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E3 ubiquitin-protein ligase CBL-C (EC 2.3.2.27) (RING finger protein 57) (RING-type E3 ubiquitin transferase CBL-C) (SH3-binding protein CBL-3) (SH3-binding protein CBL-C) (Signal transduction protein CBL-C)

 CBLC_HUMAN              Reviewed;         474 AA.
Q9ULV8; Q8N1E5; Q9Y5Z2; Q9Y5Z3;
01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
06-FEB-2007, sequence version 3.
25-OCT-2017, entry version 169.
RecName: Full=E3 ubiquitin-protein ligase CBL-C;
EC=2.3.2.27 {ECO:0000269|PubMed:14661060, ECO:0000269|PubMed:20525694, ECO:0000269|PubMed:23145173};
AltName: Full=RING finger protein 57;
AltName: Full=RING-type E3 ubiquitin transferase CBL-C {ECO:0000305};
AltName: Full=SH3-binding protein CBL-3;
AltName: Full=SH3-binding protein CBL-C;
AltName: Full=Signal transduction protein CBL-C;
Name=CBLC; Synonyms=CBL3, RNF57;
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), AND VARIANT TYR-405.
PubMed=10571044; DOI=10.1016/S0378-1119(99)00356-X;
Kim M., Tezuka T., Suzuki Y., Sugano S., Hirai M., Yamamoto T.;
"Molecular cloning and characterization of a novel cbl-family gene,
cbl-c.";
Gene 239:145-154(1999).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), VARIANT TYR-405,
FUNCTION AS EGF SIGNALING NEGATIVE REGULATOR, PHOSPHORYLATION BY EGFR
(ISOFORM 1), TISSUE SPECIFICITY, AND INTERACTION WITH CRK AND LYN.
TISSUE=Pancreatic adenocarcinoma;
PubMed=10362357; DOI=10.1038/sj.onc.1202753;
Keane M.M., Ettenberg S.A., Nau M.M., Banerjee P., Cuello M.,
Penninger J., Lipkowitz S.;
"cbl-3: a new mammalian cbl family protein.";
Oncogene 18:3365-3375(1999).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Skin;
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).
[4]
FUNCTION AS E3 UBIQUITIN-PROTEIN LIGASE, CATALYTIC ACTIVITY,
INTERACTION WITH SRC, AUTOUBIQUITINATION, AND MUTAGENESIS OF GLY-276;
TYR-341 AND CYS-351.
PubMed=14661060; DOI=10.1038/sj.onc.1207298;
Kim M., Tezuka T., Tanaka K., Yamamoto T.;
"Cbl-c suppresses v-Src-induced transformation through ubiquitin-
dependent protein degradation.";
Oncogene 23:1645-1655(2004).
[5]
FUNCTION IN RET STABILITY, INTERACTION WITH RET, AND MUTAGENESIS OF
GLY-276 AND CYS-351.
PubMed=18753381; DOI=10.1523/JNEUROSCI.2738-08.2008;
Tsui C.C., Pierchala B.A.;
"CD2AP and Cbl-3/Cbl-c constitute a critical checkpoint in the
regulation of ret signal transduction.";
J. Neurosci. 28:8789-8800(2008).
[6]
FUNCTION, CATALYTIC ACTIVITY, ENZYME REGULATION, DOMAIN, INTERACTION
WITH UBE2D2 AND UBE2D3, PHOSPHORYLATION AT TYR-341, AND MUTAGENESIS OF
TYR-341.
PubMed=20525694; DOI=10.1074/jbc.M109.091157;
Ryan P.E., Sivadasan-Nair N., Nau M.M., Nicholas S., Lipkowitz S.;
"The N terminus of Cbl-c regulates ubiquitin ligase activity by
modulating affinity for the ubiquitin-conjugating enzyme.";
J. Biol. Chem. 285:23687-23698(2010).
[7]
FUNCTION, CATALYTIC ACTIVITY, AUTOUBIQUITINATION, PHOSPHORYLATION AT
TYR-341, INTERACTION WITH TGFB1I1, AND MUTAGENESIS OF TYR-341; CYS-351
AND CYS-366.
PubMed=23145173; DOI=10.1371/journal.pone.0049428;
Ryan P.E., Kales S.C., Yadavalli R., Nau M.M., Zhang H., Lipkowitz S.;
"Cbl-c ubiquitin ligase activity is increased via the interaction of
its RING finger domain with a LIM domain of the paxillin homolog, Hic
5.";
PLoS ONE 7:E49428-E49428(2012).
[8]
X-RAY CRYSTALLOGRAPHY (2.52 ANGSTROMS) OF 9-323 IN COMPLEX WITH EGFR
PEPTIDE.
Structural genomics consortium (SGC);
"Crystal structure of Cbl-c (Cbl-3) TKB domain in complex with EGFR
py1069 peptide.";
Submitted (OCT-2010) to the PDB data bank.
[9]
X-RAY CRYSTALLOGRAPHY (1.52 ANGSTROMS) OF 1-323 IN COMPLEX WITH
CALCIUM; SRC AND EGFR PEPTIDES, CALCIUM-BINDING, INTERACTION WITH EGFR
AND SRC, AND MUTAGENESIS OF TYR-244; ARG-264; PRO-265; SER-266;
THR-268 AND GLY-276.
PubMed=22888118; DOI=10.1093/jb/mvs085;
Takeshita K., Tezuka T., Isozaki Y., Yamashita E., Suzuki M., Kim M.,
Yamanashi Y., Yamamoto T., Nakagawa A.;
"Structural flexibility regulates phosphopeptide-binding activity of
the tyrosine kinase binding domain of Cbl-c.";
J. Biochem. 152:487-495(2012).
-!- FUNCTION: Acts as an E3 ubiquitin-protein ligase, which accepts
ubiquitin from specific E2 ubiquitin-conjugating enzymes, and then
transfers it to substrates promoting their degradation by the
proteasome. Functionally coupled with the E2 ubiquitin-protein
ligases UB2D1, UB2D2 and UB2D3. Regulator of EGFR mediated signal
transduction; upon EGF activation, ubiquitinates EGFR. Isoform 1,
but not isoform 2, inhibits EGF stimulated MAPK1 activation.
Promotes ubiquitination of SRC phosphorylated at 'Tyr-419'. In
collaboration with CD2AP may act as regulatory checkpoint for Ret
signaling by modulating the rate of RET degradation after ligand
activation; CD2AP converts it from an inhibitor to a promoter of
RET degradation; the function limits the potency of GDNF on
neuronal survival. {ECO:0000269|PubMed:10362357,
ECO:0000269|PubMed:14661060, ECO:0000269|PubMed:18753381,
ECO:0000269|PubMed:20525694, ECO:0000269|PubMed:23145173}.
-!- 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. {ECO:0000269|PubMed:14661060,
ECO:0000269|PubMed:20525694, ECO:0000269|PubMed:23145173}.
-!- ENZYME REGULATION: Phosphorylation at Tyr-341 is necessary and
sufficient for the activation of E3 activity.
{ECO:0000269|PubMed:20525694}.
-!- SUBUNIT: Interacts with ubiquitin-conjugating enzyme E2 UBE2D2 and
UBE2D3. Isoform 1 interacts with EGFR (tyrosine phosphorylated).
Interacts with the SH3 domain proteins LYN and CRK. Interacts (via
RING-type zinc finger) with TGFB1I1 (via LIM zinc-binding domain
2); the interaction is direct and enhances the E3 activity.
Interacts directly with RET (inactive) and CD2AP; dissociates from
RET upon RET activation by GDNF which also increases the
interaction with CD2AP suggesting dissociation as CBLC:CD2AP
complex. Interacts with SRC; the interaction is enhanced when SRC
is phosphorylated at 'Tyr-419'. {ECO:0000269|PubMed:10362357,
ECO:0000269|PubMed:14661060, ECO:0000269|PubMed:18753381,
ECO:0000269|PubMed:20525694, ECO:0000269|PubMed:22888118,
ECO:0000269|PubMed:23145173, ECO:0000269|Ref.8}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1; Synonyms=Long;
IsoId=Q9ULV8-1; Sequence=Displayed;
Name=2; Synonyms=Short;
IsoId=Q9ULV8-2; Sequence=VSP_005732;
-!- TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:10362357}.
-!- DOMAIN: EF-hand-like and Sh2-like domains are required for N-
terminal inhibition of E3 activity. {ECO:0000269|PubMed:20525694}.
-!- DOMAIN: The N-terminus is composed of the phosphotyrosine binding
(PTB) domain, a short linker region and the RING-type zinc finger.
The PTB domain, which is also called TKB (tyrosine kinase binding)
domain, is composed of three different subdomains: a four-helix
bundle (4H), a calcium-binding EF hand and a divergent SH2 domain.
{ECO:0000255|PROSITE-ProRule:PRU00839,
ECO:0000269|PubMed:20525694}.
-!- DOMAIN: The RING-type zinc finger domain mediates binding to an E2
ubiquitin-conjugating enzyme. {ECO:0000250}.
-!- PTM: Phosphorylated on multiple tyrosine residues by SRC. Isoform
1, but not isoform 2, is phosphorylated on tyrosines by EGFR.
-!- PTM: Autoubiquitinated when phosphorylated at Tyr-341, enhanced by
SRC; suggesting proteasomal degradation.
{ECO:0000269|PubMed:14661060, ECO:0000269|PubMed:20525694,
ECO:0000269|PubMed:23145173}.
-!- MISCELLANEOUS: This protein has one functional calcium-binding
site.
-!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
and Haematology;
URL="http://atlasgeneticsoncology.org/Genes/CBLcID194.html";
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EMBL; AB028645; BAA86298.1; -; mRNA.
EMBL; AF117646; AAD34341.1; -; mRNA.
EMBL; AF117647; AAD34342.1; -; mRNA.
EMBL; BC028915; AAH28915.1; -; mRNA.
CCDS; CCDS12643.1; -. [Q9ULV8-1]
CCDS; CCDS46109.1; -. [Q9ULV8-2]
RefSeq; NP_001124324.1; NM_001130852.1. [Q9ULV8-2]
RefSeq; NP_036248.3; NM_012116.3. [Q9ULV8-1]
UniGene; Hs.466907; -.
PDB; 3OP0; X-ray; 2.52 A; A/B=9-323.
PDB; 3VRN; X-ray; 1.64 A; A=1-323.
PDB; 3VRO; X-ray; 1.80 A; A=1-323.
PDB; 3VRP; X-ray; 1.52 A; A=1-323.
PDB; 3VRQ; X-ray; 2.39 A; A/B=1-323.
PDB; 3VRR; X-ray; 2.00 A; A=1-323.
PDBsum; 3OP0; -.
PDBsum; 3VRN; -.
PDBsum; 3VRO; -.
PDBsum; 3VRP; -.
PDBsum; 3VRQ; -.
PDBsum; 3VRR; -.
ProteinModelPortal; Q9ULV8; -.
SMR; Q9ULV8; -.
BioGrid; 117156; 46.
IntAct; Q9ULV8; 20.
MINT; MINT-247027; -.
STRING; 9606.ENSP00000270279; -.
iPTMnet; Q9ULV8; -.
PhosphoSitePlus; Q9ULV8; -.
BioMuta; CBLC; -.
DMDM; 125987803; -.
EPD; Q9ULV8; -.
PaxDb; Q9ULV8; -.
PeptideAtlas; Q9ULV8; -.
PRIDE; Q9ULV8; -.
DNASU; 23624; -.
Ensembl; ENST00000270279; ENSP00000270279; ENSG00000142273. [Q9ULV8-1]
Ensembl; ENST00000341505; ENSP00000340250; ENSG00000142273. [Q9ULV8-2]
GeneID; 23624; -.
KEGG; hsa:23624; -.
UCSC; uc002ozs.4; human. [Q9ULV8-1]
CTD; 23624; -.
DisGeNET; 23624; -.
EuPathDB; HostDB:ENSG00000142273.10; -.
GeneCards; CBLC; -.
H-InvDB; HIX0202847; -.
HGNC; HGNC:15961; CBLC.
HPA; CAB008087; -.
HPA; HPA035266; -.
MIM; 608453; gene.
neXtProt; NX_Q9ULV8; -.
OpenTargets; ENSG00000142273; -.
PharmGKB; PA26117; -.
eggNOG; KOG1785; Eukaryota.
eggNOG; ENOG410YDNH; LUCA.
GeneTree; ENSGT00390000011617; -.
HOGENOM; HOG000294176; -.
HOVERGEN; HBG005255; -.
InParanoid; Q9ULV8; -.
KO; K04707; -.
OMA; WQHSDSQ; -.
OrthoDB; EOG091G06R9; -.
PhylomeDB; Q9ULV8; -.
TreeFam; TF314210; -.
SignaLink; Q9ULV8; -.
SIGNOR; Q9ULV8; -.
GeneWiki; CBLC; -.
GenomeRNAi; 23624; -.
PRO; PR:Q9ULV8; -.
Proteomes; UP000005640; Chromosome 19.
Bgee; ENSG00000142273; -.
CleanEx; HS_CBLC; -.
Genevisible; Q9ULV8; HS.
GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
GO; GO:0045121; C:membrane raft; IBA:GO_Central.
GO; GO:0005634; C:nucleus; IEA:InterPro.
GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
GO; GO:0005154; F:epidermal growth factor receptor binding; IDA:BHF-UCL.
GO; GO:0001784; F:phosphotyrosine residue binding; IDA:BHF-UCL.
GO; GO:0030971; F:receptor tyrosine kinase binding; IBA:GO_Central.
GO; GO:0017124; F:SH3 domain binding; IDA:BHF-UCL.
GO; GO:0004871; F:signal transducer activity; IEA:InterPro.
GO; GO:0061630; F:ubiquitin protein ligase activity; IDA:BHF-UCL.
GO; GO:0008270; F:zinc ion binding; TAS:ProtInc.
GO; GO:0007166; P:cell surface receptor signaling pathway; IEA:InterPro.
GO; GO:0042059; P:negative regulation of epidermal growth factor receptor signaling pathway; IDA:BHF-UCL.
GO; GO:0007175; P:negative regulation of epidermal growth factor-activated receptor activity; IDA:BHF-UCL.
GO; GO:0043407; P:negative regulation of MAP kinase activity; IDA:BHF-UCL.
GO; GO:0016567; P:protein ubiquitination; IDA:BHF-UCL.
GO; GO:0042787; P:protein ubiquitination involved in ubiquitin-dependent protein catabolic process; IDA:BHF-UCL.
CDD; cd09920; SH2_Cbl-b_TKB; 1.
Gene3D; 1.20.930.20; -; 1.
Gene3D; 3.30.40.10; -; 1.
Gene3D; 3.30.505.10; -; 1.
InterPro; IPR024162; Adaptor_Cbl.
InterPro; IPR014741; Adaptor_Cbl_EF_hand-like.
InterPro; IPR036537; Adaptor_Cbl_N_dom_sf.
InterPro; IPR003153; Adaptor_Cbl_N_hlx.
InterPro; IPR014742; Adaptor_Cbl_SH2-like.
InterPro; IPR024159; Cbl_PTB.
InterPro; IPR011992; EF-hand-dom_pair.
InterPro; IPR036860; SH2_dom_sf.
InterPro; IPR001841; Znf_RING.
InterPro; IPR013083; Znf_RING/FYVE/PHD.
InterPro; IPR017907; Znf_RING_CS.
PANTHER; PTHR23007; PTHR23007; 1.
Pfam; PF02262; Cbl_N; 1.
Pfam; PF02761; Cbl_N2; 1.
Pfam; PF02762; Cbl_N3; 1.
SMART; SM00184; RING; 1.
SUPFAM; SSF47473; SSF47473; 1.
SUPFAM; SSF47668; SSF47668; 1.
SUPFAM; SSF55550; SSF55550; 1.
PROSITE; PS51506; CBL_PTB; 1.
PROSITE; PS00518; ZF_RING_1; 1.
PROSITE; PS50089; ZF_RING_2; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; Calcium; Complete proteome;
Metal-binding; Phosphoprotein; Polymorphism; Reference proteome;
Repeat; SH3-binding; Transferase; Ubl conjugation;
Ubl conjugation pathway; Zinc; Zinc-finger.
CHAIN 1 474 E3 ubiquitin-protein ligase CBL-C.
/FTId=PRO_0000055866.
DOMAIN 7 321 Cbl-PTB. {ECO:0000255|PROSITE-
ProRule:PRU00839}.
CA_BIND 199 210
ZN_FING 351 390 RING-type. {ECO:0000255|PROSITE-
ProRule:PRU00175}.
REGION 7 145 4H.
REGION 146 218 EF-hand-like.
REGION 219 321 SH2-like.
REGION 322 350 Linker.
REGION 351 474 Interaction with RET.
{ECO:0000269|PubMed:18753381}.
BINDING 264 264 Phosphotyrosine.
MOD_RES 341 341 Phosphotyrosine; by SRC.
{ECO:0000269|PubMed:20525694,
ECO:0000269|PubMed:23145173}.
VAR_SEQ 261 306 Missing (in isoform 2).
{ECO:0000303|PubMed:10362357}.
/FTId=VSP_005732.
VARIANT 405 405 H -> Y (in dbSNP:rs3208856).
{ECO:0000269|PubMed:10362357,
ECO:0000269|PubMed:10571044}.
/FTId=VAR_018298.
MUTAGEN 244 244 Y->A: Abolishes interaction with EGFR.
Decreases interaction with SRC and
abolishes SRC ubiquitination.
{ECO:0000269|PubMed:22888118}.
MUTAGEN 244 244 Y->F: No effect on interaction with EGFR
and SRC as well as on SRC ubiquitination.
{ECO:0000269|PubMed:22888118}.
MUTAGEN 264 264 R->A: Abolishes interaction with EGFR.
Decreases interaction with SRC and
abolishes SRC ubiquitination.
{ECO:0000269|PubMed:22888118}.
MUTAGEN 265 265 P->L: Enhances interaction with EGFR and
SRC as well as SRC ubiquitination.
{ECO:0000269|PubMed:22888118}.
MUTAGEN 266 266 S->A: Decreases interactions with EGFR
and SRC as well as SRC ubiquitination.
{ECO:0000269|PubMed:22888118}.
MUTAGEN 268 268 T->A: Abolishes interaction with EGFR.
Decreases interaction with and
ubiquitination of SRC.
{ECO:0000269|PubMed:22888118}.
MUTAGEN 276 276 G->E: No effect on interaction with RET.
Binds slightly to SRC, this interaction
is independent of SRC phosphorylation.
Strongly decreases SRC ubiquitination.
Abolishes interaction with EGFR.
{ECO:0000269|PubMed:14661060,
ECO:0000269|PubMed:18753381,
ECO:0000269|PubMed:22888118}.
MUTAGEN 341 341 Y->E: Induces E3 activity and
autoubiquitination. Releases ubiquitin-
conjugating enzyme E2 UBE2D2 faster.
{ECO:0000269|PubMed:14661060,
ECO:0000269|PubMed:20525694,
ECO:0000269|PubMed:23145173}.
MUTAGEN 341 341 Y->F: Abolishes activation by EGF
stimulation and enhancement by TGFB1I1 of
E3 activity.
{ECO:0000269|PubMed:14661060,
ECO:0000269|PubMed:20525694,
ECO:0000269|PubMed:23145173}.
MUTAGEN 341 341 Missing: Abolishes E3 activity.
{ECO:0000269|PubMed:14661060,
ECO:0000269|PubMed:20525694,
ECO:0000269|PubMed:23145173}.
MUTAGEN 351 351 C->A: No effect on TGFB1I1 and SRC
interactions. Abolishes SRC
ubiquitination. Abolishes interaction
with TGFB1I1; when associated with A-366.
Abolishes interaction with RET and
inhibition of RET degradation.
{ECO:0000269|PubMed:14661060,
ECO:0000269|PubMed:18753381,
ECO:0000269|PubMed:23145173}.
MUTAGEN 366 366 C->A: Abolishes interaction with TGFB1I1.
Abolishes interaction with TGFB1I1; when
associated with A-351.
{ECO:0000269|PubMed:23145173}.
CONFLICT 234 234 N -> T (in Ref. 1; BAA86298).
{ECO:0000305}.
CONFLICT 413 413 S -> P (in Ref. 3; AAH28915).
{ECO:0000305}.
HELIX 13 31 {ECO:0000244|PDB:3VRP}.
STRAND 40 42 {ECO:0000244|PDB:3OP0}.
HELIX 44 62 {ECO:0000244|PDB:3VRP}.
STRAND 64 66 {ECO:0000244|PDB:3VRP}.
HELIX 76 97 {ECO:0000244|PDB:3VRP}.
STRAND 100 102 {ECO:0000244|PDB:3OP0}.
HELIX 108 111 {ECO:0000244|PDB:3OP0}.
HELIX 116 138 {ECO:0000244|PDB:3VRP}.
HELIX 140 142 {ECO:0000244|PDB:3VRP}.
TURN 146 148 {ECO:0000244|PDB:3VRP}.
HELIX 154 164 {ECO:0000244|PDB:3VRP}.
STRAND 168 171 {ECO:0000244|PDB:3VRP}.
HELIX 172 179 {ECO:0000244|PDB:3VRP}.
TURN 180 182 {ECO:0000244|PDB:3VRP}.
HELIX 189 198 {ECO:0000244|PDB:3VRP}.
STRAND 203 207 {ECO:0000244|PDB:3VRP}.
HELIX 208 217 {ECO:0000244|PDB:3VRP}.
HELIX 221 223 {ECO:0000244|PDB:3VRP}.
HELIX 224 232 {ECO:0000244|PDB:3VRP}.
STRAND 238 241 {ECO:0000244|PDB:3VRQ}.
HELIX 244 251 {ECO:0000244|PDB:3VRP}.
HELIX 252 254 {ECO:0000244|PDB:3VRP}.
STRAND 260 265 {ECO:0000244|PDB:3VRP}.
STRAND 267 269 {ECO:0000244|PDB:3VRP}.
STRAND 273 278 {ECO:0000244|PDB:3VRP}.
STRAND 284 287 {ECO:0000244|PDB:3VRP}.
HELIX 294 303 {ECO:0000244|PDB:3VRP}.
HELIX 320 323 {ECO:0000244|PDB:3OP0}.
SEQUENCE 474 AA; 52456 MW; 202634AEDE434544 CRC64;
MALAVAPWGR QWEEARALGR AVRMLQRLEE QCVDPRLSVS PPSLRDLLPR TAQLLREVAH
SRRAAGGGGP GGPGGSGDFL LIYLANLEAK SRQVAALLPP RGRRSANDEL FRAGSRLRRQ
LAKLAIIFSH MHAELHALFP GGKYCGHMYQ LTKAPAHTFW RESCGARCVL PWAEFESLLG
TCHPVEPGCT ALALRTTIDL TCSGHVSIFE FDVFTRLFQP WPTLLKNWQL LAVNHPGYMA
FLTYDEVQER LQACRDKPGS YIFRPSCTRL GQWAIGYVSS DGSILQTIPA NKPLSQVLLE
GQKDGFYLYP DGKTHNPDLT ELGQAEPQQR IHVSEEQLQL YWAMDSTFEL CKICAESNKD
VKIEPCGHLL CSCCLAAWQH SDSQTCPFCR CEIKGWEAVS IYQFHGQATA EDSGNSSDQE
GRELELGQVP LSAPPLPPRP DLPPRKPRNA QPKVRLLKGN SPPAALGPQD PAPA


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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
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
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
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
EIAAB05542 CBL3,CBLC,Homo sapiens,Human,RING finger protein 57,RNF57,SH3-binding protein CBL-3,SH3-binding protein CBL-C,Signal transduction protein CBL-C
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
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
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
EIAAB05536 Casitas B-lineage lymphoma proto-oncogene,CBL,CBL2,E3 ubiquitin-protein ligase CBL,Homo sapiens,Human,Proto-oncogene c-Cbl,RING finger protein 55,RNF55,Signal transduction protein CBL
EIAAB45295 E3 ubiquitin-protein ligase UHRF1,Homo sapiens,Human,HuNp95,ICBP90,Inverted CCAAT box-binding protein of 90 kDa,NP95,Nuclear protein 95,Nuclear zinc finger protein Np95,RING finger protein 106,RNF106,
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
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
EIAAB43866 ADP-ribosylation factor domain-containing protein 1,ARD1,ARFD1,E3 ubiquitin-protein ligase TRIM23,GTP-binding protein ARD-1,Homo sapiens,Human,RING finger protein 46,RNF46,TRIM23,Tripartite motif-cont


 

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