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Reviewed, UniProtKB/Swiss-Prot Q13191 (CBLB_HUMAN)

Last modified January 19, 2010. Version 112. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (7) | 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 · Web resources · Cross-references · Entry information · Relevant documents

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Names and origin

Protein namesRecommended name:
    E3 ubiquitin-protein ligase CBL-B
    EC=6.3.2.-
Alternative name(s):
    Signal transduction protein CBL-B
    SH3-binding protein CBL-B
    Casitas B-lineage lymphoma proto-oncogene b
    RING finger protein 56
Gene names
Name: CBLB
Synonyms: RNF56
ORF Names: Nbla00127
OrganismHomo sapiens (Human) [Complete proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

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Protein attributes

Sequence length982 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level.

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General annotation (Comments)

Function

E3 ubiquitin-protein ligase which accepts ubiquitin from specific E2 ubiquitin-conjugating enzymes, and transfers it to substrates, generally promoting their degradation by the proteasome. Negatively regulates TCR (T-cell receptor), BCR (B-cell receptor) and FCER1 (high affinity immunoglobulin epsilon receptor) signal transduction pathways. In naive T-cells, inhibits VAV1 activation upon TCR engagement and imposes a requirement for CD28 costimulation for proliferation and IL-2 production. Also acts by promoting PIK3R1/p85 ubiquitination, which impairs its recruitment to the TCR and subsequent activation. In activated T-cells, inhibits PLCG1 activation and calcium mobilization upon restimulation and promotes anergy. In B-cells, acts by ubiquitinating SYK and promoting its proteasomal degradation. May also be involved in EGFR ubiquitination and internalization. Ref.8 Ref.9 Ref.10 Ref.12

Pathway

Protein modification; protein ubiquitination.

Subunit structure

Interacts with SH3 domain-containing proteins LCK, CRK and SORBS1. Interacts with LCP2 and ZAP70. May interact with CBL By similarity. Interacts with SH3 domain-containing proteins VAV1, FYN, FGR, PLCG1, GRB2, CRKL, PIK3R1 and SH3KBP1/CIN85. Identified in heterotrimeric complexes with SH3KBP1/CIN85, CD2AP and ARHGEF7, where one CBLB peptide binds two copies of the other protein. Interacts with poly-ubiquitinated proteins. Dimerization is required for the binding of poly-ubiquitin, but not for the binding of mono-ubiquitin. Ref.8 Ref.9 Ref.10 Ref.2 Ref.13 Ref.14 Ref.20 Ref.21

Subcellular location

Cytoplasm. Note: Upon EGF stimulation, associates with endocytic vesicles. Ref.13

Tissue specificity

Expressed in placenta, heart, lung, kidney, spleen, ovary and testis, as well as fetal brain and liver and hematopoietic cell lines, but not in adult brain, liver, pancreas, salivary gland, or skeletal muscle. Present in lymphocytes (at protein level). Ref.8 Ref.2

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.

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

The UBA domain interacts with poly-ubiquitinated proteins.

Post-translational modification

Phosphorylated on tyrosine residues upon TCR or BCR activation, and upon various types of cell stimulation. Ref.8 Ref.9 Ref.15 Ref.16 Ref.17 Ref.18 Ref.19 Ref.22

Auto-ubiquitinated upon EGF-mediated cell activation or upon T-cell costimulation by CD28; which promotes proteasomal degradation.

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.

Contains 1 UBA domain.

Sequence caution

The sequence BAE45748.1 differs from that shown. Reason: Erroneous termination at position 904. Translated as Arg.

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Alternative products

This entry describes 4 isoforms produced by alternative splicing. [Align] [Select]
Isoform Long (identifier: Q13191-1)

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 Truncated 1 (identifier: Q13191-2)

The sequence of this isoform differs from the canonical sequence as follows:
     812-982: Missing.
Isoform Truncated 2 (identifier: Q13191-3)

The sequence of this isoform differs from the canonical sequence as follows:
     767-770: DVFD → TYRI
     771-982: Missing.
Isoform 4 (identifier: Q13191-4)

The sequence of this isoform differs from the canonical sequence as follows:
     1-939: Missing.
Note: No experimental confirmation available.

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 982982E3 ubiquitin-protein ligase CBL-B
PRO_0000055860

Regions

Domain36 – 349314CBL N-terminal
Domain204 – 2129EF-hand-like 1
Domain221 – 23212EF-hand-like 2
Domain259 – 33375SH2; atypical
Domain931 – 97040UBA
Zinc finger373 – 41240RING-type
Region36 – 1691344H
Region334 – 37239Linker
Region543 – 56826Interaction with VAV1
Region891 – 92737Interaction with SH3KBP1
Compositional bias477 – 925449Pro-rich

Sites

Binding site2861Phosphotyrosine By similarity

Amino acid modifications

Modified residue3631Phosphotyrosine Ref.19
Modified residue4801Phosphoserine Ref.15
Modified residue4841Phosphoserine Ref.15
Modified residue5211Phosphoserine Ref.18
Modified residue5251Phosphoserine Ref.18
Modified residue5291Phosphoserine Ref.18
Modified residue6141Phosphoserine Ref.17
Modified residue6651Phosphotyrosine Ref.8 Ref.19
Modified residue7091Phosphotyrosine Ref.8
Modified residue8891Phosphotyrosine Ref.16 Ref.19

Natural variations

Alternative sequence1 – 939939Missing in isoform 4.
VSP_031697
Alternative sequence767 – 7704DVFD → TYRI in isoform Truncated 2.
VSP_005730
Alternative sequence771 – 982212Missing in isoform Truncated 2.
VSP_005731
Alternative sequence812 – 982171Missing in isoform Truncated 1.
VSP_005729
Natural variant5841R → K: dbSNP rs17853100. Ref.5
VAR_025303
Natural variant8831N → D: dbSNP rs35835913.
VAR_039241

Experimental info

Mutagenesis2981G → E: Inhibits interaction with SYK. No effect on E3 activity. Ref.8 Ref.10
Mutagenesis3731C → A: Abolishes E3 activity but does not affect binding to substrates. Ref.10 Ref.11
Mutagenesis6651Y → F: Slightly inhibits interaction with CRKL. Abolishes interaction with CRKL; when associated to F-709. Ref.8
Mutagenesis7091Y → F: Inhibits interaction with CRKL. Abolishes interaction with CRKL; when associated to F-665. Ref.8
Mutagenesis9041R → A: No effect on interaction with CD2AP. Reduced interaction with SH3KBP1. Strongly reduced interaction with SH3KBP1; when associated with A-911. Ref.20 Ref.21
Mutagenesis9071K → A: No effect on interaction with SH3KBP1. Reduced interaction with CD2AP. Strongly reduced interaction with CD2AP; when associated with A-911. Ref.21
Mutagenesis9111R → A: Reduced interaction with CD2AP and with SH3KBP1. Strongly reduced interaction with CD2AP; when associated with A-907. Strongly reduced interaction with SH3KBP1; when associated with A-904. Ref.20 Ref.21
Mutagenesis9371A → E: Loss of ubiquitin binding. Reduced levels of tyrosine phosphorylation. Ref.22
Mutagenesis9401M → A: Loss of ubiquitin binding. Reduced levels of tyrosine phosphorylation. Ref.22
Mutagenesis943 – 9442GY → AQ: Abolishes interaction with ubiquitinated proteins.
Mutagenesis9461F → A: Loss of ubiquitin binding. Reduced levels of tyrosine phosphorylation. Ref.22
Mutagenesis9661I → E: Interferes with dimerization. Reduced E3 ubiquitin-protein ligase activity. Reduced levels of tyrosine phosphorylation. Ref.22
Mutagenesis9671L → A: No effect on interaction with ubiquitinated proteins. Ref.14
Sequence conflict2101G → S in AAB09291. Ref.1
Sequence conflict2101G → S in AAB09292. Ref.1
Sequence conflict2101G → S in AAB09293. Ref.1
Sequence conflict9111R → C in CAH56175. Ref.7

Secondary structure

1 ........ 982
Helix Strand Turn

Details...

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Sequences

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

Last modified February 7, 2006. Version 2.
Checksum: B4E307D31B9F0779

FASTA982109,450
        10         20         30         40         50         60 
MANSMNGRNP GGRGGNPRKG RILGIIDAIQ DAVGPPKQAA ADRRTVEKTW KLMDKVVRLC 

        70         80         90        100        110        120 
QNPKLQLKNS PPYILDILPD TYQHLRLILS KYDDNQKLAQ LSENEYFKIY IDSLMKKSKR 

       130        140        150        160        170        180 
AIRLFKEGKE RMYEEQSQDR RNLTKLSLIF SHMLAEIKAI FPNGQFQGDN FRITKADAAE 

       190        200        210        220        230        240 
FWRKFFGDKT IVPWKVFRQC LHEVHQISSG LEAMALKSTI DLTCNDYISV FEFDIFTRLF 

       250        260        270        280        290        300 
QPWGSILRNW NFLAVTHPGY MAFLTYDEVK ARLQKYSTKP GSYIFRLSCT RLGQWAIGYV 

       310        320        330        340        350        360 
TGDGNILQTI PHNKPLFQAL IDGSREGFYL YPDGRSYNPD LTGLCEPTPH DHIKVTQEQY 

       370        380        390        400        410        420 
ELYCEMGSTF QLCKICAEND KDVKIEPCGH LMCTSCLTAW QESDGQGCPF CRCEIKGTEP 

       430        440        450        460        470        480 
IIVDPFDPRD EGSRCCSIID PFGMPMLDLD DDDDREESLM MNRLANVRKC TDRQNSPVTS 

       490        500        510        520        530        540 
PGSSPLAQRR KPQPDPLQIP HLSLPPVPPR LDLIQKGIVR SPCGSPTGSP KSSPCMVRKQ 

       550        560        570        580        590        600 
DKPLPAPPPP LRDPPPPPPE RPPPIPPDNR LSRHIHHVES VPSRDPPMPL EAWCPRDVFG 

       610        620        630        640        650        660 
TNQLVGCRLL GEGSPKPGIT ASSNVNGRHS RVGSDPVLMR KHRRHDLPLE GAKVFSNGHL 

       670        680        690        700        710        720 
GSEEYDVPPR LSPPPPVTTL LPSIKCTGPL ANSLSEKTRD PVEEDDDEYK IPSSHPVSLN 

       730        740        750        760        770        780 
SQPSHCHNVK PPVRSCDNGH CMLNGTHGPS SEKKSNIPDL SIYLKGDVFD SASDPVPLPP 

       790        800        810        820        830        840 
ARPPTRDNPK HGSSLNRTPS DYDLLIPPLG EDAFDALPPS LPPPPPPARH SLIEHSKPPG 

       850        860        870        880        890        900 
SSSRPSSGQD LFLLPSDPFV DLASGQVPLP PARRLPGENV KTNRTSQDYD QLPSCSDGSQ 

       910        920        930        940        950        960 
APARPPKPRP RRTAPEIHHR KPHGPEAALE NVDAKIAKLM GEGYAFEEVK RALEIAQNNV 

       970        980 
EVARSILREF AFPPPVSPRL NL

« Hide

Isoform Truncated 1.

Checksum: A63D22F7C9C677DB
Show »

FASTA81190,883
Isoform Truncated 2.

Checksum: DEE458DFFEE1AF2F
Show »

FASTA77086,582
Isoform 4.

Checksum: 302A356C8DD9D75C
Show »

FASTA434,860

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References

« Hide 'large scale' references
[1]"Cloning and characterization of cbl-b: a SH3 binding protein with homology to the c-cbl proto-oncogene."
Keane M.M., Rivero-Lezcano O.M., Mitchell J.A., Robbins K.C., Lipkowitz S.
Oncogene 10:2367-2377(1995) [PubMed: 7784085] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS LONG; TRUNCATED 1 AND TRUNCATED 2).
[2]"Cbl-b, a member of the Sli-1/c-Cbl protein family, inhibits Vav-mediated c-Jun N-terminal kinase activation."
Bustelo X.R., Crespo P., Lopez-Barahona M., Gutkind J.S., Barbacid M.
Oncogene 15:2511-2520(1997) [PubMed: 9399639] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM LONG), TISSUE SPECIFICITY, INTERACTION WITH VAV1.
[3]"The DNA sequence, annotation and analysis of human chromosome 3."
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. expand/collapse author list , 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.
Nature 440:1194-1198(2006) [PubMed: 16641997] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]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. expand/collapse author list , 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 (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]"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 LONG), VARIANT LYS-584.
Tissue: Testis.
[6]"Neuroblastoma oligo-capping cDNA project: toward the understanding of the genesis and biology of neuroblastoma."
Ohira M., Morohashi A., Nakamura Y., Isogai E., Furuya K., Hamano S., Machida T., Aoyama M., Fukumura M., Miyazaki K., Suzuki Y., Sugano S., Hirato J., Nakagawara A.
Cancer Lett. 197:63-68(2003) [PubMed: 12880961] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 543-982 (ISOFORM LONG).
Tissue: Neuroblastoma.
[7]"The full-ORF clone resource of the German cDNA consortium."
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I.
BMC Genomics 8:399-399(2007) [PubMed: 17974005] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
Tissue: Small intestine.
[8]"Tyrosine phosphorylation and complex formation of Cbl-b upon T cell receptor stimulation."
Elly C., Witte S., Zhang Z., Rosnet O., Lipkowitz S., Altman A., Liu Y.-C.
Oncogene 18:1147-1156(1999) [PubMed: 10022120] [Abstract]
Cited for: TISSUE SPECIFICITY, MUTAGENESIS OF GLY-298; TYR-665 AND TYR-709, INTERACTION WITH GRB2 AND CRKL, PHOSPHORYLATION AT TYR-665 AND TYR-709, FUNCTION.
[9]"cbl-b inhibits epidermal growth factor receptor signaling."
Ettenberg S.A., Keane M.M., Nau M.M., Frankel M., Wang L.-M., Pierce J.H., Lipkowitz S.
Oncogene 18:1855-1866(1999) [PubMed: 10086340] [Abstract]
Cited for: FUNCTION, PHOSPHORYLATION, INTERACTION WITH GRB2 AND PIK3R1.
[10]"Cbl-b, a RING-type E3 ubiquitin ligase, targets phosphatidylinositol 3-kinase for ubiquitination in T cells."
Fang D., Wang H.-Y., Fang N., Altman Y., Elly C., Liu Y.-C.
J. Biol. Chem. 276:4872-4878(2001) [PubMed: 11087752] [Abstract]
Cited for: FUNCTION, INTERACTION WITH PIK3R1, MUTAGENESIS OF GLY-298 AND CYS-373.
[11]"Cbl-b-dependent coordinated degradation of the epidermal growth factor receptor signaling complex."
Ettenberg S.A., Magnifico A., Cuello M., Nau M.M., Rubinstein Y.R., Yarden Y., Weissman A.M., Lipkowitz S.
J. Biol. Chem. 276:27677-27684(2001) [PubMed: 11375397] [Abstract]
Cited for: UBIQUITINATION, MUTAGENESIS OF CYS-373.
[12]"Proteolysis-independent regulation of PI3K by Cbl-b-mediated ubiquitination in T cells."
Fang D., Liu Y.-C.
Nat. Immunol. 2:870-875(2001) [PubMed: 11526404] [Abstract]
Cited for: FUNCTION.
[13]"CIN85 participates in Cbl-b-mediated down-regulation of receptor tyrosine kinases."
Szymkiewicz I., Kowanetz K., Soubeyran P., Dinarina A., Lipkowitz S., Dikic I.
J. Biol. Chem. 277:39666-39672(2002) [PubMed: 12177062] [Abstract]
Cited for: INTERACTION WITH SH3KBP1, SUBCELLULAR LOCATION.
[14]"Cbl-b interacts with ubiquitinated proteins; differential functions of the UBA domains of c-Cbl and Cbl-b."
Davies G.C., Ettenberg S.A., Coats A.O., Mussante M., Ravichandran S., Collins J., Nau M.M., Lipkowitz S.
Oncogene 23:7104-7115(2004) [PubMed: 15273720] [Abstract]
Cited for: INTERACTION WITH UBIQUITINATED PROTEINS, MUTAGENESIS OF 943-GLY-TYR-944 AND LEU-967.
[15]"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
Cell 127:635-648(2006) [PubMed: 17081983] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-480 AND SER-484, MASS SPECTROMETRY.
Tissue: Epithelium.
[16]"Global survey of phosphotyrosine signaling identifies oncogenic kinases in lung cancer."
Rikova K., Guo A., Zeng Q., Possemato A., Yu J., Haack H., Nardone J., Lee K., Reeves C., Li Y., Hu Y., Tan Z., Stokes M., Sullivan L., Mitchell J., Wetzel R., Macneill J., Ren J.M. expand/collapse author list , Yuan J., Bakalarski C.E., Villen J., Kornhauser J.M., Smith B., Li D., Zhou X., Gygi S.P., Gu T.-L., Polakiewicz R.D., Rush J., Comb M.J.
Cell 131:1190-1203(2007) [PubMed: 18083107] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-889, MASS SPECTROMETRY.
[17]"Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
Mol. Cell 31:438-448(2008) [PubMed: 18691976] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-614, MASS SPECTROMETRY.
[18]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed: 18669648] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-521; SER-525 AND SER-529, MASS SPECTROMETRY.
[19]"An extensive survey of tyrosine phosphorylation revealing new sites in human mammary epithelial cells."
Heibeck T.H., Ding S.-J., Opresko L.K., Zhao R., Schepmoes A.A., Yang F., Tolmachev A.V., Monroe M.E., Camp D.G. II, Smith R.D., Wiley H.S., Qian W.-J.
J. Proteome Res. 8:3852-3861(2009) [PubMed: 19534553] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-363; TYR-665 AND TYR-889, MASS SPECTROMETRY.
Tissue: Mammary epithelium.
[20]"Cbl promotes clustering of endocytic adaptor proteins."
Jozic D., Cardenes N., Deribe Y.L., Moncalian G., Hoeller D., Groemping Y., Dikic I., Rittinger K., Bravo J.
Nat. Struct. Mol. Biol. 12:972-979(2005) [PubMed: 16228008] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) OF 899-914 IN COMPLEXES WITH SH3KBP1 AND ARHGEF7, MUTAGENESIS OF ARG-904 AND ARG-911, SUBUNIT.
[21]"Atypical polyproline recognition by the CMS N-terminal Src homology 3 domain."
Moncalian G., Cardenes N., Deribe Y.L., Spinola-Amilibia M., Dikic I., Bravo J.
J. Biol. Chem. 281:38845-38853(2006) [PubMed: 17020880] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 902-912 IN COMPLEX WITH CD2AP, MUTAGENESIS OF ARG-904; LYS-907 AND ARG-911, SUBUNIT.
[22]"Structural basis for ubiquitin-mediated dimerization and activation of the ubiquitin protein ligase Cbl-b."
Peschard P., Kozlov G., Lin T., Mirza I.A., Berghuis A.M., Lipkowitz S., Park M., Gehring K.
Mol. Cell 27:474-485(2007) [PubMed: 17679095] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.56 ANGSTROMS) OF 924-973 IN COMPLEX WITH UBIQUITIN, STRUCTURE BY NMR OF 924-973, TYROSINE PHOSPHORYLATION, MUTAGENESIS OF ALA-937; MET-940; PHE-946 AND ILE-966.
[23]"Solution structure of RSGI RUH-065, a UBA domain from human cDNA."
RIKEN structural genomics initiative (RSGI)
Submitted (MAY-2007) to the PDB data bank
Cited for: STRUCTURE BY NMR OF 931-970.
+Additional computationally mapped references.

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Cross-references

Sequence databases

EMBL
GenBank
DDBJ		U26710 mRNA. Translation: AAB09291.1.
U26711 mRNA. Translation: AAB09292.1.
U26712 mRNA. Translation: AAB09293.1.
AC016138 Genomic DNA. No translation available.
CH471052 Genomic DNA. Translation: EAW79752.1.
BC032851 mRNA. Translation: AAH32851.1.
AB075490 mRNA. Translation: BAE45748.1. Sequence problems.
BX537484 mRNA. Translation: CAH56175.1. Different initiation.
IPIIPI00292856.
IPI00382825.
IPI00793846.
IPI00914020.
RefSeqNP_733762.2.
UniGeneHs.430589

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2AK5X-ray1.85D904-911[»]
2BZ8X-ray2.00C902-912[»]
2DO6NMR-A/B931-970[»]
2J6FX-ray1.70C902-912[»]
2JNHNMR-A926-971[»]
2OOAX-ray1.56A/B924-973[»]
2OOBX-ray1.90A924-973[»]
SMRQ13191. Positions 35-426.
ModBaseSearch...

Protein-protein interaction databases

IntActQ13191. 6 interactions.
STRINGQ13191.

PTM databases

PhosphoSiteQ13191.

Proteomic databases

PRIDEQ13191.

Genome annotation databases

EnsemblENST00000264122; ENSP00000264122; ENSG00000114423; Homo sapiens. [Genome view]
GeneID868.
KEGGhsa:868.
NMPDRfig|9606.3.peg.22921.
UCSCuc003dwc.1. human.
uc003dwd.1. human.
uc003dwe.1. human.

Organism-specific databases

CTD868.
GeneCardsGC03M106859.
H-InvDBHIX0003518.
HGNCHGNC:1542. CBLB.
HPAHPA016864.
HPA018327.
HPA019880.
MIM604491. gene.
PharmGKBPA26116.
GenAtlasSearch...

Phylogenomic databases

eggNOGprNOG17632.
HOGENOMHBG715842.
HOVERGENQ13191.
InParanoidQ13191.
OMALEAWCPR.
PhylomeDBQ13191.

Enzyme and pathway databases

Pathway_Interaction_DBnfat_tfpathway. Calcineurin-regulated NFAT-dependent transcription in lymphocytes.
fcer1pathway. Fc-epsilon receptor I signaling in mast cells.

Gene expression databases

ArrayExpressQ13191.
BgeeQ13191.
CleanExHS_CBLB.
GenevestigatorQ13191.
GermOnlineENSG00000114423. Homo sapiens.

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.
IPR000449. UBA/transl_elong_EF1B_N.
IPR015940. UBA/transl_elong_EF1B_N_euk.
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.
PF00627. UBA. 1 hit.
PF00097. zf-C3HC4. 1 hit.
[Graphical view]
SMARTSM00184. RING. 1 hit.
SM00252. SH2. 1 hit.
SM00165. UBA. 1 hit.
[Graphical view]
PROSITEPS50001. SH2. False negative.
PS50030. UBA. 1 hit.
PS00518. ZF_RING_1. 1 hit.
PS50089. ZF_RING_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

NextBio3622.
SOURCESearch...

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Entry information

Entry nameCBLB_HUMAN
AccessionPrimary (citable) accession number: Q13191
Secondary accession number(s): B7WNM4 expand/collapse secondary AC list , Q13192, Q13193, Q3LIC0, Q63Z43, Q8IVC5
Entry history
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: February 7, 2006
Last modified: January 19, 2010
This is version 112 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)
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.

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PDB cross-references

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