P25391 (LAMA1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Laminin subunit alpha-1

Alternative name(s):
Laminin A chain
Laminin-1 subunit alpha
Laminin-3 subunit alpha
S-laminin subunit alpha
Short name=S-LAM alpha

Gene names

Name:	LAMA1
Synonyms:	LAMA

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	3075 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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-1 is a subunit of laminin-1 (laminin-111 or EHS laminin) and laminin-3 (laminin-121 or S-laminin).
Subcellular location	Secreted › extracellular space › extracellular matrix › basement membrane. Note: Major component.
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.
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.

Ontologies

Keywords
Biological process	Cell adhesion
Cellular component	Basement membrane Extracellular matrix Secreted
Coding sequence diversity	Polymorphism
Domain	Coiled coil Laminin EGF-like domain Repeat Signal
PTM	Disulfide bond Glycoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	axon guidance Traceable author statement. Source: Reactome branching involved in salivary gland morphogenesis Inferred from electronic annotation. Source: Compara cell adhesion Inferred from electronic annotation. Source: UniProtKB-KW cell surface receptor signaling pathway Inferred from sequence or structural similarity. Source: UniProtKB epithelial tube branching involved in lung morphogenesis Inferred from electronic annotation. Source: Compara establishment of epithelial cell apical/basal polarity Inferred from electronic annotation. Source: Compara morphogenesis of an epithelial sheet Inferred from electronic annotation. Source: Compara 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 retinal blood vessel morphogenesis Inferred from electronic annotation. Source: Compara
Cellular_component	cell-cell junction Inferred from electronic annotation. Source: Compara extracellular space Inferred from direct assay PubMed 10964500. Source: UniProtKB laminin-1 complex Inferred from direct assay PubMed 8601594. Source: UniProtKB laminin-3 complex Inferred from physical interaction PubMed 10964500. Source: UniProtKB
Molecular_function	extracellular matrix structural constituent Inferred from sequence or structural similarity. Source: UniProtKB glycosphingolipid binding Inferred from electronic annotation. Source: Compara
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 17	17	Potential
	Chain	18 – 3075	3058	Laminin subunit alpha-1		PRO_0000017054
Regions
	Domain	18 – 269	252	Laminin N-terminal
	Domain	270 – 326	57	Laminin EGF-like 1
	Domain	327 – 396	70	Laminin EGF-like 2
	Domain	397 – 453	57	Laminin EGF-like 3
	Domain	454 – 502	49	Laminin EGF-like 4
	Domain	503 – 512	10	Laminin EGF-like 5; first part
	Domain	516 – 708	193	Laminin IV type A 1
	Domain	709 – 741	33	Laminin EGF-like 5; second part
	Domain	742 – 790	49	Laminin EGF-like 6
	Domain	791 – 848	58	Laminin EGF-like 7
	Domain	849 – 901	53	Laminin EGF-like 8
	Domain	902 – 950	49	Laminin EGF-like 9
	Domain	951 – 997	47	Laminin EGF-like 10
	Domain	998 – 1043	46	Laminin EGF-like 11
	Domain	1044 – 1089	46	Laminin EGF-like 12
	Domain	1090 – 1149	60	Laminin EGF-like 13
	Domain	1150 – 1159	10	Laminin EGF-like 14; first part
	Domain	1170 – 1361	192	Laminin IV type A 2
	Domain	1362 – 1402	41	Laminin EGF-like 14; second part
	Domain	1403 – 1451	49	Laminin EGF-like 15
	Domain	1452 – 1508	57	Laminin EGF-like 16
	Domain	1509 – 1555	47	Laminin EGF-like 17
	Domain	2117 – 2297	181	Laminin G-like 1
	Domain	2305 – 2481	177	Laminin G-like 2
	Domain	2486 – 2673	188	Laminin G-like 3
	Domain	2713 – 2885	173	Laminin G-like 4
	Domain	2890 – 3070	181	Laminin G-like 5
	Region	1556 – 2116	561	Domain II and I
	Coiled coil	1706 – 1796	91	Potential
	Coiled coil	1968 – 1989	22	Potential
	Coiled coil	2088 – 2120	33	Potential
	Motif	2534 – 2536	3	Cell attachment site
Amino acid modifications
	Glycosylation	38	1	N-linked (GlcNAc...) Potential
	Glycosylation	555	1	N-linked (GlcNAc...) Potential
	Glycosylation	665	1	N-linked (GlcNAc...) Potential
	Glycosylation	763	1	N-linked (GlcNAc...) Potential
	Glycosylation	926	1	N-linked (GlcNAc...) Potential
	Glycosylation	952	1	N-linked (GlcNAc...) Potential
	Glycosylation	1045	1	N-linked (GlcNAc...) Potential
	Glycosylation	1407	1	N-linked (GlcNAc...) Potential
	Glycosylation	1579	1	N-linked (GlcNAc...) Potential
	Glycosylation	1596	1	N-linked (GlcNAc...) Potential
	Glycosylation	1678	1	N-linked (GlcNAc...) Potential
	Glycosylation	1689	1	N-linked (GlcNAc...) Potential
	Glycosylation	1698	1	N-linked (GlcNAc...) Potential
	Glycosylation	1717	1	N-linked (GlcNAc...) Potential
	Glycosylation	1804	1	N-linked (GlcNAc...) Potential
	Glycosylation	1894	1	N-linked (GlcNAc...) Potential
	Glycosylation	1898	1	N-linked (GlcNAc...) Potential
	Glycosylation	1957	1	N-linked (GlcNAc...) Potential
	Glycosylation	1974	1	N-linked (GlcNAc...) Potential
	Glycosylation	1991	1	N-linked (GlcNAc...) Potential
	Glycosylation	2038	1	N-linked (GlcNAc...) Potential
	Glycosylation	2047	1	N-linked (GlcNAc...) Potential
	Glycosylation	2094	1	N-linked (GlcNAc...) Potential
	Glycosylation	2098	1	N-linked (GlcNAc...) Potential
	Glycosylation	2243	1	N-linked (GlcNAc...) Ref.5
	Glycosylation	2244	1	N-linked (GlcNAc...) Potential
	Glycosylation	2384	1	N-linked (GlcNAc...) Potential
	Glycosylation	2408	1	N-linked (GlcNAc...) Potential
	Glycosylation	2518	1	N-linked (GlcNAc...) Potential
	Glycosylation	2619	1	N-linked (GlcNAc...) Potential
	Glycosylation	2729	1	N-linked (GlcNAc...) Potential
	Glycosylation	2852	1	N-linked (GlcNAc...) Potential
	Glycosylation	2915	1	N-linked (GlcNAc...) Potential
	Glycosylation	2983	1	N-linked (GlcNAc...) Potential
	Disulfide bond	270 ↔ 279		By similarity
	Disulfide bond	272 ↔ 290		By similarity
	Disulfide bond	292 ↔ 301		By similarity
	Disulfide bond	297 ↔ 305		Potential
	Disulfide bond	304 ↔ 324		By similarity
	Disulfide bond	327 ↔ 336		By similarity
	Disulfide bond	329 ↔ 361		By similarity
	Disulfide bond	364 ↔ 373		By similarity
	Disulfide bond	376 ↔ 394		By similarity
	Disulfide bond	397 ↔ 409		By similarity
	Disulfide bond	399 ↔ 427		By similarity
	Disulfide bond	429 ↔ 438		By similarity
	Disulfide bond	441 ↔ 451		By similarity
	Disulfide bond	454 ↔ 467		By similarity
	Disulfide bond	456 ↔ 471		By similarity
	Disulfide bond	473 ↔ 482		By similarity
	Disulfide bond	485 ↔ 500		By similarity
	Disulfide bond	742 ↔ 751		By similarity
	Disulfide bond	744 ↔ 757		By similarity
	Disulfide bond	760 ↔ 769		By similarity
	Disulfide bond	772 ↔ 788		By similarity
	Disulfide bond	791 ↔ 806		By similarity
	Disulfide bond	793 ↔ 816		By similarity
	Disulfide bond	819 ↔ 828		By similarity
	Disulfide bond	831 ↔ 846		By similarity
	Disulfide bond	849 ↔ 863		By similarity
	Disulfide bond	851 ↔ 870		By similarity
	Disulfide bond	873 ↔ 882		By similarity
	Disulfide bond	885 ↔ 899		By similarity
	Disulfide bond	902 ↔ 914		By similarity
	Disulfide bond	904 ↔ 921		By similarity
	Disulfide bond	923 ↔ 932		By similarity
	Disulfide bond	935 ↔ 948		By similarity
	Disulfide bond	951 ↔ 963		By similarity
	Disulfide bond	953 ↔ 969		By similarity
	Disulfide bond	971 ↔ 980		By similarity
	Disulfide bond	983 ↔ 995		By similarity
	Disulfide bond	998 ↔ 1007		By similarity
	Disulfide bond	1000 ↔ 1014		By similarity
	Disulfide bond	1016 ↔ 1025		By similarity
	Disulfide bond	1028 ↔ 1041		By similarity
	Disulfide bond	1044 ↔ 1056		By similarity
	Disulfide bond	1046 ↔ 1063		By similarity
	Disulfide bond	1065 ↔ 1074		By similarity
	Disulfide bond	1077 ↔ 1087		By similarity
	Disulfide bond	1090 ↔ 1102		By similarity
	Disulfide bond	1092 ↔ 1118		By similarity
	Disulfide bond	1120 ↔ 1129		By similarity
	Disulfide bond	1132 ↔ 1147		By similarity
	Disulfide bond	1403 ↔ 1412		By similarity
	Disulfide bond	1405 ↔ 1419		By similarity
	Disulfide bond	1422 ↔ 1431		By similarity
	Disulfide bond	1434 ↔ 1449		By similarity
	Disulfide bond	1452 ↔ 1466		By similarity
	Disulfide bond	1454 ↔ 1476		By similarity
	Disulfide bond	1479 ↔ 1488		By similarity
	Disulfide bond	1491 ↔ 1506		By similarity
	Disulfide bond	1509 ↔ 1521		By similarity
	Disulfide bond	1511 ↔ 1528		By similarity
	Disulfide bond	1530 ↔ 1539		By similarity
	Disulfide bond	1542 ↔ 1553		By similarity
	Disulfide bond	1556		Interchain Probable
	Disulfide bond	1560		Interchain Probable
	Disulfide bond	2271 ↔ 2297		By similarity
	Disulfide bond	2457 ↔ 2481		By similarity
	Disulfide bond	2646 ↔ 2673		By similarity
	Disulfide bond	2860 ↔ 2885		By similarity
	Disulfide bond	3039 ↔ 3070		By similarity
Natural variations
	Natural variant	349	1	L → S. Corresponds to variant rs9950267 [ dbSNP | Ensembl ].		VAR_056132
	Natural variant	559	1	V → I. Corresponds to variant rs16951079 [ dbSNP | Ensembl ].		VAR_056133
	Natural variant	674	1	N → T. Ref.1 Ref.3 Corresponds to variant rs566655 [ dbSNP | Ensembl ].		VAR_060785
	Natural variant	1340	1	M → V. Ref.1 Corresponds to variant rs662471 [ dbSNP | Ensembl ].		VAR_060786
	Natural variant	1577	1	S → A. Corresponds to variant rs12961939 [ dbSNP | Ensembl ].		VAR_056134
	Natural variant	1591	1	L → V. Corresponds to variant rs596315 [ dbSNP | Ensembl ].		VAR_056135
	Natural variant	1632	1	K → E. Corresponds to variant rs11872364 [ dbSNP | Ensembl ].		VAR_056136
	Natural variant	1682	1	D → V. Corresponds to variant rs16950981 [ dbSNP | Ensembl ].		VAR_056137
	Natural variant	1876	1	A → T. Ref.1 Ref.3 Corresponds to variant rs11664063 [ dbSNP | Ensembl ].		VAR_060787
	Natural variant	2002	1	K → E. Ref.1 Ref.3 Corresponds to variant rs607230 [ dbSNP | Ensembl ].		VAR_060788
	Natural variant	2076	1	I → T. Corresponds to variant rs671871 [ dbSNP | Ensembl ].		VAR_056138
	Natural variant	2511	1	L → M. Corresponds to variant rs60009920 [ dbSNP | Ensembl ].		VAR_061347
	Natural variant	2611	1	T → A. Corresponds to variant rs543355 [ dbSNP | Ensembl ].		VAR_056139
Experimental info
	Sequence conflict	228 – 229	2	LQ → FE in CAA41418. Ref.3
	Sequence conflict	252 – 254	3	IVT → MLP in CAA41418. Ref.3
	Sequence conflict	419	1	H → E in CAA41418. Ref.3
	Sequence conflict	519	1	V → L in CAA41418. Ref.3
	Sequence conflict	1023	1	V → G Ref.1
	Sequence conflict	1075	1	D → V in CAA41418. Ref.3
	Sequence conflict	1513	1	P → R Ref.1
	Sequence conflict	1659	1	I → V Ref.1
	Sequence conflict	1659	1	I → V in CAA41418. Ref.3
	Sequence conflict	2079 – 2080	2	NL → KV in CAA41418. Ref.3
	Sequence conflict	2692	1	P → R Ref.1
	Sequence conflict	2692	1	P → R Ref.4
	Sequence conflict	2746	1	F → L Ref.4
	Sequence conflict	2962	1	A → P Ref.1
	Sequence conflict	2962	1	A → P Ref.4
	Sequence conflict	3054	1	F → L Ref.4

Sequences

	Sequence		Length	Mass (Da)
	P25391 [UniParc]. Last modified December 15, 2009. Version 2. Checksum: 941167F8FE534745	FASTA	3,075	337,084
	10 20 30 40 50 60 MRGGVLLVLL LCVAAQCRQR GLFPAILNLA SNAHISTNAT CGEKGPEMFC KLVEHVPGRP 70 80 90 100 110 120 VRNPQCRICD GNSANPRERH PISHAIDGTN NWWQSPSIQN GREYHWVTIT LDLRQVFQVA 130 140 150 160 170 180 YVIIKAANAP RPGNWILERS LDGTTFSPWQ YYAVSDSECL SRYNITPRRG PPTYRADDEV 190 200 210 220 230 240 ICTSYYSRLV PLEHGEIHTS LINGRPSADD LSPKLLEFTS ARYIRLRLQR IRTLNADLMT 250 260 270 280 290 300 LSHREPKELD PIVTRRYYYS IKDISVGGMC ICYGHASSCP WDETTKKLQC QCEHNTCGES 310 320 330 340 350 360 CNRCCPGYHQ QPWRPGTVSS GNTCEACNCH NKAKDCYYDE SVAKQKKSLN TAGQFRGGGV 370 380 390 400 410 420 CINCLQNTMG INCETCIDGY YRPHKVSPYE DEPCRPCNCD PVGSLSSVCI KDDLHSDLHN 430 440 450 460 470 480 GKQPGQCPCK EGYTGEKCDR CQLGYKDYPT CVSCGCNPVG SASDEPCTGP CVCKENVEGK 490 500 510 520 530 540 ACDRCKPGFY NLKEKNPRGC SECFCFGVSD VCSSLSWPVG QVNSMSGWLV TDLISPRKIP 550 560 570 580 590 600 SQQDALGGRH QVSINNTAVM QRLAPKYYWA APEAYLGNKL TAFGGFLKYT VSYDIPVETV 610 620 630 640 650 660 DSNLMSHADV IIKGNGLTLS TQAEGLSLQP YEEYLNVVRL VPENFQDFHS KRQIDRDQLM 670 680 690 700 710 720 TVLANVTHLL IRANYNSAKM ALYRLESVSL DIASSNAIDL VVAADVEHCE CPQGYTGTSC 730 740 750 760 770 780 ESCLSGYYRV DGILFGGICQ PCECHGHAAE CNVHGVCIAC AHNTTGVHCE QCLPGFYGEP 790 800 810 820 830 840 SRGTPGDCQP CACPLTIASN NFSPTCHLND GDEVVCDWCA PGYSGAWCER CADGYYGNPT 850 860 870 880 890 900 VPGESCVPCD CSGNVDPSEA GHCDSVTGEC LKCLGNTDGA HCERCADGFY GDAVTAKNCR 910 920 930 940 950 960 ACECHVKGSH SAVCHLETGL CDCKPNVTGQ QCDQCLHGYY GLDSGHGCRP CNCSVAGSVS 970 980 990 1000 1010 1020 DGCTDEGQCH CVPGVAGKRC DRCAHGFYAY QDGSCTPCDC PHTQNTCDPE TGECVCPPHT 1030 1040 1050 1060 1070 1080 QGVKCEECED GHWGYDAEVG CQACNCSLVG STHHRCDVVT GHCQCKSKFG GRACDQCSLG 1090 1100 1110 1120 1130 1140 YRDFPDCVPC DCDLRGTSGD ACNLEQGLCG CVEETGACPC KENVFGPQCN ECREGTFALR 1150 1160 1170 1180 1190 1200 ADNPLGCSPC FCSGLSHLCS ELEDYVRTPV TLGSDQPLLR VVSQSNLRGT TEGVYYQAPD 1210 1220 1230 1240 1250 1260 FLLDAATVRQ HIRAEPFYWR LPQQFQGDQL MAYGGKLKYS VAFYSLDGVG TSNFEPQVLI 1270 1280 1290 1300 1310 1320 KGGRIRKQVI YMDAPAPENG VRQEQEVAMR ENFWKYFNSV SEKPVTREDF MSVLSDIEYI 1330 1340 1350 1360 1370 1380 LIKASYGQGL QQSRISDISM EVGRKAEKLH PEEEVASLLE NCVCPPGTVG FSCQDCAPGY 1390 1400 1410 1420 1430 1440 HRGKLPAGSD RGPRPLVAPC VPCSCNNHSD TCDPNTGKCL NCGDNTAGDH CDVCTSGYYG 1450 1460 1470 1480 1490 1500 KVTGSASDCA LCACPHSPPA SFSPTCVLEG DHDFRCDACL LGYEGKHCER CSSSYYGNPQ 1510 1520 1530 1540 1550 1560 TPGGSCQKCD CNPHGSVHGD CDRTSGQCVC RLGASGLRCD ECEPRHILME TDCVSCDDEC 1570 1580 1590 1600 1610 1620 VGVLLNDLDE IGDAVLSLNL TGIIPVPYGI LSNLENTTKY LQESLLKENM QKDLGKIKLE 1630 1640 1650 1660 1670 1680 GVAEETDNLQ KKLTRMLAST QKVNRATERI FKESQDLAIA IERLQMSITE IMEKTTLNQT 1690 1700 1710 1720 1730 1740 LDEDFLLPNS TLQNMQQNGT SLLEIMQIRD FTQLHQNATL ELKAAEDLLS QIQENYQKPL 1750 1760 1770 1780 1790 1800 EELEVLKEAA SHVLSKHNNE LKAAEALVRE AEAKMQESNH LLLMVNANLR EFSDKKLHVQ 1810 1820 1830 1840 1850 1860 EEQNLTSELI VQGRGLIDAA AAQTDAVQDA LEHLEDHQDK LLLWSAKIRH HIDDLVMHMS 1870 1880 1890 1900 1910 1920 QRNAVDLVYR AEDHAAEFQR LADVLYSGLE NIRNVSLNAT SAAYVHYNIQ SLIEESEELA 1930 1940 1950 1960 1970 1980 RDAHRTVTET SLLSESLVSN GKAAVQRSSR FLKEGNNLSR KLPGIALELS ELRNKTNRFQ 1990 2000 2010 2020 2030 2040 ENAVEITRQT NESLLILRAI PKGIRDKGAK TKELATSASQ SAVSTLRDVA GLSQELLNTS 2050 2060 2070 2080 2090 2100 ASLSRVNTTL RETHQLLQDS TMATLLAGRK VKDVEIQANL LFDRLKPLKM LEENLSRNLS 2110 2120 2130 2140 2150 2160 EIKLLISQAR KQAASIKVAV SADRDCIRAY QPQISSTNYN TLTLNVKTQE PDNLLFYLGS 2170 2180 2190 2200 2210 2220 STASDFLAVE MRRGRVAFLW DLGSGSTRLE FPDFPIDDNR WHSIHVARFG NIGSLSVKEM 2230 2240 2250 2260 2270 2280 SSNQKSPTKT SKSPGTANVL DVNNSTLMFV GGLGGQIKKS PAVKVTHFKG CLGEAFLNGK 2290 2300 2310 2320 2330 2340 SIGLWNYIER EGKCRGCFGS SQNEDPSFHF DGSGYSVVEK SLPATVTQII MLFNTFSPNG 2350 2360 2370 2380 2390 2400 LLLYLGSYGT KDFLSIELFR GRVKVMTDLG SGPITLLTDR RYNNGTWYKI AFQRNRKQGV 2410 2420 2430 2440 2450 2460 LAVIDAYNTS NKETKQGETP GASSDLNRLD KDPIYVGGLP RSRVVRRGVT TKSFVGCIKN 2470 2480 2490 2500 2510 2520 LEISRSTFDL LRNSYGVRKG CLLEPIRSVS FLKGGYIELP PKSLSPESEW LVTFATTNSS 2530 2540 2550 2560 2570 2580 GIILAALGGD VEKRGDREEA HVPFFSVMLI GGNIEVHVNP GDGTGLRKAL LHAPTGTCSD 2590 2600 2610 2620 2630 2640 GQAHSISLVR NRRIITVQLD ENNPVEMKLG TLVESRTINV SNLYVGGIPE GEGTSLLTMR 2650 2660 2670 2680 2690 2700 RSFHGCIKNL IFNLELLDFN SAVGHEQVDL DTCWLSERPK LAPDAEDSKL LPEPRAFPEQ 2710 2720 2730 2740 2750 2760 CVVDAALEYV PGAHQFGLTQ NSHFILPFNQ SAVRKKLSVE LSIRTFASSG LIYYMAHQNQ 2770 2780 2790 2800 2810 2820 ADYAVLQLHG GRLHFMFDLG KGRTKVSHPA LLSDGKWHTV KTDYVKRKGF ITVDGRESPM 2830 2840 2850 2860 2870 2880 VTVVGDGTML DVEGLFYLGG LPSQYQARKI GNITHSIPAC IGDVTVNSKQ LDKDSPVSAF 2890 2900 2910 2920 2930 2940 TVNRCYAVAQ EGTYFDGSGY AALVKEGYKV QSDVNITLEF RTSSQNGVLL GISTAKVDAI 2950 2960 2970 2980 2990 3000 GLELVDGKVL FHVNNGAGRI TAAYEPKTAT VLCDGKWHTL QANKSKHRIT LIVDGNAVGA 3010 3020 3030 3040 3050 3060 ESPHTQSTSV DTNNPIYVGG YPAGVKQKCL RSQTSFRGCL RKLALIKSPQ VQSFDFSRAF 3070 ELHGVFLHSC PGTES

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Molecular cloning of the cDNA encoding human laminin A chain." Haaparanta T., Uitto J., Ruoslahti E., Engvall E. Matrix 11:151-160(1991) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANTS THR-674; VAL-1340; THR-1876 AND GLU-2002.
[2]	"DNA sequence and analysis of human chromosome 18." Nusbaum C., Zody M.C., Borowsky M.L., Kamal M., Kodira C.D., Taylor T.D., Whittaker C.A., Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Yang X., Abouelleil A., Allen N.R., Anderson S., Bloom T., Bugalter B., Butler J. , Cook A., DeCaprio D., Engels R., Garber M., Gnirke A., Hafez N., Hall J.L., Norman C.H., Itoh T., Jaffe D.B., Kuroki Y., Lehoczky J., Lui A., Macdonald P., Mauceli E., Mikkelsen T.S., Naylor J.W., Nicol R., Nguyen C., Noguchi H., O'Leary S.B., Piqani B., Smith C.L., Talamas J.A., Topham K., Totoki Y., Toyoda A., Wain H.M., Young S.K., Zeng Q., Zimmer A.R., Fujiyama A., Hattori M., Birren B.W., Sakaki Y., Lander E.S. Nature 437:551-555(2005) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[3]	"Primary structure of the human laminin A chain. Limited expression in human tissues." Nissinen M., Vuolteenaho R., Boot-Handford R., Kallunki P., Tryggvason K. Biochem. J. 276:369-379(1991) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-2628, VARIANTS THR-674; THR-1876 AND GLU-2002.
[4]	"Human laminin: cloning and sequence analysis of cDNAs encoding A, B1 and B2 chains, and expression of the corresponding genes in human skin and cultured cells." Olsen D., Nagayoshi T., Fazio M., Peltonen J., Jaakkola S., Sanborn D., Sasaki T., Kuivaniemi H., Chu M.-L., Deutzmann R., Timpl R., Uitto J. Lab. Invest. 60:772-782(1989) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 2397-3072.
[5]	"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-2243, MASS SPECTROMETRY. Tissue: Liver.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AP002409 Genomic DNA. No translation available. AP005062 Genomic DNA. No translation available. AP005210 Genomic DNA. No translation available. X58531 mRNA. Translation: CAA41418.1.
IPI	IPI00375294.
PIR	S14458.
RefSeq	NP_005550.2. NM_005559.3.
UniGene	Hs.270364.
3D structure databases
ProteinModelPortal	P25391.
SMR	P25391. Positions 17-505, 708-1155, 1361-1544, 2128-2472, 2491-2674, 2701-3074.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-29324N.
MINT	MINT-6740485.
STRING	9606.ENSP00000374309.
PTM databases
PhosphoSite	P25391.
Proteomic databases
PaxDb	P25391.
PRIDE	P25391.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000389658; ENSP00000374309; ENSG00000101680.
GeneID	284217.
KEGG	hsa:284217.
UCSC	uc002knm.3. human.
Organism-specific databases
CTD	284217.
GeneCards	GC18M006941.
H-InvDB	HIX0014316.
HGNC	HGNC:6481. LAMA1.
HPA	CAB010179.
MIM	150320. gene.
neXtProt	NX_P25391.
PharmGKB	PA30270.
GenAtlas	Search...
Phylogenomic databases
eggNOG	NOG247347.
HOGENOM	HOG000293201.
HOVERGEN	HBG052298.
InParanoid	P25391.
KO	K05637.
OMA	EPFYWRL.
OrthoDB	EOG4K3KVB.
Enzyme and pathway databases
Pathway_Interaction_DB	a6b1_a6b4_integrin_pathway. a6b1 and a6b4 Integrin signaling. amb2_neutrophils_pathway. amb2 Integrin signaling. glypican_1pathway. Glypican 1 network. syndecan_2_pathway. Syndecan-2-mediated signaling events. syndecan_4_pathway. Syndecan-4-mediated signaling events.
Reactome	REACT_111045. Developmental Biology. REACT_111102. Signal Transduction.
Gene expression databases
ArrayExpress	P25391.
Bgee	P25391.
CleanEx	HS_LAMA1.
Genevestigator	P25391.
GermOnline	ENSG00000101680. Homo sapiens.
Family and domain databases
Gene3D	2.60.120.200. 5 hits.
InterPro	IPR008985. ConA-like_lec_gl_sf. IPR013320. ConA-like_subgrp. IPR002049. EGF_laminin. IPR018031. Laminin_B_subgr. IPR000034. Laminin_B_type_IV. IPR001791. Laminin_G. IPR009254. Laminin_I. IPR010307. Laminin_II. IPR008211. Laminin_N. [Graphical view]
Pfam	PF00052. Laminin_B. 2 hits. PF00053. Laminin_EGF. 17 hits. PF00054. Laminin_G_1. 5 hits. PF06008. Laminin_I. 1 hit. PF06009. Laminin_II. 1 hit. PF00055. Laminin_N. 1 hit. [Graphical view]
SMART	SM00180. EGF_Lam. 15 hits. SM00281. LamB. 2 hits. SM00282. LamG. 5 hits. SM00136. LamNT. 1 hit. [Graphical view]
SUPFAM	SSF49899. ConA_like_lec_gl. 5 hits.
PROSITE	PS00022. EGF_1. 11 hits. PS01186. EGF_2. 2 hits. PS01248. EGF_LAM_1. 15 hits. PS50027. EGF_LAM_2. 15 hits. PS50025. LAM_G_DOMAIN. 5 hits. PS51115. LAMININ_IVA. 2 hits. PS51117. LAMININ_NTER. 1 hit. [Graphical view]
ProtoNet	Search...
Other
ChiTaRS	LAMA1. human.
DrugBank	DB00009. Alteplase. DB00029. Anistreplase. DB00015. Reteplase. DB00031. Tenecteplase.
GenomeRNAi	284217.
NextBio	94628.
SOURCE	Search...

Entry information

Entry name

LAMA1_HUMAN

Accession

Primary (citable) accession number: P25391

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 1, 1992
Last sequence update:	December 15, 2009
Last modified:	May 1, 2013
This is version 139 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.