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Q9Y6N6

- LAMC3_HUMAN

UniProt

Q9Y6N6 - LAMC3_HUMAN

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Protein

Laminin subunit gamma-3

Gene

LAMC3

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. structural molecule activity Source: ProtInc

GO - Biological processi

  1. astrocyte development Source: Ensembl
  2. cell adhesion Source: UniProtKB-KW
  3. cell morphogenesis involved in differentiation Source: Ensembl
  4. extracellular matrix organization Source: Reactome
  5. retina development in camera-type eye Source: Ensembl
  6. visual perception Source: Ensembl
Complete GO annotation...

Keywords - Biological processi

Cell adhesion

Enzyme and pathway databases

ReactomeiREACT_163874. Non-integrin membrane-ECM interactions.
REACT_169262. Laminin interactions.

Names & Taxonomyi

Protein namesi
Recommended name:
Laminin subunit gamma-3
Alternative name(s):
Laminin-12 subunit gamma
Laminin-14 subunit gamma
Laminin-15 subunit gamma
Gene namesi
Name:LAMC3
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 9

Organism-specific databases

HGNCiHGNC:6494. LAMC3.

Subcellular locationi

GO - Cellular componenti

  1. basement membrane Source: UniProtKB-KW
  2. extracellular region Source: Reactome
  3. membrane Source: ProtInc
  4. proteinaceous extracellular matrix Source: ProtInc
Complete GO annotation...

Keywords - Cellular componenti

Basement membrane, Extracellular matrix, Secreted

Pathology & Biotechi

Involvement in diseasei

Cortical malformations occipital (OCCM) [MIM:614115]: A disease in which affected individuals develop seizures, sometimes associated with transient visual changes. Brain MRI shows both pachygyria and polymicrogyria restricted to the lateral occipital lobes.1 Publication
Note: The disease is caused by mutations affecting the gene represented in this entry.
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti350 – 3501G → R in OCCM. 1 Publication
VAR_066404

Keywords - Diseasei

Disease mutation

Organism-specific databases

MIMi614115. phenotype.
Orphaneti280640. Occipital pachygyria and polymicrogyria.
PharmGKBiPA30282.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1919Sequence AnalysisAdd
BLAST
Chaini20 – 15751556Laminin subunit gamma-3PRO_0000017079Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi87 – 871N-linked (GlcNAc...)Sequence Analysis
Glycosylationi119 – 1191N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi271 ↔ 280PROSITE-ProRule annotation
Disulfide bondi273 ↔ 290PROSITE-ProRule annotation
Disulfide bondi292 ↔ 301PROSITE-ProRule annotation
Glycosylationi295 – 2951N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi304 ↔ 324PROSITE-ProRule annotation
Disulfide bondi327 ↔ 336PROSITE-ProRule annotation
Glycosylationi328 – 3281N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi329 ↔ 352PROSITE-ProRule annotation
Disulfide bondi355 ↔ 364PROSITE-ProRule annotation
Disulfide bondi367 ↔ 380PROSITE-ProRule annotation
Disulfide bondi383 ↔ 395PROSITE-ProRule annotation
Disulfide bondi385 ↔ 401PROSITE-ProRule annotation
Disulfide bondi403 ↔ 412PROSITE-ProRule annotation
Disulfide bondi415 ↔ 427PROSITE-ProRule annotation
Disulfide bondi430 ↔ 441PROSITE-ProRule annotation
Disulfide bondi432 ↔ 448PROSITE-ProRule annotation
Disulfide bondi450 ↔ 459PROSITE-ProRule annotation
Disulfide bondi462 ↔ 477PROSITE-ProRule annotation
Glycosylationi631 – 6311N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi707 ↔ 715PROSITE-ProRule annotation
Disulfide bondi709 ↔ 722PROSITE-ProRule annotation
Disulfide bondi724 ↔ 733PROSITE-ProRule annotation
Disulfide bondi736 ↔ 752PROSITE-ProRule annotation
Disulfide bondi755 ↔ 763PROSITE-ProRule annotation
Disulfide bondi757 ↔ 774PROSITE-ProRule annotation
Disulfide bondi777 ↔ 786PROSITE-ProRule annotation
Disulfide bondi789 ↔ 807PROSITE-ProRule annotation
Disulfide bondi810 ↔ 824PROSITE-ProRule annotation
Disulfide bondi812 ↔ 831PROSITE-ProRule annotation
Disulfide bondi834 ↔ 843PROSITE-ProRule annotation
Glycosylationi837 – 8371N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi846 ↔ 863PROSITE-ProRule annotation
Disulfide bondi866 ↔ 880PROSITE-ProRule annotation
Disulfide bondi868 ↔ 887PROSITE-ProRule annotation
Disulfide bondi889 ↔ 898PROSITE-ProRule annotation
Disulfide bondi901 ↔ 914PROSITE-ProRule annotation
Disulfide bondi917 ↔ 929PROSITE-ProRule annotation
Disulfide bondi919 ↔ 936PROSITE-ProRule annotation
Disulfide bondi938 ↔ 947PROSITE-ProRule annotation
Disulfide bondi950 ↔ 962PROSITE-ProRule annotation
Disulfide bondi965 ↔ 977PROSITE-ProRule annotation
Disulfide bondi967 ↔ 983PROSITE-ProRule annotation
Glycosylationi980 – 9801N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi985 ↔ 994PROSITE-ProRule annotation
Disulfide bondi997 ↔ 1010PROSITE-ProRule annotation
Glycosylationi1185 – 11851N-linked (GlcNAc...)Sequence Analysis

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

MaxQBiQ9Y6N6.
PaxDbiQ9Y6N6.
PRIDEiQ9Y6N6.

Expressioni

Tissue specificityi

Broadly expressed in: skin, heart, lung, and the reproductive tracts.

Gene expression databases

BgeeiQ9Y6N6.
CleanExiHS_LAMC3.
ExpressionAtlasiQ9Y6N6. baseline and differential.
GenevestigatoriQ9Y6N6.

Organism-specific databases

HPAiHPA022814.

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-3 is a subunit of laminin-12 (laminin-213), laminin-14 (laminin-423) and laminin-15 (laminin-523).

Protein-protein interaction databases

BioGridi115603. 21 interactions.
IntActiQ9Y6N6. 21 interactions.
MINTiMINT-7034525.
STRINGi9606.ENSP00000354360.

Structurei

3D structure databases

ProteinModelPortaliQ9Y6N6.
SMRiQ9Y6N6. Positions 25-482, 662-1016.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini31 – 270240Laminin N-terminalPROSITE-ProRule annotationAdd
BLAST
Domaini271 – 32656Laminin EGF-like 1PROSITE-ProRule annotationAdd
BLAST
Domaini327 – 38256Laminin EGF-like 2PROSITE-ProRule annotationAdd
BLAST
Domaini383 – 42947Laminin EGF-like 3PROSITE-ProRule annotationAdd
BLAST
Domaini430 – 47950Laminin EGF-like 4PROSITE-ProRule annotationAdd
BLAST
Domaini480 – 48910Laminin EGF-like 5; first partPROSITE-ProRule annotation
Domaini499 – 672174Laminin IV type APROSITE-ProRule annotationAdd
BLAST
Domaini673 – 70634Laminin EGF-like 5; second partPROSITE-ProRule annotationAdd
BLAST
Domaini707 – 75448Laminin EGF-like 6PROSITE-ProRule annotationAdd
BLAST
Domaini755 – 80955Laminin EGF-like 7PROSITE-ProRule annotationAdd
BLAST
Domaini810 – 86556Laminin EGF-like 8PROSITE-ProRule annotationAdd
BLAST
Domaini866 – 91651Laminin EGF-like 9PROSITE-ProRule annotationAdd
BLAST
Domaini917 – 96448Laminin EGF-like 10PROSITE-ProRule annotationAdd
BLAST
Domaini965 – 101349Laminin EGF-like 11PROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1014 – 1575562Domain II and IAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili1073 – 113462Sequence AnalysisAdd
BLAST
Coiled coili1201 – 122828Sequence AnalysisAdd
BLAST
Coiled coili1410 – 149283Sequence AnalysisAdd
BLAST
Coiled coili1523 – 156745Sequence AnalysisAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi1059 – 10613Cell attachment siteSequence Analysis

Domaini

The alpha-helical domains I and II are thought to interact with other laminin chains to form a coiled coil structure.
Domain IV is 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.
GeneTreeiENSGT00760000118860.
HOGENOMiHOG000019301.
HOVERGENiHBG100808.
InParanoidiQ9Y6N6.
KOiK06247.
OMAiQRGRRCE.
OrthoDBiEOG7SR4KJ.
PhylomeDBiQ9Y6N6.
TreeFamiTF352481.

Family and domain databases

Gene3Di2.60.120.260. 1 hit.
InterProiIPR002049. EGF_laminin.
IPR008979. Galactose-bd-like.
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.
SM00136. LamNT. 1 hit.
[Graphical view]
PROSITEiPS00022. EGF_1. 7 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.

Q9Y6N6-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MAAAALLLGL ALLAPRAAGA GMGACYDGAG RPQRCLPVFE NAAFGRLAQA
60 70 80 90 100
SHTCGSPPED FCPHVGAAGA GAHCQRCDAA DPQRHHNASY LTDFHSQDES
110 120 130 140 150
TWWQSPSMAF GVQYPTSVNI TLRLGKAYEI TYVRLKFHTS RPESFAIYKR
160 170 180 190 200
SRADGPWEPY QFYSASCQKT YGRPEGQYLR PGEDERVAFC TSEFSDISPL
210 220 230 240 250
SGGNVAFSTL EGRPSAYNFE ESPGLQEWVT STELLISLDR LNTFGDDIFK
260 270 280 290 300
DPKVLQSYYY AVSDFSVGGR CKCNGHASEC GPDVAGQLAC RCQHNTTGTD
310 320 330 340 350
CERCLPFFQD RPWARGTAEA AHECLPCNCS GRSEECTFDR ELFRSTGHGG
360 370 380 390 400
RCHHCRDHTA GPHCERCQEN FYHWDPRMPC QPCDCQSAGS LHLQCDDTGT
410 420 430 440 450
CACKPTVTGW KCDRCLPGFH SLSEGGCRPC TCNPAGSLDT CDPRSGRCPC
460 470 480 490 500
KENVEGNLCD RCRPGTFNLQ PHNPAGCSSC FCYGHSKVCA STAQFQVHHI
510 520 530 540 550
LSDFHQGAEG WWARSVGGSE HPPQWSPNGV LLSPEDEEEL TAPEKFLGDQ
560 570 580 590 600
RFSYGQPLIL TFRVPPGDSP LPVQLRLEGT GLALSLRHSS LSGPQDAGHP
610 620 630 640 650
REVELRFHLQ ETSEDVAPPL PPFHFQRLLA NLTSLRLRVS PGPSPAGPVF
660 670 680 690 700
LTEVRLTSAR PGLSPPASWV EICSCPTGYT GQFCESCAPG YKREMPQGGP
710 720 730 740 750
YASCVPCTCN QHGTCDPNTG ICVCSHHTEG PSCERCLPGF YGNPFAGQAD
760 770 780 790 800
DCQPCPCPGQ SACTTIPESR EVVCTHCPPG QRGRRCEVCD DGFFGDPLGL
810 820 830 840 850
FGHPQPCHQC QCSGNVDPNA VGNCDPLSGH CLRCLHNTTG DHCEHCQEGF
860 870 880 890 900
YGSALAPRPA DKCMPCSCHP QGSVSEQMPC DPVTGQCSCL PHVTARDCSR
910 920 930 940 950
CYPGFFDLQP GRGCRSCKCH PLGSQEDQCH PKTGQCTCRP GVTGQACDRC
960 970 980 990 1000
QLGFFGFSIK GCRACRCSPL GAASAQCHEN GTCVCRPGFE GYKCDRCHDN
1010 1020 1030 1040 1050
FFLTADGTHC QQCPSCYALV KEEAAKLKAR LTLTEGWLQG SDCGSPWGPL
1060 1070 1080 1090 1100
DILLGEAPRG DVYQGHHLLP GAREAFLEQM MSLEGAVKAA REQLQRLNKG
1110 1120 1130 1140 1150
ARCAQAGSQK TCTQLADLEA VLESSEEEIL HAAAILASLE IPQEGPSQPT
1160 1170 1180 1190 1200
KWSHLATEAR ALARSHRDTA TKIAATAWRA LLASNTSYAL LWNLLEGRVA
1210 1220 1230 1240 1250
LETQRDLEDR YQEVQAAQKA LRTAVAEVLP EAESVLATVQ QVGADTAPYL
1260 1270 1280 1290 1300
ALLASPGALP QKSRAEDLGL KAKALEKTVA SWQHMATEAA RTLQTAAQAT
1310 1320 1330 1340 1350
LRQTEPLTKL HQEARAALTQ ASSSVQAATV TVMGARTLLA DLEGMKLQFP
1360 1370 1380 1390 1400
RPKDQAALQR KADSVSDRLL ADTRKKTKQA ERMLGNAAPL SSSAKKKGRE
1410 1420 1430 1440 1450
AEVLAKDSAK LAKALLRERK QAHRRASRLT SQTQATLQQA SQQVLASEAR
1460 1470 1480 1490 1500
RQELEEAERV GAGLSEMEQQ IRESRISLEK DIETLSELLA RLGSLDTHQA
1510 1520 1530 1540 1550
PAQALNETQW ALERLRLQLG SPGSLQRKLS LLEQESQQQE LQIQGFESDL
1560 1570
AEIRADKQNL EAILHSLPEN CASWQ
Length:1,575
Mass (Da):171,227
Last modified:October 5, 2010 - v3
Checksum:iD09DAFB3A900E1BD
GO

Sequence cautioni

The sequence AAD36991.1 differs from that shown. Reason: Frameshift at positions 598 and 609.

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti957 – 9571F → S in AAD36991. (PubMed:10225960)Curated
Sequence conflicti979 – 9791E → Y in AAD36991. (PubMed:10225960)Curated
Sequence conflicti999 – 9991D → Y in AAD36991. (PubMed:10225960)Curated
Sequence conflicti1024 – 10241A → T in AAD36991. (PubMed:10225960)Curated
Sequence conflicti1157 – 11571T → I in AAD36991. (PubMed:10225960)Curated
Sequence conflicti1309 – 13091K → KARSRLTATSASQ in CAH69983. (PubMed:15164053)Curated
Sequence conflicti1309 – 13091K → MARSRLTATFASQ in AAD36991. (PubMed:10225960)Curated
Sequence conflicti1313 – 13131E → G in AAD36991. (PubMed:10225960)Curated
Sequence conflicti1433 – 14331T → M in BAD92124. 1 PublicationCurated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti350 – 3501G → R in OCCM. 1 Publication
VAR_066404
Natural varianti522 – 5221P → S.1 Publication
Corresponds to variant rs869457 [ dbSNP | Ensembl ].
VAR_056145
Natural varianti544 – 5441E → G.2 Publications
Corresponds to variant rs10901333 [ dbSNP | Ensembl ].
VAR_056146
Natural varianti770 – 7701R → G.2 Publications
Corresponds to variant rs3739510 [ dbSNP | Ensembl ].
VAR_056147
Natural varianti1082 – 10821S → G.2 Publications
Corresponds to variant rs2275140 [ dbSNP | Ensembl ].
VAR_056148
Natural varianti1264 – 12641R → W.
Corresponds to variant rs11244275 [ dbSNP | Ensembl ].
VAR_056149

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF041835 mRNA. Translation: AAD36991.1. Frameshift.
AL583807, AL355872 Genomic DNA. Translation: CAH69983.1.
AL583807, AL355872 Genomic DNA. Translation: CAH69984.3.
AL355872, AL583807 Genomic DNA. Translation: CAX14981.1.
AB208887 mRNA. Translation: BAD92124.1.
CCDSiCCDS6938.1.
RefSeqiNP_006050.3. NM_006059.3.
UniGeneiHs.201805.

Genome annotation databases

EnsembliENST00000361069; ENSP00000354360; ENSG00000050555.
GeneIDi10319.
KEGGihsa:10319.
UCSCiuc004caa.1. human.

Polymorphism databases

DMDMi308153586.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF041835 mRNA. Translation: AAD36991.1 . Frameshift.
AL583807 , AL355872 Genomic DNA. Translation: CAH69983.1 .
AL583807 , AL355872 Genomic DNA. Translation: CAH69984.3 .
AL355872 , AL583807 Genomic DNA. Translation: CAX14981.1 .
AB208887 mRNA. Translation: BAD92124.1 .
CCDSi CCDS6938.1.
RefSeqi NP_006050.3. NM_006059.3.
UniGenei Hs.201805.

3D structure databases

ProteinModelPortali Q9Y6N6.
SMRi Q9Y6N6. Positions 25-482, 662-1016.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 115603. 21 interactions.
IntActi Q9Y6N6. 21 interactions.
MINTi MINT-7034525.
STRINGi 9606.ENSP00000354360.

Chemistry

ChEMBLi CHEMBL2364187.

Polymorphism databases

DMDMi 308153586.

Proteomic databases

MaxQBi Q9Y6N6.
PaxDbi Q9Y6N6.
PRIDEi Q9Y6N6.

Protocols and materials databases

DNASUi 10319.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000361069 ; ENSP00000354360 ; ENSG00000050555 .
GeneIDi 10319.
KEGGi hsa:10319.
UCSCi uc004caa.1. human.

Organism-specific databases

CTDi 10319.
GeneCardsi GC09P133884.
H-InvDB HIX0008477.
HGNCi HGNC:6494. LAMC3.
HPAi HPA022814.
MIMi 604349. gene.
614115. phenotype.
neXtProti NX_Q9Y6N6.
Orphaneti 280640. Occipital pachygyria and polymicrogyria.
PharmGKBi PA30282.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG235720.
GeneTreei ENSGT00760000118860.
HOGENOMi HOG000019301.
HOVERGENi HBG100808.
InParanoidi Q9Y6N6.
KOi K06247.
OMAi QRGRRCE.
OrthoDBi EOG7SR4KJ.
PhylomeDBi Q9Y6N6.
TreeFami TF352481.

Enzyme and pathway databases

Reactomei REACT_163874. Non-integrin membrane-ECM interactions.
REACT_169262. Laminin interactions.

Miscellaneous databases

ChiTaRSi LAMC3. human.
GeneWikii LAMC3.
GenomeRNAii 10319.
NextBioi 39119.
PROi Q9Y6N6.
SOURCEi Search...

Gene expression databases

Bgeei Q9Y6N6.
CleanExi HS_LAMC3.
ExpressionAtlasi Q9Y6N6. baseline and differential.
Genevestigatori Q9Y6N6.

Family and domain databases

Gene3Di 2.60.120.260. 1 hit.
InterProi IPR002049. EGF_laminin.
IPR008979. Galactose-bd-like.
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.
SM00136. LamNT. 1 hit.
[Graphical view ]
PROSITEi PS00022. EGF_1. 7 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. "Characterization and expression of the laminin gamma3 chain: a novel, non-basement membrane-associated, laminin chain."
    Koch M., Olson P.F., Albus A., Jin W., Hunter D.D., Brunken W.J., Burgeson R.E., Champliaud M.-F.
    J. Cell Biol. 145:605-618(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANTS SER-522; GLY-544; GLY-770 AND GLY-1082.
    Tissue: Placenta.
  2. "DNA sequence and analysis of human chromosome 9."
    Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S., Bagguley C.L.
    , Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A., Frankland J.A., French L., Fricker D.G., Garner P., Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S., Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E., Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D., Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E., Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K., Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M., Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J., Dunham I.
    Nature 429:369-374(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  3. "Homo sapiens protein coding cDNA."
    Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S., Ohara O., Nagase T., Kikuno R.F.
    Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 197-1575, VARIANTS GLY-544; GLY-770 AND GLY-1082.
    Tissue: Spleen.
  4. Cited for: VARIANT OCCM ARG-350.

Entry informationi

Entry nameiLAMC3_HUMAN
AccessioniPrimary (citable) accession number: Q9Y6N6
Secondary accession number(s): B1APX9, B1APY0, Q59H72
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 13, 2001
Last sequence update: October 5, 2010
Last modified: October 29, 2014
This is version 132 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 9
    Human chromosome 9: 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

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