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P55268

- LAMB2_HUMAN

UniProt

P55268 - LAMB2_HUMAN

Protein

Laminin subunit beta-2

Gene

LAMB2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 141 (01 Oct 2014)
      Sequence version 2 (21 Aug 2007)
      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. structural molecule activity Source: ProtInc

    GO - Biological processi

    1. astrocyte development Source: Ensembl
    2. axon extension involved in regeneration Source: Ensembl
    3. axon guidance Source: Ensembl
    4. cell adhesion Source: UniProtKB-KW
    5. extracellular matrix organization Source: Reactome
    6. metanephric glomerular basement membrane development Source: Ensembl
    7. metanephric glomerular visceral epithelial cell development Source: Ensembl
    8. neuromuscular junction development Source: Ensembl
    9. retina development in camera-type eye Source: Ensembl
    10. Schwann cell development Source: Ensembl
    11. visual perception Source: Ensembl

    Keywords - Biological processi

    Cell adhesion

    Enzyme and pathway databases

    ReactomeiREACT_163874. Non-integrin membrane-ECM interactions.
    REACT_163906. ECM proteoglycans.
    REACT_169262. Laminin interactions.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Laminin subunit beta-2
    Alternative name(s):
    Laminin B1s chain
    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
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 3

    Organism-specific databases

    HGNCiHGNC:6487. LAMB2.

    Subcellular locationi

    Secretedextracellular spaceextracellular matrixbasement membrane
    Note: S-laminin is concentrated in the synaptic cleft of the neuromuscular junction.

    GO - Cellular componenti

    1. basal lamina Source: ProtInc
    2. basement membrane Source: UniProtKB
    3. extracellular region Source: Reactome
    4. extracellular vesicular exosome Source: UniProt
    5. laminin-11 complex Source: BHF-UCL
    6. laminin-3 complex Source: UniProtKB
    7. synapse Source: Ensembl

    Keywords - Cellular componenti

    Basement membrane, Extracellular matrix, Secreted

    Pathology & Biotechi

    Involvement in diseasei

    Pierson syndrome (PIERSS) [MIM:609049]: Characterized by nephrotic syndrome with neonatal onset, diffuse mesangial sclerosis and eye abnormalities with microcoria as the leading clinical feature. Death usually occurs within the first weeks of life. Disease severity depends on the mutation type: nontruncating LAMB2 mutations may display variable phenotypes ranging from a milder variant of Pierson syndrome to isolated congenital nephrotic syndrome.2 Publications
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti246 – 2461R → Q in PIERSS; without ocular abnormalities. 1 Publication
    VAR_031968
    Natural varianti246 – 2461R → W in PIERSS. 1 Publication
    VAR_031969
    Natural varianti321 – 3211C → R in PIERSS; with mild ocular abnormalities. 1 Publication
    VAR_031970
    Natural varianti1380 – 13801N → K in PIERSS; with mild ocular abnormalities; associated with F-1393. 1 Publication
    VAR_031972
    Natural varianti1393 – 13931L → F in PIERSS; with mild ocular abnormalities; associated with K-1380. 1 Publication
    VAR_031973
    Nephrotic syndrome 5 with or without ocular abnormalities (NPHS5) [MIM:614199]: A form of nephrotic syndrome, a renal disease clinically characterized by severe proteinuria, resulting in complications such as hypoalbuminemia, hyperlipidemia and edema. Kidney biopsies show non-specific histologic changes such as focal segmental glomerulosclerosis and diffuse mesangial proliferation. Some affected individuals have an inherited steroid-resistant form and progress to end-stage renal failure. NPHS5 is characterized by very early onset of progressive renal failure. A subset of patients may develop mild ocular anomalies, such as myopia, nystagmus, and strabismus.1 Publication
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti147 – 1471H → R in NPHS5. 1 Publication
    VAR_066492

    Keywords - Diseasei

    Disease mutation

    Organism-specific databases

    MIMi609049. phenotype.
    614199. phenotype.
    Orphaneti306507. LAMB-2-related infantile-onset nephrotic syndrome.
    2670. Pierson syndrome.
    98915. Synaptic congenital myasthenic syndromes.
    PharmGKBiPA164741827.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 3232Sequence AnalysisAdd
    BLAST
    Chaini33 – 17981766Laminin subunit beta-2PRO_0000017068Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi248 – 2481N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi283 ↔ 292PROSITE-ProRule annotation
    Disulfide bondi285 ↔ 310PROSITE-ProRule annotation
    Disulfide bondi312 ↔ 321PROSITE-ProRule annotation
    Disulfide bondi324 ↔ 344PROSITE-ProRule annotation
    Disulfide bondi347 ↔ 356PROSITE-ProRule annotation
    Disulfide bondi349 ↔ 374PROSITE-ProRule annotation
    Glycosylationi368 – 3681N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi377 ↔ 386PROSITE-ProRule annotation
    Disulfide bondi389 ↔ 407PROSITE-ProRule annotation
    Disulfide bondi410 ↔ 423PROSITE-ProRule annotation
    Disulfide bondi412 ↔ 438PROSITE-ProRule annotation
    Disulfide bondi440 ↔ 449PROSITE-ProRule annotation
    Disulfide bondi452 ↔ 467PROSITE-ProRule annotation
    Disulfide bondi470 ↔ 484PROSITE-ProRule annotation
    Disulfide bondi472 ↔ 491PROSITE-ProRule annotation
    Disulfide bondi493 ↔ 502PROSITE-ProRule annotation
    Disulfide bondi505 ↔ 519PROSITE-ProRule annotation
    Disulfide bondi522 ↔ 534PROSITE-ProRule annotation
    Disulfide bondi524 ↔ 541PROSITE-ProRule annotation
    Disulfide bondi543 ↔ 552PROSITE-ProRule annotation
    Disulfide bondi783 ↔ 795PROSITE-ProRule annotation
    Disulfide bondi785 ↔ 802PROSITE-ProRule annotation
    Disulfide bondi804 ↔ 813PROSITE-ProRule annotation
    Disulfide bondi816 ↔ 828PROSITE-ProRule annotation
    Disulfide bondi831 ↔ 843PROSITE-ProRule annotation
    Disulfide bondi833 ↔ 850PROSITE-ProRule annotation
    Disulfide bondi852 ↔ 861PROSITE-ProRule annotation
    Disulfide bondi864 ↔ 874PROSITE-ProRule annotation
    Disulfide bondi877 ↔ 886PROSITE-ProRule annotation
    Disulfide bondi879 ↔ 893PROSITE-ProRule annotation
    Disulfide bondi896 ↔ 905PROSITE-ProRule annotation
    Disulfide bondi908 ↔ 924PROSITE-ProRule annotation
    Disulfide bondi927 ↔ 943PROSITE-ProRule annotation
    Disulfide bondi929 ↔ 954PROSITE-ProRule annotation
    Disulfide bondi956 ↔ 965PROSITE-ProRule annotation
    Disulfide bondi968 ↔ 983PROSITE-ProRule annotation
    Disulfide bondi986 ↔ 1000PROSITE-ProRule annotation
    Disulfide bondi988 ↔ 1007PROSITE-ProRule annotation
    Disulfide bondi1010 ↔ 1019PROSITE-ProRule annotation
    Disulfide bondi1022 ↔ 1035PROSITE-ProRule annotation
    Disulfide bondi1038 ↔ 1058PROSITE-ProRule annotation
    Disulfide bondi1040 ↔ 1065PROSITE-ProRule annotation
    Disulfide bondi1067 ↔ 1076PROSITE-ProRule annotation
    Disulfide bondi1079 ↔ 1092PROSITE-ProRule annotation
    Glycosylationi1085 – 10851N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi1095 ↔ 1107PROSITE-ProRule annotation
    Disulfide bondi1097 ↔ 1114PROSITE-ProRule annotation
    Disulfide bondi1116 ↔ 1125PROSITE-ProRule annotation
    Disulfide bondi1128 ↔ 1140PROSITE-ProRule annotation
    Disulfide bondi1143 ↔ 1155PROSITE-ProRule annotation
    Disulfide bondi1145 ↔ 1162PROSITE-ProRule annotation
    Disulfide bondi1164 ↔ 1173PROSITE-ProRule annotation
    Disulfide bondi1176 ↔ 1187PROSITE-ProRule annotation
    Disulfide bondi1190 – 1190InterchainCurated
    Disulfide bondi1193 – 1193InterchainCurated
    Glycosylationi1249 – 12491N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi1308 – 13081N-linked (GlcNAc...)1 Publication
    Glycosylationi1348 – 13481N-linked (GlcNAc...)1 Publication
    Glycosylationi1499 – 14991N-linked (GlcNAc...)1 Publication
    Disulfide bondi1797 – 1797InterchainCurated

    Keywords - PTMi

    Disulfide bond, Glycoprotein

    Proteomic databases

    MaxQBiP55268.
    PaxDbiP55268.
    PRIDEiP55268.

    PTM databases

    PhosphoSiteiP55268.

    Expressioni

    Gene expression databases

    ArrayExpressiP55268.
    BgeeiP55268.
    CleanExiHS_LAMB2.
    GenevestigatoriP55268.

    Organism-specific databases

    HPAiCAB000053.
    HPA001895.
    HPA050033.

    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

    BioGridi110107. 12 interactions.
    DIPiDIP-42106N.
    IntActiP55268. 11 interactions.
    MINTiMINT-1197111.
    STRINGi9606.ENSP00000307156.

    Structurei

    3D structure databases

    ProteinModelPortaliP55268.
    SMRiP55268. Positions 41-560, 792-1180.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini43 – 282240Laminin N-terminalPROSITE-ProRule annotationAdd
    BLAST
    Domaini283 – 34664Laminin EGF-like 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini347 – 40963Laminin EGF-like 2PROSITE-ProRule annotationAdd
    BLAST
    Domaini410 – 46960Laminin EGF-like 3PROSITE-ProRule annotationAdd
    BLAST
    Domaini470 – 52152Laminin EGF-like 4PROSITE-ProRule annotationAdd
    BLAST
    Domaini522 – 55231Laminin EGF-like 5; truncatedPROSITE-ProRule annotationAdd
    BLAST
    Domaini561 – 777217Laminin IV type BPROSITE-ProRule annotationAdd
    BLAST
    Domaini783 – 83048Laminin EGF-like 6PROSITE-ProRule annotationAdd
    BLAST
    Domaini831 – 87646Laminin EGF-like 7PROSITE-ProRule annotationAdd
    BLAST
    Domaini877 – 92650Laminin EGF-like 8PROSITE-ProRule annotationAdd
    BLAST
    Domaini927 – 98559Laminin EGF-like 9PROSITE-ProRule annotationAdd
    BLAST
    Domaini986 – 103752Laminin EGF-like 10PROSITE-ProRule annotationAdd
    BLAST
    Domaini1038 – 109457Laminin EGF-like 11PROSITE-ProRule annotationAdd
    BLAST
    Domaini1095 – 114248Laminin EGF-like 12PROSITE-ProRule annotationAdd
    BLAST
    Domaini1143 – 118947Laminin EGF-like 13PROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni1190 – 1409220Domain IIAdd
    BLAST
    Regioni1410 – 144233Domain alphaAdd
    BLAST
    Regioni1443 – 1798356Domain IAdd
    BLAST

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili1253 – 131967Sequence AnalysisAdd
    BLAST
    Coiled coili1472 – 152655Sequence AnalysisAdd
    BLAST
    Coiled coili1577 – 1790214Sequence 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.
    HOGENOMiHOG000007552.
    HOVERGENiHBG052301.
    InParanoidiP55268.
    KOiK06243.
    OMAiQPYCIVS.
    OrthoDBiEOG75XGK0.
    PhylomeDBiP55268.
    TreeFamiTF312903.

    Family and domain databases

    InterProiIPR013032. EGF-like_CS.
    IPR002049. 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.

    P55268-1 [UniParc]FASTAAdd to Basket

    « Hide

    MELTSRERGR GQPLPWELRL GLLLSVLAAT LAQAPAPDVP GCSRGSCYPA     50
    TGDLLVGRAD RLTASSTCGL NGPQPYCIVS HLQDEKKCFL CDSRRPFSAR 100
    DNPHSHRIQN VVTSFAPQRR AAWWQSENGI PAVTIQLDLE AEFHFTHLIM 150
    TFKTFRPAAM LVERSADFGR TWHVYRYFSY DCGADFPGVP LAPPRHWDDV 200
    VCESRYSEIE PSTEGEVIYR VLDPAIPIPD PYSSRIQNLL KITNLRVNLT 250
    RLHTLGDNLL DPRREIREKY YYALYELVVR GNCFCYGHAS ECAPAPGAPA 300
    HAEGMVHGAC ICKHNTRGLN CEQCQDFYRD LPWRPAEDGH SHACRKCECH 350
    GHTHSCHFDM AVYLASGNVS GGVCDGCQHN TAGRHCELCR PFFYRDPTKD 400
    LRDPAVCRSC DCDPMGSQDG GRCDSHDDPA LGLVSGQCRC KEHVVGTRCQ 450
    QCRDGFFGLS ISDRLGCRRC QCNARGTVPG STPCDPNSGS CYCKRLVTGR 500
    GCDRCLPGHW GLSHDLLGCR PCDCDVGGAL DPQCDEGTGQ CHCRQHMVGR 550
    RCEQVQPGYF RPFLDHLIWE AEDTRGQVLD VVERLVTPGE TPSWTGSGFV 600
    RLQEGQTLEF LVASVPKAMD YDLLLRLEPQ VPEQWAELEL IVQRPGPVPA 650
    HSLCGHLVPK DDRIQGTLQP HARYLIFPNP VCLEPGISYK LHLKLVRTGG 700
    SAQPETPYSG PGLLIDSLVL LPRVLVLEMF SGGDAAALER QATFERYQCH 750
    EEGLVPSKTS PSEACAPLLI SLSTLIYNGA LPCQCNPQGS LSSECNPHGG 800
    QCLCKPGVVG RRCDLCAPGY YGFGPTGCQA CQCSHEGALS SLCEKTSGQC 850
    LCRTGAFGLR CDRCQRGQWG FPSCRPCVCN GHADECNTHT GACLGCRDHT 900
    GGEHCERCIA GFHGDPRLPY GGQCRPCPCP EGPGSQRHFA TSCHQDEYSQ 950
    QIVCHCRAGY TGLRCEACAP GHFGDPSRPG GRCQLCECSG NIDPMDPDAC 1000
    DPHTGQCLRC LHHTEGPHCA HCKPGFHGQA ARQSCHRCTC NLLGTNPQQC 1050
    PSPDQCHCDP SSGQCPCLPN VQGPSCDRCA PNFWNLTSGH GCQPCACHPS 1100
    RARGPTCNEF TGQCHCRAGF GGRTCSECQE LHWGDPGLQC HACDCDSRGI 1150
    DTPQCHRFTG HCSCRPGVSG VRCDQCARGF SGIFPACHPC HACFGDWDRV 1200
    VQDLAARTQR LEQRAQELQQ TGVLGAFESS FWHMQEKLGI VQGIVGARNT 1250
    SAASTAQLVE ATEELRREIG EATEHLTQLE ADLTDVQDEN FNANHALSGL 1300
    ERDRLALNLT LRQLDQHLDL LKHSNFLGAY DSIRHAHSQS AEAERRANTS 1350
    ALAVPSPVSN SASARHRTEA LMDAQKEDFN SKHMANQRAL GKLSAHTHTL 1400
    SLTDINELVC GAPGDAPCAT SPCGGAGCRD EDGQPRCGGL SCNGAAATAD 1450
    LALGRARHTQ AELQRALAEG GSILSRVAET RRQASEAQQR AQAALDKANA 1500
    SRGQVEQANQ ELQELIQSVK DFLNQEGADP DSIEMVATRV LELSIPASAE 1550
    QIQHLAGAIA ERVRSLADVD AILARTVGDV RRAEQLLQDA RRARSWAEDE 1600
    KQKAETVQAA LEEAQRAQGI AQGAIRGAVA DTRDTEQTLY QVQERMAGAE 1650
    RALSSAGERA RQLDALLEAL KLKRAGNSLA ASTAEETAGS AQGRAQEAEQ 1700
    LLRGPLGDQY QTVKALAERK AQGVLAAQAR AEQLRDEARD LLQAAQDKLQ 1750
    RLQELEGTYE ENERALESKA AQLDGLEARM RSVLQAINLQ VQIYNTCQ 1798
    Length:1,798
    Mass (Da):195,981
    Last modified:August 21, 2007 - v2
    Checksum:iFFB3531AD13E1486
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti914 – 9141G → R in CAA92279. (PubMed:7698745)Curated
    Sequence conflicti1179 – 11791G → A in AAB34682. (PubMed:7795887)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti147 – 1471H → R in NPHS5. 1 Publication
    VAR_066492
    Natural varianti246 – 2461R → Q in PIERSS; without ocular abnormalities. 1 Publication
    VAR_031968
    Natural varianti246 – 2461R → W in PIERSS. 1 Publication
    VAR_031969
    Natural varianti321 – 3211C → R in PIERSS; with mild ocular abnormalities. 1 Publication
    VAR_031970
    Natural varianti987 – 9871E → K.
    Corresponds to variant rs34759087 [ dbSNP | Ensembl ].
    VAR_031971
    Natural varianti1380 – 13801N → K in PIERSS; with mild ocular abnormalities; associated with F-1393. 1 Publication
    VAR_031972
    Natural varianti1393 – 13931L → F in PIERSS; with mild ocular abnormalities; associated with K-1380. 1 Publication
    VAR_031973

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Z68155, Z68156 Genomic DNA. Translation: CAA92279.1.
    X79683 mRNA. Translation: CAA56130.1.
    S77512 mRNA. Translation: AAB34682.2.
    CCDSiCCDS2789.1.
    PIRiA55677.
    S53869.
    RefSeqiNP_002283.3. NM_002292.3.
    XP_005265184.1. XM_005265127.2.
    UniGeneiHs.439726.

    Genome annotation databases

    EnsembliENST00000305544; ENSP00000307156; ENSG00000172037.
    ENST00000418109; ENSP00000388325; ENSG00000172037.
    GeneIDi3913.
    KEGGihsa:3913.
    UCSCiuc003cwe.3. human.

    Polymorphism databases

    DMDMi156630892.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Z68155 , Z68156 Genomic DNA. Translation: CAA92279.1 .
    X79683 mRNA. Translation: CAA56130.1 .
    S77512 mRNA. Translation: AAB34682.2 .
    CCDSi CCDS2789.1.
    PIRi A55677.
    S53869.
    RefSeqi NP_002283.3. NM_002292.3.
    XP_005265184.1. XM_005265127.2.
    UniGenei Hs.439726.

    3D structure databases

    ProteinModelPortali P55268.
    SMRi P55268. Positions 41-560, 792-1180.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 110107. 12 interactions.
    DIPi DIP-42106N.
    IntActi P55268. 11 interactions.
    MINTi MINT-1197111.
    STRINGi 9606.ENSP00000307156.

    Chemistry

    ChEMBLi CHEMBL2364187.

    PTM databases

    PhosphoSitei P55268.

    Polymorphism databases

    DMDMi 156630892.

    Proteomic databases

    MaxQBi P55268.
    PaxDbi P55268.
    PRIDEi P55268.

    Protocols and materials databases

    DNASUi 3913.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000305544 ; ENSP00000307156 ; ENSG00000172037 .
    ENST00000418109 ; ENSP00000388325 ; ENSG00000172037 .
    GeneIDi 3913.
    KEGGi hsa:3913.
    UCSCi uc003cwe.3. human.

    Organism-specific databases

    CTDi 3913.
    GeneCardsi GC03M049133.
    HGNCi HGNC:6487. LAMB2.
    HPAi CAB000053.
    HPA001895.
    HPA050033.
    MIMi 150325. gene.
    609049. phenotype.
    614199. phenotype.
    neXtProti NX_P55268.
    Orphaneti 306507. LAMB-2-related infantile-onset nephrotic syndrome.
    2670. Pierson syndrome.
    98915. Synaptic congenital myasthenic syndromes.
    PharmGKBi PA164741827.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG241384.
    HOGENOMi HOG000007552.
    HOVERGENi HBG052301.
    InParanoidi P55268.
    KOi K06243.
    OMAi QPYCIVS.
    OrthoDBi EOG75XGK0.
    PhylomeDBi P55268.
    TreeFami TF312903.

    Enzyme and pathway databases

    Reactomei REACT_163874. Non-integrin membrane-ECM interactions.
    REACT_163906. ECM proteoglycans.
    REACT_169262. Laminin interactions.

    Miscellaneous databases

    ChiTaRSi LAMB2. human.
    GeneWikii Laminin,_beta_2.
    GenomeRNAii 3913.
    NextBioi 15371.
    PROi P55268.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P55268.
    Bgeei P55268.
    CleanExi HS_LAMB2.
    Genevestigatori P55268.

    Family and domain databases

    InterProi IPR013032. EGF-like_CS.
    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. "Human beta 2 chain of laminin (formerly S chain): cDNA cloning, chromosomal localization, and expression in carcinomas."
      Wewer U.M., Gerecke D.R., Durkin M.E., Kurtz K.S., Mattei M.-G., Champliaud M.-F., Burgeson R.E., Albrechtsen R.
      Genomics 24:243-252(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
    2. "The human laminin beta 2 chain (S-laminin): structure, expression in fetal tissues and chromosomal assignment of the LAMB2 gene."
      Iivanainen A., Vuolteenaho R., Sainio K., Eddy R., Shows T.B., Sariola H., Tryggvason K.
      Matrix Biol. 14:489-497(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    3. "Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry."
      Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.
      J. Proteome Res. 8:651-661(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-1308; ASN-1348 AND ASN-1499.
      Tissue: Liver.
    4. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    5. Cited for: VARIANT PIERSS TRP-246.
    6. Cited for: VARIANTS PIERSS GLN-246; ARG-321; LYS-1380 AND PHE-1393.
    7. Cited for: VARIANT NPHS5 ARG-147.

    Entry informationi

    Entry nameiLAMB2_HUMAN
    AccessioniPrimary (citable) accession number: P55268
    Secondary accession number(s): Q16321
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1996
    Last sequence update: August 21, 2007
    Last modified: October 1, 2014
    This is version 141 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

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Human chromosome 3
      Human chromosome 3: 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