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Reviewed, UniProtKB/Swiss-Prot P15502 (ELN_HUMAN)

Last modified June 16, 2009. Version 113. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Alternative products · Sequence annotation (Features) · Sequences · References · Web resources · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Elastin
Alternative name(s):
    Tropoelastin
Gene names
Name: ELN
OrganismHomo sapiens (Human)
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.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.

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 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.16
Modified residue1561Hydroxyproline; partial
Modified residue1671Hydroxyproline; partial
Modified residue1701Hydroxyproline; partial
Modified residue1771Hydroxyproline; partial
Modified residue19014-hydroxyproline; partial Ref.16 Ref.17
Modified residue2411Allysine By similarity
Modified residue2611Allysine By similarity
Modified residue2651Allysine By similarity
Modified residue28314-hydroxyproline; partial Ref.17
Modified residue28614-hydroxyproline; partial Ref.16 Ref.17
Modified residue2901Hydroxyproline; partial
Modified residue3121Allysine By similarity
Modified residue3151Allysine By similarity
Modified residue32714-hydroxyproline; partial Ref.17
Modified residue34214-hydroxyproline; partial Ref.17
Modified residue34714-hydroxyproline; partial Ref.17
Modified residue3521Hydroxyproline; partial
Modified residue3551Hydroxyproline; partial
Modified residue36014-hydroxyproline; partial Ref.17
Modified residue3751Allysine By similarity
Modified residue3791Allysine By similarity
Modified residue3821Allysine By similarity
Modified residue41514-hydroxyproline; partial Ref.16
Modified residue4211Hydroxyproline; partial
Modified residue42714-hydroxyproline; partial Ref.16 Ref.17
Modified residue4511Allysine By similarity
Modified residue4651Hydroxyproline; partial
Modified residue4671Hydroxyproline; partial
Modified residue48114-hydroxyproline; partial Ref.16
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.16 Ref.17
Modified residue58914-hydroxyproline Probable
Modified residue59814-hydroxyproline Probable
Modified residue60714-hydroxyproline; partial Ref.16
Modified residue6461Hydroxyproline; partial
Modified residue6531Allysine By similarity
Modified residue6561Allysine By similarity
Modified residue67714-hydroxyproline; partial Ref.16 Ref.17
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.
VSP_012481
Alternative sequence215 – 22814Missing in isoform 8 and isoform 11.
VSP_012482
Alternative sequence453 – 50048Missing in isoform 6, isoform 7, isoform 8 and isoform 11.
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 and isoform 11.
VSP_012487
Alternative sequence740 – 75718Missing in isoform 5, isoform 6, isoform 7, isoform 8 and isoform 11.
VSP_012488
Natural variant4221S → G: dbSNP rs2071307. Ref.3 Ref.5
VAR_020882
Natural variant6101G → R: dbSNP rs17855988.
VAR_056869

Experimental info

Sequence conflict3171G → E in CAD97910. Ref.4
Sequence conflict467 – 4693PQA → APG in AAB65620. Ref.10
Sequence conflict467 – 4693PQA → APG in AAB65621. Ref.10
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 January 4, 2005. Version 2.
Checksum: 1E06FD2C692820F8

FASTA78668,499
        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 
PSVGGVPGVG 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.

Checksum: AB06D15BA567AE46
Show »

FASTA73063,260
Isoform 2.

Checksum: 61155686228EDF3D
Show »

FASTA72462,664
Isoform 4.

Checksum: 23B7FE5B8AF85CA8
Show »

FASTA75766,136
Isoform 5.

Checksum: 19568E8A0D8B2B58
Show »

FASTA71161,635
Isoform 6.

Checksum: 864068C4C8E9F88F
Show »

FASTA68759,530
Isoform 7.

Checksum: C50C284800A88E7A
Show »

FASTA67758,819
Isoform 8.

Checksum: 5DAFC01166AB895B
Show »

FASTA65856,581
Isoform 9.

Checksum: 392ECBA04B6AF306
Show »

FASTA79269,094
Isoform 10.

Checksum: 9077C3510A0CF34B
Show »

FASTA75965,623
Isoform 11.

Checksum: 6C952DA7D0724770
Show »

FASTA57048,927

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. 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: 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. 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: 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.

Web resources

Cross-references

Sequence databases

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.
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 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. Different initiation.
U62292 Genomic DNA. Translation: AAB17544.1.
IPIIPI00163202.
IPI00177942.
IPI00446835.
IPI00472548.
IPI00513726.
IPI00514114.
IPI00514196.
IPI00514508.
IPI00514851.
IPI00515021.
IPI00925620.
PIREAHU. A32707.
RefSeqNP_001075221.1.
UniGeneHs.647061

3D structure databases

HSSPHSSP built from PDB template 1ZFJ based on UniProtKB P50099.
ModBaseSearch...

PTM databases

PhosphoSiteP15502.

Proteomic databases

PRIDEP15502.

Genome annotation databases

EnsemblENSG00000049540. Homo sapiens. [Contig view]
GeneID2006.

Organism-specific databases

GeneCardsGC07P073080.
H-InvDBHIX0006761.
HIX0019421.
HGNCHGNC:3327. ELN.
HPACAB010750.
HPA018111.
MIM123700. phenotype.
130160. gene.
185500. phenotype.
194050. phenotype.
Orphanet209. Cutis laxa.
90348. Cutis laxa, dominant type.
3193. Supravalvar aortic stenosis.
904. Williams syndrome.
PharmGKBPA27757.
GenAtlasSearch...

Phylogenomic databases

HOVERGENP15502.

Gene expression databases

ArrayExpressP15502.
BgeeP15502.
GermOnlineENSG00000049540. Homo sapiens.

Family and domain databases

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

Other Resources

DrugBankDB00533. Rofecoxib.
NextBio8119.
PMAP-CutDBP15502.
SOURCESearch...

Entry information

Entry nameELN_HUMAN
AccessionPrimary (citable) accession number: P15502
Secondary accession number(s): O15336 expand/collapse secondary AC list , O15337, Q14233, Q14234, Q14235, Q14238, Q6P0L4, Q6ZWJ6, Q75MU5, Q7Z316, Q7Z3F5, Q9UMF5
Entry history
Integrated into UniProtKB/Swiss-Prot: April 1, 1990
Last sequence update: January 4, 2005
Last modified: June 16, 2009
This is version 113 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (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

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Alternative products · Sequence annotation (Features) · Sequences · References · Web resources · Cross-references · Entry information · Relevant documents