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Q3TTA7

- CBLB_MOUSE

UniProt

Q3TTA7 - CBLB_MOUSE

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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

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. signal transducer activity Source: InterPro
  4. ubiquitin-protein transferase activity Source: InterPro
  5. 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
Complete GO annotation...

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-KW
  2. nucleus Source: InterPro
Complete GO annotation...

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 – 6641Phosphotyrosine1 Publication
Modified residuei708 – 7081Phosphotyrosine1 Publication
Modified residuei889 – 8891Phosphotyrosine1 Publication

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

MaxQBiQ3TTA7.
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. 19 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

        10         20         30         40         50
MANSMNGRNP GGRGGNPRKG RILGIIDAIQ DAVGPPKQAA ADRRTVEKTW
60 70 80 90 100
KLMDKVVRLC QNPKLQLKNS PPYILDILPD TYQHLRLILS KYDDNQKLAQ
110 120 130 140 150
LSENEYFKIY IDSLMKKSKR AIRLFKEGKE RMYEEQSQDR RNLTKLSLIF
160 170 180 190 200
SHMLAEIKAI FPNGQFQGDN FRITKADAAE FWRKFFGDKT IVPWKVFRQC
210 220 230 240 250
LHEVHQISSG LEAMALKSTI DLTCNDYISV FEFDIFTRLF QPWGSILRNW
260 270 280 290 300
NFLAVTHPGY MAFLTYDEVK ARLQKYSTKP GSYIFRLSCT RLGQWAIGYV
310 320 330 340 350
TGDGNILQTI PHNKPLFQAL IDGSREGFYL YPDGRSYNPD LTGLCEPTPH
360 370 380 390 400
DHIKVTQEQY ELYCEMGSTF QLCKICAEND KDVKIEPCGH LMCTSCLTAW
410 420 430 440 450
QESDGQGCPF CRCEIKGTEP IIVDPFDPRD EGSRCCSIID PFSIPMLDLD
460 470 480 490 500
DDDDREESLM MNRLASVRKC TDRQNSPVTS PGSSPLAQRR KPQPDPLQIP
510 520 530 540 550
HLSLPPVPPR LDLIQKGIVR SPCGSPTGSP KSSPCMVRKQ DKPLPAPPPP
560 570 580 590 600
LRDPPPPPER PPPIPPDNRL SRHFHHGESV PSRDQPMPLE AWCPRDAFGT
610 620 630 640 650
NQVMGCRILG DGSPKPGVTA NSSLNGRHSR MGSEQVLMRK HRRHDLPSEG
660 670 680 690 700
AKVFSNGHLA TEEYDVPPRL SPPPPVTTLL PSIKCTGPLA NCLSEKTRDT
710 720 730 740 750
VEDDDDEYKI PSSHPVSLNS QPSHCHNVKA PVRSCDNGHC ILNGTHGAPS
760 770 780 790 800
EMKKSNIPDL GIYLKGGGSD SASDPVPLPP ARPPPRDSPK HGSSVNRTPS
810 820 830 840 850
DYDLLIPPLG EDAFDALPPS LPPPPPPARH SLIEHSKPPG SSSRPSSGQD
860 870 880 890 900
LFLLPSDPFF DPTSGQVPLP PARRAAGDSG KANRASQDYD QLPSSSDGSQ
910 920 930 940 950
APARPPKPRP RRTAPEIHHR KPHGPEAALE NVDAKIAKLM GEGYAFEEVK
960 970 980
RALEIAQNNV EVARSILREF AFPPPVSPRL NL
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. 19 interactions.
IntActi Q3TTA7. 4 interactions.
MINTi MINT-5042139.
STRINGi 10090.ENSMUSP00000023313.

PTM databases

PhosphoSitei Q3TTA7.

Proteomic databases

MaxQBi Q3TTA7.
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

« Hide 'large scale' publications
  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 29, 2014
This is version 98 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