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P25391

- LAMA1_HUMAN

UniProt

P25391 - LAMA1_HUMAN

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Protein

Laminin subunit alpha-1

Gene

LAMA1

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. extracellular matrix structural constituent Source: UniProtKB
  2. glycosphingolipid binding Source: Ensembl

GO - Biological processi

  1. axon guidance Source: Reactome
  2. branching involved in salivary gland morphogenesis Source: Ensembl
  3. cell adhesion Source: UniProtKB-KW
  4. cell surface receptor signaling pathway Source: UniProtKB
  5. epithelial tube branching involved in lung morphogenesis Source: Ensembl
  6. establishment of epithelial cell apical/basal polarity Source: Ensembl
  7. extracellular matrix organization Source: Reactome
  8. morphogenesis of an epithelial sheet Source: Ensembl
  9. regulation of cell adhesion Source: InterPro
  10. regulation of cell migration Source: InterPro
  11. regulation of embryonic development Source: InterPro
  12. retinal blood vessel morphogenesis Source: Ensembl
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.
REACT_22205. L1CAM interactions.

Names & Taxonomyi

Protein namesi
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 namesi
Name:LAMA1
Synonyms:LAMA
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 18

Organism-specific databases

HGNCiHGNC:6481. LAMA1.

Subcellular locationi

GO - Cellular componenti

  1. basement membrane Source: UniProtKB
  2. cell-cell junction Source: Ensembl
  3. extracellular matrix Source: UniProtKB
  4. extracellular region Source: Reactome
  5. extracellular space Source: UniProtKB
  6. laminin-1 complex Source: UniProtKB
  7. laminin-3 complex Source: UniProtKB
  8. proteinaceous extracellular matrix Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Basement membrane, Extracellular matrix, Secreted

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA30270.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1717Sequence AnalysisAdd
BLAST
Chaini18 – 30753058Laminin subunit alpha-1PRO_0000017054Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi38 – 381N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi270 ↔ 279By similarity
Disulfide bondi272 ↔ 290By similarity
Disulfide bondi292 ↔ 301By similarity
Disulfide bondi297 ↔ 305Sequence Analysis
Disulfide bondi304 ↔ 324By similarity
Disulfide bondi327 ↔ 336By similarity
Disulfide bondi329 ↔ 361By similarity
Disulfide bondi364 ↔ 373By similarity
Disulfide bondi376 ↔ 394By similarity
Disulfide bondi397 ↔ 409By similarity
Disulfide bondi399 ↔ 427By similarity
Disulfide bondi429 ↔ 438By similarity
Disulfide bondi441 ↔ 451By similarity
Disulfide bondi454 ↔ 467By similarity
Disulfide bondi456 ↔ 471By similarity
Disulfide bondi473 ↔ 482By similarity
Disulfide bondi485 ↔ 500By similarity
Glycosylationi555 – 5551N-linked (GlcNAc...)Sequence Analysis
Glycosylationi665 – 6651N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi742 ↔ 751By similarity
Disulfide bondi744 ↔ 757By similarity
Disulfide bondi760 ↔ 769By similarity
Glycosylationi763 – 7631N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi772 ↔ 788By similarity
Disulfide bondi791 ↔ 806By similarity
Disulfide bondi793 ↔ 816By similarity
Disulfide bondi819 ↔ 828By similarity
Disulfide bondi831 ↔ 846By similarity
Disulfide bondi849 ↔ 863By similarity
Disulfide bondi851 ↔ 870By similarity
Disulfide bondi873 ↔ 882By similarity
Disulfide bondi885 ↔ 899By similarity
Disulfide bondi902 ↔ 914By similarity
Disulfide bondi904 ↔ 921By similarity
Disulfide bondi923 ↔ 932By similarity
Glycosylationi926 – 9261N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi935 ↔ 948By similarity
Disulfide bondi951 ↔ 963By similarity
Glycosylationi952 – 9521N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi953 ↔ 969By similarity
Disulfide bondi971 ↔ 980By similarity
Disulfide bondi983 ↔ 995By similarity
Disulfide bondi998 ↔ 1007By similarity
Disulfide bondi1000 ↔ 1014By similarity
Disulfide bondi1016 ↔ 1025By similarity
Disulfide bondi1028 ↔ 1041By similarity
Disulfide bondi1044 ↔ 1056By similarity
Glycosylationi1045 – 10451N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi1046 ↔ 1063By similarity
Disulfide bondi1065 ↔ 1074By similarity
Disulfide bondi1077 ↔ 1087By similarity
Disulfide bondi1090 ↔ 1102By similarity
Disulfide bondi1092 ↔ 1118By similarity
Disulfide bondi1120 ↔ 1129By similarity
Disulfide bondi1132 ↔ 1147By similarity
Disulfide bondi1403 ↔ 1412By similarity
Disulfide bondi1405 ↔ 1419By similarity
Glycosylationi1407 – 14071N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi1422 ↔ 1431By similarity
Disulfide bondi1434 ↔ 1449By similarity
Disulfide bondi1452 ↔ 1466By similarity
Disulfide bondi1454 ↔ 1476By similarity
Disulfide bondi1479 ↔ 1488By similarity
Disulfide bondi1491 ↔ 1506By similarity
Disulfide bondi1509 ↔ 1521By similarity
Disulfide bondi1511 ↔ 1528By similarity
Disulfide bondi1530 ↔ 1539By similarity
Disulfide bondi1542 ↔ 1553By similarity
Disulfide bondi1556 – 1556InterchainCurated
Disulfide bondi1560 – 1560InterchainCurated
Glycosylationi1579 – 15791N-linked (GlcNAc...)Sequence Analysis
Glycosylationi1596 – 15961N-linked (GlcNAc...)Sequence Analysis
Glycosylationi1678 – 16781N-linked (GlcNAc...)Sequence Analysis
Glycosylationi1689 – 16891N-linked (GlcNAc...)Sequence Analysis
Glycosylationi1698 – 16981N-linked (GlcNAc...)Sequence Analysis
Glycosylationi1717 – 17171N-linked (GlcNAc...)Sequence Analysis
Glycosylationi1804 – 18041N-linked (GlcNAc...)Sequence Analysis
Glycosylationi1894 – 18941N-linked (GlcNAc...)Sequence Analysis
Glycosylationi1898 – 18981N-linked (GlcNAc...)Sequence Analysis
Glycosylationi1957 – 19571N-linked (GlcNAc...)Sequence Analysis
Glycosylationi1974 – 19741N-linked (GlcNAc...)Sequence Analysis
Glycosylationi1991 – 19911N-linked (GlcNAc...)Sequence Analysis
Glycosylationi2038 – 20381N-linked (GlcNAc...)Sequence Analysis
Glycosylationi2047 – 20471N-linked (GlcNAc...)Sequence Analysis
Glycosylationi2094 – 20941N-linked (GlcNAc...)Sequence Analysis
Glycosylationi2098 – 20981N-linked (GlcNAc...)Sequence Analysis
Glycosylationi2243 – 22431N-linked (GlcNAc...)1 Publication
Glycosylationi2244 – 22441N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi2271 ↔ 2297By similarity
Glycosylationi2384 – 23841N-linked (GlcNAc...)Sequence Analysis
Glycosylationi2408 – 24081N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi2457 ↔ 2481By similarity
Glycosylationi2518 – 25181N-linked (GlcNAc...)Sequence Analysis
Glycosylationi2619 – 26191N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi2646 ↔ 2673By similarity
Glycosylationi2729 – 27291N-linked (GlcNAc...)Sequence Analysis
Glycosylationi2852 – 28521N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi2860 ↔ 2885By similarity
Glycosylationi2915 – 29151N-linked (GlcNAc...)Sequence Analysis
Glycosylationi2983 – 29831N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi3039 ↔ 3070By similarity

Post-translational modificationi

Tyrosine phosphorylated by PKDCC/VLK.1 Publication

Keywords - PTMi

Disulfide bond, Glycoprotein, Phosphoprotein

Proteomic databases

MaxQBiP25391.
PaxDbiP25391.
PRIDEiP25391.

PTM databases

PhosphoSiteiP25391.

Expressioni

Gene expression databases

BgeeiP25391.
CleanExiHS_LAMA1.
ExpressionAtlasiP25391. baseline and differential.
GenevestigatoriP25391.

Organism-specific databases

HPAiCAB010179.
HPA032109.
HPA032110.

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-1 is a subunit of laminin-1 (laminin-111 or EHS laminin) and laminin-3 (laminin-121 or S-laminin).

Binary interactionsi

WithEntry#Exp.IntActNotes
p4cQ8BDF82EBI-2529668,EBI-7167339From a different organism.

Protein-protein interaction databases

BioGridi129792. 12 interactions.
DIPiDIP-29324N.
IntActiP25391. 2 interactions.
MINTiMINT-6740485.
STRINGi9606.ENSP00000374309.

Structurei

3D structure databases

ProteinModelPortaliP25391.
SMRiP25391. Positions 17-505, 708-1155, 1361-1544, 2128-2472, 2491-2674, 2701-3074.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini18 – 269252Laminin N-terminalPROSITE-ProRule annotationAdd
BLAST
Domaini270 – 32657Laminin EGF-like 1PROSITE-ProRule annotationAdd
BLAST
Domaini327 – 39670Laminin EGF-like 2PROSITE-ProRule annotationAdd
BLAST
Domaini397 – 45357Laminin EGF-like 3PROSITE-ProRule annotationAdd
BLAST
Domaini454 – 50249Laminin EGF-like 4PROSITE-ProRule annotationAdd
BLAST
Domaini503 – 51210Laminin EGF-like 5; first partPROSITE-ProRule annotation
Domaini516 – 708193Laminin IV type A 1PROSITE-ProRule annotationAdd
BLAST
Domaini709 – 74133Laminin EGF-like 5; second partPROSITE-ProRule annotationAdd
BLAST
Domaini742 – 79049Laminin EGF-like 6PROSITE-ProRule annotationAdd
BLAST
Domaini791 – 84858Laminin EGF-like 7PROSITE-ProRule annotationAdd
BLAST
Domaini849 – 90153Laminin EGF-like 8PROSITE-ProRule annotationAdd
BLAST
Domaini902 – 95049Laminin EGF-like 9PROSITE-ProRule annotationAdd
BLAST
Domaini951 – 99747Laminin EGF-like 10PROSITE-ProRule annotationAdd
BLAST
Domaini998 – 104346Laminin EGF-like 11PROSITE-ProRule annotationAdd
BLAST
Domaini1044 – 108946Laminin EGF-like 12PROSITE-ProRule annotationAdd
BLAST
Domaini1090 – 114960Laminin EGF-like 13PROSITE-ProRule annotationAdd
BLAST
Domaini1150 – 115910Laminin EGF-like 14; first partPROSITE-ProRule annotation
Domaini1170 – 1361192Laminin IV type A 2PROSITE-ProRule annotationAdd
BLAST
Domaini1362 – 140241Laminin EGF-like 14; second partPROSITE-ProRule annotationAdd
BLAST
Domaini1403 – 145149Laminin EGF-like 15PROSITE-ProRule annotationAdd
BLAST
Domaini1452 – 150857Laminin EGF-like 16PROSITE-ProRule annotationAdd
BLAST
Domaini1509 – 155547Laminin EGF-like 17PROSITE-ProRule annotationAdd
BLAST
Domaini2117 – 2297181Laminin G-like 1PROSITE-ProRule annotationAdd
BLAST
Domaini2305 – 2481177Laminin G-like 2PROSITE-ProRule annotationAdd
BLAST
Domaini2486 – 2673188Laminin G-like 3PROSITE-ProRule annotationAdd
BLAST
Domaini2713 – 2885173Laminin G-like 4PROSITE-ProRule annotationAdd
BLAST
Domaini2890 – 3070181Laminin G-like 5PROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1556 – 2116561Domain II and IAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili1706 – 179691Sequence AnalysisAdd
BLAST
Coiled coili1968 – 198922Sequence AnalysisAdd
BLAST
Coiled coili2088 – 212033Sequence AnalysisAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi2534 – 25363Cell attachment site

Domaini

The alpha-helical domains I and II are thought to interact with other laminin chains to form a coiled coil structure.
Domains VI, IV and G are globular.

Sequence similaritiesi

Contains 17 laminin EGF-like domains.PROSITE-ProRule annotation
Contains 5 laminin G-like domains.PROSITE-ProRule annotation
Contains 2 laminin IV type A domains.PROSITE-ProRule annotation
Contains 1 laminin N-terminal domain.PROSITE-ProRule annotation

Keywords - Domaini

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

Phylogenomic databases

eggNOGiNOG247347.
GeneTreeiENSGT00760000118860.
HOGENOMiHOG000293201.
HOVERGENiHBG052298.
InParanoidiP25391.
KOiK05637.
OMAiEPFYWRL.
OrthoDBiEOG7SR4KJ.
PhylomeDBiP25391.
TreeFamiTF335359.

Family and domain databases

Gene3Di2.60.120.200. 5 hits.
InterProiIPR013320. ConA-like_dom.
IPR002049. EGF_laminin.
IPR018031. Laminin_B_subgr.
IPR000034. Laminin_B_type_IV.
IPR010307. Laminin_domII.
IPR001791. Laminin_G.
IPR009254. Laminin_I.
IPR008211. Laminin_N.
[Graphical view]
PfamiPF00052. Laminin_B. 2 hits.
PF00053. Laminin_EGF. 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]
SMARTiSM00180. EGF_Lam. 15 hits.
SM00281. LamB. 2 hits.
SM00282. LamG. 5 hits.
SM00136. LamNT. 1 hit.
[Graphical view]
SUPFAMiSSF49899. SSF49899. 5 hits.
PROSITEiPS00022. 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]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P25391-1 [UniParc]FASTAAdd to Basket

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        10         20         30         40         50
MRGGVLLVLL LCVAAQCRQR GLFPAILNLA SNAHISTNAT CGEKGPEMFC
60 70 80 90 100
KLVEHVPGRP VRNPQCRICD GNSANPRERH PISHAIDGTN NWWQSPSIQN
110 120 130 140 150
GREYHWVTIT LDLRQVFQVA YVIIKAANAP RPGNWILERS LDGTTFSPWQ
160 170 180 190 200
YYAVSDSECL SRYNITPRRG PPTYRADDEV ICTSYYSRLV PLEHGEIHTS
210 220 230 240 250
LINGRPSADD LSPKLLEFTS ARYIRLRLQR IRTLNADLMT LSHREPKELD
260 270 280 290 300
PIVTRRYYYS IKDISVGGMC ICYGHASSCP WDETTKKLQC QCEHNTCGES
310 320 330 340 350
CNRCCPGYHQ QPWRPGTVSS GNTCEACNCH NKAKDCYYDE SVAKQKKSLN
360 370 380 390 400
TAGQFRGGGV CINCLQNTMG INCETCIDGY YRPHKVSPYE DEPCRPCNCD
410 420 430 440 450
PVGSLSSVCI KDDLHSDLHN GKQPGQCPCK EGYTGEKCDR CQLGYKDYPT
460 470 480 490 500
CVSCGCNPVG SASDEPCTGP CVCKENVEGK ACDRCKPGFY NLKEKNPRGC
510 520 530 540 550
SECFCFGVSD VCSSLSWPVG QVNSMSGWLV TDLISPRKIP SQQDALGGRH
560 570 580 590 600
QVSINNTAVM QRLAPKYYWA APEAYLGNKL TAFGGFLKYT VSYDIPVETV
610 620 630 640 650
DSNLMSHADV IIKGNGLTLS TQAEGLSLQP YEEYLNVVRL VPENFQDFHS
660 670 680 690 700
KRQIDRDQLM TVLANVTHLL IRANYNSAKM ALYRLESVSL DIASSNAIDL
710 720 730 740 750
VVAADVEHCE CPQGYTGTSC ESCLSGYYRV DGILFGGICQ PCECHGHAAE
760 770 780 790 800
CNVHGVCIAC AHNTTGVHCE QCLPGFYGEP SRGTPGDCQP CACPLTIASN
810 820 830 840 850
NFSPTCHLND GDEVVCDWCA PGYSGAWCER CADGYYGNPT VPGESCVPCD
860 870 880 890 900
CSGNVDPSEA GHCDSVTGEC LKCLGNTDGA HCERCADGFY GDAVTAKNCR
910 920 930 940 950
ACECHVKGSH SAVCHLETGL CDCKPNVTGQ QCDQCLHGYY GLDSGHGCRP
960 970 980 990 1000
CNCSVAGSVS DGCTDEGQCH CVPGVAGKRC DRCAHGFYAY QDGSCTPCDC
1010 1020 1030 1040 1050
PHTQNTCDPE TGECVCPPHT QGVKCEECED GHWGYDAEVG CQACNCSLVG
1060 1070 1080 1090 1100
STHHRCDVVT GHCQCKSKFG GRACDQCSLG YRDFPDCVPC DCDLRGTSGD
1110 1120 1130 1140 1150
ACNLEQGLCG CVEETGACPC KENVFGPQCN ECREGTFALR ADNPLGCSPC
1160 1170 1180 1190 1200
FCSGLSHLCS ELEDYVRTPV TLGSDQPLLR VVSQSNLRGT TEGVYYQAPD
1210 1220 1230 1240 1250
FLLDAATVRQ HIRAEPFYWR LPQQFQGDQL MAYGGKLKYS VAFYSLDGVG
1260 1270 1280 1290 1300
TSNFEPQVLI KGGRIRKQVI YMDAPAPENG VRQEQEVAMR ENFWKYFNSV
1310 1320 1330 1340 1350
SEKPVTREDF MSVLSDIEYI LIKASYGQGL QQSRISDISM EVGRKAEKLH
1360 1370 1380 1390 1400
PEEEVASLLE NCVCPPGTVG FSCQDCAPGY HRGKLPAGSD RGPRPLVAPC
1410 1420 1430 1440 1450
VPCSCNNHSD TCDPNTGKCL NCGDNTAGDH CDVCTSGYYG KVTGSASDCA
1460 1470 1480 1490 1500
LCACPHSPPA SFSPTCVLEG DHDFRCDACL LGYEGKHCER CSSSYYGNPQ
1510 1520 1530 1540 1550
TPGGSCQKCD CNPHGSVHGD CDRTSGQCVC RLGASGLRCD ECEPRHILME
1560 1570 1580 1590 1600
TDCVSCDDEC VGVLLNDLDE IGDAVLSLNL TGIIPVPYGI LSNLENTTKY
1610 1620 1630 1640 1650
LQESLLKENM QKDLGKIKLE GVAEETDNLQ KKLTRMLAST QKVNRATERI
1660 1670 1680 1690 1700
FKESQDLAIA IERLQMSITE IMEKTTLNQT LDEDFLLPNS TLQNMQQNGT
1710 1720 1730 1740 1750
SLLEIMQIRD FTQLHQNATL ELKAAEDLLS QIQENYQKPL EELEVLKEAA
1760 1770 1780 1790 1800
SHVLSKHNNE LKAAEALVRE AEAKMQESNH LLLMVNANLR EFSDKKLHVQ
1810 1820 1830 1840 1850
EEQNLTSELI VQGRGLIDAA AAQTDAVQDA LEHLEDHQDK LLLWSAKIRH
1860 1870 1880 1890 1900
HIDDLVMHMS QRNAVDLVYR AEDHAAEFQR LADVLYSGLE NIRNVSLNAT
1910 1920 1930 1940 1950
SAAYVHYNIQ SLIEESEELA RDAHRTVTET SLLSESLVSN GKAAVQRSSR
1960 1970 1980 1990 2000
FLKEGNNLSR KLPGIALELS ELRNKTNRFQ ENAVEITRQT NESLLILRAI
2010 2020 2030 2040 2050
PKGIRDKGAK TKELATSASQ SAVSTLRDVA GLSQELLNTS ASLSRVNTTL
2060 2070 2080 2090 2100
RETHQLLQDS TMATLLAGRK VKDVEIQANL LFDRLKPLKM LEENLSRNLS
2110 2120 2130 2140 2150
EIKLLISQAR KQAASIKVAV SADRDCIRAY QPQISSTNYN TLTLNVKTQE
2160 2170 2180 2190 2200
PDNLLFYLGS STASDFLAVE MRRGRVAFLW DLGSGSTRLE FPDFPIDDNR
2210 2220 2230 2240 2250
WHSIHVARFG NIGSLSVKEM SSNQKSPTKT SKSPGTANVL DVNNSTLMFV
2260 2270 2280 2290 2300
GGLGGQIKKS PAVKVTHFKG CLGEAFLNGK SIGLWNYIER EGKCRGCFGS
2310 2320 2330 2340 2350
SQNEDPSFHF DGSGYSVVEK SLPATVTQII MLFNTFSPNG LLLYLGSYGT
2360 2370 2380 2390 2400
KDFLSIELFR GRVKVMTDLG SGPITLLTDR RYNNGTWYKI AFQRNRKQGV
2410 2420 2430 2440 2450
LAVIDAYNTS NKETKQGETP GASSDLNRLD KDPIYVGGLP RSRVVRRGVT
2460 2470 2480 2490 2500
TKSFVGCIKN LEISRSTFDL LRNSYGVRKG CLLEPIRSVS FLKGGYIELP
2510 2520 2530 2540 2550
PKSLSPESEW LVTFATTNSS GIILAALGGD VEKRGDREEA HVPFFSVMLI
2560 2570 2580 2590 2600
GGNIEVHVNP GDGTGLRKAL LHAPTGTCSD GQAHSISLVR NRRIITVQLD
2610 2620 2630 2640 2650
ENNPVEMKLG TLVESRTINV SNLYVGGIPE GEGTSLLTMR RSFHGCIKNL
2660 2670 2680 2690 2700
IFNLELLDFN SAVGHEQVDL DTCWLSERPK LAPDAEDSKL LPEPRAFPEQ
2710 2720 2730 2740 2750
CVVDAALEYV PGAHQFGLTQ NSHFILPFNQ SAVRKKLSVE LSIRTFASSG
2760 2770 2780 2790 2800
LIYYMAHQNQ ADYAVLQLHG GRLHFMFDLG KGRTKVSHPA LLSDGKWHTV
2810 2820 2830 2840 2850
KTDYVKRKGF ITVDGRESPM VTVVGDGTML DVEGLFYLGG LPSQYQARKI
2860 2870 2880 2890 2900
GNITHSIPAC IGDVTVNSKQ LDKDSPVSAF TVNRCYAVAQ EGTYFDGSGY
2910 2920 2930 2940 2950
AALVKEGYKV QSDVNITLEF RTSSQNGVLL GISTAKVDAI GLELVDGKVL
2960 2970 2980 2990 3000
FHVNNGAGRI TAAYEPKTAT VLCDGKWHTL QANKSKHRIT LIVDGNAVGA
3010 3020 3030 3040 3050
ESPHTQSTSV DTNNPIYVGG YPAGVKQKCL RSQTSFRGCL RKLALIKSPQ
3060 3070
VQSFDFSRAF ELHGVFLHSC PGTES
Length:3,075
Mass (Da):337,084
Last modified:December 15, 2009 - v2
Checksum:i941167F8FE534745
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti228 – 2292LQ → FE in CAA41418. (PubMed:2049067)Curated
Sequence conflicti252 – 2543IVT → MLP in CAA41418. (PubMed:2049067)Curated
Sequence conflicti419 – 4191H → E in CAA41418. (PubMed:2049067)Curated
Sequence conflicti519 – 5191V → L in CAA41418. (PubMed:2049067)Curated
Sequence conflicti1023 – 10231V → G(PubMed:1714537)Curated
Sequence conflicti1075 – 10751D → V in CAA41418. (PubMed:2049067)Curated
Sequence conflicti1513 – 15131P → R(PubMed:1714537)Curated
Sequence conflicti1659 – 16591I → V(PubMed:1714537)Curated
Sequence conflicti1659 – 16591I → V in CAA41418. (PubMed:2049067)Curated
Sequence conflicti2079 – 20802NL → KV in CAA41418. (PubMed:2049067)Curated
Sequence conflicti2692 – 26921P → R(PubMed:1714537)Curated
Sequence conflicti2692 – 26921P → R(PubMed:2733383)Curated
Sequence conflicti2746 – 27461F → L(PubMed:2733383)Curated
Sequence conflicti2962 – 29621A → P(PubMed:1714537)Curated
Sequence conflicti2962 – 29621A → P(PubMed:2733383)Curated
Sequence conflicti3054 – 30541F → L(PubMed:2733383)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti349 – 3491L → S.
Corresponds to variant rs9950267 [ dbSNP | Ensembl ].
VAR_056132
Natural varianti559 – 5591V → I.
Corresponds to variant rs16951079 [ dbSNP | Ensembl ].
VAR_056133
Natural varianti674 – 6741N → T.2 Publications
Corresponds to variant rs566655 [ dbSNP | Ensembl ].
VAR_060785
Natural varianti1340 – 13401M → V.1 Publication
Corresponds to variant rs662471 [ dbSNP | Ensembl ].
VAR_060786
Natural varianti1577 – 15771S → A.
Corresponds to variant rs12961939 [ dbSNP | Ensembl ].
VAR_056134
Natural varianti1591 – 15911L → V.
Corresponds to variant rs596315 [ dbSNP | Ensembl ].
VAR_056135
Natural varianti1632 – 16321K → E.
Corresponds to variant rs11872364 [ dbSNP | Ensembl ].
VAR_056136
Natural varianti1682 – 16821D → V.
Corresponds to variant rs16950981 [ dbSNP | Ensembl ].
VAR_056137
Natural varianti1876 – 18761A → T.2 Publications
Corresponds to variant rs11664063 [ dbSNP | Ensembl ].
VAR_060787
Natural varianti2002 – 20021K → E.2 Publications
Corresponds to variant rs607230 [ dbSNP | Ensembl ].
VAR_060788
Natural varianti2076 – 20761I → T.
Corresponds to variant rs671871 [ dbSNP | Ensembl ].
VAR_056138
Natural varianti2511 – 25111L → M.
Corresponds to variant rs60009920 [ dbSNP | Ensembl ].
VAR_061347
Natural varianti2611 – 26111T → A.
Corresponds to variant rs543355 [ dbSNP | Ensembl ].
VAR_056139

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AP002409 Genomic DNA. No translation available.
AP005062 Genomic DNA. No translation available.
AP005210 Genomic DNA. No translation available.
X58531 mRNA. Translation: CAA41418.1.
CCDSiCCDS32787.1.
PIRiS14458.
RefSeqiNP_005550.2. NM_005559.3.
UniGeneiHs.270364.

Genome annotation databases

EnsembliENST00000389658; ENSP00000374309; ENSG00000101680.
GeneIDi284217.
KEGGihsa:284217.
UCSCiuc002knm.3. human.

Polymorphism databases

DMDMi281185471.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AP002409 Genomic DNA. No translation available.
AP005062 Genomic DNA. No translation available.
AP005210 Genomic DNA. No translation available.
X58531 mRNA. Translation: CAA41418.1 .
CCDSi CCDS32787.1.
PIRi S14458.
RefSeqi NP_005550.2. NM_005559.3.
UniGenei Hs.270364.

3D structure databases

ProteinModelPortali P25391.
SMRi P25391. Positions 17-505, 708-1155, 1361-1544, 2128-2472, 2491-2674, 2701-3074.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 129792. 12 interactions.
DIPi DIP-29324N.
IntActi P25391. 2 interactions.
MINTi MINT-6740485.
STRINGi 9606.ENSP00000374309.

Chemistry

ChEMBLi CHEMBL2364187.

PTM databases

PhosphoSitei P25391.

Polymorphism databases

DMDMi 281185471.

Proteomic databases

MaxQBi P25391.
PaxDbi P25391.
PRIDEi P25391.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000389658 ; ENSP00000374309 ; ENSG00000101680 .
GeneIDi 284217.
KEGGi hsa:284217.
UCSCi uc002knm.3. human.

Organism-specific databases

CTDi 284217.
GeneCardsi GC18M006941.
H-InvDB HIX0014316.
HGNCi HGNC:6481. LAMA1.
HPAi CAB010179.
HPA032109.
HPA032110.
MIMi 150320. gene.
neXtProti NX_P25391.
PharmGKBi PA30270.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG247347.
GeneTreei ENSGT00760000118860.
HOGENOMi HOG000293201.
HOVERGENi HBG052298.
InParanoidi P25391.
KOi K05637.
OMAi EPFYWRL.
OrthoDBi EOG7SR4KJ.
PhylomeDBi P25391.
TreeFami TF335359.

Enzyme and pathway databases

Reactomei REACT_163874. Non-integrin membrane-ECM interactions.
REACT_163906. ECM proteoglycans.
REACT_169262. Laminin interactions.
REACT_22205. L1CAM interactions.

Miscellaneous databases

ChiTaRSi LAMA1. human.
GeneWikii Laminin,_alpha_1.
GenomeRNAii 284217.
NextBioi 94628.
PROi P25391.
SOURCEi Search...

Gene expression databases

Bgeei P25391.
CleanExi HS_LAMA1.
ExpressionAtlasi P25391. baseline and differential.
Genevestigatori P25391.

Family and domain databases

Gene3Di 2.60.120.200. 5 hits.
InterProi IPR013320. ConA-like_dom.
IPR002049. EGF_laminin.
IPR018031. Laminin_B_subgr.
IPR000034. Laminin_B_type_IV.
IPR010307. Laminin_domII.
IPR001791. Laminin_G.
IPR009254. Laminin_I.
IPR008211. Laminin_N.
[Graphical view ]
Pfami PF00052. Laminin_B. 2 hits.
PF00053. Laminin_EGF. 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 ]
SMARTi SM00180. EGF_Lam. 15 hits.
SM00281. LamB. 2 hits.
SM00282. LamG. 5 hits.
SM00136. LamNT. 1 hit.
[Graphical view ]
SUPFAMi SSF49899. SSF49899. 5 hits.
PROSITEi 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 ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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. 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.
    Tissue: Liver.
  6. Cited for: PHOSPHORYLATION.

Entry informationi

Entry nameiLAMA1_HUMAN
AccessioniPrimary (citable) accession number: P25391
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 1, 1992
Last sequence update: December 15, 2009
Last modified: November 26, 2014
This is version 156 of the entry and version 2 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, Reference proteome

Documents

  1. Human chromosome 18
    Human chromosome 18: 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