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Protein Page:
LAB (human)
p Phosphorylation
ac Acetylation
me Methylation
m1 Mono-methylation
m2 Di-methylation
m3 Tri-methylation
ub Ubiquitination
sm Sumoylation
ne Neddylation
gl O-GlcNAc
ga O-GalNAc
pa Palmitoylation
ad Adenylylation
sn S-Nitrosylation
ca Caspase cleavage
sc Succinylation

Overview
LAB linker for activation of B cells (LAB) is an adaptor protein. B cell antigen receptor signaling leads to its phosphorylation and interaction with the adaptor protein Grb2. Decreased expression leads to a reduction in BCR-mediated calcium flux and Erk activation. Localized to lipid rafts. Note: This description may include information from UniProtKB.
Protein type: Membrane protein, integral; Adaptor/scaffold
Cellular Component: mast cell granule; plasma membrane; integral to membrane; lipid raft
Molecular Function: protein binding; SH2 domain binding
Biological Process: B cell receptor signaling pathway; B cell activation; calcium-mediated signaling; innate immune response; mast cell degranulation
Reference #:  Q9GZY6 (UniProtKB)
Alt. Names/Synonyms: HSPC046; LAB; LAT2; linker for activation of B cells; Linker for activation of B-cells; linker for activation of T cells family, member 2; Linker for activation of T-cells family member 2; Membrane-associated adapter molecule; non-T cell activation linker; Non-T-cell activation linker; NTAL; WBS15; WBSCR15; WBSCR5; Williams-Beuren syndrome chromosomal region 15 protein; Williams-Beuren syndrome chromosomal region 5 protein; Williams-Beuren syndrome chromosome region 15; Williams-Beuren syndrome chromosome region 5; WSCR5
Gene Symbols: LAT2
Molecular weight: 26,550 Da
Basal Isoelectric point: 4.69  Predict pI for various phosphorylation states
Protein-Specific Antibodies or siRNAs from Cell Signaling Technology® Total Proteins
Select Structure to View Below

LAB

Protein Structure Not Found.


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Sites Implicated In
cell differentiation, altered: Y136‑p, Y193‑p, Y233‑p
molecular association, regulation: Y136‑p, Y193‑p, Y233‑p

Modification Sites and Domains Show Modification Legend
Click here to view phosphorylation modifications only

Modification Sites in Parent Protein, Orthologs, and Isoforms Show Modification Legend
 

Show Multiple Sequence Alignment


 SS 

SS: The number of records in which this modification site was determined using site-specific methods. SS methods include amino acid sequencing, site-directed mutagenesis, modification site-specific antibodies, specific MS strategies, etc.


 MS 

MS: The number of records in which this modification site was assigned using ONLY proteomic discovery-mode mass spectrometry.


       human

 
1 7 Y40-p AKRSEKIyQQRsLRE
0 26 S44-p EKIyQQRsLREDQQs
0 29 S51-p sLREDQQsFTGsRty
0 1 S55-p DQQsFTGsRtysLVG
0 1 T57-p QsFTGsRtysLVGQA
1 22 Y58-p sFTGsRtysLVGQAW
0 13 S59-p FTGsRtysLVGQAWP
0 2 - gap
0 2 K77-ub ADMAPTRkDkLLQFy
0 6 K79-ub MAPTRkDkLLQFyPS
1 4 Y84-p kDkLLQFyPSLEDPA
0 3 S92 PSLEDPASSRyQNFS
2 5 Y95-p EDPASSRyQNFSkGS
0 2 K100-ub SRyQNFSkGSRHGSE
1 11 Y110-p RHGSEEAyIDPIAME
2 19 Y118-p IDPIAMEyyNWGRFS
1 14 Y119-p DPIAMEyyNWGRFSk
0 1 K126-ub yNWGRFSkPPEDDDA
0 29 S135-p PEDDDANsyENVLIC
3 175 Y136-p EDDDANsyENVLICK
0 1 S183-p SGLCPSAsPEEDEEs
0 2 S190-p sPEEDEEsEDyQNsA
3 157 Y193-p EDEEsEDyQNsAsIH
0 2 S196-p EsEDyQNsAsIHQWR
0 1 S198-p EDyQNsAsIHQWREs
0 1 S205-p sIHQWREsRKVMGQL
3 7 Y233-p EEDGEPDyVNGEVAA
  mouse

 
Y41-p VKRNEKIyEQRNRQE
N45 EKIyEQRNRQENAQS
S52 NRQENAQSSAAAQTy
A56 NAQSSAAAQTysLAR
T58 QSSAAAQTysLARQV
Y59-p SSAAAQTysLARQVW
S60-p SAAAQTysLARQVWP
S78-p MDTAPNKsFERKNKM
K82 PNKsFERKNKMLFSH
K84 KsFERKNKMLFSHLE
F87 ERKNKMLFSHLEGPE
S95-p SHLEGPEsPRyQNFY
Y98-p EGPEsPRyQNFYKGS
K103 PRyQNFYKGSNQEPD
Y113 NQEPDAAYVDPIPTN
Y121-p VDPIPTNyYNWGCFQ
Y122 DPIPTNyYNWGCFQK
K129 YNWGCFQKPSEDDDS
S138 SEDDDSNSyENVLVC
Y139-p EDDDSNSyENVLVCK
- gap
F157 PESGVEDFEDyQNSV
Y160-p GVEDFEDyQNSVSIH
S163 DFEDyQNSVSIHQWR
S165 EDyQNSVSIHQWRES
S172 SIHQWRESKRTMGAP
Y192-p SPDEEPDyVNGDVAA
  rat

 
Y42 VKRNEKIYEQRNQQE
N46 EKIYEQRNQQENEQS
S53 NQQENEQSVASSQTY
S57 NEQSVASSQTYSLAR
T59 QSVASSQTYSLARPV
Y60 SVASSQTYSLARPVR
S61 VASSQTYSLARPVRT
S79 MDAASNKSFERKNKL
K83 SNKSFERKNKLLFSH
K85 KSFERKNKLLFSHLE
F88 ERKNKLLFSHLEGPE
S96 SHLEGPESPRYQNFY
Y99 EGPESPRYQNFYKGS
K104 PRYQNFYKGSRRESD
Y114 RRESDAAYVDPIPTD
Y122 VDPIPTDYYNWGCFQ
Y123 DPIPTDYYNWGCFQK
K130 YNWGCFQKPPEDNDS
S139 PEDNDSNSYENVLIC
Y140 EDNDSNSYENVLICK
- gap
S158 PESGTEESEDYQNSV
Y161 GTEESEDYQNSVSIL
S164 ESEDYQNSVSILQWR
S166 EDYQNSVSILQWRES
S173 SILQWRESKRTMGAR
Y193 SPDEEPDYVNGDVAT
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