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Protein

Laminin subunit beta-2

Gene

LAMB2

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: 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

  • structural molecule activity Source: ProtInc

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Cell adhesion

Enzyme and pathway databases

BioCyciZFISH:ENSG00000172037-MONOMER.
ReactomeiR-HSA-3000157. Laminin interactions.
R-HSA-3000171. Non-integrin membrane-ECM interactions.
R-HSA-3000178. ECM proteoglycans.
R-HSA-8874081. MET activates PTK2 signaling.
SIGNORiP55268.

Names & Taxonomyi

Protein namesi
Recommended name:
Laminin subunit beta-2
Alternative name(s):
Laminin B1s chain
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
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 3

Organism-specific databases

HGNCiHGNC:6487. LAMB2.

Subcellular locationi

GO - Cellular componenti

  • basal lamina Source: ProtInc
  • basement membrane Source: UniProtKB
  • extracellular exosome Source: UniProtKB
  • extracellular region Source: Reactome
  • laminin-11 complex Source: BHF-UCL
  • laminin-3 complex Source: UniProtKB
  • synapse Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Basement membrane, Extracellular matrix, Secreted

Pathology & Biotechi

Involvement in diseasei

Pierson syndrome (PIERSS)2 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionCharacterized by nephrotic syndrome with neonatal onset, diffuse mesangial sclerosis and eye abnormalities with microcoria as the leading clinical feature. Death usually occurs within the first weeks of life. Disease severity depends on the mutation type: nontruncating LAMB2 mutations may display variable phenotypes ranging from a milder variant of Pierson syndrome to isolated congenital nephrotic syndrome.
See also OMIM:609049
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_031968246R → Q in PIERSS; without ocular abnormalities. 1 PublicationCorresponds to variant rs121912491dbSNPEnsembl.1
Natural variantiVAR_031969246R → W in PIERSS. 1 PublicationCorresponds to variant rs121912488dbSNPEnsembl.1
Natural variantiVAR_031970321C → R in PIERSS; with mild ocular abnormalities. 1 PublicationCorresponds to variant rs121912492dbSNPEnsembl.1
Natural variantiVAR_0319721380N → K in PIERSS; with mild ocular abnormalities; associated with F-1393. 1 PublicationCorresponds to variant rs267607207dbSNPEnsembl.1
Natural variantiVAR_0319731393L → F in PIERSS; with mild ocular abnormalities; associated with K-1380. 1 PublicationCorresponds to variant rs267607208dbSNPEnsembl.1
Nephrotic syndrome 5 with or without ocular abnormalities (NPHS5)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA form of nephrotic syndrome, a renal disease clinically characterized by severe proteinuria, resulting in complications such as hypoalbuminemia, hyperlipidemia and edema. Kidney biopsies show non-specific histologic changes such as focal segmental glomerulosclerosis and diffuse mesangial proliferation. Some affected individuals have an inherited steroid-resistant form and progress to end-stage renal failure. NPHS5 is characterized by very early onset of progressive renal failure. A subset of patients may develop mild ocular anomalies, such as myopia, nystagmus, and strabismus.
See also OMIM:614199
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_066492147H → R in NPHS5. 1 PublicationCorresponds to variant rs387906644dbSNPEnsembl.1

Keywords - Diseasei

Disease mutation

Organism-specific databases

DisGeNETi3913.
MalaCardsiLAMB2.
MIMi609049. phenotype.
614199. phenotype.
OpenTargetsiENSG00000172037.
Orphaneti306507. LAMB2-related infantile-onset nephrotic syndrome.
2670. Pierson syndrome.
98915. Synaptic congenital myasthenic syndromes.
PharmGKBiPA164741827.

Chemistry databases

ChEMBLiCHEMBL2364187.

Polymorphism and mutation databases

BioMutaiLAMB2.
DMDMi156630892.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 32Sequence analysisAdd BLAST32
ChainiPRO_000001706833 – 1798Laminin subunit beta-2Add BLAST1766

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi248N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi283 ↔ 292PROSITE-ProRule annotation
Disulfide bondi285 ↔ 310PROSITE-ProRule annotation
Disulfide bondi312 ↔ 321PROSITE-ProRule annotation
Disulfide bondi324 ↔ 344PROSITE-ProRule annotation
Disulfide bondi347 ↔ 356PROSITE-ProRule annotation
Disulfide bondi349 ↔ 374PROSITE-ProRule annotation
Glycosylationi368N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi377 ↔ 386PROSITE-ProRule annotation
Disulfide bondi389 ↔ 407PROSITE-ProRule annotation
Disulfide bondi410 ↔ 423PROSITE-ProRule annotation
Disulfide bondi412 ↔ 438PROSITE-ProRule annotation
Disulfide bondi440 ↔ 449PROSITE-ProRule annotation
Disulfide bondi452 ↔ 467PROSITE-ProRule annotation
Disulfide bondi470 ↔ 484PROSITE-ProRule annotation
Disulfide bondi472 ↔ 491PROSITE-ProRule annotation
Disulfide bondi493 ↔ 502PROSITE-ProRule annotation
Disulfide bondi505 ↔ 519PROSITE-ProRule annotation
Disulfide bondi522 ↔ 534PROSITE-ProRule annotation
Disulfide bondi524 ↔ 541PROSITE-ProRule annotation
Disulfide bondi543 ↔ 552PROSITE-ProRule annotation
Disulfide bondi783 ↔ 795PROSITE-ProRule annotation
Disulfide bondi785 ↔ 802PROSITE-ProRule annotation
Disulfide bondi804 ↔ 813PROSITE-ProRule annotation
Disulfide bondi816 ↔ 828PROSITE-ProRule annotation
Disulfide bondi831 ↔ 843PROSITE-ProRule annotation
Disulfide bondi833 ↔ 850PROSITE-ProRule annotation
Disulfide bondi852 ↔ 861PROSITE-ProRule annotation
Disulfide bondi864 ↔ 874PROSITE-ProRule annotation
Disulfide bondi877 ↔ 886PROSITE-ProRule annotation
Disulfide bondi879 ↔ 893PROSITE-ProRule annotation
Disulfide bondi896 ↔ 905PROSITE-ProRule annotation
Disulfide bondi908 ↔ 924PROSITE-ProRule annotation
Disulfide bondi927 ↔ 943PROSITE-ProRule annotation
Disulfide bondi929 ↔ 954PROSITE-ProRule annotation
Disulfide bondi956 ↔ 965PROSITE-ProRule annotation
Disulfide bondi968 ↔ 983PROSITE-ProRule annotation
Disulfide bondi986 ↔ 1000PROSITE-ProRule annotation
Disulfide bondi988 ↔ 1007PROSITE-ProRule annotation
Disulfide bondi1010 ↔ 1019PROSITE-ProRule annotation
Disulfide bondi1022 ↔ 1035PROSITE-ProRule annotation
Disulfide bondi1038 ↔ 1058PROSITE-ProRule annotation
Disulfide bondi1040 ↔ 1065PROSITE-ProRule annotation
Disulfide bondi1067 ↔ 1076PROSITE-ProRule annotation
Disulfide bondi1079 ↔ 1092PROSITE-ProRule annotation
Glycosylationi1085N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi1095 ↔ 1107PROSITE-ProRule annotation
Disulfide bondi1097 ↔ 1114PROSITE-ProRule annotation
Disulfide bondi1116 ↔ 1125PROSITE-ProRule annotation
Disulfide bondi1128 ↔ 1140PROSITE-ProRule annotation
Disulfide bondi1143 ↔ 1155PROSITE-ProRule annotation
Disulfide bondi1145 ↔ 1162PROSITE-ProRule annotation
Disulfide bondi1164 ↔ 1173PROSITE-ProRule annotation
Disulfide bondi1176 ↔ 1187PROSITE-ProRule annotation
Disulfide bondi1190InterchainCurated
Disulfide bondi1193InterchainCurated
Glycosylationi1249N-linked (GlcNAc...)Sequence analysis1
Glycosylationi1308N-linked (GlcNAc...)1 Publication1
Glycosylationi1348N-linked (GlcNAc...)1 Publication1
Glycosylationi1499N-linked (GlcNAc...)1 Publication1
Modified residuei1532Phosphoserine; by FAM20C1 Publication1
Disulfide bondi1797InterchainCurated

Keywords - PTMi

Disulfide bond, Glycoprotein, Phosphoprotein

Proteomic databases

EPDiP55268.
MaxQBiP55268.
PaxDbiP55268.
PeptideAtlasiP55268.
PRIDEiP55268.

PTM databases

iPTMnetiP55268.
PhosphoSitePlusiP55268.
SwissPalmiP55268.

Expressioni

Gene expression databases

BgeeiENSG00000172037.
CleanExiHS_LAMB2.
ExpressionAtlasiP55268. baseline and differential.
GenevisibleiP55268. HS.

Organism-specific databases

HPAiCAB000053.
HPA001895.
HPA050033.

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

BioGridi110107. 31 interactors.
DIPiDIP-42106N.
IntActiP55268. 13 interactors.
MINTiMINT-1197111.
STRINGi9606.ENSP00000307156.

Structurei

3D structure databases

ProteinModelPortaliP55268.
SMRiP55268.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini43 – 282Laminin N-terminalPROSITE-ProRule annotationAdd BLAST240
Domaini283 – 346Laminin EGF-like 1PROSITE-ProRule annotationAdd BLAST64
Domaini347 – 409Laminin EGF-like 2PROSITE-ProRule annotationAdd BLAST63
Domaini410 – 469Laminin EGF-like 3PROSITE-ProRule annotationAdd BLAST60
Domaini470 – 521Laminin EGF-like 4PROSITE-ProRule annotationAdd BLAST52
Domaini522 – 552Laminin EGF-like 5; truncatedPROSITE-ProRule annotationAdd BLAST31
Domaini561 – 777Laminin IV type BPROSITE-ProRule annotationAdd BLAST217
Domaini783 – 830Laminin EGF-like 6PROSITE-ProRule annotationAdd BLAST48
Domaini831 – 876Laminin EGF-like 7PROSITE-ProRule annotationAdd BLAST46
Domaini877 – 926Laminin EGF-like 8PROSITE-ProRule annotationAdd BLAST50
Domaini927 – 985Laminin EGF-like 9PROSITE-ProRule annotationAdd BLAST59
Domaini986 – 1037Laminin EGF-like 10PROSITE-ProRule annotationAdd BLAST52
Domaini1038 – 1094Laminin EGF-like 11PROSITE-ProRule annotationAdd BLAST57
Domaini1095 – 1142Laminin EGF-like 12PROSITE-ProRule annotationAdd BLAST48
Domaini1143 – 1189Laminin EGF-like 13PROSITE-ProRule annotationAdd BLAST47

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni1190 – 1409Domain IIAdd BLAST220
Regioni1410 – 1442Domain alphaAdd BLAST33
Regioni1443 – 1798Domain IAdd BLAST356

Coiled coil

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Coiled coili1253 – 1319Sequence analysisAdd BLAST67
Coiled coili1472 – 1526Sequence analysisAdd BLAST55
Coiled coili1577 – 1790Sequence analysisAdd BLAST214

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

eggNOGiKOG0994. Eukaryota.
ENOG410XPEG. LUCA.
GeneTreeiENSGT00780000121851.
HOGENOMiHOG000007552.
HOVERGENiHBG052301.
InParanoidiP55268.
KOiK06243.
OMAiGACICKH.
OrthoDBiEOG091G009B.
PhylomeDBiP55268.
TreeFamiTF312903.

Family and domain databases

InterProiIPR013032. EGF-like_CS.
IPR000742. EGF-like_dom.
IPR002049. Laminin_EGF.
IPR013015. Laminin_IV_B.
IPR008211. Laminin_N.
[Graphical view]
PfamiPF00053. Laminin_EGF. 13 hits.
PF00055. Laminin_N. 1 hit.
[Graphical view]
SMARTiSM00181. EGF. 9 hits.
SM00180. 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.

P55268-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MELTSRERGR GQPLPWELRL GLLLSVLAAT LAQAPAPDVP GCSRGSCYPA
60 70 80 90 100
TGDLLVGRAD RLTASSTCGL NGPQPYCIVS HLQDEKKCFL CDSRRPFSAR
110 120 130 140 150
DNPHSHRIQN VVTSFAPQRR AAWWQSENGI PAVTIQLDLE AEFHFTHLIM
160 170 180 190 200
TFKTFRPAAM LVERSADFGR TWHVYRYFSY DCGADFPGVP LAPPRHWDDV
210 220 230 240 250
VCESRYSEIE PSTEGEVIYR VLDPAIPIPD PYSSRIQNLL KITNLRVNLT
260 270 280 290 300
RLHTLGDNLL DPRREIREKY YYALYELVVR GNCFCYGHAS ECAPAPGAPA
310 320 330 340 350
HAEGMVHGAC ICKHNTRGLN CEQCQDFYRD LPWRPAEDGH SHACRKCECH
360 370 380 390 400
GHTHSCHFDM AVYLASGNVS GGVCDGCQHN TAGRHCELCR PFFYRDPTKD
410 420 430 440 450
LRDPAVCRSC DCDPMGSQDG GRCDSHDDPA LGLVSGQCRC KEHVVGTRCQ
460 470 480 490 500
QCRDGFFGLS ISDRLGCRRC QCNARGTVPG STPCDPNSGS CYCKRLVTGR
510 520 530 540 550
GCDRCLPGHW GLSHDLLGCR PCDCDVGGAL DPQCDEGTGQ CHCRQHMVGR
560 570 580 590 600
RCEQVQPGYF RPFLDHLIWE AEDTRGQVLD VVERLVTPGE TPSWTGSGFV
610 620 630 640 650
RLQEGQTLEF LVASVPKAMD YDLLLRLEPQ VPEQWAELEL IVQRPGPVPA
660 670 680 690 700
HSLCGHLVPK DDRIQGTLQP HARYLIFPNP VCLEPGISYK LHLKLVRTGG
710 720 730 740 750
SAQPETPYSG PGLLIDSLVL LPRVLVLEMF SGGDAAALER QATFERYQCH
760 770 780 790 800
EEGLVPSKTS PSEACAPLLI SLSTLIYNGA LPCQCNPQGS LSSECNPHGG
810 820 830 840 850
QCLCKPGVVG RRCDLCAPGY YGFGPTGCQA CQCSHEGALS SLCEKTSGQC
860 870 880 890 900
LCRTGAFGLR CDRCQRGQWG FPSCRPCVCN GHADECNTHT GACLGCRDHT
910 920 930 940 950
GGEHCERCIA GFHGDPRLPY GGQCRPCPCP EGPGSQRHFA TSCHQDEYSQ
960 970 980 990 1000
QIVCHCRAGY TGLRCEACAP GHFGDPSRPG GRCQLCECSG NIDPMDPDAC
1010 1020 1030 1040 1050
DPHTGQCLRC LHHTEGPHCA HCKPGFHGQA ARQSCHRCTC NLLGTNPQQC
1060 1070 1080 1090 1100
PSPDQCHCDP SSGQCPCLPN VQGPSCDRCA PNFWNLTSGH GCQPCACHPS
1110 1120 1130 1140 1150
RARGPTCNEF TGQCHCRAGF GGRTCSECQE LHWGDPGLQC HACDCDSRGI
1160 1170 1180 1190 1200
DTPQCHRFTG HCSCRPGVSG VRCDQCARGF SGIFPACHPC HACFGDWDRV
1210 1220 1230 1240 1250
VQDLAARTQR LEQRAQELQQ TGVLGAFESS FWHMQEKLGI VQGIVGARNT
1260 1270 1280 1290 1300
SAASTAQLVE ATEELRREIG EATEHLTQLE ADLTDVQDEN FNANHALSGL
1310 1320 1330 1340 1350
ERDRLALNLT LRQLDQHLDL LKHSNFLGAY DSIRHAHSQS AEAERRANTS
1360 1370 1380 1390 1400
ALAVPSPVSN SASARHRTEA LMDAQKEDFN SKHMANQRAL GKLSAHTHTL
1410 1420 1430 1440 1450
SLTDINELVC GAPGDAPCAT SPCGGAGCRD EDGQPRCGGL SCNGAAATAD
1460 1470 1480 1490 1500
LALGRARHTQ AELQRALAEG GSILSRVAET RRQASEAQQR AQAALDKANA
1510 1520 1530 1540 1550
SRGQVEQANQ ELQELIQSVK DFLNQEGADP DSIEMVATRV LELSIPASAE
1560 1570 1580 1590 1600
QIQHLAGAIA ERVRSLADVD AILARTVGDV RRAEQLLQDA RRARSWAEDE
1610 1620 1630 1640 1650
KQKAETVQAA LEEAQRAQGI AQGAIRGAVA DTRDTEQTLY QVQERMAGAE
1660 1670 1680 1690 1700
RALSSAGERA RQLDALLEAL KLKRAGNSLA ASTAEETAGS AQGRAQEAEQ
1710 1720 1730 1740 1750
LLRGPLGDQY QTVKALAERK AQGVLAAQAR AEQLRDEARD LLQAAQDKLQ
1760 1770 1780 1790
RLQELEGTYE ENERALESKA AQLDGLEARM RSVLQAINLQ VQIYNTCQ
Length:1,798
Mass (Da):195,981
Last modified:August 21, 2007 - v2
Checksum:iFFB3531AD13E1486
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti914G → R in CAA92279 (PubMed:7698745).Curated1
Sequence conflicti1179G → A in AAB34682 (PubMed:7795887).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_066492147H → R in NPHS5. 1 PublicationCorresponds to variant rs387906644dbSNPEnsembl.1
Natural variantiVAR_031968246R → Q in PIERSS; without ocular abnormalities. 1 PublicationCorresponds to variant rs121912491dbSNPEnsembl.1
Natural variantiVAR_031969246R → W in PIERSS. 1 PublicationCorresponds to variant rs121912488dbSNPEnsembl.1
Natural variantiVAR_031970321C → R in PIERSS; with mild ocular abnormalities. 1 PublicationCorresponds to variant rs121912492dbSNPEnsembl.1
Natural variantiVAR_031971987E → K.Corresponds to variant rs34759087dbSNPEnsembl.1
Natural variantiVAR_0319721380N → K in PIERSS; with mild ocular abnormalities; associated with F-1393. 1 PublicationCorresponds to variant rs267607207dbSNPEnsembl.1
Natural variantiVAR_0319731393L → F in PIERSS; with mild ocular abnormalities; associated with K-1380. 1 PublicationCorresponds to variant rs267607208dbSNPEnsembl.1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z68155, Z68156 Genomic DNA. Translation: CAA92279.1.
X79683 mRNA. Translation: CAA56130.1.
S77512 mRNA. Translation: AAB34682.2.
CCDSiCCDS2789.1.
PIRiA55677.
S53869.
RefSeqiNP_002283.3. NM_002292.3.
XP_005265184.1. XM_005265127.3.
UniGeneiHs.439726.

Genome annotation databases

EnsembliENST00000305544; ENSP00000307156; ENSG00000172037.
ENST00000418109; ENSP00000388325; ENSG00000172037.
GeneIDi3913.
KEGGihsa:3913.
UCSCiuc003cwe.4. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z68155, Z68156 Genomic DNA. Translation: CAA92279.1.
X79683 mRNA. Translation: CAA56130.1.
S77512 mRNA. Translation: AAB34682.2.
CCDSiCCDS2789.1.
PIRiA55677.
S53869.
RefSeqiNP_002283.3. NM_002292.3.
XP_005265184.1. XM_005265127.3.
UniGeneiHs.439726.

3D structure databases

ProteinModelPortaliP55268.
SMRiP55268.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi110107. 31 interactors.
DIPiDIP-42106N.
IntActiP55268. 13 interactors.
MINTiMINT-1197111.
STRINGi9606.ENSP00000307156.

Chemistry databases

ChEMBLiCHEMBL2364187.

PTM databases

iPTMnetiP55268.
PhosphoSitePlusiP55268.
SwissPalmiP55268.

Polymorphism and mutation databases

BioMutaiLAMB2.
DMDMi156630892.

Proteomic databases

EPDiP55268.
MaxQBiP55268.
PaxDbiP55268.
PeptideAtlasiP55268.
PRIDEiP55268.

Protocols and materials databases

DNASUi3913.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000305544; ENSP00000307156; ENSG00000172037.
ENST00000418109; ENSP00000388325; ENSG00000172037.
GeneIDi3913.
KEGGihsa:3913.
UCSCiuc003cwe.4. human.

Organism-specific databases

CTDi3913.
DisGeNETi3913.
GeneCardsiLAMB2.
HGNCiHGNC:6487. LAMB2.
HPAiCAB000053.
HPA001895.
HPA050033.
MalaCardsiLAMB2.
MIMi150325. gene.
609049. phenotype.
614199. phenotype.
neXtProtiNX_P55268.
OpenTargetsiENSG00000172037.
Orphaneti306507. LAMB2-related infantile-onset nephrotic syndrome.
2670. Pierson syndrome.
98915. Synaptic congenital myasthenic syndromes.
PharmGKBiPA164741827.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG0994. Eukaryota.
ENOG410XPEG. LUCA.
GeneTreeiENSGT00780000121851.
HOGENOMiHOG000007552.
HOVERGENiHBG052301.
InParanoidiP55268.
KOiK06243.
OMAiGACICKH.
OrthoDBiEOG091G009B.
PhylomeDBiP55268.
TreeFamiTF312903.

Enzyme and pathway databases

BioCyciZFISH:ENSG00000172037-MONOMER.
ReactomeiR-HSA-3000157. Laminin interactions.
R-HSA-3000171. Non-integrin membrane-ECM interactions.
R-HSA-3000178. ECM proteoglycans.
R-HSA-8874081. MET activates PTK2 signaling.
SIGNORiP55268.

Miscellaneous databases

ChiTaRSiLAMB2. human.
GeneWikiiLaminin,_beta_2.
GenomeRNAii3913.
PROiP55268.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000172037.
CleanExiHS_LAMB2.
ExpressionAtlasiP55268. baseline and differential.
GenevisibleiP55268. HS.

Family and domain databases

InterProiIPR013032. EGF-like_CS.
IPR000742. EGF-like_dom.
IPR002049. Laminin_EGF.
IPR013015. Laminin_IV_B.
IPR008211. Laminin_N.
[Graphical view]
PfamiPF00053. Laminin_EGF. 13 hits.
PF00055. Laminin_N. 1 hit.
[Graphical view]
SMARTiSM00181. EGF. 9 hits.
SM00180. 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...

Entry informationi

Entry nameiLAMB2_HUMAN
AccessioniPrimary (citable) accession number: P55268
Secondary accession number(s): Q16321
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: August 21, 2007
Last modified: November 30, 2016
This is version 163 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 3
    Human chromosome 3: 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

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 one 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.