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Q9ULV8

- CBLC_HUMAN

UniProt

Q9ULV8 - CBLC_HUMAN

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Protein

E3 ubiquitin-protein ligase CBL-C

Gene

CBLC

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

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.5 Publications

Enzyme regulationi

Phosphorylation at Tyr-341 is necessary and sufficient for the activation of E3 activity.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei264 – 2641Phosphotyrosine

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Calcium bindingi199 – 21012Add
BLAST
Zinc fingeri351 – 39040RING-typePROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

  1. calcium ion binding Source: InterPro
  2. epidermal growth factor receptor binding Source: BHF-UCL
  3. ligase activity Source: UniProtKB-KW
  4. phosphotyrosine binding Source: BHF-UCL
  5. SH3 domain binding Source: BHF-UCL
  6. signal transducer activity Source: InterPro
  7. ubiquitin-protein transferase activity Source: BHF-UCL
  8. zinc ion binding Source: ProtInc

GO - Biological processi

  1. cell surface receptor signaling pathway Source: InterPro
  2. negative regulation of epidermal growth factor-activated receptor activity Source: BHF-UCL
  3. negative regulation of epidermal growth factor receptor signaling pathway Source: BHF-UCL
  4. negative regulation of MAP kinase activity Source: BHF-UCL
  5. protein ubiquitination involved in ubiquitin-dependent protein catabolic process Source: BHF-UCL
Complete GO annotation...

Keywords - Molecular functioni

Ligase

Keywords - Biological processi

Ubl conjugation pathway

Keywords - Ligandi

Calcium, Metal-binding, Zinc

Enzyme and pathway databases

SignaLinkiQ9ULV8.

Names & Taxonomyi

Protein namesi
Recommended name:
E3 ubiquitin-protein ligase CBL-C (EC:6.3.2.-)
Alternative name(s):
RING finger protein 57
SH3-binding protein CBL-3
SH3-binding protein CBL-C
Signal transduction protein CBL-C
Gene namesi
Name:CBLC
Synonyms:CBL3, RNF57
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 19

Organism-specific databases

HGNCiHGNC:15961. CBLC.

Subcellular locationi

GO - Cellular componenti

  1. extracellular vesicular exosome Source: UniProt
  2. nucleus Source: InterPro
Complete GO annotation...

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi244 – 2441Y → A: Abolishes interaction with EGFR. Decreases interaction with SRC and abolishes SRC ubiquitination. 1 Publication
Mutagenesisi244 – 2441Y → F: No effect on interaction with EGFR and SRC as well as on SRC ubiquitination. 1 Publication
Mutagenesisi264 – 2641R → A: Abolishes interaction with EGFR. Decreases interaction with SRC and abolishes SRC ubiquitination. 1 Publication
Mutagenesisi265 – 2651P → L: Enhances interaction with EGFR and SRC as well as SRC ubiquitination. 1 Publication
Mutagenesisi266 – 2661S → A: Decreases interactions with EGFR and SRC as well as SRC ubiquitination. 1 Publication
Mutagenesisi268 – 2681T → A: Abolishes interaction with EGFR. Decreases interaction with and ubiquitination of SRC. 1 Publication
Mutagenesisi276 – 2761G → 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. 3 Publications
Mutagenesisi341 – 3411Y → E: Induces E3 activity and autoubiquitination. Releases ubiquitin-conjugating enzyme E2 UBE2D2 faster. 3 Publications
Mutagenesisi341 – 3411Y → F: Abolishes activation by EGF stimulation and enhancement by TGFB1I1 of E3 activity. 3 Publications
Mutagenesisi341 – 3411Missing: Abolishes E3 activity. 3 Publications
Mutagenesisi351 – 3511C → 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. 3 Publications
Mutagenesisi366 – 3661C → A: Abolishes interaction with TGFB1I1. Abolishes interaction with TGFB1I1; when associated with A-351. 1 Publication

Organism-specific databases

PharmGKBiPA26117.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 474474E3 ubiquitin-protein ligase CBL-CPRO_0000055866Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei341 – 3411Phosphotyrosine; by SRC2 Publications

Post-translational modificationi

Phosphorylated on multiple tyrosine residues by SRC. Isoform 1, but not isoform 2, is phosphorylated on tyrosines by EGFR.
Autoubiquitinated when phosphorylated at Tyr-341, enhanced by SRC; suggesting proteasomal degradation.3 Publications

Keywords - PTMi

Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiQ9ULV8.
PaxDbiQ9ULV8.
PRIDEiQ9ULV8.

PTM databases

PhosphoSiteiQ9ULV8.

Expressioni

Tissue specificityi

Ubiquitous.1 Publication

Gene expression databases

BgeeiQ9ULV8.
CleanExiHS_CBLC.
GenevestigatoriQ9ULV8.

Organism-specific databases

HPAiCAB008087.

Interactioni

Subunit structurei

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'.7 Publications

Protein-protein interaction databases

BioGridi117156. 35 interactions.
IntActiQ9ULV8. 18 interactions.
MINTiMINT-247027.
STRINGi9606.ENSP00000270279.

Structurei

Secondary structure

1
474
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi13 – 3119Combined sources
Beta strandi40 – 423Combined sources
Helixi44 – 6219Combined sources
Beta strandi64 – 663Combined sources
Helixi76 – 9722Combined sources
Beta strandi100 – 1023Combined sources
Helixi108 – 1114Combined sources
Helixi116 – 13823Combined sources
Helixi140 – 1423Combined sources
Turni146 – 1483Combined sources
Helixi154 – 16411Combined sources
Beta strandi168 – 1714Combined sources
Helixi172 – 1798Combined sources
Turni180 – 1823Combined sources
Helixi189 – 19810Combined sources
Beta strandi203 – 2075Combined sources
Helixi208 – 21710Combined sources
Helixi221 – 2233Combined sources
Helixi224 – 2329Combined sources
Beta strandi238 – 2414Combined sources
Helixi244 – 2518Combined sources
Helixi252 – 2543Combined sources
Beta strandi260 – 2656Combined sources
Beta strandi267 – 2693Combined sources
Beta strandi273 – 2786Combined sources
Beta strandi284 – 2874Combined sources
Helixi294 – 30310Combined sources
Helixi320 – 3234Combined sources

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3OP0X-ray2.52A/B9-323[»]
3VRNX-ray1.64A1-323[»]
3VROX-ray1.80A1-323[»]
3VRPX-ray1.52A1-323[»]
3VRQX-ray2.39A/B1-323[»]
3VRRX-ray2.00A1-323[»]
ProteinModelPortaliQ9ULV8.
SMRiQ9ULV8. Positions 10-404.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini7 – 321315Cbl-PTBPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni7 – 1451394HAdd
BLAST
Regioni146 – 21873EF-hand-likeAdd
BLAST
Regioni219 – 321103SH2-likeAdd
BLAST
Regioni322 – 35029LinkerAdd
BLAST
Regioni351 – 474124Interaction with RETAdd
BLAST

Domaini

EF-hand-like and Sh2-like domains are required for N-terminal inhibition of E3 activity.1 Publication
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.1 PublicationPROSITE-ProRule annotation
The RING-type zinc finger domain mediates binding to an E2 ubiquitin-conjugating enzyme.By similarity

Sequence similaritiesi

Contains 1 Cbl-PTB (Cbl-type phosphotyrosine-binding) domain.PROSITE-ProRule annotation
Contains 1 RING-type zinc finger.PROSITE-ProRule annotation

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri351 – 39040RING-typePROSITE-ProRule annotationAdd
BLAST

Keywords - Domaini

Repeat, SH3-binding, Zinc-finger

Phylogenomic databases

eggNOGiNOG318595.
GeneTreeiENSGT00390000011617.
HOGENOMiHOG000294176.
HOVERGENiHBG005255.
InParanoidiQ9ULV8.
KOiK04707.
OMAiWQHSDSQ.
OrthoDBiEOG73BVCF.
PhylomeDBiQ9ULV8.
TreeFamiTF314210.

Family and domain databases

Gene3Di1.10.238.10. 1 hit.
1.20.930.20. 1 hit.
3.30.40.10. 1 hit.
3.30.505.10. 1 hit.
InterProiIPR024162. Adaptor_Cbl.
IPR014741. Adaptor_Cbl_EF_hand-like.
IPR003153. Adaptor_Cbl_N_hlx.
IPR014742. Adaptor_Cbl_SH2-like.
IPR024159. Cbl_PTB.
IPR011992. EF-hand-dom_pair.
IPR000980. SH2.
IPR001841. Znf_RING.
IPR013083. Znf_RING/FYVE/PHD.
IPR017907. Znf_RING_CS.
[Graphical view]
PANTHERiPTHR23007. PTHR23007. 1 hit.
PfamiPF02262. Cbl_N. 1 hit.
PF02761. Cbl_N2. 1 hit.
PF02762. Cbl_N3. 1 hit.
[Graphical view]
SMARTiSM00184. RING. 1 hit.
SM00252. SH2. 1 hit.
[Graphical view]
SUPFAMiSSF47668. SSF47668. 1 hit.
SSF55550. SSF55550. 1 hit.
PROSITEiPS51506. CBL_PTB. 1 hit.
PS00518. ZF_RING_1. 1 hit.
PS50089. ZF_RING_2. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q9ULV8-1) [UniParc]FASTAAdd to Basket

Also known as: Long

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MALAVAPWGR QWEEARALGR AVRMLQRLEE QCVDPRLSVS PPSLRDLLPR
60 70 80 90 100
TAQLLREVAH SRRAAGGGGP GGPGGSGDFL LIYLANLEAK SRQVAALLPP
110 120 130 140 150
RGRRSANDEL FRAGSRLRRQ LAKLAIIFSH MHAELHALFP GGKYCGHMYQ
160 170 180 190 200
LTKAPAHTFW RESCGARCVL PWAEFESLLG TCHPVEPGCT ALALRTTIDL
210 220 230 240 250
TCSGHVSIFE FDVFTRLFQP WPTLLKNWQL LAVNHPGYMA FLTYDEVQER
260 270 280 290 300
LQACRDKPGS YIFRPSCTRL GQWAIGYVSS DGSILQTIPA NKPLSQVLLE
310 320 330 340 350
GQKDGFYLYP DGKTHNPDLT ELGQAEPQQR IHVSEEQLQL YWAMDSTFEL
360 370 380 390 400
CKICAESNKD VKIEPCGHLL CSCCLAAWQH SDSQTCPFCR CEIKGWEAVS
410 420 430 440 450
IYQFHGQATA EDSGNSSDQE GRELELGQVP LSAPPLPPRP DLPPRKPRNA
460 470
QPKVRLLKGN SPPAALGPQD PAPA
Length:474
Mass (Da):52,456
Last modified:February 6, 2007 - v3
Checksum:i202634AEDE434544
GO
Isoform 2 (identifier: Q9ULV8-2) [UniParc]FASTAAdd to Basket

Also known as: Short

The sequence of this isoform differs from the canonical sequence as follows:
     261-306: Missing.

Show »
Length:428
Mass (Da):47,418
Checksum:i7070EDF530032CA0
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti234 – 2341N → T in BAA86298. (PubMed:10571044)Curated
Sequence conflicti413 – 4131S → P in AAH28915. (PubMed:15489334)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti405 – 4051H → Y.2 Publications
Corresponds to variant rs3208856 [ dbSNP | Ensembl ].
VAR_018298

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei261 – 30646Missing in isoform 2. 1 PublicationVSP_005732Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AB028645 mRNA. Translation: BAA86298.1.
AF117646 mRNA. Translation: AAD34341.1.
AF117647 mRNA. Translation: AAD34342.1.
BC028915 mRNA. Translation: AAH28915.1.
CCDSiCCDS12643.1. [Q9ULV8-1]
CCDS46109.1. [Q9ULV8-2]
RefSeqiNP_001124324.1. NM_001130852.1. [Q9ULV8-2]
NP_036248.3. NM_012116.3. [Q9ULV8-1]
UniGeneiHs.466907.

Genome annotation databases

EnsembliENST00000270279; ENSP00000270279; ENSG00000142273. [Q9ULV8-1]
ENST00000341505; ENSP00000340250; ENSG00000142273. [Q9ULV8-2]
GeneIDi23624.
KEGGihsa:23624.
UCSCiuc002ozs.3. human. [Q9ULV8-1]
uc010ejt.3. human. [Q9ULV8-2]

Polymorphism databases

DMDMi125987803.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AB028645 mRNA. Translation: BAA86298.1 .
AF117646 mRNA. Translation: AAD34341.1 .
AF117647 mRNA. Translation: AAD34342.1 .
BC028915 mRNA. Translation: AAH28915.1 .
CCDSi CCDS12643.1. [Q9ULV8-1 ]
CCDS46109.1. [Q9ULV8-2 ]
RefSeqi NP_001124324.1. NM_001130852.1. [Q9ULV8-2 ]
NP_036248.3. NM_012116.3. [Q9ULV8-1 ]
UniGenei Hs.466907.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
3OP0 X-ray 2.52 A/B 9-323 [» ]
3VRN X-ray 1.64 A 1-323 [» ]
3VRO X-ray 1.80 A 1-323 [» ]
3VRP X-ray 1.52 A 1-323 [» ]
3VRQ X-ray 2.39 A/B 1-323 [» ]
3VRR X-ray 2.00 A 1-323 [» ]
ProteinModelPortali Q9ULV8.
SMRi Q9ULV8. Positions 10-404.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 117156. 35 interactions.
IntActi Q9ULV8. 18 interactions.
MINTi MINT-247027.
STRINGi 9606.ENSP00000270279.

PTM databases

PhosphoSitei Q9ULV8.

Polymorphism databases

DMDMi 125987803.

Proteomic databases

MaxQBi Q9ULV8.
PaxDbi Q9ULV8.
PRIDEi Q9ULV8.

Protocols and materials databases

DNASUi 23624.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000270279 ; ENSP00000270279 ; ENSG00000142273 . [Q9ULV8-1 ]
ENST00000341505 ; ENSP00000340250 ; ENSG00000142273 . [Q9ULV8-2 ]
GeneIDi 23624.
KEGGi hsa:23624.
UCSCi uc002ozs.3. human. [Q9ULV8-1 ]
uc010ejt.3. human. [Q9ULV8-2 ]

Organism-specific databases

CTDi 23624.
GeneCardsi GC19P045281.
H-InvDB HIX0202847.
HGNCi HGNC:15961. CBLC.
HPAi CAB008087.
MIMi 608453. gene.
neXtProti NX_Q9ULV8.
PharmGKBi PA26117.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG318595.
GeneTreei ENSGT00390000011617.
HOGENOMi HOG000294176.
HOVERGENi HBG005255.
InParanoidi Q9ULV8.
KOi K04707.
OMAi WQHSDSQ.
OrthoDBi EOG73BVCF.
PhylomeDBi Q9ULV8.
TreeFami TF314210.

Enzyme and pathway databases

SignaLinki Q9ULV8.

Miscellaneous databases

GeneWikii CBLC.
GenomeRNAii 23624.
NextBioi 46378.
PROi Q9ULV8.
SOURCEi Search...

Gene expression databases

Bgeei Q9ULV8.
CleanExi HS_CBLC.
Genevestigatori Q9ULV8.

Family and domain databases

Gene3Di 1.10.238.10. 1 hit.
1.20.930.20. 1 hit.
3.30.40.10. 1 hit.
3.30.505.10. 1 hit.
InterProi IPR024162. Adaptor_Cbl.
IPR014741. Adaptor_Cbl_EF_hand-like.
IPR003153. Adaptor_Cbl_N_hlx.
IPR014742. Adaptor_Cbl_SH2-like.
IPR024159. Cbl_PTB.
IPR011992. EF-hand-dom_pair.
IPR000980. SH2.
IPR001841. Znf_RING.
IPR013083. Znf_RING/FYVE/PHD.
IPR017907. Znf_RING_CS.
[Graphical view ]
PANTHERi PTHR23007. PTHR23007. 1 hit.
Pfami PF02262. Cbl_N. 1 hit.
PF02761. Cbl_N2. 1 hit.
PF02762. Cbl_N3. 1 hit.
[Graphical view ]
SMARTi SM00184. RING. 1 hit.
SM00252. SH2. 1 hit.
[Graphical view ]
SUPFAMi SSF47668. SSF47668. 1 hit.
SSF55550. SSF55550. 1 hit.
PROSITEi PS51506. CBL_PTB. 1 hit.
PS00518. ZF_RING_1. 1 hit.
PS50089. ZF_RING_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Molecular cloning and characterization of a novel cbl-family gene, cbl-c."
    Kim M., Tezuka T., Suzuki Y., Sugano S., Hirai M., Yamamoto T.
    Gene 239:145-154(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT TYR-405.
  2. Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), VARIANT TYR-405, FUNCTION AS EGF SIGNALING NEGATIVE REGULATOR, PHOSPHORYLATION BY EGFR (ISOFORM 1), TISSUE SPECIFICITY, INTERACTION WITH CRK AND LYN.
    Tissue: Pancreatic adenocarcinoma.
  3. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Skin.
  4. "Cbl-c suppresses v-Src-induced transformation through ubiquitin-dependent protein degradation."
    Kim M., Tezuka T., Tanaka K., Yamamoto T.
    Oncogene 23:1645-1655(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION AS E3 UBIQUITIN-PROTEIN LIGASE, INTERACTION WITH SRC, AUTOUBIQUITINATION, MUTAGENESIS OF GLY-276; TYR-341 AND CYS-351.
  5. "CD2AP and Cbl-3/Cbl-c constitute a critical checkpoint in the regulation of ret signal transduction."
    Tsui C.C., Pierchala B.A.
    J. Neurosci. 28:8789-8800(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN RET STABILITY, INTERACTION WITH RET, MUTAGENESIS OF GLY-276 AND CYS-351.
  6. "The N terminus of Cbl-c regulates ubiquitin ligase activity by modulating affinity for the ubiquitin-conjugating enzyme."
    Ryan P.E., Sivadasan-Nair N., Nau M.M., Nicholas S., Lipkowitz S.
    J. Biol. Chem. 285:23687-23698(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, ENZYME REGULATION, DOMAIN, INTERACTION WITH UBE2D2 AND UBE2D3, PHOSPHORYLATION AT TYR-341, MUTAGENESIS OF TYR-341.
  7. "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."
    Ryan P.E., Kales S.C., Yadavalli R., Nau M.M., Zhang H., Lipkowitz S.
    PLoS ONE 7:E49428-E49428(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, AUTOUBIQUITINATION, PHOSPHORYLATION AT TYR-341, INTERACTION WITH TGFB1I1, MUTAGENESIS OF TYR-341; CYS-351 AND CYS-366.
  8. "Crystal structure of Cbl-c (Cbl-3) TKB domain in complex with EGFR py1069 peptide."
    Structural genomics consortium (SGC)
    Submitted (OCT-2010) to the PDB data bank
    Cited for: X-RAY CRYSTALLOGRAPHY (2.52 ANGSTROMS) OF 9-323 IN COMPLEX WITH EGFR PEPTIDE.
  9. "Structural flexibility regulates phosphopeptide-binding activity of the tyrosine kinase binding domain of Cbl-c."
    Takeshita K., Tezuka T., Isozaki Y., Yamashita E., Suzuki M., Kim M., Yamanashi Y., Yamamoto T., Nakagawa A.
    J. Biochem. 152:487-495(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.52 ANGSTROMS) OF 1-323 IN COMPLEX WITH CALCIUM; SRC AND EGFR PEPTIDES, CALCIUM-BINDING, INTERACTION WITH EGFR AND SRC, MUTAGENESIS OF TYR-244; ARG-264; PRO-265; SER-266; THR-268 AND GLY-276.

Entry informationi

Entry nameiCBLC_HUMAN
AccessioniPrimary (citable) accession number: Q9ULV8
Secondary accession number(s): Q8N1E5, Q9Y5Z2, Q9Y5Z3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: February 6, 2007
Last modified: October 29, 2014
This is version 142 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Miscellaneous

This protein has one functional calcium-binding site.

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 19
    Human chromosome 19: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3