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Protein

Laminin subunit alpha-1

Gene

LAMA1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-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

Complete GO annotation...

Keywords - Biological processi

Cell 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

HGNCiHGNC:6481. LAMA1.

Subcellular locationi

GO - Cellular componenti

  • basement membrane Source: UniProtKB
  • extracellular matrix Source: UniProtKB
  • extracellular region Source: Reactome
  • extracellular space Source: UniProtKB
  • laminin-1 complex Source: UniProtKB
  • laminin-3 complex Source: UniProtKB
  • proteinaceous extracellular matrix Source: UniProtKB
Complete GO annotation...

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
Glycosylationi38N-linked (GlcNAc...)Sequence analysis1
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
Glycosylationi555N-linked (GlcNAc...)Sequence analysis1
Glycosylationi665N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi742 ↔ 751By similarity
Disulfide bondi744 ↔ 757By similarity
Disulfide bondi760 ↔ 769By similarity
Glycosylationi763N-linked (GlcNAc...)Sequence analysis1
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
Glycosylationi926N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi935 ↔ 948By similarity
Disulfide bondi951 ↔ 963By similarity
Glycosylationi952N-linked (GlcNAc...)Sequence analysis1
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
Glycosylationi1045N-linked (GlcNAc...)Sequence analysis1
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
Glycosylationi1407N-linked (GlcNAc...)Sequence analysis1
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 bondi1556InterchainCurated
Disulfide bondi1560InterchainCurated
Glycosylationi1579N-linked (GlcNAc...)Sequence analysis1
Glycosylationi1596N-linked (GlcNAc...)Sequence analysis1
Glycosylationi1678N-linked (GlcNAc...)Sequence analysis1
Glycosylationi1689N-linked (GlcNAc...)Sequence analysis1
Glycosylationi1698N-linked (GlcNAc...)Sequence analysis1
Glycosylationi1717N-linked (GlcNAc...)Sequence analysis1
Glycosylationi1804N-linked (GlcNAc...)Sequence analysis1
Glycosylationi1894N-linked (GlcNAc...)Sequence analysis1
Glycosylationi1898N-linked (GlcNAc...)Sequence analysis1
Glycosylationi1957N-linked (GlcNAc...)Sequence analysis1
Glycosylationi1974N-linked (GlcNAc...)Sequence analysis1
Glycosylationi1991N-linked (GlcNAc...)Sequence analysis1
Glycosylationi2038N-linked (GlcNAc...)Sequence analysis1
Glycosylationi2047N-linked (GlcNAc...)Sequence analysis1
Glycosylationi2094N-linked (GlcNAc...)Sequence analysis1
Glycosylationi2098N-linked (GlcNAc...)Sequence analysis1
Glycosylationi2243N-linked (GlcNAc...)1 Publication1
Glycosylationi2244N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi2271 ↔ 2297By similarity
Glycosylationi2384N-linked (GlcNAc...)Sequence analysis1
Glycosylationi2408N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi2457 ↔ 2481By similarity
Glycosylationi2518N-linked (GlcNAc...)Sequence analysis1
Glycosylationi2619N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi2646 ↔ 2673By similarity
Glycosylationi2729N-linked (GlcNAc...)Sequence analysis1
Glycosylationi2852N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi2860 ↔ 2885By similarity
Glycosylationi2915N-linked (GlcNAc...)Sequence analysis1
Glycosylationi2983N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi3039 ↔ 3070By similarity

Post-translational modificationi

Tyrosine phosphorylated by PKDCC/VLK.1 Publication

Keywords - PTMi

Disulfide bond, Glycoprotein, Phosphoprotein

Proteomic databases

EPDiP25391.
MaxQBiP25391.
PaxDbiP25391.
PeptideAtlasiP25391.
PRIDEiP25391.

PTM databases

iPTMnetiP25391.
PhosphoSitePlusiP25391.

Expressioni

Gene expression databases

BgeeiENSG00000101680.
CleanExiHS_LAMA1.
GenevisibleiP25391. HS.

Organism-specific databases

HPAiCAB010179.
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. 39 interactors.
DIPiDIP-29324N.
IntActiP25391. 26 interactors.
MINTiMINT-6740485.
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 – 1796Sequence analysisAdd BLAST91
Coiled coili1968 – 1989Sequence analysisAdd BLAST22
Coiled coili2088 – 2120Sequence analysisAdd BLAST33

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.

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

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

Family and domain databases

Gene3Di2.60.120.200. 5 hits.
InterProiIPR013320. ConA-like_dom.
IPR000742. EGF-like_dom.
IPR009254. Laminin_aI.
IPR010307. Laminin_domII.
IPR002049. Laminin_EGF.
IPR001791. Laminin_G.
IPR000034. Laminin_IV.
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]
SMARTiSM00181. EGF. 12 hits.
SM00180. EGF_Lam. 17 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

        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

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 rs9950267dbSNPEnsembl.1
Natural variantiVAR_056133559V → I.Corresponds to variant rs16951079dbSNPEnsembl.1
Natural variantiVAR_060785674N → T.2 PublicationsCorresponds to variant rs566655dbSNPEnsembl.1
Natural variantiVAR_0607861340M → V.1 PublicationCorresponds to variant rs662471dbSNPEnsembl.1
Natural variantiVAR_0561341577S → A.Corresponds to variant rs12961939dbSNPEnsembl.1
Natural variantiVAR_0561351591L → V.Corresponds to variant rs596315dbSNPEnsembl.1
Natural variantiVAR_0561361632K → E.Corresponds to variant rs11872364dbSNPEnsembl.1
Natural variantiVAR_0561371682D → V.Corresponds to variant rs16950981dbSNPEnsembl.1
Natural variantiVAR_0607871876A → T.2 PublicationsCorresponds to variant rs11664063dbSNPEnsembl.1
Natural variantiVAR_0607882002K → E.2 PublicationsCorresponds to variant rs607230dbSNPEnsembl.1
Natural variantiVAR_0561382076I → T.Corresponds to variant rs671871dbSNPEnsembl.1
Natural variantiVAR_0613472511L → M.Corresponds to variant rs60009920dbSNPEnsembl.1
Natural variantiVAR_0561392611T → A.Corresponds to variant rs543355dbSNPEnsembl.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

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. 39 interactors.
DIPiDIP-29324N.
IntActiP25391. 26 interactors.
MINTiMINT-6740485.
STRINGi9606.ENSP00000374309.

Chemistry databases

ChEMBLiCHEMBL2364187.

PTM databases

iPTMnetiP25391.
PhosphoSitePlusiP25391.

Polymorphism and mutation databases

BioMutaiLAMA1.
DMDMi281185471.

Proteomic databases

EPDiP25391.
MaxQBiP25391.
PaxDbiP25391.
PeptideAtlasiP25391.
PRIDEiP25391.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi284217.
DisGeNETi284217.
GeneCardsiLAMA1.
H-InvDBHIX0014316.
HGNCiHGNC:6481. LAMA1.
HPAiCAB010179.
HPA032110.
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.
OMAiPCDCAHT.
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.
PROiP25391.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000101680.
CleanExiHS_LAMA1.
GenevisibleiP25391. HS.

Family and domain databases

Gene3Di2.60.120.200. 5 hits.
InterProiIPR013320. ConA-like_dom.
IPR000742. EGF-like_dom.
IPR009254. Laminin_aI.
IPR010307. Laminin_domII.
IPR002049. Laminin_EGF.
IPR001791. Laminin_G.
IPR000034. Laminin_IV.
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]
SMARTiSM00181. EGF. 12 hits.
SM00180. EGF_Lam. 17 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]
ProtoNetiSearch...

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: November 30, 2016
This is version 176 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.