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P15502

- ELN_HUMAN

UniProt

P15502 - ELN_HUMAN

Protein

Elastin

Gene

ELN

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 165 (01 Oct 2014)
      Sequence version 3 (05 Oct 2010)
      Previous versions | rss
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    Functioni

    Major structural protein of tissues such as aorta and nuchal ligament, which must expand rapidly and recover completely. Molecular determinant of the late arterial morphogenesis, stabilizing arterial structure by regulating proliferation and organization of vascular smooth muscle By similarity.By similarity

    GO - Molecular functioni

    1. extracellular matrix binding Source: Ensembl
    2. extracellular matrix constituent conferring elasticity Source: Ensembl
    3. extracellular matrix structural constituent Source: ProtInc
    4. protein binding Source: IntAct

    GO - Biological processi

    1. blood circulation Source: ProtInc
    2. blood vessel remodeling Source: Ensembl
    3. cell proliferation Source: ProtInc
    4. extracellular matrix disassembly Source: Reactome
    5. extracellular matrix organization Source: Reactome
    6. organ morphogenesis Source: ProtInc
    7. regulation of actin filament polymerization Source: Ensembl
    8. respiratory gaseous exchange Source: ProtInc
    9. skeletal muscle tissue development Source: Ensembl
    10. stress fiber assembly Source: Ensembl

    Enzyme and pathway databases

    ReactomeiREACT_118572. Degradation of the extracellular matrix.
    REACT_150331. Molecules associated with elastic fibres.
    REACT_150366. Elastic fibre formation.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Elastin
    Alternative name(s):
    Tropoelastin
    Gene namesi
    Name:ELN
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 7

    Organism-specific databases

    HGNCiHGNC:3327. ELN.

    Subcellular locationi

    Secretedextracellular spaceextracellular matrix
    Note: Extracellular matrix of elastic fibers.

    GO - Cellular componenti

    1. elastic fiber Source: BHF-UCL
    2. extracellular region Source: Reactome
    3. mitochondrion Source: Ensembl
    4. proteinaceous extracellular matrix Source: ProtInc

    Keywords - Cellular componenti

    Extracellular matrix, Secreted

    Pathology & Biotechi

    Involvement in diseasei

    Cutis laxa, autosomal dominant, 1 (ADCL1) [MIM:123700]: A connective tissue disorder characterized by loose, hyperextensible skin with decreased resilience and elasticity leading to a premature aged appearance. Face, hands, feet, joints, and torso may be differentially affected. Additional variable clinical features are gastrointestinal diverticula, hernia, and genital prolapse. Rare manifestations are pulmonary artery stenosis, aortic aneurysm, bronchiectasis, and emphysema.1 Publication
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Supravalvular aortic stenosis (SVAS) [MIM:185500]: Congenital narrowing of the ascending aorta which can occur sporadically, as an autosomal dominant condition, or as one component of Williams-Beuren syndrome.1 Publication
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    ELN is located in the Williams-Beuren syndrome (WBS) critical region. WBS results from a hemizygous deletion of several genes on chromosome 7q11.23, thought to arise as a consequence of unequal crossing over between highly homologous low-copy repeat sequences flanking the deleted region. Haploinsufficiency of ELN may be the cause of certain cardiovascular and musculo-skeletal abnormalities observed in the disease.

    Keywords - Diseasei

    Williams-Beuren syndrome

    Organism-specific databases

    MIMi123700. phenotype.
    185500. phenotype.
    Orphaneti90348. Autosomal dominant cutis laxa.
    3193. Supravalvular aortic stenosis.
    904. Williams syndrome.
    PharmGKBiPA27757.

    Protein family/group databases

    Allergomei11040. Hom s Elastin.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2626By similarityAdd
    BLAST
    Chaini27 – 786760ElastinPRO_0000021163Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei34 – 341Hydroxyproline1 Publication
    Modified residuei65 – 651Hydroxyproline; partial1 Publication
    Modified residuei67 – 671Hydroxyproline; partial1 Publication
    Modified residuei88 – 881Hydroxyproline; partial1 Publication
    Modified residuei104 – 1041AllysineBy similarity
    Modified residuei116 – 11614-hydroxyproline; partial1 Publication
    Modified residuei156 – 1561Hydroxyproline; partial1 Publication
    Modified residuei167 – 1671Hydroxyproline; partial1 Publication
    Modified residuei170 – 1701Hydroxyproline; partial1 Publication
    Modified residuei177 – 1771Hydroxyproline; partial1 Publication
    Modified residuei190 – 19014-hydroxyproline; partial2 Publications
    Modified residuei241 – 2411AllysineBy similarity
    Modified residuei261 – 2611AllysineBy similarity
    Modified residuei265 – 2651AllysineBy similarity
    Modified residuei283 – 28314-hydroxyproline; partial1 Publication
    Modified residuei286 – 28614-hydroxyproline; partial2 Publications
    Modified residuei290 – 2901Hydroxyproline; partial1 Publication
    Modified residuei312 – 3121AllysineBy similarity
    Modified residuei315 – 3151AllysineBy similarity
    Modified residuei327 – 32714-hydroxyproline; partial1 Publication
    Modified residuei342 – 34214-hydroxyproline; partial1 Publication
    Modified residuei347 – 34714-hydroxyproline; partial1 Publication
    Modified residuei352 – 3521Hydroxyproline; partial1 Publication
    Modified residuei355 – 3551Hydroxyproline; partial1 Publication
    Modified residuei360 – 36014-hydroxyproline; partial1 Publication
    Modified residuei375 – 3751AllysineBy similarity
    Modified residuei379 – 3791AllysineBy similarity
    Modified residuei382 – 3821AllysineBy similarity
    Modified residuei415 – 41514-hydroxyproline; partial1 Publication
    Modified residuei421 – 4211Hydroxyproline; partial1 Publication
    Modified residuei427 – 42714-hydroxyproline; partial2 Publications
    Modified residuei451 – 4511AllysineBy similarity
    Modified residuei465 – 4651Hydroxyproline; partial1 Publication
    Modified residuei467 – 4671Hydroxyproline; partial1 Publication
    Modified residuei481 – 48114-hydroxyproline; partial1 Publication
    Modified residuei492 – 4921AllysineBy similarity
    Modified residuei496 – 4961AllysineBy similarity
    Modified residuei522 – 5221Hydroxyproline; partial1 Publication
    Modified residuei550 – 5501Hydroxyproline; partial1 Publication
    Modified residuei558 – 5581AllysineBy similarity
    Modified residuei562 – 5621AllysineBy similarity
    Modified residuei566 – 5661AllysineBy similarity
    Modified residuei580 – 58014-hydroxyproline; partial2 Publications
    Modified residuei589 – 58914-hydroxyproline1 Publication
    Modified residuei598 – 59814-hydroxyproline1 Publication
    Modified residuei607 – 60714-hydroxyproline; partial1 Publication
    Modified residuei646 – 6461Hydroxyproline; partial1 Publication
    Modified residuei653 – 6531AllysineBy similarity
    Modified residuei656 – 6561AllysineBy similarity
    Modified residuei677 – 67714-hydroxyproline; partial2 Publications
    Modified residuei693 – 6931AllysineBy similarity
    Modified residuei697 – 6971AllysineBy similarity
    Modified residuei735 – 7351AllysineBy similarity
    Modified residuei738 – 7381AllysineBy similarity
    Modified residuei769 – 7691Hydroxyproline; partial1 Publication
    Modified residuei772 – 7721Hydroxyproline; partial1 Publication
    Disulfide bondi776 ↔ 781By similarity

    Post-translational modificationi

    Elastin is formed through the cross-linking of its soluble precursor tropoelastin. Cross-linking is initiated through the action of lysyl oxidase on exposed lysines to form allysine. Subsequent spontaneous condensation reactions with other allysine or unmodified lysine residues result in various bi-, tri-, and tetrafunctional cross-links. The most abundant cross-links in mature elastin fibers are lysinonorleucine, allysine aldol, desmosine, and isodesmosine.
    Hydroxylation on proline residues within the sequence motif, GXPG, is most likely 4-hydroxy as this fits the requirement for 4-hydroxylation in vertebrates.By similarity

    Keywords - PTMi

    Disulfide bond, Hydroxylation

    Proteomic databases

    PaxDbiP15502.
    PRIDEiP15502.

    PTM databases

    PhosphoSiteiP15502.

    Miscellaneous databases

    PMAP-CutDBP15502.

    Expressioni

    Tissue specificityi

    Expressed within the outer myometrial smooth muscle and throughout the arteriolar tree of uterus (at protein level). Also expressed in the large arteries, lung and skin.1 Publication

    Gene expression databases

    ArrayExpressiP15502.
    BgeeiP15502.
    GenevestigatoriP15502.

    Organism-specific databases

    HPAiCAB010750.
    HPA018111.
    HPA056941.

    Interactioni

    Subunit structurei

    The polymeric elastin chains are cross-linked together into an extensible 3D network. Forms a ternary complex with BGN and MFAP2. Interacts with MFAP2 via divalent cations (calcium > magnesium > manganese) in a dose-dependent and saturating manner.

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    EFEMP2O959675EBI-1222108,EBI-743414
    FBLN5Q9UBX53EBI-1222108,EBI-947897
    LOXP283002EBI-1222108,EBI-3893481

    Protein-protein interaction databases

    BioGridi108321. 14 interactions.
    IntActiP15502. 10 interactions.

    Structurei

    3D structure databases

    ProteinModelPortaliP15502.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi97 – 1026Poly-Ala
    Compositional biasi236 – 742507Ala-richAdd
    BLAST

    Sequence similaritiesi

    Belongs to the elastin family.Curated

    Keywords - Domaini

    Repeat, Signal

    Phylogenomic databases

    eggNOGiNOG331579.
    InParanoidiP15502.
    KOiK14211.
    TreeFamiTF338594.

    Family and domain databases

    InterProiIPR003979. Tropoelastin.
    [Graphical view]
    PRINTSiPR01500. TROPOELASTIN.

    Sequences (13)i

    Sequence statusi: Complete.

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

    This entry describes 13 isoformsi produced by alternative splicing. Align

    Note: Additional isoforms seem to exist.

    Isoform 3 (identifier: P15502-3) [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

    MAGLTAAAPR PGVLLLLLSI LHPSRPGGVP GAIPGGVPGG VFYPGAGLGA    50
    LGGGALGPGG KPLKPVPGGL AGAGLGAGLG AFPAVTFPGA LVPGGVADAA 100
    AAYKAAKAGA GLGGVPGVGG LGVSAGAVVP QPGAGVKPGK VPGVGLPGVY 150
    PGGVLPGARF PGVGVLPGVP TGAGVKPKAP GVGGAFAGIP GVGPFGGPQP 200
    GVPLGYPIKA PKLPGGYGLP YTTGKLPYGY GPGGVAGAAG KAGYPTGTGV 250
    GPQAAAAAAA KAAAKFGAGA AGVLPGVGGA GVPGVPGAIP GIGGIAGVGT 300
    PAAAAAAAAA AKAAKYGAAA GLVPGGPGFG PGVVGVPGAG VPGVGVPGAG 350
    IPVVPGAGIP GAAVPGVVSP EAAAKAAAKA AKYGARPGVG VGGIPTYGVG 400
    AGGFPGFGVG VGGIPGVAGV PGVGGVPGVG GVPGVGISPE AQAAAAAKAA 450
    KYGAAGAGVL GGLVPGPQAA VPGVPGTGGV PGVGTPAAAA AKAAAKAAQF 500
    GLVPGVGVAP GVGVAPGVGV APGVGLAPGV GVAPGVGVAP GVGVAPGIGP 550
    GGVAAAAKSA AKVAAKAQLR AAAGLGAGIP GLGVGVGVPG LGVGAGVPGL 600
    GVGAGVPGFG AGADEGVRRS LSPELREGDP SSSQHLPSTP SSPRVPGALA 650
    AAKAAKYGAA VPGVLGGLGA LGGVGIPGGV VGAGPAAAAA AAKAAAKAAQ 700
    FGLVGAAGLG GLGVGGLGVP GVGGLGGIPP AAAAKAAKYG AAGLGGVLGG 750
    AGQFPLGGVA ARPGFGLSPI FPGGACLGKA CGRKRK 786
    Length:786
    Mass (Da):68,469
    Last modified:October 5, 2010 - v3
    Checksum:iD3C6F4EC6BC4991F
    GO
    Isoform 1 (identifier: P15502-1) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         453-481: Missing.
         500-500: F → FALLNLA
         612-644: Missing.

    Show »
    Length:730
    Mass (Da):63,230
    Checksum:iB38B11526A0CB52D
    GO
    Isoform 2 (identifier: P15502-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         453-481: Missing.
         612-644: Missing.

    Show »
    Length:724
    Mass (Da):62,634
    Checksum:i0A7E4424F9EC0F78
    GO
    Isoform 4 (identifier: P15502-4) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         453-481: Missing.

    Show »
    Length:757
    Mass (Da):66,106
    Checksum:i2B24F955D8360738
    GO
    Isoform 5 (identifier: P15502-5) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         125-125: A → AAPSVP
         453-481: Missing.
         612-644: Missing.
         740-757: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:711
    Mass (Da):61,605
    Checksum:i151A0A4E089B3A5C
    GO
    Isoform 6 (identifier: P15502-6) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         453-500: Missing.
         612-644: Missing.
         740-757: Missing.

    Show »
    Length:687
    Mass (Da):59,500
    Checksum:i86446D90C8E2664F
    GO
    Isoform 7 (identifier: P15502-7) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         45-54: Missing.
         453-500: Missing.
         612-644: Missing.
         740-757: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:677
    Mass (Da):58,789
    Checksum:iC5082D1C00A310BA
    GO
    Isoform 8 (identifier: P15502-8) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         215-228: Missing.
         453-500: Missing.
         555-570: AAAKSAAKVAAKAQLR → G
         612-644: Missing.
         740-757: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:658
    Mass (Da):56,551
    Checksum:i5DAFC55566AB809B
    GO
    Isoform 9 (identifier: P15502-9) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         500-500: F → FALLNLA

    Note: No experimental confirmation available.

    Show »
    Length:792
    Mass (Da):69,064
    Checksum:i35AAC849F2DC2EC6
    GO
    Isoform 10 (identifier: P15502-10) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         500-500: F → FALLNLA
         612-644: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:759
    Mass (Da):65,593
    Checksum:iE8E4CBC20D02A185
    GO
    Isoform 11 (identifier: P15502-11) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         78-180: Missing.
         215-228: Missing.
         453-500: Missing.
         612-644: Missing.
         740-757: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:570
    Mass (Da):48,897
    Checksum:i6C9128F3D079D9B0
    GO
    Isoform 12 (identifier: P15502-12) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         125-125: A → AAPSVP
         453-500: Missing.
         612-644: Missing.
         740-757: Missing.

    Show »
    Length:692
    Mass (Da):59,951
    Checksum:i65D038D48352C5E9
    GO
    Isoform 13 (identifier: P15502-13) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         453-500: Missing.
         612-644: Missing.

    Show »
    Length:705
    Mass (Da):60,980
    Checksum:i78F444C823E5F8B4
    GO

    Sequence cautioni

    The sequence CAD98065.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti317 – 3171G → E in CAD97910. (PubMed:17974005)Curated
    Sequence conflicti467 – 4693PQA → APG in AAB65620. (PubMed:9215670)Curated
    Sequence conflicti467 – 4693PQA → APG in AAB65621. (PubMed:9215670)Curated
    Sequence conflicti553 – 5531V → I in BAC85506. (PubMed:14702039)Curated
    Sequence conflicti691 – 6911A → T in CAD98065. (PubMed:17974005)Curated
    Sequence conflicti773 – 7731G → D in CAD97910. (PubMed:17974005)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti422 – 4221G → S.7 Publications
    Corresponds to variant rs2071307 [ dbSNP | Ensembl ].
    VAR_020882
    Natural varianti610 – 6101G → R.2 Publications
    Corresponds to variant rs17855988 [ dbSNP | Ensembl ].
    VAR_056869

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei45 – 5410Missing in isoform 7. 1 PublicationVSP_012479
    Alternative sequencei78 – 180103Missing in isoform 11. 1 PublicationVSP_012480Add
    BLAST
    Alternative sequencei125 – 1251A → AAPSVP in isoform 5 and isoform 12. 2 PublicationsVSP_012481
    Alternative sequencei215 – 22814Missing in isoform 8 and isoform 11. 2 PublicationsVSP_012482Add
    BLAST
    Alternative sequencei453 – 50048Missing in isoform 6, isoform 7, isoform 8, isoform 11, isoform 12 and isoform 13. 4 PublicationsVSP_012483Add
    BLAST
    Alternative sequencei453 – 48129Missing in isoform 1, isoform 2, isoform 4 and isoform 5. 3 PublicationsVSP_012484Add
    BLAST
    Alternative sequencei500 – 5001F → FALLNLA in isoform 1, isoform 9 and isoform 10. 1 PublicationVSP_012485
    Alternative sequencei555 – 57016AAAKS…KAQLR → G in isoform 8. 1 PublicationVSP_012486Add
    BLAST
    Alternative sequencei612 – 64433Missing in isoform 1, isoform 2, isoform 5, isoform 6, isoform 7, isoform 8, isoform 10, isoform 11, isoform 12 and isoform 13. 6 PublicationsVSP_012487Add
    BLAST
    Alternative sequencei740 – 75718Missing in isoform 5, isoform 6, isoform 7, isoform 8, isoform 11 and isoform 12. 3 PublicationsVSP_012488Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M17282
    , M16983, M17265, M17266, M17267, M17268, M17271, M17272, M17273, M17275, M17276, M17277, M17278, M17279, M17281 Genomic DNA. Translation: AAC98393.1.
    M17282
    , M16983, M17265, M17266, M17267, M17268, M17270, M17271, M17272, M17273, M17275, M17276, M17277, M17278, M17279, M17280, M17281 Genomic DNA. Translation: AAC98394.1.
    M17282
    , M16983, M17265, M17266, M17267, M17268, M17270, M17271, M17272, M17273, M17274, M17275, M17276, M17277, M17278, M17279, M17280, M17281 Genomic DNA. Translation: AAC98395.1.
    M36860 mRNA. Translation: AAA52382.1.
    AK095990 mRNA. Translation: BAG53188.1.
    AK122731 mRNA. Translation: BAC85506.1.
    BX537939 mRNA. Translation: CAD97910.1.
    BX538199 mRNA. Translation: CAD98065.1. Different initiation.
    AK225659 mRNA. No translation available.
    AC005056 Genomic DNA. Translation: AAS07435.1.
    CH471200 Genomic DNA. Translation: EAW69627.1.
    BC065566 mRNA. Translation: AAH65566.1.
    X15603 Genomic DNA. Translation: CAA33627.1.
    U93037
    , U93034, U93035, U93036 Genomic DNA. Translation: AAB65620.1.
    U93037
    , U93034, U93035, U93036 Genomic DNA. Translation: AAB65621.1.
    M24782 mRNA. Translation: AAA53190.1.
    U63721 Genomic DNA. Translation: AAC13884.1.
    U62292 Genomic DNA. Translation: AAB17544.1.
    CCDSiCCDS43598.1. [P15502-5]
    CCDS43599.1. [P15502-7]
    CCDS47611.1. [P15502-12]
    CCDS47612.1. [P15502-13]
    CCDS5562.2. [P15502-2]
    CCDS64673.1. [P15502-1]
    CCDS64675.1. [P15502-8]
    PIRiA32707. EAHU.
    RefSeqiNP_000492.2. NM_000501.3. [P15502-2]
    NP_001075221.1. NM_001081752.2. [P15502-7]
    NP_001075222.1. NM_001081753.2. [P15502-12]
    NP_001075223.1. NM_001081754.2. [P15502-5]
    NP_001075224.1. NM_001081755.2. [P15502-13]
    NP_001265844.1. NM_001278915.1. [P15502-1]
    NP_001265845.1. NM_001278916.1. [P15502-8]
    UniGeneiHs.647061.

    Genome annotation databases

    EnsembliENST00000252034; ENSP00000252034; ENSG00000049540. [P15502-2]
    ENST00000320399; ENSP00000313565; ENSG00000049540. [P15502-4]
    ENST00000357036; ENSP00000349540; ENSG00000049540. [P15502-5]
    ENST00000380553; ENSP00000369926; ENSG00000049540. [P15502-11]
    ENST00000380562; ENSP00000369936; ENSG00000049540. [P15502-1]
    ENST00000380575; ENSP00000369949; ENSG00000049540. [P15502-7]
    ENST00000380576; ENSP00000369950; ENSG00000049540. [P15502-13]
    ENST00000380584; ENSP00000369958; ENSG00000049540. [P15502-8]
    ENST00000429192; ENSP00000391129; ENSG00000049540. [P15502-12]
    GeneIDi2006.
    KEGGihsa:2006.
    UCSCiuc003tzn.3. human. [P15502-2]
    uc003tzo.3. human. [P15502-8]
    uc003tzq.3. human. [P15502-11]
    uc003tzs.3. human. [P15502-13]
    uc003tzt.3. human. [P15502-5]
    uc003tzu.3. human. [P15502-12]
    uc003tzv.3. human. [P15502-7]
    uc003tzw.3. human. [P15502-1]

    Polymorphism databases

    DMDMi306526276.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Web resourcesi

    Wikipedia

    Elastin entry

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M17282
    , M16983 , M17265 , M17266 , M17267 , M17268 , M17271 , M17272 , M17273 , M17275 , M17276 , M17277 , M17278 , M17279 , M17281 Genomic DNA. Translation: AAC98393.1 .
    M17282
    , M16983 , M17265 , M17266 , M17267 , M17268 , M17270 , M17271 , M17272 , M17273 , M17275 , M17276 , M17277 , M17278 , M17279 , M17280 , M17281 Genomic DNA. Translation: AAC98394.1 .
    M17282
    , M16983 , M17265 , M17266 , M17267 , M17268 , M17270 , M17271 , M17272 , M17273 , M17274 , M17275 , M17276 , M17277 , M17278 , M17279 , M17280 , M17281 Genomic DNA. Translation: AAC98395.1 .
    M36860 mRNA. Translation: AAA52382.1 .
    AK095990 mRNA. Translation: BAG53188.1 .
    AK122731 mRNA. Translation: BAC85506.1 .
    BX537939 mRNA. Translation: CAD97910.1 .
    BX538199 mRNA. Translation: CAD98065.1 . Different initiation.
    AK225659 mRNA. No translation available.
    AC005056 Genomic DNA. Translation: AAS07435.1 .
    CH471200 Genomic DNA. Translation: EAW69627.1 .
    BC065566 mRNA. Translation: AAH65566.1 .
    X15603 Genomic DNA. Translation: CAA33627.1 .
    U93037
    , U93034 , U93035 , U93036 Genomic DNA. Translation: AAB65620.1 .
    U93037
    , U93034 , U93035 , U93036 Genomic DNA. Translation: AAB65621.1 .
    M24782 mRNA. Translation: AAA53190.1 .
    U63721 Genomic DNA. Translation: AAC13884.1 .
    U62292 Genomic DNA. Translation: AAB17544.1 .
    CCDSi CCDS43598.1. [P15502-5 ]
    CCDS43599.1. [P15502-7 ]
    CCDS47611.1. [P15502-12 ]
    CCDS47612.1. [P15502-13 ]
    CCDS5562.2. [P15502-2 ]
    CCDS64673.1. [P15502-1 ]
    CCDS64675.1. [P15502-8 ]
    PIRi A32707. EAHU.
    RefSeqi NP_000492.2. NM_000501.3. [P15502-2 ]
    NP_001075221.1. NM_001081752.2. [P15502-7 ]
    NP_001075222.1. NM_001081753.2. [P15502-12 ]
    NP_001075223.1. NM_001081754.2. [P15502-5 ]
    NP_001075224.1. NM_001081755.2. [P15502-13 ]
    NP_001265844.1. NM_001278915.1. [P15502-1 ]
    NP_001265845.1. NM_001278916.1. [P15502-8 ]
    UniGenei Hs.647061.

    3D structure databases

    ProteinModelPortali P15502.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 108321. 14 interactions.
    IntActi P15502. 10 interactions.

    Chemistry

    DrugBanki DB00533. Rofecoxib.

    Protein family/group databases

    Allergomei 11040. Hom s Elastin.

    PTM databases

    PhosphoSitei P15502.

    Polymorphism databases

    DMDMi 306526276.

    Proteomic databases

    PaxDbi P15502.
    PRIDEi P15502.

    Protocols and materials databases

    DNASUi 2006.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000252034 ; ENSP00000252034 ; ENSG00000049540 . [P15502-2 ]
    ENST00000320399 ; ENSP00000313565 ; ENSG00000049540 . [P15502-4 ]
    ENST00000357036 ; ENSP00000349540 ; ENSG00000049540 . [P15502-5 ]
    ENST00000380553 ; ENSP00000369926 ; ENSG00000049540 . [P15502-11 ]
    ENST00000380562 ; ENSP00000369936 ; ENSG00000049540 . [P15502-1 ]
    ENST00000380575 ; ENSP00000369949 ; ENSG00000049540 . [P15502-7 ]
    ENST00000380576 ; ENSP00000369950 ; ENSG00000049540 . [P15502-13 ]
    ENST00000380584 ; ENSP00000369958 ; ENSG00000049540 . [P15502-8 ]
    ENST00000429192 ; ENSP00000391129 ; ENSG00000049540 . [P15502-12 ]
    GeneIDi 2006.
    KEGGi hsa:2006.
    UCSCi uc003tzn.3. human. [P15502-2 ]
    uc003tzo.3. human. [P15502-8 ]
    uc003tzq.3. human. [P15502-11 ]
    uc003tzs.3. human. [P15502-13 ]
    uc003tzt.3. human. [P15502-5 ]
    uc003tzu.3. human. [P15502-12 ]
    uc003tzv.3. human. [P15502-7 ]
    uc003tzw.3. human. [P15502-1 ]

    Organism-specific databases

    CTDi 2006.
    GeneCardsi GC07P073442.
    GeneReviewsi ELN.
    H-InvDB HIX0006761.
    HGNCi HGNC:3327. ELN.
    HPAi CAB010750.
    HPA018111.
    HPA056941.
    MIMi 123700. phenotype.
    130160. gene.
    185500. phenotype.
    neXtProti NX_P15502.
    Orphaneti 90348. Autosomal dominant cutis laxa.
    3193. Supravalvular aortic stenosis.
    904. Williams syndrome.
    PharmGKBi PA27757.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG331579.
    InParanoidi P15502.
    KOi K14211.
    TreeFami TF338594.

    Enzyme and pathway databases

    Reactomei REACT_118572. Degradation of the extracellular matrix.
    REACT_150331. Molecules associated with elastic fibres.
    REACT_150366. Elastic fibre formation.

    Miscellaneous databases

    ChiTaRSi ELN. human.
    GeneWikii Elastin.
    GenomeRNAii 2006.
    NextBioi 8119.
    PMAP-CutDB P15502.
    PROi P15502.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P15502.
    Bgeei P15502.
    Genevestigatori P15502.

    Family and domain databases

    InterProi IPR003979. Tropoelastin.
    [Graphical view ]
    PRINTSi PR01500. TROPOELASTIN.
    ProtoNeti Search...

    Publicationsi

    1. "Alternative splicing of human elastin mRNA indicated by sequence analysis of cloned genomic and complementary DNA."
      Indik Z., Yeh H., Ornstein-Goldstein N., Sheppard P., Anderson N., Rosenbloom J.C., Peltonen L., Rosenbloom J.
      Proc. Natl. Acad. Sci. U.S.A. 84:5680-5684(1987) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORMS 2; 3; 4 AND 6), VARIANT SER-422.
    2. "Cloning of full-length elastin cDNAs from a human skin fibroblast recombinant cDNA library: further elucidation of alternative splicing utilizing exon-specific oligonucleotides."
      Fazio M.J., Olsen D.R., Kauh E.A., Baldwin C.T., Indik Z., Ornstein-Goldstein N., Yeh H., Rosenbloom J., Uitto J.
      J. Invest. Dermatol. 91:458-464(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT SER-422.
      Tissue: Skin fibroblast.
    3. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 11 AND 12), VARIANT SER-422.
    4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 5 AND 7).
      Tissue: Fetal kidney.
    5. Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.
      Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 13).
      Tissue: Gastric mucosa.
    6. "The DNA sequence of human chromosome 7."
      Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H., Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K., Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A., Delehaunty K.D., Miner T.L.
      , Nash W.E., Cordes M., Du H., Sun H., Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A., Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P., Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M., Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S., Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., Strowmatt C., Latreille P., Miller N., Johnson D., Murray J., Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E., Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E., Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A., Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A., Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R., McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H., Wilson R.K.
      Nature 424:157-164(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    7. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    8. "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 8), VARIANTS SER-422 AND ARG-610.
      Tissue: Eye.
    9. "Characterization of the complete human elastin gene. Delineation of unusual features in the 5'-flanking region."
      Bashir M.M., Indik Z., Yeh H., Ornstein-Goldstein N., Rosenbloom J.C., Abrams W., Fazio M., Uitto J., Rosenbloom J.
      J. Biol. Chem. 264:8887-8891(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE OF 1-27.
    10. Bressan G.M.
      Submitted (JUN-1989) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE OF 1-27.
    11. Bressan G.M.
      Submitted (OCT-1991) to the EMBL/GenBank/DDBJ databases
      Cited for: SEQUENCE REVISION.
    12. "Elastin point mutations cause an obstructive vascular disease, supravalvular aortic stenosis."
      Li D.Y., Toland A.E., Boak B.B., Atkinson D.L., Ensing G.J., Morris C.A., Keating M.T.
      Hum. Mol. Genet. 6:1021-1028(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 29-657 (ISOFORMS 9 AND 10), VARIANTS SER-422 AND ARG-610.
    13. "Isolation and characterization of human elastin cDNAs, and age-associated variation in elastin gene expression in cultured skin fibroblasts."
      Fazio M.J., Olsen D.R., Kuivaniemi H., Chu M.L., Davidson J.M., Rosenbloom J., Uitto J.
      Lab. Invest. 58:270-277(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 164-724 (ISOFORM 2), VARIANT SER-422.
      Tissue: Placenta.
    14. "Identification of genes from a 500-kb region at 7q11.23 that is commonly deleted in Williams syndrome patients."
      Osborne L.R., Martindale D.W., Scherer S.W., Shi X.-M., Huizenga J., Heng H.H.Q., Costa T., Pober B., Lew L., Brinkman J., Rommens J., Koop B.F., Tsui L.-C.
      Genomics 36:328-336(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 496-786 (ISOFORM 1/10), TISSUE SPECIFICITY.
    15. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 659-786, VARIANT SER-422.
      Tissue: Hippocampus and Placenta.
    16. "Cutis laxa arising from frameshift mutations in exon 30 of the elastin gene (ELN)."
      Zhang M.-C., He L., Giro M., Yong S.L., Tiller G.E., Davidson J.M.
      J. Biol. Chem. 274:981-986(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: INVOLVEMENT IN ADCL1.
    17. "Isolated supravalvular aortic stenosis: functional haploinsufficiency of the elastin gene as a result of nonsense-mediated decay."
      Urban Z., Michels V.V., Thibodeau S.N., Davis E.C., Bonnefont J.-P., Munnich A., Eyskens B., Gewillig M., Devriendt K., Boyd C.D.
      Hum. Genet. 106:577-588(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: INVOLVEMENT IN SVAS.
    18. "Mass spectrometric characterization of human skin elastin peptides produced by proteolytic digestion with pepsin and thermitase."
      Schmelzer C.E.H., Getie M., Neubert R.H.H.
      J. Chromatogr. A 1083:120-126(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: HYDROXYLATION AT PRO-65; PRO-67; PRO-88; PRO-116; PRO-156; PRO-177; PRO-190; PRO-286; PRO-290; PRO-415; PRO-427; PRO-465; PRO-467; PRO-481; PRO-522; PRO-580; PRO-607; PRO-646; PRO-677; PRO-769 AND PRO-772, IDENTIFICATION BY MASS SPECTROMETRY.
    19. "Characterization of peptides resulting from digestion of human skin elastin with elastase."
      Getie M., Schmelzer C.E.H., Neubert R.H.H.
      Proteins 61:649-657(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: HYDROXYLATION AT PRO-34; PRO-167; PRO-170; PRO-190; PRO-283; PRO-286; PRO-327; PRO-342; PRO-347; PRO-352; PRO-355; PRO-360; PRO-421; PRO-427; PRO-550; PRO-580; PRO-589; PRO-598 AND PRO-677, IDENTIFICATION BY MASS SPECTROMETRY.

    Entry informationi

    Entry nameiELN_HUMAN
    AccessioniPrimary (citable) accession number: P15502
    Secondary accession number(s): B3KTS6
    , O15336, O15337, Q14233, Q14234, Q14235, Q14238, Q6P0L4, Q6ZWJ6, Q75MU5, Q7Z316, Q7Z3F5, Q9UMF5
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 1, 1990
    Last sequence update: October 5, 2010
    Last modified: October 1, 2014
    This is version 165 of the entry and version 3 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

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Human chromosome 7
      Human chromosome 7: 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