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P07942

- LAMB1_HUMAN

UniProt

P07942 - LAMB1_HUMAN

Protein

Laminin subunit beta-1

Gene

LAMB1

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 (11 Jan 2011)
      Previous versions | rss
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    Functioni

    Binding to cells via a high affinity receptor, laminin is thought to mediate the attachment, migration and organization of cells into tissues during embryonic development by interacting with other extracellular matrix components. Involved in the organization of the laminar architecture of cerebral cortex. It is probably required for the integrity of the basement membrane/glia limitans that serves as an anchor point for the endfeet of radial glial cells and as a physical barrier to migrating neurons. Radial glial cells play a central role in cerebral cortical development, where they act both as the proliferative unit of the cerebral cortex and a scaffold for neurons migrating toward the pial surface.1 Publication

    GO - Molecular functioni

    1. extracellular matrix structural constituent Source: HGNC
    2. glycosphingolipid binding Source: Ensembl
    3. structural molecule activity Source: UniProtKB

    GO - Biological processi

    1. axon guidance Source: Reactome
    2. cell adhesion Source: HGNC
    3. embryo implantation Source: Ensembl
    4. extracellular matrix disassembly Source: Reactome
    5. extracellular matrix organization Source: Reactome
    6. negative regulation of cell adhesion Source: Ensembl
    7. neuronal-glial interaction involved in cerebral cortex radial glia guided migration Source: UniProtKB
    8. neuron projection development Source: UniProtKB
    9. odontogenesis Source: UniProtKB
    10. positive regulation of cell migration Source: UniProtKB
    11. positive regulation of epithelial cell proliferation Source: HGNC
    12. substrate adhesion-dependent cell spreading Source: BHF-UCL

    Keywords - Biological processi

    Cell adhesion

    Enzyme and pathway databases

    ReactomeiREACT_118572. Degradation of the extracellular matrix.
    REACT_163874. Non-integrin membrane-ECM interactions.
    REACT_163906. ECM proteoglycans.
    REACT_169262. Laminin interactions.
    REACT_22205. L1CAM interactions.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Laminin subunit beta-1
    Alternative name(s):
    Laminin B1 chain
    Laminin-1 subunit beta
    Laminin-10 subunit beta
    Laminin-12 subunit beta
    Laminin-2 subunit beta
    Laminin-6 subunit beta
    Laminin-8 subunit beta
    Gene namesi
    Name:LAMB1
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 7

    Organism-specific databases

    HGNCiHGNC:6486. LAMB1.

    Subcellular locationi

    GO - Cellular componenti

    1. basement membrane Source: UniProtKB
    2. extracellular region Source: Reactome
    3. extracellular space Source: UniProtKB
    4. extracellular vesicular exosome Source: UniProtKB
    5. laminin-10 complex Source: UniProtKB
    6. laminin-1 complex Source: UniProtKB
    7. laminin-2 complex Source: UniProtKB
    8. laminin-8 complex Source: UniProtKB
    9. perinuclear region of cytoplasm Source: UniProtKB

    Keywords - Cellular componenti

    Basement membrane, Extracellular matrix, Secreted

    Pathology & Biotechi

    Involvement in diseasei

    Lissencephaly 5 (LIS5) [MIM:615191]: An autosomal recessive brain malformation characterized by cobblestone changes in the cortex, more severe in the posterior region, and subcortical band heterotopia. Affected individuals have hydrocephalus, seizures, and severely delayed psychomotor development.1 Publication
    Note: The disease is caused by mutations affecting the gene represented in this entry.

    Keywords - Diseasei

    Lissencephaly

    Organism-specific databases

    MIMi615191. phenotype.
    Orphaneti352682. Cobblestone lissencephaly without muscular or ocular involvement.
    PharmGKBiPA30275.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2121Add
    BLAST
    Chaini22 – 17861765Laminin subunit beta-1PRO_0000017065Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi120 – 1201N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi271 ↔ 280PROSITE-ProRule annotation
    Disulfide bondi273 ↔ 298PROSITE-ProRule annotation
    Disulfide bondi300 ↔ 309PROSITE-ProRule annotation
    Disulfide bondi312 ↔ 332PROSITE-ProRule annotation
    Disulfide bondi335 ↔ 344PROSITE-ProRule annotation
    Disulfide bondi337 ↔ 362PROSITE-ProRule annotation
    Glycosylationi356 – 3561N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi365 ↔ 374PROSITE-ProRule annotation
    Disulfide bondi377 ↔ 395PROSITE-ProRule annotation
    Disulfide bondi398 ↔ 411PROSITE-ProRule annotation
    Disulfide bondi400 ↔ 426PROSITE-ProRule annotation
    Disulfide bondi428 ↔ 437PROSITE-ProRule annotation
    Disulfide bondi440 ↔ 455PROSITE-ProRule annotation
    Disulfide bondi458 ↔ 472PROSITE-ProRule annotation
    Disulfide bondi460 ↔ 479PROSITE-ProRule annotation
    Disulfide bondi481 ↔ 490PROSITE-ProRule annotation
    Disulfide bondi493 ↔ 507PROSITE-ProRule annotation
    Disulfide bondi510 ↔ 522PROSITE-ProRule annotation
    Disulfide bondi512 ↔ 529PROSITE-ProRule annotation
    Glycosylationi519 – 5191N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi531 ↔ 540PROSITE-ProRule annotation
    Glycosylationi677 – 6771N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi773 ↔ 785PROSITE-ProRule annotation
    Disulfide bondi775 ↔ 792PROSITE-ProRule annotation
    Disulfide bondi794 ↔ 803PROSITE-ProRule annotation
    Disulfide bondi806 ↔ 818PROSITE-ProRule annotation
    Disulfide bondi821 ↔ 833PROSITE-ProRule annotation
    Disulfide bondi823 ↔ 840PROSITE-ProRule annotation
    Disulfide bondi842 ↔ 851PROSITE-ProRule annotation
    Disulfide bondi854 ↔ 864PROSITE-ProRule annotation
    Disulfide bondi867 ↔ 876PROSITE-ProRule annotation
    Disulfide bondi869 ↔ 883PROSITE-ProRule annotation
    Disulfide bondi886 ↔ 895PROSITE-ProRule annotation
    Disulfide bondi898 ↔ 914PROSITE-ProRule annotation
    Disulfide bondi917 ↔ 933PROSITE-ProRule annotation
    Disulfide bondi919 ↔ 944PROSITE-ProRule annotation
    Disulfide bondi946 ↔ 955PROSITE-ProRule annotation
    Disulfide bondi958 ↔ 973PROSITE-ProRule annotation
    Disulfide bondi976 ↔ 990PROSITE-ProRule annotation
    Disulfide bondi978 ↔ 997PROSITE-ProRule annotation
    Disulfide bondi1000 ↔ 1009PROSITE-ProRule annotation
    Disulfide bondi1012 ↔ 1025PROSITE-ProRule annotation
    Disulfide bondi1028 ↔ 1040PROSITE-ProRule annotation
    Disulfide bondi1030 ↔ 1054PROSITE-ProRule annotation
    Glycosylationi1041 – 10411N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi1056 ↔ 1065PROSITE-ProRule annotation
    Disulfide bondi1068 ↔ 1081PROSITE-ProRule annotation
    Disulfide bondi1084 ↔ 1096PROSITE-ProRule annotation
    Disulfide bondi1086 ↔ 1103PROSITE-ProRule annotation
    Disulfide bondi1105 ↔ 1114PROSITE-ProRule annotation
    Disulfide bondi1117 ↔ 1129PROSITE-ProRule annotation
    Disulfide bondi1132 ↔ 1144PROSITE-ProRule annotation
    Disulfide bondi1134 ↔ 1151PROSITE-ProRule annotation
    Disulfide bondi1153 ↔ 1162PROSITE-ProRule annotation
    Disulfide bondi1165 ↔ 1176PROSITE-ProRule annotation
    Disulfide bondi1179 – 1179InterchainCurated
    Disulfide bondi1182 – 1182InterchainCurated
    Glycosylationi1195 – 11951N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi1279 – 12791N-linked (GlcNAc...)2 Publications
    Glycosylationi1336 – 13361N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi1343 – 13431N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi1487 – 14871N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi1542 – 15421N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi1785 – 1785InterchainCurated

    Keywords - PTMi

    Disulfide bond, Glycoprotein

    Proteomic databases

    MaxQBiP07942.
    PaxDbiP07942.
    PRIDEiP07942.

    PTM databases

    PhosphoSiteiP07942.

    Expressioni

    Gene expression databases

    ArrayExpressiP07942.
    BgeeiP07942.
    CleanExiHS_LAMB1.
    GenevestigatoriP07942.

    Organism-specific databases

    HPAiCAB004256.
    HPA004056.
    HPA004132.

    Interactioni

    Subunit structurei

    Laminin is a complex glycoprotein, consisting of three different polypeptide chains (alpha, beta, gamma), which are bound to each other by disulfide bonds into a cross-shaped molecule comprising one long and three short arms with globules at each end. Beta-1 is a subunit of laminin-1 (laminin-111 or EHS laminin), laminin-2 (laminin-211 or merosin), laminin-6 (laminin-311 or K-laminin), laminin-8 (laminin-411), laminin-10 (laminin-511) and laminin-12 (laminin-213).

    Protein-protein interaction databases

    BioGridi110106. 20 interactions.
    IntActiP07942. 10 interactions.
    MINTiMINT-2860329.
    STRINGi9606.ENSP00000222399.

    Structurei

    3D structure databases

    ProteinModelPortaliP07942.
    SMRiP07942. Positions 29-492.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

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

    Region

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

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili1216 – 1315100Sequence AnalysisAdd
    BLAST
    Coiled coili1353 – 138836Sequence AnalysisAdd
    BLAST
    Coiled coili1442 – 1781340Sequence 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.
    KOiK05636.
    PhylomeDBiP07942.
    TreeFamiTF312903.

    Family and domain databases

    InterProiIPR002049. EGF_laminin.
    IPR013015. Laminin_IV.
    IPR008211. Laminin_N.
    IPR009053. Prefoldin.
    [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]
    SUPFAMiSSF46579. SSF46579. 1 hit.
    PROSITEiPS00022. EGF_1. 9 hits.
    PS01186. EGF_2. 2 hits.
    PS01248. EGF_LAM_1. 11 hits.
    PS50027. EGF_LAM_2. 13 hits.
    PS51116. LAMININ_IVB. 1 hit.
    PS51117. LAMININ_NTER. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    P07942-1 [UniParc]FASTAAdd to Basket

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    MGLLQLLAFS FLALCRARVR AQEPEFSYGC AEGSCYPATG DLLIGRAQKL     50
    SVTSTCGLHK PEPYCIVSHL QEDKKCFICN SQDPYHETLN PDSHLIENVV 100
    TTFAPNRLKI WWQSENGVEN VTIQLDLEAE FHFTHLIMTF KTFRPAAMLI 150
    ERSSDFGKTW GVYRYFAYDC EASFPGISTG PMKKVDDIIC DSRYSDIEPS 200
    TEGEVIFRAL DPAFKIEDPY SPRIQNLLKI TNLRIKFVKL HTLGDNLLDS 250
    RMEIREKYYY AVYDMVVRGN CFCYGHASEC APVDGFNEEV EGMVHGHCMC 300
    RHNTKGLNCE LCMDFYHDLP WRPAEGRNSN ACKKCNCNEH SISCHFDMAV 350
    YLATGNVSGG VCDDCQHNTM GRNCEQCKPF YYQHPERDIR DPNFCERCTC 400
    DPAGSQNEGI CDSYTDFSTG LIAGQCRCKL NVEGEHCDVC KEGFYDLSSE 450
    DPFGCKSCAC NPLGTIPGGN PCDSETGHCY CKRLVTGQHC DQCLPEHWGL 500
    SNDLDGCRPC DCDLGGALNN SCFAESGQCS CRPHMIGRQC NEVEPGYYFA 550
    TLDHYLYEAE EANLGPGVSI VERQYIQDRI PSWTGAGFVR VPEGAYLEFF 600
    IDNIPYSMEY DILIRYEPQL PDHWEKAVIT VQRPGRIPTS SRCGNTIPDD 650
    DNQVVSLSPG SRYVVLPRPV CFEKGTNYTV RLELPQYTSS DSDVESPYTL 700
    IDSLVLMPYC KSLDIFTVGG SGDGVVTNSA WETFQRYRCL ENSRSVVKTP 750
    MTDVCRNIIF SISALLHQTG LACECDPQGS LSSVCDPNGG QCQCRPNVVG 800
    RTCNRCAPGT FGFGPSGCKP CECHLQGSVN AFCNPVTGQC HCFQGVYARQ 850
    CDRCLPGHWG FPSCQPCQCN GHADDCDPVT GECLNCQDYT MGHNCERCLA 900
    GYYGDPIIGS GDHCRPCPCP DGPDSGRQFA RSCYQDPVTL QLACVCDPGY 950
    IGSRCDDCAS GYFGNPSEVG GSCQPCQCHN NIDTTDPEAC DKETGRCLKC 1000
    LYHTEGEHCQ FCRFGYYGDA LQQDCRKCVC NYLGTVQEHC NGSDCQCDKA 1050
    TGQCLCLPNV IGQNCDRCAP NTWQLASGTG CDPCNCNAAH SFGPSCNEFT 1100
    GQCQCMPGFG GRTCSECQEL FWGDPDVECR ACDCDPRGIE TPQCDQSTGQ 1150
    CVCVEGVEGP RCDKCTRGYS GVFPDCTPCH QCFALWDVII AELTNRTHRF 1200
    LEKAKALKIS GVIGPYRETV DSVERKVSEI KDILAQSPAA EPLKNIGNLF 1250
    EEAEKLIKDV TEMMAQVEVK LSDTTSQSNS TAKELDSLQT EAESLDNTVK 1300
    ELAEQLEFIK NSDIRGALDS ITKYFQMSLE AEERVNASTT EPNSTVEQSA 1350
    LMRDRVEDVM MERESQFKEK QEEQARLLDE LAGKLQSLDL SAAAEMTCGT 1400
    PPGASCSETE CGGPNCRTDE GERKCGGPGC GGLVTVAHNA WQKAMDLDQD 1450
    VLSALAEVEQ LSKMVSEAKL RADEAKQSAE DILLKTNATK EKMDKSNEEL 1500
    RNLIKQIRNF LTQDSADLDS IEAVANEVLK MEMPSTPQQL QNLTEDIRER 1550
    VESLSQVEVI LQHSAADIAR AEMLLEEAKR ASKSATDVKV TADMVKEALE 1600
    EAEKAQVAAE KAIKQADEDI QGTQNLLTSI ESETAASEET LFNASQRISE 1650
    LERNVEELKR KAAQNSGEAE YIEKVVYTVK QSAEDVKKTL DGELDEKYKK 1700
    VENLIAKKTE ESADARRKAE MLQNEAKTLL AQANSKLQLL KDLERKYEDN 1750
    QRYLEDKAQE LARLEGEVRS LLKDISQKVA VYSTCL 1786
    Length:1,786
    Mass (Da):198,038
    Last modified:January 11, 2011 - v2
    Checksum:i8F8EF96E765B9A0D
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti1470 – 14701L → V in AAA59487. (PubMed:3661559)Curated
    Sequence conflicti1696 – 16961E → G in AAA59487. (PubMed:3661559)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti379 – 3791P → S.
    Corresponds to variant rs28750165 [ dbSNP | Ensembl ].
    VAR_061349
    Natural varianti670 – 6701V → A.
    Corresponds to variant rs20555 [ dbSNP | Ensembl ].
    VAR_014698
    Natural varianti860 – 8601G → S.
    Corresponds to variant rs35710474 [ dbSNP | Ensembl ].
    VAR_032774
    Natural varianti1022 – 10221Q → R.3 Publications
    Corresponds to variant rs20556 [ dbSNP | Ensembl ].
    VAR_014699

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M61951
    , M58147, M61917, M61918, M61921, M61922, M61923, M61924, M61925, M61926, M61927, M61928, M61929, M61930, M61931, M61932, M61933, M61934, M61935, M61936, M61938, M61939, M61940, M61941, M61942, M61943, M61944, M61945, M61946, M61947, M61948, M61949, M61950 Genomic DNA. Translation: AAA59486.1.
    M55370
    , M55378, M55365, M55371, M55372, M55373, M55374, M55375, M55376, M55344, M55345, M55346, M55347, M55348, M55349, M55350, M55351, M55352, M55353, M55355, M55356, M55357, M55358, M55359, M55360, M55361, M55362, M55363, M55364, M55366, M55367, M55368, M55369 Genomic DNA. Translation: AAA59485.1.
    M61916 mRNA. Translation: AAA59482.1.
    CH236947 Genomic DNA. Translation: EAL24388.1.
    BC113455 mRNA. Translation: AAI13456.1.
    M20206 mRNA. Translation: AAA59487.1.
    CCDSiCCDS5750.1.
    PIRiS13547. MMHUB1.
    RefSeqiNP_002282.2. NM_002291.2.
    UniGeneiHs.650585.

    Genome annotation databases

    EnsembliENST00000222399; ENSP00000222399; ENSG00000091136.
    GeneIDi3912.
    KEGGihsa:3912.
    UCSCiuc003vew.2. human.

    Polymorphism databases

    DMDMi317373377.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M61951
    , M58147 , M61917 , M61918 , M61921 , M61922 , M61923 , M61924 , M61925 , M61926 , M61927 , M61928 , M61929 , M61930 , M61931 , M61932 , M61933 , M61934 , M61935 , M61936 , M61938 , M61939 , M61940 , M61941 , M61942 , M61943 , M61944 , M61945 , M61946 , M61947 , M61948 , M61949 , M61950 Genomic DNA. Translation: AAA59486.1 .
    M55370
    , M55378 , M55365 , M55371 , M55372 , M55373 , M55374 , M55375 , M55376 , M55344 , M55345 , M55346 , M55347 , M55348 , M55349 , M55350 , M55351 , M55352 , M55353 , M55355 , M55356 , M55357 , M55358 , M55359 , M55360 , M55361 , M55362 , M55363 , M55364 , M55366 , M55367 , M55368 , M55369 Genomic DNA. Translation: AAA59485.1 .
    M61916 mRNA. Translation: AAA59482.1 .
    CH236947 Genomic DNA. Translation: EAL24388.1 .
    BC113455 mRNA. Translation: AAI13456.1 .
    M20206 mRNA. Translation: AAA59487.1 .
    CCDSi CCDS5750.1.
    PIRi S13547. MMHUB1.
    RefSeqi NP_002282.2. NM_002291.2.
    UniGenei Hs.650585.

    3D structure databases

    ProteinModelPortali P07942.
    SMRi P07942. Positions 29-492.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 110106. 20 interactions.
    IntActi P07942. 10 interactions.
    MINTi MINT-2860329.
    STRINGi 9606.ENSP00000222399.

    Chemistry

    ChEMBLi CHEMBL2364187.
    DrugBanki DB00009. Alteplase.
    DB00029. Anistreplase.
    DB00015. Reteplase.
    DB00031. Tenecteplase.

    PTM databases

    PhosphoSitei P07942.

    Polymorphism databases

    DMDMi 317373377.

    Proteomic databases

    MaxQBi P07942.
    PaxDbi P07942.
    PRIDEi P07942.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000222399 ; ENSP00000222399 ; ENSG00000091136 .
    GeneIDi 3912.
    KEGGi hsa:3912.
    UCSCi uc003vew.2. human.

    Organism-specific databases

    CTDi 3912.
    GeneCardsi GC07M107564.
    H-InvDB HIX0025323.
    HGNCi HGNC:6486. LAMB1.
    HPAi CAB004256.
    HPA004056.
    HPA004132.
    MIMi 150240. gene.
    615191. phenotype.
    neXtProti NX_P07942.
    Orphaneti 352682. Cobblestone lissencephaly without muscular or ocular involvement.
    PharmGKBi PA30275.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG241384.
    HOGENOMi HOG000007552.
    HOVERGENi HBG052301.
    KOi K05636.
    PhylomeDBi P07942.
    TreeFami TF312903.

    Enzyme and pathway databases

    Reactomei REACT_118572. Degradation of the extracellular matrix.
    REACT_163874. Non-integrin membrane-ECM interactions.
    REACT_163906. ECM proteoglycans.
    REACT_169262. Laminin interactions.
    REACT_22205. L1CAM interactions.

    Miscellaneous databases

    ChiTaRSi LAMB1. human.
    GeneWikii Laminin,_beta_1.
    GenomeRNAii 3912.
    NextBioi 15367.
    PROi P07942.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P07942.
    Bgeei P07942.
    CleanExi HS_LAMB1.
    Genevestigatori P07942.

    Family and domain databases

    InterProi IPR002049. EGF_laminin.
    IPR013015. Laminin_IV.
    IPR008211. Laminin_N.
    IPR009053. Prefoldin.
    [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 ]
    SUPFAMi SSF46579. SSF46579. 1 hit.
    PROSITEi PS00022. EGF_1. 9 hits.
    PS01186. EGF_2. 2 hits.
    PS01248. EGF_LAM_1. 11 hits.
    PS50027. EGF_LAM_2. 13 hits.
    PS51116. LAMININ_IVB. 1 hit.
    PS51117. LAMININ_NTER. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Structure of the human laminin B1 chain gene."
      Vuolteenaho R., Chow L.T., Tryggvason K.
      J. Biol. Chem. 265:15611-15616(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT ARG-1022.
    2. "Human laminin B1 chain. A multidomain protein with gene (LAMB1) locus in the q22 region of chromosome 7."
      Pikkarainen T., Eddy R., Fukushima Y., Byers M., Shows T., Pihlajaniemi T., Saraste M., Tryggvason K.
      J. Biol. Chem. 262:10454-10462(1987) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT ARG-1022.
    3. "Human chromosome 7: DNA sequence and biology."
      Scherer S.W., Cheung J., MacDonald J.R., Osborne L.R., Nakabayashi K., Herbrick J.-A., Carson A.R., Parker-Katiraee L., Skaug J., Khaja R., Zhang J., Hudek A.K., Li M., Haddad M., Duggan G.E., Fernandez B.A., Kanematsu E., Gentles S.
      , Christopoulos C.C., Choufani S., Kwasnicka D., Zheng X.H., Lai Z., Nusskern D.R., Zhang Q., Gu Z., Lu F., Zeesman S., Nowaczyk M.J., Teshima I., Chitayat D., Shuman C., Weksberg R., Zackai E.H., Grebe T.A., Cox S.R., Kirkpatrick S.J., Rahman N., Friedman J.M., Heng H.H.Q., Pelicci P.G., Lo-Coco F., Belloni E., Shaffer L.G., Pober B., Morton C.C., Gusella J.F., Bruns G.A.P., Korf B.R., Quade B.J., Ligon A.H., Ferguson H., Higgins A.W., Leach N.T., Herrick S.R., Lemyre E., Farra C.G., Kim H.-G., Summers A.M., Gripp K.W., Roberts W., Szatmari P., Winsor E.J.T., Grzeschik K.-H., Teebi A., Minassian B.A., Kere J., Armengol L., Pujana M.A., Estivill X., Wilson M.D., Koop B.F., Tosi S., Moore G.E., Boright A.P., Zlotorynski E., Kerem B., Kroisel P.M., Petek E., Oscier D.G., Mould S.J., Doehner H., Doehner K., Rommens J.M., Vincent J.B., Venter J.C., Li P.W., Mural R.J., Adams M.D., Tsui L.-C.
      Science 300:767-772(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    4. "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: Colon.
    5. "Isolation of a cDNA clone for the human laminin-B1 chain and its gene localization."
      Jaye M., Modi W.S., Ricca G.A., Mudd R., Chiu I.M., O'Brien S.J., Drohan W.N.
      Am. J. Hum. Genet. 41:605-615(1987) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1276-1709.
    6. "Human plasma N-glycoproteome analysis by immunoaffinity subtraction, hydrazide chemistry, and mass spectrometry."
      Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E., Moore R.J., Smith R.D.
      J. Proteome Res. 4:2070-2080(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-1279.
      Tissue: Plasma.
    7. "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-1279.
      Tissue: Liver.
    8. Cited for: INVOLVEMENT IN LIS5, FUNCTION.
    9. Cited for: VARIANT [LARGE SCALE ANALYSIS] ARG-1022, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiLAMB1_HUMAN
    AccessioniPrimary (citable) accession number: P07942
    Secondary accession number(s): Q14D91
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 1, 1988
    Last sequence update: January 11, 2011
    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

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Human chromosome 7
      Human chromosome 7: 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