Q3TTA7 (CBLB_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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 names

Name:

Cblb

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	982 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

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.3 Ref.4 Ref.5 Ref.6 Ref.9 Ref.10
Pathway	Protein modification; protein ubiquitination.
Subunit structure	Interacts with SH3 domain-containing proteins FYN, FGR, 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 By similarity. Interacts with SH3 domain-containing proteins VAV1, PLCG1, PIK3R1, LCK, CRK and SORBS1. May interact with CBL. Interacts with LCP2 and ZAP70. Ref.4 Ref.8
Subcellular location	Cytoplasm. Note: In adipocytes, translocates to the plasma membrane upon insulin stimulation. Ref.8
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 By similarity.
Post-translational modification	Phosphorylated on tyrosine and serine residues upon TCR or BCR activation. Phosphorylated on Tyr-664 and Tyr-708 in adipocytes following insulin stimulation. Ref.8 Ref.9 Auto-ubiquitinated upon EGF-mediated cell activation or upon T-cell costimulation by CD28; which promotes proteasomal degradation.
Disruption phenotype	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. Ref.5
Miscellaneous	This protein has one functional calcium-binding site By similarity.
Sequence similarities	Contains 1 Cbl-PTB (Cbl-type phosphotyrosine-binding) domain. Contains 1 RING-type zinc finger. Contains 1 UBA domain.

Ontologies

Keywords
Biological process	Ubl conjugation pathway
Cellular component	Cytoplasm
Coding sequence diversity	Alternative splicing
Domain	Repeat Zinc-finger
Ligand	Calcium Metal-binding Zinc
Molecular function	Ligase
PTM	Phosphoprotein Ubl conjugation
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	T cell activation Inferred from mutant phenotype Ref.3. Source: MGI cell surface receptor signaling pathway Inferred from electronic annotation. Source: InterPro immune response Inferred from mutant phenotype Ref.3. Source: MGI intracellular signal transduction Inferred from mutant phenotype Ref.3. Source: MGI negative regulation of T cell receptor signaling pathway Inferred from mutant phenotype PubMed 14738763. Source: MGI negative regulation of alpha-beta T cell proliferation Inferred from mutant phenotype PubMed 14973438. Source: MGI positive regulation of T cell anergy Inferred from mutant phenotype PubMed 14973438. Source: MGI positive regulation of protein catabolic process Inferred from mutant phenotype PubMed 14973438. Source: MGI
Cellular_component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell nucleus Inferred from electronic annotation. Source: InterPro
Molecular_function	calcium ion binding Inferred from electronic annotation. Source: InterPro signal transducer activity Inferred from electronic annotation. Source: InterPro ubiquitin-protein ligase activity Inferred from electronic annotation. Source: InterPro zinc ion binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
Myd88	P22366	2	EBI-3649276,EBI-525108
Ticam1	Q80UF7	2	EBI-3649276,EBI-3649271

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q3TTA7-1)

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: Q3TTA7-2)

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

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 982	982	E3 ubiquitin-protein ligase CBL-B		PRO_0000055861
Regions
	Domain	35 – 343	309	Cbl-PTB
	Domain	931 – 970	40	UBA
	Calcium binding	219 – 232	14	By similarity
	Zinc finger	373 – 412	40	RING-type
	Region	35 – 167	133	4H
	Region	168 – 240	73	EF-hand-like
	Region	241 – 343	103	SH2-like
	Region	344 – 372	29	Linker
	Region	543 – 567	25	Interaction with VAV1 By similarity
	Region	891 – 927	37	Interaction with SH3KBP1 By similarity
	Compositional bias	477 – 566	90	Pro-rich
	Compositional bias	672 – 675	4	Poly-Pro
	Compositional bias	775 – 871	97	Pro-rich
Sites
	Binding site	286	1	Phosphotyrosine By similarity
Amino acid modifications
	Modified residue	282	1	Phosphoserine; by PKC/PRKCQ By similarity
	Modified residue	521	1	Phosphoserine By similarity
	Modified residue	525	1	Phosphoserine By similarity
	Modified residue	529	1	Phosphoserine By similarity
	Modified residue	664	1	Phosphotyrosine Ref.8
	Modified residue	708	1	Phosphotyrosine Ref.8
	Modified residue	889	1	Phosphotyrosine Ref.11
Natural variations
	Alternative sequence	1 – 152	152	Missing in isoform 2.		VSP_017222
Experimental info
	Sequence conflict	176	1	A → T in BAE36418. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified July 27, 2011. Version 3. Checksum: 14B55C4106F84A86	FASTA	982	109,092
	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 PFSIPMLDLD DDDDREESLM MNRLASVRKC TDRQNSPVTS 490 500 510 520 530 540 PGSSPLAQRR KPQPDPLQIP HLSLPPVPPR LDLIQKGIVR SPCGSPTGSP KSSPCMVRKQ 550 560 570 580 590 600 DKPLPAPPPP LRDPPPPPER PPPIPPDNRL SRHFHHGESV PSRDQPMPLE AWCPRDAFGT 610 620 630 640 650 660 NQVMGCRILG DGSPKPGVTA NSSLNGRHSR MGSEQVLMRK HRRHDLPSEG AKVFSNGHLA 670 680 690 700 710 720 TEEYDVPPRL SPPPPVTTLL PSIKCTGPLA NCLSEKTRDT VEDDDDEYKI PSSHPVSLNS 730 740 750 760 770 780 QPSHCHNVKA PVRSCDNGHC ILNGTHGAPS EMKKSNIPDL GIYLKGGGSD SASDPVPLPP 790 800 810 820 830 840 ARPPPRDSPK HGSSVNRTPS DYDLLIPPLG EDAFDALPPS LPPPPPPARH SLIEHSKPPG 850 860 870 880 890 900 SSSRPSSGQD LFLLPSDPFF DPTSGQVPLP PARRAAGDSG KANRASQDYD QLPSSSDGSQ 910 920 930 940 950 960 APARPPKPRP RRTAPEIHHR KPHGPEAALE NVDAKIAKLM GEGYAFEEVK RALEIAQNNV 970 980 EVARSILREF AFPPPVSPRL NL
	Isoform 2 [UniParc]. Checksum: AD8C574827907824	FASTA	830	91,524
	10 20 30 40 50 60 MLAEIKAIFP NGQFQGDNFR ITKADAAEFW RKFFGDKTIV PWKVFRQCLH EVHQISSGLE 70 80 90 100 110 120 AMALKSTIDL TCNDYISVFE FDIFTRLFQP WGSILRNWNF LAVTHPGYMA FLTYDEVKAR 130 140 150 160 170 180 LQKYSTKPGS YIFRLSCTRL GQWAIGYVTG DGNILQTIPH NKPLFQALID GSREGFYLYP 190 200 210 220 230 240 DGRSYNPDLT GLCEPTPHDH IKVTQEQYEL YCEMGSTFQL CKICAENDKD VKIEPCGHLM 250 260 270 280 290 300 CTSCLTAWQE SDGQGCPFCR CEIKGTEPII VDPFDPRDEG SRCCSIIDPF SIPMLDLDDD 310 320 330 340 350 360 DDREESLMMN RLASVRKCTD RQNSPVTSPG SSPLAQRRKP QPDPLQIPHL SLPPVPPRLD 370 380 390 400 410 420 LIQKGIVRSP CGSPTGSPKS SPCMVRKQDK PLPAPPPPLR DPPPPPERPP PIPPDNRLSR 430 440 450 460 470 480 HFHHGESVPS RDQPMPLEAW CPRDAFGTNQ VMGCRILGDG SPKPGVTANS SLNGRHSRMG 490 500 510 520 530 540 SEQVLMRKHR RHDLPSEGAK VFSNGHLATE EYDVPPRLSP PPPVTTLLPS IKCTGPLANC 550 560 570 580 590 600 LSEKTRDTVE DDDDEYKIPS SHPVSLNSQP SHCHNVKAPV RSCDNGHCIL NGTHGAPSEM 610 620 630 640 650 660 KKSNIPDLGI YLKGGGSDSA SDPVPLPPAR PPPRDSPKHG SSVNRTPSDY DLLIPPLGED 670 680 690 700 710 720 AFDALPPSLP PPPPPARHSL IEHSKPPGSS SRPSSGQDLF LLPSDPFFDP TSGQVPLPPA 730 740 750 760 770 780 RRAAGDSGKA NRASQDYDQL PSSSDGSQAP ARPPKPRPRR TAPEIHHRKP HGPEAALENV 790 800 810 820 830 DAKIAKLMGE GYAFEEVKRA LEIAQNNVEV ARSILREFAF PPPVSPRLNL

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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]	"Lineage-specific biology revealed by a finished genome assembly of the mouse." Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. , Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., Eichler E.E., Ponting C.P. PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract] 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]	"Negative regulation of lymphocyte activation and autoimmunity by the molecular adaptor Cbl-b." Bachmaier K., Krawczyk C., Kozieradzki I., Kong Y.-Y., Sasaki T., Oliveira-dos-Santos A., Mariathasan S., Bouchard D., Wakeham A., Itie A., Le J., Ohashi P.S., Sarosi I., Nishina H., Lipkowitz S., Penninger J.M. Nature 403:211-216(2000) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, INTERACTION WITH PIK3R1; LCP2; ZAP70; LCK; PLCG1 AND VAV1.
[5]	"Cbl-b regulates the CD28 dependence of T-cell activation." Chiang Y.J., Kole H.K., Brown K., Naramura M., Fukuhara S., Hu R.-J., Jang I.K., Gutkind J.S., Shevach E., Gu H. Nature 403:216-220(2000) [PubMed] [Europe PMC] [Abstract] 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]	"Essential role of the E3 ubiquitin ligase Cbl-b in T cell anergy induction." Jeon M.-S., Atfield A., Venuprasad K., Krawczyk C., Sarao R., Elly C., Yang C., Arya S., Bachmaier K., Su L., Bouchard D., Jones R., Gronski M., Ohashi P., Wada T., Bloom D., Fathman C.G., Liu Y.-C., Penninger J.M. Immunity 21:167-177(2004) [PubMed] [Europe PMC] [Abstract] 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, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	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.
IPI	IPI00266006. IPI00660894.
RefSeq	NP_001028410.1. NM_001033238.1.
UniGene	Mm.328206.
3D structure databases
ProteinModelPortal	Q3TTA7.
SMR	Q3TTA7. Positions 42-427, 929-972.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q3TTA7. 2 interactions.
STRING	10090.ENSMUSP00000023313.
PTM databases
PhosphoSite	Q3TTA7.
Proteomic databases
PaxDb	Q3TTA7.
PRIDE	Q3TTA7.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	208650.
KEGG	mmu:208650.
UCSC	uc007zlf.1. mouse.
Organism-specific databases
CTD	868.
MGI	MGI:2146430. Cblb.
Phylogenomic databases
eggNOG	NOG242251.
HOGENOM	HOG000294176.
HOVERGEN	HBG005255.
InParanoid	Q3TTA7.
KO	K04707.
OrthoDB	EOG4PG60J.
Enzyme and pathway databases
UniPathway	UPA00143.
Gene expression databases
CleanEx	MM_CBLB.
Genevestigator	Q3TTA7.
GermOnline	ENSMUSG00000022637. Mus musculus.
Family and domain databases
Gene3D	1.10.238.10. 1 hit. 1.20.930.20. 1 hit. 3.30.40.10. 1 hit. 3.30.505.10. 1 hit.
InterPro	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-like_dom. IPR000980. SH2. IPR000449. UBA/transl_elong_EF1B_N. IPR015940. UBA/transl_elong_EF1B_N_euk. IPR001841. Znf_RING. IPR013083. Znf_RING/FYVE/PHD. IPR017907. Znf_RING_CS. [Graphical view]
PANTHER	PTHR23007. PTHR23007. 1 hit.
Pfam	PF02262. Cbl_N. 1 hit. PF02761. Cbl_N2. 1 hit. PF02762. Cbl_N3. 1 hit. PF00627. UBA. 1 hit. [Graphical view]
SMART	SM00184. RING. 1 hit. SM00252. SH2. 1 hit. SM00165. UBA. 1 hit. [Graphical view]
SUPFAM	SSF47668. Adaptor_Cbl_N. 1 hit.
PROSITE	PS51506. CBL_PTB. 1 hit. PS50030. UBA. 1 hit. PS00518. ZF_RING_1. 1 hit. PS50089. ZF_RING_2. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	372367.
SOURCE	Search...

Entry information

Entry name

CBLB_MOUSE

Accession

Primary (citable) accession number: Q3TTA7
Secondary accession number(s): E9QMY2

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 7, 2006
Last sequence update:	July 27, 2011
Last modified:	May 1, 2013
This is version 83 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program