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P02468

- LAMC1_MOUSE

UniProt

P02468 - LAMC1_MOUSE

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Protein

Laminin subunit gamma-1

Gene

Lamc1

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.

GO - Molecular functioni

  1. extracellular matrix structural constituent Source: HGNC
  2. glycosphingolipid binding Source: MGI

GO - Biological processi

  1. cell adhesion Source: HGNC
  2. cell migration Source: HGNC
  3. extracellular matrix disassembly Source: HGNC
  4. hemidesmosome assembly Source: HGNC
  5. neuron projection development Source: MGI
  6. protein complex assembly Source: HGNC
Complete GO annotation...

Keywords - Biological processi

Cell adhesion

Enzyme and pathway databases

ReactomeiREACT_196607. Non-integrin membrane-ECM interactions.
REACT_202342. Laminin interactions.
REACT_219680. L1CAM interactions.

Names & Taxonomyi

Protein namesi
Recommended name:
Laminin subunit gamma-1
Alternative name(s):
Laminin B2 chain
Laminin-1 subunit gamma
Laminin-10 subunit gamma
Laminin-11 subunit gamma
Laminin-2 subunit gamma
Laminin-3 subunit gamma
Laminin-4 subunit gamma
Laminin-6 subunit gamma
Laminin-7 subunit gamma
Laminin-8 subunit gamma
Laminin-9 subunit gamma
S-laminin subunit gamma
Short name:
S-LAM gamma
Gene namesi
Name:Lamc1
Synonyms:Lamb-2, Lamc-1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Unplaced

Organism-specific databases

MGIiMGI:99914. Lamc1.

Subcellular locationi

GO - Cellular componenti

  1. basal lamina Source: MGI
  2. basement membrane Source: HGNC
  3. extracellular region Source: Reactome
  4. laminin-10 complex 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 – 3333Add
BLAST
Chaini34 – 16071574Laminin subunit gamma-1PRO_0000017075Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi58 – 581N-linked (GlcNAc...)Sequence Analysis
Glycosylationi132 – 1321N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi284 ↔ 293PROSITE-ProRule annotation
Disulfide bondi286 ↔ 303PROSITE-ProRule annotation
Disulfide bondi305 ↔ 314PROSITE-ProRule annotation
Disulfide bondi340 ↔ 349PROSITE-ProRule annotation
Disulfide bondi342 ↔ 365PROSITE-ProRule annotation
Disulfide bondi368 ↔ 377PROSITE-ProRule annotation
Disulfide bondi380 ↔ 393PROSITE-ProRule annotation
Disulfide bondi396 ↔ 408PROSITE-ProRule annotation
Disulfide bondi398 ↔ 414PROSITE-ProRule annotation
Disulfide bondi416 ↔ 425PROSITE-ProRule annotation
Disulfide bondi428 ↔ 440PROSITE-ProRule annotation
Disulfide bondi443 ↔ 454PROSITE-ProRule annotation
Disulfide bondi445 ↔ 461PROSITE-ProRule annotation
Disulfide bondi463 ↔ 472PROSITE-ProRule annotation
Disulfide bondi475 ↔ 490PROSITE-ProRule annotation
Glycosylationi574 – 5741N-linked (GlcNAc...)Sequence Analysis
Glycosylationi648 – 6481N-linked (GlcNAc...)1 Publication
Disulfide bondi722 ↔ 731PROSITE-ProRule annotation
Disulfide bondi724 ↔ 738PROSITE-ProRule annotation
Disulfide bondi740 ↔ 749PROSITE-ProRule annotation
Disulfide bondi752 ↔ 768PROSITE-ProRule annotation
Disulfide bondi771 ↔ 779
Disulfide bondi773 ↔ 790
Disulfide bondi793 ↔ 802
Disulfide bondi805 ↔ 823
Disulfide bondi826 ↔ 840
Disulfide bondi828 ↔ 847
Disulfide bondi850 ↔ 859
Disulfide bondi862 ↔ 879
Disulfide bondi882 ↔ 896
Disulfide bondi884 ↔ 903
Disulfide bondi905 ↔ 914
Disulfide bondi917 ↔ 930
Disulfide bondi933 ↔ 945PROSITE-ProRule annotation
Disulfide bondi935 ↔ 952PROSITE-ProRule annotation
Disulfide bondi954 ↔ 963PROSITE-ProRule annotation
Disulfide bondi966 ↔ 978PROSITE-ProRule annotation
Disulfide bondi981 ↔ 993PROSITE-ProRule annotation
Disulfide bondi983 ↔ 999PROSITE-ProRule annotation
Disulfide bondi1001 ↔ 1010PROSITE-ProRule annotation
Disulfide bondi1013 ↔ 1026PROSITE-ProRule annotation
Glycosylationi1020 – 10201N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi1029 – 1029InterchainCurated
Disulfide bondi1032 – 1032InterchainCurated
Glycosylationi1105 – 11051N-linked (GlcNAc...)1 Publication
Glycosylationi1159 – 11591N-linked (GlcNAc...)Sequence Analysis
Glycosylationi1173 – 11731N-linked (GlcNAc...)Sequence Analysis
Glycosylationi1203 – 12031N-linked (GlcNAc...)1 Publication
Glycosylationi1221 – 12211N-linked (GlcNAc...)1 Publication
Glycosylationi1239 – 12391N-linked (GlcNAc...)Sequence Analysis
Glycosylationi1378 – 13781N-linked (GlcNAc...)Sequence Analysis
Glycosylationi1393 – 13931N-linked (GlcNAc...)1 Publication
Glycosylationi1437 – 14371N-linked (GlcNAc...)Sequence Analysis
Modified residuei1491 – 14911PhosphoserineBy similarity
Disulfide bondi1598 – 1598Interchain (with beta-1 chain)

Keywords - PTMi

Disulfide bond, Glycoprotein, Phosphoprotein

Proteomic databases

MaxQBiP02468.
PaxDbiP02468.
PRIDEiP02468.

PTM databases

PhosphoSiteiP02468.

Expressioni

Tissue specificityi

Found in the basement membranes (major component).

Gene expression databases

CleanExiMM_LAMC1.
GenevestigatoriP02468.

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. Gamma-1 is a subunit of laminin-1 (laminin-111 or EHS laminin), laminin-2 (laminin-211 or merosin), laminin-3 (laminin-121 or S-laminin), laminin-4 (laminin-221 or S-merosin), laminin-6 (laminin-311 or K-laminin), laminin-7 (laminin-321 or KS-laminin), laminin-8 (laminin-411), laminin-9 (laminin-421), laminin-10 (laminin-511) and laminin-11 (laminin-521).

Binary interactionsi

WithEntry#Exp.IntActNotes
Lamb1P024694EBI-7059830,EBI-6662997
Nid1P104933EBI-7059830,EBI-1032117

Protein-protein interaction databases

DIPiDIP-41793N.
IntActiP02468. 5 interactions.
MINTiMINT-1031545.

Structurei

Secondary structure

1
1607
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Turni55 – 584Combined sources
Beta strandi62 – 643Combined sources
Beta strandi72 – 754Combined sources
Beta strandi87 – 904Combined sources
Beta strandi92 – 943Combined sources
Turni95 – 973Combined sources
Helixi101 – 1044Combined sources
Beta strandi110 – 1123Combined sources
Helixi121 – 1233Combined sources
Beta strandi126 – 1283Combined sources
Beta strandi131 – 15323Combined sources
Beta strandi156 – 16813Combined sources
Beta strandi171 – 1777Combined sources
Helixi180 – 1845Combined sources
Beta strandi202 – 2054Combined sources
Beta strandi212 – 2143Combined sources
Beta strandi216 – 2216Combined sources
Turni222 – 2254Combined sources
Helixi229 – 2346Combined sources
Helixi236 – 2416Combined sources
Beta strandi243 – 25311Combined sources
Helixi259 – 2613Combined sources
Helixi265 – 2684Combined sources
Beta strandi274 – 28411Combined sources
Beta strandi293 – 2953Combined sources
Beta strandi301 – 3033Combined sources
Beta strandi309 – 3113Combined sources
Helixi342 – 3443Combined sources
Beta strandi349 – 3513Combined sources
Helixi353 – 3586Combined sources
Beta strandi363 – 3653Combined sources
Turni369 – 3713Combined sources
Beta strandi372 – 3743Combined sources
Beta strandi382 – 3854Combined sources
Beta strandi779 – 7813Combined sources
Beta strandi783 – 7853Combined sources
Beta strandi788 – 7903Combined sources
Beta strandi797 – 7993Combined sources
Beta strandi809 – 8124Combined sources
Beta strandi816 – 8194Combined sources
Beta strandi821 – 8255Combined sources
Beta strandi834 – 8374Combined sources
Turni842 – 8443Combined sources
Beta strandi846 – 8494Combined sources
Turni856 – 8594Combined sources
Beta strandi866 – 8683Combined sources
Helixi875 – 8773Combined sources
Beta strandi878 – 8814Combined sources
Turni886 – 8883Combined sources
Helixi890 – 8923Combined sources
Turni898 – 9003Combined sources
Beta strandi909 – 9113Combined sources
Helixi924 – 9263Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1KLOX-ray2.10A771-932[»]
1NPEX-ray2.30B769-932[»]
1TLENMR-A824-881[»]
4AQTX-ray3.20A33-395[»]
ProteinModelPortaliP02468.
SMRiP02468. Positions 37-492, 680-1012, 1283-1522.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP02468.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini44 – 283240Laminin N-terminalPROSITE-ProRule annotationAdd
BLAST
Domaini284 – 33956Laminin EGF-like 1PROSITE-ProRule annotationAdd
BLAST
Domaini340 – 39556Laminin EGF-like 2PROSITE-ProRule annotationAdd
BLAST
Domaini396 – 44247Laminin EGF-like 3PROSITE-ProRule annotationAdd
BLAST
Domaini443 – 49250Laminin EGF-like 4PROSITE-ProRule annotationAdd
BLAST
Domaini493 – 50210Laminin EGF-like 5; first partPROSITE-ProRule annotation
Domaini512 – 687176Laminin IV type APROSITE-ProRule annotationAdd
BLAST
Domaini688 – 72134Laminin EGF-like 5; second partPROSITE-ProRule annotationAdd
BLAST
Domaini722 – 77049Laminin EGF-like 6PROSITE-ProRule annotationAdd
BLAST
Domaini771 – 82555Laminin EGF-like 7PROSITE-ProRule annotationAdd
BLAST
Domaini826 – 88156Laminin EGF-like 8; nidogen-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini882 – 93251Laminin EGF-like 9PROSITE-ProRule annotationAdd
BLAST
Domaini933 – 98048Laminin EGF-like 10PROSITE-ProRule annotationAdd
BLAST
Domaini981 – 102848Laminin EGF-like 11PROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1029 – 1607579Domain II and IAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili1034 – 1594561Sequence 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 11 laminin EGF-like domains.PROSITE-ProRule annotation
Contains 1 laminin IV type A 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

eggNOGiNOG235720.
HOGENOMiHOG000019301.
HOVERGENiHBG100808.
InParanoidiP02468.
PhylomeDBiP02468.

Family and domain databases

Gene3Di2.60.120.260. 1 hit.
InterProiIPR013032. EGF-like_CS.
IPR002049. EGF_laminin.
IPR008979. Galactose-bd-like.
IPR018031. Laminin_B_subgr.
IPR000034. Laminin_B_type_IV.
IPR008211. Laminin_N.
[Graphical view]
PfamiPF00052. Laminin_B. 1 hit.
PF00053. Laminin_EGF. 11 hits.
PF00055. Laminin_N. 1 hit.
[Graphical view]
SMARTiSM00180. EGF_Lam. 10 hits.
SM00281. LamB. 1 hit.
SM00136. LamNT. 1 hit.
[Graphical view]
PROSITEiPS00022. EGF_1. 8 hits.
PS01186. EGF_2. 2 hits.
PS01248. EGF_LAM_1. 10 hits.
PS50027. EGF_LAM_2. 10 hits.
PS51115. LAMININ_IVA. 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.

P02468-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MTGGGRAALA LQPRGRLWPL LAVLAAVAGC VRAAMDECAD EGGRPQRCMP
60 70 80 90 100
EFVNAAFNVT VVATNTCGTP PEEYCVQTGV TGVTKSCHLC DAGQQHLQHG
110 120 130 140 150
AAFLTDYNNQ ADTTWWQSQT MLAGVQYPNS INLTLHLGKA FDITYVRLKF
160 170 180 190 200
HTSRPESFAI YKRTREDGPW IPYQYYSGSC ENTYSKANRG FIRTGGDEQQ
210 220 230 240 250
ALCTDEFSDI SPLTGGNVAF STLEGRPSAY NFDNSPVLQE WVTATDIRVT
260 270 280 290 300
LNRLNTFGDE VFNEPKVLKS YYYAISDFAV GGRCKCNGHA SECVKNEFDK
310 320 330 340 350
LMCNCKHNTY GVDCEKCLPF FNDRPWRRAT AESASESLPC DCNGRSQECY
360 370 380 390 400
FDPELYRSTG HGGHCTNCRD NTDGAKCERC RENFFRLGNT EACSPCHCSP
410 420 430 440 450
VGSLSTQCDS YGRCSCKPGV MGDKCDRCQP GFHSLTEAGC RPCSCDLRGS
460 470 480 490 500
TDECNVETGR CVCKDNVEGF NCERCKPGFF NLESSNPKGC TPCFCFGHSS
510 520 530 540 550
VCTNAVGYSV YDISSTFQID EDGWRVEQRD GSEASLEWSS DRQDIAVISD
560 570 580 590 600
SYFPRYFIAP VKFLGNQVLS YGQNLSFSFR VDRRDTRLSA EDLVLEGAGL
610 620 630 640 650
RVSVPLIAQG NSYPSETTVK YIFRLHEATD YPWRPALSPF EFQKLLNNLT
660 670 680 690 700
SIKIRGTYSE RTAGYLDDVT LQSARPGPGV PATWVESCTC PVGYGGQFCE
710 720 730 740 750
TCLPGYRRET PSLGPYSPCV LCTCNGHSET CDPETGVCDC RDNTAGPHCE
760 770 780 790 800
KCSDGYYGDS TLGTSSDCQP CPCPGGSSCA IVPKTKEVVC THCPTGTAGK
810 820 830 840 850
RCELCDDGYF GDPLGSNGPV RLCRPCQCND NIDPNAVGNC NRLTGECLKC
860 870 880 890 900
IYNTAGFYCD RCKEGFFGNP LAPNPADKCK ACACNPYGTV QQQSSCNPVT
910 920 930 940 950
GQCQCLPHVS GRDCGTCDPG YYNLQSGQGC ERCDCHALGS TNGQCDIRTG
960 970 980 990 1000
QCECQPGITG QHCERCETNH FGFGPEGCKP CDCHHEGSLS LQCKDDGRCE
1010 1020 1030 1040 1050
CREGFVGNRC DQCEENYFYN RSWPGCQECP ACYRLVKDKA AEHRVKLQEL
1060 1070 1080 1090 1100
ESLIANLGTG DDMVTDQAFE DRLKEAEREV TDLLREAQEV KDVDQNLMDR
1110 1120 1130 1140 1150
LQRVNSSLHS QISRLQNIRN TIEETGILAE RARSRVESTE QLIEIASREL
1160 1170 1180 1190 1200
EKAKMAAANV SITQPESTGE PNNMTLLAEE ARRLAERHKQ EADDIVRVAK
1210 1220 1230 1240 1250
TANETSAEAY NLLLRTLAGE NQTALEIEEL NRKYEQAKNI SQDLEKQAAR
1260 1270 1280 1290 1300
VHEEAKRAGD KAVEIYASVA QLTPVDSEAL ENEANKIKKE AADLDRLIDQ
1310 1320 1330 1340 1350
KLKDYEDLRE DMRGKEHEVK NLLEKGKAEQ QTADQLLARA DAAKALAEEA
1360 1370 1380 1390 1400
AKKGRSTLQE ANDILNNLKD FDRRVNDNKT AAEEALRRIP AINRTIAEAN
1410 1420 1430 1440 1450
EKTREAQLAL GNAAADATEA KNKAHEAERI ASAVQKNATS TKADAERTFG
1460 1470 1480 1490 1500
EVTDLDNEVN GMLRQLEEAE NELKRKQDDA DQDMMMAGMA SQAAQEAELN
1510 1520 1530 1540 1550
ARKAKNSVSS LLSQLNNLLD QLGQLDTVDL NKLNEIEGSL NKAKDEMKAS
1560 1570 1580 1590 1600
DLDRKVSDLE SEARKQEAAI MDYNRDIAEI IKDIHNLEDI KKTLPTGCFN

TPSIEKP
Length:1,607
Mass (Da):177,298
Last modified:July 1, 1989 - v2
Checksum:i81B7B08E4869F242
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti216 – 2161G → A in AAA39409. (PubMed:2836421)Curated
Sequence conflicti260 – 2601E → D(PubMed:3167041)Curated
Sequence conflicti337 – 3371S → C in AAA39408. (PubMed:3167041)Curated
Sequence conflicti447 – 4482LR → PS in AAA39408. (PubMed:3167041)Curated
Sequence conflicti544 – 5441D → Y in AAA39408. (PubMed:3167041)Curated
Sequence conflicti662 – 6621T → S in AAA39408. (PubMed:3167041)Curated
Sequence conflicti886 – 8861Missing in AAA39408. (PubMed:3167041)Curated
Sequence conflicti1158 – 11581Missing in AAA39408. (PubMed:3167041)Curated
Sequence conflicti1434 – 14341V → A in AAA39408. (PubMed:3167041)Curated
Sequence conflicti1475 – 14751R → K in CAA28838. (PubMed:6209134)Curated
Sequence conflicti1576 – 15761D → N in CAA28838. (PubMed:6209134)Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X05211 mRNA. Translation: CAA28838.1.
J03484 mRNA. Translation: AAA39405.1.
J02930 mRNA. Translation: AAA39408.1.
J03749 Genomic DNA. Translation: AAA39409.1.
CCDSiCCDS15370.1.
PIRiA28469. MMMSB2.
S55783.
UniGeneiMm.1249.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X05211 mRNA. Translation: CAA28838.1 .
J03484 mRNA. Translation: AAA39405.1 .
J02930 mRNA. Translation: AAA39408.1 .
J03749 Genomic DNA. Translation: AAA39409.1 .
CCDSi CCDS15370.1.
PIRi A28469. MMMSB2.
S55783.
UniGenei Mm.1249.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1KLO X-ray 2.10 A 771-932 [» ]
1NPE X-ray 2.30 B 769-932 [» ]
1TLE NMR - A 824-881 [» ]
4AQT X-ray 3.20 A 33-395 [» ]
ProteinModelPortali P02468.
SMRi P02468. Positions 37-492, 680-1012, 1283-1522.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

DIPi DIP-41793N.
IntActi P02468. 5 interactions.
MINTi MINT-1031545.

PTM databases

PhosphoSitei P02468.

Proteomic databases

MaxQBi P02468.
PaxDbi P02468.
PRIDEi P02468.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Organism-specific databases

MGIi MGI:99914. Lamc1.

Phylogenomic databases

eggNOGi NOG235720.
HOGENOMi HOG000019301.
HOVERGENi HBG100808.
InParanoidi P02468.
PhylomeDBi P02468.

Enzyme and pathway databases

Reactomei REACT_196607. Non-integrin membrane-ECM interactions.
REACT_202342. Laminin interactions.
REACT_219680. L1CAM interactions.

Miscellaneous databases

ChiTaRSi Lamc1. mouse.
EvolutionaryTracei P02468.
PROi P02468.
SOURCEi Search...

Gene expression databases

CleanExi MM_LAMC1.
Genevestigatori P02468.

Family and domain databases

Gene3Di 2.60.120.260. 1 hit.
InterProi IPR013032. EGF-like_CS.
IPR002049. EGF_laminin.
IPR008979. Galactose-bd-like.
IPR018031. Laminin_B_subgr.
IPR000034. Laminin_B_type_IV.
IPR008211. Laminin_N.
[Graphical view ]
Pfami PF00052. Laminin_B. 1 hit.
PF00053. Laminin_EGF. 11 hits.
PF00055. Laminin_N. 1 hit.
[Graphical view ]
SMARTi SM00180. EGF_Lam. 10 hits.
SM00281. LamB. 1 hit.
SM00136. LamNT. 1 hit.
[Graphical view ]
PROSITEi PS00022. EGF_1. 8 hits.
PS01186. EGF_2. 2 hits.
PS01248. EGF_LAM_1. 10 hits.
PS50027. EGF_LAM_2. 10 hits.
PS51115. LAMININ_IVA. 1 hit.
PS51117. LAMININ_NTER. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "The laminin B2 chain has a multidomain structure homologous to the B1 chain."
    Sasaki M., Yamada Y.
    J. Biol. Chem. 262:17111-17117(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "Primary structure of the mouse laminin B2 chain and comparison with laminin B1."
    Durkin M.E., Bartos B.B., Liu S.-H., Phillips S.L., Chung A.E.
    Biochemistry 27:5198-5204(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  3. "The laminin B2 chain promoter contains unique repeat sequences and is active in transient transfection."
    Ogawa K., Burbelo P.D., Sasaki M., Yamada Y.
    J. Biol. Chem. 263:8384-8389(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-239.
  4. "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 1391-1607.
  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-648; ASN-1105; ASN-1203; ASN-1221 AND ASN-1393.
  6. "Crystal structure of three consecutive laminin-type epidermal growth factor-like (LE) modules of laminin gamma1 chain harboring the nidogen binding site."
    Stetefeld J., Mayer U., Timpl R., Huber R.
    J. Mol. Biol. 257:644-657(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 771-932.
  7. "Structure of the nidogen binding LE module of the laminin gamma1 chain in solution."
    Baumgartner R., Czisch M., Mayer U., Poeschl E., Huber R., Timpl R., Holak T.A.
    J. Mol. Biol. 257:658-668(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 824-881.

Entry informationi

Entry nameiLAMC1_MOUSE
AccessioniPrimary (citable) accession number: P02468
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 1, 1989
Last modified: November 26, 2014
This is version 151 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, 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

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