Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

P24043

- LAMA2_HUMAN

UniProt

P24043 - LAMA2_HUMAN

Protein

Laminin subunit alpha-2

Gene

LAMA2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 159 (01 Oct 2014)
      Sequence version 4 (25 Nov 2008)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    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. axon guidance Source: Ensembl
    2. cell adhesion Source: UniProtKB-KW
    3. extracellular matrix organization Source: Reactome
    4. muscle organ development Source: ProtInc
    5. myelination in peripheral nervous system Source: Ensembl
    6. positive regulation of synaptic transmission, cholinergic Source: Ensembl
    7. regulation of cell adhesion Source: InterPro
    8. regulation of cell migration Source: InterPro
    9. regulation of embryonic development Source: InterPro

    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 alpha-2
    Alternative name(s):
    Laminin M chain
    Laminin-12 subunit alpha
    Laminin-2 subunit alpha
    Laminin-4 subunit alpha
    Merosin heavy chain
    Gene namesi
    Name:LAMA2
    Synonyms:LAMM
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 6

    Organism-specific databases

    HGNCiHGNC:6482. LAMA2.

    Subcellular locationi

    GO - Cellular componenti

    1. basement membrane Source: UniProtKB
    2. dendritic spine Source: Ensembl
    3. extracellular region Source: Reactome
    4. extracellular vesicular exosome Source: UniProt
    5. laminin-1 complex Source: InterPro
    6. sarcolemma Source: Ensembl

    Keywords - Cellular componenti

    Basement membrane, Extracellular matrix, Secreted

    Pathology & Biotechi

    Involvement in diseasei

    Merosin-deficient congenital muscular dystrophy 1A (MDC1A) [MIM:607855]: Characterized by difficulty walking, hypotonia, proximal weakness, hyporeflexia, and white matter hypodensity on MRI.2 Publications
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti527 – 5271C → Y in MDC1A. 1 Publication
    VAR_015743
    Natural varianti862 – 8621C → R in MDC1A. 1 Publication
    VAR_015744
    Natural varianti2564 – 25641L → P in MDC1A. 1 Publication
    VAR_015745

    Keywords - Diseasei

    Congenital muscular dystrophy, Disease mutation

    Organism-specific databases

    MIMi607855. phenotype.
    Orphaneti258. Congenital muscular dystrophy type 1A.
    PharmGKBiPA30271.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2222Sequence AnalysisAdd
    BLAST
    Chaini23 – 31223100Laminin subunit alpha-2PRO_0000017056Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi55 – 551N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi89 – 891N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi287 ↔ 296By similarity
    Disulfide bondi289 ↔ 307By similarity
    Glycosylationi303 – 3031N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi309 ↔ 318By similarity
    Disulfide bondi321 ↔ 341By similarity
    Disulfide bondi344 ↔ 353By similarity
    Disulfide bondi346 ↔ 378By similarity
    Glycosylationi363 – 3631N-linked (GlcNAc...)1 Publication
    Glycosylationi380 – 3801N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi381 ↔ 390By similarity
    Disulfide bondi393 ↔ 411By similarity
    Disulfide bondi414 ↔ 426By similarity
    Disulfide bondi416 ↔ 442By similarity
    Disulfide bondi444 ↔ 453By similarity
    Disulfide bondi456 ↔ 466By similarity
    Disulfide bondi469 ↔ 482By similarity
    Glycosylationi470 – 4701N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi471 ↔ 486By similarity
    Disulfide bondi488 ↔ 497By similarity
    Disulfide bondi500 ↔ 515By similarity
    Glycosylationi746 – 7461N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi757 ↔ 766By similarity
    Disulfide bondi759 ↔ 773By similarity
    Disulfide bondi776 ↔ 785By similarity
    Disulfide bondi788 ↔ 804By similarity
    Disulfide bondi807 ↔ 822By similarity
    Disulfide bondi809 ↔ 832By similarity
    Disulfide bondi835 ↔ 844By similarity
    Disulfide bondi847 ↔ 862By similarity
    Disulfide bondi865 ↔ 879By similarity
    Disulfide bondi867 ↔ 886By similarity
    Disulfide bondi889 ↔ 898By similarity
    Disulfide bondi901 ↔ 915By similarity
    Disulfide bondi918 ↔ 930By similarity
    Disulfide bondi920 ↔ 937By similarity
    Disulfide bondi939 ↔ 948By similarity
    Disulfide bondi951 ↔ 964By similarity
    Disulfide bondi967 ↔ 979By similarity
    Disulfide bondi969 ↔ 985By similarity
    Disulfide bondi987 ↔ 996By similarity
    Disulfide bondi999 ↔ 1011By similarity
    Disulfide bondi1014 ↔ 1023By similarity
    Disulfide bondi1016 ↔ 1030By similarity
    Disulfide bondi1032 ↔ 1041By similarity
    Disulfide bondi1044 ↔ 1057By similarity
    Disulfide bondi1060 ↔ 1072By similarity
    Glycosylationi1061 – 10611N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi1062 ↔ 1079By similarity
    Disulfide bondi1081 ↔ 1090By similarity
    Disulfide bondi1093 ↔ 1103By similarity
    Disulfide bondi1106 ↔ 1118By similarity
    Disulfide bondi1108 ↔ 1134By similarity
    Disulfide bondi1136 ↔ 1145By similarity
    Disulfide bondi1148 ↔ 1163By similarity
    Disulfide bondi1420 ↔ 1429By similarity
    Disulfide bondi1422 ↔ 1436By similarity
    Disulfide bondi1439 ↔ 1448By similarity
    Disulfide bondi1451 ↔ 1466By similarity
    Disulfide bondi1469 ↔ 1484By similarity
    Disulfide bondi1471 ↔ 1494By similarity
    Disulfide bondi1497 ↔ 1506By similarity
    Disulfide bondi1509 ↔ 1524By similarity
    Disulfide bondi1527 ↔ 1539By similarity
    Disulfide bondi1529 ↔ 1546By similarity
    Disulfide bondi1548 ↔ 1557By similarity
    Disulfide bondi1560 ↔ 1571By similarity
    Disulfide bondi1574 – 1574InterchainCurated
    Disulfide bondi1578 – 1578InterchainCurated
    Glycosylationi1597 – 15971N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi1614 – 16141N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi1700 – 17001N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi1810 – 18101N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi1901 – 19011N-linked (GlcNAc...)1 Publication
    Glycosylationi1916 – 19161N-linked (GlcNAc...)1 Publication
    Glycosylationi1920 – 19201N-linked (GlcNAc...)1 Publication
    Glycosylationi2017 – 20171N-linked (GlcNAc...)1 Publication
    Glycosylationi2028 – 20281N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi2045 – 20451N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi2126 – 21261N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi2240 – 22401N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi2302 ↔ 2328By similarity
    Glycosylationi2360 – 23601N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi2435 – 24351N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi2478 – 24781N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi2495 ↔ 2521By similarity
    Glycosylationi2551 – 25511N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi2558 – 25581N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi2648 – 26481N-linked (GlcNAc...)1 Publication
    Disulfide bondi2683 ↔ 2710By similarity
    Glycosylationi2868 – 28681N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi2893 – 28931N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi2909 ↔ 2934By similarity

    Keywords - PTMi

    Disulfide bond, Glycoprotein

    Proteomic databases

    PaxDbiP24043.
    PRIDEiP24043.

    PTM databases

    PhosphoSiteiP24043.

    Expressioni

    Tissue specificityi

    Placenta, striated muscle, peripheral nerve, cardiac muscle, pancreas, lung, spleen, kidney, adrenal gland, skin, testis, meninges, choroid plexus, and some other regions of the brain; not in liver, thymus and bone.

    Gene expression databases

    ArrayExpressiP24043.
    BgeeiP24043.
    CleanExiHS_LAMA2.
    GenevestigatoriP24043.

    Organism-specific databases

    HPAiCAB040310.

    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. Alpha-2 is a subunit of laminin-2 (laminin-211 or merosin), laminin-4 (laminin-221 or S-merosin) and laminin-12 (laminin-213). Interacts with FBLN1, FBLN2 and NID2.

    Protein-protein interaction databases

    BioGridi110102. 3 interactions.
    DIPiDIP-42562N.
    IntActiP24043. 4 interactions.
    MINTiMINT-2635209.
    STRINGi9606.ENSP00000400365.

    Structurei

    3D structure databases

    ProteinModelPortaliP24043.
    SMRiP24043. Positions 2939-3120.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini35 – 286252Laminin N-terminalPROSITE-ProRule annotationAdd
    BLAST
    Domaini287 – 34357Laminin EGF-like 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini344 – 41370Laminin EGF-like 2PROSITE-ProRule annotationAdd
    BLAST
    Domaini414 – 46855Laminin EGF-like 3PROSITE-ProRule annotationAdd
    BLAST
    Domaini469 – 51749Laminin EGF-like 4PROSITE-ProRule annotationAdd
    BLAST
    Domaini518 – 52710Laminin EGF-like 5; first partPROSITE-ProRule annotation
    Domaini531 – 723193Laminin IV type A 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini724 – 75633Laminin EGF-like 5; second partPROSITE-ProRule annotationAdd
    BLAST
    Domaini757 – 80650Laminin EGF-like 6PROSITE-ProRule annotationAdd
    BLAST
    Domaini807 – 86458Laminin EGF-like 7PROSITE-ProRule annotationAdd
    BLAST
    Domaini865 – 91753Laminin EGF-like 8PROSITE-ProRule annotationAdd
    BLAST
    Domaini918 – 96649Laminin EGF-like 9PROSITE-ProRule annotationAdd
    BLAST
    Domaini967 – 101347Laminin EGF-like 10PROSITE-ProRule annotationAdd
    BLAST
    Domaini1014 – 105946Laminin EGF-like 11PROSITE-ProRule annotationAdd
    BLAST
    Domaini1060 – 110546Laminin EGF-like 12PROSITE-ProRule annotationAdd
    BLAST
    Domaini1106 – 116560Laminin EGF-like 13PROSITE-ProRule annotationAdd
    BLAST
    Domaini1166 – 117510Laminin EGF-like 14; first partPROSITE-ProRule annotation
    Domaini1176 – 1379204Laminin IV type A 2PROSITE-ProRule annotationAdd
    BLAST
    Domaini1380 – 141940Laminin EGF-like 14; second partPROSITE-ProRule annotationAdd
    BLAST
    Domaini1420 – 146849Laminin EGF-like 15PROSITE-ProRule annotationAdd
    BLAST
    Domaini1469 – 152658Laminin EGF-like 16PROSITE-ProRule annotationAdd
    BLAST
    Domaini1527 – 157347Laminin EGF-like 17PROSITE-ProRule annotationAdd
    BLAST
    Domaini2145 – 2328184Laminin G-like 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini2340 – 2521182Laminin G-like 2PROSITE-ProRule annotationAdd
    BLAST
    Domaini2526 – 2710185Laminin G-like 3PROSITE-ProRule annotationAdd
    BLAST
    Domaini2763 – 2934172Laminin G-like 4PROSITE-ProRule annotationAdd
    BLAST
    Domaini2939 – 3110172Laminin G-like 5PROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni1574 – 2144571Domain II and IAdd
    BLAST

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili1630 – 2150521Sequence 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, IV and G are globular.

    Sequence similaritiesi

    Contains 17 laminin EGF-like domains.PROSITE-ProRule annotation
    Contains 5 laminin G-like domains.PROSITE-ProRule annotation
    Contains 2 laminin IV type A 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

    eggNOGiCOG0419.
    HOGENOMiHOG000293201.
    HOVERGENiHBG052298.
    KOiK05637.
    OMAiHTTTKGI.
    OrthoDBiEOG7SR4KJ.
    PhylomeDBiP24043.
    TreeFamiTF335359.

    Family and domain databases

    Gene3Di2.60.120.200. 5 hits.
    2.60.120.260. 2 hits.
    InterProiIPR008985. ConA-like_lec_gl_sf.
    IPR013320. ConA-like_subgrp.
    IPR002049. EGF_laminin.
    IPR008979. Galactose-bd-like.
    IPR018031. Laminin_B_subgr.
    IPR000034. Laminin_B_type_IV.
    IPR001791. Laminin_G.
    IPR009254. Laminin_I.
    IPR010307. Laminin_II.
    IPR008211. Laminin_N.
    [Graphical view]
    PfamiPF00052. Laminin_B. 2 hits.
    PF00053. Laminin_EGF. 16 hits.
    PF00054. Laminin_G_1. 4 hits.
    PF02210. Laminin_G_2. 1 hit.
    PF06008. Laminin_I. 1 hit.
    PF06009. Laminin_II. 1 hit.
    PF00055. Laminin_N. 1 hit.
    [Graphical view]
    SMARTiSM00180. EGF_Lam. 15 hits.
    SM00281. LamB. 2 hits.
    SM00282. LamG. 5 hits.
    SM00136. LamNT. 1 hit.
    [Graphical view]
    SUPFAMiSSF49785. SSF49785. 1 hit.
    SSF49899. SSF49899. 5 hits.
    PROSITEiPS00022. EGF_1. 11 hits.
    PS01186. EGF_2. 3 hits.
    PS01248. EGF_LAM_1. 14 hits.
    PS50027. EGF_LAM_2. 15 hits.
    PS50025. LAM_G_DOMAIN. 5 hits.
    PS51115. LAMININ_IVA. 2 hits.
    PS51117. LAMININ_NTER. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    P24043-1 [UniParc]FASTAAdd to Basket

    « Hide

    MPGAAGVLLL LLLSGGLGGV QAQRPQQQRQ SQAHQQRGLF PAVLNLASNA     50
    LITTNATCGE KGPEMYCKLV EHVPGQPVRN PQCRICNQNS SNPNQRHPIT 100
    NAIDGKNTWW QSPSIKNGIE YHYVTITLDL QQVFQIAYVI VKAANSPRPG 150
    NWILERSLDD VEYKPWQYHA VTDTECLTLY NIYPRTGPPS YAKDDEVICT 200
    SFYSKIHPLE NGEIHISLIN GRPSADDPSP ELLEFTSARY IRLRFQRIRT 250
    LNADLMMFAH KDPREIDPIV TRRYYYSVKD ISVGGMCICY GHARACPLDP 300
    ATNKSRCECE HNTCGDSCDQ CCPGFHQKPW RAGTFLTKTE CEACNCHGKA 350
    EECYYDENVA RRNLSLNIRG KYIGGGVCIN CTQNTAGINC ETCTDGFFRP 400
    KGVSPNYPRP CQPCHCDPIG SLNEVCVKDE KHARRGLAPG SCHCKTGFGG 450
    VSCDRCARGY TGYPDCKACN CSGLGSKNED PCFGPCICKE NVEGGDCSRC 500
    KSGFFNLQED NWKGCDECFC SGVSNRCQSS YWTYGKIQDM SGWYLTDLPG 550
    RIRVAPQQDD LDSPQQISIS NAEARQALPH SYYWSAPAPY LGNKLPAVGG 600
    QLTFTISYDL EEEEEDTERV LQLMIILEGN DLSISTAQDE VYLHPSEEHT 650
    NVLLLKEESF TIHGTHFPVR RKEFMTVLAN LKRVLLQITY SFGMDAIFRL 700
    SSVNLESAVS YPTDGSIAAA VEVCQCPPGY TGSSCESCWP RHRRVNGTIF 750
    GGICEPCQCF GHAESCDDVT GECLNCKDHT GGPYCDKCLP GFYGEPTKGT 800
    SEDCQPCACP LNIPSNNFSP TCHLDRSLGL ICDGCPVGYT GPRCERCAEG 850
    YFGQPSVPGG SCQPCQCNDN LDFSIPGSCD SLSGSCLICK PGTTGRYCEL 900
    CADGYFGDAV DAKNCQPCRC NAGGSFSEVC HSQTGQCECR ANVQGQRCDK 950
    CKAGTFGLQS ARGCVPCNCN SFGSKSFDCE ESGQCWCQPG VTGKKCDRCA 1000
    HGYFNFQEGG CTACECSHLG NNCDPKTGRC ICPPNTIGEK CSKCAPNTWG 1050
    HSITTGCKAC NCSTVGSLDF QCNVNTGQCN CHPKFSGAKC TECSRGHWNY 1100
    PRCNLCDCFL PGTDATTCDS ETKKCSCSDQ TGQCTCKVNV EGIHCDRCRP 1150
    GKFGLDAKNP LGCSSCYCFG TTTQCSEAKG LIRTWVTLKA EQTILPLVDE 1200
    ALQHTTTKGI VFQHPEIVAH MDLMREDLHL EPFYWKLPEQ FEGKKLMAYG 1250
    GKLKYAIYFE AREETGFSTY NPQVIIRGGT PTHARIIVRH MAAPLIGQLT 1300
    RHEIEMTEKE WKYYGDDPRV HRTVTREDFL DILYDIHYIL IKATYGNFMR 1350
    QSRISEISME VAEQGRGTTM TPPADLIEKC DCPLGYSGLS CEACLPGFYR 1400
    LRSQPGGRTP GPTLGTCVPC QCNGHSSLCD PETSICQNCQ HHTAGDFCER 1450
    CALGYYGIVK GLPNDCQQCA CPLISSSNNF SPSCVAEGLD DYRCTACPRG 1500
    YEGQYCERCA PGYTGSPGNP GGSCQECECD PYGSLPVPCD PVTGFCTCRP 1550
    GATGRKCDGC KHWHAREGWE CVFCGDECTG LLLGDLARLE QMVMSINLTG 1600
    PLPAPYKMLY GLENMTQELK HLLSPQRAPE RLIQLAEGNL NTLVTEMNEL 1650
    LTRATKVTAD GEQTGQDAER TNTRAKSLGE FIKELARDAE AVNEKAIKLN 1700
    ETLGTRDEAF ERNLEGLQKE IDQMIKELRR KNLETQKEIA EDELVAAEAL 1750
    LKKVKKLFGE SRGENEEMEK DLREKLADYK NKVDDAWDLL REATDKIREA 1800
    NRLFAVNQKN MTALEKKKEA VESGKRQIEN TLKEGNDILD EANRLADEIN 1850
    SIIDYVEDIQ TKLPPMSEEL NDKIDDLSQE IKDRKLAEKV SQAESHAAQL 1900
    NDSSAVLDGI LDEAKNISFN ATAAFKAYSN IKDYIDEAEK VAKEAKDLAH 1950
    EATKLATGPR GLLKEDAKGC LQKSFRILNE AKKLANDVKE NEDHLNGLKT 2000
    RIENADARNG DLLRTLNDTL GKLSAIPNDT AAKLQAVKDK ARQANDTAKD 2050
    VLAQITELHQ NLDGLKKNYN KLADSVAKTN AVVKDPSKNK IIADADATVK 2100
    NLEQEADRLI DKLKPIKELE DNLKKNISEI KELINQARKQ ANSIKVSVSS 2150
    GGDCIRTYKP EIKKGSYNNI VVNVKTAVAD NLLFYLGSAK FIDFLAIEMR 2200
    KGKVSFLWDV GSGVGRVEYP DLTIDDSYWY RIVASRTGRN GTISVRALDG 2250
    PKASIVPSTH HSTSPPGYTI LDVDANAMLF VGGLTGKLKK ADAVRVITFT 2300
    GCMGETYFDN KPIGLWNFRE KEGDCKGCTV SPQVEDSEGT IQFDGEGYAL 2350
    VSRPIRWYPN ISTVMFKFRT FSSSALLMYL ATRDLRDFMS VELTDGHIKV 2400
    SYDLGSGMAS VVSNQNHNDG KWKSFTLSRI QKQANISIVD IDTNQEENIA 2450
    TSSSGNNFGL DLKADDKIYF GGLPTLRNLS MKARPEVNLK KYSGCLKDIE 2500
    ISRTPYNILS SPDYVGVTKG CSLENVYTVS FPKPGFVELS PVPIDVGTEI 2550
    NLSFSTKNES GIILLGSGGT PAPPRRKRRQ TGQAYYAILL NRGRLEVHLS 2600
    TGARTMRKIV IRPEPNLFHD GREHSVHVER TRGIFTVQVD ENRRYMQNLT 2650
    VEQPIEVKKL FVGGAPPEFQ PSPLRNIPPF EGCIWNLVIN SVPMDFARPV 2700
    SFKNADIGRC AHQKLREDED GAAPAEIVIQ PEPVPTPAFP TPTPVLTHGP 2750
    CAAESEPALL IGSKQFGLSR NSHIAIAFDD TKVKNRLTIE LEVRTEAESG 2800
    LLFYMARINH ADFATVQLRN GLPYFSYDLG SGDTHTMIPT KINDGQWHKI 2850
    KIMRSKQEGI LYVDGASNRT ISPKKADILD VVGMLYVGGL PINYTTRRIG 2900
    PVTYSIDGCV RNLHMAEAPA DLEQPTSSFH VGTCFANAQR GTYFDGTGFA 2950
    KAVGGFKVGL DLLVEFEFRT TTTTGVLLGI SSQKMDGMGI EMIDEKLMFH 3000
    VDNGAGRFTA VYDAGVPGHL CDGQWHKVTA NKIKHRIELT VDGNQVEAQS 3050
    PNPASTSADT NDPVFVGGFP DDLKQFGLTT SIPFRGCIRS LKLTKGTGKP 3100
    LEVNFAKALE LRGVQPVSCP AN 3122
    Length:3,122
    Mass (Da):343,905
    Last modified:November 25, 2008 - v4
    Checksum:iE2C13BD6FC1B7BAC
    GO

    Sequence cautioni

    The sequence AAA63215.1 differs from that shown. Reason: Frameshift at position 3098.
    The sequence CAA81394.1 differs from that shown. Reason: Frameshift at position 3098.
    The sequence AAB18388.1 differs from that shown. Reason: Erroneous gene model prediction.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti588 – 5881A → R in AAB18388. (PubMed:8910357)Curated
    Sequence conflicti1740 – 17401A → D(PubMed:7535762)Curated
    Sequence conflicti1827 – 18271Q → G(PubMed:7535762)Curated
    Sequence conflicti1981 – 19811A → V in AAA63215. (PubMed:2185464)Curated
    Sequence conflicti2437 – 24371S → Y in AAB18388. (PubMed:8910357)Curated
    Sequence conflicti2624 – 26241H → R in AAA63215. (PubMed:2185464)Curated
    Sequence conflicti2807 – 28071R → A in CAA81394. (PubMed:8294519)Curated
    Sequence conflicti2807 – 28071R → A in AAB18388. (PubMed:8910357)Curated
    Sequence conflicti2969 – 29691R → A in CAA81394. (PubMed:8294519)Curated
    Sequence conflicti2969 – 29691R → A in AAB18388. (PubMed:8910357)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti96 – 961R → S.
    Corresponds to variant rs34626728 [ dbSNP | Ensembl ].
    VAR_047713
    Natural varianti240 – 2401Y → H.
    Corresponds to variant rs3778142 [ dbSNP | Ensembl ].
    VAR_047714
    Natural varianti527 – 5271C → Y in MDC1A. 1 Publication
    VAR_015743
    Natural varianti545 – 5451L → Q.1 Publication
    Corresponds to variant rs118083923 [ dbSNP | Ensembl ].
    VAR_004165
    Natural varianti619 – 6191R → H.1 Publication
    Corresponds to variant rs3816665 [ dbSNP | Ensembl ].
    VAR_004166
    Natural varianti644 – 6441H → D.
    Corresponds to variant rs35879899 [ dbSNP | Ensembl ].
    VAR_047715
    Natural varianti862 – 8621C → R in MDC1A. 1 Publication
    VAR_015744
    Natural varianti919 – 9191R → L.1 Publication
    Corresponds to variant rs35277491 [ dbSNP | Ensembl ].
    VAR_004167
    Natural varianti1138 – 11381V → M.
    Corresponds to variant rs2306942 [ dbSNP | Ensembl ].
    VAR_047716
    Natural varianti1160 – 11601P → A in a breast cancer sample; somatic mutation. 1 Publication
    VAR_035819
    Natural varianti1205 – 12051T → A.
    Corresponds to variant rs35889149 [ dbSNP | Ensembl ].
    VAR_047717
    Natural varianti1561 – 15611K → Q.
    Corresponds to variant rs4143752 [ dbSNP | Ensembl ].
    VAR_047718
    Natural varianti1945 – 19451A → T.
    Corresponds to variant rs3828736 [ dbSNP | Ensembl ].
    VAR_047719
    Natural varianti2564 – 25641L → P in MDC1A. 1 Publication
    VAR_015745
    Natural varianti2586 – 25861Y → H.1 Publication
    VAR_004168
    Natural varianti2587 – 25871A → V.3 Publications
    Corresponds to variant rs6569605 [ dbSNP | Ensembl ].
    VAR_047720
    Natural varianti2614 – 26141E → K.1 Publication
    VAR_004169
    Natural varianti2636 – 26361T → A.
    Corresponds to variant rs2244008 [ dbSNP | Ensembl ].
    VAR_047721
    Natural varianti3029 – 30291T → A.
    Corresponds to variant rs34551216 [ dbSNP | Ensembl ].
    VAR_047722

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Z26653 mRNA. Translation: CAA81394.1. Frameshift.
    U66796
    , U66733, U66734, U66735, U66736, U66737, U66738, U66739, U66740, U66741, U66742, U66743, U66745, U66746, U66747, U66748, U66749, U66750, U66751, U66752, U66753, U66754, U66755, U66756, U66757, U66758, U66759, U66760, U66761, U66762, U66763, U66764, U66765, U66766, U66768, U66769, U66770, U66771, U66772, U66773, U66774, U66775, U66776, U66777, U66778, U66779, U66780, U66781, U66782, U66783, U66784, U66785, U66786, U66787, U66788, U66789, U66790, U66791, U66792, U66793, U66794, U66795 Genomic DNA. Translation: AAB18388.1. Sequence problems.
    AL583853
    , AL356124, AL445439, AL513527, AL590613, AL669984 Genomic DNA. Translation: CAH70492.1.
    AL590613
    , AL356124, AL445439, AL513527, AL583853, AL669984 Genomic DNA. Translation: CAH70771.1.
    AL445439
    , AL356124, AL513527, AL583853, AL590613, AL669984 Genomic DNA. Translation: CAH72952.1.
    AL513527
    , AL356124, AL445439, AL583853, AL590613, AL669984 Genomic DNA. Translation: CAI15185.1.
    AL669984
    , AL356124, AL445439, AL513527, AL583853, AL590613 Genomic DNA. Translation: CAI16682.1.
    AL356124
    , AL445439, AL513527, AL583853, AL590613, AL669984 Genomic DNA. Translation: CAI22470.1.
    AL589927 Genomic DNA. No translation available.
    M59832 mRNA. Translation: AAA63215.1. Frameshift.
    CCDSiCCDS5138.1.
    PIRiPX0082. MMHUMH.
    RefSeqiNP_000417.2. NM_000426.3.
    NP_001073291.1. NM_001079823.1.
    UniGeneiHs.200841.

    Genome annotation databases

    EnsembliENST00000421865; ENSP00000400365; ENSG00000196569.
    GeneIDi3908.
    KEGGihsa:3908.
    UCSCiuc003qbn.3. human.

    Polymorphism databases

    DMDMi215274259.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Z26653 mRNA. Translation: CAA81394.1 . Frameshift.
    U66796
    , U66733 , U66734 , U66735 , U66736 , U66737 , U66738 , U66739 , U66740 , U66741 , U66742 , U66743 , U66745 , U66746 , U66747 , U66748 , U66749 , U66750 , U66751 , U66752 , U66753 , U66754 , U66755 , U66756 , U66757 , U66758 , U66759 , U66760 , U66761 , U66762 , U66763 , U66764 , U66765 , U66766 , U66768 , U66769 , U66770 , U66771 , U66772 , U66773 , U66774 , U66775 , U66776 , U66777 , U66778 , U66779 , U66780 , U66781 , U66782 , U66783 , U66784 , U66785 , U66786 , U66787 , U66788 , U66789 , U66790 , U66791 , U66792 , U66793 , U66794 , U66795 Genomic DNA. Translation: AAB18388.1 . Sequence problems.
    AL583853
    , AL356124 , AL445439 , AL513527 , AL590613 , AL669984 Genomic DNA. Translation: CAH70492.1 .
    AL590613
    , AL356124 , AL445439 , AL513527 , AL583853 , AL669984 Genomic DNA. Translation: CAH70771.1 .
    AL445439
    , AL356124 , AL513527 , AL583853 , AL590613 , AL669984 Genomic DNA. Translation: CAH72952.1 .
    AL513527
    , AL356124 , AL445439 , AL583853 , AL590613 , AL669984 Genomic DNA. Translation: CAI15185.1 .
    AL669984
    , AL356124 , AL445439 , AL513527 , AL583853 , AL590613 Genomic DNA. Translation: CAI16682.1 .
    AL356124
    , AL445439 , AL513527 , AL583853 , AL590613 , AL669984 Genomic DNA. Translation: CAI22470.1 .
    AL589927 Genomic DNA. No translation available.
    M59832 mRNA. Translation: AAA63215.1 . Frameshift.
    CCDSi CCDS5138.1.
    PIRi PX0082. MMHUMH.
    RefSeqi NP_000417.2. NM_000426.3.
    NP_001073291.1. NM_001079823.1.
    UniGenei Hs.200841.

    3D structure databases

    ProteinModelPortali P24043.
    SMRi P24043. Positions 2939-3120.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 110102. 3 interactions.
    DIPi DIP-42562N.
    IntActi P24043. 4 interactions.
    MINTi MINT-2635209.
    STRINGi 9606.ENSP00000400365.

    Chemistry

    ChEMBLi CHEMBL2364187.

    PTM databases

    PhosphoSitei P24043.

    Polymorphism databases

    DMDMi 215274259.

    Proteomic databases

    PaxDbi P24043.
    PRIDEi P24043.

    Protocols and materials databases

    DNASUi 3908.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000421865 ; ENSP00000400365 ; ENSG00000196569 .
    GeneIDi 3908.
    KEGGi hsa:3908.
    UCSCi uc003qbn.3. human.

    Organism-specific databases

    CTDi 3908.
    GeneCardsi GC06P129246.
    GeneReviewsi LAMA2.
    HGNCi HGNC:6482. LAMA2.
    HPAi CAB040310.
    MIMi 156225. gene.
    607855. phenotype.
    neXtProti NX_P24043.
    Orphaneti 258. Congenital muscular dystrophy type 1A.
    PharmGKBi PA30271.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0419.
    HOGENOMi HOG000293201.
    HOVERGENi HBG052298.
    KOi K05637.
    OMAi HTTTKGI.
    OrthoDBi EOG7SR4KJ.
    PhylomeDBi P24043.
    TreeFami TF335359.

    Enzyme and pathway databases

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

    Miscellaneous databases

    GeneWikii Laminin,_alpha_2.
    GenomeRNAii 3908.
    NextBioi 15339.
    PROi P24043.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P24043.
    Bgeei P24043.
    CleanExi HS_LAMA2.
    Genevestigatori P24043.

    Family and domain databases

    Gene3Di 2.60.120.200. 5 hits.
    2.60.120.260. 2 hits.
    InterProi IPR008985. ConA-like_lec_gl_sf.
    IPR013320. ConA-like_subgrp.
    IPR002049. EGF_laminin.
    IPR008979. Galactose-bd-like.
    IPR018031. Laminin_B_subgr.
    IPR000034. Laminin_B_type_IV.
    IPR001791. Laminin_G.
    IPR009254. Laminin_I.
    IPR010307. Laminin_II.
    IPR008211. Laminin_N.
    [Graphical view ]
    Pfami PF00052. Laminin_B. 2 hits.
    PF00053. Laminin_EGF. 16 hits.
    PF00054. Laminin_G_1. 4 hits.
    PF02210. Laminin_G_2. 1 hit.
    PF06008. Laminin_I. 1 hit.
    PF06009. Laminin_II. 1 hit.
    PF00055. Laminin_N. 1 hit.
    [Graphical view ]
    SMARTi SM00180. EGF_Lam. 15 hits.
    SM00281. LamB. 2 hits.
    SM00282. LamG. 5 hits.
    SM00136. LamNT. 1 hit.
    [Graphical view ]
    SUPFAMi SSF49785. SSF49785. 1 hit.
    SSF49899. SSF49899. 5 hits.
    PROSITEi PS00022. EGF_1. 11 hits.
    PS01186. EGF_2. 3 hits.
    PS01248. EGF_LAM_1. 14 hits.
    PS50027. EGF_LAM_2. 15 hits.
    PS50025. LAM_G_DOMAIN. 5 hits.
    PS51115. LAMININ_IVA. 2 hits.
    PS51117. LAMININ_NTER. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Human laminin M chain (merosin): complete primary structure, chromosomal assignment, and expression of the M and A chain in human fetal tissues."
      Vuolteenaho R., Nissinen M., Sainio K., Byers M., Eddy R., Hirvonen H., Shows T.B., Sariola H., Engvall E., Tryggvason K.
      J. Cell Biol. 124:381-394(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT VAL-2587.
      Tissue: Placenta.
    2. "Structure of the human laminin alpha2-chain gene (LAMA2), which is affected in congenital muscular dystrophy."
      Zhang X., Vuolteenaho R., Tryggvason K.
      J. Biol. Chem. 271:27664-27669(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT VAL-2587.
    3. "The DNA sequence and analysis of human chromosome 6."
      Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D.
      , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.
      Nature 425:805-811(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    4. "Human laminin M chain: epitope analysis of its monoclonal antibodies by immunoscreening of cDNA clones and tissue expression."
      Hori H., Kanamori T., Mizuta T., Yamaguchi N., Liu Y., Nagai Y.
      J. Biochem. 116:1212-1219(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1360-3122.
    5. "Merosin, a tissue-specific basement membrane protein, is a laminin-like protein."
      Ehrig K., Leivo I., Argraves W.S., Ruoslahti E., Engvall E.
      Proc. Natl. Acad. Sci. U.S.A. 87:3264-3268(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1981-3122, PARTIAL PROTEIN SEQUENCE, VARIANT VAL-2587.
      Tissue: Placenta.
    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-363.
      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-1901; ASN-1916; ASN-1920; ASN-2017 AND ASN-2648.
      Tissue: Liver.
    8. "Novel single base polymorphisms and rare sequence variants in the laminin 2-chain coding region detected by RNA/SSCP analysis."
      Panicker S.G., Mendell J.T., Chen L., Feng B., Sahenk Z., Marzluf G.A., Amato A.A., Mendell J.R.
      Hum. Mutat. 13:174-174(1999)
      Cited for: VARIANTS GLN-545; HIS-619; LEU-919; HIS-2586 AND LYS-2614.
    9. "Congenital muscular dystrophy with primary partial laminin alpha-2 chain deficiency: molecular study."
      He Y., Jones K.J., Vignier N., Morgan G., Chevallay M., Barois A., Estournet-Mathiaud B., Hori H., Mizuta T., Tome F.M.S., North K.N., Guicheney P.
      Neurology 57:1319-1322(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT MDC1A PRO-2564.
    10. "Clinical and molecular study in congenital muscular dystrophy with partial laminin alpha-2 (LAMA2) deficiency."
      Tezak Z., Prandini P., Boscaro M., Marin A., Devaney J., Marino M., Fanin M., Trevisan C.P., Park J., Tyson W., Finkel R., Garcia C., Angelini C., Hoffman E.P., Pegoraro E.
      Hum. Mutat. 21:103-111(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS MDC1A TYR-527 AND ARG-862.
    11. Cited for: VARIANT [LARGE SCALE ANALYSIS] ALA-1160.

    Entry informationi

    Entry nameiLAMA2_HUMAN
    AccessioniPrimary (citable) accession number: P24043
    Secondary accession number(s): Q14736, Q5VUM2, Q93022
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: March 1, 1992
    Last sequence update: November 25, 2008
    Last modified: October 1, 2014
    This is version 159 of the entry and version 4 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 6
      Human chromosome 6: 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