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Protein

Fibulin-1

Gene

Fbln1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Incorporated into fibronectin-containing matrix fibers. May play a role in cell adhesion and migration along protein fibers within the extracellular matrix (ECM). Could be important for certain developmental processes and contribute to the supramolecular organization of ECM architecture, in particular to those of basement membranes.

GO - Molecular functioni

  1. calcium ion binding Source: InterPro
  2. peptidase activator activity Source: MGI

GO - Biological processi

  1. embryo implantation Source: Ensembl
  2. extracellular matrix organization Source: MGI
  3. positive regulation of peptidase activity Source: GOC
Complete GO annotation...

Keywords - Ligandi

Calcium

Enzyme and pathway databases

ReactomeiREACT_198998. Molecules associated with elastic fibres.

Names & Taxonomyi

Protein namesi
Recommended name:
Fibulin-1
Short name:
FIBL-1
Alternative name(s):
Basement-membrane protein 90
Short name:
BM-90
Gene namesi
Name:Fbln1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 15

Organism-specific databases

MGIiMGI:95487. Fbln1.

Subcellular locationi

GO - Cellular componenti

  1. basement membrane Source: MGI
  2. extracellular space Source: MGI
  3. extracellular vesicular exosome Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Extracellular matrix, Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 29291 PublicationAdd
BLAST
Chaini30 – 705676Fibulin-1PRO_0000007564Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi36 ↔ 61By similarity
Disulfide bondi37 ↔ 68By similarity
Disulfide bondi50 ↔ 69By similarity
Disulfide bondi78 ↔ 109By similarity
Disulfide bondi91 ↔ 110By similarity
Glycosylationi98 – 981N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi112 ↔ 136By similarity
Disulfide bondi113 ↔ 143By similarity
Disulfide bondi126 ↔ 144By similarity
Disulfide bondi182 ↔ 192By similarity
Disulfide bondi188 ↔ 201By similarity
Disulfide bondi203 ↔ 216By similarity
Disulfide bondi222 ↔ 235By similarity
Disulfide bondi229 ↔ 244By similarity
Disulfide bondi250 ↔ 262By similarity
Disulfide bondi268 ↔ 281By similarity
Disulfide bondi275 ↔ 290By similarity
Disulfide bondi296 ↔ 308By similarity
Disulfide bondi314 ↔ 327By similarity
Disulfide bondi321 ↔ 336By similarity
Disulfide bondi343 ↔ 356By similarity
Disulfide bondi362 ↔ 375By similarity
Disulfide bondi369 ↔ 384By similarity
Disulfide bondi386 ↔ 399By similarity
Disulfide bondi405 ↔ 417By similarity
Disulfide bondi413 ↔ 426By similarity
Disulfide bondi428 ↔ 441By similarity
Disulfide bondi447 ↔ 456By similarity
Disulfide bondi452 ↔ 465By similarity
Disulfide bondi467 ↔ 481By similarity
Disulfide bondi487 ↔ 500By similarity
Disulfide bondi496 ↔ 509By similarity
Disulfide bondi511 ↔ 525By similarity
Disulfide bondi531 ↔ 544By similarity
Glycosylationi537 – 5371N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi538 ↔ 553By similarity
Glycosylationi541 – 5411N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi558 ↔ 579By similarity

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

MaxQBiQ08879.
PaxDbiQ08879.
PRIDEiQ08879.

PTM databases

PhosphoSiteiQ08879.

Expressioni

Tissue specificityi

Detected in most organs (brain, heart, lung, spleen, liver and kidney). Neurons are the predominant source of production in the brain. Not expressed significantly by astrocytes or microglia.1 Publication

Developmental stagei

The differential expression of the fibulin family contributes to the formation of molecularly distinct extracellular matrices already during early developmental stages of a large number of tissues. Increase expression at neonate stage in the brain. Expressed in interdigital regions of the handplate of a 12 dpc embryo and in the lateral perichondrial region. Similar expression persists in the 13 dpc handplate particularly in the perichondrial regions and apical aspects of the developing digits.3 Publications

Inductioni

Glucocorticoids suppressed mRNA expression and protein synthesis.

Gene expression databases

BgeeiQ08879.
CleanExiMM_FBLN1.
ExpressionAtlasiQ08879. baseline and differential.
GenevestigatoriQ08879.

Interactioni

Subunit structurei

Homomultimerizes and interacts with various extracellular matrix components such as FN1, LAMA1, LMA2, NID, ACAN, CSPG2 and type IV collagen. Interacts also with papillomavirus E6 proteins. Binding analysis demonstrated for isoform C a 100-fold stronger binding to the basement membrane protein NID than for isoform D. Interacts with FBLN7.5 Publications

Protein-protein interaction databases

BioGridi199605. 1 interaction.
IntActiQ08879. 1 interaction.
MINTiMINT-245863.

Structurei

3D structure databases

ProteinModelPortaliQ08879.
SMRiQ08879. Positions 186-528.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini36 – 7641Anaphylatoxin-like 1PROSITE-ProRule annotationAdd
BLAST
Domaini77 – 11135Anaphylatoxin-like 2PROSITE-ProRule annotationAdd
BLAST
Domaini112 – 14433Anaphylatoxin-like 3PROSITE-ProRule annotationAdd
BLAST
Domaini178 – 21740EGF-like 1PROSITE-ProRule annotationAdd
BLAST
Domaini218 – 26346EGF-like 2; calcium-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini264 – 30946EGF-like 3; calcium-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini310 – 35748EGF-like 4; calcium-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini358 – 40043EGF-like 5; calcium-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini401 – 44242EGF-like 6; calcium-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini443 – 48240EGF-like 7; calcium-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini483 – 52644EGF-like 8; calcium-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini527 – 58054EGF-like 9; calcium-bindingPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni358 – 44285Self-association and FN1-bindingBy similarityAdd
BLAST

Sequence similaritiesi

Belongs to the fibulin family.Curated
Contains 3 anaphylatoxin-like domains.PROSITE-ProRule annotation
Contains 9 EGF-like domains.PROSITE-ProRule annotation

Keywords - Domaini

EGF-like domain, Repeat, Signal

Phylogenomic databases

eggNOGiNOG12793.
GeneTreeiENSGT00760000118806.
HOGENOMiHOG000007079.
HOVERGENiHBG051559.
InParanoidiQ08879.
KOiK17307.
OMAiECPRLPL.
OrthoDBiEOG7P5T0C.
PhylomeDBiQ08879.
TreeFamiTF317514.

Family and domain databases

InterProiIPR000020. Anaphylatoxin/fibulin.
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.
IPR017048. Fibulin-1.
IPR009030. Growth_fac_rcpt_N_dom.
[Graphical view]
PfamiPF01821. ANATO. 2 hits.
PF12662. cEGF. 3 hits.
PF07645. EGF_CA. 4 hits.
[Graphical view]
PIRSFiPIRSF036313. Fibulin-1. 1 hit.
SMARTiSM00104. ANATO. 3 hits.
SM00181. EGF. 2 hits.
SM00179. EGF_CA. 7 hits.
[Graphical view]
SUPFAMiSSF57184. SSF57184. 4 hits.
PROSITEiPS01177. ANAPHYLATOXIN_1. 3 hits.
PS01178. ANAPHYLATOXIN_2. 3 hits.
PS00010. ASX_HYDROXYL. 4 hits.
PS01186. EGF_2. 3 hits.
PS50026. EGF_3. 4 hits.
PS01187. EGF_CA. 8 hits.
[Graphical view]

Sequences (4)i

Sequence statusi: Complete.

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

This entry describes 4 isoformsi produced by alternative splicing. Align

Isoform D (identifier: Q08879-1) [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
MERPVPSRLV PLPLLLLSSL SLLAARANAD ISMEACCTDG NQMANQHRDC
60 70 80 90 100
SLPYTSESKE CRMVQEQCCH NQLEELHCAT GINLASEPEG CASLHSYNSS
110 120 130 140 150
LETIFIKRCC HCCMLGKASL ARDQTCEPIV MISYQCGLVF RACCVKAREN
160 170 180 190 200
SDFVQGNGAD LQDPAKIPDE EDQEDPYLND RCRGGGPCKQ QCRDTGDEVI
210 220 230 240 250
CSCFVGYQLQ SDGVSCEDIN ECITGSHNCR LGESCINTVG SFRCQRDSSC
260 270 280 290 300
GTGYELTEDN NCKDIDECET GIHNCPPDFI CQNTLGSFRC RPKLQCKSGF
310 320 330 340 350
IQDALGNCID INECLSISAP CPVGQTCINT EGSYTCQKNV PNCGRGYHLN
360 370 380 390 400
EEGTRCVDVD ECSPPAEPCG KGHHCLNSPG SFRCECKAGF YFDGISRTCV
410 420 430 440 450
DINECQRYPG RLCGHKCENT PGSFHCSCSA GFRLSVDGRS CEDVNECLNS
460 470 480 490 500
PCSQECANVY GSYQCYCRRG YQLSDVDGVT CEDIDECALP TGGHICSYRC
510 520 530 540 550
INIPGSFQCS CPSSGYRLAP NGRNCQDIDE CVTGIHNCSI NETCFNIQGS
560 570 580 590 600
FRCLSFECPE NYRRSADTFR QEKTDTVRCI KSCRPNDEAC VRDPVHTVSH
610 620 630 640 650
TVISLPTFRE FTRPEEIIFL RAVTPLYPAN QADIIFDITE GNLRDSFDII
660 670 680 690 700
KRYEDGMTVG VVRQVRPIVG PFYAVLKLEM NYVLGGVVSH RNVVNVHIFV

SEYWF
Length:705
Mass (Da):78,033
Last modified:May 9, 2003 - v2
Checksum:i76C527A12E97D0E1
GO
Isoform A (identifier: Q08879-3)

Sequence is not available
Length:
Mass (Da):
Isoform B (identifier: Q08879-4)

Sequence is not available
Length:
Mass (Da):
Isoform C (identifier: Q08879-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     569-705: FRQEKTDTVR...VHIFVSEYWF → RCERLPCHEN...KLFIFVSAEL

Show »
Length:685
Mass (Da):75,284
Checksum:iEF0D77D7F66B73B8
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti30 – 301D → N AA sequence (PubMed:2249686)Curated
Sequence conflicti40 – 401G → P in CAA50207. (PubMed:8354280)Curated
Sequence conflicti363 – 3631S → A in CAA50207. (PubMed:8354280)Curated
Sequence conflicti385 – 3851E → K in BAC39669. (PubMed:16141072)Curated
Sequence conflicti553 – 5531C → Q AA sequence (PubMed:2249686)Curated
Sequence conflicti558 – 5581C → Q AA sequence (PubMed:2249686)Curated
Isoform C (identifier: Q08879-2)
Sequence conflicti571 – 5711E → A in CAA50206. (PubMed:8354280)Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei569 – 705137FRQEK…SEYWF → RCERLPCHENQECPRLPLRI TYYHLSFPTNIQVPAVVFRM GPSSAVPGDSMQLAITAGNE EGFFTTRKVSHHSGVVALTK PIPEPRDLLLTVKMDLYRHG TVSSFVAKLFIFVSAEL in isoform C. 3 PublicationsVSP_001386Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X70854 mRNA. Translation: CAA50207.1.
X70853 mRNA. Translation: CAA50206.1.
AK086451 mRNA. Translation: BAC39669.1.
AK035388 mRNA. Translation: BAC29054.1.
BC007140 mRNA. Translation: AAH07140.1.
AY040588 Genomic DNA. Translation: AAK82944.1.
CCDSiCCDS27719.1. [Q08879-1]
PIRiS34968.
S78040.
RefSeqiNP_034310.2. NM_010180.2. [Q08879-1]
XP_006520500.1. XM_006520437.1. [Q08879-2]
UniGeneiMm.297992.

Genome annotation databases

EnsembliENSMUST00000057410; ENSMUSP00000054583; ENSMUSG00000006369. [Q08879-1]
ENSMUST00000109432; ENSMUSP00000105058; ENSMUSG00000006369. [Q08879-2]
GeneIDi14114.
KEGGimmu:14114.
UCSCiuc007xdb.2. mouse. [Q08879-2]
uc011zxk.1. mouse. [Q08879-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X70854 mRNA. Translation: CAA50207.1.
X70853 mRNA. Translation: CAA50206.1.
AK086451 mRNA. Translation: BAC39669.1.
AK035388 mRNA. Translation: BAC29054.1.
BC007140 mRNA. Translation: AAH07140.1.
AY040588 Genomic DNA. Translation: AAK82944.1.
CCDSiCCDS27719.1. [Q08879-1]
PIRiS34968.
S78040.
RefSeqiNP_034310.2. NM_010180.2. [Q08879-1]
XP_006520500.1. XM_006520437.1. [Q08879-2]
UniGeneiMm.297992.

3D structure databases

ProteinModelPortaliQ08879.
SMRiQ08879. Positions 186-528.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi199605. 1 interaction.
IntActiQ08879. 1 interaction.
MINTiMINT-245863.

PTM databases

PhosphoSiteiQ08879.

Proteomic databases

MaxQBiQ08879.
PaxDbiQ08879.
PRIDEiQ08879.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000057410; ENSMUSP00000054583; ENSMUSG00000006369. [Q08879-1]
ENSMUST00000109432; ENSMUSP00000105058; ENSMUSG00000006369. [Q08879-2]
GeneIDi14114.
KEGGimmu:14114.
UCSCiuc007xdb.2. mouse. [Q08879-2]
uc011zxk.1. mouse. [Q08879-1]

Organism-specific databases

CTDi2192.
MGIiMGI:95487. Fbln1.

Phylogenomic databases

eggNOGiNOG12793.
GeneTreeiENSGT00760000118806.
HOGENOMiHOG000007079.
HOVERGENiHBG051559.
InParanoidiQ08879.
KOiK17307.
OMAiECPRLPL.
OrthoDBiEOG7P5T0C.
PhylomeDBiQ08879.
TreeFamiTF317514.

Enzyme and pathway databases

ReactomeiREACT_198998. Molecules associated with elastic fibres.

Miscellaneous databases

NextBioi285170.
PROiQ08879.
SOURCEiSearch...

Gene expression databases

BgeeiQ08879.
CleanExiMM_FBLN1.
ExpressionAtlasiQ08879. baseline and differential.
GenevestigatoriQ08879.

Family and domain databases

InterProiIPR000020. Anaphylatoxin/fibulin.
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.
IPR017048. Fibulin-1.
IPR009030. Growth_fac_rcpt_N_dom.
[Graphical view]
PfamiPF01821. ANATO. 2 hits.
PF12662. cEGF. 3 hits.
PF07645. EGF_CA. 4 hits.
[Graphical view]
PIRSFiPIRSF036313. Fibulin-1. 1 hit.
SMARTiSM00104. ANATO. 3 hits.
SM00181. EGF. 2 hits.
SM00179. EGF_CA. 7 hits.
[Graphical view]
SUPFAMiSSF57184. SSF57184. 4 hits.
PROSITEiPS01177. ANAPHYLATOXIN_1. 3 hits.
PS01178. ANAPHYLATOXIN_2. 3 hits.
PS00010. ASX_HYDROXYL. 4 hits.
PS01186. EGF_2. 3 hits.
PS50026. EGF_3. 4 hits.
PS01187. EGF_CA. 8 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Sequence of extracellular mouse protein BM-90/fibulin and its calcium-dependent binding to other basement-membrane ligands."
    Pan T.-C., Kluge M., Zhang R.Z., Mayer U., Timpl R., Chu M.-L.
    Eur. J. Biochem. 215:733-740(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS C AND D), LIGANDS INTERACTION.
  2. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM C).
    Strain: C57BL/6J.
    Tissue: Head and Urinary bladder.
  3. "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 C).
    Tissue: Mammary tumor.
  4. "Structural and functional characterization of the human and mouse fibulin-1 gene promoters: role of Sp1 and Sp3."
    Castoldi M., Chu M.-L.
    Biochem. J. 362:41-50(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-26.
  5. "Characterization of a novel calcium-binding 90-kDa glycoprotein (BM-90) shared by basement membranes and serum."
    Kluge M., Mann K., Dziadek M., Timpl R.
    Eur. J. Biochem. 193:651-659(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 30-53; 110-117; 231-243; 339-387; 434-439; 469-476; 553-563 AND 574-581.
  6. "Structural characterization of two variants of fibulin-1 that differ in nidogen affinity."
    Sasaki T., Kostka G., Goehring W., Wiedemann H., Mann K., Chu M.-L., Timpl R.
    J. Mol. Biol. 245:241-250(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION OF NID AFFINITY.
  7. "Fibulin-1 and fibulin-2 expression during organogenesis in the developing mouse embryo."
    Zhang H.-Y., Timpl R., Sasaki T., Chu M.-L., Ekblom P.
    Dev. Dyn. 205:348-364(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: DEVELOPMENTAL STAGE.
  8. "Binding of fibulin-1 to nidogen depends on its C-terminal globular domain and a specific array of calcium-binding epidermal growth factor-like (EG) modules."
    Adam S., Goehring W., Wiedemann H., Chu M.-L., Timpl R., Kostka G.
    J. Mol. Biol. 272:226-236(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NID-BINDING SITE.
    Strain: 129/Sv.
  9. "Binding of the G domains of laminin alpha1 and alpha2 chains and perlecan to heparin, sulfatides, alpha-dystroglycan and several extracellular matrix proteins."
    Talts J.F., Andac Z., Goehring W., Brancaccio A., Timpl R.
    EMBO J. 18:863-870(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH LAMA2.
  10. "Fibulin-1 is a ligand for the C-type lectin domains of aggrecan and versican."
    Aspberg A., Adam S., Kostka G., Timpl R., Heinegaard D.
    J. Biol. Chem. 274:20444-20449(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH ACAN AND CSPG2.
  11. "Recombinant domains of mouse nidogen-1 and their binding to basement membrane proteins and monoclonal antibodies."
    Ries A., Goehring W., Fox J.W., Timpl R., Sasaki T.
    Eur. J. Biochem. 268:5119-5128(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH NID.
  12. "Glucocorticoids down-regulate the extracellular matrix proteins fibronectin, fibulin-1 and fibulin-2 in bone marrow stroma."
    Gu Y.-C., Talts J.F., Gullberg D., Timpl R., Ekblom M.
    Eur. J. Haematol. 67:176-184(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: DOWN-REGULATION BY GLUCOCORTICOIDS.
  13. "Fibulin-1 binds the amino-terminal head of beta-amyloid precursor protein and modulates its physiological function."
    Ohsawa I., Takamura C., Kohsaka S.
    J. Neurochem. 76:1411-1420(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
  14. "Interaction of oncogenic papillomavirus E6 proteins with fibulin-1."
    Du M., Fan X., Hong E., Chen J.J.
    Biochem. Biophys. Res. Commun. 296:962-969(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH E6, INHIBITION OF E6-MEDIATED TRANSFORMATION.
  15. "The fibulin-1 gene (FBLN1) is disrupted in a t(12;22) associated with a complex type of synpolydactyly."
    Debeer P., Schoenmakers E.F.P.M., Twal W.O., Argraves W.S., De Smet L., Fryns J.-P., Van De Ven W.J.M.
    J. Med. Genet. 39:98-104(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: DEVELOPMENTAL STAGE.
  16. "TM14 is a new member of the fibulin family (fibulin-7) that interacts with extracellular matrix molecules and is active for cell binding."
    de Vega S., Iwamoto T., Nakamura T., Hozumi K., McKnight D.A., Fisher L.W., Fukumoto S., Yamada Y.
    J. Biol. Chem. 282:30878-30888(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH FBLN7.

Entry informationi

Entry nameiFBLN1_MOUSE
AccessioniPrimary (citable) accession number: Q08879
Secondary accession number(s): Q08878
, Q8C3B1, Q91ZC9, Q922K8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1994
Last sequence update: May 9, 2003
Last modified: February 4, 2015
This is version 151 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. 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.