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Q12805 (FBLN3_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 149. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:EFEMP1
Synonyms:FBLN3, FBNL
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length493 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.11 Ref.13 Ref.14

Subunit structure

Interacts with ECM1. Interacts with TIMP3. Ref.10 Ref.12

Subcellular location

Secretedextracellular space By similarity. Secretedextracellular spaceextracellular matrix By similarity. Note: Localizes to the lamina propria underneath the olfactory epithelium By similarity. Ref.14

Tissue specificity

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. Ref.9 Ref.14

Involvement in disease

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.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.9 Ref.15 Ref.16 Ref.17

Miscellaneous

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

Sequence similarities

Belongs to the fibulin family.

Contains 6 EGF-like domains.

Ontologies

Keywords
   Cellular componentExtracellular matrix
Secreted
   Coding sequence diversityAlternative splicing
Polymorphism
   DiseaseDisease mutation
   DomainEGF-like domain
Repeat
Signal
   LigandCalcium
   Molecular functionGrowth factor
   PTMDisulfide bond
Glycoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processepidermal growth factor receptor signaling pathway

Inferred from direct assay Ref.11. Source: UniProtKB

extracellular matrix organization

Traceable author statement. Source: Reactome

negative regulation of chondrocyte differentiation

Inferred from direct assay Ref.14. Source: UniProtKB

peptidyl-tyrosine phosphorylation

Inferred from direct assay Ref.11. Source: UniProtKB

regulation of transcription, DNA-templated

Inferred from direct assay Ref.14. Source: UniProtKB

visual perception

Traceable author statement Ref.15. Source: ProtInc

   Cellular_componentextracellular region

Traceable author statement. Source: Reactome

extracellular space

Inferred from direct assay Ref.14. Source: UniProtKB

proteinaceous extracellular matrix

Traceable author statement Ref.15. Source: ProtInc

   Molecular_functioncalcium ion binding

Inferred from electronic annotation. Source: InterPro

epidermal growth factor receptor binding

Inferred from direct assay Ref.11. Source: UniProtKB

epidermal growth factor-activated receptor activity

Inferred from direct assay Ref.11. Source: UniProtKB

protein binding

Inferred from physical interaction Ref.12. Source: UniProtKB

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Q9WMX22EBI-536772,EBI-6863748From a different organism.
ARAFP103983EBI-536772,EBI-365961
ATN1P542593EBI-536772,EBI-945980

Alternative products

This entry describes 5 isoforms produced by alternative splicing. [Align] [Select]

Note: Experimental confirmation may be lacking for some isoforms.
Isoform 1 (identifier: Q12805-1)

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.
Isoform 2 (identifier: Q12805-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-8: Missing.
Isoform 3 (identifier: Q12805-3)

The sequence of this isoform differs from the canonical sequence as follows:
     58-58: Missing.
Isoform 4 (identifier: Q12805-4)

The sequence of this isoform differs from the canonical sequence as follows:
     106-106: Missing.
Isoform 5 (identifier: Q12805-5)

The sequence of this isoform differs from the canonical sequence as follows:
     1-58: Missing.
     214-293: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1717 Potential
Chain18 – 493476EGF-containing fibulin-like extracellular matrix protein 1
PRO_0000007570

Regions

Domain26 – 7146EGF-like 1; atypical
Domain173 – 21341EGF-like 2; calcium-binding Potential
Domain214 – 25340EGF-like 3; calcium-binding Potential
Domain254 – 29340EGF-like 4; calcium-binding Potential
Domain294 – 33340EGF-like 5; calcium-binding Potential
Domain334 – 37845EGF-like 6; calcium-binding Potential
Region259 – 493235Mediates interaction with TIMP3

Amino acid modifications

Glycosylation2491N-linked (GlcNAc...) Potential
Disulfide bond177 ↔ 190 By similarity
Disulfide bond184 ↔ 199 By similarity
Disulfide bond201 ↔ 212 By similarity
Disulfide bond218 ↔ 228 By similarity
Disulfide bond224 ↔ 237 By similarity
Disulfide bond239 ↔ 252 By similarity
Disulfide bond258 ↔ 268 By similarity
Disulfide bond264 ↔ 277 By similarity
Disulfide bond279 ↔ 292 By similarity
Disulfide bond298 ↔ 309 By similarity
Disulfide bond305 ↔ 318 By similarity
Disulfide bond320 ↔ 332 By similarity
Disulfide bond338 ↔ 350 By similarity
Disulfide bond344 ↔ 359 By similarity
Disulfide bond365 ↔ 377 By similarity

Natural variations

Alternative sequence1 – 5858Missing in isoform 5.
VSP_054372
Alternative sequence1 – 88Missing in isoform 2.
VSP_001392
Alternative sequence581Missing in isoform 3.
VSP_001393
Alternative sequence1061Missing in isoform 4.
VSP_001394
Alternative sequence214 – 29380Missing in isoform 5.
VSP_054373
Natural variant2201I → F. Ref.15
VAR_009512
Natural variant3451R → 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. Ref.9 Ref.15 Ref.16 Ref.17
VAR_009513

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified December 1, 2000. Version 2.
Checksum: 128CA5ED140DF414

FASTA49354,641
        10         20         30         40         50         60 
MLKALFLTML TLALVKSQDT EETITYTQCT DGYEWDPVRQ QCKDIDECDI VPDACKGGMK 

        70         80         90        100        110        120 
CVNHYGGYLC LPKTAQIIVN NEQPQQETQP AEGTSGATTG VVAASSMATS GVLPGGGFVA 

       130        140        150        160        170        180 
SAAAVAGPEM QTGRNNFVIR RNPADPQRIP SNPSHRIQCA AGYEQSEHNV CQDIDECTAG 

       190        200        210        220        230        240 
THNCRADQVC INLRGSFACQ CPPGYQKRGE QCVDIDECTI PPYCHQRCVN TPGSFYCQCS 

       250        260        270        280        290        300 
PGFQLAANNY TCVDINECDA SNQCAQQCYN ILGSFICQCN QGYELSSDRL NCEDIDECRT 

       310        320        330        340        350        360 
SSYLCQYQCV NEPGKFSCMC PQGYQVVRSR TCQDINECET TNECREDEMC WNYHGGFRCY 

       370        380        390        400        410        420 
PRNPCQDPYI LTPENRCVCP VSNAMCRELP QSIVYKYMSI RSDRSVPSDI FQIQATTIYA 

       430        440        450        460        470        480 
NTINTFRIKS GNENGEFYLR QTSPVSAMLV LVKSLSGPRE HIVDLEMLTV SSIGTFRTSS 

       490 
VLRLTIIVGP FSF 

« Hide

Isoform 2 [UniParc].

Checksum: CF3DF7CCD89C58AC
Show »

FASTA48553,722
Isoform 3 [UniParc].

Checksum: FD09CF260582EA63
Show »

FASTA49254,583
Isoform 4 [UniParc].

Checksum: EF7B59437CAA3C67
Show »

FASTA49254,553
Isoform 5 [UniParc].

Checksum: 3E9B55D15D9331EE
Show »

FASTA35539,195

References

« Hide 'large scale' references
[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]"EFEMP1 is not associated with sporadic early onset drusen."
Sauer C.G., White K., Kellner U., Rudolph G., Jurklies B., Pauleikhoff D., Weber B.H.
Ophthalmic Genet. 22:27-34(2001) [PubMed] [Europe PMC] [Abstract]
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. expand/collapse author list , 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. expand/collapse author list , 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]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
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]"Fibulin-3 negatively regulates chondrocyte differentiation."
Wakabayashi T., Matsumine A., Nakazora S., Hasegawa M., Iino T., Ota H., Sonoda H., Sudo A., Uchida A.
Biochem. Biophys. Res. Commun. 391:1116-1121(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
[15]"A single EFEMP1 mutation associated with both malattia Leventinese and Doyne honeycomb retinal dystrophy."
Stone E.M., Lotery A.J., Munier F.L., Heon E., Piguet B., Guymer R.H., Vandenburgh K., Cousin P., Nishimura D., Swiderski R.E., Silvestri G., Mackey D.A., Hagerman G.S., Bird A.C., Sheffield V.C., Schorderet D.F.
Nat. Genet. 22:199-202(1999) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U03877 mRNA. Translation: AAA65590.1.
AY004330 expand/collapse EMBL AC list , 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.
CCDSCCDS1857.1. [Q12805-1]
PIRI38449.
RefSeqNP_001034437.1. NM_001039348.2. [Q12805-1]
NP_001034438.1. NM_001039349.2. [Q12805-1]
UniGeneHs.732348.
Hs.76224.

3D structure databases

ProteinModelPortalQ12805.
SMRQ12805. Positions 44-78, 172-409.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid108496. 15 interactions.
IntActQ12805. 23 interactions.
MINTMINT-1466511.
STRING9606.ENSP00000347596.

PTM databases

PhosphoSiteQ12805.

Polymorphism databases

DMDM9973182.

Proteomic databases

MaxQBQ12805.
PaxDbQ12805.
PRIDEQ12805.

Protocols and materials databases

DNASU2202.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000355426; ENSP00000347596; ENSG00000115380. [Q12805-1]
ENST00000394554; ENSP00000378057; ENSG00000115380. [Q12805-1]
ENST00000394555; ENSP00000378058; ENSG00000115380. [Q12805-1]
ENST00000424836; ENSP00000399145; ENSG00000115380.
GeneID2202.
KEGGhsa:2202.
UCSCuc002rzi.3. human. [Q12805-1]

Organism-specific databases

CTD2202.
GeneCardsGC02M056093.
HGNCHGNC:3218. EFEMP1.
HPACAB016368.
MIM126600. phenotype.
601548. gene.
neXtProtNX_Q12805.
Orphanet75376. Familial drusen.
PharmGKBPA27652.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG250502.
HOGENOMHOG000234337.
HOVERGENHBG051560.
InParanoidQ12805.
KOK18262.
OMAVQTGRNN.
OrthoDBEOG7W9RTF.
PhylomeDBQ12805.
TreeFamTF317514.

Enzyme and pathway databases

ReactomeREACT_118779. Extracellular matrix organization.

Gene expression databases

ArrayExpressQ12805.
BgeeQ12805.
CleanExHS_EFEMP1.
GenevestigatorQ12805.

Family and domain databases

InterProIPR026823. 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]
PfamPF12662. cEGF. 2 hits.
PF07645. EGF_CA. 3 hits.
[Graphical view]
SMARTSM00179. EGF_CA. 4 hits.
[Graphical view]
SUPFAMSSF57184. SSF57184. 1 hit.
PROSITEPS00010. ASX_HYDROXYL. 4 hits.
PS01186. EGF_2. 4 hits.
PS50026. EGF_3. 4 hits.
PS01187. EGF_CA. 6 hits.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSEFEMP1. human.
GeneWikiEFEMP1.
GenomeRNAi2202.
NextBio35475649.
PROQ12805.
SOURCESearch...

Entry information

Entry nameFBLN3_HUMAN
AccessionPrimary (citable) accession number: Q12805
Secondary accession number(s): A8K3I4 expand/collapse secondary AC list , B4DW75, D6W5D2, Q541U7
Entry history
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: December 1, 2000
Last modified: July 9, 2014
This is version 149 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 2

Human chromosome 2: entries, gene names and cross-references to MIM