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P55268

- LAMB2_HUMAN

UniProt

P55268 - LAMB2_HUMAN

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Protein

Laminin subunit beta-2

Gene

LAMB2

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. structural molecule activity Source: ProtInc

GO - Biological processi

  1. astrocyte development Source: Ensembl
  2. axon extension involved in regeneration Source: Ensembl
  3. axon guidance Source: Ensembl
  4. cell adhesion Source: UniProtKB-KW
  5. extracellular matrix organization Source: Reactome
  6. metanephric glomerular basement membrane development Source: Ensembl
  7. metanephric glomerular visceral epithelial cell development Source: Ensembl
  8. neuromuscular junction development Source: Ensembl
  9. retina development in camera-type eye Source: Ensembl
  10. Schwann cell development Source: Ensembl
  11. visual perception 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.

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
ProteomesiUP000005640: Chromosome 3

Organism-specific databases

HGNCiHGNC:6487. LAMB2.

Subcellular locationi

Secretedextracellular spaceextracellular matrixbasement membrane
Note: S-laminin is concentrated in the synaptic cleft of the neuromuscular junction.

GO - Cellular componenti

  1. basal lamina Source: ProtInc
  2. basement membrane Source: UniProtKB
  3. extracellular region Source: Reactome
  4. extracellular vesicular exosome Source: UniProtKB
  5. laminin-11 complex Source: BHF-UCL
  6. laminin-3 complex Source: UniProtKB
  7. synapse Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Basement membrane, Extracellular matrix, Secreted

Pathology & Biotechi

Involvement in diseasei

Pierson syndrome (PIERSS) [MIM:609049]: Characterized 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.2 Publications
Note: The disease is caused by mutations affecting the gene represented in this entry.
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti246 – 2461R → Q in PIERSS; without ocular abnormalities. 1 Publication
VAR_031968
Natural varianti246 – 2461R → W in PIERSS. 1 Publication
VAR_031969
Natural varianti321 – 3211C → R in PIERSS; with mild ocular abnormalities. 1 Publication
VAR_031970
Natural varianti1380 – 13801N → K in PIERSS; with mild ocular abnormalities; associated with F-1393. 1 Publication
VAR_031972
Natural varianti1393 – 13931L → F in PIERSS; with mild ocular abnormalities; associated with K-1380. 1 Publication
VAR_031973
Nephrotic syndrome 5 with or without ocular abnormalities (NPHS5) [MIM:614199]: A 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.1 Publication
Note: The disease is caused by mutations affecting the gene represented in this entry.
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti147 – 1471H → R in NPHS5. 1 Publication
VAR_066492

Keywords - Diseasei

Disease mutation

Organism-specific databases

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

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 3232Sequence AnalysisAdd
BLAST
Chaini33 – 17981766Laminin subunit beta-2PRO_0000017068Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi248 – 2481N-linked (GlcNAc...)Sequence Analysis
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
Glycosylationi368 – 3681N-linked (GlcNAc...)Sequence Analysis
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
Glycosylationi1085 – 10851N-linked (GlcNAc...)Sequence Analysis
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 bondi1190 – 1190InterchainCurated
Disulfide bondi1193 – 1193InterchainCurated
Glycosylationi1249 – 12491N-linked (GlcNAc...)Sequence Analysis
Glycosylationi1308 – 13081N-linked (GlcNAc...)1 Publication
Glycosylationi1348 – 13481N-linked (GlcNAc...)1 Publication
Glycosylationi1499 – 14991N-linked (GlcNAc...)1 Publication
Disulfide bondi1797 – 1797InterchainCurated

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

MaxQBiP55268.
PaxDbiP55268.
PRIDEiP55268.

PTM databases

PhosphoSiteiP55268.

Expressioni

Gene expression databases

BgeeiP55268.
CleanExiHS_LAMB2.
ExpressionAtlasiP55268. baseline and differential.
GenevestigatoriP55268.

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. 17 interactions.
DIPiDIP-42106N.
IntActiP55268. 11 interactions.
MINTiMINT-1197111.
STRINGi9606.ENSP00000307156.

Structurei

3D structure databases

ProteinModelPortaliP55268.
SMRiP55268. Positions 41-560, 792-1180.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini43 – 282240Laminin N-terminalPROSITE-ProRule annotationAdd
BLAST
Domaini283 – 34664Laminin EGF-like 1PROSITE-ProRule annotationAdd
BLAST
Domaini347 – 40963Laminin EGF-like 2PROSITE-ProRule annotationAdd
BLAST
Domaini410 – 46960Laminin EGF-like 3PROSITE-ProRule annotationAdd
BLAST
Domaini470 – 52152Laminin EGF-like 4PROSITE-ProRule annotationAdd
BLAST
Domaini522 – 55231Laminin EGF-like 5; truncatedPROSITE-ProRule annotationAdd
BLAST
Domaini561 – 777217Laminin IV type BPROSITE-ProRule annotationAdd
BLAST
Domaini783 – 83048Laminin EGF-like 6PROSITE-ProRule annotationAdd
BLAST
Domaini831 – 87646Laminin EGF-like 7PROSITE-ProRule annotationAdd
BLAST
Domaini877 – 92650Laminin EGF-like 8PROSITE-ProRule annotationAdd
BLAST
Domaini927 – 98559Laminin EGF-like 9PROSITE-ProRule annotationAdd
BLAST
Domaini986 – 103752Laminin EGF-like 10PROSITE-ProRule annotationAdd
BLAST
Domaini1038 – 109457Laminin EGF-like 11PROSITE-ProRule annotationAdd
BLAST
Domaini1095 – 114248Laminin EGF-like 12PROSITE-ProRule annotationAdd
BLAST
Domaini1143 – 118947Laminin EGF-like 13PROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1190 – 1409220Domain IIAdd
BLAST
Regioni1410 – 144233Domain alphaAdd
BLAST
Regioni1443 – 1798356Domain IAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili1253 – 131967Sequence AnalysisAdd
BLAST
Coiled coili1472 – 152655Sequence AnalysisAdd
BLAST
Coiled coili1577 – 1790214Sequence 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.
GeneTreeiENSGT00760000118860.
HOGENOMiHOG000007552.
HOVERGENiHBG052301.
InParanoidiP55268.
KOiK06243.
OMAiQPYCIVS.
OrthoDBiEOG75XGK0.
PhylomeDBiP55268.
TreeFamiTF312903.

Family and domain databases

InterProiIPR013032. EGF-like_CS.
IPR002049. 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.

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)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti914 – 9141G → R in CAA92279. (PubMed:7698745)Curated
Sequence conflicti1179 – 11791G → A in AAB34682. (PubMed:7795887)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti147 – 1471H → R in NPHS5. 1 Publication
VAR_066492
Natural varianti246 – 2461R → Q in PIERSS; without ocular abnormalities. 1 Publication
VAR_031968
Natural varianti246 – 2461R → W in PIERSS. 1 Publication
VAR_031969
Natural varianti321 – 3211C → R in PIERSS; with mild ocular abnormalities. 1 Publication
VAR_031970
Natural varianti987 – 9871E → K.
Corresponds to variant rs34759087 [ dbSNP | Ensembl ].
VAR_031971
Natural varianti1380 – 13801N → K in PIERSS; with mild ocular abnormalities; associated with F-1393. 1 Publication
VAR_031972
Natural varianti1393 – 13931L → F in PIERSS; with mild ocular abnormalities; associated with K-1380. 1 Publication
VAR_031973

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_005265127.2.
UniGeneiHs.439726.

Genome annotation databases

EnsembliENST00000305544; ENSP00000307156; ENSG00000172037.
ENST00000418109; ENSP00000388325; ENSG00000172037.
GeneIDi3913.
KEGGihsa:3913.
UCSCiuc003cwe.3. human.

Polymorphism databases

DMDMi156630892.

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 .
CCDSi CCDS2789.1.
PIRi A55677.
S53869.
RefSeqi NP_002283.3. NM_002292.3.
XP_005265184.1. XM_005265127.2.
UniGenei Hs.439726.

3D structure databases

ProteinModelPortali P55268.
SMRi P55268. Positions 41-560, 792-1180.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 110107. 17 interactions.
DIPi DIP-42106N.
IntActi P55268. 11 interactions.
MINTi MINT-1197111.
STRINGi 9606.ENSP00000307156.

Chemistry

ChEMBLi CHEMBL2364187.

PTM databases

PhosphoSitei P55268.

Polymorphism databases

DMDMi 156630892.

Proteomic databases

MaxQBi P55268.
PaxDbi P55268.
PRIDEi P55268.

Protocols and materials databases

DNASUi 3913.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000305544 ; ENSP00000307156 ; ENSG00000172037 .
ENST00000418109 ; ENSP00000388325 ; ENSG00000172037 .
GeneIDi 3913.
KEGGi hsa:3913.
UCSCi uc003cwe.3. human.

Organism-specific databases

CTDi 3913.
GeneCardsi GC03M049163.
HGNCi HGNC:6487. LAMB2.
HPAi CAB000053.
HPA001895.
HPA050033.
MIMi 150325. gene.
609049. phenotype.
614199. phenotype.
neXtProti NX_P55268.
Orphaneti 306507. LAMB2-related infantile-onset nephrotic syndrome.
2670. Pierson syndrome.
98915. Synaptic congenital myasthenic syndromes.
PharmGKBi PA164741827.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG241384.
GeneTreei ENSGT00760000118860.
HOGENOMi HOG000007552.
HOVERGENi HBG052301.
InParanoidi P55268.
KOi K06243.
OMAi QPYCIVS.
OrthoDBi EOG75XGK0.
PhylomeDBi P55268.
TreeFami TF312903.

Enzyme and pathway databases

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

Miscellaneous databases

ChiTaRSi LAMB2. human.
GeneWikii Laminin,_beta_2.
GenomeRNAii 3913.
NextBioi 15371.
PROi P55268.
SOURCEi Search...

Gene expression databases

Bgeei P55268.
CleanExi HS_LAMB2.
ExpressionAtlasi P55268. baseline and differential.
Genevestigatori P55268.

Family and domain databases

InterProi IPR013032. EGF-like_CS.
IPR002049. EGF_laminin.
IPR013015. Laminin_IV.
IPR008211. Laminin_N.
[Graphical view ]
Pfami PF00053. Laminin_EGF. 13 hits.
PF00055. Laminin_N. 1 hit.
[Graphical view ]
SMARTi SM00180. EGF_Lam. 13 hits.
SM00136. LamNT. 1 hit.
[Graphical view ]
PROSITEi 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.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Human beta 2 chain of laminin (formerly S chain): cDNA cloning, chromosomal localization, and expression in carcinomas."
    Wewer U.M., Gerecke D.R., Durkin M.E., Kurtz K.S., Mattei M.-G., Champliaud M.-F., Burgeson R.E., Albrechtsen R.
    Genomics 24:243-252(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
  2. "The human laminin beta 2 chain (S-laminin): structure, expression in fetal tissues and chromosomal assignment of the LAMB2 gene."
    Iivanainen A., Vuolteenaho R., Sainio K., Eddy R., Shows T.B., Sariola H., Tryggvason K.
    Matrix Biol. 14:489-497(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  3. "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-1308; ASN-1348 AND ASN-1499.
    Tissue: Liver.
  4. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  5. Cited for: VARIANT PIERSS TRP-246.
  6. Cited for: VARIANTS PIERSS GLN-246; ARG-321; LYS-1380 AND PHE-1393.
  7. Cited for: VARIANT NPHS5 ARG-147.

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 26, 2014
This is version 143 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

External Data

Dasty 3