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UniProtKB - P02469 (LAMB1_MOUSE)

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Protein

Laminin subunit beta-1

Gene

Lamb1

Organism
Mus musculus (Mouse)
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 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

  • enzyme binding Source: MGI
  • extracellular matrix structural constituent Source: HGNC
  • glycosphingolipid binding Source: MGI
  • integrin binding Source: MGI
Complete GO annotation...

GO - Biological processi

  • axon guidance Source: Reactome
  • cell migration Source: MGI
  • embryo implantation Source: MGI
  • extracellular matrix disassembly Source: Reactome
  • extracellular matrix organization Source: Reactome
  • learning or memory Source: UniProtKB
  • negative regulation of cell adhesion Source: UniProtKB
  • neuronal-glial interaction involved in cerebral cortex radial glia guided migration Source: MGI
  • neuron projection development Source: MGI
  • odontogenesis Source: HGNC
  • positive regulation of cell migration Source: HGNC
  • substrate adhesion-dependent cell spreading Source: MGI
Complete GO annotation...

Keywordsi

Biological processCell adhesion

Enzyme and pathway databases

ReactomeiR-MMU-1474228. Degradation of the extracellular matrix.
R-MMU-3000157. Laminin interactions.
R-MMU-3000171. Non-integrin membrane-ECM interactions.
R-MMU-3000471. Scavenging by Class B Receptors.
R-MMU-373760. L1CAM interactions.
R-MMU-381426. Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs).
R-MMU-8874081. MET activates PTK2 signaling.
R-MMU-8957275. Post-translational protein phosphorylation.

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 lineageiEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Myomorpha › Muroidea › Muridae › Murinae › Mus › Mus
Proteomesi
  • UP000000589 Componenti: Chromosome 12

Organism-specific databases

MGIiMGI:96743. Lamb1.

Subcellular locationi

GO - Cellular componenti

  • basal lamina Source: MGI
  • basement membrane Source: UniProtKB
  • extracellular exosome Source: MGI
  • extracellular matrix Source: MGI
  • extracellular region Source: Reactome
  • extracellular space Source: BHF-UCL
  • laminin-10 complex Source: MGI
  • laminin-1 complex Source: MGI
  • laminin-2 complex Source: HGNC
  • laminin-8 complex Source: HGNC
  • laminin complex Source: MGI
  • nucleus Source: MGI
  • perinuclear region of cytoplasm Source: UniProtKB
  • proteinaceous extracellular matrix Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Basement membrane, Extracellular matrix, Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 21Add BLAST21
ChainiPRO_000001706622 – 1786Laminin subunit beta-1Add BLAST1765

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi120N-linked (GlcNAc...) asparagineSequence analysis1
Modified residuei250PhosphoserineCombined sources1
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...) asparagineSequence 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...) asparagineSequence analysis1
Disulfide bondi531 ↔ 540PROSITE-ProRule annotation
Glycosylationi677N-linked (GlcNAc...) asparagineSequence 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...) asparagineSequence 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...) asparagineSequence analysis1
Glycosylationi1279N-linked (GlcNAc...) asparagine1 Publication1
Glycosylationi1336N-linked (GlcNAc...) asparagine1 Publication1
Glycosylationi1343N-linked (GlcNAc...) asparagine1 Publication1
Glycosylationi1487N-linked (GlcNAc...) asparagineSequence analysis1
Modified residuei1496PhosphoserineBy similarity1
Glycosylationi1542N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi1643N-linked (GlcNAc...) asparagineSequence analysis1
Modified residuei1666PhosphoserineBy similarity1
Disulfide bondi1785InterchainCurated

Keywords - PTMi

Disulfide bond, Glycoprotein, Phosphoprotein

Proteomic databases

MaxQBiP02469.
PaxDbiP02469.
PeptideAtlasiP02469.
PRIDEiP02469.

PTM databases

iPTMnetiP02469.
PhosphoSitePlusiP02469.

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

BgeeiENSMUSG00000002900.
CleanExiMM_LAMB1-1.
ExpressionAtlasiP02469. baseline and differential.
GenevisibleiP02469. MM.

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

Show more details

GO - Molecular functioni

  • enzyme binding Source: MGI
  • integrin binding Source: MGI
Complete GO annotation...

Protein-protein interaction databases

BioGridi201101. 4 interactors.
IntActiP02469. 7 interactors.
MINTiMINT-1206337.
STRINGi10090.ENSMUSP00000002979.

Structurei

Secondary structure

11786
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi30 – 32Combined sources3
Beta strandi40 – 43Combined sources4
Helixi47 – 49Combined sources3
Beta strandi58 – 60Combined sources3
Beta strandi62 – 67Combined sources6
Beta strandi69 – 72Combined sources4
Beta strandi74 – 79Combined sources6
Turni87 – 89Combined sources3
Helixi96 – 98Combined sources3
Beta strandi122 – 142Combined sources21
Beta strandi146 – 155Combined sources10
Beta strandi161 – 169Combined sources9
Turni170 – 172Combined sources3
Beta strandi173 – 177Combined sources5
Turni200 – 202Combined sources3
Beta strandi204 – 210Combined sources7
Beta strandi212 – 214Combined sources3
Helixi222 – 228Combined sources7
Beta strandi229 – 239Combined sources11
Helixi252 – 255Combined sources4
Beta strandi261 – 270Combined sources10
Beta strandi304 – 309Combined sources6
Beta strandi342 – 346Combined sources5
Helixi348 – 353Combined sources6
Beta strandi360 – 364Combined sources5
Beta strandi369 – 371Combined sources3
Beta strandi381 – 383Combined sources3
Beta strandi385 – 387Combined sources3
Beta strandi395 – 397Combined sources3
Turni402 – 404Combined sources3
Helixi407 – 409Combined sources3
Helixi417 – 419Combined sources3
Turni434 – 437Combined sources4
Beta strandi454 – 457Combined sources4
Turni462 – 464Combined sources3
Turni474 – 476Combined sources3
Turni488 – 490Combined sources3
Helixi1739 – 1784Combined sources46

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4AQSX-ray3.11A22-542[»]
5MC9X-ray2.13B1735-1786[»]
ProteinModelPortaliP02469.
SMRiP02469.
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 coili1368 – 1388Sequence analysisAdd BLAST21
Coiled coili1448 – 1778Sequence analysisAdd BLAST331

Keywords - Domaini

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

Phylogenomic databases

eggNOGiKOG0994. Eukaryota.
ENOG410XPEG. LUCA.
GeneTreeiENSGT00780000121851.
HOVERGENiHBG052301.
InParanoidiP02469.

Family and domain databases

Gene3Di2.60.120.260. 1 hit.
InterProiView protein in InterPro
IPR000742. EGF-like_dom.
IPR008979. Galactose-bd-like.
IPR002049. Laminin_EGF.
IPR013015. Laminin_IV_B.
IPR008211. Laminin_N.
PfamiView protein in Pfam
PF00053. Laminin_EGF. 13 hits.
PF00055. Laminin_N. 1 hit.
SMARTiView protein in SMART
SM00181. EGF. 10 hits.
SM00180. EGF_Lam. 13 hits.
SM00136. LamNT. 1 hit.
PROSITEiView protein in PROSITE
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.

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 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti159A → T in AAA39407 (PubMed:3493487).Curated1
Sequence conflicti569I → V in AAA39407 (PubMed:3493487).Curated1
Sequence conflicti993E → D in AAA39407 (PubMed:3493487).Curated1
Sequence conflicti1393V → A in AAA39407 (PubMed:3493487).Curated1
Sequence conflicti1393V → A in CAA28839 (PubMed:6209134).Curated1
Sequence conflicti1531 – 1534MEMP → SGNA in AAA39407 (PubMed:3493487).Curated4
Sequence conflicti1692G → C in CAA28839 (PubMed:6209134).Curated1
Sequence conflicti1749D → N in CAA28839 (PubMed:6209134).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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_006515055.2. XM_006514992.3.
XP_006515056.1. XM_006514993.1.
UniGeneiMm.172674.

Genome annotation databases

EnsembliENSMUST00000169088; ENSMUSP00000132778; ENSMUSG00000002900.
GeneIDi16777.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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_006515055.2. XM_006514992.3.
XP_006515056.1. XM_006514993.1.
UniGeneiMm.172674.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4AQSX-ray3.11A22-542[»]
5MC9X-ray2.13B1735-1786[»]
ProteinModelPortaliP02469.
SMRiP02469.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi201101. 4 interactors.
IntActiP02469. 7 interactors.
MINTiMINT-1206337.
STRINGi10090.ENSMUSP00000002979.

PTM databases

iPTMnetiP02469.
PhosphoSitePlusiP02469.

Proteomic databases

MaxQBiP02469.
PaxDbiP02469.
PeptideAtlasiP02469.
PRIDEiP02469.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000169088; ENSMUSP00000132778; ENSMUSG00000002900.
GeneIDi16777.

Organism-specific databases

CTDi3912.
MGIiMGI:96743. Lamb1.

Phylogenomic databases

eggNOGiKOG0994. Eukaryota.
ENOG410XPEG. LUCA.
GeneTreeiENSGT00780000121851.
HOVERGENiHBG052301.
InParanoidiP02469.

Enzyme and pathway databases

ReactomeiR-MMU-1474228. Degradation of the extracellular matrix.
R-MMU-3000157. Laminin interactions.
R-MMU-3000171. Non-integrin membrane-ECM interactions.
R-MMU-3000471. Scavenging by Class B Receptors.
R-MMU-373760. L1CAM interactions.
R-MMU-381426. Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs).
R-MMU-8874081. MET activates PTK2 signaling.
R-MMU-8957275. Post-translational protein phosphorylation.

Miscellaneous databases

ChiTaRSiLamb1. mouse.
PROiPR:P02469.
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000002900.
CleanExiMM_LAMB1-1.
ExpressionAtlasiP02469. baseline and differential.
GenevisibleiP02469. MM.

Family and domain databases

Gene3Di2.60.120.260. 1 hit.
InterProiView protein in InterPro
IPR000742. EGF-like_dom.
IPR008979. Galactose-bd-like.
IPR002049. Laminin_EGF.
IPR013015. Laminin_IV_B.
IPR008211. Laminin_N.
PfamiView protein in Pfam
PF00053. Laminin_EGF. 13 hits.
PF00055. Laminin_N. 1 hit.
SMARTiView protein in SMART
SM00181. EGF. 10 hits.
SM00180. EGF_Lam. 13 hits.
SM00136. LamNT. 1 hit.
PROSITEiView protein in PROSITE
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.
ProtoNetiSearch...

Entry informationi

Entry nameiLAMB1_MOUSE
AccessioniPrimary (citable) accession number: P02469
Secondary accession number(s): E9PXZ9
Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 27, 2011
Last modified: June 7, 2017
This is version 165 of the entry and version 3 of the sequence. See 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

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.