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Protein

EMILIN-1

Gene

EMILIN1

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

Functioni

May be responsible for anchoring smooth muscle cells to elastic fibers, and may be involved not only in the formation of the elastic fiber, but also in the processes that regulate vessel assembly. Has cell adhesive capacity.

GO - Molecular functioni

  1. extracellular matrix constituent conferring elasticity Source: Ensembl

GO - Biological processi

  1. cell adhesion Source: ProtInc
  2. extracellular matrix organization Source: Reactome
  3. positive regulation of cell-substrate adhesion Source: Ensembl
Complete GO annotation...

Keywords - Biological processi

Cell adhesion

Enzyme and pathway databases

ReactomeiREACT_150331. Molecules associated with elastic fibres.

Names & Taxonomyi

Protein namesi
Recommended name:
EMILIN-1
Alternative name(s):
Elastin microfibril interface-located protein 1
Short name:
Elastin microfibril interfacer 1
Gene namesi
Name:EMILIN1
Synonyms:EMI
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 2

Organism-specific databases

HGNCiHGNC:19880. EMILIN1.

Subcellular locationi

Secretedextracellular spaceextracellular matrix
Note: Found mainly at the interface between amorphous elastin and microfibrils.

GO - Cellular componenti

  1. collagen trimer Source: UniProtKB-KW
  2. extracellular matrix Source: UniProtKB
  3. extracellular region Source: Reactome
  4. extracellular vesicular exosome Source: UniProtKB
  5. proteinaceous extracellular matrix Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Extracellular matrix, Secreted

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA134922135.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2121Sequence AnalysisAdd
BLAST
Chaini22 – 1016995EMILIN-1PRO_0000007815Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi60 ↔ 121PROSITE-ProRule annotation
Disulfide bondi85 ↔ 92PROSITE-ProRule annotation
Disulfide bondi120 ↔ 129PROSITE-ProRule annotation
Glycosylationi154 – 1541N-linked (GlcNAc...)Sequence Analysis
Glycosylationi415 – 4151N-linked (GlcNAc...)1 Publication
Glycosylationi455 – 4551N-linked (GlcNAc...)2 Publications
Glycosylationi561 – 5611N-linked (GlcNAc...)Sequence Analysis
Glycosylationi658 – 6581N-linked (GlcNAc...)Sequence Analysis
Glycosylationi766 – 7661N-linked (GlcNAc...)1 Publication
Glycosylationi794 – 7941N-linked (GlcNAc...)1 Publication

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

MaxQBiQ9Y6C2.
PaxDbiQ9Y6C2.
PRIDEiQ9Y6C2.

2D gel databases

REPRODUCTION-2DPAGEQ9Y6C2.

PTM databases

PhosphoSiteiQ9Y6C2.

Expressioni

Tissue specificityi

Distributed in tissues where resilience and elastic recoil are prominent. Highest levels in the adult small intestine, aorta, lung, uterus, and appendix and in the fetal spleen, kidney, lung, and heart; intermediate expression was detected in adult liver, ovary, colon, stomach, lymph node and spleen; adult heart, bladder, prostate, adrenal gland, mammary gland, placenta and kidney showed low expression whereas a series of other adult tissues, including skeletal muscle and different regions of adult brain show no expression.1 Publication

Gene expression databases

BgeeiQ9Y6C2.
CleanExiHS_EMILIN1.
GenevestigatoriQ9Y6C2.

Organism-specific databases

HPAiHPA002822.

Interactioni

Subunit structurei

Homotrimer associated through a moderately stable interaction of the C-terminal globular C1q domains, allowing the nucleation of the triple helix and then a further quaternary assembly to higher-order polymers via intermolecular disulfide bonds. Interacts with EMILIN2.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
MTMR9Q96QG73EBI-744586,EBI-744593

Protein-protein interaction databases

BioGridi116292. 19 interactions.
DIPiDIP-35733N.
IntActiQ9Y6C2. 11 interactions.
MINTiMINT-133181.
STRINGi9606.ENSP00000369677.

Structurei

Secondary structure

1
1016
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi872 – 8765Combined sources
Beta strandi884 – 8863Combined sources
Beta strandi891 – 8977Combined sources
Turni902 – 9054Combined sources
Beta strandi906 – 9083Combined sources
Beta strandi913 – 9197Combined sources
Beta strandi929 – 9335Combined sources
Turni935 – 9373Combined sources
Beta strandi942 – 9465Combined sources
Beta strandi972 – 9743Combined sources
Beta strandi982 – 9865Combined sources
Beta strandi1002 – 10098Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2KA3NMR-A/B/C867-1016[»]
2OIINMR-A/B/C867-1016[»]
ProteinModelPortaliQ9Y6C2.
SMRiQ9Y6C2. Positions 867-1016.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9Y6C2.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini56 – 13176EMIPROSITE-ProRule annotationAdd
BLAST
Domaini814 – 86451Collagen-likeAdd
BLAST
Domaini866 – 1013148C1qPROSITE-ProRule annotationAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili216 – 25641Sequence AnalysisAdd
BLAST
Coiled coili356 – 42065Sequence AnalysisAdd
BLAST
Coiled coili576 – 60328Sequence AnalysisAdd
BLAST
Coiled coili685 – 75268Sequence AnalysisAdd
BLAST
Coiled coili835 – 85723Sequence AnalysisAdd
BLAST

Sequence similaritiesi

Contains 1 C1q domain.PROSITE-ProRule annotation
Contains 1 collagen-like domain.Curated
Contains 1 EMI domain.PROSITE-ProRule annotation

Keywords - Domaini

Coiled coil, Collagen, Signal

Phylogenomic databases

eggNOGiNOG244192.
GeneTreeiENSGT00660000095314.
HOGENOMiHOG000112364.
HOVERGENiHBG051473.
InParanoidiQ9Y6C2.
OMAiLEGVCER.
OrthoDBiEOG74R1RX.
PhylomeDBiQ9Y6C2.
TreeFamiTF331033.

Family and domain databases

Gene3Di2.60.120.40. 1 hit.
InterProiIPR001073. C1q.
IPR008160. Collagen.
IPR011489. EMI_domain.
IPR008983. Tumour_necrosis_fac-like_dom.
[Graphical view]
PfamiPF00386. C1q. 1 hit.
PF01391. Collagen. 1 hit.
PF07546. EMI. 1 hit.
[Graphical view]
SUPFAMiSSF49842. SSF49842. 1 hit.
PROSITEiPS50871. C1Q. 1 hit.
PS51041. EMI. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

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

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q9Y6C2-1) [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
MAPRTLWSCY LCCLLTAAAG AASYPPRGFS LYTGSSGALS PGGPQAQIAP
60 70 80 90 100
RPASRHRNWC AYVVTRTVSC VLEDGVETYV KYQPCAWGQP QCPQSIMYRR
110 120 130 140 150
FLRPRYRVAY KTVTDMEWRC CQGYGGDDCA ESPAPALGPA SSTPRPLAQP
160 170 180 190 200
ARPNLSGSSA GSPLSGLGGE GPGESEKVQQ LEEQVQSLTK ELQGLRGVLQ
210 220 230 240 250
GLSGRLAEDV QRAVETAFNG RQQPADAAAR PGVHETLNEI QHQLQLLDTR
260 270 280 290 300
VSTHDQELGH LNNHHGGSSS SGGSRAPAPA SAPPGPSEEL LRQLEQRLQE
310 320 330 340 350
SCSVCLAGLD GFRRQQQEDR ERLRAMEKLL ASVEERQRHL AGLAVGRRPP
360 370 380 390 400
QECCSPELGR RLAELERRLD VVAGSVTVLS GRRGTELGGA AGQGGHPPGY
410 420 430 440 450
TSLASRLSRL EDRFNSTLGP SEEQEESWPG APGGLSHWLP AARGRLEQLG
460 470 480 490 500
GLLANVSGEL GGRLDLLEEQ VAGAMQACGQ LCSGAPGEQD SQVSEILSAL
510 520 530 540 550
ERRVLDSEGQ LRLVGSGLHT VEAAGEARQA TLEGLQEVVG RLQDRVDAQD
560 570 580 590 600
ETAAEFTLRL NLTAARLGQL EGLLQAHGDE GCGACGGVQE ELGRLRDGVE
610 620 630 640 650
RCSCPLLPPR GPGAGPGVGG PSRGPLDGFS VFGGSSGSAL QALQGELSEV
660 670 680 690 700
ILSFSSLNDS LNELQTTVEG QGADLADLGA TKDRIISEIN RLQQEATEHA
710 720 730 740 750
TESEERFRGL EEGQAQAGQC PSLEGRLGRL EGVCERLDTV AGGLQGLREG
760 770 780 790 800
LSRHVAGLWA GLRETNTTSQ MQAALLEKLV GGQAGLGRRL GALNSSLQLL
810 820 830 840 850
EDRLHQLSLK DLTGPAGEAG PPGPPGLQGP PGPAGPPGSP GKDGQEGPIG
860 870 880 890 900
PPGPQGEQGV EGAPAAPVPQ VAFSAALSLP RSEPGTVPFD RVLLNDGGYY
910 920 930 940 950
DPETGVFTAP LAGRYLLSAV LTGHRHEKVE AVLSRSNQGV ARVDSGGYEP
960 970 980 990 1000
EGLENKPVAE SQPSPGTLGV FSLILPLQAG DTVCVDLVMG QLAHSEEPLT
1010
IFSGALLYGD PELEHA
Length:1,016
Mass (Da):106,667
Last modified:September 2, 2008 - v2
Checksum:iA447F74E17DBCBA8
GO
Isoform 2 (identifier: Q9Y6C2-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-674: Missing.
     675-675: L → M
     813-813: T → TGEGTK

Note: No experimental confirmation available.

Show »
Length:347
Mass (Da):35,928
Checksum:i1AFAB73C44E6F09C
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti149 – 1491Q → R.5 Publications
Corresponds to variant rs2736976 [ dbSNP | Ensembl ].
VAR_046095
Natural varianti536 – 5361Q → R.
Corresponds to variant rs36069611 [ dbSNP | Ensembl ].
VAR_046096
Natural varianti903 – 9031E → K.
Corresponds to variant rs36045790 [ dbSNP | Ensembl ].
VAR_046097

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 674674Missing in isoform 2. CuratedVSP_055478Add
BLAST
Alternative sequencei675 – 6751L → M in isoform 2. CuratedVSP_055479
Alternative sequencei813 – 8131T → TGEGTK in isoform 2. CuratedVSP_055480

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF088916 mRNA. Translation: AAD42161.1.
AF162780 Genomic DNA. Translation: AAF25006.1.
AC013403 Genomic DNA. Translation: AAX93166.1.
CH471053 Genomic DNA. Translation: EAX00645.1.
BC007530 mRNA. Translation: AAH07530.1.
BC009947 mRNA. Translation: AAH09947.2.
BC136279 mRNA. Translation: AAI36280.1.
BC142688 mRNA. Translation: AAI42689.1.
AL050138 mRNA. Translation: CAB43287.2.
CCDSiCCDS1733.1. [Q9Y6C2-1]
PIRiT08772.
RefSeqiNP_008977.1. NM_007046.3.
UniGeneiHs.63348.

Genome annotation databases

EnsembliENST00000613734; ENSP00000481146; ENSG00000138080. [Q9Y6C2-2]
GeneIDi11117.
KEGGihsa:11117.
UCSCiuc002rii.4. human. [Q9Y6C2-1]
uc002rik.4. human.

Polymorphism databases

DMDMi205371751.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF088916 mRNA. Translation: AAD42161.1.
AF162780 Genomic DNA. Translation: AAF25006.1.
AC013403 Genomic DNA. Translation: AAX93166.1.
CH471053 Genomic DNA. Translation: EAX00645.1.
BC007530 mRNA. Translation: AAH07530.1.
BC009947 mRNA. Translation: AAH09947.2.
BC136279 mRNA. Translation: AAI36280.1.
BC142688 mRNA. Translation: AAI42689.1.
AL050138 mRNA. Translation: CAB43287.2.
CCDSiCCDS1733.1. [Q9Y6C2-1]
PIRiT08772.
RefSeqiNP_008977.1. NM_007046.3.
UniGeneiHs.63348.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2KA3NMR-A/B/C867-1016[»]
2OIINMR-A/B/C867-1016[»]
ProteinModelPortaliQ9Y6C2.
SMRiQ9Y6C2. Positions 867-1016.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi116292. 19 interactions.
DIPiDIP-35733N.
IntActiQ9Y6C2. 11 interactions.
MINTiMINT-133181.
STRINGi9606.ENSP00000369677.

PTM databases

PhosphoSiteiQ9Y6C2.

Polymorphism databases

DMDMi205371751.

2D gel databases

REPRODUCTION-2DPAGEQ9Y6C2.

Proteomic databases

MaxQBiQ9Y6C2.
PaxDbiQ9Y6C2.
PRIDEiQ9Y6C2.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000613734; ENSP00000481146; ENSG00000138080. [Q9Y6C2-2]
GeneIDi11117.
KEGGihsa:11117.
UCSCiuc002rii.4. human. [Q9Y6C2-1]
uc002rik.4. human.

Organism-specific databases

CTDi11117.
GeneCardsiGC02P027301.
HGNCiHGNC:19880. EMILIN1.
HPAiHPA002822.
MIMi130660. gene.
neXtProtiNX_Q9Y6C2.
PharmGKBiPA134922135.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG244192.
GeneTreeiENSGT00660000095314.
HOGENOMiHOG000112364.
HOVERGENiHBG051473.
InParanoidiQ9Y6C2.
OMAiLEGVCER.
OrthoDBiEOG74R1RX.
PhylomeDBiQ9Y6C2.
TreeFamiTF331033.

Enzyme and pathway databases

ReactomeiREACT_150331. Molecules associated with elastic fibres.

Miscellaneous databases

ChiTaRSiEMILIN1. human.
EvolutionaryTraceiQ9Y6C2.
GeneWikiiEMILIN1.
GenomeRNAii11117.
NextBioi35520086.
PROiQ9Y6C2.
SOURCEiSearch...

Gene expression databases

BgeeiQ9Y6C2.
CleanExiHS_EMILIN1.
GenevestigatoriQ9Y6C2.

Family and domain databases

Gene3Di2.60.120.40. 1 hit.
InterProiIPR001073. C1q.
IPR008160. Collagen.
IPR011489. EMI_domain.
IPR008983. Tumour_necrosis_fac-like_dom.
[Graphical view]
PfamiPF00386. C1q. 1 hit.
PF01391. Collagen. 1 hit.
PF07546. EMI. 1 hit.
[Graphical view]
SUPFAMiSSF49842. SSF49842. 1 hit.
PROSITEiPS50871. C1Q. 1 hit.
PS51041. EMI. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "EMILIN, a component of the elastic fiber and a new member of the C1q/tumor necrosis factor superfamily of proteins."
    Doliana R., Mongiat M., Bucciotti F., Giacomello E., Deutzmann R., Volpin D., Bressan G.M., Colombatti A.
    J. Biol. Chem. 274:16773-16781(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT ARG-149.
  2. "Structure, chromosomal localization, and promoter analysis of the human elastin microfibril interface located protein (EMILIN) gene."
    Doliana R., Canton A., Bucciotti F., Mongiat M., Bonaldo P., Colombatti A.
    J. Biol. Chem. 275:785-792(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT ARG-149.
  3. "Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
    Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H.
    , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
    Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], VARIANT ARG-149.
  5. "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 1), VARIANT ARG-149.
    Tissue: Brain.
  6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 27-1016 (ISOFORM 1), VARIANT ARG-149.
    Tissue: Uterus.
  7. "Isolation and characterization of EMILIN-2, a new component of the growing EMILINs family and a member of the EMI domain-containing superfamily."
    Doliana R., Bot S., Mungiguerra G., Canton A., Cilli S.P., Colombatti A.
    J. Biol. Chem. 276:12003-12011(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY.
  8. "Elucidation of N-glycosylation sites on human platelet proteins: a glycoproteomic approach."
    Lewandrowski U., Moebius J., Walter U., Sickmann A.
    Mol. Cell. Proteomics 5:226-233(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-455.
    Tissue: Platelet.
  9. "Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry."
    Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.
    J. Proteome Res. 8:651-661(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-415; ASN-455; ASN-766 AND ASN-794.
    Tissue: Liver.
  10. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  11. "NMR-based homology model for the solution structure of the C-terminal globular domain of EMILIN1."
    Verdone G., Corazza A., Colebrooke S.A., Cicero D., Eliseo T., Boyd J., Doliana R., Fogolari F., Viglino P., Colombatti A., Campbell I.D., Esposito G.
    J. Biomol. NMR 43:79-96(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 867-1016, SUBUNIT.

Entry informationi

Entry nameiEMIL1_HUMAN
AccessioniPrimary (citable) accession number: Q9Y6C2
Secondary accession number(s): A5PL03
, H0Y7A0, Q53SY9, Q96G58, Q96IH6, Q9UG76
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 3, 2003
Last sequence update: September 2, 2008
Last modified: March 4, 2015
This is version 126 of the entry and version 2 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

Miscellaneous

Its deposition precedes the appearance of elastin and is simultaneous with that of fibrillin 1.

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 2
    Human chromosome 2: 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. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.