Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Laminin subunit alpha-2

Gene

LAMA2

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

  • structural molecule activity Source: ProtInc

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Cell adhesion

Enzyme and pathway databases

BioCyciZFISH:G66-33013-MONOMER.
ReactomeiR-HSA-3000157. Laminin interactions.
R-HSA-3000171. Non-integrin membrane-ECM interactions.
R-HSA-3000178. ECM proteoglycans.
R-HSA-8874081. MET activates PTK2 signaling.
SIGNORiP24043.

Names & Taxonomyi

Protein namesi
Recommended name:
Laminin subunit alpha-2
Alternative name(s):
Laminin M chain
Laminin-12 subunit alpha
Laminin-2 subunit alpha
Laminin-4 subunit alpha
Merosin heavy chain
Gene namesi
Name:LAMA2
Synonyms:LAMM
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 6

Organism-specific databases

HGNCiHGNC:6482. LAMA2.

Subcellular locationi

GO - Cellular componenti

  • basal lamina Source: Ensembl
  • basement membrane Source: UniProtKB
  • dendritic spine Source: Ensembl
  • extracellular exosome Source: UniProtKB
  • extracellular region Source: Reactome
  • sarcolemma Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Basement membrane, Extracellular matrix, Secreted

Pathology & Biotechi

Involvement in diseasei

Merosin-deficient congenital muscular dystrophy 1A (MDC1A)3 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionCharacterized by difficulty walking, hypotonia, proximal weakness, hyporeflexia, and white matter hypodensity on MRI.
See also OMIM:607855
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_015743527C → Y in MDC1A. 1 PublicationCorresponds to variant rs121913574dbSNPEnsembl.1
Natural variantiVAR_015744862C → R in MDC1A. 1 PublicationCorresponds to variant rs121913573dbSNPEnsembl.1
Natural variantiVAR_0157452564L → P in MDC1A. 1 PublicationCorresponds to variant rs121913570dbSNPEnsembl.1
Natural variantiVAR_0765602889G → R in MDC1A. 1 Publication1

Keywords - Diseasei

Congenital muscular dystrophy, Disease mutation

Organism-specific databases

DisGeNETi3908.
MalaCardsiLAMA2.
MIMi607855. phenotype.
OpenTargetsiENSG00000196569.
Orphaneti258. Congenital muscular dystrophy type 1A.
PharmGKBiPA30271.

Chemistry databases

ChEMBLiCHEMBL2364187.

Polymorphism and mutation databases

BioMutaiLAMA2.
DMDMi215274259.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 22Sequence analysisAdd BLAST22
ChainiPRO_000001705623 – 3122Laminin subunit alpha-2Add BLAST3100

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi55N-linked (GlcNAc...)Sequence analysis1
Glycosylationi89N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi287 ↔ 296By similarity
Disulfide bondi289 ↔ 307By similarity
Glycosylationi303N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi309 ↔ 318By similarity
Disulfide bondi321 ↔ 341By similarity
Disulfide bondi344 ↔ 353By similarity
Disulfide bondi346 ↔ 378By similarity
Glycosylationi363N-linked (GlcNAc...)1 Publication1
Glycosylationi380N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi381 ↔ 390By similarity
Disulfide bondi393 ↔ 411By similarity
Disulfide bondi414 ↔ 426By similarity
Disulfide bondi416 ↔ 442By similarity
Disulfide bondi444 ↔ 453By similarity
Disulfide bondi456 ↔ 466By similarity
Disulfide bondi469 ↔ 482By similarity
Glycosylationi470N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi471 ↔ 486By similarity
Disulfide bondi488 ↔ 497By similarity
Disulfide bondi500 ↔ 515By similarity
Glycosylationi746N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi757 ↔ 766By similarity
Disulfide bondi759 ↔ 773By similarity
Disulfide bondi776 ↔ 785By similarity
Disulfide bondi788 ↔ 804By similarity
Disulfide bondi807 ↔ 822By similarity
Disulfide bondi809 ↔ 832By similarity
Disulfide bondi835 ↔ 844By similarity
Disulfide bondi847 ↔ 862By similarity
Disulfide bondi865 ↔ 879By similarity
Disulfide bondi867 ↔ 886By similarity
Disulfide bondi889 ↔ 898By similarity
Disulfide bondi901 ↔ 915By similarity
Disulfide bondi918 ↔ 930By similarity
Disulfide bondi920 ↔ 937By similarity
Disulfide bondi939 ↔ 948By similarity
Disulfide bondi951 ↔ 964By similarity
Disulfide bondi967 ↔ 979By similarity
Disulfide bondi969 ↔ 985By similarity
Disulfide bondi987 ↔ 996By similarity
Disulfide bondi999 ↔ 1011By similarity
Disulfide bondi1014 ↔ 1023By similarity
Disulfide bondi1016 ↔ 1030By similarity
Disulfide bondi1032 ↔ 1041By similarity
Disulfide bondi1044 ↔ 1057By similarity
Disulfide bondi1060 ↔ 1072By similarity
Glycosylationi1061N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi1062 ↔ 1079By similarity
Disulfide bondi1081 ↔ 1090By similarity
Disulfide bondi1093 ↔ 1103By similarity
Disulfide bondi1106 ↔ 1118By similarity
Disulfide bondi1108 ↔ 1134By similarity
Disulfide bondi1136 ↔ 1145By similarity
Disulfide bondi1148 ↔ 1163By similarity
Disulfide bondi1420 ↔ 1429By similarity
Disulfide bondi1422 ↔ 1436By similarity
Disulfide bondi1439 ↔ 1448By similarity
Disulfide bondi1451 ↔ 1466By similarity
Disulfide bondi1469 ↔ 1484By similarity
Disulfide bondi1471 ↔ 1494By similarity
Disulfide bondi1497 ↔ 1506By similarity
Disulfide bondi1509 ↔ 1524By similarity
Disulfide bondi1527 ↔ 1539By similarity
Disulfide bondi1529 ↔ 1546By similarity
Disulfide bondi1548 ↔ 1557By similarity
Disulfide bondi1560 ↔ 1571By similarity
Disulfide bondi1574InterchainCurated
Disulfide bondi1578InterchainCurated
Glycosylationi1597N-linked (GlcNAc...)Sequence analysis1
Glycosylationi1614N-linked (GlcNAc...)Sequence analysis1
Glycosylationi1700N-linked (GlcNAc...)Sequence analysis1
Glycosylationi1810N-linked (GlcNAc...)Sequence analysis1
Glycosylationi1901N-linked (GlcNAc...)1 Publication1
Glycosylationi1916N-linked (GlcNAc...)1 Publication1
Glycosylationi1920N-linked (GlcNAc...)1 Publication1
Glycosylationi2017N-linked (GlcNAc...)1 Publication1
Glycosylationi2028N-linked (GlcNAc...)Sequence analysis1
Glycosylationi2045N-linked (GlcNAc...)Sequence analysis1
Glycosylationi2126N-linked (GlcNAc...)Sequence analysis1
Glycosylationi2240N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi2302 ↔ 2328By similarity
Glycosylationi2360N-linked (GlcNAc...)Sequence analysis1
Glycosylationi2435N-linked (GlcNAc...)Sequence analysis1
Glycosylationi2478N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi2495 ↔ 2521By similarity
Glycosylationi2551N-linked (GlcNAc...)Sequence analysis1
Glycosylationi2558N-linked (GlcNAc...)Sequence analysis1
Glycosylationi2648N-linked (GlcNAc...)1 Publication1
Disulfide bondi2683 ↔ 2710By similarity
Glycosylationi2868N-linked (GlcNAc...)Sequence analysis1
Glycosylationi2893N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi2909 ↔ 2934By similarity

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

EPDiP24043.
PaxDbiP24043.
PeptideAtlasiP24043.
PRIDEiP24043.

PTM databases

iPTMnetiP24043.
PhosphoSitePlusiP24043.

Expressioni

Tissue specificityi

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

Gene expression databases

BgeeiENSG00000196569.
CleanExiHS_LAMA2.
ExpressionAtlasiP24043. baseline and differential.
GenevisibleiP24043. HS.

Organism-specific databases

HPAiCAB040310.

Interactioni

Subunit structurei

Laminin is a complex glycoprotein, consisting of three different polypeptide chains (alpha, beta, gamma), which are bound to each other by disulfide bonds into a cross-shaped molecule comprising one long and three short arms with globules at each end. Alpha-2 is a subunit of laminin-2 (laminin-211 or merosin), laminin-4 (laminin-221 or S-merosin) and laminin-12 (laminin-213). Interacts with FBLN1, FBLN2 and NID2.

Protein-protein interaction databases

BioGridi110102. 6 interactors.
DIPiDIP-42562N.
IntActiP24043. 7 interactors.
MINTiMINT-2635209.
STRINGi9606.ENSP00000400365.

Structurei

Secondary structure

13122
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi1184 – 1186Combined sources3
Beta strandi1197 – 1199Combined sources3
Beta strandi1210 – 1213Combined sources4
Beta strandi1216 – 1220Combined sources5
Helixi1221 – 1230Combined sources10
Beta strandi1232 – 1236Combined sources5
Helixi1239 – 1241Combined sources3
Beta strandi1242 – 1244Combined sources3
Helixi1246 – 1248Combined sources3
Beta strandi1252 – 1265Combined sources14
Turni1267 – 1270Combined sources4
Beta strandi1273 – 1280Combined sources8
Turni1281 – 1283Combined sources3
Beta strandi1285 – 1289Combined sources5
Beta strandi1300 – 1308Combined sources9
Helixi1326 – 1334Combined sources9
Beta strandi1336 – 1342Combined sources7
Beta strandi1346 – 1361Combined sources16

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4YEPX-ray1.19A/B1181-1362[»]
4YEQX-ray3.20U1177-1379[»]
ProteinModelPortaliP24043.
SMRiP24043.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini35 – 286Laminin N-terminalPROSITE-ProRule annotationAdd BLAST252
Domaini287 – 343Laminin EGF-like 1PROSITE-ProRule annotationAdd BLAST57
Domaini344 – 413Laminin EGF-like 2PROSITE-ProRule annotationAdd BLAST70
Domaini414 – 468Laminin EGF-like 3PROSITE-ProRule annotationAdd BLAST55
Domaini469 – 517Laminin EGF-like 4PROSITE-ProRule annotationAdd BLAST49
Domaini518 – 527Laminin EGF-like 5; first partPROSITE-ProRule annotation10
Domaini531 – 723Laminin IV type A 1PROSITE-ProRule annotationAdd BLAST193
Domaini724 – 756Laminin EGF-like 5; second partPROSITE-ProRule annotationAdd BLAST33
Domaini757 – 806Laminin EGF-like 6PROSITE-ProRule annotationAdd BLAST50
Domaini807 – 864Laminin EGF-like 7PROSITE-ProRule annotationAdd BLAST58
Domaini865 – 917Laminin EGF-like 8PROSITE-ProRule annotationAdd BLAST53
Domaini918 – 966Laminin EGF-like 9PROSITE-ProRule annotationAdd BLAST49
Domaini967 – 1013Laminin EGF-like 10PROSITE-ProRule annotationAdd BLAST47
Domaini1014 – 1059Laminin EGF-like 11PROSITE-ProRule annotationAdd BLAST46
Domaini1060 – 1105Laminin EGF-like 12PROSITE-ProRule annotationAdd BLAST46
Domaini1106 – 1165Laminin EGF-like 13PROSITE-ProRule annotationAdd BLAST60
Domaini1166 – 1175Laminin EGF-like 14; first partPROSITE-ProRule annotation10
Domaini1176 – 1379Laminin IV type A 2PROSITE-ProRule annotationAdd BLAST204
Domaini1380 – 1419Laminin EGF-like 14; second partPROSITE-ProRule annotationAdd BLAST40
Domaini1420 – 1468Laminin EGF-like 15PROSITE-ProRule annotationAdd BLAST49
Domaini1469 – 1526Laminin EGF-like 16PROSITE-ProRule annotationAdd BLAST58
Domaini1527 – 1573Laminin EGF-like 17PROSITE-ProRule annotationAdd BLAST47
Domaini2145 – 2328Laminin G-like 1PROSITE-ProRule annotationAdd BLAST184
Domaini2340 – 2521Laminin G-like 2PROSITE-ProRule annotationAdd BLAST182
Domaini2526 – 2710Laminin G-like 3PROSITE-ProRule annotationAdd BLAST185
Domaini2763 – 2934Laminin G-like 4PROSITE-ProRule annotationAdd BLAST172
Domaini2939 – 3110Laminin G-like 5PROSITE-ProRule annotationAdd BLAST172

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni1574 – 2144Domain II and IAdd BLAST571

Coiled coil

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Coiled coili1630 – 2150Sequence analysisAdd BLAST521

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.
InParanoidiP24043.
KOiK05637.
OMAiGYFNFQE.
OrthoDBiEOG091G005L.
PhylomeDBiP24043.
TreeFamiTF335359.

Family and domain databases

Gene3Di2.60.120.200. 5 hits.
2.60.120.260. 2 hits.
InterProiIPR013320. ConA-like_dom.
IPR000742. EGF-like_dom.
IPR008979. Galactose-bd-like.
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. 16 hits.
PF00054. Laminin_G_1. 4 hits.
PF02210. Laminin_G_2. 1 hit.
PF06008. Laminin_I. 1 hit.
PF06009. Laminin_II. 1 hit.
PF00055. Laminin_N. 1 hit.
[Graphical view]
SMARTiSM00181. EGF. 8 hits.
SM00180. EGF_Lam. 16 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. 3 hits.
PS01248. EGF_LAM_1. 14 hits.
PS50027. EGF_LAM_2. 15 hits.
PS50025. LAM_G_DOMAIN. 5 hits.
PS51115. LAMININ_IVA. 2 hits.
PS51117. LAMININ_NTER. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P24043-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPGAAGVLLL LLLSGGLGGV QAQRPQQQRQ SQAHQQRGLF PAVLNLASNA
60 70 80 90 100
LITTNATCGE KGPEMYCKLV EHVPGQPVRN PQCRICNQNS SNPNQRHPIT
110 120 130 140 150
NAIDGKNTWW QSPSIKNGIE YHYVTITLDL QQVFQIAYVI VKAANSPRPG
160 170 180 190 200
NWILERSLDD VEYKPWQYHA VTDTECLTLY NIYPRTGPPS YAKDDEVICT
210 220 230 240 250
SFYSKIHPLE NGEIHISLIN GRPSADDPSP ELLEFTSARY IRLRFQRIRT
260 270 280 290 300
LNADLMMFAH KDPREIDPIV TRRYYYSVKD ISVGGMCICY GHARACPLDP
310 320 330 340 350
ATNKSRCECE HNTCGDSCDQ CCPGFHQKPW RAGTFLTKTE CEACNCHGKA
360 370 380 390 400
EECYYDENVA RRNLSLNIRG KYIGGGVCIN CTQNTAGINC ETCTDGFFRP
410 420 430 440 450
KGVSPNYPRP CQPCHCDPIG SLNEVCVKDE KHARRGLAPG SCHCKTGFGG
460 470 480 490 500
VSCDRCARGY TGYPDCKACN CSGLGSKNED PCFGPCICKE NVEGGDCSRC
510 520 530 540 550
KSGFFNLQED NWKGCDECFC SGVSNRCQSS YWTYGKIQDM SGWYLTDLPG
560 570 580 590 600
RIRVAPQQDD LDSPQQISIS NAEARQALPH SYYWSAPAPY LGNKLPAVGG
610 620 630 640 650
QLTFTISYDL EEEEEDTERV LQLMIILEGN DLSISTAQDE VYLHPSEEHT
660 670 680 690 700
NVLLLKEESF TIHGTHFPVR RKEFMTVLAN LKRVLLQITY SFGMDAIFRL
710 720 730 740 750
SSVNLESAVS YPTDGSIAAA VEVCQCPPGY TGSSCESCWP RHRRVNGTIF
760 770 780 790 800
GGICEPCQCF GHAESCDDVT GECLNCKDHT GGPYCDKCLP GFYGEPTKGT
810 820 830 840 850
SEDCQPCACP LNIPSNNFSP TCHLDRSLGL ICDGCPVGYT GPRCERCAEG
860 870 880 890 900
YFGQPSVPGG SCQPCQCNDN LDFSIPGSCD SLSGSCLICK PGTTGRYCEL
910 920 930 940 950
CADGYFGDAV DAKNCQPCRC NAGGSFSEVC HSQTGQCECR ANVQGQRCDK
960 970 980 990 1000
CKAGTFGLQS ARGCVPCNCN SFGSKSFDCE ESGQCWCQPG VTGKKCDRCA
1010 1020 1030 1040 1050
HGYFNFQEGG CTACECSHLG NNCDPKTGRC ICPPNTIGEK CSKCAPNTWG
1060 1070 1080 1090 1100
HSITTGCKAC NCSTVGSLDF QCNVNTGQCN CHPKFSGAKC TECSRGHWNY
1110 1120 1130 1140 1150
PRCNLCDCFL PGTDATTCDS ETKKCSCSDQ TGQCTCKVNV EGIHCDRCRP
1160 1170 1180 1190 1200
GKFGLDAKNP LGCSSCYCFG TTTQCSEAKG LIRTWVTLKA EQTILPLVDE
1210 1220 1230 1240 1250
ALQHTTTKGI VFQHPEIVAH MDLMREDLHL EPFYWKLPEQ FEGKKLMAYG
1260 1270 1280 1290 1300
GKLKYAIYFE AREETGFSTY NPQVIIRGGT PTHARIIVRH MAAPLIGQLT
1310 1320 1330 1340 1350
RHEIEMTEKE WKYYGDDPRV HRTVTREDFL DILYDIHYIL IKATYGNFMR
1360 1370 1380 1390 1400
QSRISEISME VAEQGRGTTM TPPADLIEKC DCPLGYSGLS CEACLPGFYR
1410 1420 1430 1440 1450
LRSQPGGRTP GPTLGTCVPC QCNGHSSLCD PETSICQNCQ HHTAGDFCER
1460 1470 1480 1490 1500
CALGYYGIVK GLPNDCQQCA CPLISSSNNF SPSCVAEGLD DYRCTACPRG
1510 1520 1530 1540 1550
YEGQYCERCA PGYTGSPGNP GGSCQECECD PYGSLPVPCD PVTGFCTCRP
1560 1570 1580 1590 1600
GATGRKCDGC KHWHAREGWE CVFCGDECTG LLLGDLARLE QMVMSINLTG
1610 1620 1630 1640 1650
PLPAPYKMLY GLENMTQELK HLLSPQRAPE RLIQLAEGNL NTLVTEMNEL
1660 1670 1680 1690 1700
LTRATKVTAD GEQTGQDAER TNTRAKSLGE FIKELARDAE AVNEKAIKLN
1710 1720 1730 1740 1750
ETLGTRDEAF ERNLEGLQKE IDQMIKELRR KNLETQKEIA EDELVAAEAL
1760 1770 1780 1790 1800
LKKVKKLFGE SRGENEEMEK DLREKLADYK NKVDDAWDLL REATDKIREA
1810 1820 1830 1840 1850
NRLFAVNQKN MTALEKKKEA VESGKRQIEN TLKEGNDILD EANRLADEIN
1860 1870 1880 1890 1900
SIIDYVEDIQ TKLPPMSEEL NDKIDDLSQE IKDRKLAEKV SQAESHAAQL
1910 1920 1930 1940 1950
NDSSAVLDGI LDEAKNISFN ATAAFKAYSN IKDYIDEAEK VAKEAKDLAH
1960 1970 1980 1990 2000
EATKLATGPR GLLKEDAKGC LQKSFRILNE AKKLANDVKE NEDHLNGLKT
2010 2020 2030 2040 2050
RIENADARNG DLLRTLNDTL GKLSAIPNDT AAKLQAVKDK ARQANDTAKD
2060 2070 2080 2090 2100
VLAQITELHQ NLDGLKKNYN KLADSVAKTN AVVKDPSKNK IIADADATVK
2110 2120 2130 2140 2150
NLEQEADRLI DKLKPIKELE DNLKKNISEI KELINQARKQ ANSIKVSVSS
2160 2170 2180 2190 2200
GGDCIRTYKP EIKKGSYNNI VVNVKTAVAD NLLFYLGSAK FIDFLAIEMR
2210 2220 2230 2240 2250
KGKVSFLWDV GSGVGRVEYP DLTIDDSYWY RIVASRTGRN GTISVRALDG
2260 2270 2280 2290 2300
PKASIVPSTH HSTSPPGYTI LDVDANAMLF VGGLTGKLKK ADAVRVITFT
2310 2320 2330 2340 2350
GCMGETYFDN KPIGLWNFRE KEGDCKGCTV SPQVEDSEGT IQFDGEGYAL
2360 2370 2380 2390 2400
VSRPIRWYPN ISTVMFKFRT FSSSALLMYL ATRDLRDFMS VELTDGHIKV
2410 2420 2430 2440 2450
SYDLGSGMAS VVSNQNHNDG KWKSFTLSRI QKQANISIVD IDTNQEENIA
2460 2470 2480 2490 2500
TSSSGNNFGL DLKADDKIYF GGLPTLRNLS MKARPEVNLK KYSGCLKDIE
2510 2520 2530 2540 2550
ISRTPYNILS SPDYVGVTKG CSLENVYTVS FPKPGFVELS PVPIDVGTEI
2560 2570 2580 2590 2600
NLSFSTKNES GIILLGSGGT PAPPRRKRRQ TGQAYYAILL NRGRLEVHLS
2610 2620 2630 2640 2650
TGARTMRKIV IRPEPNLFHD GREHSVHVER TRGIFTVQVD ENRRYMQNLT
2660 2670 2680 2690 2700
VEQPIEVKKL FVGGAPPEFQ PSPLRNIPPF EGCIWNLVIN SVPMDFARPV
2710 2720 2730 2740 2750
SFKNADIGRC AHQKLREDED GAAPAEIVIQ PEPVPTPAFP TPTPVLTHGP
2760 2770 2780 2790 2800
CAAESEPALL IGSKQFGLSR NSHIAIAFDD TKVKNRLTIE LEVRTEAESG
2810 2820 2830 2840 2850
LLFYMARINH ADFATVQLRN GLPYFSYDLG SGDTHTMIPT KINDGQWHKI
2860 2870 2880 2890 2900
KIMRSKQEGI LYVDGASNRT ISPKKADILD VVGMLYVGGL PINYTTRRIG
2910 2920 2930 2940 2950
PVTYSIDGCV RNLHMAEAPA DLEQPTSSFH VGTCFANAQR GTYFDGTGFA
2960 2970 2980 2990 3000
KAVGGFKVGL DLLVEFEFRT TTTTGVLLGI SSQKMDGMGI EMIDEKLMFH
3010 3020 3030 3040 3050
VDNGAGRFTA VYDAGVPGHL CDGQWHKVTA NKIKHRIELT VDGNQVEAQS
3060 3070 3080 3090 3100
PNPASTSADT NDPVFVGGFP DDLKQFGLTT SIPFRGCIRS LKLTKGTGKP
3110 3120
LEVNFAKALE LRGVQPVSCP AN
Length:3,122
Mass (Da):343,905
Last modified:November 25, 2008 - v4
Checksum:iE2C13BD6FC1B7BAC
GO

Sequence cautioni

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

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti588A → R in AAB18388 (PubMed:8910357).Curated1
Sequence conflicti1740A → D (PubMed:7535762).Curated1
Sequence conflicti1827Q → G (PubMed:7535762).Curated1
Sequence conflicti1981A → V in AAA63215 (PubMed:2185464).Curated1
Sequence conflicti2437S → Y in AAB18388 (PubMed:8910357).Curated1
Sequence conflicti2624H → R in AAA63215 (PubMed:2185464).Curated1
Sequence conflicti2807R → A in CAA81394 (PubMed:8294519).Curated1
Sequence conflicti2807R → A in AAB18388 (PubMed:8910357).Curated1
Sequence conflicti2969R → A in CAA81394 (PubMed:8294519).Curated1
Sequence conflicti2969R → A in AAB18388 (PubMed:8910357).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_04771396R → S.Corresponds to variant rs34626728dbSNPEnsembl.1
Natural variantiVAR_047714240Y → H.Corresponds to variant rs3778142dbSNPEnsembl.1
Natural variantiVAR_015743527C → Y in MDC1A. 1 PublicationCorresponds to variant rs121913574dbSNPEnsembl.1
Natural variantiVAR_004165545L → Q.1 PublicationCorresponds to variant rs118083923dbSNPEnsembl.1
Natural variantiVAR_004166619R → H.1 PublicationCorresponds to variant rs3816665dbSNPEnsembl.1
Natural variantiVAR_047715644H → D.Corresponds to variant rs35879899dbSNPEnsembl.1
Natural variantiVAR_015744862C → R in MDC1A. 1 PublicationCorresponds to variant rs121913573dbSNPEnsembl.1
Natural variantiVAR_004167919R → L.1 PublicationCorresponds to variant rs35277491dbSNPEnsembl.1
Natural variantiVAR_0477161138V → M.Corresponds to variant rs2306942dbSNPEnsembl.1
Natural variantiVAR_0358191160P → A in a breast cancer sample; somatic mutation. 1 Publication1
Natural variantiVAR_0477171205T → A.Corresponds to variant rs35889149dbSNPEnsembl.1
Natural variantiVAR_0477181561K → Q.Corresponds to variant rs4143752dbSNPEnsembl.1
Natural variantiVAR_0477191945A → T.Corresponds to variant rs3828736dbSNPEnsembl.1
Natural variantiVAR_0157452564L → P in MDC1A. 1 PublicationCorresponds to variant rs121913570dbSNPEnsembl.1
Natural variantiVAR_0041682586Y → H.1 Publication1
Natural variantiVAR_0477202587A → V.3 PublicationsCorresponds to variant rs6569605dbSNPEnsembl.1
Natural variantiVAR_0041692614E → K.1 Publication1
Natural variantiVAR_0477212636T → A.Corresponds to variant rs2244008dbSNPEnsembl.1
Natural variantiVAR_0765602889G → R in MDC1A. 1 Publication1
Natural variantiVAR_0477223029T → A.Corresponds to variant rs34551216dbSNPEnsembl.1

Sequence databases

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

Genome annotation databases

EnsembliENST00000421865; ENSP00000400365; ENSG00000196569.
GeneIDi3908.
KEGGihsa:3908.
UCSCiuc063rgy.1. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

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

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4YEPX-ray1.19A/B1181-1362[»]
4YEQX-ray3.20U1177-1379[»]
ProteinModelPortaliP24043.
SMRiP24043.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi110102. 6 interactors.
DIPiDIP-42562N.
IntActiP24043. 7 interactors.
MINTiMINT-2635209.
STRINGi9606.ENSP00000400365.

Chemistry databases

ChEMBLiCHEMBL2364187.

PTM databases

iPTMnetiP24043.
PhosphoSitePlusiP24043.

Polymorphism and mutation databases

BioMutaiLAMA2.
DMDMi215274259.

Proteomic databases

EPDiP24043.
PaxDbiP24043.
PeptideAtlasiP24043.
PRIDEiP24043.

Protocols and materials databases

DNASUi3908.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000421865; ENSP00000400365; ENSG00000196569.
GeneIDi3908.
KEGGihsa:3908.
UCSCiuc063rgy.1. human.

Organism-specific databases

CTDi3908.
DisGeNETi3908.
GeneCardsiLAMA2.
GeneReviewsiLAMA2.
HGNCiHGNC:6482. LAMA2.
HPAiCAB040310.
MalaCardsiLAMA2.
MIMi156225. gene.
607855. phenotype.
neXtProtiNX_P24043.
OpenTargetsiENSG00000196569.
Orphaneti258. Congenital muscular dystrophy type 1A.
PharmGKBiPA30271.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG1836. Eukaryota.
ENOG410XRDC. LUCA.
GeneTreeiENSGT00780000121851.
HOGENOMiHOG000293201.
HOVERGENiHBG052298.
InParanoidiP24043.
KOiK05637.
OMAiGYFNFQE.
OrthoDBiEOG091G005L.
PhylomeDBiP24043.
TreeFamiTF335359.

Enzyme and pathway databases

BioCyciZFISH:G66-33013-MONOMER.
ReactomeiR-HSA-3000157. Laminin interactions.
R-HSA-3000171. Non-integrin membrane-ECM interactions.
R-HSA-3000178. ECM proteoglycans.
R-HSA-8874081. MET activates PTK2 signaling.
SIGNORiP24043.

Miscellaneous databases

ChiTaRSiLAMA2. human.
GeneWikiiLaminin,_alpha_2.
GenomeRNAii3908.
PROiP24043.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000196569.
CleanExiHS_LAMA2.
ExpressionAtlasiP24043. baseline and differential.
GenevisibleiP24043. HS.

Family and domain databases

Gene3Di2.60.120.200. 5 hits.
2.60.120.260. 2 hits.
InterProiIPR013320. ConA-like_dom.
IPR000742. EGF-like_dom.
IPR008979. Galactose-bd-like.
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. 16 hits.
PF00054. Laminin_G_1. 4 hits.
PF02210. Laminin_G_2. 1 hit.
PF06008. Laminin_I. 1 hit.
PF06009. Laminin_II. 1 hit.
PF00055. Laminin_N. 1 hit.
[Graphical view]
SMARTiSM00181. EGF. 8 hits.
SM00180. EGF_Lam. 16 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. 3 hits.
PS01248. EGF_LAM_1. 14 hits.
PS50027. EGF_LAM_2. 15 hits.
PS50025. LAM_G_DOMAIN. 5 hits.
PS51115. LAMININ_IVA. 2 hits.
PS51117. LAMININ_NTER. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiLAMA2_HUMAN
AccessioniPrimary (citable) accession number: P24043
Secondary accession number(s): Q14736, Q5VUM2, Q93022
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 1, 1992
Last sequence update: November 25, 2008
Last modified: November 30, 2016
This is version 181 of the entry and version 4 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 6
    Human chromosome 6: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. 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.