Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

P15502

- ELN_HUMAN

UniProt

P15502 - ELN_HUMAN

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

Elastin

Gene

ELN

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

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

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
Complete GO annotation...

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
Complete GO annotation...

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

BgeeiP15502.
ExpressionAtlasiP15502. baseline and differential.
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.
GeneTreeiENSGT00730000111510.
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

        10         20         30         40         50
MAGLTAAAPR PGVLLLLLSI LHPSRPGGVP GAIPGGVPGG VFYPGAGLGA
60 70 80 90 100
LGGGALGPGG KPLKPVPGGL AGAGLGAGLG AFPAVTFPGA LVPGGVADAA
110 120 130 140 150
AAYKAAKAGA GLGGVPGVGG LGVSAGAVVP QPGAGVKPGK VPGVGLPGVY
160 170 180 190 200
PGGVLPGARF PGVGVLPGVP TGAGVKPKAP GVGGAFAGIP GVGPFGGPQP
210 220 230 240 250
GVPLGYPIKA PKLPGGYGLP YTTGKLPYGY GPGGVAGAAG KAGYPTGTGV
260 270 280 290 300
GPQAAAAAAA KAAAKFGAGA AGVLPGVGGA GVPGVPGAIP GIGGIAGVGT
310 320 330 340 350
PAAAAAAAAA AKAAKYGAAA GLVPGGPGFG PGVVGVPGAG VPGVGVPGAG
360 370 380 390 400
IPVVPGAGIP GAAVPGVVSP EAAAKAAAKA AKYGARPGVG VGGIPTYGVG
410 420 430 440 450
AGGFPGFGVG VGGIPGVAGV PGVGGVPGVG GVPGVGISPE AQAAAAAKAA
460 470 480 490 500
KYGAAGAGVL GGLVPGPQAA VPGVPGTGGV PGVGTPAAAA AKAAAKAAQF
510 520 530 540 550
GLVPGVGVAP GVGVAPGVGV APGVGLAPGV GVAPGVGVAP GVGVAPGIGP
560 570 580 590 600
GGVAAAAKSA AKVAAKAQLR AAAGLGAGIP GLGVGVGVPG LGVGAGVPGL
610 620 630 640 650
GVGAGVPGFG AGADEGVRRS LSPELREGDP SSSQHLPSTP SSPRVPGALA
660 670 680 690 700
AAKAAKYGAA VPGVLGGLGA LGGVGIPGGV VGAGPAAAAA AAKAAAKAAQ
710 720 730 740 750
FGLVGAAGLG GLGVGGLGVP GVGGLGGIPP AAAAKAAKYG AAGLGGVLGG
760 770 780
AGQFPLGGVA ARPGFGLSPI FPGGACLGKA CGRKRK
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]
CCDS75616.1. [P15502-3]
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 ]
CCDS75616.1. [P15502-3 ]
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.

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.
GeneTreei ENSGT00730000111510.
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

Bgeei P15502.
ExpressionAtlasi P15502. baseline and differential.
Genevestigatori P15502.

Family and domain databases

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

Publicationsi

« Hide 'large scale' publications
  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 29, 2014
This is version 166 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