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Protein

Laminin subunit beta-2

Gene

Lamb2

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at transcript 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.1 Publication
Laminin-3 (S-laminin) regulates the formation of motor nerve terminals.1 Publication

GO - Molecular functioni

  1. integrin binding Source: MGI

GO - Biological processi

  1. astrocyte development Source: MGI
  2. axon extension involved in regeneration Source: MGI
  3. axon guidance Source: MGI
  4. cell adhesion Source: UniProtKB-KW
  5. cell morphogenesis involved in differentiation Source: MGI
  6. metanephric glomerular basement membrane development Source: MGI
  7. metanephric glomerular visceral epithelial cell development Source: MGI
  8. neuromuscular junction development Source: MGI
  9. neuron projection development Source: MGI
  10. retina development in camera-type eye Source: MGI
  11. Schwann cell development Source: MGI
  12. synapse organization Source: MGI
  13. visual perception Source: MGI
Complete GO annotation...

Keywords - Biological processi

Cell adhesion

Enzyme and pathway databases

ReactomeiREACT_286043. Laminin interactions.
REACT_320075. Non-integrin membrane-ECM interactions.
REACT_354321. ECM proteoglycans.

Names & Taxonomyi

Protein namesi
Recommended name:
Laminin subunit beta-2
Alternative 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
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Chromosome 9

Organism-specific databases

MGIiMGI:99916. Lamb2.

Subcellular locationi

GO - Cellular componenti

  1. basal lamina Source: MGI
  2. basement membrane Source: UniProtKB
  3. extracellular region Source: Reactome
  4. extracellular vesicular exosome Source: MGI
  5. laminin-3 complex Source: MGI
  6. laminin complex Source: MGI
  7. synapse Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Basement membrane, Extracellular matrix, Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 3535Sequence AnalysisAdd
BLAST
Chaini36 – 17991764Laminin subunit beta-2PRO_0000017069Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi251 – 2511N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi286 ↔ 295PROSITE-ProRule annotation
Disulfide bondi288 ↔ 313PROSITE-ProRule annotation
Disulfide bondi315 ↔ 324PROSITE-ProRule annotation
Disulfide bondi327 ↔ 347PROSITE-ProRule annotation
Disulfide bondi350 ↔ 359PROSITE-ProRule annotation
Disulfide bondi352 ↔ 377PROSITE-ProRule annotation
Glycosylationi371 – 3711N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi380 ↔ 389PROSITE-ProRule annotation
Disulfide bondi392 ↔ 410PROSITE-ProRule annotation
Disulfide bondi413 ↔ 426PROSITE-ProRule annotation
Disulfide bondi415 ↔ 441PROSITE-ProRule annotation
Disulfide bondi443 ↔ 452PROSITE-ProRule annotation
Disulfide bondi455 ↔ 470PROSITE-ProRule annotation
Disulfide bondi473 ↔ 487PROSITE-ProRule annotation
Disulfide bondi475 ↔ 494PROSITE-ProRule annotation
Disulfide bondi496 ↔ 505PROSITE-ProRule annotation
Disulfide bondi508 ↔ 522PROSITE-ProRule annotation
Disulfide bondi525 ↔ 537PROSITE-ProRule annotation
Disulfide bondi527 ↔ 544PROSITE-ProRule annotation
Disulfide bondi546 ↔ 555PROSITE-ProRule annotation
Disulfide bondi784 ↔ 796PROSITE-ProRule annotation
Disulfide bondi786 ↔ 803PROSITE-ProRule annotation
Disulfide bondi805 ↔ 814PROSITE-ProRule annotation
Disulfide bondi817 ↔ 829PROSITE-ProRule annotation
Disulfide bondi832 ↔ 844PROSITE-ProRule annotation
Disulfide bondi834 ↔ 851PROSITE-ProRule annotation
Disulfide bondi853 ↔ 862PROSITE-ProRule annotation
Disulfide bondi865 ↔ 875PROSITE-ProRule annotation
Disulfide bondi878 ↔ 887PROSITE-ProRule annotation
Disulfide bondi880 ↔ 894PROSITE-ProRule annotation
Disulfide bondi897 ↔ 906PROSITE-ProRule annotation
Disulfide bondi909 ↔ 925PROSITE-ProRule annotation
Disulfide bondi928 ↔ 944PROSITE-ProRule annotation
Disulfide bondi930 ↔ 955PROSITE-ProRule annotation
Disulfide bondi957 ↔ 966PROSITE-ProRule annotation
Disulfide bondi969 ↔ 984PROSITE-ProRule annotation
Disulfide bondi987 ↔ 1001PROSITE-ProRule annotation
Disulfide bondi989 ↔ 1008PROSITE-ProRule annotation
Disulfide bondi1011 ↔ 1020PROSITE-ProRule annotation
Disulfide bondi1023 ↔ 1036PROSITE-ProRule annotation
Disulfide bondi1039 ↔ 1059PROSITE-ProRule annotation
Disulfide bondi1041 ↔ 1066PROSITE-ProRule annotation
Disulfide bondi1068 ↔ 1077PROSITE-ProRule annotation
Disulfide bondi1080 ↔ 1093PROSITE-ProRule annotation
Glycosylationi1086 – 10861N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi1096 ↔ 1108PROSITE-ProRule annotation
Disulfide bondi1098 ↔ 1115PROSITE-ProRule annotation
Disulfide bondi1117 ↔ 1126PROSITE-ProRule annotation
Disulfide bondi1129 ↔ 1141PROSITE-ProRule annotation
Disulfide bondi1144 ↔ 1156PROSITE-ProRule annotation
Disulfide bondi1146 ↔ 1163PROSITE-ProRule annotation
Disulfide bondi1165 ↔ 1174PROSITE-ProRule annotation
Disulfide bondi1177 ↔ 1188PROSITE-ProRule annotation
Disulfide bondi1191 – 1191InterchainCurated
Disulfide bondi1194 – 1194InterchainCurated
Glycosylationi1250 – 12501N-linked (GlcNAc...)Sequence Analysis
Glycosylationi1309 – 13091N-linked (GlcNAc...)Sequence Analysis
Glycosylationi1349 – 13491N-linked (GlcNAc...)Sequence Analysis
Glycosylationi1500 – 15001N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi1798 – 1798InterchainCurated

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

MaxQBiQ61292.
PaxDbiQ61292.
PRIDEiQ61292.

PTM databases

PhosphoSiteiQ61292.

Expressioni

Tissue specificityi

Neuromuscular synapse and kidney glomerulus.

Gene expression databases

BgeeiQ61292.
CleanExiMM_LAMB2.
ExpressionAtlasiQ61292. baseline and differential.
GenevestigatoriQ61292.

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).

Protein-protein interaction databases

IntActiQ61292. 2 interactions.
MINTiMINT-4100139.
STRINGi10090.ENSMUSP00000069087.

Structurei

3D structure databases

ProteinModelPortaliQ61292.
SMRiQ61292. Positions 44-507.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini46 – 285240Laminin N-terminalPROSITE-ProRule annotationAdd
BLAST
Domaini286 – 34964Laminin EGF-like 1PROSITE-ProRule annotationAdd
BLAST
Domaini350 – 41263Laminin EGF-like 2PROSITE-ProRule annotationAdd
BLAST
Domaini413 – 47260Laminin EGF-like 3PROSITE-ProRule annotationAdd
BLAST
Domaini473 – 52452Laminin EGF-like 4PROSITE-ProRule annotationAdd
BLAST
Domaini525 – 55531Laminin EGF-like 5; truncatedPROSITE-ProRule annotationAdd
BLAST
Domaini564 – 778215Laminin IV type BPROSITE-ProRule annotationAdd
BLAST
Domaini784 – 83148Laminin EGF-like 6PROSITE-ProRule annotationAdd
BLAST
Domaini832 – 87746Laminin EGF-like 7PROSITE-ProRule annotationAdd
BLAST
Domaini878 – 92750Laminin EGF-like 8PROSITE-ProRule annotationAdd
BLAST
Domaini928 – 98659Laminin EGF-like 9PROSITE-ProRule annotationAdd
BLAST
Domaini987 – 103852Laminin EGF-like 10PROSITE-ProRule annotationAdd
BLAST
Domaini1039 – 109557Laminin EGF-like 11PROSITE-ProRule annotationAdd
BLAST
Domaini1096 – 114348Laminin EGF-like 12PROSITE-ProRule annotationAdd
BLAST
Domaini1144 – 119047Laminin EGF-like 13PROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1191 – 1410220Domain IIAdd
BLAST
Regioni1411 – 144333Domain alphaAdd
BLAST
Regioni1444 – 1799356Domain IAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili1257 – 130448Sequence AnalysisAdd
BLAST
Coiled coili1473 – 152755Sequence AnalysisAdd
BLAST
Coiled coili1577 – 1791215Sequence AnalysisAdd
BLAST

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.

Sequence similaritiesi

Contains 13 laminin EGF-like domains.PROSITE-ProRule annotation
Contains 1 laminin IV type B domain.PROSITE-ProRule annotation
Contains 1 laminin N-terminal domain.PROSITE-ProRule annotation

Keywords - Domaini

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

Phylogenomic databases

eggNOGiNOG241384.
GeneTreeiENSGT00780000121851.
HOGENOMiHOG000007552.
HOVERGENiHBG052301.
InParanoidiQ61292.
KOiK06243.
OMAiQPYCIVS.
OrthoDBiEOG75XGK0.
TreeFamiTF312903.

Family and domain databases

InterProiIPR002049. EGF_laminin.
IPR013015. Laminin_IV.
IPR008211. Laminin_N.
[Graphical view]
PfamiPF00053. Laminin_EGF. 13 hits.
PF00055. Laminin_N. 1 hit.
[Graphical view]
SMARTiSM00180. EGF_Lam. 13 hits.
SM00136. LamNT. 1 hit.
[Graphical view]
PROSITEiPS00022. 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.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

Q61292-1 [UniParc]FASTAAdd to basket

« Hide

        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
Length:1,799
Mass (Da):196,579
Last modified:July 26, 2011 - v2
Checksum:i37CA24B9CDA0791F
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti545 – 5451R → P in AAC53535 (PubMed:8662701).Curated
Sequence conflicti581 – 5811G → V in AAC53535 (PubMed:8662701).Curated
Sequence conflicti677 – 6771F → V in AAC53535 (PubMed:8662701).Curated
Sequence conflicti956 – 9561Q → H in AAC53535 (PubMed:8662701).Curated
Sequence conflicti959 – 9591E → A in AAC53535 (PubMed:8662701).Curated
Sequence conflicti973 – 9731H → P in AAC53535 (PubMed:8662701).Curated
Sequence conflicti1306 – 13061L → F in AAC53535 (PubMed:8662701).Curated
Sequence conflicti1449 – 14491T → P in AAC53535 (PubMed:8662701).Curated
Sequence conflicti1460 – 14601T → S in AAC53535 (PubMed:8662701).Curated
Sequence conflicti1487 – 14871E → A in AAC53535 (PubMed:8662701).Curated
Sequence conflicti1627 – 16271W → R in AAC53535 (PubMed:8662701).Curated

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.
CCDSiCCDS23528.1.
PIRiI48749.
RefSeqiNP_032509.2. NM_008483.3.
XP_006511711.1. XM_006511648.2.
UniGeneiMm.425599.

Genome annotation databases

EnsembliENSMUST00000065014; ENSMUSP00000069087; ENSMUSG00000052911.
GeneIDi16779.
KEGGimmu:16779.
UCSCiuc009rpr.2. mouse.

Cross-referencesi

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.
CCDSiCCDS23528.1.
PIRiI48749.
RefSeqiNP_032509.2. NM_008483.3.
XP_006511711.1. XM_006511648.2.
UniGeneiMm.425599.

3D structure databases

ProteinModelPortaliQ61292.
SMRiQ61292. Positions 44-507.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ61292. 2 interactions.
MINTiMINT-4100139.
STRINGi10090.ENSMUSP00000069087.

PTM databases

PhosphoSiteiQ61292.

Proteomic databases

MaxQBiQ61292.
PaxDbiQ61292.
PRIDEiQ61292.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000065014; ENSMUSP00000069087; ENSMUSG00000052911.
GeneIDi16779.
KEGGimmu:16779.
UCSCiuc009rpr.2. mouse.

Organism-specific databases

CTDi3913.
MGIiMGI:99916. Lamb2.

Phylogenomic databases

eggNOGiNOG241384.
GeneTreeiENSGT00780000121851.
HOGENOMiHOG000007552.
HOVERGENiHBG052301.
InParanoidiQ61292.
KOiK06243.
OMAiQPYCIVS.
OrthoDBiEOG75XGK0.
TreeFamiTF312903.

Enzyme and pathway databases

ReactomeiREACT_286043. Laminin interactions.
REACT_320075. Non-integrin membrane-ECM interactions.
REACT_354321. ECM proteoglycans.

Miscellaneous databases

ChiTaRSiLamb2. mouse.
NextBioi290628.
PROiQ61292.
SOURCEiSearch...

Gene expression databases

BgeeiQ61292.
CleanExiMM_LAMB2.
ExpressionAtlasiQ61292. baseline and differential.
GenevestigatoriQ61292.

Family and domain databases

InterProiIPR002049. EGF_laminin.
IPR013015. Laminin_IV.
IPR008211. Laminin_N.
[Graphical view]
PfamiPF00053. Laminin_EGF. 13 hits.
PF00055. Laminin_N. 1 hit.
[Graphical view]
SMARTiSM00180. EGF_Lam. 13 hits.
SM00136. LamNT. 1 hit.
[Graphical view]
PROSITEiPS00022. 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.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Structural organization of the human and mouse laminin beta2 chain genes, and alternative splicing at the 5' end of the human transcript."
    Durkin M.E., Gautam M., Loechel S., Sanes J.R., Merlie J.P., Albrechtsen R., Wewer U.M.
    J. Biol. Chem. 271:13407-13416(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: 129/J.
  2. Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
    Submitted (JUN-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  3. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: FVB/N.
    Tissue: Mammary tumor.
  4. "S-laminin gene (Lams) maps to F1 band of mouse chromosome 9."
    Aberdam D., Galliano M.-F., Mattei M.-G., Ortonne J.-P., Meneguzzi G.
    Mamm. Genome 5:393-394(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 348-428.
    Tissue: Lung.
  5. "Aberrant differentiation of neuromuscular junctions in mice lacking s-laminin/laminin beta 2."
    Noakes P.G., Gautam M., Mudd J., Sanes J.R., Merlie J.P.
    Nature 374:258-262(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
    Strain: 129/J.

Entry informationi

Entry nameiLAMB2_MOUSE
AccessioniPrimary (citable) accession number: Q61292
Secondary accession number(s): Q62182, Q8R0Y0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 31, 1997
Last sequence update: July 26, 2011
Last modified: March 31, 2015
This is version 124 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.