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Q12805

- FBLN3_HUMAN

UniProt

Q12805 - FBLN3_HUMAN

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Protein

EGF-containing fibulin-like extracellular matrix protein 1

Gene

EFEMP1

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

Functioni

Binds EGFR, the EGF receptor, inducing EGFR autophosphorylation and the activation of downstream signaling pathways. May play a role in cell adhesion and migration. May function as a negative regulator of chondrocyte differentiation. In the olfactory epithelium, it may regulate glial cell migration, differentiation and the ability of glial cells to support neuronal neurite outgrowth.3 Publications

GO - Molecular functioni

  1. calcium ion binding Source: InterPro
  2. epidermal growth factor-activated receptor activity Source: UniProtKB
  3. epidermal growth factor receptor binding Source: UniProtKB

GO - Biological processi

  1. epidermal growth factor receptor signaling pathway Source: UniProtKB
  2. extracellular matrix organization Source: Reactome
  3. negative regulation of chondrocyte differentiation Source: UniProtKB
  4. peptidyl-tyrosine phosphorylation Source: UniProtKB
  5. regulation of transcription, DNA-templated Source: UniProtKB
  6. visual perception Source: ProtInc
Complete GO annotation...

Keywords - Molecular functioni

Growth factor

Keywords - Ligandi

Calcium

Enzyme and pathway databases

ReactomeiREACT_150331. Molecules associated with elastic fibres.

Names & Taxonomyi

Protein namesi
Recommended name:
EGF-containing fibulin-like extracellular matrix protein 1
Alternative name(s):
Extracellular protein S1-5
Fibrillin-like protein
Fibulin-3
Short name:
FIBL-3
Gene namesi
Name:EFEMP1
Synonyms:FBLN3, FBNL
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 2

Organism-specific databases

HGNCiHGNC:3218. EFEMP1.

Subcellular locationi

Secretedextracellular space By similarity. Secretedextracellular spaceextracellular matrix By similarity
Note: Localizes to the lamina propria underneath the olfactory epithelium.By similarity

GO - Cellular componenti

  1. extracellular region Source: Reactome
  2. extracellular space Source: UniProtKB
  3. extracellular vesicular exosome Source: UniProtKB
  4. proteinaceous extracellular matrix Source: ProtInc
Complete GO annotation...

Keywords - Cellular componenti

Extracellular matrix, Secreted

Pathology & Biotechi

Involvement in diseasei

Doyne honeycomb retinal dystrophy (DHRD) [MIM:126600]: Autosomal dominant disease characterized by yellow-white deposits known as drusen that accumulate beneath the retinal pigment epithelium.2 Publications
Note: The disease is caused by mutations affecting the gene represented in this entry.
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti345 – 3451R → W in DHRD; misfolded, accumulates in cells due to inefficient secretion; induces the formation of deposits between Bruch's membrane and the retinal pigment epithelium where it accumulates. 2 Publications
VAR_009513

Keywords - Diseasei

Disease mutation

Organism-specific databases

MIMi126600. phenotype.
Orphaneti75376. Familial drusen.
PharmGKBiPA27652.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1717Sequence AnalysisAdd
BLAST
Chaini18 – 493476EGF-containing fibulin-like extracellular matrix protein 1PRO_0000007570Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi177 ↔ 190PROSITE-ProRule annotation
Disulfide bondi184 ↔ 199PROSITE-ProRule annotation
Disulfide bondi201 ↔ 212PROSITE-ProRule annotation
Disulfide bondi218 ↔ 228PROSITE-ProRule annotation
Disulfide bondi224 ↔ 237PROSITE-ProRule annotation
Disulfide bondi239 ↔ 252PROSITE-ProRule annotation
Glycosylationi249 – 2491N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi258 ↔ 268PROSITE-ProRule annotation
Disulfide bondi264 ↔ 277PROSITE-ProRule annotation
Disulfide bondi279 ↔ 292PROSITE-ProRule annotation
Disulfide bondi298 ↔ 309PROSITE-ProRule annotation
Disulfide bondi305 ↔ 318PROSITE-ProRule annotation
Disulfide bondi320 ↔ 332PROSITE-ProRule annotation
Disulfide bondi338 ↔ 350PROSITE-ProRule annotation
Disulfide bondi344 ↔ 359PROSITE-ProRule annotation
Disulfide bondi365 ↔ 377PROSITE-ProRule annotation

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

MaxQBiQ12805.
PaxDbiQ12805.
PRIDEiQ12805.

PTM databases

PhosphoSiteiQ12805.

Expressioni

Tissue specificityi

In the eye, associated with photoreceptor outer and inner segment regions, the nerve fiber layer, outer nuclear layer and inner and outer plexiform layers of the retina.2 Publications

Gene expression databases

BgeeiQ12805.
CleanExiHS_EFEMP1.
ExpressionAtlasiQ12805. baseline and differential.
GenevestigatoriQ12805.

Organism-specific databases

HPAiCAB016368.

Interactioni

Subunit structurei

Interacts with ECM1. Interacts with TIMP3.2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
Q9WMX22EBI-536772,EBI-6863748From a different organism.
ARAFP103983EBI-536772,EBI-365961
ATN1P542593EBI-536772,EBI-945980

Protein-protein interaction databases

BioGridi108496. 15 interactions.
IntActiQ12805. 24 interactions.
MINTiMINT-1466511.
STRINGi9606.ENSP00000347596.

Structurei

3D structure databases

ProteinModelPortaliQ12805.
SMRiQ12805. Positions 44-78, 172-409.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini26 – 7146EGF-like 1; atypicalPROSITE-ProRule annotationAdd
BLAST
Domaini173 – 21341EGF-like 2; calcium-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini214 – 25340EGF-like 3; calcium-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini254 – 29340EGF-like 4; calcium-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini294 – 33340EGF-like 5; calcium-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini334 – 37845EGF-like 6; calcium-bindingPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni259 – 493235Mediates interaction with TIMP3Add
BLAST

Sequence similaritiesi

Belongs to the fibulin family.Curated
Contains 6 EGF-like domains.PROSITE-ProRule annotation

Keywords - Domaini

EGF-like domain, Repeat, Signal

Phylogenomic databases

eggNOGiNOG250502.
GeneTreeiENSGT00760000118806.
HOGENOMiHOG000234337.
HOVERGENiHBG051560.
InParanoidiQ12805.
KOiK18262.
OMAiVQTGRNN.
OrthoDBiEOG7W9RTF.
PhylomeDBiQ12805.
TreeFamiTF317514.

Family and domain databases

InterProiIPR026823. cEGF.
IPR000742. EG-like_dom.
IPR001881. EGF-like_Ca-bd_dom.
IPR013032. EGF-like_CS.
IPR000152. EGF-type_Asp/Asn_hydroxyl_site.
IPR018097. EGF_Ca-bd_CS.
IPR009030. Growth_fac_rcpt_N_dom.
[Graphical view]
PfamiPF12662. cEGF. 2 hits.
PF07645. EGF_CA. 3 hits.
[Graphical view]
SMARTiSM00179. EGF_CA. 4 hits.
[Graphical view]
SUPFAMiSSF57184. SSF57184. 1 hit.
PROSITEiPS00010. ASX_HYDROXYL. 4 hits.
PS01186. EGF_2. 4 hits.
PS50026. EGF_3. 4 hits.
PS01187. EGF_CA. 6 hits.
[Graphical view]

Sequences (5)i

Sequence statusi: Complete.

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

This entry describes 5 isoformsi produced by alternative splicing. Align

Note: Experimental confirmation may be lacking for some isoforms.

Isoform 1 (identifier: Q12805-1) [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
MLKALFLTML TLALVKSQDT EETITYTQCT DGYEWDPVRQ QCKDIDECDI
60 70 80 90 100
VPDACKGGMK CVNHYGGYLC LPKTAQIIVN NEQPQQETQP AEGTSGATTG
110 120 130 140 150
VVAASSMATS GVLPGGGFVA SAAAVAGPEM QTGRNNFVIR RNPADPQRIP
160 170 180 190 200
SNPSHRIQCA AGYEQSEHNV CQDIDECTAG THNCRADQVC INLRGSFACQ
210 220 230 240 250
CPPGYQKRGE QCVDIDECTI PPYCHQRCVN TPGSFYCQCS PGFQLAANNY
260 270 280 290 300
TCVDINECDA SNQCAQQCYN ILGSFICQCN QGYELSSDRL NCEDIDECRT
310 320 330 340 350
SSYLCQYQCV NEPGKFSCMC PQGYQVVRSR TCQDINECET TNECREDEMC
360 370 380 390 400
WNYHGGFRCY PRNPCQDPYI LTPENRCVCP VSNAMCRELP QSIVYKYMSI
410 420 430 440 450
RSDRSVPSDI FQIQATTIYA NTINTFRIKS GNENGEFYLR QTSPVSAMLV
460 470 480 490
LVKSLSGPRE HIVDLEMLTV SSIGTFRTSS VLRLTIIVGP FSF
Length:493
Mass (Da):54,641
Last modified:December 1, 2000 - v2
Checksum:i128CA5ED140DF414
GO
Isoform 2 (identifier: Q12805-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-8: Missing.

Show »
Length:485
Mass (Da):53,722
Checksum:iCF3DF7CCD89C58AC
GO
Isoform 3 (identifier: Q12805-3) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     58-58: Missing.

Show »
Length:492
Mass (Da):54,583
Checksum:iFD09CF260582EA63
GO
Isoform 4 (identifier: Q12805-4) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     106-106: Missing.

Show »
Length:492
Mass (Da):54,553
Checksum:iEF7B59437CAA3C67
GO
Isoform 5 (identifier: Q12805-5) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-58: Missing.
     214-293: Missing.

Note: No experimental confirmation available.

Show »
Length:355
Mass (Da):39,195
Checksum:i3E9B55D15D9331EE
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti220 – 2201I → F.1 Publication
VAR_009512
Natural varianti345 – 3451R → W in DHRD; misfolded, accumulates in cells due to inefficient secretion; induces the formation of deposits between Bruch's membrane and the retinal pigment epithelium where it accumulates. 2 Publications
VAR_009513

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 5858Missing in isoform 5. 1 PublicationVSP_054372Add
BLAST
Alternative sequencei1 – 88Missing in isoform 2. CuratedVSP_001392
Alternative sequencei58 – 581Missing in isoform 3. CuratedVSP_001393
Alternative sequencei106 – 1061Missing in isoform 4. CuratedVSP_001394
Alternative sequencei214 – 29380Missing in isoform 5. 1 PublicationVSP_054373Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U03877 mRNA. Translation: AAA65590.1.
AY004330
, AY004321, AY004322, AY004325, AY004324, AY004323, AY004326, AY004328, AY004329, AY004327 Genomic DNA. Translation: AAK11491.1.
AK290599 mRNA. Translation: BAF83288.1.
AK301402 mRNA. Translation: BAG62937.1.
AC010895 Genomic DNA. No translation available.
AC096549 Genomic DNA. No translation available.
CH471053 Genomic DNA. Translation: EAX00080.1.
CH471053 Genomic DNA. Translation: EAX00081.1.
CH471053 Genomic DNA. Translation: EAX00082.1.
BC014410 mRNA. Translation: AAH14410.1.
BC098561 mRNA. Translation: AAH98561.1.
CCDSiCCDS1857.1. [Q12805-1]
PIRiI38449.
RefSeqiNP_001034437.1. NM_001039348.2. [Q12805-1]
NP_001034438.1. NM_001039349.2. [Q12805-1]
UniGeneiHs.732348.
Hs.76224.

Genome annotation databases

EnsembliENST00000355426; ENSP00000347596; ENSG00000115380. [Q12805-1]
ENST00000394555; ENSP00000378058; ENSG00000115380. [Q12805-1]
GeneIDi2202.
KEGGihsa:2202.
UCSCiuc002rzi.3. human. [Q12805-1]

Polymorphism databases

DMDMi9973182.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Web resourcesi

Mutations of the EFEMP1 gene

Retina International's Scientific Newsletter

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U03877 mRNA. Translation: AAA65590.1 .
AY004330
, AY004321 , AY004322 , AY004325 , AY004324 , AY004323 , AY004326 , AY004328 , AY004329 , AY004327 Genomic DNA. Translation: AAK11491.1 .
AK290599 mRNA. Translation: BAF83288.1 .
AK301402 mRNA. Translation: BAG62937.1 .
AC010895 Genomic DNA. No translation available.
AC096549 Genomic DNA. No translation available.
CH471053 Genomic DNA. Translation: EAX00080.1 .
CH471053 Genomic DNA. Translation: EAX00081.1 .
CH471053 Genomic DNA. Translation: EAX00082.1 .
BC014410 mRNA. Translation: AAH14410.1 .
BC098561 mRNA. Translation: AAH98561.1 .
CCDSi CCDS1857.1. [Q12805-1 ]
PIRi I38449.
RefSeqi NP_001034437.1. NM_001039348.2. [Q12805-1 ]
NP_001034438.1. NM_001039349.2. [Q12805-1 ]
UniGenei Hs.732348.
Hs.76224.

3D structure databases

ProteinModelPortali Q12805.
SMRi Q12805. Positions 44-78, 172-409.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 108496. 15 interactions.
IntActi Q12805. 24 interactions.
MINTi MINT-1466511.
STRINGi 9606.ENSP00000347596.

PTM databases

PhosphoSitei Q12805.

Polymorphism databases

DMDMi 9973182.

Proteomic databases

MaxQBi Q12805.
PaxDbi Q12805.
PRIDEi Q12805.

Protocols and materials databases

DNASUi 2202.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000355426 ; ENSP00000347596 ; ENSG00000115380 . [Q12805-1 ]
ENST00000394555 ; ENSP00000378058 ; ENSG00000115380 . [Q12805-1 ]
GeneIDi 2202.
KEGGi hsa:2202.
UCSCi uc002rzi.3. human. [Q12805-1 ]

Organism-specific databases

CTDi 2202.
GeneCardsi GC02M056093.
HGNCi HGNC:3218. EFEMP1.
HPAi CAB016368.
MIMi 126600. phenotype.
601548. gene.
neXtProti NX_Q12805.
Orphaneti 75376. Familial drusen.
PharmGKBi PA27652.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG250502.
GeneTreei ENSGT00760000118806.
HOGENOMi HOG000234337.
HOVERGENi HBG051560.
InParanoidi Q12805.
KOi K18262.
OMAi VQTGRNN.
OrthoDBi EOG7W9RTF.
PhylomeDBi Q12805.
TreeFami TF317514.

Enzyme and pathway databases

Reactomei REACT_150331. Molecules associated with elastic fibres.

Miscellaneous databases

ChiTaRSi EFEMP1. human.
GeneWikii EFEMP1.
GenomeRNAii 2202.
NextBioi 35475649.
PROi Q12805.
SOURCEi Search...

Gene expression databases

Bgeei Q12805.
CleanExi HS_EFEMP1.
ExpressionAtlasi Q12805. baseline and differential.
Genevestigatori Q12805.

Family and domain databases

InterProi IPR026823. cEGF.
IPR000742. EG-like_dom.
IPR001881. EGF-like_Ca-bd_dom.
IPR013032. EGF-like_CS.
IPR000152. EGF-type_Asp/Asn_hydroxyl_site.
IPR018097. EGF_Ca-bd_CS.
IPR009030. Growth_fac_rcpt_N_dom.
[Graphical view ]
Pfami PF12662. cEGF. 2 hits.
PF07645. EGF_CA. 3 hits.
[Graphical view ]
SMARTi SM00179. EGF_CA. 4 hits.
[Graphical view ]
SUPFAMi SSF57184. SSF57184. 1 hit.
PROSITEi PS00010. ASX_HYDROXYL. 4 hits.
PS01186. EGF_2. 4 hits.
PS50026. EGF_3. 4 hits.
PS01187. EGF_CA. 6 hits.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "An overexpressed gene transcript in senescent and quiescent human fibroblasts encoding a novel protein in the epidermal growth factor-like repeat family stimulates DNA synthesis."
    Lecka-Czernik B., Lumpkin C.K. Jr., Goldstein S.
    Mol. Cell. Biol. 15:120-128(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], POSSIBLE ALTERNATIVE SPLICING.
    Tissue: Skin.
  2. "Structure and chromosomal assignment of the human S1-5 gene (FBNL) that is highly homologous to fibrillin."
    Ikegawa S., Toda T., Okui K., Nakamura Y.
    Genomics 35:590-592(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  3. "Sequence, recombinant expression and tissue localization of two novel extracellular matrix proteins, fibulin-3 and fibulin-4."
    Giltay R., Timpl R., Kostka G.
    Matrix Biol. 18:469-480(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  4. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  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] (ISOFORMS 1 AND 5).
    Tissue: Synovium.
  6. "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].
  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 1).
    Tissue: Lung.
  9. "Aberrant accumulation of EFEMP1 underlies drusen formation in Malattia Leventinese and age-related macular degeneration."
    Marmorstein L.Y., Munier F.L., Arsenijevic Y., Schorderet D.F., McLaughlin P.J., Chung D., Traboulsi E., Marmorstein A.D.
    Proc. Natl. Acad. Sci. U.S.A. 99:13067-13072(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY, CHARACTERIZATION OF VARIANT DHRD TRP-345.
  10. "Tissue inhibitor of metalloproteinases-3 (TIMP-3) is a binding partner of epithelial growth factor-containing fibulin-like extracellular matrix protein 1 (EFEMP1). Implications for macular degenerations."
    Klenotic P.A., Munier F.L., Marmorstein L.Y., Anand-Apte B.
    J. Biol. Chem. 279:30469-30473(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH TIMP3.
  11. "EFEMP1 binds the EGF receptor and activates MAPK and Akt pathways in pancreatic carcinoma cells."
    Camaj P., Seeliger H., Ischenko I., Krebs S., Blum H., De Toni E.N., Faktorova D., Jauch K.W., Bruns C.J.
    Biol. Chem. 390:1293-1302(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN EGFR ACTIVATION.
  12. "ECM1 interacts with fibulin-3 and the beta 3 chain of laminin 332 through its serum albumin subdomain-like 2 domain."
    Sercu S., Lambeir A.M., Steenackers E., El Ghalbzouri A., Geentjens K., Sasaki T., Oyama N., Merregaert J.
    Matrix Biol. 28:160-169(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH ECM1.
  13. "Fibulin-3 is uniquely upregulated in malignant gliomas and promotes tumor cell motility and invasion."
    Hu B., Thirtamara-Rajamani K.K., Sim H., Viapiano M.S.
    Mol. Cancer Res. 7:1756-1770(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  14. Cited for: FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
  15. Cited for: VARIANT DHRD TRP-345, VARIANT PHE-220.
  16. "Dominant radial drusen and Arg345Trp EFEMP1 mutation."
    Matsumoto M., Traboulsi E.I.
    Am. J. Ophthalmol. 131:810-812(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT DHRD TRP-345.
  17. "The R345W mutation in EFEMP1 is pathogenic and causes AMD-like deposits in mice."
    Fu L., Garland D., Yang Z., Shukla D., Rajendran A., Pearson E., Stone E.M., Zhang K., Pierce E.A.
    Hum. Mol. Genet. 16:2411-2422(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION OF VARIANT DHRD TRP-345.

Entry informationi

Entry nameiFBLN3_HUMAN
AccessioniPrimary (citable) accession number: Q12805
Secondary accession number(s): A8K3I4
, B4DW75, D6W5D2, Q541U7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: December 1, 2000
Last modified: October 29, 2014
This is version 152 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

Up-regulated in malignant gliomas. May increase glioma cell adhesiveness and invasive properties.

Keywords - Technical termi

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. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3