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Q13751

- LAMB3_HUMAN

UniProt

Q13751 - LAMB3_HUMAN

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Protein

Laminin subunit beta-3

Gene

LAMB3

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. brown fat cell differentiation Source: Ensembl
  2. cell adhesion Source: UniProtKB-KW
  3. cell junction assembly Source: Reactome
  4. endodermal cell differentiation Source: UniProtKB
  5. epidermis development Source: ProtInc
  6. extracellular matrix disassembly Source: Reactome
  7. extracellular matrix organization Source: Reactome
  8. hemidesmosome assembly Source: Reactome
Complete GO annotation...

Keywords - Biological processi

Cell adhesion

Enzyme and pathway databases

ReactomeiREACT_118572. Degradation of the extracellular matrix.
REACT_150180. Assembly of collagen fibrils and other multimeric structures.
REACT_150268. Anchoring fibril formation.
REACT_163874. Non-integrin membrane-ECM interactions.
REACT_169262. Laminin interactions.
REACT_20537. Type I hemidesmosome assembly.

Names & Taxonomyi

Protein namesi
Recommended name:
Laminin subunit beta-3
Alternative name(s):
Epiligrin subunit bata
Kalinin B1 chain
Kalinin subunit beta
Laminin B1k chain
Laminin-5 subunit beta
Nicein subunit beta
Gene namesi
Name:LAMB3
Synonyms:LAMNB1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 1

Organism-specific databases

HGNCiHGNC:6490. LAMB3.

Subcellular locationi

GO - Cellular componenti

  1. extracellular region Source: Reactome
  2. laminin-5 complex Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Basement membrane, Extracellular matrix, Secreted

Pathology & Biotechi

Involvement in diseasei

Epidermolysis bullosa, junctional, Herlitz type (H-JEB) [MIM:226700]: An infantile and lethal form of junctional epidermolysis bullosa, a group of blistering skin diseases characterized by tissue separation which occurs within the dermo-epidermal basement In the Herlitz type, death occurs usually within the first six months of life. Occasionally, children survive to teens. It is marked by bullous lesions at birth and extensive denudation of skin and mucous membranes that may be hemorrhagic.1 Publication
Note: The disease is caused by mutations affecting the gene represented in this entry.
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti679 – 6791P → L in H-JEB. 1 Publication
VAR_004171
Generalized atrophic benign epidermolysis bullosa (GABEB) [MIM:226650]: A non-lethal, adult form of junctional epidermolysis bullosa characterized by life-long blistering of the skin, associated with hair and tooth abnormalities.2 Publications
Note: The disease is caused by mutations affecting the gene represented in this entry.
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti199 – 1991G → A in GABEB; somatic second-site mutation. 1 Publication
VAR_037310
Natural varianti207 – 2071K → Q in GABEB; somatic second-site mutation. 1 Publication
VAR_037311
Natural varianti210 – 2101E → K in GABEB. 2 Publications
VAR_004170

Keywords - Diseasei

Disease mutation, Epidermolysis bullosa

Organism-specific databases

MIMi226650. phenotype.
226700. phenotype.
Orphaneti79402. Generalized junctional epidermolysis bullosa, non-Herlitz type.
100031. Hypoplastic amelogenesis imperfecta.
79404. Junctional epidermolysis bullosa, Herlitz type.
PharmGKBiPA30278.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1717Sequence AnalysisAdd
BLAST
Chaini18 – 11721155Laminin subunit beta-3PRO_0000017071Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi220 – 2201N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi250 ↔ 259PROSITE-ProRule annotation
Disulfide bondi252 ↔ 279PROSITE-ProRule annotation
Disulfide bondi281 ↔ 290PROSITE-ProRule annotation
Disulfide bondi293 ↔ 313PROSITE-ProRule annotation
Disulfide bondi316 ↔ 325PROSITE-ProRule annotation
Disulfide bondi318 ↔ 343PROSITE-ProRule annotation
Disulfide bondi346 ↔ 355PROSITE-ProRule annotation
Disulfide bondi358 ↔ 376PROSITE-ProRule annotation
Disulfide bondi379 ↔ 392PROSITE-ProRule annotation
Disulfide bondi381 ↔ 399PROSITE-ProRule annotation
Disulfide bondi401 ↔ 410PROSITE-ProRule annotation
Disulfide bondi413 ↔ 428PROSITE-ProRule annotation
Disulfide bondi431 ↔ 444PROSITE-ProRule annotation
Disulfide bondi433 ↔ 451PROSITE-ProRule annotation
Disulfide bondi453 ↔ 462PROSITE-ProRule annotation
Disulfide bondi465 ↔ 478PROSITE-ProRule annotation
Disulfide bondi481 ↔ 493PROSITE-ProRule annotation
Disulfide bondi483 ↔ 500PROSITE-ProRule annotation
Disulfide bondi502 ↔ 511PROSITE-ProRule annotation
Disulfide bondi519 ↔ 531PROSITE-ProRule annotation
Disulfide bondi534 ↔ 546PROSITE-ProRule annotation
Disulfide bondi536 ↔ 553PROSITE-ProRule annotation
Disulfide bondi555 ↔ 564PROSITE-ProRule annotation
Disulfide bondi567 ↔ 578PROSITE-ProRule annotation
Disulfide bondi581 – 581InterchainCurated
Disulfide bondi584 – 584InterchainCurated
Glycosylationi604 – 6041N-linked (GlcNAc...)Sequence Analysis
Glycosylationi810 – 8101N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi1171 – 1171InterchainCurated

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

MaxQBiQ13751.
PaxDbiQ13751.
PRIDEiQ13751.

PTM databases

PhosphoSiteiQ13751.

Miscellaneous databases

PMAP-CutDBQ13751.

Expressioni

Tissue specificityi

Found in the basement membranes (major component).

Gene expression databases

BgeeiQ13751.
CleanExiHS_LAMB3.
ExpressionAtlasiQ13751. baseline and differential.
GenevestigatoriQ13751.

Organism-specific databases

HPAiHPA008069.

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-3 is a subunit of laminin-5 (laminin-332 or epiligrin/kalinin/nicein). Interacts with ECM1.1 Publication

Protein-protein interaction databases

BioGridi110108. 3 interactions.
IntActiQ13751. 1 interaction.
MINTiMINT-4053402.
STRINGi9606.ENSP00000348384.

Structurei

3D structure databases

ProteinModelPortaliQ13751.
SMRiQ13751. Positions 20-566.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini22 – 249228Laminin N-terminalPROSITE-ProRule annotationAdd
BLAST
Domaini250 – 31566Laminin EGF-like 1PROSITE-ProRule annotationAdd
BLAST
Domaini316 – 37863Laminin EGF-like 2PROSITE-ProRule annotationAdd
BLAST
Domaini379 – 43052Laminin EGF-like 3PROSITE-ProRule annotationAdd
BLAST
Domaini431 – 48050Laminin EGF-like 4PROSITE-ProRule annotationAdd
BLAST
Domaini481 – 53353Laminin EGF-like 5PROSITE-ProRule annotationAdd
BLAST
Domaini534 – 58047Laminin EGF-like 6PROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni579 – 785207Domain IIAdd
BLAST
Regioni786 – 81631Domain alphaAdd
BLAST
Regioni817 – 1170354Domain IAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili723 – 75735Sequence AnalysisAdd
BLAST
Coiled coili831 – 88454Sequence AnalysisAdd
BLAST
Coiled coili948 – 1133186Sequence AnalysisAdd
BLAST

Domaini

The alpha-helical domains I and II are thought to interact with other laminin chains to form a coiled coil structure.
Domain VI is globular.

Sequence similaritiesi

Contains 6 laminin EGF-like domains.PROSITE-ProRule annotation
Contains 1 laminin N-terminal domain.PROSITE-ProRule annotation

Keywords - Domaini

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

Phylogenomic databases

eggNOGiNOG289025.
GeneTreeiENSGT00760000118860.
HOGENOMiHOG000113279.
HOVERGENiHBG052302.
InParanoidiQ13751.
KOiK06244.
OMAiRSQMEED.
OrthoDBiEOG77WWBQ.
PhylomeDBiQ13751.
TreeFamiTF352481.

Family and domain databases

InterProiIPR013032. EGF-like_CS.
IPR002049. EGF_laminin.
IPR008211. Laminin_N.
[Graphical view]
PfamiPF00053. Laminin_EGF. 6 hits.
PF00055. Laminin_N. 1 hit.
[Graphical view]
SMARTiSM00180. EGF_Lam. 6 hits.
SM00136. LamNT. 1 hit.
[Graphical view]
PROSITEiPS00022. EGF_1. 5 hits.
PS01186. EGF_2. 1 hit.
PS01248. EGF_LAM_1. 5 hits.
PS50027. EGF_LAM_2. 6 hits.
PS51117. LAMININ_NTER. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

Q13751-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MRPFFLLCFA LPGLLHAQQA CSRGACYPPV GDLLVGRTRF LRASSTCGLT
60 70 80 90 100
KPETYCTQYG EWQMKCCKCD SRQPHNYYSH RVENVASSSG PMRWWQSQND
110 120 130 140 150
VNPVSLQLDL DRRFQLQEVM MEFQGPMPAG MLIERSSDFG KTWRVYQYLA
160 170 180 190 200
ADCTSTFPRV RQGRPQSWQD VRCQSLPQRP NARLNGGKVQ LNLMDLVSGI
210 220 230 240 250
PATQSQKIQE VGEITNLRVN FTRLAPVPQR GYHPPSAYYA VSQLRLQGSC
260 270 280 290 300
FCHGHADRCA PKPGASAGPS TAVQVHDVCV CQHNTAGPNC ERCAPFYNNR
310 320 330 340 350
PWRPAEGQDA HECQRCDCNG HSETCHFDPA VFAASQGAYG GVCDNCRDHT
360 370 380 390 400
EGKNCERCQL HYFRNRRPGA SIQETCISCE CDPDGAVPGA PCDPVTGQCV
410 420 430 440 450
CKEHVQGERC DLCKPGFTGL TYANPQGCHR CDCNILGSRR DMPCDEESGR
460 470 480 490 500
CLCLPNVVGP KCDQCAPYHW KLASGQGCEP CACDPHNSLS PQCNQFTGQC
510 520 530 540 550
PCREGFGGLM CSAAAIRQCP DRTYGDVATG CRACDCDFRG TEGPGCDKAS
560 570 580 590 600
GRCLCRPGLT GPRCDQCQRG YCNRYPVCVA CHPCFQTYDA DLREQALRFG
610 620 630 640 650
RLRNATASLW SGPGLEDRGL ASRILDAKSK IEQIRAVLSS PAVTEQEVAQ
660 670 680 690 700
VASAILSLRR TLQGLQLDLP LEEETLSLPR DLESLDRSFN GLLTMYQRKR
710 720 730 740 750
EQFEKISSAD PSGAFRMLST AYEQSAQAAQ QVSDSSRLLD QLRDSRREAE
760 770 780 790 800
RLVRQAGGGG GTGSPKLVAL RLEMSSLPDL TPTFNKLCGN SRQMACTPIS
810 820 830 840 850
CPGELCPQDN GTACGSRCRG VLPRAGGAFL MAGQVAEQLR GFNAQLQRTR
860 870 880 890 900
QMIRAAEESA SQIQSSAQRL ETQVSASRSQ MEEDVRRTRL LIQQVRDFLT
910 920 930 940 950
DPDTDAATIQ EVSEAVLALW LPTDSATVLQ KMNEIQAIAA RLPNVDLVLS
960 970 980 990 1000
QTKQDIARAR RLQAEAEEAR SRAHAVEGQV EDVVGNLRQG TVALQEAQDT
1010 1020 1030 1040 1050
MQGTSRSLRL IQDRVAEVQQ VLRPAEKLVT SMTKQLGDFW TRMEELRHQA
1060 1070 1080 1090 1100
RQQGAEAVQA QQLAEGASEQ ALSAQEGFER IKQKYAELKD RLGQSSMLGE
1110 1120 1130 1140 1150
QGARIQSVKT EAEELFGETM EMMDRMKDME LELLRGSQAI MLRSADLTGL
1160 1170
EKRVEQIRDH INGRVLYYAT CK
Length:1,172
Mass (Da):129,572
Last modified:November 1, 1996 - v1
Checksum:i61BC1A60BBD4FA05
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti124 – 1241Q → R in AAA61834. (PubMed:7512558)Curated
Sequence conflicti269 – 2691Missing in AAA61834. (PubMed:7512558)Curated
Sequence conflicti388 – 3881P → A in AAA61834. (PubMed:7512558)Curated
Sequence conflicti426 – 4272QG → RR in AAA61834. (PubMed:7512558)Curated
Sequence conflicti440 – 4412RD → E in AAA61834. (PubMed:7512558)Curated
Sequence conflicti489 – 50012LSPQC…FTGQC → PQPTVQPVHRAV in BAA22263. (PubMed:8530036)CuratedAdd
BLAST
Sequence conflicti603 – 6031R → P in AAA61834. (PubMed:7512558)Curated
Sequence conflicti815 – 8151G → A in AAA61834. (PubMed:7512558)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti181 – 1811N → D.
Corresponds to variant rs2235542 [ dbSNP | Ensembl ].
VAR_037309
Natural varianti199 – 1991G → A in GABEB; somatic second-site mutation. 1 Publication
VAR_037310
Natural varianti207 – 2071K → Q in GABEB; somatic second-site mutation. 1 Publication
VAR_037311
Natural varianti210 – 2101E → K in GABEB. 2 Publications
VAR_004170
Natural varianti292 – 2921R → L.
Corresponds to variant rs12091253 [ dbSNP | Ensembl ].
VAR_037312
Natural varianti438 – 4381S → T.
Corresponds to variant rs2229468 [ dbSNP | Ensembl ].
VAR_034060
Natural varianti450 – 4501R → C in a colorectal cancer sample; somatic mutation. 1 Publication
VAR_035820
Natural varianti527 – 5271V → M.
Corresponds to variant rs2076349 [ dbSNP | Ensembl ].
VAR_037313
Natural varianti679 – 6791P → L in H-JEB. 1 Publication
VAR_004171
Natural varianti690 – 6901N → S.
Corresponds to variant rs2229466 [ dbSNP | Ensembl ].
VAR_034061
Natural varianti852 – 8521M → L.1 Publication
Corresponds to variant rs12748250 [ dbSNP | Ensembl ].
VAR_034062
Natural varianti926 – 9261A → D.
Corresponds to variant rs2076222 [ dbSNP | Ensembl ].
VAR_037314
Natural varianti988 – 9881R → W.
Corresponds to variant rs2229467 [ dbSNP | Ensembl ].
VAR_034063

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
L25541 mRNA. Translation: AAA61834.1.
U17760
, U17745, U17746, U17747, U17748, U17749, U17750, U17751, U17752, U17753, U17754, U17755, U17756, U17757, U17758, U17759 Genomic DNA. Translation: AAC51352.1.
D37766 mRNA. Translation: BAA22263.1.
AY035783 mRNA. Translation: AAK61364.1.
AL023754 Genomic DNA. Translation: CAA19297.2.
AL023754, AL031316 Genomic DNA. Translation: CAI19989.1.
AL031316, AL023754 Genomic DNA. Translation: CAI20062.1.
CH471100 Genomic DNA. Translation: EAW93448.1.
CH471100 Genomic DNA. Translation: EAW93449.1.
BC075838 mRNA. Translation: AAH75838.1.
CCDSiCCDS1487.1.
PIRiA53612.
RefSeqiNP_000219.2. NM_000228.2.
NP_001017402.1. NM_001017402.1.
NP_001121113.1. NM_001127641.1.
XP_005273181.1. XM_005273124.2.
UniGeneiHs.497636.

Genome annotation databases

EnsembliENST00000356082; ENSP00000348384; ENSG00000196878.
ENST00000367030; ENSP00000355997; ENSG00000196878.
ENST00000391911; ENSP00000375778; ENSG00000196878.
GeneIDi3914.
KEGGihsa:3914.
UCSCiuc001hhg.3. human.

Polymorphism databases

DMDMi2497600.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
L25541 mRNA. Translation: AAA61834.1 .
U17760
, U17745 , U17746 , U17747 , U17748 , U17749 , U17750 , U17751 , U17752 , U17753 , U17754 , U17755 , U17756 , U17757 , U17758 , U17759 Genomic DNA. Translation: AAC51352.1 .
D37766 mRNA. Translation: BAA22263.1 .
AY035783 mRNA. Translation: AAK61364.1 .
AL023754 Genomic DNA. Translation: CAA19297.2 .
AL023754 , AL031316 Genomic DNA. Translation: CAI19989.1 .
AL031316 , AL023754 Genomic DNA. Translation: CAI20062.1 .
CH471100 Genomic DNA. Translation: EAW93448.1 .
CH471100 Genomic DNA. Translation: EAW93449.1 .
BC075838 mRNA. Translation: AAH75838.1 .
CCDSi CCDS1487.1.
PIRi A53612.
RefSeqi NP_000219.2. NM_000228.2.
NP_001017402.1. NM_001017402.1.
NP_001121113.1. NM_001127641.1.
XP_005273181.1. XM_005273124.2.
UniGenei Hs.497636.

3D structure databases

ProteinModelPortali Q13751.
SMRi Q13751. Positions 20-566.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 110108. 3 interactions.
IntActi Q13751. 1 interaction.
MINTi MINT-4053402.
STRINGi 9606.ENSP00000348384.

Chemistry

ChEMBLi CHEMBL2364187.

PTM databases

PhosphoSitei Q13751.

Polymorphism databases

DMDMi 2497600.

Proteomic databases

MaxQBi Q13751.
PaxDbi Q13751.
PRIDEi Q13751.

Protocols and materials databases

DNASUi 3914.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000356082 ; ENSP00000348384 ; ENSG00000196878 .
ENST00000367030 ; ENSP00000355997 ; ENSG00000196878 .
ENST00000391911 ; ENSP00000375778 ; ENSG00000196878 .
GeneIDi 3914.
KEGGi hsa:3914.
UCSCi uc001hhg.3. human.

Organism-specific databases

CTDi 3914.
GeneCardsi GC01M209788.
GeneReviewsi LAMB3.
HGNCi HGNC:6490. LAMB3.
HPAi HPA008069.
MIMi 150310. gene.
226650. phenotype.
226700. phenotype.
neXtProti NX_Q13751.
Orphaneti 79402. Generalized junctional epidermolysis bullosa, non-Herlitz type.
100031. Hypoplastic amelogenesis imperfecta.
79404. Junctional epidermolysis bullosa, Herlitz type.
PharmGKBi PA30278.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG289025.
GeneTreei ENSGT00760000118860.
HOGENOMi HOG000113279.
HOVERGENi HBG052302.
InParanoidi Q13751.
KOi K06244.
OMAi RSQMEED.
OrthoDBi EOG77WWBQ.
PhylomeDBi Q13751.
TreeFami TF352481.

Enzyme and pathway databases

Reactomei REACT_118572. Degradation of the extracellular matrix.
REACT_150180. Assembly of collagen fibrils and other multimeric structures.
REACT_150268. Anchoring fibril formation.
REACT_163874. Non-integrin membrane-ECM interactions.
REACT_169262. Laminin interactions.
REACT_20537. Type I hemidesmosome assembly.

Miscellaneous databases

ChiTaRSi LAMB3. human.
GeneWikii Laminin,_beta_3.
GenomeRNAii 3914.
NextBioi 15375.
PMAP-CutDB Q13751.
PROi Q13751.
SOURCEi Search...

Gene expression databases

Bgeei Q13751.
CleanExi HS_LAMB3.
ExpressionAtlasi Q13751. baseline and differential.
Genevestigatori Q13751.

Family and domain databases

InterProi IPR013032. EGF-like_CS.
IPR002049. EGF_laminin.
IPR008211. Laminin_N.
[Graphical view ]
Pfami PF00053. Laminin_EGF. 6 hits.
PF00055. Laminin_N. 1 hit.
[Graphical view ]
SMARTi SM00180. EGF_Lam. 6 hits.
SM00136. LamNT. 1 hit.
[Graphical view ]
PROSITEi PS00022. EGF_1. 5 hits.
PS01186. EGF_2. 1 hit.
PS01248. EGF_LAM_1. 5 hits.
PS50027. EGF_LAM_2. 6 hits.
PS51117. LAMININ_NTER. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "The complete primary structure for a novel laminin chain, the laminin B1k chain."
    Gerecke D.R., Wagman D.W., Champliaud M.-F., Burgeson R.E.
    J. Biol. Chem. 269:11073-11080(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 172-190.
  2. "Cloning of the beta 3 chain gene (LAMB3) of human laminin 5, a candidate gene in junctional epidermolysis bullosa."
    Pulkkinen L., Gerecke D.R., Christiano A.M., Wagman D.W., Burgeson R.E., Uitto J.
    Genomics 25:192-198(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  3. "Chromosomal loci of 50 human keratinocyte cDNAs assigned by fluorescence in situ hybridization."
    Morishima Y., Ariyama T., Yamanishi K., Abe T., Ueda E., Yasuno H., Inazawa J.
    Genomics 28:273-279(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Epidermis.
  4. "In vivo restoration of laminin 5 beta 3 expression and function in junctional epidermolysis bullosa."
    Robbins P.B., Lin Q., Goodnough J.B., Tian H., Chen X., Khavari P.A.
    Proc. Natl. Acad. Sci. U.S.A. 98:5193-5198(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  5. "The DNA sequence and biological annotation of human chromosome 1."
    Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.
    , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
    Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], VARIANT LEU-852.
  7. "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(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Eye.
  8. "ECM1 interacts with fibulin-3 and the beta 3 chain of laminin 332 through its serum albumin subdomain-like 2 domain."
    Sercu S., Lambeir A.M., Steenackers E., El Ghalbzouri A., Geentjens K., Sasaki T., Oyama N., Merregaert J.
    Matrix Biol. 28:160-169(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH ECM1.
  9. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  10. "Detection of sequence variants in the gene encoding the beta 3 chain of laminin 5 (LAMB3)."
    Pulkkinen L., McGrath J.A., Christiano A.M., Uitto J.
    Hum. Mutat. 6:77-84(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT H-JEB LEU-679.
  11. "E210K mutation in the gene encoding the beta3 chain of laminin-5 (LAMB3) is predictive of a phenotype of generalized atrophic benign epidermolysis bullosa."
    Mellerio J.E., Eady R.A.J., Atherton D.J., Lake B.D., McGrath J.A.
    Br. J. Dermatol. 139:325-331(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT GABEB LYS-210.
  12. Cited for: VARIANT [LARGE SCALE ANALYSIS] CYS-450.
  13. "Revertant mosaicism in junctional epidermolysis bullosa due to multiple correcting second-site mutations in LAMB3."
    Pasmooij A.M.G., Pas H.H., Bolling M.C., Jonkman M.F.
    J. Clin. Invest. 117:1240-1248(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS GABEB ALA-199; GLN-207 AND LYS-210.

Entry informationi

Entry nameiLAMB3_HUMAN
AccessioniPrimary (citable) accession number: Q13751
Secondary accession number(s): D3DT88
, O14947, Q14733, Q9UJK4, Q9UJL1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1996
Last modified: October 29, 2014
This is version 151 of the entry and version 1 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, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 1
    Human chromosome 1: 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