CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-006492
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Fibrillin-2 
Protein Synonyms/Alias
  
Gene Name
 FBN2 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
1582RVGNCYLKFGPRGDGubiquitination[1]
2861SYLHTAKKKLMPGTYmethylation[2]
2879ITSIPLYKKKELKKLmethylation[2]
Reference
 [1] Systems-wide analysis of ubiquitylation dynamics reveals a key role for PAF15 ubiquitylation in DNA-damage bypass.
 Povlsen LK, Beli P, Wagner SA, Poulsen SL, Sylvestersen KB, Poulsen JW, Nielsen ML, Bekker-Jensen S, Mailand N, Choudhary C.
 Nat Cell Biol. 2012 Oct;14(10):1089-98. [PMID: 23000965]
 [2] Large-scale global identification of protein lysine methylation in vivo.
 Cao XJ, Arnaudo AM, Garcia BA.
 Epigenetics. 2013 May 1;8(5):477-85. [PMID: 23644510] 
Functional Description
 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 (By similarity). 
Sequence Annotation
 DOMAIN 111 142 EGF-like 1.
 DOMAIN 145 176 EGF-like 2.
 DOMAIN 176 208 EGF-like 3.
 DOMAIN 214 266 TB 1.
 DOMAIN 276 317 EGF-like 4; calcium-binding.
 DOMAIN 318 359 EGF-like 5; calcium-binding.
 DOMAIN 364 417 TB 2.
 DOMAIN 494 534 EGF-like 6.
 DOMAIN 535 574 EGF-like 7; calcium-binding.
 DOMAIN 575 616 EGF-like 8; calcium-binding.
 DOMAIN 617 657 EGF-like 9; calcium-binding.
 DOMAIN 658 698 EGF-like 10; calcium-binding.
 DOMAIN 704 756 TB 3.
 DOMAIN 768 809 EGF-like 11; calcium-binding.
 DOMAIN 810 851 EGF-like 12; calcium-binding.
 DOMAIN 852 891 EGF-like 13; calcium-binding.
 DOMAIN 896 947 TB 4.
 DOMAIN 955 996 EGF-like 14; calcium-binding.
 DOMAIN 1001 1052 TB 5.
 DOMAIN 1073 1114 EGF-like 15; calcium-binding.
 DOMAIN 1115 1157 EGF-like 16; calcium-binding.
 DOMAIN 1158 1199 EGF-like 17; calcium-binding.
 DOMAIN 1200 1241 EGF-like 18; calcium-binding.
 DOMAIN 1242 1282 EGF-like 19; calcium-binding.
 DOMAIN 1283 1324 EGF-like 20; calcium-binding.
 DOMAIN 1325 1366 EGF-like 21; calcium-binding.
 DOMAIN 1367 1407 EGF-like 22; calcium-binding.
 DOMAIN 1408 1448 EGF-like 23; calcium-binding.
 DOMAIN 1449 1490 EGF-like 24; calcium-binding.
 DOMAIN 1491 1531 EGF-like 25; calcium-binding.
 DOMAIN 1532 1572 EGF-like 26; calcium-binding.
 DOMAIN 1577 1633 TB 6.
 DOMAIN 1650 1691 EGF-like 27; calcium-binding.
 DOMAIN 1692 1733 EGF-like 28; calcium-binding.
 DOMAIN 1738 1791 TB 7.
 DOMAIN 1808 1849 EGF-like 29; calcium-binding.
 DOMAIN 1850 1891 EGF-like 30; calcium-binding.
 DOMAIN 1892 1933 EGF-like 31; calcium-binding.
 DOMAIN 1934 1972 EGF-like 32; calcium-binding.
 DOMAIN 1973 2015 EGF-like 33; calcium-binding.
 DOMAIN 2016 2055 EGF-like 34; calcium-binding.
 DOMAIN 2056 2097 EGF-like 35; calcium-binding.
 DOMAIN 2102 2155 TB 8.
 DOMAIN 2171 2212 EGF-like 36; calcium-binding.
 DOMAIN 2213 2252 EGF-like 37; calcium-binding.
 DOMAIN 2253 2293 EGF-like 38; calcium-binding.
 DOMAIN 2294 2337 EGF-like 39; calcium-binding.
 DOMAIN 2338 2379 EGF-like 40; calcium-binding.
 DOMAIN 2384 2437 TB 9.
 DOMAIN 2449 2490 EGF-like 41; calcium-binding.
 DOMAIN 2491 2531 EGF-like 42; calcium-binding.
 DOMAIN 2532 2570 EGF-like 43; calcium-binding.
 DOMAIN 2571 2613 EGF-like 44; calcium-binding.
 DOMAIN 2614 2653 EGF-like 45; calcium-binding.
 DOMAIN 2654 2694 EGF-like 46; calcium-binding.
 DOMAIN 2695 2734 EGF-like 47; calcium-binding.
 CARBOHYD 492 492 N-linked (GlcNAc...) (Potential).
 CARBOHYD 1112 1112 N-linked (GlcNAc...).
 CARBOHYD 1414 1414 N-linked (GlcNAc...) (Potential).
 CARBOHYD 1529 1529 N-linked (GlcNAc...) (Potential).
 CARBOHYD 1625 1625 N-linked (GlcNAc...) (Potential).
 CARBOHYD 1714 1714 N-linked (GlcNAc...) (Potential).
 CARBOHYD 1745 1745 N-linked (GlcNAc...) (Potential).
 CARBOHYD 1756 1756 N-linked (GlcNAc...) (Potential).
 CARBOHYD 1945 1945 N-linked (GlcNAc...) (Potential).
 CARBOHYD 2120 2120 N-linked (GlcNAc...) (Potential).
 CARBOHYD 2225 2225 N-linked (GlcNAc...) (Potential).
 CARBOHYD 2808 2808 N-linked (GlcNAc...) (Potential).
 DISULFID 115 124 By similarity.
 DISULFID 119 130 By similarity.
 DISULFID 132 141 By similarity.
 DISULFID 149 159 By similarity.
 DISULFID 153 164 By similarity.
 DISULFID 166 175 By similarity.
 DISULFID 180 190 By similarity.
 DISULFID 184 196 By similarity.
 DISULFID 198 207 By similarity.
 DISULFID 280 292 By similarity.
 DISULFID 287 301 By similarity.
 DISULFID 303 316 By similarity.
 DISULFID 322 334 By similarity.
 DISULFID 329 343 By similarity.
 DISULFID 345 358 By similarity.
 DISULFID 498 510 By similarity.
 DISULFID 505 519 By similarity.
 DISULFID 521 533 By similarity.
 DISULFID 539 549 By similarity.
 DISULFID 544 558 By similarity.
 DISULFID 560 573 By similarity.
 DISULFID 579 591 By similarity.
 DISULFID 586 600 By similarity.
 DISULFID 602 615 By similarity.
 DISULFID 621 632 By similarity.
 DISULFID 627 641 By similarity.
 DISULFID 643 656 By similarity.
 DISULFID 662 673 By similarity.
 DISULFID 668 682 By similarity.
 DISULFID 684 697 By similarity.
 DISULFID 772 784 By similarity.
 DISULFID 779 793 By similarity.
 DISULFID 795 808 By similarity.
 DISULFID 814 826 By similarity.
 DISULFID 821 835 By similarity.
 DISULFID 837 850 By similarity.
 DISULFID 856 866 By similarity.
 DISULFID 861 875 By similarity.
 DISULFID 877 890 By similarity.
 DISULFID 959 971 By similarity.
 DISULFID 966 980 By similarity.
 DISULFID 982 995 By similarity.
 DISULFID 1077 1089 By similarity.
 DISULFID 1084 1098 By similarity.
 DISULFID 1100 1113 By similarity.
 DISULFID 1119 1131 By similarity.
 DISULFID 1126 1140 By similarity.
 DISULFID 1142 1156 By similarity.
 DISULFID 1162 1174 By similarity.
 DISULFID 1169 1183 By similarity.
 DISULFID 1185 1198 By similarity.
 DISULFID 1204 1216 By similarity.
 DISULFID 1211 1225 By similarity.
 DISULFID 1227 1240 By similarity.
 DISULFID 1246 1257 By similarity.
 DISULFID 1253 1266 By similarity.
 DISULFID 1268 1281 By similarity.
 DISULFID 1287 1299 By similarity.
 DISULFID 1294 1308 By similarity.
 DISULFID 1310 1323 By similarity.
 DISULFID 1329 1341 By similarity.
 DISULFID 1336 1350 By similarity.
 DISULFID 1352 1365 By similarity.
 DISULFID 1371 1384 By similarity.
 DISULFID 1378 1393 By similarity.
 DISULFID 1395 1406 By similarity.
 DISULFID 1412 1425 By similarity.
 DISULFID 1419 1434 By similarity.
 DISULFID 1436 1447 By similarity.
 DISULFID 1453 1465 By similarity.
 DISULFID 1460 1474 By similarity.
 DISULFID 1476 1489 By similarity.
 DISULFID 1495 1506 By similarity.
 DISULFID 1501 1515 By similarity.
 DISULFID 1517 1530 By similarity.
 DISULFID 1536 1547 By similarity.
 DISULFID 1542 1556 By similarity.
 DISULFID 1558 1571 By similarity.
 DISULFID 1654 1666 By similarity.
 DISULFID 1661 1675 By similarity.
 DISULFID 1677 1690 By similarity.
 DISULFID 1696 1708 By similarity.
 DISULFID 1703 1717 By similarity.
 DISULFID 1719 1732 By similarity.
 DISULFID 1812 1824 By similarity.
 DISULFID 1819 1833 By similarity.
 DISULFID 1835 1848 By similarity.
 DISULFID 1854 1867 By similarity.
 DISULFID 1861 1876 By similarity.
 DISULFID 1878 1890 By similarity.
 DISULFID 1896 1908 By similarity.
 DISULFID 1903 1917 By similarity.
 DISULFID 1919 1932 By similarity.
 DISULFID 1938 1948 By similarity.
 DISULFID 1943 1957 By similarity.
 DISULFID 1959 1971 By similarity.
 DISULFID 1977 1990 By similarity.
 DISULFID 1985 1999 By similarity.
 DISULFID 2001 2014 By similarity.
 DISULFID 2020 2032 By similarity.
 DISULFID 2027 2041 By similarity.
 DISULFID 2043 2054 By similarity.
 DISULFID 2060 2072 By similarity.
 DISULFID 2067 2081 By similarity.
 DISULFID 2083 2096 By similarity.
 DISULFID 2175 2187 By similarity.
 DISULFID 2182 2196 By similarity.
 DISULFID 2198 2211 By similarity.
 DISULFID 2217 2228 By similarity.
 DISULFID 2223 2237 By similarity.
 DISULFID 2239 2251 By similarity.
 DISULFID 2257 2268 By similarity.
 DISULFID 2264 2277 By similarity.
 DISULFID 2279 2292 By similarity.
 DISULFID 2298 2312 By similarity.
 DISULFID 2305 2321 By similarity.
 DISULFID 2323 2336 By similarity.
 DISULFID 2342 2354 By similarity.
 DISULFID 2349 2363 By similarity.
 DISULFID 2365 2378 By similarity.
 DISULFID 2453 2465 By similarity.
 DISULFID 2460 2474 By similarity.
 DISULFID 2476 2489 By similarity.
 DISULFID 2495 2506 By similarity.
 DISULFID 2502 2515 By similarity.
 DISULFID 2517 2530 By similarity.
 DISULFID 2536 2547 By similarity.
 DISULFID 2543 2556 By similarity.
 DISULFID 2558 2569 By similarity.
 DISULFID 2575 2588 By similarity.
 DISULFID 2582 2597 By similarity.
 DISULFID 2599 2612 By similarity.
 DISULFID 2618 2628 By similarity.
 DISULFID 2624 2637 By similarity.
 DISULFID 2639 2652 By similarity.
 DISULFID 2658 2669 By similarity.
 DISULFID 2664 2678 By similarity.
 DISULFID 2680 2693 By similarity.
 DISULFID 2699 2710 By similarity.
 DISULFID 2706 2719 By similarity.
 DISULFID 2721 2733 By similarity.  
Keyword
 Alternative splicing; Calcium; Complete proteome; Disease mutation; Disulfide bond; EGF-like domain; Extracellular matrix; Glycoprotein; Polymorphism; Reference proteome; Repeat; Secreted; Signal. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 2912 AA 
Protein Sequence
MGRRRRLCLQ LYFLWLGCVV LWAQGTAGQP QPPPPKPPRP QPPPQQVRSA TAGSEGGFLA 60
PEYREEGAAV ASRVRRRGQQ DVLRGPNVCG SRFHSYCCPG WKTLPGGNQC IVPICRNSCG 120
DGFCSRPNMC TCSSGQISST CGSKSIQQCS VRCMNGGTCA DDHCQCQKGY IGTYCGQPVC 180
ENGCQNGGRC IGPNRCACVY GFTGPQCERD YRTGPCFTQV NNQMCQGQLT GIVCTKTLCC 240
ATIGRAWGHP CEMCPAQPQP CRRGFIPNIR TGACQDVDEC QAIPGICQGG NCINTVGSFE 300
CRCPAGHKQS ETTQKCEDID ECSIIPGICE TGECSNTVGS YFCVCPRGYV TSTDGSRCID 360
QRTGMCFSGL VNGRCAQELP GRMTKMQCCC EPGRCWGIGT IPEACPVRGS EEYRRLCMDG 420
LPMGGIPGSA GSRPGGTGGN GFAPSGNGNG YGPGGTGFIP IPGGNGFSPG VGGAGVGAGG 480
QGPIITGLTI LNQTIDICKH HANLCLNGRC IPTVSSYRCE CNMGYKQDAN GDCIDVDECT 540
SNPCTNGDCV NTPGSYYCKC HAGFQRTPTK QACIDIDECI QNGVLCKNGR CVNTDGSFQC 600
ICNAGFELTT DGKNCVDHDE CTTTNMCLNG MCINEDGSFK CICKPGFVLA PNGRYCTDVD 660
ECQTPGICMN GHCINSEGSF RCDCPPGLAV GMDGRVCVDT HMRSTCYGGI KKGVCVRPFP 720
GAVTKSECCC ANPDYGFGEP CQPCPAKNSA EFHGLCSSGV GITVDGRDIN ECALDPDICA 780
NGICENLRGS YRCNCNSGYE PDASGRNCID IDECLVNRLL CDNGLCRNTP GSYSCTCPPG 840
YVFRTETETC EDINECESNP CVNGACRNNL GSFNCECSPG SKLSSTGLIC IDSLKGTCWL 900
NIQDSRCEVN INGATLKSEC CATLGAAWGS PCERCELDTA CPRGLARIKG VTCEDVNECE 960
VFPGVCPNGR CVNSKGSFHC ECPEGLTLDG TGRVCLDIRM EQCYLKWDED ECIHPVPGKF 1020
RMDACCCAVG AAWGTECEEC PKPGTKEYET LCPRGAGFAN RGDVLTGRPF YKDINECKAF 1080
PGMCTYGKCR NTIGSFKCRC NSGFALDMEE RNCTDIDECR ISPDLCGSGI CVNTPGSFEC 1140
ECFEGYESGF MMMKNCMDID ECERNPLLCR GGTCVNTEGS FQCDCPLGHE LSPSREDCVD 1200
INECSLSDNL CRNGKCVNMI GTYQCSCNPG YQATPDRQGC TDIDECMIMN GGCDTQCTNS 1260
EGSYECSCSE GYALMPDGRS CADIDECENN PDICDGGQCT NIPGEYRCLC YDGFMASMDM 1320
KTCIDVNECD LNSNICMFGE CENTKGSFIC HCQLGYSVKK GTTGCTDVDE CEIGAHNCDM 1380
HASCLNIPGS FKCSCREGWI GNGIKCIDLD ECSNGTHQCS INAQCVNTPG SYRCACSEGF 1440
TGDGFTCSDV DECAENINLC ENGQCLNVPG AYRCECEMGF TPASDSRSCQ DIDECSFQNI 1500
CVFGTCNNLP GMFHCICDDG YELDRTGGNC TDIDECADPI NCVNGLCVNT PGRYECNCPP 1560
DFQLNPTGVG CVDNRVGNCY LKFGPRGDGS LSCNTEIGVG VSRSSCCCSL GKAWGNPCET 1620
CPPVNSTEYY TLCPGGEGFR PNPITIILED IDECQELPGL CQGGNCINTF GSFQCECPQG 1680
YYLSEDTRIC EDIDECFAHP GVCGPGTCYN TLGNYTCICP PEYMQVNGGH NCMDMRKSFC 1740
YRSYNGTTCE NELPFNVTKR MCCCTYNVGK AWNKPCEPCP TPGTADFKTI CGNIPGFTFD 1800
IHTGKAVDID ECKEIPGICA NGVCINQIGS FRCECPTGFS YNDLLLVCED IDECSNGDNL 1860
CQRNADCINS PGSYRCECAA GFKLSPNGAC VDRNECLEIP NVCSHGLCVD LQGSYQCICH 1920
NGFKASQDQT MCMDVDECER HPCGNGTCKN TVGSYNCLCY PGFELTHNND CLDIDECSSF 1980
FGQVCRNGRC FNEIGSFKCL CNEGYELTPD GKNCIDTNEC VALPGSCSPG TCQNLEGSFR 2040
CICPPGYEVK SENCIDINEC DEDPNICLFG SCTNTPGGFQ CLCPPGFVLS DNGRRCFDTR 2100
QSFCFTNFEN GKCSVPKAFN TTKAKCCCSK MPGEGWGDPC ELCPKDDEVA FQDLCPYGHG 2160
TVPSLHDTRE DVNECLESPG ICSNGQCINT DGSFRCECPM GYNLDYTGVR CVDTDECSIG 2220
NPCGNGTCTN VIGSFECNCN EGFEPGPMMN CEDINECAQN PLLCAFRCMN TFGSYECTCP 2280
IGYALREDQK MCKDLDECAE GLHDCESRGM MCKNLIGTFM CICPPGMARR PDGEGCVDEN 2340
ECRTKPGICE NGRCVNIIGS YRCECNEGFQ SSSSGTECLD NRQGLCFAEV LQTICQMASS 2400
SRNLVTKSEC CCDGGRGWGH QCELCPLPGT AQYKKICPHG PGYTTDGRDI DECKVMPNLC 2460
TNGQCINTMG SFRCFCKVGY TTDISGTSCI DLDECSQSPK PCNYICKNTE GSYQCSCPRG 2520
YVLQEDGKTC KDLDECQTKQ HNCQFLCVNT LGGFTCKCPP GFTQHHTACI DNNECGSQPS 2580
LCGAKGICQN TPGSFSCECQ RGFSLDATGL NCEDVDECDG NHRCQHGCQN ILGGYRCGCP 2640
QGYIQHYQWN QCVDENECSN PNACGSASCY NTLGSYKCAC PSGFSFDQFS SACHDVNECS 2700
SSKNPCNYGC SNTEGGYLCG CPPGYYRVGQ GHCVSGMGFN KGQYLSLDTE VDEENALSPE 2760
ACYECKINGY SKKDSRQKRS IHEPDPTAVE QISLESVDMD SPVNMKFNLS HLGSKEHILE 2820
LRPAIQPLNN HIRYVISQGN DDSVFRIHQR NGLSYLHTAK KKLMPGTYTL EITSIPLYKK 2880
KELKKLEESN EDDYLLGELG EALRMRLQIQ LY 2912 
Gene Ontology
 GO:0001527; C:microfibril; TAS:BHF-UCL.
 GO:0005509; F:calcium ion binding; IEA:InterPro.
 GO:0005201; F:extracellular matrix structural constituent; TAS:ProtInc.
 GO:0060346; P:bone trabecula formation; ISS:BHF-UCL.
 GO:0030326; P:embryonic limb morphogenesis; IEA:Compara.
 GO:0030198; P:extracellular matrix organization; TAS:Reactome.
 GO:0030501; P:positive regulation of bone mineralization; ISS:BHF-UCL.
 GO:0045669; P:positive regulation of osteoblast differentiation; ISS:BHF-UCL.
 GO:0035583; P:sequestering of TGFbeta in extracellular matrix; ISS:BHF-UCL. 
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.
 IPR017878; TB_dom. 
Pfam
 PF12662; cEGF
 PF07645; EGF_CA
 PF00683; TB 
SMART
 SM00181; EGF
 SM00179; EGF_CA 
PROSITE
 PS00010; ASX_HYDROXYL
 PS00022; EGF_1
 PS01186; EGF_2
 PS50026; EGF_3
 PS01187; EGF_CA
 PS51364; TB 
PRINTS