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Q16363

- LAMA4_HUMAN

UniProt

Q16363 - LAMA4_HUMAN

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Protein

Laminin subunit alpha-4

Gene

LAMA4

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. extracellular matrix structural constituent Source: ProtInc

GO - Biological processi

  1. blood vessel development Source: Ensembl
  2. brown fat cell differentiation Source: Ensembl
  3. cell adhesion Source: UniProtKB-KW
  4. extracellular matrix organization Source: Reactome
  5. regulation of cell adhesion Source: InterPro
  6. regulation of cell migration Source: InterPro
  7. regulation of embryonic development Source: InterPro
Complete GO annotation...

Keywords - Biological processi

Cell adhesion

Enzyme and pathway databases

ReactomeiREACT_163874. Non-integrin membrane-ECM interactions.
REACT_163906. ECM proteoglycans.
REACT_169262. Laminin interactions.

Names & Taxonomyi

Protein namesi
Recommended name:
Laminin subunit alpha-4
Alternative name(s):
Laminin-14 subunit alpha
Laminin-8 subunit alpha
Laminin-9 subunit alpha
Gene namesi
Name:LAMA4
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 6

Organism-specific databases

HGNCiHGNC:6484. LAMA4.

Subcellular locationi

GO - Cellular componenti

  1. basal lamina Source: ProtInc
  2. basement membrane Source: UniProtKB
  3. extracellular region Source: Reactome
  4. extracellular vesicular exosome Source: UniProtKB
  5. laminin-1 complex Source: InterPro
Complete GO annotation...

Keywords - Cellular componenti

Basement membrane, Extracellular matrix, Secreted

Pathology & Biotechi

Involvement in diseasei

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.1 Publication
Note: The disease is caused by mutations affecting the gene represented in this entry.
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti950 – 9501P → L in CMD1JJ; loss of integrin-binding capacity. 1 Publication
VAR_069708

Keywords - Diseasei

Cardiomyopathy, Disease mutation

Organism-specific databases

MIMi615235. phenotype.
Orphaneti154. Familial isolated dilated cardiomyopathy.
PharmGKBiPA30273.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2424Sequence AnalysisAdd
BLAST
Chaini25 – 18231799Laminin subunit alpha-4PRO_0000017060Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi82 ↔ 91By similarity
Disulfide bondi84 ↔ 98By similarity
Disulfide bondi101 ↔ 110By similarity
Glycosylationi104 – 1041N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi113 ↔ 129By similarity
Disulfide bondi132 ↔ 146By similarity
Disulfide bondi134 ↔ 155By similarity
Disulfide bondi157 ↔ 166By similarity
Disulfide bondi169 ↔ 184By similarity
Disulfide bondi187 ↔ 202By similarity
Disulfide bondi189 ↔ 209By similarity
Disulfide bondi212 ↔ 221By similarity
Glycosylationi215 – 2151N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi224 ↔ 238By similarity
Disulfide bondi273 – 273InterchainCurated
Disulfide bondi276 – 276InterchainCurated
Glycosylationi315 – 3151N-linked (GlcNAc...)Sequence Analysis
Glycosylationi465 – 4651N-linked (GlcNAc...)Sequence Analysis
Glycosylationi531 – 5311N-linked (GlcNAc...)Sequence Analysis
Glycosylationi557 – 5571N-linked (GlcNAc...)1 Publication
Glycosylationi578 – 5781N-linked (GlcNAc...)1 Publication
Glycosylationi581 – 5811N-linked (GlcNAc...)1 Publication
Glycosylationi638 – 6381N-linked (GlcNAc...)Sequence Analysis
Glycosylationi646 – 6461N-linked (GlcNAc...)Sequence Analysis
Glycosylationi742 – 7421N-linked (GlcNAc...)1 Publication
Glycosylationi758 – 7581N-linked (GlcNAc...)Sequence Analysis
Glycosylationi761 – 7611N-linked (GlcNAc...)Sequence Analysis
Glycosylationi787 – 7871N-linked (GlcNAc...)1 Publication
Glycosylationi810 – 8101N-linked (GlcNAc...)1 Publication
Disulfide bondi1005 ↔ 1035By similarity
Glycosylationi1093 – 10931N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi1201 ↔ 1227By similarity
Glycosylationi1288 – 12881N-linked (GlcNAc...)Sequence Analysis
Glycosylationi1366 – 13661N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi1370 ↔ 1402By similarity
Glycosylationi1418 – 14181N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi1617 ↔ 1640By similarity
Disulfide bondi1792 ↔ 1820By similarity

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

MaxQBiQ16363.
PaxDbiQ16363.
PRIDEiQ16363.

PTM databases

PhosphoSiteiQ16363.

Expressioni

Tissue specificityi

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.

Gene expression databases

BgeeiQ16363.
CleanExiHS_LAMA4.
ExpressionAtlasiQ16363. baseline and differential.
GenevestigatoriQ16363.

Organism-specific databases

HPAiHPA015693.

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

Binary interactionsi

WithEntry#Exp.IntActNotes
TP53P046372EBI-711505,EBI-366083

Protein-protein interaction databases

BioGridi110104. 20 interactions.
IntActiQ16363. 18 interactions.
MINTiMINT-1200879.
STRINGi9606.ENSP00000230538.

Structurei

3D structure databases

ProteinModelPortaliQ16363.
SMRiQ16363. Positions 45-280, 875-1382, 1490-1821.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini82 – 13150Laminin EGF-like 1PROSITE-ProRule annotationAdd
BLAST
Domaini132 – 18655Laminin EGF-like 2PROSITE-ProRule annotationAdd
BLAST
Domaini187 – 24054Laminin EGF-like 3PROSITE-ProRule annotationAdd
BLAST
Domaini241 – 25515Laminin EGF-like 4; truncatedPROSITE-ProRule annotationAdd
BLAST
Domaini833 – 1035203Laminin G-like 1PROSITE-ProRule annotationAdd
BLAST
Domaini1047 – 1227181Laminin G-like 2PROSITE-ProRule annotationAdd
BLAST
Domaini1234 – 1402169Laminin G-like 3PROSITE-ProRule annotationAdd
BLAST
Domaini1469 – 1640172Laminin G-like 4PROSITE-ProRule annotationAdd
BLAST
Domaini1647 – 1820174Laminin G-like 5PROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni256 – 832577Domain II and IAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili320 – 40384Sequence AnalysisAdd
BLAST
Coiled coili473 – 52856Sequence AnalysisAdd
BLAST
Coiled coili581 – 61434Sequence AnalysisAdd
BLAST
Coiled coili662 – 72463Sequence AnalysisAdd
BLAST
Coiled coili777 – 80630Sequence AnalysisAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi724 – 7263Cell 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 G is globular.

Sequence similaritiesi

Contains 4 laminin EGF-like domains.PROSITE-ProRule annotation
Contains 5 laminin G-like domains.PROSITE-ProRule annotation

Keywords - Domaini

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

Phylogenomic databases

eggNOGiNOG247347.
GeneTreeiENSGT00760000119121.
HOVERGENiHBG052299.
InParanoidiQ16363.
KOiK06241.
OMAiSICITHN.
PhylomeDBiQ16363.
TreeFamiTF335359.

Family and domain databases

Gene3Di2.60.120.200. 5 hits.
InterProiIPR013320. ConA-like_dom.
IPR002049. EGF_laminin.
IPR010307. Laminin_domII.
IPR001791. Laminin_G.
IPR009254. Laminin_I.
[Graphical view]
PfamiPF00053. Laminin_EGF. 3 hits.
PF02210. Laminin_G_2. 5 hits.
PF06008. Laminin_I. 1 hit.
PF06009. Laminin_II. 1 hit.
[Graphical view]
SMARTiSM00180. EGF_Lam. 3 hits.
SM00282. LamG. 5 hits.
[Graphical view]
SUPFAMiSSF49899. SSF49899. 5 hits.
PROSITEiPS00022. EGF_1. 1 hit.
PS01248. EGF_LAM_1. 3 hits.
PS50027. EGF_LAM_2. 3 hits.
PS50025. LAM_G_DOMAIN. 5 hits.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

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

This entry describes 3 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q16363-1) [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
MALSSAWRSV LPLWLLWSAA CSRAASGDDN AFPFDIEGSS AVGRQDPPET
60 70 80 90 100
SEPRVALGRL PPAAEKCNAG FFHTLSGECV PCDCNGNSNE CLDGSGYCVH
110 120 130 140 150
CQRNTTGEHC EKCLDGYIGD SIRGAPQFCQ PCPCPLPHLA NFAESCYRKN
160 170 180 190 200
GAVRCICNEN YAGPNCERCA PGYYGNPLLI GSTCKKCDCS GNSDPNLIFE
210 220 230 240 250
DCDEVTGQCR NCLRNTTGFK CERCAPGYYG DARIAKNCAV CNCGGGPCDS
260 270 280 290 300
VTGECLEEGF EPPTGMDCPT ISCDKCVWDL TDALRLAALS IEEGKSGVLS
310 320 330 340 350
VSSGAAAHRH VNEINATIYL LKTKLSEREN QYALRKIQIN NAENTMKSLL
360 370 380 390 400
SDVEELVEKE NQASRKGQLV QKESMDTINH ASQLVEQAHD MRDKIQEINN
410 420 430 440 450
KMLYYGEEHE LSPKEISEKL VLAQKMLEEI RSRQPFFTQR ELVDEEADEA
460 470 480 490 500
YELLSQAESW QRLHNETRTL FPVVLEQLDD YNAKLSDLQE ALDQALNYVR
510 520 530 540 550
DAEDMNRATA ARQRDHEKQQ ERVREQMEVV NMSLSTSADS LTTPRLTLSE
560 570 580 590 600
LDDIIKNASG IYAEIDGAKS ELQVKLSNLS NLSHDLVQEA IDHAQDLQQE
610 620 630 640 650
ANELSRKLHS SDMNGLVQKA LDASNVYENI VNYVSEANET AEFALNTTDR
660 670 680 690 700
IYDAVSGIDT QIIYHKDESE NLLNQARELQ AKAESSSDEA VADTSRRVGG
710 720 730 740 750
ALARKSALKT RLSDAVKQLQ AAERGDAQQR LGQSRLITEE ANRTTMEVQQ
760 770 780 790 800
ATAPMANNLT NWSQNLQHFD SSAYNTAVNS ARDAVRNLTE VVPQLLDQLR
810 820 830 840 850
TVEQKRPASN VSASIQRIRE LIAQTRSVAS KIQVSMMFDG QSAVEVHSRT
860 870 880 890 900
SMDDLKAFTS LSLYMKPPVK RPELTETADQ FILYLGSKNA KKEYMGLAIK
910 920 930 940 950
NDNLVYVYNL GTKDVEIPLD SKPVSSWPAY FSIVKIERVG KHGKVFLTVP
960 970 980 990 1000
SLSSTAEEKF IKKGEFSGDD SLLDLDPEDT VFYVGGVPSN FKLPTSLNLP
1010 1020 1030 1040 1050
GFVGCLELAT LNNDVISLYN FKHIYNMDPS TSVPCARDKL AFTQSRAASY
1060 1070 1080 1090 1100
FFDGSGYAVV RDITRRGKFG QVTRFDIEVR TPADNGLILL MVNGSMFFRL
1110 1120 1130 1140 1150
EMRNGYLHVF YDFGFSGGPV HLEDTLKKAQ INDAKYHEIS IIYHNDKKMI
1160 1170 1180 1190 1200
LVVDRRHVKS MDNEKMKIPF TDIYIGGAPP EILQSRALRA HLPLDINFRG
1210 1220 1230 1240 1250
CMKGFQFQKK DFNLLEQTET LGVGYGCPED SLISRRAYFN GQSFIASIQK
1260 1270 1280 1290 1300
ISFFDGFEGG FNFRTLQPNG LLFYYASGSD VFSISLDNGT VIMDVKGIKV
1310 1320 1330 1340 1350
QSVDKQYNDG LSHFVISSVS PTRYELIVDK SRVGSKNPTK GKIEQTQASE
1360 1370 1380 1390 1400
KKFYFGGSPI SAQYANFTGC ISNAYFTRVD RDVEVEDFQR YTEKVHTSLY
1410 1420 1430 1440 1450
ECPIESSPLF LLHKKGKNLS KPKASQNKKG GKSKDAPSWD PVALKLPERN
1460 1470 1480 1490 1500
TPRNSHCHLS NSPRAIEHAY QYGGTANSRQ EFEHLKGDFG AKSQFSIRLR
1510 1520 1530 1540 1550
TRSSHGMIFY VSDQEENDFM TLFLAHGRLV YMFNVGHKKL KIRSQEKYND
1560 1570 1580 1590 1600
GLWHDVIFIR ERSSGRLVID GLRVLEESLP PTEATWKIKG PIYLGGVAPG
1610 1620 1630 1640 1650
KAVKNVQINS IYSFSGCLSN LQLNGASITS ASQTFSVTPC FEGPMETGTY
1660 1670 1680 1690 1700
FSTEGGYVVL DESFNIGLKF EIAFEVRPRS SSGTLVHGHS VNGEYLNVHM
1710 1720 1730 1740 1750
KNGQVIVKVN NGIRDFSTSV TPKQSLCDGR WHRITVIRDS NVVQLDVDSE
1760 1770 1780 1790 1800
VNHVVGPLNP KPIDHREPVF VGGVPESLLT PRLAPSKPFT GCIRHFVIDG
1810 1820
HPVSFSKAAL VSGAVSINSC PAA
Length:1,823
Mass (Da):202,524
Last modified:March 23, 2010 - v4
Checksum:i25BFB6120C2A86F1
GO
Isoform 2 (identifier: Q16363-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     266-272: Missing.

Show »
Length:1,816
Mass (Da):201,776
Checksum:iAEC1A024B5A180ED
GO
Isoform 3 (identifier: Q16363-3) [UniParc]FASTAAdd to Basket

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

Show »
Length:120
Mass (Da):12,819
Checksum:i6ABF63CBA663BF3F
GO

Sequence cautioni

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

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti143 – 1431A → P in AAB34635. (PubMed:7781776)Curated
Sequence conflicti178 – 1781L → F in AAB34635. (PubMed:7781776)Curated
Sequence conflicti283 – 2831A → D in AAB34635. (PubMed:7781776)Curated
Sequence conflicti283 – 2831A → D in CAA62596. (PubMed:8706685)Curated
Sequence conflicti283 – 2831A → D in BAE06109. 1 PublicationCurated
Sequence conflicti283 – 2831A → D in CAA54258. (PubMed:7959779)Curated
Sequence conflicti1064 – 10641T → P in AAB34635. (PubMed:7781776)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti94 – 941G → S.
Corresponds to variant rs35349917 [ dbSNP | Ensembl ].
VAR_056140
Natural varianti154 – 1541R → W.
Corresponds to variant rs11757455 [ dbSNP | Ensembl ].
VAR_056141
Natural varianti283 – 2831A → E.
Corresponds to variant rs9400522 [ dbSNP | Ensembl ].
VAR_061348
Natural varianti492 – 4921L → H.
Corresponds to variant rs3752579 [ dbSNP | Ensembl ].
VAR_056142
Natural varianti498 – 4981Y → H.2 Publications
Corresponds to variant rs1050348 [ dbSNP | Ensembl ].
VAR_025550
Natural varianti950 – 9501P → L in CMD1JJ; loss of integrin-binding capacity. 1 Publication
VAR_069708
Natural varianti1117 – 11171G → S.3 Publications
Corresponds to variant rs2032567 [ dbSNP | Ensembl ].
VAR_025551
Natural varianti1119 – 11191P → R.3 Publications
Corresponds to variant rs1050349 [ dbSNP | Ensembl ].
VAR_025552
Natural varianti1549 – 15491N → S.1 Publication
Corresponds to variant rs12110554 [ dbSNP | Ensembl ].
VAR_056143
Natural varianti1815 – 18151V → I.
Corresponds to variant rs3734292 [ dbSNP | Ensembl ].
VAR_056144

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei66 – 12055KCNAG…GYIGD → VQCPCHCHPAGAPAPPRAVP HSSFSLSPPLSSPQCLESFT WARSVRKLEIKSFPL in isoform 3. 2 PublicationsVSP_038853Add
BLAST
Alternative sequencei121 – 18231703Missing in isoform 3. 2 PublicationsVSP_038854Add
BLAST
Alternative sequencei266 – 2727Missing in isoform 2. 3 PublicationsVSP_017542

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
CCDSiCCDS34514.1. [Q16363-2]
CCDS43491.1. [Q16363-1]
CCDS43492.1. [Q16363-3]
PIRiS68960.
RefSeqiNP_001098676.2. NM_001105206.2.
NP_001098677.2. NM_001105207.2.
NP_001098678.1. NM_001105208.2. [Q16363-3]
NP_001098679.1. NM_001105209.2. [Q16363-3]
NP_002281.3. NM_002290.4.
UniGeneiHs.654572.

Genome annotation databases

EnsembliENST00000368638; ENSP00000357627; ENSG00000112769. [Q16363-3]
ENST00000453937; ENSP00000398226; ENSG00000112769. [Q16363-3]
ENST00000455073; ENSP00000408604; ENSG00000112769. [Q16363-3]
GeneIDi3910.
KEGGihsa:3910.
UCSCiuc003pvt.3. human. [Q16363-2]
uc003pvu.3. human. [Q16363-1]
uc010kdz.2. human. [Q16363-3]

Polymorphism databases

DMDMi292495093.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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 .
CCDSi CCDS34514.1. [Q16363-2 ]
CCDS43491.1. [Q16363-1 ]
CCDS43492.1. [Q16363-3 ]
PIRi S68960.
RefSeqi NP_001098676.2. NM_001105206.2.
NP_001098677.2. NM_001105207.2.
NP_001098678.1. NM_001105208.2. [Q16363-3 ]
NP_001098679.1. NM_001105209.2. [Q16363-3 ]
NP_002281.3. NM_002290.4.
UniGenei Hs.654572.

3D structure databases

ProteinModelPortali Q16363.
SMRi Q16363. Positions 45-280, 875-1382, 1490-1821.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 110104. 20 interactions.
IntActi Q16363. 18 interactions.
MINTi MINT-1200879.
STRINGi 9606.ENSP00000230538.

Chemistry

ChEMBLi CHEMBL2364187.

PTM databases

PhosphoSitei Q16363.

Polymorphism databases

DMDMi 292495093.

Proteomic databases

MaxQBi Q16363.
PaxDbi Q16363.
PRIDEi Q16363.

Protocols and materials databases

DNASUi 3910.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000368638 ; ENSP00000357627 ; ENSG00000112769 . [Q16363-3 ]
ENST00000453937 ; ENSP00000398226 ; ENSG00000112769 . [Q16363-3 ]
ENST00000455073 ; ENSP00000408604 ; ENSG00000112769 . [Q16363-3 ]
GeneIDi 3910.
KEGGi hsa:3910.
UCSCi uc003pvt.3. human. [Q16363-2 ]
uc003pvu.3. human. [Q16363-1 ]
uc010kdz.2. human. [Q16363-3 ]

Organism-specific databases

CTDi 3910.
GeneCardsi GC06M112475.
HGNCi HGNC:6484. LAMA4.
HPAi HPA015693.
MIMi 600133. gene.
615235. phenotype.
neXtProti NX_Q16363.
Orphaneti 154. Familial isolated dilated cardiomyopathy.
PharmGKBi PA30273.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG247347.
GeneTreei ENSGT00760000119121.
HOVERGENi HBG052299.
InParanoidi Q16363.
KOi K06241.
OMAi SICITHN.
PhylomeDBi Q16363.
TreeFami TF335359.

Enzyme and pathway databases

Reactomei REACT_163874. Non-integrin membrane-ECM interactions.
REACT_163906. ECM proteoglycans.
REACT_169262. Laminin interactions.

Miscellaneous databases

ChiTaRSi LAMA4. human.
GeneWikii Laminin,_alpha_4.
GenomeRNAii 3910.
NextBioi 15351.
PROi Q16363.
SOURCEi Search...

Gene expression databases

Bgeei Q16363.
CleanExi HS_LAMA4.
ExpressionAtlasi Q16363. baseline and differential.
Genevestigatori Q16363.

Family and domain databases

Gene3Di 2.60.120.200. 5 hits.
InterProi IPR013320. ConA-like_dom.
IPR002049. EGF_laminin.
IPR010307. Laminin_domII.
IPR001791. Laminin_G.
IPR009254. Laminin_I.
[Graphical view ]
Pfami PF00053. Laminin_EGF. 3 hits.
PF02210. Laminin_G_2. 5 hits.
PF06008. Laminin_I. 1 hit.
PF06009. Laminin_II. 1 hit.
[Graphical view ]
SMARTi SM00180. EGF_Lam. 3 hits.
SM00282. LamG. 5 hits.
[Graphical view ]
SUPFAMi SSF49899. SSF49899. 5 hits.
PROSITEi PS00022. EGF_1. 1 hit.
PS01248. EGF_LAM_1. 3 hits.
PS50027. EGF_LAM_2. 3 hits.
PS50025. LAM_G_DOMAIN. 5 hits.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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. Cited for: VARIANT CMD1JJ LEU-950, CHARACTERIZATION OF VARIANT CMD1JJ LEU-950.

Entry informationi

Entry nameiLAMA4_HUMAN
AccessioniPrimary (citable) accession number: Q16363
Secondary accession number(s): Q14731
, Q14735, Q15335, Q4LE44, Q5SZG8, Q9BTB8, Q9UE18, Q9UJN9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: March 23, 2010
Last modified: October 29, 2014
This is version 153 of the entry and version 4 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

Caution

Gene LAMA4 was formerly called LAMA3.Curated

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 6
    Human chromosome 6: 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