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Protein

E3 ubiquitin-protein ligase CBL-B

Gene

CBLB

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: 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: protein ubiquitination

This protein is involved in the pathway protein ubiquitination, which is part of Protein modification.
View all proteins of this organism that are known to be involved in the pathway protein ubiquitination and in Protein modification.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei286PhosphotyrosineBy similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Calcium bindingi219 – 232PROSITE-ProRule annotationAdd BLAST14
Zinc fingeri373 – 412RING-typePROSITE-ProRule annotationAdd BLAST40

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Ligase

Keywords - Biological processi

Ubl conjugation pathway

Keywords - Ligandi

Calcium, Metal-binding, Zinc

Enzyme and pathway databases

BioCyciZFISH:ENSG00000114423-MONOMER.
BRENDAi6.3.2.19. 2681.
ReactomeiR-HSA-983168. Antigen processing: Ubiquitination & Proteasome degradation.
R-HSA-983695. Antigen activates B Cell Receptor (BCR) leading to generation of second messengers.
SignaLinkiQ13191.
SIGNORiQ13191.
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
RING finger protein 56
SH3-binding protein CBL-B
Signal transduction protein CBL-B
Gene namesi
Name:CBLB
Synonyms:RNF56
ORF Names:Nbla00127
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 3

Organism-specific databases

HGNCiHGNC:1542. CBLB.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi298G → E: Inhibits interaction with SYK. No effect on E3 activity. 2 Publications1
Mutagenesisi363Y → E: Decreases affinity for E2 ubiquitin-conjugating enzymes. 1 Publication1
Mutagenesisi373C → A: Abolishes E3 activity but does not affect binding to substrates. 2 Publications1
Mutagenesisi665Y → F: Slightly inhibits interaction with CRKL. Abolishes interaction with CRKL; when associated with F-709. 1 Publication1
Mutagenesisi709Y → F: Inhibits interaction with CRKL. Abolishes interaction with CRKL; when associated with F-665. 1 Publication1
Mutagenesisi904R → A: No effect on interaction with CD2AP. Reduced interaction with SH3KBP1. Strongly reduced interaction with SH3KBP1; when associated with A-911. 2 Publications1
Mutagenesisi907K → A: No effect on interaction with SH3KBP1. Reduced interaction with CD2AP. Strongly reduced interaction with CD2AP; when associated with A-911. 1 Publication1
Mutagenesisi911R → 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. 2 Publications1
Mutagenesisi937A → E: Loss of ubiquitin binding. Reduced levels of tyrosine phosphorylation. 1 Publication1
Mutagenesisi940M → A: Loss of ubiquitin binding. Reduced levels of tyrosine phosphorylation. 1 Publication1
Mutagenesisi943 – 944GY → AQ: Abolishes interaction with ubiquitinated proteins. 1 Publication2
Mutagenesisi946F → A: Loss of ubiquitin binding. Reduced levels of tyrosine phosphorylation. 1 Publication1
Mutagenesisi966I → E: Interferes with dimerization. Reduced E3 ubiquitin-protein ligase activity. Reduced levels of tyrosine phosphorylation. 1 Publication1
Mutagenesisi967L → A: No effect on interaction with ubiquitinated proteins. 1 Publication1

Organism-specific databases

DisGeNETi868.
OpenTargetsiENSG00000114423.
PharmGKBiPA26116.

Polymorphism and mutation databases

BioMutaiCBLB.
DMDMi88911265.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000558601 – 982E3 ubiquitin-protein ligase CBL-BAdd BLAST982

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei282Phosphoserine; by PKC/PRKCQ1 Publication1
Modified residuei363Phosphotyrosine1 Publication1
Modified residuei476PhosphoserineBy similarity1
Modified residuei480PhosphoserineBy similarity1
Modified residuei484PhosphoserineBy similarity1
Modified residuei521PhosphoserineCombined sources1
Modified residuei525PhosphoserineCombined sources1
Modified residuei529PhosphoserineCombined sources1
Modified residuei634PhosphoserineBy similarity1
Modified residuei665Phosphotyrosine1 Publication1
Modified residuei709Phosphotyrosine1 Publication1
Modified residuei889PhosphotyrosineBy similarity1

Post-translational modificationi

Phosphorylated on tyrosine and serine residues upon TCR or BCR activation, and upon various types of cell stimulation.4 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

EPDiQ13191.
MaxQBiQ13191.
PaxDbiQ13191.
PeptideAtlasiQ13191.
PRIDEiQ13191.

PTM databases

iPTMnetiQ13191.
PhosphoSitePlusiQ13191.

Expressioni

Tissue specificityi

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).2 Publications

Gene expression databases

BgeeiENSG00000114423.
CleanExiHS_CBLB.
ExpressionAtlasiQ13191. baseline and differential.
GenevisibleiQ13191. HS.

Organism-specific databases

HPAiHPA018327.
HPA019880.

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).10 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
ASAP1Q9ULH12EBI-744027,EBI-346622
CD2APQ9Y5K611EBI-744027,EBI-298152
CRKP461084EBI-744027,EBI-886
CRKLP461094EBI-744027,EBI-910
FYNP06241-33EBI-744027,EBI-10691738
GLRX3O760033EBI-744027,EBI-374781
GORASP2Q9H8Y86EBI-744027,EBI-739467
GRB2P6299310EBI-744027,EBI-401755
NCK1P163334EBI-744027,EBI-389883
NCK2O436394EBI-744027,EBI-713635
SH3KBP1Q96B9721EBI-744027,EBI-346595
UBASH3BQ8TF425EBI-744027,EBI-1380492

GO - Molecular functioni

Protein-protein interaction databases

BioGridi107316. 60 interactors.
DIPiDIP-33091N.
IntActiQ13191. 37 interactors.
MINTiMINT-256380.
STRINGi9606.ENSP00000264122.

Structurei

Secondary structure

1982
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi43 – 60Combined sources18
Helixi63 – 65Combined sources3
Beta strandi69 – 72Combined sources4
Helixi74 – 91Combined sources18
Helixi95 – 102Combined sources8
Helixi105 – 128Combined sources24
Helixi129 – 133Combined sources5
Helixi138 – 160Combined sources23
Helixi162 – 164Combined sources3
Helixi168 – 170Combined sources3
Helixi176 – 186Combined sources11
Beta strandi190 – 193Combined sources4
Helixi194 – 204Combined sources11
Helixi210 – 220Combined sources11
Beta strandi225 – 229Combined sources5
Helixi230 – 239Combined sources10
Helixi243 – 245Combined sources3
Helixi246 – 253Combined sources8
Beta strandi260 – 263Combined sources4
Helixi266 – 273Combined sources8
Helixi274 – 276Combined sources3
Beta strandi282 – 287Combined sources6
Beta strandi289 – 291Combined sources3
Beta strandi295 – 300Combined sources6
Beta strandi306 – 309Combined sources4
Beta strandi312 – 314Combined sources3
Helixi316 – 325Combined sources10
Helixi332 – 334Combined sources3
Helixi342 – 344Combined sources3
Beta strandi352 – 354Combined sources3
Helixi357 – 364Combined sources8
Turni365 – 367Combined sources3
Beta strandi370 – 372Combined sources3
Turni374 – 376Combined sources3
Beta strandi377 – 380Combined sources4
Beta strandi383 – 386Combined sources4
Helixi394 – 402Combined sources9
Turni409 – 411Combined sources3
Beta strandi417 – 420Combined sources4
Beta strandi422 – 424Combined sources3
Helixi933 – 941Combined sources9
Helixi946 – 955Combined sources10
Turni956 – 958Combined sources3
Helixi960 – 970Combined sources11

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2AK5X-ray1.85D904-911[»]
2BZ8X-ray2.00C902-912[»]
2DO6NMR-A/B931-970[»]
2J6FX-ray1.70C902-912[»]
2JNHNMR-A926-971[»]
2LDRNMR-A351-426[»]
2OOAX-ray1.56A/B924-973[»]
2OOBX-ray1.90A924-973[»]
3PFVX-ray2.27A/B38-344[»]
3VGOX-ray3.10A/B/C39-426[»]
3ZNIX-ray2.21A/E/I/M36-427[»]
ProteinModelPortaliQ13191.
SMRiQ13191.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ13191.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini35 – 343Cbl-PTBPROSITE-ProRule annotationAdd BLAST309
Domaini931 – 970UBAPROSITE-ProRule annotationAdd BLAST40

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni35 – 1674HAdd BLAST133
Regioni168 – 240EF-hand-likeAdd BLAST73
Regioni241 – 343SH2-likeAdd BLAST103
Regioni344 – 372LinkerAdd BLAST29
Regioni543 – 568Interaction with VAV11 PublicationAdd BLAST26
Regioni891 – 927Interaction with SH3KBP11 PublicationAdd BLAST37

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi477 – 925Pro-richAdd BLAST449

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.

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)DescriptionActionsGraphical viewLength
Zinc fingeri373 – 412RING-typePROSITE-ProRule annotationAdd BLAST40

Keywords - Domaini

Repeat, Zinc-finger

Phylogenomic databases

eggNOGiKOG1785. Eukaryota.
ENOG410YDNH. LUCA.
GeneTreeiENSGT00390000011617.
HOVERGENiHBG005255.
InParanoidiQ13191.
KOiK04707.
OMAiCCSIIDP.
OrthoDBiEOG091G0GPE.
PhylomeDBiQ13191.
TreeFamiTF314210.

Family and domain databases

CDDicd09920. SH2_Cbl-b_TKB. 1 hit.
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.
IPR001841. Znf_RING.
IPR013083. Znf_RING/FYVE/PHD.
IPR017907. Znf_RING_CS.
[Graphical view]
PANTHERiPTHR23007. PTHR23007. 2 hits.
PfamiPF02262. Cbl_N. 1 hit.
PF02761. Cbl_N2. 1 hit.
PF02762. Cbl_N3. 1 hit.
[Graphical view]
SMARTiSM00184. RING. 1 hit.
SM00165. UBA. 1 hit.
[Graphical view]
SUPFAMiSSF47473. SSF47473. 1 hit.
SSF47668. 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 (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform Long (identifier: Q13191-1) [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 PFGMPMLDLD
460 470 480 490 500
DDDDREESLM MNRLANVRKC TDRQNSPVTS PGSSPLAQRR KPQPDPLQIP
510 520 530 540 550
HLSLPPVPPR LDLIQKGIVR SPCGSPTGSP KSSPCMVRKQ DKPLPAPPPP
560 570 580 590 600
LRDPPPPPPE RPPPIPPDNR LSRHIHHVES VPSRDPPMPL EAWCPRDVFG
610 620 630 640 650
TNQLVGCRLL GEGSPKPGIT ASSNVNGRHS RVGSDPVLMR KHRRHDLPLE
660 670 680 690 700
GAKVFSNGHL GSEEYDVPPR LSPPPPVTTL LPSIKCTGPL ANSLSEKTRD
710 720 730 740 750
PVEEDDDEYK IPSSHPVSLN SQPSHCHNVK PPVRSCDNGH CMLNGTHGPS
760 770 780 790 800
SEKKSNIPDL SIYLKGDVFD SASDPVPLPP ARPPTRDNPK HGSSLNRTPS
810 820 830 840 850
DYDLLIPPLG EDAFDALPPS LPPPPPPARH SLIEHSKPPG SSSRPSSGQD
860 870 880 890 900
LFLLPSDPFV DLASGQVPLP PARRLPGENV KTNRTSQDYD QLPSCSDGSQ
910 920 930 940 950
APARPPKPRP RRTAPEIHHR KPHGPEAALE NVDAKIAKLM GEGYAFEEVK
960 970 980
RALEIAQNNV EVARSILREF AFPPPVSPRL NL
Length:982
Mass (Da):109,450
Last modified:February 7, 2006 - v2
Checksum:iB4E307D31B9F0779
GO
Isoform Truncated 1 (identifier: Q13191-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     812-982: Missing.

Show »
Length:811
Mass (Da):90,883
Checksum:iA63D22F7C9C677DB
GO
Isoform Truncated 2 (identifier: Q13191-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     767-770: DVFD → TYRI
     771-982: Missing.

Show »
Length:770
Mass (Da):86,582
Checksum:iDEE458DFFEE1AF2F
GO

Sequence cautioni

The sequence BAE45748 differs from that shown. Reason: Erroneous termination at position 904. Translated as Arg.Curated
The sequence CAH56175 differs from that shown. Probable cloning artifact.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti210G → S in AAB09291 (PubMed:7784085).Curated1
Sequence conflicti210G → S in AAB09292 (PubMed:7784085).Curated1
Sequence conflicti210G → S in AAB09293 (PubMed:7784085).Curated1
Sequence conflicti911R → C in CAH56175 (PubMed:17974005).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_025303584R → K.1 PublicationCorresponds to variant rs17853100dbSNPEnsembl.1
Natural variantiVAR_039241883N → D.Corresponds to variant rs35835913dbSNPEnsembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_005730767 – 770DVFD → TYRI in isoform Truncated 2. 1 Publication4
Alternative sequenceiVSP_005731771 – 982Missing in isoform Truncated 2. 1 PublicationAdd BLAST212
Alternative sequenceiVSP_005729812 – 982Missing in isoform Truncated 1. 1 PublicationAdd BLAST171

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U26710 mRNA. Translation: AAB09291.1.
U26711 mRNA. Translation: AAB09292.1.
U26712 mRNA. Translation: AAB09293.1.
DQ349203 mRNA. Translation: ABC86700.1.
AK292792 mRNA. Translation: BAF85481.1.
AC016138 Genomic DNA. No translation available.
CH471052 Genomic DNA. Translation: EAW79752.1.
CH471052 Genomic DNA. Translation: EAW79753.1.
CH471052 Genomic DNA. Translation: EAW79754.1.
BC032851 mRNA. Translation: AAH32851.1.
AB075490 mRNA. Translation: BAE45748.1. Sequence problems.
BX537484 mRNA. Translation: CAH56175.1. Sequence problems.
CCDSiCCDS2948.1. [Q13191-1]
RefSeqiNP_001308717.1. NM_001321788.1. [Q13191-1]
NP_733762.2. NM_170662.4. [Q13191-1]
XP_011511559.1. XM_011513257.1. [Q13191-1]
UniGeneiHs.430589.

Genome annotation databases

EnsembliENST00000264122; ENSP00000264122; ENSG00000114423. [Q13191-1]
ENST00000403724; ENSP00000384816; ENSG00000114423. [Q13191-3]
GeneIDi868.
KEGGihsa:868.
UCSCiuc003dwc.4. human. [Q13191-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U26710 mRNA. Translation: AAB09291.1.
U26711 mRNA. Translation: AAB09292.1.
U26712 mRNA. Translation: AAB09293.1.
DQ349203 mRNA. Translation: ABC86700.1.
AK292792 mRNA. Translation: BAF85481.1.
AC016138 Genomic DNA. No translation available.
CH471052 Genomic DNA. Translation: EAW79752.1.
CH471052 Genomic DNA. Translation: EAW79753.1.
CH471052 Genomic DNA. Translation: EAW79754.1.
BC032851 mRNA. Translation: AAH32851.1.
AB075490 mRNA. Translation: BAE45748.1. Sequence problems.
BX537484 mRNA. Translation: CAH56175.1. Sequence problems.
CCDSiCCDS2948.1. [Q13191-1]
RefSeqiNP_001308717.1. NM_001321788.1. [Q13191-1]
NP_733762.2. NM_170662.4. [Q13191-1]
XP_011511559.1. XM_011513257.1. [Q13191-1]
UniGeneiHs.430589.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2AK5X-ray1.85D904-911[»]
2BZ8X-ray2.00C902-912[»]
2DO6NMR-A/B931-970[»]
2J6FX-ray1.70C902-912[»]
2JNHNMR-A926-971[»]
2LDRNMR-A351-426[»]
2OOAX-ray1.56A/B924-973[»]
2OOBX-ray1.90A924-973[»]
3PFVX-ray2.27A/B38-344[»]
3VGOX-ray3.10A/B/C39-426[»]
3ZNIX-ray2.21A/E/I/M36-427[»]
ProteinModelPortaliQ13191.
SMRiQ13191.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi107316. 60 interactors.
DIPiDIP-33091N.
IntActiQ13191. 37 interactors.
MINTiMINT-256380.
STRINGi9606.ENSP00000264122.

PTM databases

iPTMnetiQ13191.
PhosphoSitePlusiQ13191.

Polymorphism and mutation databases

BioMutaiCBLB.
DMDMi88911265.

Proteomic databases

EPDiQ13191.
MaxQBiQ13191.
PaxDbiQ13191.
PeptideAtlasiQ13191.
PRIDEiQ13191.

Protocols and materials databases

DNASUi868.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000264122; ENSP00000264122; ENSG00000114423. [Q13191-1]
ENST00000403724; ENSP00000384816; ENSG00000114423. [Q13191-3]
GeneIDi868.
KEGGihsa:868.
UCSCiuc003dwc.4. human. [Q13191-1]

Organism-specific databases

CTDi868.
DisGeNETi868.
GeneCardsiCBLB.
H-InvDBHIX0003518.
HGNCiHGNC:1542. CBLB.
HPAiHPA018327.
HPA019880.
MIMi604491. gene.
neXtProtiNX_Q13191.
OpenTargetsiENSG00000114423.
PharmGKBiPA26116.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG1785. Eukaryota.
ENOG410YDNH. LUCA.
GeneTreeiENSGT00390000011617.
HOVERGENiHBG005255.
InParanoidiQ13191.
KOiK04707.
OMAiCCSIIDP.
OrthoDBiEOG091G0GPE.
PhylomeDBiQ13191.
TreeFamiTF314210.

Enzyme and pathway databases

UniPathwayiUPA00143.
BioCyciZFISH:ENSG00000114423-MONOMER.
BRENDAi6.3.2.19. 2681.
ReactomeiR-HSA-983168. Antigen processing: Ubiquitination & Proteasome degradation.
R-HSA-983695. Antigen activates B Cell Receptor (BCR) leading to generation of second messengers.
SignaLinkiQ13191.
SIGNORiQ13191.

Miscellaneous databases

ChiTaRSiCBLB. human.
EvolutionaryTraceiQ13191.
GeneWikiiCBLB_(gene).
GenomeRNAii868.
PROiQ13191.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000114423.
CleanExiHS_CBLB.
ExpressionAtlasiQ13191. baseline and differential.
GenevisibleiQ13191. HS.

Family and domain databases

CDDicd09920. SH2_Cbl-b_TKB. 1 hit.
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.
IPR001841. Znf_RING.
IPR013083. Znf_RING/FYVE/PHD.
IPR017907. Znf_RING_CS.
[Graphical view]
PANTHERiPTHR23007. PTHR23007. 2 hits.
PfamiPF02262. Cbl_N. 1 hit.
PF02761. Cbl_N2. 1 hit.
PF02762. Cbl_N3. 1 hit.
[Graphical view]
SMARTiSM00184. RING. 1 hit.
SM00165. UBA. 1 hit.
[Graphical view]
SUPFAMiSSF47473. SSF47473. 1 hit.
SSF47668. 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]
ProtoNetiSearch...

Entry informationi

Entry nameiCBLB_HUMAN
AccessioniPrimary (citable) accession number: Q13191
Secondary accession number(s): A8K9S7
, B7WNM4, Q13192, Q13193, Q3LIC0, Q63Z43, Q8IVC5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: February 7, 2006
Last modified: November 30, 2016
This is version 185 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
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.

Miscellaneousi

Miscellaneous

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

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 3
    Human chromosome 3: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  6. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  7. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.