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P02469

- LAMB1_MOUSE

UniProt

P02469 - LAMB1_MOUSE

Protein

Laminin subunit beta-1

Gene

Lamb1

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 140 (01 Oct 2014)
      Sequence version 3 (27 Jul 2011)
      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. Involved in the organization of the laminar architecture of the cerebral cortex By similarity. It is probably required for the integrity of the basement membrane/glia limitans that serves as an anchor point for the endfeet of radial glial cells and as a physical barrier to migrating neurons By similarity. Radial glial cells play a central role in cerebral cortical development, where they act both as the proliferative unit of the cerebral cortex and a scaffold for neurons migrating toward the pial surface By similarity.By similarity

    GO - Molecular functioni

    1. enzyme binding Source: MGI
    2. extracellular matrix structural constituent Source: HGNC
    3. glycosphingolipid binding Source: MGI
    4. integrin binding Source: MGI
    5. protein binding Source: UniProtKB

    GO - Biological processi

    1. cell adhesion Source: UniProtKB-KW
    2. cell migration Source: MGI
    3. embryo implantation Source: MGI
    4. learning or memory Source: UniProtKB
    5. negative regulation of cell adhesion Source: UniProtKB
    6. neuron projection development Source: HGNC
    7. odontogenesis Source: HGNC
    8. positive regulation of cell migration 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 beta-1
    Alternative name(s):
    Laminin B1 chain
    Laminin-1 subunit beta
    Laminin-10 subunit beta
    Laminin-12 subunit beta
    Laminin-2 subunit beta
    Laminin-6 subunit beta
    Laminin-8 subunit beta
    Gene namesi
    Name:Lamb1
    Synonyms:Lamb-1, Lamb1-1
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 12

    Organism-specific databases

    MGIiMGI:96743. Lamb1.

    Subcellular locationi

    GO - Cellular componenti

    1. basal lamina Source: MGI
    2. basement membrane Source: UniProtKB
    3. extracellular region Source: Reactome
    4. laminin-10 complex Source: HGNC
    5. laminin-1 complex Source: HGNC
    6. laminin-2 complex Source: HGNC
    7. laminin-8 complex Source: HGNC
    8. laminin complex Source: MGI
    9. perinuclear region of cytoplasm Source: UniProtKB
    10. proteinaceous extracellular matrix Source: MGI

    Keywords - Cellular componenti

    Basement membrane, Extracellular matrix, Secreted

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2121Add
    BLAST
    Chaini22 – 17861765Laminin subunit beta-1PRO_0000017066Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi120 – 1201N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi271 ↔ 280PROSITE-ProRule annotation
    Disulfide bondi273 ↔ 298PROSITE-ProRule annotation
    Disulfide bondi300 ↔ 309PROSITE-ProRule annotation
    Disulfide bondi312 ↔ 332PROSITE-ProRule annotation
    Disulfide bondi335 ↔ 344PROSITE-ProRule annotation
    Disulfide bondi337 ↔ 362PROSITE-ProRule annotation
    Glycosylationi356 – 3561N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi365 ↔ 374PROSITE-ProRule annotation
    Disulfide bondi377 ↔ 395PROSITE-ProRule annotation
    Disulfide bondi398 ↔ 411PROSITE-ProRule annotation
    Disulfide bondi400 ↔ 426PROSITE-ProRule annotation
    Disulfide bondi428 ↔ 437PROSITE-ProRule annotation
    Disulfide bondi440 ↔ 455PROSITE-ProRule annotation
    Disulfide bondi458 ↔ 472PROSITE-ProRule annotation
    Disulfide bondi460 ↔ 479PROSITE-ProRule annotation
    Disulfide bondi481 ↔ 490PROSITE-ProRule annotation
    Disulfide bondi493 ↔ 507PROSITE-ProRule annotation
    Disulfide bondi510 ↔ 522PROSITE-ProRule annotation
    Disulfide bondi512 ↔ 529PROSITE-ProRule annotation
    Glycosylationi519 – 5191N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi531 ↔ 540PROSITE-ProRule annotation
    Glycosylationi677 – 6771N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi773 ↔ 785PROSITE-ProRule annotation
    Disulfide bondi775 ↔ 792PROSITE-ProRule annotation
    Disulfide bondi794 ↔ 803PROSITE-ProRule annotation
    Disulfide bondi806 ↔ 818PROSITE-ProRule annotation
    Disulfide bondi821 ↔ 833PROSITE-ProRule annotation
    Disulfide bondi823 ↔ 840PROSITE-ProRule annotation
    Disulfide bondi842 ↔ 851PROSITE-ProRule annotation
    Disulfide bondi854 ↔ 864PROSITE-ProRule annotation
    Disulfide bondi867 ↔ 876PROSITE-ProRule annotation
    Disulfide bondi869 ↔ 883PROSITE-ProRule annotation
    Disulfide bondi886 ↔ 895PROSITE-ProRule annotation
    Disulfide bondi898 ↔ 914PROSITE-ProRule annotation
    Disulfide bondi917 ↔ 933PROSITE-ProRule annotation
    Disulfide bondi919 ↔ 944PROSITE-ProRule annotation
    Disulfide bondi946 ↔ 955PROSITE-ProRule annotation
    Disulfide bondi958 ↔ 973PROSITE-ProRule annotation
    Disulfide bondi976 ↔ 990PROSITE-ProRule annotation
    Disulfide bondi978 ↔ 997PROSITE-ProRule annotation
    Disulfide bondi1000 ↔ 1009PROSITE-ProRule annotation
    Disulfide bondi1012 ↔ 1025PROSITE-ProRule annotation
    Disulfide bondi1028 ↔ 1040PROSITE-ProRule annotation
    Disulfide bondi1030 ↔ 1054PROSITE-ProRule annotation
    Glycosylationi1041 – 10411N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi1056 ↔ 1065PROSITE-ProRule annotation
    Disulfide bondi1068 ↔ 1081PROSITE-ProRule annotation
    Disulfide bondi1084 ↔ 1096PROSITE-ProRule annotation
    Disulfide bondi1086 ↔ 1103PROSITE-ProRule annotation
    Disulfide bondi1105 ↔ 1114PROSITE-ProRule annotation
    Disulfide bondi1117 ↔ 1129PROSITE-ProRule annotation
    Disulfide bondi1132 ↔ 1144PROSITE-ProRule annotation
    Disulfide bondi1134 ↔ 1151PROSITE-ProRule annotation
    Disulfide bondi1153 ↔ 1162PROSITE-ProRule annotation
    Disulfide bondi1165 ↔ 1176PROSITE-ProRule annotation
    Disulfide bondi1179 – 1179InterchainCurated
    Disulfide bondi1182 – 1182InterchainCurated
    Glycosylationi1195 – 11951N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi1279 – 12791N-linked (GlcNAc...)1 Publication
    Glycosylationi1336 – 13361N-linked (GlcNAc...)1 Publication
    Glycosylationi1343 – 13431N-linked (GlcNAc...)1 Publication
    Glycosylationi1487 – 14871N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi1542 – 15421N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi1643 – 16431N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi1785 – 1785InterchainCurated

    Keywords - PTMi

    Disulfide bond, Glycoprotein

    Proteomic databases

    MaxQBiP02469.
    PaxDbiP02469.
    PRIDEiP02469.

    PTM databases

    PhosphoSiteiP02469.

    Expressioni

    Tissue specificityi

    Widely expressed in the embryo. High levels are detected in the cerebellar basement membrane, at postnatal day 7.1 Publication

    Gene expression databases

    ArrayExpressiP02469.
    BgeeiP02469.
    CleanExiMM_LAMB1-1.
    GenevestigatoriP02469.

    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. Beta-1 is a subunit of laminin-1 (laminin-111 or EHS laminin), laminin-2 (laminin-211 or merosin), laminin-6 (laminin-311 or K-laminin), laminin-8 (laminin-411), laminin-10 (laminin-511) and laminin-12 (laminin-213).

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    AGRNP316962EBI-6662997,EBI-457650From a different organism.
    Lamc1P024684EBI-6662997,EBI-7059830

    Protein-protein interaction databases

    IntActiP02469. 6 interactions.
    MINTiMINT-1206337.

    Structurei

    Secondary structure

    1
    1786
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi30 – 323
    Beta strandi40 – 434
    Helixi47 – 493
    Beta strandi58 – 603
    Beta strandi62 – 676
    Beta strandi69 – 724
    Beta strandi74 – 796
    Turni87 – 893
    Helixi96 – 983
    Beta strandi122 – 14221
    Beta strandi146 – 15510
    Beta strandi161 – 1699
    Turni170 – 1723
    Beta strandi173 – 1775
    Turni200 – 2023
    Beta strandi204 – 2107
    Beta strandi212 – 2143
    Helixi222 – 2287
    Beta strandi229 – 23911
    Helixi252 – 2554
    Beta strandi261 – 27010
    Beta strandi304 – 3096
    Beta strandi342 – 3465
    Helixi348 – 3536
    Beta strandi360 – 3645
    Beta strandi369 – 3713
    Beta strandi381 – 3833
    Beta strandi385 – 3873
    Beta strandi395 – 3973
    Turni402 – 4043
    Helixi407 – 4093
    Helixi417 – 4193
    Turni434 – 4374
    Beta strandi454 – 4574
    Turni462 – 4643
    Turni474 – 4763
    Turni488 – 4903

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    4AQSX-ray3.11A22-542[»]
    ProteinModelPortaliP02469.
    SMRiP02469. Positions 29-492.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini31 – 270240Laminin N-terminalPROSITE-ProRule annotationAdd
    BLAST
    Domaini271 – 33464Laminin EGF-like 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini335 – 39763Laminin EGF-like 2PROSITE-ProRule annotationAdd
    BLAST
    Domaini398 – 45760Laminin EGF-like 3PROSITE-ProRule annotationAdd
    BLAST
    Domaini458 – 50952Laminin EGF-like 4PROSITE-ProRule annotationAdd
    BLAST
    Domaini510 – 54031Laminin EGF-like 5; truncatedPROSITE-ProRule annotationAdd
    BLAST
    Domaini549 – 767219Laminin IV type BPROSITE-ProRule annotationAdd
    BLAST
    Domaini773 – 82048Laminin EGF-like 6PROSITE-ProRule annotationAdd
    BLAST
    Domaini821 – 86646Laminin EGF-like 7PROSITE-ProRule annotationAdd
    BLAST
    Domaini867 – 91650Laminin EGF-like 8PROSITE-ProRule annotationAdd
    BLAST
    Domaini917 – 97559Laminin EGF-like 9PROSITE-ProRule annotationAdd
    BLAST
    Domaini976 – 102752Laminin EGF-like 10PROSITE-ProRule annotationAdd
    BLAST
    Domaini1028 – 108356Laminin EGF-like 11PROSITE-ProRule annotationAdd
    BLAST
    Domaini1084 – 113148Laminin EGF-like 12PROSITE-ProRule annotationAdd
    BLAST
    Domaini1132 – 117847Laminin EGF-like 13PROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni1179 – 1397219Domain IIAdd
    BLAST
    Regioni1398 – 143033Domain alphaAdd
    BLAST
    Regioni1431 – 1786356Domain IAdd
    BLAST

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili1216 – 1315100Sequence AnalysisAdd
    BLAST
    Coiled coili1368 – 138821Sequence AnalysisAdd
    BLAST
    Coiled coili1448 – 1778331Sequence AnalysisAdd
    BLAST

    Sequence similaritiesi

    Contains 13 laminin EGF-like domains.PROSITE-ProRule annotation
    Contains 1 laminin IV type B 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

    eggNOGiNOG241384.
    GeneTreeiENSGT00720000108616.
    HOVERGENiHBG052301.
    InParanoidiP02469.
    KOiK05636.
    OrthoDBiEOG75XGK0.

    Family and domain databases

    InterProiIPR002049. EGF_laminin.
    IPR013015. Laminin_IV.
    IPR008211. Laminin_N.
    [Graphical view]
    PfamiPF00053. Laminin_EGF. 13 hits.
    PF00055. Laminin_N. 1 hit.
    [Graphical view]
    SMARTiSM00180. EGF_Lam. 13 hits.
    SM00136. LamNT. 1 hit.
    [Graphical view]
    PROSITEiPS00022. EGF_1. 9 hits.
    PS01186. EGF_2. 2 hits.
    PS01248. EGF_LAM_1. 11 hits.
    PS50027. EGF_LAM_2. 13 hits.
    PS51116. LAMININ_IVB. 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.

    P02469-1 [UniParc]FASTAAdd to Basket

    « Hide

    MGLLQVFAFG VLALWGTRVC AQEPEFSYGC AEGSCYPATG DLLIGRAQKL     50
    SVTSTCGLHK PEPYCIVSHL QEDKKCFICD SRDPYHETLN PDSHLIENVV 100
    TTFAPNRLKI WWQSENGVEN VTIQLDLEAE FHFTHLIMTF KTFRPAAMLI 150
    ERSSDFGKAW GVYRYFAYDC ESSFPGISTG PMKKVDDIIC DSRYSDIEPS 200
    TEGEVIFRAL DPAFKIEDPY SPRIQNLLKI TNLRIKFVKL HTLGDNLLDS 250
    RMEIREKYYY AVYDMVVRGN CFCYGHASEC APVDGVNEEV EGMVHGHCMC 300
    RHNTKGLNCE LCMDFYHDLP WRPAEGRNSN ACKKCNCNEH SSSCHFDMAV 350
    FLATGNVSGG VCDNCQHNTM GRNCEQCKPF YFQHPERDIR DPNLCEPCTC 400
    DPAGSENGGI CDGYTDFSVG LIAGQCRCKL HVEGERCDVC KEGFYDLSAE 450
    DPYGCKSCAC NPLGTIPGGN PCDSETGYCY CKRLVTGQRC DQCLPQHWGL 500
    SNDLDGCRPC DCDLGGALNN SCSEDSGQCS CLPHMIGRQC NEVESGYYFT 550
    TLDHYIYEAE EANLGPGVIV VERQYIQDRI PSWTGPGFVR VPEGAYLEFF 600
    IDNIPYSMEY EILIRYEPQL PDHWEKAVIT VQRPGKIPAS SRCGNTVPDD 650
    DNQVVSLSPG SRYVVLPRPV CFEKGMNYTV RLELPQYTAS GSDVESPYTF 700
    IDSLVLMPYC KSLDIFTVGG SGDGEVTNSA WETFQRYRCL ENSRSVVKTP 750
    MTDVCRNIIF SISALIHQTG LACECDPQGS LSSVCDPNGG QCQCRPNVVG 800
    RTCNRCAPGT FGFGPNGCKP CDCHLQGSAS AFCDAITGQC HCFQGIYARQ 850
    CDRCLPGYWG FPSCQPCQCN GHALDCDTVT GECLSCQDYT TGHNCERCLA 900
    GYYGDPIIGS GDHCRPCPCP DGPDSGRQFA RSCYQDPVTL QLACVCDPGY 950
    IGSRCDDCAS GFFGNPSDFG GSCQPCQCHH NIDTTDPEAC DKETGRCLKC 1000
    LYHTEGDHCQ LCQYGYYGDA LRQDCRKCVC NYLGTVKEHC NGSDCHCDKA 1050
    TGQCSCLPNV IGQNCDRCAP NTWQLASGTG CGPCNCNAAH SFGPSCNEFT 1100
    GQCQCMPGFG GRTCSECQEL FWGDPDVECR ACDCDPRGIE TPQCDQSTGQ 1150
    CVCVEGVEGP RCDKCTRGYS GVFPDCTPCH QCFALWDAII GELTNRTHKF 1200
    LEKAKALKIS GVIGPYRETV DSVEKKVNEI KDILAQSPAA EPLKNIGILF 1250
    EEAEKLTKDV TEKMAQVEVK LTDTASQSNS TAGELGALQA EAESLDKTVK 1300
    ELAEQLEFIK NSDIQGALDS ITKYFQMSLE AEKRVNASTT DPNSTVEQSA 1350
    LTRDRVEDLM LERESPFKEQ QEEQARLLDE LAGKLQSLDL SAVAQMTCGT 1400
    PPGADCSESE CGGPNCRTDE GEKKCGGPGC GGLVTVAHSA WQKAMDFDRD 1450
    VLSALAEVEQ LSKMVSEAKV RADEAKQNAQ DVLLKTNATK EKVDKSNEDL 1500
    RNLIKQIRNF LTEDSADLDS IEAVANEVLK MEMPSTPQQL QNLTEDIRER 1550
    VETLSQVEVI LQQSAADIAR AELLLEEAKR ASKSATDVKV TADMVKEALE 1600
    EAEKAQVAAE KAIKQADEDI QGTQNLLTSI ESETAASEET LTNASQRISK 1650
    LERNVEELKR KAAQNSGEAE YIEKVVYSVK QNADDVKKTL DGELDEKYKK 1700
    VESLIAQKTE ESADARRKAE LLQNEAKTLL AQANSKLQLL EDLERKYEDN 1750
    QKYLEDKAQE LVRLEGEVRS LLKDISEKVA VYSTCL 1786
    Length:1,786
    Mass (Da):197,090
    Last modified:July 27, 2011 - v3
    Checksum:iE7F258170C3626DD
    GO

    Sequence cautioni

    The sequence AAA39407.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti159 – 1591A → T in AAA39407. (PubMed:3493487)Curated
    Sequence conflicti569 – 5691I → V in AAA39407. (PubMed:3493487)Curated
    Sequence conflicti993 – 9931E → D in AAA39407. (PubMed:3493487)Curated
    Sequence conflicti1393 – 13931V → A in AAA39407. (PubMed:3493487)Curated
    Sequence conflicti1393 – 13931V → A in CAA28839. (PubMed:6209134)Curated
    Sequence conflicti1531 – 15344MEMP → SGNA in AAA39407. (PubMed:3493487)Curated
    Sequence conflicti1692 – 16921G → C in CAA28839. (PubMed:6209134)Curated
    Sequence conflicti1749 – 17491D → N in CAA28839. (PubMed:6209134)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M15525 mRNA. Translation: AAA39407.1. Different initiation.
    CR974423 Genomic DNA. No translation available.
    CT571245 Genomic DNA. No translation available.
    X05212 mRNA. Translation: CAA28839.1.
    PIRiA26413. MMMSB1.
    RefSeqiXP_006515056.1. XM_006514993.1.
    UniGeneiMm.172674.

    Genome annotation databases

    EnsembliENSMUST00000169088; ENSMUSP00000132778; ENSMUSG00000002900.
    GeneIDi16777.
    KEGGimmu:16777.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M15525 mRNA. Translation: AAA39407.1 . Different initiation.
    CR974423 Genomic DNA. No translation available.
    CT571245 Genomic DNA. No translation available.
    X05212 mRNA. Translation: CAA28839.1 .
    PIRi A26413. MMMSB1.
    RefSeqi XP_006515056.1. XM_006514993.1.
    UniGenei Mm.172674.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    4AQS X-ray 3.11 A 22-542 [» ]
    ProteinModelPortali P02469.
    SMRi P02469. Positions 29-492.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi P02469. 6 interactions.
    MINTi MINT-1206337.

    PTM databases

    PhosphoSitei P02469.

    Proteomic databases

    MaxQBi P02469.
    PaxDbi P02469.
    PRIDEi P02469.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000169088 ; ENSMUSP00000132778 ; ENSMUSG00000002900 .
    GeneIDi 16777.
    KEGGi mmu:16777.

    Organism-specific databases

    CTDi 3912.
    MGIi MGI:96743. Lamb1.

    Phylogenomic databases

    eggNOGi NOG241384.
    GeneTreei ENSGT00720000108616.
    HOVERGENi HBG052301.
    InParanoidi P02469.
    KOi K05636.
    OrthoDBi EOG75XGK0.

    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

    ChiTaRSi LAMB1. mouse.
    PROi P02469.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P02469.
    Bgeei P02469.
    CleanExi MM_LAMB1-1.
    Genevestigatori P02469.

    Family and domain databases

    InterProi IPR002049. EGF_laminin.
    IPR013015. Laminin_IV.
    IPR008211. Laminin_N.
    [Graphical view ]
    Pfami PF00053. Laminin_EGF. 13 hits.
    PF00055. Laminin_N. 1 hit.
    [Graphical view ]
    SMARTi SM00180. EGF_Lam. 13 hits.
    SM00136. LamNT. 1 hit.
    [Graphical view ]
    PROSITEi PS00022. EGF_1. 9 hits.
    PS01186. EGF_2. 2 hits.
    PS01248. EGF_LAM_1. 11 hits.
    PS50027. EGF_LAM_2. 13 hits.
    PS51116. LAMININ_IVB. 1 hit.
    PS51117. LAMININ_NTER. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Sequence of the cDNA encoding the laminin B1 chain reveals a multidomain protein containing cysteine-rich repeats."
      Sasaki M., Kato S., Kohno K., Martin G.R., Yamada Y.
      Proc. Natl. Acad. Sci. U.S.A. 84:935-939(1987) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: C57BL/6J.
    3. "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 1292-1786.
    4. "Cloning of the mouse laminin alpha 4 cDNA. Expression in a subset of endothelium."
      Frieser M., Noeckel H., Pausch F., Roeder C., Hahn A., Deutzmann R., Sorokin L.M.
      Eur. J. Biochem. 246:727-735(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 165-172; 539-547 AND 712-719.
      Strain: BALB/c.
      Tissue: Endothelial cell.
    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-1279; ASN-1336 AND ASN-1343.
    6. Cited for: TISSUE SPECIFICITY.

    Entry informationi

    Entry nameiLAMB1_MOUSE
    AccessioniPrimary (citable) accession number: P02469
    Secondary accession number(s): E9PXZ9
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 21, 1986
    Last sequence update: July 27, 2011
    Last modified: October 1, 2014
    This is version 140 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, 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