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P24043 (LAMA2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 157. Feed History...

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

Names and origin

Protein namesRecommended 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 names
Name:LAMA2
Synonyms:LAMM
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length3122 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Binding to cells via a high affinity receptor, laminin is thought to mediate the attachment, migration and organization of cells into tissues during embryonic development by interacting with other extracellular matrix components.

Subunit structure

Laminin is a complex glycoprotein, consisting of three different polypeptide chains (alpha, beta, gamma), which are bound to each other by disulfide bonds into a cross-shaped molecule comprising one long and three short arms with globules at each end. Alpha-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.

Subcellular location

Secretedextracellular spaceextracellular matrixbasement membrane. Note: Major component.

Tissue specificity

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.

Domain

The alpha-helical domains I and II are thought to interact with other laminin chains to form a coiled coil structure.

Domains VI, IV and G are globular.

Involvement in disease

Merosin-deficient congenital muscular dystrophy 1A (MDC1A) [MIM:607855]: Characterized by difficulty walking, hypotonia, proximal weakness, hyporeflexia, and white matter hypodensity on MRI.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.10 Ref.11

Sequence similarities

Contains 17 laminin EGF-like domains.

Contains 5 laminin G-like domains.

Contains 2 laminin IV type A domains.

Contains 1 laminin N-terminal domain.

Sequence caution

The sequence AAA63215.1 differs from that shown. Reason: Frameshift at position 3098.

The sequence AAB18388.1 differs from that shown. Reason: Erroneous gene model prediction.

The sequence CAA81394.1 differs from that shown. Reason: Frameshift at position 3098.

Ontologies

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

Inferred from electronic annotation. Source: Ensembl

cell adhesion

Inferred from electronic annotation. Source: UniProtKB-KW

extracellular matrix organization

Traceable author statement. Source: Reactome

muscle organ development

Traceable author statement PubMed 7550355. Source: ProtInc

myelination in peripheral nervous system

Inferred from electronic annotation. Source: Ensembl

positive regulation of synaptic transmission, cholinergic

Inferred from electronic annotation. Source: Ensembl

regulation of cell adhesion

Inferred from electronic annotation. Source: InterPro

regulation of cell migration

Inferred from electronic annotation. Source: InterPro

regulation of embryonic development

Inferred from electronic annotation. Source: InterPro

   Cellular_componentbasement membrane

Inferred from direct assay PubMed 14557481PubMed 2099832. Source: UniProtKB

dendritic spine

Inferred from electronic annotation. Source: Ensembl

extracellular region

Traceable author statement. Source: Reactome

laminin-1 complex

Inferred from electronic annotation. Source: InterPro

sarcolemma

Inferred from electronic annotation. Source: Ensembl

   Molecular_functionstructural molecule activity

Traceable author statement Ref.5. Source: ProtInc

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2222 Potential
Chain23 – 31223100Laminin subunit alpha-2
PRO_0000017056

Regions

Domain35 – 286252Laminin N-terminal
Domain287 – 34357Laminin EGF-like 1
Domain344 – 41370Laminin EGF-like 2
Domain414 – 46855Laminin EGF-like 3
Domain469 – 51749Laminin EGF-like 4
Domain518 – 52710Laminin EGF-like 5; first part
Domain531 – 723193Laminin IV type A 1
Domain724 – 75633Laminin EGF-like 5; second part
Domain757 – 80650Laminin EGF-like 6
Domain807 – 86458Laminin EGF-like 7
Domain865 – 91753Laminin EGF-like 8
Domain918 – 96649Laminin EGF-like 9
Domain967 – 101347Laminin EGF-like 10
Domain1014 – 105946Laminin EGF-like 11
Domain1060 – 110546Laminin EGF-like 12
Domain1106 – 116560Laminin EGF-like 13
Domain1166 – 117510Laminin EGF-like 14; first part
Domain1176 – 1379204Laminin IV type A 2
Domain1380 – 141940Laminin EGF-like 14; second part
Domain1420 – 146849Laminin EGF-like 15
Domain1469 – 152658Laminin EGF-like 16
Domain1527 – 157347Laminin EGF-like 17
Domain2145 – 2328184Laminin G-like 1
Domain2340 – 2521182Laminin G-like 2
Domain2526 – 2710185Laminin G-like 3
Domain2763 – 2934172Laminin G-like 4
Domain2939 – 3110172Laminin G-like 5
Region1574 – 2144571Domain II and I
Coiled coil1630 – 2150521 Potential

Amino acid modifications

Glycosylation551N-linked (GlcNAc...) Potential
Glycosylation891N-linked (GlcNAc...) Potential
Glycosylation3031N-linked (GlcNAc...) Potential
Glycosylation3631N-linked (GlcNAc...) Ref.6
Glycosylation3801N-linked (GlcNAc...) Potential
Glycosylation4701N-linked (GlcNAc...) Potential
Glycosylation7461N-linked (GlcNAc...) Potential
Glycosylation10611N-linked (GlcNAc...) Potential
Glycosylation15971N-linked (GlcNAc...) Potential
Glycosylation16141N-linked (GlcNAc...) Potential
Glycosylation17001N-linked (GlcNAc...) Potential
Glycosylation18101N-linked (GlcNAc...) Potential
Glycosylation19011N-linked (GlcNAc...) Ref.7
Glycosylation19161N-linked (GlcNAc...) Ref.7
Glycosylation19201N-linked (GlcNAc...) Ref.7
Glycosylation20171N-linked (GlcNAc...) Ref.7
Glycosylation20281N-linked (GlcNAc...) Potential
Glycosylation20451N-linked (GlcNAc...) Potential
Glycosylation21261N-linked (GlcNAc...) Potential
Glycosylation22401N-linked (GlcNAc...) Potential
Glycosylation23601N-linked (GlcNAc...) Potential
Glycosylation24351N-linked (GlcNAc...) Potential
Glycosylation24781N-linked (GlcNAc...) Potential
Glycosylation25511N-linked (GlcNAc...) Potential
Glycosylation25581N-linked (GlcNAc...) Potential
Glycosylation26481N-linked (GlcNAc...) Ref.7
Glycosylation28681N-linked (GlcNAc...) Potential
Glycosylation28931N-linked (GlcNAc...) Potential
Disulfide bond287 ↔ 296 By similarity
Disulfide bond289 ↔ 307 By similarity
Disulfide bond309 ↔ 318 By similarity
Disulfide bond321 ↔ 341 By similarity
Disulfide bond344 ↔ 353 By similarity
Disulfide bond346 ↔ 378 By similarity
Disulfide bond381 ↔ 390 By similarity
Disulfide bond393 ↔ 411 By similarity
Disulfide bond414 ↔ 426 By similarity
Disulfide bond416 ↔ 442 By similarity
Disulfide bond444 ↔ 453 By similarity
Disulfide bond456 ↔ 466 By similarity
Disulfide bond469 ↔ 482 By similarity
Disulfide bond471 ↔ 486 By similarity
Disulfide bond488 ↔ 497 By similarity
Disulfide bond500 ↔ 515 By similarity
Disulfide bond757 ↔ 766 By similarity
Disulfide bond759 ↔ 773 By similarity
Disulfide bond776 ↔ 785 By similarity
Disulfide bond788 ↔ 804 By similarity
Disulfide bond807 ↔ 822 By similarity
Disulfide bond809 ↔ 832 By similarity
Disulfide bond835 ↔ 844 By similarity
Disulfide bond847 ↔ 862 By similarity
Disulfide bond865 ↔ 879 By similarity
Disulfide bond867 ↔ 886 By similarity
Disulfide bond889 ↔ 898 By similarity
Disulfide bond901 ↔ 915 By similarity
Disulfide bond918 ↔ 930 By similarity
Disulfide bond920 ↔ 937 By similarity
Disulfide bond939 ↔ 948 By similarity
Disulfide bond951 ↔ 964 By similarity
Disulfide bond967 ↔ 979 By similarity
Disulfide bond969 ↔ 985 By similarity
Disulfide bond987 ↔ 996 By similarity
Disulfide bond999 ↔ 1011 By similarity
Disulfide bond1014 ↔ 1023 By similarity
Disulfide bond1016 ↔ 1030 By similarity
Disulfide bond1032 ↔ 1041 By similarity
Disulfide bond1044 ↔ 1057 By similarity
Disulfide bond1060 ↔ 1072 By similarity
Disulfide bond1062 ↔ 1079 By similarity
Disulfide bond1081 ↔ 1090 By similarity
Disulfide bond1093 ↔ 1103 By similarity
Disulfide bond1106 ↔ 1118 By similarity
Disulfide bond1108 ↔ 1134 By similarity
Disulfide bond1136 ↔ 1145 By similarity
Disulfide bond1148 ↔ 1163 By similarity
Disulfide bond1420 ↔ 1429 By similarity
Disulfide bond1422 ↔ 1436 By similarity
Disulfide bond1439 ↔ 1448 By similarity
Disulfide bond1451 ↔ 1466 By similarity
Disulfide bond1469 ↔ 1484 By similarity
Disulfide bond1471 ↔ 1494 By similarity
Disulfide bond1497 ↔ 1506 By similarity
Disulfide bond1509 ↔ 1524 By similarity
Disulfide bond1527 ↔ 1539 By similarity
Disulfide bond1529 ↔ 1546 By similarity
Disulfide bond1548 ↔ 1557 By similarity
Disulfide bond1560 ↔ 1571 By similarity
Disulfide bond1574Interchain Probable
Disulfide bond1578Interchain Probable
Disulfide bond2302 ↔ 2328 By similarity
Disulfide bond2495 ↔ 2521 By similarity
Disulfide bond2683 ↔ 2710 By similarity
Disulfide bond2909 ↔ 2934 By similarity

Natural variations

Natural variant961R → S.
Corresponds to variant rs34626728 [ dbSNP | Ensembl ].
VAR_047713
Natural variant2401Y → H.
Corresponds to variant rs3778142 [ dbSNP | Ensembl ].
VAR_047714
Natural variant5271C → Y in MDC1A. Ref.11
VAR_015743
Natural variant5451L → Q. Ref.8
Corresponds to variant rs118083923 [ dbSNP | Ensembl ].
VAR_004165
Natural variant6191R → H. Ref.8
Corresponds to variant rs3816665 [ dbSNP | Ensembl ].
VAR_004166
Natural variant6441H → D.
Corresponds to variant rs35879899 [ dbSNP | Ensembl ].
VAR_047715
Natural variant8621C → R in MDC1A. Ref.11
VAR_015744
Natural variant9191R → L. Ref.8
Corresponds to variant rs35277491 [ dbSNP | Ensembl ].
VAR_004167
Natural variant11381V → M.
Corresponds to variant rs2306942 [ dbSNP | Ensembl ].
VAR_047716
Natural variant11601P → A in a breast cancer sample; somatic mutation. Ref.12
VAR_035819
Natural variant12051T → A.
Corresponds to variant rs35889149 [ dbSNP | Ensembl ].
VAR_047717
Natural variant15611K → Q.
Corresponds to variant rs4143752 [ dbSNP | Ensembl ].
VAR_047718
Natural variant19451A → T.
Corresponds to variant rs3828736 [ dbSNP | Ensembl ].
VAR_047719
Natural variant25641L → P in MDC1A. Ref.10
VAR_015745
Natural variant25861Y → H. Ref.8
VAR_004168
Natural variant25871A → V. Ref.1 Ref.2 Ref.5
Corresponds to variant rs6569605 [ dbSNP | Ensembl ].
VAR_047720
Natural variant26141E → K. Ref.8
VAR_004169
Natural variant26361T → A.
Corresponds to variant rs2244008 [ dbSNP | Ensembl ].
VAR_047721
Natural variant30291T → A.
Corresponds to variant rs34551216 [ dbSNP | Ensembl ].
VAR_047722

Experimental info

Sequence conflict5881A → R in AAB18388. Ref.2
Sequence conflict17401A → D Ref.4
Sequence conflict18271Q → G Ref.4
Sequence conflict19811A → V in AAA63215. Ref.5
Sequence conflict24371S → Y in AAB18388. Ref.2
Sequence conflict26241H → R in AAA63215. Ref.5
Sequence conflict28071R → A in CAA81394. Ref.1
Sequence conflict28071R → A in AAB18388. Ref.2
Sequence conflict29691R → A in CAA81394. Ref.1
Sequence conflict29691R → A in AAB18388. Ref.2

Sequences

Sequence LengthMass (Da)Tools
P24043 [UniParc].

Last modified November 25, 2008. Version 4.
Checksum: E2C13BD6FC1B7BAC

FASTA3,122343,905
        10         20         30         40         50         60 
MPGAAGVLLL LLLSGGLGGV QAQRPQQQRQ SQAHQQRGLF PAVLNLASNA LITTNATCGE 

        70         80         90        100        110        120 
KGPEMYCKLV EHVPGQPVRN PQCRICNQNS SNPNQRHPIT NAIDGKNTWW QSPSIKNGIE 

       130        140        150        160        170        180 
YHYVTITLDL QQVFQIAYVI VKAANSPRPG NWILERSLDD VEYKPWQYHA VTDTECLTLY 

       190        200        210        220        230        240 
NIYPRTGPPS YAKDDEVICT SFYSKIHPLE NGEIHISLIN GRPSADDPSP ELLEFTSARY 

       250        260        270        280        290        300 
IRLRFQRIRT LNADLMMFAH KDPREIDPIV TRRYYYSVKD ISVGGMCICY GHARACPLDP 

       310        320        330        340        350        360 
ATNKSRCECE HNTCGDSCDQ CCPGFHQKPW RAGTFLTKTE CEACNCHGKA EECYYDENVA 

       370        380        390        400        410        420 
RRNLSLNIRG KYIGGGVCIN CTQNTAGINC ETCTDGFFRP KGVSPNYPRP CQPCHCDPIG 

       430        440        450        460        470        480 
SLNEVCVKDE KHARRGLAPG SCHCKTGFGG VSCDRCARGY TGYPDCKACN CSGLGSKNED 

       490        500        510        520        530        540 
PCFGPCICKE NVEGGDCSRC KSGFFNLQED NWKGCDECFC SGVSNRCQSS YWTYGKIQDM 

       550        560        570        580        590        600 
SGWYLTDLPG RIRVAPQQDD LDSPQQISIS NAEARQALPH SYYWSAPAPY LGNKLPAVGG 

       610        620        630        640        650        660 
QLTFTISYDL EEEEEDTERV LQLMIILEGN DLSISTAQDE VYLHPSEEHT NVLLLKEESF 

       670        680        690        700        710        720 
TIHGTHFPVR RKEFMTVLAN LKRVLLQITY SFGMDAIFRL SSVNLESAVS YPTDGSIAAA 

       730        740        750        760        770        780 
VEVCQCPPGY TGSSCESCWP RHRRVNGTIF GGICEPCQCF GHAESCDDVT GECLNCKDHT 

       790        800        810        820        830        840 
GGPYCDKCLP GFYGEPTKGT SEDCQPCACP LNIPSNNFSP TCHLDRSLGL ICDGCPVGYT 

       850        860        870        880        890        900 
GPRCERCAEG YFGQPSVPGG SCQPCQCNDN LDFSIPGSCD SLSGSCLICK PGTTGRYCEL 

       910        920        930        940        950        960 
CADGYFGDAV DAKNCQPCRC NAGGSFSEVC HSQTGQCECR ANVQGQRCDK CKAGTFGLQS 

       970        980        990       1000       1010       1020 
ARGCVPCNCN SFGSKSFDCE ESGQCWCQPG VTGKKCDRCA HGYFNFQEGG CTACECSHLG 

      1030       1040       1050       1060       1070       1080 
NNCDPKTGRC ICPPNTIGEK CSKCAPNTWG HSITTGCKAC NCSTVGSLDF QCNVNTGQCN 

      1090       1100       1110       1120       1130       1140 
CHPKFSGAKC TECSRGHWNY PRCNLCDCFL PGTDATTCDS ETKKCSCSDQ TGQCTCKVNV 

      1150       1160       1170       1180       1190       1200 
EGIHCDRCRP GKFGLDAKNP LGCSSCYCFG TTTQCSEAKG LIRTWVTLKA EQTILPLVDE 

      1210       1220       1230       1240       1250       1260 
ALQHTTTKGI VFQHPEIVAH MDLMREDLHL EPFYWKLPEQ FEGKKLMAYG GKLKYAIYFE 

      1270       1280       1290       1300       1310       1320 
AREETGFSTY NPQVIIRGGT PTHARIIVRH MAAPLIGQLT RHEIEMTEKE WKYYGDDPRV 

      1330       1340       1350       1360       1370       1380 
HRTVTREDFL DILYDIHYIL IKATYGNFMR QSRISEISME VAEQGRGTTM TPPADLIEKC 

      1390       1400       1410       1420       1430       1440 
DCPLGYSGLS CEACLPGFYR LRSQPGGRTP GPTLGTCVPC QCNGHSSLCD PETSICQNCQ 

      1450       1460       1470       1480       1490       1500 
HHTAGDFCER CALGYYGIVK GLPNDCQQCA CPLISSSNNF SPSCVAEGLD DYRCTACPRG 

      1510       1520       1530       1540       1550       1560 
YEGQYCERCA PGYTGSPGNP GGSCQECECD PYGSLPVPCD PVTGFCTCRP GATGRKCDGC 

      1570       1580       1590       1600       1610       1620 
KHWHAREGWE CVFCGDECTG LLLGDLARLE QMVMSINLTG PLPAPYKMLY GLENMTQELK 

      1630       1640       1650       1660       1670       1680 
HLLSPQRAPE RLIQLAEGNL NTLVTEMNEL LTRATKVTAD GEQTGQDAER TNTRAKSLGE 

      1690       1700       1710       1720       1730       1740 
FIKELARDAE AVNEKAIKLN ETLGTRDEAF ERNLEGLQKE IDQMIKELRR KNLETQKEIA 

      1750       1760       1770       1780       1790       1800 
EDELVAAEAL LKKVKKLFGE SRGENEEMEK DLREKLADYK NKVDDAWDLL REATDKIREA 

      1810       1820       1830       1840       1850       1860 
NRLFAVNQKN MTALEKKKEA VESGKRQIEN TLKEGNDILD EANRLADEIN SIIDYVEDIQ 

      1870       1880       1890       1900       1910       1920 
TKLPPMSEEL NDKIDDLSQE IKDRKLAEKV SQAESHAAQL NDSSAVLDGI LDEAKNISFN 

      1930       1940       1950       1960       1970       1980 
ATAAFKAYSN IKDYIDEAEK VAKEAKDLAH EATKLATGPR GLLKEDAKGC LQKSFRILNE 

      1990       2000       2010       2020       2030       2040 
AKKLANDVKE NEDHLNGLKT RIENADARNG DLLRTLNDTL GKLSAIPNDT AAKLQAVKDK 

      2050       2060       2070       2080       2090       2100 
ARQANDTAKD VLAQITELHQ NLDGLKKNYN KLADSVAKTN AVVKDPSKNK IIADADATVK 

      2110       2120       2130       2140       2150       2160 
NLEQEADRLI DKLKPIKELE DNLKKNISEI KELINQARKQ ANSIKVSVSS GGDCIRTYKP 

      2170       2180       2190       2200       2210       2220 
EIKKGSYNNI VVNVKTAVAD NLLFYLGSAK FIDFLAIEMR KGKVSFLWDV GSGVGRVEYP 

      2230       2240       2250       2260       2270       2280 
DLTIDDSYWY RIVASRTGRN GTISVRALDG PKASIVPSTH HSTSPPGYTI LDVDANAMLF 

      2290       2300       2310       2320       2330       2340 
VGGLTGKLKK ADAVRVITFT GCMGETYFDN KPIGLWNFRE KEGDCKGCTV SPQVEDSEGT 

      2350       2360       2370       2380       2390       2400 
IQFDGEGYAL VSRPIRWYPN ISTVMFKFRT FSSSALLMYL ATRDLRDFMS VELTDGHIKV 

      2410       2420       2430       2440       2450       2460 
SYDLGSGMAS VVSNQNHNDG KWKSFTLSRI QKQANISIVD IDTNQEENIA TSSSGNNFGL 

      2470       2480       2490       2500       2510       2520 
DLKADDKIYF GGLPTLRNLS MKARPEVNLK KYSGCLKDIE ISRTPYNILS SPDYVGVTKG 

      2530       2540       2550       2560       2570       2580 
CSLENVYTVS FPKPGFVELS PVPIDVGTEI NLSFSTKNES GIILLGSGGT PAPPRRKRRQ 

      2590       2600       2610       2620       2630       2640 
TGQAYYAILL NRGRLEVHLS TGARTMRKIV IRPEPNLFHD GREHSVHVER TRGIFTVQVD 

      2650       2660       2670       2680       2690       2700 
ENRRYMQNLT VEQPIEVKKL FVGGAPPEFQ PSPLRNIPPF EGCIWNLVIN SVPMDFARPV 

      2710       2720       2730       2740       2750       2760 
SFKNADIGRC AHQKLREDED GAAPAEIVIQ PEPVPTPAFP TPTPVLTHGP CAAESEPALL 

      2770       2780       2790       2800       2810       2820 
IGSKQFGLSR NSHIAIAFDD TKVKNRLTIE LEVRTEAESG LLFYMARINH ADFATVQLRN 

      2830       2840       2850       2860       2870       2880 
GLPYFSYDLG SGDTHTMIPT KINDGQWHKI KIMRSKQEGI LYVDGASNRT ISPKKADILD 

      2890       2900       2910       2920       2930       2940 
VVGMLYVGGL PINYTTRRIG PVTYSIDGCV RNLHMAEAPA DLEQPTSSFH VGTCFANAQR 

      2950       2960       2970       2980       2990       3000 
GTYFDGTGFA KAVGGFKVGL DLLVEFEFRT TTTTGVLLGI SSQKMDGMGI EMIDEKLMFH 

      3010       3020       3030       3040       3050       3060 
VDNGAGRFTA VYDAGVPGHL CDGQWHKVTA NKIKHRIELT VDGNQVEAQS PNPASTSADT 

      3070       3080       3090       3100       3110       3120 
NDPVFVGGFP DDLKQFGLTT SIPFRGCIRS LKLTKGTGKP LEVNFAKALE LRGVQPVSCP 


AN 

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References

« Hide 'large scale' references
[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. expand/collapse author list , 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]Erratum
Panicker S.G., Mendell J.T., Chen L., Feng B., Sahenk Z., Marzluf G.A., Amato A.A., Mendell J.R.
Hum. Mutat. 13:340-340(1999)
[10]"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.
[11]"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.
[12]"The consensus coding sequences of human breast and colorectal cancers."
Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V. expand/collapse author list , Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., Velculescu V.E.
Science 314:268-274(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT [LARGE SCALE ANALYSIS] ALA-1160.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
Z26653 mRNA. Translation: CAA81394.1. Frameshift.
U66796 expand/collapse EMBL AC list , 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 expand/collapse EMBL AC list , AL356124, AL445439, AL513527, AL590613, AL669984 Genomic DNA. Translation: CAH70492.1.
AL590613 expand/collapse EMBL AC list , AL356124, AL445439, AL513527, AL583853, AL669984 Genomic DNA. Translation: CAH70771.1.
AL445439 expand/collapse EMBL AC list , AL356124, AL513527, AL583853, AL590613, AL669984 Genomic DNA. Translation: CAH72952.1.
AL513527 expand/collapse EMBL AC list , AL356124, AL445439, AL583853, AL590613, AL669984 Genomic DNA. Translation: CAI15185.1.
AL669984 expand/collapse EMBL AC list , AL356124, AL445439, AL513527, AL583853, AL590613 Genomic DNA. Translation: CAI16682.1.
AL356124 expand/collapse EMBL AC list , AL445439, AL513527, AL583853, AL590613, AL669984 Genomic DNA. Translation: CAI22470.1.
AL589927 Genomic DNA. No translation available.
M59832 mRNA. Translation: AAA63215.1. Frameshift.
CCDSCCDS5138.1.
PIRMMHUMH. PX0082.
RefSeqNP_000417.2. NM_000426.3.
NP_001073291.1. NM_001079823.1.
UniGeneHs.200841.

3D structure databases

ProteinModelPortalP24043.
SMRP24043. Positions 2939-3120.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid110102. 3 interactions.
DIPDIP-42562N.
IntActP24043. 3 interactions.
MINTMINT-2635209.
STRING9606.ENSP00000400365.

Chemistry

ChEMBLCHEMBL2364187.

PTM databases

PhosphoSiteP24043.

Polymorphism databases

DMDM215274259.

Proteomic databases

PaxDbP24043.
PRIDEP24043.

Protocols and materials databases

DNASU3908.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000421865; ENSP00000400365; ENSG00000196569.
GeneID3908.
KEGGhsa:3908.
UCSCuc003qbn.3. human.

Organism-specific databases

CTD3908.
GeneCardsGC06P129246.
GeneReviewsLAMA2.
HGNCHGNC:6482. LAMA2.
HPACAB040310.
MIM156225. gene.
607855. phenotype.
neXtProtNX_P24043.
Orphanet258. Congenital muscular dystrophy type 1A.
PharmGKBPA30271.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0419.
HOGENOMHOG000293201.
HOVERGENHBG052298.
KOK05637.
OMAHTTTKGI.
OrthoDBEOG7SR4KJ.
PhylomeDBP24043.
TreeFamTF335359.

Enzyme and pathway databases

ReactomeREACT_118779. Extracellular matrix organization.

Gene expression databases

ArrayExpressP24043.
BgeeP24043.
CleanExHS_LAMA2.
GenevestigatorP24043.

Family and domain databases

Gene3D2.60.120.200. 5 hits.
2.60.120.260. 2 hits.
InterProIPR008985. ConA-like_lec_gl_sf.
IPR013320. ConA-like_subgrp.
IPR002049. EGF_laminin.
IPR008979. Galactose-bd-like.
IPR018031. Laminin_B_subgr.
IPR000034. Laminin_B_type_IV.
IPR001791. Laminin_G.
IPR009254. Laminin_I.
IPR010307. Laminin_II.
IPR008211. Laminin_N.
[Graphical view]
PfamPF00052. Laminin_B. 2 hits.
PF00053. Laminin_EGF. 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]
SMARTSM00180. EGF_Lam. 15 hits.
SM00281. LamB. 2 hits.
SM00282. LamG. 5 hits.
SM00136. LamNT. 1 hit.
[Graphical view]
SUPFAMSSF49785. SSF49785. 1 hit.
SSF49899. SSF49899. 5 hits.
PROSITEPS00022. 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]
ProtoNetSearch...

Other

GeneWikiLaminin,_alpha_2.
GenomeRNAi3908.
NextBio15339.
PROP24043.
SOURCESearch...

Entry information

Entry nameLAMA2_HUMAN
AccessionPrimary (citable) accession number: P24043
Secondary accession number(s): Q14736, Q5VUM2, Q93022
Entry history
Integrated into UniProtKB/Swiss-Prot: March 1, 1992
Last sequence update: November 25, 2008
Last modified: July 9, 2014
This is version 157 of the entry and version 4 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

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

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 6

Human chromosome 6: entries, gene names and cross-references to MIM