; P51965; -.
PeptideAtlas; P51965; -.
PRIDE; P51965; -.
Ensembl; ENST00000306627; ENSP00000303709; ENSG00000170142. [P51965-1]
Ensembl; ENST00000346855; ENSP00000329113; ENSG00000170142. [P51965-3]
Ensembl; ENST00000424381; ENSP00000411351; ENSG00000170142. [P51965-2]
GeneID; 7324; -.
KEGG; hsa:7324; -.
UCSC; uc003cch.4; human. [P51965-1]
CTD; 7324; -.
DisGeNET; 7324; -.
EuPathDB; HostDB:ENSG00000170142.11; -.
GeneCards; UBE2E1; -.
HGNC; HGNC:12477; UBE2E1.
HPA; CAB073413; -.
HPA; HPA030445; -.
MIM; 602916; gene.
neXtProt; NX_P51965; -.
OpenTargets; ENSG00000170142; -.
PharmGKB; PA37127; -.
eggNOG; KOG0417; Eukaryota.
eggNOG; COG5078; LUCA.
GeneTree; ENSGT00910000143990; -.
HOGENOM; HOG000233455; -.
HOVERGEN; HBG063308; -.
InParanoid; P51965; -.
KO; K20217; -.
OMA; IVFRTRI; -.
OrthoDB; EOG091G0GF8; -.
PhylomeDB; P51965; -.
TreeFam; TF101117; -.
BRENDA; 2.3.2.B6; 2681.
Reactome; R-HSA-1169408; ISG15 antiviral mechanism.
Reactome; R-HSA-141430; Inactivation of APC/C via direct inhibition of the APC/C complex.
Reactome; R-HSA-174048; APC/C:Cdc20 mediated degradation of Cyclin B.
Reactome; R-HSA-174084; Autodegradation of Cdh1 by Cdh1:APC/C.
Reactome; R-HSA-174154; APC/C:Cdc20 mediated degradation of Securin.
Reactome; R-HSA-174178; APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1.
Reactome; R-HSA-174184; Cdc20:Phospho-APC/C mediated degradation of Cyclin A.
Reactome; R-HSA-176407; Conversion from APC/C:Cdc20 to APC/C:Cdh1 in late anaphase.
Reactome; R-HSA-176408; Regulation of APC/C activators between G1/S and early anaphase.
Reactome; R-HSA-176409; APC/C:Cdc20 mediated degradation of mitotic proteins.
Reactome; R-HSA-176412; Phosphorylation of the APC/C.
Reactome; R-HSA-179409; APC-Cdc20 mediated degradation of Nek2A.
Reactome; R-HSA-2467813; Separation of Sister Chromatids.
Reactome; R-HSA-2559582; Senescence-Associated Secretory Phenotype (SASP).
Reactome; R-HSA-69017; CDK-mediated phosphorylation and removal of Cdc6.
Reactome; R-HSA-8866652; Synthesis of active ubiquitin: roles of E1 and E2 enzymes.
Reactome; R-HSA-8866654; E3 ubiquitin ligases ubiquitinate target proteins.
Reactome; R-HSA-983168; Antigen processing: Ubiquitination & Proteasome degradation.
SignaLink; P51965; -.
UniPathway; UPA00143; -.
ChiTaRS; UBE2E1; human.
EvolutionaryTrace; P51965; -.
GeneWiki; UBE2E1; -.
GenomeRNAi; 7324; -.
PRO; PR:P51965; -.
Proteomes; UP000005640; Chromosome 3.
Bgee; ENSG00000170142; -.
CleanEx; HS_UBE2E1; -.
ExpressionAtlas; P51965; baseline and differential.
Genevisible; P51965; HS.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0000151; C:ubiquitin ligase complex; IDA:UniProtKB.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0042296; F:ISG15 transferase activity; IDA:HGNC.
GO; GO:0061631; F:ubiquitin conjugating enzyme activity; IDA:BHF-UCL.
GO; GO:0004842; F:ubiquitin-protein transferase activity; IDA:UniProtKB.
GO; GO:0031145; P:anaphase-promoting complex-dependent catabolic process; TAS:Reactome.
GO; GO:0033523; P:histone H2B ubiquitination; IDA:UniProtKB.
GO; GO:0010390; P:histone monoubiquitination; IDA:UniProtKB.
GO; GO:0032020; P:ISG15-protein conjugation; IDA:HGNC.
GO; GO:0070936; P:protein K48-linked ubiquitination; IDA:UniProtKB.
GO; GO:0000209; P:protein polyubiquitination; IDA:UniProtKB.
GO; GO:0016567; P:protein ubiquitination; IDA:BHF-UCL.
GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; TAS:ProtInc.
CDD; cd00195; UBCc; 1.
Gene3D; 3.10.110.10; -; 1.
InterPro; IPR000608; UBQ-conjugat_E2.
InterPro; IPR023313; UBQ-conjugating_AS.
InterPro; IPR016135; UBQ-conjugating_enzyme/RWD.
Pfam; PF00179; UQ_con; 1.
SUPFAM; SSF54495; SSF54495; 1.
PROSITE; PS00183; UBIQUITIN_CONJUGAT_1; 1.
PROSITE; PS50127; UBIQUITIN_CONJUGAT_2; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Alternative splicing; ATP-binding;
Complete proteome; Isopeptide bond; Nucleotide-binding; Nucleus;
Polymorphism; Reference proteome; Transferase; Ubl conjugation;
Ubl conjugation pathway.
INIT_MET 1 1 Removed. {ECO:0000244|PubMed:19413330,
ECO:0000244|PubMed:21406692}.
CHAIN 2 193 Ubiquitin-conjugating enzyme E2 E1.
/FTId=PRO_0000082470.
COMPBIAS 9 18 Poly-Ser.
ACT_SITE 131 131 Glycyl thioester intermediate.
{ECO:0000255|PROSITE-ProRule:PRU00388,
ECO:0000255|PROSITE-ProRule:PRU10133}.
MOD_RES 2 2 N-acetylserine.
{ECO:0000244|PubMed:19413330,
ECO:0000244|PubMed:21406692}.
CROSSLNK 136 136 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ISG15).
VAR_SEQ 1 50 MSDDDSRASTSSSSSSSSNQQTEKETNTPKKKESKVSMSKN
SKLLSTSAK -> MKEVGRPREVRGRPGKS (in
isoform 2).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_045884.
VAR_SEQ 51 67 Missing (in isoform 3).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_047200.
VARIANT 25 25 E -> D (in dbSNP:rs36060625).
/FTId=VAR_061868.
CONFLICT 131 131 C -> R (in Ref. 5; BI223271).
{ECO:0000305}.
HELIX 22 24 {ECO:0000244|PDB:3BZH}.
HELIX 42 44 {ECO:0000244|PDB:5LBN}.
HELIX 47 61 {ECO:0000244|PDB:5LBN}.
STRAND 67 74 {ECO:0000244|PDB:5LBN}.
STRAND 78 84 {ECO:0000244|PDB:5LBN}.
TURN 90 93 {ECO:0000244|PDB:5LBN}.
STRAND 95 101 {ECO:0000244|PDB:5LBN}.
TURN 104 107 {ECO:0000244|PDB:5LBN}.
STRAND 112 117 {ECO:0000244|PDB:5LBN}.
HELIX 133 135 {ECO:0000244|PDB:5LBN}.
TURN 136 138 {ECO:0000244|PDB:3BZH}.
HELIX 145 157 {ECO:0000244|PDB:5LBN}.
HELIX 167 175 {ECO:0000244|PDB:5LBN}.
HELIX 177 191 {ECO:0000244|PDB:5LBN}.
SEQUENCE 193 AA; 21404 MW; 2FBC50BE2A6A0008 CRC64;
MSDDDSRAST SSSSSSSSNQ QTEKETNTPK KKESKVSMSK NSKLLSTSAK RIQKELADIT
LDPPPNCSAG PKGDNIYEWR STILGPPGSV YEGGVFFLDI TFTPEYPFKP PKVTFRTRIY
HCNINSQGVI CLDILKDNWS PALTISKVLL SICSLLTDCN PADPLVGSIA TQYMTNRAEH
DRMARQWTKR YAT


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EIAAB44901 Homo sapiens,Human,KIAA1734,UBE2O,Ubiquitin carrier protein O,Ubiquitin-conjugating enzyme E2 O,Ubiquitin-conjugating enzyme E2 of 230 kDa,Ubiquitin-conjugating enzyme E2-230K,Ubiquitin-protein ligase
EIAAB44905 E2epf,Mouse,Mus musculus,Ube2s,Ubiquitin carrier protein S,Ubiquitin-conjugating enzyme E2 S,Ubiquitin-conjugating enzyme E2-24 kDa,Ubiquitin-conjugating enzyme E2-EPF5,Ubiquitin-protein ligase S
EIAAB44902 Kiaa1734,Mouse,Mus musculus,Ube2o,Ubiquitin carrier protein O,Ubiquitin-conjugating enzyme E2 O,Ubiquitin-conjugating enzyme E2 of 230 kDa,Ubiquitin-conjugating enzyme E2-230K,Ubiquitin-protein ligase
EIAAB44903 E2EPF,E2-EPF,Homo sapiens,Human,OK_SW-cl.73,UBE2S,Ubiquitin carrier protein S,Ubiquitin-conjugating enzyme E2 S,Ubiquitin-conjugating enzyme E2-24 kDa,Ubiquitin-conjugating enzyme E2-EPF5,Ubiquitin-pr
EIAAB44789 Homo sapiens,Human,UBC5C,UBCH5C,UBE2D3,Ubiquitin carrier protein D3,Ubiquitin-conjugating enzyme E2 D3,Ubiquitin-conjugating enzyme E2(17)KB 3,Ubiquitin-conjugating enzyme E2-17 kDa 3,Ubiquitin-protei
EIAAB44783 Mouse,Mus musculus,Ubc4,Ubch4,Ubch5b,Ube2d2,Ubiquitin carrier protein D2,Ubiquitin-conjugating enzyme E2 D2,Ubiquitin-conjugating enzyme E2(17)KB 2,Ubiquitin-conjugating enzyme E2-17 kDa 2,Ubiquitin-p
EIAAB44784 Homo sapiens,Human,UBC4,UBC5B,UBCH4,UBCH5B,UBE2D2,Ubiquitin carrier protein D2,Ubiquitin-conjugating enzyme E2 D2,Ubiquitin-conjugating enzyme E2(17)KB 2,Ubiquitin-conjugating enzyme E2-17 kDa 2,Ubiqu
EIAAB44752 Rat,Rattus norvegicus,Ube2d2,Ube2d2b,Ubiquitin carrier protein D2B,Ubiquitin-conjugating enzyme E2 D2B,Ubiquitin-conjugating enzyme E2(17)KB 2B,Ubiquitin-conjugating enzyme E2-17 kDa 2B,Ubiquitin-prot
EIAAB44782 Rat,Rattus norvegicus,Ubc4,Ubch4,Ubch5b,Ube2d2,Ubiquitin carrier protein D2,Ubiquitin-conjugating enzyme E2 D2,Ubiquitin-conjugating enzyme E2(17)KB 2,Ubiquitin-conjugating enzyme E2-17 kDa 2,Ubiquiti
EIAAB44779 Rat,Rattus norvegicus,Ube2d1,Ubiquitin carrier protein D1,Ubiquitin-conjugating enzyme E2 D1,Ubiquitin-conjugating enzyme E2(17)KB 1,Ubiquitin-conjugating enzyme E2-17 kDa 1,Ubiquitin-protein ligase D
EIAAB44778 Mouse,Mus musculus,Ube2d1,Ubiquitin carrier protein D1,Ubiquitin-conjugating enzyme E2 D1,Ubiquitin-conjugating enzyme E2(17)KB 1,Ubiquitin-conjugating enzyme E2-17 kDa 1,Ubiquitin-protein ligase D1
EIAAB44788 Mouse,Mus musculus,Ube2d3,Ubiquitin carrier protein D3,Ubiquitin-conjugating enzyme E2 D3,Ubiquitin-conjugating enzyme E2(17)KB 3,Ubiquitin-conjugating enzyme E2-17 kDa 3,Ubiquitin-protein ligase D3
EIAAB44786 PAPase,Phosphoarginine phosphatase,Rat,Rattus norvegicus,Ube2d3,Ubiquitin carrier protein D3,Ubiquitin-conjugating enzyme E2 D3,Ubiquitin-conjugating enzyme E2(17)KB 3,Ubiquitin-conjugating enzyme E2-
U1063h CLIA hHR6B,Homo sapiens,HR6B,Human,RAD6 homolog B,RAD6B,UBE2B,Ubiquitin carrier protein B,Ubiquitin-conjugating enzyme E2 B,Ubiquitin-conjugating enzyme E2-17 kDa,Ubiquitin-protein ligase B 96T
E1063h ELISA kit hHR6B,Homo sapiens,HR6B,Human,RAD6 homolog B,RAD6B,UBE2B,Ubiquitin carrier protein B,Ubiquitin-conjugating enzyme E2 B,Ubiquitin-conjugating enzyme E2-17 kDa,Ubiquitin-protein ligase B 96T
E1063h ELISA hHR6B,Homo sapiens,HR6B,Human,RAD6 homolog B,RAD6B,UBE2B,Ubiquitin carrier protein B,Ubiquitin-conjugating enzyme E2 B,Ubiquitin-conjugating enzyme E2-17 kDa,Ubiquitin-protein ligase B 96T
E1063Rb ELISA HR6B,Oryctolagus cuniculus,Rabbit,RAD6 homolog B,RAD6B,UBE2B,Ubiquitin carrier protein B,Ubiquitin-conjugating enzyme E2 B,Ubiquitin-conjugating enzyme E2(14k),Ubiquitin-protein ligase B 96T
E1063Rb ELISA kit HR6B,Oryctolagus cuniculus,Rabbit,RAD6 homolog B,RAD6B,UBE2B,Ubiquitin carrier protein B,Ubiquitin-conjugating enzyme E2 B,Ubiquitin-conjugating enzyme E2(14k),Ubiquitin-protein ligase B 96T
U1063Rb CLIA HR6B,Oryctolagus cuniculus,Rabbit,RAD6 homolog B,RAD6B,UBE2B,Ubiquitin carrier protein B,Ubiquitin-conjugating enzyme E2 B,Ubiquitin-conjugating enzyme E2(14k),Ubiquitin-protein ligase B 96T
EIAAB44895 HIP2,HIP-2,Homo sapiens,Human,Huntingtin-interacting protein 2,LIG,UBE2K,Ubiquitin carrier protein,Ubiquitin-conjugating enzyme E2 K,Ubiquitin-conjugating enzyme E2(25K),Ubiquitin-conjugating enzyme E
U1063r CLIA HR6B,RAD6 homolog B,Rad6b,Rat,Rattus norvegicus,Ube2b,Ubiquitin carrier protein B,Ubiquitin-conjugating enzyme E2 B,Ubiquitin-conjugating enzyme E2(14k),Ubiquitin-protein ligase B 96T
E1063r ELISA kit HR6B,RAD6 homolog B,Rad6b,Rat,Rattus norvegicus,Ube2b,Ubiquitin carrier protein B,Ubiquitin-conjugating enzyme E2 B,Ubiquitin-conjugating enzyme E2(14k),Ubiquitin-protein ligase B 96T
E1063r ELISA HR6B,RAD6 homolog B,Rad6b,Rat,Rattus norvegicus,Ube2b,Ubiquitin carrier protein B,Ubiquitin-conjugating enzyme E2 B,Ubiquitin-conjugating enzyme E2(14k),Ubiquitin-protein ligase B 96T
EIAAB44898 Bendless-like ubiquitin-conjugating enzyme,BLU,Homo sapiens,Human,Ubc13,UBE2N,Ubiquitin carrier protein N,Ubiquitin-conjugating enzyme E2 N,Ubiquitin-protein ligase N
EIAAB44896 Hip2,HIP-2,Huntingtin-interacting protein 2,Mouse,Mus musculus,Ube2k,Ubiquitin carrier protein,Ubiquitin-conjugating enzyme E2 K,Ubiquitin-conjugating enzyme E2(25K),Ubiquitin-conjugating enzyme E2-25


 

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