Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q16363 (LAMA4_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 147. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Laminin subunit alpha-4
Alternative name(s):
Laminin-14 subunit alpha
Laminin-8 subunit alpha
Laminin-9 subunit alpha
Gene names
Name:LAMA4
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1823 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence 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.

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. Alpha-4 is a subunit of laminin-8 (laminin-411), laminin-9 (laminin-421) and laminin-14 (laminin-423).

Subcellular location

Secretedextracellular spaceextracellular matrixbasement membrane. Note: Major component.

Tissue specificity

In adult, strong expression in heart, lung, ovary small and large intestines, placenta, liver; weak or no expression in skeletal muscle, kidney, pancreas, testis, prostate, brain. High expression in fetal lung and kidney. Expression in fetal and newborn tissues is observed in certain mesenchymal cells in tissues such as smooth muscle and dermis.

Domain

The alpha-helical domains I and II are thought to interact with other laminin chains to form a coiled coil structure.

Domain G is globular.

Involvement in disease

Cardiomyopathy, dilated 1JJ (CMD1JJ) [MIM:615235]: A disorder characterized by ventricular dilation and impaired systolic function, resulting in congestive heart failure and arrhythmia. Patients are at risk of premature death.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.10

Sequence similarities

Contains 4 laminin EGF-like domains.

Contains 5 laminin G-like domains.

Caution

Gene LAMA4 was formerly called LAMA3.

Sequence caution

The sequence BAE06109.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q16363-1)

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 2 (identifier: Q16363-2)

The sequence of this isoform differs from the canonical sequence as follows:
     266-272: Missing.
Isoform 3 (identifier: Q16363-3)

The sequence of this isoform differs from the canonical sequence as follows:
     66-120: KCNAGFFHTL...EKCLDGYIGD → VQCPCHCHPA...RKLEIKSFPL
     121-1823: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2424 Potential
Chain25 – 18231799Laminin subunit alpha-4
PRO_0000017060

Regions

Domain82 – 13150Laminin EGF-like 1
Domain132 – 18655Laminin EGF-like 2
Domain187 – 24054Laminin EGF-like 3
Domain241 – 25515Laminin EGF-like 4; truncated
Domain833 – 1035203Laminin G-like 1
Domain1047 – 1227181Laminin G-like 2
Domain1234 – 1402169Laminin G-like 3
Domain1469 – 1640172Laminin G-like 4
Domain1647 – 1820174Laminin G-like 5
Region256 – 832577Domain II and I
Coiled coil320 – 40384 Potential
Coiled coil473 – 52856 Potential
Coiled coil581 – 61434 Potential
Coiled coil662 – 72463 Potential
Coiled coil777 – 80630 Potential
Motif724 – 7263Cell attachment site Potential

Amino acid modifications

Glycosylation1041N-linked (GlcNAc...) Potential
Glycosylation2151N-linked (GlcNAc...) Potential
Glycosylation3151N-linked (GlcNAc...) Potential
Glycosylation4651N-linked (GlcNAc...) Potential
Glycosylation5311N-linked (GlcNAc...) Potential
Glycosylation5571N-linked (GlcNAc...) Ref.9
Glycosylation5781N-linked (GlcNAc...) Ref.9
Glycosylation5811N-linked (GlcNAc...) Ref.9
Glycosylation6381N-linked (GlcNAc...) Potential
Glycosylation6461N-linked (GlcNAc...) Potential
Glycosylation7421N-linked (GlcNAc...) Ref.9
Glycosylation7581N-linked (GlcNAc...) Potential
Glycosylation7611N-linked (GlcNAc...) Potential
Glycosylation7871N-linked (GlcNAc...) Ref.9
Glycosylation8101N-linked (GlcNAc...) Ref.9
Glycosylation10931N-linked (GlcNAc...) Potential
Glycosylation12881N-linked (GlcNAc...) Potential
Glycosylation13661N-linked (GlcNAc...) Potential
Glycosylation14181N-linked (GlcNAc...) Potential
Disulfide bond82 ↔ 91 By similarity
Disulfide bond84 ↔ 98 By similarity
Disulfide bond101 ↔ 110 By similarity
Disulfide bond113 ↔ 129 By similarity
Disulfide bond132 ↔ 146 By similarity
Disulfide bond134 ↔ 155 By similarity
Disulfide bond157 ↔ 166 By similarity
Disulfide bond169 ↔ 184 By similarity
Disulfide bond187 ↔ 202 By similarity
Disulfide bond189 ↔ 209 By similarity
Disulfide bond212 ↔ 221 By similarity
Disulfide bond224 ↔ 238 By similarity
Disulfide bond273Interchain Probable
Disulfide bond276Interchain Probable
Disulfide bond1005 ↔ 1035 By similarity
Disulfide bond1201 ↔ 1227 By similarity
Disulfide bond1370 ↔ 1402 By similarity
Disulfide bond1617 ↔ 1640 By similarity
Disulfide bond1792 ↔ 1820 By similarity

Natural variations

Alternative sequence66 – 12055KCNAG…GYIGD → VQCPCHCHPAGAPAPPRAVP HSSFSLSPPLSSPQCLESFT WARSVRKLEIKSFPL in isoform 3.
VSP_038853
Alternative sequence121 – 18231703Missing in isoform 3.
VSP_038854
Alternative sequence266 – 2727Missing in isoform 2.
VSP_017542
Natural variant941G → S.
Corresponds to variant rs35349917 [ dbSNP | Ensembl ].
VAR_056140
Natural variant1541R → W.
Corresponds to variant rs11757455 [ dbSNP | Ensembl ].
VAR_056141
Natural variant2831A → E.
Corresponds to variant rs9400522 [ dbSNP | Ensembl ].
VAR_061348
Natural variant4921L → H.
Corresponds to variant rs3752579 [ dbSNP | Ensembl ].
VAR_056142
Natural variant4981Y → H. Ref.2 Ref.8
Corresponds to variant rs1050348 [ dbSNP | Ensembl ].
VAR_025550
Natural variant9501P → L in CMD1JJ; loss of integrin-binding capacity. Ref.10
VAR_069708
Natural variant11171G → S. Ref.1 Ref.2 Ref.8
Corresponds to variant rs2032567 [ dbSNP | Ensembl ].
VAR_025551
Natural variant11191P → R. Ref.1 Ref.2 Ref.8
Corresponds to variant rs1050349 [ dbSNP | Ensembl ].
VAR_025552
Natural variant15491N → S. Ref.2
Corresponds to variant rs12110554 [ dbSNP | Ensembl ].
VAR_056143
Natural variant18151V → I.
Corresponds to variant rs3734292 [ dbSNP | Ensembl ].
VAR_056144

Experimental info

Sequence conflict1431A → P in AAB34635. Ref.1
Sequence conflict1781L → F in AAB34635. Ref.1
Sequence conflict2831A → D in AAB34635. Ref.1
Sequence conflict2831A → D in CAA62596. Ref.2
Sequence conflict2831A → D in BAE06109. Ref.3
Sequence conflict2831A → D in CAA54258. Ref.8
Sequence conflict10641T → P in AAB34635. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified March 23, 2010. Version 4.
Checksum: 25BFB6120C2A86F1

FASTA1,823202,524
        10         20         30         40         50         60 
MALSSAWRSV LPLWLLWSAA CSRAASGDDN AFPFDIEGSS AVGRQDPPET SEPRVALGRL 

        70         80         90        100        110        120 
PPAAEKCNAG FFHTLSGECV PCDCNGNSNE CLDGSGYCVH CQRNTTGEHC EKCLDGYIGD 

       130        140        150        160        170        180 
SIRGAPQFCQ PCPCPLPHLA NFAESCYRKN GAVRCICNEN YAGPNCERCA PGYYGNPLLI 

       190        200        210        220        230        240 
GSTCKKCDCS GNSDPNLIFE DCDEVTGQCR NCLRNTTGFK CERCAPGYYG DARIAKNCAV 

       250        260        270        280        290        300 
CNCGGGPCDS VTGECLEEGF EPPTGMDCPT ISCDKCVWDL TDALRLAALS IEEGKSGVLS 

       310        320        330        340        350        360 
VSSGAAAHRH VNEINATIYL LKTKLSEREN QYALRKIQIN NAENTMKSLL SDVEELVEKE 

       370        380        390        400        410        420 
NQASRKGQLV QKESMDTINH ASQLVEQAHD MRDKIQEINN KMLYYGEEHE LSPKEISEKL 

       430        440        450        460        470        480 
VLAQKMLEEI RSRQPFFTQR ELVDEEADEA YELLSQAESW QRLHNETRTL FPVVLEQLDD 

       490        500        510        520        530        540 
YNAKLSDLQE ALDQALNYVR DAEDMNRATA ARQRDHEKQQ ERVREQMEVV NMSLSTSADS 

       550        560        570        580        590        600 
LTTPRLTLSE LDDIIKNASG IYAEIDGAKS ELQVKLSNLS NLSHDLVQEA IDHAQDLQQE 

       610        620        630        640        650        660 
ANELSRKLHS SDMNGLVQKA LDASNVYENI VNYVSEANET AEFALNTTDR IYDAVSGIDT 

       670        680        690        700        710        720 
QIIYHKDESE NLLNQARELQ AKAESSSDEA VADTSRRVGG ALARKSALKT RLSDAVKQLQ 

       730        740        750        760        770        780 
AAERGDAQQR LGQSRLITEE ANRTTMEVQQ ATAPMANNLT NWSQNLQHFD SSAYNTAVNS 

       790        800        810        820        830        840 
ARDAVRNLTE VVPQLLDQLR TVEQKRPASN VSASIQRIRE LIAQTRSVAS KIQVSMMFDG 

       850        860        870        880        890        900 
QSAVEVHSRT SMDDLKAFTS LSLYMKPPVK RPELTETADQ FILYLGSKNA KKEYMGLAIK 

       910        920        930        940        950        960 
NDNLVYVYNL GTKDVEIPLD SKPVSSWPAY FSIVKIERVG KHGKVFLTVP SLSSTAEEKF 

       970        980        990       1000       1010       1020 
IKKGEFSGDD SLLDLDPEDT VFYVGGVPSN FKLPTSLNLP GFVGCLELAT LNNDVISLYN 

      1030       1040       1050       1060       1070       1080 
FKHIYNMDPS TSVPCARDKL AFTQSRAASY FFDGSGYAVV RDITRRGKFG QVTRFDIEVR 

      1090       1100       1110       1120       1130       1140 
TPADNGLILL MVNGSMFFRL EMRNGYLHVF YDFGFSGGPV HLEDTLKKAQ INDAKYHEIS 

      1150       1160       1170       1180       1190       1200 
IIYHNDKKMI LVVDRRHVKS MDNEKMKIPF TDIYIGGAPP EILQSRALRA HLPLDINFRG 

      1210       1220       1230       1240       1250       1260 
CMKGFQFQKK DFNLLEQTET LGVGYGCPED SLISRRAYFN GQSFIASIQK ISFFDGFEGG 

      1270       1280       1290       1300       1310       1320 
FNFRTLQPNG LLFYYASGSD VFSISLDNGT VIMDVKGIKV QSVDKQYNDG LSHFVISSVS 

      1330       1340       1350       1360       1370       1380 
PTRYELIVDK SRVGSKNPTK GKIEQTQASE KKFYFGGSPI SAQYANFTGC ISNAYFTRVD 

      1390       1400       1410       1420       1430       1440 
RDVEVEDFQR YTEKVHTSLY ECPIESSPLF LLHKKGKNLS KPKASQNKKG GKSKDAPSWD 

      1450       1460       1470       1480       1490       1500 
PVALKLPERN TPRNSHCHLS NSPRAIEHAY QYGGTANSRQ EFEHLKGDFG AKSQFSIRLR 

      1510       1520       1530       1540       1550       1560 
TRSSHGMIFY VSDQEENDFM TLFLAHGRLV YMFNVGHKKL KIRSQEKYND GLWHDVIFIR 

      1570       1580       1590       1600       1610       1620 
ERSSGRLVID GLRVLEESLP PTEATWKIKG PIYLGGVAPG KAVKNVQINS IYSFSGCLSN 

      1630       1640       1650       1660       1670       1680 
LQLNGASITS ASQTFSVTPC FEGPMETGTY FSTEGGYVVL DESFNIGLKF EIAFEVRPRS 

      1690       1700       1710       1720       1730       1740 
SSGTLVHGHS VNGEYLNVHM KNGQVIVKVN NGIRDFSTSV TPKQSLCDGR WHRITVIRDS 

      1750       1760       1770       1780       1790       1800 
NVVQLDVDSE VNHVVGPLNP KPIDHREPVF VGGVPESLLT PRLAPSKPFT GCIRHFVIDG 

      1810       1820 
HPVSFSKAAL VSGAVSINSC PAA 

« Hide

Isoform 2 [UniParc].

Checksum: AEC1A024B5A180ED
Show »

FASTA1,816201,776
Isoform 3 [UniParc].

Checksum: 6ABF63CBA663BF3F
Show »

FASTA12012,819

References

« Hide 'large scale' references
[1]"Primary structure and expression of a novel human laminin alpha 4 chain."
Iivanainen A., Sainio K., Sariola H., Tryggvason K.
FEBS Lett. 365:183-188(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), VARIANTS SER-1117 AND ARG-1119.
Tissue: Fetal lung.
[2]"The complete cDNA sequence of laminin alpha 4 and its relationship to the other human laminin alpha chains."
Richards A.J., Al-Imara L., Pope F.M.
Eur. J. Biochem. 238:813-821(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), VARIANTS HIS-498; SER-1117; ARG-1119 AND SER-1549.
[3]"Preparation of a set of expression-ready clones of mammalian long cDNAs encoding large proteins by the ORF trap cloning method."
Nakajima D., Saito K., Yamakawa H., Kikuno R.F., Nakayama M., Ohara R., Okazaki N., Koga H., Nagase T., Ohara O.
Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Tissue: Brain.
[4]"Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
[5]"The DNA sequence and analysis of human chromosome 6."
Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D. expand/collapse author list , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.
Nature 425:805-811(2003) [PubMed] [Europe PMC] [Abstract]
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 3).
Tissue: Pancreas.
[7]"The structural organisation of LAMA4, the gene encoding laminin alpha4."
Richards A.J., Luccarini C., Pope F.M.
Eur. J. Biochem. 248:15-23(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-24.
Tissue: Heart.
[8]"Localization of the gene (LAMA4) to chromosome 6q21 and isolation of a partial cDNA encoding a variant laminin A chain."
Richards A.J., Al-Imara L., Carter N.P., Lloyd J.C., Leversha M.A., Pope F.M.
Genomics 22:237-239(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 236-1823 (ISOFORM 2), VARIANTS HIS-498; SER-1117 AND ARG-1119.
Tissue: Heart.
[9]"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-557; ASN-578; ASN-581; ASN-742; ASN-787 AND ASN-810.
Tissue: Liver.
[10]"Laminin-alpha4 and integrin-linked kinase mutations cause human cardiomyopathy via simultaneous defects in cardiomyocytes and endothelial cells."
Knoell R., Postel R., Wang J., Kraetzner R., Hennecke G., Vacaru A.M., Vakeel P., Schubert C., Murthy K., Rana B.K., Kube D., Knoell G., Schaefer K., Hayashi T., Holm T., Kimura A., Schork N., Toliat M.R. expand/collapse author list , Nuernberg P., Schultheiss H.P., Schaper W., Schaper J., Bos E., Den Hertog J., van Eeden F.J., Peters P.J., Hasenfuss G., Chien K.R., Bakkers J.
Circulation 116:515-525(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT CMD1JJ LEU-950, CHARACTERIZATION OF VARIANT CMD1JJ LEU-950.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
S78569 mRNA. Translation: AAB34635.1.
X91171 mRNA. Translation: CAA62596.1.
X70904 mRNA. Translation: CAA50261.1.
AB210027 mRNA. Translation: BAE06109.1. Different initiation.
BT006690 mRNA. Translation: AAP35336.1.
Z99289, AL590106 Genomic DNA. Translation: CAI42325.1.
AL590106 Genomic DNA. Translation: CAI12948.1.
AL590106 Genomic DNA. Translation: CAI12949.1.
AL590106, Z99289 Genomic DNA. Translation: CAI12950.1.
BC004241 mRNA. Translation: AAH04241.1.
Y14240 Genomic DNA. Translation: CAA74636.1.
X76939 mRNA. Translation: CAA54258.1.
PIRS68960.
RefSeqNP_001098676.2. NM_001105206.2.
NP_001098677.2. NM_001105207.2.
NP_001098678.1. NM_001105208.2.
NP_001098679.1. NM_001105209.2.
NP_002281.3. NM_002290.4.
UniGeneHs.654572.

3D structure databases

ProteinModelPortalQ16363.
SMRQ16363. Positions 33-280, 835-1390, 1455-1822.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid110104. 15 interactions.
IntActQ16363. 18 interactions.
MINTMINT-1200879.
STRING9606.ENSP00000230538.

Chemistry

ChEMBLCHEMBL2364187.

PTM databases

PhosphoSiteQ16363.

Polymorphism databases

DMDM292495093.

Proteomic databases

PaxDbQ16363.
PRIDEQ16363.

Protocols and materials databases

DNASU3910.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000230538; ENSP00000230538; ENSG00000112769. [Q16363-1]
ENST00000368638; ENSP00000357627; ENSG00000112769. [Q16363-3]
ENST00000389463; ENSP00000374114; ENSG00000112769. [Q16363-2]
ENST00000424408; ENSP00000416470; ENSG00000112769. [Q16363-2]
ENST00000453937; ENSP00000398226; ENSG00000112769. [Q16363-3]
ENST00000455073; ENSP00000408604; ENSG00000112769. [Q16363-3]
ENST00000522006; ENSP00000429488; ENSG00000112769. [Q16363-2]
ENST00000578470; ENSP00000464350; ENSG00000263699. [Q16363-3]
ENST00000584877; ENSP00000462802; ENSG00000263699. [Q16363-3]
ENST00000584945; ENSP00000464560; ENSG00000263699. [Q16363-3]
GeneID3910.
KEGGhsa:3910.
UCSCuc003pvt.3. human. [Q16363-2]
uc003pvu.3. human. [Q16363-1]
uc010kdz.2. human. [Q16363-3]

Organism-specific databases

CTD3910.
GeneCardsGC06M112475.
HGNCHGNC:6484. LAMA4.
HPAHPA015693.
MIM600133. gene.
615235. phenotype.
neXtProtNX_Q16363.
Orphanet154. Familial isolated dilated cardiomyopathy.
PharmGKBPA30273.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG247347.
HOVERGENHBG052299.
InParanoidQ16363.
KOK06241.
OMASICITHN.
PhylomeDBQ16363.
TreeFamTF335359.

Enzyme and pathway databases

ReactomeREACT_118779. Extracellular matrix organization.

Gene expression databases

ArrayExpressQ16363.
BgeeQ16363.
CleanExHS_LAMA4.
GenevestigatorQ16363.

Family and domain databases

Gene3D2.60.120.200. 5 hits.
InterProIPR008985. ConA-like_lec_gl_sf.
IPR013320. ConA-like_subgrp.
IPR002049. EGF_laminin.
IPR001791. Laminin_G.
IPR009254. Laminin_I.
IPR010307. Laminin_II.
[Graphical view]
PfamPF00053. Laminin_EGF. 3 hits.
PF02210. Laminin_G_2. 5 hits.
PF06008. Laminin_I. 1 hit.
PF06009. Laminin_II. 1 hit.
[Graphical view]
SMARTSM00180. EGF_Lam. 3 hits.
SM00282. LamG. 5 hits.
[Graphical view]
SUPFAMSSF49899. SSF49899. 5 hits.
PROSITEPS00022. EGF_1. 1 hit.
PS01248. EGF_LAM_1. 3 hits.
PS50027. EGF_LAM_2. 3 hits.
PS50025. LAM_G_DOMAIN. 5 hits.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSLAMA4. human.
GeneWikiLaminin,_alpha_4.
GenomeRNAi3910.
NextBio15351.
PROQ16363.
SOURCESearch...

Entry information

Entry nameLAMA4_HUMAN
AccessionPrimary (citable) accession number: Q16363
Secondary accession number(s): Q14731 expand/collapse secondary AC list , Q14735, Q15335, Q4LE44, Q5SZG8, Q9BTB8, Q9UE18, Q9UJN9
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: March 23, 2010
Last modified: April 16, 2014
This is version 147 of the entry and version 4 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 6

Human chromosome 6: entries, gene names and cross-references to MIM