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Sequence of CBLC_HUMAN

EC Number:2.3.2.27

EC Number
Recommended Name
Accession Code
Organism
No of amino acids
Molecular Weight [Da]
Source
RING-type E3 ubiquitin transferase
Q9ULV8
Homo sapiens
474
52456
Reaction
[E2 ubiquitin-conjugating enzyme]-S-ubiquitinyl-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-N6-ubiquitinyl-L-lysine
Other sequences found for EC No. 2.3.2.27

General information:

Sequence
show sequence in fasta format
  0 MALAVAPWGR QWEEARALGR AVRMLQRLEE QCVDPRLSVS PPSLRDLLPR TAQLLREVAH
 60 SRRAAGGGGP GGPGGSGDFL LIYLANLEAK SRQVAALLPP RGRRSANDEL FRAGSRLRRQ
120 LAKLAIIFSH MHAELHALFP GGKYCGHMYQ LTKAPAHTFW RESCGARCVL PWAEFESLLG
180 TCHPVEPGCT ALALRTTIDL TCSGHVSIFE FDVFTRLFQP WPTLLKNWQL LAVNHPGYMA
240 FLTYDEVQER LQACRDKPGS YIFRPSCTRL GQWAIGYVSS DGSILQTIPA NKPLSQVLLE
300 GQKDGFYLYP DGKTHNPDLT ELGQAEPQQR IHVSEEQLQL YWAMDSTFEL CKICAESNKD
360 VKIEPCGHLL CSCCLAAWQH SDSQTCPFCR CEIKGWEAVS IYQFHGQATA EDSGNSSDQE
420 GRELELGQVP LSAPPLPPRP DLPPRKPRNA QPKVRLLKGN SPPAALGPQD PAPA
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Sequence related references
Sequence Reference
Authors
Title
Journal
Volume
Pages
Year
PubMed ID
777798
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
777799
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
777800
The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).
Genome Res.
14
2121-2127
2004
777801
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
777802
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
777803
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
777804
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
0-0
2012
777806
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