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P24043

- LAMA2_HUMAN

UniProt

P24043 - LAMA2_HUMAN

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Protein

Laminin subunit alpha-2

Gene

LAMA2

Organism
Homo sapiens (Human)
Status
Reviewed - 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

  1. structural molecule activity Source: ProtInc

GO - Biological processi

  1. axon guidance Source: Ensembl
  2. cell adhesion Source: UniProtKB-KW
  3. extracellular matrix organization Source: Reactome
  4. muscle organ development Source: ProtInc
  5. myelination in peripheral nervous system Source: Ensembl
  6. positive regulation of synaptic transmission, cholinergic Source: Ensembl
  7. regulation of cell adhesion Source: InterPro
  8. regulation of cell migration Source: InterPro
  9. regulation of embryonic development Source: InterPro
Complete GO annotation...

Keywords - Biological processi

Cell adhesion

Enzyme and pathway databases

ReactomeiREACT_163874. Non-integrin membrane-ECM interactions.
REACT_163906. ECM proteoglycans.
REACT_169262. Laminin interactions.

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
ProteomesiUP000005640: Chromosome 6

Organism-specific databases

HGNCiHGNC:6482. LAMA2.

Subcellular locationi

GO - Cellular componenti

  1. basement membrane Source: UniProtKB
  2. dendritic spine Source: Ensembl
  3. extracellular region Source: Reactome
  4. extracellular vesicular exosome Source: UniProt
  5. laminin-1 complex Source: InterPro
  6. 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) [MIM:607855]: Characterized by difficulty walking, hypotonia, proximal weakness, hyporeflexia, and white matter hypodensity on MRI.2 Publications
Note: The disease is caused by mutations affecting the gene represented in this entry.
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti527 – 5271C → Y in MDC1A. 1 Publication
VAR_015743
Natural varianti862 – 8621C → R in MDC1A. 1 Publication
VAR_015744
Natural varianti2564 – 25641L → P in MDC1A. 1 Publication
VAR_015745

Keywords - Diseasei

Congenital muscular dystrophy, Disease mutation

Organism-specific databases

MIMi607855. phenotype.
Orphaneti258. Congenital muscular dystrophy type 1A.
PharmGKBiPA30271.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2222Sequence AnalysisAdd
BLAST
Chaini23 – 31223100Laminin subunit alpha-2PRO_0000017056Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi55 – 551N-linked (GlcNAc...)Sequence Analysis
Glycosylationi89 – 891N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi287 ↔ 296By similarity
Disulfide bondi289 ↔ 307By similarity
Glycosylationi303 – 3031N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi309 ↔ 318By similarity
Disulfide bondi321 ↔ 341By similarity
Disulfide bondi344 ↔ 353By similarity
Disulfide bondi346 ↔ 378By similarity
Glycosylationi363 – 3631N-linked (GlcNAc...)1 Publication
Glycosylationi380 – 3801N-linked (GlcNAc...)Sequence Analysis
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
Glycosylationi470 – 4701N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi471 ↔ 486By similarity
Disulfide bondi488 ↔ 497By similarity
Disulfide bondi500 ↔ 515By similarity
Glycosylationi746 – 7461N-linked (GlcNAc...)Sequence Analysis
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
Glycosylationi1061 – 10611N-linked (GlcNAc...)Sequence Analysis
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 bondi1574 – 1574InterchainCurated
Disulfide bondi1578 – 1578InterchainCurated
Glycosylationi1597 – 15971N-linked (GlcNAc...)Sequence Analysis
Glycosylationi1614 – 16141N-linked (GlcNAc...)Sequence Analysis
Glycosylationi1700 – 17001N-linked (GlcNAc...)Sequence Analysis
Glycosylationi1810 – 18101N-linked (GlcNAc...)Sequence Analysis
Glycosylationi1901 – 19011N-linked (GlcNAc...)1 Publication
Glycosylationi1916 – 19161N-linked (GlcNAc...)1 Publication
Glycosylationi1920 – 19201N-linked (GlcNAc...)1 Publication
Glycosylationi2017 – 20171N-linked (GlcNAc...)1 Publication
Glycosylationi2028 – 20281N-linked (GlcNAc...)Sequence Analysis
Glycosylationi2045 – 20451N-linked (GlcNAc...)Sequence Analysis
Glycosylationi2126 – 21261N-linked (GlcNAc...)Sequence Analysis
Glycosylationi2240 – 22401N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi2302 ↔ 2328By similarity
Glycosylationi2360 – 23601N-linked (GlcNAc...)Sequence Analysis
Glycosylationi2435 – 24351N-linked (GlcNAc...)Sequence Analysis
Glycosylationi2478 – 24781N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi2495 ↔ 2521By similarity
Glycosylationi2551 – 25511N-linked (GlcNAc...)Sequence Analysis
Glycosylationi2558 – 25581N-linked (GlcNAc...)Sequence Analysis
Glycosylationi2648 – 26481N-linked (GlcNAc...)1 Publication
Disulfide bondi2683 ↔ 2710By similarity
Glycosylationi2868 – 28681N-linked (GlcNAc...)Sequence Analysis
Glycosylationi2893 – 28931N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi2909 ↔ 2934By similarity

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

PaxDbiP24043.
PRIDEiP24043.

PTM databases

PhosphoSiteiP24043.

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

BgeeiP24043.
CleanExiHS_LAMA2.
GenevestigatoriP24043.

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. 3 interactions.
DIPiDIP-42562N.
IntActiP24043. 4 interactions.
MINTiMINT-2635209.
STRINGi9606.ENSP00000400365.

Structurei

3D structure databases

ProteinModelPortaliP24043.
SMRiP24043. Positions 2939-3120.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini35 – 286252Laminin N-terminalPROSITE-ProRule annotationAdd
BLAST
Domaini287 – 34357Laminin EGF-like 1PROSITE-ProRule annotationAdd
BLAST
Domaini344 – 41370Laminin EGF-like 2PROSITE-ProRule annotationAdd
BLAST
Domaini414 – 46855Laminin EGF-like 3PROSITE-ProRule annotationAdd
BLAST
Domaini469 – 51749Laminin EGF-like 4PROSITE-ProRule annotationAdd
BLAST
Domaini518 – 52710Laminin EGF-like 5; first partPROSITE-ProRule annotation
Domaini531 – 723193Laminin IV type A 1PROSITE-ProRule annotationAdd
BLAST
Domaini724 – 75633Laminin EGF-like 5; second partPROSITE-ProRule annotationAdd
BLAST
Domaini757 – 80650Laminin EGF-like 6PROSITE-ProRule annotationAdd
BLAST
Domaini807 – 86458Laminin EGF-like 7PROSITE-ProRule annotationAdd
BLAST
Domaini865 – 91753Laminin EGF-like 8PROSITE-ProRule annotationAdd
BLAST
Domaini918 – 96649Laminin EGF-like 9PROSITE-ProRule annotationAdd
BLAST
Domaini967 – 101347Laminin EGF-like 10PROSITE-ProRule annotationAdd
BLAST
Domaini1014 – 105946Laminin EGF-like 11PROSITE-ProRule annotationAdd
BLAST
Domaini1060 – 110546Laminin EGF-like 12PROSITE-ProRule annotationAdd
BLAST
Domaini1106 – 116560Laminin EGF-like 13PROSITE-ProRule annotationAdd
BLAST
Domaini1166 – 117510Laminin EGF-like 14; first partPROSITE-ProRule annotation
Domaini1176 – 1379204Laminin IV type A 2PROSITE-ProRule annotationAdd
BLAST
Domaini1380 – 141940Laminin EGF-like 14; second partPROSITE-ProRule annotationAdd
BLAST
Domaini1420 – 146849Laminin EGF-like 15PROSITE-ProRule annotationAdd
BLAST
Domaini1469 – 152658Laminin EGF-like 16PROSITE-ProRule annotationAdd
BLAST
Domaini1527 – 157347Laminin EGF-like 17PROSITE-ProRule annotationAdd
BLAST
Domaini2145 – 2328184Laminin G-like 1PROSITE-ProRule annotationAdd
BLAST
Domaini2340 – 2521182Laminin G-like 2PROSITE-ProRule annotationAdd
BLAST
Domaini2526 – 2710185Laminin G-like 3PROSITE-ProRule annotationAdd
BLAST
Domaini2763 – 2934172Laminin G-like 4PROSITE-ProRule annotationAdd
BLAST
Domaini2939 – 3110172Laminin G-like 5PROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1574 – 2144571Domain II and IAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili1630 – 2150521Sequence AnalysisAdd
BLAST

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

eggNOGiCOG0419.
GeneTreeiENSGT00760000119121.
HOGENOMiHOG000293201.
HOVERGENiHBG052298.
InParanoidiP24043.
KOiK05637.
OMAiHTTTKGI.
OrthoDBiEOG7SR4KJ.
PhylomeDBiP24043.
TreeFamiTF335359.

Family and domain databases

Gene3Di2.60.120.200. 5 hits.
2.60.120.260. 2 hits.
InterProiIPR013320. ConA-like_dom.
IPR002049. EGF_laminin.
IPR008979. Galactose-bd-like.
IPR018031. Laminin_B_subgr.
IPR000034. Laminin_B_type_IV.
IPR010307. Laminin_domII.
IPR001791. Laminin_G.
IPR009254. Laminin_I.
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]
SMARTiSM00180. EGF_Lam. 15 hits.
SM00281. LamB. 2 hits.
SM00282. LamG. 5 hits.
SM00136. LamNT. 1 hit.
[Graphical view]
SUPFAMiSSF49785. SSF49785. 1 hit.
SSF49899. 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 [UniParc]FASTAAdd to Basket

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        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 AAA63215.1 differs from that shown. Reason: Frameshift at position 3098.
The sequence CAA81394.1 differs from that shown. Reason: Frameshift at position 3098.
The sequence AAB18388.1 differs from that shown. Reason: Erroneous gene model prediction.

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti588 – 5881A → R in AAB18388. (PubMed:8910357)Curated
Sequence conflicti1740 – 17401A → D(PubMed:7535762)Curated
Sequence conflicti1827 – 18271Q → G(PubMed:7535762)Curated
Sequence conflicti1981 – 19811A → V in AAA63215. (PubMed:2185464)Curated
Sequence conflicti2437 – 24371S → Y in AAB18388. (PubMed:8910357)Curated
Sequence conflicti2624 – 26241H → R in AAA63215. (PubMed:2185464)Curated
Sequence conflicti2807 – 28071R → A in CAA81394. (PubMed:8294519)Curated
Sequence conflicti2807 – 28071R → A in AAB18388. (PubMed:8910357)Curated
Sequence conflicti2969 – 29691R → A in CAA81394. (PubMed:8294519)Curated
Sequence conflicti2969 – 29691R → A in AAB18388. (PubMed:8910357)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti96 – 961R → S.
Corresponds to variant rs34626728 [ dbSNP | Ensembl ].
VAR_047713
Natural varianti240 – 2401Y → H.
Corresponds to variant rs3778142 [ dbSNP | Ensembl ].
VAR_047714
Natural varianti527 – 5271C → Y in MDC1A. 1 Publication
VAR_015743
Natural varianti545 – 5451L → Q.1 Publication
Corresponds to variant rs118083923 [ dbSNP | Ensembl ].
VAR_004165
Natural varianti619 – 6191R → H.1 Publication
Corresponds to variant rs3816665 [ dbSNP | Ensembl ].
VAR_004166
Natural varianti644 – 6441H → D.
Corresponds to variant rs35879899 [ dbSNP | Ensembl ].
VAR_047715
Natural varianti862 – 8621C → R in MDC1A. 1 Publication
VAR_015744
Natural varianti919 – 9191R → L.1 Publication
Corresponds to variant rs35277491 [ dbSNP | Ensembl ].
VAR_004167
Natural varianti1138 – 11381V → M.
Corresponds to variant rs2306942 [ dbSNP | Ensembl ].
VAR_047716
Natural varianti1160 – 11601P → A in a breast cancer sample; somatic mutation. 1 Publication
VAR_035819
Natural varianti1205 – 12051T → A.
Corresponds to variant rs35889149 [ dbSNP | Ensembl ].
VAR_047717
Natural varianti1561 – 15611K → Q.
Corresponds to variant rs4143752 [ dbSNP | Ensembl ].
VAR_047718
Natural varianti1945 – 19451A → T.
Corresponds to variant rs3828736 [ dbSNP | Ensembl ].
VAR_047719
Natural varianti2564 – 25641L → P in MDC1A. 1 Publication
VAR_015745
Natural varianti2586 – 25861Y → H.1 Publication
VAR_004168
Natural varianti2587 – 25871A → V.3 Publications
Corresponds to variant rs6569605 [ dbSNP | Ensembl ].
VAR_047720
Natural varianti2614 – 26141E → K.1 Publication
VAR_004169
Natural varianti2636 – 26361T → A.
Corresponds to variant rs2244008 [ dbSNP | Ensembl ].
VAR_047721
Natural varianti3029 – 30291T → A.
Corresponds to variant rs34551216 [ dbSNP | Ensembl ].
VAR_047722

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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.
UCSCiuc003qbn.3. human.

Polymorphism databases

DMDMi215274259.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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.
CCDSi CCDS5138.1.
PIRi PX0082. MMHUMH.
RefSeqi NP_000417.2. NM_000426.3.
NP_001073291.1. NM_001079823.1.
UniGenei Hs.200841.

3D structure databases

ProteinModelPortali P24043.
SMRi P24043. Positions 2939-3120.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 110102. 3 interactions.
DIPi DIP-42562N.
IntActi P24043. 4 interactions.
MINTi MINT-2635209.
STRINGi 9606.ENSP00000400365.

Chemistry

ChEMBLi CHEMBL2364187.

PTM databases

PhosphoSitei P24043.

Polymorphism databases

DMDMi 215274259.

Proteomic databases

PaxDbi P24043.
PRIDEi P24043.

Protocols and materials databases

DNASUi 3908.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000421865 ; ENSP00000400365 ; ENSG00000196569 .
GeneIDi 3908.
KEGGi hsa:3908.
UCSCi uc003qbn.3. human.

Organism-specific databases

CTDi 3908.
GeneCardsi GC06P129246.
GeneReviewsi LAMA2.
HGNCi HGNC:6482. LAMA2.
HPAi CAB040310.
MIMi 156225. gene.
607855. phenotype.
neXtProti NX_P24043.
Orphaneti 258. Congenital muscular dystrophy type 1A.
PharmGKBi PA30271.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0419.
GeneTreei ENSGT00760000119121.
HOGENOMi HOG000293201.
HOVERGENi HBG052298.
InParanoidi P24043.
KOi K05637.
OMAi HTTTKGI.
OrthoDBi EOG7SR4KJ.
PhylomeDBi P24043.
TreeFami TF335359.

Enzyme and pathway databases

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

Miscellaneous databases

GeneWikii Laminin,_alpha_2.
GenomeRNAii 3908.
NextBioi 15339.
PROi P24043.
SOURCEi Search...

Gene expression databases

Bgeei P24043.
CleanExi HS_LAMA2.
Genevestigatori P24043.

Family and domain databases

Gene3Di 2.60.120.200. 5 hits.
2.60.120.260. 2 hits.
InterProi IPR013320. ConA-like_dom.
IPR002049. EGF_laminin.
IPR008979. Galactose-bd-like.
IPR018031. Laminin_B_subgr.
IPR000034. Laminin_B_type_IV.
IPR010307. Laminin_domII.
IPR001791. Laminin_G.
IPR009254. Laminin_I.
IPR008211. Laminin_N.
[Graphical view ]
Pfami PF00052. 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 ]
SMARTi SM00180. EGF_Lam. 15 hits.
SM00281. LamB. 2 hits.
SM00282. LamG. 5 hits.
SM00136. LamNT. 1 hit.
[Graphical view ]
SUPFAMi SSF49785. SSF49785. 1 hit.
SSF49899. SSF49899. 5 hits.
PROSITEi PS00022. 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 ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Human laminin M chain (merosin): complete primary structure, chromosomal assignment, and expression of the M and A chain in human fetal tissues."
    Vuolteenaho R., Nissinen M., Sainio K., Byers M., Eddy R., Hirvonen H., Shows T.B., Sariola H., Engvall E., Tryggvason K.
    J. Cell Biol. 124:381-394(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT VAL-2587.
    Tissue: Placenta.
  2. "Structure of the human laminin alpha2-chain gene (LAMA2), which is affected in congenital muscular dystrophy."
    Zhang X., Vuolteenaho R., Tryggvason K.
    J. Biol. Chem. 271:27664-27669(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT VAL-2587.
  3. "The DNA sequence and analysis of human chromosome 6."
    Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D.
    , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.
    Nature 425:805-811(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. "Human laminin M chain: epitope analysis of its monoclonal antibodies by immunoscreening of cDNA clones and tissue expression."
    Hori H., Kanamori T., Mizuta T., Yamaguchi N., Liu Y., Nagai Y.
    J. Biochem. 116:1212-1219(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1360-3122.
  5. "Merosin, a tissue-specific basement membrane protein, is a laminin-like protein."
    Ehrig K., Leivo I., Argraves W.S., Ruoslahti E., Engvall E.
    Proc. Natl. Acad. Sci. U.S.A. 87:3264-3268(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1981-3122, PARTIAL PROTEIN SEQUENCE, VARIANT VAL-2587.
    Tissue: Placenta.
  6. "Human plasma N-glycoproteome analysis by immunoaffinity subtraction, hydrazide chemistry, and mass spectrometry."
    Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E., Moore R.J., Smith R.D.
    J. Proteome Res. 4:2070-2080(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-363.
    Tissue: Plasma.
  7. "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-1901; ASN-1916; ASN-1920; ASN-2017 AND ASN-2648.
    Tissue: Liver.
  8. "Novel single base polymorphisms and rare sequence variants in the laminin 2-chain coding region detected by RNA/SSCP analysis."
    Panicker S.G., Mendell J.T., Chen L., Feng B., Sahenk Z., Marzluf G.A., Amato A.A., Mendell J.R.
    Hum. Mutat. 13:174-174(1999)
    Cited for: VARIANTS GLN-545; HIS-619; LEU-919; HIS-2586 AND LYS-2614.
  9. "Congenital muscular dystrophy with primary partial laminin alpha-2 chain deficiency: molecular study."
    He Y., Jones K.J., Vignier N., Morgan G., Chevallay M., Barois A., Estournet-Mathiaud B., Hori H., Mizuta T., Tome F.M.S., North K.N., Guicheney P.
    Neurology 57:1319-1322(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT MDC1A PRO-2564.
  10. "Clinical and molecular study in congenital muscular dystrophy with partial laminin alpha-2 (LAMA2) deficiency."
    Tezak Z., Prandini P., Boscaro M., Marin A., Devaney J., Marino M., Fanin M., Trevisan C.P., Park J., Tyson W., Finkel R., Garcia C., Angelini C., Hoffman E.P., Pegoraro E.
    Hum. Mutat. 21:103-111(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS MDC1A TYR-527 AND ARG-862.
  11. Cited for: VARIANT [LARGE SCALE ANALYSIS] ALA-1160.

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: October 29, 2014
This is version 160 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

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. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3