Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

UniProtKB - P11047 (LAMC1_HUMAN)

(max 400 entries)x

Your basket is currently empty. i

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

Laminin subunit gamma-1

Gene

LAMC1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

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.

GO - Molecular functioni

  • extracellular matrix structural constituent Source: HGNC
View the complete GO annotation on QuickGO ...

GO - Biological processi

  • cell adhesion Source: HGNC
  • cell migration Source: HGNC
  • cellular protein metabolic process Source: Reactome
  • endoderm development Source: ProtInc
  • extracellular matrix disassembly Source: HGNC
  • extracellular matrix organization Source: Reactome
  • hemidesmosome assembly Source: HGNC
  • positive regulation of epithelial cell proliferation Source: HGNC
  • post-translational protein modification Source: Reactome
  • protein-containing complex assembly Source: HGNC
  • substrate adhesion-dependent cell spreading Source: BHF-UCL
View the complete GO annotation on QuickGO ...

Keywordsi

Biological processCell adhesion

Enzyme and pathway databases

ReactomeiR-HSA-1474228 Degradation of the extracellular matrix
R-HSA-3000157 Laminin interactions
R-HSA-3000171 Non-integrin membrane-ECM interactions
R-HSA-3000178 ECM proteoglycans
R-HSA-373760 L1CAM interactions
R-HSA-381426 Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs)
R-HSA-8874081 MET activates PTK2 signaling
R-HSA-8957275 Post-translational protein phosphorylation
SIGNORiP11047

Names & Taxonomyi

Protein namesi
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 namesi
Name:LAMC1
Synonyms:LAMB2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo
Proteomesi
  • UP000005640 Componenti: Chromosome 1

Organism-specific databases

EuPathDBiHostDB:ENSG00000135862.5
HGNCiHGNC:6492 LAMC1
MIMi150290 gene
neXtProtiNX_P11047

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Basement membrane, Extracellular matrix, Secreted

Pathology & Biotechi

Organism-specific databases

DisGeNETi3915
OpenTargetsiENSG00000135862
PharmGKBiPA30280

Chemistry databases

ChEMBLiCHEMBL2364187

Polymorphism and mutation databases

BioMutaiLAMC1
DMDMi224471885

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 33Add BLAST33
ChainiPRO_000001707434 – 1609Laminin subunit gamma-1Add BLAST1576

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi60N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi134N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi286 ↔ 295PROSITE-ProRule annotation
Disulfide bondi288 ↔ 305PROSITE-ProRule annotation
Disulfide bondi307 ↔ 316PROSITE-ProRule annotation
Disulfide bondi319 ↔ 339PROSITE-ProRule annotation
Disulfide bondi342 ↔ 351PROSITE-ProRule annotation
Disulfide bondi344 ↔ 367PROSITE-ProRule annotation
Disulfide bondi370 ↔ 379PROSITE-ProRule annotation
Disulfide bondi382 ↔ 395PROSITE-ProRule annotation
Disulfide bondi398 ↔ 410PROSITE-ProRule annotation
Disulfide bondi400 ↔ 416PROSITE-ProRule annotation
Disulfide bondi418 ↔ 427PROSITE-ProRule annotation
Disulfide bondi430 ↔ 442PROSITE-ProRule annotation
Disulfide bondi445 ↔ 456PROSITE-ProRule annotation
Disulfide bondi447 ↔ 463PROSITE-ProRule annotation
Disulfide bondi465 ↔ 474PROSITE-ProRule annotation
Disulfide bondi477 ↔ 492PROSITE-ProRule annotation
Glycosylationi576N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi650N-linked (GlcNAc...) asparagine2 Publications1
Disulfide bondi724 ↔ 733PROSITE-ProRule annotation
Disulfide bondi726 ↔ 740PROSITE-ProRule annotation
Disulfide bondi742 ↔ 751PROSITE-ProRule annotation
Disulfide bondi754 ↔ 770PROSITE-ProRule annotation
Disulfide bondi773 ↔ 781PROSITE-ProRule annotation
Disulfide bondi775 ↔ 792PROSITE-ProRule annotation
Disulfide bondi795 ↔ 804PROSITE-ProRule annotation
Disulfide bondi807 ↔ 825PROSITE-ProRule annotation
Disulfide bondi828 ↔ 842PROSITE-ProRule annotation
Disulfide bondi830 ↔ 849PROSITE-ProRule annotation
Disulfide bondi852 ↔ 861PROSITE-ProRule annotation
Disulfide bondi864 ↔ 881PROSITE-ProRule annotation
Disulfide bondi884 ↔ 898PROSITE-ProRule annotation
Disulfide bondi886 ↔ 905PROSITE-ProRule annotation
Disulfide bondi907 ↔ 916PROSITE-ProRule annotation
Disulfide bondi919 ↔ 932PROSITE-ProRule annotation
Disulfide bondi935 ↔ 947PROSITE-ProRule annotation
Disulfide bondi937 ↔ 954PROSITE-ProRule annotation
Disulfide bondi956 ↔ 965PROSITE-ProRule annotation
Disulfide bondi968 ↔ 980PROSITE-ProRule annotation
Disulfide bondi983 ↔ 995PROSITE-ProRule annotation
Disulfide bondi985 ↔ 1001PROSITE-ProRule annotation
Disulfide bondi1003 ↔ 1012PROSITE-ProRule annotation
Disulfide bondi1015 ↔ 1028PROSITE-ProRule annotation
Glycosylationi1022N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi1031InterchainCurated
Disulfide bondi1034InterchainCurated
Glycosylationi1107N-linked (GlcNAc...) asparagine2 Publications1
Modified residuei1149Phosphoserine; by FAM20C1 Publication1
Glycosylationi1161N-linked (GlcNAc...) asparagine1 Publication1
Glycosylationi1175N-linked (GlcNAc...) asparagine1 Publication1
Glycosylationi1205N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi1223N-linked (GlcNAc...) asparagine1 Publication1
Glycosylationi1241N-linked (GlcNAc...) asparagine1 Publication1
Glycosylationi1380N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi1395N-linked (GlcNAc...) asparagine2 Publications1
Glycosylationi1439N-linked (GlcNAc...) asparagineSequence analysis1
Modified residuei1493PhosphoserineCombined sources1
Disulfide bondi1600InterchainCurated

Keywords - PTMi

Disulfide bond, Glycoprotein, Phosphoprotein

Proteomic databases

EPDiP11047
MaxQBiP11047
PaxDbiP11047
PeptideAtlasiP11047
PRIDEiP11047
ProteomicsDBi52689

PTM databases

CarbonylDBiP11047
iPTMnetiP11047
PhosphoSitePlusiP11047
SwissPalmiP11047

Expressioni

Tissue specificityi

Found in the basement membranes (major component).

Gene expression databases

BgeeiENSG00000135862
CleanExiHS_LAMB2
HS_LAMC1
ExpressionAtlasiP11047 baseline and differential
GenevisibleiP11047 HS

Organism-specific databases

HPAiCAB004486
CAB078163
HPA001908
HPA001909

Interactioni

Subunit structurei

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).

Protein-protein interaction databases

BioGridi110109, 35 interactors
CORUMiP11047
IntActiP11047, 13 interactors
MINTiP11047
STRINGi9606.ENSP00000258341

Structurei

Secondary structure

11609
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi1536 – 1552Combined sources17
Helixi1554 – 1595Combined sources42

3D structure databases

ProteinModelPortaliP11047
SMRiP11047
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini46 – 285Laminin N-terminalPROSITE-ProRule annotationAdd BLAST240
Domaini286 – 341Laminin EGF-like 1PROSITE-ProRule annotationAdd BLAST56
Domaini342 – 397Laminin EGF-like 2PROSITE-ProRule annotationAdd BLAST56
Domaini398 – 444Laminin EGF-like 3PROSITE-ProRule annotationAdd BLAST47
Domaini445 – 494Laminin EGF-like 4PROSITE-ProRule annotationAdd BLAST50
Domaini495 – 504Laminin EGF-like 5; first partPROSITE-ProRule annotation10
Domaini514 – 689Laminin IV type APROSITE-ProRule annotationAdd BLAST176
Domaini690 – 723Laminin EGF-like 5; second partPROSITE-ProRule annotationAdd BLAST34
Domaini724 – 772Laminin EGF-like 6PROSITE-ProRule annotationAdd BLAST49
Domaini773 – 827Laminin EGF-like 7PROSITE-ProRule annotationAdd BLAST55
Domaini828 – 883Laminin EGF-like 8PROSITE-ProRule annotationAdd BLAST56
Domaini884 – 934Laminin EGF-like 9PROSITE-ProRule annotationAdd BLAST51
Domaini935 – 982Laminin EGF-like 10PROSITE-ProRule annotationAdd BLAST48
Domaini983 – 1030Laminin EGF-like 11PROSITE-ProRule annotationAdd BLAST48

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni1030 – 1609Domain II and IAdd BLAST580

Coiled coil

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Coiled coili1038 – 1609Sequence analysisAdd BLAST572

Domaini

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.

Keywords - Domaini

Coiled coil, Laminin EGF-like domain, Repeat, Signal

Phylogenomic databases

eggNOGiKOG1836 Eukaryota
ENOG410XRDC LUCA
GeneTreeiENSGT00780000121851
HOGENOMiHOG000019301
HOVERGENiHBG100808
InParanoidiP11047
KOiK05635
OMAiGSCENTY
OrthoDBiEOG091G005L
PhylomeDBiP11047
TreeFamiTF352481

Family and domain databases

Gene3Di2.60.120.1490, 1 hit
InterProiView protein in InterPro
IPR000742 EGF-like_dom
IPR002049 Laminin_EGF
IPR000034 Laminin_IV
IPR008211 Laminin_N
IPR038684 Laminin_N_sf
PfamiView protein in Pfam
PF00052 Laminin_B, 1 hit
PF00053 Laminin_EGF, 10 hits
PF00055 Laminin_N, 1 hit
SMARTiView protein in SMART
SM00181 EGF, 8 hits
SM00180 EGF_Lam, 10 hits
SM00281 LamB, 1 hit
SM00136 LamNT, 1 hit
PROSITEiView protein in 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

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P11047-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MRGSHRAAPA LRPRGRLWPV LAVLAAAAAA GCAQAAMDEC TDEGGRPQRC 
        60         70         80         90        100
MPEFVNAAFN VTVVATNTCG TPPEEYCVQT GVTGVTKSCH LCDAGQPHLQ 
       110        120        130        140        150
HGAAFLTDYN NQADTTWWQS QTMLAGVQYP SSINLTLHLG KAFDITYVRL 
       160        170        180        190        200
KFHTSRPESF AIYKRTREDG PWIPYQYYSG SCENTYSKAN RGFIRTGGDE 
       210        220        230        240        250
QQALCTDEFS DISPLTGGNV AFSTLEGRPS AYNFDNSPVL QEWVTATDIR 
       260        270        280        290        300
VTLNRLNTFG DEVFNDPKVL KSYYYAISDF AVGGRCKCNG HASECMKNEF 
       310        320        330        340        350
DKLVCNCKHN TYGVDCEKCL PFFNDRPWRR ATAESASECL PCDCNGRSQE 
       360        370        380        390        400
CYFDPELYRS TGHGGHCTNC QDNTDGAHCE RCRENFFRLG NNEACSSCHC 
       410        420        430        440        450
SPVGSLSTQC DSYGRCSCKP GVMGDKCDRC QPGFHSLTEA GCRPCSCDPS 
       460        470        480        490        500
GSIDECNIET GRCVCKDNVE GFNCERCKPG FFNLESSNPR GCTPCFCFGH 
       510        520        530        540        550
SSVCTNAVGY SVYSISSTFQ IDEDGWRAEQ RDGSEASLEW SSERQDIAVI 
       560        570        580        590        600
SDSYFPRYFI APAKFLGKQV LSYGQNLSFS FRVDRRDTRL SAEDLVLEGA 
       610        620        630        640        650
GLRVSVPLIA QGNSYPSETT VKYVFRLHEA TDYPWRPALT PFEFQKLLNN 
       660        670        680        690        700
LTSIKIRGTY SERSAGYLDD VTLASARPGP GVPATWVESC TCPVGYGGQF 
       710        720        730        740        750
CEMCLSGYRR ETPNLGPYSP CVLCACNGHS ETCDPETGVC NCRDNTAGPH 
       760        770        780        790        800
CEKCSDGYYG DSTAGTSSDC QPCPCPGGSS CAVVPKTKEV VCTNCPTGTT 
       810        820        830        840        850
GKRCELCDDG YFGDPLGRNG PVRLCRLCQC SDNIDPNAVG NCNRLTGECL 
       860        870        880        890        900
KCIYNTAGFY CDRCKDGFFG NPLAPNPADK CKACNCNLYG TMKQQSSCNP 
       910        920        930        940        950
VTGQCECLPH VTGQDCGACD PGFYNLQSGQ GCERCDCHAL GSTNGQCDIR 
       960        970        980        990       1000
TGQCECQPGI TGQHCERCEV NHFGFGPEGC KPCDCHPEGS LSLQCKDDGR 
      1010       1020       1030       1040       1050
CECREGFVGN RCDQCEENYF YNRSWPGCQE CPACYRLVKD KVADHRVKLQ 
      1060       1070       1080       1090       1100
ELESLIANLG TGDEMVTDQA FEDRLKEAER EVMDLLREAQ DVKDVDQNLM 
      1110       1120       1130       1140       1150
DRLQRVNNTL SSQISRLQNI RNTIEETGNL AEQARAHVEN TERLIEIASR 
      1160       1170       1180       1190       1200
ELEKAKVAAA NVSVTQPEST GDPNNMTLLA EEARKLAERH KQEADDIVRV 
      1210       1220       1230       1240       1250
AKTANDTSTE AYNLLLRTLA GENQTAFEIE ELNRKYEQAK NISQDLEKQA 
      1260       1270       1280       1290       1300
ARVHEEAKRA GDKAVEIYAS VAQLSPLDSE TLENEANNIK MEAENLEQLI 
      1310       1320       1330       1340       1350
DQKLKDYEDL REDMRGKELE VKNLLEKGKT EQQTADQLLA RADAAKALAE 
      1360       1370       1380       1390       1400
EAAKKGRDTL QEANDILNNL KDFDRRVNDN KTAAEEALRK IPAINQTITE 
      1410       1420       1430       1440       1450
ANEKTREAQQ ALGSAAADAT EAKNKAHEAE RIASAVQKNA TSTKAEAERT 
      1460       1470       1480       1490       1500
FAEVTDLDNE VNNMLKQLQE AEKELKRKQD DADQDMMMAG MASQAAQEAE 
      1510       1520       1530       1540       1550
INARKAKNSV TSLLSIINDL LEQLGQLDTV DLNKLNEIEG TLNKAKDEMK 
      1560       1570       1580       1590       1600
VSDLDRKVSD LENEAKKQEA AIMDYNRDIE EIMKDIRNLE DIRKTLPSGC 

FNTPSIEKP
Length:1,609
Mass (Da):177,603
Last modified:March 3, 2009 - v3
Checksum:i42D9A9958EEBBB01
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti212I → F in AAA59492 (PubMed:1985895).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_014700458I → V2 PublicationsCorresponds to variant dbSNP:rs20563Ensembl.1
Natural variantiVAR_054488731E → K. Corresponds to variant dbSNP:rs2230157Ensembl.1
Natural variantiVAR_014701888L → P2 PublicationsCorresponds to variant dbSNP:rs20558Ensembl.1
Natural variantiVAR_0358211116R → H in a colorectal cancer sample; somatic mutation. 1 PublicationCorresponds to variant dbSNP:rs548688323Ensembl.1
Natural variantiVAR_0147021121R → Q. Corresponds to variant dbSNP:rs20559Ensembl.1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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 Genomic DNA No translation available.
AL450304 Genomic DNA No translation available.
X13939 mRNA Translation: CAA32122.1
M27654 mRNA Translation: AAA59489.1
CCDSiCCDS1351.1
PIRiS13548 MMHUB2
RefSeqiNP_002284.3, NM_002293.3
UniGeneiHs.609663

Genome annotation databases

EnsembliENST00000258341; ENSP00000258341; ENSG00000135862
GeneIDi3915
KEGGihsa:3915
UCSCiuc001gpy.4 human

Keywords - Coding sequence diversityi

Polymorphism

Similar proteinsi

Entry informationi

Entry nameiLAMC1_HUMAN
AccessioniPrimary (citable) accession number: P11047
Secondary accession number(s): Q5VYE7
Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: March 3, 2009
Last modified: June 20, 2018
This is version 208 of the entry and version 3 of the sequence. See complete history.
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 1
    Human chromosome 1: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references

We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.

Do not show this banner again
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health