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Q61292

- LAMB2_MOUSE

UniProt

Q61292 - LAMB2_MOUSE

Protein

Laminin subunit beta-2

Gene

Lamb2

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 119 (01 Oct 2014)
      Sequence version 2 (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.1 Publication
    Laminin-3 (S-laminin) regulates the formation of motor nerve terminals.1 Publication

    GO - Molecular functioni

    1. integrin binding Source: MGI

    GO - Biological processi

    1. astrocyte development Source: MGI
    2. axon extension involved in regeneration Source: MGI
    3. axon guidance Source: MGI
    4. cell adhesion Source: UniProtKB-KW
    5. cell morphogenesis involved in differentiation Source: MGI
    6. metanephric glomerular basement membrane development Source: MGI
    7. metanephric glomerular visceral epithelial cell development Source: MGI
    8. neuromuscular junction development Source: MGI
    9. neuron projection development Source: MGI
    10. retina development in camera-type eye Source: MGI
    11. Schwann cell development Source: MGI
    12. synapse organization Source: MGI
    13. visual perception Source: MGI

    Keywords - Biological processi

    Cell adhesion

    Enzyme and pathway databases

    ReactomeiREACT_196606. ECM proteoglycans.
    REACT_196607. Non-integrin membrane-ECM interactions.
    REACT_202342. Laminin interactions.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Laminin subunit beta-2
    Alternative name(s):
    Laminin-11 subunit beta
    Laminin-14 subunit beta
    Laminin-15 subunit beta
    Laminin-3 subunit beta
    Laminin-4 subunit beta
    Laminin-7 subunit beta
    Laminin-9 subunit beta
    S-laminin subunit beta
    Short name:
    S-LAM beta
    Gene namesi
    Name:Lamb2
    Synonyms:Lams
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 9

    Organism-specific databases

    MGIiMGI:99916. Lamb2.

    Subcellular locationi

    GO - Cellular componenti

    1. basal lamina Source: MGI
    2. basement membrane Source: UniProtKB
    3. extracellular region Source: Reactome
    4. laminin-3 complex Source: MGI
    5. laminin complex Source: MGI
    6. synapse Source: MGI

    Keywords - Cellular componenti

    Basement membrane, Extracellular matrix, Secreted

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 3535Sequence AnalysisAdd
    BLAST
    Chaini36 – 17991764Laminin subunit beta-2PRO_0000017069Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi251 – 2511N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi286 ↔ 295PROSITE-ProRule annotation
    Disulfide bondi288 ↔ 313PROSITE-ProRule annotation
    Disulfide bondi315 ↔ 324PROSITE-ProRule annotation
    Disulfide bondi327 ↔ 347PROSITE-ProRule annotation
    Disulfide bondi350 ↔ 359PROSITE-ProRule annotation
    Disulfide bondi352 ↔ 377PROSITE-ProRule annotation
    Glycosylationi371 – 3711N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi380 ↔ 389PROSITE-ProRule annotation
    Disulfide bondi392 ↔ 410PROSITE-ProRule annotation
    Disulfide bondi413 ↔ 426PROSITE-ProRule annotation
    Disulfide bondi415 ↔ 441PROSITE-ProRule annotation
    Disulfide bondi443 ↔ 452PROSITE-ProRule annotation
    Disulfide bondi455 ↔ 470PROSITE-ProRule annotation
    Disulfide bondi473 ↔ 487PROSITE-ProRule annotation
    Disulfide bondi475 ↔ 494PROSITE-ProRule annotation
    Disulfide bondi496 ↔ 505PROSITE-ProRule annotation
    Disulfide bondi508 ↔ 522PROSITE-ProRule annotation
    Disulfide bondi525 ↔ 537PROSITE-ProRule annotation
    Disulfide bondi527 ↔ 544PROSITE-ProRule annotation
    Disulfide bondi546 ↔ 555PROSITE-ProRule annotation
    Disulfide bondi784 ↔ 796PROSITE-ProRule annotation
    Disulfide bondi786 ↔ 803PROSITE-ProRule annotation
    Disulfide bondi805 ↔ 814PROSITE-ProRule annotation
    Disulfide bondi817 ↔ 829PROSITE-ProRule annotation
    Disulfide bondi832 ↔ 844PROSITE-ProRule annotation
    Disulfide bondi834 ↔ 851PROSITE-ProRule annotation
    Disulfide bondi853 ↔ 862PROSITE-ProRule annotation
    Disulfide bondi865 ↔ 875PROSITE-ProRule annotation
    Disulfide bondi878 ↔ 887PROSITE-ProRule annotation
    Disulfide bondi880 ↔ 894PROSITE-ProRule annotation
    Disulfide bondi897 ↔ 906PROSITE-ProRule annotation
    Disulfide bondi909 ↔ 925PROSITE-ProRule annotation
    Disulfide bondi928 ↔ 944PROSITE-ProRule annotation
    Disulfide bondi930 ↔ 955PROSITE-ProRule annotation
    Disulfide bondi957 ↔ 966PROSITE-ProRule annotation
    Disulfide bondi969 ↔ 984PROSITE-ProRule annotation
    Disulfide bondi987 ↔ 1001PROSITE-ProRule annotation
    Disulfide bondi989 ↔ 1008PROSITE-ProRule annotation
    Disulfide bondi1011 ↔ 1020PROSITE-ProRule annotation
    Disulfide bondi1023 ↔ 1036PROSITE-ProRule annotation
    Disulfide bondi1039 ↔ 1059PROSITE-ProRule annotation
    Disulfide bondi1041 ↔ 1066PROSITE-ProRule annotation
    Disulfide bondi1068 ↔ 1077PROSITE-ProRule annotation
    Disulfide bondi1080 ↔ 1093PROSITE-ProRule annotation
    Glycosylationi1086 – 10861N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi1096 ↔ 1108PROSITE-ProRule annotation
    Disulfide bondi1098 ↔ 1115PROSITE-ProRule annotation
    Disulfide bondi1117 ↔ 1126PROSITE-ProRule annotation
    Disulfide bondi1129 ↔ 1141PROSITE-ProRule annotation
    Disulfide bondi1144 ↔ 1156PROSITE-ProRule annotation
    Disulfide bondi1146 ↔ 1163PROSITE-ProRule annotation
    Disulfide bondi1165 ↔ 1174PROSITE-ProRule annotation
    Disulfide bondi1177 ↔ 1188PROSITE-ProRule annotation
    Disulfide bondi1191 – 1191InterchainCurated
    Disulfide bondi1194 – 1194InterchainCurated
    Glycosylationi1250 – 12501N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi1309 – 13091N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi1349 – 13491N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi1500 – 15001N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi1798 – 1798InterchainCurated

    Keywords - PTMi

    Disulfide bond, Glycoprotein

    Proteomic databases

    MaxQBiQ61292.
    PaxDbiQ61292.
    PRIDEiQ61292.

    PTM databases

    PhosphoSiteiQ61292.

    Expressioni

    Tissue specificityi

    Neuromuscular synapse and kidney glomerulus.

    Gene expression databases

    ArrayExpressiQ61292.
    BgeeiQ61292.
    CleanExiMM_LAMB2.
    GenevestigatoriQ61292.

    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-2 is a subunit of laminin-3 (laminin-121 or S-laminin), laminin-4 (laminin-221 or S-merosin), laminin-7 (laminin-321 or KS-laminin), laminin-9 (laminin-421), laminin-11 (laminin-521), laminin-14 (laminin-423) and laminin-15 (laminin-523).

    Protein-protein interaction databases

    IntActiQ61292. 2 interactions.
    MINTiMINT-4100139.
    STRINGi10090.ENSMUSP00000069087.

    Structurei

    3D structure databases

    ProteinModelPortaliQ61292.
    SMRiQ61292. Positions 44-507.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini46 – 285240Laminin N-terminalPROSITE-ProRule annotationAdd
    BLAST
    Domaini286 – 34964Laminin EGF-like 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini350 – 41263Laminin EGF-like 2PROSITE-ProRule annotationAdd
    BLAST
    Domaini413 – 47260Laminin EGF-like 3PROSITE-ProRule annotationAdd
    BLAST
    Domaini473 – 52452Laminin EGF-like 4PROSITE-ProRule annotationAdd
    BLAST
    Domaini525 – 55531Laminin EGF-like 5; truncatedPROSITE-ProRule annotationAdd
    BLAST
    Domaini564 – 778215Laminin IV type BPROSITE-ProRule annotationAdd
    BLAST
    Domaini784 – 83148Laminin EGF-like 6PROSITE-ProRule annotationAdd
    BLAST
    Domaini832 – 87746Laminin EGF-like 7PROSITE-ProRule annotationAdd
    BLAST
    Domaini878 – 92750Laminin EGF-like 8PROSITE-ProRule annotationAdd
    BLAST
    Domaini928 – 98659Laminin EGF-like 9PROSITE-ProRule annotationAdd
    BLAST
    Domaini987 – 103852Laminin EGF-like 10PROSITE-ProRule annotationAdd
    BLAST
    Domaini1039 – 109557Laminin EGF-like 11PROSITE-ProRule annotationAdd
    BLAST
    Domaini1096 – 114348Laminin EGF-like 12PROSITE-ProRule annotationAdd
    BLAST
    Domaini1144 – 119047Laminin EGF-like 13PROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni1191 – 1410220Domain IIAdd
    BLAST
    Regioni1411 – 144333Domain alphaAdd
    BLAST
    Regioni1444 – 1799356Domain IAdd
    BLAST

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili1257 – 130448Sequence AnalysisAdd
    BLAST
    Coiled coili1473 – 152755Sequence AnalysisAdd
    BLAST
    Coiled coili1577 – 1791215Sequence 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 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.
    HOGENOMiHOG000007552.
    HOVERGENiHBG052301.
    InParanoidiQ8R0Y0.
    KOiK06243.
    OMAiQPYCIVS.
    OrthoDBiEOG75XGK0.
    TreeFamiTF312903.

    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. 10 hits.
    PS01186. EGF_2. 2 hits.
    PS01248. EGF_LAM_1. 12 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.

    Q61292-1 [UniParc]FASTAAdd to Basket

    « Hide

    MEWASGEPGR GRQGQPLPWE LRLGLLLSVL AATLAQAPSL DVPGCSRGSC     50
    YPATGDLLVG RADRLTASST CGLHSPQPYC IVSHLQDEKK CFLCDSRRPF 100
    SARDNPNSHR IQNVVTSFAP QRRTAWWQSE NGVPMVTIQL DLEAEFHFTH 150
    LIMTFKTFRP AAMLVERSAD FGRTWHVYRY FSYDCGADFP GIPLAPPRRW 200
    DDVVCESRYS EIEPSTEGEV IYRVLDPAIP IPDPYSSRIQ NLLKITNLRV 250
    NLTRLHTLGD NLLDPRREIR EKYYYALYEL VIRGNCFCYG HASQCAPAPG 300
    APAHAEGMVH GACICKHNTR GLNCEQCQDF YQDLPWHPAE DGHTHACRKC 350
    ECNGHTHSCH FDMAVYLASG NVSGGVCDGC QHNTAGRHCE FCRPFFYRDP 400
    TKDMRDPAVC RPCDCDPMGS QDGGRCDSHD DPVLGLVSGQ CRCKEHVVGT 450
    RCQQCRDGFF GLSASDPRGC QRCQCNSRGT VPGSSPCDSS SGTCFCKRLV 500
    TGHGCDRCLP GHWGLSHDLL GCRPCDCDVG GALDPQCDEA TGQCRCRQHM 550
    IGRRCEQVQP GYFRPFLDHL TWEAEAAQGQ GLEVVERLVT NRETPSWTGP 600
    GFVRLREGQE VEFLVTSLPR AMDYDLLLRW EPQVPEQWAE LELMVQRPGP 650
    VSAHSPCGHV LPKDDRIQGM LHPNTRFLVF PRPVCLEPGI SYKLKLKLIG 700
    TGGRAQPETS YSGLLIDSLV LQPHVLVLEM FSGGDAAALE RRTTFERYRC 750
    HEEGLMPSKA PLSETCAPLL ISVSALIYNG ALPCQCDPQG SLSSECSPHG 800
    GQCRCKPGVV GRRCDVCATG YYGFGPAGCQ ACQCSPDGAL SALCEGTSGQ 850
    CPCRPGAFGL RCDHCQRGQW GFPNCRPCVC NGRADECDTH TGACLGCRDY 900
    TGGEHCERCI AGFHGDPRLP YGGQCRPCPC PEGPGSQRHF ATSCHRDGYS 950
    QQIVCQCREG YTGLRCEACA PGHFGDPSKP GGRCQLCECS GNIDPMDPDA 1000
    CDPHTGQCLR CLHNTEGPHC GYCKPGFHGQ AARQSCHRCT CNLLGTDPRR 1050
    CPSTDLCHCD PSTGQCPCLP HVQGLNCDHC APNFWNFTSG RGCQPCACHP 1100
    SRARGPTCNE FTGQCHCHAG FGGRTCSECQ ELYWGDPGLQ CRACDCDPRG 1150
    IDKPQCHRST GHCSCRPGVS GVRCDQCARG FSGVFPACHP CHACFGDWDR 1200
    VVQDLAARTR RLEQWAQELQ QTGVLGAFES SFLNMQGKLG MVQAIMSARN 1250
    ASAASTAKLV EATEGLRHEI GKTTERLTQL EAELTAVQDE NFNANHALSG 1300
    LERDGLALNL TLRQLDQHLE ILKHSNFLGA YDSIRHAHSQ STEAERRANA 1350
    STFAVPSPVS NSADTRRRTE VLMGAQKENF NRQHLANQQA LGRLSAHAHT 1400
    LSLTGINELV CGAPGDAPCA TSPCGGAGCR DEDGQPRCGG LGCSGAAATA 1450
    DLALGRARHT QAELQRALVE GGGILSRVSE TRRQAEEAQQ RAQAALDKAN 1500
    ASRGQVEQAN QELRELIQNV KDFLSQEGAD PDSIEMVATR VLDISIPASP 1550
    EQIQRLASEI AERVRSLADV DTILAHTMGD VRRAEQLLQD AHRARSRAEG 1600
    ERQKAETVQA ALEEAQRAQG AAQGAIWGAV VDTQNTEQTL QRVQERMAGA 1650
    EKSLNSAGER ARQLDALLEA LKLKRAGNSL AASTAEETAG SAQSRAREAE 1700
    KQLREQVGDQ YQTVRALAER KAEGVLAAQA RAEQLRDEAR DLLQAAQDKL 1750
    QRLQELEGTY EENERALEGK AAQLDGLEAR MRSVLQAINL QVQIYNTCQ 1799
    Length:1,799
    Mass (Da):196,579
    Last modified:July 27, 2011 - v2
    Checksum:i37CA24B9CDA0791F
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti545 – 5451R → P in AAC53535. (PubMed:8662701)Curated
    Sequence conflicti581 – 5811G → V in AAC53535. (PubMed:8662701)Curated
    Sequence conflicti677 – 6771F → V in AAC53535. (PubMed:8662701)Curated
    Sequence conflicti956 – 9561Q → H in AAC53535. (PubMed:8662701)Curated
    Sequence conflicti959 – 9591E → A in AAC53535. (PubMed:8662701)Curated
    Sequence conflicti973 – 9731H → P in AAC53535. (PubMed:8662701)Curated
    Sequence conflicti1306 – 13061L → F in AAC53535. (PubMed:8662701)Curated
    Sequence conflicti1449 – 14491T → P in AAC53535. (PubMed:8662701)Curated
    Sequence conflicti1460 – 14601T → S in AAC53535. (PubMed:8662701)Curated
    Sequence conflicti1487 – 14871E → A in AAC53535. (PubMed:8662701)Curated
    Sequence conflicti1627 – 16271W → R in AAC53535. (PubMed:8662701)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U43541, U42624 Genomic DNA. Translation: AAC53535.1.
    CH466560 Genomic DNA. Translation: EDL21291.1.
    CH466560 Genomic DNA. Translation: EDL21292.1.
    BC026051 mRNA. Translation: AAH26051.1.
    X75928 mRNA. Translation: CAA53532.1.
    CCDSiCCDS23528.1.
    PIRiI48749.
    RefSeqiNP_032509.2. NM_008483.3.
    XP_006511711.1. XM_006511648.1.
    UniGeneiMm.425599.

    Genome annotation databases

    EnsembliENSMUST00000065014; ENSMUSP00000069087; ENSMUSG00000052911.
    GeneIDi16779.
    KEGGimmu:16779.
    UCSCiuc009rpr.2. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U43541 , U42624 Genomic DNA. Translation: AAC53535.1 .
    CH466560 Genomic DNA. Translation: EDL21291.1 .
    CH466560 Genomic DNA. Translation: EDL21292.1 .
    BC026051 mRNA. Translation: AAH26051.1 .
    X75928 mRNA. Translation: CAA53532.1 .
    CCDSi CCDS23528.1.
    PIRi I48749.
    RefSeqi NP_032509.2. NM_008483.3.
    XP_006511711.1. XM_006511648.1.
    UniGenei Mm.425599.

    3D structure databases

    ProteinModelPortali Q61292.
    SMRi Q61292. Positions 44-507.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi Q61292. 2 interactions.
    MINTi MINT-4100139.
    STRINGi 10090.ENSMUSP00000069087.

    PTM databases

    PhosphoSitei Q61292.

    Proteomic databases

    MaxQBi Q61292.
    PaxDbi Q61292.
    PRIDEi Q61292.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000065014 ; ENSMUSP00000069087 ; ENSMUSG00000052911 .
    GeneIDi 16779.
    KEGGi mmu:16779.
    UCSCi uc009rpr.2. mouse.

    Organism-specific databases

    CTDi 3913.
    MGIi MGI:99916. Lamb2.

    Phylogenomic databases

    eggNOGi NOG241384.
    GeneTreei ENSGT00720000108616.
    HOGENOMi HOG000007552.
    HOVERGENi HBG052301.
    InParanoidi Q8R0Y0.
    KOi K06243.
    OMAi QPYCIVS.
    OrthoDBi EOG75XGK0.
    TreeFami TF312903.

    Enzyme and pathway databases

    Reactomei REACT_196606. ECM proteoglycans.
    REACT_196607. Non-integrin membrane-ECM interactions.
    REACT_202342. Laminin interactions.

    Miscellaneous databases

    ChiTaRSi LAMB2. mouse.
    NextBioi 290628.
    PROi Q61292.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q61292.
    Bgeei Q61292.
    CleanExi MM_LAMB2.
    Genevestigatori Q61292.

    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. 10 hits.
    PS01186. EGF_2. 2 hits.
    PS01248. EGF_LAM_1. 12 hits.
    PS50027. EGF_LAM_2. 13 hits.
    PS51116. LAMININ_IVB. 1 hit.
    PS51117. LAMININ_NTER. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Structural organization of the human and mouse laminin beta2 chain genes, and alternative splicing at the 5' end of the human transcript."
      Durkin M.E., Gautam M., Loechel S., Sanes J.R., Merlie J.P., Albrechtsen R., Wewer U.M.
      J. Biol. Chem. 271:13407-13416(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: 129/J.
    2. Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
      Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    3. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: FVB/N.
      Tissue: Mammary tumor.
    4. "S-laminin gene (Lams) maps to F1 band of mouse chromosome 9."
      Aberdam D., Galliano M.-F., Mattei M.-G., Ortonne J.-P., Meneguzzi G.
      Mamm. Genome 5:393-394(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 348-428.
      Tissue: Lung.
    5. "Aberrant differentiation of neuromuscular junctions in mice lacking s-laminin/laminin beta 2."
      Noakes P.G., Gautam M., Mudd J., Sanes J.R., Merlie J.P.
      Nature 374:258-262(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
      Strain: 129/J.

    Entry informationi

    Entry nameiLAMB2_MOUSE
    AccessioniPrimary (citable) accession number: Q61292
    Secondary accession number(s): Q62182, Q8R0Y0
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1997
    Last sequence update: July 27, 2011
    Last modified: October 1, 2014
    This is version 119 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

    Complete proteome, Reference proteome

    Documents

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

    External Data

    Dasty 3