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P02469

- LAMB1_MOUSE

UniProt

P02469 - LAMB1_MOUSE

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Protein

Laminin subunit beta-1

Gene

Lamb1

Organism
Mus musculus (Mouse)
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. Involved in the organization of the laminar architecture of the cerebral cortex (By similarity). 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 (By similarity). 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 (By similarity).By similarity

GO - Molecular functioni

  1. enzyme binding Source: MGI
  2. extracellular matrix structural constituent Source: HGNC
  3. glycosphingolipid binding Source: MGI
  4. integrin binding Source: MGI

GO - Biological processi

  1. cell adhesion Source: UniProtKB-KW
  2. cell migration Source: MGI
  3. embryo implantation Source: MGI
  4. learning or memory Source: UniProtKB
  5. negative regulation of cell adhesion Source: UniProtKB
  6. neuron projection development Source: HGNC
  7. odontogenesis Source: HGNC
  8. positive regulation of cell migration Source: HGNC
Complete GO annotation...

Keywords - Biological processi

Cell adhesion

Enzyme and pathway databases

ReactomeiREACT_196606. ECM proteoglycans.
REACT_196607. Non-integrin membrane-ECM interactions.
REACT_199052. Degradation of the extracellular matrix.
REACT_202342. Laminin interactions.
REACT_219680. 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
Synonyms:Lamb-1, Lamb1-1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 12

Organism-specific databases

MGIiMGI:96743. Lamb1.

Subcellular locationi

GO - Cellular componenti

  1. basal lamina Source: MGI
  2. basement membrane Source: UniProtKB
  3. extracellular region Source: Reactome
  4. laminin-10 complex Source: HGNC
  5. laminin-1 complex Source: HGNC
  6. laminin-2 complex Source: HGNC
  7. laminin-8 complex Source: HGNC
  8. laminin complex Source: MGI
  9. perinuclear region of cytoplasm Source: UniProtKB
  10. proteinaceous extracellular matrix Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Basement membrane, Extracellular matrix, Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2121Add
BLAST
Chaini22 – 17861765Laminin subunit beta-1PRO_0000017066Add
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...)1 Publication
Glycosylationi1336 – 13361N-linked (GlcNAc...)1 Publication
Glycosylationi1343 – 13431N-linked (GlcNAc...)1 Publication
Glycosylationi1487 – 14871N-linked (GlcNAc...)Sequence Analysis
Glycosylationi1542 – 15421N-linked (GlcNAc...)Sequence Analysis
Glycosylationi1643 – 16431N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi1785 – 1785InterchainCurated

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

MaxQBiP02469.
PaxDbiP02469.
PRIDEiP02469.

PTM databases

PhosphoSiteiP02469.

Expressioni

Tissue specificityi

Widely expressed in the embryo. High levels are detected in the cerebellar basement membrane, at postnatal day 7.1 Publication

Gene expression databases

BgeeiP02469.
CleanExiMM_LAMB1-1.
ExpressionAtlasiP02469. baseline and differential.
GenevestigatoriP02469.

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).

Binary interactionsi

WithEntry#Exp.IntActNotes
AGRNP316962EBI-6662997,EBI-457650From a different organism.
Lamc1P024684EBI-6662997,EBI-7059830

Protein-protein interaction databases

IntActiP02469. 6 interactions.
MINTiMINT-1206337.

Structurei

Secondary structure

1
1786
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi30 – 323
Beta strandi40 – 434
Helixi47 – 493
Beta strandi58 – 603
Beta strandi62 – 676
Beta strandi69 – 724
Beta strandi74 – 796
Turni87 – 893
Helixi96 – 983
Beta strandi122 – 14221
Beta strandi146 – 15510
Beta strandi161 – 1699
Turni170 – 1723
Beta strandi173 – 1775
Turni200 – 2023
Beta strandi204 – 2107
Beta strandi212 – 2143
Helixi222 – 2287
Beta strandi229 – 23911
Helixi252 – 2554
Beta strandi261 – 27010
Beta strandi304 – 3096
Beta strandi342 – 3465
Helixi348 – 3536
Beta strandi360 – 3645
Beta strandi369 – 3713
Beta strandi381 – 3833
Beta strandi385 – 3873
Beta strandi395 – 3973
Turni402 – 4043
Helixi407 – 4093
Helixi417 – 4193
Turni434 – 4374
Beta strandi454 – 4574
Turni462 – 4643
Turni474 – 4763
Turni488 – 4903

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4AQSX-ray3.11A22-542[»]
ProteinModelPortaliP02469.
SMRiP02469. 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 coili1368 – 138821Sequence AnalysisAdd
BLAST
Coiled coili1448 – 1778331Sequence AnalysisAdd
BLAST

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.
GeneTreeiENSGT00760000118860.
HOVERGENiHBG052301.
InParanoidiP02469.
KOiK05636.
OrthoDBiEOG75XGK0.

Family and domain databases

InterProiIPR002049. EGF_laminin.
IPR013015. Laminin_IV.
IPR008211. Laminin_N.
[Graphical view]
PfamiPF00053. Laminin_EGF. 13 hits.
PF00055. Laminin_N. 1 hit.
[Graphical view]
SMARTiSM00180. EGF_Lam. 13 hits.
SM00136. LamNT. 1 hit.
[Graphical view]
PROSITEiPS00022. EGF_1. 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.

P02469-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MGLLQVFAFG VLALWGTRVC AQEPEFSYGC AEGSCYPATG DLLIGRAQKL
60 70 80 90 100
SVTSTCGLHK PEPYCIVSHL QEDKKCFICD SRDPYHETLN PDSHLIENVV
110 120 130 140 150
TTFAPNRLKI WWQSENGVEN VTIQLDLEAE FHFTHLIMTF KTFRPAAMLI
160 170 180 190 200
ERSSDFGKAW GVYRYFAYDC ESSFPGISTG PMKKVDDIIC DSRYSDIEPS
210 220 230 240 250
TEGEVIFRAL DPAFKIEDPY SPRIQNLLKI TNLRIKFVKL HTLGDNLLDS
260 270 280 290 300
RMEIREKYYY AVYDMVVRGN CFCYGHASEC APVDGVNEEV EGMVHGHCMC
310 320 330 340 350
RHNTKGLNCE LCMDFYHDLP WRPAEGRNSN ACKKCNCNEH SSSCHFDMAV
360 370 380 390 400
FLATGNVSGG VCDNCQHNTM GRNCEQCKPF YFQHPERDIR DPNLCEPCTC
410 420 430 440 450
DPAGSENGGI CDGYTDFSVG LIAGQCRCKL HVEGERCDVC KEGFYDLSAE
460 470 480 490 500
DPYGCKSCAC NPLGTIPGGN PCDSETGYCY CKRLVTGQRC DQCLPQHWGL
510 520 530 540 550
SNDLDGCRPC DCDLGGALNN SCSEDSGQCS CLPHMIGRQC NEVESGYYFT
560 570 580 590 600
TLDHYIYEAE EANLGPGVIV VERQYIQDRI PSWTGPGFVR VPEGAYLEFF
610 620 630 640 650
IDNIPYSMEY EILIRYEPQL PDHWEKAVIT VQRPGKIPAS SRCGNTVPDD
660 670 680 690 700
DNQVVSLSPG SRYVVLPRPV CFEKGMNYTV RLELPQYTAS GSDVESPYTF
710 720 730 740 750
IDSLVLMPYC KSLDIFTVGG SGDGEVTNSA WETFQRYRCL ENSRSVVKTP
760 770 780 790 800
MTDVCRNIIF SISALIHQTG LACECDPQGS LSSVCDPNGG QCQCRPNVVG
810 820 830 840 850
RTCNRCAPGT FGFGPNGCKP CDCHLQGSAS AFCDAITGQC HCFQGIYARQ
860 870 880 890 900
CDRCLPGYWG FPSCQPCQCN GHALDCDTVT GECLSCQDYT TGHNCERCLA
910 920 930 940 950
GYYGDPIIGS GDHCRPCPCP DGPDSGRQFA RSCYQDPVTL QLACVCDPGY
960 970 980 990 1000
IGSRCDDCAS GFFGNPSDFG GSCQPCQCHH NIDTTDPEAC DKETGRCLKC
1010 1020 1030 1040 1050
LYHTEGDHCQ LCQYGYYGDA LRQDCRKCVC NYLGTVKEHC NGSDCHCDKA
1060 1070 1080 1090 1100
TGQCSCLPNV IGQNCDRCAP NTWQLASGTG CGPCNCNAAH SFGPSCNEFT
1110 1120 1130 1140 1150
GQCQCMPGFG GRTCSECQEL FWGDPDVECR ACDCDPRGIE TPQCDQSTGQ
1160 1170 1180 1190 1200
CVCVEGVEGP RCDKCTRGYS GVFPDCTPCH QCFALWDAII GELTNRTHKF
1210 1220 1230 1240 1250
LEKAKALKIS GVIGPYRETV DSVEKKVNEI KDILAQSPAA EPLKNIGILF
1260 1270 1280 1290 1300
EEAEKLTKDV TEKMAQVEVK LTDTASQSNS TAGELGALQA EAESLDKTVK
1310 1320 1330 1340 1350
ELAEQLEFIK NSDIQGALDS ITKYFQMSLE AEKRVNASTT DPNSTVEQSA
1360 1370 1380 1390 1400
LTRDRVEDLM LERESPFKEQ QEEQARLLDE LAGKLQSLDL SAVAQMTCGT
1410 1420 1430 1440 1450
PPGADCSESE CGGPNCRTDE GEKKCGGPGC GGLVTVAHSA WQKAMDFDRD
1460 1470 1480 1490 1500
VLSALAEVEQ LSKMVSEAKV RADEAKQNAQ DVLLKTNATK EKVDKSNEDL
1510 1520 1530 1540 1550
RNLIKQIRNF LTEDSADLDS IEAVANEVLK MEMPSTPQQL QNLTEDIRER
1560 1570 1580 1590 1600
VETLSQVEVI LQQSAADIAR AELLLEEAKR ASKSATDVKV TADMVKEALE
1610 1620 1630 1640 1650
EAEKAQVAAE KAIKQADEDI QGTQNLLTSI ESETAASEET LTNASQRISK
1660 1670 1680 1690 1700
LERNVEELKR KAAQNSGEAE YIEKVVYSVK QNADDVKKTL DGELDEKYKK
1710 1720 1730 1740 1750
VESLIAQKTE ESADARRKAE LLQNEAKTLL AQANSKLQLL EDLERKYEDN
1760 1770 1780
QKYLEDKAQE LVRLEGEVRS LLKDISEKVA VYSTCL
Length:1,786
Mass (Da):197,090
Last modified:July 27, 2011 - v3
Checksum:iE7F258170C3626DD
GO

Sequence cautioni

The sequence AAA39407.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti159 – 1591A → T in AAA39407. (PubMed:3493487)Curated
Sequence conflicti569 – 5691I → V in AAA39407. (PubMed:3493487)Curated
Sequence conflicti993 – 9931E → D in AAA39407. (PubMed:3493487)Curated
Sequence conflicti1393 – 13931V → A in AAA39407. (PubMed:3493487)Curated
Sequence conflicti1393 – 13931V → A in CAA28839. (PubMed:6209134)Curated
Sequence conflicti1531 – 15344MEMP → SGNA in AAA39407. (PubMed:3493487)Curated
Sequence conflicti1692 – 16921G → C in CAA28839. (PubMed:6209134)Curated
Sequence conflicti1749 – 17491D → N in CAA28839. (PubMed:6209134)Curated

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M15525 mRNA. Translation: AAA39407.1. Different initiation.
CR974423 Genomic DNA. No translation available.
CT571245 Genomic DNA. No translation available.
X05212 mRNA. Translation: CAA28839.1.
PIRiA26413. MMMSB1.
RefSeqiXP_006515056.1. XM_006514993.1.
UniGeneiMm.172674.

Genome annotation databases

EnsembliENSMUST00000169088; ENSMUSP00000132778; ENSMUSG00000002900.
GeneIDi16777.
KEGGimmu:16777.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M15525 mRNA. Translation: AAA39407.1 . Different initiation.
CR974423 Genomic DNA. No translation available.
CT571245 Genomic DNA. No translation available.
X05212 mRNA. Translation: CAA28839.1 .
PIRi A26413. MMMSB1.
RefSeqi XP_006515056.1. XM_006514993.1.
UniGenei Mm.172674.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
4AQS X-ray 3.11 A 22-542 [» ]
ProteinModelPortali P02469.
SMRi P02469. Positions 29-492.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

IntActi P02469. 6 interactions.
MINTi MINT-1206337.

PTM databases

PhosphoSitei P02469.

Proteomic databases

MaxQBi P02469.
PaxDbi P02469.
PRIDEi P02469.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000169088 ; ENSMUSP00000132778 ; ENSMUSG00000002900 .
GeneIDi 16777.
KEGGi mmu:16777.

Organism-specific databases

CTDi 3912.
MGIi MGI:96743. Lamb1.

Phylogenomic databases

eggNOGi NOG241384.
GeneTreei ENSGT00760000118860.
HOVERGENi HBG052301.
InParanoidi P02469.
KOi K05636.
OrthoDBi EOG75XGK0.

Enzyme and pathway databases

Reactomei REACT_196606. ECM proteoglycans.
REACT_196607. Non-integrin membrane-ECM interactions.
REACT_199052. Degradation of the extracellular matrix.
REACT_202342. Laminin interactions.
REACT_219680. L1CAM interactions.

Miscellaneous databases

ChiTaRSi LAMB1. mouse.
PROi P02469.
SOURCEi Search...

Gene expression databases

Bgeei P02469.
CleanExi MM_LAMB1-1.
ExpressionAtlasi P02469. baseline and differential.
Genevestigatori P02469.

Family and domain databases

InterProi IPR002049. EGF_laminin.
IPR013015. Laminin_IV.
IPR008211. Laminin_N.
[Graphical view ]
Pfami PF00053. Laminin_EGF. 13 hits.
PF00055. Laminin_N. 1 hit.
[Graphical view ]
SMARTi SM00180. EGF_Lam. 13 hits.
SM00136. LamNT. 1 hit.
[Graphical view ]
PROSITEi PS00022. EGF_1. 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 ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Sequence of the cDNA encoding the laminin B1 chain reveals a multidomain protein containing cysteine-rich repeats."
    Sasaki M., Kato S., Kohno K., Martin G.R., Yamada Y.
    Proc. Natl. Acad. Sci. U.S.A. 84:935-939(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6J.
  3. "Sequencing of laminin B chain cDNAs reveals C-terminal regions of coiled-coil alpha-helix."
    Barlow D.P., Green N.M., Kurkinen M., Hogan B.L.M.
    EMBO J. 3:2355-2362(1984) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1292-1786.
  4. "Cloning of the mouse laminin alpha 4 cDNA. Expression in a subset of endothelium."
    Frieser M., Noeckel H., Pausch F., Roeder C., Hahn A., Deutzmann R., Sorokin L.M.
    Eur. J. Biochem. 246:727-735(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 165-172; 539-547 AND 712-719.
    Strain: BALB/c.
    Tissue: Endothelial cell.
  5. "Mass-spectrometric identification and relative quantification of N-linked cell surface glycoproteins."
    Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M., Schiess R., Aebersold R., Watts J.D.
    Nat. Biotechnol. 27:378-386(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-1279; ASN-1336 AND ASN-1343.
  6. Cited for: TISSUE SPECIFICITY.

Entry informationi

Entry nameiLAMB1_MOUSE
AccessioniPrimary (citable) accession number: P02469
Secondary accession number(s): E9PXZ9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 27, 2011
Last modified: October 29, 2014
This is version 141 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3