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Protein Page:
LAMB1 (human)
p Phosphorylation
a Acetylation
m Methylation
m1 Mono-methylation
m2 Di-methylation
m3 Tri-methylation
u Ubiquitination
s Sumoylation
n Neddylation
gl O-GlcNAc
ga O-GalNAc
h Palmitoylation
ad Adenylylation
sn S-Nitrosylation
ca Caspase cleavage

Overview
LAMB1 Binding to cells via a high affinity receptor, laminin is thought to mediate the attachment, migration and organization of cells into tissues during embryonic development by interacting with other extracellular matrix components. Note: This description may include information from UniProtKB.
Protein type: Secreted; Motility/polarity/chemotaxis; Secreted, signal peptide
Cellular Component: extracellular matrix; extracellular space; laminin-8 complex; laminin-1 complex; laminin-2 complex; perinuclear region of cytoplasm; laminin-10 complex; extracellular region; basement membrane
Molecular Function: integrin binding; enzyme binding; extracellular matrix structural constituent; structural molecule activity; glycosphingolipid binding
Biological Process: odontogenesis; axon guidance; cell migration; negative regulation of cell adhesion; cell adhesion; embryo implantation; positive regulation of epithelial cell proliferation; neurite development; positive regulation of cell migration
Reference #:  P07942 (UniProtKB)
Alt. Names/Synonyms: CLM; cutis laxa with marfanoid phenotype; LAMB1; Laminin B1 chain; Laminin subunit beta-1; laminin, beta 1; Laminin-1 subunit beta; Laminin-10 subunit beta; Laminin-12 subunit beta; Laminin-2 subunit beta; Laminin-6 subunit beta; Laminin-8 subunit beta; MGC142015
Gene Symbols: LAMB1
Molecular weight: 198,038 Da
Basal Isoelectric point: 4.83  Predict pI for various phosphorylation states
Select Structure to View Below

LAMB1

Protein Structure Not Found.


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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

► Hide Isoforms
 
0 1 S154-p AMLIERSsDFGKTWG
0 1 K215-u RALDPAFkIEDPysP
0 1 Y220-p AFkIEDPysPRIQNL
0 1 S221-p FkIEDPysPRIQNLL
0 1 T231-p IQNLLKItNLRIKFV
0 1 T242-p IKFVKLHtLGDNLLD
0 1 S250 LGDNLLDSRMEIREK
0 1 T369-p CDDCQHNtMGRNCEQ
0 1 - gap
0 1 S1222 PYRETVDSVERKVSE
0 2 K1310-u AEQLEFIkNSDIRGA
0 1 S1365-p DVMMEREsQFKEKQE
0 1 T1435-ga PGCGGLVtVAHNAWQ
0 1 S1453 DLDQDVLSALAEVEQ
0 1 K1697 LDGELDEKYKKVENL
0 1 K1708 VENLIAKKTEESADA
0 2 S1735-p TLLAQANsKLQLLKD
0 1 K1736 LLAQANsKLQLLKDL
  LAMB1 iso3  
S154 AMLIERSSDFGKTWG
K215 RALDPAFKIEDPYSP
Y220 AFKIEDPYSPRIQNL
S221 FKIEDPYSPRIQNLL
T231 IQNLLKITNLRIKFV
T242 IKFVKLHTLGDNLLD
S250 LGDNLLDSRMEIREK
T369 CDDCQHNTMGRNCEQ
S825-p CKRRFLKsIVMHSFR
- gap
- gap
- gap
- under review  
- gap
- under review  
- gap
- gap
- under review  
  mouse

 
S154 AMLIERSSDFGKAWG
K215 RALDPAFKIEDPYSP
Y220 AFKIEDPYSPRIQNL
S221 FKIEDPYSPRIQNLL
T231 IQNLLKITNLRIKFV
T242 IKFVKLHTLGDNLLD
S250-p LGDNLLDsRMEIREK
T369 CDNCQHNTMGRNCEQ
- gap
S1222-p PYRETVDsVEKKVNE
K1310-u AEQLEFIkNSDIQGA
S1365 DLMLERESPFKEQQE
T1435 PGCGGLVTVAHSAWQ
S1453-p DFDRDVLsALAEVEQ
K1697-a LDGELDEkYKKVESL
K1708-u VESLIAQkTEESADA
S1735 TLLAQANSkLQLLED
K1736-a LLAQANSkLQLLEDL
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