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Q13753

- LAMC2_HUMAN

UniProt

Q13753 - LAMC2_HUMAN

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Protein

Laminin subunit gamma-2

Gene

LAMC2

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. Ladsin exerts cell-scattering activity toward a wide variety of cells, including epithelial, endothelial, and fibroblastic cells.1 Publication

GO - Molecular functioni

  1. heparin binding Source: UniProtKB-KW

GO - Biological processi

  1. cell adhesion Source: UniProtKB-KW
  2. cell junction assembly Source: Reactome
  3. epidermis development Source: ProtInc
  4. extracellular matrix disassembly Source: Reactome
  5. extracellular matrix organization Source: Reactome
  6. hemidesmosome assembly Source: Reactome
Complete GO annotation...

Keywords - Biological processi

Cell adhesion

Keywords - Ligandi

Heparin-binding

Enzyme and pathway databases

ReactomeiREACT_118572. Degradation of the extracellular matrix.
REACT_150180. Assembly of collagen fibrils and other multimeric structures.
REACT_150268. Anchoring fibril formation.
REACT_163874. Non-integrin membrane-ECM interactions.
REACT_169262. Laminin interactions.
REACT_20537. Type I hemidesmosome assembly.

Names & Taxonomyi

Protein namesi
Recommended name:
Laminin subunit gamma-2
Alternative name(s):
Cell-scattering factor 140 kDa subunit
Short name:
CSF 140 kDa subunit
Epiligrin subunit gamma
Kalinin subunit gamma
Kalinin/nicein/epiligrin 100 kDa subunit
Ladsin 140 kDa subunit
Laminin B2t chain
Laminin-5 subunit gamma
Large adhesive scatter factor 140 kDa subunit
Nicein subunit gamma
Gene namesi
Name:LAMC2
Synonyms:LAMB2T, LAMNB2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 1

Organism-specific databases

HGNCiHGNC:6493. LAMC2.

Subcellular locationi

GO - Cellular componenti

  1. cell cortex Source: Ensembl
  2. extracellular region Source: Reactome
  3. extracellular space Source: Ensembl
  4. laminin-2 complex Source: Ensembl
  5. laminin-5 complex Source: Ensembl
  6. membrane Source: Ensembl
  7. perinuclear region of cytoplasm Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Basement membrane, Extracellular matrix, Secreted

Pathology & Biotechi

Involvement in diseasei

Epidermolysis bullosa, junctional, Herlitz type (H-JEB) [MIM:226700]: An infantile and lethal form of junctional epidermolysis bullosa, a group of blistering skin diseases characterized by tissue separation which occurs within the dermo-epidermal basement In the Herlitz type, death occurs usually within the first six months of life. Occasionally, children survive to teens. It is marked by bullous lesions at birth and extensive denudation of skin and mucous membranes that may be hemorrhagic.
Note: The disease is caused by mutations affecting the gene represented in this entry.

Keywords - Diseasei

Epidermolysis bullosa

Organism-specific databases

MIMi226700. phenotype.
Orphaneti79402. Generalized junctional epidermolysis bullosa, non-Herlitz type.
79405. Junctional epidermolysis bullosa inversa.
79404. Junctional epidermolysis bullosa, Herlitz type.
PharmGKBiPA30281.

Protein family/group databases

Allergomei8331. Hom s Laminin gamma_2.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2121Sequence AnalysisAdd
BLAST
Chaini22 – 11931172Laminin subunit gamma-2PRO_0000017077Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi28 ↔ 37PROSITE-ProRule annotation
Disulfide bondi30 ↔ 53PROSITE-ProRule annotation
Disulfide bondi56 ↔ 65PROSITE-ProRule annotation
Disulfide bondi68 ↔ 81PROSITE-ProRule annotation
Disulfide bondi84 ↔ 96PROSITE-ProRule annotation
Disulfide bondi86 ↔ 102PROSITE-ProRule annotation
Disulfide bondi104 ↔ 113PROSITE-ProRule annotation
Disulfide bondi116 ↔ 128PROSITE-ProRule annotation
Disulfide bondi139 ↔ 150PROSITE-ProRule annotation
Disulfide bondi141 ↔ 155PROSITE-ProRule annotation
Disulfide bondi157 ↔ 166PROSITE-ProRule annotation
Disulfide bondi169 ↔ 184PROSITE-ProRule annotation
Glycosylationi342 – 3421N-linked (GlcNAc...)Sequence Analysis
Glycosylationi362 – 3621N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi462 ↔ 470PROSITE-ProRule annotation
Disulfide bondi464 ↔ 481PROSITE-ProRule annotation
Disulfide bondi484 ↔ 493PROSITE-ProRule annotation
Disulfide bondi496 ↔ 514PROSITE-ProRule annotation
Disulfide bondi517 ↔ 531PROSITE-ProRule annotation
Disulfide bondi519 ↔ 538PROSITE-ProRule annotation
Disulfide bondi541 ↔ 550PROSITE-ProRule annotation
Disulfide bondi553 ↔ 570PROSITE-ProRule annotation
Disulfide bondi573 ↔ 585PROSITE-ProRule annotation
Disulfide bondi575 ↔ 591PROSITE-ProRule annotation
Disulfide bondi593 ↔ 602PROSITE-ProRule annotation
Disulfide bondi609 – 609InterchainCurated
Disulfide bondi612 – 612InterchainCurated
Glycosylationi942 – 9421N-linked (GlcNAc...)Sequence Analysis
Glycosylationi1033 – 10331N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi1184 – 1184InterchainCurated

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

MaxQBiQ13753.
PaxDbiQ13753.
PeptideAtlasiQ13753.
PRIDEiQ13753.

PTM databases

PhosphoSiteiQ13753.

Miscellaneous databases

PMAP-CutDBQ13753.

Expressioni

Tissue specificityi

The large variant is expressed only in specific epithelial cells of embryonic and neonatal tissues. In 17-week old embryo the small variant is found in cerebral cortex, lung, and distal tubes of kidney, but not in epithelia except for distal tubuli.

Gene expression databases

BgeeiQ13753.
CleanExiHS_LAMC2.
GenevestigatoriQ13753.

Organism-specific databases

HPAiCAB004257.
HPA024638.

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-2 is a subunit of laminin-5 (laminin-332 or epiligrin/kalinin/nicein).

Protein-protein interaction databases

BioGridi110112. 6 interactions.
DIPiDIP-190N.
IntActiQ13753. 1 interaction.
MINTiMINT-4053464.
STRINGi9606.ENSP00000264144.

Structurei

3D structure databases

ProteinModelPortaliQ13753.
SMRiQ13753. Positions 6-168, 384-604.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini28 – 8356Laminin EGF-like 1PROSITE-ProRule annotationAdd
BLAST
Domaini84 – 13047Laminin EGF-like 2PROSITE-ProRule annotationAdd
BLAST
Domaini139 – 18648Laminin EGF-like 3PROSITE-ProRule annotationAdd
BLAST
Domaini187 – 19610Laminin EGF-like 4; first partPROSITE-ProRule annotation
Domaini213 – 381169Laminin IV type APROSITE-ProRule annotationAdd
BLAST
Domaini382 – 41534Laminin EGF-like 4; second partPROSITE-ProRule annotationAdd
BLAST
Domaini416 – 46146Laminin EGF-like 5PROSITE-ProRule annotationAdd
BLAST
Domaini462 – 51655Laminin EGF-like 6PROSITE-ProRule annotationAdd
BLAST
Domaini517 – 57256Laminin EGF-like 7PROSITE-ProRule annotationAdd
BLAST
Domaini573 – 60230Laminin EGF-like 8; truncatedPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni603 – 1193591Domain II and IAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili611 – 718108Sequence AnalysisAdd
BLAST
Coiled coili811 – 1076266Sequence AnalysisAdd
BLAST
Coiled coili1117 – 119377Sequence AnalysisAdd
BLAST

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 8 laminin EGF-like domains.PROSITE-ProRule annotation
Contains 1 laminin IV type A domain.PROSITE-ProRule annotation

Keywords - Domaini

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

Phylogenomic databases

eggNOGiNOG285700.
GeneTreeiENSGT00760000118860.
HOVERGENiHBG062127.
InParanoidiQ13753.
KOiK06246.
OMAiDRCLPCN.
OrthoDBiEOG7SR4KJ.
PhylomeDBiQ13753.

Family and domain databases

InterProiIPR002049. EGF_laminin.
IPR018031. Laminin_B_subgr.
IPR000034. Laminin_B_type_IV.
[Graphical view]
PfamiPF00052. Laminin_B. 1 hit.
PF00053. Laminin_EGF. 7 hits.
[Graphical view]
SMARTiSM00180. EGF_Lam. 6 hits.
SM00281. LamB. 1 hit.
[Graphical view]
PROSITEiPS00022. EGF_1. 4 hits.
PS01186. EGF_2. 2 hits.
PS01248. EGF_LAM_1. 6 hits.
PS50027. EGF_LAM_2. 6 hits.
PS51115. LAMININ_IVA. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform Long (identifier: Q13753-1) [UniParc]FASTAAdd to Basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MPALWLGCCL CFSLLLPAAR ATSRREVCDC NGKSRQCIFD RELHRQTGNG
60 70 80 90 100
FRCLNCNDNT DGIHCEKCKN GFYRHRERDR CLPCNCNSKG SLSARCDNSG
110 120 130 140 150
RCSCKPGVTG ARCDRCLPGF HMLTDAGCTQ DQRLLDSKCD CDPAGIAGPC
160 170 180 190 200
DAGRCVCKPA VTGERCDRCR SGYYNLDGGN PEGCTQCFCY GHSASCRSSA
210 220 230 240 250
EYSVHKITST FHQDVDGWKA VQRNGSPAKL QWSQRHQDVF SSAQRLDPVY
260 270 280 290 300
FVAPAKFLGN QQVSYGQSLS FDYRVDRGGR HPSAHDVILE GAGLRITAPL
310 320 330 340 350
MPLGKTLPCG LTKTYTFRLN EHPSNNWSPQ LSYFEYRRLL RNLTALRIRA
360 370 380 390 400
TYGEYSTGYI DNVTLISARP VSGAPAPWVE QCICPVGYKG QFCQDCASGY
410 420 430 440 450
KRDSARLGPF GTCIPCNCQG GGACDPDTGD CYSGDENPDI ECADCPIGFY
460 470 480 490 500
NDPHDPRSCK PCPCHNGFSC SVMPETEEVV CNNCPPGVTG ARCELCADGY
510 520 530 540 550
FGDPFGEHGP VRPCQPCQCN NNVDPSASGN CDRLTGRCLK CIHNTAGIYC
560 570 580 590 600
DQCKAGYFGD PLAPNPADKC RACNCNPMGS EPVGCRSDGT CVCKPGFGGP
610 620 630 640 650
NCEHGAFSCP ACYNQVKIQM DQFMQQLQRM EALISKAQGG DGVVPDTELE
660 670 680 690 700
GRMQQAEQAL QDILRDAQIS EGASRSLGLQ LAKVRSQENS YQSRLDDLKM
710 720 730 740 750
TVERVRALGS QYQNRVRDTH RLITQMQLSL AESEASLGNT NIPASDHYVG
760 770 780 790 800
PNGFKSLAQE ATRLAESHVE SASNMEQLTR ETEDYSKQAL SLVRKALHEG
810 820 830 840 850
VGSGSGSPDG AVVQGLVEKL EKTKSLAQQL TREATQAEIE ADRSYQHSLR
860 870 880 890 900
LLDSVSRLQG VSDQSFQVEE AKRIKQKADS LSSLVTRHMD EFKRTQKNLG
910 920 930 940 950
NWKEEAQQLL QNGKSGREKS DQLLSRANLA KSRAQEALSM GNATFYEVES
960 970 980 990 1000
ILKNLREFDL QVDNRKAEAE EAMKRLSYIS QKVSDASDKT QQAERALGSA
1010 1020 1030 1040 1050
AADAQRAKNG AGEALEISSE IEQEIGSLNL EANVTADGAL AMEKGLASLK
1060 1070 1080 1090 1100
SEMREVEGEL ERKELEFDTN MDAVQMVITE AQKVDTRAKN AGVTIQDTLN
1110 1120 1130 1140 1150
TLDGLLHLMD QPLSVDEEGL VLLEQKLSRA KTQINSQLRP MMSELEERAR
1160 1170 1180 1190
QQRGHLHLLE TSIDGILADV KNLENIRDNL PPGCYNTQAL EQQ
Length:1,193
Mass (Da):130,976
Last modified:March 7, 2006 - v2
Checksum:i0BBE1A56516C5C9A
GO
Isoform Short (identifier: Q13753-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1110-1193: DQPLSVDEEG...CYNTQALEQQ → GM

Show »
Length:1,111
Mass (Da):121,604
Checksum:i7762993F3D7F89DF
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti12 – 121F → L in CAA52108. (PubMed:8306988)Curated
Sequence conflicti473 – 4731M → I in CAA78728. (PubMed:1383240)Curated
Sequence conflicti473 – 4731M → I in CAA78729. (PubMed:1383240)Curated
Sequence conflicti521 – 5211N → S in CAA78728. (PubMed:1383240)Curated
Sequence conflicti521 – 5211N → S in CAA78729. (PubMed:1383240)Curated
Sequence conflicti857 – 8571R → P in CAA78728. (PubMed:1383240)Curated
Sequence conflicti857 – 8571R → P in CAA78729. (PubMed:1383240)Curated
Sequence conflicti883 – 8831S → T in AAC50457. (PubMed:8786121)Curated
Sequence conflicti883 – 8831S → T in AAC50456. (PubMed:8786121)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti111 – 1111A → P.
Corresponds to variant rs12065473 [ dbSNP | Ensembl ].
VAR_050081
Natural varianti115 – 1151R → Q.
Corresponds to variant rs17481405 [ dbSNP | Ensembl ].
VAR_050082
Natural varianti124 – 1241T → M.
Corresponds to variant rs11586699 [ dbSNP | Ensembl ].
VAR_050083
Natural varianti136 – 1361D → V.
Corresponds to variant rs12037099 [ dbSNP | Ensembl ].
VAR_050084
Natural varianti247 – 2471D → E.
Corresponds to variant rs2296306 [ dbSNP | Ensembl ].
VAR_022017
Natural varianti608 – 6081S → I.
Corresponds to variant rs4373715 [ dbSNP | Ensembl ].
VAR_050085
Natural varianti733 – 7331S → T.
Corresponds to variant rs2296303 [ dbSNP | Ensembl ].
VAR_020304

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1110 – 119384DQPLS…ALEQQ → GM in isoform Short. 1 PublicationVSP_003040Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z15008 mRNA. Translation: CAA78728.1.
Z15009 mRNA. Translation: CAA78729.1.
X73902 mRNA. Translation: CAA52108.1.
U31201
, U31178, U31179, U31180, U31181, U31182, U31183, U31184, U31186, U31187, U31188, U31189, U31190, U31191, U31192, U31193, U31194, U31195, U31196, U31197, U31198, U31199 Genomic DNA. Translation: AAC50457.1.
U31200
, U31178, U31179, U31180, U31181, U31182, U31183, U31184, U31186, U31187, U31188, U31189, U31190, U31191, U31192, U31193, U31194, U31195, U31196, U31197, U31198 Genomic DNA. Translation: AAC50456.1.
AL354953 Genomic DNA. Translation: CAH70980.1.
CH471067 Genomic DNA. Translation: EAW91146.1.
BC112286 mRNA. Translation: AAI12287.1.
BC113378 mRNA. Translation: AAI13379.1.
CCDSiCCDS1352.1. [Q13753-1]
CCDS44285.1. [Q13753-2]
PIRiA44018.
RefSeqiNP_005553.2. NM_005562.2. [Q13753-1]
NP_061486.2. NM_018891.2. [Q13753-2]
UniGeneiHs.591484.

Genome annotation databases

EnsembliENST00000264144; ENSP00000264144; ENSG00000058085. [Q13753-1]
ENST00000493293; ENSP00000432063; ENSG00000058085. [Q13753-2]
GeneIDi3918.
KEGGihsa:3918.
UCSCiuc001gpz.4. human. [Q13753-2]
uc001gqa.2. human. [Q13753-1]

Polymorphism databases

DMDMi90185107.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z15008 mRNA. Translation: CAA78728.1 .
Z15009 mRNA. Translation: CAA78729.1 .
X73902 mRNA. Translation: CAA52108.1 .
U31201
, U31178 , U31179 , U31180 , U31181 , U31182 , U31183 , U31184 , U31186 , U31187 , U31188 , U31189 , U31190 , U31191 , U31192 , U31193 , U31194 , U31195 , U31196 , U31197 , U31198 , U31199 Genomic DNA. Translation: AAC50457.1 .
U31200
, U31178 , U31179 , U31180 , U31181 , U31182 , U31183 , U31184 , U31186 , U31187 , U31188 , U31189 , U31190 , U31191 , U31192 , U31193 , U31194 , U31195 , U31196 , U31197 , U31198 Genomic DNA. Translation: AAC50456.1 .
AL354953 Genomic DNA. Translation: CAH70980.1 .
CH471067 Genomic DNA. Translation: EAW91146.1 .
BC112286 mRNA. Translation: AAI12287.1 .
BC113378 mRNA. Translation: AAI13379.1 .
CCDSi CCDS1352.1. [Q13753-1 ]
CCDS44285.1. [Q13753-2 ]
PIRi A44018.
RefSeqi NP_005553.2. NM_005562.2. [Q13753-1 ]
NP_061486.2. NM_018891.2. [Q13753-2 ]
UniGenei Hs.591484.

3D structure databases

ProteinModelPortali Q13753.
SMRi Q13753. Positions 6-168, 384-604.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 110112. 6 interactions.
DIPi DIP-190N.
IntActi Q13753. 1 interaction.
MINTi MINT-4053464.
STRINGi 9606.ENSP00000264144.

Chemistry

ChEMBLi CHEMBL2364187.

Protein family/group databases

Allergomei 8331. Hom s Laminin gamma_2.

PTM databases

PhosphoSitei Q13753.

Polymorphism databases

DMDMi 90185107.

Proteomic databases

MaxQBi Q13753.
PaxDbi Q13753.
PeptideAtlasi Q13753.
PRIDEi Q13753.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000264144 ; ENSP00000264144 ; ENSG00000058085 . [Q13753-1 ]
ENST00000493293 ; ENSP00000432063 ; ENSG00000058085 . [Q13753-2 ]
GeneIDi 3918.
KEGGi hsa:3918.
UCSCi uc001gpz.4. human. [Q13753-2 ]
uc001gqa.2. human. [Q13753-1 ]

Organism-specific databases

CTDi 3918.
GeneCardsi GC01P183155.
GeneReviewsi LAMC2.
HGNCi HGNC:6493. LAMC2.
HPAi CAB004257.
HPA024638.
MIMi 150292. gene.
226700. phenotype.
neXtProti NX_Q13753.
Orphaneti 79402. Generalized junctional epidermolysis bullosa, non-Herlitz type.
79405. Junctional epidermolysis bullosa inversa.
79404. Junctional epidermolysis bullosa, Herlitz type.
PharmGKBi PA30281.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG285700.
GeneTreei ENSGT00760000118860.
HOVERGENi HBG062127.
InParanoidi Q13753.
KOi K06246.
OMAi DRCLPCN.
OrthoDBi EOG7SR4KJ.
PhylomeDBi Q13753.

Enzyme and pathway databases

Reactomei REACT_118572. Degradation of the extracellular matrix.
REACT_150180. Assembly of collagen fibrils and other multimeric structures.
REACT_150268. Anchoring fibril formation.
REACT_163874. Non-integrin membrane-ECM interactions.
REACT_169262. Laminin interactions.
REACT_20537. Type I hemidesmosome assembly.

Miscellaneous databases

ChiTaRSi LAMC2. human.
GeneWikii Laminin,_gamma_2.
GenomeRNAii 3918.
NextBioi 15391.
PMAP-CutDB Q13753.
PROi Q13753.
SOURCEi Search...

Gene expression databases

Bgeei Q13753.
CleanExi HS_LAMC2.
Genevestigatori Q13753.

Family and domain databases

InterProi IPR002049. EGF_laminin.
IPR018031. Laminin_B_subgr.
IPR000034. Laminin_B_type_IV.
[Graphical view ]
Pfami PF00052. Laminin_B. 1 hit.
PF00053. Laminin_EGF. 7 hits.
[Graphical view ]
SMARTi SM00180. EGF_Lam. 6 hits.
SM00281. LamB. 1 hit.
[Graphical view ]
PROSITEi PS00022. EGF_1. 4 hits.
PS01186. EGF_2. 2 hits.
PS01248. EGF_LAM_1. 6 hits.
PS50027. EGF_LAM_2. 6 hits.
PS51115. LAMININ_IVA. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "A truncated laminin chain homologous to the B2 chain: structure, spatial expression, and chromosomal assignment."
    Kallunki P., Sainio K., Eddy R., Byers M., Kallunki T., Sariola H., Beck K., Hirvonen H., Shows T.B., Tryggvason K.
    J. Cell Biol. 119:679-693(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], ALTERNATIVE SPLICING.
    Tissue: Fibrosarcoma.
  2. Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 1090-1114.
    Tissue: Epidermis and Keratinocyte.
  3. "Structure of the human laminin gamma 2 chain gene (LAMC2): alternative splicing with different tissue distribution of two transcripts."
    Airenne T., Haakana H., Sainio K., Kallunki T., Kallunki P., Sariola H., Tryggvason K.
    Genomics 32:54-64(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], ALTERNATIVE SPLICING.
    Tissue: Placenta.
  4. "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].
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM SHORT).
    Tissue: Cerebellum.
  7. "A large cell-adhesive scatter factor secreted by human gastric carcinoma cells."
    Miyazaki K., Kikkawa Y., Nakamura A., Yasumitsu H., Umeda M.
    Proc. Natl. Acad. Sci. U.S.A. 90:11767-11771(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE OF 435-449, FUNCTION, HEPARIN-BINDING.
  8. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiLAMC2_HUMAN
AccessioniPrimary (citable) accession number: Q13753
Secondary accession number(s): Q02536
, Q02537, Q13752, Q14941, Q14DF7, Q2M1N2, Q5VYE8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: March 7, 2006
Last modified: October 29, 2014
This is version 155 of the entry and version 2 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

Miscellaneous

Binds heparin.By similarity

Keywords - Technical termi

Complete proteome, Direct protein sequencing, 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