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P11047

- LAMC1_HUMAN

UniProt

P11047 - LAMC1_HUMAN

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Protein
Laminin subunit gamma-1
Gene
LAMC1, LAMB2
Organism
Homo sapiens (Human)
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: Ensembl

GO - Biological processi

  1. axon guidance Source: Reactome
  2. cell adhesion Source: HGNC
  3. cell migration Source: HGNC
  4. endoderm development Source: ProtInc
  5. extracellular matrix disassembly Source: HGNC
  6. extracellular matrix organization Source: Reactome
  7. hemidesmosome assembly Source: HGNC
  8. positive regulation of epithelial cell proliferation Source: HGNC
  9. protein complex assembly Source: HGNC
  10. 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 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:LAMB2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 1

Organism-specific databases

HGNCiHGNC:6492. LAMC1.

Subcellular locationi

GO - Cellular componenti

  1. basement membrane Source: UniProtKB
  2. extracellular region Source: Reactome
  3. extracellular space Source: UniProtKB
  4. extracellular vesicular exosome Source: UniProtKB
  5. laminin-1 complex Source: UniProtKB
  6. laminin-10 complex Source: BHF-UCL
  7. laminin-11 complex Source: BHF-UCL
Complete GO annotation...

Keywords - Cellular componenti

Basement membrane, Extracellular matrix, Secreted

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA30280.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 3333
Add
BLAST
Chaini34 – 16091576Laminin subunit gamma-1
PRO_0000017074Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi60 – 601N-linked (GlcNAc...) Reviewed prediction
Glycosylationi134 – 1341N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi286 ↔ 295 By similarity
Disulfide bondi288 ↔ 305 By similarity
Disulfide bondi307 ↔ 316 By similarity
Disulfide bondi319 ↔ 339 By similarity
Disulfide bondi342 ↔ 351 By similarity
Disulfide bondi344 ↔ 367 By similarity
Disulfide bondi370 ↔ 379 By similarity
Disulfide bondi382 ↔ 395 By similarity
Disulfide bondi398 ↔ 410 By similarity
Disulfide bondi400 ↔ 416 By similarity
Disulfide bondi418 ↔ 427 By similarity
Disulfide bondi430 ↔ 442 By similarity
Disulfide bondi445 ↔ 456 By similarity
Disulfide bondi447 ↔ 463 By similarity
Disulfide bondi465 ↔ 474 By similarity
Disulfide bondi477 ↔ 492 By similarity
Glycosylationi576 – 5761N-linked (GlcNAc...) Reviewed prediction
Glycosylationi650 – 6501N-linked (GlcNAc...)2 Publications
Disulfide bondi724 ↔ 733 By similarity
Disulfide bondi726 ↔ 740 By similarity
Disulfide bondi742 ↔ 751 By similarity
Disulfide bondi754 ↔ 770 By similarity
Disulfide bondi773 ↔ 781 By similarity
Disulfide bondi775 ↔ 792 By similarity
Disulfide bondi795 ↔ 804 By similarity
Disulfide bondi807 ↔ 825 By similarity
Disulfide bondi828 ↔ 842 By similarity
Disulfide bondi830 ↔ 849 By similarity
Disulfide bondi852 ↔ 861 By similarity
Disulfide bondi864 ↔ 881 By similarity
Disulfide bondi884 ↔ 898 By similarity
Disulfide bondi886 ↔ 905 By similarity
Disulfide bondi907 ↔ 916 By similarity
Disulfide bondi919 ↔ 932 By similarity
Disulfide bondi935 ↔ 947 By similarity
Disulfide bondi937 ↔ 954 By similarity
Disulfide bondi956 ↔ 965 By similarity
Disulfide bondi968 ↔ 980 By similarity
Disulfide bondi983 ↔ 995 By similarity
Disulfide bondi985 ↔ 1001 By similarity
Disulfide bondi1003 ↔ 1012 By similarity
Disulfide bondi1015 ↔ 1028 By similarity
Glycosylationi1022 – 10221N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi1031 – 1031Interchain Inferred
Disulfide bondi1034 – 1034Interchain Inferred
Glycosylationi1107 – 11071N-linked (GlcNAc...)2 Publications
Glycosylationi1161 – 11611N-linked (GlcNAc...)1 Publication
Glycosylationi1175 – 11751N-linked (GlcNAc...)1 Publication
Glycosylationi1205 – 12051N-linked (GlcNAc...) Reviewed prediction
Glycosylationi1223 – 12231N-linked (GlcNAc...)1 Publication
Glycosylationi1241 – 12411N-linked (GlcNAc...)1 Publication
Glycosylationi1380 – 13801N-linked (GlcNAc...) Reviewed prediction
Glycosylationi1395 – 13951N-linked (GlcNAc...)2 Publications
Glycosylationi1439 – 14391N-linked (GlcNAc...) Reviewed prediction
Modified residuei1493 – 14931Phosphoserine1 Publication
Disulfide bondi1600 – 1600Interchain Inferred

Keywords - PTMi

Disulfide bond, Glycoprotein, Phosphoprotein

Proteomic databases

MaxQBiP11047.
PaxDbiP11047.
PRIDEiP11047.

PTM databases

PhosphoSiteiP11047.

Expressioni

Tissue specificityi

Found in the basement membranes (major component).

Gene expression databases

BgeeiP11047.
CleanExiHS_LAMB2.
HS_LAMC1.
GenevestigatoriP11047.

Organism-specific databases

HPAiCAB004486.
HPA001908.
HPA001909.

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).

Protein-protein interaction databases

BioGridi110109. 20 interactions.
IntActiP11047. 9 interactions.
MINTiMINT-1184520.
STRINGi9606.ENSP00000258341.

Structurei

3D structure databases

ProteinModelPortaliP11047.
SMRiP11047. Positions 39-396, 773-934.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini46 – 285240Laminin N-terminal
Add
BLAST
Domaini286 – 34156Laminin EGF-like 1
Add
BLAST
Domaini342 – 39756Laminin EGF-like 2
Add
BLAST
Domaini398 – 44447Laminin EGF-like 3
Add
BLAST
Domaini445 – 49450Laminin EGF-like 4
Add
BLAST
Domaini495 – 50410Laminin EGF-like 5; first part
Domaini514 – 689176Laminin IV type A
Add
BLAST
Domaini690 – 72334Laminin EGF-like 5; second part
Add
BLAST
Domaini724 – 77249Laminin EGF-like 6
Add
BLAST
Domaini773 – 82755Laminin EGF-like 7
Add
BLAST
Domaini828 – 88356Laminin EGF-like 8
Add
BLAST
Domaini884 – 93451Laminin EGF-like 9
Add
BLAST
Domaini935 – 98248Laminin EGF-like 10
Add
BLAST
Domaini983 – 103048Laminin EGF-like 11
Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1030 – 1609580Domain II and I
Add
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili1038 – 1609572 Reviewed prediction
Add
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

Keywords - Domaini

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

Phylogenomic databases

eggNOGiNOG235720.
HOGENOMiHOG000019301.
HOVERGENiHBG100808.
InParanoidiP11047.
KOiK05635.
OMAiEATDYPW.
OrthoDBiEOG7SR4KJ.
PhylomeDBiP11047.
TreeFamiTF352481.

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. 10 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. 11 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.

P11047-1 [UniParc]FASTAAdd to Basket

« Hide

MRGSHRAAPA LRPRGRLWPV LAVLAAAAAA GCAQAAMDEC TDEGGRPQRC     50
MPEFVNAAFN VTVVATNTCG TPPEEYCVQT GVTGVTKSCH LCDAGQPHLQ 100
HGAAFLTDYN NQADTTWWQS QTMLAGVQYP SSINLTLHLG KAFDITYVRL 150
KFHTSRPESF AIYKRTREDG PWIPYQYYSG SCENTYSKAN RGFIRTGGDE 200
QQALCTDEFS DISPLTGGNV AFSTLEGRPS AYNFDNSPVL QEWVTATDIR 250
VTLNRLNTFG DEVFNDPKVL KSYYYAISDF AVGGRCKCNG HASECMKNEF 300
DKLVCNCKHN TYGVDCEKCL PFFNDRPWRR ATAESASECL PCDCNGRSQE 350
CYFDPELYRS TGHGGHCTNC QDNTDGAHCE RCRENFFRLG NNEACSSCHC 400
SPVGSLSTQC DSYGRCSCKP GVMGDKCDRC QPGFHSLTEA GCRPCSCDPS 450
GSIDECNIET GRCVCKDNVE GFNCERCKPG FFNLESSNPR GCTPCFCFGH 500
SSVCTNAVGY SVYSISSTFQ IDEDGWRAEQ RDGSEASLEW SSERQDIAVI 550
SDSYFPRYFI APAKFLGKQV LSYGQNLSFS FRVDRRDTRL SAEDLVLEGA 600
GLRVSVPLIA QGNSYPSETT VKYVFRLHEA TDYPWRPALT PFEFQKLLNN 650
LTSIKIRGTY SERSAGYLDD VTLASARPGP GVPATWVESC TCPVGYGGQF 700
CEMCLSGYRR ETPNLGPYSP CVLCACNGHS ETCDPETGVC NCRDNTAGPH 750
CEKCSDGYYG DSTAGTSSDC QPCPCPGGSS CAVVPKTKEV VCTNCPTGTT 800
GKRCELCDDG YFGDPLGRNG PVRLCRLCQC SDNIDPNAVG NCNRLTGECL 850
KCIYNTAGFY CDRCKDGFFG NPLAPNPADK CKACNCNLYG TMKQQSSCNP 900
VTGQCECLPH VTGQDCGACD PGFYNLQSGQ GCERCDCHAL GSTNGQCDIR 950
TGQCECQPGI TGQHCERCEV NHFGFGPEGC KPCDCHPEGS LSLQCKDDGR 1000
CECREGFVGN RCDQCEENYF YNRSWPGCQE CPACYRLVKD KVADHRVKLQ 1050
ELESLIANLG TGDEMVTDQA FEDRLKEAER EVMDLLREAQ DVKDVDQNLM 1100
DRLQRVNNTL SSQISRLQNI RNTIEETGNL AEQARAHVEN TERLIEIASR 1150
ELEKAKVAAA NVSVTQPEST GDPNNMTLLA EEARKLAERH KQEADDIVRV 1200
AKTANDTSTE AYNLLLRTLA GENQTAFEIE ELNRKYEQAK NISQDLEKQA 1250
ARVHEEAKRA GDKAVEIYAS VAQLSPLDSE TLENEANNIK MEAENLEQLI 1300
DQKLKDYEDL REDMRGKELE VKNLLEKGKT EQQTADQLLA RADAAKALAE 1350
EAAKKGRDTL QEANDILNNL KDFDRRVNDN KTAAEEALRK IPAINQTITE 1400
ANEKTREAQQ ALGSAAADAT EAKNKAHEAE RIASAVQKNA TSTKAEAERT 1450
FAEVTDLDNE VNNMLKQLQE AEKELKRKQD DADQDMMMAG MASQAAQEAE 1500
INARKAKNSV TSLLSIINDL LEQLGQLDTV DLNKLNEIEG TLNKAKDEMK 1550
VSDLDRKVSD LENEAKKQEA AIMDYNRDIE EIMKDIRNLE DIRKTLPSGC 1600
FNTPSIEKP 1609
Length:1,609
Mass (Da):177,603
Last modified:March 3, 2009 - v3
Checksum:i42D9A9958EEBBB01
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti458 – 4581I → V.2 Publications
Corresponds to variant rs20563 [ dbSNP | Ensembl ].
VAR_014700
Natural varianti731 – 7311E → K.
Corresponds to variant rs2230157 [ dbSNP | Ensembl ].
VAR_054488
Natural varianti888 – 8881L → P.2 Publications
Corresponds to variant rs20558 [ dbSNP | Ensembl ].
VAR_014701
Natural varianti1116 – 11161R → H in a colorectal cancer sample; somatic mutation. 1 Publication
VAR_035821
Natural varianti1121 – 11211R → Q.
Corresponds to variant rs20559 [ dbSNP | Ensembl ].
VAR_014702

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti212 – 2121I → F in AAA59492. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
J03202 mRNA. Translation: AAA59488.1.
M55210
, M55217, M55201, M55211, M55212, M55213, M55214, M55215, M55216, M55192, M55193, M55194, M55195, M55196, M55197, M55198, M55199, M55200, M55202, M55203, M55204, M55205, M55206, M55207, M55208, M55209 Genomic DNA. Translation: AAA59492.1.
AL354953, AL450304 Genomic DNA. Translation: CAH70981.1.
AL450304, AL354953 Genomic DNA. Translation: CAI14877.1.
X13939 mRNA. Translation: CAA32122.1.
M27654 mRNA. Translation: AAA59489.1.
CCDSiCCDS1351.1.
PIRiS13548. MMHUB2.
RefSeqiNP_002284.3. NM_002293.3.
UniGeneiHs.609663.

Genome annotation databases

EnsembliENST00000258341; ENSP00000258341; ENSG00000135862.
GeneIDi3915.
KEGGihsa:3915.
UCSCiuc001gpy.4. human.

Polymorphism databases

DMDMi224471885.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
J03202 mRNA. Translation: AAA59488.1 .
M55210
, M55217 , M55201 , M55211 , M55212 , M55213 , M55214 , M55215 , M55216 , M55192 , M55193 , M55194 , M55195 , M55196 , M55197 , M55198 , M55199 , M55200 , M55202 , M55203 , M55204 , M55205 , M55206 , M55207 , M55208 , M55209 Genomic DNA. Translation: AAA59492.1 .
AL354953 , AL450304 Genomic DNA. Translation: CAH70981.1 .
AL450304 , AL354953 Genomic DNA. Translation: CAI14877.1 .
X13939 mRNA. Translation: CAA32122.1 .
M27654 mRNA. Translation: AAA59489.1 .
CCDSi CCDS1351.1.
PIRi S13548. MMHUB2.
RefSeqi NP_002284.3. NM_002293.3.
UniGenei Hs.609663.

3D structure databases

ProteinModelPortali P11047.
SMRi P11047. Positions 39-396, 773-934.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 110109. 20 interactions.
IntActi P11047. 9 interactions.
MINTi MINT-1184520.
STRINGi 9606.ENSP00000258341.

Chemistry

ChEMBLi CHEMBL2364187.
DrugBanki DB00009. Alteplase.
DB00029. Anistreplase.
DB00015. Reteplase.
DB00031. Tenecteplase.

PTM databases

PhosphoSitei P11047.

Polymorphism databases

DMDMi 224471885.

Proteomic databases

MaxQBi P11047.
PaxDbi P11047.
PRIDEi P11047.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000258341 ; ENSP00000258341 ; ENSG00000135862 .
GeneIDi 3915.
KEGGi hsa:3915.
UCSCi uc001gpy.4. human.

Organism-specific databases

CTDi 3915.
GeneCardsi GC01P182992.
H-InvDB HIX0001405.
HGNCi HGNC:6492. LAMC1.
HPAi CAB004486.
HPA001908.
HPA001909.
MIMi 150290. gene.
neXtProti NX_P11047.
PharmGKBi PA30280.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG235720.
HOGENOMi HOG000019301.
HOVERGENi HBG100808.
InParanoidi P11047.
KOi K05635.
OMAi EATDYPW.
OrthoDBi EOG7SR4KJ.
PhylomeDBi P11047.
TreeFami TF352481.

Enzyme and pathway databases

Reactomei REACT_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

ChiTaRSi LAMC1. human.
GeneWikii Laminin,_gamma_1.
GenomeRNAii 3915.
NextBioi 15381.
PROi P11047.
SOURCEi Search...

Gene expression databases

Bgeei P11047.
CleanExi HS_LAMB2.
HS_LAMC1.
Genevestigatori P11047.

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. 10 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. 11 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. "Human laminin B2 chain. Comparison of the complete amino acid sequence with the B1 chain reveals variability in sequence homology between different structural domains."
    Pikkarainen T., Kallunki T., Tryggvason K.
    J. Biol. Chem. 263:6751-6758(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANTS VAL-458 AND PRO-888.
  2. "Structure of the human laminin B2 chain gene reveals extensive divergence from the laminin B1 chain gene."
    Kallunki T., Ikonen J., Chow L.T., Kallunki P., Tryggvason K.
    J. Biol. Chem. 266:221-228(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS VAL-458 AND PRO-888.
  3. "The DNA sequence and biological annotation of human chromosome 1."
    Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.
    , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
    Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. "Differences in human laminin B2 sequences."
    Santos C.L.S., Sabbaga J., Brentani R.
    DNA Seq. 1:275-277(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1282-1609.
    Tissue: Endothelial cell.
  5. "Isolation of a human laminin B2 (LAMB2) cDNA clone and assignment of the gene to chromosome region 1q25-->q31."
    Fukushima Y., Pikkarainen T., Kallunki T., Eddy R.L., Byers M.G., Haley L.L., Henry W.M., Tryggvason K., Shows T.B.
    Cytogenet. Cell Genet. 48:137-141(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1393-1609.
  6. "Identification and quantification of N-linked glycoproteins using hydrazide chemistry, stable isotope labeling and mass spectrometry."
    Zhang H., Li X.-J., Martin D.B., Aebersold R.
    Nat. Biotechnol. 21:660-666(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: GLYCOSYLATION AT ASN-650.
  7. "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-1107; ASN-1161; ASN-1175; ASN-1223 AND ASN-1395.
    Tissue: Plasma.
  8. "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-650; ASN-1107; ASN-1241 AND ASN-1395.
    Tissue: Liver.
  9. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  10. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
    Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
    Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1493, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  11. Cited for: VARIANT [LARGE SCALE ANALYSIS] HIS-1116.

Entry informationi

Entry nameiLAMC1_HUMAN
AccessioniPrimary (citable) accession number: P11047
Secondary accession number(s): Q5VYE7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: March 3, 2009
Last modified: September 3, 2014
This is version 170 of the entry and version 3 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 1
    Human chromosome 1: 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

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