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Q75N90 (FBN3_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 106. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Fibrillin-3
Gene names
Name:FBN3
Synonyms:KIAA1776
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length2809 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript 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-containing microfibrils provide long-term force bearing structural support. Ref.1

Subcellular location

Secretedextracellular spaceextracellular matrix Ref.1.

Tissue specificity

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. Ref.1

Post-translational modification

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

Sequence similarities

Belongs to the fibrillin family.

Contains 44 EGF-like domains.

Contains 9 TB (TGF-beta binding) domains.

Sequence caution

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

Ontologies

Keywords
   Cellular componentExtracellular matrix
Secreted
   Coding sequence diversityPolymorphism
   DomainEGF-like domain
Repeat
Signal
   LigandCalcium
   PTMDisulfide bond
Glycoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Cellular_componentproteinaceous extracellular matrix

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functioncalcium ion binding

Inferred from electronic annotation. Source: InterPro

extracellular matrix structural constituent

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 3131 Potential
Chain32 – 28092778Fibrillin-3
PRO_0000007586

Regions

Domain147 – 17933EGF-like 1
Domain185 – 23753TB 1
Domain247 – 28842EGF-like 2; calcium-binding
Domain293 – 34654TB 2
Domain408 – 44841EGF-like 3
Domain449 – 48840EGF-like 4; calcium-binding
Domain489 – 53042EGF-like 5; calcium-binding
Domain531 – 57141EGF-like 6; calcium-binding
Domain572 – 61241EGF-like 7; calcium-binding
Domain618 – 67053TB 3
Domain682 – 72342EGF-like 8; calcium-binding
Domain724 – 76542EGF-like 9; calcium-binding
Domain766 – 80540EGF-like 10; calcium-binding
Domain810 – 86152TB 4
Domain869 – 91042EGF-like 11; calcium-binding
Domain915 – 96652TB 5
Domain986 – 102742EGF-like 12; calcium-binding
Domain1028 – 107043EGF-like 13; calcium-binding
Domain1071 – 111242EGF-like 14; calcium-binding
Domain1113 – 115442EGF-like 15; calcium-binding
Domain1155 – 119541EGF-like 16; calcium-binding
Domain1196 – 123742EGF-like 17
Domain1238 – 127942EGF-like 18; calcium-binding
Domain1280 – 132041EGF-like 19; calcium-binding
Domain1321 – 136141EGF-like 20; calcium-binding
Domain1362 – 140342EGF-like 21; calcium-binding
Domain1404 – 144441EGF-like 22; calcium-binding
Domain1445 – 148541EGF-like 23; calcium-binding
Domain1490 – 154657TB 6
Domain1563 – 160442EGF-like 24; calcium-binding
Domain1605 – 164642EGF-like 25; calcium-binding
Domain1651 – 170353TB 7
Domain1721 – 176242EGF-like 26; calcium-binding
Domain1763 – 180442EGF-like 27; calcium-binding
Domain1805 – 184642EGF-like 28
Domain1847 – 188539EGF-like 29; calcium-binding
Domain1886 – 192843EGF-like 30; calcium-binding
Domain1929 – 196840EGF-like 31; calcium-binding
Domain1969 – 201042EGF-like 32; calcium-binding
Domain2015 – 206854TB 8
Domain2084 – 212542EGF-like 33; calcium-binding
Domain2126 – 216540EGF-like 34; calcium-binding
Domain2166 – 220641EGF-like 35; calcium-binding
Domain2207 – 225145EGF-like 36; calcium-binding
Domain2252 – 229342EGF-like 37; calcium-binding
Domain2298 – 235154TB 9
Domain2363 – 240442EGF-like 38; calcium-binding
Domain2405 – 244541EGF-like 39; calcium-binding
Domain2446 – 248439EGF-like 40; calcium-binding
Domain2485 – 252743EGF-like 41; calcium-binding
Domain2528 – 256740EGF-like 42; calcium-binding
Domain2568 – 260942EGF-like 43; calcium-binding
Domain2610 – 264940EGF-like 44; calcium-binding

Amino acid modifications

Glycosylation4061N-linked (GlcNAc...) Potential
Glycosylation10251N-linked (GlcNAc...) Potential
Glycosylation14421N-linked (GlcNAc...) Potential
Glycosylation15381N-linked (GlcNAc...) Potential
Glycosylation16271N-linked (GlcNAc...) Potential
Glycosylation16581N-linked (GlcNAc...) Potential
Glycosylation16681N-linked (GlcNAc...) Potential
Glycosylation18581N-linked (GlcNAc...) Potential
Glycosylation20331N-linked (GlcNAc...) Potential
Glycosylation27131N-linked (GlcNAc...) Potential
Disulfide bond151 ↔ 161 By similarity
Disulfide bond155 ↔ 167 By similarity
Disulfide bond169 ↔ 178 By similarity
Disulfide bond251 ↔ 263 By similarity
Disulfide bond258 ↔ 272 By similarity
Disulfide bond274 ↔ 287 By similarity
Disulfide bond412 ↔ 424 By similarity
Disulfide bond419 ↔ 433 By similarity
Disulfide bond435 ↔ 447 By similarity
Disulfide bond453 ↔ 463 By similarity
Disulfide bond458 ↔ 472 By similarity
Disulfide bond474 ↔ 487 By similarity
Disulfide bond493 ↔ 505 By similarity
Disulfide bond500 ↔ 514 By similarity
Disulfide bond516 ↔ 529 By similarity
Disulfide bond535 ↔ 546 By similarity
Disulfide bond541 ↔ 555 By similarity
Disulfide bond557 ↔ 570 By similarity
Disulfide bond576 ↔ 587 By similarity
Disulfide bond582 ↔ 596 By similarity
Disulfide bond598 ↔ 611 By similarity
Disulfide bond686 ↔ 698 By similarity
Disulfide bond693 ↔ 707 By similarity
Disulfide bond709 ↔ 722 By similarity
Disulfide bond728 ↔ 740 By similarity
Disulfide bond735 ↔ 749 By similarity
Disulfide bond751 ↔ 764 By similarity
Disulfide bond770 ↔ 780 By similarity
Disulfide bond775 ↔ 789 By similarity
Disulfide bond791 ↔ 804 By similarity
Disulfide bond873 ↔ 885 By similarity
Disulfide bond880 ↔ 894 By similarity
Disulfide bond896 ↔ 909 By similarity
Disulfide bond990 ↔ 1002 By similarity
Disulfide bond997 ↔ 1011 By similarity
Disulfide bond1013 ↔ 1026 By similarity
Disulfide bond1032 ↔ 1044 By similarity
Disulfide bond1039 ↔ 1053 By similarity
Disulfide bond1055 ↔ 1069 By similarity
Disulfide bond1075 ↔ 1087 By similarity
Disulfide bond1082 ↔ 1096 By similarity
Disulfide bond1098 ↔ 1111 By similarity
Disulfide bond1117 ↔ 1129 By similarity
Disulfide bond1124 ↔ 1138 By similarity
Disulfide bond1140 ↔ 1153 By similarity
Disulfide bond1159 ↔ 1170 By similarity
Disulfide bond1166 ↔ 1179 By similarity
Disulfide bond1181 ↔ 1194 By similarity
Disulfide bond1200 ↔ 1212 By similarity
Disulfide bond1207 ↔ 1221 By similarity
Disulfide bond1223 ↔ 1236 By similarity
Disulfide bond1242 ↔ 1254 By similarity
Disulfide bond1249 ↔ 1263 By similarity
Disulfide bond1265 ↔ 1278 By similarity
Disulfide bond1284 ↔ 1297 By similarity
Disulfide bond1291 ↔ 1306 By similarity
Disulfide bond1308 ↔ 1319 By similarity
Disulfide bond1325 ↔ 1338 By similarity
Disulfide bond1332 ↔ 1347 By similarity
Disulfide bond1349 ↔ 1360 By similarity
Disulfide bond1366 ↔ 1378 By similarity
Disulfide bond1373 ↔ 1387 By similarity
Disulfide bond1389 ↔ 1402 By similarity
Disulfide bond1408 ↔ 1419 By similarity
Disulfide bond1414 ↔ 1428 By similarity
Disulfide bond1430 ↔ 1443 By similarity
Disulfide bond1449 ↔ 1460 By similarity
Disulfide bond1455 ↔ 1469 By similarity
Disulfide bond1471 ↔ 1484 By similarity
Disulfide bond1567 ↔ 1579 By similarity
Disulfide bond1574 ↔ 1588 By similarity
Disulfide bond1590 ↔ 1603 By similarity
Disulfide bond1609 ↔ 1621 By similarity
Disulfide bond1616 ↔ 1630 By similarity
Disulfide bond1632 ↔ 1645 By similarity
Disulfide bond1725 ↔ 1737 By similarity
Disulfide bond1732 ↔ 1746 By similarity
Disulfide bond1748 ↔ 1761 By similarity
Disulfide bond1767 ↔ 1780 By similarity
Disulfide bond1774 ↔ 1789 By similarity
Disulfide bond1791 ↔ 1803 By similarity
Disulfide bond1809 ↔ 1821 By similarity
Disulfide bond1816 ↔ 1830 By similarity
Disulfide bond1832 ↔ 1845 By similarity
Disulfide bond1851 ↔ 1861 By similarity
Disulfide bond1856 ↔ 1870 By similarity
Disulfide bond1872 ↔ 1884 By similarity
Disulfide bond1890 ↔ 1903 By similarity
Disulfide bond1898 ↔ 1912 By similarity
Disulfide bond1914 ↔ 1927 By similarity
Disulfide bond1933 ↔ 1945 By similarity
Disulfide bond1940 ↔ 1954 By similarity
Disulfide bond1956 ↔ 1967 By similarity
Disulfide bond1973 ↔ 1985 By similarity
Disulfide bond1980 ↔ 1994 By similarity
Disulfide bond1996 ↔ 2009 By similarity
Disulfide bond2088 ↔ 2100 By similarity
Disulfide bond2095 ↔ 2109 By similarity
Disulfide bond2111 ↔ 2124 By similarity
Disulfide bond2130 ↔ 2141 By similarity
Disulfide bond2136 ↔ 2150 By similarity
Disulfide bond2152 ↔ 2164 By similarity
Disulfide bond2170 ↔ 2181 By similarity
Disulfide bond2177 ↔ 2190 By similarity
Disulfide bond2192 ↔ 2205 By similarity
Disulfide bond2211 ↔ 2225 By similarity
Disulfide bond2218 ↔ 2234 By similarity
Disulfide bond2236 ↔ 2250 By similarity
Disulfide bond2256 ↔ 2268 By similarity
Disulfide bond2263 ↔ 2277 By similarity
Disulfide bond2279 ↔ 2292 By similarity
Disulfide bond2367 ↔ 2379 By similarity
Disulfide bond2374 ↔ 2388 By similarity
Disulfide bond2390 ↔ 2403 By similarity
Disulfide bond2409 ↔ 2420 By similarity
Disulfide bond2416 ↔ 2429 By similarity
Disulfide bond2431 ↔ 2444 By similarity
Disulfide bond2450 ↔ 2461 By similarity
Disulfide bond2457 ↔ 2470 By similarity
Disulfide bond2472 ↔ 2483 By similarity
Disulfide bond2489 ↔ 2502 By similarity
Disulfide bond2496 ↔ 2511 By similarity
Disulfide bond2513 ↔ 2526 By similarity
Disulfide bond2532 ↔ 2542 By similarity
Disulfide bond2538 ↔ 2551 By similarity
Disulfide bond2553 ↔ 2566 By similarity
Disulfide bond2572 ↔ 2584 By similarity
Disulfide bond2579 ↔ 2593 By similarity
Disulfide bond2595 ↔ 2608 By similarity
Disulfide bond2614 ↔ 2625 By similarity
Disulfide bond2621 ↔ 2634 By similarity
Disulfide bond2636 ↔ 2648 By similarity

Natural variations

Natural variant1191G → A.
Corresponds to variant rs3813773 [ dbSNP | Ensembl ].
VAR_019493
Natural variant3291P → L.
Corresponds to variant rs7246376 [ dbSNP | Ensembl ].
VAR_055736
Natural variant3711M → I.
Corresponds to variant rs35999680 [ dbSNP | Ensembl ].
VAR_055737
Natural variant4731R → Q. Ref.2
Corresponds to variant rs35277492 [ dbSNP | Ensembl ].
VAR_019494
Natural variant5421V → I.
Corresponds to variant rs36124795 [ dbSNP | Ensembl ].
VAR_055738
Natural variant6621D → N. Ref.1 Ref.2 Ref.3
Corresponds to variant rs4804271 [ dbSNP | Ensembl ].
VAR_019495
Natural variant8681D → N.
Corresponds to variant rs35025963 [ dbSNP | Ensembl ].
VAR_055739
Natural variant9351R → L. Ref.2
VAR_019496
Natural variant9381V → F. Ref.2
VAR_019497
Natural variant10831R → W. Ref.2
Corresponds to variant rs35579498 [ dbSNP | Ensembl ].
VAR_019498
Natural variant12091Q → R.
Corresponds to variant rs34684510 [ dbSNP | Ensembl ].
VAR_055740
Natural variant12931S → G.
Corresponds to variant rs4804063 [ dbSNP | Ensembl ].
VAR_055741
Natural variant12931S → N.
Corresponds to variant rs4804063 [ dbSNP | Ensembl ].
VAR_019499
Natural variant13261V → I. Ref.3
Corresponds to variant rs12975322 [ dbSNP | Ensembl ].
VAR_019500
Natural variant14311N → I.
Corresponds to variant rs17160194 [ dbSNP | Ensembl ].
VAR_055742
Natural variant16141G → S. Ref.1 Ref.2
Corresponds to variant rs33967815 [ dbSNP | Ensembl ].
VAR_019501
Natural variant18061R → Q. Ref.3
Corresponds to variant rs3829817 [ dbSNP | Ensembl ].
VAR_019502
Natural variant18501E → K.
Corresponds to variant rs10404519 [ dbSNP | Ensembl ].
VAR_055743
Natural variant18691N → K. Ref.2
Corresponds to variant rs12150963 [ dbSNP | Ensembl ].
VAR_019503
Natural variant19041L → F.
Corresponds to variant rs12608849 [ dbSNP | Ensembl ].
VAR_055744
Natural variant19041L → P. Ref.2
Corresponds to variant rs12608849 [ dbSNP | Ensembl ].
VAR_019504
Natural variant19391T → N.
Corresponds to variant rs7245558 [ dbSNP | Ensembl ].
VAR_055745
Natural variant19581P → H.
Corresponds to variant rs7245429 [ dbSNP | Ensembl ].
VAR_019505
Natural variant19661H → D.
Corresponds to variant rs34167077 [ dbSNP | Ensembl ].
VAR_055746
Natural variant20051N → T.
Corresponds to variant rs17202741 [ dbSNP | Ensembl ].
VAR_055747
Natural variant23141S → N.
Corresponds to variant rs17160151 [ dbSNP | Ensembl ].
VAR_055748
Natural variant24711R → H.
Corresponds to variant rs3848570 [ dbSNP | Ensembl ].
VAR_055749
Natural variant25401H → Q.
Corresponds to variant rs35477781 [ dbSNP | Ensembl ].
VAR_055750
Natural variant25941V → I.
Corresponds to variant rs35318692 [ dbSNP | Ensembl ].
VAR_055751
Natural variant26101E → D. Ref.1 Ref.2 Ref.3
Corresponds to variant rs7257948 [ dbSNP | Ensembl ].
VAR_019506

Sequences

Sequence LengthMass (Da)Tools
Q75N90 [UniParc].

Last modified May 18, 2010. Version 3.
Checksum: FE47EF22C1307C14

FASTA2,809300,356
        10         20         30         40         50         60 
MTLEGLYLAR GPLARLLLAW SALLCMAGGQ GRWDGALEAA GPGRVRRRGS PGILQGPNVC 

        70         80         90        100        110        120 
GSRFHAYCCP GWRTFPGRSQ CVVPICRRAC GEGFCSQPNL CTCADGTLAP SCGVSRGSGC 

       130        140        150        160        170        180 
SVSCMNGGTC RGASCLCQKG YTGTVCGQPI CDRGCHNGGR CIGPNRCACV YGFMGPQCER 

       190        200        210        220        230        240 
DYRTGPCFGQ VGPEGCQHQL TGLVCTKALC CATVGRAWGL PCELCPAQPH PCRRGFIPNI 

       250        260        270        280        290        300 
HTGACQDVDE CQAVPGLCQG GSCVNMVGSF HCRCPVGHRL SDSSAACEDY RAGACFSVLF 

       310        320        330        340        350        360 
GGRCAGDLAG HYTRRQCCCD RGRCWAAGPV PELCPPRGSN EFQQLCAQRL PLLPGHPGLF 

       370        380        390        400        410        420 
PGLLGFGSNG MGPPLGPARL NPHGSDARGI PSLGPGNSNI GTATLNQTID ICRHFTNLCL 

       430        440        450        460        470        480 
NGRCLPTPSS YRCECNVGYT QDVRGECIDV DECTSSPCHH GDCVNIPGTY HCRCYPGFQA 

       490        500        510        520        530        540 
TPTRQACVDV DECIVSGGLC HLGRCVNTEG SFQCVCNAGF ELSPDGKNCV DHNECATSTM 

       550        560        570        580        590        600 
CVNGVCLNED GSFSCLCKPG FLLAPGGHYC MDIDECQTPG ICVNGHCTNT EGSFRCQCLG 

       610        620        630        640        650        660 
GLAVGTDGRV CVDTHVRSTC YGAIEKGSCA RPFPGTVTKS ECCCANPDHG FGEPCQLCPA 

       670        680        690        700        710        720 
KDSAEFQALC SSGLGITTDG RDINECALDP EVCANGVCEN LRGSYRCVCN LGYEAGASGK 

       730        740        750        760        770        780 
DCTDVDECAL NSLLCDNGWC QNSPGSYSCS CPPGFHFWQD TEICKDVDEC LSSPCVSGVC 

       790        800        810        820        830        840 
RNLAGSYTCK CGPGSRLDPS GTFCLDSTKG TCWLKIQESR CEVNLQGASL RSECCATLGA 

       850        860        870        880        890        900 
AWGSPCERCE IDPACARGFA RMTGVTCDDV NECESFPGVC PNGRCVNTAG SFRCECPEGL 

       910        920        930        940        950        960 
MLDASGRLCV DVRLEPCFLR WDEDECGVTL PGKYRMDVCC CSIGAVWGVE CEACPDPESL 

       970        980        990       1000       1010       1020 
EFASLCPRGL GFASRDFLSG RPFYKDVNEC KVFPGLCTHG TCRNTVGSFH CACAGGFALD 

      1030       1040       1050       1060       1070       1080 
AQERNCTDID ECRISPDLCG QGTCVNTPGS FECECFPGYE SGFMLMKNCM DVDECARDPL 

      1090       1100       1110       1120       1130       1140 
LCRGGTCTNT DGSYKCQCPP GHELTAKGTA CEDIDECSLS DGLCPHGQCV NVIGAFQCSC 

      1150       1160       1170       1180       1190       1200 
HAGFQSTPDR QGCVDINECR VQNGGCDVHC INTEGSYRCS CGQGYSLMPD GRACADVDEC 

      1210       1220       1230       1240       1250       1260 
EENPRVCDQG HCTNMPGGHR CLCYDGFMAT PDMRTCVDVD ECDLNPHICL HGDCENTKGS 

      1270       1280       1290       1300       1310       1320 
FVCHCQLGYM VRKGATGCSD VDECEVGGHN CDSHASCLNI PGSFSCRCLP GWVGDGFECH 

      1330       1340       1350       1360       1370       1380 
DLDECVSQEH RCSPRGDCLN VPGSYRCTCR QGFAGDGFFC EDRDECAENV DLCDNGQCLN 

      1390       1400       1410       1420       1430       1440 
APGGYRCECE MGFDPTEDHR ACQDVDECAQ GNLCAFGSCE NLPGMFRCIC NGGYELDRGG 

      1450       1460       1470       1480       1490       1500 
GNCTDINECA DPVNCINGVC INTPGSYLCS CPQDFELNPS GVGCVDTRAG NCFLETHDRG 

      1510       1520       1530       1540       1550       1560 
DSGISCSAEI GVGVTRASCC CSLGRAWGNP CELCPMANTT EYRTLCPGGE GFQPNRITVI 

      1570       1580       1590       1600       1610       1620 
LEDIDECQEL PGLCQGGDCV NTFGSFQCEC PPGYHLSEHT RICEDIDECS THSGICGPGT 

      1630       1640       1650       1660       1670       1680 
CYNTLGNYTC VCPAEYLQVN GGNNCMDMRK SVCFRHYNGT CQNELAFNVT RKMCCCSYNI 

      1690       1700       1710       1720       1730       1740 
GQAWNRPCEA CPTPISPDYQ ILCGNQAPGF LTDIHTGKPL DIDECGEIPA ICANGICINQ 

      1750       1760       1770       1780       1790       1800 
IGSFRCECPA GFNYNSILLA CEDVDECGSR ESPCQQNADC INIPGSYRCK CTRGYKLSPG 

      1810       1820       1830       1840       1850       1860 
GACVGRNECR EIPNVCSHGD CMDTEGSYMC LCHRGFQASA DQTLCMDIDE CDRQPCGNGT 

      1870       1880       1890       1900       1910       1920 
CKNIIGSYNC LCFPGFVVTH NGDCVDFDEC TTLVGQVCRF GHCLNTAGSF HCLCQDGFEL 

      1930       1940       1950       1960       1970       1980 
TADGKNCVDT NECLSLAGTC LPGTCQNLEG SFRCICPPGF QVQSDHCIDI DECSEEPNLC 

      1990       2000       2010       2020       2030       2040 
LFGTCTNSPG SFQCLCPPGF VLSDNGHRCF DTRQSFCFTR FEAGKCSVPK AFNTTKTRCC 

      2050       2060       2070       2080       2090       2100 
CSKRPGEGWG DPCELCPQEG SAAFQELCPF GHGAVPGPDD SREDVNECAE NPGVCTNGVC 

      2110       2120       2130       2140       2150       2160 
VNTDGSFRCE CPFGYSLDFT GINCVDTDEC SVGHPCGQGT CTNVIGGFEC ACADGFEPGL 

      2170       2180       2190       2200       2210       2220 
MMTCEDIDEC SLNPLLCAFR CHNTEGSYLC TCPAGYTLRE DGAMCRDVDE CADGQQDCHA 

      2230       2240       2250       2260       2270       2280 
RGMECKNLIG TFACVCPPGM RPLPGSGEGC TDDNECHAQP DLCVNGRCVN TAGSFRCDCD 

      2290       2300       2310       2320       2330       2340 
EGFQPSPTLT ECHDIRQGPC FAEVLQTMCR SLSSSSEAVT RAECCCGGGR GWGPRCELCP 

      2350       2360       2370       2380       2390       2400 
LPGTSAYRKL CPHGSGYTAE GRDVDECRML AHLCAHGECI NSLGSFRCHC QAGYTPDATA 

      2410       2420       2430       2440       2450       2460 
TTCLDMDECS QVPKPCTFLC KNTKGSFLCS CPRGYLLEED GRTCKDLDEC TSRQHNCQFL 

      2470       2480       2490       2500       2510       2520 
CVNTVGAFTC RCPPGFTQHH QACFDNDECS AQPGPCGAHG HCHNTPGSFR CECHQGFTLV 

      2530       2540       2550       2560       2570       2580 
SSGHGCEDVN ECDGPHRCQH GCQNQLGGYR CSCPQGFTQH SQWAQCVDEN ECALSPPTCG 

      2590       2600       2610       2620       2630       2640 
SASCRNTLGG FRCVCPSGFD FDQALGGCQE VDECAGRRGP CSYSCANTPG GFLCGCPQGY 

      2650       2660       2670       2680       2690       2700 
FRAGQGHCVS GLGFSPGPQD TPDKEELLSS EACYECKING LSPRDRPRRS AHRDHQVNLA 

      2710       2720       2730       2740       2750       2760 
TLDSEALLTL GLNLSHLGRA ERILELRPAL EGLEGRIRYV IVRGNEQGFF RMHHLRGVSS 

      2770       2780       2790       2800 
LQLGRRRPGP GTYRLEVVSH MAGPWGVQPE GQPGPWGQAL RLKVQLQLL 

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS12196.1.
RefSeqNP_115823.3. NM_032447.3.
UniGeneHs.370362.

3D structure databases

ProteinModelPortalQ75N90.
SMRQ75N90. Positions 46-612, 682-910, 983-2636.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid124100. 13 interactions.
IntActQ75N90. 14 interactions.
MINTMINT-4095014.
STRING9606.ENSP00000270509.

PTM databases

PhosphoSiteQ75N90.

Polymorphism databases

DMDM296439346.

Proteomic databases

PaxDbQ75N90.
PRIDEQ75N90.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000270509; ENSP00000270509; ENSG00000142449.
ENST00000600128; ENSP00000470498; ENSG00000142449.
ENST00000601739; ENSP00000472324; ENSG00000142449.
GeneID84467.
KEGGhsa:84467.
UCSCuc002mjf.3. human.

Organism-specific databases

CTD84467.
GeneCardsGC19M008130.
H-InvDBHIX0014707.
HGNCHGNC:18794. FBN3.
HPAHPA049482.
MIM608529. gene.
neXtProtNX_Q75N90.
PharmGKBPA38681.
HUGESearch...
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG12793.
HOGENOMHOG000231768.
HOVERGENHBG005643.
InParanoidQ75N90.
OMASCARPFP.
OrthoDBEOG7RV9F6.
PhylomeDBQ75N90.
TreeFamTF316849.

Enzyme and pathway databases

ReactomeREACT_118779. Extracellular matrix organization.

Gene expression databases

BgeeQ75N90.
CleanExHS_FBN3.
GenevestigatorQ75N90.

Family and domain databases

Gene3D3.90.290.10. 9 hits.
InterProIPR026823. 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]
PANTHERPTHR24039. PTHR24039. 1 hit.
PfamPF12662. cEGF. 3 hits.
PF00008. EGF. 1 hit.
PF07645. EGF_CA. 38 hits.
PF00683. TB. 9 hits.
[Graphical view]
PIRSFPIRSF036312. Fibrillin. 1 hit.
SMARTSM00181. EGF. 4 hits.
SM00179. EGF_CA. 41 hits.
[Graphical view]
SUPFAMSSF57184. SSF57184. 12 hits.
SSF57581. SSF57581. 9 hits.
PROSITEPS00010. 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]
ProtoNetSearch...

Other

GenomeRNAi84467.
NextBio74278.
PROQ75N90.
SOURCESearch...

Entry information

Entry nameFBN3_HUMAN
AccessionPrimary (citable) accession number: Q75N90
Secondary accession number(s): Q75N91 expand/collapse secondary AC list , Q75N92, Q75N93, Q86SJ5, Q96JP8
Entry history
Integrated into UniProtKB/Swiss-Prot: July 19, 2004
Last sequence update: May 18, 2010
Last modified: July 9, 2014
This is version 106 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 19

Human chromosome 19: entries, gene names and cross-references to MIM