Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Q3TTA7

- CBLB_MOUSE

UniProt

Q3TTA7 - CBLB_MOUSE

Protein

E3 ubiquitin-protein ligase CBL-B

Gene

Cblb

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 97 (01 Oct 2014)
      Sequence version 3 (27 Jul 2011)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

    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. Slightly promotes SRC ubiquitination. May be involved in EGFR ubiquitination and internalization. May be functionally coupled with the E2 ubiquitin-protein ligase UB2D3.6 Publications

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei286 – 2861PhosphotyrosineBy similarity

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Calcium bindingi219 – 23214PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri373 – 41240RING-typePROSITE-ProRule annotationAdd
    BLAST

    GO - Molecular functioni

    1. calcium ion binding Source: InterPro
    2. ligase activity Source: UniProtKB-KW
    3. protein binding Source: IntAct
    4. signal transducer activity Source: InterPro
    5. ubiquitin-protein transferase activity Source: InterPro
    6. zinc ion binding Source: InterPro

    GO - Biological processi

    1. cell surface receptor signaling pathway Source: InterPro
    2. immune response Source: MGI
    3. intracellular signal transduction Source: MGI
    4. negative regulation of alpha-beta T cell proliferation Source: MGI
    5. negative regulation of T cell receptor signaling pathway Source: MGI
    6. positive regulation of protein catabolic process Source: MGI
    7. positive regulation of T cell anergy Source: MGI
    8. T cell activation Source: MGI

    Keywords - Molecular functioni

    Ligase

    Keywords - Biological processi

    Ubl conjugation pathway

    Keywords - Ligandi

    Calcium, Metal-binding, Zinc

    Enzyme and pathway databases

    UniPathwayiUPA00143.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    E3 ubiquitin-protein ligase CBL-B (EC:6.3.2.-)
    Alternative name(s):
    Casitas B-lineage lymphoma proto-oncogene b
    SH3-binding protein CBL-B
    Signal transduction protein CBL-B
    Gene namesi
    Name:Cblb
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Unplaced

    Organism-specific databases

    MGIiMGI:2146430. Cblb.

    Subcellular locationi

    Cytoplasm 1 Publication
    Note: In adipocytes, translocates to the plasma membrane upon insulin stimulation.

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-SubCell
    2. nucleus Source: InterPro

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Disruption phenotypei

    Mice are fertile and grossly normal. However, they show a high sensitivity to autoimmune diseases and may develop a spontaneous generalized autoimmune disorder characterized by auto-antibody production, infiltration of activated T- and B-lymphocytes into various organs and parenchymal damage.1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 982982E3 ubiquitin-protein ligase CBL-BPRO_0000055861Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei282 – 2821Phosphoserine; by PKC/PRKCQBy similarity
    Modified residuei521 – 5211PhosphoserineBy similarity
    Modified residuei525 – 5251PhosphoserineBy similarity
    Modified residuei529 – 5291PhosphoserineBy similarity
    Modified residuei633 – 6331PhosphoserineBy similarity
    Modified residuei664 – 6641Phosphotyrosine2 Publications
    Modified residuei708 – 7081Phosphotyrosine2 Publications
    Modified residuei889 – 8891Phosphotyrosine2 Publications

    Post-translational modificationi

    Phosphorylated on tyrosine and serine residues upon TCR or BCR activation. Phosphorylated on Tyr-664 and Tyr-708 in adipocytes following insulin stimulation.3 Publications
    Auto-ubiquitinated upon EGF-mediated cell activation or upon T-cell costimulation by CD28; which promotes proteasomal degradation.1 Publication

    Keywords - PTMi

    Phosphoprotein, Ubl conjugation

    Proteomic databases

    PaxDbiQ3TTA7.
    PRIDEiQ3TTA7.

    PTM databases

    PhosphoSiteiQ3TTA7.

    Expressioni

    Gene expression databases

    CleanExiMM_CBLB.
    GenevestigatoriQ3TTA7.

    Interactioni

    Subunit structurei

    Interacts with SH3 domain-containing proteins LCK, CRK and SORBS1. Interacts with LCP2 and ZAP70. May interact with CBL. 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. Interacts with EGFR (phosphorylated).2 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    Myd88P223662EBI-3649276,EBI-525108
    Ticam1Q80UF72EBI-3649276,EBI-3649271

    Protein-protein interaction databases

    BioGridi229001. 17 interactions.
    IntActiQ3TTA7. 4 interactions.
    MINTiMINT-5042139.
    STRINGi10090.ENSMUSP00000023313.

    Structurei

    3D structure databases

    ProteinModelPortaliQ3TTA7.
    SMRiQ3TTA7. Positions 38-427, 929-972.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini35 – 343309Cbl-PTBPROSITE-ProRule annotationAdd
    BLAST
    Domaini931 – 97040UBAPROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni35 – 1671334HAdd
    BLAST
    Regioni168 – 24073EF-hand-likeAdd
    BLAST
    Regioni241 – 343103SH2-likeAdd
    BLAST
    Regioni344 – 37229LinkerAdd
    BLAST
    Regioni543 – 56725Interaction with VAV1By similarityAdd
    BLAST
    Regioni891 – 92737Interaction with SH3KBP1By similarityAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi477 – 56690Pro-richAdd
    BLAST
    Compositional biasi672 – 6754Poly-Pro
    Compositional biasi775 – 87197Pro-richAdd
    BLAST

    Domaini

    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.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
    Contains 1 UBA domain.PROSITE-ProRule annotation

    Zinc finger

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri373 – 41240RING-typePROSITE-ProRule annotationAdd
    BLAST

    Keywords - Domaini

    Repeat, Zinc-finger

    Phylogenomic databases

    eggNOGiNOG242251.
    HOGENOMiHOG000294176.
    HOVERGENiHBG005255.
    InParanoidiQ3TTA7.
    KOiK04707.

    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.
    IPR015940. UBA/transl_elong_EF1B_N_euk.
    IPR000449. UBA/Ts_N.
    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.
    PF00627. UBA. 1 hit.
    [Graphical view]
    SMARTiSM00184. RING. 1 hit.
    SM00252. SH2. 1 hit.
    SM00165. UBA. 1 hit.
    [Graphical view]
    SUPFAMiSSF47668. SSF47668. 1 hit.
    SSF55550. SSF55550. 1 hit.
    PROSITEiPS51506. CBL_PTB. 1 hit.
    PS50030. UBA. 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: Q3TTA7-1) [UniParc]FASTAAdd to Basket

    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

    MANSMNGRNP GGRGGNPRKG RILGIIDAIQ DAVGPPKQAA ADRRTVEKTW    50
    KLMDKVVRLC QNPKLQLKNS PPYILDILPD TYQHLRLILS KYDDNQKLAQ 100
    LSENEYFKIY IDSLMKKSKR AIRLFKEGKE RMYEEQSQDR RNLTKLSLIF 150
    SHMLAEIKAI FPNGQFQGDN FRITKADAAE FWRKFFGDKT IVPWKVFRQC 200
    LHEVHQISSG LEAMALKSTI DLTCNDYISV FEFDIFTRLF QPWGSILRNW 250
    NFLAVTHPGY MAFLTYDEVK ARLQKYSTKP GSYIFRLSCT RLGQWAIGYV 300
    TGDGNILQTI PHNKPLFQAL IDGSREGFYL YPDGRSYNPD LTGLCEPTPH 350
    DHIKVTQEQY ELYCEMGSTF QLCKICAEND KDVKIEPCGH LMCTSCLTAW 400
    QESDGQGCPF CRCEIKGTEP IIVDPFDPRD EGSRCCSIID PFSIPMLDLD 450
    DDDDREESLM MNRLASVRKC TDRQNSPVTS PGSSPLAQRR KPQPDPLQIP 500
    HLSLPPVPPR LDLIQKGIVR SPCGSPTGSP KSSPCMVRKQ DKPLPAPPPP 550
    LRDPPPPPER PPPIPPDNRL SRHFHHGESV PSRDQPMPLE AWCPRDAFGT 600
    NQVMGCRILG DGSPKPGVTA NSSLNGRHSR MGSEQVLMRK HRRHDLPSEG 650
    AKVFSNGHLA TEEYDVPPRL SPPPPVTTLL PSIKCTGPLA NCLSEKTRDT 700
    VEDDDDEYKI PSSHPVSLNS QPSHCHNVKA PVRSCDNGHC ILNGTHGAPS 750
    EMKKSNIPDL GIYLKGGGSD SASDPVPLPP ARPPPRDSPK HGSSVNRTPS 800
    DYDLLIPPLG EDAFDALPPS LPPPPPPARH SLIEHSKPPG SSSRPSSGQD 850
    LFLLPSDPFF DPTSGQVPLP PARRAAGDSG KANRASQDYD QLPSSSDGSQ 900
    APARPPKPRP RRTAPEIHHR KPHGPEAALE NVDAKIAKLM GEGYAFEEVK 950
    RALEIAQNNV EVARSILREF AFPPPVSPRL NL 982
    Length:982
    Mass (Da):109,092
    Last modified:July 27, 2011 - v3
    Checksum:i14B55C4106F84A86
    GO
    Isoform 2 (identifier: Q3TTA7-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-152: Missing.

    Show »
    Length:830
    Mass (Da):91,524
    Checksum:iAD8C574827907824
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti176 – 1761A → T in BAE36418. (PubMed:16141072)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 152152Missing in isoform 2. 1 PublicationVSP_017222Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK147367 mRNA. No translation available.
    AK161486 mRNA. Translation: BAE36418.1.
    AC117780 Genomic DNA. No translation available.
    AC154251 Genomic DNA. No translation available.
    AC154478 Genomic DNA. No translation available.
    RefSeqiNP_001028410.1. NM_001033238.1.
    XP_006522010.1. XM_006521947.1. [Q3TTA7-1]
    XP_006522011.1. XM_006521948.1. [Q3TTA7-1]
    XP_006522012.1. XM_006521949.1. [Q3TTA7-1]
    XP_006522013.1. XM_006521950.1. [Q3TTA7-1]
    XP_006522015.1. XM_006521952.1.
    UniGeneiMm.328206.

    Genome annotation databases

    GeneIDi208650.
    KEGGimmu:208650.
    UCSCiuc007zlf.1. mouse. [Q3TTA7-1]

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK147367 mRNA. No translation available.
    AK161486 mRNA. Translation: BAE36418.1 .
    AC117780 Genomic DNA. No translation available.
    AC154251 Genomic DNA. No translation available.
    AC154478 Genomic DNA. No translation available.
    RefSeqi NP_001028410.1. NM_001033238.1.
    XP_006522010.1. XM_006521947.1. [Q3TTA7-1 ]
    XP_006522011.1. XM_006521948.1. [Q3TTA7-1 ]
    XP_006522012.1. XM_006521949.1. [Q3TTA7-1 ]
    XP_006522013.1. XM_006521950.1. [Q3TTA7-1 ]
    XP_006522015.1. XM_006521952.1.
    UniGenei Mm.328206.

    3D structure databases

    ProteinModelPortali Q3TTA7.
    SMRi Q3TTA7. Positions 38-427, 929-972.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 229001. 17 interactions.
    IntActi Q3TTA7. 4 interactions.
    MINTi MINT-5042139.
    STRINGi 10090.ENSMUSP00000023313.

    PTM databases

    PhosphoSitei Q3TTA7.

    Proteomic databases

    PaxDbi Q3TTA7.
    PRIDEi Q3TTA7.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 208650.
    KEGGi mmu:208650.
    UCSCi uc007zlf.1. mouse. [Q3TTA7-1 ]

    Organism-specific databases

    CTDi 868.
    MGIi MGI:2146430. Cblb.

    Phylogenomic databases

    eggNOGi NOG242251.
    HOGENOMi HOG000294176.
    HOVERGENi HBG005255.
    InParanoidi Q3TTA7.
    KOi K04707.

    Enzyme and pathway databases

    UniPathwayi UPA00143 .

    Miscellaneous databases

    NextBioi 372367.
    PROi Q3TTA7.
    SOURCEi Search...

    Gene expression databases

    CleanExi MM_CBLB.
    Genevestigatori Q3TTA7.

    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.
    IPR015940. UBA/transl_elong_EF1B_N_euk.
    IPR000449. UBA/Ts_N.
    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.
    PF00627. UBA. 1 hit.
    [Graphical view ]
    SMARTi SM00184. RING. 1 hit.
    SM00252. SH2. 1 hit.
    SM00165. UBA. 1 hit.
    [Graphical view ]
    SUPFAMi SSF47668. SSF47668. 1 hit.
    SSF55550. SSF55550. 1 hit.
    PROSITEi PS51506. CBL_PTB. 1 hit.
    PS50030. UBA. 1 hit.
    PS00518. ZF_RING_1. 1 hit.
    PS50089. ZF_RING_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "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.
      , 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] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
      Strain: C57BL/6J.
      Tissue: Testis.
    2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: C57BL/6J.
    3. "Cbl-b is a negative regulator of receptor clustering and raft aggregation in T cells."
      Krawczyk C., Bachmaier K., Sasaki T., Jones R.G., Snapper S.B., Bouchard D., Kozieradzki I., Ohashi P.S., Alt F.W., Penninger J.M.
      Immunity 13:463-473(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    4. Cited for: FUNCTION, INTERACTION WITH PIK3R1; LCP2; ZAP70; LCK; PLCG1 AND VAV1.
    5. Cited for: FUNCTION, DISRUPTION PHENOTYPE.
    6. "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] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    7. "Regulation of T cell activation threshold by CD28 costimulation through targeting Cbl-b for ubiquitination."
      Zhang J., Bardos T., Li D., Gal I., Vermes C., Xu J., Mikecz K., Finnegan A., Lipkowitz S., Glant T.T.
      J. Immunol. 169:2236-2240(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: UBIQUITINATION.
    8. "The roles of Cbl-b and c-Cbl in insulin-stimulated glucose transport."
      Liu J., DeYoung S.M., Hwang J.B., O'Leary E.E., Saltiel A.R.
      J. Biol. Chem. 278:36754-36762(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT TYR-664 AND TYR-708, INTERACTION WITH CBL; CRK AND SORBS1, SUBCELLULAR LOCATION.
    9. "Cbl-b negatively regulates B cell antigen receptor signaling in mature B cells through ubiquitination of the tyrosine kinase Syk."
      Sohn H.W., Gu H., Pierce S.K.
      J. Exp. Med. 197:1511-1524(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION, FUNCTION.
    10. Cited for: FUNCTION.
    11. "Immunoaffinity profiling of tyrosine phosphorylation in cancer cells."
      Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H., Zha X.-M., Polakiewicz R.D., Comb M.J.
      Nat. Biotechnol. 23:94-101(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-889, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiCBLB_MOUSE
    AccessioniPrimary (citable) accession number: Q3TTA7
    Secondary accession number(s): E9QMY2
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 7, 2006
    Last sequence update: July 27, 2011
    Last modified: October 1, 2014
    This is version 97 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Miscellaneous

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

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3