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Q13753

- LAMC2_HUMAN

UniProt

Q13753 - LAMC2_HUMAN

Protein

Laminin subunit gamma-2

Gene

LAMC2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 154 (01 Oct 2014)
      Sequence version 2 (07 Mar 2006)
      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. Ladsin exerts cell-scattering activity toward a wide variety of cells, including epithelial, endothelial, and fibroblastic cells.1 Publication

    GO - Molecular functioni

    1. heparin binding Source: UniProtKB-KW

    GO - Biological processi

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

    Keywords - Biological processi

    Cell adhesion

    Keywords - Ligandi

    Heparin-binding

    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 gamma-2
    Alternative name(s):
    Cell-scattering factor 140 kDa subunit
    Short name:
    CSF 140 kDa subunit
    Epiligrin subunit gamma
    Kalinin subunit gamma
    Kalinin/nicein/epiligrin 100 kDa subunit
    Ladsin 140 kDa subunit
    Laminin B2t chain
    Laminin-5 subunit gamma
    Large adhesive scatter factor 140 kDa subunit
    Nicein subunit gamma
    Gene namesi
    Name:LAMC2
    Synonyms:LAMB2T, LAMNB2
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 1

    Organism-specific databases

    HGNCiHGNC:6493. LAMC2.

    Subcellular locationi

    GO - Cellular componenti

    1. cell cortex Source: Ensembl
    2. extracellular region Source: Reactome
    3. extracellular space Source: Ensembl
    4. laminin-2 complex Source: Ensembl
    5. laminin-5 complex Source: Ensembl
    6. membrane Source: Ensembl
    7. perinuclear region of cytoplasm 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.
    Note: The disease is caused by mutations affecting the gene represented in this entry.

    Keywords - Diseasei

    Epidermolysis bullosa

    Organism-specific databases

    MIMi226700. phenotype.
    Orphaneti79402. Generalized junctional epidermolysis bullosa, non-Herlitz type.
    79405. Junctional epidermolysis bullosa inversa.
    79404. Junctional epidermolysis bullosa, Herlitz type.
    PharmGKBiPA30281.

    Protein family/group databases

    Allergomei8331. Hom s Laminin gamma_2.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2121Sequence AnalysisAdd
    BLAST
    Chaini22 – 11931172Laminin subunit gamma-2PRO_0000017077Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi28 ↔ 37PROSITE-ProRule annotation
    Disulfide bondi30 ↔ 53PROSITE-ProRule annotation
    Disulfide bondi56 ↔ 65PROSITE-ProRule annotation
    Disulfide bondi68 ↔ 81PROSITE-ProRule annotation
    Disulfide bondi84 ↔ 96PROSITE-ProRule annotation
    Disulfide bondi86 ↔ 102PROSITE-ProRule annotation
    Disulfide bondi104 ↔ 113PROSITE-ProRule annotation
    Disulfide bondi116 ↔ 128PROSITE-ProRule annotation
    Disulfide bondi139 ↔ 150PROSITE-ProRule annotation
    Disulfide bondi141 ↔ 155PROSITE-ProRule annotation
    Disulfide bondi157 ↔ 166PROSITE-ProRule annotation
    Disulfide bondi169 ↔ 184PROSITE-ProRule annotation
    Glycosylationi342 – 3421N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi362 – 3621N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi462 ↔ 470PROSITE-ProRule annotation
    Disulfide bondi464 ↔ 481PROSITE-ProRule annotation
    Disulfide bondi484 ↔ 493PROSITE-ProRule annotation
    Disulfide bondi496 ↔ 514PROSITE-ProRule annotation
    Disulfide bondi517 ↔ 531PROSITE-ProRule annotation
    Disulfide bondi519 ↔ 538PROSITE-ProRule annotation
    Disulfide bondi541 ↔ 550PROSITE-ProRule annotation
    Disulfide bondi553 ↔ 570PROSITE-ProRule annotation
    Disulfide bondi573 ↔ 585PROSITE-ProRule annotation
    Disulfide bondi575 ↔ 591PROSITE-ProRule annotation
    Disulfide bondi593 ↔ 602PROSITE-ProRule annotation
    Disulfide bondi609 – 609InterchainCurated
    Disulfide bondi612 – 612InterchainCurated
    Glycosylationi942 – 9421N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi1033 – 10331N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi1184 – 1184InterchainCurated

    Keywords - PTMi

    Disulfide bond, Glycoprotein

    Proteomic databases

    MaxQBiQ13753.
    PaxDbiQ13753.
    PeptideAtlasiQ13753.
    PRIDEiQ13753.

    PTM databases

    PhosphoSiteiQ13753.

    Miscellaneous databases

    PMAP-CutDBQ13753.

    Expressioni

    Tissue specificityi

    The large variant is expressed only in specific epithelial cells of embryonic and neonatal tissues. In 17-week old embryo the small variant is found in cerebral cortex, lung, and distal tubes of kidney, but not in epithelia except for distal tubuli.

    Gene expression databases

    BgeeiQ13753.
    CleanExiHS_LAMC2.
    GenevestigatoriQ13753.

    Organism-specific databases

    HPAiCAB004257.
    HPA024638.

    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-2 is a subunit of laminin-5 (laminin-332 or epiligrin/kalinin/nicein).

    Protein-protein interaction databases

    BioGridi110112. 5 interactions.
    DIPiDIP-190N.
    IntActiQ13753. 1 interaction.
    MINTiMINT-4053464.
    STRINGi9606.ENSP00000264144.

    Structurei

    3D structure databases

    ProteinModelPortaliQ13753.
    SMRiQ13753. Positions 6-168, 384-604.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini28 – 8356Laminin EGF-like 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini84 – 13047Laminin EGF-like 2PROSITE-ProRule annotationAdd
    BLAST
    Domaini139 – 18648Laminin EGF-like 3PROSITE-ProRule annotationAdd
    BLAST
    Domaini187 – 19610Laminin EGF-like 4; first partPROSITE-ProRule annotation
    Domaini213 – 381169Laminin IV type APROSITE-ProRule annotationAdd
    BLAST
    Domaini382 – 41534Laminin EGF-like 4; second partPROSITE-ProRule annotationAdd
    BLAST
    Domaini416 – 46146Laminin EGF-like 5PROSITE-ProRule annotationAdd
    BLAST
    Domaini462 – 51655Laminin EGF-like 6PROSITE-ProRule annotationAdd
    BLAST
    Domaini517 – 57256Laminin EGF-like 7PROSITE-ProRule annotationAdd
    BLAST
    Domaini573 – 60230Laminin EGF-like 8; truncatedPROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni603 – 1193591Domain II and IAdd
    BLAST

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili611 – 718108Sequence AnalysisAdd
    BLAST
    Coiled coili811 – 1076266Sequence AnalysisAdd
    BLAST
    Coiled coili1117 – 119377Sequence 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 IV is globular.

    Sequence similaritiesi

    Contains 8 laminin EGF-like domains.PROSITE-ProRule annotation
    Contains 1 laminin IV type A domain.PROSITE-ProRule annotation

    Keywords - Domaini

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

    Phylogenomic databases

    eggNOGiNOG285700.
    HOVERGENiHBG062127.
    InParanoidiQ13753.
    KOiK06246.
    OMAiDRCLPCN.
    OrthoDBiEOG7SR4KJ.
    PhylomeDBiQ13753.

    Family and domain databases

    InterProiIPR002049. EGF_laminin.
    IPR018031. Laminin_B_subgr.
    IPR000034. Laminin_B_type_IV.
    [Graphical view]
    PfamiPF00052. Laminin_B. 1 hit.
    PF00053. Laminin_EGF. 7 hits.
    [Graphical view]
    SMARTiSM00180. EGF_Lam. 6 hits.
    SM00281. LamB. 1 hit.
    [Graphical view]
    PROSITEiPS00022. EGF_1. 4 hits.
    PS01186. EGF_2. 2 hits.
    PS01248. EGF_LAM_1. 6 hits.
    PS50027. EGF_LAM_2. 6 hits.
    PS51115. LAMININ_IVA. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

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

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform Long (identifier: Q13753-1) [UniParc]FASTAAdd to Basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MPALWLGCCL CFSLLLPAAR ATSRREVCDC NGKSRQCIFD RELHRQTGNG     50
    FRCLNCNDNT DGIHCEKCKN GFYRHRERDR CLPCNCNSKG SLSARCDNSG 100
    RCSCKPGVTG ARCDRCLPGF HMLTDAGCTQ DQRLLDSKCD CDPAGIAGPC 150
    DAGRCVCKPA VTGERCDRCR SGYYNLDGGN PEGCTQCFCY GHSASCRSSA 200
    EYSVHKITST FHQDVDGWKA VQRNGSPAKL QWSQRHQDVF SSAQRLDPVY 250
    FVAPAKFLGN QQVSYGQSLS FDYRVDRGGR HPSAHDVILE GAGLRITAPL 300
    MPLGKTLPCG LTKTYTFRLN EHPSNNWSPQ LSYFEYRRLL RNLTALRIRA 350
    TYGEYSTGYI DNVTLISARP VSGAPAPWVE QCICPVGYKG QFCQDCASGY 400
    KRDSARLGPF GTCIPCNCQG GGACDPDTGD CYSGDENPDI ECADCPIGFY 450
    NDPHDPRSCK PCPCHNGFSC SVMPETEEVV CNNCPPGVTG ARCELCADGY 500
    FGDPFGEHGP VRPCQPCQCN NNVDPSASGN CDRLTGRCLK CIHNTAGIYC 550
    DQCKAGYFGD PLAPNPADKC RACNCNPMGS EPVGCRSDGT CVCKPGFGGP 600
    NCEHGAFSCP ACYNQVKIQM DQFMQQLQRM EALISKAQGG DGVVPDTELE 650
    GRMQQAEQAL QDILRDAQIS EGASRSLGLQ LAKVRSQENS YQSRLDDLKM 700
    TVERVRALGS QYQNRVRDTH RLITQMQLSL AESEASLGNT NIPASDHYVG 750
    PNGFKSLAQE ATRLAESHVE SASNMEQLTR ETEDYSKQAL SLVRKALHEG 800
    VGSGSGSPDG AVVQGLVEKL EKTKSLAQQL TREATQAEIE ADRSYQHSLR 850
    LLDSVSRLQG VSDQSFQVEE AKRIKQKADS LSSLVTRHMD EFKRTQKNLG 900
    NWKEEAQQLL QNGKSGREKS DQLLSRANLA KSRAQEALSM GNATFYEVES 950
    ILKNLREFDL QVDNRKAEAE EAMKRLSYIS QKVSDASDKT QQAERALGSA 1000
    AADAQRAKNG AGEALEISSE IEQEIGSLNL EANVTADGAL AMEKGLASLK 1050
    SEMREVEGEL ERKELEFDTN MDAVQMVITE AQKVDTRAKN AGVTIQDTLN 1100
    TLDGLLHLMD QPLSVDEEGL VLLEQKLSRA KTQINSQLRP MMSELEERAR 1150
    QQRGHLHLLE TSIDGILADV KNLENIRDNL PPGCYNTQAL EQQ 1193
    Length:1,193
    Mass (Da):130,976
    Last modified:March 7, 2006 - v2
    Checksum:i0BBE1A56516C5C9A
    GO
    Isoform Short (identifier: Q13753-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1110-1193: DQPLSVDEEG...CYNTQALEQQ → GM

    Show »
    Length:1,111
    Mass (Da):121,604
    Checksum:i7762993F3D7F89DF
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti12 – 121F → L in CAA52108. (PubMed:8306988)Curated
    Sequence conflicti473 – 4731M → I in CAA78728. (PubMed:1383240)Curated
    Sequence conflicti473 – 4731M → I in CAA78729. (PubMed:1383240)Curated
    Sequence conflicti521 – 5211N → S in CAA78728. (PubMed:1383240)Curated
    Sequence conflicti521 – 5211N → S in CAA78729. (PubMed:1383240)Curated
    Sequence conflicti857 – 8571R → P in CAA78728. (PubMed:1383240)Curated
    Sequence conflicti857 – 8571R → P in CAA78729. (PubMed:1383240)Curated
    Sequence conflicti883 – 8831S → T in AAC50457. (PubMed:8786121)Curated
    Sequence conflicti883 – 8831S → T in AAC50456. (PubMed:8786121)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti111 – 1111A → P.
    Corresponds to variant rs12065473 [ dbSNP | Ensembl ].
    VAR_050081
    Natural varianti115 – 1151R → Q.
    Corresponds to variant rs17481405 [ dbSNP | Ensembl ].
    VAR_050082
    Natural varianti124 – 1241T → M.
    Corresponds to variant rs11586699 [ dbSNP | Ensembl ].
    VAR_050083
    Natural varianti136 – 1361D → V.
    Corresponds to variant rs12037099 [ dbSNP | Ensembl ].
    VAR_050084
    Natural varianti247 – 2471D → E.
    Corresponds to variant rs2296306 [ dbSNP | Ensembl ].
    VAR_022017
    Natural varianti608 – 6081S → I.
    Corresponds to variant rs4373715 [ dbSNP | Ensembl ].
    VAR_050085
    Natural varianti733 – 7331S → T.
    Corresponds to variant rs2296303 [ dbSNP | Ensembl ].
    VAR_020304

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1110 – 119384DQPLS…ALEQQ → GM in isoform Short. 1 PublicationVSP_003040Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Z15008 mRNA. Translation: CAA78728.1.
    Z15009 mRNA. Translation: CAA78729.1.
    X73902 mRNA. Translation: CAA52108.1.
    U31201
    , U31178, U31179, U31180, U31181, U31182, U31183, U31184, U31186, U31187, U31188, U31189, U31190, U31191, U31192, U31193, U31194, U31195, U31196, U31197, U31198, U31199 Genomic DNA. Translation: AAC50457.1.
    U31200
    , U31178, U31179, U31180, U31181, U31182, U31183, U31184, U31186, U31187, U31188, U31189, U31190, U31191, U31192, U31193, U31194, U31195, U31196, U31197, U31198 Genomic DNA. Translation: AAC50456.1.
    AL354953 Genomic DNA. Translation: CAH70980.1.
    CH471067 Genomic DNA. Translation: EAW91146.1.
    BC112286 mRNA. Translation: AAI12287.1.
    BC113378 mRNA. Translation: AAI13379.1.
    CCDSiCCDS1352.1. [Q13753-1]
    CCDS44285.1. [Q13753-2]
    PIRiA44018.
    RefSeqiNP_005553.2. NM_005562.2. [Q13753-1]
    NP_061486.2. NM_018891.2. [Q13753-2]
    UniGeneiHs.591484.

    Genome annotation databases

    EnsembliENST00000264144; ENSP00000264144; ENSG00000058085. [Q13753-1]
    ENST00000493293; ENSP00000432063; ENSG00000058085. [Q13753-2]
    GeneIDi3918.
    KEGGihsa:3918.
    UCSCiuc001gpz.4. human. [Q13753-2]
    uc001gqa.2. human. [Q13753-1]

    Polymorphism databases

    DMDMi90185107.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Z15008 mRNA. Translation: CAA78728.1 .
    Z15009 mRNA. Translation: CAA78729.1 .
    X73902 mRNA. Translation: CAA52108.1 .
    U31201
    , U31178 , U31179 , U31180 , U31181 , U31182 , U31183 , U31184 , U31186 , U31187 , U31188 , U31189 , U31190 , U31191 , U31192 , U31193 , U31194 , U31195 , U31196 , U31197 , U31198 , U31199 Genomic DNA. Translation: AAC50457.1 .
    U31200
    , U31178 , U31179 , U31180 , U31181 , U31182 , U31183 , U31184 , U31186 , U31187 , U31188 , U31189 , U31190 , U31191 , U31192 , U31193 , U31194 , U31195 , U31196 , U31197 , U31198 Genomic DNA. Translation: AAC50456.1 .
    AL354953 Genomic DNA. Translation: CAH70980.1 .
    CH471067 Genomic DNA. Translation: EAW91146.1 .
    BC112286 mRNA. Translation: AAI12287.1 .
    BC113378 mRNA. Translation: AAI13379.1 .
    CCDSi CCDS1352.1. [Q13753-1 ]
    CCDS44285.1. [Q13753-2 ]
    PIRi A44018.
    RefSeqi NP_005553.2. NM_005562.2. [Q13753-1 ]
    NP_061486.2. NM_018891.2. [Q13753-2 ]
    UniGenei Hs.591484.

    3D structure databases

    ProteinModelPortali Q13753.
    SMRi Q13753. Positions 6-168, 384-604.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 110112. 5 interactions.
    DIPi DIP-190N.
    IntActi Q13753. 1 interaction.
    MINTi MINT-4053464.
    STRINGi 9606.ENSP00000264144.

    Chemistry

    ChEMBLi CHEMBL2364187.

    Protein family/group databases

    Allergomei 8331. Hom s Laminin gamma_2.

    PTM databases

    PhosphoSitei Q13753.

    Polymorphism databases

    DMDMi 90185107.

    Proteomic databases

    MaxQBi Q13753.
    PaxDbi Q13753.
    PeptideAtlasi Q13753.
    PRIDEi Q13753.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000264144 ; ENSP00000264144 ; ENSG00000058085 . [Q13753-1 ]
    ENST00000493293 ; ENSP00000432063 ; ENSG00000058085 . [Q13753-2 ]
    GeneIDi 3918.
    KEGGi hsa:3918.
    UCSCi uc001gpz.4. human. [Q13753-2 ]
    uc001gqa.2. human. [Q13753-1 ]

    Organism-specific databases

    CTDi 3918.
    GeneCardsi GC01P183155.
    GeneReviewsi LAMC2.
    HGNCi HGNC:6493. LAMC2.
    HPAi CAB004257.
    HPA024638.
    MIMi 150292. gene.
    226700. phenotype.
    neXtProti NX_Q13753.
    Orphaneti 79402. Generalized junctional epidermolysis bullosa, non-Herlitz type.
    79405. Junctional epidermolysis bullosa inversa.
    79404. Junctional epidermolysis bullosa, Herlitz type.
    PharmGKBi PA30281.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG285700.
    HOVERGENi HBG062127.
    InParanoidi Q13753.
    KOi K06246.
    OMAi DRCLPCN.
    OrthoDBi EOG7SR4KJ.
    PhylomeDBi Q13753.

    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 LAMC2. human.
    GeneWikii Laminin,_gamma_2.
    GenomeRNAii 3918.
    NextBioi 15391.
    PMAP-CutDB Q13753.
    PROi Q13753.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q13753.
    CleanExi HS_LAMC2.
    Genevestigatori Q13753.

    Family and domain databases

    InterProi IPR002049. EGF_laminin.
    IPR018031. Laminin_B_subgr.
    IPR000034. Laminin_B_type_IV.
    [Graphical view ]
    Pfami PF00052. Laminin_B. 1 hit.
    PF00053. Laminin_EGF. 7 hits.
    [Graphical view ]
    SMARTi SM00180. EGF_Lam. 6 hits.
    SM00281. LamB. 1 hit.
    [Graphical view ]
    PROSITEi PS00022. EGF_1. 4 hits.
    PS01186. EGF_2. 2 hits.
    PS01248. EGF_LAM_1. 6 hits.
    PS50027. EGF_LAM_2. 6 hits.
    PS51115. LAMININ_IVA. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "A truncated laminin chain homologous to the B2 chain: structure, spatial expression, and chromosomal assignment."
      Kallunki P., Sainio K., Eddy R., Byers M., Kallunki T., Sariola H., Beck K., Hirvonen H., Shows T.B., Tryggvason K.
      J. Cell Biol. 119:679-693(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], ALTERNATIVE SPLICING.
      Tissue: Fibrosarcoma.
    2. Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 1090-1114.
      Tissue: Epidermis and Keratinocyte.
    3. "Structure of the human laminin gamma 2 chain gene (LAMC2): alternative splicing with different tissue distribution of two transcripts."
      Airenne T., Haakana H., Sainio K., Kallunki T., Kallunki P., Sariola H., Tryggvason K.
      Genomics 32:54-64(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], ALTERNATIVE SPLICING.
      Tissue: Placenta.
    4. "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].
    5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    6. "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] (ISOFORM SHORT).
      Tissue: Cerebellum.
    7. "A large cell-adhesive scatter factor secreted by human gastric carcinoma cells."
      Miyazaki K., Kikkawa Y., Nakamura A., Yasumitsu H., Umeda M.
      Proc. Natl. Acad. Sci. U.S.A. 90:11767-11771(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE OF 435-449, FUNCTION, HEPARIN-BINDING.
    8. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiLAMC2_HUMAN
    AccessioniPrimary (citable) accession number: Q13753
    Secondary accession number(s): Q02536
    , Q02537, Q13752, Q14941, Q14DF7, Q2M1N2, Q5VYE8
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1997
    Last sequence update: March 7, 2006
    Last modified: October 1, 2014
    This is version 154 of the entry and version 2 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

    Miscellaneous

    Binds heparin.By similarity

    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