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P11047

- LAMC1_HUMAN

UniProt

P11047 - LAMC1_HUMAN

Protein

Laminin subunit gamma-1

Gene

LAMC1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 171 (01 Oct 2014)
      Sequence version 3 (03 Mar 2009)
      Previous versions | rss
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    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

    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: Chromosome 1

    Organism-specific databases

    HGNCiHGNC:6492. LAMC1.

    Subcellular locationi

    GO - Cellular componenti

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

    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.
    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. 20 interactions.
    IntActiP11047. 10 interactions.
    MINTiMINT-1184520.
    STRINGi9606.ENSP00000258341.

    Structurei

    3D structure databases

    ProteinModelPortaliP11047.
    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.
    HOGENOMiHOG000019301.
    HOVERGENiHBG100808.
    InParanoidiP11047.
    KOiK05635.
    OMAiEATDYPW.
    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

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    MRGSHRAAPA LRPRGRLWPV LAVLAAAAAA GCAQAAMDEC TDEGGRPQRC     50
    MPEFVNAAFN VTVVATNTCG TPPEEYCVQT GVTGVTKSCH LCDAGQPHLQ 100
    HGAAFLTDYN NQADTTWWQS QTMLAGVQYP SSINLTLHLG KAFDITYVRL 150
    KFHTSRPESF AIYKRTREDG PWIPYQYYSG SCENTYSKAN RGFIRTGGDE 200
    QQALCTDEFS DISPLTGGNV AFSTLEGRPS AYNFDNSPVL QEWVTATDIR 250
    VTLNRLNTFG DEVFNDPKVL KSYYYAISDF AVGGRCKCNG HASECMKNEF 300
    DKLVCNCKHN TYGVDCEKCL PFFNDRPWRR ATAESASECL PCDCNGRSQE 350
    CYFDPELYRS TGHGGHCTNC QDNTDGAHCE RCRENFFRLG NNEACSSCHC 400
    SPVGSLSTQC DSYGRCSCKP GVMGDKCDRC QPGFHSLTEA GCRPCSCDPS 450
    GSIDECNIET GRCVCKDNVE GFNCERCKPG FFNLESSNPR GCTPCFCFGH 500
    SSVCTNAVGY SVYSISSTFQ IDEDGWRAEQ RDGSEASLEW SSERQDIAVI 550
    SDSYFPRYFI APAKFLGKQV LSYGQNLSFS FRVDRRDTRL SAEDLVLEGA 600
    GLRVSVPLIA QGNSYPSETT VKYVFRLHEA TDYPWRPALT PFEFQKLLNN 650
    LTSIKIRGTY SERSAGYLDD VTLASARPGP GVPATWVESC TCPVGYGGQF 700
    CEMCLSGYRR ETPNLGPYSP CVLCACNGHS ETCDPETGVC NCRDNTAGPH 750
    CEKCSDGYYG DSTAGTSSDC QPCPCPGGSS CAVVPKTKEV VCTNCPTGTT 800
    GKRCELCDDG YFGDPLGRNG PVRLCRLCQC SDNIDPNAVG NCNRLTGECL 850
    KCIYNTAGFY CDRCKDGFFG NPLAPNPADK CKACNCNLYG TMKQQSSCNP 900
    VTGQCECLPH VTGQDCGACD PGFYNLQSGQ GCERCDCHAL GSTNGQCDIR 950
    TGQCECQPGI TGQHCERCEV NHFGFGPEGC KPCDCHPEGS LSLQCKDDGR 1000
    CECREGFVGN RCDQCEENYF YNRSWPGCQE CPACYRLVKD KVADHRVKLQ 1050
    ELESLIANLG TGDEMVTDQA FEDRLKEAER EVMDLLREAQ DVKDVDQNLM 1100
    DRLQRVNNTL SSQISRLQNI RNTIEETGNL AEQARAHVEN TERLIEIASR 1150
    ELEKAKVAAA NVSVTQPEST GDPNNMTLLA EEARKLAERH KQEADDIVRV 1200
    AKTANDTSTE AYNLLLRTLA GENQTAFEIE ELNRKYEQAK NISQDLEKQA 1250
    ARVHEEAKRA GDKAVEIYAS VAQLSPLDSE TLENEANNIK MEAENLEQLI 1300
    DQKLKDYEDL REDMRGKELE VKNLLEKGKT EQQTADQLLA RADAAKALAE 1350
    EAAKKGRDTL QEANDILNNL KDFDRRVNDN KTAAEEALRK IPAINQTITE 1400
    ANEKTREAQQ ALGSAAADAT EAKNKAHEAE RIASAVQKNA TSTKAEAERT 1450
    FAEVTDLDNE VNNMLKQLQE AEKELKRKQD DADQDMMMAG MASQAAQEAE 1500
    INARKAKNSV TSLLSIINDL LEQLGQLDTV DLNKLNEIEG TLNKAKDEMK 1550
    VSDLDRKVSD LENEAKKQEA AIMDYNRDIE EIMKDIRNLE DIRKTLPSGC 1600
    FNTPSIEKP 1609
    Length:1,609
    Mass (Da):177,603
    Last modified:March 3, 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:
    EMBL
    GenBank
    DDBJ
    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:
    EMBL
    GenBank
    DDBJ
    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 .
    CCDSi CCDS1351.1.
    PIRi S13548. MMHUB2.
    RefSeqi NP_002284.3. NM_002293.3.
    UniGenei Hs.609663.

    3D structure databases

    ProteinModelPortali P11047.
    SMRi P11047. Positions 39-396, 773-934.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 110109. 20 interactions.
    IntActi P11047. 10 interactions.
    MINTi MINT-1184520.
    STRINGi 9606.ENSP00000258341.

    Chemistry

    ChEMBLi CHEMBL2364187.
    DrugBanki DB00009. Alteplase.
    DB00029. Anistreplase.
    DB00015. Reteplase.
    DB00031. Tenecteplase.

    PTM databases

    PhosphoSitei P11047.

    Polymorphism databases

    DMDMi 224471885.

    Proteomic databases

    MaxQBi P11047.
    PaxDbi P11047.
    PRIDEi P11047.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000258341 ; ENSP00000258341 ; ENSG00000135862 .
    GeneIDi 3915.
    KEGGi hsa:3915.
    UCSCi uc001gpy.4. human.

    Organism-specific databases

    CTDi 3915.
    GeneCardsi GC01P182992.
    H-InvDB HIX0001405.
    HGNCi HGNC:6492. LAMC1.
    HPAi CAB004486.
    HPA001908.
    HPA001909.
    MIMi 150290. gene.
    neXtProti NX_P11047.
    PharmGKBi PA30280.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG235720.
    HOGENOMi HOG000019301.
    HOVERGENi HBG100808.
    InParanoidi P11047.
    KOi K05635.
    OMAi EATDYPW.
    OrthoDBi EOG7SR4KJ.
    PhylomeDBi P11047.
    TreeFami TF352481.

    Enzyme and pathway databases

    Reactomei REACT_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

    ChiTaRSi LAMC1. human.
    GeneWikii Laminin,_gamma_1.
    GenomeRNAii 3915.
    NextBioi 15381.
    PROi P11047.
    SOURCEi Search...

    Gene expression databases

    Bgeei P11047.
    CleanExi HS_LAMB2.
    HS_LAMC1.
    Genevestigatori P11047.

    Family and domain databases

    Gene3Di 2.60.120.260. 1 hit.
    InterProi IPR013032. EGF-like_CS.
    IPR002049. EGF_laminin.
    IPR008979. Galactose-bd-like.
    IPR018031. Laminin_B_subgr.
    IPR000034. Laminin_B_type_IV.
    IPR008211. Laminin_N.
    [Graphical view ]
    Pfami PF00052. Laminin_B. 1 hit.
    PF00053. Laminin_EGF. 10 hits.
    PF00055. Laminin_N. 1 hit.
    [Graphical view ]
    SMARTi SM00180. EGF_Lam. 10 hits.
    SM00281. LamB. 1 hit.
    SM00136. LamNT. 1 hit.
    [Graphical view ]
    PROSITEi 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 ]
    ProtoNeti Search...

    Publicationsi

    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.
      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. 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. 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: July 1, 1989
    Last sequence update: March 3, 2009
    Last modified: October 1, 2014
    This is version 171 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