Reviewed,
UniProtKB/Swiss-Prot P15502 (ELN_HUMAN)
Last modified
June 16, 2009.
Version 113.
History...
Clusters with 100%,
90%,
50% identity |
Documents (5) |
Third-party data |
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Names and origin
| Protein names | Recommended name: Elastin Alternative name(s): Tropoelastin | ||
| Gene names |
| ||
| Organism | Homo sapiens (Human) | ||
| Taxonomic identifier | 9606 [NCBI] | ||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo |
Protein attributes
| Sequence length | 786 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is further processed into a mature form. |
| Protein existence | Evidence at protein level. |
General annotation (Comments)
| Function | 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. |
| Subunit structure | 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. |
| Subcellular location | Secreted › extracellular space › extracellular matrix. Note: Extracellular matrix of elastic fibers. |
| Tissue specificity | 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. Ref.12 |
| Post-translational modification | 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. |
| Involvement in disease | Defects in ELN are a cause of autosomal dominant cutis laxa [MIM:123700]. Cutis laxa is a rare connective tissue disorder characterized by loose, hyperextensible skin with decreased resilience and elasticity leading to a premature aged appearance. The skin changes are often accompanied by extracutaneous manifestations, including pulmonary emphysema, bladder diverticula, pulmonary artery stenosis and pyloric stenosis. Haploinsufficiency of ELN may be the cause of certain cardiovascular and musculo-skeletal abnormalities observed in Williams-Beuren syndrome (WBS) [MIM:194050]. WBS is a rare developmental disorder and a contiguous gene deletion syndrome involving genes from chromosome band 7q11.23. Defects in ELN are the cause of supravalvular aortic stenosis (SVAS) [MIM:185500]. SVAS is a congenital narrowing of the ascending aorta which can occur sporadically, as an autosomal dominant condition, or as one component of Williams-Beuren syndrome. Ref.15 |
| Sequence similarities | Belongs to the elastin family. |
Ontologies
| Keywords | |
|---|---|
| Cellular component | Extracellular matrix Secreted |
| Coding sequence diversity | Alternative splicing Polymorphism |
| Disease | Williams-Beuren syndrome |
| Domain | Repeat Signal |
| PTM | Disulfide bond Hydroxylation |
| Gene Ontology (GO) | |
| Biological process | blood circulation Ref.14 Traceable author statement. Source: ProtInc cell proliferationTraceable author statement. Source: ProtInc organ morphogenesisTraceable author statement. Source: ProtInc respiratory gaseous exchange Ref.14Traceable author statement. Source: ProtInc |
| Cellular component | extracellular space Inferred from electronic annotation. Source: UniProtKB-SubCell proteinaceous extracellular matrixNon-traceable author statement. Source: UniProtKB |
| Molecular function | extracellular matrix constituent conferring elasticity Non-traceable author statement. Source: UniProtKB |
| Complete GO annotation... | |
Alternative products
| This entry describes 11 isoforms produced by alternative splicing. [Align] [Select] Note: Additional isoforms seem to exist. | ||||||
| Isoform 3 (identifier: P15502-3) This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry. | ||||||
| Isoform 1 (identifier: P15502-1) The sequence of this isoform differs from the canonical sequence as follows: 453-481: Missing. 500-500: F → FALLNLA 612-644: Missing. | ||||||
| Isoform 2 (identifier: P15502-2) The sequence of this isoform differs from the canonical sequence as follows: 453-481: Missing. 612-644: Missing. | ||||||
| Isoform 4 (identifier: P15502-4) The sequence of this isoform differs from the canonical sequence as follows: 453-481: Missing. | ||||||
| Isoform 5 (identifier: P15502-5) 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. | ||||||
| Isoform 6 (identifier: P15502-6) The sequence of this isoform differs from the canonical sequence as follows: 453-500: Missing. 612-644: Missing. 740-757: Missing. | ||||||
| Isoform 7 (identifier: P15502-7) 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. | ||||||
| Isoform 8 (identifier: P15502-8) 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. | ||||||
| Isoform 9 (identifier: P15502-9) The sequence of this isoform differs from the canonical sequence as follows: 500-500: F → FALLNLA | ||||||
| Note: No experimental confirmation available. | ||||||
| Isoform 10 (identifier: P15502-10) The sequence of this isoform differs from the canonical sequence as follows: 500-500: F → FALLNLA 612-644: Missing. | ||||||
| Note: No experimental confirmation available. | ||||||
| Isoform 11 (identifier: P15502-11) 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. |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||||
Molecule processing | |||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|
| Signal peptide | 1 – 26 | 26 | By similarity | ||||||||
| Chain | 27 – 786 | 760 | Elastin | PRO_0000021163 | |||||||
Regions | |||||||||||
| Compositional bias | 97 – 102 | 6 | Poly-Ala | ||||||||
| Compositional bias | 236 – 742 | 507 | Ala-rich | ||||||||
Amino acid modifications | |||||||||||
| Modified residue | 34 | 1 | Hydroxyproline | ||||||||
| Modified residue | 65 | 1 | Hydroxyproline; partial | ||||||||
| Modified residue | 67 | 1 | Hydroxyproline; partial | ||||||||
| Modified residue | 88 | 1 | Hydroxyproline; partial | ||||||||
| Modified residue | 104 | 1 | Allysine By similarity | ||||||||
| Modified residue | 116 | 1 | 4-hydroxyproline; partial Ref.16 | ||||||||
| Modified residue | 156 | 1 | Hydroxyproline; partial | ||||||||
| Modified residue | 167 | 1 | Hydroxyproline; partial | ||||||||
| Modified residue | 170 | 1 | Hydroxyproline; partial | ||||||||
| Modified residue | 177 | 1 | Hydroxyproline; partial | ||||||||
| Modified residue | 190 | 1 | 4-hydroxyproline; partial Ref.16 Ref.17 | ||||||||
| Modified residue | 241 | 1 | Allysine By similarity | ||||||||
| Modified residue | 261 | 1 | Allysine By similarity | ||||||||
| Modified residue | 265 | 1 | Allysine By similarity | ||||||||
| Modified residue | 283 | 1 | 4-hydroxyproline; partial Ref.17 | ||||||||
| Modified residue | 286 | 1 | 4-hydroxyproline; partial Ref.16 Ref.17 | ||||||||
| Modified residue | 290 | 1 | Hydroxyproline; partial | ||||||||
| Modified residue | 312 | 1 | Allysine By similarity | ||||||||
| Modified residue | 315 | 1 | Allysine By similarity | ||||||||
| Modified residue | 327 | 1 | 4-hydroxyproline; partial Ref.17 | ||||||||
| Modified residue | 342 | 1 | 4-hydroxyproline; partial Ref.17 | ||||||||
| Modified residue | 347 | 1 | 4-hydroxyproline; partial Ref.17 | ||||||||
| Modified residue | 352 | 1 | Hydroxyproline; partial | ||||||||
| Modified residue | 355 | 1 | Hydroxyproline; partial | ||||||||
| Modified residue | 360 | 1 | 4-hydroxyproline; partial Ref.17 | ||||||||
| Modified residue | 375 | 1 | Allysine By similarity | ||||||||
| Modified residue | 379 | 1 | Allysine By similarity | ||||||||
| Modified residue | 382 | 1 | Allysine By similarity | ||||||||
| Modified residue | 415 | 1 | 4-hydroxyproline; partial Ref.16 | ||||||||
| Modified residue | 421 | 1 | Hydroxyproline; partial | ||||||||
| Modified residue | 427 | 1 | 4-hydroxyproline; partial Ref.16 Ref.17 | ||||||||
| Modified residue | 451 | 1 | Allysine By similarity | ||||||||
| Modified residue | 465 | 1 | Hydroxyproline; partial | ||||||||
| Modified residue | 467 | 1 | Hydroxyproline; partial | ||||||||
| Modified residue | 481 | 1 | 4-hydroxyproline; partial Ref.16 | ||||||||
| Modified residue | 492 | 1 | Allysine By similarity | ||||||||
| Modified residue | 496 | 1 | Allysine By similarity | ||||||||
| Modified residue | 522 | 1 | Hydroxyproline; partial | ||||||||
| Modified residue | 550 | 1 | Hydroxyproline; partial | ||||||||
| Modified residue | 558 | 1 | Allysine By similarity | ||||||||
| Modified residue | 562 | 1 | Allysine By similarity | ||||||||
| Modified residue | 566 | 1 | Allysine By similarity | ||||||||
| Modified residue | 580 | 1 | 4-hydroxyproline; partial Ref.16 Ref.17 | ||||||||
| Modified residue | 589 | 1 | 4-hydroxyproline Probable | ||||||||
| Modified residue | 598 | 1 | 4-hydroxyproline Probable | ||||||||
| Modified residue | 607 | 1 | 4-hydroxyproline; partial Ref.16 | ||||||||
| Modified residue | 646 | 1 | Hydroxyproline; partial | ||||||||
| Modified residue | 653 | 1 | Allysine By similarity | ||||||||
| Modified residue | 656 | 1 | Allysine By similarity | ||||||||
| Modified residue | 677 | 1 | 4-hydroxyproline; partial Ref.16 Ref.17 | ||||||||
| Modified residue | 693 | 1 | Allysine By similarity | ||||||||
| Modified residue | 697 | 1 | Allysine By similarity | ||||||||
| Modified residue | 735 | 1 | Allysine By similarity | ||||||||
| Modified residue | 738 | 1 | Allysine By similarity | ||||||||
| Modified residue | 769 | 1 | Hydroxyproline; partial | ||||||||
| Modified residue | 772 | 1 | Hydroxyproline; partial | ||||||||
| Disulfide bond | 776 ↔ 781 | By similarity | |||||||||
Natural variations | |||||||||||
| Alternative sequence | 45 – 54 | 10 | Missing in isoform 7. | VSP_012479 | |||||||
| Alternative sequence | 78 – 180 | 103 | Missing in isoform 11. | VSP_012480 | |||||||
| Alternative sequence | 125 | 1 | A → AAPSVP in isoform 5. | VSP_012481 | |||||||
| Alternative sequence | 215 – 228 | 14 | Missing in isoform 8 and isoform 11. | VSP_012482 | |||||||
| Alternative sequence | 453 – 500 | 48 | Missing in isoform 6, isoform 7, isoform 8 and isoform 11. | VSP_012483 | |||||||
| Alternative sequence | 453 – 481 | 29 | Missing in isoform 1, isoform 2, isoform 4 and isoform 5. | VSP_012484 | |||||||
| Alternative sequence | 500 | 1 | F → FALLNLA in isoform 1, isoform 9 and isoform 10. | VSP_012485 | |||||||
| Alternative sequence | 555 – 570 | 16 | AAAKS…KAQLR → G in isoform 8. | VSP_012486 | |||||||
| Alternative sequence | 612 – 644 | 33 | Missing in isoform 1, isoform 2, isoform 5, isoform 6, isoform 7, isoform 8, isoform 10 and isoform 11. | VSP_012487 | |||||||
| Alternative sequence | 740 – 757 | 18 | Missing in isoform 5, isoform 6, isoform 7, isoform 8 and isoform 11. | VSP_012488 | |||||||
| Natural variant | 422 | 1 | S → G: dbSNP rs2071307. Ref.3 Ref.5 | VAR_020882 | |||||||
| Natural variant | 610 | 1 | G → R: dbSNP rs17855988. | VAR_056869 | |||||||
Experimental info | |||||||||||
| Sequence conflict | 317 | 1 | G → E in CAD97910. Ref.4 | ||||||||
| Sequence conflict | 467 – 469 | 3 | PQA → APG in AAB65620. Ref.10 | ||||||||
| Sequence conflict | 467 – 469 | 3 | PQA → APG in AAB65621. Ref.10 | ||||||||
| Sequence conflict | 553 | 1 | V → I in BAC85506. Ref.3 | ||||||||
| Sequence conflict | 691 | 1 | A → T in CAD98065. Ref.4 | ||||||||
| Sequence conflict | 773 | 1 | G → D in CAD97910. Ref.4 | ||||||||
Sequences
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References
| « Hide 'large scale' references | |
| [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: 3039501] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORMS 2; 3; 4 AND 6). |
| [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: 3171221] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). 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. Sugano S.Nat. Genet. 36:40-45(2004) [PubMed: 14702039] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 11). |
| [4] | "The full-ORF clone resource of the German cDNA consortium." Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Blocker H., Heubner D., Hoerlein A., Michel G., Wedler H., Kohrer K., Ottenwalder B., Poustka A., Wiemann S., Schupp I. BMC Genomics 8:399-399(2007) [PubMed: 17974005] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 5 AND 7), VARIANT GLY-422. Tissue: Fetal kidney. |
| [5] | "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. Wilson R.K.Nature 424:157-164(2003) [PubMed: 12853948] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], VARIANT GLY-422. |
| [6] | "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 8), VARIANT ARG-610. Tissue: Eye. |
| [7] | "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: 2722804] [Abstract] Cited for: NUCLEOTIDE SEQUENCE OF 1-27. |
| [8] | Bressan G.M. Submitted (JUN-1989) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE OF 1-27. |
| [9] | Bressan G.M. Submitted (OCT-1991) to the EMBL/GenBank/DDBJ databases Cited for: SEQUENCE REVISION. |
| [10] | "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: 9215670] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 29-657 (ISOFORMS 9 AND 10), VARIANT ARG-610. |
| [11] | "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: 2831431] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 164-724 (ISOFORM 2). Tissue: Placenta. |
| [12] | "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: 8812460] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 500-786, TISSUE SPECIFICITY. |
| [13] | "LIM-kinase1 hemizygosity implicated in impaired visuospatial constructive cognition." Frangiskakis J.M., Ewart A.K., Morris C.A., Mervis C.B., Bertrand J., Robinson B.F., Klein B.P., Ensing G.J., Everett L.A., Green E.D., Proeschel C., Gutowski N.J., Noble M., Atkinson D.L., Odelberg S.J., Keating M.T. Cell 86:59-69(1996) [PubMed: 8689688] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 659-786. Tissue: Hippocampus and Placenta. |
| [14] | "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: 9873040] [Abstract] Cited for: INVOLVEMENT IN CUTIS LAXA. |
| [15] | "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: 10942104] [Abstract] Cited for: INVOLVEMENT IN SVAS. |
| [16] | "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: 16078697] [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, MASS SPECTROMETRY. |
| [17] | "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: 16161116] [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, MASS SPECTROMETRY. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |
|---|---|
M17282 M17281 Genomic DNA. Translation: AAC98393.1. M17282 M17281 Genomic DNA. Translation: AAC98394.1. M17282 M17281 Genomic DNA. Translation: AAC98395.1. M36860 mRNA. Translation: AAA52382.1. AK122731 mRNA. Translation: BAC85506.1. BX537939 mRNA. Translation: CAD97910.1. BX538199 mRNA. Translation: CAD98065.1. Different initiation. AC005056 Genomic DNA. Translation: AAS07435.1. BC065566 mRNA. Translation: AAH65566.1. X15603 Genomic DNA. Translation: CAA33627.1. U93037 U93036 Genomic DNA. Translation: AAB65620.1. U93037 U93036 Genomic DNA. Translation: AAB65621.1. M24782 mRNA. Translation: AAA53190.1. U63721 Genomic DNA. Translation: AAC13884.1. Different initiation. U62292 Genomic DNA. Translation: AAB17544.1. | |
| IPI | IPI00163202. IPI00177942. IPI00446835. IPI00472548. IPI00513726. IPI00514114. IPI00514196. IPI00514508. IPI00514851. IPI00515021. IPI00925620. |
| PIR | EAHU. A32707. |
| RefSeq | NP_001075221.1. |
| UniGene | Hs.647061 |
3D structure databases | |
| HSSP | HSSP built from PDB template 1ZFJ based on UniProtKB P50099. |
| ModBase | Search... |
PTM databases | |
| PhosphoSite | P15502. |
Proteomic databases | |
| PRIDE | P15502. |
Genome annotation databases | |
| Ensembl | ENSG00000049540. Homo sapiens. [Contig view] |
| GeneID | 2006. |
Organism-specific databases | |
| GeneCards | GC07P073080. |
| H-InvDB | HIX0006761. HIX0019421. |
| HGNC | HGNC:3327. ELN. |
| HPA | CAB010750. HPA018111. |
| MIM | 123700. phenotype. 130160. gene. 185500. phenotype. 194050. phenotype. |
| Orphanet | 209. Cutis laxa. 90348. Cutis laxa, dominant type. 3193. Supravalvar aortic stenosis. 904. Williams syndrome. |
| PharmGKB | PA27757. |
| GenAtlas | Search... |
Phylogenomic databases | |
| HOVERGEN | P15502. |
Gene expression databases | |
| ArrayExpress | P15502. |
| Bgee | P15502. |
| GermOnline | ENSG00000049540. Homo sapiens. |
Family and domain databases | |
| InterPro | IPR003979. Tropoelastin. [Graphical view] |
| PRINTS | PR01500. TROPOELASTIN. |
| ProtoNet | Search... |
Other Resources | |
| DrugBank | DB00533. Rofecoxib. |
| NextBio | 8119. |
| PMAP-CutDB | P15502. |
| SOURCE | Search... |
Entry information
| Entry name | ELN_HUMAN | ||||||||
| Accession | Primary (citable) accession number: P15502 Secondary accession number(s): O15336 Q9UMF5 | ||||||||
| Entry history |
| ||||||||
| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HPI (Human Proteome Initiative) | ||||||||
Relevant documents
| Human chromosome 7 Human chromosome 7: entries, gene names and cross-references to MIM |
| Human entries with polymorphisms or disease mutations List of human entries with polymorphisms or disease mutations |
| Human polymorphisms and disease mutations Index of human polymorphisms and disease mutations |
| MIM cross-references Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot |
| SIMILARITY comments Index of protein domains and families |

Clusters with


