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Q13751

- LAMB3_HUMAN

UniProt

Q13751 - LAMB3_HUMAN

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Protein
Laminin subunit beta-3
Gene
LAMB3, LAMNB1
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. protein binding Source: UniProtKB
  2. 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. epidermis development Source: ProtInc
  5. extracellular matrix disassembly Source: Reactome
  6. extracellular matrix organization Source: Reactome
  7. 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.
Note: The disease is caused by mutations affecting the gene represented in this entry.1 Publication
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.
Note: The disease is caused by mutations affecting the gene represented in this entry.2 Publications
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 – 1717 Reviewed prediction
Add
BLAST
Chaini18 – 11721155Laminin subunit beta-3
PRO_0000017071Add
BLAST

Amino acid modifications

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

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

ArrayExpressiQ13751.
BgeeiQ13751.
CleanExiHS_LAMB3.
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.

Family & Domainsi

Domains and Repeats

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

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni579 – 785207Domain II
Add
BLAST
Regioni786 – 81631Domain alpha
Add
BLAST
Regioni817 – 1170354Domain I
Add
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili723 – 75735 Reviewed prediction
Add
BLAST
Coiled coili831 – 88454 Reviewed prediction
Add
BLAST
Coiled coili948 – 1133186 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.
Domain VI is globular.

Sequence similaritiesi

Keywords - Domaini

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

Phylogenomic databases

eggNOGiNOG289025.
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

MRPFFLLCFA LPGLLHAQQA CSRGACYPPV GDLLVGRTRF LRASSTCGLT     50
KPETYCTQYG EWQMKCCKCD SRQPHNYYSH RVENVASSSG PMRWWQSQND 100
VNPVSLQLDL DRRFQLQEVM MEFQGPMPAG MLIERSSDFG KTWRVYQYLA 150
ADCTSTFPRV RQGRPQSWQD VRCQSLPQRP NARLNGGKVQ LNLMDLVSGI 200
PATQSQKIQE VGEITNLRVN FTRLAPVPQR GYHPPSAYYA VSQLRLQGSC 250
FCHGHADRCA PKPGASAGPS TAVQVHDVCV CQHNTAGPNC ERCAPFYNNR 300
PWRPAEGQDA HECQRCDCNG HSETCHFDPA VFAASQGAYG GVCDNCRDHT 350
EGKNCERCQL HYFRNRRPGA SIQETCISCE CDPDGAVPGA PCDPVTGQCV 400
CKEHVQGERC DLCKPGFTGL TYANPQGCHR CDCNILGSRR DMPCDEESGR 450
CLCLPNVVGP KCDQCAPYHW KLASGQGCEP CACDPHNSLS PQCNQFTGQC 500
PCREGFGGLM CSAAAIRQCP DRTYGDVATG CRACDCDFRG TEGPGCDKAS 550
GRCLCRPGLT GPRCDQCQRG YCNRYPVCVA CHPCFQTYDA DLREQALRFG 600
RLRNATASLW SGPGLEDRGL ASRILDAKSK IEQIRAVLSS PAVTEQEVAQ 650
VASAILSLRR TLQGLQLDLP LEEETLSLPR DLESLDRSFN GLLTMYQRKR 700
EQFEKISSAD PSGAFRMLST AYEQSAQAAQ QVSDSSRLLD QLRDSRREAE 750
RLVRQAGGGG GTGSPKLVAL RLEMSSLPDL TPTFNKLCGN SRQMACTPIS 800
CPGELCPQDN GTACGSRCRG VLPRAGGAFL MAGQVAEQLR GFNAQLQRTR 850
QMIRAAEESA SQIQSSAQRL ETQVSASRSQ MEEDVRRTRL LIQQVRDFLT 900
DPDTDAATIQ EVSEAVLALW LPTDSATVLQ KMNEIQAIAA RLPNVDLVLS 950
QTKQDIARAR RLQAEAEEAR SRAHAVEGQV EDVVGNLRQG TVALQEAQDT 1000
MQGTSRSLRL IQDRVAEVQQ VLRPAEKLVT SMTKQLGDFW TRMEELRHQA 1050
RQQGAEAVQA QQLAEGASEQ ALSAQEGFER IKQKYAELKD RLGQSSMLGE 1100
QGARIQSVKT EAEELFGETM EMMDRMKDME LELLRGSQAI MLRSADLTGL 1150
EKRVEQIRDH INGRVLYYAT CK 1172
Length:1,172
Mass (Da):129,572
Last modified:November 1, 1996 - v1
Checksum:i61BC1A60BBD4FA05
GO

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 conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti124 – 1241Q → R in AAA61834. 1 Publication
Sequence conflicti269 – 2691Missing in AAA61834. 1 Publication
Sequence conflicti388 – 3881P → A in AAA61834. 1 Publication
Sequence conflicti426 – 4272QG → RR in AAA61834. 1 Publication
Sequence conflicti440 – 4412RD → E in AAA61834. 1 Publication
Sequence conflicti489 – 50012LSPQC…FTGQC → PQPTVQPVHRAV in BAA22263. 1 Publication
Add
BLAST
Sequence conflicti603 – 6031R → P in AAA61834. 1 Publication
Sequence conflicti815 – 8151G → A in AAA61834. 1 Publication

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.
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

ArrayExpressi Q13751.
Bgeei Q13751.
CleanExi HS_LAMB3.
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: September 3, 2014
This is version 149 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

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