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P15502 (ELN_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 163. Feed History...

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

Names and origin

Protein namesRecommended name:
Elastin
Alternative name(s):
Tropoelastin
Gene names
Name:ELN
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length786 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence 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

Secretedextracellular spaceextracellular 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.14

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

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.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.16

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.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.17

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.

Sequence similarities

Belongs to the elastin family.

Sequence caution

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

Ontologies

Keywords
   Cellular componentExtracellular matrix
Secreted
   Coding sequence diversityAlternative splicing
Polymorphism
   DiseaseWilliams-Beuren syndrome
   DomainRepeat
Signal
   PTMDisulfide bond
Hydroxylation
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processblood circulation

Traceable author statement PubMed 8096434Ref.16. Source: ProtInc

blood vessel remodeling

Inferred from electronic annotation. Source: Ensembl

cell proliferation

Traceable author statement PubMed 9607766. Source: ProtInc

extracellular matrix disassembly

Traceable author statement. Source: Reactome

extracellular matrix organization

Traceable author statement. Source: Reactome

organ morphogenesis

Traceable author statement PubMed 9580666. Source: ProtInc

regulation of actin filament polymerization

Inferred from electronic annotation. Source: Ensembl

respiratory gaseous exchange

Traceable author statement Ref.16. Source: ProtInc

skeletal muscle tissue development

Inferred from electronic annotation. Source: Ensembl

stress fiber assembly

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentelastic fiber

Inferred from direct assay PubMed 10424889. Source: BHF-UCL

extracellular region

Traceable author statement. Source: Reactome

mitochondrion

Inferred from electronic annotation. Source: Ensembl

proteinaceous extracellular matrix

Traceable author statement PubMed 9580666. Source: ProtInc

   Molecular_functionextracellular matrix binding

Inferred from electronic annotation. Source: Ensembl

extracellular matrix constituent conferring elasticity

Inferred from electronic annotation. Source: Ensembl

extracellular matrix structural constituent

Traceable author statement PubMed 9580666. Source: ProtInc

protein binding

Inferred from physical interaction PubMed 19570982. Source: IntAct

Complete GO annotation...

Binary interactions

Alternative products

This entry describes 13 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.
Isoform 12 (identifier: P15502-12)

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.
Isoform 13 (identifier: P15502-13)

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2626 By similarity
Chain27 – 786760Elastin
PRO_0000021163

Regions

Compositional bias97 – 1026Poly-Ala
Compositional bias236 – 742507Ala-rich

Amino acid modifications

Modified residue341Hydroxyproline
Modified residue651Hydroxyproline; partial
Modified residue671Hydroxyproline; partial
Modified residue881Hydroxyproline; partial
Modified residue1041Allysine By similarity
Modified residue11614-hydroxyproline; partial Ref.18
Modified residue1561Hydroxyproline; partial
Modified residue1671Hydroxyproline; partial
Modified residue1701Hydroxyproline; partial
Modified residue1771Hydroxyproline; partial
Modified residue19014-hydroxyproline; partial Ref.18 Ref.19
Modified residue2411Allysine By similarity
Modified residue2611Allysine By similarity
Modified residue2651Allysine By similarity
Modified residue28314-hydroxyproline; partial Ref.19
Modified residue28614-hydroxyproline; partial Ref.18 Ref.19
Modified residue2901Hydroxyproline; partial
Modified residue3121Allysine By similarity
Modified residue3151Allysine By similarity
Modified residue32714-hydroxyproline; partial Ref.19
Modified residue34214-hydroxyproline; partial Ref.19
Modified residue34714-hydroxyproline; partial Ref.19
Modified residue3521Hydroxyproline; partial
Modified residue3551Hydroxyproline; partial
Modified residue36014-hydroxyproline; partial Ref.19
Modified residue3751Allysine By similarity
Modified residue3791Allysine By similarity
Modified residue3821Allysine By similarity
Modified residue41514-hydroxyproline; partial Ref.18
Modified residue4211Hydroxyproline; partial
Modified residue42714-hydroxyproline; partial Ref.18 Ref.19
Modified residue4511Allysine By similarity
Modified residue4651Hydroxyproline; partial
Modified residue4671Hydroxyproline; partial
Modified residue48114-hydroxyproline; partial Ref.18
Modified residue4921Allysine By similarity
Modified residue4961Allysine By similarity
Modified residue5221Hydroxyproline; partial
Modified residue5501Hydroxyproline; partial
Modified residue5581Allysine By similarity
Modified residue5621Allysine By similarity
Modified residue5661Allysine By similarity
Modified residue58014-hydroxyproline; partial Ref.18 Ref.19
Modified residue58914-hydroxyproline Probable
Modified residue59814-hydroxyproline Probable
Modified residue60714-hydroxyproline; partial Ref.18
Modified residue6461Hydroxyproline; partial
Modified residue6531Allysine By similarity
Modified residue6561Allysine By similarity
Modified residue67714-hydroxyproline; partial Ref.18 Ref.19
Modified residue6931Allysine By similarity
Modified residue6971Allysine By similarity
Modified residue7351Allysine By similarity
Modified residue7381Allysine By similarity
Modified residue7691Hydroxyproline; partial
Modified residue7721Hydroxyproline; partial
Disulfide bond776 ↔ 781 By similarity

Natural variations

Alternative sequence45 – 5410Missing in isoform 7.
VSP_012479
Alternative sequence78 – 180103Missing in isoform 11.
VSP_012480
Alternative sequence1251A → AAPSVP in isoform 5 and isoform 12.
VSP_012481
Alternative sequence215 – 22814Missing in isoform 8 and isoform 11.
VSP_012482
Alternative sequence453 – 50048Missing in isoform 6, isoform 7, isoform 8, isoform 11, isoform 12 and isoform 13.
VSP_012483
Alternative sequence453 – 48129Missing in isoform 1, isoform 2, isoform 4 and isoform 5.
VSP_012484
Alternative sequence5001F → FALLNLA in isoform 1, isoform 9 and isoform 10.
VSP_012485
Alternative sequence555 – 57016AAAKS…KAQLR → G in isoform 8.
VSP_012486
Alternative sequence612 – 64433Missing in isoform 1, isoform 2, isoform 5, isoform 6, isoform 7, isoform 8, isoform 10, isoform 11, isoform 12 and isoform 13.
VSP_012487
Alternative sequence740 – 75718Missing in isoform 5, isoform 6, isoform 7, isoform 8, isoform 11 and isoform 12.
VSP_012488
Natural variant4221G → S. Ref.1 Ref.2 Ref.3 Ref.8 Ref.12 Ref.13 Ref.15
Corresponds to variant rs2071307 [ dbSNP | Ensembl ].
VAR_020882
Natural variant6101G → R. Ref.8 Ref.12
Corresponds to variant rs17855988 [ dbSNP | Ensembl ].
VAR_056869

Experimental info

Sequence conflict3171G → E in CAD97910. Ref.4
Sequence conflict467 – 4693PQA → APG in AAB65620. Ref.12
Sequence conflict467 – 4693PQA → APG in AAB65621. Ref.12
Sequence conflict5531V → I in BAC85506. Ref.3
Sequence conflict6911A → T in CAD98065. Ref.4
Sequence conflict7731G → D in CAD97910. Ref.4

Sequences

Sequence LengthMass (Da)Tools
Isoform 3 [UniParc].

Last modified October 5, 2010. Version 3.
Checksum: D3C6F4EC6BC4991F

FASTA78668,469
        10         20         30         40         50         60 
MAGLTAAAPR PGVLLLLLSI LHPSRPGGVP GAIPGGVPGG VFYPGAGLGA LGGGALGPGG 

        70         80         90        100        110        120 
KPLKPVPGGL AGAGLGAGLG AFPAVTFPGA LVPGGVADAA AAYKAAKAGA GLGGVPGVGG 

       130        140        150        160        170        180 
LGVSAGAVVP QPGAGVKPGK VPGVGLPGVY PGGVLPGARF PGVGVLPGVP TGAGVKPKAP 

       190        200        210        220        230        240 
GVGGAFAGIP GVGPFGGPQP GVPLGYPIKA PKLPGGYGLP YTTGKLPYGY GPGGVAGAAG 

       250        260        270        280        290        300 
KAGYPTGTGV GPQAAAAAAA KAAAKFGAGA AGVLPGVGGA GVPGVPGAIP GIGGIAGVGT 

       310        320        330        340        350        360 
PAAAAAAAAA AKAAKYGAAA GLVPGGPGFG PGVVGVPGAG VPGVGVPGAG IPVVPGAGIP 

       370        380        390        400        410        420 
GAAVPGVVSP EAAAKAAAKA AKYGARPGVG VGGIPTYGVG AGGFPGFGVG VGGIPGVAGV 

       430        440        450        460        470        480 
PGVGGVPGVG GVPGVGISPE AQAAAAAKAA KYGAAGAGVL GGLVPGPQAA VPGVPGTGGV 

       490        500        510        520        530        540 
PGVGTPAAAA AKAAAKAAQF GLVPGVGVAP GVGVAPGVGV APGVGLAPGV GVAPGVGVAP 

       550        560        570        580        590        600 
GVGVAPGIGP GGVAAAAKSA AKVAAKAQLR AAAGLGAGIP GLGVGVGVPG LGVGAGVPGL 

       610        620        630        640        650        660 
GVGAGVPGFG AGADEGVRRS LSPELREGDP SSSQHLPSTP SSPRVPGALA AAKAAKYGAA 

       670        680        690        700        710        720 
VPGVLGGLGA LGGVGIPGGV VGAGPAAAAA AAKAAAKAAQ FGLVGAAGLG GLGVGGLGVP 

       730        740        750        760        770        780 
GVGGLGGIPP AAAAKAAKYG AAGLGGVLGG AGQFPLGGVA ARPGFGLSPI FPGGACLGKA 


CGRKRK 

« Hide

Isoform 1 [UniParc].

Checksum: B38B11526A0CB52D
Show »

FASTA73063,230
Isoform 2 [UniParc].

Checksum: 0A7E4424F9EC0F78
Show »

FASTA72462,634
Isoform 4 [UniParc].

Checksum: 2B24F955D8360738
Show »

FASTA75766,106
Isoform 5 [UniParc].

Checksum: 151A0A4E089B3A5C
Show »

FASTA71161,605
Isoform 6 [UniParc].

Checksum: 86446D90C8E2664F
Show »

FASTA68759,500
Isoform 7 [UniParc].

Checksum: C5082D1C00A310BA
Show »

FASTA67758,789
Isoform 8 [UniParc].

Checksum: 5DAFC55566AB809B
Show »

FASTA65856,551
Isoform 9 [UniParc].

Checksum: 35AAC849F2DC2EC6
Show »

FASTA79269,064
Isoform 10 [UniParc].

Checksum: E8E4CBC20D02A185
Show »

FASTA75965,593
Isoform 11 [UniParc].

Checksum: 6C9128F3D079D9B0
Show »

FASTA57048,897
Isoform 12 [UniParc].

Checksum: 65D038D48352C5E9
Show »

FASTA69259,951
Isoform 13 [UniParc].

Checksum: 78F444C823E5F8B4
Show »

FASTA70560,980

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] [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. expand/collapse author list , 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]"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., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I.
BMC Genomics 8:399-399(2007) [PubMed] [Europe PMC] [Abstract]
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. expand/collapse author list , 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]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
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]"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] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Web resources

Wikipedia

Elastin entry

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M17282 expand/collapse EMBL AC list , M16983, M17265, M17266, M17267, M17268, M17271, M17272, M17273, M17275, M17276, M17277, M17278, M17279, M17281 Genomic DNA. Translation: AAC98393.1.
M17282 expand/collapse EMBL AC list , M16983, M17265, M17266, M17267, M17268, M17270, M17271, M17272, M17273, M17275, M17276, M17277, M17278, M17279, M17280, M17281 Genomic DNA. Translation: AAC98394.1.
M17282 expand/collapse EMBL AC list , 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 expand/collapse EMBL AC list , U93034, U93035, U93036 Genomic DNA. Translation: AAB65620.1.
U93037 expand/collapse EMBL AC list , 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.
CCDSCCDS43598.1. [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]
PIREAHU. A32707.
RefSeqNP_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]
UniGeneHs.647061.

3D structure databases

ProteinModelPortalP15502.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid108321. 14 interactions.
IntActP15502. 10 interactions.

Chemistry

DrugBankDB00533. Rofecoxib.

Protein family/group databases

Allergome11040. Hom s Elastin.

PTM databases

PhosphoSiteP15502.

Polymorphism databases

DMDM306526276.

Proteomic databases

PaxDbP15502.
PRIDEP15502.

Protocols and materials databases

DNASU2006.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000252034; 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]
ENST00000570795; ENSP00000459197; ENSG00000262184. [P15502-5]
ENST00000571321; ENSP00000460375; ENSG00000262184. [P15502-2]
ENST00000572979; ENSP00000461042; ENSG00000262184. [P15502-11]
ENST00000573296; ENSP00000461780; ENSG00000262184. [P15502-13]
ENST00000573446; ENSP00000461371; ENSG00000262184. [P15502-7]
ENST00000573673; ENSP00000459103; ENSG00000262184. [P15502-12]
ENST00000575260; ENSP00000460737; ENSG00000262184. [P15502-1]
ENST00000576288; ENSP00000460338; ENSG00000262184. [P15502-8]
ENST00000576801; ENSP00000458848; ENSG00000262184. [P15502-4]
GeneID2006.
KEGGhsa:2006.
UCSCuc003tzn.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

CTD2006.
GeneCardsGC07P073442.
GeneReviewsELN.
H-InvDBHIX0006761.
HGNCHGNC:3327. ELN.
HPACAB010750.
HPA018111.
HPA056941.
MIM123700. phenotype.
130160. gene.
185500. phenotype.
neXtProtNX_P15502.
Orphanet90348. Autosomal dominant cutis laxa.
3193. Supravalvular aortic stenosis.
904. Williams syndrome.
PharmGKBPA27757.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG331579.
InParanoidP15502.
KOK14211.
TreeFamTF338594.

Enzyme and pathway databases

ReactomeREACT_118779. Extracellular matrix organization.

Gene expression databases

ArrayExpressP15502.
BgeeP15502.
GenevestigatorP15502.

Family and domain databases

InterProIPR003979. Tropoelastin.
[Graphical view]
PRINTSPR01500. TROPOELASTIN.
ProtoNetSearch...

Other

ChiTaRSELN. human.
GeneWikiElastin.
GenomeRNAi2006.
NextBio8119.
PMAP-CutDBP15502.
PROP15502.
SOURCESearch...

Entry information

Entry nameELN_HUMAN
AccessionPrimary (citable) accession number: P15502
Secondary accession number(s): B3KTS6 expand/collapse secondary AC list , O15336, O15337, Q14233, Q14234, Q14235, Q14238, Q6P0L4, Q6ZWJ6, Q75MU5, Q7Z316, Q7Z3F5, Q9UMF5
Entry history
Integrated into UniProtKB/Swiss-Prot: April 1, 1990
Last sequence update: October 5, 2010
Last modified: July 9, 2014
This is version 163 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

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

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 7

Human chromosome 7: entries, gene names and cross-references to MIM