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Q16363

- LAMA4_HUMAN

UniProt

Q16363 - LAMA4_HUMAN

Protein

Laminin subunit alpha-4

Gene

LAMA4

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 152 (01 Oct 2014)
      Sequence version 4 (23 Mar 2010)
      Previous versions | rss
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    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

    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

    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

    ArrayExpressiQ16363.
    BgeeiQ16363.
    CleanExiHS_LAMA4.
    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. 15 interactions.
    IntActiQ16363. 18 interactions.
    MINTiMINT-1200879.
    STRINGi9606.ENSP00000230538.

    Structurei

    3D structure databases

    ProteinModelPortaliQ16363.
    SMRiQ16363. Positions 82-280, 875-1382, 1456-1823.
    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.
    HOVERGENiHBG052299.
    InParanoidiQ16363.
    KOiK06241.
    OMAiSICITHN.
    PhylomeDBiQ16363.
    TreeFamiTF335359.

    Family and domain databases

    Gene3Di2.60.120.200. 5 hits.
    InterProiIPR008985. ConA-like_lec_gl_sf.
    IPR013320. ConA-like_subgrp.
    IPR002049. EGF_laminin.
    IPR001791. Laminin_G.
    IPR009254. Laminin_I.
    IPR010307. Laminin_II.
    [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

    MALSSAWRSV LPLWLLWSAA CSRAASGDDN AFPFDIEGSS AVGRQDPPET     50
    SEPRVALGRL PPAAEKCNAG FFHTLSGECV PCDCNGNSNE CLDGSGYCVH 100
    CQRNTTGEHC EKCLDGYIGD SIRGAPQFCQ PCPCPLPHLA NFAESCYRKN 150
    GAVRCICNEN YAGPNCERCA PGYYGNPLLI GSTCKKCDCS GNSDPNLIFE 200
    DCDEVTGQCR NCLRNTTGFK CERCAPGYYG DARIAKNCAV CNCGGGPCDS 250
    VTGECLEEGF EPPTGMDCPT ISCDKCVWDL TDALRLAALS IEEGKSGVLS 300
    VSSGAAAHRH VNEINATIYL LKTKLSEREN QYALRKIQIN NAENTMKSLL 350
    SDVEELVEKE NQASRKGQLV QKESMDTINH ASQLVEQAHD MRDKIQEINN 400
    KMLYYGEEHE LSPKEISEKL VLAQKMLEEI RSRQPFFTQR ELVDEEADEA 450
    YELLSQAESW QRLHNETRTL FPVVLEQLDD YNAKLSDLQE ALDQALNYVR 500
    DAEDMNRATA ARQRDHEKQQ ERVREQMEVV NMSLSTSADS LTTPRLTLSE 550
    LDDIIKNASG IYAEIDGAKS ELQVKLSNLS NLSHDLVQEA IDHAQDLQQE 600
    ANELSRKLHS SDMNGLVQKA LDASNVYENI VNYVSEANET AEFALNTTDR 650
    IYDAVSGIDT QIIYHKDESE NLLNQARELQ AKAESSSDEA VADTSRRVGG 700
    ALARKSALKT RLSDAVKQLQ AAERGDAQQR LGQSRLITEE ANRTTMEVQQ 750
    ATAPMANNLT NWSQNLQHFD SSAYNTAVNS ARDAVRNLTE VVPQLLDQLR 800
    TVEQKRPASN VSASIQRIRE LIAQTRSVAS KIQVSMMFDG QSAVEVHSRT 850
    SMDDLKAFTS LSLYMKPPVK RPELTETADQ FILYLGSKNA KKEYMGLAIK 900
    NDNLVYVYNL GTKDVEIPLD SKPVSSWPAY FSIVKIERVG KHGKVFLTVP 950
    SLSSTAEEKF IKKGEFSGDD SLLDLDPEDT VFYVGGVPSN FKLPTSLNLP 1000
    GFVGCLELAT LNNDVISLYN FKHIYNMDPS TSVPCARDKL AFTQSRAASY 1050
    FFDGSGYAVV RDITRRGKFG QVTRFDIEVR TPADNGLILL MVNGSMFFRL 1100
    EMRNGYLHVF YDFGFSGGPV HLEDTLKKAQ INDAKYHEIS IIYHNDKKMI 1150
    LVVDRRHVKS MDNEKMKIPF TDIYIGGAPP EILQSRALRA HLPLDINFRG 1200
    CMKGFQFQKK DFNLLEQTET LGVGYGCPED SLISRRAYFN GQSFIASIQK 1250
    ISFFDGFEGG FNFRTLQPNG LLFYYASGSD VFSISLDNGT VIMDVKGIKV 1300
    QSVDKQYNDG LSHFVISSVS PTRYELIVDK SRVGSKNPTK GKIEQTQASE 1350
    KKFYFGGSPI SAQYANFTGC ISNAYFTRVD RDVEVEDFQR YTEKVHTSLY 1400
    ECPIESSPLF LLHKKGKNLS KPKASQNKKG GKSKDAPSWD PVALKLPERN 1450
    TPRNSHCHLS NSPRAIEHAY QYGGTANSRQ EFEHLKGDFG AKSQFSIRLR 1500
    TRSSHGMIFY VSDQEENDFM TLFLAHGRLV YMFNVGHKKL KIRSQEKYND 1550
    GLWHDVIFIR ERSSGRLVID GLRVLEESLP PTEATWKIKG PIYLGGVAPG 1600
    KAVKNVQINS IYSFSGCLSN LQLNGASITS ASQTFSVTPC FEGPMETGTY 1650
    FSTEGGYVVL DESFNIGLKF EIAFEVRPRS SSGTLVHGHS VNGEYLNVHM 1700
    KNGQVIVKVN NGIRDFSTSV TPKQSLCDGR WHRITVIRDS NVVQLDVDSE 1750
    VNHVVGPLNP KPIDHREPVF VGGVPESLLT PRLAPSKPFT GCIRHFVIDG 1800
    HPVSFSKAAL VSGAVSINSC PAA 1823
    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

    EnsembliENST00000230538; 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]
    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 82-280, 875-1382, 1456-1823.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 110104. 15 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 ENST00000230538 ; 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 ]
    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.
    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

    ArrayExpressi Q16363.
    Bgeei Q16363.
    CleanExi HS_LAMA4.
    Genevestigatori Q16363.

    Family and domain databases

    Gene3Di 2.60.120.200. 5 hits.
    InterProi IPR008985. ConA-like_lec_gl_sf.
    IPR013320. ConA-like_subgrp.
    IPR002049. EGF_laminin.
    IPR001791. Laminin_G.
    IPR009254. Laminin_I.
    IPR010307. Laminin_II.
    [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

    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 1, 2014
    This is version 152 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