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Protein

Laminin subunit beta-1

Gene

LAMB1

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. Involved in the organization of the laminar architecture of cerebral cortex. It is probably required for the integrity of the basement membrane/glia limitans that serves as an anchor point for the endfeet of radial glial cells and as a physical barrier to migrating neurons. Radial glial cells play a central role in cerebral cortical development, where they act both as the proliferative unit of the cerebral cortex and a scaffold for neurons migrating toward the pial surface.1 Publication

GO - Molecular functioni

  • extracellular matrix structural constituent Source: HGNC
  • structural molecule activity Source: UniProtKB

GO - Biological processi

  • cell adhesion Source: HGNC
  • endodermal cell differentiation Source: UniProtKB
  • extracellular matrix organization Source: Reactome
  • neuronal-glial interaction involved in cerebral cortex radial glia guided migration Source: UniProtKB
  • neuron projection development Source: UniProtKB
  • odontogenesis Source: UniProtKB
  • positive regulation of cell migration Source: UniProtKB
  • positive regulation of epithelial cell proliferation Source: HGNC
  • substrate adhesion-dependent cell spreading Source: BHF-UCL
Complete GO annotation...

Keywords - Biological processi

Cell adhesion

Enzyme and pathway databases

BioCyciZFISH:ENSG00000091136-MONOMER.
ReactomeiR-HSA-1474228. Degradation of the extracellular matrix.
R-HSA-3000157. Laminin interactions.
R-HSA-3000171. Non-integrin membrane-ECM interactions.
R-HSA-3000178. ECM proteoglycans.
R-HSA-373760. L1CAM interactions.
R-HSA-8874081. MET activates PTK2 signaling.
SIGNORiP07942.

Names & Taxonomyi

Protein namesi
Recommended name:
Laminin subunit beta-1
Alternative name(s):
Laminin B1 chain
Laminin-1 subunit beta
Laminin-10 subunit beta
Laminin-12 subunit beta
Laminin-2 subunit beta
Laminin-6 subunit beta
Laminin-8 subunit beta
Gene namesi
Name:LAMB1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 7

Organism-specific databases

HGNCiHGNC:6486. LAMB1.

Subcellular locationi

GO - Cellular componenti

  • basement membrane Source: UniProtKB
  • extracellular exosome Source: UniProtKB
  • extracellular matrix Source: UniProtKB
  • extracellular region Source: Reactome
  • extracellular space Source: UniProtKB
  • laminin-10 complex Source: UniProtKB
  • laminin-1 complex Source: UniProtKB
  • laminin-2 complex Source: UniProtKB
  • laminin-8 complex Source: UniProtKB
  • perinuclear region of cytoplasm Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Basement membrane, Extracellular matrix, Secreted

Pathology & Biotechi

Involvement in diseasei

Lissencephaly 5 (LIS5)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionAn autosomal recessive brain malformation characterized by cobblestone changes in the cortex, more severe in the posterior region, and subcortical band heterotopia. Affected individuals have hydrocephalus, seizures, and severely delayed psychomotor development.
See also OMIM:615191

Keywords - Diseasei

Lissencephaly

Organism-specific databases

DisGeNETi3912.
MalaCardsiLAMB1.
MIMi615191. phenotype.
OpenTargetsiENSG00000091136.
Orphaneti352682. Cobblestone lissencephaly without muscular or ocular involvement.
PharmGKBiPA30275.

Chemistry databases

ChEMBLiCHEMBL2364187.

Polymorphism and mutation databases

BioMutaiLAMB1.
DMDMi317373377.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 21Add BLAST21
ChainiPRO_000001706522 – 1786Laminin subunit beta-1Add BLAST1765

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi120N-linked (GlcNAc...)Sequence analysis1
Modified residuei250PhosphoserineBy similarity1
Disulfide bondi271 ↔ 280PROSITE-ProRule annotation
Disulfide bondi273 ↔ 298PROSITE-ProRule annotation
Disulfide bondi300 ↔ 309PROSITE-ProRule annotation
Disulfide bondi312 ↔ 332PROSITE-ProRule annotation
Disulfide bondi335 ↔ 344PROSITE-ProRule annotation
Disulfide bondi337 ↔ 362PROSITE-ProRule annotation
Glycosylationi356N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi365 ↔ 374PROSITE-ProRule annotation
Disulfide bondi377 ↔ 395PROSITE-ProRule annotation
Disulfide bondi398 ↔ 411PROSITE-ProRule annotation
Disulfide bondi400 ↔ 426PROSITE-ProRule annotation
Disulfide bondi428 ↔ 437PROSITE-ProRule annotation
Disulfide bondi440 ↔ 455PROSITE-ProRule annotation
Disulfide bondi458 ↔ 472PROSITE-ProRule annotation
Disulfide bondi460 ↔ 479PROSITE-ProRule annotation
Disulfide bondi481 ↔ 490PROSITE-ProRule annotation
Disulfide bondi493 ↔ 507PROSITE-ProRule annotation
Disulfide bondi510 ↔ 522PROSITE-ProRule annotation
Disulfide bondi512 ↔ 529PROSITE-ProRule annotation
Glycosylationi519N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi531 ↔ 540PROSITE-ProRule annotation
Glycosylationi677N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi773 ↔ 785PROSITE-ProRule annotation
Disulfide bondi775 ↔ 792PROSITE-ProRule annotation
Disulfide bondi794 ↔ 803PROSITE-ProRule annotation
Disulfide bondi806 ↔ 818PROSITE-ProRule annotation
Disulfide bondi821 ↔ 833PROSITE-ProRule annotation
Disulfide bondi823 ↔ 840PROSITE-ProRule annotation
Disulfide bondi842 ↔ 851PROSITE-ProRule annotation
Disulfide bondi854 ↔ 864PROSITE-ProRule annotation
Disulfide bondi867 ↔ 876PROSITE-ProRule annotation
Disulfide bondi869 ↔ 883PROSITE-ProRule annotation
Disulfide bondi886 ↔ 895PROSITE-ProRule annotation
Disulfide bondi898 ↔ 914PROSITE-ProRule annotation
Disulfide bondi917 ↔ 933PROSITE-ProRule annotation
Disulfide bondi919 ↔ 944PROSITE-ProRule annotation
Disulfide bondi946 ↔ 955PROSITE-ProRule annotation
Disulfide bondi958 ↔ 973PROSITE-ProRule annotation
Disulfide bondi976 ↔ 990PROSITE-ProRule annotation
Disulfide bondi978 ↔ 997PROSITE-ProRule annotation
Disulfide bondi1000 ↔ 1009PROSITE-ProRule annotation
Disulfide bondi1012 ↔ 1025PROSITE-ProRule annotation
Disulfide bondi1028 ↔ 1040PROSITE-ProRule annotation
Disulfide bondi1030 ↔ 1054PROSITE-ProRule annotation
Glycosylationi1041N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi1056 ↔ 1065PROSITE-ProRule annotation
Disulfide bondi1068 ↔ 1081PROSITE-ProRule annotation
Disulfide bondi1084 ↔ 1096PROSITE-ProRule annotation
Disulfide bondi1086 ↔ 1103PROSITE-ProRule annotation
Disulfide bondi1105 ↔ 1114PROSITE-ProRule annotation
Disulfide bondi1117 ↔ 1129PROSITE-ProRule annotation
Disulfide bondi1132 ↔ 1144PROSITE-ProRule annotation
Disulfide bondi1134 ↔ 1151PROSITE-ProRule annotation
Disulfide bondi1153 ↔ 1162PROSITE-ProRule annotation
Disulfide bondi1165 ↔ 1176PROSITE-ProRule annotation
Disulfide bondi1179InterchainCurated
Disulfide bondi1182InterchainCurated
Glycosylationi1195N-linked (GlcNAc...)Sequence analysis1
Glycosylationi1279N-linked (GlcNAc...)2 Publications1
Glycosylationi1336N-linked (GlcNAc...)Sequence analysis1
Glycosylationi1343N-linked (GlcNAc...)Sequence analysis1
Modified residuei1478Phosphoserine; by FAM20C1 Publication1
Glycosylationi1487N-linked (GlcNAc...)Sequence analysis1
Modified residuei1496Phosphoserine; by FAM20C1 Publication1
Glycosylationi1542N-linked (GlcNAc...)Sequence analysis1
Modified residuei1666Phosphoserine; by FAM20C1 Publication1
Modified residuei1682Phosphoserine; by FAM20C1 Publication1
Disulfide bondi1785InterchainCurated

Keywords - PTMi

Disulfide bond, Glycoprotein, Phosphoprotein

Proteomic databases

EPDiP07942.
MaxQBiP07942.
PaxDbiP07942.
PeptideAtlasiP07942.
PRIDEiP07942.

PTM databases

iPTMnetiP07942.
PhosphoSitePlusiP07942.
SwissPalmiP07942.

Expressioni

Gene expression databases

BgeeiENSG00000091136.
CleanExiHS_LAMB1.
ExpressionAtlasiP07942. baseline and differential.
GenevisibleiP07942. HS.

Organism-specific databases

HPAiCAB004256.
HPA004056.
HPA004132.

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-1 is a subunit of laminin-1 (laminin-111 or EHS laminin), laminin-2 (laminin-211 or merosin), laminin-6 (laminin-311 or K-laminin), laminin-8 (laminin-411), laminin-10 (laminin-511) and laminin-12 (laminin-213).

Protein-protein interaction databases

BioGridi110106. 40 interactors.
IntActiP07942. 20 interactors.
MINTiMINT-2860329.
STRINGi9606.ENSP00000222399.

Structurei

3D structure databases

ProteinModelPortaliP07942.
SMRiP07942.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini31 – 270Laminin N-terminalPROSITE-ProRule annotationAdd BLAST240
Domaini271 – 334Laminin EGF-like 1PROSITE-ProRule annotationAdd BLAST64
Domaini335 – 397Laminin EGF-like 2PROSITE-ProRule annotationAdd BLAST63
Domaini398 – 457Laminin EGF-like 3PROSITE-ProRule annotationAdd BLAST60
Domaini458 – 509Laminin EGF-like 4PROSITE-ProRule annotationAdd BLAST52
Domaini510 – 540Laminin EGF-like 5; truncatedPROSITE-ProRule annotationAdd BLAST31
Domaini549 – 767Laminin IV type BPROSITE-ProRule annotationAdd BLAST219
Domaini773 – 820Laminin EGF-like 6PROSITE-ProRule annotationAdd BLAST48
Domaini821 – 866Laminin EGF-like 7PROSITE-ProRule annotationAdd BLAST46
Domaini867 – 916Laminin EGF-like 8PROSITE-ProRule annotationAdd BLAST50
Domaini917 – 975Laminin EGF-like 9PROSITE-ProRule annotationAdd BLAST59
Domaini976 – 1027Laminin EGF-like 10PROSITE-ProRule annotationAdd BLAST52
Domaini1028 – 1083Laminin EGF-like 11PROSITE-ProRule annotationAdd BLAST56
Domaini1084 – 1131Laminin EGF-like 12PROSITE-ProRule annotationAdd BLAST48
Domaini1132 – 1178Laminin EGF-like 13PROSITE-ProRule annotationAdd BLAST47

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni1179 – 1397Domain IIAdd BLAST219
Regioni1398 – 1430Domain alphaAdd BLAST33
Regioni1431 – 1786Domain IAdd BLAST356

Coiled coil

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Coiled coili1216 – 1315Sequence analysisAdd BLAST100
Coiled coili1353 – 1388Sequence analysisAdd BLAST36
Coiled coili1442 – 1781Sequence analysisAdd BLAST340

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.
InParanoidiP07942.
KOiK05636.
PhylomeDBiP07942.
TreeFamiTF312903.

Family and domain databases

InterProiIPR000742. EGF-like_dom.
IPR002049. Laminin_EGF.
IPR013015. Laminin_IV_B.
IPR008211. Laminin_N.
IPR009053. Prefoldin.
[Graphical view]
PfamiPF00053. Laminin_EGF. 13 hits.
PF00055. Laminin_N. 1 hit.
[Graphical view]
SMARTiSM00181. EGF. 8 hits.
SM00180. EGF_Lam. 13 hits.
SM00136. LamNT. 1 hit.
[Graphical view]
SUPFAMiSSF46579. SSF46579. 1 hit.
PROSITEiPS00022. EGF_1. 9 hits.
PS01186. EGF_2. 2 hits.
PS01248. EGF_LAM_1. 11 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.

P07942-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGLLQLLAFS FLALCRARVR AQEPEFSYGC AEGSCYPATG DLLIGRAQKL
60 70 80 90 100
SVTSTCGLHK PEPYCIVSHL QEDKKCFICN SQDPYHETLN PDSHLIENVV
110 120 130 140 150
TTFAPNRLKI WWQSENGVEN VTIQLDLEAE FHFTHLIMTF KTFRPAAMLI
160 170 180 190 200
ERSSDFGKTW GVYRYFAYDC EASFPGISTG PMKKVDDIIC DSRYSDIEPS
210 220 230 240 250
TEGEVIFRAL DPAFKIEDPY SPRIQNLLKI TNLRIKFVKL HTLGDNLLDS
260 270 280 290 300
RMEIREKYYY AVYDMVVRGN CFCYGHASEC APVDGFNEEV EGMVHGHCMC
310 320 330 340 350
RHNTKGLNCE LCMDFYHDLP WRPAEGRNSN ACKKCNCNEH SISCHFDMAV
360 370 380 390 400
YLATGNVSGG VCDDCQHNTM GRNCEQCKPF YYQHPERDIR DPNFCERCTC
410 420 430 440 450
DPAGSQNEGI CDSYTDFSTG LIAGQCRCKL NVEGEHCDVC KEGFYDLSSE
460 470 480 490 500
DPFGCKSCAC NPLGTIPGGN PCDSETGHCY CKRLVTGQHC DQCLPEHWGL
510 520 530 540 550
SNDLDGCRPC DCDLGGALNN SCFAESGQCS CRPHMIGRQC NEVEPGYYFA
560 570 580 590 600
TLDHYLYEAE EANLGPGVSI VERQYIQDRI PSWTGAGFVR VPEGAYLEFF
610 620 630 640 650
IDNIPYSMEY DILIRYEPQL PDHWEKAVIT VQRPGRIPTS SRCGNTIPDD
660 670 680 690 700
DNQVVSLSPG SRYVVLPRPV CFEKGTNYTV RLELPQYTSS DSDVESPYTL
710 720 730 740 750
IDSLVLMPYC KSLDIFTVGG SGDGVVTNSA WETFQRYRCL ENSRSVVKTP
760 770 780 790 800
MTDVCRNIIF SISALLHQTG LACECDPQGS LSSVCDPNGG QCQCRPNVVG
810 820 830 840 850
RTCNRCAPGT FGFGPSGCKP CECHLQGSVN AFCNPVTGQC HCFQGVYARQ
860 870 880 890 900
CDRCLPGHWG FPSCQPCQCN GHADDCDPVT GECLNCQDYT MGHNCERCLA
910 920 930 940 950
GYYGDPIIGS GDHCRPCPCP DGPDSGRQFA RSCYQDPVTL QLACVCDPGY
960 970 980 990 1000
IGSRCDDCAS GYFGNPSEVG GSCQPCQCHN NIDTTDPEAC DKETGRCLKC
1010 1020 1030 1040 1050
LYHTEGEHCQ FCRFGYYGDA LQQDCRKCVC NYLGTVQEHC NGSDCQCDKA
1060 1070 1080 1090 1100
TGQCLCLPNV IGQNCDRCAP NTWQLASGTG CDPCNCNAAH SFGPSCNEFT
1110 1120 1130 1140 1150
GQCQCMPGFG GRTCSECQEL FWGDPDVECR ACDCDPRGIE TPQCDQSTGQ
1160 1170 1180 1190 1200
CVCVEGVEGP RCDKCTRGYS GVFPDCTPCH QCFALWDVII AELTNRTHRF
1210 1220 1230 1240 1250
LEKAKALKIS GVIGPYRETV DSVERKVSEI KDILAQSPAA EPLKNIGNLF
1260 1270 1280 1290 1300
EEAEKLIKDV TEMMAQVEVK LSDTTSQSNS TAKELDSLQT EAESLDNTVK
1310 1320 1330 1340 1350
ELAEQLEFIK NSDIRGALDS ITKYFQMSLE AEERVNASTT EPNSTVEQSA
1360 1370 1380 1390 1400
LMRDRVEDVM MERESQFKEK QEEQARLLDE LAGKLQSLDL SAAAEMTCGT
1410 1420 1430 1440 1450
PPGASCSETE CGGPNCRTDE GERKCGGPGC GGLVTVAHNA WQKAMDLDQD
1460 1470 1480 1490 1500
VLSALAEVEQ LSKMVSEAKL RADEAKQSAE DILLKTNATK EKMDKSNEEL
1510 1520 1530 1540 1550
RNLIKQIRNF LTQDSADLDS IEAVANEVLK MEMPSTPQQL QNLTEDIRER
1560 1570 1580 1590 1600
VESLSQVEVI LQHSAADIAR AEMLLEEAKR ASKSATDVKV TADMVKEALE
1610 1620 1630 1640 1650
EAEKAQVAAE KAIKQADEDI QGTQNLLTSI ESETAASEET LFNASQRISE
1660 1670 1680 1690 1700
LERNVEELKR KAAQNSGEAE YIEKVVYTVK QSAEDVKKTL DGELDEKYKK
1710 1720 1730 1740 1750
VENLIAKKTE ESADARRKAE MLQNEAKTLL AQANSKLQLL KDLERKYEDN
1760 1770 1780
QRYLEDKAQE LARLEGEVRS LLKDISQKVA VYSTCL
Length:1,786
Mass (Da):198,038
Last modified:January 11, 2011 - v2
Checksum:i8F8EF96E765B9A0D
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti1470L → V in AAA59487 (PubMed:3661559).Curated1
Sequence conflicti1696E → G in AAA59487 (PubMed:3661559).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_061349379P → S.Corresponds to variant rs28750165dbSNPEnsembl.1
Natural variantiVAR_014698670V → A.Corresponds to variant rs20555dbSNPEnsembl.1
Natural variantiVAR_032774860G → S.Corresponds to variant rs35710474dbSNPEnsembl.1
Natural variantiVAR_0146991022Q → R.Combined sources2 PublicationsCorresponds to variant rs20556dbSNPEnsembl.1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M61951
, M58147, M61917, M61918, M61921, M61922, M61923, M61924, M61925, M61926, M61927, M61928, M61929, M61930, M61931, M61932, M61933, M61934, M61935, M61936, M61938, M61939, M61940, M61941, M61942, M61943, M61944, M61945, M61946, M61947, M61948, M61949, M61950 Genomic DNA. Translation: AAA59486.1.
M55370
, M55378, M55365, M55371, M55372, M55373, M55374, M55375, M55376, M55344, M55345, M55346, M55347, M55348, M55349, M55350, M55351, M55352, M55353, M55355, M55356, M55357, M55358, M55359, M55360, M55361, M55362, M55363, M55364, M55366, M55367, M55368, M55369 Genomic DNA. Translation: AAA59485.1.
M61916 mRNA. Translation: AAA59482.1.
CH236947 Genomic DNA. Translation: EAL24388.1.
BC113455 mRNA. Translation: AAI13456.1.
M20206 mRNA. Translation: AAA59487.1.
CCDSiCCDS5750.1.
PIRiS13547. MMHUB1.
RefSeqiNP_002282.2. NM_002291.2.
UniGeneiHs.650585.

Genome annotation databases

EnsembliENST00000222399; ENSP00000222399; ENSG00000091136.
GeneIDi3912.
KEGGihsa:3912.
UCSCiuc003vew.3. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M61951
, M58147, M61917, M61918, M61921, M61922, M61923, M61924, M61925, M61926, M61927, M61928, M61929, M61930, M61931, M61932, M61933, M61934, M61935, M61936, M61938, M61939, M61940, M61941, M61942, M61943, M61944, M61945, M61946, M61947, M61948, M61949, M61950 Genomic DNA. Translation: AAA59486.1.
M55370
, M55378, M55365, M55371, M55372, M55373, M55374, M55375, M55376, M55344, M55345, M55346, M55347, M55348, M55349, M55350, M55351, M55352, M55353, M55355, M55356, M55357, M55358, M55359, M55360, M55361, M55362, M55363, M55364, M55366, M55367, M55368, M55369 Genomic DNA. Translation: AAA59485.1.
M61916 mRNA. Translation: AAA59482.1.
CH236947 Genomic DNA. Translation: EAL24388.1.
BC113455 mRNA. Translation: AAI13456.1.
M20206 mRNA. Translation: AAA59487.1.
CCDSiCCDS5750.1.
PIRiS13547. MMHUB1.
RefSeqiNP_002282.2. NM_002291.2.
UniGeneiHs.650585.

3D structure databases

ProteinModelPortaliP07942.
SMRiP07942.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi110106. 40 interactors.
IntActiP07942. 20 interactors.
MINTiMINT-2860329.
STRINGi9606.ENSP00000222399.

Chemistry databases

ChEMBLiCHEMBL2364187.

PTM databases

iPTMnetiP07942.
PhosphoSitePlusiP07942.
SwissPalmiP07942.

Polymorphism and mutation databases

BioMutaiLAMB1.
DMDMi317373377.

Proteomic databases

EPDiP07942.
MaxQBiP07942.
PaxDbiP07942.
PeptideAtlasiP07942.
PRIDEiP07942.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000222399; ENSP00000222399; ENSG00000091136.
GeneIDi3912.
KEGGihsa:3912.
UCSCiuc003vew.3. human.

Organism-specific databases

CTDi3912.
DisGeNETi3912.
GeneCardsiLAMB1.
H-InvDBHIX0025323.
HGNCiHGNC:6486. LAMB1.
HPAiCAB004256.
HPA004056.
HPA004132.
MalaCardsiLAMB1.
MIMi150240. gene.
615191. phenotype.
neXtProtiNX_P07942.
OpenTargetsiENSG00000091136.
Orphaneti352682. Cobblestone lissencephaly without muscular or ocular involvement.
PharmGKBiPA30275.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG0994. Eukaryota.
ENOG410XPEG. LUCA.
GeneTreeiENSGT00780000121851.
HOGENOMiHOG000007552.
HOVERGENiHBG052301.
InParanoidiP07942.
KOiK05636.
PhylomeDBiP07942.
TreeFamiTF312903.

Enzyme and pathway databases

BioCyciZFISH:ENSG00000091136-MONOMER.
ReactomeiR-HSA-1474228. Degradation of the extracellular matrix.
R-HSA-3000157. Laminin interactions.
R-HSA-3000171. Non-integrin membrane-ECM interactions.
R-HSA-3000178. ECM proteoglycans.
R-HSA-373760. L1CAM interactions.
R-HSA-8874081. MET activates PTK2 signaling.
SIGNORiP07942.

Miscellaneous databases

ChiTaRSiLAMB1. human.
GeneWikiiLaminin,_beta_1.
GenomeRNAii3912.
PROiP07942.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000091136.
CleanExiHS_LAMB1.
ExpressionAtlasiP07942. baseline and differential.
GenevisibleiP07942. HS.

Family and domain databases

InterProiIPR000742. EGF-like_dom.
IPR002049. Laminin_EGF.
IPR013015. Laminin_IV_B.
IPR008211. Laminin_N.
IPR009053. Prefoldin.
[Graphical view]
PfamiPF00053. Laminin_EGF. 13 hits.
PF00055. Laminin_N. 1 hit.
[Graphical view]
SMARTiSM00181. EGF. 8 hits.
SM00180. EGF_Lam. 13 hits.
SM00136. LamNT. 1 hit.
[Graphical view]
SUPFAMiSSF46579. SSF46579. 1 hit.
PROSITEiPS00022. EGF_1. 9 hits.
PS01186. EGF_2. 2 hits.
PS01248. EGF_LAM_1. 11 hits.
PS50027. EGF_LAM_2. 13 hits.
PS51116. LAMININ_IVB. 1 hit.
PS51117. LAMININ_NTER. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiLAMB1_HUMAN
AccessioniPrimary (citable) accession number: P07942
Secondary accession number(s): Q14D91
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1988
Last sequence update: January 11, 2011
Last modified: November 30, 2016
This is version 176 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 7
    Human chromosome 7: 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.