LAMB1

Protein identityUniProt · HPA

UniProt accession

P07942

Gene

LAMB1

Ensembl

ENSG00000091136

Chromosome

7

Canonical length

1786 aa

Protein class

Cancer-related genes, Disease related genes, Human disease related genes, Plasma proteins, Predicted intracellular proteins, Predicted secreted proteins

Secretome location

Secreted to extracellular matrix

OverviewNCBI Gene

Laminins, a family of extracellular matrix glycoproteins, are the major noncollagenous constituent of basement membranes. They have been implicated in a wide variety of biological processes including cell adhesion, differentiation, migration, signaling, neurite outgrowth and metastasis. Laminins are composed of 3 non identical chains: laminin alpha, beta and gamma (formerly A, B1, and B2, respectively) and they form a cruciform structure consisting of 3 short arms, each formed by a different chain, and a long arm composed of all 3 chains. Each laminin chain is a multidomain protein encoded by a distinct gene. Several isoforms of each chain have been described. Different alpha, beta and gamma chain isomers combine to give rise to different heterotrimeric laminin isoforms which are designated by Arabic numerals in the order of their discovery, i.e. alpha1beta1gamma1 heterotrimer is laminin 1. The biological functions of the different chains and trimer molecules are largely unknown, but some of the chains have been shown to differ with respect to their tissue distribution, presumably reflecting diverse functions in vivo. This gene encodes the beta chain isoform laminin, beta 1. The beta 1 chain has 7 structurally distinct domains which it shares with other beta chain isomers. The C-terminal helical region containing domains I and II are separated by domain alpha, domains III and V contain several EGF-like repeats, and domains IV and VI have a globular conformation. Laminin, beta 1 is expressed in most tissues that produce basement membranes, and is one of the 3 chains constituting laminin 1, the first laminin isolated from Engelbreth-Holm-Swarm (EHS) tumor. A sequence in the beta 1 chain that is involved in cell attachment, chemotaxis, and binding to the laminin receptor was identified and shown to have the capacity to inhibit metastasis. [provided by RefSeq, Aug 2011]

Canonical amino-acid sequenceUniProt

1786 residues, UniProt reviewed canonical sequence.

>P07942|LAMB1
     1  MGLLQLLAFS FLALCRARVR AQEPEFSYGC AEGSCYPATG DLLIGRAQKL SVTSTCGLHK
    61  PEPYCIVSHL QEDKKCFICN SQDPYHETLN PDSHLIENVV TTFAPNRLKI WWQSENGVEN
   121  VTIQLDLEAE FHFTHLIMTF KTFRPAAMLI ERSSDFGKTW GVYRYFAYDC EASFPGISTG
   181  PMKKVDDIIC DSRYSDIEPS TEGEVIFRAL DPAFKIEDPY SPRIQNLLKI TNLRIKFVKL
   241  HTLGDNLLDS RMEIREKYYY AVYDMVVRGN CFCYGHASEC APVDGFNEEV EGMVHGHCMC
   301  RHNTKGLNCE LCMDFYHDLP WRPAEGRNSN ACKKCNCNEH SISCHFDMAV YLATGNVSGG
   361  VCDDCQHNTM GRNCEQCKPF YYQHPERDIR DPNFCERCTC DPAGSQNEGI CDSYTDFSTG
   421  LIAGQCRCKL NVEGEHCDVC KEGFYDLSSE DPFGCKSCAC NPLGTIPGGN PCDSETGHCY
   481  CKRLVTGQHC DQCLPEHWGL SNDLDGCRPC DCDLGGALNN SCFAESGQCS CRPHMIGRQC
   541  NEVEPGYYFA TLDHYLYEAE EANLGPGVSI VERQYIQDRI PSWTGAGFVR VPEGAYLEFF
   601  IDNIPYSMEY DILIRYEPQL PDHWEKAVIT VQRPGRIPTS SRCGNTIPDD DNQVVSLSPG
   661  SRYVVLPRPV CFEKGTNYTV RLELPQYTSS DSDVESPYTL IDSLVLMPYC KSLDIFTVGG
   721  SGDGVVTNSA WETFQRYRCL ENSRSVVKTP MTDVCRNIIF SISALLHQTG LACECDPQGS
   781  LSSVCDPNGG QCQCRPNVVG RTCNRCAPGT FGFGPSGCKP CECHLQGSVN AFCNPVTGQC
   841  HCFQGVYARQ CDRCLPGHWG FPSCQPCQCN GHADDCDPVT GECLNCQDYT MGHNCERCLA
   901  GYYGDPIIGS GDHCRPCPCP DGPDSGRQFA RSCYQDPVTL QLACVCDPGY IGSRCDDCAS
   961  GYFGNPSEVG GSCQPCQCHN NIDTTDPEAC DKETGRCLKC LYHTEGEHCQ FCRFGYYGDA
  1021  LQQDCRKCVC NYLGTVQEHC NGSDCQCDKA TGQCLCLPNV IGQNCDRCAP NTWQLASGTG
  1081  CDPCNCNAAH SFGPSCNEFT GQCQCMPGFG GRTCSECQEL FWGDPDVECR ACDCDPRGIE
  1141  TPQCDQSTGQ CVCVEGVEGP RCDKCTRGYS GVFPDCTPCH QCFALWDVII AELTNRTHRF
  1201  LEKAKALKIS GVIGPYRETV DSVERKVSEI KDILAQSPAA EPLKNIGNLF EEAEKLIKDV
  1261  TEMMAQVEVK LSDTTSQSNS TAKELDSLQT EAESLDNTVK ELAEQLEFIK NSDIRGALDS
  1321  ITKYFQMSLE AEERVNASTT EPNSTVEQSA LMRDRVEDVM MERESQFKEK QEEQARLLDE
  1381  LAGKLQSLDL SAAAEMTCGT PPGASCSETE CGGPNCRTDE GERKCGGPGC GGLVTVAHNA
  1441  WQKAMDLDQD VLSALAEVEQ LSKMVSEAKL RADEAKQSAE DILLKTNATK EKMDKSNEEL
  1501  RNLIKQIRNF LTQDSADLDS IEAVANEVLK MEMPSTPQQL QNLTEDIRER VESLSQVEVI
  1561  LQHSAADIAR AEMLLEEAKR ASKSATDVKV TADMVKEALE EAEKAQVAAE KAIKQADEDI
  1621  QGTQNLLTSI ESETAASEET LFNASQRISE LERNVEELKR KAAQNSGEAE YIEKVVYTVK
  1681  QSAEDVKKTL DGELDEKYKK VENLIAKKTE ESADARRKAE MLQNEAKTLL AQANSKLQLL
  1741  KDLERKYEDN QRYLEDKAQE LARLEGEVRS LLKDISQKVA VYSTCL

LocalizationUniProt · AlphaFold · HPA

Whether an antibody against LAMB1 can act on the native protein depends on physical access: surface and secreted proteins are reachable by circulating antibodies, intracellular proteins usually are not.

Antibody reachability

Secreted

Secreted

Yes

Transmembrane segments

0

Mean surface accessibility (rSASA)

0.35

Highest tissue expression

145 nTPM

Expression across tissuesHPA

DiseaseUniProt · ClinVar · IEDB · PubMed

Four sources answering four different questions about LAMB1.

Disease | AllUniProt

Conditions LAMB1 is implicated in, by any mechanism.

• Lissencephaly 5 (LIS5) MIM:615191

Disease | GeneticClinVar

45 pathogenic / likely-pathogenic of 1,140 ClinVar records.

Conditions with pathogenic or likely-pathogenic variants.

• Cobblestone lissencephaly without muscular or ocular involvement
• Leukoencephalopathy without lacunae, adult-onset
• Classic lissencephaly
• Intellectual disability
• Acute myeloid leukemia

Genetic constraint and essentialitygnomAD · DepMap

Does the body need this protein intact? Low LOEUF or a strong DepMap dependency means loss or blockade of the protein is likely to be felt.

gnomAD LOEUF (loss-of-function intolerance)

0.64

gnomAD pLI

0

gnomAD missense Z

0.54

DepMap mean gene effect

0.01

DepMap dependency class

selective

Cancer expressionTCGA

Across TCGA tumor cohorts, this protein is over-expressed in roughly 5% of surveyed tumor types (aggregate summary; per-cohort expression, alteration, and survival load in the interactive view).

OntologyGO

Biological processes

• cell adhesion
• embryo implantation
• endodermal cell differentiation
• negative regulation of cell adhesion
• neuron projection development
• odontogenesis
• positive regulation of cell adhesion
• positive regulation of cell migration
• positive regulation of epithelial cell proliferation
• positive regulation of integrin-mediated signaling pathway
• positive regulation of muscle cell differentiation
• regulation of basement membrane organization
• regulation of cell adhesion
• regulation of cell migration
• regulation of embryonic development
• signal transduction
• substrate adhesion-dependent cell spreading
• neuronal-glial interaction involved in cerebral cortex radial glia guided migration

Molecular functions

• enzyme binding
• extracellular matrix structural constituent
• glycosphingolipid binding
• integrin binding
• structural molecule activity

Cellular components

• basement membrane
• endoplasmic reticulum lumen
• extracellular exosome
• extracellular matrix
• extracellular region
• extracellular space
• laminin-1 complex
• laminin-10 complex
• laminin-2 complex
• nucleus
• perinuclear region of cytoplasm
• protein complex involved in cell-matrix adhesion
• laminin-8 complex

Protein domainsUniProt · Pfam · InterPro

• EGF-like domain
• Laminin-type EGF domain
• Laminin, N-terminal
• Laminin IV type B
• Laminin/Netrin Extracellular Matrix
• LAMB1/2/3/4, helical domain
• Laminin/attractin/netrin-like, EGF domain
• Laminin EGF domain
• Laminin N-terminal (Domain VI)
• Laminin IV type B domain
• LAMB1-4 helical domain
• Laminin/attractin EGF domain

KeywordsUniProt

• Basement membrane
• Cell adhesion
• Coiled coil
• Disulfide bond
• Extracellular matrix
• Glycoprotein
• Laminin EGF-like domain
• Lissencephaly
• Phosphoprotein
• Repeat
• Secreted
• Signal

InteractionsUniProt · HPA

Protein binding partners of LAMB1 in the human serome: UniProt-annotated complex subunits plus reported interactors. Each links to its own Seroatlas record.

• ITGB1
• FBXO6