SubmitCancel

Skip Header

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

P24043

- LAMA2_HUMAN

UniProt

P24043 - LAMA2_HUMAN

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein
Laminin subunit alpha-2
Gene
LAMA2, LAMM
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
Complete GO annotation...

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.
Note: The disease is caused by mutations affecting the gene represented in this entry.2 Publications
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 – 2222 Reviewed prediction
Add
BLAST
Chaini23 – 31223100Laminin subunit alpha-2
PRO_0000017056Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi55 – 551N-linked (GlcNAc...) Reviewed prediction
Glycosylationi89 – 891N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi287 ↔ 296 By similarity
Disulfide bondi289 ↔ 307 By similarity
Glycosylationi303 – 3031N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi309 ↔ 318 By similarity
Disulfide bondi321 ↔ 341 By similarity
Disulfide bondi344 ↔ 353 By similarity
Disulfide bondi346 ↔ 378 By similarity
Glycosylationi363 – 3631N-linked (GlcNAc...)1 Publication
Glycosylationi380 – 3801N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi381 ↔ 390 By similarity
Disulfide bondi393 ↔ 411 By similarity
Disulfide bondi414 ↔ 426 By similarity
Disulfide bondi416 ↔ 442 By similarity
Disulfide bondi444 ↔ 453 By similarity
Disulfide bondi456 ↔ 466 By similarity
Disulfide bondi469 ↔ 482 By similarity
Glycosylationi470 – 4701N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi471 ↔ 486 By similarity
Disulfide bondi488 ↔ 497 By similarity
Disulfide bondi500 ↔ 515 By similarity
Glycosylationi746 – 7461N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi757 ↔ 766 By similarity
Disulfide bondi759 ↔ 773 By similarity
Disulfide bondi776 ↔ 785 By similarity
Disulfide bondi788 ↔ 804 By similarity
Disulfide bondi807 ↔ 822 By similarity
Disulfide bondi809 ↔ 832 By similarity
Disulfide bondi835 ↔ 844 By similarity
Disulfide bondi847 ↔ 862 By similarity
Disulfide bondi865 ↔ 879 By similarity
Disulfide bondi867 ↔ 886 By similarity
Disulfide bondi889 ↔ 898 By similarity
Disulfide bondi901 ↔ 915 By similarity
Disulfide bondi918 ↔ 930 By similarity
Disulfide bondi920 ↔ 937 By similarity
Disulfide bondi939 ↔ 948 By similarity
Disulfide bondi951 ↔ 964 By similarity
Disulfide bondi967 ↔ 979 By similarity
Disulfide bondi969 ↔ 985 By similarity
Disulfide bondi987 ↔ 996 By similarity
Disulfide bondi999 ↔ 1011 By similarity
Disulfide bondi1014 ↔ 1023 By similarity
Disulfide bondi1016 ↔ 1030 By similarity
Disulfide bondi1032 ↔ 1041 By similarity
Disulfide bondi1044 ↔ 1057 By similarity
Disulfide bondi1060 ↔ 1072 By similarity
Glycosylationi1061 – 10611N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi1062 ↔ 1079 By similarity
Disulfide bondi1081 ↔ 1090 By similarity
Disulfide bondi1093 ↔ 1103 By similarity
Disulfide bondi1106 ↔ 1118 By similarity
Disulfide bondi1108 ↔ 1134 By similarity
Disulfide bondi1136 ↔ 1145 By similarity
Disulfide bondi1148 ↔ 1163 By similarity
Disulfide bondi1420 ↔ 1429 By similarity
Disulfide bondi1422 ↔ 1436 By similarity
Disulfide bondi1439 ↔ 1448 By similarity
Disulfide bondi1451 ↔ 1466 By similarity
Disulfide bondi1469 ↔ 1484 By similarity
Disulfide bondi1471 ↔ 1494 By similarity
Disulfide bondi1497 ↔ 1506 By similarity
Disulfide bondi1509 ↔ 1524 By similarity
Disulfide bondi1527 ↔ 1539 By similarity
Disulfide bondi1529 ↔ 1546 By similarity
Disulfide bondi1548 ↔ 1557 By similarity
Disulfide bondi1560 ↔ 1571 By similarity
Disulfide bondi1574 – 1574Interchain Inferred
Disulfide bondi1578 – 1578Interchain Inferred
Glycosylationi1597 – 15971N-linked (GlcNAc...) Reviewed prediction
Glycosylationi1614 – 16141N-linked (GlcNAc...) Reviewed prediction
Glycosylationi1700 – 17001N-linked (GlcNAc...) Reviewed prediction
Glycosylationi1810 – 18101N-linked (GlcNAc...) Reviewed prediction
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...) Reviewed prediction
Glycosylationi2045 – 20451N-linked (GlcNAc...) Reviewed prediction
Glycosylationi2126 – 21261N-linked (GlcNAc...) Reviewed prediction
Glycosylationi2240 – 22401N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi2302 ↔ 2328 By similarity
Glycosylationi2360 – 23601N-linked (GlcNAc...) Reviewed prediction
Glycosylationi2435 – 24351N-linked (GlcNAc...) Reviewed prediction
Glycosylationi2478 – 24781N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi2495 ↔ 2521 By similarity
Glycosylationi2551 – 25511N-linked (GlcNAc...) Reviewed prediction
Glycosylationi2558 – 25581N-linked (GlcNAc...) Reviewed prediction
Glycosylationi2648 – 26481N-linked (GlcNAc...)1 Publication
Disulfide bondi2683 ↔ 2710 By similarity
Glycosylationi2868 – 28681N-linked (GlcNAc...) Reviewed prediction
Glycosylationi2893 – 28931N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi2909 ↔ 2934 By 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

ArrayExpressiP24043.
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. 3 interactions.
MINTiMINT-2635209.
STRINGi9606.ENSP00000400365.

Structurei

3D structure databases

ProteinModelPortaliP24043.
SMRiP24043. Positions 2939-3120.

Family & Domainsi

Domains and Repeats

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

Region

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

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili1630 – 2150521 Reviewed prediction
Add
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

Keywords - Domaini

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

Phylogenomic databases

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

Family and domain databases

Gene3Di2.60.120.200. 5 hits.
2.60.120.260. 2 hits.
InterProiIPR008985. 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]
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.

P24043-1 [UniParc]FASTAAdd to Basket

« Hide

MPGAAGVLLL LLLSGGLGGV QAQRPQQQRQ SQAHQQRGLF PAVLNLASNA     50
LITTNATCGE KGPEMYCKLV EHVPGQPVRN PQCRICNQNS SNPNQRHPIT 100
NAIDGKNTWW QSPSIKNGIE YHYVTITLDL QQVFQIAYVI VKAANSPRPG 150
NWILERSLDD VEYKPWQYHA VTDTECLTLY NIYPRTGPPS YAKDDEVICT 200
SFYSKIHPLE NGEIHISLIN GRPSADDPSP ELLEFTSARY IRLRFQRIRT 250
LNADLMMFAH KDPREIDPIV TRRYYYSVKD ISVGGMCICY GHARACPLDP 300
ATNKSRCECE HNTCGDSCDQ CCPGFHQKPW RAGTFLTKTE CEACNCHGKA 350
EECYYDENVA RRNLSLNIRG KYIGGGVCIN CTQNTAGINC ETCTDGFFRP 400
KGVSPNYPRP CQPCHCDPIG SLNEVCVKDE KHARRGLAPG SCHCKTGFGG 450
VSCDRCARGY TGYPDCKACN CSGLGSKNED PCFGPCICKE NVEGGDCSRC 500
KSGFFNLQED NWKGCDECFC SGVSNRCQSS YWTYGKIQDM SGWYLTDLPG 550
RIRVAPQQDD LDSPQQISIS NAEARQALPH SYYWSAPAPY LGNKLPAVGG 600
QLTFTISYDL EEEEEDTERV LQLMIILEGN DLSISTAQDE VYLHPSEEHT 650
NVLLLKEESF TIHGTHFPVR RKEFMTVLAN LKRVLLQITY SFGMDAIFRL 700
SSVNLESAVS YPTDGSIAAA VEVCQCPPGY TGSSCESCWP RHRRVNGTIF 750
GGICEPCQCF GHAESCDDVT GECLNCKDHT GGPYCDKCLP GFYGEPTKGT 800
SEDCQPCACP LNIPSNNFSP TCHLDRSLGL ICDGCPVGYT GPRCERCAEG 850
YFGQPSVPGG SCQPCQCNDN LDFSIPGSCD SLSGSCLICK PGTTGRYCEL 900
CADGYFGDAV DAKNCQPCRC NAGGSFSEVC HSQTGQCECR ANVQGQRCDK 950
CKAGTFGLQS ARGCVPCNCN SFGSKSFDCE ESGQCWCQPG VTGKKCDRCA 1000
HGYFNFQEGG CTACECSHLG NNCDPKTGRC ICPPNTIGEK CSKCAPNTWG 1050
HSITTGCKAC NCSTVGSLDF QCNVNTGQCN CHPKFSGAKC TECSRGHWNY 1100
PRCNLCDCFL PGTDATTCDS ETKKCSCSDQ TGQCTCKVNV EGIHCDRCRP 1150
GKFGLDAKNP LGCSSCYCFG TTTQCSEAKG LIRTWVTLKA EQTILPLVDE 1200
ALQHTTTKGI VFQHPEIVAH MDLMREDLHL EPFYWKLPEQ FEGKKLMAYG 1250
GKLKYAIYFE AREETGFSTY NPQVIIRGGT PTHARIIVRH MAAPLIGQLT 1300
RHEIEMTEKE WKYYGDDPRV HRTVTREDFL DILYDIHYIL IKATYGNFMR 1350
QSRISEISME VAEQGRGTTM TPPADLIEKC DCPLGYSGLS CEACLPGFYR 1400
LRSQPGGRTP GPTLGTCVPC QCNGHSSLCD PETSICQNCQ HHTAGDFCER 1450
CALGYYGIVK GLPNDCQQCA CPLISSSNNF SPSCVAEGLD DYRCTACPRG 1500
YEGQYCERCA PGYTGSPGNP GGSCQECECD PYGSLPVPCD PVTGFCTCRP 1550
GATGRKCDGC KHWHAREGWE CVFCGDECTG LLLGDLARLE QMVMSINLTG 1600
PLPAPYKMLY GLENMTQELK HLLSPQRAPE RLIQLAEGNL NTLVTEMNEL 1650
LTRATKVTAD GEQTGQDAER TNTRAKSLGE FIKELARDAE AVNEKAIKLN 1700
ETLGTRDEAF ERNLEGLQKE IDQMIKELRR KNLETQKEIA EDELVAAEAL 1750
LKKVKKLFGE SRGENEEMEK DLREKLADYK NKVDDAWDLL REATDKIREA 1800
NRLFAVNQKN MTALEKKKEA VESGKRQIEN TLKEGNDILD EANRLADEIN 1850
SIIDYVEDIQ TKLPPMSEEL NDKIDDLSQE IKDRKLAEKV SQAESHAAQL 1900
NDSSAVLDGI LDEAKNISFN ATAAFKAYSN IKDYIDEAEK VAKEAKDLAH 1950
EATKLATGPR GLLKEDAKGC LQKSFRILNE AKKLANDVKE NEDHLNGLKT 2000
RIENADARNG DLLRTLNDTL GKLSAIPNDT AAKLQAVKDK ARQANDTAKD 2050
VLAQITELHQ NLDGLKKNYN KLADSVAKTN AVVKDPSKNK IIADADATVK 2100
NLEQEADRLI DKLKPIKELE DNLKKNISEI KELINQARKQ ANSIKVSVSS 2150
GGDCIRTYKP EIKKGSYNNI VVNVKTAVAD NLLFYLGSAK FIDFLAIEMR 2200
KGKVSFLWDV GSGVGRVEYP DLTIDDSYWY RIVASRTGRN GTISVRALDG 2250
PKASIVPSTH HSTSPPGYTI LDVDANAMLF VGGLTGKLKK ADAVRVITFT 2300
GCMGETYFDN KPIGLWNFRE KEGDCKGCTV SPQVEDSEGT IQFDGEGYAL 2350
VSRPIRWYPN ISTVMFKFRT FSSSALLMYL ATRDLRDFMS VELTDGHIKV 2400
SYDLGSGMAS VVSNQNHNDG KWKSFTLSRI QKQANISIVD IDTNQEENIA 2450
TSSSGNNFGL DLKADDKIYF GGLPTLRNLS MKARPEVNLK KYSGCLKDIE 2500
ISRTPYNILS SPDYVGVTKG CSLENVYTVS FPKPGFVELS PVPIDVGTEI 2550
NLSFSTKNES GIILLGSGGT PAPPRRKRRQ TGQAYYAILL NRGRLEVHLS 2600
TGARTMRKIV IRPEPNLFHD GREHSVHVER TRGIFTVQVD ENRRYMQNLT 2650
VEQPIEVKKL FVGGAPPEFQ PSPLRNIPPF EGCIWNLVIN SVPMDFARPV 2700
SFKNADIGRC AHQKLREDED GAAPAEIVIQ PEPVPTPAFP TPTPVLTHGP 2750
CAAESEPALL IGSKQFGLSR NSHIAIAFDD TKVKNRLTIE LEVRTEAESG 2800
LLFYMARINH ADFATVQLRN GLPYFSYDLG SGDTHTMIPT KINDGQWHKI 2850
KIMRSKQEGI LYVDGASNRT ISPKKADILD VVGMLYVGGL PINYTTRRIG 2900
PVTYSIDGCV RNLHMAEAPA DLEQPTSSFH VGTCFANAQR GTYFDGTGFA 2950
KAVGGFKVGL DLLVEFEFRT TTTTGVLLGI SSQKMDGMGI EMIDEKLMFH 3000
VDNGAGRFTA VYDAGVPGHL CDGQWHKVTA NKIKHRIELT VDGNQVEAQS 3050
PNPASTSADT NDPVFVGGFP DDLKQFGLTT SIPFRGCIRS LKLTKGTGKP 3100
LEVNFAKALE LRGVQPVSCP AN 3122
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.

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 conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti588 – 5881A → R in AAB18388. 1 Publication
Sequence conflicti1740 – 17401A → D1 Publication
Sequence conflicti1827 – 18271Q → G1 Publication
Sequence conflicti1981 – 19811A → V in AAA63215. 1 Publication
Sequence conflicti2437 – 24371S → Y in AAB18388. 1 Publication
Sequence conflicti2624 – 26241H → R in AAA63215. 1 Publication
Sequence conflicti2807 – 28071R → A in CAA81394. 1 Publication
Sequence conflicti2807 – 28071R → A in AAB18388. 1 Publication
Sequence conflicti2969 – 29691R → A in CAA81394. 1 Publication
Sequence conflicti2969 – 29691R → A in AAB18388. 1 Publication

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...

Protein-protein interaction databases

BioGridi 110102. 3 interactions.
DIPi DIP-42562N.
IntActi P24043. 3 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.
HOGENOMi HOG000293201.
HOVERGENi HBG052298.
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

ArrayExpressi P24043.
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 IPR008985. 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 ]
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: September 3, 2014
This is version 158 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

Similar proteinsi