P23142 (FBLN1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Fibulin-1
Short name=FIBL-1

Gene names

Name:	FBLN1
ORF Names:	PP213

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	703 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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	Secreted › extracellular space › extracellular 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.

Ontologies

Keywords
Biological process	Host-virus interaction
Cellular component	Extracellular matrix Secreted
Coding sequence diversity	Alternative splicing Chromosomal rearrangement Polymorphism
Domain	EGF-like domain Repeat Signal
Ligand	Calcium
PTM	Disulfide bond Glycoprotein
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	embryo implantation Inferred from electronic annotation. Source: Compara extracellular matrix organization Traceable author statement. Source: Reactome virus-host interaction Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	basement membrane Inferred from electronic annotation. Source: Compara extracellular space Inferred from direct assay PubMed 20551380. Source: BHF-UCL proteinaceous extracellular matrix Traceable author statement Ref.1. Source: ProtInc
Molecular_function	calcium ion binding Inferred from electronic annotation. Source: InterPro extracellular matrix structural constituent Traceable author statement Ref.1. Source: ProtInc peptidase activator activity Inferred from electronic annotation. Source: Compara
Complete GO annotation...

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:
     567-601: LQQEKTDTVRCIKSCRPNDVTCVFDPVHTISHTVI → 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 key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Signal peptide	1 – 29	29	Ref.8
	Chain	30 – 703	674	Fibulin-1		PRO_0000007563
Regions
	Domain	36 – 76	41	Anaphylatoxin-like 1
	Domain	77 – 111	35	Anaphylatoxin-like 2
	Domain	112 – 144	33	Anaphylatoxin-like 3
	Domain	176 – 215	40	EGF-like 1
	Domain	216 – 261	46	EGF-like 2; calcium-binding Potential
	Domain	262 – 307	46	EGF-like 3; calcium-binding Potential
	Domain	308 – 355	48	EGF-like 4; calcium-binding Potential
	Domain	356 – 398	43	EGF-like 5; calcium-binding
	Domain	399 – 440	42	EGF-like 6; calcium-binding
	Domain	441 – 480	40	EGF-like 7; calcium-binding
	Domain	481 – 524	44	EGF-like 8; calcium-binding
	Domain	525 – 578	54	EGF-like 9; calcium-binding
	Region	356 – 440	85	Self-association and FN1-binding; calcium is necessary for homotypic binding, but not for heterotypic binding
Amino acid modifications
	Glycosylation	98	1	N-linked (GlcNAc...) Potential
	Glycosylation	535	1	N-linked (GlcNAc...) Potential
	Glycosylation	539	1	N-linked (GlcNAc...) Potential
	Disulfide bond	36 ↔ 61		By similarity
	Disulfide bond	37 ↔ 68		By similarity
	Disulfide bond	50 ↔ 69		By similarity
	Disulfide bond	78 ↔ 109		By similarity
	Disulfide bond	91 ↔ 110		By similarity
	Disulfide bond	112 ↔ 136		By similarity
	Disulfide bond	113 ↔ 143		By similarity
	Disulfide bond	126 ↔ 144		By similarity
	Disulfide bond	180 ↔ 190		By similarity
	Disulfide bond	186 ↔ 199		By similarity
	Disulfide bond	201 ↔ 214		By similarity
	Disulfide bond	220 ↔ 233		By similarity
	Disulfide bond	227 ↔ 242		By similarity
	Disulfide bond	248 ↔ 260		By similarity
	Disulfide bond	266 ↔ 279		By similarity
	Disulfide bond	273 ↔ 288		By similarity
	Disulfide bond	294 ↔ 306		By similarity
	Disulfide bond	312 ↔ 325		By similarity
	Disulfide bond	319 ↔ 334		By similarity
	Disulfide bond	341 ↔ 354		By similarity
	Disulfide bond	360 ↔ 373		By similarity
	Disulfide bond	367 ↔ 382		By similarity
	Disulfide bond	384 ↔ 397		By similarity
	Disulfide bond	403 ↔ 415		By similarity
	Disulfide bond	411 ↔ 424		By similarity
	Disulfide bond	426 ↔ 439		By similarity
	Disulfide bond	445 ↔ 454		By similarity
	Disulfide bond	450 ↔ 463		By similarity
	Disulfide bond	465 ↔ 479		By similarity
	Disulfide bond	485 ↔ 498		By similarity
	Disulfide bond	494 ↔ 507		By similarity
	Disulfide bond	509 ↔ 523		By similarity
	Disulfide bond	529 ↔ 542		By similarity
	Disulfide bond	536 ↔ 551		By similarity
	Disulfide bond	556 ↔ 577		By similarity
Natural variations
	Alternative sequence	567 – 703	137	Missing in isoform A.		VSP_001383
	Alternative sequence	567 – 703	137	LQQEK…SEYWF → RCERLPCHENRECSKLPLRI TYYHLSFPTNIQAPAVVFRM GPSSAVPGDSMQLAITGGNE EGFFTTRKVSPHSGVVALTK PVPEPRDLLLTVKMDLSRHG TVSSFVAKLFIFVSAEL in isoform C.		VSP_001385
	Alternative sequence	567 – 601	35	LQQEK…SHTVI → QKSKKGRQNTPAGSSKEDCR VLPWKQGLEDTHLDA in isoform B.		VSP_001384
	Natural variant	141	1	Q → R. Ref.1 Ref.2 Ref.3 Ref.4 Ref.6 Corresponds to variant rs136730 [ dbSNP | Ensembl ].		VAR_015650
	Natural variant	509	1	C → S. Corresponds to variant rs1802787 [ dbSNP | Ensembl ].		VAR_055720
	Natural variant	695	1	H → R. Ref.3 Corresponds to variant rs13268 [ dbSNP | Ensembl ].		VAR_055721
Experimental info
	Sequence conflict	13	1	P → Q in AAH22497. Ref.6
	Sequence conflict	36	1	C → S AA sequence Ref.8
	Sequence conflict	41 – 42	2	HR → SH AA sequence Ref.8
	Sequence conflict	521	1	R → S in AAH22497. Ref.6
	Sequence conflict	548	1	G → A in CAA37770. Ref.1
	Sequence conflict	548	1	G → A in CAA37771. Ref.1
	Sequence conflict	548	1	G → A in CAA37772. Ref.1
	Sequence conflict	548	1	G → A in AAB17099. Ref.2
	Sequence conflict	548	1	G → A in AAK37822. Ref.3
Isoform C:
	Sequence conflict	650	1	E → K in AAG17241. Ref.4
	Sequence conflict	662	1	L → F in AAG17241. Ref.4
	Sequence conflict	680 – 682	3	SAE → FAK in AAG17241. Ref.4

Sequences

	Sequence		Length	Mass (Da)
	Isoform D [UniParc]. Last modified November 25, 2008. Version 4. Checksum: 302F7ED2DF34CA71	FASTA	703	77,214
	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
	Isoform A [UniParc]. Checksum: 2F8AAA8886D2A1C0	FASTA	566	61,552
	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 TCFNIQGGFR CLAFECPENY RRSAAT
	Isoform B [UniParc]. Checksum: 813A87A43545D9ED	FASTA	703	77,139
	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 RRSAATQKSK KGRQNTPAGS SKEDCRVLPW KQGLEDTHLD 610 620 630 640 650 660 ASLPTFREFT RPEEIIFLRA ITPPHPASQA NIIFDITEGN LRDSFDIIKR YMDGMTVGVV 670 680 690 700 RQVRPIVGPF HAVLKLEMNY VVGGVVSHRN VVNVHIFVSE YWF
	Isoform C [UniParc]. Checksum: B6B9ED49F590F612	FASTA	683	74,434
	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 RRSAATRCER LPCHENRECS KLPLRITYYH LSFPTNIQAP 610 620 630 640 650 660 AVVFRMGPSS AVPGDSMQLA ITGGNEEGFF TTRKVSPHSG VVALTKPVPE PRDLLLTVKM 670 680 DLSRHGTVSS FVAKLFIFVS AEL

References

	« Hide 'large scale' referencesShow '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. , 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. , 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.
+	Additional computationally mapped references.

Web resources

Atlas of Genetics and Cytogenetics in Oncology and Haematology

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. Z95331, Z98047, AL021391 Genomic DNA. Translation: CAI41717.1. Z98047, Z95331, AL021391 Genomic DNA. Translation: CAI19628.1. Z95331, AL021391, Z98047 Genomic DNA. Translation: CAQ08435.1. Z98047, AL021391, Z95331 Genomic DNA. Translation: CAQ10154.1. BC022497 mRNA. Translation: AAH22497.1. AY040589 Genomic DNA. Translation: AAK82945.1.
IPI	IPI00218803. IPI00296534. IPI00296537. IPI00333852.
PIR	C36346.
RefSeq	NP_001987.2. NM_001996.3. NP_006476.2. NM_006485.3. NP_006477.2. NM_006486.2. NP_006478.2. NM_006487.2.
UniGene	Hs.24601.
3D structure databases
ProteinModelPortal	P23142.
ModBase	Search...
Protein-protein interaction databases
IntAct	P23142. 23 interactions.
MINT	MINT-5005948.
PTM databases
PhosphoSite	P23142.
Polymorphism databases
DMDM	215274249.
Proteomic databases
PaxDb	P23142.
PRIDE	P23142.
Protocols and materials databases
DNASU	2192.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000262722; ENSP00000262722; ENSG00000077942. ENST00000327858; ENSP00000331544; ENSG00000077942. ENST00000340923; ENSP00000342212; ENSG00000077942.
GeneID	2192.
KEGG	hsa:2192.
UCSC	uc003bgg.1. human. uc003bgh.3. human.
Organism-specific databases
CTD	2192.
GeneCards	GC22P045898.
HGNC	HGNC:3600. FBLN1.
HPA	CAB004393. HPA001612. HPA001613.
MIM	135820. gene. 608180. phenotype.
neXtProt	NX_P23142.
Orphanet	295197. Synpolydactyly type 2.
PharmGKB	PA28013.
GenAtlas	Search...
Phylogenomic databases
eggNOG	NOG12793.
HOVERGEN	HBG051559.
Enzyme and pathway databases
Reactome	REACT_118779. Extracellular matrix organization.
Gene expression databases
ArrayExpress	P23142.
Bgee	P23142.
Genevestigator	P23142.
GermOnline	ENSG00000077942. Homo sapiens.
Family and domain databases
InterPro	IPR000020. Anaphylatoxin/fibulin. IPR026823. cEGF. IPR000742. EG-like_dom. IPR001881. EGF-like_Ca-bd. IPR013032. EGF-like_CS. IPR000152. EGF-type_Asp/Asn_hydroxyl_site. IPR018097. EGF_Ca-bd_CS. IPR017048. Fibulin-1. [Graphical view]
Pfam	PF01821. ANATO. 2 hits. PF12662. cEGF. 2 hits. PF07645. EGF_CA. 5 hits. [Graphical view]
PIRSF	PIRSF036313. Fibulin-1. 1 hit.
SMART	SM00104. ANATO. 3 hits. SM00181. EGF. 2 hits. SM00179. EGF_CA. 7 hits. [Graphical view]
PROSITE	PS01177. ANAPHYLATOXIN_1. 3 hits. PS01178. ANAPHYLATOXIN_2. 3 hits. PS00010. ASX_HYDROXYL. 4 hits. PS00022. EGF_1. False negative. PS01186. EGF_2. 3 hits. PS50026. EGF_3. 5 hits. PS01187. EGF_CA. 8 hits. [Graphical view]
ProtoNet	Search...
Other
ChiTaRS	FBLN1. human.
GenomeRNAi	2192.
NextBio	8855.
SOURCE	Search...

Entry information

Entry name

FBLN1_HUMAN

Accession

Primary (citable) accession number: P23142
Secondary accession number(s): B0QY42 , 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:	May 29, 2013
This is version 168 of the entry and version 4 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.