UniProtKB - Q61292 (LAMB2_MOUSE)
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Protein
Laminin subunit beta-2
Gene
Lamb2
Organism
Mus musculus (Mouse)
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.1 Publication
Laminin-3 (S-laminin) regulates the formation of motor nerve terminals.1 Publication
GO - Molecular functioni
- integrin binding Source: MGI
GO - Biological processi
- astrocyte development Source: MGI
- axon extension involved in regeneration Source: MGI
- axon guidance Source: MGI
- cell adhesion Source: UniProtKB-KW
- cell morphogenesis involved in differentiation Source: MGI
- metanephric glomerular basement membrane development Source: MGI
- metanephric glomerular visceral epithelial cell development Source: MGI
- neuromuscular junction development Source: MGI
- neuron projection development Source: MGI
- retina development in camera-type eye Source: MGI
- Schwann cell development Source: MGI
- synapse organization Source: MGI
- visual perception Source: MGI
Keywordsi
Biological process | Cell adhesion |
Enzyme and pathway databases
Reactomei | R-MMU-3000157 Laminin interactions R-MMU-381426 Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs) R-MMU-8874081 MET activates PTK2 signaling R-MMU-8957275 Post-translational protein phosphorylation |
Names & Taxonomyi
Protein namesi | Recommended name: Laminin subunit beta-2Alternative name(s): Laminin-11 subunit beta Laminin-14 subunit beta Laminin-15 subunit beta Laminin-3 subunit beta Laminin-4 subunit beta Laminin-7 subunit beta Laminin-9 subunit beta S-laminin subunit beta Short name: S-LAM beta |
Gene namesi | Name:Lamb2 Synonyms:Lams |
Organismi | Mus musculus (Mouse) |
Taxonomic identifieri | 10090 [NCBI] |
Taxonomic lineagei | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Myomorpha › Muroidea › Muridae › Murinae › Mus › Mus |
Proteomesi |
|
Organism-specific databases
MGIi | MGI:99916 Lamb2 |
Subcellular locationi
Keywords - Cellular componenti
Basement membrane, Extracellular matrix, SecretedPTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Signal peptidei | 1 – 35 | Sequence analysisAdd BLAST | 35 | |
ChainiPRO_0000017069 | 36 – 1799 | Laminin subunit beta-2Add BLAST | 1764 |
Amino acid modifications
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Glycosylationi | 251 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Disulfide bondi | 286 ↔ 295 | PROSITE-ProRule annotation | ||
Disulfide bondi | 288 ↔ 313 | PROSITE-ProRule annotation | ||
Disulfide bondi | 315 ↔ 324 | PROSITE-ProRule annotation | ||
Disulfide bondi | 327 ↔ 347 | PROSITE-ProRule annotation | ||
Disulfide bondi | 350 ↔ 359 | PROSITE-ProRule annotation | ||
Disulfide bondi | 352 ↔ 377 | PROSITE-ProRule annotation | ||
Glycosylationi | 371 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Disulfide bondi | 380 ↔ 389 | PROSITE-ProRule annotation | ||
Disulfide bondi | 392 ↔ 410 | PROSITE-ProRule annotation | ||
Disulfide bondi | 413 ↔ 426 | PROSITE-ProRule annotation | ||
Disulfide bondi | 415 ↔ 441 | PROSITE-ProRule annotation | ||
Disulfide bondi | 443 ↔ 452 | PROSITE-ProRule annotation | ||
Disulfide bondi | 455 ↔ 470 | PROSITE-ProRule annotation | ||
Disulfide bondi | 473 ↔ 487 | PROSITE-ProRule annotation | ||
Disulfide bondi | 475 ↔ 494 | PROSITE-ProRule annotation | ||
Disulfide bondi | 496 ↔ 505 | PROSITE-ProRule annotation | ||
Disulfide bondi | 508 ↔ 522 | PROSITE-ProRule annotation | ||
Disulfide bondi | 525 ↔ 537 | PROSITE-ProRule annotation | ||
Disulfide bondi | 527 ↔ 544 | PROSITE-ProRule annotation | ||
Disulfide bondi | 546 ↔ 555 | PROSITE-ProRule annotation | ||
Disulfide bondi | 784 ↔ 796 | PROSITE-ProRule annotation | ||
Disulfide bondi | 786 ↔ 803 | PROSITE-ProRule annotation | ||
Disulfide bondi | 805 ↔ 814 | PROSITE-ProRule annotation | ||
Disulfide bondi | 817 ↔ 829 | PROSITE-ProRule annotation | ||
Disulfide bondi | 832 ↔ 844 | PROSITE-ProRule annotation | ||
Disulfide bondi | 834 ↔ 851 | PROSITE-ProRule annotation | ||
Disulfide bondi | 853 ↔ 862 | PROSITE-ProRule annotation | ||
Disulfide bondi | 865 ↔ 875 | PROSITE-ProRule annotation | ||
Disulfide bondi | 878 ↔ 887 | PROSITE-ProRule annotation | ||
Disulfide bondi | 880 ↔ 894 | PROSITE-ProRule annotation | ||
Disulfide bondi | 897 ↔ 906 | PROSITE-ProRule annotation | ||
Disulfide bondi | 909 ↔ 925 | PROSITE-ProRule annotation | ||
Disulfide bondi | 928 ↔ 944 | PROSITE-ProRule annotation | ||
Disulfide bondi | 930 ↔ 955 | PROSITE-ProRule annotation | ||
Disulfide bondi | 957 ↔ 966 | PROSITE-ProRule annotation | ||
Disulfide bondi | 969 ↔ 984 | PROSITE-ProRule annotation | ||
Disulfide bondi | 987 ↔ 1001 | PROSITE-ProRule annotation | ||
Disulfide bondi | 989 ↔ 1008 | PROSITE-ProRule annotation | ||
Disulfide bondi | 1011 ↔ 1020 | PROSITE-ProRule annotation | ||
Disulfide bondi | 1023 ↔ 1036 | PROSITE-ProRule annotation | ||
Disulfide bondi | 1039 ↔ 1059 | PROSITE-ProRule annotation | ||
Disulfide bondi | 1041 ↔ 1066 | PROSITE-ProRule annotation | ||
Disulfide bondi | 1068 ↔ 1077 | PROSITE-ProRule annotation | ||
Disulfide bondi | 1080 ↔ 1093 | PROSITE-ProRule annotation | ||
Glycosylationi | 1086 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Disulfide bondi | 1096 ↔ 1108 | PROSITE-ProRule annotation | ||
Disulfide bondi | 1098 ↔ 1115 | PROSITE-ProRule annotation | ||
Disulfide bondi | 1117 ↔ 1126 | PROSITE-ProRule annotation | ||
Disulfide bondi | 1129 ↔ 1141 | PROSITE-ProRule annotation | ||
Disulfide bondi | 1144 ↔ 1156 | PROSITE-ProRule annotation | ||
Disulfide bondi | 1146 ↔ 1163 | PROSITE-ProRule annotation | ||
Disulfide bondi | 1165 ↔ 1174 | PROSITE-ProRule annotation | ||
Disulfide bondi | 1177 ↔ 1188 | PROSITE-ProRule annotation | ||
Disulfide bondi | 1191 | InterchainCurated | ||
Disulfide bondi | 1194 | InterchainCurated | ||
Glycosylationi | 1250 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Glycosylationi | 1309 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Glycosylationi | 1349 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Glycosylationi | 1500 | N-linked (GlcNAc...) asparagineSequence analysis | 1 | |
Modified residuei | 1533 | PhosphoserineBy similarity | 1 | |
Disulfide bondi | 1798 | InterchainCurated |
Keywords - PTMi
Disulfide bond, Glycoprotein, PhosphoproteinProteomic databases
MaxQBi | Q61292 |
PaxDbi | Q61292 |
PeptideAtlasi | Q61292 |
PRIDEi | Q61292 |
PTM databases
iPTMneti | Q61292 |
PhosphoSitePlusi | Q61292 |
Expressioni
Tissue specificityi
Neuromuscular synapse and kidney glomerulus.
Gene expression databases
Bgeei | ENSMUSG00000052911 |
CleanExi | MM_LAMB2 |
ExpressionAtlasi | Q61292 baseline and differential |
Genevisiblei | Q61292 MM |
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. Beta-2 is a subunit of laminin-3 (laminin-121 or S-laminin), laminin-4 (laminin-221 or S-merosin), laminin-7 (laminin-321 or KS-laminin), laminin-9 (laminin-421), laminin-11 (laminin-521), laminin-14 (laminin-423) and laminin-15 (laminin-523).
GO - Molecular functioni
- integrin binding Source: MGI
Protein-protein interaction databases
IntActi | Q61292 2 interactors. |
MINTi | Q61292 |
STRINGi | 10090.ENSMUSP00000069087 |
Structurei
3D structure databases
ProteinModelPortali | Q61292 |
SMRi | Q61292 |
ModBasei | Search... |
MobiDBi | Search... |
Family & Domainsi
Domains and Repeats
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Domaini | 46 – 285 | Laminin N-terminalPROSITE-ProRule annotationAdd BLAST | 240 | |
Domaini | 286 – 349 | Laminin EGF-like 1PROSITE-ProRule annotationAdd BLAST | 64 | |
Domaini | 350 – 412 | Laminin EGF-like 2PROSITE-ProRule annotationAdd BLAST | 63 | |
Domaini | 413 – 472 | Laminin EGF-like 3PROSITE-ProRule annotationAdd BLAST | 60 | |
Domaini | 473 – 524 | Laminin EGF-like 4PROSITE-ProRule annotationAdd BLAST | 52 | |
Domaini | 525 – 555 | Laminin EGF-like 5; truncatedPROSITE-ProRule annotationAdd BLAST | 31 | |
Domaini | 564 – 778 | Laminin IV type BPROSITE-ProRule annotationAdd BLAST | 215 | |
Domaini | 784 – 831 | Laminin EGF-like 6PROSITE-ProRule annotationAdd BLAST | 48 | |
Domaini | 832 – 877 | Laminin EGF-like 7PROSITE-ProRule annotationAdd BLAST | 46 | |
Domaini | 878 – 927 | Laminin EGF-like 8PROSITE-ProRule annotationAdd BLAST | 50 | |
Domaini | 928 – 986 | Laminin EGF-like 9PROSITE-ProRule annotationAdd BLAST | 59 | |
Domaini | 987 – 1038 | Laminin EGF-like 10PROSITE-ProRule annotationAdd BLAST | 52 | |
Domaini | 1039 – 1095 | Laminin EGF-like 11PROSITE-ProRule annotationAdd BLAST | 57 | |
Domaini | 1096 – 1143 | Laminin EGF-like 12PROSITE-ProRule annotationAdd BLAST | 48 | |
Domaini | 1144 – 1190 | Laminin EGF-like 13PROSITE-ProRule annotationAdd BLAST | 47 |
Region
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Regioni | 1191 – 1410 | Domain IIAdd BLAST | 220 | |
Regioni | 1411 – 1443 | Domain alphaAdd BLAST | 33 | |
Regioni | 1444 – 1799 | Domain IAdd BLAST | 356 |
Coiled coil
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Coiled coili | 1257 – 1304 | Sequence analysisAdd BLAST | 48 | |
Coiled coili | 1473 – 1527 | Sequence analysisAdd BLAST | 55 | |
Coiled coili | 1577 – 1791 | Sequence analysisAdd BLAST | 215 |
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 ENOG410XPEG LUCA |
GeneTreei | ENSGT00780000121851 |
HOGENOMi | HOG000007552 |
HOVERGENi | HBG052301 |
InParanoidi | Q61292 |
KOi | K06243 |
OMAi | GACICKH |
OrthoDBi | EOG091G009B |
TreeFami | TF312903 |
Family and domain databases
Gene3Di | 2.60.120.14901 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
Q61292-1 [UniParc]FASTAAdd to basket
10 20 30 40 50
MEWASGEPGR GRQGQPLPWE LRLGLLLSVL AATLAQAPSL DVPGCSRGSC
60 70 80 90 100
YPATGDLLVG RADRLTASST CGLHSPQPYC IVSHLQDEKK CFLCDSRRPF
110 120 130 140 150
SARDNPNSHR IQNVVTSFAP QRRTAWWQSE NGVPMVTIQL DLEAEFHFTH
160 170 180 190 200
LIMTFKTFRP AAMLVERSAD FGRTWHVYRY FSYDCGADFP GIPLAPPRRW
210 220 230 240 250
DDVVCESRYS EIEPSTEGEV IYRVLDPAIP IPDPYSSRIQ NLLKITNLRV
260 270 280 290 300
NLTRLHTLGD NLLDPRREIR EKYYYALYEL VIRGNCFCYG HASQCAPAPG
310 320 330 340 350
APAHAEGMVH GACICKHNTR GLNCEQCQDF YQDLPWHPAE DGHTHACRKC
360 370 380 390 400
ECNGHTHSCH FDMAVYLASG NVSGGVCDGC QHNTAGRHCE FCRPFFYRDP
410 420 430 440 450
TKDMRDPAVC RPCDCDPMGS QDGGRCDSHD DPVLGLVSGQ CRCKEHVVGT
460 470 480 490 500
RCQQCRDGFF GLSASDPRGC QRCQCNSRGT VPGSSPCDSS SGTCFCKRLV
510 520 530 540 550
TGHGCDRCLP GHWGLSHDLL GCRPCDCDVG GALDPQCDEA TGQCRCRQHM
560 570 580 590 600
IGRRCEQVQP GYFRPFLDHL TWEAEAAQGQ GLEVVERLVT NRETPSWTGP
610 620 630 640 650
GFVRLREGQE VEFLVTSLPR AMDYDLLLRW EPQVPEQWAE LELMVQRPGP
660 670 680 690 700
VSAHSPCGHV LPKDDRIQGM LHPNTRFLVF PRPVCLEPGI SYKLKLKLIG
710 720 730 740 750
TGGRAQPETS YSGLLIDSLV LQPHVLVLEM FSGGDAAALE RRTTFERYRC
760 770 780 790 800
HEEGLMPSKA PLSETCAPLL ISVSALIYNG ALPCQCDPQG SLSSECSPHG
810 820 830 840 850
GQCRCKPGVV GRRCDVCATG YYGFGPAGCQ ACQCSPDGAL SALCEGTSGQ
860 870 880 890 900
CPCRPGAFGL RCDHCQRGQW GFPNCRPCVC NGRADECDTH TGACLGCRDY
910 920 930 940 950
TGGEHCERCI AGFHGDPRLP YGGQCRPCPC PEGPGSQRHF ATSCHRDGYS
960 970 980 990 1000
QQIVCQCREG YTGLRCEACA PGHFGDPSKP GGRCQLCECS GNIDPMDPDA
1010 1020 1030 1040 1050
CDPHTGQCLR CLHNTEGPHC GYCKPGFHGQ AARQSCHRCT CNLLGTDPRR
1060 1070 1080 1090 1100
CPSTDLCHCD PSTGQCPCLP HVQGLNCDHC APNFWNFTSG RGCQPCACHP
1110 1120 1130 1140 1150
SRARGPTCNE FTGQCHCHAG FGGRTCSECQ ELYWGDPGLQ CRACDCDPRG
1160 1170 1180 1190 1200
IDKPQCHRST GHCSCRPGVS GVRCDQCARG FSGVFPACHP CHACFGDWDR
1210 1220 1230 1240 1250
VVQDLAARTR RLEQWAQELQ QTGVLGAFES SFLNMQGKLG MVQAIMSARN
1260 1270 1280 1290 1300
ASAASTAKLV EATEGLRHEI GKTTERLTQL EAELTAVQDE NFNANHALSG
1310 1320 1330 1340 1350
LERDGLALNL TLRQLDQHLE ILKHSNFLGA YDSIRHAHSQ STEAERRANA
1360 1370 1380 1390 1400
STFAVPSPVS NSADTRRRTE VLMGAQKENF NRQHLANQQA LGRLSAHAHT
1410 1420 1430 1440 1450
LSLTGINELV CGAPGDAPCA TSPCGGAGCR DEDGQPRCGG LGCSGAAATA
1460 1470 1480 1490 1500
DLALGRARHT QAELQRALVE GGGILSRVSE TRRQAEEAQQ RAQAALDKAN
1510 1520 1530 1540 1550
ASRGQVEQAN QELRELIQNV KDFLSQEGAD PDSIEMVATR VLDISIPASP
1560 1570 1580 1590 1600
EQIQRLASEI AERVRSLADV DTILAHTMGD VRRAEQLLQD AHRARSRAEG
1610 1620 1630 1640 1650
ERQKAETVQA ALEEAQRAQG AAQGAIWGAV VDTQNTEQTL QRVQERMAGA
1660 1670 1680 1690 1700
EKSLNSAGER ARQLDALLEA LKLKRAGNSL AASTAEETAG SAQSRAREAE
1710 1720 1730 1740 1750
KQLREQVGDQ YQTVRALAER KAEGVLAAQA RAEQLRDEAR DLLQAAQDKL
1760 1770 1780 1790
QRLQELEGTY EENERALEGK AAQLDGLEAR MRSVLQAINL QVQIYNTCQ
Experimental Info
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Sequence conflicti | 545 | R → P in AAC53535 (PubMed:8662701).Curated | 1 | |
Sequence conflicti | 581 | G → V in AAC53535 (PubMed:8662701).Curated | 1 | |
Sequence conflicti | 677 | F → V in AAC53535 (PubMed:8662701).Curated | 1 | |
Sequence conflicti | 956 | Q → H in AAC53535 (PubMed:8662701).Curated | 1 | |
Sequence conflicti | 959 | E → A in AAC53535 (PubMed:8662701).Curated | 1 | |
Sequence conflicti | 973 | H → P in AAC53535 (PubMed:8662701).Curated | 1 | |
Sequence conflicti | 1306 | L → F in AAC53535 (PubMed:8662701).Curated | 1 | |
Sequence conflicti | 1449 | T → P in AAC53535 (PubMed:8662701).Curated | 1 | |
Sequence conflicti | 1460 | T → S in AAC53535 (PubMed:8662701).Curated | 1 | |
Sequence conflicti | 1487 | E → A in AAC53535 (PubMed:8662701).Curated | 1 | |
Sequence conflicti | 1627 | W → R in AAC53535 (PubMed:8662701).Curated | 1 |
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | U43541, U42624 Genomic DNA Translation: AAC53535.1 CH466560 Genomic DNA Translation: EDL21291.1 CH466560 Genomic DNA Translation: EDL21292.1 BC026051 mRNA Translation: AAH26051.1 X75928 mRNA Translation: CAA53532.1 |
CCDSi | CCDS23528.1 |
PIRi | I48749 |
RefSeqi | NP_032509.2, NM_008483.3 XP_006511711.1, XM_006511648.2 |
UniGenei | Mm.27560 Mm.425599 |
Genome annotation databases
Ensembli | ENSMUST00000065014; ENSMUSP00000069087; ENSMUSG00000052911 |
GeneIDi | 16779 |
KEGGi | mmu:16779 |
UCSCi | uc009rpr.2 mouse |
Similar proteinsi
Entry informationi
Entry namei | LAMB2_MOUSE | |
Accessioni | Q61292Primary (citable) accession number: Q61292 Secondary accession number(s): Q62182, Q8R0Y0 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | November 1, 1997 |
Last sequence update: | July 27, 2011 | |
Last modified: | April 25, 2018 | |
This is version 148 of the entry and version 2 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Chordata Protein Annotation Program |