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P23142 (FBLN1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 178. 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·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Fibulin-1

Short name=FIBL-1
Gene names
Name:FBLN1
ORF Names:PP213
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length703 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Has been implicated in a role in cellular transformation and tumor invasion, it appears to be a tumor suppressor. May play a role in haemostasis and thrombosis owing to its ability to bind fibrinogen and incorporate into clots. Could play a significant role in modulating the neurotrophic activities of APP, particularly soluble APP. Ref.10 Ref.15 Ref.17 Ref.19

Subunit structure

Homomultimerizes and interacts with various extracellular matrix components such as FN1, LAMA1, LAMA2, NID, ACAN, CSPG2 and type IV collagen. Interacts also with APP, NOV, FGB and HPV type 16, HPV type 18, HPV type 31 and BPV type 1 E6 proteins. Interacts with FBLN7 By similarity. Ref.2 Ref.9 Ref.11 Ref.18 Ref.20 Ref.21

Subcellular location

Secretedextracellular spaceextracellular matrix.

Tissue specificity

Isoform A and isoform B are only expressed in placenta. Isoform C and isoform D are expressed in a variety of tissues and cultured cells. Ref.2

Developmental stage

Widely expressed during embryonic development. Prominent in the matrix of the leptomeningeal anlage, in basement membranes of the neuroepithelium and the perineurium of peripheral nerves. In embryos of gestational week (gw) 4, staining was observed in the early mesenchymal bone anlagen. In gw 6.5 and 8, all perichondrial structures showed expression but the chondrocytes themselves showed no staining. In gw 10, expression is prominent in the interterritorial matrix surrounding the hypertrophic chondrocytes. Ref.12

Induction

Expression increased by estrogen in ovarian cancer cells. Ref.13 Ref.16 Ref.23

Involvement in disease

A chromosomal aberration involving FBLN1 is found in a complex type of synpolydactyly referred to as 3/3-prime/4 synpolydactyly associated with metacarpal and metatarsal synostoses. Reciprocal translocation t(12;22)(p11.2;q13.3) with RASSF8. Fibroblasts derived from a patient with synpolydactyly displayed alterations in the level of isoform D splice variant incorporated into the ECM and secreted into the conditioned culture medium. By contrast, the expression of isoform C was not perturbed in the patients fibroblasts. Furthermore, no aberrant polypeptides were detected in extracts of cultured patients fibroblasts. The translocation t(12;22) may result in haploinsufficiency of the isoform D splice variant, which could lead to the observed limb malformation.

Elevated expression and altered processing of FBLN1 protein is associated with human breast cancer.

Sequence similarities

Belongs to the fibulin family.

Contains 3 anaphylatoxin-like domains.

Contains 9 EGF-like domains.

Sequence caution

The sequence AAG17241.1 differs from that shown. Reason: Frameshift at positions 116, 619 and 639.

Alternative products

This entry describes 4 isoforms produced by alternative splicing. [Align] [Select]
Isoform D (identifier: P23142-1)

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 A (identifier: P23142-2)

The sequence of this isoform differs from the canonical sequence as follows:
     567-703: Missing.
Isoform B (identifier: P23142-3)

The sequence of this isoform differs from the canonical sequence as follows:
     567-703: LQQEKTDTVR...VHIFVSEYWF → QKSKKGRQNTPAGSSKEDCRVLPWKQGLEDTHLDA
Isoform C (identifier: P23142-4)

The sequence of this isoform differs from the canonical sequence as follows:
     567-703: LQQEKTDTVR...VHIFVSEYWF → RCERLPCHEN...KLFIFVSAEL

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2929 Ref.8
Chain30 – 703674Fibulin-1
PRO_0000007563

Regions

Domain36 – 7641Anaphylatoxin-like 1
Domain77 – 11135Anaphylatoxin-like 2
Domain112 – 14433Anaphylatoxin-like 3
Domain176 – 21540EGF-like 1
Domain216 – 26146EGF-like 2; calcium-binding Potential
Domain262 – 30746EGF-like 3; calcium-binding Potential
Domain308 – 35548EGF-like 4; calcium-binding Potential
Domain356 – 39843EGF-like 5; calcium-binding
Domain399 – 44042EGF-like 6; calcium-binding
Domain441 – 48040EGF-like 7; calcium-binding
Domain481 – 52444EGF-like 8; calcium-binding
Domain525 – 57854EGF-like 9; calcium-binding
Region356 – 44085Self-association and FN1-binding; calcium is necessary for homotypic binding, but not for heterotypic binding

Amino acid modifications

Glycosylation981N-linked (GlcNAc...) (complex) Ref.25
Glycosylation5351N-linked (GlcNAc...) Potential
Glycosylation5391N-linked (GlcNAc...) Potential
Disulfide bond36 ↔ 61 By similarity
Disulfide bond37 ↔ 68 By similarity
Disulfide bond50 ↔ 69 By similarity
Disulfide bond78 ↔ 109 By similarity
Disulfide bond91 ↔ 110 By similarity
Disulfide bond112 ↔ 136 By similarity
Disulfide bond113 ↔ 143 By similarity
Disulfide bond126 ↔ 144 By similarity
Disulfide bond180 ↔ 190 By similarity
Disulfide bond186 ↔ 199 By similarity
Disulfide bond201 ↔ 214 By similarity
Disulfide bond220 ↔ 233 By similarity
Disulfide bond227 ↔ 242 By similarity
Disulfide bond248 ↔ 260 By similarity
Disulfide bond266 ↔ 279 By similarity
Disulfide bond273 ↔ 288 By similarity
Disulfide bond294 ↔ 306 By similarity
Disulfide bond312 ↔ 325 By similarity
Disulfide bond319 ↔ 334 By similarity
Disulfide bond341 ↔ 354 By similarity
Disulfide bond360 ↔ 373 By similarity
Disulfide bond367 ↔ 382 By similarity
Disulfide bond384 ↔ 397 By similarity
Disulfide bond403 ↔ 415 By similarity
Disulfide bond411 ↔ 424 By similarity
Disulfide bond426 ↔ 439 By similarity
Disulfide bond445 ↔ 454 By similarity
Disulfide bond450 ↔ 463 By similarity
Disulfide bond465 ↔ 479 By similarity
Disulfide bond485 ↔ 498 By similarity
Disulfide bond494 ↔ 507 By similarity
Disulfide bond509 ↔ 523 By similarity
Disulfide bond529 ↔ 542 By similarity
Disulfide bond536 ↔ 551 By similarity
Disulfide bond556 ↔ 577 By similarity

Natural variations

Alternative sequence567 – 703137Missing in isoform A.
VSP_001383
Alternative sequence567 – 703137LQQEK…SEYWF → QKSKKGRQNTPAGSSKEDCR VLPWKQGLEDTHLDA in isoform B.
VSP_001384
Alternative sequence567 – 703137LQQEK…SEYWF → RCERLPCHENRECSKLPLRI TYYHLSFPTNIQAPAVVFRM GPSSAVPGDSMQLAITGGNE EGFFTTRKVSPHSGVVALTK PVPEPRDLLLTVKMDLSRHG TVSSFVAKLFIFVSAEL in isoform C.
VSP_001385
Natural variant1411Q → R. Ref.1 Ref.2 Ref.3 Ref.4 Ref.6
Corresponds to variant rs136730 [ dbSNP | Ensembl ].
VAR_015650
Natural variant5091C → S.
Corresponds to variant rs1802787 [ dbSNP | Ensembl ].
VAR_055720
Natural variant6951H → R. Ref.3
Corresponds to variant rs13268 [ dbSNP | Ensembl ].
VAR_055721

Experimental info

Sequence conflict131P → Q in AAH22497. Ref.6
Sequence conflict361C → S AA sequence Ref.8
Sequence conflict41 – 422HR → SH AA sequence Ref.8
Sequence conflict5211R → S in AAH22497. Ref.6
Sequence conflict5481G → A in CAA37770. Ref.1
Sequence conflict5481G → A in CAA37771. Ref.1
Sequence conflict5481G → A in CAA37772. Ref.1
Sequence conflict5481G → A in AAB17099. Ref.2
Sequence conflict5481G → A in AAK37822. Ref.3
Isoform C:
Sequence conflict6501E → K in AAG17241. Ref.4
Sequence conflict6621L → F in AAG17241. Ref.4
Sequence conflict680 – 6823SAE → FAK in AAG17241. Ref.4

Sequences

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

Last modified November 25, 2008. Version 4.
Checksum: 302F7ED2DF34CA71

FASTA70377,214
        10         20         30         40         50         60 
MERAAPSRRV PLPLLLLGGL ALLAAGVDAD VLLEACCADG HRMATHQKDC SLPYATESKE 

        70         80         90        100        110        120 
CRMVQEQCCH SQLEELHCAT GISLANEQDR CATPHGDNAS LEATFVKRCC HCCLLGRAAQ 

       130        140        150        160        170        180 
AQGQSCEYSL MVGYQCGQVF QACCVKSQET GDLDVGGLQE TDKIIEVEEE QEDPYLNDRC 

       190        200        210        220        230        240 
RGGGPCKQQC RDTGDEVVCS CFVGYQLLSD GVSCEDVNEC ITGSHSCRLG ESCINTVGSF 

       250        260        270        280        290        300 
RCQRDSSCGT GYELTEDNSC KDIDECESGI HNCLPDFICQ NTLGSFRCRP KLQCKSGFIQ 

       310        320        330        340        350        360 
DALGNCIDIN ECLSISAPCP IGHTCINTEG SYTCQKNVPN CGRGYHLNEE GTRCVDVDEC 

       370        380        390        400        410        420 
APPAEPCGKG HRCVNSPGSF RCECKTGYYF DGISRMCVDV NECQRYPGRL CGHKCENTLG 

       430        440        450        460        470        480 
SYLCSCSVGF RLSVDGRSCE DINECSSSPC SQECANVYGS YQCYCRRGYQ LSDVDGVTCE 

       490        500        510        520        530        540 
DIDECALPTG GHICSYRCIN IPGSFQCSCP SSGYRLAPNG RNCQDIDECV TGIHNCSINE 

       550        560        570        580        590        600 
TCFNIQGGFR CLAFECPENY RRSAATLQQE KTDTVRCIKS CRPNDVTCVF DPVHTISHTV 

       610        620        630        640        650        660 
ISLPTFREFT RPEEIIFLRA ITPPHPASQA NIIFDITEGN LRDSFDIIKR YMDGMTVGVV 

       670        680        690        700 
RQVRPIVGPF HAVLKLEMNY VVGGVVSHRN VVNVHIFVSE YWF 

« Hide

Isoform A [UniParc].

Checksum: 2F8AAA8886D2A1C0
Show »

FASTA56661,552
Isoform B [UniParc].

Checksum: 2203FEF959DB3925
Show »

FASTA60165,443
Isoform C [UniParc].

Checksum: B6B9ED49F590F612
Show »

FASTA68374,434

References

« Hide 'large scale' references
[1]"Fibulin is an extracellular matrix and plasma glycoprotein with repeated domain structure."
Argraves W.S., Tran H., Burgess W.H., Dickerson K.
J. Cell Biol. 111:3155-3164(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS A; B AND C), VARIANT ARG-141.
[2]"Human fibulin-1D: molecular cloning, expression and similarity with S1-5 protein, a new member of the fibulin gene family."
Tran H., Mattei M.-G., Godyna S., Argraves W.S.
Matrix Biol. 15:479-493(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM D), TISSUE SPECIFICITY, VARIANT ARG-141, INTERACTION WITH FN1 AND FGB.
[3]"Translational control of specific genes during differentiation of HL-60 cells."
Krichevsky A.M., Metzer E., Rosen H.
J. Biol. Chem. 274:14295-14305(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM D), VARIANTS ARG-141 AND ARG-695.
[4]"Large-scale cDNA transfection screening for genes related to cancer development and progression."
Wan D., Gong Y., Qin W., Zhang P., Li J., Wei L., Zhou X., Li H., Qiu X., Zhong F., He L., Yu J., Yao G., Jiang H., Qian L., Yu Y., Shu H., Chen X. expand/collapse author list , Xu H., Guo M., Pan Z., Chen Y., Ge C., Yang S., Gu J.
Proc. Natl. Acad. Sci. U.S.A. 101:15724-15729(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM C), VARIANT ARG-141.
[5]"The DNA sequence of human chromosome 22."
Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M., Clamp M., Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., Bagguley C., Bailey J., Barlow K.F., Bates K.N., Beasley O.P., Bird C.P., Blakey S.E., Bridgeman A.M. expand/collapse author list , Buck D., Burgess J., Burrill W.D., Burton J., Carder C., Carter N.P., Chen Y., Clark G., Clegg S.M., Cobley V.E., Cole C.G., Collier R.E., Connor R., Conroy D., Corby N.R., Coville G.J., Cox A.V., Davis J., Dawson E., Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M., Ellington A.G., Evans K.L., Fey J.M., Fleming K., French L., Garner A.A., Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C., Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S., Hunt S.E., Jones M.C., Kershaw J., Kimberley A.M., King A., Laird G.K., Langford C.F., Leversha M.A., Lloyd C., Lloyd D.M., Martyn I.D., Mashreghi-Mohammadi M., Matthews L.H., Mccann O.T., Mcclay J., Mclaren S., McMurray A.A., Milne S.A., Mortimore B.J., Odell C.N., Pavitt R., Pearce A.V., Pearson D., Phillimore B.J.C.T., Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y., Rogers L., Ross M.T., Scott C.E., Sehra H.K., Skuce C.D., Smalley S., Smith M.L., Soderlund C., Spragon L., Steward C.A., Sulston J.E., Swann R.M., Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L., Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L., Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N., Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J., Shintani A., Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., Roe B.A., Chen F., Chu L., Crabtree J., Deschamps S., Do A., Do T., Dorman A., Fang F., Fu Y., Hu P., Hua A., Kenton S., Lai H., Lao H.I., Lewis J., Lewis S., Lin S.-P., Loh P., Malaj E., Nguyen T., Pan H., Phan S., Qi S., Qian Y., Ray L., Ren Q., Shaull S., Sloan D., Song L., Wang Q., Wang Y., Wang Z., White J., Willingham D., Wu H., Yao Z., Zhan M., Zhang G., Chissoe S., Murray J., Miller N., Minx P., Fulton R., Johnson D., Bemis G., Bentley D., Bradshaw H., Bourne S., Cordes M., Du Z., Fulton L., Goela D., Graves T., Hawkins J., Hinds K., Kemp K., Latreille P., Layman D., Ozersky P., Rohlfing T., Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K., Nelson J., Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R., Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., Budarf M.L., McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., Edelmann L., Kim U.J., Shizuya H., Simon M.I., Dumanski J.P., Peyrard M., Kedra D., Seroussi E., Fransson I., Tapia I., Bruder C.E., O'Brien K.P., Wilkinson P., Bodenteich A., Hartman K., Hu X., Khan A.S., Lane L., Tilahun Y., Wright H.
Nature 402:489-495(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]"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), VARIANT ARG-141.
Tissue: Brain.
[7]"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.
[8]"Fibulin, a novel protein that interacts with the fibronectin receptor beta subunit cytoplasmic domain."
Argraves W.S., Dickerson K., Burgess W.H., Ruoslahti E.
Cell 58:623-629(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 30-44.
[9]"Fibulin binds to itself and to the carboxyl-terminal heparin-binding region of fibronectin."
Balbona K., Tran H., Godyna S., Ingham K.C., Strickland D.K., Argraves W.S.
J. Biol. Chem. 267:20120-20125(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: SELF-ASSOCIATION, INTERACTION WITH FN1.
[10]"The association of human fibulin-1 with elastic fibers: an immunohistological, ultrastructural, and RNA study."
Roark E.F., Keene D.R., Haudenschild C.C., Godyna S., Little C.D., Argraves W.S.
J. Histochem. Cytochem. 43:401-411(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: POSSIBLE FUNCTION.
[11]"The interaction of fibulin-1 with fibrinogen. A potential role in hemostasis and thrombosis."
Tran H., Tanaka A., Litvinovich S.V., Medved L.V., Haudenschild C.C., Argraves W.S.
J. Biol. Chem. 270:19458-19464(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH FGB.
[12]"The extracellular matrix proteins fibulin-1 and fibulin-2 in the early human embryo."
Miosge N., Gotz W., Sasaki T., Chu M.-L., Timpl R., Herken R.
Histochem. J. 28:109-116(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: DEVELOPMENTAL STAGE.
[13]"Estrogens increase the expression of fibulin-1, an extracellular matrix protein secreted by human ovarian cancer cells."
Clinton G.M., Rougeot C., Derancourt J., Roger P., Defrenne A., Godyna S., Argraves W.S., Rochefort H.
Proc. Natl. Acad. Sci. U.S.A. 93:316-320(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: INDUCTION.
[14]"The self-association and fibronectin-binding sites of fibulin-1 map to calcium-binding epidermal growth factor-like domains."
Tran H., VanDusen W.J., Argraves W.S.
J. Biol. Chem. 272:22600-22606(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: CALCIUM-BINDING, SELF-ASSOCIATION, FN1-BINDING SITES.
[15]"Suppression of anchorage-independent growth and matrigel invasion and delayed tumor formation by elevated expression of fibulin-1D in human fibrosarcoma-derived cell lines."
Qing J., Maher V.M., Tran H., Argraves W.S., Dunstan R.W., McCormick J.J.
Oncogene 15:2159-2168(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: ROLE IN TUMOR FORMATION AND INVASION.
[16]"Increased immunostaining of fibulin-1, an estrogen-regulated protein in the stroma of human ovarian epithelial tumors."
Roger P., Pujol P., Lucas A., Baldet P., Rochefort H.
Am. J. Pathol. 153:1579-1588(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: INDUCTION.
[17]"Estradiol and fibulin-1 inhibit motility of human ovarian- and breast-cancer cells induced by fibronectin."
Hayashido Y., Lucas A., Rougeot C., Godyna S., Argraves W.S., Rochefort H.
Int. J. Cancer 75:654-658(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: ROLE IN TUMOR FORMATION AND INVASION.
[18]"The C-terminal domain of the regulatory protein NOVH is sufficient to promote interaction with fibulin 1C: a clue for a role of NOVH in cell-adhesion signaling."
Perbal B., Martinerie C., Sainson R., Werner M., He B., Roizman B.
Proc. Natl. Acad. Sci. U.S.A. 96:869-874(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH NOV.
[19]"Fibulin-1 suppression of fibronectin-regulated cell adhesion and motility."
Twal W.O., Czirok A., Hegedus B., Knaak C., Chintalapudi M.R., Okagawa H., Sugi Y., Argraves W.S.
J. Cell Sci. 114:4587-4598(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: ROLE IN CELL ADHESION AND MOTILITY.
[20]"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: INTERACTION WITH APP.
[21]"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 HIGH-RISK HUMAN PAPILLOMAVIRUSES E6 PROTEIN, INHIBITION OF E6-MEDIATED TRANSFORMATION.
[22]"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: CHROMOSOMAL TRANSLOCATION.
[23]"Estrogen induction and overexpression of fibulin-1C mRNA in ovarian cancer cells."
Moll F., Katsaros D., Lazennec G., Hellio N., Roger P., Giacalone P.-L., Chalbos D., Maudelonde T., Rochefort H., Pujol P.
Oncogene 21:1097-1107(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: INDUCTION.
[24]"Elevated expression and altered processing of fibulin-1 protein in human breast cancer."
Greene L.M., Twal W.O., Duffy M.J., McDermott E.W., Hill A.D., O'Higgins N.J., McCann A.H., Dervan P.A., Argraves W.S., Gallagher W.M.
Br. J. Cancer 88:871-878(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: ASSOCIATION WITH BREAST CANCER.
[25]"A strategy for precise and large scale identification of core fucosylated glycoproteins."
Jia W., Lu Z., Fu Y., Wang H.P., Wang L.H., Chi H., Yuan Z.F., Zheng Z.B., Song L.N., Han H.H., Liang Y.M., Wang J.L., Cai Y., Zhang Y.K., Deng Y.L., Ying W.T., He S.M., Qian X.H.
Mol. Cell. Proteomics 8:913-923(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION AT ASN-98.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X53741 mRNA. Translation: CAA37770.1.
X53742 mRNA. Translation: CAA37771.1.
X53743 mRNA. Translation: CAA37772.1.
U01244 mRNA. Translation: AAB17099.1.
AF126110 mRNA. Translation: AAK37822.1.
AF217999 mRNA. Translation: AAG17241.1. Frameshift.
AL021391 Genomic DNA. No translation available.
Z95331 Genomic DNA. No translation available.
Z98047 Genomic DNA. No translation available.
BC022497 mRNA. Translation: AAH22497.1.
AY040589 Genomic DNA. Translation: AAK82945.1.
CCDSCCDS14067.1. [P23142-1]
CCDS14069.1. [P23142-4]
CCDS43028.1. [P23142-2]
PIRC36346.
RefSeqNP_001987.2. NM_001996.3.
NP_006476.2. NM_006485.3.
NP_006477.2. NM_006486.2.
NP_006478.2. NM_006487.2.
UniGeneHs.24601.

3D structure databases

ProteinModelPortalP23142.
SMRP23142. Positions 184-591.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid108486. 30 interactions.
IntActP23142. 26 interactions.
MINTMINT-5005948.

PTM databases

PhosphoSiteP23142.

Polymorphism databases

DMDM215274249.

Proteomic databases

MaxQBP23142.
PaxDbP23142.
PRIDEP23142.

Protocols and materials databases

DNASU2192.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000262722; ENSP00000262722; ENSG00000077942. [P23142-4]
ENST00000327858; ENSP00000331544; ENSG00000077942. [P23142-1]
ENST00000340923; ENSP00000342212; ENSG00000077942. [P23142-2]
ENST00000442170; ENSP00000393812; ENSG00000077942.
GeneID2192.
KEGGhsa:2192.
UCSCuc003bgg.1. human. [P23142-1]
uc003bgh.3. human. [P23142-4]

Organism-specific databases

CTD2192.
GeneCardsGC22P045898.
HGNCHGNC:3600. FBLN1.
HPACAB004393.
HPA001612.
HPA001613.
MIM135820. gene.
608180. phenotype.
neXtProtNX_P23142.
Orphanet295197. Synpolydactyly type 2.
PharmGKBPA28013.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG12793.
HOGENOMHOG000007079.
HOVERGENHBG051559.
KOK17307.
PhylomeDBP23142.
TreeFamTF317514.

Enzyme and pathway databases

ReactomeREACT_118779. Extracellular matrix organization.

Gene expression databases

ArrayExpressP23142.
BgeeP23142.
GenevestigatorP23142.

Family and domain databases

InterProIPR000020. 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]
PfamPF01821. ANATO. 2 hits.
PF12662. cEGF. 2 hits.
PF07645. EGF_CA. 5 hits.
[Graphical view]
PIRSFPIRSF036313. Fibulin-1. 1 hit.
SMARTSM00104. ANATO. 3 hits.
SM00181. EGF. 2 hits.
SM00179. EGF_CA. 7 hits.
[Graphical view]
SUPFAMSSF57184. SSF57184. 2 hits.
PROSITEPS01177. ANAPHYLATOXIN_1. 3 hits.
PS01178. ANAPHYLATOXIN_2. 3 hits.
PS00010. ASX_HYDROXYL. 4 hits.
PS01186. EGF_2. 3 hits.
PS50026. EGF_3. 5 hits.
PS01187. EGF_CA. 8 hits.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSFBLN1. human.
GeneWikiFBLN1.
GenomeRNAi2192.
NextBio8855.
PROP23142.
SOURCESearch...

Entry information

Entry nameFBLN1_HUMAN
AccessionPrimary (citable) accession number: P23142
Secondary accession number(s): B0QY42 expand/collapse secondary AC list , B1AHL4, P23143, P23144, P37888, Q5TIC4, Q8TBH8, Q9HBQ5, Q9UC21, Q9UGR4, Q9UH41
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1991
Last sequence update: November 25, 2008
Last modified: July 9, 2014
This is version 178 of the entry and version 4 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 22

Human chromosome 22: entries, gene names and cross-references to MIM