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Reviewed, UniProtKB/Swiss-Prot Q80XL1 (CBLC_MOUSE)

Last modified January 19, 2010. Version 62. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Alternative products · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein namesRecommended name:
    Signal transduction protein CBL-C
Alternative name(s):
    SH3-binding protein CBL-C
    CBL-3
Gene names
Name: Cblc
Synonyms: Cbl3
OrganismMus musculus (Mouse)
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus

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Protein attributes

Sequence length496 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level.

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General annotation (Comments)

Function

Regulator of EGFR mediated signal transduction By similarity.

Subunit structure

Interacts with a restricted range of SH3 domain proteins By similarity.

Subcellular location

Nucleus Potential.

Tissue specificity

Ubiquitously expressed. Ref.1

Developmental stage

Expressed at E14.5 in liver, lung and brain. Ref.1

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 By similarity.

The RING-type zinc finger domain mediates binding to an E2 ubiquitin-conjugating enzyme By similarity.

Post-translational modification

Phosphorylated on tyrosines by EGFR By similarity.

Miscellaneous

This protein has one functional calcium-binding site By similarity.

Sequence similarities

Contains 1 CBL N-terminal domain.

Contains 2 EF-hand-like domains.

Contains 1 RING-type zinc finger.

Contains 1 SH2 domain.

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Ontologies

Keywords
   Cellular componentNucleus
   Coding sequence diversityAlternative splicing
   DomainRepeat
SH2 domain
Zinc-finger
   LigandCalcium
Metal-binding
Zinc
   PTMPhosphoprotein
Gene Ontology (GO)
   Biological processcell surface receptor linked signal transduction

Inferred from electronic annotation. Source: InterPro

   Cellular componentnucleus

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functioncalcium ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

signal transducer activity

Inferred from electronic annotation. Source: InterPro

zinc ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

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Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q80XL1-1)

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.
Isoform 2 (identifier: Q80XL1-2)

The sequence of this isoform differs from the canonical sequence as follows:
     259-259: S → R
     260-496: Missing.

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 496496Signal transduction protein CBL-C
PRO_0000055867

Regions

Domain8 – 326319CBL N-terminal
Domain181 – 1899EF-hand-like 1
Domain198 – 20912EF-hand-like 2
Domain236 – 31075SH2; atypical
Zinc finger350 – 38940RING-type
Region8 – 1461394H By similarity
Region311 – 34939Linker By similarity
Motif88 – 914Nuclear localization signal By similarity

Sites

Binding site2631Phosphotyrosine By similarity

Natural variations

Alternative sequence2591S → R in isoform 2.
VSP_014946
Alternative sequence260 – 496237Missing in isoform 2.
VSP_014947

Experimental info

Sequence conflict81R → Q in AAK01405. Ref.1
Sequence conflict3711S → G in AAK01405. Ref.1
Sequence conflict3751A → S in BAB26782. Ref.2
Sequence conflict4161G → D in AAH46337. Ref.3

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Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified August 16, 2005. Version 2.
Checksum: 4DBE4A14C3D1BF57

FASTA49655,715
        10         20         30         40         50         60 
MAAAAAPRGW QRGEPRALSR AVKLLQRLEE QCRDPRMVTG PPSLRDLLPR TAQLLGEVAK 

        70         80         90        100        110        120 
ARREAREDPE GPGGADDFLA IYLANLEVKG RQVAELLPPR GKKDVNQDVF REGSRFRRQL 

       130        140        150        160        170        180 
AKLALIFSHM HAELSALFPA GKYCGHLYQL TKGSAHIFWR QNCGVRCVLP WAEFQSLLCA 

       190        200        210        220        230        240 
CHPVEPGPTM QALRSTLDLT CNGHVSVFEF DVFTRLFQPW PTLLRNWQLL AVNHPGYMAF 

       250        260        270        280        290        300 
LTYDEVQTRL QAYRDKPGSY IFRPSCTRLG QWAIGYVSSD GSILQTIPLN KPLLQVLLKG 

       310        320        330        340        350        360 
QKDGIFLFPD GKKHNPDLTE LCRVEPYQRI QVSEEQLLLY QAMNSTFQLC KICAERDKDV 

       370        380        390        400        410        420 
RIEPCGHLLC SCCLAAWQDS DSQTCPFCRC EIKGREAVSI CQAQERPTEV RTAADGSRDN 

       430        440        450        460        470        480 
CHQEAAEQKL GPVIPSAPSL LPEDQFPQGP QDKGWLTLAP LALPRLRPPL PLPKMASVLW 

       490 
EVTSRPRARE EATESS

« Hide

Isoform 2.

Checksum: 5EA7613675F647DF
Show »

FASTA25929,316

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References

« Hide 'large scale' references
[1]"Characterization of the mouse Cblc/Cbl3 gene."
Fiore F., Ollendorff V., Birnbaum D.
Biochem. Biophys. Res. Commun. 280:182-187(2001) [PubMed: 11162497] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
Strain: C57BL/6.
[2]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed: 16141072] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
Strain: C57BL/6J.
Tissue: Tongue.
[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: 15489334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Strain: FVB/N.
Tissue: Colon.
+Additional computationally mapped references.

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Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AF319956 mRNA. Translation: AAK01405.1.
AK009399 mRNA. Translation: BAB26265.1.
AK010228 mRNA. Translation: BAB26782.1.
BC046337 mRNA. Translation: AAH46337.1.
IPIIPI00330742.
IPI00649974.
RefSeqNP_075713.3.
UniGeneMm.81698

3D structure databases

SMRQ80XL1. Positions 13-319, 343-397.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ80XL1.

PTM databases

PhosphoSiteQ80XL1.

Proteomic databases

PRIDEQ80XL1.

Genome annotation databases

EnsemblENSMUST00000043822; ENSMUSP00000039955; ENSMUSG00000040525; Mus musculus. [Genome view]
ENSMUST00000108449; ENSMUSP00000104088; ENSMUSG00000040525; Mus musculus. [Genome view]
GeneID80794.
UCSCuc009fnh.1. mouse.
uc009fni.1. mouse.

Organism-specific databases

CTD80794.
MGIMGI:1931457. Cblc.

Phylogenomic databases

eggNOGroNOG10921.
HOGENOMHBG444458.
HOVERGENQ80XL1.
InParanoidQ80XL1.
OMASINTIFH.
PhylomeDBQ80XL1.

Gene expression databases

ArrayExpressQ80XL1.
BgeeQ80XL1.
CleanExMM_CBLC.
GenevestigatorQ80XL1.
GermOnlineENSMUSG00000040525. Mus musculus.

Family and domain databases

InterProIPR014741. Adaptor_Cbl_EF_Hand-like.
IPR003153. Adaptor_Cbl_N.
IPR014742. Adaptor_Cbl_SH2-like.
IPR011992. EF-hand-like_dom.
IPR000980. SH2.
IPR018957. Znf_C3HC4_RING-type.
IPR001841. Znf_RING.
IPR017907. Znf_RING_CS.
[Graphical view]
Gene3DG3DSA:1.20.930.20. Adaptor_Cbl_N. 1 hit.
G3DSA:1.10.238.10. EF-Hand_type. 1 hit.
G3DSA:3.30.505.10. SH2. 1 hit.
PfamPF02262. Cbl_N. 1 hit.
PF02761. Cbl_N2. 1 hit.
PF02762. Cbl_N3. 1 hit.
PF00097. zf-C3HC4. 1 hit.
[Graphical view]
SMARTSM00184. RING. 1 hit.
SM00252. SH2. 1 hit.
[Graphical view]
PROSITEPS50001. SH2. False negative.
PS00518. ZF_RING_1. 1 hit.
PS50089. ZF_RING_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

NextBio350129.
SOURCESearch...

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Entry information

Entry nameCBLC_MOUSE
AccessionPrimary (citable) accession number: Q80XL1
Secondary accession number(s): Q99PB6, Q9D6L2, Q9D7A9
Entry history
Integrated into UniProtKB/Swiss-Prot: August 16, 2005
Last sequence update: August 16, 2005
Last modified: January 19, 2010
This is version 62 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

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Relevant documents

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Alternative products · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents