FBLN1_HUMAN
ID FBLN1_HUMAN Reviewed; 703 AA.
AC P23142; B0QY42; B1AHL4; P23143; P23144; P37888; Q5TIC4; Q8TBH8; Q9HBQ5;
AC Q9UC21; Q9UGR4; Q9UH41;
DT 01-NOV-1991, integrated into UniProtKB/Swiss-Prot.
DT 25-NOV-2008, sequence version 4.
DT 03-AUG-2022, entry version 245.
DE RecName: Full=Fibulin-1;
DE Short=FIBL-1;
DE Flags: Precursor;
GN Name=FBLN1; ORFNames=PP213;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS A; B AND C), AND VARIANT ARG-141.
RX PubMed=2269669; DOI=10.1083/jcb.111.6.3155;
RA Argraves W.S., Tran H., Burgess W.H., Dickerson K.;
RT "Fibulin is an extracellular matrix and plasma glycoprotein with repeated
RT domain structure.";
RL J. Cell Biol. 111:3155-3164(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM D), TISSUE SPECIFICITY, VARIANT
RP ARG-141, AND INTERACTION WITH FN1 AND FGB.
RX PubMed=9106159; DOI=10.1016/s0945-053x(97)90021-4;
RA Tran H., Mattei M.-G., Godyna S., Argraves W.S.;
RT "Human fibulin-1D: molecular cloning, expression and similarity with S1-5
RT protein, a new member of the fibulin gene family.";
RL Matrix Biol. 15:479-493(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM D), AND VARIANTS ARG-141 AND ARG-695.
RX PubMed=10318851; DOI=10.1074/jbc.274.20.14295;
RA Krichevsky A.M., Metzer E., Rosen H.;
RT "Translational control of specific genes during differentiation of HL-60
RT cells.";
RL J. Biol. Chem. 274:14295-14305(1999).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM C), AND VARIANT ARG-141.
RX PubMed=15498874; DOI=10.1073/pnas.0404089101;
RA Wan D., Gong Y., Qin W., Zhang P., Li J., Wei L., Zhou X., Li H., Qiu X.,
RA Zhong F., He L., Yu J., Yao G., Jiang H., Qian L., Yu Y., Shu H., Chen X.,
RA Xu H., Guo M., Pan Z., Chen Y., Ge C., Yang S., Gu J.;
RT "Large-scale cDNA transfection screening for genes related to cancer
RT development and progression.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:15724-15729(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=10591208; DOI=10.1038/990031;
RA Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M., Clamp M.,
RA Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., Bagguley C.,
RA Bailey J., Barlow K.F., Bates K.N., Beasley O.P., Bird C.P., Blakey S.E.,
RA Bridgeman A.M., Buck D., Burgess J., Burrill W.D., Burton J., Carder C.,
RA Carter N.P., Chen Y., Clark G., Clegg S.M., Cobley V.E., Cole C.G.,
RA Collier R.E., Connor R., Conroy D., Corby N.R., Coville G.J., Cox A.V.,
RA Davis J., Dawson E., Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M.,
RA Ellington A.G., Evans K.L., Fey J.M., Fleming K., French L., Garner A.A.,
RA Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C.,
RA Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S., Hunt S.E.,
RA Jones M.C., Kershaw J., Kimberley A.M., King A., Laird G.K., Langford C.F.,
RA Leversha M.A., Lloyd C., Lloyd D.M., Martyn I.D., Mashreghi-Mohammadi M.,
RA Matthews L.H., Mccann O.T., Mcclay J., Mclaren S., McMurray A.A.,
RA Milne S.A., Mortimore B.J., Odell C.N., Pavitt R., Pearce A.V., Pearson D.,
RA Phillimore B.J.C.T., Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y.,
RA Rogers L., Ross M.T., Scott C.E., Sehra H.K., Skuce C.D., Smalley S.,
RA Smith M.L., Soderlund C., Spragon L., Steward C.A., Sulston J.E.,
RA Swann R.M., Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L.,
RA Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L.,
RA Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N.,
RA Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J., Shintani A.,
RA Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., Roe B.A., Chen F., Chu L.,
RA Crabtree J., Deschamps S., Do A., Do T., Dorman A., Fang F., Fu Y., Hu P.,
RA Hua A., Kenton S., Lai H., Lao H.I., Lewis J., Lewis S., Lin S.-P., Loh P.,
RA Malaj E., Nguyen T., Pan H., Phan S., Qi S., Qian Y., Ray L., Ren Q.,
RA Shaull S., Sloan D., Song L., Wang Q., Wang Y., Wang Z., White J.,
RA Willingham D., Wu H., Yao Z., Zhan M., Zhang G., Chissoe S., Murray J.,
RA Miller N., Minx P., Fulton R., Johnson D., Bemis G., Bentley D.,
RA Bradshaw H., Bourne S., Cordes M., Du Z., Fulton L., Goela D., Graves T.,
RA Hawkins J., Hinds K., Kemp K., Latreille P., Layman D., Ozersky P.,
RA Rohlfing T., Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K.,
RA Nelson J., Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R.,
RA Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., Budarf M.L.,
RA McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., Edelmann L., Kim U.J.,
RA Shizuya H., Simon M.I., Dumanski J.P., Peyrard M., Kedra D., Seroussi E.,
RA Fransson I., Tapia I., Bruder C.E., O'Brien K.P., Wilkinson P.,
RA Bodenteich A., Hartman K., Hu X., Khan A.S., Lane L., Tilahun Y.,
RA Wright H.;
RT "The DNA sequence of human chromosome 22.";
RL Nature 402:489-495(1999).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM C), AND VARIANT ARG-141.
RC TISSUE=Brain;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [7]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-26.
RX PubMed=11829738; DOI=10.1042/0264-6021:3620041;
RA Castoldi M., Chu M.-L.;
RT "Structural and functional characterization of the human and mouse fibulin-
RT 1 gene promoters: role of Sp1 and Sp3.";
RL Biochem. J. 362:41-50(2002).
RN [8]
RP PROTEIN SEQUENCE OF 30-44.
RX PubMed=2527614; DOI=10.1016/0092-8674(89)90097-4;
RA Argraves W.S., Dickerson K., Burgess W.H., Ruoslahti E.;
RT "Fibulin, a novel protein that interacts with the fibronectin receptor beta
RT subunit cytoplasmic domain.";
RL Cell 58:623-629(1989).
RN [9]
RP SELF-ASSOCIATION, AND INTERACTION WITH FN1.
RX PubMed=1400330; DOI=10.1016/s0021-9258(19)88674-x;
RA Balbona K., Tran H., Godyna S., Ingham K.C., Strickland D.K.,
RA Argraves W.S.;
RT "Fibulin binds to itself and to the carboxyl-terminal heparin-binding
RT region of fibronectin.";
RL J. Biol. Chem. 267:20120-20125(1992).
RN [10]
RP POSSIBLE FUNCTION.
RX PubMed=7534784; DOI=10.1177/43.4.7534784;
RA Roark E.F., Keene D.R., Haudenschild C.C., Godyna S., Little C.D.,
RA Argraves W.S.;
RT "The association of human fibulin-1 with elastic fibers: an
RT immunohistological, ultrastructural, and RNA study.";
RL J. Histochem. Cytochem. 43:401-411(1995).
RN [11]
RP INTERACTION WITH FGB.
RX PubMed=7642629; DOI=10.1074/jbc.270.33.19458;
RA Tran H., Tanaka A., Litvinovich S.V., Medved L.V., Haudenschild C.C.,
RA Argraves W.S.;
RT "The interaction of fibulin-1 with fibrinogen. A potential role in
RT hemostasis and thrombosis.";
RL J. Biol. Chem. 270:19458-19464(1995).
RN [12]
RP DEVELOPMENTAL STAGE.
RX PubMed=8737292; DOI=10.1007/bf02331415;
RA Miosge N., Gotz W., Sasaki T., Chu M.-L., Timpl R., Herken R.;
RT "The extracellular matrix proteins fibulin-1 and fibulin-2 in the early
RT human embryo.";
RL Histochem. J. 28:109-116(1996).
RN [13]
RP INDUCTION.
RX PubMed=8552629; DOI=10.1073/pnas.93.1.316;
RA Clinton G.M., Rougeot C., Derancourt J., Roger P., Defrenne A., Godyna S.,
RA Argraves W.S., Rochefort H.;
RT "Estrogens increase the expression of fibulin-1, an extracellular matrix
RT protein secreted by human ovarian cancer cells.";
RL Proc. Natl. Acad. Sci. U.S.A. 93:316-320(1996).
RN [14]
RP CALCIUM-BINDING, SELF-ASSOCIATION, AND FN1-BINDING SITES.
RX PubMed=9278415; DOI=10.1074/jbc.272.36.22600;
RA Tran H., VanDusen W.J., Argraves W.S.;
RT "The self-association and fibronectin-binding sites of fibulin-1 map to
RT calcium-binding epidermal growth factor-like domains.";
RL J. Biol. Chem. 272:22600-22606(1997).
RN [15]
RP ROLE IN TUMOR FORMATION AND INVASION.
RX PubMed=9393974; DOI=10.1038/sj.onc.1201385;
RA Qing J., Maher V.M., Tran H., Argraves W.S., Dunstan R.W., McCormick J.J.;
RT "Suppression of anchorage-independent growth and matrigel invasion and
RT delayed tumor formation by elevated expression of fibulin-1D in human
RT fibrosarcoma-derived cell lines.";
RL Oncogene 15:2159-2168(1997).
RN [16]
RP INDUCTION.
RX PubMed=9811350; DOI=10.1016/s0002-9440(10)65746-x;
RA Roger P., Pujol P., Lucas A., Baldet P., Rochefort H.;
RT "Increased immunostaining of fibulin-1, an estrogen-regulated protein in
RT the stroma of human ovarian epithelial tumors.";
RL Am. J. Pathol. 153:1579-1588(1998).
RN [17]
RP ROLE IN TUMOR FORMATION AND INVASION.
RX PubMed=9466671;
RX DOI=10.1002/(sici)1097-0215(19980209)75:4<654::aid-ijc26>3.0.co;2-7;
RA Hayashido Y., Lucas A., Rougeot C., Godyna S., Argraves W.S., Rochefort H.;
RT "Estradiol and fibulin-1 inhibit motility of human ovarian- and breast-
RT cancer cells induced by fibronectin.";
RL Int. J. Cancer 75:654-658(1998).
RN [18]
RP INTERACTION WITH CCN3.
RX PubMed=9927660; DOI=10.1073/pnas.96.3.869;
RA Perbal B., Martinerie C., Sainson R., Werner M., He B., Roizman B.;
RT "The C-terminal domain of the regulatory protein NOVH is sufficient to
RT promote interaction with fibulin 1C: a clue for a role of NOVH in cell-
RT adhesion signaling.";
RL Proc. Natl. Acad. Sci. U.S.A. 96:869-874(1999).
RN [19]
RP ROLE IN CELL ADHESION AND MOTILITY.
RX PubMed=11792823; DOI=10.1242/jcs.114.24.4587;
RA Twal W.O., Czirok A., Hegedus B., Knaak C., Chintalapudi M.R., Okagawa H.,
RA Sugi Y., Argraves W.S.;
RT "Fibulin-1 suppression of fibronectin-regulated cell adhesion and
RT motility.";
RL J. Cell Sci. 114:4587-4598(2001).
RN [20]
RP INTERACTION WITH APP.
RX PubMed=11238726; DOI=10.1046/j.1471-4159.2001.00144.x;
RA Ohsawa I., Takamura C., Kohsaka S.;
RT "Fibulin-1 binds the amino-terminal head of beta-amyloid precursor protein
RT and modulates its physiological function.";
RL J. Neurochem. 76:1411-1420(2001).
RN [21]
RP INTERACTION WITH HIGH-RISK HUMAN PAPILLOMAVIRUSES E6 PROTEIN (MICROBIAL
RP INFECTION), AND INHIBITION OF E6-MEDIATED TRANSFORMATION.
RX PubMed=12200142; DOI=10.1016/s0006-291x(02)02041-7;
RA Du M., Fan X., Hong E., Chen J.J.;
RT "Interaction of oncogenic papillomavirus E6 proteins with fibulin-1.";
RL Biochem. Biophys. Res. Commun. 296:962-969(2002).
RN [22]
RP CHROMOSOMAL TRANSLOCATION WITH RASSF8.
RX PubMed=11836357; DOI=10.1136/jmg.39.2.98;
RA Debeer P., Schoenmakers E.F.P.M., Twal W.O., Argraves W.S., De Smet L.,
RA Fryns J.-P., Van De Ven W.J.M.;
RT "The fibulin-1 gene (FBLN1) is disrupted in a t(12;22) associated with a
RT complex type of synpolydactyly.";
RL J. Med. Genet. 39:98-104(2002).
RN [23]
RP INDUCTION.
RX PubMed=11850827; DOI=10.1038/sj.onc.1205171;
RA Moll F., Katsaros D., Lazennec G., Hellio N., Roger P., Giacalone P.-L.,
RA Chalbos D., Maudelonde T., Rochefort H., Pujol P.;
RT "Estrogen induction and overexpression of fibulin-1C mRNA in ovarian cancer
RT cells.";
RL Oncogene 21:1097-1107(2002).
RN [24]
RP ASSOCIATION WITH BREAST CANCER.
RX PubMed=12644824; DOI=10.1038/sj.bjc.6600802;
RA Greene L.M., Twal W.O., Duffy M.J., McDermott E.W., Hill A.D.,
RA O'Higgins N.J., McCann A.H., Dervan P.A., Argraves W.S., Gallagher W.M.;
RT "Elevated expression and altered processing of fibulin-1 protein in human
RT breast cancer.";
RL Br. J. Cancer 88:871-878(2003).
RN [25]
RP GLYCOSYLATION AT ASN-98.
RX PubMed=19139490; DOI=10.1074/mcp.m800504-mcp200;
RA Jia W., Lu Z., Fu Y., Wang H.P., Wang L.H., Chi H., Yuan Z.F., Zheng Z.B.,
RA Song L.N., Han H.H., Liang Y.M., Wang J.L., Cai Y., Zhang Y.K., Deng Y.L.,
RA Ying W.T., He S.M., Qian X.H.;
RT "A strategy for precise and large scale identification of core fucosylated
RT glycoproteins.";
RL Mol. Cell. Proteomics 8:913-923(2009).
RN [26]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [27]
RP VARIANT PHE-397.
RX PubMed=24084572; DOI=10.1038/ejhg.2013.210;
RA Bohlega S., Al-Ajlan H., Al-Saif A.;
RT "Mutation of fibulin-1 causes a novel syndrome involving the central
RT nervous system and connective tissues.";
RL Eur. J. Hum. Genet. 22:640-643(2014).
CC -!- FUNCTION: Incorporated into fibronectin-containing matrix fibers. May
CC play a role in cell adhesion and migration along protein fibers within
CC the extracellular matrix (ECM). Could be important for certain
CC developmental processes and contribute to the supramolecular
CC organization of ECM architecture, in particular to those of basement
CC membranes. Has been implicated in a role in cellular transformation and
CC tumor invasion, it appears to be a tumor suppressor. May play a role in
CC haemostasis and thrombosis owing to its ability to bind fibrinogen and
CC incorporate into clots. Could play a significant role in modulating the
CC neurotrophic activities of APP, particularly soluble APP.
CC {ECO:0000269|PubMed:11792823, ECO:0000269|PubMed:9393974,
CC ECO:0000269|PubMed:9466671}.
CC -!- SUBUNIT: Homomultimerizes and interacts with various extracellular
CC matrix components such as FN1, LAMA1, LAMA2, NID, ACAN, CSPG2 and type
CC IV collagen. Interacts also with APP and FGB. Interacts with FBLN7 (By
CC similarity). Interacts with CCN3 (PubMed:9927660). {ECO:0000250,
CC ECO:0000269|PubMed:9927660}.
CC -!- SUBUNIT: (Microbial infection) Interacts with human papillomavirus/HPV
CC type 16, 18 and 31 proteins E6. {ECO:0000269|PubMed:12200142}.
CC -!- INTERACTION:
CC P23142-4; Q9UIJ7: AK3; NbExp=3; IntAct=EBI-11956479, EBI-3916527;
CC P23142-4; Q5BKT4: ALG10; NbExp=3; IntAct=EBI-11956479, EBI-13064220;
CC P23142-4; P05067: APP; NbExp=3; IntAct=EBI-11956479, EBI-77613;
CC P23142-4; P54252: ATXN3; NbExp=3; IntAct=EBI-11956479, EBI-946046;
CC P23142-4; Q9UKJ5: CHIC2; NbExp=3; IntAct=EBI-11956479, EBI-741528;
CC P23142-4; Q02930-3: CREB5; NbExp=3; IntAct=EBI-11956479, EBI-10192698;
CC P23142-4; P42830: CXCL5; NbExp=3; IntAct=EBI-11956479, EBI-12175919;
CC P23142-4; P49639: HOXA1; NbExp=3; IntAct=EBI-11956479, EBI-740785;
CC P23142-4; Q8IUC1: KRTAP11-1; NbExp=3; IntAct=EBI-11956479, EBI-1052037;
CC P23142-4; Q3LHN2: KRTAP19-2; NbExp=3; IntAct=EBI-11956479, EBI-12196745;
CC P23142-4; Q5T7P2: LCE1A; NbExp=3; IntAct=EBI-11956479, EBI-11962058;
CC P23142-4; Q5T7P3: LCE1B; NbExp=3; IntAct=EBI-11956479, EBI-10245913;
CC P23142-4; Q5T751: LCE1C; NbExp=3; IntAct=EBI-11956479, EBI-12224199;
CC P23142-4; Q5T754: LCE1F; NbExp=3; IntAct=EBI-11956479, EBI-11958008;
CC P23142-4; Q5TA76: LCE3A; NbExp=3; IntAct=EBI-11956479, EBI-9394625;
CC P23142-4; Q5TCM9: LCE5A; NbExp=3; IntAct=EBI-11956479, EBI-11955689;
CC P23142-4; Q96FE5: LINGO1; NbExp=3; IntAct=EBI-11956479, EBI-719955;
CC P23142-4; Q8IXW0: LMNTD2; NbExp=3; IntAct=EBI-11956479, EBI-12028858;
CC P23142-4; Q6FHY5: MEOX2; NbExp=3; IntAct=EBI-11956479, EBI-16439278;
CC P23142-4; P52815: MRPL12; NbExp=3; IntAct=EBI-11956479, EBI-358272;
CC P23142-4; Q02548: PAX5; NbExp=3; IntAct=EBI-11956479, EBI-296331;
CC P23142-4; Q8N2U9: SLC66A2; NbExp=3; IntAct=EBI-11956479, EBI-3907610;
CC P23142-4; O43609: SPRY1; NbExp=3; IntAct=EBI-11956479, EBI-3866665;
CC P23142-4; Q8IWZ5: TRIM42; NbExp=3; IntAct=EBI-11956479, EBI-5235829;
CC P23142-4; Q9H9P5-5: UNKL; NbExp=3; IntAct=EBI-11956479, EBI-12817837;
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC matrix.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=D;
CC IsoId=P23142-1; Sequence=Displayed;
CC Name=A;
CC IsoId=P23142-2; Sequence=VSP_001383;
CC Name=B;
CC IsoId=P23142-3; Sequence=VSP_001384;
CC Name=C;
CC IsoId=P23142-4; Sequence=VSP_001385;
CC -!- TISSUE SPECIFICITY: Isoform A and isoform B are only expressed in
CC placenta. Isoform C and isoform D are expressed in a variety of tissues
CC and cultured cells. {ECO:0000269|PubMed:9106159}.
CC -!- DEVELOPMENTAL STAGE: Widely expressed during embryonic development.
CC Prominent in the matrix of the leptomeningeal anlage, in basement
CC membranes of the neuroepithelium and the perineurium of peripheral
CC nerves. In embryos of gestational week (gw) 4, staining was observed in
CC the early mesenchymal bone anlagen. In gw 6.5 and 8, all perichondrial
CC structures showed expression but the chondrocytes themselves showed no
CC staining. In gw 10, expression is prominent in the interterritorial
CC matrix surrounding the hypertrophic chondrocytes.
CC {ECO:0000269|PubMed:8737292}.
CC -!- INDUCTION: Expression increased by estrogen in ovarian cancer cells.
CC {ECO:0000269|PubMed:11850827, ECO:0000269|PubMed:8552629,
CC ECO:0000269|PubMed:9811350}.
CC -!- DISEASE: Note=A chromosomal aberration involving FBLN1 is found in a
CC complex type of synpolydactyly referred to as 3/3-prime/4
CC synpolydactyly associated with metacarpal and metatarsal synostoses.
CC Reciprocal translocation t(12;22)(p11.2;q13.3) with RASSF8. Fibroblasts
CC derived from a patient with synpolydactyly displayed alterations in the
CC level of isoform D splice variant incorporated into the ECM and
CC secreted into the conditioned culture medium. By contrast, the
CC expression of isoform C was not perturbed in the patients fibroblasts.
CC Furthermore, no aberrant polypeptides were detected in extracts of
CC cultured patients fibroblasts. The translocation t(12;22) may result in
CC haploinsufficiency of the isoform D splice variant, which could lead to
CC the observed limb malformation. {ECO:0000269|PubMed:11836357}.
CC -!- DISEASE: Note=Elevated expression and altered processing of FBLN1
CC protein is associated with human breast cancer.
CC {ECO:0000269|PubMed:12644824}.
CC -!- SIMILARITY: Belongs to the fibulin family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAG17241.1; Type=Frameshift; Evidence={ECO:0000305};
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/FBLN1ID44462ch22q13.html";
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DR EMBL; X53741; CAA37770.1; -; mRNA.
DR EMBL; X53742; CAA37771.1; -; mRNA.
DR EMBL; X53743; CAA37772.1; -; mRNA.
DR EMBL; U01244; AAB17099.1; -; mRNA.
DR EMBL; AF126110; AAK37822.1; -; mRNA.
DR EMBL; AF217999; AAG17241.1; ALT_FRAME; mRNA.
DR EMBL; AL021391; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; Z95331; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; Z98047; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC022497; AAH22497.1; -; mRNA.
DR EMBL; AY040589; AAK82945.1; -; Genomic_DNA.
DR CCDS; CCDS14067.1; -. [P23142-1]
DR CCDS; CCDS14068.1; -. [P23142-3]
DR CCDS; CCDS14069.1; -. [P23142-4]
DR CCDS; CCDS43028.1; -. [P23142-2]
DR PIR; C36346; C36346.
DR RefSeq; NP_001987.2; NM_001996.3. [P23142-4]
DR RefSeq; NP_006476.2; NM_006485.3. [P23142-3]
DR RefSeq; NP_006477.2; NM_006486.2. [P23142-1]
DR RefSeq; NP_006478.2; NM_006487.2. [P23142-2]
DR AlphaFoldDB; P23142; -.
DR BioGRID; 108486; 125.
DR IntAct; P23142; 83.
DR MINT; P23142; -.
DR STRING; 9606.ENSP00000331544; -.
DR GlyConnect; 1244; 8 N-Linked glycans (2 sites).
DR GlyGen; P23142; 4 sites, 10 N-linked glycans (2 sites), 1 O-linked glycan (1 site).
DR iPTMnet; P23142; -.
DR PhosphoSitePlus; P23142; -.
DR BioMuta; FBLN1; -.
DR DMDM; 215274249; -.
DR CPTAC; non-CPTAC-1123; -.
DR EPD; P23142; -.
DR jPOST; P23142; -.
DR MassIVE; P23142; -.
DR MaxQB; P23142; -.
DR PaxDb; P23142; -.
DR PeptideAtlas; P23142; -.
DR PRIDE; P23142; -.
DR ProteomicsDB; 2960; -.
DR ProteomicsDB; 54057; -. [P23142-1]
DR ProteomicsDB; 54058; -. [P23142-2]
DR ProteomicsDB; 54059; -. [P23142-3]
DR ProteomicsDB; 54060; -. [P23142-4]
DR Antibodypedia; 886; 329 antibodies from 34 providers.
DR DNASU; 2192; -.
DR Ensembl; ENST00000262722.11; ENSP00000262722.7; ENSG00000077942.19. [P23142-4]
DR Ensembl; ENST00000327858.11; ENSP00000331544.6; ENSG00000077942.19. [P23142-1]
DR Ensembl; ENST00000340923.9; ENSP00000342212.5; ENSG00000077942.19. [P23142-2]
DR Ensembl; ENST00000442170.6; ENSP00000393812.2; ENSG00000077942.19. [P23142-3]
DR GeneID; 2192; -.
DR KEGG; hsa:2192; -.
DR MANE-Select; ENST00000327858.11; ENSP00000331544.6; NM_006486.3; NP_006477.3.
DR UCSC; uc003bgg.2; human. [P23142-1]
DR CTD; 2192; -.
DR DisGeNET; 2192; -.
DR GeneCards; FBLN1; -.
DR HGNC; HGNC:3600; FBLN1.
DR HPA; ENSG00000077942; Low tissue specificity.
DR MalaCards; FBLN1; -.
DR MIM; 135820; gene.
DR MIM; 608180; phenotype.
DR neXtProt; NX_P23142; -.
DR OpenTargets; ENSG00000077942; -.
DR Orphanet; 404451; FBLN1-related developmental delay-central nervous system anomaly-syndactyly syndrome.
DR Orphanet; 295197; Synpolydactyly type 2.
DR PharmGKB; PA28013; -.
DR VEuPathDB; HostDB:ENSG00000077942; -.
DR eggNOG; KOG1217; Eukaryota.
DR GeneTree; ENSGT00940000156642; -.
DR HOGENOM; CLU_004826_1_1_1; -.
DR InParanoid; P23142; -.
DR OMA; LRITHYH; -.
DR OrthoDB; 1174178at2759; -.
DR PhylomeDB; P23142; -.
DR TreeFam; TF317514; -.
DR PathwayCommons; P23142; -.
DR Reactome; R-HSA-2129379; Molecules associated with elastic fibres.
DR SignaLink; P23142; -.
DR BioGRID-ORCS; 2192; 10 hits in 1069 CRISPR screens.
DR ChiTaRS; FBLN1; human.
DR GeneWiki; FBLN1; -.
DR GenomeRNAi; 2192; -.
DR Pharos; P23142; Tbio.
DR PRO; PR:P23142; -.
DR Proteomes; UP000005640; Chromosome 22.
DR RNAct; P23142; protein.
DR Bgee; ENSG00000077942; Expressed in endocervix and 190 other tissues.
DR ExpressionAtlas; P23142; baseline and differential.
DR Genevisible; P23142; HS.
DR GO; GO:0005604; C:basement membrane; IEA:Ensembl.
DR GO; GO:0062023; C:collagen-containing extracellular matrix; HDA:BHF-UCL.
DR GO; GO:0071953; C:elastic fiber; IDA:UniProtKB.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0031012; C:extracellular matrix; IDA:UniProtKB.
DR GO; GO:0005576; C:extracellular region; HDA:BHF-UCL.
DR GO; GO:0005615; C:extracellular space; IDA:UniProtKB.
DR GO; GO:0005509; F:calcium ion binding; IDA:UniProtKB.
DR GO; GO:0005201; F:extracellular matrix structural constituent; IDA:UniProtKB.
DR GO; GO:0070051; F:fibrinogen binding; IPI:UniProtKB.
DR GO; GO:0001968; F:fibronectin binding; IPI:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; IDA:UniProtKB.
DR GO; GO:0005178; F:integrin binding; IDA:UniProtKB.
DR GO; GO:0016504; F:peptidase activator activity; IEA:Ensembl.
DR GO; GO:0008022; F:protein C-terminus binding; IPI:UniProtKB.
DR GO; GO:0044877; F:protein-containing complex binding; IPI:UniProtKB.
DR GO; GO:0072378; P:blood coagulation, fibrin clot formation; IDA:UniProtKB.
DR GO; GO:0007566; P:embryo implantation; IEA:Ensembl.
DR GO; GO:0030198; P:extracellular matrix organization; IEA:Ensembl.
DR GO; GO:0007162; P:negative regulation of cell adhesion; IDA:UniProtKB.
DR GO; GO:2000146; P:negative regulation of cell motility; IDA:UniProtKB.
DR GO; GO:0070373; P:negative regulation of ERK1 and ERK2 cascade; IDA:UniProtKB.
DR GO; GO:0001933; P:negative regulation of protein phosphorylation; IDA:UniProtKB.
DR GO; GO:2000647; P:negative regulation of stem cell proliferation; IDA:UniProtKB.
DR GO; GO:1900025; P:negative regulation of substrate adhesion-dependent cell spreading; IDA:UniProtKB.
DR GO; GO:1904188; P:negative regulation of transformation of host cell by virus; IMP:UniProtKB.
DR GO; GO:0071635; P:negative regulation of transforming growth factor beta production; IDA:UniProtKB.
DR GO; GO:0048146; P:positive regulation of fibroblast proliferation; IDA:UniProtKB.
DR GO; GO:0010628; P:positive regulation of gene expression; IDA:UniProtKB.
DR GO; GO:1904237; P:positive regulation of substrate-dependent cell migration, cell attachment to substrate; IDA:UniProtKB.
DR CDD; cd00017; ANATO; 2.
DR InterPro; IPR000020; Anaphylatoxin/fibulin.
DR InterPro; IPR026823; cEGF.
DR InterPro; IPR001881; EGF-like_Ca-bd_dom.
DR InterPro; IPR000742; EGF-like_dom.
DR InterPro; IPR000152; EGF-type_Asp/Asn_hydroxyl_site.
DR InterPro; IPR018097; EGF_Ca-bd_CS.
DR InterPro; IPR017048; Fibulin-1.
DR InterPro; IPR009030; Growth_fac_rcpt_cys_sf.
DR Pfam; PF12662; cEGF; 3.
DR Pfam; PF07645; EGF_CA; 4.
DR PIRSF; PIRSF036313; Fibulin-1; 1.
DR SMART; SM00104; ANATO; 3.
DR SMART; SM00181; EGF; 9.
DR SMART; SM00179; EGF_CA; 8.
DR SUPFAM; SSF57184; SSF57184; 2.
DR PROSITE; PS01177; ANAPHYLATOXIN_1; 3.
DR PROSITE; PS01178; ANAPHYLATOXIN_2; 3.
DR PROSITE; PS00010; ASX_HYDROXYL; 4.
DR PROSITE; PS01186; EGF_2; 3.
DR PROSITE; PS50026; EGF_3; 5.
DR PROSITE; PS01187; EGF_CA; 8.
PE 1: Evidence at protein level;
KW Alternative splicing; Calcium; Chromosomal rearrangement;
KW Direct protein sequencing; Disulfide bond; EGF-like domain;
KW Extracellular matrix; Glycoprotein; Host-virus interaction;
KW Reference proteome; Repeat; Secreted; Signal.
FT SIGNAL 1..29
FT /evidence="ECO:0000269|PubMed:2527614"
FT CHAIN 30..703
FT /note="Fibulin-1"
FT /id="PRO_0000007563"
FT DOMAIN 36..76
FT /note="Anaphylatoxin-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00022"
FT DOMAIN 77..111
FT /note="Anaphylatoxin-like 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00022"
FT DOMAIN 112..144
FT /note="Anaphylatoxin-like 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00022"
FT DOMAIN 176..215
FT /note="EGF-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 216..261
FT /note="EGF-like 2; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 262..307
FT /note="EGF-like 3; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 308..355
FT /note="EGF-like 4; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 356..398
FT /note="EGF-like 5; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 399..440
FT /note="EGF-like 6; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 441..480
FT /note="EGF-like 7; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 481..524
FT /note="EGF-like 8; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 525..578
FT /note="EGF-like 9; calcium-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT REGION 356..440
FT /note="Self-association and FN1-binding; calcium is
FT necessary for homotypic binding, but not for heterotypic
FT binding"
FT CARBOHYD 98
FT /note="N-linked (GlcNAc...) (complex) asparagine"
FT /evidence="ECO:0000269|PubMed:19139490"
FT CARBOHYD 535
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 539
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 36..61
FT /evidence="ECO:0000250"
FT DISULFID 37..68
FT /evidence="ECO:0000250"
FT DISULFID 50..69
FT /evidence="ECO:0000250"
FT DISULFID 78..109
FT /evidence="ECO:0000250"
FT DISULFID 91..110
FT /evidence="ECO:0000250"
FT DISULFID 112..136
FT /evidence="ECO:0000250"
FT DISULFID 113..143
FT /evidence="ECO:0000250"
FT DISULFID 126..144
FT /evidence="ECO:0000250"
FT DISULFID 180..190
FT /evidence="ECO:0000250"
FT DISULFID 186..199
FT /evidence="ECO:0000250"
FT DISULFID 201..214
FT /evidence="ECO:0000250"
FT DISULFID 220..233
FT /evidence="ECO:0000250"
FT DISULFID 227..242
FT /evidence="ECO:0000250"
FT DISULFID 248..260
FT /evidence="ECO:0000250"
FT DISULFID 266..279
FT /evidence="ECO:0000250"
FT DISULFID 273..288
FT /evidence="ECO:0000250"
FT DISULFID 294..306
FT /evidence="ECO:0000250"
FT DISULFID 312..325
FT /evidence="ECO:0000250"
FT DISULFID 319..334
FT /evidence="ECO:0000250"
FT DISULFID 341..354
FT /evidence="ECO:0000250"
FT DISULFID 360..373
FT /evidence="ECO:0000250"
FT DISULFID 367..382
FT /evidence="ECO:0000250"
FT DISULFID 384..397
FT /evidence="ECO:0000250"
FT DISULFID 403..415
FT /evidence="ECO:0000250"
FT DISULFID 411..424
FT /evidence="ECO:0000250"
FT DISULFID 426..439
FT /evidence="ECO:0000250"
FT DISULFID 445..454
FT /evidence="ECO:0000250"
FT DISULFID 450..463
FT /evidence="ECO:0000250"
FT DISULFID 465..479
FT /evidence="ECO:0000250"
FT DISULFID 485..498
FT /evidence="ECO:0000250"
FT DISULFID 494..507
FT /evidence="ECO:0000250"
FT DISULFID 509..523
FT /evidence="ECO:0000250"
FT DISULFID 529..542
FT /evidence="ECO:0000250"
FT DISULFID 536..551
FT /evidence="ECO:0000250"
FT DISULFID 556..577
FT /evidence="ECO:0000250"
FT VAR_SEQ 567..703
FT /note="Missing (in isoform A)"
FT /evidence="ECO:0000303|PubMed:2269669"
FT /id="VSP_001383"
FT VAR_SEQ 567..703
FT /note="LQQEKTDTVRCIKSCRPNDVTCVFDPVHTISHTVISLPTFREFTRPEEIIFL
FT RAITPPHPASQANIIFDITEGNLRDSFDIIKRYMDGMTVGVVRQVRPIVGPFHAVLKLE
FT MNYVVGGVVSHRNVVNVHIFVSEYWF -> QKSKKGRQNTPAGSSKEDCRVLPWKQGLE
FT DTHLDA (in isoform B)"
FT /evidence="ECO:0000303|PubMed:2269669"
FT /id="VSP_001384"
FT VAR_SEQ 567..703
FT /note="LQQEKTDTVRCIKSCRPNDVTCVFDPVHTISHTVISLPTFREFTRPEEIIFL
FT RAITPPHPASQANIIFDITEGNLRDSFDIIKRYMDGMTVGVVRQVRPIVGPFHAVLKLE
FT MNYVVGGVVSHRNVVNVHIFVSEYWF -> RCERLPCHENRECSKLPLRITYYHLSFPT
FT NIQAPAVVFRMGPSSAVPGDSMQLAITGGNEEGFFTTRKVSPHSGVVALTKPVPEPRDL
FT LLTVKMDLSRHGTVSSFVAKLFIFVSAEL (in isoform C)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:15498874, ECO:0000303|PubMed:2269669"
FT /id="VSP_001385"
FT VARIANT 141
FT /note="Q -> R (in dbSNP:rs136730)"
FT /evidence="ECO:0000269|PubMed:10318851,
FT ECO:0000269|PubMed:15489334, ECO:0000269|PubMed:15498874,
FT ECO:0000269|PubMed:2269669, ECO:0000269|PubMed:9106159"
FT /id="VAR_015650"
FT VARIANT 397
FT /note="C -> F (found in a family with syndactyly,
FT undescended testes, delayed motor milestones, intellectual
FT disability and signs of brain atrophy; unknown pathological
FT significance; dbSNP:rs397509432)"
FT /evidence="ECO:0000269|PubMed:24084572"
FT /id="VAR_072739"
FT VARIANT 509
FT /note="C -> S (in dbSNP:rs1802787)"
FT /id="VAR_055720"
FT VARIANT 695
FT /note="H -> R (in dbSNP:rs13268)"
FT /evidence="ECO:0000269|PubMed:10318851"
FT /id="VAR_055721"
FT CONFLICT 13
FT /note="P -> Q (in Ref. 6; AAH22497)"
FT /evidence="ECO:0000305"
FT CONFLICT 36
FT /note="C -> S (in Ref. 8; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 41..42
FT /note="HR -> SH (in Ref. 8; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 521
FT /note="R -> S (in Ref. 6; AAH22497)"
FT /evidence="ECO:0000305"
FT CONFLICT 548
FT /note="G -> A (in Ref. 1; CAA37770/CAA37771/CAA37772, 2;
FT AAB17099 and 3; AAK37822)"
FT /evidence="ECO:0000305"
FT CONFLICT P23142-4:650
FT /note="E -> K (in Ref. 4; AAG17241)"
FT /evidence="ECO:0000305"
FT CONFLICT P23142-4:662
FT /note="L -> F (in Ref. 4; AAG17241)"
FT /evidence="ECO:0000305"
FT CONFLICT P23142-4:680..682
FT /note="SAE -> FAK (in Ref. 4; AAG17241)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 703 AA; 77214 MW; 302F7ED2DF34CA71 CRC64;
MERAAPSRRV PLPLLLLGGL ALLAAGVDAD VLLEACCADG HRMATHQKDC SLPYATESKE
CRMVQEQCCH SQLEELHCAT GISLANEQDR CATPHGDNAS LEATFVKRCC HCCLLGRAAQ
AQGQSCEYSL MVGYQCGQVF QACCVKSQET GDLDVGGLQE TDKIIEVEEE QEDPYLNDRC
RGGGPCKQQC RDTGDEVVCS CFVGYQLLSD GVSCEDVNEC ITGSHSCRLG ESCINTVGSF
RCQRDSSCGT GYELTEDNSC KDIDECESGI HNCLPDFICQ NTLGSFRCRP KLQCKSGFIQ
DALGNCIDIN ECLSISAPCP IGHTCINTEG SYTCQKNVPN CGRGYHLNEE GTRCVDVDEC
APPAEPCGKG HRCVNSPGSF RCECKTGYYF DGISRMCVDV NECQRYPGRL CGHKCENTLG
SYLCSCSVGF RLSVDGRSCE DINECSSSPC SQECANVYGS YQCYCRRGYQ LSDVDGVTCE
DIDECALPTG GHICSYRCIN IPGSFQCSCP SSGYRLAPNG RNCQDIDECV TGIHNCSINE
TCFNIQGGFR CLAFECPENY RRSAATLQQE KTDTVRCIKS CRPNDVTCVF DPVHTISHTV
ISLPTFREFT RPEEIIFLRA ITPPHPASQA NIIFDITEGN LRDSFDIIKR YMDGMTVGVV
RQVRPIVGPF HAVLKLEMNY VVGGVVSHRN VVNVHIFVSE YWF