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P11047 (LAMC1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 169. 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 gamma-1
Alternative name(s):
Laminin B2 chain
Laminin-1 subunit gamma
Laminin-10 subunit gamma
Laminin-11 subunit gamma
Laminin-2 subunit gamma
Laminin-3 subunit gamma
Laminin-4 subunit gamma
Laminin-6 subunit gamma
Laminin-7 subunit gamma
Laminin-8 subunit gamma
Laminin-9 subunit gamma
S-laminin subunit gamma
Short name=S-LAM gamma
Gene names
Name:LAMC1
Synonyms:LAMB2
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1609 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.

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. Gamma-1 is a subunit of laminin-1 (laminin-111 or EHS laminin), laminin-2 (laminin-211 or merosin), laminin-3 (laminin-121 or S-laminin), laminin-4 (laminin-221 or S-merosin), laminin-6 (laminin-311 or K-laminin), laminin-7 (laminin-321 or KS-laminin), laminin-8 (laminin-411), laminin-9 (laminin-421), laminin-10 (laminin-511) and laminin-11 (laminin-521).

Subcellular location

Secretedextracellular spaceextracellular matrixbasement membrane.

Tissue specificity

Found in the basement membranes (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.

Sequence similarities

Contains 11 laminin EGF-like domains.

Contains 1 laminin IV type A domain.

Contains 1 laminin N-terminal domain.

Ontologies

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

Traceable author statement. Source: Reactome

cell adhesion

Inferred from direct assay PubMed 15159456. Source: HGNC

cell migration

Inferred from mutant phenotype PubMed 15561105. Source: HGNC

endoderm development

Traceable author statement PubMed 9885251. Source: ProtInc

extracellular matrix disassembly

Inferred from mutant phenotype PubMed 15159456. Source: HGNC

extracellular matrix organization

Traceable author statement. Source: Reactome

hemidesmosome assembly

Inferred from mutant phenotype PubMed 15159456. Source: HGNC

positive regulation of epithelial cell proliferation

Traceable author statement PubMed 14557481. Source: HGNC

protein complex assembly

Inferred from direct assay PubMed 15159456. Source: HGNC

substrate adhesion-dependent cell spreading

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

   Cellular_componentbasement membrane

Inferred from direct assay PubMed 14557481. Source: UniProtKB

extracellular region

Traceable author statement. Source: Reactome

extracellular space

Non-traceable author statement PubMed 10964500. Source: UniProtKB

extracellular vesicular exosome

Inferred from direct assay PubMed 21362503. Source: UniProtKB

laminin-1 complex

Non-traceable author statement PubMed 10964500. Source: UniProtKB

laminin-10 complex

Traceable author statement PubMed 16236823. Source: BHF-UCL

laminin-11 complex

Traceable author statement PubMed 16236823. Source: BHF-UCL

   Molecular_functionextracellular matrix structural constituent

Inferred from mutant phenotype PubMed 15159456. Source: HGNC

glycosphingolipid binding

Inferred from electronic annotation. Source: Ensembl

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 3333
Chain34 – 16091576Laminin subunit gamma-1
PRO_0000017074

Regions

Domain46 – 285240Laminin N-terminal
Domain286 – 34156Laminin EGF-like 1
Domain342 – 39756Laminin EGF-like 2
Domain398 – 44447Laminin EGF-like 3
Domain445 – 49450Laminin EGF-like 4
Domain495 – 50410Laminin EGF-like 5; first part
Domain514 – 689176Laminin IV type A
Domain690 – 72334Laminin EGF-like 5; second part
Domain724 – 77249Laminin EGF-like 6
Domain773 – 82755Laminin EGF-like 7
Domain828 – 88356Laminin EGF-like 8
Domain884 – 93451Laminin EGF-like 9
Domain935 – 98248Laminin EGF-like 10
Domain983 – 103048Laminin EGF-like 11
Region1030 – 1609580Domain II and I
Coiled coil1038 – 1609572 Potential

Amino acid modifications

Modified residue14931Phosphoserine Ref.10
Glycosylation601N-linked (GlcNAc...) Potential
Glycosylation1341N-linked (GlcNAc...) Potential
Glycosylation5761N-linked (GlcNAc...) Potential
Glycosylation6501N-linked (GlcNAc...) Ref.6 Ref.8
Glycosylation10221N-linked (GlcNAc...) Potential
Glycosylation11071N-linked (GlcNAc...) Ref.7 Ref.8
Glycosylation11611N-linked (GlcNAc...) Ref.7
Glycosylation11751N-linked (GlcNAc...) Ref.7
Glycosylation12051N-linked (GlcNAc...) Potential
Glycosylation12231N-linked (GlcNAc...) Ref.7
Glycosylation12411N-linked (GlcNAc...) Ref.8
Glycosylation13801N-linked (GlcNAc...) Potential
Glycosylation13951N-linked (GlcNAc...) Ref.7 Ref.8
Glycosylation14391N-linked (GlcNAc...) Potential
Disulfide bond286 ↔ 295 By similarity
Disulfide bond288 ↔ 305 By similarity
Disulfide bond307 ↔ 316 By similarity
Disulfide bond319 ↔ 339 By similarity
Disulfide bond342 ↔ 351 By similarity
Disulfide bond344 ↔ 367 By similarity
Disulfide bond370 ↔ 379 By similarity
Disulfide bond382 ↔ 395 By similarity
Disulfide bond398 ↔ 410 By similarity
Disulfide bond400 ↔ 416 By similarity
Disulfide bond418 ↔ 427 By similarity
Disulfide bond430 ↔ 442 By similarity
Disulfide bond445 ↔ 456 By similarity
Disulfide bond447 ↔ 463 By similarity
Disulfide bond465 ↔ 474 By similarity
Disulfide bond477 ↔ 492 By similarity
Disulfide bond724 ↔ 733 By similarity
Disulfide bond726 ↔ 740 By similarity
Disulfide bond742 ↔ 751 By similarity
Disulfide bond754 ↔ 770 By similarity
Disulfide bond773 ↔ 781 By similarity
Disulfide bond775 ↔ 792 By similarity
Disulfide bond795 ↔ 804 By similarity
Disulfide bond807 ↔ 825 By similarity
Disulfide bond828 ↔ 842 By similarity
Disulfide bond830 ↔ 849 By similarity
Disulfide bond852 ↔ 861 By similarity
Disulfide bond864 ↔ 881 By similarity
Disulfide bond884 ↔ 898 By similarity
Disulfide bond886 ↔ 905 By similarity
Disulfide bond907 ↔ 916 By similarity
Disulfide bond919 ↔ 932 By similarity
Disulfide bond935 ↔ 947 By similarity
Disulfide bond937 ↔ 954 By similarity
Disulfide bond956 ↔ 965 By similarity
Disulfide bond968 ↔ 980 By similarity
Disulfide bond983 ↔ 995 By similarity
Disulfide bond985 ↔ 1001 By similarity
Disulfide bond1003 ↔ 1012 By similarity
Disulfide bond1015 ↔ 1028 By similarity
Disulfide bond1031Interchain Probable
Disulfide bond1034Interchain Probable
Disulfide bond1600Interchain Probable

Natural variations

Natural variant4581I → V. Ref.1 Ref.2
Corresponds to variant rs20563 [ dbSNP | Ensembl ].
VAR_014700
Natural variant7311E → K.
Corresponds to variant rs2230157 [ dbSNP | Ensembl ].
VAR_054488
Natural variant8881L → P. Ref.1 Ref.2
Corresponds to variant rs20558 [ dbSNP | Ensembl ].
VAR_014701
Natural variant11161R → H in a colorectal cancer sample; somatic mutation. Ref.11
VAR_035821
Natural variant11211R → Q.
Corresponds to variant rs20559 [ dbSNP | Ensembl ].
VAR_014702

Experimental info

Sequence conflict2121I → F in AAA59492. Ref.2

Sequences

Sequence LengthMass (Da)Tools
P11047 [UniParc].

Last modified March 3, 2009. Version 3.
Checksum: 42D9A9958EEBBB01

FASTA1,609177,603
        10         20         30         40         50         60 
MRGSHRAAPA LRPRGRLWPV LAVLAAAAAA GCAQAAMDEC TDEGGRPQRC MPEFVNAAFN 

        70         80         90        100        110        120 
VTVVATNTCG TPPEEYCVQT GVTGVTKSCH LCDAGQPHLQ HGAAFLTDYN NQADTTWWQS 

       130        140        150        160        170        180 
QTMLAGVQYP SSINLTLHLG KAFDITYVRL KFHTSRPESF AIYKRTREDG PWIPYQYYSG 

       190        200        210        220        230        240 
SCENTYSKAN RGFIRTGGDE QQALCTDEFS DISPLTGGNV AFSTLEGRPS AYNFDNSPVL 

       250        260        270        280        290        300 
QEWVTATDIR VTLNRLNTFG DEVFNDPKVL KSYYYAISDF AVGGRCKCNG HASECMKNEF 

       310        320        330        340        350        360 
DKLVCNCKHN TYGVDCEKCL PFFNDRPWRR ATAESASECL PCDCNGRSQE CYFDPELYRS 

       370        380        390        400        410        420 
TGHGGHCTNC QDNTDGAHCE RCRENFFRLG NNEACSSCHC SPVGSLSTQC DSYGRCSCKP 

       430        440        450        460        470        480 
GVMGDKCDRC QPGFHSLTEA GCRPCSCDPS GSIDECNIET GRCVCKDNVE GFNCERCKPG 

       490        500        510        520        530        540 
FFNLESSNPR GCTPCFCFGH SSVCTNAVGY SVYSISSTFQ IDEDGWRAEQ RDGSEASLEW 

       550        560        570        580        590        600 
SSERQDIAVI SDSYFPRYFI APAKFLGKQV LSYGQNLSFS FRVDRRDTRL SAEDLVLEGA 

       610        620        630        640        650        660 
GLRVSVPLIA QGNSYPSETT VKYVFRLHEA TDYPWRPALT PFEFQKLLNN LTSIKIRGTY 

       670        680        690        700        710        720 
SERSAGYLDD VTLASARPGP GVPATWVESC TCPVGYGGQF CEMCLSGYRR ETPNLGPYSP 

       730        740        750        760        770        780 
CVLCACNGHS ETCDPETGVC NCRDNTAGPH CEKCSDGYYG DSTAGTSSDC QPCPCPGGSS 

       790        800        810        820        830        840 
CAVVPKTKEV VCTNCPTGTT GKRCELCDDG YFGDPLGRNG PVRLCRLCQC SDNIDPNAVG 

       850        860        870        880        890        900 
NCNRLTGECL KCIYNTAGFY CDRCKDGFFG NPLAPNPADK CKACNCNLYG TMKQQSSCNP 

       910        920        930        940        950        960 
VTGQCECLPH VTGQDCGACD PGFYNLQSGQ GCERCDCHAL GSTNGQCDIR TGQCECQPGI 

       970        980        990       1000       1010       1020 
TGQHCERCEV NHFGFGPEGC KPCDCHPEGS LSLQCKDDGR CECREGFVGN RCDQCEENYF 

      1030       1040       1050       1060       1070       1080 
YNRSWPGCQE CPACYRLVKD KVADHRVKLQ ELESLIANLG TGDEMVTDQA FEDRLKEAER 

      1090       1100       1110       1120       1130       1140 
EVMDLLREAQ DVKDVDQNLM DRLQRVNNTL SSQISRLQNI RNTIEETGNL AEQARAHVEN 

      1150       1160       1170       1180       1190       1200 
TERLIEIASR ELEKAKVAAA NVSVTQPEST GDPNNMTLLA EEARKLAERH KQEADDIVRV 

      1210       1220       1230       1240       1250       1260 
AKTANDTSTE AYNLLLRTLA GENQTAFEIE ELNRKYEQAK NISQDLEKQA ARVHEEAKRA 

      1270       1280       1290       1300       1310       1320 
GDKAVEIYAS VAQLSPLDSE TLENEANNIK MEAENLEQLI DQKLKDYEDL REDMRGKELE 

      1330       1340       1350       1360       1370       1380 
VKNLLEKGKT EQQTADQLLA RADAAKALAE EAAKKGRDTL QEANDILNNL KDFDRRVNDN 

      1390       1400       1410       1420       1430       1440 
KTAAEEALRK IPAINQTITE ANEKTREAQQ ALGSAAADAT EAKNKAHEAE RIASAVQKNA 

      1450       1460       1470       1480       1490       1500 
TSTKAEAERT FAEVTDLDNE VNNMLKQLQE AEKELKRKQD DADQDMMMAG MASQAAQEAE 

      1510       1520       1530       1540       1550       1560 
INARKAKNSV TSLLSIINDL LEQLGQLDTV DLNKLNEIEG TLNKAKDEMK VSDLDRKVSD 

      1570       1580       1590       1600 
LENEAKKQEA AIMDYNRDIE EIMKDIRNLE DIRKTLPSGC FNTPSIEKP 

« Hide

References

« Hide 'large scale' references
[1]"Human laminin B2 chain. Comparison of the complete amino acid sequence with the B1 chain reveals variability in sequence homology between different structural domains."
Pikkarainen T., Kallunki T., Tryggvason K.
J. Biol. Chem. 263:6751-6758(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANTS VAL-458 AND PRO-888.
[2]"Structure of the human laminin B2 chain gene reveals extensive divergence from the laminin B1 chain gene."
Kallunki T., Ikonen J., Chow L.T., Kallunki P., Tryggvason K.
J. Biol. Chem. 266:221-228(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS VAL-458 AND PRO-888.
[3]"The DNA sequence and biological annotation of human chromosome 1."
Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K. expand/collapse author list , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]"Differences in human laminin B2 sequences."
Santos C.L.S., Sabbaga J., Brentani R.
DNA Seq. 1:275-277(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1282-1609.
Tissue: Endothelial cell.
[5]"Isolation of a human laminin B2 (LAMB2) cDNA clone and assignment of the gene to chromosome region 1q25-->q31."
Fukushima Y., Pikkarainen T., Kallunki T., Eddy R.L., Byers M.G., Haley L.L., Henry W.M., Tryggvason K., Shows T.B.
Cytogenet. Cell Genet. 48:137-141(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1393-1609.
[6]"Identification and quantification of N-linked glycoproteins using hydrazide chemistry, stable isotope labeling and mass spectrometry."
Zhang H., Li X.-J., Martin D.B., Aebersold R.
Nat. Biotechnol. 21:660-666(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION AT ASN-650.
[7]"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-1107; ASN-1161; ASN-1175; ASN-1223 AND ASN-1395.
Tissue: Plasma.
[8]"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-650; ASN-1107; ASN-1241 AND ASN-1395.
Tissue: Liver.
[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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[10]"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1493, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[11]"The consensus coding sequences of human breast and colorectal cancers."
Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V. expand/collapse author list , Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., Velculescu V.E.
Science 314:268-274(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT [LARGE SCALE ANALYSIS] HIS-1116.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
J03202 mRNA. Translation: AAA59488.1.
M55210 expand/collapse EMBL AC list , M55217, M55201, M55211, M55212, M55213, M55214, M55215, M55216, M55192, M55193, M55194, M55195, M55196, M55197, M55198, M55199, M55200, M55202, M55203, M55204, M55205, M55206, M55207, M55208, M55209 Genomic DNA. Translation: AAA59492.1.
AL354953, AL450304 Genomic DNA. Translation: CAH70981.1.
AL450304, AL354953 Genomic DNA. Translation: CAI14877.1.
X13939 mRNA. Translation: CAA32122.1.
M27654 mRNA. Translation: AAA59489.1.
CCDSCCDS1351.1.
PIRMMHUB2. S13548.
RefSeqNP_002284.3. NM_002293.3.
UniGeneHs.609663.

3D structure databases

ProteinModelPortalP11047.
SMRP11047. Positions 39-396, 773-934.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid110109. 20 interactions.
IntActP11047. 9 interactions.
MINTMINT-1184520.
STRING9606.ENSP00000258341.

Chemistry

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

PTM databases

PhosphoSiteP11047.

Polymorphism databases

DMDM224471885.

Proteomic databases

MaxQBP11047.
PaxDbP11047.
PRIDEP11047.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000258341; ENSP00000258341; ENSG00000135862.
GeneID3915.
KEGGhsa:3915.
UCSCuc001gpy.4. human.

Organism-specific databases

CTD3915.
GeneCardsGC01P182992.
H-InvDBHIX0001405.
HGNCHGNC:6492. LAMC1.
HPACAB004486.
HPA001908.
HPA001909.
MIM150290. gene.
neXtProtNX_P11047.
PharmGKBPA30280.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG235720.
HOGENOMHOG000019301.
HOVERGENHBG100808.
InParanoidP11047.
KOK05635.
OMAEATDYPW.
OrthoDBEOG7SR4KJ.
PhylomeDBP11047.
TreeFamTF352481.

Enzyme and pathway databases

ReactomeREACT_111045. Developmental Biology.
REACT_118779. Extracellular matrix organization.

Gene expression databases

BgeeP11047.
CleanExHS_LAMB2.
HS_LAMC1.
GenevestigatorP11047.

Family and domain databases

Gene3D2.60.120.260. 1 hit.
InterProIPR013032. EGF-like_CS.
IPR002049. EGF_laminin.
IPR008979. Galactose-bd-like.
IPR018031. Laminin_B_subgr.
IPR000034. Laminin_B_type_IV.
IPR008211. Laminin_N.
[Graphical view]
PfamPF00052. Laminin_B. 1 hit.
PF00053. Laminin_EGF. 10 hits.
PF00055. Laminin_N. 1 hit.
[Graphical view]
SMARTSM00180. EGF_Lam. 10 hits.
SM00281. LamB. 1 hit.
SM00136. LamNT. 1 hit.
[Graphical view]
PROSITEPS00022. EGF_1. 8 hits.
PS01186. EGF_2. 2 hits.
PS01248. EGF_LAM_1. 11 hits.
PS50027. EGF_LAM_2. 10 hits.
PS51115. LAMININ_IVA. 1 hit.
PS51117. LAMININ_NTER. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSLAMC1. human.
GeneWikiLaminin,_gamma_1.
GenomeRNAi3915.
NextBio15381.
PROP11047.
SOURCESearch...

Entry information

Entry nameLAMC1_HUMAN
AccessionPrimary (citable) accession number: P11047
Secondary accession number(s): Q5VYE7
Entry history
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: March 3, 2009
Last modified: July 9, 2014
This is version 169 of the entry and version 3 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 1

Human chromosome 1: entries, gene names and cross-references to MIM