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Q13751

- LAMB3_HUMAN

UniProt

Q13751 - LAMB3_HUMAN

Protein

Laminin subunit beta-3

Gene

LAMB3

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 150 (01 Oct 2014)
      Sequence version 1 (01 Nov 1996)
      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. protein binding Source: UniProtKB
    2. structural molecule activity Source: ProtInc

    GO - Biological processi

    1. brown fat cell differentiation Source: Ensembl
    2. cell adhesion Source: UniProtKB-KW
    3. cell junction assembly Source: Reactome
    4. epidermis development Source: ProtInc
    5. extracellular matrix disassembly Source: Reactome
    6. extracellular matrix organization Source: Reactome
    7. hemidesmosome assembly Source: Reactome

    Keywords - Biological processi

    Cell adhesion

    Enzyme and pathway databases

    ReactomeiREACT_118572. Degradation of the extracellular matrix.
    REACT_150180. Assembly of collagen fibrils and other multimeric structures.
    REACT_150268. Anchoring fibril formation.
    REACT_163874. Non-integrin membrane-ECM interactions.
    REACT_169262. Laminin interactions.
    REACT_20537. Type I hemidesmosome assembly.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Laminin subunit beta-3
    Alternative name(s):
    Epiligrin subunit bata
    Kalinin B1 chain
    Kalinin subunit beta
    Laminin B1k chain
    Laminin-5 subunit beta
    Nicein subunit beta
    Gene namesi
    Name:LAMB3
    Synonyms:LAMNB1
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 1

    Organism-specific databases

    HGNCiHGNC:6490. LAMB3.

    Subcellular locationi

    GO - Cellular componenti

    1. extracellular region Source: Reactome
    2. laminin-5 complex Source: Ensembl

    Keywords - Cellular componenti

    Basement membrane, Extracellular matrix, Secreted

    Pathology & Biotechi

    Involvement in diseasei

    Epidermolysis bullosa, junctional, Herlitz type (H-JEB) [MIM:226700]: An infantile and lethal form of junctional epidermolysis bullosa, a group of blistering skin diseases characterized by tissue separation which occurs within the dermo-epidermal basement In the Herlitz type, death occurs usually within the first six months of life. Occasionally, children survive to teens. It is marked by bullous lesions at birth and extensive denudation of skin and mucous membranes that may be hemorrhagic.1 Publication
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti679 – 6791P → L in H-JEB. 1 Publication
    VAR_004171
    Generalized atrophic benign epidermolysis bullosa (GABEB) [MIM:226650]: A non-lethal, adult form of junctional epidermolysis bullosa characterized by life-long blistering of the skin, associated with hair and tooth abnormalities.2 Publications
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti199 – 1991G → A in GABEB; somatic second-site mutation. 1 Publication
    VAR_037310
    Natural varianti207 – 2071K → Q in GABEB; somatic second-site mutation. 1 Publication
    VAR_037311
    Natural varianti210 – 2101E → K in GABEB. 2 Publications
    VAR_004170

    Keywords - Diseasei

    Disease mutation, Epidermolysis bullosa

    Organism-specific databases

    MIMi226650. phenotype.
    226700. phenotype.
    Orphaneti79402. Generalized junctional epidermolysis bullosa, non-Herlitz type.
    100031. Hypoplastic amelogenesis imperfecta.
    79404. Junctional epidermolysis bullosa, Herlitz type.
    PharmGKBiPA30278.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 1717Sequence AnalysisAdd
    BLAST
    Chaini18 – 11721155Laminin subunit beta-3PRO_0000017071Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi220 – 2201N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi250 ↔ 259PROSITE-ProRule annotation
    Disulfide bondi252 ↔ 279PROSITE-ProRule annotation
    Disulfide bondi281 ↔ 290PROSITE-ProRule annotation
    Disulfide bondi293 ↔ 313PROSITE-ProRule annotation
    Disulfide bondi316 ↔ 325PROSITE-ProRule annotation
    Disulfide bondi318 ↔ 343PROSITE-ProRule annotation
    Disulfide bondi346 ↔ 355PROSITE-ProRule annotation
    Disulfide bondi358 ↔ 376PROSITE-ProRule annotation
    Disulfide bondi379 ↔ 392PROSITE-ProRule annotation
    Disulfide bondi381 ↔ 399PROSITE-ProRule annotation
    Disulfide bondi401 ↔ 410PROSITE-ProRule annotation
    Disulfide bondi413 ↔ 428PROSITE-ProRule annotation
    Disulfide bondi431 ↔ 444PROSITE-ProRule annotation
    Disulfide bondi433 ↔ 451PROSITE-ProRule annotation
    Disulfide bondi453 ↔ 462PROSITE-ProRule annotation
    Disulfide bondi465 ↔ 478PROSITE-ProRule annotation
    Disulfide bondi481 ↔ 493PROSITE-ProRule annotation
    Disulfide bondi483 ↔ 500PROSITE-ProRule annotation
    Disulfide bondi502 ↔ 511PROSITE-ProRule annotation
    Disulfide bondi519 ↔ 531PROSITE-ProRule annotation
    Disulfide bondi534 ↔ 546PROSITE-ProRule annotation
    Disulfide bondi536 ↔ 553PROSITE-ProRule annotation
    Disulfide bondi555 ↔ 564PROSITE-ProRule annotation
    Disulfide bondi567 ↔ 578PROSITE-ProRule annotation
    Disulfide bondi581 – 581InterchainCurated
    Disulfide bondi584 – 584InterchainCurated
    Glycosylationi604 – 6041N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi810 – 8101N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi1171 – 1171InterchainCurated

    Keywords - PTMi

    Disulfide bond, Glycoprotein

    Proteomic databases

    MaxQBiQ13751.
    PaxDbiQ13751.
    PRIDEiQ13751.

    PTM databases

    PhosphoSiteiQ13751.

    Miscellaneous databases

    PMAP-CutDBQ13751.

    Expressioni

    Tissue specificityi

    Found in the basement membranes (major component).

    Gene expression databases

    ArrayExpressiQ13751.
    BgeeiQ13751.
    CleanExiHS_LAMB3.
    GenevestigatoriQ13751.

    Organism-specific databases

    HPAiHPA008069.

    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-3 is a subunit of laminin-5 (laminin-332 or epiligrin/kalinin/nicein). Interacts with ECM1.1 Publication

    Protein-protein interaction databases

    BioGridi110108. 3 interactions.
    IntActiQ13751. 1 interaction.
    MINTiMINT-4053402.
    STRINGi9606.ENSP00000348384.

    Structurei

    3D structure databases

    ProteinModelPortaliQ13751.
    SMRiQ13751. Positions 20-566.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini22 – 249228Laminin N-terminalPROSITE-ProRule annotationAdd
    BLAST
    Domaini250 – 31566Laminin EGF-like 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini316 – 37863Laminin EGF-like 2PROSITE-ProRule annotationAdd
    BLAST
    Domaini379 – 43052Laminin EGF-like 3PROSITE-ProRule annotationAdd
    BLAST
    Domaini431 – 48050Laminin EGF-like 4PROSITE-ProRule annotationAdd
    BLAST
    Domaini481 – 53353Laminin EGF-like 5PROSITE-ProRule annotationAdd
    BLAST
    Domaini534 – 58047Laminin EGF-like 6PROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni579 – 785207Domain IIAdd
    BLAST
    Regioni786 – 81631Domain alphaAdd
    BLAST
    Regioni817 – 1170354Domain IAdd
    BLAST

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili723 – 75735Sequence AnalysisAdd
    BLAST
    Coiled coili831 – 88454Sequence AnalysisAdd
    BLAST
    Coiled coili948 – 1133186Sequence AnalysisAdd
    BLAST

    Domaini

    The alpha-helical domains I and II are thought to interact with other laminin chains to form a coiled coil structure.
    Domain VI is globular.

    Sequence similaritiesi

    Contains 6 laminin EGF-like domains.PROSITE-ProRule annotation
    Contains 1 laminin N-terminal domain.PROSITE-ProRule annotation

    Keywords - Domaini

    Coiled coil, Laminin EGF-like domain, Repeat, Signal

    Phylogenomic databases

    eggNOGiNOG289025.
    HOGENOMiHOG000113279.
    HOVERGENiHBG052302.
    InParanoidiQ13751.
    KOiK06244.
    OMAiRSQMEED.
    OrthoDBiEOG77WWBQ.
    PhylomeDBiQ13751.
    TreeFamiTF352481.

    Family and domain databases

    InterProiIPR013032. EGF-like_CS.
    IPR002049. EGF_laminin.
    IPR008211. Laminin_N.
    [Graphical view]
    PfamiPF00053. Laminin_EGF. 6 hits.
    PF00055. Laminin_N. 1 hit.
    [Graphical view]
    SMARTiSM00180. EGF_Lam. 6 hits.
    SM00136. LamNT. 1 hit.
    [Graphical view]
    PROSITEiPS00022. EGF_1. 5 hits.
    PS01186. EGF_2. 1 hit.
    PS01248. EGF_LAM_1. 5 hits.
    PS50027. EGF_LAM_2. 6 hits.
    PS51117. LAMININ_NTER. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    Q13751-1 [UniParc]FASTAAdd to Basket

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    MRPFFLLCFA LPGLLHAQQA CSRGACYPPV GDLLVGRTRF LRASSTCGLT     50
    KPETYCTQYG EWQMKCCKCD SRQPHNYYSH RVENVASSSG PMRWWQSQND 100
    VNPVSLQLDL DRRFQLQEVM MEFQGPMPAG MLIERSSDFG KTWRVYQYLA 150
    ADCTSTFPRV RQGRPQSWQD VRCQSLPQRP NARLNGGKVQ LNLMDLVSGI 200
    PATQSQKIQE VGEITNLRVN FTRLAPVPQR GYHPPSAYYA VSQLRLQGSC 250
    FCHGHADRCA PKPGASAGPS TAVQVHDVCV CQHNTAGPNC ERCAPFYNNR 300
    PWRPAEGQDA HECQRCDCNG HSETCHFDPA VFAASQGAYG GVCDNCRDHT 350
    EGKNCERCQL HYFRNRRPGA SIQETCISCE CDPDGAVPGA PCDPVTGQCV 400
    CKEHVQGERC DLCKPGFTGL TYANPQGCHR CDCNILGSRR DMPCDEESGR 450
    CLCLPNVVGP KCDQCAPYHW KLASGQGCEP CACDPHNSLS PQCNQFTGQC 500
    PCREGFGGLM CSAAAIRQCP DRTYGDVATG CRACDCDFRG TEGPGCDKAS 550
    GRCLCRPGLT GPRCDQCQRG YCNRYPVCVA CHPCFQTYDA DLREQALRFG 600
    RLRNATASLW SGPGLEDRGL ASRILDAKSK IEQIRAVLSS PAVTEQEVAQ 650
    VASAILSLRR TLQGLQLDLP LEEETLSLPR DLESLDRSFN GLLTMYQRKR 700
    EQFEKISSAD PSGAFRMLST AYEQSAQAAQ QVSDSSRLLD QLRDSRREAE 750
    RLVRQAGGGG GTGSPKLVAL RLEMSSLPDL TPTFNKLCGN SRQMACTPIS 800
    CPGELCPQDN GTACGSRCRG VLPRAGGAFL MAGQVAEQLR GFNAQLQRTR 850
    QMIRAAEESA SQIQSSAQRL ETQVSASRSQ MEEDVRRTRL LIQQVRDFLT 900
    DPDTDAATIQ EVSEAVLALW LPTDSATVLQ KMNEIQAIAA RLPNVDLVLS 950
    QTKQDIARAR RLQAEAEEAR SRAHAVEGQV EDVVGNLRQG TVALQEAQDT 1000
    MQGTSRSLRL IQDRVAEVQQ VLRPAEKLVT SMTKQLGDFW TRMEELRHQA 1050
    RQQGAEAVQA QQLAEGASEQ ALSAQEGFER IKQKYAELKD RLGQSSMLGE 1100
    QGARIQSVKT EAEELFGETM EMMDRMKDME LELLRGSQAI MLRSADLTGL 1150
    EKRVEQIRDH INGRVLYYAT CK 1172
    Length:1,172
    Mass (Da):129,572
    Last modified:November 1, 1996 - v1
    Checksum:i61BC1A60BBD4FA05
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti124 – 1241Q → R in AAA61834. (PubMed:7512558)Curated
    Sequence conflicti269 – 2691Missing in AAA61834. (PubMed:7512558)Curated
    Sequence conflicti388 – 3881P → A in AAA61834. (PubMed:7512558)Curated
    Sequence conflicti426 – 4272QG → RR in AAA61834. (PubMed:7512558)Curated
    Sequence conflicti440 – 4412RD → E in AAA61834. (PubMed:7512558)Curated
    Sequence conflicti489 – 50012LSPQC…FTGQC → PQPTVQPVHRAV in BAA22263. (PubMed:8530036)CuratedAdd
    BLAST
    Sequence conflicti603 – 6031R → P in AAA61834. (PubMed:7512558)Curated
    Sequence conflicti815 – 8151G → A in AAA61834. (PubMed:7512558)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti181 – 1811N → D.
    Corresponds to variant rs2235542 [ dbSNP | Ensembl ].
    VAR_037309
    Natural varianti199 – 1991G → A in GABEB; somatic second-site mutation. 1 Publication
    VAR_037310
    Natural varianti207 – 2071K → Q in GABEB; somatic second-site mutation. 1 Publication
    VAR_037311
    Natural varianti210 – 2101E → K in GABEB. 2 Publications
    VAR_004170
    Natural varianti292 – 2921R → L.
    Corresponds to variant rs12091253 [ dbSNP | Ensembl ].
    VAR_037312
    Natural varianti438 – 4381S → T.
    Corresponds to variant rs2229468 [ dbSNP | Ensembl ].
    VAR_034060
    Natural varianti450 – 4501R → C in a colorectal cancer sample; somatic mutation. 1 Publication
    VAR_035820
    Natural varianti527 – 5271V → M.
    Corresponds to variant rs2076349 [ dbSNP | Ensembl ].
    VAR_037313
    Natural varianti679 – 6791P → L in H-JEB. 1 Publication
    VAR_004171
    Natural varianti690 – 6901N → S.
    Corresponds to variant rs2229466 [ dbSNP | Ensembl ].
    VAR_034061
    Natural varianti852 – 8521M → L.1 Publication
    Corresponds to variant rs12748250 [ dbSNP | Ensembl ].
    VAR_034062
    Natural varianti926 – 9261A → D.
    Corresponds to variant rs2076222 [ dbSNP | Ensembl ].
    VAR_037314
    Natural varianti988 – 9881R → W.
    Corresponds to variant rs2229467 [ dbSNP | Ensembl ].
    VAR_034063

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L25541 mRNA. Translation: AAA61834.1.
    U17760
    , U17745, U17746, U17747, U17748, U17749, U17750, U17751, U17752, U17753, U17754, U17755, U17756, U17757, U17758, U17759 Genomic DNA. Translation: AAC51352.1.
    D37766 mRNA. Translation: BAA22263.1.
    AY035783 mRNA. Translation: AAK61364.1.
    AL023754 Genomic DNA. Translation: CAA19297.2.
    AL023754, AL031316 Genomic DNA. Translation: CAI19989.1.
    AL031316, AL023754 Genomic DNA. Translation: CAI20062.1.
    CH471100 Genomic DNA. Translation: EAW93448.1.
    CH471100 Genomic DNA. Translation: EAW93449.1.
    BC075838 mRNA. Translation: AAH75838.1.
    CCDSiCCDS1487.1.
    PIRiA53612.
    RefSeqiNP_000219.2. NM_000228.2.
    NP_001017402.1. NM_001017402.1.
    NP_001121113.1. NM_001127641.1.
    XP_005273181.1. XM_005273124.2.
    UniGeneiHs.497636.

    Genome annotation databases

    EnsembliENST00000356082; ENSP00000348384; ENSG00000196878.
    ENST00000367030; ENSP00000355997; ENSG00000196878.
    ENST00000391911; ENSP00000375778; ENSG00000196878.
    GeneIDi3914.
    KEGGihsa:3914.
    UCSCiuc001hhg.3. human.

    Polymorphism databases

    DMDMi2497600.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L25541 mRNA. Translation: AAA61834.1 .
    U17760
    , U17745 , U17746 , U17747 , U17748 , U17749 , U17750 , U17751 , U17752 , U17753 , U17754 , U17755 , U17756 , U17757 , U17758 , U17759 Genomic DNA. Translation: AAC51352.1 .
    D37766 mRNA. Translation: BAA22263.1 .
    AY035783 mRNA. Translation: AAK61364.1 .
    AL023754 Genomic DNA. Translation: CAA19297.2 .
    AL023754 , AL031316 Genomic DNA. Translation: CAI19989.1 .
    AL031316 , AL023754 Genomic DNA. Translation: CAI20062.1 .
    CH471100 Genomic DNA. Translation: EAW93448.1 .
    CH471100 Genomic DNA. Translation: EAW93449.1 .
    BC075838 mRNA. Translation: AAH75838.1 .
    CCDSi CCDS1487.1.
    PIRi A53612.
    RefSeqi NP_000219.2. NM_000228.2.
    NP_001017402.1. NM_001017402.1.
    NP_001121113.1. NM_001127641.1.
    XP_005273181.1. XM_005273124.2.
    UniGenei Hs.497636.

    3D structure databases

    ProteinModelPortali Q13751.
    SMRi Q13751. Positions 20-566.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 110108. 3 interactions.
    IntActi Q13751. 1 interaction.
    MINTi MINT-4053402.
    STRINGi 9606.ENSP00000348384.

    Chemistry

    ChEMBLi CHEMBL2364187.

    PTM databases

    PhosphoSitei Q13751.

    Polymorphism databases

    DMDMi 2497600.

    Proteomic databases

    MaxQBi Q13751.
    PaxDbi Q13751.
    PRIDEi Q13751.

    Protocols and materials databases

    DNASUi 3914.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000356082 ; ENSP00000348384 ; ENSG00000196878 .
    ENST00000367030 ; ENSP00000355997 ; ENSG00000196878 .
    ENST00000391911 ; ENSP00000375778 ; ENSG00000196878 .
    GeneIDi 3914.
    KEGGi hsa:3914.
    UCSCi uc001hhg.3. human.

    Organism-specific databases

    CTDi 3914.
    GeneCardsi GC01M209788.
    GeneReviewsi LAMB3.
    HGNCi HGNC:6490. LAMB3.
    HPAi HPA008069.
    MIMi 150310. gene.
    226650. phenotype.
    226700. phenotype.
    neXtProti NX_Q13751.
    Orphaneti 79402. Generalized junctional epidermolysis bullosa, non-Herlitz type.
    100031. Hypoplastic amelogenesis imperfecta.
    79404. Junctional epidermolysis bullosa, Herlitz type.
    PharmGKBi PA30278.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG289025.
    HOGENOMi HOG000113279.
    HOVERGENi HBG052302.
    InParanoidi Q13751.
    KOi K06244.
    OMAi RSQMEED.
    OrthoDBi EOG77WWBQ.
    PhylomeDBi Q13751.
    TreeFami TF352481.

    Enzyme and pathway databases

    Reactomei REACT_118572. Degradation of the extracellular matrix.
    REACT_150180. Assembly of collagen fibrils and other multimeric structures.
    REACT_150268. Anchoring fibril formation.
    REACT_163874. Non-integrin membrane-ECM interactions.
    REACT_169262. Laminin interactions.
    REACT_20537. Type I hemidesmosome assembly.

    Miscellaneous databases

    ChiTaRSi LAMB3. human.
    GeneWikii Laminin,_beta_3.
    GenomeRNAii 3914.
    NextBioi 15375.
    PMAP-CutDB Q13751.
    PROi Q13751.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q13751.
    Bgeei Q13751.
    CleanExi HS_LAMB3.
    Genevestigatori Q13751.

    Family and domain databases

    InterProi IPR013032. EGF-like_CS.
    IPR002049. EGF_laminin.
    IPR008211. Laminin_N.
    [Graphical view ]
    Pfami PF00053. Laminin_EGF. 6 hits.
    PF00055. Laminin_N. 1 hit.
    [Graphical view ]
    SMARTi SM00180. EGF_Lam. 6 hits.
    SM00136. LamNT. 1 hit.
    [Graphical view ]
    PROSITEi PS00022. EGF_1. 5 hits.
    PS01186. EGF_2. 1 hit.
    PS01248. EGF_LAM_1. 5 hits.
    PS50027. EGF_LAM_2. 6 hits.
    PS51117. LAMININ_NTER. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "The complete primary structure for a novel laminin chain, the laminin B1k chain."
      Gerecke D.R., Wagman D.W., Champliaud M.-F., Burgeson R.E.
      J. Biol. Chem. 269:11073-11080(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 172-190.
    2. "Cloning of the beta 3 chain gene (LAMB3) of human laminin 5, a candidate gene in junctional epidermolysis bullosa."
      Pulkkinen L., Gerecke D.R., Christiano A.M., Wagman D.W., Burgeson R.E., Uitto J.
      Genomics 25:192-198(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    3. "Chromosomal loci of 50 human keratinocyte cDNAs assigned by fluorescence in situ hybridization."
      Morishima Y., Ariyama T., Yamanishi K., Abe T., Ueda E., Yasuno H., Inazawa J.
      Genomics 28:273-279(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Epidermis.
    4. "In vivo restoration of laminin 5 beta 3 expression and function in junctional epidermolysis bullosa."
      Robbins P.B., Lin Q., Goodnough J.B., Tian H., Chen X., Khavari P.A.
      Proc. Natl. Acad. Sci. U.S.A. 98:5193-5198(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    5. "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].
    6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], VARIANT LEU-852.
    7. "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].
      Tissue: Eye.
    8. "ECM1 interacts with fibulin-3 and the beta 3 chain of laminin 332 through its serum albumin subdomain-like 2 domain."
      Sercu S., Lambeir A.M., Steenackers E., El Ghalbzouri A., Geentjens K., Sasaki T., Oyama N., Merregaert J.
      Matrix Biol. 28:160-169(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH ECM1.
    9. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    10. "Detection of sequence variants in the gene encoding the beta 3 chain of laminin 5 (LAMB3)."
      Pulkkinen L., McGrath J.A., Christiano A.M., Uitto J.
      Hum. Mutat. 6:77-84(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT H-JEB LEU-679.
    11. "E210K mutation in the gene encoding the beta3 chain of laminin-5 (LAMB3) is predictive of a phenotype of generalized atrophic benign epidermolysis bullosa."
      Mellerio J.E., Eady R.A.J., Atherton D.J., Lake B.D., McGrath J.A.
      Br. J. Dermatol. 139:325-331(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT GABEB LYS-210.
    12. Cited for: VARIANT [LARGE SCALE ANALYSIS] CYS-450.
    13. "Revertant mosaicism in junctional epidermolysis bullosa due to multiple correcting second-site mutations in LAMB3."
      Pasmooij A.M.G., Pas H.H., Bolling M.C., Jonkman M.F.
      J. Clin. Invest. 117:1240-1248(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS GABEB ALA-199; GLN-207 AND LYS-210.

    Entry informationi

    Entry nameiLAMB3_HUMAN
    AccessioniPrimary (citable) accession number: Q13751
    Secondary accession number(s): D3DT88
    , O14947, Q14733, Q9UJK4, Q9UJL1
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1997
    Last sequence update: November 1, 1996
    Last modified: October 1, 2014
    This is version 150 of the entry and version 1 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, Direct protein sequencing, 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