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Protein

Laminin subunit alpha-1

Gene

LAMA1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

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

GO - Biological processi

Keywordsi

Biological processCell adhesion

Enzyme and pathway databases

ReactomeiR-HSA-3000157 Laminin interactions
R-HSA-3000171 Non-integrin membrane-ECM interactions
R-HSA-3000178 ECM proteoglycans
R-HSA-373760 L1CAM interactions
R-HSA-8874081 MET activates PTK2 signaling
SIGNORiP25391

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
Proteomesi
  • UP000005640 Componenti: Chromosome 18

Organism-specific databases

EuPathDBiHostDB:ENSG00000101680.13
HGNCiHGNC:6481 LAMA1
MIMi150320 gene
neXtProtiNX_P25391

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Basement membrane, Extracellular matrix, Secreted

Pathology & Biotechi

Involvement in diseasei

Poretti-Boltshauser syndrome (PTBHS)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionAn autosomal recessive disorder characterized by cerebellar dysplasia, cerebellar vermis atrophy, cerebellar cysts in most patients, high myopia, variable retinal dystrophy, and eye movement abnormalities including strabismus, ocular apraxia, nystagmus. Affected individuals have ataxia, delayed motor development, language impairment, and intellectual disability with variable severity.
See also OMIM:615960

Organism-specific databases

DisGeNETi284217
MalaCardsiLAMA1
MIMi615960 phenotype
OpenTargetsiENSG00000101680
Orphaneti370022 Ataxia-intellectual disability-oculomotor apraxia-cerebellar cysts syndrome
PharmGKBiPA30270

Chemistry databases

ChEMBLiCHEMBL2364187

Polymorphism and mutation databases

BioMutaiLAMA1
DMDMi281185471

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 17Sequence analysisAdd BLAST17
ChainiPRO_000001705418 – 3075Laminin subunit alpha-1Add BLAST3058

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi270 ↔ 279PROSITE-ProRule annotation
Disulfide bondi272 ↔ 290PROSITE-ProRule annotation
Disulfide bondi292 ↔ 301PROSITE-ProRule annotation
Disulfide bondi304 ↔ 324PROSITE-ProRule annotation
Disulfide bondi327 ↔ 336PROSITE-ProRule annotation
Disulfide bondi329 ↔ 361PROSITE-ProRule annotation
Disulfide bondi364 ↔ 373PROSITE-ProRule annotation
Disulfide bondi376 ↔ 394PROSITE-ProRule annotation
Disulfide bondi397 ↔ 409PROSITE-ProRule annotation
Disulfide bondi399 ↔ 427PROSITE-ProRule annotation
Disulfide bondi429 ↔ 438PROSITE-ProRule annotation
Disulfide bondi441 ↔ 451PROSITE-ProRule annotation
Disulfide bondi454 ↔ 467PROSITE-ProRule annotation
Disulfide bondi456 ↔ 471PROSITE-ProRule annotation
Disulfide bondi473 ↔ 482PROSITE-ProRule annotation
Disulfide bondi485 ↔ 500PROSITE-ProRule annotation
Glycosylationi665N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi742 ↔ 751PROSITE-ProRule annotation
Disulfide bondi744 ↔ 757PROSITE-ProRule annotation
Disulfide bondi760 ↔ 769PROSITE-ProRule annotation
Disulfide bondi772 ↔ 788PROSITE-ProRule annotation
Disulfide bondi791 ↔ 806PROSITE-ProRule annotation
Disulfide bondi793 ↔ 816PROSITE-ProRule annotation
Disulfide bondi819 ↔ 828PROSITE-ProRule annotation
Disulfide bondi831 ↔ 846PROSITE-ProRule annotation
Disulfide bondi849 ↔ 863PROSITE-ProRule annotation
Disulfide bondi851 ↔ 870PROSITE-ProRule annotation
Disulfide bondi873 ↔ 882PROSITE-ProRule annotation
Disulfide bondi885 ↔ 899PROSITE-ProRule annotation
Disulfide bondi902 ↔ 914PROSITE-ProRule annotation
Disulfide bondi904 ↔ 921PROSITE-ProRule annotation
Disulfide bondi923 ↔ 932PROSITE-ProRule annotation
Disulfide bondi935 ↔ 948PROSITE-ProRule annotation
Disulfide bondi951 ↔ 963PROSITE-ProRule annotation
Disulfide bondi953 ↔ 969PROSITE-ProRule annotation
Disulfide bondi971 ↔ 980PROSITE-ProRule annotation
Disulfide bondi983 ↔ 995PROSITE-ProRule annotation
Disulfide bondi998 ↔ 1007PROSITE-ProRule annotation
Disulfide bondi1000 ↔ 1014PROSITE-ProRule annotation
Disulfide bondi1016 ↔ 1025PROSITE-ProRule annotation
Disulfide bondi1028 ↔ 1041PROSITE-ProRule annotation
Disulfide bondi1044 ↔ 1056PROSITE-ProRule annotation
Disulfide bondi1046 ↔ 1063PROSITE-ProRule annotation
Disulfide bondi1065 ↔ 1074PROSITE-ProRule annotation
Disulfide bondi1077 ↔ 1087PROSITE-ProRule annotation
Disulfide bondi1090 ↔ 1102PROSITE-ProRule annotation
Disulfide bondi1092 ↔ 1118PROSITE-ProRule annotation
Disulfide bondi1120 ↔ 1129PROSITE-ProRule annotation
Disulfide bondi1132 ↔ 1147PROSITE-ProRule annotation
Disulfide bondi1403 ↔ 1412PROSITE-ProRule annotation
Disulfide bondi1405 ↔ 1419PROSITE-ProRule annotation
Disulfide bondi1422 ↔ 1431PROSITE-ProRule annotation
Disulfide bondi1434 ↔ 1449PROSITE-ProRule annotation
Disulfide bondi1452 ↔ 1466PROSITE-ProRule annotation
Disulfide bondi1454 ↔ 1476PROSITE-ProRule annotation
Disulfide bondi1479 ↔ 1488PROSITE-ProRule annotation
Disulfide bondi1491 ↔ 1506PROSITE-ProRule annotation
Disulfide bondi1509 ↔ 1521PROSITE-ProRule annotation
Disulfide bondi1511 ↔ 1528PROSITE-ProRule annotation
Disulfide bondi1530 ↔ 1539PROSITE-ProRule annotation
Disulfide bondi1542 ↔ 1553PROSITE-ProRule annotation
Disulfide bondi1556InterchainCurated
Disulfide bondi1560InterchainCurated
Glycosylationi1579N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi1689N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi1717N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi2047N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi2243N-linked (GlcNAc...) asparagine1 Publication1
Disulfide bondi2271 ↔ 2297PROSITE-ProRule annotation
Disulfide bondi2457 ↔ 2481PROSITE-ProRule annotation
Disulfide bondi2646 ↔ 2673PROSITE-ProRule annotation
Disulfide bondi2860 ↔ 2885PROSITE-ProRule annotation
Disulfide bondi3039 ↔ 3070PROSITE-ProRule annotation

Post-translational modificationi

Tyrosine phosphorylated by PKDCC/VLK.1 Publication

Keywords - PTMi

Disulfide bond, Glycoprotein, Phosphoprotein

Proteomic databases

EPDiP25391
MaxQBiP25391
PaxDbiP25391
PeptideAtlasiP25391
PRIDEiP25391
ProteomicsDBi54269

PTM databases

GlyConnecti1438
iPTMnetiP25391
PhosphoSitePlusiP25391

Expressioni

Gene expression databases

BgeeiENSG00000101680 Expressed in 106 organ(s), highest expression level in metanephros
CleanExiHS_LAMA1
ExpressionAtlasiP25391 baseline and differential
GenevisibleiP25391 HS

Organism-specific databases

HPAiCAB010179

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 Vaccinia virus.

GO - Molecular functioni

Protein-protein interaction databases

BioGridi129792, 40 interactors
ComplexPortaliCPX-1770 Laminin-111 complex
CPX-1772 Laminin-121 complex
DIPiDIP-29324N
IntActiP25391, 28 interactors
MINTiP25391
STRINGi9606.ENSP00000374309

Structurei

3D structure databases

ProteinModelPortaliP25391
SMRiP25391
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini18 – 269Laminin N-terminalPROSITE-ProRule annotationAdd BLAST252
Domaini270 – 326Laminin EGF-like 1PROSITE-ProRule annotationAdd BLAST57
Domaini327 – 396Laminin EGF-like 2PROSITE-ProRule annotationAdd BLAST70
Domaini397 – 453Laminin EGF-like 3PROSITE-ProRule annotationAdd BLAST57
Domaini454 – 502Laminin EGF-like 4PROSITE-ProRule annotationAdd BLAST49
Domaini503 – 512Laminin EGF-like 5; first partPROSITE-ProRule annotation10
Domaini516 – 708Laminin IV type A 1PROSITE-ProRule annotationAdd BLAST193
Domaini709 – 741Laminin EGF-like 5; second partPROSITE-ProRule annotationAdd BLAST33
Domaini742 – 790Laminin EGF-like 6PROSITE-ProRule annotationAdd BLAST49
Domaini791 – 848Laminin EGF-like 7PROSITE-ProRule annotationAdd BLAST58
Domaini849 – 901Laminin EGF-like 8PROSITE-ProRule annotationAdd BLAST53
Domaini902 – 950Laminin EGF-like 9PROSITE-ProRule annotationAdd BLAST49
Domaini951 – 997Laminin EGF-like 10PROSITE-ProRule annotationAdd BLAST47
Domaini998 – 1043Laminin EGF-like 11PROSITE-ProRule annotationAdd BLAST46
Domaini1044 – 1089Laminin EGF-like 12PROSITE-ProRule annotationAdd BLAST46
Domaini1090 – 1149Laminin EGF-like 13PROSITE-ProRule annotationAdd BLAST60
Domaini1150 – 1159Laminin EGF-like 14; first partPROSITE-ProRule annotation10
Domaini1170 – 1361Laminin IV type A 2PROSITE-ProRule annotationAdd BLAST192
Domaini1362 – 1402Laminin EGF-like 14; second partPROSITE-ProRule annotationAdd BLAST41
Domaini1403 – 1451Laminin EGF-like 15PROSITE-ProRule annotationAdd BLAST49
Domaini1452 – 1508Laminin EGF-like 16PROSITE-ProRule annotationAdd BLAST57
Domaini1509 – 1555Laminin EGF-like 17PROSITE-ProRule annotationAdd BLAST47
Domaini2117 – 2297Laminin G-like 1PROSITE-ProRule annotationAdd BLAST181
Domaini2305 – 2481Laminin G-like 2PROSITE-ProRule annotationAdd BLAST177
Domaini2486 – 2673Laminin G-like 3PROSITE-ProRule annotationAdd BLAST188
Domaini2713 – 2885Laminin G-like 4PROSITE-ProRule annotationAdd BLAST173
Domaini2890 – 3070Laminin G-like 5PROSITE-ProRule annotationAdd BLAST181

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni1556 – 2116Domain II and IAdd BLAST561

Coiled coil

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Coiled coili1706 – 1783Sequence analysisAdd BLAST78

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi2534 – 2536Cell attachment site3

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.

Keywords - Domaini

Coiled coil, Laminin EGF-like domain, Repeat, Signal

Phylogenomic databases

eggNOGiKOG1836 Eukaryota
ENOG410XRDC LUCA
GeneTreeiENSGT00780000121851
HOGENOMiHOG000293201
HOVERGENiHBG052298
InParanoidiP25391
KOiK05637
OMAiICQPCEC
OrthoDBiEOG091G005L
PhylomeDBiP25391
TreeFamiTF335359

Family and domain databases

Gene3Di2.60.120.1490, 1 hit
InterProiView protein in InterPro
IPR013320 ConA-like_dom_sf
IPR000742 EGF-like_dom
IPR009254 Laminin_aI
IPR010307 Laminin_dom_II
IPR002049 Laminin_EGF
IPR001791 Laminin_G
IPR000034 Laminin_IV
IPR008211 Laminin_N
IPR038684 Laminin_N_sf
PfamiView protein in Pfam
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
SMARTiView protein in SMART
SM00181 EGF, 12 hits
SM00180 EGF_Lam, 17 hits
SM00281 LamB, 2 hits
SM00282 LamG, 5 hits
SM00136 LamNT, 1 hit
SUPFAMiSSF49899 SSF49899, 5 hits
PROSITEiView protein in PROSITE
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

Sequence (1+)i

Sequence statusi: Complete.

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

This entry has 1 described isoform and 1 potential isoform that is computationally mapped.Show allAlign All

P25391-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MRGGVLLVLL LCVAAQCRQR GLFPAILNLA SNAHISTNAT CGEKGPEMFC
60 70 80 90 100
KLVEHVPGRP VRNPQCRICD GNSANPRERH PISHAIDGTN NWWQSPSIQN
110 120 130 140 150
GREYHWVTIT LDLRQVFQVA YVIIKAANAP RPGNWILERS LDGTTFSPWQ
160 170 180 190 200
YYAVSDSECL SRYNITPRRG PPTYRADDEV ICTSYYSRLV PLEHGEIHTS
210 220 230 240 250
LINGRPSADD LSPKLLEFTS ARYIRLRLQR IRTLNADLMT LSHREPKELD
260 270 280 290 300
PIVTRRYYYS IKDISVGGMC ICYGHASSCP WDETTKKLQC QCEHNTCGES
310 320 330 340 350
CNRCCPGYHQ QPWRPGTVSS GNTCEACNCH NKAKDCYYDE SVAKQKKSLN
360 370 380 390 400
TAGQFRGGGV CINCLQNTMG INCETCIDGY YRPHKVSPYE DEPCRPCNCD
410 420 430 440 450
PVGSLSSVCI KDDLHSDLHN GKQPGQCPCK EGYTGEKCDR CQLGYKDYPT
460 470 480 490 500
CVSCGCNPVG SASDEPCTGP CVCKENVEGK ACDRCKPGFY NLKEKNPRGC
510 520 530 540 550
SECFCFGVSD VCSSLSWPVG QVNSMSGWLV TDLISPRKIP SQQDALGGRH
560 570 580 590 600
QVSINNTAVM QRLAPKYYWA APEAYLGNKL TAFGGFLKYT VSYDIPVETV
610 620 630 640 650
DSNLMSHADV IIKGNGLTLS TQAEGLSLQP YEEYLNVVRL VPENFQDFHS
660 670 680 690 700
KRQIDRDQLM TVLANVTHLL IRANYNSAKM ALYRLESVSL DIASSNAIDL
710 720 730 740 750
VVAADVEHCE CPQGYTGTSC ESCLSGYYRV DGILFGGICQ PCECHGHAAE
760 770 780 790 800
CNVHGVCIAC AHNTTGVHCE QCLPGFYGEP SRGTPGDCQP CACPLTIASN
810 820 830 840 850
NFSPTCHLND GDEVVCDWCA PGYSGAWCER CADGYYGNPT VPGESCVPCD
860 870 880 890 900
CSGNVDPSEA GHCDSVTGEC LKCLGNTDGA HCERCADGFY GDAVTAKNCR
910 920 930 940 950
ACECHVKGSH SAVCHLETGL CDCKPNVTGQ QCDQCLHGYY GLDSGHGCRP
960 970 980 990 1000
CNCSVAGSVS DGCTDEGQCH CVPGVAGKRC DRCAHGFYAY QDGSCTPCDC
1010 1020 1030 1040 1050
PHTQNTCDPE TGECVCPPHT QGVKCEECED GHWGYDAEVG CQACNCSLVG
1060 1070 1080 1090 1100
STHHRCDVVT GHCQCKSKFG GRACDQCSLG YRDFPDCVPC DCDLRGTSGD
1110 1120 1130 1140 1150
ACNLEQGLCG CVEETGACPC KENVFGPQCN ECREGTFALR ADNPLGCSPC
1160 1170 1180 1190 1200
FCSGLSHLCS ELEDYVRTPV TLGSDQPLLR VVSQSNLRGT TEGVYYQAPD
1210 1220 1230 1240 1250
FLLDAATVRQ HIRAEPFYWR LPQQFQGDQL MAYGGKLKYS VAFYSLDGVG
1260 1270 1280 1290 1300
TSNFEPQVLI KGGRIRKQVI YMDAPAPENG VRQEQEVAMR ENFWKYFNSV
1310 1320 1330 1340 1350
SEKPVTREDF MSVLSDIEYI LIKASYGQGL QQSRISDISM EVGRKAEKLH
1360 1370 1380 1390 1400
PEEEVASLLE NCVCPPGTVG FSCQDCAPGY HRGKLPAGSD RGPRPLVAPC
1410 1420 1430 1440 1450
VPCSCNNHSD TCDPNTGKCL NCGDNTAGDH CDVCTSGYYG KVTGSASDCA
1460 1470 1480 1490 1500
LCACPHSPPA SFSPTCVLEG DHDFRCDACL LGYEGKHCER CSSSYYGNPQ
1510 1520 1530 1540 1550
TPGGSCQKCD CNPHGSVHGD CDRTSGQCVC RLGASGLRCD ECEPRHILME
1560 1570 1580 1590 1600
TDCVSCDDEC VGVLLNDLDE IGDAVLSLNL TGIIPVPYGI LSNLENTTKY
1610 1620 1630 1640 1650
LQESLLKENM QKDLGKIKLE GVAEETDNLQ KKLTRMLAST QKVNRATERI
1660 1670 1680 1690 1700
FKESQDLAIA IERLQMSITE IMEKTTLNQT LDEDFLLPNS TLQNMQQNGT
1710 1720 1730 1740 1750
SLLEIMQIRD FTQLHQNATL ELKAAEDLLS QIQENYQKPL EELEVLKEAA
1760 1770 1780 1790 1800
SHVLSKHNNE LKAAEALVRE AEAKMQESNH LLLMVNANLR EFSDKKLHVQ
1810 1820 1830 1840 1850
EEQNLTSELI VQGRGLIDAA AAQTDAVQDA LEHLEDHQDK LLLWSAKIRH
1860 1870 1880 1890 1900
HIDDLVMHMS QRNAVDLVYR AEDHAAEFQR LADVLYSGLE NIRNVSLNAT
1910 1920 1930 1940 1950
SAAYVHYNIQ SLIEESEELA RDAHRTVTET SLLSESLVSN GKAAVQRSSR
1960 1970 1980 1990 2000
FLKEGNNLSR KLPGIALELS ELRNKTNRFQ ENAVEITRQT NESLLILRAI
2010 2020 2030 2040 2050
PKGIRDKGAK TKELATSASQ SAVSTLRDVA GLSQELLNTS ASLSRVNTTL
2060 2070 2080 2090 2100
RETHQLLQDS TMATLLAGRK VKDVEIQANL LFDRLKPLKM LEENLSRNLS
2110 2120 2130 2140 2150
EIKLLISQAR KQAASIKVAV SADRDCIRAY QPQISSTNYN TLTLNVKTQE
2160 2170 2180 2190 2200
PDNLLFYLGS STASDFLAVE MRRGRVAFLW DLGSGSTRLE FPDFPIDDNR
2210 2220 2230 2240 2250
WHSIHVARFG NIGSLSVKEM SSNQKSPTKT SKSPGTANVL DVNNSTLMFV
2260 2270 2280 2290 2300
GGLGGQIKKS PAVKVTHFKG CLGEAFLNGK SIGLWNYIER EGKCRGCFGS
2310 2320 2330 2340 2350
SQNEDPSFHF DGSGYSVVEK SLPATVTQII MLFNTFSPNG LLLYLGSYGT
2360 2370 2380 2390 2400
KDFLSIELFR GRVKVMTDLG SGPITLLTDR RYNNGTWYKI AFQRNRKQGV
2410 2420 2430 2440 2450
LAVIDAYNTS NKETKQGETP GASSDLNRLD KDPIYVGGLP RSRVVRRGVT
2460 2470 2480 2490 2500
TKSFVGCIKN LEISRSTFDL LRNSYGVRKG CLLEPIRSVS FLKGGYIELP
2510 2520 2530 2540 2550
PKSLSPESEW LVTFATTNSS GIILAALGGD VEKRGDREEA HVPFFSVMLI
2560 2570 2580 2590 2600
GGNIEVHVNP GDGTGLRKAL LHAPTGTCSD GQAHSISLVR NRRIITVQLD
2610 2620 2630 2640 2650
ENNPVEMKLG TLVESRTINV SNLYVGGIPE GEGTSLLTMR RSFHGCIKNL
2660 2670 2680 2690 2700
IFNLELLDFN SAVGHEQVDL DTCWLSERPK LAPDAEDSKL LPEPRAFPEQ
2710 2720 2730 2740 2750
CVVDAALEYV PGAHQFGLTQ NSHFILPFNQ SAVRKKLSVE LSIRTFASSG
2760 2770 2780 2790 2800
LIYYMAHQNQ ADYAVLQLHG GRLHFMFDLG KGRTKVSHPA LLSDGKWHTV
2810 2820 2830 2840 2850
KTDYVKRKGF ITVDGRESPM VTVVGDGTML DVEGLFYLGG LPSQYQARKI
2860 2870 2880 2890 2900
GNITHSIPAC IGDVTVNSKQ LDKDSPVSAF TVNRCYAVAQ EGTYFDGSGY
2910 2920 2930 2940 2950
AALVKEGYKV QSDVNITLEF RTSSQNGVLL GISTAKVDAI GLELVDGKVL
2960 2970 2980 2990 3000
FHVNNGAGRI TAAYEPKTAT VLCDGKWHTL QANKSKHRIT LIVDGNAVGA
3010 3020 3030 3040 3050
ESPHTQSTSV DTNNPIYVGG YPAGVKQKCL RSQTSFRGCL RKLALIKSPQ
3060 3070
VQSFDFSRAF ELHGVFLHSC PGTES
Length:3,075
Mass (Da):337,084
Last modified:December 15, 2009 - v2
Checksum:i941167F8FE534745
GO

Computationally mapped potential isoform sequencesi

There is 1 potential isoform mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
A0A1W2PQN4A0A1W2PQN4_HUMAN
Laminin subunit alpha-1
LAMA1
217Annotation score:

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti228 – 229LQ → FE in CAA41418 (PubMed:2049067).Curated2
Sequence conflicti252 – 254IVT → MLP in CAA41418 (PubMed:2049067).Curated3
Sequence conflicti419H → E in CAA41418 (PubMed:2049067).Curated1
Sequence conflicti519V → L in CAA41418 (PubMed:2049067).Curated1
Sequence conflicti1023V → G no nucleotide entry (PubMed:1714537).Curated1
Sequence conflicti1075D → V in CAA41418 (PubMed:2049067).Curated1
Sequence conflicti1513P → R no nucleotide entry (PubMed:1714537).Curated1
Sequence conflicti1659I → V no nucleotide entry (PubMed:1714537).Curated1
Sequence conflicti1659I → V in CAA41418 (PubMed:2049067).Curated1
Sequence conflicti2079 – 2080NL → KV in CAA41418 (PubMed:2049067).Curated2
Sequence conflicti2692P → R no nucleotide entry (PubMed:1714537).Curated1
Sequence conflicti2692P → R no nucleotide entry (PubMed:2733383).Curated1
Sequence conflicti2746F → L no nucleotide entry (PubMed:2733383).Curated1
Sequence conflicti2962A → P no nucleotide entry (PubMed:1714537).Curated1
Sequence conflicti2962A → P no nucleotide entry (PubMed:2733383).Curated1
Sequence conflicti3054F → L no nucleotide entry (PubMed:2733383).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_056132349L → S. Corresponds to variant dbSNP:rs9950267Ensembl.1
Natural variantiVAR_056133559V → I. Corresponds to variant dbSNP:rs16951079Ensembl.1
Natural variantiVAR_060785674N → T2 PublicationsCorresponds to variant dbSNP:rs566655Ensembl.1
Natural variantiVAR_0607861340M → V1 PublicationCorresponds to variant dbSNP:rs662471Ensembl.1
Natural variantiVAR_0561341577S → A. Corresponds to variant dbSNP:rs12961939Ensembl.1
Natural variantiVAR_0561351591L → V. Corresponds to variant dbSNP:rs596315Ensembl.1
Natural variantiVAR_0561361632K → E. Corresponds to variant dbSNP:rs11872364Ensembl.1
Natural variantiVAR_0561371682D → V. Corresponds to variant dbSNP:rs16950981Ensembl.1
Natural variantiVAR_0607871876A → T2 PublicationsCorresponds to variant dbSNP:rs11664063Ensembl.1
Natural variantiVAR_0607882002K → E2 PublicationsCorresponds to variant dbSNP:rs607230Ensembl.1
Natural variantiVAR_0561382076I → T. Corresponds to variant dbSNP:rs671871Ensembl.1
Natural variantiVAR_0613472511L → M. Corresponds to variant dbSNP:rs60009920Ensembl.1
Natural variantiVAR_0561392611T → A. Corresponds to variant dbSNP:rs543355Ensembl.1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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

Keywords - Coding sequence diversityi

Polymorphism

Similar proteinsi

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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

3D structure databases

ProteinModelPortaliP25391
SMRiP25391
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi129792, 40 interactors
ComplexPortaliCPX-1770 Laminin-111 complex
CPX-1772 Laminin-121 complex
DIPiDIP-29324N
IntActiP25391, 28 interactors
MINTiP25391
STRINGi9606.ENSP00000374309

Chemistry databases

ChEMBLiCHEMBL2364187

PTM databases

GlyConnecti1438
iPTMnetiP25391
PhosphoSitePlusiP25391

Polymorphism and mutation databases

BioMutaiLAMA1
DMDMi281185471

Proteomic databases

EPDiP25391
MaxQBiP25391
PaxDbiP25391
PeptideAtlasiP25391
PRIDEiP25391
ProteomicsDBi54269

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi284217
DisGeNETi284217
EuPathDBiHostDB:ENSG00000101680.13
GeneCardsiLAMA1
H-InvDBiHIX0014316
HGNCiHGNC:6481 LAMA1
HPAiCAB010179
MalaCardsiLAMA1
MIMi150320 gene
615960 phenotype
neXtProtiNX_P25391
OpenTargetsiENSG00000101680
Orphaneti370022 Ataxia-intellectual disability-oculomotor apraxia-cerebellar cysts syndrome
PharmGKBiPA30270
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG1836 Eukaryota
ENOG410XRDC LUCA
GeneTreeiENSGT00780000121851
HOGENOMiHOG000293201
HOVERGENiHBG052298
InParanoidiP25391
KOiK05637
OMAiICQPCEC
OrthoDBiEOG091G005L
PhylomeDBiP25391
TreeFamiTF335359

Enzyme and pathway databases

ReactomeiR-HSA-3000157 Laminin interactions
R-HSA-3000171 Non-integrin membrane-ECM interactions
R-HSA-3000178 ECM proteoglycans
R-HSA-373760 L1CAM interactions
R-HSA-8874081 MET activates PTK2 signaling
SIGNORiP25391

Miscellaneous databases

ChiTaRSiLAMA1 human
GeneWikiiLaminin,_alpha_1
GenomeRNAii284217
PROiPR:P25391
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000101680 Expressed in 106 organ(s), highest expression level in metanephros
CleanExiHS_LAMA1
ExpressionAtlasiP25391 baseline and differential
GenevisibleiP25391 HS

Family and domain databases

Gene3Di2.60.120.1490, 1 hit
InterProiView protein in InterPro
IPR013320 ConA-like_dom_sf
IPR000742 EGF-like_dom
IPR009254 Laminin_aI
IPR010307 Laminin_dom_II
IPR002049 Laminin_EGF
IPR001791 Laminin_G
IPR000034 Laminin_IV
IPR008211 Laminin_N
IPR038684 Laminin_N_sf
PfamiView protein in Pfam
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
SMARTiView protein in SMART
SM00181 EGF, 12 hits
SM00180 EGF_Lam, 17 hits
SM00281 LamB, 2 hits
SM00282 LamG, 5 hits
SM00136 LamNT, 1 hit
SUPFAMiSSF49899 SSF49899, 5 hits
PROSITEiView protein in PROSITE
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
ProtoNetiSearch...

Entry informationi

Entry nameiLAMA1_HUMAN
AccessioniPrimary (citable) accession number: P25391
Entry historyiIntegrated into UniProtKB/Swiss-Prot: May 1, 1992
Last sequence update: December 15, 2009
Last modified: October 10, 2018
This is version 194 of the entry and version 2 of the sequence. See 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 entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  2. Human chromosome 18
    Human chromosome 18: entries, gene names and cross-references to MIM
  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
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health

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