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)

P25391

- LAMA1_HUMAN

UniProt

P25391 - LAMA1_HUMAN

Protein

Laminin subunit alpha-1

Gene

LAMA1

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 154 (01 Oct 2014)
      Sequence version 2 (15 Dec 2009)
      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. extracellular matrix structural constituent Source: UniProtKB
    2. glycosphingolipid binding Source: Ensembl
    3. protein binding Source: IntAct

    GO - Biological processi

    1. axon guidance Source: Reactome
    2. branching involved in salivary gland morphogenesis Source: Ensembl
    3. cell adhesion Source: UniProtKB-KW
    4. cell surface receptor signaling pathway Source: UniProtKB
    5. epithelial tube branching involved in lung morphogenesis Source: Ensembl
    6. establishment of epithelial cell apical/basal polarity Source: Ensembl
    7. extracellular matrix organization Source: Reactome
    8. morphogenesis of an epithelial sheet Source: Ensembl
    9. regulation of cell adhesion Source: InterPro
    10. regulation of cell migration Source: InterPro
    11. regulation of embryonic development Source: InterPro
    12. retinal blood vessel morphogenesis 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.
    REACT_22205. L1CAM interactions.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Laminin subunit alpha-1
    Alternative name(s):
    Laminin A chain
    Laminin-1 subunit alpha
    Laminin-3 subunit alpha
    S-laminin subunit alpha
    Short name:
    S-LAM alpha
    Gene namesi
    Name:LAMA1
    Synonyms:LAMA
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 18

    Organism-specific databases

    HGNCiHGNC:6481. LAMA1.

    Subcellular locationi

    GO - Cellular componenti

    1. basement membrane Source: UniProtKB
    2. cell-cell junction Source: Ensembl
    3. extracellular region Source: Reactome
    4. extracellular space Source: UniProtKB
    5. laminin-1 complex Source: UniProtKB
    6. laminin-3 complex Source: UniProtKB
    7. proteinaceous extracellular matrix Source: UniProtKB

    Keywords - Cellular componenti

    Basement membrane, Extracellular matrix, Secreted

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA30270.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 1717Sequence AnalysisAdd
    BLAST
    Chaini18 – 30753058Laminin subunit alpha-1PRO_0000017054Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi38 – 381N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi270 ↔ 279By similarity
    Disulfide bondi272 ↔ 290By similarity
    Disulfide bondi292 ↔ 301By similarity
    Disulfide bondi297 ↔ 305Sequence Analysis
    Disulfide bondi304 ↔ 324By similarity
    Disulfide bondi327 ↔ 336By similarity
    Disulfide bondi329 ↔ 361By similarity
    Disulfide bondi364 ↔ 373By similarity
    Disulfide bondi376 ↔ 394By similarity
    Disulfide bondi397 ↔ 409By similarity
    Disulfide bondi399 ↔ 427By similarity
    Disulfide bondi429 ↔ 438By similarity
    Disulfide bondi441 ↔ 451By similarity
    Disulfide bondi454 ↔ 467By similarity
    Disulfide bondi456 ↔ 471By similarity
    Disulfide bondi473 ↔ 482By similarity
    Disulfide bondi485 ↔ 500By similarity
    Glycosylationi555 – 5551N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi665 – 6651N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi742 ↔ 751By similarity
    Disulfide bondi744 ↔ 757By similarity
    Disulfide bondi760 ↔ 769By similarity
    Glycosylationi763 – 7631N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi772 ↔ 788By similarity
    Disulfide bondi791 ↔ 806By similarity
    Disulfide bondi793 ↔ 816By similarity
    Disulfide bondi819 ↔ 828By similarity
    Disulfide bondi831 ↔ 846By similarity
    Disulfide bondi849 ↔ 863By similarity
    Disulfide bondi851 ↔ 870By similarity
    Disulfide bondi873 ↔ 882By similarity
    Disulfide bondi885 ↔ 899By similarity
    Disulfide bondi902 ↔ 914By similarity
    Disulfide bondi904 ↔ 921By similarity
    Disulfide bondi923 ↔ 932By similarity
    Glycosylationi926 – 9261N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi935 ↔ 948By similarity
    Disulfide bondi951 ↔ 963By similarity
    Glycosylationi952 – 9521N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi953 ↔ 969By similarity
    Disulfide bondi971 ↔ 980By similarity
    Disulfide bondi983 ↔ 995By similarity
    Disulfide bondi998 ↔ 1007By similarity
    Disulfide bondi1000 ↔ 1014By similarity
    Disulfide bondi1016 ↔ 1025By similarity
    Disulfide bondi1028 ↔ 1041By similarity
    Disulfide bondi1044 ↔ 1056By similarity
    Glycosylationi1045 – 10451N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi1046 ↔ 1063By similarity
    Disulfide bondi1065 ↔ 1074By similarity
    Disulfide bondi1077 ↔ 1087By similarity
    Disulfide bondi1090 ↔ 1102By similarity
    Disulfide bondi1092 ↔ 1118By similarity
    Disulfide bondi1120 ↔ 1129By similarity
    Disulfide bondi1132 ↔ 1147By similarity
    Disulfide bondi1403 ↔ 1412By similarity
    Disulfide bondi1405 ↔ 1419By similarity
    Glycosylationi1407 – 14071N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi1422 ↔ 1431By similarity
    Disulfide bondi1434 ↔ 1449By similarity
    Disulfide bondi1452 ↔ 1466By similarity
    Disulfide bondi1454 ↔ 1476By similarity
    Disulfide bondi1479 ↔ 1488By similarity
    Disulfide bondi1491 ↔ 1506By similarity
    Disulfide bondi1509 ↔ 1521By similarity
    Disulfide bondi1511 ↔ 1528By similarity
    Disulfide bondi1530 ↔ 1539By similarity
    Disulfide bondi1542 ↔ 1553By similarity
    Disulfide bondi1556 – 1556InterchainCurated
    Disulfide bondi1560 – 1560InterchainCurated
    Glycosylationi1579 – 15791N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi1596 – 15961N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi1678 – 16781N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi1689 – 16891N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi1698 – 16981N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi1717 – 17171N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi1804 – 18041N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi1894 – 18941N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi1898 – 18981N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi1957 – 19571N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi1974 – 19741N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi1991 – 19911N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi2038 – 20381N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi2047 – 20471N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi2094 – 20941N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi2098 – 20981N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi2243 – 22431N-linked (GlcNAc...)1 Publication
    Glycosylationi2244 – 22441N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi2271 ↔ 2297By similarity
    Glycosylationi2384 – 23841N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi2408 – 24081N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi2457 ↔ 2481By similarity
    Glycosylationi2518 – 25181N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi2619 – 26191N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi2646 ↔ 2673By similarity
    Glycosylationi2729 – 27291N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi2852 – 28521N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi2860 ↔ 2885By similarity
    Glycosylationi2915 – 29151N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi2983 – 29831N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi3039 ↔ 3070By similarity

    Keywords - PTMi

    Disulfide bond, Glycoprotein

    Proteomic databases

    MaxQBiP25391.
    PaxDbiP25391.
    PRIDEiP25391.

    PTM databases

    PhosphoSiteiP25391.

    Expressioni

    Gene expression databases

    ArrayExpressiP25391.
    BgeeiP25391.
    CleanExiHS_LAMA1.
    GenevestigatoriP25391.

    Organism-specific databases

    HPAiCAB010179.
    HPA032109.
    HPA032110.

    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-1 is a subunit of laminin-1 (laminin-111 or EHS laminin) and laminin-3 (laminin-121 or S-laminin).

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    p4cQ8BDF82EBI-2529668,EBI-7167339From a different organism.

    Protein-protein interaction databases

    BioGridi129792. 10 interactions.
    DIPiDIP-29324N.
    IntActiP25391. 2 interactions.
    MINTiMINT-6740485.
    STRINGi9606.ENSP00000374309.

    Structurei

    3D structure databases

    ProteinModelPortaliP25391.
    SMRiP25391. Positions 17-537, 708-1155, 1361-1544, 2128-2472, 2491-2674, 2701-3074.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini18 – 269252Laminin N-terminalPROSITE-ProRule annotationAdd
    BLAST
    Domaini270 – 32657Laminin EGF-like 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini327 – 39670Laminin EGF-like 2PROSITE-ProRule annotationAdd
    BLAST
    Domaini397 – 45357Laminin EGF-like 3PROSITE-ProRule annotationAdd
    BLAST
    Domaini454 – 50249Laminin EGF-like 4PROSITE-ProRule annotationAdd
    BLAST
    Domaini503 – 51210Laminin EGF-like 5; first partPROSITE-ProRule annotation
    Domaini516 – 708193Laminin IV type A 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini709 – 74133Laminin EGF-like 5; second partPROSITE-ProRule annotationAdd
    BLAST
    Domaini742 – 79049Laminin EGF-like 6PROSITE-ProRule annotationAdd
    BLAST
    Domaini791 – 84858Laminin EGF-like 7PROSITE-ProRule annotationAdd
    BLAST
    Domaini849 – 90153Laminin EGF-like 8PROSITE-ProRule annotationAdd
    BLAST
    Domaini902 – 95049Laminin EGF-like 9PROSITE-ProRule annotationAdd
    BLAST
    Domaini951 – 99747Laminin EGF-like 10PROSITE-ProRule annotationAdd
    BLAST
    Domaini998 – 104346Laminin EGF-like 11PROSITE-ProRule annotationAdd
    BLAST
    Domaini1044 – 108946Laminin EGF-like 12PROSITE-ProRule annotationAdd
    BLAST
    Domaini1090 – 114960Laminin EGF-like 13PROSITE-ProRule annotationAdd
    BLAST
    Domaini1150 – 115910Laminin EGF-like 14; first partPROSITE-ProRule annotation
    Domaini1170 – 1361192Laminin IV type A 2PROSITE-ProRule annotationAdd
    BLAST
    Domaini1362 – 140241Laminin EGF-like 14; second partPROSITE-ProRule annotationAdd
    BLAST
    Domaini1403 – 145149Laminin EGF-like 15PROSITE-ProRule annotationAdd
    BLAST
    Domaini1452 – 150857Laminin EGF-like 16PROSITE-ProRule annotationAdd
    BLAST
    Domaini1509 – 155547Laminin EGF-like 17PROSITE-ProRule annotationAdd
    BLAST
    Domaini2117 – 2297181Laminin G-like 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini2305 – 2481177Laminin G-like 2PROSITE-ProRule annotationAdd
    BLAST
    Domaini2486 – 2673188Laminin G-like 3PROSITE-ProRule annotationAdd
    BLAST
    Domaini2713 – 2885173Laminin G-like 4PROSITE-ProRule annotationAdd
    BLAST
    Domaini2890 – 3070181Laminin G-like 5PROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni1556 – 2116561Domain II and IAdd
    BLAST

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili1706 – 179691Sequence AnalysisAdd
    BLAST
    Coiled coili1968 – 198922Sequence AnalysisAdd
    BLAST
    Coiled coili2088 – 212033Sequence AnalysisAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi2534 – 25363Cell attachment site

    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

    eggNOGiNOG247347.
    HOGENOMiHOG000293201.
    HOVERGENiHBG052298.
    InParanoidiP25391.
    KOiK05637.
    OMAiEPFYWRL.
    OrthoDBiEOG7SR4KJ.
    PhylomeDBiP25391.
    TreeFamiTF335359.

    Family and domain databases

    Gene3Di2.60.120.200. 5 hits.
    InterProiIPR008985. ConA-like_lec_gl_sf.
    IPR013320. ConA-like_subgrp.
    IPR002049. EGF_laminin.
    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. 17 hits.
    PF00054. Laminin_G_1. 5 hits.
    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]
    SUPFAMiSSF49899. SSF49899. 5 hits.
    PROSITEiPS00022. EGF_1. 11 hits.
    PS01186. EGF_2. 2 hits.
    PS01248. EGF_LAM_1. 15 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.

    P25391-1 [UniParc]FASTAAdd to Basket

    « Hide

    MRGGVLLVLL LCVAAQCRQR GLFPAILNLA SNAHISTNAT CGEKGPEMFC     50
    KLVEHVPGRP VRNPQCRICD GNSANPRERH PISHAIDGTN NWWQSPSIQN 100
    GREYHWVTIT LDLRQVFQVA YVIIKAANAP RPGNWILERS LDGTTFSPWQ 150
    YYAVSDSECL SRYNITPRRG PPTYRADDEV ICTSYYSRLV PLEHGEIHTS 200
    LINGRPSADD LSPKLLEFTS ARYIRLRLQR IRTLNADLMT LSHREPKELD 250
    PIVTRRYYYS IKDISVGGMC ICYGHASSCP WDETTKKLQC QCEHNTCGES 300
    CNRCCPGYHQ QPWRPGTVSS GNTCEACNCH NKAKDCYYDE SVAKQKKSLN 350
    TAGQFRGGGV CINCLQNTMG INCETCIDGY YRPHKVSPYE DEPCRPCNCD 400
    PVGSLSSVCI KDDLHSDLHN GKQPGQCPCK EGYTGEKCDR CQLGYKDYPT 450
    CVSCGCNPVG SASDEPCTGP CVCKENVEGK ACDRCKPGFY NLKEKNPRGC 500
    SECFCFGVSD VCSSLSWPVG QVNSMSGWLV TDLISPRKIP SQQDALGGRH 550
    QVSINNTAVM QRLAPKYYWA APEAYLGNKL TAFGGFLKYT VSYDIPVETV 600
    DSNLMSHADV IIKGNGLTLS TQAEGLSLQP YEEYLNVVRL VPENFQDFHS 650
    KRQIDRDQLM TVLANVTHLL IRANYNSAKM ALYRLESVSL DIASSNAIDL 700
    VVAADVEHCE CPQGYTGTSC ESCLSGYYRV DGILFGGICQ PCECHGHAAE 750
    CNVHGVCIAC AHNTTGVHCE QCLPGFYGEP SRGTPGDCQP CACPLTIASN 800
    NFSPTCHLND GDEVVCDWCA PGYSGAWCER CADGYYGNPT VPGESCVPCD 850
    CSGNVDPSEA GHCDSVTGEC LKCLGNTDGA HCERCADGFY GDAVTAKNCR 900
    ACECHVKGSH SAVCHLETGL CDCKPNVTGQ QCDQCLHGYY GLDSGHGCRP 950
    CNCSVAGSVS DGCTDEGQCH CVPGVAGKRC DRCAHGFYAY QDGSCTPCDC 1000
    PHTQNTCDPE TGECVCPPHT QGVKCEECED GHWGYDAEVG CQACNCSLVG 1050
    STHHRCDVVT GHCQCKSKFG GRACDQCSLG YRDFPDCVPC DCDLRGTSGD 1100
    ACNLEQGLCG CVEETGACPC KENVFGPQCN ECREGTFALR ADNPLGCSPC 1150
    FCSGLSHLCS ELEDYVRTPV TLGSDQPLLR VVSQSNLRGT TEGVYYQAPD 1200
    FLLDAATVRQ HIRAEPFYWR LPQQFQGDQL MAYGGKLKYS VAFYSLDGVG 1250
    TSNFEPQVLI KGGRIRKQVI YMDAPAPENG VRQEQEVAMR ENFWKYFNSV 1300
    SEKPVTREDF MSVLSDIEYI LIKASYGQGL QQSRISDISM EVGRKAEKLH 1350
    PEEEVASLLE NCVCPPGTVG FSCQDCAPGY HRGKLPAGSD RGPRPLVAPC 1400
    VPCSCNNHSD TCDPNTGKCL NCGDNTAGDH CDVCTSGYYG KVTGSASDCA 1450
    LCACPHSPPA SFSPTCVLEG DHDFRCDACL LGYEGKHCER CSSSYYGNPQ 1500
    TPGGSCQKCD CNPHGSVHGD CDRTSGQCVC RLGASGLRCD ECEPRHILME 1550
    TDCVSCDDEC VGVLLNDLDE IGDAVLSLNL TGIIPVPYGI LSNLENTTKY 1600
    LQESLLKENM QKDLGKIKLE GVAEETDNLQ KKLTRMLAST QKVNRATERI 1650
    FKESQDLAIA IERLQMSITE IMEKTTLNQT LDEDFLLPNS TLQNMQQNGT 1700
    SLLEIMQIRD FTQLHQNATL ELKAAEDLLS QIQENYQKPL EELEVLKEAA 1750
    SHVLSKHNNE LKAAEALVRE AEAKMQESNH LLLMVNANLR EFSDKKLHVQ 1800
    EEQNLTSELI VQGRGLIDAA AAQTDAVQDA LEHLEDHQDK LLLWSAKIRH 1850
    HIDDLVMHMS QRNAVDLVYR AEDHAAEFQR LADVLYSGLE NIRNVSLNAT 1900
    SAAYVHYNIQ SLIEESEELA RDAHRTVTET SLLSESLVSN GKAAVQRSSR 1950
    FLKEGNNLSR KLPGIALELS ELRNKTNRFQ ENAVEITRQT NESLLILRAI 2000
    PKGIRDKGAK TKELATSASQ SAVSTLRDVA GLSQELLNTS ASLSRVNTTL 2050
    RETHQLLQDS TMATLLAGRK VKDVEIQANL LFDRLKPLKM LEENLSRNLS 2100
    EIKLLISQAR KQAASIKVAV SADRDCIRAY QPQISSTNYN TLTLNVKTQE 2150
    PDNLLFYLGS STASDFLAVE MRRGRVAFLW DLGSGSTRLE FPDFPIDDNR 2200
    WHSIHVARFG NIGSLSVKEM SSNQKSPTKT SKSPGTANVL DVNNSTLMFV 2250
    GGLGGQIKKS PAVKVTHFKG CLGEAFLNGK SIGLWNYIER EGKCRGCFGS 2300
    SQNEDPSFHF DGSGYSVVEK SLPATVTQII MLFNTFSPNG LLLYLGSYGT 2350
    KDFLSIELFR GRVKVMTDLG SGPITLLTDR RYNNGTWYKI AFQRNRKQGV 2400
    LAVIDAYNTS NKETKQGETP GASSDLNRLD KDPIYVGGLP RSRVVRRGVT 2450
    TKSFVGCIKN LEISRSTFDL LRNSYGVRKG CLLEPIRSVS FLKGGYIELP 2500
    PKSLSPESEW LVTFATTNSS GIILAALGGD VEKRGDREEA HVPFFSVMLI 2550
    GGNIEVHVNP GDGTGLRKAL LHAPTGTCSD GQAHSISLVR NRRIITVQLD 2600
    ENNPVEMKLG TLVESRTINV SNLYVGGIPE GEGTSLLTMR RSFHGCIKNL 2650
    IFNLELLDFN SAVGHEQVDL DTCWLSERPK LAPDAEDSKL LPEPRAFPEQ 2700
    CVVDAALEYV PGAHQFGLTQ NSHFILPFNQ SAVRKKLSVE LSIRTFASSG 2750
    LIYYMAHQNQ ADYAVLQLHG GRLHFMFDLG KGRTKVSHPA LLSDGKWHTV 2800
    KTDYVKRKGF ITVDGRESPM VTVVGDGTML DVEGLFYLGG LPSQYQARKI 2850
    GNITHSIPAC IGDVTVNSKQ LDKDSPVSAF TVNRCYAVAQ EGTYFDGSGY 2900
    AALVKEGYKV QSDVNITLEF RTSSQNGVLL GISTAKVDAI GLELVDGKVL 2950
    FHVNNGAGRI TAAYEPKTAT VLCDGKWHTL QANKSKHRIT LIVDGNAVGA 3000
    ESPHTQSTSV DTNNPIYVGG YPAGVKQKCL RSQTSFRGCL RKLALIKSPQ 3050
    VQSFDFSRAF ELHGVFLHSC PGTES 3075
    Length:3,075
    Mass (Da):337,084
    Last modified:December 15, 2009 - v2
    Checksum:i941167F8FE534745
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti228 – 2292LQ → FE in CAA41418. (PubMed:2049067)Curated
    Sequence conflicti252 – 2543IVT → MLP in CAA41418. (PubMed:2049067)Curated
    Sequence conflicti419 – 4191H → E in CAA41418. (PubMed:2049067)Curated
    Sequence conflicti519 – 5191V → L in CAA41418. (PubMed:2049067)Curated
    Sequence conflicti1023 – 10231V → G(PubMed:1714537)Curated
    Sequence conflicti1075 – 10751D → V in CAA41418. (PubMed:2049067)Curated
    Sequence conflicti1513 – 15131P → R(PubMed:1714537)Curated
    Sequence conflicti1659 – 16591I → V(PubMed:1714537)Curated
    Sequence conflicti1659 – 16591I → V in CAA41418. (PubMed:2049067)Curated
    Sequence conflicti2079 – 20802NL → KV in CAA41418. (PubMed:2049067)Curated
    Sequence conflicti2692 – 26921P → R(PubMed:1714537)Curated
    Sequence conflicti2692 – 26921P → R(PubMed:2733383)Curated
    Sequence conflicti2746 – 27461F → L(PubMed:2733383)Curated
    Sequence conflicti2962 – 29621A → P(PubMed:1714537)Curated
    Sequence conflicti2962 – 29621A → P(PubMed:2733383)Curated
    Sequence conflicti3054 – 30541F → L(PubMed:2733383)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti349 – 3491L → S.
    Corresponds to variant rs9950267 [ dbSNP | Ensembl ].
    VAR_056132
    Natural varianti559 – 5591V → I.
    Corresponds to variant rs16951079 [ dbSNP | Ensembl ].
    VAR_056133
    Natural varianti674 – 6741N → T.2 Publications
    Corresponds to variant rs566655 [ dbSNP | Ensembl ].
    VAR_060785
    Natural varianti1340 – 13401M → V.1 Publication
    Corresponds to variant rs662471 [ dbSNP | Ensembl ].
    VAR_060786
    Natural varianti1577 – 15771S → A.
    Corresponds to variant rs12961939 [ dbSNP | Ensembl ].
    VAR_056134
    Natural varianti1591 – 15911L → V.
    Corresponds to variant rs596315 [ dbSNP | Ensembl ].
    VAR_056135
    Natural varianti1632 – 16321K → E.
    Corresponds to variant rs11872364 [ dbSNP | Ensembl ].
    VAR_056136
    Natural varianti1682 – 16821D → V.
    Corresponds to variant rs16950981 [ dbSNP | Ensembl ].
    VAR_056137
    Natural varianti1876 – 18761A → T.2 Publications
    Corresponds to variant rs11664063 [ dbSNP | Ensembl ].
    VAR_060787
    Natural varianti2002 – 20021K → E.2 Publications
    Corresponds to variant rs607230 [ dbSNP | Ensembl ].
    VAR_060788
    Natural varianti2076 – 20761I → T.
    Corresponds to variant rs671871 [ dbSNP | Ensembl ].
    VAR_056138
    Natural varianti2511 – 25111L → M.
    Corresponds to variant rs60009920 [ dbSNP | Ensembl ].
    VAR_061347
    Natural varianti2611 – 26111T → A.
    Corresponds to variant rs543355 [ dbSNP | Ensembl ].
    VAR_056139

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AP002409 Genomic DNA. No translation available.
    AP005062 Genomic DNA. No translation available.
    AP005210 Genomic DNA. No translation available.
    X58531 mRNA. Translation: CAA41418.1.
    CCDSiCCDS32787.1.
    PIRiS14458.
    RefSeqiNP_005550.2. NM_005559.3.
    UniGeneiHs.270364.

    Genome annotation databases

    EnsembliENST00000389658; ENSP00000374309; ENSG00000101680.
    GeneIDi284217.
    KEGGihsa:284217.
    UCSCiuc002knm.3. human.

    Polymorphism databases

    DMDMi281185471.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AP002409 Genomic DNA. No translation available.
    AP005062 Genomic DNA. No translation available.
    AP005210 Genomic DNA. No translation available.
    X58531 mRNA. Translation: CAA41418.1 .
    CCDSi CCDS32787.1.
    PIRi S14458.
    RefSeqi NP_005550.2. NM_005559.3.
    UniGenei Hs.270364.

    3D structure databases

    ProteinModelPortali P25391.
    SMRi P25391. Positions 17-537, 708-1155, 1361-1544, 2128-2472, 2491-2674, 2701-3074.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 129792. 10 interactions.
    DIPi DIP-29324N.
    IntActi P25391. 2 interactions.
    MINTi MINT-6740485.
    STRINGi 9606.ENSP00000374309.

    Chemistry

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

    PTM databases

    PhosphoSitei P25391.

    Polymorphism databases

    DMDMi 281185471.

    Proteomic databases

    MaxQBi P25391.
    PaxDbi P25391.
    PRIDEi P25391.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000389658 ; ENSP00000374309 ; ENSG00000101680 .
    GeneIDi 284217.
    KEGGi hsa:284217.
    UCSCi uc002knm.3. human.

    Organism-specific databases

    CTDi 284217.
    GeneCardsi GC18M006941.
    H-InvDB HIX0014316.
    HGNCi HGNC:6481. LAMA1.
    HPAi CAB010179.
    HPA032109.
    HPA032110.
    MIMi 150320. gene.
    neXtProti NX_P25391.
    PharmGKBi PA30270.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG247347.
    HOGENOMi HOG000293201.
    HOVERGENi HBG052298.
    InParanoidi P25391.
    KOi K05637.
    OMAi EPFYWRL.
    OrthoDBi EOG7SR4KJ.
    PhylomeDBi P25391.
    TreeFami TF335359.

    Enzyme and pathway databases

    Reactomei REACT_163874. Non-integrin membrane-ECM interactions.
    REACT_163906. ECM proteoglycans.
    REACT_169262. Laminin interactions.
    REACT_22205. L1CAM interactions.

    Miscellaneous databases

    ChiTaRSi LAMA1. human.
    GeneWikii Laminin,_alpha_1.
    GenomeRNAii 284217.
    NextBioi 94628.
    PROi P25391.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P25391.
    Bgeei P25391.
    CleanExi HS_LAMA1.
    Genevestigatori P25391.

    Family and domain databases

    Gene3Di 2.60.120.200. 5 hits.
    InterProi IPR008985. ConA-like_lec_gl_sf.
    IPR013320. ConA-like_subgrp.
    IPR002049. EGF_laminin.
    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. 17 hits.
    PF00054. Laminin_G_1. 5 hits.
    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 SSF49899. SSF49899. 5 hits.
    PROSITEi PS00022. EGF_1. 11 hits.
    PS01186. EGF_2. 2 hits.
    PS01248. EGF_LAM_1. 15 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. "Molecular cloning of the cDNA encoding human laminin A chain."
      Haaparanta T., Uitto J., Ruoslahti E., Engvall E.
      Matrix 11:151-160(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANTS THR-674; VAL-1340; THR-1876 AND GLU-2002.
    2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    3. "Primary structure of the human laminin A chain. Limited expression in human tissues."
      Nissinen M., Vuolteenaho R., Boot-Handford R., Kallunki P., Tryggvason K.
      Biochem. J. 276:369-379(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-2628, VARIANTS THR-674; THR-1876 AND GLU-2002.
    4. "Human laminin: cloning and sequence analysis of cDNAs encoding A, B1 and B2 chains, and expression of the corresponding genes in human skin and cultured cells."
      Olsen D., Nagayoshi T., Fazio M., Peltonen J., Jaakkola S., Sanborn D., Sasaki T., Kuivaniemi H., Chu M.-L., Deutzmann R., Timpl R., Uitto J.
      Lab. Invest. 60:772-782(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 2397-3072.
    5. "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-2243.
      Tissue: Liver.

    Entry informationi

    Entry nameiLAMA1_HUMAN
    AccessioniPrimary (citable) accession number: P25391
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 1, 1992
    Last sequence update: December 15, 2009
    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 18
      Human chromosome 18: 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