UniProtKB - P11046 (LAMB1_DROME)
Protein
Laminin subunit beta-1
Gene
LanB1
Organism
Drosophila melanogaster (Fruit fly)
Status
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 (By similarity). Required for Ndg localization to the basement membrane (PubMed:30260959).By similarity1 Publication
GO - Biological processi
- animal organ development Source: FlyBase
- animal organ morphogenesis Source: GO_Central
- basement membrane assembly Source: FlyBase
- basement membrane organization Source: UniProtKB
- cardiac muscle cell development Source: FlyBase
- cell adhesion mediated by integrin Source: FlyBase
- cell migration Source: FlyBase
- defense response to Gram-negative bacterium Source: FlyBase
- embryonic heart tube morphogenesis Source: FlyBase
- extracellular matrix organization Source: FlyBase
- gonad development Source: FlyBase
- positive regulation of innate immune response Source: FlyBase
- substrate adhesion-dependent cell spreading Source: FlyBase
- tissue development Source: GO_Central
Keywordsi
Biological process | Cell adhesion |
Enzyme and pathway databases
Reactomei | R-DME-1474228, Degradation of the extracellular matrix R-DME-3000157, Laminin interactions R-DME-373752, Netrin-1 signaling R-DME-381426, Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs) R-DME-446107, Type I hemidesmosome assembly R-DME-8957275, Post-translational protein phosphorylation |
Names & Taxonomyi
Protein namesi | Recommended name: Laminin subunit beta-1Alternative name(s): Laminin B1 chain |
Gene namesi | Name:LanB1 Synonyms:lamB1 ORF Names:CG7123 |
Organismi | Drosophila melanogaster (Fruit fly) |
Taxonomic identifieri | 7227 [NCBI] |
Taxonomic lineagei | Eukaryota › Metazoa › Ecdysozoa › Arthropoda › Hexapoda › Insecta › Pterygota › Neoptera › Holometabola › Diptera › Brachycera › Muscomorpha › Ephydroidea › Drosophilidae › Drosophila › Sophophora › |
Proteomesi |
|
Organism-specific databases
FlyBasei | FBgn0261800, LanB1 |
Subcellular locationi
Extracellular region or secreted
- basement membrane 1 Publication
Extracellular region or secreted
- extracellular region Source: UniProtKB-KW
Other locations
- basement membrane Source: FlyBase
- collagen-containing extracellular matrix Source: FlyBase
- laminin complex Source: GO_Central
Keywords - Cellular componenti
Basement membrane, Extracellular matrix, SecretedPathology & Biotechi
Disruption phenotypei
PTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Signal peptidei | 1 – 24 | Sequence analysisAdd BLAST | 24 | |
ChainiPRO_0000017073 | 25 – 1788 | Laminin subunit beta-1Add BLAST | 1764 |
Amino acid modifications
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Glycosylationi | 138 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Glycosylationi | 201 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Glycosylationi | 232 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Disulfide bondi | 288 ↔ 297 | PROSITE-ProRule annotation | ||
Disulfide bondi | 290 ↔ 318 | PROSITE-ProRule annotation | ||
Disulfide bondi | 320 ↔ 329 | PROSITE-ProRule annotation | ||
Disulfide bondi | 332 ↔ 352 | PROSITE-ProRule annotation | ||
Disulfide bondi | 355 ↔ 364 | PROSITE-ProRule annotation | ||
Disulfide bondi | 357 ↔ 382 | PROSITE-ProRule annotation | ||
Disulfide bondi | 385 ↔ 394 | PROSITE-ProRule annotation | ||
Disulfide bondi | 397 ↔ 415 | PROSITE-ProRule annotation | ||
Disulfide bondi | 418 ↔ 431 | PROSITE-ProRule annotation | ||
Disulfide bondi | 420 ↔ 446 | PROSITE-ProRule annotation | ||
Disulfide bondi | 448 ↔ 457 | PROSITE-ProRule annotation | ||
Disulfide bondi | 460 ↔ 475 | PROSITE-ProRule annotation | ||
Disulfide bondi | 478 ↔ 491 | PROSITE-ProRule annotation | ||
Disulfide bondi | 480 ↔ 498 | PROSITE-ProRule annotation | ||
Glycosylationi | 487 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Disulfide bondi | 500 ↔ 509 | PROSITE-ProRule annotation | ||
Disulfide bondi | 512 ↔ 526 | PROSITE-ProRule annotation | ||
Disulfide bondi | 529 ↔ 541 | PROSITE-ProRule annotation | ||
Disulfide bondi | 531 ↔ 548 | PROSITE-ProRule annotation | ||
Disulfide bondi | 550 ↔ 559 | PROSITE-ProRule annotation | ||
Glycosylationi | 591 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Disulfide bondi | 789 ↔ 801 | PROSITE-ProRule annotation | ||
Disulfide bondi | 791 ↔ 808 | PROSITE-ProRule annotation | ||
Disulfide bondi | 810 ↔ 819 | PROSITE-ProRule annotation | ||
Disulfide bondi | 822 ↔ 834 | PROSITE-ProRule annotation | ||
Disulfide bondi | 837 ↔ 849 | PROSITE-ProRule annotation | ||
Disulfide bondi | 839 ↔ 856 | PROSITE-ProRule annotation | ||
Disulfide bondi | 858 ↔ 867 | PROSITE-ProRule annotation | ||
Disulfide bondi | 870 ↔ 880 | PROSITE-ProRule annotation | ||
Disulfide bondi | 883 ↔ 892 | PROSITE-ProRule annotation | ||
Disulfide bondi | 885 ↔ 899 | PROSITE-ProRule annotation | ||
Disulfide bondi | 902 ↔ 911 | PROSITE-ProRule annotation | ||
Disulfide bondi | 914 ↔ 930 | PROSITE-ProRule annotation | ||
Disulfide bondi | 933 ↔ 949 | PROSITE-ProRule annotation | ||
Disulfide bondi | 935 ↔ 960 | PROSITE-ProRule annotation | ||
Disulfide bondi | 962 ↔ 971 | PROSITE-ProRule annotation | ||
Disulfide bondi | 974 ↔ 988 | PROSITE-ProRule annotation | ||
Disulfide bondi | 991 ↔ 1005 | PROSITE-ProRule annotation | ||
Disulfide bondi | 993 ↔ 1012 | PROSITE-ProRule annotation | ||
Disulfide bondi | 1015 ↔ 1024 | PROSITE-ProRule annotation | ||
Disulfide bondi | 1027 ↔ 1040 | PROSITE-ProRule annotation | ||
Disulfide bondi | 1043 ↔ 1057 | PROSITE-ProRule annotation | ||
Disulfide bondi | 1045 ↔ 1064 | PROSITE-ProRule annotation | ||
Glycosylationi | 1051 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Disulfide bondi | 1066 ↔ 1075 | PROSITE-ProRule annotation | ||
Disulfide bondi | 1078 ↔ 1091 | PROSITE-ProRule annotation | ||
Disulfide bondi | 1094 ↔ 1106 | PROSITE-ProRule annotation | ||
Disulfide bondi | 1096 ↔ 1113 | PROSITE-ProRule annotation | ||
Disulfide bondi | 1115 ↔ 1124 | PROSITE-ProRule annotation | ||
Disulfide bondi | 1127 ↔ 1139 | PROSITE-ProRule annotation | ||
Disulfide bondi | 1142 ↔ 1154 | PROSITE-ProRule annotation | ||
Disulfide bondi | 1144 ↔ 1161 | PROSITE-ProRule annotation | ||
Disulfide bondi | 1163 ↔ 1172 | PROSITE-ProRule annotation | ||
Disulfide bondi | 1175 ↔ 1186 | PROSITE-ProRule annotation | ||
Disulfide bondi | 1189 | InterchainCurated | ||
Disulfide bondi | 1192 | InterchainCurated | ||
Glycosylationi | 1246 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Glycosylationi | 1301 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Glycosylationi | 1330 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Glycosylationi | 1341 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Glycosylationi | 1473 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Glycosylationi | 1493 | N-linked (GlcNAc...) asparagine1 Publication | 1 | |
Glycosylationi | 1515 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Glycosylationi | 1581 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Glycosylationi | 1644 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Glycosylationi | 1703 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Disulfide bondi | 1786 | InterchainCurated |
Keywords - PTMi
Disulfide bond, GlycoproteinProteomic databases
PaxDbi | P11046 |
PRIDEi | P11046 |
PTM databases
iPTMneti | P11046 |
Expressioni
Tissue specificityi
Found in the basement membranes (major component).
Developmental stagei
In the larva, expressed mainly by fat body adipocytes and blood cells and secreted in the basal membranes that surround the fat body, imaginal disks, tracheae, salivary glands, midgut, mature muscles and heart (at protein level).1 Publication
Gene expression databases
Bgeei | FBgn0261800, Expressed in embryonic/larval hemocyte (Drosophila) and 42 other tissues |
Genevisiblei | P11046, DM |
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.
Protein-protein interaction databases
BioGRIDi | 60207, 27 interactors |
IntActi | P11046, 9 interactors |
STRINGi | 7227.FBpp0079113 |
Family & Domainsi
Domains and Repeats
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Domaini | 50 – 287 | Laminin N-terminalPROSITE-ProRule annotationAdd BLAST | 238 | |
Domaini | 288 – 354 | Laminin EGF-like 1PROSITE-ProRule annotationAdd BLAST | 67 | |
Domaini | 355 – 417 | Laminin EGF-like 2PROSITE-ProRule annotationAdd BLAST | 63 | |
Domaini | 418 – 477 | Laminin EGF-like 3PROSITE-ProRule annotationAdd BLAST | 60 | |
Domaini | 478 – 528 | Laminin EGF-like 4PROSITE-ProRule annotationAdd BLAST | 51 | |
Domaini | 529 – 559 | Laminin EGF-like 5; truncatedPROSITE-ProRule annotationAdd BLAST | 31 | |
Domaini | 567 – 783 | Laminin IV type BPROSITE-ProRule annotationAdd BLAST | 217 | |
Domaini | 789 – 836 | Laminin EGF-like 6PROSITE-ProRule annotationAdd BLAST | 48 | |
Domaini | 837 – 882 | Laminin EGF-like 7PROSITE-ProRule annotationAdd BLAST | 46 | |
Domaini | 883 – 932 | Laminin EGF-like 8PROSITE-ProRule annotationAdd BLAST | 50 | |
Domaini | 933 – 990 | Laminin EGF-like 9PROSITE-ProRule annotationAdd BLAST | 58 | |
Domaini | 991 – 1042 | Laminin EGF-like 10PROSITE-ProRule annotationAdd BLAST | 52 | |
Domaini | 1043 – 1093 | Laminin EGF-like 11PROSITE-ProRule annotationAdd BLAST | 51 | |
Domaini | 1094 – 1141 | Laminin EGF-like 12PROSITE-ProRule annotationAdd BLAST | 48 | |
Domaini | 1142 – 1188 | Laminin EGF-like 13PROSITE-ProRule annotationAdd BLAST | 47 |
Region
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Regioni | 1189 – 1405 | Domain IIAdd BLAST | 217 | |
Regioni | 1406 – 1432 | Domain alphaAdd BLAST | 27 | |
Regioni | 1433 – 1788 | Domain IAdd BLAST | 356 |
Coiled coil
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Coiled coili | 1255 – 1405 | Sequence analysisAdd BLAST | 151 | |
Coiled coili | 1453 – 1505 | Sequence analysisAdd BLAST | 53 | |
Coiled coili | 1540 – 1561 | Sequence analysisAdd BLAST | 22 | |
Coiled coili | 1608 – 1762 | Sequence analysisAdd BLAST | 155 |
Motif
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Motifi | 641 – 643 | Cell attachment siteSequence analysis | 3 |
Domaini
The alpha-helical domains I and II are thought to interact with other laminin chains to form a coiled coil structure.
Domains VI and IV are globular.
Keywords - Domaini
Coiled coil, Laminin EGF-like domain, Repeat, SignalPhylogenomic databases
eggNOGi | KOG0994, Eukaryota |
GeneTreei | ENSGT00940000167171 |
HOGENOMi | CLU_001560_1_0_1 |
InParanoidi | P11046 |
OMAi | QCQPCEC |
OrthoDBi | 65841at2759 |
PhylomeDBi | P11046 |
Family and domain databases
Gene3Di | 2.60.120.1490, 1 hit |
InterProi | View protein in InterPro IPR000742, EGF-like_dom IPR002049, Laminin_EGF IPR013015, Laminin_IV_B IPR008211, Laminin_N IPR038684, Laminin_N_sf |
Pfami | View protein in Pfam PF00053, Laminin_EGF, 13 hits PF00055, Laminin_N, 1 hit |
SMARTi | View protein in SMART SM00181, EGF, 8 hits SM00180, EGF_Lam, 13 hits SM00136, LamNT, 1 hit |
PROSITEi | View protein in PROSITE PS00022, EGF_1, 10 hits PS01186, EGF_2, 2 hits PS01248, EGF_LAM_1, 12 hits PS50027, EGF_LAM_2, 13 hits PS51116, LAMININ_IVB, 1 hit PS51117, LAMININ_NTER, 1 hit |
i Sequence
Sequence statusi: Complete.
: The displayed sequence is further processed into a mature form. Sequence processingi
P11046-1 [UniParc]FASTAAdd to basket
10 20 30 40 50
MLELRLIVVI VLALLSWQWD PVDSQRPPQH GRRDRPKYPP NKFIKTHPCE
60 70 80 90 100
RSSCYPATGN LLIGRENRLT ASSTCGLHSP ERFCILSHLQ DKKCFLCDTR
110 120 130 140 150
EETKHDPYKN HRIGQIIYKT KPGTNIPTWW QSENGKENAT IQLDLEAEFH
160 170 180 190 200
FTHLIITFTT FRPAAMYIER SFDFGQTWHI YRYFAYDCKE SFPGVPTVLE
210 220 230 240 250
NITDVMCTSR YSNVEPSRNG EVIFRVLPPN INVTDPYAEH VQNQLKMTNL
260 270 280 290 300
RIQMTKLHKL GDNLLDSRLE NEEKYYYGIS NMVVRGSCSC YGHASQCLPL
310 320 330 340 350
DPAFSQADNE DGMVHGRCEC THNTKGMNCE ECEDFFNDLP WKPAFGKKTN
360 370 380 390 400
ACKKCECNDH AVSCHFDEAV FTASGFVSGG VCDNCLHNTR GQHCEECMPY
410 420 430 440 450
FYRDPEQDIT SERVCQPCDC DPQGSSDDGI CDSLNELEEG AVAGACHCKA
460 470 480 490 500
FVTGRRCNQC KDGYWNLQSD NPEGCEPCTC NPLGTLNNSG CVMRTGECKC
510 520 530 540 550
KKYVTGKDCN QCMPETYGLS ESPEGCSLCN CDAGGSYDNY CDVISGQCRC
560 570 580 590 600
RPHMTGRSCS QPKQNYFIPL LPEVHEAEVV DECISYGANG NCSLVAETPD
610 620 630 640 650
GSFTGIGFTR VPENSELVFT VGDIPRSMPY DAVIRYQSTS RGDWENAFIT
660 670 680 690 700
LVRPDQVDPE GGCGELAAAT SSETRIPFSL PDRSRQVVAL NEVCLEAGKV
710 720 730 740 750
YKFRIYFERK RHDVDSPTAT ILVDSLTLIP RIDVTPIFQG SVLADIRKKD
760 770 780 790 800
YEKYNCKSSL YDMNYKSDPK CQNLDNILSV FVHDGASMCN CNPTGSLSKV
810 820 830 840 850
CESNGGYCQC KPNVVGRQCD QCAPGTYGFG PEGCKACDCN SIGSKDKYCD
860 870 880 890 900
LITGQCQCVP NTYGRECNQC QPGYWNFPEC RVCQCNGHAA TCDPIQGTCI
910 920 930 940 950
DCQDSTTGYS CDSCLDGYYG NPLFGSEIGC RPCRCPETVA SGLAHADGCS
960 970 980 990 1000
LDTRNNNMLC HCQEGYSGSR CEICADNFFG NPDNGGTCSK CECSNNVDLY
1010 1020 1030 1040 1050
DTGNCDRQTG ACLKCLYQTT GDHCELCKDG FFGDALQQNC QQCECDFLGT
1060 1070 1080 1090 1100
NNTIAHCDRF TGQCPCLPNV QGVRCDQCAE NHWKIASGEG CESCNCDPIG
1110 1120 1130 1140 1150
ALHEQCNSYT GQCQCKPGFG GRACNQCQAH YWGNPNEKCQ PCECDQFGAA
1160 1170 1180 1190 1200
DFQCDRETGN CVCHEGIGGY KCNECARGYI GQFPHCSPCG ECFNNWDLIL
1210 1220 1230 1240 1250
SALEDATTAT ILRAKEIKQV GATGAYTSEF SELDKKLQHI RNLLQNTSVS
1260 1270 1280 1290 1300
LVDIEKLDYE TQSLRDQLQA SHGRLSETEQ NLDDIYNSLS LSGVELESLQ
1310 1320 1330 1340 1350
NHSRLVQQLS KELKENGIQL QESNIEGALN LTRHAYERVS NLSTLKDEAN
1360 1370 1380 1390 1400
ELASNTDRNC KRVENLSNKI QAEADDLANN NKLIEDYRAE LTSLTSQIPE
1410 1420 1430 1440 1450
LNNQVCGKPG DPCDSLCGGA GCGHCGGFLS CEHGAKTHSE EALKVAKDAE
1460 1470 1480 1490 1500
TAITSKKDQA DQTIRALTQA KLNASEAYEK AKRGFEQSER YLNQTNANIK
1510 1520 1530 1540 1550
LAENLFIALN NFQENKTASP SESKELAQKT LDLDLKLEPE EIETLGDQIN
1560 1570 1580 1590 1600
RAVSSLKNVE AIIYRTKPDL DRVNNLQSIA NATKEKADKI LDSANSVVES
1610 1620 1630 1640 1650
LAAADESQGK AKDAIQQANS NIELAGQDLE KIDEETYSAE APANNTAQQV
1660 1670 1680 1690 1700
EKLAKKVQKL QNNIMKNDRD AKEITKEAGS VKLEAMRARG EANNLQSATS
1710 1720 1730 1740 1750
ATNQTLTDRA SRSENARERA KQLLQRASKL TVDTNAKLKD LNDLQTVYLN
1760 1770 1780
KNQQLLRLQA EIGPLNKELN EHLIHIKERG SHYRQCYT
Sequence cautioni
The sequence AAM11329 differs from that shown. Reason: Erroneous initiation. Truncated N-terminus.Curated
The sequence AAT94451 differs from that shown. Reason: Frameshift.Curated
Experimental Info
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Sequence conflicti | 12 | L → LAL in AAD19752 (PubMed:8397815).Curated | 1 | |
Sequence conflicti | 12 | L → LAL in AAA28663 (PubMed:3365769).Curated | 1 | |
Sequence conflicti | 666 | L → H in AAD19752 (PubMed:8397815).Curated | 1 | |
Sequence conflicti | 724 – 725 | DS → VT in AAA28663 (PubMed:3365769).Curated | 2 | |
Sequence conflicti | 766 – 767 | KS → NA in AAD19752 (PubMed:8397815).Curated | 2 | |
Sequence conflicti | 766 – 767 | KS → NA in AAA28663 (PubMed:3365769).Curated | 2 | |
Sequence conflicti | 939 | V → I in AAT94451 (Ref. 5) Curated | 1 | |
Sequence conflicti | 946 – 947 | Missing in AAD19752 (PubMed:8397815).Curated | 2 | |
Sequence conflicti | 946 – 947 | Missing in AAA28663 (PubMed:3365769).Curated | 2 | |
Sequence conflicti | 1356 – 1373 | TDRNC…KIQAE → SDRIAREWKICLIRFRPN in AAD19752 (PubMed:8397815).CuratedAdd BLAST | 18 | |
Sequence conflicti | 1356 – 1373 | TDRNC…KIQAE → SDRIAREWKICLIRFRPN in AAA28663 (PubMed:3365769).CuratedAdd BLAST | 18 |
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | M95811 Genomic DNA Translation: AAD19752.1 M19525 mRNA Translation: AAA28663.1 AE014134 Genomic DNA Translation: AAF52563.1 AE014134 Genomic DNA Translation: AAN10647.1 BT015222 mRNA Translation: AAT94451.1 Frameshift. AY095001 mRNA Translation: AAM11329.1 Different initiation. |
PIRi | A28783, MMFFB1 |
RefSeqi | NP_476618.1, NM_057270.5 NP_723319.1, NM_164773.3 |
Genome annotation databases
EnsemblMetazoai | FBtr0079490; FBpp0079113; FBgn0261800 FBtr0079491; FBpp0079114; FBgn0261800 |
GeneIDi | 34068 |
KEGGi | dme:Dmel_CG7123 |
Similar proteinsi
Cross-referencesi
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | M95811 Genomic DNA Translation: AAD19752.1 M19525 mRNA Translation: AAA28663.1 AE014134 Genomic DNA Translation: AAF52563.1 AE014134 Genomic DNA Translation: AAN10647.1 BT015222 mRNA Translation: AAT94451.1 Frameshift. AY095001 mRNA Translation: AAM11329.1 Different initiation. |
PIRi | A28783, MMFFB1 |
RefSeqi | NP_476618.1, NM_057270.5 NP_723319.1, NM_164773.3 |
3D structure databases
SMRi | P11046 |
ModBasei | Search... |
Protein-protein interaction databases
BioGRIDi | 60207, 27 interactors |
IntActi | P11046, 9 interactors |
STRINGi | 7227.FBpp0079113 |
PTM databases
iPTMneti | P11046 |
Proteomic databases
PaxDbi | P11046 |
PRIDEi | P11046 |
Genome annotation databases
EnsemblMetazoai | FBtr0079490; FBpp0079113; FBgn0261800 FBtr0079491; FBpp0079114; FBgn0261800 |
GeneIDi | 34068 |
KEGGi | dme:Dmel_CG7123 |
Organism-specific databases
CTDi | 34068 |
FlyBasei | FBgn0261800, LanB1 |
Phylogenomic databases
eggNOGi | KOG0994, Eukaryota |
GeneTreei | ENSGT00940000167171 |
HOGENOMi | CLU_001560_1_0_1 |
InParanoidi | P11046 |
OMAi | QCQPCEC |
OrthoDBi | 65841at2759 |
PhylomeDBi | P11046 |
Enzyme and pathway databases
Reactomei | R-DME-1474228, Degradation of the extracellular matrix R-DME-3000157, Laminin interactions R-DME-373752, Netrin-1 signaling R-DME-381426, Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs) R-DME-446107, Type I hemidesmosome assembly R-DME-8957275, Post-translational protein phosphorylation |
Miscellaneous databases
BioGRID-ORCSi | 34068, 0 hits in 3 CRISPR screens |
ChiTaRSi | LanB1, fly |
GenomeRNAii | 34068 |
PROi | PR:P11046 |
Gene expression databases
Bgeei | FBgn0261800, Expressed in embryonic/larval hemocyte (Drosophila) and 42 other tissues |
Genevisiblei | P11046, DM |
Family and domain databases
Gene3Di | 2.60.120.1490, 1 hit |
InterProi | View protein in InterPro IPR000742, EGF-like_dom IPR002049, Laminin_EGF IPR013015, Laminin_IV_B IPR008211, Laminin_N IPR038684, Laminin_N_sf |
Pfami | View protein in Pfam PF00053, Laminin_EGF, 13 hits PF00055, Laminin_N, 1 hit |
SMARTi | View protein in SMART SM00181, EGF, 8 hits SM00180, EGF_Lam, 13 hits SM00136, LamNT, 1 hit |
PROSITEi | View protein in PROSITE PS00022, EGF_1, 10 hits PS01186, EGF_2, 2 hits PS01248, EGF_LAM_1, 12 hits PS50027, EGF_LAM_2, 13 hits PS51116, LAMININ_IVB, 1 hit PS51117, LAMININ_NTER, 1 hit |
ProtoNeti | Search... |
MobiDBi | Search... |
Entry informationi
Entry namei | LAMB1_DROME | |
Accessioni | P11046Primary (citable) accession number: P11046 Secondary accession number(s): A4V0D8 Q9XZT4 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | July 1, 1989 |
Last sequence update: | November 13, 2007 | |
Last modified: | April 7, 2021 | |
This is version 199 of the entry and version 4 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Drosophila annotation project |
Miscellaneousi
Keywords - Technical termi
Reference proteomeDocuments
- Drosophila
Drosophila: entries, gene names and cross-references to FlyBase