Q13753 (LAMC2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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 names

Name:	LAMC2
Synonyms:	LAMB2T, LAMNB2

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	1193 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	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. Ref.7
Subunit structure	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).
Subcellular location	Secreted › extracellular space › extracellular matrix › basement membrane. Note: Major component.
Tissue specificity	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.
Domain	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.
Involvement in disease	Defects in LAMC2 are a cause of epidermolysis bullosa junctional Herlitz type (H-JEB) [MIM:226700]; also known as junctional epidermolysis bullosa Herlitz-Pearson type. JEB defines a group of blistering skin diseases characterized by tissue separation which occurs within the dermo-epidermal basement membrane. H-JEB is a severe, infantile and lethal form. Death occurs usually within the first six months of life. Occasionally, children survive to teens. H-JEB is marked by bullous lesions at birth and extensive denudation of skin and mucous membranes that may be hemorrhagic.
Miscellaneous	Binds heparin By similarity.
Sequence similarities	Contains 8 laminin EGF-like domains. Contains 1 laminin IV type A domain.

Ontologies

Keywords
Biological process	Cell adhesion
Cellular component	Basement membrane Extracellular matrix Secreted
Coding sequence diversity	Alternative splicing Polymorphism
Disease	Epidermolysis bullosa
Domain	Coiled coil Laminin EGF-like domain Repeat Signal
Ligand	Heparin-binding
PTM	Disulfide bond Glycoprotein Phosphoprotein
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological process	cell adhesion Inferred from electronic annotation. Source: UniProtKB-KW epidermis development Traceable author statement. Source: ProtInc hemidesmosome assembly Traceable author statement. Source: Reactome
Molecular function	heparin binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform Long (identifier: Q13753-1)

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.

Isoform Short (identifier: Q13753-2)

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

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 21	21	Potential
	Chain	22 – 1193	1172	Laminin subunit gamma-2		PRO_0000017077
Regions
	Domain	28 – 83	56	Laminin EGF-like 1
	Domain	84 – 130	47	Laminin EGF-like 2
	Domain	139 – 186	48	Laminin EGF-like 3
	Domain	187 – 196	10	Laminin EGF-like 4; first part
	Domain	213 – 381	169	Laminin IV type A
	Domain	382 – 415	34	Laminin EGF-like 4; second part
	Domain	416 – 461	46	Laminin EGF-like 5
	Domain	462 – 516	55	Laminin EGF-like 6
	Domain	517 – 572	56	Laminin EGF-like 7
	Domain	573 – 602	30	Laminin EGF-like 8; truncated
	Region	603 – 1193	591	Domain II and I
	Coiled coil	611 – 718	108	Potential
	Coiled coil	811 – 1076	266	Potential
	Coiled coil	1117 – 1193	77	Potential
Amino acid modifications
	Modified residue	250	1	Phosphotyrosine Ref.8
	Modified residue	265	1	Phosphotyrosine Ref.8
	Modified residue	273	1	Phosphotyrosine Ref.8
	Glycosylation	342	1	N-linked (GlcNAc...) Potential
	Glycosylation	362	1	N-linked (GlcNAc...) Potential
	Glycosylation	942	1	N-linked (GlcNAc...) Potential
	Glycosylation	1033	1	N-linked (GlcNAc...) Potential
	Disulfide bond	28 ↔ 37		By similarity
	Disulfide bond	30 ↔ 53		By similarity
	Disulfide bond	56 ↔ 65		By similarity
	Disulfide bond	68 ↔ 81		By similarity
	Disulfide bond	84 ↔ 96		By similarity
	Disulfide bond	86 ↔ 102		By similarity
	Disulfide bond	104 ↔ 113		By similarity
	Disulfide bond	116 ↔ 128		By similarity
	Disulfide bond	139 ↔ 150		By similarity
	Disulfide bond	141 ↔ 155		By similarity
	Disulfide bond	157 ↔ 166		By similarity
	Disulfide bond	169 ↔ 184		By similarity
	Disulfide bond	462 ↔ 470		By similarity
	Disulfide bond	464 ↔ 481		By similarity
	Disulfide bond	484 ↔ 493		By similarity
	Disulfide bond	496 ↔ 514		By similarity
	Disulfide bond	517 ↔ 531		By similarity
	Disulfide bond	519 ↔ 538		By similarity
	Disulfide bond	541 ↔ 550		By similarity
	Disulfide bond	553 ↔ 570		By similarity
	Disulfide bond	573 ↔ 585		By similarity
	Disulfide bond	575 ↔ 591		By similarity
	Disulfide bond	593 ↔ 602		By similarity
	Disulfide bond	609		Interchain Probable
	Disulfide bond	612		Interchain Probable
	Disulfide bond	1184		Interchain Probable
Natural variations
	Alternative sequence	1110 – 1193	84	DQPLS…ALEQQ → GM in isoform Short.		VSP_003040
	Natural variant	111	1	A → P. Corresponds to variant rs12065473 [ dbSNP | Ensembl ].		VAR_050081
	Natural variant	115	1	R → Q. Corresponds to variant rs17481405 [ dbSNP | Ensembl ].		VAR_050082
	Natural variant	124	1	T → M. Corresponds to variant rs11586699 [ dbSNP | Ensembl ].		VAR_050083
	Natural variant	136	1	D → V. Corresponds to variant rs12037099 [ dbSNP | Ensembl ].		VAR_050084
	Natural variant	247	1	D → E. Corresponds to variant rs2296306 [ dbSNP | Ensembl ].		VAR_022017
	Natural variant	608	1	S → I. Corresponds to variant rs4373715 [ dbSNP | Ensembl ].		VAR_050085
	Natural variant	733	1	S → T. Corresponds to variant rs2296303 [ dbSNP | Ensembl ].		VAR_020304
Experimental info
	Sequence conflict	12	1	F → L in CAA52108. Ref.2
	Sequence conflict	473	1	M → I in CAA78728. Ref.1
	Sequence conflict	473	1	M → I in CAA78729. Ref.1
	Sequence conflict	521	1	N → S in CAA78728. Ref.1
	Sequence conflict	521	1	N → S in CAA78729. Ref.1
	Sequence conflict	857	1	R → P in CAA78728. Ref.1
	Sequence conflict	857	1	R → P in CAA78729. Ref.1
	Sequence conflict	883	1	S → T in AAC50457. Ref.3
	Sequence conflict	883	1	S → T in AAC50456. Ref.3

Sequences

	Sequence		Length	Mass (Da)
	Isoform Long [UniParc]. Last modified March 7, 2006. Version 2. Checksum: 0BBE1A56516C5C9A	FASTA	1,193	130,976
	10 20 30 40 50 60 MPALWLGCCL CFSLLLPAAR ATSRREVCDC NGKSRQCIFD RELHRQTGNG FRCLNCNDNT 70 80 90 100 110 120 DGIHCEKCKN GFYRHRERDR CLPCNCNSKG SLSARCDNSG RCSCKPGVTG ARCDRCLPGF 130 140 150 160 170 180 HMLTDAGCTQ DQRLLDSKCD CDPAGIAGPC DAGRCVCKPA VTGERCDRCR SGYYNLDGGN 190 200 210 220 230 240 PEGCTQCFCY GHSASCRSSA EYSVHKITST FHQDVDGWKA VQRNGSPAKL QWSQRHQDVF 250 260 270 280 290 300 SSAQRLDPVY FVAPAKFLGN QQVSYGQSLS FDYRVDRGGR HPSAHDVILE GAGLRITAPL 310 320 330 340 350 360 MPLGKTLPCG LTKTYTFRLN EHPSNNWSPQ LSYFEYRRLL RNLTALRIRA TYGEYSTGYI 370 380 390 400 410 420 DNVTLISARP VSGAPAPWVE QCICPVGYKG QFCQDCASGY KRDSARLGPF GTCIPCNCQG 430 440 450 460 470 480 GGACDPDTGD CYSGDENPDI ECADCPIGFY NDPHDPRSCK PCPCHNGFSC SVMPETEEVV 490 500 510 520 530 540 CNNCPPGVTG ARCELCADGY FGDPFGEHGP VRPCQPCQCN NNVDPSASGN CDRLTGRCLK 550 560 570 580 590 600 CIHNTAGIYC DQCKAGYFGD PLAPNPADKC RACNCNPMGS EPVGCRSDGT CVCKPGFGGP 610 620 630 640 650 660 NCEHGAFSCP ACYNQVKIQM DQFMQQLQRM EALISKAQGG DGVVPDTELE GRMQQAEQAL 670 680 690 700 710 720 QDILRDAQIS EGASRSLGLQ LAKVRSQENS YQSRLDDLKM TVERVRALGS QYQNRVRDTH 730 740 750 760 770 780 RLITQMQLSL AESEASLGNT NIPASDHYVG PNGFKSLAQE ATRLAESHVE SASNMEQLTR 790 800 810 820 830 840 ETEDYSKQAL SLVRKALHEG VGSGSGSPDG AVVQGLVEKL EKTKSLAQQL TREATQAEIE 850 860 870 880 890 900 ADRSYQHSLR LLDSVSRLQG VSDQSFQVEE AKRIKQKADS LSSLVTRHMD EFKRTQKNLG 910 920 930 940 950 960 NWKEEAQQLL QNGKSGREKS DQLLSRANLA KSRAQEALSM GNATFYEVES ILKNLREFDL 970 980 990 1000 1010 1020 QVDNRKAEAE EAMKRLSYIS QKVSDASDKT QQAERALGSA AADAQRAKNG AGEALEISSE 1030 1040 1050 1060 1070 1080 IEQEIGSLNL EANVTADGAL AMEKGLASLK SEMREVEGEL ERKELEFDTN MDAVQMVITE 1090 1100 1110 1120 1130 1140 AQKVDTRAKN AGVTIQDTLN TLDGLLHLMD QPLSVDEEGL VLLEQKLSRA KTQINSQLRP 1150 1160 1170 1180 1190 MMSELEERAR QQRGHLHLLE TSIDGILADV KNLENIRDNL PPGCYNTQAL EQQ
	Isoform Short [UniParc]. Checksum: 7762993F3D7F89DF	FASTA	1,111	121,604
	10 20 30 40 50 60 MPALWLGCCL CFSLLLPAAR ATSRREVCDC NGKSRQCIFD RELHRQTGNG FRCLNCNDNT 70 80 90 100 110 120 DGIHCEKCKN GFYRHRERDR CLPCNCNSKG SLSARCDNSG RCSCKPGVTG ARCDRCLPGF 130 140 150 160 170 180 HMLTDAGCTQ DQRLLDSKCD CDPAGIAGPC DAGRCVCKPA VTGERCDRCR SGYYNLDGGN 190 200 210 220 230 240 PEGCTQCFCY GHSASCRSSA EYSVHKITST FHQDVDGWKA VQRNGSPAKL QWSQRHQDVF 250 260 270 280 290 300 SSAQRLDPVY FVAPAKFLGN QQVSYGQSLS FDYRVDRGGR HPSAHDVILE GAGLRITAPL 310 320 330 340 350 360 MPLGKTLPCG LTKTYTFRLN EHPSNNWSPQ LSYFEYRRLL RNLTALRIRA TYGEYSTGYI 370 380 390 400 410 420 DNVTLISARP VSGAPAPWVE QCICPVGYKG QFCQDCASGY KRDSARLGPF GTCIPCNCQG 430 440 450 460 470 480 GGACDPDTGD CYSGDENPDI ECADCPIGFY NDPHDPRSCK PCPCHNGFSC SVMPETEEVV 490 500 510 520 530 540 CNNCPPGVTG ARCELCADGY FGDPFGEHGP VRPCQPCQCN NNVDPSASGN CDRLTGRCLK 550 560 570 580 590 600 CIHNTAGIYC DQCKAGYFGD PLAPNPADKC RACNCNPMGS EPVGCRSDGT CVCKPGFGGP 610 620 630 640 650 660 NCEHGAFSCP ACYNQVKIQM DQFMQQLQRM EALISKAQGG DGVVPDTELE GRMQQAEQAL 670 680 690 700 710 720 QDILRDAQIS EGASRSLGLQ LAKVRSQENS YQSRLDDLKM TVERVRALGS QYQNRVRDTH 730 740 750 760 770 780 RLITQMQLSL AESEASLGNT NIPASDHYVG PNGFKSLAQE ATRLAESHVE SASNMEQLTR 790 800 810 820 830 840 ETEDYSKQAL SLVRKALHEG VGSGSGSPDG AVVQGLVEKL EKTKSLAQQL TREATQAEIE 850 860 870 880 890 900 ADRSYQHSLR LLDSVSRLQG VSDQSFQVEE AKRIKQKADS LSSLVTRHMD EFKRTQKNLG 910 920 930 940 950 960 NWKEEAQQLL QNGKSGREKS DQLLSRANLA KSRAQEALSM GNATFYEVES ILKNLREFDL 970 980 990 1000 1010 1020 QVDNRKAEAE EAMKRLSYIS QKVSDASDKT QQAERALGSA AADAQRAKNG AGEALEISSE 1030 1040 1050 1060 1070 1080 IEQEIGSLNL EANVTADGAL AMEKGLASLK SEMREVEGEL ERKELEFDTN MDAVQMVITE 1090 1100 1110 AQKVDTRAKN AGVTIQDTLN TLDGLLHLMG M

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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: 1383240] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], ALTERNATIVE SPLICING. Tissue: Fibrosarcoma.
[2]	"The 100-kDa chain of nicein/kalinin is a laminin B2 chain variant." Vailly J., Verrando P., Champliaud M.-F., Gerecke D., Wagman D.W., Baudoin C., Aberdam D., Burgeson R., Bauer E., Ortonne J.-P. Eur. J. Biochem. 219:209-218(1994) [PubMed: 8306988] [Abstract] 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: 8786121] [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: 16710414] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases 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: 15489334] [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: 8265624] [Abstract] Cited for: NUCLEOTIDE SEQUENCE OF 435-449, FUNCTION, HEPARIN-BINDING.
[8]	"Global survey of phosphotyrosine signaling identifies oncogenic kinases in lung cancer." Rikova K., Guo A., Zeng Q., Possemato A., Yu J., Haack H., Nardone J., Lee K., Reeves C., Li Y., Hu Y., Tan Z., Stokes M., Sullivan L., Mitchell J., Wetzel R., Macneill J., Ren J.M. , Yuan J., Bakalarski C.E., Villen J., Kornhauser J.M., Smith B., Li D., Zhou X., Gygi S.P., Gu T.-L., Polakiewicz R.D., Rush J., Comb M.J. Cell 131:1190-1203(2007) [PubMed: 18083107] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-250; TYR-265 AND TYR-273, MASS SPECTROMETRY. Tissue: Lung carcinoma.
+	Additional computationally mapped references.

Web resources

GeneReviews

Cross-references

Sequence databases
EMBL GenBank DDBJ	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. BC113378 mRNA. Translation: AAI13379.1.
IPI	IPI00015117. IPI00220572.
PIR	A44018.
RefSeq	NP_005553.2. NM_005562.2. NP_061486.2. NM_018891.2.
UniGene	Hs.591484.
3D structure databases
ProteinModelPortal	Q13753.
SMR	Q13753. Positions 26-185, 381-602.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-190N.
MINT	MINT-4053464.
STRING	Q13753.
Protein family/group databases
Allergome	8331. Hom s Laminin gamma_2.
PTM databases
PhosphoSite	Q13753.
Polymorphism databases
DMDM	90185107.
Proteomic databases
PeptideAtlas	Q13753.
PRIDE	Q13753.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000264144; ENSP00000264144; ENSG00000058085.
GeneID	3918.
KEGG	hsa:3918.
NMPDR	fig|9606.3.peg.2740.
UCSC	uc001gqa.2. human.
Organism-specific databases
CTD	3918.
GeneCards	GC01P183155.
HGNC	HGNC:6493. LAMC2.
HPA	CAB004257. HPA024638.
MIM	150292. gene. 226700. phenotype.
neXtProt	NX_Q13753.
Orphanet	79402. Generalized junctional epidermolysis bullosa, non-Herlitz type. 79404. Junctional epidermolysis bullosa, Herlitz type.
PharmGKB	PA30281.
GenAtlas	Search...
Phylogenomic databases
eggNOG	prNOG16841.
GeneTree	ENSGT00600000084051.
HOGENOM	HBG358231.
HOVERGEN	HBG062127.
InParanoid	Q13753.
OMA	CPACYNQ.
OrthoDB	EOG4ZCT3N.
PhylomeDB	Q13753.
Enzyme and pathway databases
Pathway_Interaction_DB	a6b1_a6b4_integrin_pathway. a6b1 and a6b4 Integrin signaling. amb2_neutrophils_pathway. amb2 Integrin signaling.
Reactome	REACT_111155. Cell-Cell communication.
Gene expression databases
ArrayExpress	Q13753.
Bgee	Q13753.
CleanEx	HS_LAMC2.
Genevestigator	Q13753.
GermOnline	ENSG00000058085. Homo sapiens.
Family and domain databases
InterPro	IPR002049. EGF_laminin. IPR009030. Growth_fac_rcpt. IPR018031. Laminin_B_subgr. IPR000034. Laminin_B_type_IV. [Graphical view]
KO	K06246.
Pfam	PF00052. Laminin_B. 1 hit. PF00053. Laminin_EGF. 7 hits. [Graphical view]
SMART	SM00180. EGF_Lam. 6 hits. SM00281. LamB. 1 hit. [Graphical view]
SUPFAM	SSF57184. Grow_fac_recept. 1 hit.
PROSITE	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]
ProtoNet	Search...
Other
NextBio	15391.
PMAP-CutDB	Q13753.
SOURCE	Search...

Entry information

Entry name

LAMC2_HUMAN

Accession

Primary (citable) accession number: Q13753
Secondary accession number(s): Q02536 , Q02537, Q13752, Q14941, Q14DF7, Q5VYE8

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1997
Last sequence update:	March 7, 2006
Last modified:	January 25, 2012
This is version 128 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.