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Protein

Laminin subunit gamma-1

Gene

LAMC1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-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

  1. extracellular matrix structural constituent Source: HGNC
  2. glycosphingolipid binding Source: Ensembl

GO - Biological processi

  1. axon guidance Source: Reactome
  2. cell adhesion Source: HGNC
  3. cell migration Source: HGNC
  4. endoderm development Source: ProtInc
  5. extracellular matrix disassembly Source: HGNC
  6. extracellular matrix organization Source: Reactome
  7. hemidesmosome assembly Source: HGNC
  8. positive regulation of epithelial cell proliferation Source: HGNC
  9. protein complex assembly Source: HGNC
  10. substrate adhesion-dependent cell spreading Source: BHF-UCL
Complete GO annotation...

Keywords - Biological processi

Cell adhesion

Enzyme and pathway databases

ReactomeiREACT_118572. Degradation of the extracellular matrix.
REACT_163874. Non-integrin membrane-ECM interactions.
REACT_163906. ECM proteoglycans.
REACT_169262. Laminin interactions.
REACT_22205. L1CAM interactions.

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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 1

Organism-specific databases

HGNCiHGNC:6492. LAMC1.

Subcellular locationi

GO - Cellular componenti

  1. basement membrane Source: UniProtKB
  2. extracellular matrix Source: UniProtKB
  3. extracellular region Source: Reactome
  4. extracellular space Source: UniProtKB
  5. extracellular vesicular exosome Source: UniProtKB
  6. laminin-10 complex Source: BHF-UCL
  7. laminin-11 complex Source: BHF-UCL
  8. laminin-1 complex Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Basement membrane, Extracellular matrix, Secreted

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA30280.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 3333Add
BLAST
Chaini34 – 16091576Laminin subunit gamma-1PRO_0000017074Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi60 – 601N-linked (GlcNAc...)Sequence Analysis
Glycosylationi134 – 1341N-linked (GlcNAc...)Sequence Analysis
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
Glycosylationi576 – 5761N-linked (GlcNAc...)Sequence Analysis
Glycosylationi650 – 6501N-linked (GlcNAc...)2 Publications
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
Glycosylationi1022 – 10221N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi1031 – 1031InterchainCurated
Disulfide bondi1034 – 1034InterchainCurated
Glycosylationi1107 – 11071N-linked (GlcNAc...)2 Publications
Glycosylationi1161 – 11611N-linked (GlcNAc...)1 Publication
Glycosylationi1175 – 11751N-linked (GlcNAc...)1 Publication
Glycosylationi1205 – 12051N-linked (GlcNAc...)Sequence Analysis
Glycosylationi1223 – 12231N-linked (GlcNAc...)1 Publication
Glycosylationi1241 – 12411N-linked (GlcNAc...)1 Publication
Glycosylationi1380 – 13801N-linked (GlcNAc...)Sequence Analysis
Glycosylationi1395 – 13951N-linked (GlcNAc...)2 Publications
Glycosylationi1439 – 14391N-linked (GlcNAc...)Sequence Analysis
Modified residuei1493 – 14931Phosphoserine1 Publication
Disulfide bondi1600 – 1600InterchainCurated

Keywords - PTMi

Disulfide bond, Glycoprotein, Phosphoprotein

Proteomic databases

MaxQBiP11047.
PaxDbiP11047.
PRIDEiP11047.

PTM databases

PhosphoSiteiP11047.

Expressioni

Tissue specificityi

Found in the basement membranes (major component).

Gene expression databases

BgeeiP11047.
CleanExiHS_LAMB2.
HS_LAMC1.
ExpressionAtlasiP11047. baseline and differential.
GenevestigatoriP11047.

Organism-specific databases

HPAiCAB004486.
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. 26 interactions.
IntActiP11047. 10 interactions.
MINTiMINT-1184520.
STRINGi9606.ENSP00000258341.

Structurei

3D structure databases

SMRiP11047. Positions 39-396, 773-934.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini46 – 285240Laminin N-terminalPROSITE-ProRule annotationAdd
BLAST
Domaini286 – 34156Laminin EGF-like 1PROSITE-ProRule annotationAdd
BLAST
Domaini342 – 39756Laminin EGF-like 2PROSITE-ProRule annotationAdd
BLAST
Domaini398 – 44447Laminin EGF-like 3PROSITE-ProRule annotationAdd
BLAST
Domaini445 – 49450Laminin EGF-like 4PROSITE-ProRule annotationAdd
BLAST
Domaini495 – 50410Laminin EGF-like 5; first partPROSITE-ProRule annotation
Domaini514 – 689176Laminin IV type APROSITE-ProRule annotationAdd
BLAST
Domaini690 – 72334Laminin EGF-like 5; second partPROSITE-ProRule annotationAdd
BLAST
Domaini724 – 77249Laminin EGF-like 6PROSITE-ProRule annotationAdd
BLAST
Domaini773 – 82755Laminin EGF-like 7PROSITE-ProRule annotationAdd
BLAST
Domaini828 – 88356Laminin EGF-like 8PROSITE-ProRule annotationAdd
BLAST
Domaini884 – 93451Laminin EGF-like 9PROSITE-ProRule annotationAdd
BLAST
Domaini935 – 98248Laminin EGF-like 10PROSITE-ProRule annotationAdd
BLAST
Domaini983 – 103048Laminin EGF-like 11PROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1030 – 1609580Domain II and IAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili1038 – 1609572Sequence AnalysisAdd
BLAST

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.

Sequence similaritiesi

Contains 11 laminin EGF-like domains.PROSITE-ProRule annotation
Contains 1 laminin IV type A domain.PROSITE-ProRule annotation
Contains 1 laminin N-terminal domain.PROSITE-ProRule annotation

Keywords - Domaini

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

Phylogenomic databases

eggNOGiNOG235720.
GeneTreeiENSGT00780000121851.
HOGENOMiHOG000019301.
HOVERGENiHBG100808.
InParanoidiP11047.
KOiK05635.
OMAiATDYPWR.
OrthoDBiEOG7SR4KJ.
PhylomeDBiP11047.
TreeFamiTF352481.

Family and domain databases

Gene3Di2.60.120.260. 1 hit.
InterProiIPR013032. EGF-like_CS.
IPR002049. EGF_laminin.
IPR008979. Galactose-bd-like.
IPR018031. Laminin_B_subgr.
IPR000034. Laminin_B_type_IV.
IPR008211. Laminin_N.
[Graphical view]
PfamiPF00052. Laminin_B. 1 hit.
PF00053. Laminin_EGF. 10 hits.
PF00055. Laminin_N. 1 hit.
[Graphical view]
SMARTiSM00180. EGF_Lam. 10 hits.
SM00281. LamB. 1 hit.
SM00136. LamNT. 1 hit.
[Graphical view]
PROSITEiPS00022. 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]

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 2, 2009 - v3
Checksum:i42D9A9958EEBBB01
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti212 – 2121I → F in AAA59492 (PubMed:1985895).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti458 – 4581I → V.2 Publications
Corresponds to variant rs20563 [ dbSNP | Ensembl ].
VAR_014700
Natural varianti731 – 7311E → K.
Corresponds to variant rs2230157 [ dbSNP | Ensembl ].
VAR_054488
Natural varianti888 – 8881L → P.2 Publications
Corresponds to variant rs20558 [ dbSNP | Ensembl ].
VAR_014701
Natural varianti1116 – 11161R → H in a colorectal cancer sample; somatic mutation. 1 Publication
VAR_035821
Natural varianti1121 – 11211R → Q.
Corresponds to variant rs20559 [ dbSNP | Ensembl ].
VAR_014702

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, AL450304 Genomic DNA. Translation: CAH70981.1.
AL450304, AL354953 Genomic DNA. Translation: CAI14877.1.
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.

Polymorphism databases

DMDMi224471885.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

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, AL450304 Genomic DNA. Translation: CAH70981.1.
AL450304, AL354953 Genomic DNA. Translation: CAI14877.1.
X13939 mRNA. Translation: CAA32122.1.
M27654 mRNA. Translation: AAA59489.1.
CCDSiCCDS1351.1.
PIRiS13548. MMHUB2.
RefSeqiNP_002284.3. NM_002293.3.
UniGeneiHs.609663.

3D structure databases

SMRiP11047. Positions 39-396, 773-934.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi110109. 26 interactions.
IntActiP11047. 10 interactions.
MINTiMINT-1184520.
STRINGi9606.ENSP00000258341.

Chemistry

ChEMBLiCHEMBL2364187.

PTM databases

PhosphoSiteiP11047.

Polymorphism databases

DMDMi224471885.

Proteomic databases

MaxQBiP11047.
PaxDbiP11047.
PRIDEiP11047.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi3915.
GeneCardsiGC01P182992.
H-InvDBHIX0001405.
HGNCiHGNC:6492. LAMC1.
HPAiCAB004486.
HPA001908.
HPA001909.
MIMi150290. gene.
neXtProtiNX_P11047.
PharmGKBiPA30280.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG235720.
GeneTreeiENSGT00780000121851.
HOGENOMiHOG000019301.
HOVERGENiHBG100808.
InParanoidiP11047.
KOiK05635.
OMAiATDYPWR.
OrthoDBiEOG7SR4KJ.
PhylomeDBiP11047.
TreeFamiTF352481.

Enzyme and pathway databases

ReactomeiREACT_118572. Degradation of the extracellular matrix.
REACT_163874. Non-integrin membrane-ECM interactions.
REACT_163906. ECM proteoglycans.
REACT_169262. Laminin interactions.
REACT_22205. L1CAM interactions.

Miscellaneous databases

ChiTaRSiLAMC1. human.
GeneWikiiLaminin,_gamma_1.
GenomeRNAii3915.
NextBioi15381.
PROiP11047.
SOURCEiSearch...

Gene expression databases

BgeeiP11047.
CleanExiHS_LAMB2.
HS_LAMC1.
ExpressionAtlasiP11047. baseline and differential.
GenevestigatoriP11047.

Family and domain databases

Gene3Di2.60.120.260. 1 hit.
InterProiIPR013032. EGF-like_CS.
IPR002049. EGF_laminin.
IPR008979. Galactose-bd-like.
IPR018031. Laminin_B_subgr.
IPR000034. Laminin_B_type_IV.
IPR008211. Laminin_N.
[Graphical view]
PfamiPF00052. Laminin_B. 1 hit.
PF00053. Laminin_EGF. 10 hits.
PF00055. Laminin_N. 1 hit.
[Graphical view]
SMARTiSM00180. EGF_Lam. 10 hits.
SM00281. LamB. 1 hit.
SM00136. LamNT. 1 hit.
[Graphical view]
PROSITEiPS00022. 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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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(1987) [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(1990) [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(2005) [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(1990) [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(1987) [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(2002) [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(2004) [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(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-650; ASN-1107; ASN-1241 AND ASN-1395.
    Tissue: Liver.
  9. 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(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1493, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  11. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  12. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  13. Cited for: VARIANT [LARGE SCALE ANALYSIS] HIS-1116.

Entry informationi

Entry nameiLAMC1_HUMAN
AccessioniPrimary (citable) accession number: P11047
Secondary accession number(s): Q5VYE7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 30, 1989
Last sequence update: March 2, 2009
Last modified: March 31, 2015
This is version 176 of the entry and version 3 of the sequence. [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

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. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.