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P02468

- LAMC1_MOUSE

UniProt

P02468 - LAMC1_MOUSE

Protein

Laminin subunit gamma-1

Gene

Lamc1

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 149 (01 Oct 2014)
      Sequence version 2 (01 Jul 1989)
      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: MGI
    3. protein binding Source: IntAct

    GO - Biological processi

    1. cell adhesion Source: HGNC
    2. cell migration Source: HGNC
    3. extracellular matrix disassembly Source: HGNC
    4. hemidesmosome assembly Source: HGNC
    5. neuron projection development Source: MGI
    6. protein complex assembly Source: HGNC

    Keywords - Biological processi

    Cell adhesion

    Enzyme and pathway databases

    ReactomeiREACT_196606. ECM proteoglycans.
    REACT_196607. Non-integrin membrane-ECM interactions.
    REACT_199052. Degradation of the extracellular matrix.
    REACT_202342. Laminin interactions.
    REACT_219680. 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:Lamb-2, Lamc-1
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Unplaced

    Organism-specific databases

    MGIiMGI:99914. Lamc1.

    Subcellular locationi

    GO - Cellular componenti

    1. basal lamina Source: MGI
    2. basement membrane Source: HGNC
    3. extracellular region Source: Reactome
    4. laminin-10 complex Source: MGI

    Keywords - Cellular componenti

    Basement membrane, Extracellular matrix, Secreted

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 3333Add
    BLAST
    Chaini34 – 16071574Laminin subunit gamma-1PRO_0000017075Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi58 – 581N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi132 – 1321N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi284 ↔ 293PROSITE-ProRule annotation
    Disulfide bondi286 ↔ 303PROSITE-ProRule annotation
    Disulfide bondi305 ↔ 314PROSITE-ProRule annotation
    Disulfide bondi340 ↔ 349PROSITE-ProRule annotation
    Disulfide bondi342 ↔ 365PROSITE-ProRule annotation
    Disulfide bondi368 ↔ 377PROSITE-ProRule annotation
    Disulfide bondi380 ↔ 393PROSITE-ProRule annotation
    Disulfide bondi396 ↔ 408PROSITE-ProRule annotation
    Disulfide bondi398 ↔ 414PROSITE-ProRule annotation
    Disulfide bondi416 ↔ 425PROSITE-ProRule annotation
    Disulfide bondi428 ↔ 440PROSITE-ProRule annotation
    Disulfide bondi443 ↔ 454PROSITE-ProRule annotation
    Disulfide bondi445 ↔ 461PROSITE-ProRule annotation
    Disulfide bondi463 ↔ 472PROSITE-ProRule annotation
    Disulfide bondi475 ↔ 490PROSITE-ProRule annotation
    Glycosylationi574 – 5741N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi648 – 6481N-linked (GlcNAc...)1 Publication
    Disulfide bondi722 ↔ 731PROSITE-ProRule annotation
    Disulfide bondi724 ↔ 738PROSITE-ProRule annotation
    Disulfide bondi740 ↔ 749PROSITE-ProRule annotation
    Disulfide bondi752 ↔ 768PROSITE-ProRule annotation
    Disulfide bondi771 ↔ 779
    Disulfide bondi773 ↔ 790
    Disulfide bondi793 ↔ 802
    Disulfide bondi805 ↔ 823
    Disulfide bondi826 ↔ 840
    Disulfide bondi828 ↔ 847
    Disulfide bondi850 ↔ 859
    Disulfide bondi862 ↔ 879
    Disulfide bondi882 ↔ 896
    Disulfide bondi884 ↔ 903
    Disulfide bondi905 ↔ 914
    Disulfide bondi917 ↔ 930
    Disulfide bondi933 ↔ 945PROSITE-ProRule annotation
    Disulfide bondi935 ↔ 952PROSITE-ProRule annotation
    Disulfide bondi954 ↔ 963PROSITE-ProRule annotation
    Disulfide bondi966 ↔ 978PROSITE-ProRule annotation
    Disulfide bondi981 ↔ 993PROSITE-ProRule annotation
    Disulfide bondi983 ↔ 999PROSITE-ProRule annotation
    Disulfide bondi1001 ↔ 1010PROSITE-ProRule annotation
    Disulfide bondi1013 ↔ 1026PROSITE-ProRule annotation
    Glycosylationi1020 – 10201N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi1029 – 1029InterchainCurated
    Disulfide bondi1032 – 1032InterchainCurated
    Glycosylationi1105 – 11051N-linked (GlcNAc...)1 Publication
    Glycosylationi1159 – 11591N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi1173 – 11731N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi1203 – 12031N-linked (GlcNAc...)1 Publication
    Glycosylationi1221 – 12211N-linked (GlcNAc...)1 Publication
    Glycosylationi1239 – 12391N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi1378 – 13781N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi1393 – 13931N-linked (GlcNAc...)1 Publication
    Glycosylationi1437 – 14371N-linked (GlcNAc...)Sequence Analysis
    Modified residuei1491 – 14911PhosphoserineBy similarity
    Disulfide bondi1598 – 1598Interchain (with beta-1 chain)

    Keywords - PTMi

    Disulfide bond, Glycoprotein, Phosphoprotein

    Proteomic databases

    MaxQBiP02468.
    PaxDbiP02468.
    PRIDEiP02468.

    PTM databases

    PhosphoSiteiP02468.

    Expressioni

    Tissue specificityi

    Found in the basement membranes (major component).

    Gene expression databases

    CleanExiMM_LAMC1.
    GenevestigatoriP02468.

    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).

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    Lamb1P024694EBI-7059830,EBI-6662997

    Protein-protein interaction databases

    DIPiDIP-41793N.
    IntActiP02468. 4 interactions.
    MINTiMINT-1031545.

    Structurei

    Secondary structure

    1
    1607
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Turni55 – 584
    Beta strandi62 – 643
    Beta strandi72 – 754
    Beta strandi87 – 904
    Beta strandi92 – 943
    Turni95 – 973
    Helixi101 – 1044
    Beta strandi110 – 1123
    Helixi121 – 1233
    Beta strandi126 – 1283
    Beta strandi131 – 15323
    Beta strandi156 – 16813
    Beta strandi171 – 1777
    Helixi180 – 1845
    Beta strandi202 – 2054
    Beta strandi212 – 2143
    Beta strandi216 – 2216
    Turni222 – 2254
    Helixi229 – 2346
    Helixi236 – 2416
    Beta strandi243 – 25311
    Helixi259 – 2613
    Helixi265 – 2684
    Beta strandi274 – 28411
    Beta strandi293 – 2953
    Beta strandi301 – 3033
    Beta strandi309 – 3113
    Helixi342 – 3443
    Beta strandi349 – 3513
    Helixi353 – 3586
    Beta strandi363 – 3653
    Turni369 – 3713
    Beta strandi372 – 3743
    Beta strandi382 – 3854
    Beta strandi779 – 7813
    Beta strandi783 – 7853
    Beta strandi788 – 7903
    Beta strandi797 – 7993
    Beta strandi809 – 8124
    Beta strandi816 – 8194
    Beta strandi821 – 8255
    Beta strandi834 – 8374
    Turni842 – 8443
    Beta strandi846 – 8494
    Turni856 – 8594
    Beta strandi866 – 8683
    Helixi875 – 8773
    Beta strandi878 – 8814
    Turni886 – 8883
    Helixi890 – 8923
    Turni898 – 9003
    Beta strandi909 – 9113
    Helixi924 – 9263

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1KLOX-ray2.10A771-932[»]
    1NPEX-ray2.30B769-932[»]
    1TLENMR-A824-881[»]
    4AQTX-ray3.20A33-395[»]
    ProteinModelPortaliP02468.
    SMRiP02468. Positions 37-492, 680-1012, 1283-1522.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP02468.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini44 – 283240Laminin N-terminalPROSITE-ProRule annotationAdd
    BLAST
    Domaini284 – 33956Laminin EGF-like 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini340 – 39556Laminin EGF-like 2PROSITE-ProRule annotationAdd
    BLAST
    Domaini396 – 44247Laminin EGF-like 3PROSITE-ProRule annotationAdd
    BLAST
    Domaini443 – 49250Laminin EGF-like 4PROSITE-ProRule annotationAdd
    BLAST
    Domaini493 – 50210Laminin EGF-like 5; first partPROSITE-ProRule annotation
    Domaini512 – 687176Laminin IV type APROSITE-ProRule annotationAdd
    BLAST
    Domaini688 – 72134Laminin EGF-like 5; second partPROSITE-ProRule annotationAdd
    BLAST
    Domaini722 – 77049Laminin EGF-like 6PROSITE-ProRule annotationAdd
    BLAST
    Domaini771 – 82555Laminin EGF-like 7PROSITE-ProRule annotationAdd
    BLAST
    Domaini826 – 88156Laminin EGF-like 8; nidogen-bindingPROSITE-ProRule annotationAdd
    BLAST
    Domaini882 – 93251Laminin EGF-like 9PROSITE-ProRule annotationAdd
    BLAST
    Domaini933 – 98048Laminin EGF-like 10PROSITE-ProRule annotationAdd
    BLAST
    Domaini981 – 102848Laminin EGF-like 11PROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni1029 – 1607579Domain II and IAdd
    BLAST

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili1034 – 1594561Sequence 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.
    InParanoidiP02468.
    PhylomeDBiP02468.

    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. 11 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. 10 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.

    P02468-1 [UniParc]FASTAAdd to Basket

    « Hide

    MTGGGRAALA LQPRGRLWPL LAVLAAVAGC VRAAMDECAD EGGRPQRCMP     50
    EFVNAAFNVT VVATNTCGTP PEEYCVQTGV TGVTKSCHLC DAGQQHLQHG 100
    AAFLTDYNNQ ADTTWWQSQT MLAGVQYPNS INLTLHLGKA FDITYVRLKF 150
    HTSRPESFAI YKRTREDGPW IPYQYYSGSC ENTYSKANRG FIRTGGDEQQ 200
    ALCTDEFSDI SPLTGGNVAF STLEGRPSAY NFDNSPVLQE WVTATDIRVT 250
    LNRLNTFGDE VFNEPKVLKS YYYAISDFAV GGRCKCNGHA SECVKNEFDK 300
    LMCNCKHNTY GVDCEKCLPF FNDRPWRRAT AESASESLPC DCNGRSQECY 350
    FDPELYRSTG HGGHCTNCRD NTDGAKCERC RENFFRLGNT EACSPCHCSP 400
    VGSLSTQCDS YGRCSCKPGV MGDKCDRCQP GFHSLTEAGC RPCSCDLRGS 450
    TDECNVETGR CVCKDNVEGF NCERCKPGFF NLESSNPKGC TPCFCFGHSS 500
    VCTNAVGYSV YDISSTFQID EDGWRVEQRD GSEASLEWSS DRQDIAVISD 550
    SYFPRYFIAP VKFLGNQVLS YGQNLSFSFR VDRRDTRLSA EDLVLEGAGL 600
    RVSVPLIAQG NSYPSETTVK YIFRLHEATD YPWRPALSPF EFQKLLNNLT 650
    SIKIRGTYSE RTAGYLDDVT LQSARPGPGV PATWVESCTC PVGYGGQFCE 700
    TCLPGYRRET PSLGPYSPCV LCTCNGHSET CDPETGVCDC RDNTAGPHCE 750
    KCSDGYYGDS TLGTSSDCQP CPCPGGSSCA IVPKTKEVVC THCPTGTAGK 800
    RCELCDDGYF GDPLGSNGPV RLCRPCQCND NIDPNAVGNC NRLTGECLKC 850
    IYNTAGFYCD RCKEGFFGNP LAPNPADKCK ACACNPYGTV QQQSSCNPVT 900
    GQCQCLPHVS GRDCGTCDPG YYNLQSGQGC ERCDCHALGS TNGQCDIRTG 950
    QCECQPGITG QHCERCETNH FGFGPEGCKP CDCHHEGSLS LQCKDDGRCE 1000
    CREGFVGNRC DQCEENYFYN RSWPGCQECP ACYRLVKDKA AEHRVKLQEL 1050
    ESLIANLGTG DDMVTDQAFE DRLKEAEREV TDLLREAQEV KDVDQNLMDR 1100
    LQRVNSSLHS QISRLQNIRN TIEETGILAE RARSRVESTE QLIEIASREL 1150
    EKAKMAAANV SITQPESTGE PNNMTLLAEE ARRLAERHKQ EADDIVRVAK 1200
    TANETSAEAY NLLLRTLAGE NQTALEIEEL NRKYEQAKNI SQDLEKQAAR 1250
    VHEEAKRAGD KAVEIYASVA QLTPVDSEAL ENEANKIKKE AADLDRLIDQ 1300
    KLKDYEDLRE DMRGKEHEVK NLLEKGKAEQ QTADQLLARA DAAKALAEEA 1350
    AKKGRSTLQE ANDILNNLKD FDRRVNDNKT AAEEALRRIP AINRTIAEAN 1400
    EKTREAQLAL GNAAADATEA KNKAHEAERI ASAVQKNATS TKADAERTFG 1450
    EVTDLDNEVN GMLRQLEEAE NELKRKQDDA DQDMMMAGMA SQAAQEAELN 1500
    ARKAKNSVSS LLSQLNNLLD QLGQLDTVDL NKLNEIEGSL NKAKDEMKAS 1550
    DLDRKVSDLE SEARKQEAAI MDYNRDIAEI IKDIHNLEDI KKTLPTGCFN 1600
    TPSIEKP 1607
    Length:1,607
    Mass (Da):177,298
    Last modified:July 1, 1989 - v2
    Checksum:i81B7B08E4869F242
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti216 – 2161G → A in AAA39409. (PubMed:2836421)Curated
    Sequence conflicti260 – 2601E → D(PubMed:3167041)Curated
    Sequence conflicti337 – 3371S → C in AAA39408. (PubMed:3167041)Curated
    Sequence conflicti447 – 4482LR → PS in AAA39408. (PubMed:3167041)Curated
    Sequence conflicti544 – 5441D → Y in AAA39408. (PubMed:3167041)Curated
    Sequence conflicti662 – 6621T → S in AAA39408. (PubMed:3167041)Curated
    Sequence conflicti886 – 8861Missing in AAA39408. (PubMed:3167041)Curated
    Sequence conflicti1158 – 11581Missing in AAA39408. (PubMed:3167041)Curated
    Sequence conflicti1434 – 14341V → A in AAA39408. (PubMed:3167041)Curated
    Sequence conflicti1475 – 14751R → K in CAA28838. (PubMed:6209134)Curated
    Sequence conflicti1576 – 15761D → N in CAA28838. (PubMed:6209134)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X05211 mRNA. Translation: CAA28838.1.
    J03484 mRNA. Translation: AAA39405.1.
    J02930 mRNA. Translation: AAA39408.1.
    J03749 Genomic DNA. Translation: AAA39409.1.
    CCDSiCCDS15370.1.
    PIRiA28469. MMMSB2.
    S55783.
    UniGeneiMm.1249.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X05211 mRNA. Translation: CAA28838.1 .
    J03484 mRNA. Translation: AAA39405.1 .
    J02930 mRNA. Translation: AAA39408.1 .
    J03749 Genomic DNA. Translation: AAA39409.1 .
    CCDSi CCDS15370.1.
    PIRi A28469. MMMSB2.
    S55783.
    UniGenei Mm.1249.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1KLO X-ray 2.10 A 771-932 [» ]
    1NPE X-ray 2.30 B 769-932 [» ]
    1TLE NMR - A 824-881 [» ]
    4AQT X-ray 3.20 A 33-395 [» ]
    ProteinModelPortali P02468.
    SMRi P02468. Positions 37-492, 680-1012, 1283-1522.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    DIPi DIP-41793N.
    IntActi P02468. 4 interactions.
    MINTi MINT-1031545.

    PTM databases

    PhosphoSitei P02468.

    Proteomic databases

    MaxQBi P02468.
    PaxDbi P02468.
    PRIDEi P02468.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Organism-specific databases

    MGIi MGI:99914. Lamc1.

    Phylogenomic databases

    eggNOGi NOG235720.
    HOGENOMi HOG000019301.
    HOVERGENi HBG100808.
    InParanoidi P02468.
    PhylomeDBi P02468.

    Enzyme and pathway databases

    Reactomei REACT_196606. ECM proteoglycans.
    REACT_196607. Non-integrin membrane-ECM interactions.
    REACT_199052. Degradation of the extracellular matrix.
    REACT_202342. Laminin interactions.
    REACT_219680. L1CAM interactions.

    Miscellaneous databases

    EvolutionaryTracei P02468.
    PROi P02468.
    SOURCEi Search...

    Gene expression databases

    CleanExi MM_LAMC1.
    Genevestigatori P02468.

    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. 11 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. 10 hits.
    PS50027. EGF_LAM_2. 10 hits.
    PS51115. LAMININ_IVA. 1 hit.
    PS51117. LAMININ_NTER. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "The laminin B2 chain has a multidomain structure homologous to the B1 chain."
      Sasaki M., Yamada Y.
      J. Biol. Chem. 262:17111-17117(1987) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    2. "Primary structure of the mouse laminin B2 chain and comparison with laminin B1."
      Durkin M.E., Bartos B.B., Liu S.-H., Phillips S.L., Chung A.E.
      Biochemistry 27:5198-5204(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    3. "The laminin B2 chain promoter contains unique repeat sequences and is active in transient transfection."
      Ogawa K., Burbelo P.D., Sasaki M., Yamada Y.
      J. Biol. Chem. 263:8384-8389(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-239.
    4. "Sequencing of laminin B chain cDNAs reveals C-terminal regions of coiled-coil alpha-helix."
      Barlow D.P., Green N.M., Kurkinen M., Hogan B.L.M.
      EMBO J. 3:2355-2362(1984) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1391-1607.
    5. "Mass-spectrometric identification and relative quantification of N-linked cell surface glycoproteins."
      Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M., Schiess R., Aebersold R., Watts J.D.
      Nat. Biotechnol. 27:378-386(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-648; ASN-1105; ASN-1203; ASN-1221 AND ASN-1393.
    6. "Crystal structure of three consecutive laminin-type epidermal growth factor-like (LE) modules of laminin gamma1 chain harboring the nidogen binding site."
      Stetefeld J., Mayer U., Timpl R., Huber R.
      J. Mol. Biol. 257:644-657(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 771-932.
    7. "Structure of the nidogen binding LE module of the laminin gamma1 chain in solution."
      Baumgartner R., Czisch M., Mayer U., Poeschl E., Huber R., Timpl R., Holak T.A.
      J. Mol. Biol. 257:658-668(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF 824-881.

    Entry informationi

    Entry nameiLAMC1_MOUSE
    AccessioniPrimary (citable) accession number: P02468
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 21, 1986
    Last sequence update: July 1, 1989
    Last modified: October 1, 2014
    This is version 149 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3