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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

  • extracellular matrix structural constituent Source: HGNC

GO - Biological processi

  • cell adhesion Source: HGNC
  • cell migration Source: HGNC
  • 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
  • protein complex assembly Source: HGNC
  • substrate adhesion-dependent cell spreading Source: BHF-UCL
Complete GO annotation...

Keywords - Biological processi

Cell adhesion

Enzyme and pathway databases

BioCyciZFISH:ENSG00000135862-MONOMER.
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-8874081. MET activates PTK2 signaling.

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
Proteomesi
  • UP000005640 Componenti: Chromosome 1

Organism-specific databases

HGNCiHGNC:6492. LAMC1.

Subcellular locationi

GO - Cellular componenti

  • basement membrane Source: UniProtKB
  • extracellular exosome Source: UniProtKB
  • extracellular matrix Source: UniProtKB
  • extracellular region Source: Reactome
  • extracellular space Source: UniProtKB
  • laminin-10 complex Source: BHF-UCL
  • laminin-11 complex Source: BHF-UCL
  • laminin-1 complex Source: UniProtKB
Complete GO annotation...

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...)Sequence analysis1
Glycosylationi134N-linked (GlcNAc...)Sequence 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...)Sequence analysis1
Glycosylationi650N-linked (GlcNAc...)2 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...)Sequence analysis1
Disulfide bondi1031InterchainCurated
Disulfide bondi1034InterchainCurated
Glycosylationi1107N-linked (GlcNAc...)2 Publications1
Modified residuei1149Phosphoserine; by FAM20C1 Publication1
Glycosylationi1161N-linked (GlcNAc...)1 Publication1
Glycosylationi1175N-linked (GlcNAc...)1 Publication1
Glycosylationi1205N-linked (GlcNAc...)Sequence analysis1
Glycosylationi1223N-linked (GlcNAc...)1 Publication1
Glycosylationi1241N-linked (GlcNAc...)1 Publication1
Glycosylationi1380N-linked (GlcNAc...)Sequence analysis1
Glycosylationi1395N-linked (GlcNAc...)2 Publications1
Glycosylationi1439N-linked (GlcNAc...)Sequence analysis1
Modified residuei1493PhosphoserineCombined sources1
Disulfide bondi1600InterchainCurated

Keywords - PTMi

Disulfide bond, Glycoprotein, Phosphoprotein

Proteomic databases

EPDiP11047.
MaxQBiP11047.
PaxDbiP11047.
PeptideAtlasiP11047.
PRIDEiP11047.

PTM databases

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.
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. 34 interactors.
IntActiP11047. 13 interactors.
MINTiMINT-1184520.
STRINGi9606.ENSP00000258341.

Structurei

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.

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

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

Family and domain databases

Gene3Di2.60.120.260. 1 hit.
InterProiIPR000742. EGF-like_dom.
IPR008979. Galactose-bd-like.
IPR002049. Laminin_EGF.
IPR000034. Laminin_IV.
IPR008211. Laminin_N.
[Graphical view]
PfamiPF00052. Laminin_B. 1 hit.
PF00053. Laminin_EGF. 10 hits.
PF00055. Laminin_N. 1 hit.
[Graphical view]
SMARTiSM00181. EGF. 8 hits.
SM00180. 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 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 → V.2 PublicationsCorresponds to variant rs20563dbSNPEnsembl.1
Natural variantiVAR_054488731E → K.Corresponds to variant rs2230157dbSNPEnsembl.1
Natural variantiVAR_014701888L → P.2 PublicationsCorresponds to variant rs20558dbSNPEnsembl.1
Natural variantiVAR_0358211116R → H in a colorectal cancer sample; somatic mutation. 1 PublicationCorresponds to variant rs548688323dbSNPEnsembl.1
Natural variantiVAR_0147021121R → Q.Corresponds to variant rs20559dbSNPEnsembl.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, 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.

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

ProteinModelPortaliP11047.
SMRiP11047.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi110109. 34 interactors.
IntActiP11047. 13 interactors.
MINTiMINT-1184520.
STRINGi9606.ENSP00000258341.

Chemistry databases

ChEMBLiCHEMBL2364187.

PTM databases

iPTMnetiP11047.
PhosphoSitePlusiP11047.
SwissPalmiP11047.

Polymorphism and mutation databases

BioMutaiLAMC1.
DMDMi224471885.

Proteomic databases

EPDiP11047.
MaxQBiP11047.
PaxDbiP11047.
PeptideAtlasiP11047.
PRIDEiP11047.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi3915.
DisGeNETi3915.
GeneCardsiLAMC1.
H-InvDBHIX0001405.
HGNCiHGNC:6492. LAMC1.
HPAiCAB004486.
HPA001908.
HPA001909.
MIMi150290. gene.
neXtProtiNX_P11047.
OpenTargetsiENSG00000135862.
PharmGKBiPA30280.
GenAtlasiSearch...

Phylogenomic databases

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

Enzyme and pathway databases

BioCyciZFISH:ENSG00000135862-MONOMER.
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-8874081. MET activates PTK2 signaling.

Miscellaneous databases

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

Gene expression databases

BgeeiENSG00000135862.
CleanExiHS_LAMB2.
HS_LAMC1.
ExpressionAtlasiP11047. baseline and differential.
GenevisibleiP11047. HS.

Family and domain databases

Gene3Di2.60.120.260. 1 hit.
InterProiIPR000742. EGF-like_dom.
IPR008979. Galactose-bd-like.
IPR002049. Laminin_EGF.
IPR000034. Laminin_IV.
IPR008211. Laminin_N.
[Graphical view]
PfamiPF00052. Laminin_B. 1 hit.
PF00053. Laminin_EGF. 10 hits.
PF00055. Laminin_N. 1 hit.
[Graphical view]
SMARTiSM00181. EGF. 8 hits.
SM00180. 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...

Entry informationi

Entry nameiLAMC1_HUMAN
AccessioniPrimary (citable) accession number: P11047
Secondary accession number(s): Q5VYE7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: March 3, 2009
Last modified: November 30, 2016
This is version 194 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

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 one 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.