SubmitCancel

Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

P55268

- LAMB2_HUMAN

UniProt

P55268 - LAMB2_HUMAN

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein
Laminin subunit beta-2
Gene
LAMB2, LAMS
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. Schwann cell development Source: Ensembl
  2. astrocyte development Source: Ensembl
  3. axon extension involved in regeneration Source: Ensembl
  4. axon guidance Source: Ensembl
  5. cell adhesion Source: UniProtKB-KW
  6. extracellular matrix organization Source: Reactome
  7. metanephric glomerular basement membrane development Source: Ensembl
  8. metanephric glomerular visceral epithelial cell development Source: Ensembl
  9. neuromuscular junction development Source: Ensembl
  10. retina development in camera-type eye 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: UniProt
  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.
Note: The disease is caused by mutations affecting the gene represented in this entry.2 Publications
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.
Note: The disease is caused by mutations affecting the gene represented in this entry.1 Publication
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. LAMB-2-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 – 3232 Reviewed prediction
Add
BLAST
Chaini33 – 17981766Laminin subunit beta-2
PRO_0000017068Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi248 – 2481N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi283 ↔ 292 By similarity
Disulfide bondi285 ↔ 310 By similarity
Disulfide bondi312 ↔ 321 By similarity
Disulfide bondi324 ↔ 344 By similarity
Disulfide bondi347 ↔ 356 By similarity
Disulfide bondi349 ↔ 374 By similarity
Glycosylationi368 – 3681N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi377 ↔ 386 By similarity
Disulfide bondi389 ↔ 407 By similarity
Disulfide bondi410 ↔ 423 By similarity
Disulfide bondi412 ↔ 438 By similarity
Disulfide bondi440 ↔ 449 By similarity
Disulfide bondi452 ↔ 467 By similarity
Disulfide bondi470 ↔ 484 By similarity
Disulfide bondi472 ↔ 491 By similarity
Disulfide bondi493 ↔ 502 By similarity
Disulfide bondi505 ↔ 519 By similarity
Disulfide bondi522 ↔ 534 By similarity
Disulfide bondi524 ↔ 541 By similarity
Disulfide bondi543 ↔ 552 By similarity
Disulfide bondi783 ↔ 795 By similarity
Disulfide bondi785 ↔ 802 By similarity
Disulfide bondi804 ↔ 813 By similarity
Disulfide bondi816 ↔ 828 By similarity
Disulfide bondi831 ↔ 843 By similarity
Disulfide bondi833 ↔ 850 By similarity
Disulfide bondi852 ↔ 861 By similarity
Disulfide bondi864 ↔ 874 By similarity
Disulfide bondi877 ↔ 886 By similarity
Disulfide bondi879 ↔ 893 By similarity
Disulfide bondi896 ↔ 905 By similarity
Disulfide bondi908 ↔ 924 By similarity
Disulfide bondi927 ↔ 943 By similarity
Disulfide bondi929 ↔ 954 By similarity
Disulfide bondi956 ↔ 965 By similarity
Disulfide bondi968 ↔ 983 By similarity
Disulfide bondi986 ↔ 1000 By similarity
Disulfide bondi988 ↔ 1007 By similarity
Disulfide bondi1010 ↔ 1019 By similarity
Disulfide bondi1022 ↔ 1035 By similarity
Disulfide bondi1038 ↔ 1058 By similarity
Disulfide bondi1040 ↔ 1065 By similarity
Disulfide bondi1067 ↔ 1076 By similarity
Disulfide bondi1079 ↔ 1092 By similarity
Glycosylationi1085 – 10851N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi1095 ↔ 1107 By similarity
Disulfide bondi1097 ↔ 1114 By similarity
Disulfide bondi1116 ↔ 1125 By similarity
Disulfide bondi1128 ↔ 1140 By similarity
Disulfide bondi1143 ↔ 1155 By similarity
Disulfide bondi1145 ↔ 1162 By similarity
Disulfide bondi1164 ↔ 1173 By similarity
Disulfide bondi1176 ↔ 1187 By similarity
Disulfide bondi1190 – 1190Interchain Inferred
Disulfide bondi1193 – 1193Interchain Inferred
Glycosylationi1249 – 12491N-linked (GlcNAc...) Reviewed prediction
Glycosylationi1308 – 13081N-linked (GlcNAc...)1 Publication
Glycosylationi1348 – 13481N-linked (GlcNAc...)1 Publication
Glycosylationi1499 – 14991N-linked (GlcNAc...)1 Publication
Disulfide bondi1797 – 1797Interchain Inferred

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

MaxQBiP55268.
PaxDbiP55268.
PRIDEiP55268.

PTM databases

PhosphoSiteiP55268.

Expressioni

Gene expression databases

ArrayExpressiP55268.
BgeeiP55268.
CleanExiHS_LAMB2.
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. 12 interactions.
DIPiDIP-42106N.
IntActiP55268. 10 interactions.
MINTiMINT-1197111.
STRINGi9606.ENSP00000307156.

Structurei

3D structure databases

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

Family & Domainsi

Domains and Repeats

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

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1190 – 1409220Domain II
Add
BLAST
Regioni1410 – 144233Domain alpha
Add
BLAST
Regioni1443 – 1798356Domain I
Add
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili1253 – 131967 Reviewed prediction
Add
BLAST
Coiled coili1472 – 152655 Reviewed prediction
Add
BLAST
Coiled coili1577 – 1790214 Reviewed prediction
Add
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

Keywords - Domaini

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

Phylogenomic databases

eggNOGiNOG241384.
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

MELTSRERGR GQPLPWELRL GLLLSVLAAT LAQAPAPDVP GCSRGSCYPA     50
TGDLLVGRAD RLTASSTCGL NGPQPYCIVS HLQDEKKCFL CDSRRPFSAR 100
DNPHSHRIQN VVTSFAPQRR AAWWQSENGI PAVTIQLDLE AEFHFTHLIM 150
TFKTFRPAAM LVERSADFGR TWHVYRYFSY DCGADFPGVP LAPPRHWDDV 200
VCESRYSEIE PSTEGEVIYR VLDPAIPIPD PYSSRIQNLL KITNLRVNLT 250
RLHTLGDNLL DPRREIREKY YYALYELVVR GNCFCYGHAS ECAPAPGAPA 300
HAEGMVHGAC ICKHNTRGLN CEQCQDFYRD LPWRPAEDGH SHACRKCECH 350
GHTHSCHFDM AVYLASGNVS GGVCDGCQHN TAGRHCELCR PFFYRDPTKD 400
LRDPAVCRSC DCDPMGSQDG GRCDSHDDPA LGLVSGQCRC KEHVVGTRCQ 450
QCRDGFFGLS ISDRLGCRRC QCNARGTVPG STPCDPNSGS CYCKRLVTGR 500
GCDRCLPGHW GLSHDLLGCR PCDCDVGGAL DPQCDEGTGQ CHCRQHMVGR 550
RCEQVQPGYF RPFLDHLIWE AEDTRGQVLD VVERLVTPGE TPSWTGSGFV 600
RLQEGQTLEF LVASVPKAMD YDLLLRLEPQ VPEQWAELEL IVQRPGPVPA 650
HSLCGHLVPK DDRIQGTLQP HARYLIFPNP VCLEPGISYK LHLKLVRTGG 700
SAQPETPYSG PGLLIDSLVL LPRVLVLEMF SGGDAAALER QATFERYQCH 750
EEGLVPSKTS PSEACAPLLI SLSTLIYNGA LPCQCNPQGS LSSECNPHGG 800
QCLCKPGVVG RRCDLCAPGY YGFGPTGCQA CQCSHEGALS SLCEKTSGQC 850
LCRTGAFGLR CDRCQRGQWG FPSCRPCVCN GHADECNTHT GACLGCRDHT 900
GGEHCERCIA GFHGDPRLPY GGQCRPCPCP EGPGSQRHFA TSCHQDEYSQ 950
QIVCHCRAGY TGLRCEACAP GHFGDPSRPG GRCQLCECSG NIDPMDPDAC 1000
DPHTGQCLRC LHHTEGPHCA HCKPGFHGQA ARQSCHRCTC NLLGTNPQQC 1050
PSPDQCHCDP SSGQCPCLPN VQGPSCDRCA PNFWNLTSGH GCQPCACHPS 1100
RARGPTCNEF TGQCHCRAGF GGRTCSECQE LHWGDPGLQC HACDCDSRGI 1150
DTPQCHRFTG HCSCRPGVSG VRCDQCARGF SGIFPACHPC HACFGDWDRV 1200
VQDLAARTQR LEQRAQELQQ TGVLGAFESS FWHMQEKLGI VQGIVGARNT 1250
SAASTAQLVE ATEELRREIG EATEHLTQLE ADLTDVQDEN FNANHALSGL 1300
ERDRLALNLT LRQLDQHLDL LKHSNFLGAY DSIRHAHSQS AEAERRANTS 1350
ALAVPSPVSN SASARHRTEA LMDAQKEDFN SKHMANQRAL GKLSAHTHTL 1400
SLTDINELVC GAPGDAPCAT SPCGGAGCRD EDGQPRCGGL SCNGAAATAD 1450
LALGRARHTQ AELQRALAEG GSILSRVAET RRQASEAQQR AQAALDKANA 1500
SRGQVEQANQ ELQELIQSVK DFLNQEGADP DSIEMVATRV LELSIPASAE 1550
QIQHLAGAIA ERVRSLADVD AILARTVGDV RRAEQLLQDA RRARSWAEDE 1600
KQKAETVQAA LEEAQRAQGI AQGAIRGAVA DTRDTEQTLY QVQERMAGAE 1650
RALSSAGERA RQLDALLEAL KLKRAGNSLA ASTAEETAGS AQGRAQEAEQ 1700
LLRGPLGDQY QTVKALAERK AQGVLAAQAR AEQLRDEARD LLQAAQDKLQ 1750
RLQELEGTYE ENERALESKA AQLDGLEARM RSVLQAINLQ VQIYNTCQ 1798
Length:1,798
Mass (Da):195,981
Last modified:August 21, 2007 - v2
Checksum:iFFB3531AD13E1486
GO

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 conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti914 – 9141G → R in CAA92279. 1 Publication
Sequence conflicti1179 – 11791G → A in AAB34682. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
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. 12 interactions.
DIPi DIP-42106N.
IntActi P55268. 10 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 GC03M049133.
HGNCi HGNC:6487. LAMB2.
HPAi CAB000053.
HPA001895.
HPA050033.
MIMi 150325. gene.
609049. phenotype.
614199. phenotype.
neXtProti NX_P55268.
Orphaneti 306507. LAMB-2-related infantile-onset nephrotic syndrome.
2670. Pierson syndrome.
98915. Synaptic congenital myasthenic syndromes.
PharmGKBi PA164741827.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG241384.
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

ArrayExpressi P55268.
Bgeei P55268.
CleanExi HS_LAMB2.
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: September 3, 2014
This is version 140 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

Similar proteinsi