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Q9Y6C2

- EMIL1_HUMAN

UniProt

Q9Y6C2 - EMIL1_HUMAN

Protein

EMILIN-1

Gene

EMILIN1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 121 (01 Oct 2014)
      Sequence version 2 (02 Sep 2008)
      Previous versions | rss
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    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
    2. protein binding Source: UniProtKB

    GO - Biological processi

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

    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 region Source: UniProtKB-KW
    3. extracellular vesicular exosome Source: UniProtKB
    4. proteinaceous extracellular matrix Source: UniProtKB-SubCell

    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

    Protein-protein interaction databases

    BioGridi116292. 10 interactions.
    DIPiDIP-35733N.
    IntActiQ9Y6C2. 10 interactions.
    MINTiMINT-133181.
    STRINGi9606.ENSP00000369677.

    Structurei

    Secondary structure

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

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    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.
    HOGENOMiHOG000112364.
    HOVERGENiHBG051473.
    InParanoidiQ9Y6C2.
    OMAiQQEATEH.
    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. Align

    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

    MAPRTLWSCY LCCLLTAAAG AASYPPRGFS LYTGSSGALS PGGPQAQIAP     50
    RPASRHRNWC AYVVTRTVSC VLEDGVETYV KYQPCAWGQP QCPQSIMYRR 100
    FLRPRYRVAY KTVTDMEWRC CQGYGGDDCA ESPAPALGPA SSTPRPLAQP 150
    ARPNLSGSSA GSPLSGLGGE GPGESEKVQQ LEEQVQSLTK ELQGLRGVLQ 200
    GLSGRLAEDV QRAVETAFNG RQQPADAAAR PGVHETLNEI QHQLQLLDTR 250
    VSTHDQELGH LNNHHGGSSS SGGSRAPAPA SAPPGPSEEL LRQLEQRLQE 300
    SCSVCLAGLD GFRRQQQEDR ERLRAMEKLL ASVEERQRHL AGLAVGRRPP 350
    QECCSPELGR RLAELERRLD VVAGSVTVLS GRRGTELGGA AGQGGHPPGY 400
    TSLASRLSRL EDRFNSTLGP SEEQEESWPG APGGLSHWLP AARGRLEQLG 450
    GLLANVSGEL GGRLDLLEEQ VAGAMQACGQ LCSGAPGEQD SQVSEILSAL 500
    ERRVLDSEGQ LRLVGSGLHT VEAAGEARQA TLEGLQEVVG RLQDRVDAQD 550
    ETAAEFTLRL NLTAARLGQL EGLLQAHGDE GCGACGGVQE ELGRLRDGVE 600
    RCSCPLLPPR GPGAGPGVGG PSRGPLDGFS VFGGSSGSAL QALQGELSEV 650
    ILSFSSLNDS LNELQTTVEG QGADLADLGA TKDRIISEIN RLQQEATEHA 700
    TESEERFRGL EEGQAQAGQC PSLEGRLGRL EGVCERLDTV AGGLQGLREG 750
    LSRHVAGLWA GLRETNTTSQ MQAALLEKLV GGQAGLGRRL GALNSSLQLL 800
    EDRLHQLSLK DLTGPAGEAG PPGPPGLQGP PGPAGPPGSP GKDGQEGPIG 850
    PPGPQGEQGV EGAPAAPVPQ VAFSAALSLP RSEPGTVPFD RVLLNDGGYY 900
    DPETGVFTAP LAGRYLLSAV LTGHRHEKVE AVLSRSNQGV ARVDSGGYEP 950
    EGLENKPVAE SQPSPGTLGV FSLILPLQAG DTVCVDLVMG QLAHSEEPLT 1000
    IFSGALLYGD PELEHA 1016
    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:
    EMBL
    GenBank
    DDBJ
    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.
    PIRiT08772.
    RefSeqiNP_008977.1. NM_007046.3.
    UniGeneiHs.63348.

    Genome annotation databases

    EnsembliENST00000380320; ENSP00000369677; ENSG00000138080. [Q9Y6C2-1]
    GeneIDi11117.
    KEGGihsa:11117.
    UCSCiuc002rii.4. human.

    Polymorphism databases

    DMDMi205371751.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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 .
    CCDSi CCDS1733.1.
    PIRi T08772.
    RefSeqi NP_008977.1. NM_007046.3.
    UniGenei Hs.63348.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2KA3 NMR - A/B/C 867-1016 [» ]
    2OII NMR - A/B/C 867-1016 [» ]
    ProteinModelPortali Q9Y6C2.
    SMRi Q9Y6C2. Positions 867-1016.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 116292. 10 interactions.
    DIPi DIP-35733N.
    IntActi Q9Y6C2. 10 interactions.
    MINTi MINT-133181.
    STRINGi 9606.ENSP00000369677.

    PTM databases

    PhosphoSitei Q9Y6C2.

    Polymorphism databases

    DMDMi 205371751.

    2D gel databases

    REPRODUCTION-2DPAGE Q9Y6C2.

    Proteomic databases

    MaxQBi Q9Y6C2.
    PaxDbi Q9Y6C2.
    PRIDEi Q9Y6C2.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000380320 ; ENSP00000369677 ; ENSG00000138080 . [Q9Y6C2-1 ]
    GeneIDi 11117.
    KEGGi hsa:11117.
    UCSCi uc002rii.4. human.

    Organism-specific databases

    CTDi 11117.
    GeneCardsi GC02P027301.
    HGNCi HGNC:19880. EMILIN1.
    HPAi HPA002822.
    MIMi 130660. gene.
    neXtProti NX_Q9Y6C2.
    PharmGKBi PA134922135.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG244192.
    HOGENOMi HOG000112364.
    HOVERGENi HBG051473.
    InParanoidi Q9Y6C2.
    OMAi QQEATEH.
    OrthoDBi EOG74R1RX.
    PhylomeDBi Q9Y6C2.
    TreeFami TF331033.

    Enzyme and pathway databases

    Reactomei REACT_150331. Molecules associated with elastic fibres.

    Miscellaneous databases

    ChiTaRSi EMILIN1. human.
    EvolutionaryTracei Q9Y6C2.
    GeneWikii EMILIN1.
    GenomeRNAii 11117.
    NextBioi 42252.
    PROi Q9Y6C2.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q9Y6C2.
    CleanExi HS_EMILIN1.
    Genevestigatori Q9Y6C2.

    Family and domain databases

    Gene3Di 2.60.120.40. 1 hit.
    InterProi IPR001073. C1q.
    IPR008160. Collagen.
    IPR011489. EMI_domain.
    IPR008983. Tumour_necrosis_fac-like_dom.
    [Graphical view ]
    Pfami PF00386. C1q. 1 hit.
    PF01391. Collagen. 1 hit.
    PF07546. EMI. 1 hit.
    [Graphical view ]
    SUPFAMi SSF49842. SSF49842. 1 hit.
    PROSITEi PS50871. C1Q. 1 hit.
    PS51041. EMI. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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. "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: October 1, 2014
    This is version 121 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