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Protein

EMILIN-2

Gene

EMILIN2

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

  • extracellular matrix constituent conferring elasticity Source: UniProtKB

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Cell adhesion

Enzyme and pathway databases

ReactomeiR-HSA-2129379. Molecules associated with elastic fibres.

Names & Taxonomyi

Protein namesi
Recommended name:
EMILIN-2
Alternative name(s):
Elastin microfibril interface-located protein 2
Short name:
Elastin microfibril interfacer 2
Protein FOAP-10
Gene namesi
Name:EMILIN2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 18

Organism-specific databases

HGNCiHGNC:19881. EMILIN2.

Subcellular locationi

GO - Cellular componenti

  • collagen trimer Source: UniProtKB-KW
  • extracellular matrix Source: UniProtKB
  • extracellular region Source: UniProtKB
  • proteinaceous extracellular matrix Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Extracellular matrix, Secreted

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA134880588.

Polymorphism and mutation databases

BioMutaiEMILIN2.
DMDMi296439365.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 3030Sequence analysisAdd
BLAST
Chaini31 – 10531023EMILIN-2PRO_0000007817Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi48 ↔ 110PROSITE-ProRule annotation
Glycosylationi55 – 551N-linked (GlcNAc...)Sequence analysis
Disulfide bondi74 ↔ 81PROSITE-ProRule annotation
Disulfide bondi109 ↔ 118PROSITE-ProRule annotation
Glycosylationi275 – 2751N-linked (GlcNAc...)Sequence analysis
Glycosylationi458 – 4581N-linked (GlcNAc...)Sequence analysis
Glycosylationi510 – 5101N-linked (GlcNAc...)Sequence analysis
Glycosylationi587 – 5871N-linked (GlcNAc...)Sequence analysis
Glycosylationi616 – 6161N-linked (GlcNAc...)1 Publication
Glycosylationi745 – 7451N-linked (GlcNAc...)Sequence analysis
Glycosylationi974 – 9741N-linked (GlcNAc...)Sequence analysis

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

EPDiQ9BXX0.
MaxQBiQ9BXX0.
PaxDbiQ9BXX0.
PRIDEiQ9BXX0.

PTM databases

iPTMnetiQ9BXX0.
PhosphoSiteiQ9BXX0.

Expressioni

Tissue specificityi

Highest levels are present in fetal heart and adult lung. Intermediate levels in peripheral leukocytes, placenta, and spinal cord and low expression in fetal brain, spleen, thymus, and lung and in adult heart, aorta, testis, bone marrow, small intestine, thymus, lymph node, and appendix.

Gene expression databases

BgeeiQ9BXX0.
CleanExiHS_EMILIN2.
GenevisibleiQ9BXX0. HS.

Organism-specific databases

HPAiHPA040739.
HPA040890.

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 (By similarity). Interacts with EMILIN1.By similarity

Protein-protein interaction databases

BioGridi123848. 9 interactions.
STRINGi9606.ENSP00000254528.

Structurei

3D structure databases

ProteinModelPortaliQ9BXX0.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini44 – 12077EMIPROSITE-ProRule annotationAdd
BLAST
Domaini840 – 89253Collagen-likeAdd
BLAST
Domaini901 – 1052152C1qPROSITE-ProRule annotationAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili177 – 21539Sequence analysisAdd
BLAST
Coiled coili253 – 34088Sequence analysisAdd
BLAST
Coiled coili369 – 38921Sequence analysisAdd
BLAST
Coiled coili578 – 63457Sequence analysisAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi784 – 83956Pro-richAdd
BLAST
Compositional biasi893 – 9019Pro-rich

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

eggNOGiENOG410IFE8. Eukaryota.
ENOG410ZUQR. LUCA.
GeneTreeiENSGT00660000095314.
HOGENOMiHOG000060078.
HOVERGENiHBG051474.
InParanoidiQ9BXX0.
OMAiWCAYIVN.
OrthoDBiEOG74R1RX.
PhylomeDBiQ9BXX0.
TreeFamiTF331033.

Family and domain databases

Gene3Di2.60.120.40. 1 hit.
InterProiIPR001073. C1q_dom.
IPR011489. EMI_domain.
IPR008983. Tumour_necrosis_fac-like_dom.
[Graphical view]
PfamiPF00386. C1q. 1 hit.
PF07546. EMI. 1 hit.
[Graphical view]
SMARTiSM00110. C1Q. 1 hit.
[Graphical view]
SUPFAMiSSF49842. SSF49842. 1 hit.
PROSITEiPS50871. C1Q. 1 hit.
PS51041. EMI. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

Q9BXX0-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MWQPRRPWPR VPWRWALALL ALVGAGLCHA GPQPGYPARP SARNKNWCAY
60 70 80 90 100
IVNKNVSCSV LEGSESFIQA QYNCAWNQMP CPSALVYRVN FRPRYVTRYK
110 120 130 140 150
TVTQLEWRCC PGFRGGDCQE GPKDPVKTLR PTPARPRNSL KKATDNEPSQ
160 170 180 190 200
FSEPRKTLSP TGTAQPSWGV DPKEGPQELQ EKKIQVLEEK VLRLTRTVLD
210 220 230 240 250
LQSSLAGVSE NLKHATQDDA SRTRAPGLSS QHPKPDTTVS GDTETGQSPG
260 270 280 290 300
VFNTKESGMK DIKSELAEVK DTLKNKSDKL EELDGKVKGY EGQLRQLQEA
310 320 330 340 350
AQGPTVTMTT NELYQAYVDS KIDALREELM EGMDRKLADL KNSCEYKLTG
360 370 380 390 400
LQQQCDDYGS SYLGVIELIG EKETSLRKEI NNLRARLQEP SAQANCCDSE
410 420 430 440 450
KNGDIGQQIK TLDQKIERVA EATRMLNGRL DNEFDRLIVP EPDVDFDAKW
460 470 480 490 500
NELDARINVT EKNAEEHCFY IEETLRGAIN GEVGDLKQLV DQKIQSLEDR
510 520 530 540 550
LGSVLLQMTN NTGAELSPPG AAALPGVSGS GDERVMMELN HLKDKVQVVE
560 570 580 590 600
DICLLNIQGK PHGMEGALPN REDRAVRDSL HLLKSLNDTM HRKFQETEQT
610 620 630 640 650
IQKLQQDFSF LYSQLNHTEN DVTHLQKEMS NCRAGENAGM GRFTKVGEQE
660 670 680 690 700
RTVDTLPSPQ HPVAHCCSQL EERWQRLQSQ VISELDACKE CTQGVQREVS
710 720 730 740 750
MVEGRVSHME KTCSKLDSIS GNLQRIKEGL NKHVSSLWNC VRQMNGTLRS
760 770 780 790 800
HSRDISGLKN SVQQFYSHVF QISTDLQDLV KFQPSAKAPS PPPPAEAPKE
810 820 830 840 850
PLQPEPAPPR PSGPATAEDP GRRPVLPQRP PEERPPQPPG STGVIAETGQ
860 870 880 890 900
AGPPAGAGVS GRGLPRGVDG QTGSGTVPGA EGFAGAPGYP KSPPVASPGA
910 920 930 940 950
PVPSLVSFSA GLTQKPFPSD GGVVLFNKVL VNDGDVYNPS TGVFTAPYDG
960 970 980 990 1000
RYLITATLTP ERDAYVEAVL SVSNASVAQL HTAGYRREFL EYHRPPGALH
1010 1020 1030 1040 1050
TCGGPGAFHL IVHLKAGDAV NVVVTGGKLA HTDFDEMYST FSGVFLYPFL

SHL
Length:1,053
Mass (Da):115,687
Last modified:May 18, 2010 - v3
Checksum:i9F2895AB0AC5E8EF
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti545 – 5451K → G in AAK37963 (PubMed:11278945).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti215 – 2151A → T.
Corresponds to variant rs16943977 [ dbSNP | Ensembl ].
VAR_057528
Natural varianti259 – 2591M → V.
Corresponds to variant rs35267664 [ dbSNP | Ensembl ].
VAR_057529
Natural varianti903 – 9031P → S.1 Publication
Corresponds to variant rs56288451 [ dbSNP | Ensembl ].
VAR_062003

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF270513 mRNA. Translation: AAK37963.1.
AP000919 Genomic DNA. No translation available.
AP001011 Genomic DNA. No translation available.
CH471113 Genomic DNA. Translation: EAX01690.1.
BC136541 mRNA. Translation: AAI36542.1.
AK090519 mRNA. Translation: BAC03470.1.
AB026706 mRNA. Translation: BAB61020.1.
CCDSiCCDS11828.1.
RefSeqiNP_114437.2. NM_032048.2.
UniGeneiHs.532815.

Genome annotation databases

EnsembliENST00000254528; ENSP00000254528; ENSG00000132205.
GeneIDi84034.
KEGGihsa:84034.
UCSCiuc002kln.4. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF270513 mRNA. Translation: AAK37963.1.
AP000919 Genomic DNA. No translation available.
AP001011 Genomic DNA. No translation available.
CH471113 Genomic DNA. Translation: EAX01690.1.
BC136541 mRNA. Translation: AAI36542.1.
AK090519 mRNA. Translation: BAC03470.1.
AB026706 mRNA. Translation: BAB61020.1.
CCDSiCCDS11828.1.
RefSeqiNP_114437.2. NM_032048.2.
UniGeneiHs.532815.

3D structure databases

ProteinModelPortaliQ9BXX0.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi123848. 9 interactions.
STRINGi9606.ENSP00000254528.

PTM databases

iPTMnetiQ9BXX0.
PhosphoSiteiQ9BXX0.

Polymorphism and mutation databases

BioMutaiEMILIN2.
DMDMi296439365.

Proteomic databases

EPDiQ9BXX0.
MaxQBiQ9BXX0.
PaxDbiQ9BXX0.
PRIDEiQ9BXX0.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000254528; ENSP00000254528; ENSG00000132205.
GeneIDi84034.
KEGGihsa:84034.
UCSCiuc002kln.4. human.

Organism-specific databases

CTDi84034.
GeneCardsiEMILIN2.
H-InvDBHIX0021047.
HGNCiHGNC:19881. EMILIN2.
HPAiHPA040739.
HPA040890.
MIMi608928. gene.
neXtProtiNX_Q9BXX0.
PharmGKBiPA134880588.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiENOG410IFE8. Eukaryota.
ENOG410ZUQR. LUCA.
GeneTreeiENSGT00660000095314.
HOGENOMiHOG000060078.
HOVERGENiHBG051474.
InParanoidiQ9BXX0.
OMAiWCAYIVN.
OrthoDBiEOG74R1RX.
PhylomeDBiQ9BXX0.
TreeFamiTF331033.

Enzyme and pathway databases

ReactomeiR-HSA-2129379. Molecules associated with elastic fibres.

Miscellaneous databases

ChiTaRSiEMILIN2. human.
GenomeRNAii84034.
NextBioi73184.
PROiQ9BXX0.
SOURCEiSearch...

Gene expression databases

BgeeiQ9BXX0.
CleanExiHS_EMILIN2.
GenevisibleiQ9BXX0. HS.

Family and domain databases

Gene3Di2.60.120.40. 1 hit.
InterProiIPR001073. C1q_dom.
IPR011489. EMI_domain.
IPR008983. Tumour_necrosis_fac-like_dom.
[Graphical view]
PfamiPF00386. C1q. 1 hit.
PF07546. EMI. 1 hit.
[Graphical view]
SMARTiSM00110. C1Q. 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. "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: NUCLEOTIDE SEQUENCE [MRNA], VARIANT SER-903.
    Tissue: Kidney.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. "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].
  5. "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] OF 590-1053.
    Tissue: Adrenal gland.
  6. "Homo sapiens mRNA for FOAP-10 protein, partial cds."
    Fujii Y., Takayama K., Tsuritani K., Yajima Y., Amemiya T., Ukai Y., Naito K., Kawaguchi A.
    Submitted (APR-1999) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 846-1053.
    Tissue: Macrophage.
  7. "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-616.
    Tissue: Liver.

Entry informationi

Entry nameiEMIL2_HUMAN
AccessioniPrimary (citable) accession number: Q9BXX0
Secondary accession number(s): B2RMY3, Q8NBH3, Q96JQ4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 3, 2003
Last sequence update: May 18, 2010
Last modified: May 11, 2016
This is version 117 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 18
    Human chromosome 18: 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

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 one 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.