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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
  • glycosphingolipid binding Source: Ensembl
  • structural molecule activity Source: UniProtKB

GO - Biological processi

  • axon guidance Source: Reactome
  • cell adhesion Source: HGNC
  • embryo implantation Source: Ensembl
  • endodermal cell differentiation Source: UniProtKB
  • extracellular matrix disassembly Source: Reactome
  • extracellular matrix organization Source: Reactome
  • negative regulation of cell adhesion Source: Ensembl
  • 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

ReactomeiREACT_118572. Degradation of the extracellular matrix.
REACT_163874. Non-integrin membrane-ECM interactions.
REACT_163906. ECM proteoglycans.
REACT_169262. Laminin interactions.
REACT_22205. L1CAM interactions.

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
ProteomesiUP000005640 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

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

Polymorphism and mutation databases

BioMutaiLAMB1.
DMDMi317373377.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2121Add
BLAST
Chaini22 – 17861765Laminin subunit beta-1PRO_0000017065Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi120 – 1201N-linked (GlcNAc...)Sequence Analysis
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
Glycosylationi356 – 3561N-linked (GlcNAc...)Sequence Analysis
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
Glycosylationi519 – 5191N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi531 ↔ 540PROSITE-ProRule annotation
Glycosylationi677 – 6771N-linked (GlcNAc...)Sequence Analysis
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
Glycosylationi1041 – 10411N-linked (GlcNAc...)Sequence Analysis
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 bondi1179 – 1179InterchainCurated
Disulfide bondi1182 – 1182InterchainCurated
Glycosylationi1195 – 11951N-linked (GlcNAc...)Sequence Analysis
Glycosylationi1279 – 12791N-linked (GlcNAc...)2 Publications
Glycosylationi1336 – 13361N-linked (GlcNAc...)Sequence Analysis
Glycosylationi1343 – 13431N-linked (GlcNAc...)Sequence Analysis
Glycosylationi1487 – 14871N-linked (GlcNAc...)Sequence Analysis
Glycosylationi1542 – 15421N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi1785 – 1785InterchainCurated

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

MaxQBiP07942.
PaxDbiP07942.
PRIDEiP07942.

PTM databases

PhosphoSiteiP07942.

Expressioni

Gene expression databases

BgeeiP07942.
CleanExiHS_LAMB1.
ExpressionAtlasiP07942. baseline and differential.
GenevestigatoriP07942.

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. 31 interactions.
IntActiP07942. 11 interactions.
MINTiMINT-2860329.
STRINGi9606.ENSP00000222399.

Structurei

3D structure databases

ProteinModelPortaliP07942.
SMRiP07942. Positions 29-492.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini31 – 270240Laminin N-terminalPROSITE-ProRule annotationAdd
BLAST
Domaini271 – 33464Laminin EGF-like 1PROSITE-ProRule annotationAdd
BLAST
Domaini335 – 39763Laminin EGF-like 2PROSITE-ProRule annotationAdd
BLAST
Domaini398 – 45760Laminin EGF-like 3PROSITE-ProRule annotationAdd
BLAST
Domaini458 – 50952Laminin EGF-like 4PROSITE-ProRule annotationAdd
BLAST
Domaini510 – 54031Laminin EGF-like 5; truncatedPROSITE-ProRule annotationAdd
BLAST
Domaini549 – 767219Laminin IV type BPROSITE-ProRule annotationAdd
BLAST
Domaini773 – 82048Laminin EGF-like 6PROSITE-ProRule annotationAdd
BLAST
Domaini821 – 86646Laminin EGF-like 7PROSITE-ProRule annotationAdd
BLAST
Domaini867 – 91650Laminin EGF-like 8PROSITE-ProRule annotationAdd
BLAST
Domaini917 – 97559Laminin EGF-like 9PROSITE-ProRule annotationAdd
BLAST
Domaini976 – 102752Laminin EGF-like 10PROSITE-ProRule annotationAdd
BLAST
Domaini1028 – 108356Laminin EGF-like 11PROSITE-ProRule annotationAdd
BLAST
Domaini1084 – 113148Laminin EGF-like 12PROSITE-ProRule annotationAdd
BLAST
Domaini1132 – 117847Laminin EGF-like 13PROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1179 – 1397219Domain IIAdd
BLAST
Regioni1398 – 143033Domain alphaAdd
BLAST
Regioni1431 – 1786356Domain IAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili1216 – 1315100Sequence AnalysisAdd
BLAST
Coiled coili1353 – 138836Sequence AnalysisAdd
BLAST
Coiled coili1442 – 1781340Sequence 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.
GeneTreeiENSGT00780000121851.
HOGENOMiHOG000007552.
HOVERGENiHBG052301.
InParanoidiP07942.
KOiK05636.
PhylomeDBiP07942.
TreeFamiTF312903.

Family and domain databases

InterProiIPR002049. EGF_laminin.
IPR013015. Laminin_IV.
IPR008211. Laminin_N.
IPR009053. Prefoldin.
[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]
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)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti1470 – 14701L → V in AAA59487 (PubMed:3661559).Curated
Sequence conflicti1696 – 16961E → G in AAA59487 (PubMed:3661559).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti379 – 3791P → S.
Corresponds to variant rs28750165 [ dbSNP | Ensembl ].
VAR_061349
Natural varianti670 – 6701V → A.
Corresponds to variant rs20555 [ dbSNP | Ensembl ].
VAR_014698
Natural varianti860 – 8601G → S.
Corresponds to variant rs35710474 [ dbSNP | Ensembl ].
VAR_032774
Natural varianti1022 – 10221Q → R.3 Publications
Corresponds to variant rs20556 [ dbSNP | Ensembl ].
VAR_014699

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.2. 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. Positions 29-492.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi110106. 31 interactions.
IntActiP07942. 11 interactions.
MINTiMINT-2860329.
STRINGi9606.ENSP00000222399.

Chemistry

ChEMBLiCHEMBL2364187.

PTM databases

PhosphoSiteiP07942.

Polymorphism and mutation databases

BioMutaiLAMB1.
DMDMi317373377.

Proteomic databases

MaxQBiP07942.
PaxDbiP07942.
PRIDEiP07942.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000222399; ENSP00000222399; ENSG00000091136.
GeneIDi3912.
KEGGihsa:3912.
UCSCiuc003vew.2. human.

Organism-specific databases

CTDi3912.
GeneCardsiGC07M107564.
H-InvDBHIX0025323.
HGNCiHGNC:6486. LAMB1.
HPAiCAB004256.
HPA004056.
HPA004132.
MIMi150240. gene.
615191. phenotype.
neXtProtiNX_P07942.
Orphaneti352682. Cobblestone lissencephaly without muscular or ocular involvement.
PharmGKBiPA30275.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG241384.
GeneTreeiENSGT00780000121851.
HOGENOMiHOG000007552.
HOVERGENiHBG052301.
InParanoidiP07942.
KOiK05636.
PhylomeDBiP07942.
TreeFamiTF312903.

Enzyme and pathway databases

ReactomeiREACT_118572. Degradation of the extracellular matrix.
REACT_163874. Non-integrin membrane-ECM interactions.
REACT_163906. ECM proteoglycans.
REACT_169262. Laminin interactions.
REACT_22205. L1CAM interactions.

Miscellaneous databases

ChiTaRSiLAMB1. human.
GeneWikiiLaminin,_beta_1.
GenomeRNAii3912.
NextBioi15367.
PROiP07942.
SOURCEiSearch...

Gene expression databases

BgeeiP07942.
CleanExiHS_LAMB1.
ExpressionAtlasiP07942. baseline and differential.
GenevestigatoriP07942.

Family and domain databases

InterProiIPR002049. EGF_laminin.
IPR013015. Laminin_IV.
IPR008211. Laminin_N.
IPR009053. Prefoldin.
[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]
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...

Publicationsi

« Hide 'large scale' publications
  1. "Structure of the human laminin B1 chain gene."
    Vuolteenaho R., Chow L.T., Tryggvason K.
    J. Biol. Chem. 265:15611-15616(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT ARG-1022.
  2. "Human laminin B1 chain. A multidomain protein with gene (LAMB1) locus in the q22 region of chromosome 7."
    Pikkarainen T., Eddy R., Fukushima Y., Byers M., Shows T., Pihlajaniemi T., Saraste M., Tryggvason K.
    J. Biol. Chem. 262:10454-10462(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT ARG-1022.
  3. "Human chromosome 7: DNA sequence and biology."
    Scherer S.W., Cheung J., MacDonald J.R., Osborne L.R., Nakabayashi K., Herbrick J.-A., Carson A.R., Parker-Katiraee L., Skaug J., Khaja R., Zhang J., Hudek A.K., Li M., Haddad M., Duggan G.E., Fernandez B.A., Kanematsu E., Gentles S.
    , Christopoulos C.C., Choufani S., Kwasnicka D., Zheng X.H., Lai Z., Nusskern D.R., Zhang Q., Gu Z., Lu F., Zeesman S., Nowaczyk M.J., Teshima I., Chitayat D., Shuman C., Weksberg R., Zackai E.H., Grebe T.A., Cox S.R., Kirkpatrick S.J., Rahman N., Friedman J.M., Heng H.H.Q., Pelicci P.G., Lo-Coco F., Belloni E., Shaffer L.G., Pober B., Morton C.C., Gusella J.F., Bruns G.A.P., Korf B.R., Quade B.J., Ligon A.H., Ferguson H., Higgins A.W., Leach N.T., Herrick S.R., Lemyre E., Farra C.G., Kim H.-G., Summers A.M., Gripp K.W., Roberts W., Szatmari P., Winsor E.J.T., Grzeschik K.-H., Teebi A., Minassian B.A., Kere J., Armengol L., Pujana M.A., Estivill X., Wilson M.D., Koop B.F., Tosi S., Moore G.E., Boright A.P., Zlotorynski E., Kerem B., Kroisel P.M., Petek E., Oscier D.G., Mould S.J., Doehner H., Doehner K., Rommens J.M., Vincent J.B., Venter J.C., Li P.W., Mural R.J., Adams M.D., Tsui L.-C.
    Science 300:767-772(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. "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: Colon.
  5. "Isolation of a cDNA clone for the human laminin-B1 chain and its gene localization."
    Jaye M., Modi W.S., Ricca G.A., Mudd R., Chiu I.M., O'Brien S.J., Drohan W.N.
    Am. J. Hum. Genet. 41:605-615(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1276-1709.
  6. "Human plasma N-glycoproteome analysis by immunoaffinity subtraction, hydrazide chemistry, and mass spectrometry."
    Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E., Moore R.J., Smith R.D.
    J. Proteome Res. 4:2070-2080(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-1279.
    Tissue: Plasma.
  7. "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-1279.
    Tissue: Liver.
  8. Cited for: INVOLVEMENT IN LIS5, FUNCTION.
  9. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  10. Cited for: VARIANT [LARGE SCALE ANALYSIS] ARG-1022, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

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: May 27, 2015
This is version 160 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

External Data

Dasty 3

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 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.