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P07942 (LAMB1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 152. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Laminin subunit beta-1
Alternative name(s):
Laminin B1 chain
Laminin-1 subunit beta
Laminin-10 subunit beta
Laminin-12 subunit beta
Laminin-2 subunit beta
Laminin-6 subunit beta
Laminin-8 subunit beta
Gene names
Name:LAMB1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1786 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Involved in the organization of the laminar architecture of cerebral cortex. It is probably required for the integrity of the basement membrane/glia limitans that serves as an anchor point for the endfeet of radial glial cells and as a physical barrier to migrating neurons. Radial glial cells play a central role in cerebral cortical development, where they act both as the proliferative unit of the cerebral cortex and a scaffold for neurons migrating toward the pial surface. Ref.8

Subunit structure

Laminin is a complex glycoprotein, consisting of three different polypeptide chains (alpha, beta, gamma), which are bound to each other by disulfide bonds into a cross-shaped molecule comprising one long and three short arms with globules at each end. Beta-1 is a subunit of laminin-1 (laminin-111 or EHS laminin), laminin-2 (laminin-211 or merosin), laminin-6 (laminin-311 or K-laminin), laminin-8 (laminin-411), laminin-10 (laminin-511) and laminin-12 (laminin-213).

Subcellular location

Secretedextracellular spaceextracellular matrixbasement membrane. Note: Major component.

Domain

The alpha-helical domains I and II are thought to interact with other laminin chains to form a coiled coil structure.

Domains VI and IV are globular.

Involvement in disease

Lissencephaly 5 (LIS5) [MIM:615191]: An autosomal recessive brain malformation characterized by cobblestone changes in the cortex, more severe in the posterior region, and subcortical band heterotopia. Affected individuals have hydrocephalus, seizures, and severely delayed psychomotor development.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.8

Sequence similarities

Contains 13 laminin EGF-like domains.

Contains 1 laminin IV type B domain.

Contains 1 laminin N-terminal domain.

Ontologies

Keywords
   Biological processCell adhesion
   Cellular componentBasement membrane
Extracellular matrix
Secreted
   Coding sequence diversityPolymorphism
   DiseaseLissencephaly
   DomainCoiled coil
Laminin EGF-like domain
Repeat
Signal
   PTMDisulfide bond
Glycoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processaxon guidance

Traceable author statement. Source: Reactome

cell adhesion

Traceable author statement PubMed 14557481. Source: HGNC

embryo implantation

Inferred from electronic annotation. Source: Ensembl

extracellular matrix disassembly

Traceable author statement. Source: Reactome

extracellular matrix organization

Traceable author statement. Source: Reactome

negative regulation of cell adhesion

Inferred from electronic annotation. Source: Ensembl

neuron projection development

Inferred from direct assay PubMed 15894315. Source: UniProtKB

neuronal-glial interaction involved in cerebral cortex radial glia guided migration

Inferred from mutant phenotype Ref.8. Source: UniProtKB

odontogenesis

Inferred from direct assay PubMed 15894315. Source: UniProtKB

positive regulation of cell migration

Inferred from direct assay PubMed 16289578. Source: UniProtKB

positive regulation of epithelial cell proliferation

Traceable author statement PubMed 14557481. Source: HGNC

substrate adhesion-dependent cell spreading

Inferred from direct assay PubMed 16236823. Source: BHF-UCL

   Cellular_componentbasement membrane

Inferred from direct assay PubMed 14557481PubMed 2099832. Source: UniProtKB

extracellular region

Traceable author statement. Source: Reactome

extracellular space

Inferred from direct assay PubMed 10964500. Source: UniProtKB

extracellular vesicular exosome

Inferred from direct assay PubMed 21362503. Source: UniProtKB

laminin-1 complex

Inferred from direct assay PubMed 16289578. Source: UniProtKB

laminin-10 complex

Inferred from direct assay PubMed 10964500PubMed 16289578. Source: UniProtKB

laminin-2 complex

Inferred from direct assay PubMed 16289578. Source: UniProtKB

laminin-8 complex

Inferred from direct assay PubMed 16289578. Source: UniProtKB

perinuclear region of cytoplasm

Inferred from sequence or structural similarity. Source: UniProtKB

   Molecular_functionextracellular matrix structural constituent

Inferred from direct assay PubMed 16289578. Source: HGNC

glycosphingolipid binding

Inferred from electronic annotation. Source: Ensembl

structural molecule activity

Non-traceable author statement PubMed 10842354. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2121
Chain22 – 17861765Laminin subunit beta-1
PRO_0000017065

Regions

Domain31 – 270240Laminin N-terminal
Domain271 – 33464Laminin EGF-like 1
Domain335 – 39763Laminin EGF-like 2
Domain398 – 45760Laminin EGF-like 3
Domain458 – 50952Laminin EGF-like 4
Domain510 – 54031Laminin EGF-like 5; truncated
Domain549 – 767219Laminin IV type B
Domain773 – 82048Laminin EGF-like 6
Domain821 – 86646Laminin EGF-like 7
Domain867 – 91650Laminin EGF-like 8
Domain917 – 97559Laminin EGF-like 9
Domain976 – 102752Laminin EGF-like 10
Domain1028 – 108356Laminin EGF-like 11
Domain1084 – 113148Laminin EGF-like 12
Domain1132 – 117847Laminin EGF-like 13
Region1179 – 1397219Domain II
Region1398 – 143033Domain alpha
Region1431 – 1786356Domain I
Coiled coil1216 – 1315100 Potential
Coiled coil1353 – 138836 Potential
Coiled coil1442 – 1781340 Potential

Amino acid modifications

Glycosylation1201N-linked (GlcNAc...) Potential
Glycosylation3561N-linked (GlcNAc...) Potential
Glycosylation5191N-linked (GlcNAc...) Potential
Glycosylation6771N-linked (GlcNAc...) Potential
Glycosylation10411N-linked (GlcNAc...) Potential
Glycosylation11951N-linked (GlcNAc...) Potential
Glycosylation12791N-linked (GlcNAc...) Ref.6 Ref.7
Glycosylation13361N-linked (GlcNAc...) Potential
Glycosylation13431N-linked (GlcNAc...) Potential
Glycosylation14871N-linked (GlcNAc...) Potential
Glycosylation15421N-linked (GlcNAc...) Potential
Disulfide bond271 ↔ 280 By similarity
Disulfide bond273 ↔ 298 By similarity
Disulfide bond300 ↔ 309 By similarity
Disulfide bond312 ↔ 332 By similarity
Disulfide bond335 ↔ 344 By similarity
Disulfide bond337 ↔ 362 By similarity
Disulfide bond365 ↔ 374 By similarity
Disulfide bond377 ↔ 395 By similarity
Disulfide bond398 ↔ 411 By similarity
Disulfide bond400 ↔ 426 By similarity
Disulfide bond428 ↔ 437 By similarity
Disulfide bond440 ↔ 455 By similarity
Disulfide bond458 ↔ 472 By similarity
Disulfide bond460 ↔ 479 By similarity
Disulfide bond481 ↔ 490 By similarity
Disulfide bond493 ↔ 507 By similarity
Disulfide bond510 ↔ 522 By similarity
Disulfide bond512 ↔ 529 By similarity
Disulfide bond531 ↔ 540 By similarity
Disulfide bond773 ↔ 785 By similarity
Disulfide bond775 ↔ 792 By similarity
Disulfide bond794 ↔ 803 By similarity
Disulfide bond806 ↔ 818 By similarity
Disulfide bond821 ↔ 833 By similarity
Disulfide bond823 ↔ 840 By similarity
Disulfide bond842 ↔ 851 By similarity
Disulfide bond854 ↔ 864 By similarity
Disulfide bond867 ↔ 876 By similarity
Disulfide bond869 ↔ 883 By similarity
Disulfide bond886 ↔ 895 By similarity
Disulfide bond898 ↔ 914 By similarity
Disulfide bond917 ↔ 933 By similarity
Disulfide bond919 ↔ 944 By similarity
Disulfide bond946 ↔ 955 By similarity
Disulfide bond958 ↔ 973 By similarity
Disulfide bond976 ↔ 990 By similarity
Disulfide bond978 ↔ 997 By similarity
Disulfide bond1000 ↔ 1009 By similarity
Disulfide bond1012 ↔ 1025 By similarity
Disulfide bond1028 ↔ 1040 By similarity
Disulfide bond1030 ↔ 1054 By similarity
Disulfide bond1056 ↔ 1065 By similarity
Disulfide bond1068 ↔ 1081 By similarity
Disulfide bond1084 ↔ 1096 By similarity
Disulfide bond1086 ↔ 1103 By similarity
Disulfide bond1105 ↔ 1114 By similarity
Disulfide bond1117 ↔ 1129 By similarity
Disulfide bond1132 ↔ 1144 By similarity
Disulfide bond1134 ↔ 1151 By similarity
Disulfide bond1153 ↔ 1162 By similarity
Disulfide bond1165 ↔ 1176 By similarity
Disulfide bond1179Interchain Probable
Disulfide bond1182Interchain Probable
Disulfide bond1785Interchain Probable

Natural variations

Natural variant3791P → S.
Corresponds to variant rs28750165 [ dbSNP | Ensembl ].
VAR_061349
Natural variant6701V → A.
Corresponds to variant rs20555 [ dbSNP | Ensembl ].
VAR_014698
Natural variant8601G → S.
Corresponds to variant rs35710474 [ dbSNP | Ensembl ].
VAR_032774
Natural variant10221Q → R. Ref.1 Ref.2 Ref.9
Corresponds to variant rs20556 [ dbSNP | Ensembl ].
VAR_014699

Experimental info

Sequence conflict14701L → V in AAA59487. Ref.5
Sequence conflict16961E → G in AAA59487. Ref.5

Sequences

Sequence LengthMass (Da)Tools
P07942 [UniParc].

Last modified January 11, 2011. Version 2.
Checksum: 8F8EF96E765B9A0D

FASTA1,786198,038
        10         20         30         40         50         60 
MGLLQLLAFS FLALCRARVR AQEPEFSYGC AEGSCYPATG DLLIGRAQKL SVTSTCGLHK 

        70         80         90        100        110        120 
PEPYCIVSHL QEDKKCFICN SQDPYHETLN PDSHLIENVV TTFAPNRLKI WWQSENGVEN 

       130        140        150        160        170        180 
VTIQLDLEAE FHFTHLIMTF KTFRPAAMLI ERSSDFGKTW GVYRYFAYDC EASFPGISTG 

       190        200        210        220        230        240 
PMKKVDDIIC DSRYSDIEPS TEGEVIFRAL DPAFKIEDPY SPRIQNLLKI TNLRIKFVKL 

       250        260        270        280        290        300 
HTLGDNLLDS RMEIREKYYY AVYDMVVRGN CFCYGHASEC APVDGFNEEV EGMVHGHCMC 

       310        320        330        340        350        360 
RHNTKGLNCE LCMDFYHDLP WRPAEGRNSN ACKKCNCNEH SISCHFDMAV YLATGNVSGG 

       370        380        390        400        410        420 
VCDDCQHNTM GRNCEQCKPF YYQHPERDIR DPNFCERCTC DPAGSQNEGI CDSYTDFSTG 

       430        440        450        460        470        480 
LIAGQCRCKL NVEGEHCDVC KEGFYDLSSE DPFGCKSCAC NPLGTIPGGN PCDSETGHCY 

       490        500        510        520        530        540 
CKRLVTGQHC DQCLPEHWGL SNDLDGCRPC DCDLGGALNN SCFAESGQCS CRPHMIGRQC 

       550        560        570        580        590        600 
NEVEPGYYFA TLDHYLYEAE EANLGPGVSI VERQYIQDRI PSWTGAGFVR VPEGAYLEFF 

       610        620        630        640        650        660 
IDNIPYSMEY DILIRYEPQL PDHWEKAVIT VQRPGRIPTS SRCGNTIPDD DNQVVSLSPG 

       670        680        690        700        710        720 
SRYVVLPRPV CFEKGTNYTV RLELPQYTSS DSDVESPYTL IDSLVLMPYC KSLDIFTVGG 

       730        740        750        760        770        780 
SGDGVVTNSA WETFQRYRCL ENSRSVVKTP MTDVCRNIIF SISALLHQTG LACECDPQGS 

       790        800        810        820        830        840 
LSSVCDPNGG QCQCRPNVVG RTCNRCAPGT FGFGPSGCKP CECHLQGSVN AFCNPVTGQC 

       850        860        870        880        890        900 
HCFQGVYARQ CDRCLPGHWG FPSCQPCQCN GHADDCDPVT GECLNCQDYT MGHNCERCLA 

       910        920        930        940        950        960 
GYYGDPIIGS GDHCRPCPCP DGPDSGRQFA RSCYQDPVTL QLACVCDPGY IGSRCDDCAS 

       970        980        990       1000       1010       1020 
GYFGNPSEVG GSCQPCQCHN NIDTTDPEAC DKETGRCLKC LYHTEGEHCQ FCRFGYYGDA 

      1030       1040       1050       1060       1070       1080 
LQQDCRKCVC NYLGTVQEHC NGSDCQCDKA TGQCLCLPNV IGQNCDRCAP NTWQLASGTG 

      1090       1100       1110       1120       1130       1140 
CDPCNCNAAH SFGPSCNEFT GQCQCMPGFG GRTCSECQEL FWGDPDVECR ACDCDPRGIE 

      1150       1160       1170       1180       1190       1200 
TPQCDQSTGQ CVCVEGVEGP RCDKCTRGYS GVFPDCTPCH QCFALWDVII AELTNRTHRF 

      1210       1220       1230       1240       1250       1260 
LEKAKALKIS GVIGPYRETV DSVERKVSEI KDILAQSPAA EPLKNIGNLF EEAEKLIKDV 

      1270       1280       1290       1300       1310       1320 
TEMMAQVEVK LSDTTSQSNS TAKELDSLQT EAESLDNTVK ELAEQLEFIK NSDIRGALDS 

      1330       1340       1350       1360       1370       1380 
ITKYFQMSLE AEERVNASTT EPNSTVEQSA LMRDRVEDVM MERESQFKEK QEEQARLLDE 

      1390       1400       1410       1420       1430       1440 
LAGKLQSLDL SAAAEMTCGT PPGASCSETE CGGPNCRTDE GERKCGGPGC GGLVTVAHNA 

      1450       1460       1470       1480       1490       1500 
WQKAMDLDQD VLSALAEVEQ LSKMVSEAKL RADEAKQSAE DILLKTNATK EKMDKSNEEL 

      1510       1520       1530       1540       1550       1560 
RNLIKQIRNF LTQDSADLDS IEAVANEVLK MEMPSTPQQL QNLTEDIRER VESLSQVEVI 

      1570       1580       1590       1600       1610       1620 
LQHSAADIAR AEMLLEEAKR ASKSATDVKV TADMVKEALE EAEKAQVAAE KAIKQADEDI 

      1630       1640       1650       1660       1670       1680 
QGTQNLLTSI ESETAASEET LFNASQRISE LERNVEELKR KAAQNSGEAE YIEKVVYTVK 

      1690       1700       1710       1720       1730       1740 
QSAEDVKKTL DGELDEKYKK VENLIAKKTE ESADARRKAE MLQNEAKTLL AQANSKLQLL 

      1750       1760       1770       1780 
KDLERKYEDN QRYLEDKAQE LARLEGEVRS LLKDISQKVA VYSTCL 

« Hide

References

« Hide 'large scale' references
[1]"Structure of the human laminin B1 chain gene."
Vuolteenaho R., Chow L.T., Tryggvason K.
J. Biol. Chem. 265:15611-15616(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT ARG-1022.
[2]"Human laminin B1 chain. A multidomain protein with gene (LAMB1) locus in the q22 region of chromosome 7."
Pikkarainen T., Eddy R., Fukushima Y., Byers M., Shows T., Pihlajaniemi T., Saraste M., Tryggvason K.
J. Biol. Chem. 262:10454-10462(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT ARG-1022.
[3]"Human chromosome 7: DNA sequence and biology."
Scherer S.W., Cheung J., MacDonald J.R., Osborne L.R., Nakabayashi K., Herbrick J.-A., Carson A.R., Parker-Katiraee L., Skaug J., Khaja R., Zhang J., Hudek A.K., Li M., Haddad M., Duggan G.E., Fernandez B.A., Kanematsu E., Gentles S. expand/collapse author list , Christopoulos C.C., Choufani S., Kwasnicka D., Zheng X.H., Lai Z., Nusskern D.R., Zhang Q., Gu Z., Lu F., Zeesman S., Nowaczyk M.J., Teshima I., Chitayat D., Shuman C., Weksberg R., Zackai E.H., Grebe T.A., Cox S.R., Kirkpatrick S.J., Rahman N., Friedman J.M., Heng H.H.Q., Pelicci P.G., Lo-Coco F., Belloni E., Shaffer L.G., Pober B., Morton C.C., Gusella J.F., Bruns G.A.P., Korf B.R., Quade B.J., Ligon A.H., Ferguson H., Higgins A.W., Leach N.T., Herrick S.R., Lemyre E., Farra C.G., Kim H.-G., Summers A.M., Gripp K.W., Roberts W., Szatmari P., Winsor E.J.T., Grzeschik K.-H., Teebi A., Minassian B.A., Kere J., Armengol L., Pujana M.A., Estivill X., Wilson M.D., Koop B.F., Tosi S., Moore G.E., Boright A.P., Zlotorynski E., Kerem B., Kroisel P.M., Petek E., Oscier D.G., Mould S.J., Doehner H., Doehner K., Rommens J.M., Vincent J.B., Venter J.C., Li P.W., Mural R.J., Adams M.D., Tsui L.-C.
Science 300:767-772(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Colon.
[5]"Isolation of a cDNA clone for the human laminin-B1 chain and its gene localization."
Jaye M., Modi W.S., Ricca G.A., Mudd R., Chiu I.M., O'Brien S.J., Drohan W.N.
Am. J. Hum. Genet. 41:605-615(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1276-1709.
[6]"Human plasma N-glycoproteome analysis by immunoaffinity subtraction, hydrazide chemistry, and mass spectrometry."
Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E., Moore R.J., Smith R.D.
J. Proteome Res. 4:2070-2080(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-1279.
Tissue: Plasma.
[7]"Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry."
Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.
J. Proteome Res. 8:651-661(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-1279.
Tissue: Liver.
[8]"Mutations in LAMB1 cause cobblestone brain malformation without muscular or ocular abnormalities."
Radmanesh F., Caglayan A.O., Silhavy J.L., Yilmaz C., Cantagrel V., Omar T., Rosti B., Kaymakcalan H., Gabriel S., Li M., Sestan N., Bilguvar K., Dobyns W.B., Zaki M.S., Gunel M., Gleeson J.G.
Am. J. Hum. Genet. 92:468-474(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: INVOLVEMENT IN LIS5, FUNCTION.
[9]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT [LARGE SCALE ANALYSIS] ARG-1022, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M61951 expand/collapse EMBL AC list , M58147, M61917, M61918, M61921, M61922, M61923, M61924, M61925, M61926, M61927, M61928, M61929, M61930, M61931, M61932, M61933, M61934, M61935, M61936, M61938, M61939, M61940, M61941, M61942, M61943, M61944, M61945, M61946, M61947, M61948, M61949, M61950 Genomic DNA. Translation: AAA59486.1.
M55370 expand/collapse EMBL AC list , M55378, M55365, M55371, M55372, M55373, M55374, M55375, M55376, M55344, M55345, M55346, M55347, M55348, M55349, M55350, M55351, M55352, M55353, M55355, M55356, M55357, M55358, M55359, M55360, M55361, M55362, M55363, M55364, M55366, M55367, M55368, M55369 Genomic DNA. Translation: AAA59485.1.
M61916 mRNA. Translation: AAA59482.1.
CH236947 Genomic DNA. Translation: EAL24388.1.
BC113455 mRNA. Translation: AAI13456.1.
M20206 mRNA. Translation: AAA59487.1.
CCDSCCDS5750.1.
PIRMMHUB1. S13547.
RefSeqNP_002282.2. NM_002291.2.
UniGeneHs.650585.

3D structure databases

ProteinModelPortalP07942.
SMRP07942. Positions 29-492.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid110106. 20 interactions.
IntActP07942. 9 interactions.
MINTMINT-2860329.
STRING9606.ENSP00000222399.

Chemistry

ChEMBLCHEMBL2364187.
DrugBankDB00009. Alteplase.
DB00029. Anistreplase.
DB00015. Reteplase.
DB00031. Tenecteplase.

PTM databases

PhosphoSiteP07942.

Polymorphism databases

DMDM317373377.

Proteomic databases

MaxQBP07942.
PaxDbP07942.
PRIDEP07942.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000222399; ENSP00000222399; ENSG00000091136.
GeneID3912.
KEGGhsa:3912.
UCSCuc003vew.2. human.

Organism-specific databases

CTD3912.
GeneCardsGC07M107564.
H-InvDBHIX0025323.
HGNCHGNC:6486. LAMB1.
HPACAB004256.
HPA004056.
HPA004132.
MIM150240. gene.
615191. phenotype.
neXtProtNX_P07942.
Orphanet352682. Cobblestone lissencephaly without muscular or ocular involvement.
PharmGKBPA30275.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG241384.
HOGENOMHOG000007552.
HOVERGENHBG052301.
KOK05636.
PhylomeDBP07942.
TreeFamTF312903.

Enzyme and pathway databases

ReactomeREACT_111045. Developmental Biology.
REACT_118779. Extracellular matrix organization.

Gene expression databases

ArrayExpressP07942.
BgeeP07942.
CleanExHS_LAMB1.
GenevestigatorP07942.

Family and domain databases

InterProIPR002049. EGF_laminin.
IPR013015. Laminin_IV.
IPR008211. Laminin_N.
IPR009053. Prefoldin.
[Graphical view]
PfamPF00053. Laminin_EGF. 13 hits.
PF00055. Laminin_N. 1 hit.
[Graphical view]
SMARTSM00180. EGF_Lam. 13 hits.
SM00136. LamNT. 1 hit.
[Graphical view]
SUPFAMSSF46579. SSF46579. 1 hit.
PROSITEPS00022. EGF_1. 9 hits.
PS01186. EGF_2. 2 hits.
PS01248. EGF_LAM_1. 11 hits.
PS50027. EGF_LAM_2. 13 hits.
PS51116. LAMININ_IVB. 1 hit.
PS51117. LAMININ_NTER. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSLAMB1. human.
GeneWikiLaminin,_beta_1.
GenomeRNAi3912.
NextBio15367.
PROP07942.
SOURCESearch...

Entry information

Entry nameLAMB1_HUMAN
AccessionPrimary (citable) accession number: P07942
Secondary accession number(s): Q14D91
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1988
Last sequence update: January 11, 2011
Last modified: July 9, 2014
This is version 152 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 7

Human chromosome 7: entries, gene names and cross-references to MIM