UniProt Accession

 LAMA1_HUMAN; P25391 

Genbank Protein ID

 AP002409; AP005062; AP005210; X58531 

Genbank Nucleotide ID

 CAA41418.1 

Protein Name

 Laminin subunit alpha-1 

Protein Synonyms/Alias

 Laminin A chain; Laminin-1 subunit alpha; Laminin-3 subunit alpha; S-laminin subunit alpha; S-LAM alpha 

Gene Name

 LAMA1 

Gene Synonyms/Alias

 LAMA 

Created Date

 July 27, 2013 

Organism

 Homo sapiens (Human) 

NCBI Taxa ID

 9606 

Lysine Modification

Position	Peptide	Type	References
566	VMQRLAPKYYWAAPE	ubiquitination	[1]
651	NFQDFHSKRQIDRDQ	ubiquitination	[1]
897	YGDAVTAKNCRACEC	ubiquitination	[1]
1066	VTGHCQCKSKFGGRA	ubiquitination	[1]
1068	GHCQCKSKFGGRACD	ubiquitination	[1]
1121	ETGACPCKENVFGPQ	ubiquitination	[1]
1236	QLMAYGGKLKYSVAF	ubiquitination	[1]
1238	MAYGGKLKYSVAFYS	ubiquitination	[1]
1261	FEPQVLIKGGRIRKQ	ubiquitination	[1]
1267	IKGGRIRKQVIYMDA	ubiquitination	[1]
1295	AMRENFWKYFNSVSE	ubiquitination	[1]
1303	YFNSVSEKPVTREDF	ubiquitination	[1]
1345	ISMEVGRKAEKLHPE	ubiquitination	[1]
1348	EVGRKAEKLHPEEEV	ubiquitination	[1]
1384	APGYHRGKLPAGSDR	ubiquitination	[1]
1486	CLLGYEGKHCERCSS	ubiquitination	[1]
1607	YLQESLLKENMQKDL	ubiquitination	[1]
1612	LLKENMQKDLGKIKL	ubiquitination	[1]
1618	QKDLGKIKLEGVAEE	ubiquitination	[1]
1631	EETDNLQKKLTRMLA	ubiquitination	[1]
1632	ETDNLQKKLTRMLAS	ubiquitination	[1]
1642	RMLASTQKVNRATER	ubiquitination	[1]
1738	QIQENYQKPLEELEV	ubiquitination	[1]
1747	LEELEVLKEAASHVL	ubiquitination	[1]
1756	AASHVLSKHNNELKA	ubiquitination	[1]
1762	SKHNNELKAAEALVR	ubiquitination	[1]
1847	KLLLWSAKIRHHIDD	ubiquitination	[1]
1942	ESLVSNGKAAVQRSS	ubiquitination	[1]
1953	QRSSRFLKEGNNLSR	ubiquitination	[1]
1961	EGNNLSRKLPGIALE	ubiquitination	[1]
2007	IPKGIRDKGAKTKEL	ubiquitination	[1]
2010	GIRDKGAKTKELATS	ubiquitination	[1]
2012	RDKGAKTKELATSAS	ubiquitination	[1]
2086	NLLFDRLKPLKMLEE	ubiquitination	[1]
2089	FDRLKPLKMLEENLS	ubiquitination	[1]
2103	SRNLSEIKLLISQAR	ubiquitination	[1]
2111	LLISQARKQAASIKV	ubiquitination	[1]
2117	RKQAASIKVAVSADR	ubiquitination	[1]
2218	NIGSLSVKEMSSNQK	ubiquitination	[1]
2225	KEMSSNQKSPTKTSK	ubiquitination	[1]
2232	KSPTKTSKSPGTANV	ubiquitination	[1]
2258	GGLGGQIKKSPAVKV	ubiquitination	[1]
2259	GLGGQIKKSPAVKVT	ubiquitination	[1]
2264	IKKSPAVKVTHFKGC	ubiquitination	[1]
2269	AVKVTHFKGCLGEAF	ubiquitination	[1]
2280	GEAFLNGKSIGLWNY	ubiquitination	[1]
2364	ELFRGRVKVMTDLGS	ubiquitination	[1]
2389	YNNGTWYKIAFQRNR	ubiquitination	[1]
2397	IAFQRNRKQGVLAVI	ubiquitination	[1]
2412	DAYNTSNKETKQGET	ubiquitination	[1]
2415	NTSNKETKQGETPGA	ubiquitination	[1]
2431	SDLNRLDKDPIYVGG	ubiquitination	[1]
2452	VRRGVTTKSFVGCIK	ubiquitination	[1]
2459	KSFVGCIKNLEISRS	ubiquitination	[1]
2479	RNSYGVRKGCLLEPI	methylation	[2]
2479	RNSYGVRKGCLLEPI	ubiquitination	[1]
2493	IRSVSFLKGGYIELP	ubiquitination	[1]
2568	GDGTGLRKALLHAPT	ubiquitination	[1]
2736	NQSAVRKKLSVELSI	ubiquitination	[1]
2781	HFMFDLGKGRTKVSH	ubiquitination	[1]
2785	DLGKGRTKVSHPALL	ubiquitination	[1]
2796	PALLSDGKWHTVKTD	ubiquitination	[1]
2801	DGKWHTVKTDYVKRK	ubiquitination	[1]
2806	TVKTDYVKRKGFITV	ubiquitination	[1]
2808	KTDYVKRKGFITVDG	ubiquitination	[1]
2849	PSQYQARKIGNITHS	ubiquitination	[1]
2869	GDVTVNSKQLDKDSP	ubiquitination	[1]
2873	VNSKQLDKDSPVSAF	ubiquitination	[1]
2905	SGYAALVKEGYKVQS	ubiquitination	[1]
2936	LLGISTAKVDAIGLE	ubiquitination	[1]
2948	GLELVDGKVLFHVNN	ubiquitination	[1]
2976	ATVLCDGKWHTLQAN	ubiquitination	[1]
2984	WHTLQANKSKHRITL	ubiquitination	[1]
3026	GGYPAGVKQKCLRSQ	ubiquitination	[1]
3028	YPAGVKQKCLRSQTS	ubiquitination	[1]
3047	LRKLALIKSPQVQSF	ubiquitination	[1]

Reference

 [1] Global identification of modular cullin-RING ligase substrates.
 Emanuele MJ, Elia AE, Xu Q, Thoma CR, Izhar L, Leng Y, Guo A, Chen YN, Rush J, Hsu PW, Yen HC, Elledge SJ.
 Cell. 2011 Oct 14;147(2):459-74. [PMID: 21963094]
 [2] Large-scale global identification of protein lysine methylation in vivo.
 Cao XJ, Arnaudo AM, Garcia BA.
 Epigenetics. 2013 May 1;8(5):477-85. [PMID: 23644510] 

Functional Description

 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. 

Sequence Annotation

 DOMAIN 18 269 Laminin N-terminal.
 DOMAIN 270 326 Laminin EGF-like 1.
 DOMAIN 327 396 Laminin EGF-like 2.
 DOMAIN 397 453 Laminin EGF-like 3.
 DOMAIN 454 502 Laminin EGF-like 4.
 DOMAIN 503 512 Laminin EGF-like 5; first part.
 DOMAIN 516 708 Laminin IV type A 1.
 DOMAIN 709 741 Laminin EGF-like 5; second part.
 DOMAIN 742 790 Laminin EGF-like 6.
 DOMAIN 791 848 Laminin EGF-like 7.
 DOMAIN 849 901 Laminin EGF-like 8.
 DOMAIN 902 950 Laminin EGF-like 9.
 DOMAIN 951 997 Laminin EGF-like 10.
 DOMAIN 998 1043 Laminin EGF-like 11.
 DOMAIN 1044 1089 Laminin EGF-like 12.
 DOMAIN 1090 1149 Laminin EGF-like 13.
 DOMAIN 1150 1159 Laminin EGF-like 14; first part.
 DOMAIN 1170 1361 Laminin IV type A 2.
 DOMAIN 1362 1402 Laminin EGF-like 14; second part.
 DOMAIN 1403 1451 Laminin EGF-like 15.
 DOMAIN 1452 1508 Laminin EGF-like 16.
 DOMAIN 1509 1555 Laminin EGF-like 17.
 DOMAIN 2117 2297 Laminin G-like 1.
 DOMAIN 2305 2481 Laminin G-like 2.
 DOMAIN 2486 2673 Laminin G-like 3.
 DOMAIN 2713 2885 Laminin G-like 4.
 DOMAIN 2890 3070 Laminin G-like 5.
 REGION 1556 2116 Domain II and I.
 MOTIF 2534 2536 Cell attachment site.
 CARBOHYD 38 38 N-linked (GlcNAc...) (Potential).
 CARBOHYD 555 555 N-linked (GlcNAc...) (Potential).
 CARBOHYD 665 665 N-linked (GlcNAc...) (Potential).
 CARBOHYD 763 763 N-linked (GlcNAc...) (Potential).
 CARBOHYD 926 926 N-linked (GlcNAc...) (Potential).
 CARBOHYD 952 952 N-linked (GlcNAc...) (Potential).
 CARBOHYD 1045 1045 N-linked (GlcNAc...) (Potential).
 CARBOHYD 1407 1407 N-linked (GlcNAc...) (Potential).
 CARBOHYD 1579 1579 N-linked (GlcNAc...) (Potential).
 CARBOHYD 1596 1596 N-linked (GlcNAc...) (Potential).
 CARBOHYD 1678 1678 N-linked (GlcNAc...) (Potential).
 CARBOHYD 1689 1689 N-linked (GlcNAc...) (Potential).
 CARBOHYD 1698 1698 N-linked (GlcNAc...) (Potential).
 CARBOHYD 1717 1717 N-linked (GlcNAc...) (Potential).
 CARBOHYD 1804 1804 N-linked (GlcNAc...) (Potential).
 CARBOHYD 1894 1894 N-linked (GlcNAc...) (Potential).
 CARBOHYD 1898 1898 N-linked (GlcNAc...) (Potential).
 CARBOHYD 1957 1957 N-linked (GlcNAc...) (Potential).
 CARBOHYD 1974 1974 N-linked (GlcNAc...) (Potential).
 CARBOHYD 1991 1991 N-linked (GlcNAc...) (Potential).
 CARBOHYD 2038 2038 N-linked (GlcNAc...) (Potential).
 CARBOHYD 2047 2047 N-linked (GlcNAc...) (Potential).
 CARBOHYD 2094 2094 N-linked (GlcNAc...) (Potential).
 CARBOHYD 2098 2098 N-linked (GlcNAc...) (Potential).
 CARBOHYD 2243 2243 N-linked (GlcNAc...).
 CARBOHYD 2244 2244 N-linked (GlcNAc...) (Potential).
 CARBOHYD 2384 2384 N-linked (GlcNAc...) (Potential).
 CARBOHYD 2408 2408 N-linked (GlcNAc...) (Potential).
 CARBOHYD 2518 2518 N-linked (GlcNAc...) (Potential).
 CARBOHYD 2619 2619 N-linked (GlcNAc...) (Potential).
 CARBOHYD 2729 2729 N-linked (GlcNAc...) (Potential).
 CARBOHYD 2852 2852 N-linked (GlcNAc...) (Potential).
 CARBOHYD 2915 2915 N-linked (GlcNAc...) (Potential).
 CARBOHYD 2983 2983 N-linked (GlcNAc...) (Potential).
 DISULFID 270 279 By similarity.
 DISULFID 272 290 By similarity.
 DISULFID 292 301 By similarity.
 DISULFID 297 305 Potential.
 DISULFID 304 324 By similarity.
 DISULFID 327 336 By similarity.
 DISULFID 329 361 By similarity.
 DISULFID 364 373 By similarity.
 DISULFID 376 394 By similarity.
 DISULFID 397 409 By similarity.
 DISULFID 399 427 By similarity.
 DISULFID 429 438 By similarity.
 DISULFID 441 451 By similarity.
 DISULFID 454 467 By similarity.
 DISULFID 456 471 By similarity.
 DISULFID 473 482 By similarity.
 DISULFID 485 500 By similarity.
 DISULFID 742 751 By similarity.
 DISULFID 744 757 By similarity.
 DISULFID 760 769 By similarity.
 DISULFID 772 788 By similarity.
 DISULFID 791 806 By similarity.
 DISULFID 793 816 By similarity.
 DISULFID 819 828 By similarity.
 DISULFID 831 846 By similarity.
 DISULFID 849 863 By similarity.
 DISULFID 851 870 By similarity.
 DISULFID 873 882 By similarity.
 DISULFID 885 899 By similarity.
 DISULFID 902 914 By similarity.
 DISULFID 904 921 By similarity.
 DISULFID 923 932 By similarity.
 DISULFID 935 948 By similarity.
 DISULFID 951 963 By similarity.
 DISULFID 953 969 By similarity.
 DISULFID 971 980 By similarity.
 DISULFID 983 995 By similarity.
 DISULFID 998 1007 By similarity.
 DISULFID 1000 1014 By similarity.
 DISULFID 1016 1025 By similarity.
 DISULFID 1028 1041 By similarity.
 DISULFID 1044 1056 By similarity.
 DISULFID 1046 1063 By similarity.
 DISULFID 1065 1074 By similarity.
 DISULFID 1077 1087 By similarity.
 DISULFID 1090 1102 By similarity.
 DISULFID 1092 1118 By similarity.
 DISULFID 1120 1129 By similarity.
 DISULFID 1132 1147 By similarity.
 DISULFID 1403 1412 By similarity.
 DISULFID 1405 1419 By similarity.
 DISULFID 1422 1431 By similarity.
 DISULFID 1434 1449 By similarity.
 DISULFID 1452 1466 By similarity.
 DISULFID 1454 1476 By similarity.
 DISULFID 1479 1488 By similarity.
 DISULFID 1491 1506 By similarity.
 DISULFID 1509 1521 By similarity.
 DISULFID 1511 1528 By similarity.
 DISULFID 1530 1539 By similarity.
 DISULFID 1542 1553 By similarity.
 DISULFID 1556 1556 Interchain (Probable).
 DISULFID 1560 1560 Interchain (Probable).
 DISULFID 2271 2297 By similarity.
 DISULFID 2457 2481 By similarity.
 DISULFID 2646 2673 By similarity.
 DISULFID 2860 2885 By similarity.
 DISULFID 3039 3070 By similarity.  

Keyword

 Basement membrane; Cell adhesion; Coiled coil; Complete proteome; Disulfide bond; Extracellular matrix; Glycoprotein; Laminin EGF-like domain; Polymorphism; Reference proteome; Repeat; Secreted; Signal. 

Sequence Source

 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 

Protein Length

 3075 AA 

Protein Sequence

Gene Ontology

 GO:0005911; C:cell-cell junction; IEA:Compara.
 GO:0005615; C:extracellular space; IDA:UniProtKB.
 GO:0005606; C:laminin-1 complex; IDA:UniProtKB.
 GO:0005608; C:laminin-3 complex; IPI:UniProtKB.
 GO:0005201; F:extracellular matrix structural constituent; ISS:UniProtKB.
 GO:0043208; F:glycosphingolipid binding; IEA:Compara.
 GO:0007411; P:axon guidance; TAS:Reactome.
 GO:0060445; P:branching involved in salivary gland morphogenesis; IEA:Compara.
 GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
 GO:0007166; P:cell surface receptor signaling pathway; ISS:UniProtKB.
 GO:0060441; P:epithelial tube branching involved in lung morphogenesis; IEA:Compara.
 GO:0045198; P:establishment of epithelial cell apical/basal polarity; IEA:Compara.
 GO:0002011; P:morphogenesis of an epithelial sheet; IEA:Compara.
 GO:0030155; P:regulation of cell adhesion; IEA:InterPro.
 GO:0030334; P:regulation of cell migration; IEA:InterPro.
 GO:0045995; P:regulation of embryonic development; IEA:InterPro.
 GO:0061304; P:retinal blood vessel morphogenesis; IEA:Compara. 

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. 

Pfam

 PF00052; Laminin_B
 PF00053; Laminin_EGF
 PF00054; Laminin_G_1
 PF06008; Laminin_I
 PF06009; Laminin_II
 PF00055; Laminin_N 

SMART

 SM00180; EGF_Lam
 SM00281; LamB
 SM00282; LamG
 SM00136; LamNT 

PROSITE

 PS00022; EGF_1
 PS01186; EGF_2
 PS01248; EGF_LAM_1
 PS50027; EGF_LAM_2
 PS50025; LAM_G_DOMAIN
 PS51115; LAMININ_IVA
 PS51117; LAMININ_NTER 

PRINTS