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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
Complete GO annotation...

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-SubCell
  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.
Note: The disease is caused by mutations affecting the gene represented in this entry.1 Publication
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 – 1919 Reviewed prediction
Add
BLAST
Chaini20 – 15751556Laminin subunit gamma-3
PRO_0000017079Add
BLAST

Amino acid modifications

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

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

ArrayExpressiQ9Y6N6.
BgeeiQ9Y6N6.
CleanExiHS_LAMC3.
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.

Family & Domainsi

Domains and Repeats

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

Region

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

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili1073 – 113462 Reviewed prediction
Add
BLAST
Coiled coili1201 – 122828 Reviewed prediction
Add
BLAST
Coiled coili1410 – 149283 Reviewed prediction
Add
BLAST
Coiled coili1523 – 156745 Reviewed prediction
Add
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi1059 – 10613Cell attachment site Reviewed prediction

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

Keywords - Domaini

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

Phylogenomic databases

eggNOGiNOG235720.
HOGENOMiHOG000019301.
HOVERGENiHBG100808.
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

MAAAALLLGL ALLAPRAAGA GMGACYDGAG RPQRCLPVFE NAAFGRLAQA     50
SHTCGSPPED FCPHVGAAGA GAHCQRCDAA DPQRHHNASY LTDFHSQDES 100
TWWQSPSMAF GVQYPTSVNI TLRLGKAYEI TYVRLKFHTS RPESFAIYKR 150
SRADGPWEPY QFYSASCQKT YGRPEGQYLR PGEDERVAFC TSEFSDISPL 200
SGGNVAFSTL EGRPSAYNFE ESPGLQEWVT STELLISLDR LNTFGDDIFK 250
DPKVLQSYYY AVSDFSVGGR CKCNGHASEC GPDVAGQLAC RCQHNTTGTD 300
CERCLPFFQD RPWARGTAEA AHECLPCNCS GRSEECTFDR ELFRSTGHGG 350
RCHHCRDHTA GPHCERCQEN FYHWDPRMPC QPCDCQSAGS LHLQCDDTGT 400
CACKPTVTGW KCDRCLPGFH SLSEGGCRPC TCNPAGSLDT CDPRSGRCPC 450
KENVEGNLCD RCRPGTFNLQ PHNPAGCSSC FCYGHSKVCA STAQFQVHHI 500
LSDFHQGAEG WWARSVGGSE HPPQWSPNGV LLSPEDEEEL TAPEKFLGDQ 550
RFSYGQPLIL TFRVPPGDSP LPVQLRLEGT GLALSLRHSS LSGPQDAGHP 600
REVELRFHLQ ETSEDVAPPL PPFHFQRLLA NLTSLRLRVS PGPSPAGPVF 650
LTEVRLTSAR PGLSPPASWV EICSCPTGYT GQFCESCAPG YKREMPQGGP 700
YASCVPCTCN QHGTCDPNTG ICVCSHHTEG PSCERCLPGF YGNPFAGQAD 750
DCQPCPCPGQ SACTTIPESR EVVCTHCPPG QRGRRCEVCD DGFFGDPLGL 800
FGHPQPCHQC QCSGNVDPNA VGNCDPLSGH CLRCLHNTTG DHCEHCQEGF 850
YGSALAPRPA DKCMPCSCHP QGSVSEQMPC DPVTGQCSCL PHVTARDCSR 900
CYPGFFDLQP GRGCRSCKCH PLGSQEDQCH PKTGQCTCRP GVTGQACDRC 950
QLGFFGFSIK GCRACRCSPL GAASAQCHEN GTCVCRPGFE GYKCDRCHDN 1000
FFLTADGTHC QQCPSCYALV KEEAAKLKAR LTLTEGWLQG SDCGSPWGPL 1050
DILLGEAPRG DVYQGHHLLP GAREAFLEQM MSLEGAVKAA REQLQRLNKG 1100
ARCAQAGSQK TCTQLADLEA VLESSEEEIL HAAAILASLE IPQEGPSQPT 1150
KWSHLATEAR ALARSHRDTA TKIAATAWRA LLASNTSYAL LWNLLEGRVA 1200
LETQRDLEDR YQEVQAAQKA LRTAVAEVLP EAESVLATVQ QVGADTAPYL 1250
ALLASPGALP QKSRAEDLGL KAKALEKTVA SWQHMATEAA RTLQTAAQAT 1300
LRQTEPLTKL HQEARAALTQ ASSSVQAATV TVMGARTLLA DLEGMKLQFP 1350
RPKDQAALQR KADSVSDRLL ADTRKKTKQA ERMLGNAAPL SSSAKKKGRE 1400
AEVLAKDSAK LAKALLRERK QAHRRASRLT SQTQATLQQA SQQVLASEAR 1450
RQELEEAERV GAGLSEMEQQ IRESRISLEK DIETLSELLA RLGSLDTHQA 1500
PAQALNETQW ALERLRLQLG SPGSLQRKLS LLEQESQQQE LQIQGFESDL 1550
AEIRADKQNL EAILHSLPEN CASWQ 1575
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.

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 conflict

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

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...

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.
HOGENOMi HOG000019301.
HOVERGENi HBG100808.
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

ArrayExpressi Q9Y6N6.
Bgeei Q9Y6N6.
CleanExi HS_LAMC3.
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: September 3, 2014
This is version 130 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

Dasty 3

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