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Protein

Fibrillin-2

Gene

Fbn2

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein 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-2-containing microfibrils regulate the early process of elastic fiber assembly. Regulates osteoblast maturation by controlling TGF-beta bioavailability and calibrating TGF-beta and BMP levels, respectively.1 Publication

GO - Molecular functioni

  • calcium ion binding Source: MGI
  • extracellular matrix structural constituent Source: InterPro

GO - Biological processi

  • bone trabecula formation Source: BHF-UCL
  • camera-type eye development Source: Ensembl
  • embryonic eye morphogenesis Source: Ensembl
  • embryonic limb morphogenesis Source: MGI
  • limb morphogenesis Source: MGI
  • positive regulation of bone mineralization Source: BHF-UCL
  • positive regulation of osteoblast differentiation Source: BHF-UCL
  • sequestering of TGFbeta in extracellular matrix Source: BHF-UCL
Complete GO annotation...

Keywords - Ligandi

Calcium

Enzyme and pathway databases

ReactomeiR-MMU-1474228. Degradation of the extracellular matrix.
R-MMU-1566948. Elastic fibre formation.
R-MMU-2129379. Molecules associated with elastic fibres.

Names & Taxonomyi

Protein namesi
Recommended name:
Fibrillin-2
Gene namesi
Name:Fbn2
Synonyms:Fbn-2
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 18

Organism-specific databases

MGIiMGI:95490. Fbn2.

Subcellular locationi

GO - Cellular componenti

  • extracellular matrix Source: UniProtKB
  • extracellular region Source: MGI
  • microfibril Source: BHF-UCL
Complete GO annotation...

Keywords - Cellular componenti

Extracellular matrix, Secreted

Pathology & Biotechi

Disruption phenotypei

Mice display a low bone mass phenotype that is associated with reduced bone formation.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2828Sequence analysisAdd
BLAST
Chaini29 – 29072879Fibrillin-2PRO_0000007585Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi115 ↔ 124PROSITE-ProRule annotation
Disulfide bondi119 ↔ 130PROSITE-ProRule annotation
Disulfide bondi132 ↔ 141PROSITE-ProRule annotation
Disulfide bondi149 ↔ 159PROSITE-ProRule annotation
Disulfide bondi153 ↔ 164PROSITE-ProRule annotation
Disulfide bondi166 ↔ 175PROSITE-ProRule annotation
Disulfide bondi180 ↔ 190PROSITE-ProRule annotation
Disulfide bondi184 ↔ 196PROSITE-ProRule annotation
Disulfide bondi198 ↔ 207PROSITE-ProRule annotation
Disulfide bondi280 ↔ 292PROSITE-ProRule annotation
Disulfide bondi287 ↔ 301PROSITE-ProRule annotation
Disulfide bondi303 ↔ 316PROSITE-ProRule annotation
Disulfide bondi322 ↔ 334PROSITE-ProRule annotation
Disulfide bondi329 ↔ 343PROSITE-ProRule annotation
Disulfide bondi345 ↔ 358PROSITE-ProRule annotation
Glycosylationi485 – 4851N-linked (GlcNAc...)Sequence analysis
Disulfide bondi491 ↔ 503PROSITE-ProRule annotation
Disulfide bondi498 ↔ 512PROSITE-ProRule annotation
Disulfide bondi514 ↔ 526PROSITE-ProRule annotation
Disulfide bondi532 ↔ 542PROSITE-ProRule annotation
Disulfide bondi537 ↔ 551PROSITE-ProRule annotation
Disulfide bondi553 ↔ 566PROSITE-ProRule annotation
Disulfide bondi572 ↔ 584PROSITE-ProRule annotation
Disulfide bondi579 ↔ 593PROSITE-ProRule annotation
Disulfide bondi595 ↔ 608PROSITE-ProRule annotation
Disulfide bondi614 ↔ 625PROSITE-ProRule annotation
Disulfide bondi620 ↔ 634PROSITE-ProRule annotation
Disulfide bondi636 ↔ 649PROSITE-ProRule annotation
Disulfide bondi655 ↔ 666PROSITE-ProRule annotation
Disulfide bondi661 ↔ 675PROSITE-ProRule annotation
Disulfide bondi677 ↔ 690PROSITE-ProRule annotation
Disulfide bondi765 ↔ 777PROSITE-ProRule annotation
Disulfide bondi772 ↔ 786PROSITE-ProRule annotation
Disulfide bondi788 ↔ 801PROSITE-ProRule annotation
Disulfide bondi807 ↔ 819PROSITE-ProRule annotation
Disulfide bondi814 ↔ 828PROSITE-ProRule annotation
Disulfide bondi830 ↔ 843PROSITE-ProRule annotation
Disulfide bondi849 ↔ 859PROSITE-ProRule annotation
Disulfide bondi854 ↔ 868PROSITE-ProRule annotation
Disulfide bondi870 ↔ 883PROSITE-ProRule annotation
Disulfide bondi952 ↔ 964PROSITE-ProRule annotation
Disulfide bondi959 ↔ 973PROSITE-ProRule annotation
Disulfide bondi975 ↔ 988PROSITE-ProRule annotation
Disulfide bondi1070 ↔ 1082PROSITE-ProRule annotation
Disulfide bondi1077 ↔ 1091PROSITE-ProRule annotation
Disulfide bondi1093 ↔ 1106PROSITE-ProRule annotation
Glycosylationi1105 – 11051N-linked (GlcNAc...)Sequence analysis
Disulfide bondi1112 ↔ 1124PROSITE-ProRule annotation
Disulfide bondi1119 ↔ 1133PROSITE-ProRule annotation
Disulfide bondi1135 ↔ 1149PROSITE-ProRule annotation
Disulfide bondi1155 ↔ 1167PROSITE-ProRule annotation
Disulfide bondi1162 ↔ 1176PROSITE-ProRule annotation
Disulfide bondi1178 ↔ 1191PROSITE-ProRule annotation
Disulfide bondi1197 ↔ 1209PROSITE-ProRule annotation
Disulfide bondi1204 ↔ 1218PROSITE-ProRule annotation
Disulfide bondi1220 ↔ 1233PROSITE-ProRule annotation
Disulfide bondi1239 ↔ 1250PROSITE-ProRule annotation
Disulfide bondi1246 ↔ 1259PROSITE-ProRule annotation
Disulfide bondi1261 ↔ 1274PROSITE-ProRule annotation
Disulfide bondi1280 ↔ 1292PROSITE-ProRule annotation
Disulfide bondi1287 ↔ 1301PROSITE-ProRule annotation
Disulfide bondi1303 ↔ 1316PROSITE-ProRule annotation
Disulfide bondi1322 ↔ 1334PROSITE-ProRule annotation
Disulfide bondi1329 ↔ 1343PROSITE-ProRule annotation
Disulfide bondi1345 ↔ 1358PROSITE-ProRule annotation
Disulfide bondi1364 ↔ 1377PROSITE-ProRule annotation
Disulfide bondi1371 ↔ 1386PROSITE-ProRule annotation
Disulfide bondi1388 ↔ 1399PROSITE-ProRule annotation
Disulfide bondi1405 ↔ 1418PROSITE-ProRule annotation
Glycosylationi1407 – 14071N-linked (GlcNAc...)Sequence analysis
Disulfide bondi1412 ↔ 1427PROSITE-ProRule annotation
Disulfide bondi1429 ↔ 1440PROSITE-ProRule annotation
Disulfide bondi1446 ↔ 1458PROSITE-ProRule annotation
Disulfide bondi1453 ↔ 1467PROSITE-ProRule annotation
Disulfide bondi1469 ↔ 1482PROSITE-ProRule annotation
Disulfide bondi1488 ↔ 1499PROSITE-ProRule annotation
Disulfide bondi1494 ↔ 1508PROSITE-ProRule annotation
Disulfide bondi1510 ↔ 1523PROSITE-ProRule annotation
Glycosylationi1522 – 15221N-linked (GlcNAc...)Sequence analysis
Disulfide bondi1529 ↔ 1540PROSITE-ProRule annotation
Disulfide bondi1535 ↔ 1549PROSITE-ProRule annotation
Disulfide bondi1551 ↔ 1564PROSITE-ProRule annotation
Glycosylationi1558 – 15581N-linked (GlcNAc...)Sequence analysis
Glycosylationi1618 – 16181N-linked (GlcNAc...)Sequence analysis
Disulfide bondi1647 ↔ 1659PROSITE-ProRule annotation
Disulfide bondi1654 ↔ 1668PROSITE-ProRule annotation
Disulfide bondi1670 ↔ 1683PROSITE-ProRule annotation
Disulfide bondi1689 ↔ 1701PROSITE-ProRule annotation
Disulfide bondi1696 ↔ 1710PROSITE-ProRule annotation
Glycosylationi1707 – 17071N-linked (GlcNAc...)Sequence analysis
Disulfide bondi1712 ↔ 1725PROSITE-ProRule annotation
Glycosylationi1738 – 17381N-linked (GlcNAc...)Sequence analysis
Glycosylationi1749 – 17491N-linked (GlcNAc...)Sequence analysis
Disulfide bondi1805 ↔ 1817PROSITE-ProRule annotation
Disulfide bondi1812 ↔ 1826PROSITE-ProRule annotation
Disulfide bondi1828 ↔ 1841PROSITE-ProRule annotation
Disulfide bondi1847 ↔ 1860PROSITE-ProRule annotation
Disulfide bondi1854 ↔ 1869PROSITE-ProRule annotation
Disulfide bondi1871 ↔ 1883PROSITE-ProRule annotation
Disulfide bondi1889 ↔ 1901PROSITE-ProRule annotation
Disulfide bondi1896 ↔ 1910PROSITE-ProRule annotation
Disulfide bondi1912 ↔ 1925PROSITE-ProRule annotation
Disulfide bondi1931 ↔ 1941PROSITE-ProRule annotation
Disulfide bondi1936 ↔ 1950PROSITE-ProRule annotation
Glycosylationi1938 – 19381N-linked (GlcNAc...)Sequence analysis
Disulfide bondi1952 ↔ 1964PROSITE-ProRule annotation
Disulfide bondi1970 ↔ 1983PROSITE-ProRule annotation
Disulfide bondi1978 ↔ 1992PROSITE-ProRule annotation
Disulfide bondi1994 ↔ 2007PROSITE-ProRule annotation
Disulfide bondi2013 ↔ 2025PROSITE-ProRule annotation
Disulfide bondi2020 ↔ 2034PROSITE-ProRule annotation
Disulfide bondi2036 ↔ 2047PROSITE-ProRule annotation
Disulfide bondi2053 ↔ 2065PROSITE-ProRule annotation
Disulfide bondi2060 ↔ 2074PROSITE-ProRule annotation
Disulfide bondi2076 ↔ 2089PROSITE-ProRule annotation
Glycosylationi2113 – 21131N-linked (GlcNAc...)Sequence analysis
Disulfide bondi2168 ↔ 2180PROSITE-ProRule annotation
Disulfide bondi2175 ↔ 2189PROSITE-ProRule annotation
Disulfide bondi2191 ↔ 2204PROSITE-ProRule annotation
Disulfide bondi2210 ↔ 2221PROSITE-ProRule annotation
Disulfide bondi2216 ↔ 2230PROSITE-ProRule annotation
Glycosylationi2218 – 22181N-linked (GlcNAc...)Sequence analysis
Disulfide bondi2232 ↔ 2244PROSITE-ProRule annotation
Disulfide bondi2250 ↔ 2261PROSITE-ProRule annotation
Disulfide bondi2257 ↔ 2270PROSITE-ProRule annotation
Disulfide bondi2272 ↔ 2285PROSITE-ProRule annotation
Disulfide bondi2291 ↔ 2305PROSITE-ProRule annotation
Disulfide bondi2298 ↔ 2314PROSITE-ProRule annotation
Disulfide bondi2316 ↔ 2329PROSITE-ProRule annotation
Disulfide bondi2335 ↔ 2347PROSITE-ProRule annotation
Disulfide bondi2342 ↔ 2356PROSITE-ProRule annotation
Disulfide bondi2358 ↔ 2371PROSITE-ProRule annotation
Disulfide bondi2446 ↔ 2458PROSITE-ProRule annotation
Disulfide bondi2453 ↔ 2467PROSITE-ProRule annotation
Disulfide bondi2469 ↔ 2482PROSITE-ProRule annotation
Disulfide bondi2488 ↔ 2499PROSITE-ProRule annotation
Disulfide bondi2495 ↔ 2508PROSITE-ProRule annotation
Disulfide bondi2510 ↔ 2523PROSITE-ProRule annotation
Disulfide bondi2529 ↔ 2540PROSITE-ProRule annotation
Disulfide bondi2536 ↔ 2549PROSITE-ProRule annotation
Disulfide bondi2551 ↔ 2562PROSITE-ProRule annotation
Disulfide bondi2568 ↔ 2581PROSITE-ProRule annotation
Disulfide bondi2575 ↔ 2590PROSITE-ProRule annotation
Disulfide bondi2592 ↔ 2605PROSITE-ProRule annotation
Disulfide bondi2611 ↔ 2621PROSITE-ProRule annotation
Disulfide bondi2617 ↔ 2630PROSITE-ProRule annotation
Disulfide bondi2632 ↔ 2645PROSITE-ProRule annotation
Disulfide bondi2651 ↔ 2662PROSITE-ProRule annotation
Disulfide bondi2657 ↔ 2671PROSITE-ProRule annotation
Disulfide bondi2673 ↔ 2686PROSITE-ProRule annotation
Disulfide bondi2692 ↔ 2703PROSITE-ProRule annotation
Disulfide bondi2699 ↔ 2712PROSITE-ProRule annotation
Disulfide bondi2714 ↔ 2726PROSITE-ProRule annotation
Glycosylationi2803 – 28031N-linked (GlcNAc...)Sequence analysis

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

MaxQBiQ61555.
PaxDbiQ61555.
PRIDEiQ61555.

PTM databases

PhosphoSiteiQ61555.

Expressioni

Gene expression databases

BgeeiQ61555.
CleanExiMM_FBN2.
GenevisibleiQ61555. MM.

Interactioni

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000025497.

Structurei

3D structure databases

ProteinModelPortaliQ61555.
SMRiQ61555. Positions 75-208, 845-989, 1107-1192, 1524-1684, 2164-2245.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini111 – 14232EGF-like 1PROSITE-ProRule annotationAdd
BLAST
Domaini145 – 17632EGF-like 2PROSITE-ProRule annotationAdd
BLAST
Domaini176 – 20833EGF-like 3PROSITE-ProRule annotationAdd
BLAST
Domaini214 – 26653TB 1Add
BLAST
Domaini276 – 31742EGF-like 4; calcium-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini318 – 35942EGF-like 5; calcium-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini364 – 41754TB 2Add
BLAST
Domaini487 – 52741EGF-like 6PROSITE-ProRule annotationAdd
BLAST
Domaini528 – 56740EGF-like 7; calcium-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini568 – 60942EGF-like 8; calcium-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini610 – 65041EGF-like 9; calcium-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini651 – 69141EGF-like 10; calcium-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini697 – 74953TB 3Add
BLAST
Domaini761 – 80242EGF-like 11; calcium-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini803 – 84442EGF-like 12; calcium-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini845 – 88339EGF-like 13; calcium-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini889 – 94052TB 4Add
BLAST
Domaini948 – 98942EGF-like 14; calcium-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini994 – 104552TB 5Add
BLAST
Domaini1066 – 110742EGF-like 15; calcium-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini1108 – 115043EGF-like 16; calcium-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini1151 – 119242EGF-like 17; calcium-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini1193 – 123442EGF-like 18; calcium-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini1235 – 127541EGF-like 19; calcium-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini1276 – 131742EGF-like 20; calcium-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini1318 – 135942EGF-like 21; calcium-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini1360 – 140041EGF-like 22; calcium-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini1401 – 144141EGF-like 23; calcium-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini1442 – 148342EGF-like 24; calcium-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini1484 – 152441EGF-like 25; calcium-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini1525 – 156541EGF-like 26; calcium-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini1570 – 162657TB 6Add
BLAST
Domaini1643 – 168442EGF-like 27; calcium-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini1685 – 172642EGF-like 28; calcium-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini1731 – 178454TB 7Add
BLAST
Domaini1801 – 184242EGF-like 29; calcium-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini1843 – 188442EGF-like 30; calcium-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini1885 – 192642EGF-like 31; calcium-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini1927 – 196539EGF-like 32; calcium-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini1966 – 200843EGF-like 33; calcium-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini2009 – 204840EGF-like 34; calcium-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini2049 – 209042EGF-like 35; calcium-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini2095 – 214854TB 8Add
BLAST
Domaini2164 – 220542EGF-like 36; calcium-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini2206 – 224540EGF-like 37; calcium-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini2246 – 228641EGF-like 38; calcium-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini2287 – 233044EGF-like 39; calcium-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini2331 – 237242EGF-like 40; calcium-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini2377 – 243054TB 9Add
BLAST
Domaini2442 – 248342EGF-like 41; calcium-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini2484 – 252441EGF-like 42; calcium-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini2525 – 256339EGF-like 43; calcium-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini2564 – 260643EGF-like 44; calcium-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini2607 – 264640EGF-like 45; calcium-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini2647 – 268741EGF-like 46; calcium-bindingPROSITE-ProRule annotationAdd
BLAST
Domaini2688 – 272740EGF-like 47; calcium-bindingPROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the fibrillin family.Curated
Contains 47 EGF-like domains.PROSITE-ProRule annotation
Contains 9 TB (TGF-beta binding) domains.Curated

Keywords - Domaini

EGF-like domain, Repeat, Signal

Phylogenomic databases

eggNOGiENOG410IR7H. Eukaryota.
ENOG410XSTY. LUCA.
GeneTreeiENSGT00760000118806.
HOGENOMiHOG000231768.
HOVERGENiHBG005643.
InParanoidiQ61555.
OMAiSGRNCID.
OrthoDBiEOG7RV9F6.
TreeFamiTF316849.

Family and domain databases

Gene3Di3.90.290.10. 9 hits.
InterProiIPR026823. cEGF.
IPR001881. EGF-like_Ca-bd_dom.
IPR013032. EGF-like_CS.
IPR000742. EGF-like_dom.
IPR000152. EGF-type_Asp/Asn_hydroxyl_site.
IPR018097. EGF_Ca-bd_CS.
IPR011398. FBN.
IPR009030. Growth_fac_rcpt_.
IPR017878. TB_dom.
[Graphical view]
PANTHERiPTHR24039. PTHR24039. 1 hit.
PfamiPF12662. cEGF. 2 hits.
PF07645. EGF_CA. 39 hits.
PF00683. TB. 9 hits.
[Graphical view]
PIRSFiPIRSF036312. Fibrillin. 1 hit.
SMARTiSM00181. EGF. 46 hits.
SM00179. EGF_CA. 44 hits.
[Graphical view]
SUPFAMiSSF57184. SSF57184. 13 hits.
SSF57581. SSF57581. 9 hits.
PROSITEiPS00010. ASX_HYDROXYL. 43 hits.
PS00022. EGF_1. 2 hits.
PS01186. EGF_2. 37 hits.
PS50026. EGF_3. 45 hits.
PS01187. EGF_CA. 43 hits.
PS51364. TB. 9 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

Q61555-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGRRRRLCLQ PYFVWLGCVA LWAQGTDGQP QPPPPKTLRP QPPPQQVRPA
60 70 80 90 100
VAGSEGGFMG PEYRDEGAVA ASRVRRRGQQ EILRGPNVCG SRFHSYCCPG
110 120 130 140 150
WKTLPGGNQC IVPICRNSCG DGFCSRPNMC TCSSGQISPT CGAKSIQQCS
160 170 180 190 200
VRCMNGGTCA DDHCQCQKGY IGTYCGQPVC ENGCQNGGRC IGPNRCACVY
210 220 230 240 250
GFTGPQCERD YRTGPCFTQV NNQMCQGQLT GIVCTKTLCC ATIGRAWGHP
260 270 280 290 300
CEMCPAQPQP CRRGFIPNIR TGACQDVDEC QAIPGLCQGG NCINTVGSFE
310 320 330 340 350
CRCPAGHKQS ETTQKCEDID ECSVIPGVCE TGDCSNTVGS YFCLCPRGFV
360 370 380 390 400
TSTDGSRCID QRAGTCFSGL VNGRCAQELP GRMAKAQCCC EPGRCWSIGT
410 420 430 440 450
IPEACPVRGS EEYRRLCLDG LPMGGIPGSS VSRPGGTGST GNGYGPGGTG
460 470 480 490 500
FLPIPGDNGF SPGVGGAGVG AGGQGPIITG LTILNQTIDI CKHHANLCLN
510 520 530 540 550
GRCIPTVSSY RCECNMGYKQ DANGDCIDVD ECTSNPCSNG DCVNTPGSYY
560 570 580 590 600
CKCHAGFQRT PTKQACIDID ECIQNGVLCK NGRCVNTDGS FQCICNAGFE
610 620 630 640 650
LTTDGKNCVD HDECTTTNMC LNGMCINEDG SFKCVCKPGF ILAPNGRYCT
660 670 680 690 700
DVDECQTPGI CMNGHCINNE GSFRCDCPPG LAVGVDGRVC VDTHMRSTCY
710 720 730 740 750
GEIKKGVCVR PFPGAVTKSE CCCANPDYGF GEPCQPCPAK NSAEFHGLCS
760 770 780 790 800
SGIGITVDGR DINECALDPD ICANGICENL RGSYRCNCNS GYEPDASGRN
810 820 830 840 850
CIDIDECLVN RLLCDNGLCR NTPGSYSCTC PPGYVFRTET ETCEDVNECE
860 870 880 890 900
SNPCVNGACR NNLGSFHCEC SPGSKLSSTG LICIDSLKGT CWLNIQDNRC
910 920 930 940 950
EVNINGATLK SECCATLGAA WGSPCERCEL DAACPRGFAR IKGVTCEDVN
960 970 980 990 1000
ECEVFPGVCP NGRCVNSKGS FHCECPEGLT LDGTGRVCLD IRMEHCFLKW
1010 1020 1030 1040 1050
DEDECIHPVP GKFRMDACCC AVGAAWGTEC EECPKPGTKE YETLCPRGPG
1060 1070 1080 1090 1100
FANRGDILTG RPFYKDINEC KAFPGMCTYG KCRNTIGSFK CRCNNGFALD
1110 1120 1130 1140 1150
MEERNCTDID ECRISPDLCG SGICVNTPGS FECECFEGYE SGFMMMKNCM
1160 1170 1180 1190 1200
DIDECERNPL LCRGGTCVNT EGSFQCDCPL GHELSPSRED CVDINECSLS
1210 1220 1230 1240 1250
DNLCRNGKCV NMIGTYQCSC NPGYQATPDR QGCTDIDECM IMNGGCDTQC
1260 1270 1280 1290 1300
TNSEGSYECS CSEGYALMPD GRSCADIDEC ENNPDICDGG QCTNIPGEYR
1310 1320 1330 1340 1350
CLCYDGFMAS MDMKTCIDVN ECDLNPNICM FGECENTKGS FICHCQLGYS
1360 1370 1380 1390 1400
VKKGTTGCTD VDECEIGAHN CDMHASCLNV PGSFKCSCRE GWVGNGIKCI
1410 1420 1430 1440 1450
DLDECANGTH QCSINAQCVN TPGSYRCACS EGFTGDGFTC SDVDECAENT
1460 1470 1480 1490 1500
NLCENGQCLN VPGAYRCECE MGFTPASDSR SCQDIDECSF QNICVFGTCN
1510 1520 1530 1540 1550
NLPGMFHCIC DDGYELDRTG GNCTDIDECA DPINCVNGLC VNTPGRYECN
1560 1570 1580 1590 1600
CPPDFQLNPT GVGCVDNRVG NCYLKFGPRG DGSLSCNTEV GVGVSRSSCC
1610 1620 1630 1640 1650
CSLGKAWGNP CETCPPVNST EYYTLCPGGE GFRPNPITII LEDIDECQEL
1660 1670 1680 1690 1700
PGLCQGGNCI NTFGSFQCEC PQGYYLSEET RICEDIDECF AHPGVCGPGT
1710 1720 1730 1740 1750
CYNTLGNYTC ICPPEYMQVN GGHNCMDMRK SFCYRSYNGT TCENELPFNV
1760 1770 1780 1790 1800
TKRMCCCTYN VGKAWNKPCE PCPTPGTADF KTICGNIPGF TFDIHTGKAV
1810 1820 1830 1840 1850
DIDECKEIPG ICANGVCINQ IGSFRCECPT GFSYNDLLLV CEDIDECSNG
1860 1870 1880 1890 1900
DNLCQRNADC INSPGSYRCE CAAGFKLSPN GACVDRNECL EIPNVCSHGL
1910 1920 1930 1940 1950
CVDLQGSYQC ICNNGFKASQ DQTMCMDVDE CERHPCGNGT CKNTVGSYNC
1960 1970 1980 1990 2000
LCYPGFELTH NNDCLDIDEC SSFFGQVCRN GRCFNEIGSF KCLCNEGYEL
2010 2020 2030 2040 2050
TPDGKNCIDT NECVALPGSC SPGTCQNLEG SFRCICPPGY EVRSENCIDI
2060 2070 2080 2090 2100
NECDEDPNIC LFGSCTNTPG GFQCICPPGF VLSDNGRRCF DTRQSFCFTN
2110 2120 2130 2140 2150
FENGKCSVPK AFNTTKAKCC CSKMPGEGWG DPCELCPKDD EVAFQDLCPY
2160 2170 2180 2190 2200
GHGTVPSLHD TREDVNECLE SPGICSNGQC INTDGSFRCE CPMGYNLDYT
2210 2220 2230 2240 2250
GVRCVDTDEC SIGNPCGNGT CTNVIGSFEC TCNEGFEPGP MMNCEDINEC
2260 2270 2280 2290 2300
AQNPLLCAFR CMNTFGSYEC TCPVGYALRE DQKMCKDLDE CAEGLHDCES
2310 2320 2330 2340 2350
RGMMCKNLIG TFMCICPPGM ARRPDGEGCV DENECRTKPG ICENGRCVNI
2360 2370 2380 2390 2400
IGSYRCECNE GFQSSSSGTE CLDNRQGLCF AEVLQTMCQM ASSSRNLVTK
2410 2420 2430 2440 2450
SECCCDGGRG WGHQCELCPL PGTAQYKKIC PHGPGYATDG RDIDECKVMP
2460 2470 2480 2490 2500
SLCTNGQCVN TMGSFRCFCK VGYTTDISGT ACVDLDECSQ SPKPCNFICK
2510 2520 2530 2540 2550
NTKGSYQCSC PRGYVLQEDG KTCKDLDECQ TKQHNCQFLC VNTLGGFTCK
2560 2570 2580 2590 2600
CPPGFTQHHT ACIDNNECGS QPSLCGAKGI CQNTPGSFSC ECQRGFSLDA
2610 2620 2630 2640 2650
SGLNCEDVDE CDGNHRCQHG CQNILGGYRC GCPQGYVQHY QWNQCVDENE
2660 2670 2680 2690 2700
CSNPGACGSA SCYNTLGSYK CACPSGFSFD QFSSACHDVN ECSSSKNPCS
2710 2720 2730 2740 2750
YGCSNTEGGY LCGCPPGYFR VGQGHCVSGM GFNKGQYLSV DAEAEDDENA
2760 2770 2780 2790 2800
LSPEACYECK INGYTKKDGR RKRSAQEPEP ASAEEQISLE SVAMDSPVNM
2810 2820 2830 2840 2850
KFNLSGLGSK EHILELVPAI EPLNNHIRYV ISQGNEDGVF RIHQRNGLSY
2860 2870 2880 2890 2900
LHTAKKKLAP GTYTLEITSI PLYGKKELRK LEEHNEDDYL LGVLGEALRM

RLQIQLY
Length:2,907
Mass (Da):313,818
Last modified:July 27, 2011 - v2
Checksum:i57FCD5188B1D63FF
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti39 – 391R → W in AAA74908 (PubMed:7744963).Curated
Sequence conflicti70 – 701A → R in AAA74908 (PubMed:7744963).Curated
Sequence conflicti143 – 1431A → R in AAA74908 (PubMed:7744963).Curated
Sequence conflicti263 – 2631R → P in AAA74908 (PubMed:7744963).Curated
Sequence conflicti263 – 2631R → P in AAC60685 (PubMed:8307578).Curated
Sequence conflicti440 – 4401T → N in AAA74908 (PubMed:7744963).Curated
Sequence conflicti513 – 5131E → R in AAA74908 (PubMed:7744963).Curated
Sequence conflicti587 – 5871T → S in AAA74908 (PubMed:7744963).Curated
Sequence conflicti783 – 7831S → T in AAA74908 (PubMed:7744963).Curated
Sequence conflicti836 – 8372FR → LP in AAA74908 (PubMed:7744963).Curated
Sequence conflicti919 – 9191A → G in AAA74908 (PubMed:7744963).Curated
Sequence conflicti1064 – 10641Y → C in AAA74908 (PubMed:7744963).Curated
Sequence conflicti1559 – 15591P → A in AAA74908 (PubMed:7744963).Curated
Sequence conflicti1590 – 15901V → A in AAA74908 (PubMed:7744963).Curated
Sequence conflicti1622 – 16221Y → H in AAA74908 (PubMed:7744963).Curated
Sequence conflicti1765 – 17651W → G in AAA74908 (PubMed:7744963).Curated
Sequence conflicti1937 – 19371G → A in AAA74908 (PubMed:7744963).Curated
Sequence conflicti2227 – 22271S → C in AAA74908 (PubMed:7744963).Curated
Sequence conflicti2277 – 22771A → G in AAA74908 (PubMed:7744963).Curated
Sequence conflicti2475 – 24751T → M in AAA74908 (PubMed:7744963).Curated
Sequence conflicti2634 – 26363QGY → HGD in AAA74908 (PubMed:7744963).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L39790 Genomic DNA. Translation: AAA74908.1.
AC102317 Genomic DNA. No translation available.
AC127358 Genomic DNA. No translation available.
S69359 Unassigned DNA. Translation: AAC60685.1.
CCDSiCCDS37827.1.
PIRiA57278.
RefSeqiNP_034311.2. NM_010181.2.
XP_006544558.1. XM_006544495.2.
UniGeneiMm.20271.

Genome annotation databases

EnsembliENSMUST00000025497; ENSMUSP00000025497; ENSMUSG00000024598.
GeneIDi102642295.
14119.
KEGGimmu:102642295.
mmu:14119.
UCSCiuc008ezn.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L39790 Genomic DNA. Translation: AAA74908.1.
AC102317 Genomic DNA. No translation available.
AC127358 Genomic DNA. No translation available.
S69359 Unassigned DNA. Translation: AAC60685.1.
CCDSiCCDS37827.1.
PIRiA57278.
RefSeqiNP_034311.2. NM_010181.2.
XP_006544558.1. XM_006544495.2.
UniGeneiMm.20271.

3D structure databases

ProteinModelPortaliQ61555.
SMRiQ61555. Positions 75-208, 845-989, 1107-1192, 1524-1684, 2164-2245.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000025497.

PTM databases

PhosphoSiteiQ61555.

Proteomic databases

MaxQBiQ61555.
PaxDbiQ61555.
PRIDEiQ61555.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000025497; ENSMUSP00000025497; ENSMUSG00000024598.
GeneIDi102642295.
14119.
KEGGimmu:102642295.
mmu:14119.
UCSCiuc008ezn.1. mouse.

Organism-specific databases

CTDi2201.
MGIiMGI:95490. Fbn2.

Phylogenomic databases

eggNOGiENOG410IR7H. Eukaryota.
ENOG410XSTY. LUCA.
GeneTreeiENSGT00760000118806.
HOGENOMiHOG000231768.
HOVERGENiHBG005643.
InParanoidiQ61555.
OMAiSGRNCID.
OrthoDBiEOG7RV9F6.
TreeFamiTF316849.

Enzyme and pathway databases

ReactomeiR-MMU-1474228. Degradation of the extracellular matrix.
R-MMU-1566948. Elastic fibre formation.
R-MMU-2129379. Molecules associated with elastic fibres.

Miscellaneous databases

ChiTaRSiFbn2. mouse.
PROiQ61555.
SOURCEiSearch...

Gene expression databases

BgeeiQ61555.
CleanExiMM_FBN2.
GenevisibleiQ61555. MM.

Family and domain databases

Gene3Di3.90.290.10. 9 hits.
InterProiIPR026823. cEGF.
IPR001881. EGF-like_Ca-bd_dom.
IPR013032. EGF-like_CS.
IPR000742. EGF-like_dom.
IPR000152. EGF-type_Asp/Asn_hydroxyl_site.
IPR018097. EGF_Ca-bd_CS.
IPR011398. FBN.
IPR009030. Growth_fac_rcpt_.
IPR017878. TB_dom.
[Graphical view]
PANTHERiPTHR24039. PTHR24039. 1 hit.
PfamiPF12662. cEGF. 2 hits.
PF07645. EGF_CA. 39 hits.
PF00683. TB. 9 hits.
[Graphical view]
PIRSFiPIRSF036312. Fibrillin. 1 hit.
SMARTiSM00181. EGF. 46 hits.
SM00179. EGF_CA. 44 hits.
[Graphical view]
SUPFAMiSSF57184. SSF57184. 13 hits.
SSF57581. SSF57581. 9 hits.
PROSITEiPS00010. ASX_HYDROXYL. 43 hits.
PS00022. EGF_1. 2 hits.
PS01186. EGF_2. 37 hits.
PS50026. EGF_3. 45 hits.
PS01187. EGF_CA. 43 hits.
PS51364. TB. 9 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Developmental expression of fibrillin genes suggests heterogeneity of extracellular microfibrils."
    Zhang H., Hu W., Ramirez F.
    J. Cell Biol. 129:1165-1176(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6J.
  3. "Fibrillin genes map to regions of conserved mouse/human synteny on mouse chromosomes 2 and 18."
    Li X., Pereira L., Zhang H., Sanguineti C., Ramirez F., Bonadio J., Francke U.
    Genomics 18:667-672(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 210-317.
  4. Lubec G., Sunyer B., Chen W.-Q.
    Submitted (JAN-2009) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 2429-2441, IDENTIFICATION BY MASS SPECTROMETRY.
    Strain: OF1.
    Tissue: Hippocampus.
  5. "Fibrillin-1 and -2 differentially modulate endogenous TGF-{beta} and BMP bioavailability during bone formation."
    Nistala H., Lee-Arteaga S., Smaldone S., Siciliano G., Carta L., Ono R.N., Sengle G., Arteaga-Solis E., Levasseur R., Ducy P., Sakai L.Y., Karsenty G., Ramirez F.
    J. Cell Biol. 190:1107-1121(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, DISRUPTION PHENOTYPE.

Entry informationi

Entry nameiFBN2_MOUSE
AccessioniPrimary (citable) accession number: Q61555
Secondary accession number(s): E9QJZ4, Q63957
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 15, 1998
Last sequence update: July 27, 2011
Last modified: June 8, 2016
This is version 145 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.