Q61555 (FBN2_MOUSE) Reviewed, UniProtKB/Swiss-Prot
Last modified
May 29, 2013.
Version 118.
History...
Clusters with 
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | Recommended name: Fibrillin-2 | ||||
| Gene names |
| ||||
| Organism | Mus musculus (Mouse) [Reference proteome] | ||||
| Taxonomic identifier | 10090 [NCBI] | ||||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus |
Protein attributes
| Sequence length | 2907 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is further processed into a mature form. |
| Protein existence | Evidence at protein level |
General annotation (Comments)
| Function | 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. Ref.5 |
| Subcellular location | |
| Disruption phenotype | Mice display a low bone mass phenotype that is associated with reduced bone formation. Ref.5 |
| Sequence similarities | Belongs to the fibrillin family. Contains 47 EGF-like domains. Contains 9 TB (TGF-beta binding) domains. |
Ontologies
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||||
Molecule processing | |||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|
| Signal peptide | 1 – 28 | 28 | Potential | ||||||||
| Chain | 29 – 2907 | 2879 | Fibrillin-2 | PRO_0000007585 | |||||||
Regions | |||||||||||
| Domain | 111 – 142 | 32 | EGF-like 1 | ||||||||
| Domain | 145 – 176 | 32 | EGF-like 2 | ||||||||
| Domain | 176 – 208 | 33 | EGF-like 3 | ||||||||
| Domain | 214 – 266 | 53 | TB 1 | ||||||||
| Domain | 276 – 317 | 42 | EGF-like 4; calcium-binding | ||||||||
| Domain | 318 – 359 | 42 | EGF-like 5; calcium-binding | ||||||||
| Domain | 364 – 417 | 54 | TB 2 | ||||||||
| Domain | 487 – 527 | 41 | EGF-like 6 | ||||||||
| Domain | 528 – 567 | 40 | EGF-like 7; calcium-binding | ||||||||
| Domain | 568 – 609 | 42 | EGF-like 8; calcium-binding | ||||||||
| Domain | 610 – 650 | 41 | EGF-like 9; calcium-binding | ||||||||
| Domain | 651 – 691 | 41 | EGF-like 10; calcium-binding | ||||||||
| Domain | 697 – 749 | 53 | TB 3 | ||||||||
| Domain | 761 – 802 | 42 | EGF-like 11; calcium-binding | ||||||||
| Domain | 803 – 844 | 42 | EGF-like 12; calcium-binding | ||||||||
| Domain | 845 – 883 | 39 | EGF-like 13; calcium-binding | ||||||||
| Domain | 889 – 940 | 52 | TB 4 | ||||||||
| Domain | 948 – 989 | 42 | EGF-like 14; calcium-binding | ||||||||
| Domain | 994 – 1045 | 52 | TB 5 | ||||||||
| Domain | 1066 – 1107 | 42 | EGF-like 15; calcium-binding | ||||||||
| Domain | 1108 – 1150 | 43 | EGF-like 16; calcium-binding | ||||||||
| Domain | 1151 – 1192 | 42 | EGF-like 17; calcium-binding | ||||||||
| Domain | 1193 – 1234 | 42 | EGF-like 18; calcium-binding | ||||||||
| Domain | 1235 – 1275 | 41 | EGF-like 19; calcium-binding | ||||||||
| Domain | 1276 – 1317 | 42 | EGF-like 20; calcium-binding | ||||||||
| Domain | 1318 – 1359 | 42 | EGF-like 21; calcium-binding | ||||||||
| Domain | 1360 – 1400 | 41 | EGF-like 22; calcium-binding | ||||||||
| Domain | 1401 – 1441 | 41 | EGF-like 23; calcium-binding | ||||||||
| Domain | 1442 – 1483 | 42 | EGF-like 24; calcium-binding | ||||||||
| Domain | 1484 – 1524 | 41 | EGF-like 25; calcium-binding | ||||||||
| Domain | 1525 – 1565 | 41 | EGF-like 26; calcium-binding | ||||||||
| Domain | 1570 – 1626 | 57 | TB 6 | ||||||||
| Domain | 1643 – 1684 | 42 | EGF-like 27; calcium-binding | ||||||||
| Domain | 1685 – 1726 | 42 | EGF-like 28; calcium-binding | ||||||||
| Domain | 1731 – 1784 | 54 | TB 7 | ||||||||
| Domain | 1801 – 1842 | 42 | EGF-like 29; calcium-binding | ||||||||
| Domain | 1843 – 1884 | 42 | EGF-like 30; calcium-binding | ||||||||
| Domain | 1885 – 1926 | 42 | EGF-like 31; calcium-binding | ||||||||
| Domain | 1927 – 1965 | 39 | EGF-like 32; calcium-binding | ||||||||
| Domain | 1966 – 2008 | 43 | EGF-like 33; calcium-binding | ||||||||
| Domain | 2009 – 2048 | 40 | EGF-like 34; calcium-binding | ||||||||
| Domain | 2049 – 2090 | 42 | EGF-like 35; calcium-binding | ||||||||
| Domain | 2095 – 2148 | 54 | TB 8 | ||||||||
| Domain | 2164 – 2205 | 42 | EGF-like 36; calcium-binding | ||||||||
| Domain | 2206 – 2245 | 40 | EGF-like 37; calcium-binding | ||||||||
| Domain | 2246 – 2286 | 41 | EGF-like 38; calcium-binding | ||||||||
| Domain | 2287 – 2330 | 44 | EGF-like 39; calcium-binding | ||||||||
| Domain | 2331 – 2372 | 42 | EGF-like 40; calcium-binding | ||||||||
| Domain | 2377 – 2430 | 54 | TB 9 | ||||||||
| Domain | 2442 – 2483 | 42 | EGF-like 41; calcium-binding | ||||||||
| Domain | 2484 – 2524 | 41 | EGF-like 42; calcium-binding | ||||||||
| Domain | 2525 – 2563 | 39 | EGF-like 43; calcium-binding | ||||||||
| Domain | 2564 – 2606 | 43 | EGF-like 44; calcium-binding | ||||||||
| Domain | 2607 – 2646 | 40 | EGF-like 45; calcium-binding | ||||||||
| Domain | 2647 – 2687 | 41 | EGF-like 46; calcium-binding | ||||||||
| Domain | 2688 – 2727 | 40 | EGF-like 47; calcium-binding | ||||||||
Amino acid modifications | |||||||||||
| Glycosylation | 485 | 1 | N-linked (GlcNAc...) Potential | ||||||||
| Glycosylation | 1105 | 1 | N-linked (GlcNAc...) Potential | ||||||||
| Glycosylation | 1407 | 1 | N-linked (GlcNAc...) Potential | ||||||||
| Glycosylation | 1522 | 1 | N-linked (GlcNAc...) Potential | ||||||||
| Glycosylation | 1558 | 1 | N-linked (GlcNAc...) Potential | ||||||||
| Glycosylation | 1618 | 1 | N-linked (GlcNAc...) Potential | ||||||||
| Glycosylation | 1707 | 1 | N-linked (GlcNAc...) Potential | ||||||||
| Glycosylation | 1738 | 1 | N-linked (GlcNAc...) Potential | ||||||||
| Glycosylation | 1749 | 1 | N-linked (GlcNAc...) Potential | ||||||||
| Glycosylation | 1938 | 1 | N-linked (GlcNAc...) Potential | ||||||||
| Glycosylation | 2113 | 1 | N-linked (GlcNAc...) Potential | ||||||||
| Glycosylation | 2218 | 1 | N-linked (GlcNAc...) Potential | ||||||||
| Glycosylation | 2803 | 1 | N-linked (GlcNAc...) Potential | ||||||||
| Disulfide bond | 115 ↔ 124 | By similarity | |||||||||
| Disulfide bond | 119 ↔ 130 | By similarity | |||||||||
| Disulfide bond | 132 ↔ 141 | By similarity | |||||||||
| Disulfide bond | 149 ↔ 159 | By similarity | |||||||||
| Disulfide bond | 153 ↔ 164 | By similarity | |||||||||
| Disulfide bond | 166 ↔ 175 | By similarity | |||||||||
| Disulfide bond | 180 ↔ 190 | By similarity | |||||||||
| Disulfide bond | 184 ↔ 196 | By similarity | |||||||||
| Disulfide bond | 198 ↔ 207 | By similarity | |||||||||
| Disulfide bond | 280 ↔ 292 | By similarity | |||||||||
| Disulfide bond | 287 ↔ 301 | By similarity | |||||||||
| Disulfide bond | 303 ↔ 316 | By similarity | |||||||||
| Disulfide bond | 322 ↔ 334 | By similarity | |||||||||
| Disulfide bond | 329 ↔ 343 | By similarity | |||||||||
| Disulfide bond | 345 ↔ 358 | By similarity | |||||||||
| Disulfide bond | 491 ↔ 503 | By similarity | |||||||||
| Disulfide bond | 498 ↔ 512 | By similarity | |||||||||
| Disulfide bond | 514 ↔ 526 | By similarity | |||||||||
| Disulfide bond | 532 ↔ 542 | By similarity | |||||||||
| Disulfide bond | 537 ↔ 551 | By similarity | |||||||||
| Disulfide bond | 553 ↔ 566 | By similarity | |||||||||
| Disulfide bond | 572 ↔ 584 | By similarity | |||||||||
| Disulfide bond | 579 ↔ 593 | By similarity | |||||||||
| Disulfide bond | 595 ↔ 608 | By similarity | |||||||||
| Disulfide bond | 614 ↔ 625 | By similarity | |||||||||
| Disulfide bond | 620 ↔ 634 | By similarity | |||||||||
| Disulfide bond | 636 ↔ 649 | By similarity | |||||||||
| Disulfide bond | 655 ↔ 666 | By similarity | |||||||||
| Disulfide bond | 661 ↔ 675 | By similarity | |||||||||
| Disulfide bond | 677 ↔ 690 | By similarity | |||||||||
| Disulfide bond | 765 ↔ 777 | By similarity | |||||||||
| Disulfide bond | 772 ↔ 786 | By similarity | |||||||||
| Disulfide bond | 788 ↔ 801 | By similarity | |||||||||
| Disulfide bond | 807 ↔ 819 | By similarity | |||||||||
| Disulfide bond | 814 ↔ 828 | By similarity | |||||||||
| Disulfide bond | 830 ↔ 843 | By similarity | |||||||||
| Disulfide bond | 849 ↔ 859 | By similarity | |||||||||
| Disulfide bond | 854 ↔ 868 | By similarity | |||||||||
| Disulfide bond | 870 ↔ 883 | By similarity | |||||||||
| Disulfide bond | 952 ↔ 964 | By similarity | |||||||||
| Disulfide bond | 959 ↔ 973 | By similarity | |||||||||
| Disulfide bond | 975 ↔ 988 | By similarity | |||||||||
| Disulfide bond | 1070 ↔ 1082 | By similarity | |||||||||
| Disulfide bond | 1077 ↔ 1091 | By similarity | |||||||||
| Disulfide bond | 1093 ↔ 1106 | By similarity | |||||||||
| Disulfide bond | 1112 ↔ 1124 | By similarity | |||||||||
| Disulfide bond | 1119 ↔ 1133 | By similarity | |||||||||
| Disulfide bond | 1135 ↔ 1149 | By similarity | |||||||||
| Disulfide bond | 1155 ↔ 1167 | By similarity | |||||||||
| Disulfide bond | 1162 ↔ 1176 | By similarity | |||||||||
| Disulfide bond | 1178 ↔ 1191 | By similarity | |||||||||
| Disulfide bond | 1197 ↔ 1209 | By similarity | |||||||||
| Disulfide bond | 1204 ↔ 1218 | By similarity | |||||||||
| Disulfide bond | 1220 ↔ 1233 | By similarity | |||||||||
| Disulfide bond | 1239 ↔ 1250 | By similarity | |||||||||
| Disulfide bond | 1246 ↔ 1259 | By similarity | |||||||||
| Disulfide bond | 1261 ↔ 1274 | By similarity | |||||||||
| Disulfide bond | 1280 ↔ 1292 | By similarity | |||||||||
| Disulfide bond | 1287 ↔ 1301 | By similarity | |||||||||
| Disulfide bond | 1303 ↔ 1316 | By similarity | |||||||||
| Disulfide bond | 1322 ↔ 1334 | By similarity | |||||||||
| Disulfide bond | 1329 ↔ 1343 | By similarity | |||||||||
| Disulfide bond | 1345 ↔ 1358 | By similarity | |||||||||
| Disulfide bond | 1364 ↔ 1377 | By similarity | |||||||||
| Disulfide bond | 1371 ↔ 1386 | By similarity | |||||||||
| Disulfide bond | 1388 ↔ 1399 | By similarity | |||||||||
| Disulfide bond | 1405 ↔ 1418 | By similarity | |||||||||
| Disulfide bond | 1412 ↔ 1427 | By similarity | |||||||||
| Disulfide bond | 1429 ↔ 1440 | By similarity | |||||||||
| Disulfide bond | 1446 ↔ 1458 | By similarity | |||||||||
| Disulfide bond | 1453 ↔ 1467 | By similarity | |||||||||
| Disulfide bond | 1469 ↔ 1482 | By similarity | |||||||||
| Disulfide bond | 1488 ↔ 1499 | By similarity | |||||||||
| Disulfide bond | 1494 ↔ 1508 | By similarity | |||||||||
| Disulfide bond | 1510 ↔ 1523 | By similarity | |||||||||
| Disulfide bond | 1529 ↔ 1540 | By similarity | |||||||||
| Disulfide bond | 1535 ↔ 1549 | By similarity | |||||||||
| Disulfide bond | 1551 ↔ 1564 | By similarity | |||||||||
| Disulfide bond | 1647 ↔ 1659 | By similarity | |||||||||
| Disulfide bond | 1654 ↔ 1668 | By similarity | |||||||||
| Disulfide bond | 1670 ↔ 1683 | By similarity | |||||||||
| Disulfide bond | 1689 ↔ 1701 | By similarity | |||||||||
| Disulfide bond | 1696 ↔ 1710 | By similarity | |||||||||
| Disulfide bond | 1712 ↔ 1725 | By similarity | |||||||||
| Disulfide bond | 1805 ↔ 1817 | By similarity | |||||||||
| Disulfide bond | 1812 ↔ 1826 | By similarity | |||||||||
| Disulfide bond | 1828 ↔ 1841 | By similarity | |||||||||
| Disulfide bond | 1847 ↔ 1860 | By similarity | |||||||||
| Disulfide bond | 1854 ↔ 1869 | By similarity | |||||||||
| Disulfide bond | 1871 ↔ 1883 | By similarity | |||||||||
| Disulfide bond | 1889 ↔ 1901 | By similarity | |||||||||
| Disulfide bond | 1896 ↔ 1910 | By similarity | |||||||||
| Disulfide bond | 1912 ↔ 1925 | By similarity | |||||||||
| Disulfide bond | 1931 ↔ 1941 | By similarity | |||||||||
| Disulfide bond | 1936 ↔ 1950 | By similarity | |||||||||
| Disulfide bond | 1952 ↔ 1964 | By similarity | |||||||||
| Disulfide bond | 1970 ↔ 1983 | By similarity | |||||||||
| Disulfide bond | 1978 ↔ 1992 | By similarity | |||||||||
| Disulfide bond | 1994 ↔ 2007 | By similarity | |||||||||
| Disulfide bond | 2013 ↔ 2025 | By similarity | |||||||||
| Disulfide bond | 2020 ↔ 2034 | By similarity | |||||||||
| Disulfide bond | 2036 ↔ 2047 | By similarity | |||||||||
| Disulfide bond | 2053 ↔ 2065 | By similarity | |||||||||
| Disulfide bond | 2060 ↔ 2074 | By similarity | |||||||||
| Disulfide bond | 2076 ↔ 2089 | By similarity | |||||||||
| Disulfide bond | 2168 ↔ 2180 | By similarity | |||||||||
| Disulfide bond | 2175 ↔ 2189 | By similarity | |||||||||
| Disulfide bond | 2191 ↔ 2204 | By similarity | |||||||||
| Disulfide bond | 2210 ↔ 2221 | By similarity | |||||||||
| Disulfide bond | 2216 ↔ 2230 | By similarity | |||||||||
| Disulfide bond | 2232 ↔ 2244 | By similarity | |||||||||
| Disulfide bond | 2250 ↔ 2261 | By similarity | |||||||||
| Disulfide bond | 2257 ↔ 2270 | By similarity | |||||||||
| Disulfide bond | 2272 ↔ 2285 | By similarity | |||||||||
| Disulfide bond | 2291 ↔ 2305 | By similarity | |||||||||
| Disulfide bond | 2298 ↔ 2314 | By similarity | |||||||||
| Disulfide bond | 2316 ↔ 2329 | By similarity | |||||||||
| Disulfide bond | 2335 ↔ 2347 | By similarity | |||||||||
| Disulfide bond | 2342 ↔ 2356 | By similarity | |||||||||
| Disulfide bond | 2358 ↔ 2371 | By similarity | |||||||||
| Disulfide bond | 2446 ↔ 2458 | By similarity | |||||||||
| Disulfide bond | 2453 ↔ 2467 | By similarity | |||||||||
| Disulfide bond | 2469 ↔ 2482 | By similarity | |||||||||
| Disulfide bond | 2488 ↔ 2499 | By similarity | |||||||||
| Disulfide bond | 2495 ↔ 2508 | By similarity | |||||||||
| Disulfide bond | 2510 ↔ 2523 | By similarity | |||||||||
| Disulfide bond | 2529 ↔ 2540 | By similarity | |||||||||
| Disulfide bond | 2536 ↔ 2549 | By similarity | |||||||||
| Disulfide bond | 2551 ↔ 2562 | By similarity | |||||||||
| Disulfide bond | 2568 ↔ 2581 | By similarity | |||||||||
| Disulfide bond | 2575 ↔ 2590 | By similarity | |||||||||
| Disulfide bond | 2592 ↔ 2605 | By similarity | |||||||||
| Disulfide bond | 2611 ↔ 2621 | By similarity | |||||||||
| Disulfide bond | 2617 ↔ 2630 | By similarity | |||||||||
| Disulfide bond | 2632 ↔ 2645 | By similarity | |||||||||
| Disulfide bond | 2651 ↔ 2662 | By similarity | |||||||||
| Disulfide bond | 2657 ↔ 2671 | By similarity | |||||||||
| Disulfide bond | 2673 ↔ 2686 | By similarity | |||||||||
| Disulfide bond | 2692 ↔ 2703 | By similarity | |||||||||
| Disulfide bond | 2699 ↔ 2712 | By similarity | |||||||||
| Disulfide bond | 2714 ↔ 2726 | By similarity | |||||||||
Experimental info | |||||||||||
| Sequence conflict | 39 | 1 | R → W in AAA74908. Ref.1 | ||||||||
| Sequence conflict | 70 | 1 | A → R in AAA74908. Ref.1 | ||||||||
| Sequence conflict | 143 | 1 | A → R in AAA74908. Ref.1 | ||||||||
| Sequence conflict | 263 | 1 | R → P in AAA74908. Ref.1 | ||||||||
| Sequence conflict | 263 | 1 | R → P in AAC60685. Ref.3 | ||||||||
| Sequence conflict | 440 | 1 | T → N in AAA74908. Ref.1 | ||||||||
| Sequence conflict | 513 | 1 | E → R in AAA74908. Ref.1 | ||||||||
| Sequence conflict | 587 | 1 | T → S in AAA74908. Ref.1 | ||||||||
| Sequence conflict | 783 | 1 | S → T in AAA74908. Ref.1 | ||||||||
| Sequence conflict | 836 – 837 | 2 | FR → LP in AAA74908. Ref.1 | ||||||||
| Sequence conflict | 919 | 1 | A → G in AAA74908. Ref.1 | ||||||||
| Sequence conflict | 1064 | 1 | Y → C in AAA74908. Ref.1 | ||||||||
| Sequence conflict | 1559 | 1 | P → A in AAA74908. Ref.1 | ||||||||
| Sequence conflict | 1590 | 1 | V → A in AAA74908. Ref.1 | ||||||||
| Sequence conflict | 1622 | 1 | Y → H in AAA74908. Ref.1 | ||||||||
| Sequence conflict | 1765 | 1 | W → G in AAA74908. Ref.1 | ||||||||
| Sequence conflict | 1937 | 1 | G → A in AAA74908. Ref.1 | ||||||||
| Sequence conflict | 2227 | 1 | S → C in AAA74908. Ref.1 | ||||||||
| Sequence conflict | 2277 | 1 | A → G in AAA74908. Ref.1 | ||||||||
| Sequence conflict | 2475 | 1 | T → M in AAA74908. Ref.1 | ||||||||
| Sequence conflict | 2634 – 2636 | 3 | QGY → HGD in AAA74908. Ref.1 | ||||||||
Sequences
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References
| « Hide 'large scale' references | |
| [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] | "Lineage-specific biology revealed by a finished genome assembly of the mouse." Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.  Ponting C.P.PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract] 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, 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. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | L39790 Genomic DNA. Translation: AAA74908.1. AC102317 Genomic DNA. No translation available. AC127358 Genomic DNA. No translation available. S69359 Unassigned DNA. Translation: AAC60685.1. |
| IPI | IPI00122439. |
| PIR | A57278. |
| RefSeq | NP_034311.2. NM_010181.2. XP_001473465.1. XM_001473415.1. |
| UniGene | Mm.20271. |
3D structure databases | |
| ProteinModelPortal | Q61555. |
| SMR | Q61555. Positions 845-989, 1107-1192, 1524-1684, 2164-2245. |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | 10090.ENSMUSP00000025497. |
PTM databases | |
| PhosphoSite | Q61555. |
Proteomic databases | |
| PaxDb | Q61555. |
| PRIDE | Q61555. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| Ensembl | ENSMUST00000025497; ENSMUSP00000025497; ENSMUSG00000024598. |
| GeneID | 100047082. 14119. |
| KEGG | mmu:100047082. mmu:14119. |
| UCSC | uc008ezn.1. mouse. |
Organism-specific databases | |
| CTD | 2201. |
| MGI | MGI:95490. Fbn2. |
Phylogenomic databases | |
| eggNOG | NOG12793. |
| GeneTree | ENSGT00700000104076. |
| HOGENOM | HOG000231768. |
| HOVERGEN | HBG005643. |
| InParanoid | Q61555. |
| OMA | SGRNCID. |
| OrthoDB | EOG45TCM7. |
Gene expression databases | |
| Bgee | Q61555. |
| CleanEx | MM_FBN2. |
| Genevestigator | Q61555. |
| GermOnline | ENSMUSG00000024598. Mus musculus. |
Family and domain databases | |
| Gene3D | 3.90.290.10. 9 hits. |
| InterPro | IPR026823. cEGF. IPR000742. EG-like_dom. IPR001881. EGF-like_Ca-bd. IPR013032. EGF-like_CS. IPR000152. EGF-type_Asp/Asn_hydroxyl_site. IPR018097. EGF_Ca-bd_CS. IPR011398. FBN. IPR009030. Growth_fac_rcpt_N_dom. IPR017878. TB_dom. [Graphical view] |
| PANTHER | PTHR24039:SF0. PTHR24039:SF0. 1 hit. |
| Pfam | PF12662. cEGF. 2 hits. PF07645. EGF_CA. 39 hits. PF00683. TB. 9 hits. [Graphical view] |
| PIRSF | PIRSF036312. Fibrillin. 1 hit. |
| SMART | SM00181. EGF. 3 hits. SM00179. EGF_CA. 43 hits. [Graphical view] |
| SUPFAM | SSF57581. Fibril-assoc. 9 hits. SSF57184. Grow_fac_recept. 1 hit. |
| PROSITE | PS00010. 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] |
| ProtoNet | Search... |
Other | |
| NextBio | 285184. |
| SOURCE | Search... |
Entry information
| Entry name | FBN2_MOUSE | ||||||||
| Accession | Primary (citable) accession number: Q61555 Secondary accession number(s): E9QJZ4, Q63957 | ||||||||
| Entry history |
| ||||||||
| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Chordata Protein Annotation Program | ||||||||
Relevant documents
| MGD cross-references Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot |
| SIMILARITY comments Index of protein domains and families |