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Q75N90

- FBN3_HUMAN

UniProt

Q75N90 - FBN3_HUMAN

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Protein

Fibrillin-3

Gene

FBN3

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at transcript leveli

Functioni

Fibrillins are structural components of 10-12 nm extracellular calcium-binding microfibrils, which occur either in association with elastin or in elastin-free bundles. Fibrillin-containing microfibrils provide long-term force bearing structural support.1 Publication

GO - Molecular functioni

  1. calcium ion binding Source: InterPro
  2. extracellular matrix structural constituent Source: InterPro
Complete GO annotation...

Keywords - Ligandi

Calcium

Enzyme and pathway databases

ReactomeiREACT_118572. Degradation of the extracellular matrix.
REACT_150331. Molecules associated with elastic fibres.
REACT_150366. Elastic fibre formation.

Names & Taxonomyi

Protein namesi
Recommended name:
Fibrillin-3
Gene namesi
Name:FBN3
Synonyms:KIAA1776
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 19

Organism-specific databases

HGNCiHGNC:18794. FBN3.

Subcellular locationi

Secretedextracellular spaceextracellular matrix 1 Publication

GO - Cellular componenti

  1. proteinaceous extracellular matrix Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Extracellular matrix, Secreted

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA38681.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 3131Sequence AnalysisAdd
BLAST
Chaini32 – 28092778Fibrillin-3PRO_0000007586Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi151 ↔ 161PROSITE-ProRule annotation
Disulfide bondi155 ↔ 167PROSITE-ProRule annotation
Disulfide bondi169 ↔ 178PROSITE-ProRule annotation
Disulfide bondi251 ↔ 263PROSITE-ProRule annotation
Disulfide bondi258 ↔ 272PROSITE-ProRule annotation
Disulfide bondi274 ↔ 287PROSITE-ProRule annotation
Glycosylationi406 – 4061N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi412 ↔ 424PROSITE-ProRule annotation
Disulfide bondi419 ↔ 433PROSITE-ProRule annotation
Disulfide bondi435 ↔ 447PROSITE-ProRule annotation
Disulfide bondi453 ↔ 463PROSITE-ProRule annotation
Disulfide bondi458 ↔ 472PROSITE-ProRule annotation
Disulfide bondi474 ↔ 487PROSITE-ProRule annotation
Disulfide bondi493 ↔ 505PROSITE-ProRule annotation
Disulfide bondi500 ↔ 514PROSITE-ProRule annotation
Disulfide bondi516 ↔ 529PROSITE-ProRule annotation
Disulfide bondi535 ↔ 546PROSITE-ProRule annotation
Disulfide bondi541 ↔ 555PROSITE-ProRule annotation
Disulfide bondi557 ↔ 570PROSITE-ProRule annotation
Disulfide bondi576 ↔ 587PROSITE-ProRule annotation
Disulfide bondi582 ↔ 596PROSITE-ProRule annotation
Disulfide bondi598 ↔ 611PROSITE-ProRule annotation
Disulfide bondi686 ↔ 698PROSITE-ProRule annotation
Disulfide bondi693 ↔ 707PROSITE-ProRule annotation
Disulfide bondi709 ↔ 722PROSITE-ProRule annotation
Disulfide bondi728 ↔ 740PROSITE-ProRule annotation
Disulfide bondi735 ↔ 749PROSITE-ProRule annotation
Disulfide bondi751 ↔ 764PROSITE-ProRule annotation
Disulfide bondi770 ↔ 780PROSITE-ProRule annotation
Disulfide bondi775 ↔ 789PROSITE-ProRule annotation
Disulfide bondi791 ↔ 804PROSITE-ProRule annotation
Disulfide bondi873 ↔ 885PROSITE-ProRule annotation
Disulfide bondi880 ↔ 894PROSITE-ProRule annotation
Disulfide bondi896 ↔ 909PROSITE-ProRule annotation
Disulfide bondi990 ↔ 1002PROSITE-ProRule annotation
Disulfide bondi997 ↔ 1011PROSITE-ProRule annotation
Disulfide bondi1013 ↔ 1026PROSITE-ProRule annotation
Glycosylationi1025 – 10251N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi1032 ↔ 1044PROSITE-ProRule annotation
Disulfide bondi1039 ↔ 1053PROSITE-ProRule annotation
Disulfide bondi1055 ↔ 1069PROSITE-ProRule annotation
Disulfide bondi1075 ↔ 1087PROSITE-ProRule annotation
Disulfide bondi1082 ↔ 1096PROSITE-ProRule annotation
Disulfide bondi1098 ↔ 1111PROSITE-ProRule annotation
Disulfide bondi1117 ↔ 1129PROSITE-ProRule annotation
Disulfide bondi1124 ↔ 1138PROSITE-ProRule annotation
Disulfide bondi1140 ↔ 1153PROSITE-ProRule annotation
Disulfide bondi1159 ↔ 1170PROSITE-ProRule annotation
Disulfide bondi1166 ↔ 1179PROSITE-ProRule annotation
Disulfide bondi1181 ↔ 1194PROSITE-ProRule annotation
Disulfide bondi1200 ↔ 1212PROSITE-ProRule annotation
Disulfide bondi1207 ↔ 1221PROSITE-ProRule annotation
Disulfide bondi1223 ↔ 1236PROSITE-ProRule annotation
Disulfide bondi1242 ↔ 1254PROSITE-ProRule annotation
Disulfide bondi1249 ↔ 1263PROSITE-ProRule annotation
Disulfide bondi1265 ↔ 1278PROSITE-ProRule annotation
Disulfide bondi1284 ↔ 1297PROSITE-ProRule annotation
Disulfide bondi1291 ↔ 1306PROSITE-ProRule annotation
Disulfide bondi1308 ↔ 1319PROSITE-ProRule annotation
Disulfide bondi1325 ↔ 1338PROSITE-ProRule annotation
Disulfide bondi1332 ↔ 1347PROSITE-ProRule annotation
Disulfide bondi1349 ↔ 1360PROSITE-ProRule annotation
Disulfide bondi1366 ↔ 1378PROSITE-ProRule annotation
Disulfide bondi1373 ↔ 1387PROSITE-ProRule annotation
Disulfide bondi1389 ↔ 1402PROSITE-ProRule annotation
Disulfide bondi1408 ↔ 1419PROSITE-ProRule annotation
Disulfide bondi1414 ↔ 1428PROSITE-ProRule annotation
Disulfide bondi1430 ↔ 1443PROSITE-ProRule annotation
Glycosylationi1442 – 14421N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi1449 ↔ 1460PROSITE-ProRule annotation
Disulfide bondi1455 ↔ 1469PROSITE-ProRule annotation
Disulfide bondi1471 ↔ 1484PROSITE-ProRule annotation
Glycosylationi1538 – 15381N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi1567 ↔ 1579PROSITE-ProRule annotation
Disulfide bondi1574 ↔ 1588PROSITE-ProRule annotation
Disulfide bondi1590 ↔ 1603PROSITE-ProRule annotation
Disulfide bondi1609 ↔ 1621PROSITE-ProRule annotation
Disulfide bondi1616 ↔ 1630PROSITE-ProRule annotation
Glycosylationi1627 – 16271N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi1632 ↔ 1645PROSITE-ProRule annotation
Glycosylationi1658 – 16581N-linked (GlcNAc...)Sequence Analysis
Glycosylationi1668 – 16681N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi1725 ↔ 1737PROSITE-ProRule annotation
Disulfide bondi1732 ↔ 1746PROSITE-ProRule annotation
Disulfide bondi1748 ↔ 1761PROSITE-ProRule annotation
Disulfide bondi1767 ↔ 1780PROSITE-ProRule annotation
Disulfide bondi1774 ↔ 1789PROSITE-ProRule annotation
Disulfide bondi1791 ↔ 1803PROSITE-ProRule annotation
Disulfide bondi1809 ↔ 1821PROSITE-ProRule annotation
Disulfide bondi1816 ↔ 1830PROSITE-ProRule annotation
Disulfide bondi1832 ↔ 1845PROSITE-ProRule annotation
Disulfide bondi1851 ↔ 1861PROSITE-ProRule annotation
Disulfide bondi1856 ↔ 1870PROSITE-ProRule annotation
Glycosylationi1858 – 18581N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi1872 ↔ 1884PROSITE-ProRule annotation
Disulfide bondi1890 ↔ 1903PROSITE-ProRule annotation
Disulfide bondi1898 ↔ 1912PROSITE-ProRule annotation
Disulfide bondi1914 ↔ 1927PROSITE-ProRule annotation
Disulfide bondi1933 ↔ 1945PROSITE-ProRule annotation
Disulfide bondi1940 ↔ 1954PROSITE-ProRule annotation
Disulfide bondi1956 ↔ 1967PROSITE-ProRule annotation
Disulfide bondi1973 ↔ 1985PROSITE-ProRule annotation
Disulfide bondi1980 ↔ 1994PROSITE-ProRule annotation
Disulfide bondi1996 ↔ 2009PROSITE-ProRule annotation
Glycosylationi2033 – 20331N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi2088 ↔ 2100PROSITE-ProRule annotation
Disulfide bondi2095 ↔ 2109PROSITE-ProRule annotation
Disulfide bondi2111 ↔ 2124PROSITE-ProRule annotation
Disulfide bondi2130 ↔ 2141PROSITE-ProRule annotation
Disulfide bondi2136 ↔ 2150PROSITE-ProRule annotation
Disulfide bondi2152 ↔ 2164PROSITE-ProRule annotation
Disulfide bondi2170 ↔ 2181PROSITE-ProRule annotation
Disulfide bondi2177 ↔ 2190PROSITE-ProRule annotation
Disulfide bondi2192 ↔ 2205PROSITE-ProRule annotation
Disulfide bondi2211 ↔ 2225PROSITE-ProRule annotation
Disulfide bondi2218 ↔ 2234PROSITE-ProRule annotation
Disulfide bondi2236 ↔ 2250PROSITE-ProRule annotation
Disulfide bondi2256 ↔ 2268PROSITE-ProRule annotation
Disulfide bondi2263 ↔ 2277PROSITE-ProRule annotation
Disulfide bondi2279 ↔ 2292PROSITE-ProRule annotation
Disulfide bondi2367 ↔ 2379PROSITE-ProRule annotation
Disulfide bondi2374 ↔ 2388PROSITE-ProRule annotation
Disulfide bondi2390 ↔ 2403PROSITE-ProRule annotation
Disulfide bondi2409 ↔ 2420PROSITE-ProRule annotation
Disulfide bondi2416 ↔ 2429PROSITE-ProRule annotation
Disulfide bondi2431 ↔ 2444PROSITE-ProRule annotation
Disulfide bondi2450 ↔ 2461PROSITE-ProRule annotation
Disulfide bondi2457 ↔ 2470PROSITE-ProRule annotation
Disulfide bondi2472 ↔ 2483PROSITE-ProRule annotation
Disulfide bondi2489 ↔ 2502PROSITE-ProRule annotation
Disulfide bondi2496 ↔ 2511PROSITE-ProRule annotation
Disulfide bondi2513 ↔ 2526PROSITE-ProRule annotation
Disulfide bondi2532 ↔ 2542PROSITE-ProRule annotation
Disulfide bondi2538 ↔ 2551PROSITE-ProRule annotation
Disulfide bondi2553 ↔ 2566PROSITE-ProRule annotation
Disulfide bondi2572 ↔ 2584PROSITE-ProRule annotation
Disulfide bondi2579 ↔ 2593PROSITE-ProRule annotation
Disulfide bondi2595 ↔ 2608PROSITE-ProRule annotation
Disulfide bondi2614 ↔ 2625PROSITE-ProRule annotation
Disulfide bondi2621 ↔ 2634PROSITE-ProRule annotation
Disulfide bondi2636 ↔ 2648PROSITE-ProRule annotation
Glycosylationi2713 – 27131N-linked (GlcNAc...)Sequence Analysis

Post-translational modificationi

Probably forms intermolecular disulfide bonds either with other FBN3 molecules or with other components of the microfibrils.By similarity

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

PaxDbiQ75N90.
PRIDEiQ75N90.

PTM databases

PhosphoSiteiQ75N90.

Expressioni

Tissue specificityi

Predominantly expressed in connective tissues such as skeletal muscle, tendon, skin, perichondrium and periosteum. Highly expressed in fetal lung, brain, kidney. Expressed at low level in prostate, testis, mammary gland, uterus, ovary, placenta, bladder, adrenal gland, thyroid, fetal thymus, fetal liver, liver, fetal heart and heart.1 Publication

Gene expression databases

BgeeiQ75N90.
CleanExiHS_FBN3.
GenevestigatoriQ75N90.

Organism-specific databases

HPAiHPA049482.

Interactioni

Protein-protein interaction databases

BioGridi124100. 13 interactions.
IntActiQ75N90. 15 interactions.
MINTiMINT-4095014.
STRINGi9606.ENSP00000270509.

Structurei

3D structure databases

ProteinModelPortaliQ75N90.
SMRiQ75N90. Positions 46-179, 181-612, 682-910, 983-2636.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini147 – 17933EGF-like 1PROSITE-ProRule annotationAdd
BLAST
Domaini185 – 23753TB 1Add
BLAST
Domaini247 – 28842EGF-like 2; calcium-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini293 – 34654TB 2Add
BLAST
Domaini408 – 44841EGF-like 3PROSITE-ProRule annotationAdd
BLAST
Domaini449 – 48840EGF-like 4; calcium-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini489 – 53042EGF-like 5; calcium-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini531 – 57141EGF-like 6; calcium-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini572 – 61241EGF-like 7; calcium-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini618 – 67053TB 3Add
BLAST
Domaini682 – 72342EGF-like 8; calcium-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini724 – 76542EGF-like 9; calcium-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini766 – 80540EGF-like 10; calcium-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini810 – 86152TB 4Add
BLAST
Domaini869 – 91042EGF-like 11; calcium-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini915 – 96652TB 5Add
BLAST
Domaini986 – 102742EGF-like 12; calcium-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini1028 – 107043EGF-like 13; calcium-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini1071 – 111242EGF-like 14; calcium-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini1113 – 115442EGF-like 15; calcium-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini1155 – 119541EGF-like 16; calcium-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini1196 – 123742EGF-like 17PROSITE-ProRule annotationAdd
BLAST
Domaini1238 – 127942EGF-like 18; calcium-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini1280 – 132041EGF-like 19; calcium-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini1321 – 136141EGF-like 20; calcium-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini1362 – 140342EGF-like 21; calcium-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini1404 – 144441EGF-like 22; calcium-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini1445 – 148541EGF-like 23; calcium-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini1490 – 154657TB 6Add
BLAST
Domaini1563 – 160442EGF-like 24; calcium-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini1605 – 164642EGF-like 25; calcium-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini1651 – 170353TB 7Add
BLAST
Domaini1721 – 176242EGF-like 26; calcium-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini1763 – 180442EGF-like 27; calcium-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini1805 – 184642EGF-like 28PROSITE-ProRule annotationAdd
BLAST
Domaini1847 – 188539EGF-like 29; calcium-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini1886 – 192843EGF-like 30; calcium-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini1929 – 196840EGF-like 31; calcium-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini1969 – 201042EGF-like 32; calcium-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini2015 – 206854TB 8Add
BLAST
Domaini2084 – 212542EGF-like 33; calcium-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini2126 – 216540EGF-like 34; calcium-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini2166 – 220641EGF-like 35; calcium-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini2207 – 225145EGF-like 36; calcium-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini2252 – 229342EGF-like 37; calcium-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini2298 – 235154TB 9Add
BLAST
Domaini2363 – 240442EGF-like 38; calcium-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini2405 – 244541EGF-like 39; calcium-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini2446 – 248439EGF-like 40; calcium-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini2485 – 252743EGF-like 41; calcium-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini2528 – 256740EGF-like 42; calcium-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini2568 – 260942EGF-like 43; calcium-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini2610 – 264940EGF-like 44; calcium-bindingPROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the fibrillin family.Curated
Contains 44 EGF-like domains.PROSITE-ProRule annotation
Contains 9 TB (TGF-beta binding) domains.Curated

Keywords - Domaini

EGF-like domain, Repeat, Signal

Phylogenomic databases

eggNOGiNOG12793.
GeneTreeiENSGT00770000120465.
HOGENOMiHOG000231768.
HOVERGENiHBG005643.
InParanoidiQ75N90.
OMAiSCARPFP.
OrthoDBiEOG7RV9F6.
PhylomeDBiQ75N90.
TreeFamiTF316849.

Family and domain databases

Gene3Di3.90.290.10. 9 hits.
InterProiIPR026823. 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.
IPR011398. FBN/EtMIC4.
IPR009030. Growth_fac_rcpt_N_dom.
IPR017878. TB_dom.
[Graphical view]
PANTHERiPTHR24039. PTHR24039. 1 hit.
PfamiPF12662. cEGF. 3 hits.
PF00008. EGF. 1 hit.
PF07645. EGF_CA. 38 hits.
PF00683. TB. 9 hits.
[Graphical view]
PIRSFiPIRSF036312. Fibrillin. 1 hit.
SMARTiSM00181. EGF. 4 hits.
SM00179. EGF_CA. 41 hits.
[Graphical view]
SUPFAMiSSF57184. SSF57184. 12 hits.
SSF57581. SSF57581. 9 hits.
PROSITEiPS00010. ASX_HYDROXYL. 41 hits.
PS00022. EGF_1. 2 hits.
PS01186. EGF_2. 36 hits.
PS50026. EGF_3. 44 hits.
PS01187. EGF_CA. 40 hits.
PS51364. TB. 9 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

Q75N90-1 [UniParc]FASTAAdd to Basket

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        10         20         30         40         50
MTLEGLYLAR GPLARLLLAW SALLCMAGGQ GRWDGALEAA GPGRVRRRGS
60 70 80 90 100
PGILQGPNVC GSRFHAYCCP GWRTFPGRSQ CVVPICRRAC GEGFCSQPNL
110 120 130 140 150
CTCADGTLAP SCGVSRGSGC SVSCMNGGTC RGASCLCQKG YTGTVCGQPI
160 170 180 190 200
CDRGCHNGGR CIGPNRCACV YGFMGPQCER DYRTGPCFGQ VGPEGCQHQL
210 220 230 240 250
TGLVCTKALC CATVGRAWGL PCELCPAQPH PCRRGFIPNI HTGACQDVDE
260 270 280 290 300
CQAVPGLCQG GSCVNMVGSF HCRCPVGHRL SDSSAACEDY RAGACFSVLF
310 320 330 340 350
GGRCAGDLAG HYTRRQCCCD RGRCWAAGPV PELCPPRGSN EFQQLCAQRL
360 370 380 390 400
PLLPGHPGLF PGLLGFGSNG MGPPLGPARL NPHGSDARGI PSLGPGNSNI
410 420 430 440 450
GTATLNQTID ICRHFTNLCL NGRCLPTPSS YRCECNVGYT QDVRGECIDV
460 470 480 490 500
DECTSSPCHH GDCVNIPGTY HCRCYPGFQA TPTRQACVDV DECIVSGGLC
510 520 530 540 550
HLGRCVNTEG SFQCVCNAGF ELSPDGKNCV DHNECATSTM CVNGVCLNED
560 570 580 590 600
GSFSCLCKPG FLLAPGGHYC MDIDECQTPG ICVNGHCTNT EGSFRCQCLG
610 620 630 640 650
GLAVGTDGRV CVDTHVRSTC YGAIEKGSCA RPFPGTVTKS ECCCANPDHG
660 670 680 690 700
FGEPCQLCPA KDSAEFQALC SSGLGITTDG RDINECALDP EVCANGVCEN
710 720 730 740 750
LRGSYRCVCN LGYEAGASGK DCTDVDECAL NSLLCDNGWC QNSPGSYSCS
760 770 780 790 800
CPPGFHFWQD TEICKDVDEC LSSPCVSGVC RNLAGSYTCK CGPGSRLDPS
810 820 830 840 850
GTFCLDSTKG TCWLKIQESR CEVNLQGASL RSECCATLGA AWGSPCERCE
860 870 880 890 900
IDPACARGFA RMTGVTCDDV NECESFPGVC PNGRCVNTAG SFRCECPEGL
910 920 930 940 950
MLDASGRLCV DVRLEPCFLR WDEDECGVTL PGKYRMDVCC CSIGAVWGVE
960 970 980 990 1000
CEACPDPESL EFASLCPRGL GFASRDFLSG RPFYKDVNEC KVFPGLCTHG
1010 1020 1030 1040 1050
TCRNTVGSFH CACAGGFALD AQERNCTDID ECRISPDLCG QGTCVNTPGS
1060 1070 1080 1090 1100
FECECFPGYE SGFMLMKNCM DVDECARDPL LCRGGTCTNT DGSYKCQCPP
1110 1120 1130 1140 1150
GHELTAKGTA CEDIDECSLS DGLCPHGQCV NVIGAFQCSC HAGFQSTPDR
1160 1170 1180 1190 1200
QGCVDINECR VQNGGCDVHC INTEGSYRCS CGQGYSLMPD GRACADVDEC
1210 1220 1230 1240 1250
EENPRVCDQG HCTNMPGGHR CLCYDGFMAT PDMRTCVDVD ECDLNPHICL
1260 1270 1280 1290 1300
HGDCENTKGS FVCHCQLGYM VRKGATGCSD VDECEVGGHN CDSHASCLNI
1310 1320 1330 1340 1350
PGSFSCRCLP GWVGDGFECH DLDECVSQEH RCSPRGDCLN VPGSYRCTCR
1360 1370 1380 1390 1400
QGFAGDGFFC EDRDECAENV DLCDNGQCLN APGGYRCECE MGFDPTEDHR
1410 1420 1430 1440 1450
ACQDVDECAQ GNLCAFGSCE NLPGMFRCIC NGGYELDRGG GNCTDINECA
1460 1470 1480 1490 1500
DPVNCINGVC INTPGSYLCS CPQDFELNPS GVGCVDTRAG NCFLETHDRG
1510 1520 1530 1540 1550
DSGISCSAEI GVGVTRASCC CSLGRAWGNP CELCPMANTT EYRTLCPGGE
1560 1570 1580 1590 1600
GFQPNRITVI LEDIDECQEL PGLCQGGDCV NTFGSFQCEC PPGYHLSEHT
1610 1620 1630 1640 1650
RICEDIDECS THSGICGPGT CYNTLGNYTC VCPAEYLQVN GGNNCMDMRK
1660 1670 1680 1690 1700
SVCFRHYNGT CQNELAFNVT RKMCCCSYNI GQAWNRPCEA CPTPISPDYQ
1710 1720 1730 1740 1750
ILCGNQAPGF LTDIHTGKPL DIDECGEIPA ICANGICINQ IGSFRCECPA
1760 1770 1780 1790 1800
GFNYNSILLA CEDVDECGSR ESPCQQNADC INIPGSYRCK CTRGYKLSPG
1810 1820 1830 1840 1850
GACVGRNECR EIPNVCSHGD CMDTEGSYMC LCHRGFQASA DQTLCMDIDE
1860 1870 1880 1890 1900
CDRQPCGNGT CKNIIGSYNC LCFPGFVVTH NGDCVDFDEC TTLVGQVCRF
1910 1920 1930 1940 1950
GHCLNTAGSF HCLCQDGFEL TADGKNCVDT NECLSLAGTC LPGTCQNLEG
1960 1970 1980 1990 2000
SFRCICPPGF QVQSDHCIDI DECSEEPNLC LFGTCTNSPG SFQCLCPPGF
2010 2020 2030 2040 2050
VLSDNGHRCF DTRQSFCFTR FEAGKCSVPK AFNTTKTRCC CSKRPGEGWG
2060 2070 2080 2090 2100
DPCELCPQEG SAAFQELCPF GHGAVPGPDD SREDVNECAE NPGVCTNGVC
2110 2120 2130 2140 2150
VNTDGSFRCE CPFGYSLDFT GINCVDTDEC SVGHPCGQGT CTNVIGGFEC
2160 2170 2180 2190 2200
ACADGFEPGL MMTCEDIDEC SLNPLLCAFR CHNTEGSYLC TCPAGYTLRE
2210 2220 2230 2240 2250
DGAMCRDVDE CADGQQDCHA RGMECKNLIG TFACVCPPGM RPLPGSGEGC
2260 2270 2280 2290 2300
TDDNECHAQP DLCVNGRCVN TAGSFRCDCD EGFQPSPTLT ECHDIRQGPC
2310 2320 2330 2340 2350
FAEVLQTMCR SLSSSSEAVT RAECCCGGGR GWGPRCELCP LPGTSAYRKL
2360 2370 2380 2390 2400
CPHGSGYTAE GRDVDECRML AHLCAHGECI NSLGSFRCHC QAGYTPDATA
2410 2420 2430 2440 2450
TTCLDMDECS QVPKPCTFLC KNTKGSFLCS CPRGYLLEED GRTCKDLDEC
2460 2470 2480 2490 2500
TSRQHNCQFL CVNTVGAFTC RCPPGFTQHH QACFDNDECS AQPGPCGAHG
2510 2520 2530 2540 2550
HCHNTPGSFR CECHQGFTLV SSGHGCEDVN ECDGPHRCQH GCQNQLGGYR
2560 2570 2580 2590 2600
CSCPQGFTQH SQWAQCVDEN ECALSPPTCG SASCRNTLGG FRCVCPSGFD
2610 2620 2630 2640 2650
FDQALGGCQE VDECAGRRGP CSYSCANTPG GFLCGCPQGY FRAGQGHCVS
2660 2670 2680 2690 2700
GLGFSPGPQD TPDKEELLSS EACYECKING LSPRDRPRRS AHRDHQVNLA
2710 2720 2730 2740 2750
TLDSEALLTL GLNLSHLGRA ERILELRPAL EGLEGRIRYV IVRGNEQGFF
2760 2770 2780 2790 2800
RMHHLRGVSS LQLGRRRPGP GTYRLEVVSH MAGPWGVQPE GQPGPWGQAL

RLKVQLQLL
Length:2,809
Mass (Da):300,356
Last modified:May 18, 2010 - v3
Checksum:iFE47EF22C1307C14
GO

Sequence cautioni

The sequence BAB47408.2 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti119 – 1191G → A.
Corresponds to variant rs3813773 [ dbSNP | Ensembl ].
VAR_019493
Natural varianti329 – 3291P → L.
Corresponds to variant rs7246376 [ dbSNP | Ensembl ].
VAR_055736
Natural varianti371 – 3711M → I.
Corresponds to variant rs35999680 [ dbSNP | Ensembl ].
VAR_055737
Natural varianti473 – 4731R → Q.1 Publication
Corresponds to variant rs35277492 [ dbSNP | Ensembl ].
VAR_019494
Natural varianti542 – 5421V → I.
Corresponds to variant rs36124795 [ dbSNP | Ensembl ].
VAR_055738
Natural varianti662 – 6621D → N.3 Publications
Corresponds to variant rs4804271 [ dbSNP | Ensembl ].
VAR_019495
Natural varianti868 – 8681D → N.
Corresponds to variant rs35025963 [ dbSNP | Ensembl ].
VAR_055739
Natural varianti935 – 9351R → L.1 Publication
VAR_019496
Natural varianti938 – 9381V → F.1 Publication
VAR_019497
Natural varianti1083 – 10831R → W.1 Publication
Corresponds to variant rs35579498 [ dbSNP | Ensembl ].
VAR_019498
Natural varianti1209 – 12091Q → R.
Corresponds to variant rs34684510 [ dbSNP | Ensembl ].
VAR_055740
Natural varianti1293 – 12931S → G.
Corresponds to variant rs4804063 [ dbSNP | Ensembl ].
VAR_055741
Natural varianti1293 – 12931S → N.
Corresponds to variant rs4804063 [ dbSNP | Ensembl ].
VAR_019499
Natural varianti1326 – 13261V → I.1 Publication
Corresponds to variant rs12975322 [ dbSNP | Ensembl ].
VAR_019500
Natural varianti1431 – 14311N → I.
Corresponds to variant rs17160194 [ dbSNP | Ensembl ].
VAR_055742
Natural varianti1614 – 16141G → S.2 Publications
Corresponds to variant rs33967815 [ dbSNP | Ensembl ].
VAR_019501
Natural varianti1806 – 18061R → Q.1 Publication
Corresponds to variant rs3829817 [ dbSNP | Ensembl ].
VAR_019502
Natural varianti1850 – 18501E → K.
Corresponds to variant rs10404519 [ dbSNP | Ensembl ].
VAR_055743
Natural varianti1869 – 18691N → K.1 Publication
Corresponds to variant rs12150963 [ dbSNP | Ensembl ].
VAR_019503
Natural varianti1904 – 19041L → F.
Corresponds to variant rs12608849 [ dbSNP | Ensembl ].
VAR_055744
Natural varianti1904 – 19041L → P.1 Publication
Corresponds to variant rs12608849 [ dbSNP | Ensembl ].
VAR_019504
Natural varianti1939 – 19391T → N.
Corresponds to variant rs7245558 [ dbSNP | Ensembl ].
VAR_055745
Natural varianti1958 – 19581P → H.
Corresponds to variant rs7245429 [ dbSNP | Ensembl ].
VAR_019505
Natural varianti1966 – 19661H → D.
Corresponds to variant rs34167077 [ dbSNP | Ensembl ].
VAR_055746
Natural varianti2005 – 20051N → T.
Corresponds to variant rs17202741 [ dbSNP | Ensembl ].
VAR_055747
Natural varianti2314 – 23141S → N.
Corresponds to variant rs17160151 [ dbSNP | Ensembl ].
VAR_055748
Natural varianti2471 – 24711R → H.
Corresponds to variant rs3848570 [ dbSNP | Ensembl ].
VAR_055749
Natural varianti2540 – 25401H → Q.
Corresponds to variant rs35477781 [ dbSNP | Ensembl ].
VAR_055750
Natural varianti2594 – 25941V → I.
Corresponds to variant rs35318692 [ dbSNP | Ensembl ].
VAR_055751
Natural varianti2610 – 26101E → D.3 Publications
Corresponds to variant rs7257948 [ dbSNP | Ensembl ].
VAR_019506

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY165863 mRNA. Translation: AAO18145.1.
AY165864 mRNA. Translation: AAO18146.1.
AY165865 mRNA. Translation: AAO18147.1.
AB177797 Genomic DNA. Translation: BAD16733.1.
AB177798 Genomic DNA. Translation: BAD16734.1.
AB177799 Genomic DNA. Translation: BAD16735.1.
AB177800 Genomic DNA. Translation: BAD16736.1.
AB053450 mRNA. Translation: BAB47408.2. Different initiation.
AC008946 Genomic DNA. No translation available.
AC022146 Genomic DNA. No translation available.
CCDSiCCDS12196.1.
RefSeqiNP_115823.3. NM_032447.3.
UniGeneiHs.370362.

Genome annotation databases

EnsembliENST00000270509; ENSP00000270509; ENSG00000142449.
ENST00000600128; ENSP00000470498; ENSG00000142449.
ENST00000601739; ENSP00000472324; ENSG00000142449.
GeneIDi84467.
KEGGihsa:84467.
UCSCiuc002mjf.3. human.

Polymorphism databases

DMDMi296439346.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY165863 mRNA. Translation: AAO18145.1 .
AY165864 mRNA. Translation: AAO18146.1 .
AY165865 mRNA. Translation: AAO18147.1 .
AB177797 Genomic DNA. Translation: BAD16733.1 .
AB177798 Genomic DNA. Translation: BAD16734.1 .
AB177799 Genomic DNA. Translation: BAD16735.1 .
AB177800 Genomic DNA. Translation: BAD16736.1 .
AB053450 mRNA. Translation: BAB47408.2 . Different initiation.
AC008946 Genomic DNA. No translation available.
AC022146 Genomic DNA. No translation available.
CCDSi CCDS12196.1.
RefSeqi NP_115823.3. NM_032447.3.
UniGenei Hs.370362.

3D structure databases

ProteinModelPortali Q75N90.
SMRi Q75N90. Positions 46-179, 181-612, 682-910, 983-2636.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 124100. 13 interactions.
IntActi Q75N90. 15 interactions.
MINTi MINT-4095014.
STRINGi 9606.ENSP00000270509.

PTM databases

PhosphoSitei Q75N90.

Polymorphism databases

DMDMi 296439346.

Proteomic databases

PaxDbi Q75N90.
PRIDEi Q75N90.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000270509 ; ENSP00000270509 ; ENSG00000142449 .
ENST00000600128 ; ENSP00000470498 ; ENSG00000142449 .
ENST00000601739 ; ENSP00000472324 ; ENSG00000142449 .
GeneIDi 84467.
KEGGi hsa:84467.
UCSCi uc002mjf.3. human.

Organism-specific databases

CTDi 84467.
GeneCardsi GC19M008130.
H-InvDB HIX0014707.
HGNCi HGNC:18794. FBN3.
HPAi HPA049482.
MIMi 608529. gene.
neXtProti NX_Q75N90.
PharmGKBi PA38681.
HUGEi Search...
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG12793.
GeneTreei ENSGT00770000120465.
HOGENOMi HOG000231768.
HOVERGENi HBG005643.
InParanoidi Q75N90.
OMAi SCARPFP.
OrthoDBi EOG7RV9F6.
PhylomeDBi Q75N90.
TreeFami TF316849.

Enzyme and pathway databases

Reactomei REACT_118572. Degradation of the extracellular matrix.
REACT_150331. Molecules associated with elastic fibres.
REACT_150366. Elastic fibre formation.

Miscellaneous databases

ChiTaRSi FBN3. human.
GenomeRNAii 84467.
NextBioi 74278.
PROi Q75N90.
SOURCEi Search...

Gene expression databases

Bgeei Q75N90.
CleanExi HS_FBN3.
Genevestigatori Q75N90.

Family and domain databases

Gene3Di 3.90.290.10. 9 hits.
InterProi 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.
IPR011398. FBN/EtMIC4.
IPR009030. Growth_fac_rcpt_N_dom.
IPR017878. TB_dom.
[Graphical view ]
PANTHERi PTHR24039. PTHR24039. 1 hit.
Pfami PF12662. cEGF. 3 hits.
PF00008. EGF. 1 hit.
PF07645. EGF_CA. 38 hits.
PF00683. TB. 9 hits.
[Graphical view ]
PIRSFi PIRSF036312. Fibrillin. 1 hit.
SMARTi SM00181. EGF. 4 hits.
SM00179. EGF_CA. 41 hits.
[Graphical view ]
SUPFAMi SSF57184. SSF57184. 12 hits.
SSF57581. SSF57581. 9 hits.
PROSITEi PS00010. ASX_HYDROXYL. 41 hits.
PS00022. EGF_1. 2 hits.
PS01186. EGF_2. 36 hits.
PS50026. EGF_3. 44 hits.
PS01187. EGF_CA. 40 hits.
PS51364. TB. 9 hits.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Differential expression of fibrillin-3 adds to microfibril variety in human and avian, but not rodent, connective tissues."
    Corson G.M., Charbonneau N.L., Keene D.R., Sakai L.Y.
    Genomics 83:461-472(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, VARIANTS ASN-662; SER-1614 AND ASP-2610.
  2. "Three novel mutations of the fibrillin-1 gene and ten single nucleotide polymorphisms of the fibrillin-3 gene in Marfan syndrome patients."
    Uyeda T., Takahashi T., Eto S., Sato T., Xu G., Kanezaki R., Toki T., Yonesaka S., Ito E.
    J. Hum. Genet. 49:404-407(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS GLN-473; ASN-662; LEU-935; PHE-938; TRP-1083; SER-1614; LYS-1869; PRO-1904 AND ASP-2610.
  3. "Prediction of the coding sequences of unidentified human genes. XX. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro."
    Nagase T., Nakayama M., Nakajima D., Kikuno R., Ohara O.
    DNA Res. 8:85-95(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANTS ASN-662; ILE-1326; GLN-1806 AND ASP-2610.
    Tissue: Brain.
  4. Nakajima D., Nakayama M., Kikuno R., Nagase T., Ohara O.
    Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: SEQUENCE REVISION.
  5. "The DNA sequence and biology of human chromosome 19."
    Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S., Carrano A.V.
    , Caoile C., Chan Y.M., Christensen M., Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E., Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M., Rubin E.M., Lucas S.M.
    Nature 428:529-535(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Entry informationi

Entry nameiFBN3_HUMAN
AccessioniPrimary (citable) accession number: Q75N90
Secondary accession number(s): Q75N91
, Q75N92, Q75N93, Q86SJ5, Q96JP8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 19, 2004
Last sequence update: May 18, 2010
Last modified: November 26, 2014
This is version 110 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 19
    Human chromosome 19: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3