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P25391 (LAMA1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 149. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:LAMA1
Synonyms:LAMA
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length3075 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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.

Subunit structure

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).

Subcellular location

Secretedextracellular spaceextracellular matrixbasement membrane. Note: Major component.

Domain

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 similarities

Contains 17 laminin EGF-like domains.

Contains 5 laminin G-like domains.

Contains 2 laminin IV type A domains.

Contains 1 laminin N-terminal domain.

Ontologies

Keywords
   Biological processCell adhesion
   Cellular componentBasement membrane
Extracellular matrix
Secreted
   Coding sequence diversityPolymorphism
   DomainCoiled coil
Laminin EGF-like domain
Repeat
Signal
   PTMDisulfide bond
Glycoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processaxon guidance

Traceable author statement. Source: Reactome

branching involved in salivary gland morphogenesis

Inferred from electronic annotation. Source: Ensembl

cell adhesion

Inferred from electronic annotation. Source: UniProtKB-KW

cell surface receptor signaling pathway

Inferred from sequence or structural similarity. Source: UniProtKB

epithelial tube branching involved in lung morphogenesis

Inferred from electronic annotation. Source: Ensembl

establishment of epithelial cell apical/basal polarity

Inferred from electronic annotation. Source: Ensembl

extracellular matrix organization

Traceable author statement. Source: Reactome

morphogenesis of an epithelial sheet

Inferred from electronic annotation. Source: Ensembl

regulation of cell adhesion

Inferred from electronic annotation. Source: InterPro

regulation of cell migration

Inferred from electronic annotation. Source: InterPro

regulation of embryonic development

Inferred from electronic annotation. Source: InterPro

retinal blood vessel morphogenesis

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentbasement membrane

Inferred from direct assay PubMed 10964500PubMed 2099832. Source: UniProtKB

cell-cell junction

Inferred from electronic annotation. Source: Ensembl

extracellular region

Traceable author statement. Source: Reactome

extracellular space

Inferred from direct assay PubMed 10964500. Source: UniProtKB

laminin-1 complex

Inferred from direct assay PubMed 8601594. Source: UniProtKB

laminin-3 complex

Inferred from physical interaction PubMed 10964500. Source: UniProtKB

proteinaceous extracellular matrix

Inferred from sequence or structural similarity. Source: UniProtKB

   Molecular_functionextracellular matrix structural constituent

Inferred from sequence or structural similarity. Source: UniProtKB

glycosphingolipid binding

Inferred from electronic annotation. Source: Ensembl

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

p4cQ8BDF82EBI-2529668,EBI-7167339From a different organism.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1717 Potential
Chain18 – 30753058Laminin subunit alpha-1
PRO_0000017054

Regions

Domain18 – 269252Laminin N-terminal
Domain270 – 32657Laminin EGF-like 1
Domain327 – 39670Laminin EGF-like 2
Domain397 – 45357Laminin EGF-like 3
Domain454 – 50249Laminin EGF-like 4
Domain503 – 51210Laminin EGF-like 5; first part
Domain516 – 708193Laminin IV type A 1
Domain709 – 74133Laminin EGF-like 5; second part
Domain742 – 79049Laminin EGF-like 6
Domain791 – 84858Laminin EGF-like 7
Domain849 – 90153Laminin EGF-like 8
Domain902 – 95049Laminin EGF-like 9
Domain951 – 99747Laminin EGF-like 10
Domain998 – 104346Laminin EGF-like 11
Domain1044 – 108946Laminin EGF-like 12
Domain1090 – 114960Laminin EGF-like 13
Domain1150 – 115910Laminin EGF-like 14; first part
Domain1170 – 1361192Laminin IV type A 2
Domain1362 – 140241Laminin EGF-like 14; second part
Domain1403 – 145149Laminin EGF-like 15
Domain1452 – 150857Laminin EGF-like 16
Domain1509 – 155547Laminin EGF-like 17
Domain2117 – 2297181Laminin G-like 1
Domain2305 – 2481177Laminin G-like 2
Domain2486 – 2673188Laminin G-like 3
Domain2713 – 2885173Laminin G-like 4
Domain2890 – 3070181Laminin G-like 5
Region1556 – 2116561Domain II and I
Coiled coil1706 – 179691 Potential
Coiled coil1968 – 198922 Potential
Coiled coil2088 – 212033 Potential
Motif2534 – 25363Cell attachment site

Amino acid modifications

Glycosylation381N-linked (GlcNAc...) Potential
Glycosylation5551N-linked (GlcNAc...) Potential
Glycosylation6651N-linked (GlcNAc...) Potential
Glycosylation7631N-linked (GlcNAc...) Potential
Glycosylation9261N-linked (GlcNAc...) Potential
Glycosylation9521N-linked (GlcNAc...) Potential
Glycosylation10451N-linked (GlcNAc...) Potential
Glycosylation14071N-linked (GlcNAc...) Potential
Glycosylation15791N-linked (GlcNAc...) Potential
Glycosylation15961N-linked (GlcNAc...) Potential
Glycosylation16781N-linked (GlcNAc...) Potential
Glycosylation16891N-linked (GlcNAc...) Potential
Glycosylation16981N-linked (GlcNAc...) Potential
Glycosylation17171N-linked (GlcNAc...) Potential
Glycosylation18041N-linked (GlcNAc...) Potential
Glycosylation18941N-linked (GlcNAc...) Potential
Glycosylation18981N-linked (GlcNAc...) Potential
Glycosylation19571N-linked (GlcNAc...) Potential
Glycosylation19741N-linked (GlcNAc...) Potential
Glycosylation19911N-linked (GlcNAc...) Potential
Glycosylation20381N-linked (GlcNAc...) Potential
Glycosylation20471N-linked (GlcNAc...) Potential
Glycosylation20941N-linked (GlcNAc...) Potential
Glycosylation20981N-linked (GlcNAc...) Potential
Glycosylation22431N-linked (GlcNAc...) Ref.5
Glycosylation22441N-linked (GlcNAc...) Potential
Glycosylation23841N-linked (GlcNAc...) Potential
Glycosylation24081N-linked (GlcNAc...) Potential
Glycosylation25181N-linked (GlcNAc...) Potential
Glycosylation26191N-linked (GlcNAc...) Potential
Glycosylation27291N-linked (GlcNAc...) Potential
Glycosylation28521N-linked (GlcNAc...) Potential
Glycosylation29151N-linked (GlcNAc...) Potential
Glycosylation29831N-linked (GlcNAc...) Potential
Disulfide bond270 ↔ 279 By similarity
Disulfide bond272 ↔ 290 By similarity
Disulfide bond292 ↔ 301 By similarity
Disulfide bond297 ↔ 305 Potential
Disulfide bond304 ↔ 324 By similarity
Disulfide bond327 ↔ 336 By similarity
Disulfide bond329 ↔ 361 By similarity
Disulfide bond364 ↔ 373 By similarity
Disulfide bond376 ↔ 394 By similarity
Disulfide bond397 ↔ 409 By similarity
Disulfide bond399 ↔ 427 By similarity
Disulfide bond429 ↔ 438 By similarity
Disulfide bond441 ↔ 451 By similarity
Disulfide bond454 ↔ 467 By similarity
Disulfide bond456 ↔ 471 By similarity
Disulfide bond473 ↔ 482 By similarity
Disulfide bond485 ↔ 500 By similarity
Disulfide bond742 ↔ 751 By similarity
Disulfide bond744 ↔ 757 By similarity
Disulfide bond760 ↔ 769 By similarity
Disulfide bond772 ↔ 788 By similarity
Disulfide bond791 ↔ 806 By similarity
Disulfide bond793 ↔ 816 By similarity
Disulfide bond819 ↔ 828 By similarity
Disulfide bond831 ↔ 846 By similarity
Disulfide bond849 ↔ 863 By similarity
Disulfide bond851 ↔ 870 By similarity
Disulfide bond873 ↔ 882 By similarity
Disulfide bond885 ↔ 899 By similarity
Disulfide bond902 ↔ 914 By similarity
Disulfide bond904 ↔ 921 By similarity
Disulfide bond923 ↔ 932 By similarity
Disulfide bond935 ↔ 948 By similarity
Disulfide bond951 ↔ 963 By similarity
Disulfide bond953 ↔ 969 By similarity
Disulfide bond971 ↔ 980 By similarity
Disulfide bond983 ↔ 995 By similarity
Disulfide bond998 ↔ 1007 By similarity
Disulfide bond1000 ↔ 1014 By similarity
Disulfide bond1016 ↔ 1025 By similarity
Disulfide bond1028 ↔ 1041 By similarity
Disulfide bond1044 ↔ 1056 By similarity
Disulfide bond1046 ↔ 1063 By similarity
Disulfide bond1065 ↔ 1074 By similarity
Disulfide bond1077 ↔ 1087 By similarity
Disulfide bond1090 ↔ 1102 By similarity
Disulfide bond1092 ↔ 1118 By similarity
Disulfide bond1120 ↔ 1129 By similarity
Disulfide bond1132 ↔ 1147 By similarity
Disulfide bond1403 ↔ 1412 By similarity
Disulfide bond1405 ↔ 1419 By similarity
Disulfide bond1422 ↔ 1431 By similarity
Disulfide bond1434 ↔ 1449 By similarity
Disulfide bond1452 ↔ 1466 By similarity
Disulfide bond1454 ↔ 1476 By similarity
Disulfide bond1479 ↔ 1488 By similarity
Disulfide bond1491 ↔ 1506 By similarity
Disulfide bond1509 ↔ 1521 By similarity
Disulfide bond1511 ↔ 1528 By similarity
Disulfide bond1530 ↔ 1539 By similarity
Disulfide bond1542 ↔ 1553 By similarity
Disulfide bond1556Interchain Probable
Disulfide bond1560Interchain Probable
Disulfide bond2271 ↔ 2297 By similarity
Disulfide bond2457 ↔ 2481 By similarity
Disulfide bond2646 ↔ 2673 By similarity
Disulfide bond2860 ↔ 2885 By similarity
Disulfide bond3039 ↔ 3070 By similarity

Natural variations

Natural variant3491L → S.
Corresponds to variant rs9950267 [ dbSNP | Ensembl ].
VAR_056132
Natural variant5591V → I.
Corresponds to variant rs16951079 [ dbSNP | Ensembl ].
VAR_056133
Natural variant6741N → T. Ref.1 Ref.3
Corresponds to variant rs566655 [ dbSNP | Ensembl ].
VAR_060785
Natural variant13401M → V. Ref.1
Corresponds to variant rs662471 [ dbSNP | Ensembl ].
VAR_060786
Natural variant15771S → A.
Corresponds to variant rs12961939 [ dbSNP | Ensembl ].
VAR_056134
Natural variant15911L → V.
Corresponds to variant rs596315 [ dbSNP | Ensembl ].
VAR_056135
Natural variant16321K → E.
Corresponds to variant rs11872364 [ dbSNP | Ensembl ].
VAR_056136
Natural variant16821D → V.
Corresponds to variant rs16950981 [ dbSNP | Ensembl ].
VAR_056137
Natural variant18761A → T. Ref.1 Ref.3
Corresponds to variant rs11664063 [ dbSNP | Ensembl ].
VAR_060787
Natural variant20021K → E. Ref.1 Ref.3
Corresponds to variant rs607230 [ dbSNP | Ensembl ].
VAR_060788
Natural variant20761I → T.
Corresponds to variant rs671871 [ dbSNP | Ensembl ].
VAR_056138
Natural variant25111L → M.
Corresponds to variant rs60009920 [ dbSNP | Ensembl ].
VAR_061347
Natural variant26111T → A.
Corresponds to variant rs543355 [ dbSNP | Ensembl ].
VAR_056139

Experimental info

Sequence conflict228 – 2292LQ → FE in CAA41418. Ref.3
Sequence conflict252 – 2543IVT → MLP in CAA41418. Ref.3
Sequence conflict4191H → E in CAA41418. Ref.3
Sequence conflict5191V → L in CAA41418. Ref.3
Sequence conflict10231V → G Ref.1
Sequence conflict10751D → V in CAA41418. Ref.3
Sequence conflict15131P → R Ref.1
Sequence conflict16591I → V Ref.1
Sequence conflict16591I → V in CAA41418. Ref.3
Sequence conflict2079 – 20802NL → KV in CAA41418. Ref.3
Sequence conflict26921P → R Ref.1
Sequence conflict26921P → R Ref.4
Sequence conflict27461F → L Ref.4
Sequence conflict29621A → P Ref.1
Sequence conflict29621A → P Ref.4
Sequence conflict30541F → L Ref.4

Sequences

Sequence LengthMass (Da)Tools
P25391 [UniParc].

Last modified December 15, 2009. Version 2.
Checksum: 941167F8FE534745

FASTA3,075337,084
        10         20         30         40         50         60 
MRGGVLLVLL LCVAAQCRQR GLFPAILNLA SNAHISTNAT CGEKGPEMFC KLVEHVPGRP 

        70         80         90        100        110        120 
VRNPQCRICD GNSANPRERH PISHAIDGTN NWWQSPSIQN GREYHWVTIT LDLRQVFQVA 

       130        140        150        160        170        180 
YVIIKAANAP RPGNWILERS LDGTTFSPWQ YYAVSDSECL SRYNITPRRG PPTYRADDEV 

       190        200        210        220        230        240 
ICTSYYSRLV PLEHGEIHTS LINGRPSADD LSPKLLEFTS ARYIRLRLQR IRTLNADLMT 

       250        260        270        280        290        300 
LSHREPKELD PIVTRRYYYS IKDISVGGMC ICYGHASSCP WDETTKKLQC QCEHNTCGES 

       310        320        330        340        350        360 
CNRCCPGYHQ QPWRPGTVSS GNTCEACNCH NKAKDCYYDE SVAKQKKSLN TAGQFRGGGV 

       370        380        390        400        410        420 
CINCLQNTMG INCETCIDGY YRPHKVSPYE DEPCRPCNCD PVGSLSSVCI KDDLHSDLHN 

       430        440        450        460        470        480 
GKQPGQCPCK EGYTGEKCDR CQLGYKDYPT CVSCGCNPVG SASDEPCTGP CVCKENVEGK 

       490        500        510        520        530        540 
ACDRCKPGFY NLKEKNPRGC SECFCFGVSD VCSSLSWPVG QVNSMSGWLV TDLISPRKIP 

       550        560        570        580        590        600 
SQQDALGGRH QVSINNTAVM QRLAPKYYWA APEAYLGNKL TAFGGFLKYT VSYDIPVETV 

       610        620        630        640        650        660 
DSNLMSHADV IIKGNGLTLS TQAEGLSLQP YEEYLNVVRL VPENFQDFHS KRQIDRDQLM 

       670        680        690        700        710        720 
TVLANVTHLL IRANYNSAKM ALYRLESVSL DIASSNAIDL VVAADVEHCE CPQGYTGTSC 

       730        740        750        760        770        780 
ESCLSGYYRV DGILFGGICQ PCECHGHAAE CNVHGVCIAC AHNTTGVHCE QCLPGFYGEP 

       790        800        810        820        830        840 
SRGTPGDCQP CACPLTIASN NFSPTCHLND GDEVVCDWCA PGYSGAWCER CADGYYGNPT 

       850        860        870        880        890        900 
VPGESCVPCD CSGNVDPSEA GHCDSVTGEC LKCLGNTDGA HCERCADGFY GDAVTAKNCR 

       910        920        930        940        950        960 
ACECHVKGSH SAVCHLETGL CDCKPNVTGQ QCDQCLHGYY GLDSGHGCRP CNCSVAGSVS 

       970        980        990       1000       1010       1020 
DGCTDEGQCH CVPGVAGKRC DRCAHGFYAY QDGSCTPCDC PHTQNTCDPE TGECVCPPHT 

      1030       1040       1050       1060       1070       1080 
QGVKCEECED GHWGYDAEVG CQACNCSLVG STHHRCDVVT GHCQCKSKFG GRACDQCSLG 

      1090       1100       1110       1120       1130       1140 
YRDFPDCVPC DCDLRGTSGD ACNLEQGLCG CVEETGACPC KENVFGPQCN ECREGTFALR 

      1150       1160       1170       1180       1190       1200 
ADNPLGCSPC FCSGLSHLCS ELEDYVRTPV TLGSDQPLLR VVSQSNLRGT TEGVYYQAPD 

      1210       1220       1230       1240       1250       1260 
FLLDAATVRQ HIRAEPFYWR LPQQFQGDQL MAYGGKLKYS VAFYSLDGVG TSNFEPQVLI 

      1270       1280       1290       1300       1310       1320 
KGGRIRKQVI YMDAPAPENG VRQEQEVAMR ENFWKYFNSV SEKPVTREDF MSVLSDIEYI 

      1330       1340       1350       1360       1370       1380 
LIKASYGQGL QQSRISDISM EVGRKAEKLH PEEEVASLLE NCVCPPGTVG FSCQDCAPGY 

      1390       1400       1410       1420       1430       1440 
HRGKLPAGSD RGPRPLVAPC VPCSCNNHSD TCDPNTGKCL NCGDNTAGDH CDVCTSGYYG 

      1450       1460       1470       1480       1490       1500 
KVTGSASDCA LCACPHSPPA SFSPTCVLEG DHDFRCDACL LGYEGKHCER CSSSYYGNPQ 

      1510       1520       1530       1540       1550       1560 
TPGGSCQKCD CNPHGSVHGD CDRTSGQCVC RLGASGLRCD ECEPRHILME TDCVSCDDEC 

      1570       1580       1590       1600       1610       1620 
VGVLLNDLDE IGDAVLSLNL TGIIPVPYGI LSNLENTTKY LQESLLKENM QKDLGKIKLE 

      1630       1640       1650       1660       1670       1680 
GVAEETDNLQ KKLTRMLAST QKVNRATERI FKESQDLAIA IERLQMSITE IMEKTTLNQT 

      1690       1700       1710       1720       1730       1740 
LDEDFLLPNS TLQNMQQNGT SLLEIMQIRD FTQLHQNATL ELKAAEDLLS QIQENYQKPL 

      1750       1760       1770       1780       1790       1800 
EELEVLKEAA SHVLSKHNNE LKAAEALVRE AEAKMQESNH LLLMVNANLR EFSDKKLHVQ 

      1810       1820       1830       1840       1850       1860 
EEQNLTSELI VQGRGLIDAA AAQTDAVQDA LEHLEDHQDK LLLWSAKIRH HIDDLVMHMS 

      1870       1880       1890       1900       1910       1920 
QRNAVDLVYR AEDHAAEFQR LADVLYSGLE NIRNVSLNAT SAAYVHYNIQ SLIEESEELA 

      1930       1940       1950       1960       1970       1980 
RDAHRTVTET SLLSESLVSN GKAAVQRSSR FLKEGNNLSR KLPGIALELS ELRNKTNRFQ 

      1990       2000       2010       2020       2030       2040 
ENAVEITRQT NESLLILRAI PKGIRDKGAK TKELATSASQ SAVSTLRDVA GLSQELLNTS 

      2050       2060       2070       2080       2090       2100 
ASLSRVNTTL RETHQLLQDS TMATLLAGRK VKDVEIQANL LFDRLKPLKM LEENLSRNLS 

      2110       2120       2130       2140       2150       2160 
EIKLLISQAR KQAASIKVAV SADRDCIRAY QPQISSTNYN TLTLNVKTQE PDNLLFYLGS 

      2170       2180       2190       2200       2210       2220 
STASDFLAVE MRRGRVAFLW DLGSGSTRLE FPDFPIDDNR WHSIHVARFG NIGSLSVKEM 

      2230       2240       2250       2260       2270       2280 
SSNQKSPTKT SKSPGTANVL DVNNSTLMFV GGLGGQIKKS PAVKVTHFKG CLGEAFLNGK 

      2290       2300       2310       2320       2330       2340 
SIGLWNYIER EGKCRGCFGS SQNEDPSFHF DGSGYSVVEK SLPATVTQII MLFNTFSPNG 

      2350       2360       2370       2380       2390       2400 
LLLYLGSYGT KDFLSIELFR GRVKVMTDLG SGPITLLTDR RYNNGTWYKI AFQRNRKQGV 

      2410       2420       2430       2440       2450       2460 
LAVIDAYNTS NKETKQGETP GASSDLNRLD KDPIYVGGLP RSRVVRRGVT TKSFVGCIKN 

      2470       2480       2490       2500       2510       2520 
LEISRSTFDL LRNSYGVRKG CLLEPIRSVS FLKGGYIELP PKSLSPESEW LVTFATTNSS 

      2530       2540       2550       2560       2570       2580 
GIILAALGGD VEKRGDREEA HVPFFSVMLI GGNIEVHVNP GDGTGLRKAL LHAPTGTCSD 

      2590       2600       2610       2620       2630       2640 
GQAHSISLVR NRRIITVQLD ENNPVEMKLG TLVESRTINV SNLYVGGIPE GEGTSLLTMR 

      2650       2660       2670       2680       2690       2700 
RSFHGCIKNL IFNLELLDFN SAVGHEQVDL DTCWLSERPK LAPDAEDSKL LPEPRAFPEQ 

      2710       2720       2730       2740       2750       2760 
CVVDAALEYV PGAHQFGLTQ NSHFILPFNQ SAVRKKLSVE LSIRTFASSG LIYYMAHQNQ 

      2770       2780       2790       2800       2810       2820 
ADYAVLQLHG GRLHFMFDLG KGRTKVSHPA LLSDGKWHTV KTDYVKRKGF ITVDGRESPM 

      2830       2840       2850       2860       2870       2880 
VTVVGDGTML DVEGLFYLGG LPSQYQARKI GNITHSIPAC IGDVTVNSKQ LDKDSPVSAF 

      2890       2900       2910       2920       2930       2940 
TVNRCYAVAQ EGTYFDGSGY AALVKEGYKV QSDVNITLEF RTSSQNGVLL GISTAKVDAI 

      2950       2960       2970       2980       2990       3000 
GLELVDGKVL FHVNNGAGRI TAAYEPKTAT VLCDGKWHTL QANKSKHRIT LIVDGNAVGA 

      3010       3020       3030       3040       3050       3060 
ESPHTQSTSV DTNNPIYVGG YPAGVKQKCL RSQTSFRGCL RKLALIKSPQ VQSFDFSRAF 

      3070 
ELHGVFLHSC PGTES 

« Hide

References

« Hide 'large scale' references
[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]"DNA sequence and analysis of human chromosome 18."
Nusbaum C., Zody M.C., Borowsky M.L., Kamal M., Kodira C.D., Taylor T.D., Whittaker C.A., Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Yang X., Abouelleil A., Allen N.R., Anderson S., Bloom T., Bugalter B., Butler J. expand/collapse author list , Cook A., DeCaprio D., Engels R., Garber M., Gnirke A., Hafez N., Hall J.L., Norman C.H., Itoh T., Jaffe D.B., Kuroki Y., Lehoczky J., Lui A., Macdonald P., Mauceli E., Mikkelsen T.S., Naylor J.W., Nicol R., Nguyen C., Noguchi H., O'Leary S.B., Piqani B., Smith C.L., Talamas J.A., Topham K., Totoki Y., Toyoda A., Wain H.M., Young S.K., Zeng Q., Zimmer A.R., Fujiyama A., Hattori M., Birren B.W., Sakaki Y., Lander E.S.
Nature 437:551-555(2005) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AP002409 Genomic DNA. No translation available.
AP005062 Genomic DNA. No translation available.
AP005210 Genomic DNA. No translation available.
X58531 mRNA. Translation: CAA41418.1.
PIRS14458.
RefSeqNP_005550.2. NM_005559.3.
UniGeneHs.270364.

3D structure databases

ProteinModelPortalP25391.
SMRP25391. Positions 12-535, 708-1155, 1361-1586, 2128-2472, 2491-2674, 2701-3074.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid129792. 10 interactions.
DIPDIP-29324N.
IntActP25391. 2 interactions.
MINTMINT-6740485.
STRING9606.ENSP00000374309.

Chemistry

ChEMBLCHEMBL2364187.
DrugBankDB00009. Alteplase.
DB00029. Anistreplase.
DB00015. Reteplase.
DB00031. Tenecteplase.

PTM databases

PhosphoSiteP25391.

Polymorphism databases

DMDM281185471.

Proteomic databases

PaxDbP25391.
PRIDEP25391.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000389658; ENSP00000374309; ENSG00000101680.
GeneID284217.
KEGGhsa:284217.
UCSCuc002knm.3. human.

Organism-specific databases

CTD284217.
GeneCardsGC18M006941.
H-InvDBHIX0014316.
HGNCHGNC:6481. LAMA1.
HPACAB010179.
HPA032109.
HPA032110.
MIM150320. gene.
neXtProtNX_P25391.
PharmGKBPA30270.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG247347.
HOGENOMHOG000293201.
HOVERGENHBG052298.
InParanoidP25391.
KOK05637.
OMAEPFYWRL.
OrthoDBEOG7SR4KJ.
PhylomeDBP25391.
TreeFamTF335359.

Enzyme and pathway databases

ReactomeREACT_111045. Developmental Biology.
REACT_118779. Extracellular matrix organization.

Gene expression databases

ArrayExpressP25391.
BgeeP25391.
CleanExHS_LAMA1.
GenevestigatorP25391.

Family and domain databases

Gene3D2.60.120.200. 5 hits.
InterProIPR008985. 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]
PfamPF00052. 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]
SMARTSM00180. EGF_Lam. 15 hits.
SM00281. LamB. 2 hits.
SM00282. LamG. 5 hits.
SM00136. LamNT. 1 hit.
[Graphical view]
SUPFAMSSF49899. SSF49899. 5 hits.
PROSITEPS00022. 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]
ProtoNetSearch...

Other

ChiTaRSLAMA1. human.
GeneWikiLaminin,_alpha_1.
GenomeRNAi284217.
NextBio94628.
PROP25391.
SOURCESearch...

Entry information

Entry nameLAMA1_HUMAN
AccessionPrimary (citable) accession number: P25391
Entry history
Integrated into UniProtKB/Swiss-Prot: May 1, 1992
Last sequence update: December 15, 2009
Last modified: April 16, 2014
This is version 149 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 18

Human chromosome 18: entries, gene names and cross-references to MIM