SubmitCancel

Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

Q08879

- FBLN1_MOUSE

UniProt

Q08879 - FBLN1_MOUSE

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

Fibulin-1

Gene
Fbln1
Organism
Mus musculus (Mouse)
Status
Reviewed - 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
  3. protein binding 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: Ensembl
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 ↔ 61 By similarity
Disulfide bondi37 ↔ 68 By similarity
Disulfide bondi50 ↔ 69 By similarity
Disulfide bondi78 ↔ 109 By similarity
Disulfide bondi91 ↔ 110 By similarity
Glycosylationi98 – 981N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi112 ↔ 136 By similarity
Disulfide bondi113 ↔ 143 By similarity
Disulfide bondi126 ↔ 144 By similarity
Disulfide bondi182 ↔ 192 By similarity
Disulfide bondi188 ↔ 201 By similarity
Disulfide bondi203 ↔ 216 By similarity
Disulfide bondi222 ↔ 235 By similarity
Disulfide bondi229 ↔ 244 By similarity
Disulfide bondi250 ↔ 262 By similarity
Disulfide bondi268 ↔ 281 By similarity
Disulfide bondi275 ↔ 290 By similarity
Disulfide bondi296 ↔ 308 By similarity
Disulfide bondi314 ↔ 327 By similarity
Disulfide bondi321 ↔ 336 By similarity
Disulfide bondi343 ↔ 356 By similarity
Disulfide bondi362 ↔ 375 By similarity
Disulfide bondi369 ↔ 384 By similarity
Disulfide bondi386 ↔ 399 By similarity
Disulfide bondi405 ↔ 417 By similarity
Disulfide bondi413 ↔ 426 By similarity
Disulfide bondi428 ↔ 441 By similarity
Disulfide bondi447 ↔ 456 By similarity
Disulfide bondi452 ↔ 465 By similarity
Disulfide bondi467 ↔ 481 By similarity
Disulfide bondi487 ↔ 500 By similarity
Disulfide bondi496 ↔ 509 By similarity
Disulfide bondi511 ↔ 525 By similarity
Disulfide bondi531 ↔ 544 By similarity
Glycosylationi537 – 5371N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi538 ↔ 553 By similarity
Glycosylationi541 – 5411N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi558 ↔ 579 By 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.1 Publication

Gene expression databases

ArrayExpressiQ08879.
BgeeiQ08879.
CleanExiMM_FBLN1.
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 FBLN7.6 Publications

Protein-protein interaction databases

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

Structurei

3D structure databases

ProteinModelPortaliQ08879.
SMRiQ08879. Positions 186-528.

Family & Domainsi

Domains and Repeats

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

Region

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

Sequence similaritiesi

Belongs to the fibulin family.
Contains 9 EGF-like domains.

Keywords - Domaini

EGF-like domain, Repeat, Signal

Phylogenomic databases

eggNOGiNOG12793.
GeneTreeiENSGT00750000117498.
HOGENOMiHOG000007079.
HOVERGENiHBG051559.
InParanoidiQ08879.
KOiK17307.
OMAiNDEACVR.
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

MERPVPSRLV PLPLLLLSSL SLLAARANAD ISMEACCTDG NQMANQHRDC    50
SLPYTSESKE CRMVQEQCCH NQLEELHCAT GINLASEPEG CASLHSYNSS 100
LETIFIKRCC HCCMLGKASL ARDQTCEPIV MISYQCGLVF RACCVKAREN 150
SDFVQGNGAD LQDPAKIPDE EDQEDPYLND RCRGGGPCKQ QCRDTGDEVI 200
CSCFVGYQLQ SDGVSCEDIN ECITGSHNCR LGESCINTVG SFRCQRDSSC 250
GTGYELTEDN NCKDIDECET GIHNCPPDFI CQNTLGSFRC RPKLQCKSGF 300
IQDALGNCID INECLSISAP CPVGQTCINT EGSYTCQKNV PNCGRGYHLN 350
EEGTRCVDVD ECSPPAEPCG KGHHCLNSPG SFRCECKAGF YFDGISRTCV 400
DINECQRYPG RLCGHKCENT PGSFHCSCSA GFRLSVDGRS CEDVNECLNS 450
PCSQECANVY GSYQCYCRRG YQLSDVDGVT CEDIDECALP TGGHICSYRC 500
INIPGSFQCS CPSSGYRLAP NGRNCQDIDE CVTGIHNCSI NETCFNIQGS 550
FRCLSFECPE NYRRSADTFR QEKTDTVRCI KSCRPNDEAC VRDPVHTVSH 600
TVISLPTFRE FTRPEEIIFL RAVTPLYPAN QADIIFDITE GNLRDSFDII 650
KRYEDGMTVG VVRQVRPIVG PFYAVLKLEM NYVLGGVVSH RNVVNVHIFV 700
SEYWF 705
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

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei569 – 705137FRQEK…SEYWF → RCERLPCHENQECPRLPLRI TYYHLSFPTNIQVPAVVFRM GPSSAVPGDSMQLAITAGNE EGFFTTRKVSHHSGVVALTK PIPEPRDLLLTVKMDLYRHG TVSSFVAKLFIFVSAEL in isoform C. VSP_001386Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti30 – 301D → N AA sequence 1 Publication
Sequence conflicti40 – 401G → P in CAA50207. 1 Publication
Sequence conflicti363 – 3631S → A in CAA50207. 1 Publication
Sequence conflicti385 – 3851E → K in BAC39669. 1 Publication
Sequence conflicti553 – 5531C → Q AA sequence 1 Publication
Sequence conflicti558 – 5581C → Q AA sequence 1 Publication
Isoform C (identifier: Q08879-2)
Sequence conflicti571 – 5711E → A in CAA50206. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
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 .
CCDSi CCDS27719.1. [Q08879-1 ]
PIRi S34968.
S78040.
RefSeqi NP_034310.2. NM_010180.2. [Q08879-1 ]
XP_006520500.1. XM_006520437.1. [Q08879-2 ]
UniGenei Mm.297992.

3D structure databases

ProteinModelPortali Q08879.
SMRi Q08879. Positions 186-528.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 199605. 1 interaction.
IntActi Q08879. 1 interaction.
MINTi MINT-245863.

PTM databases

PhosphoSitei Q08879.

Proteomic databases

MaxQBi Q08879.
PaxDbi Q08879.
PRIDEi Q08879.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000057410 ; ENSMUSP00000054583 ; ENSMUSG00000006369 . [Q08879-1 ]
ENSMUST00000109432 ; ENSMUSP00000105058 ; ENSMUSG00000006369 . [Q08879-2 ]
GeneIDi 14114.
KEGGi mmu:14114.
UCSCi uc007xdb.2. mouse. [Q08879-2 ]
uc011zxk.1. mouse. [Q08879-1 ]

Organism-specific databases

CTDi 2192.
MGIi MGI:95487. Fbln1.

Phylogenomic databases

eggNOGi NOG12793.
GeneTreei ENSGT00750000117498.
HOGENOMi HOG000007079.
HOVERGENi HBG051559.
InParanoidi Q08879.
KOi K17307.
OMAi NDEACVR.
OrthoDBi EOG7P5T0C.
PhylomeDBi Q08879.
TreeFami TF317514.

Enzyme and pathway databases

Reactomei REACT_198998. Molecules associated with elastic fibres.

Miscellaneous databases

ChiTaRSi FBLN1. mouse.
NextBioi 285170.
PROi Q08879.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q08879.
Bgeei Q08879.
CleanExi MM_FBLN1.
Genevestigatori Q08879.

Family and domain databases

InterProi IPR000020. 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 ]
Pfami PF01821. ANATO. 2 hits.
PF12662. cEGF. 3 hits.
PF07645. EGF_CA. 4 hits.
[Graphical view ]
PIRSFi PIRSF036313. Fibulin-1. 1 hit.
SMARTi SM00104. ANATO. 3 hits.
SM00181. EGF. 2 hits.
SM00179. EGF_CA. 7 hits.
[Graphical view ]
SUPFAMi SSF57184. SSF57184. 4 hits.
PROSITEi PS01177. 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 ]
ProtoNeti Search...

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: September 3, 2014
This is version 146 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