P11047 (LAMC1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	1609 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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	Secreted › extracellular space › extracellular matrix › basement 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 process	Cell adhesion
Cellular component	Basement membrane Extracellular matrix Secreted
Coding sequence diversity	Polymorphism
Domain	Coiled coil Laminin EGF-like domain Repeat Signal
PTM	Disulfide bond Glycoprotein Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	axon guidance Traceable author statement. Source: Reactome 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 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_component	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_function	extracellular matrix structural constituent Inferred from mutant phenotype PubMed 15159456. Source: HGNC glycosphingolipid binding Inferred from electronic annotation. Source: Compara
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 33	33
	Chain	34 – 1609	1576	Laminin subunit gamma-1		PRO_0000017074
Regions
	Domain	46 – 285	240	Laminin N-terminal
	Domain	286 – 341	56	Laminin EGF-like 1
	Domain	342 – 397	56	Laminin EGF-like 2
	Domain	398 – 444	47	Laminin EGF-like 3
	Domain	445 – 494	50	Laminin EGF-like 4
	Domain	495 – 504	10	Laminin EGF-like 5; first part
	Domain	514 – 689	176	Laminin IV type A
	Domain	690 – 723	34	Laminin EGF-like 5; second part
	Domain	724 – 772	49	Laminin EGF-like 6
	Domain	773 – 827	55	Laminin EGF-like 7
	Domain	828 – 883	56	Laminin EGF-like 8
	Domain	884 – 934	51	Laminin EGF-like 9
	Domain	935 – 982	48	Laminin EGF-like 10
	Domain	983 – 1030	48	Laminin EGF-like 11
	Region	1030 – 1609	580	Domain II and I
	Coiled coil	1038 – 1609	572	Potential
Amino acid modifications
	Modified residue	1493	1	Phosphoserine Ref.10
	Glycosylation	60	1	N-linked (GlcNAc...) Potential
	Glycosylation	134	1	N-linked (GlcNAc...) Potential
	Glycosylation	576	1	N-linked (GlcNAc...) Potential
	Glycosylation	650	1	N-linked (GlcNAc...) Ref.6 Ref.8
	Glycosylation	1022	1	N-linked (GlcNAc...) Potential
	Glycosylation	1107	1	N-linked (GlcNAc...) Ref.7 Ref.8
	Glycosylation	1161	1	N-linked (GlcNAc...) Ref.7
	Glycosylation	1175	1	N-linked (GlcNAc...) Ref.7
	Glycosylation	1205	1	N-linked (GlcNAc...) Potential
	Glycosylation	1223	1	N-linked (GlcNAc...) Ref.7
	Glycosylation	1241	1	N-linked (GlcNAc...) Ref.8
	Glycosylation	1380	1	N-linked (GlcNAc...) Potential
	Glycosylation	1395	1	N-linked (GlcNAc...) Ref.7 Ref.8
	Glycosylation	1439	1	N-linked (GlcNAc...) Potential
	Disulfide bond	286 ↔ 295		By similarity
	Disulfide bond	288 ↔ 305		By similarity
	Disulfide bond	307 ↔ 316		By similarity
	Disulfide bond	319 ↔ 339		By similarity
	Disulfide bond	342 ↔ 351		By similarity
	Disulfide bond	344 ↔ 367		By similarity
	Disulfide bond	370 ↔ 379		By similarity
	Disulfide bond	382 ↔ 395		By similarity
	Disulfide bond	398 ↔ 410		By similarity
	Disulfide bond	400 ↔ 416		By similarity
	Disulfide bond	418 ↔ 427		By similarity
	Disulfide bond	430 ↔ 442		By similarity
	Disulfide bond	445 ↔ 456		By similarity
	Disulfide bond	447 ↔ 463		By similarity
	Disulfide bond	465 ↔ 474		By similarity
	Disulfide bond	477 ↔ 492		By similarity
	Disulfide bond	724 ↔ 733		By similarity
	Disulfide bond	726 ↔ 740		By similarity
	Disulfide bond	742 ↔ 751		By similarity
	Disulfide bond	754 ↔ 770		By similarity
	Disulfide bond	773 ↔ 781		By similarity
	Disulfide bond	775 ↔ 792		By similarity
	Disulfide bond	795 ↔ 804		By similarity
	Disulfide bond	807 ↔ 825		By similarity
	Disulfide bond	828 ↔ 842		By similarity
	Disulfide bond	830 ↔ 849		By similarity
	Disulfide bond	852 ↔ 861		By similarity
	Disulfide bond	864 ↔ 881		By similarity
	Disulfide bond	884 ↔ 898		By similarity
	Disulfide bond	886 ↔ 905		By similarity
	Disulfide bond	907 ↔ 916		By similarity
	Disulfide bond	919 ↔ 932		By similarity
	Disulfide bond	935 ↔ 947		By similarity
	Disulfide bond	937 ↔ 954		By similarity
	Disulfide bond	956 ↔ 965		By similarity
	Disulfide bond	968 ↔ 980		By similarity
	Disulfide bond	983 ↔ 995		By similarity
	Disulfide bond	985 ↔ 1001		By similarity
	Disulfide bond	1003 ↔ 1012		By similarity
	Disulfide bond	1015 ↔ 1028		By similarity
	Disulfide bond	1031		Interchain Probable
	Disulfide bond	1034		Interchain Probable
	Disulfide bond	1600		Interchain Probable
Natural variations
	Natural variant	458	1	I → V. Ref.1 Ref.2 Corresponds to variant rs20563 [ dbSNP | Ensembl ].		VAR_014700
	Natural variant	731	1	E → K. Corresponds to variant rs2230157 [ dbSNP | Ensembl ].		VAR_054488
	Natural variant	888	1	L → P. Ref.1 Ref.2 Corresponds to variant rs20558 [ dbSNP | Ensembl ].		VAR_014701
	Natural variant	1116	1	R → H in a colorectal cancer sample; somatic mutation. Ref.11		VAR_035821
	Natural variant	1121	1	R → Q. Corresponds to variant rs20559 [ dbSNP | Ensembl ].		VAR_014702
Experimental info
	Sequence conflict	212	1	I → F in AAA59492. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	P11047 [UniParc]. Last modified March 3, 2009. Version 3. Checksum: 42D9A9958EEBBB01	FASTA	1,609	177,603
	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

References

	« Hide 'large scale' referencesShow '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. , 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, MASS SPECTROMETRY. 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, MASS SPECTROMETRY. 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, MASS SPECTROMETRY.
[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. , 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 , 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.
IPI	IPI00298281.
PIR	MMHUB2. S13548.
RefSeq	NP_002284.3. NM_002293.3.
UniGene	Hs.609663.
3D structure databases
ProteinModelPortal	P11047.
ModBase	Search...
Protein-protein interaction databases
IntAct	P11047. 5 interactions.
MINT	MINT-1184520.
STRING	9606.ENSP00000258341.
PTM databases
PhosphoSite	P11047.
Polymorphism databases
DMDM	224471885.
Proteomic databases
PaxDb	P11047.
PRIDE	P11047.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000258341; ENSP00000258341; ENSG00000135862.
GeneID	3915.
KEGG	hsa:3915.
UCSC	uc001gpy.4. human.
Organism-specific databases
CTD	3915.
GeneCards	GC01P182992.
H-InvDB	HIX0001405.
HGNC	HGNC:6492. LAMC1.
HPA	CAB004486. HPA001908. HPA001909.
MIM	150290. gene.
neXtProt	NX_P11047.
PharmGKB	PA30280.
GenAtlas	Search...
Phylogenomic databases
eggNOG	NOG235720.
HOGENOM	HOG000019301.
HOVERGEN	HBG100808.
InParanoid	P11047.
KO	K05635.
OMA	EATDYPW.
OrthoDB	EOG49GKFS.
PhylomeDB	P11047.
Enzyme and pathway databases
Pathway_Interaction_DB	smad2_3nuclearpathway. Regulation of nuclear SMAD2/3 signaling.
Reactome	REACT_111045. Developmental Biology. REACT_111102. Signal Transduction.
Gene expression databases
Bgee	P11047.
CleanEx	HS_LAMB2. HS_LAMC1.
Genevestigator	P11047.
GermOnline	ENSG00000135862. Homo sapiens.
Family and domain databases
InterPro	IPR013032. EGF-like_CS. IPR002049. EGF_laminin. IPR018031. Laminin_B_subgr. IPR000034. Laminin_B_type_IV. IPR008211. Laminin_N. [Graphical view]
Pfam	PF00052. Laminin_B. 1 hit. PF00053. Laminin_EGF. 10 hits. PF00055. Laminin_N. 1 hit. [Graphical view]
SMART	SM00180. EGF_Lam. 10 hits. SM00281. LamB. 1 hit. SM00136. LamNT. 1 hit. [Graphical view]
PROSITE	PS00022. 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]
ProtoNet	Search...
Other
ChiTaRS	LAMC1. human.
DrugBank	DB00009. Alteplase. DB00029. Anistreplase. DB00015. Reteplase. DB00031. Tenecteplase.
GenomeRNAi	3915.
NextBio	15381.
SOURCE	Search...

Entry information

Entry name

LAMC1_HUMAN

Accession

Primary (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:	May 1, 2013
This is version 156 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.