Predict Disorder


This version of PONDR-FIT is for academic use only. Commercial users must obtain permission from http://www.pondr.com/. PONDR-FIT is statistically not different from VL3 for fully disordered and fully structured
proteins, and slightly better (1 std) than VSL2 when both structure and disorder are present.



Enter the sequence file in Fasta or EMBL sequence format, as described below.


Examples of input


You may specify regions of interest with the following syntax
on the header lines: >... #100-200 regionname #300-400 otherregion
For example:

>DisProt|DP00002|sp|P02400|pir|A35109 #1-110
MKYLAAYLLLVQGGNAAPSAADIKAVVESVGAEVDEARINELLSSLEGKGSLEEIIAEGQ
KKFATVPTGGASSAAAGAAGAAAGGDAAEEEKEEEAKEESDDDMGFGLFD           


    EMBL format files can also be entered and edited.  All comment lines,
    such as "MoRF II." must be ended with a period.  New sequence
    features can be added as "FT   NAME  33   44   Comment."
    where there must be three spaces between "FT" and the feature "NAME".
For example:

ID   STE5_YEAST              Reviewed;         917 AA.
AC   P32917;
FT   CHAIN         1    917       Protein STE5.
FT   IDR           740   917       
FT   IDR          1    165           Predicted intrinsically disordered.
FT   IDR          255   360   
FT   MORF     20    20       MoRF II.
FT   MORF     80    80   
FT   MORF    325    325    MoRF II.    
FT                                /FTId=PRO_0000072266.
FT   COMPBIAS    775    876       Asp/Glu-rich (acidic).
FT   MOD_RES     329    329      Phosphoserine.
FT   MOD_RES     898    898       Phosphoserine.
FT   CONFLICT    331    332      Conflict.
FT   CONFLICT2   341    343      Another conflict.
FT   CONFLICT    821    821
FT   HELIX       593    604       Helix.
FT   STRAND      612    616     Strand.
FT   HELIX       618    620      
FT   HELIX       625    640     
FT   STRAND      645    650
FT   STRAND      653    657
FT   HELIX       661    664
FT   HELIX       668    672
FT   HELIX       673    676
FT   HELIX       685    692
FT   STRAND      704    707
FT   TURN        713    715     Turn.
FT   HELIX       717    719
FT   HELIX       723    725
FT   STRAND      736    739
FT   HELIX       760    770
SQ   SEQUENCE   917 AA;  102727 MW;  0435BDA0196B2D6F CRC64;
     MMETPTDNIV SPFHNFGSST QYSGTLSRTP NQIIELEKPS TLSPLSRGKK WTEKLARFQR
     SSAKKKRFSP SPISSSTFSF SPKSRVTSSN SSGNEDGNLM NTPSTVSTDY LPQHPHRTSS
     LPRPNSNLFH ASNSNLSRAN EPPRAENLSD NIPPKVAPFG YPIQRTSIKK SFLNASCTLC
     DEPISNRRKG EKIIELACGH LSHQECLIIS FGTTSKADVR ALFPFCTKCK KDTNKAVQCI
     PENDELKDIL ISDFLIHKIP DSELSITPQS RFPPYSPLLP PFGLSYTPVE RQTIYSQAPS
     LNPNLILAAP PKERNQIPQK KSNYTFLHSP LGHRRIPSGA NSILADTSVA LSANDSISAV
     SNSVRAKDDE TKTTLPLLRS YFIQILLNNF QEELQDWRID GDYGLLRLVD KLMISKDGQR
     YIQCWCFLFE DAFVIAEVDN DVDVLEIRLK NLEVFTPIAN LRMTTLEASV LKCTLNKQHC
     ADLSDLYIVQ NINSDESTTV QKWISGILNQ DFVFNEDNIT STLPILPIIK NFSKDVGNGR
     HETSTFLGLI NPNKVVEVGN VHDNDTVIIR RGFTLNSGEC SRQSTVDSIQ SVLTTISSIL
     SLKREKPDNL AIILQIDFTK LKEEDSLIVV YNSLKALTIK FARLQFCFVD RNNYVLDYGS
     VLHKIDSLDS ISNLKSKSSS TQFSPIWLKN TLYPENIHEH LGIVAVSNSN MEAKKSILFQ
     DYRCFTSFGR RRPNELKIKV GYLNVDYSDK IDELVEASSW TFVLETLCYS FGLSFDEHDD
     DDEEDNDDST DNELDNSSGS LSDAESTTTI HIDSPFDNEN ATANMVNDRN LLTEGEHSNI
     ENLETVASSV QPALIPNIRF SLHSEEEGTN ENENENDMPV LLLSDMDKGI DGITRRSSFS
     SLIESGNNNC PLHMDYI
//
Cut here --------------------------   second example:

ID   APC_HUMAN               Reviewed;        2843 AA.
AC   P25054; Q15162; Q15163; Q93042;
DR   GO; GO:0005912; C:adherens junction; IEA:UniProtKB-SubCell.
DR   GO; GO:0034747; C:Axin-APC-beta-catenin-GSK3B complex; IDA:UniProtKB.
DR   GO; GO:0030877; C:beta-catenin destruction complex; IDA:UniProtKB.
DR   GO; GO:0005813; C:centrosome; IDA:UniProtKB.
DR   GO; GO:0005829; C:cytosol; EXP:Reactome.
DR   GO; GO:0000776; C:kinetochore; IDA:UniProtKB.
DR   GO; GO:0016328; C:lateral plasma membrane; IDA:MGI.
DR   GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR   GO; GO:0005923; C:tight junction; IDA:UniProtKB.
DR   GO; GO:0008013; F:beta-catenin binding; IPI:UniProtKB.
DR   GO; GO:0008017; F:microtubule binding; IDA:UniProtKB.
DR   GO; GO:0019901; F:protein kinase binding; IPI:UniProtKB.
DR   GO; GO:0019887; F:protein kinase regulator activity; IDA:UniProtKB.
DR   GO; GO:0007155; P:cell adhesion; NAS:UniProtKB.
DR   GO; GO:0007050; P:cell cycle arrest; IDA:UniProtKB.
DR   GO; GO:0000281; P:cytokinesis after mitosis; IMP:MGI.
DR   GO; GO:0007094; P:mitotic cell cycle spindle assembly checkpoint; IMP:MGI.
DR   GO; GO:0045736; P:negative regulation of cyclin-dependent pro...; IDA:UniProtKB.
DR   GO; GO:0007026; P:negative regulation of microtubule depolyme...; IDA:UniProtKB.
DR   GO; GO:0043065; P:positive regulation of apoptosis; IMP:MGI.
DR   GO; GO:0030335; P:positive regulation of cell migration; IMP:MGI.
DR   GO; GO:0031274; P:positive regulation of pseudopodium assembly; IMP:MGI.
DR   GO; GO:0006461; P:protein complex assembly; IDA:UniProtKB.
DR   GO; GO:0051988; P:regulation of attachment of spindle microtu...; NAS:UniProtKB.
DR   GO; GO:0006974; P:response to DNA damage stimulus; IDA:UniProtKB.
DR   GO; GO:0070830; P:tight junction assembly; NAS:UniProtKB.
DR   GO; GO:0060070; P:Wnt receptor signaling pathway through beta...; NAS:UniProtKB.
DR   InterPro; IPR009240; APC_15aa.
DR   InterPro; IPR009234; APC_basic.
DR   InterPro; IPR009223; APC_crr.
DR   InterPro; IPR011989; ARM-like.
DR   InterPro; IPR016024; ARM-type_fold.
DR   InterPro; IPR000225; Armadillo.
DR   InterPro; IPR009232; EB1_bd.
DR   InterPro; IPR009224; SAMP.
DR   Gene3D; G3DSA:1.25.10.10; ARM-like; 1.
DR   Pfam; PF05972; APC_15aa; 4.
DR   Pfam; PF05956; APC_basic; 1.
DR   Pfam; PF05923; APC_crr; 7.
DR   Pfam; PF00514; Arm; 3.
DR   Pfam; PF05937; EB1_binding; 1.
DR   Pfam; PF05924; SAMP; 3.
DR   SMART; SM00185; ARM; 6.
DR   SUPFAM; SSF48371; ARM-type_fold; 1.
DR   PROSITE; PS50176; ARM_REPEAT; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Alternative splicing; Cell junction; Coiled coil;
KW   Complete proteome; Disease mutation; Phosphoprotein; Polymorphism;
KW   Repeat; Tumor suppressor; Ubl conjugation; Wnt signaling pathway.
FT   CHAIN         1   2843       Adenomatous polyposis coli protein, evidence: protein.
FT                                /FTId=PRO_0000064627.
FT   PFAM_ASEED3       1369   1394  Pfam PF05923 repeated motifs bind beta-catenin, first three  (1369-1394, 1485-1510, 1636-1661) are near cancer linked SNPs.
FT   PFAM_ASEED3       1485   1510
FT   PFAM_ASEED3       1636   1661
FT   PFAM_ASEED3       1840   1866
FT   PFAM_ASEED3       1948   1973
FT   PFAM_ASEED3       2006   2031
FT   PFAM_ASEED       512   553   Pfam PF00514 Armadillo/beta-catenin-like repeats, form super-helix of helices.
FT   PFAM_ASEED       556   597
FT   PFAM_ASEED       649   689
FT   PFAM_ASEED       691   731
FT   PFAM_ASEED2     2223   2579   Pfam PF05956 APC_basic domain, interacts with microtubules.
FT   PFAM_ASEED4       2670   2843   Pfam PF05937 EB1_binding, binds the microtubule-associating protein EB-1. 
FT   PFAM_A11     126   208   Pfam PF11414 suppressor APC, 126-208.
FT   PFAM_A1          1020   1035 Pfam PF05972 APC 15 residue motifs (not included in seeds),
FT              near cancer mutations.      
FT   PFAM_A2         1256   1281  Pfam PF05923, APC_cysteine-rich region near cancer related SNPs, binds beta-catenin.  
FT   PFAM_A          1569   1589 Pfam PF05924  SAMP motif binds axin, pdb:1emu.       
FT   PFAM_A          1718   1738  
FT   PFAM_A          2034   2053 
FT   PFAM_A1          1136   1151
FT   PFAM_A1          1155   1170
FT   PFAM_A1          1172   1187
FT   DISORDER           1  158     Predicted instrinsically disordered regions (IDRs, 1-158, 177-401, 427-441, 730-1486, 1491-1636, 1655-2641, 2663-2843).
FT   DISORDER           177  401
FT   DISORDER           427  441
FT   DISORDER           730  1486
FT   DISORDER           1491 1636  
FT   DISORDER           1655 2641
FT   DISORDER           2663 2843   
FT   MORF  2       19          Predicted molecular recognition features (MoRFs).
FT   MORF  34      51
FT   MORF  76      93
FT   MORF  111     128
FT   MORF  158     175
FT   MORF  223     240
FT   MORF  768     785
FT   MORF  799     816
FT   MORF  880     897
FT   MORF  928     945
FT   MORF  997     1014
FT   MORF  1081    1098
FT   MORF  1171    1188
FT   MORF  1256    1273
FT   MORF  1348    1365
FT   MORF  1381    1398
FT   MORF  1486    1503
FT   MORF  1574    1591
FT   MORF  1629    1646
FT   MORF  1732    1749
FT   MORF  1889    1906
FT   MORF  1925    1942
FT   MORF  1953    1970
FT   MORF  2011    2028
FT   MORF  2032    2049
FT   MORF  2068    2085
FT   MORF  2099    2116
FT   MORF  2195    2212
FT   MORF  2399    2416
FT   MORF  2434    2451
FT   MORF  2508    2525
FT   MORF  2586    2603
FT   MORF  2648    2665
FT   MORF  2715    2732
FT   MORF  2826    2843
FT   PDB3      1482  1528    X-ray diffraction evidence, APC_HUMAN(1482-1528)-beta-catenin complex, PDB  1V18.
FT   PDB31    1482  1484    APC residues not located in the 1V18 experiment.
FT   PDB31    1500  1503
FT   PDB4    1484   1498   X-ray diffraction evidence, phosphorylated APC_HUMAN(1484-1498)-beta-catenin/ICAT complex, PDB 1T08.
FT   PDB5    1362  1540  X-ray diffraction evidence, phosphorylated APC_HUMAN()-beta-catenin complex, PDB 1TH1.
FT   PDB51   1362  1467   APC residues not located in the 1TH1 experiment.
FT   PDB51   1497  1502
FT   PDB51   1530  1540
FT   PDB2    2832  2843      Solution NMR evidence, the APC_HUMAN(2832-2843)-PTP-BL_MOUSE complex, PDB 1VJ6.
FT   PDB21    2832  2837    APC residues not observed in the 1VJ6 experiment, 2822-2827.
FT   PDB1        126   250     X-ray diffraction evidence, APC_HUMAN(126-250), PDB 1M5I.
FT   PDB11         126   178   APC residues not located in the 1M5I experiment, 126-178, 240-250.
FT   PDB11         240   250
FT   PDB6   1021   1035    X-ray diffraction evidence, APC_HUMAN(1021-1035)-beta-catenin complex , PDB 1JPP.
FT   PDB61  1035   1035    APC residues not located in the 1JPP experiment.
FT   PDB7   2  55          X-ray diffraction evidence, APC_HUMAN(2-55), PDB 1DEB.
FT   PDB71  2  2      APC residue 2 was not located in the 1DEB experiment. 
FT   PDB8   2034   2049  X-ray diffraction evidence, APC_HUMAN(2034-2049)-AXIN complex, PDB 1EMU, all residues observed.
FT   PDB91             1362   1745    CD and NMR experimental data measured only for the longest fragment (1362-1745) that could be obtained in large quantity.     
FT   REGION77  2035   2050   Axin binding, PDB: 1emu.
FT   REGION88  1021   1031   Beta-Catenin binding, PDB 1jpp...1th1.
FT   REGION88  1468   1529   
FT   REPEAT      453    495       Armadillo/beta-catenin-like repeats (ARM).
FT   REPEAT      505    547       
FT   REPEAT      548    591       
FT   REPEAT      592    638       
FT   REPEAT      639    683       
FT   REPEAT      684    725       
FT   REPEAT      726    767       
FT   REGION      960   1337       Down-regulation mediated by direct ubiquitination.
FT   COMPBIAS      1    730       Leu-rich.
FT   COMPBIAS    731   2832       Ser-rich.
FT   COMPBIAS   1131   1156       Asp/Glu.
FT   COMPBIAS   1558   1577       Asp/Glu.
FT   MOD_RES     780    780       Phosphorylation.
FT   MOD_RES     987    987
FT   MOD_RES2   1038   1038       Phosphorylation by similarity.
FT   MOD_RES    1042   1042       
FT   MOD_RES2    1180   1180      
FT   MOD_RES    1360   1360       
FT   MOD_RES2    1371   1371      
FT   MOD_RES    1438   1438       
FT   MOD_RES    1559   1559      
FT   MOD_RES2    1697   1697      
FT   MOD_RES    1861   1861       
FT   MOD_RES    1863   1863       
FT   MOD_RES    1864   1864       
FT   MOD_RES    2088   2088       
FT   MOD_RES    2093   2093       
FT   MOD_RES    2096   2096       
FT   MOD_RES    2125   2125       
FT   MOD_RES    2143   2143       
FT   MOD_RES2    2151   2151       
FT   MOD_RES    2260   2260       
FT   MOD_RES2    2266   2266       
FT   MOD_RES    2270   2270       
FT   MOD_RES    2283   2283       
FT   MOD_RES    2398   2398       
FT   MOD_RES    2464   2464       
FT   MOD_RES    2469   2469       
FT   MOD_RES    2473   2473       
FT   MOD_RES    2533   2533       
FT   MOD_RES    2535   2535       
FT   MOD_RES    2671   2671       
FT   MOD_RES    2674   2674       
FT   MOD_RES2    2676   2676       
FT   MOD_RES2    2679   2679       
FT   MOD_RES2    2710   2710      
FT   MOD_RES    2789   2789       
FT   MOD_RES    2835   2835       
FT   MOD_RES    2837   2837       
FT   MOD_RES    2838   2838       
FT   VAR_SEQ     312    412       Missing in isoform Short.
FT                                /FTId=VSP_004115.
FT   VARIANT1      99     99       R>W in FAP (familial adenomatous polyposis); could be rare.
FT                                /FTId=VAR_009613.
FT   VARIANT2     171    171       All in FAP: S>I  R>C       S>G  S>T  S>C     I>T L>F 
FT                                 R>C                                    P>L  A>P  R>W.
FT                                /FTId=VAR_005032.
FT   VARIANT2     414    414       
FT                                /FTId=VAR_005033.
FT   VARIANT2     722    722       
FT                                /FTId=VAR_009614.
FT   VARIANT2     784    784       
FT                                /FTId=VAR_005034.
FT   VARIANT2    2621   2621       
FT                                /FTId=VAR_005056.
FT   VARIANT2    2738   2738       
FT                                /FTId=VAR_008994.
FT   VARIANT2    2839   2839       
FT                                /FTId=VAR_005057.
FT   VARIANT2    1171   1171      
FT                                /FTId=VAR_008992.
FT   VARIANT2    1176   1176       
FT                                /FTId=VAR_005044.
FT   VARIANT2    1184   1184       
FT                                /FTId=VAR_009616.
FT   VARIANT2    1348   1348       
FT                                /FTId=VAR_005053.
FT   VARIANT22     890    890       V>I in colorectal carcinoma; from a
FT                                patient with MMRCS.
FT                                /FTId=VAR_012975.
FT   VARIANT32     906    906       S>Y  Y>C in colorectal tumor.
FT                                /FTId=VAR_005037.
FT   VARIANT32    1027   1027       
FT                                /FTId=VAR_005040.
FT   VARIANT51     880    880       I>T in colorectal carcinoma and
FT                                gastric cancer; from a patient with MMRCS.
FT                                /FTId=VAR_005036.
FT   VARIANT52     942    942       In gastric cancer:          G>C    N>D G>E R>H F>S I>T G>E V>A.
FT                                /FTId=VAR_005039.
FT   VARIANT52     817    817      
FT                                /FTId=VAR_005035.
FT   VARIANT52    1120   1120       
FT                                dbSNP:rs28933379.
FT                                /FTId=VAR_005042.
FT   VARIANT52    1171   1171       
FT                                /FTId=VAR_005043.
FT   VARIANT52    1197   1197       
FT                                /FTId=VAR_005045.
FT   VARIANT52    1259   1259       
FT                                /FTId=VAR_005046.
FT   VARIANT52    1312   1312       
FT                                /FTId=VAR_005050.
FT   VARIANT52    1326   1326       
FT                                /FTId=VAR_005052.
FT   VARIANT42     911    911       E>G T>A in FAP and colorectal tumor.
FT                                /FTId=VAR_005038.
FT   VARIANT42    1313   1313       
FT                                /FTId=VAR_005051.
FT   VARIANT35    1254   1254       I>F in a colorectal cancer sample
FT                                (somatic mutation)          D>H in colorectal tumor.
FT                                /FTId=VAR_035794.
FT   VARIANT35    1422   1422       
FT                                /FTId=VAR_005054.
FT   VARIANT65    1508   1508       A>V in colorectal carcinoma from a
FT                                patient with MMRCS.
FT                                /FTId=VAR_012976.
FT   VARIANT26    1296   1296       A>V in MDB (medulloblastoma), sporadic:          A>V    V>I  S>G.
FT                                /FTId=VAR_017653.
FT   VARIANT26    1472   1472     
FT                                /FTId=VAR_017654.
FT   VARIANT26    1495   1495     
FT                                /FTId=VAR_017655.
FT   VARIANT46    1307   1307       I>K 6% of Ashkenazi Jews;
FT                                small increased risk of colon, breast cancer.
FT                                /FTId=VAR_005049.
FT   VARIANT37    1317   1317       E>Q may contribute to colorectal
FT                                tumor development.
FT                                /FTId=VAR_009617.
FT   MUTAGEN    2841   2841       T>L, V>Q: Loss of interaction with Scribble,
FT       which plays a role in polarization of epithelial and neuronal cells.
FT   MUTAGEN    2843   2843       
SQ   SEQUENCE   2843 AA;  311646 MW;  77E194AE4A91DC5A CRC64;
     MAAASYDQLL KQVEALKMEN SNLRQELEDN SNHLTKLETE ASNMKEVLKQ LQGSIEDEAM
     ASSGQIDLLE RLKELNLDSS NFPGVKLRSK MSLRSYGSRE GSVSSRSGEC SPVPMGSFPR
     RGFVNGSRES TGYLEELEKE RSLLLADLDK EEKEKDWYYA QLQNLTKRID SLPLTENFSL
     QTDMTRRQLE YEARQIRVAM EEQLGTCQDM EKRAQRRIAR IQQIEKDILR IRQLLQSQAT
     EAERSSQNKH ETGSHDAERQ NEGQGVGEIN MATSGNGQGS TTRMDHETAS VLSSSSTHSA
     PRRLTSHLGT KVEMVYSLLS MLGTHDKDDM SRTLLAMSSS QDSCISMRQS GCLPLLIQLL
     HGNDKDSVLL GNSRGSKEAR ARASAALHNI IHSQPDDKRG RREIRVLHLL EQIRAYCETC
     WEWQEAHEPG MDQDKNPMPA PVEHQICPAV CVLMKLSFDE EHRHAMNELG GLQAIAELLQ
     VDCEMYGLTN DHYSITLRRY AGMALTNLTF GDVANKATLC SMKGCMRALV AQLKSESEDL
     QQVIASVLRN LSWRADVNSK KTLREVGSVK ALMECALEVK KESTLKSVLS ALWNLSAHCT
     ENKADICAVD GALAFLVGTL TYRSQTNTLA IIESGGGILR NVSSLIATNE DHRQILRENN
     CLQTLLQHLK SHSLTIVSNA CGTLWNLSAR NPKDQEALWD MGAVSMLKNL IHSKHKMIAM
     GSAAALRNLM ANRPAKYKDA NIMSPGSSLP SLHVRKQKAL EAELDAQHLS ETFDNIDNLS
     PKASHRSKQR HKQSLYGDYV FDTNRHDDNR SDNFNTGNMT VLSPYLNTTV LPSSSSSRGS
     LDSSRSEKDR SLERERGIGL GNYHPATENP GTSSKRGLQI STTAAQIAKV MEEVSAIHTS
     QEDRSSGSTT ELHCVTDERN ALRRSSAAHT HSNTYNFTKS ENSNRTCSMP YAKLEYKRSS
     NDSLNSVSSS DGYGKRGQMK PSIESYSEDD ESKFCSYGQY PADLAHKIHS ANHMDDNDGE
     LDTPINYSLK YSDEQLNSGR QSPSQNERWA RPKHIIEDEI KQSEQRQSRN QSTTYPVYTE
     STDDKHLKFQ PHFGQQECVS PYRSRGANGS ETNRVGSNHG INQNVSQSLC QEDDYEDDKP
     TNYSERYSEE EQHEEEERPT NYSIKYNEEK RHVDQPIDYS LKYATDIPSS QKQSFSFSKS
     SSGQSSKTEH MSSSSENTST PSSNAKRQNQ LHPSSAQSRS GQPQKAATCK VSSINQETIQ
     TYCVEDTPIC FSRCSSLSSL SSAEDEIGCN QTTQEADSAN TLQIAEIKEK IGTRSAEDPV
     SEVPAVSQHP RTKSSRLQGS SLSSESARHK AVEFSSGAKS PSKSGAQTPK SPPEHYVQET
     PLMFSRCTSV SSLDSFESRS IASSVQSEPC SGMVSGIISP SDLPDSPGQT MPPSRSKTPP
     PPPQTAQTKR EVPKNKAPTA EKRESGPKQA AVNAAVQRVQ VLPDADTLLH FATESTPDGF
     SCSSSLSALS LDEPFIQKDV ELRIMPPVQE NDNGNETESE QPKESNENQE KEAEKTIDSE
     KDLLDDSDDD DIEILEECII SAMPTKSSRK AKKPAQTASK LPPPVARKPS QLPVYKLLPS
     QNRLQPQKHV SFTPGDDMPR VYCVEGTPIN FSTATSLSDL TIESPPNELA AGEGVRGGAQ
     SGEFEKRDTI PTEGRSTDEA QGGKTSSVTI PELDDNKAEE GDILAECINS AMPKGKSHKP
     FRVKKIMDQV QQASASSSAP NKNQLDGKKK KPTSPVKPIP QNTEYRTRVR KNADSKNNLN
     AERVFSDNKD SKKQNLKNNS KVFNDKLPNN EDRVRGSFAF DSPHHYTPIE GTPYCFSRND
     SLSSLDFDDD DVDLSREKAE LRKAKENKES EAKVTSHTEL TSNQQSANKT QAIAKQPINR
     GQPKPILQKQ STFPQSSKDI PDRGAATDEK LQNFAIENTP VCFSHNSSLS SLSDIDQENN
     NKENEPIKET EPPDSQGEPS KPQASGYAPK SFHVEDTPVC FSRNSSLSSL SIDSEDDLLQ
     ECISSAMPKK KKPSRLKGDN EKHSPRNMGG ILGEDLTLDL KDIQRPDSEH GLSPDSENFD
     WKAIQEGANS IVSSLHQAAA AACLSRQASS DSDSILSLKS GISLGSPFHL TPDQEEKPFT
     SNKGPRILKP GEKSTLETKK IESESKGIKG GKKVYKSLIT GKVRSNSEIS GQMKQPLQAN
     MPSISRGRTM IHIPGVRNSS SSTSPVSKKG PPLKTPASKS PSEGQTATTS PRGAKPSVKS
     ELSPVARQTS QIGGSSKAPS RSGSRDSTPS RPAQQPLSRP IQSPGRNSIS PGRNGISPPN
     KLSQLPRTSS PSTASTKSSG SGKMSYTSPG RQMSQQNLTK QTGLSKNASS IPRSESASKG
     LNQMNNGNGA NKKVELSRMS STKSSGSESD RSERPVLVRQ STFIKEAPSP TLRRKLEESA
     SFESLSPSSR PASPTRSQAQ TPVLSPSLPD MSLSTHSSVQ AGGWRKLPPN LSPTIEYNDG
     RPAKRHDIAR SHSESPSRLP INRSGTWKRE HSKHSSSLPR VSTWRRTGSS SSILSASSES
     SEKAKSEDEK HVNSISGTKQ SKENQVSAKG TWRKIKENEF SPTNSTSQTV SSGATNGAES
     KTLIYQMAPA VSKTEDVWVR IEDCPINNPR SGRSPTGNTP PVIDSVSEKA NPNIKDSKDN
     QAKQNVGNGS VPMRTVGLEN RLNSFIQVDA PDQKGTEIKP GQNNPVPVSE TNESSIVERT
     PFSSSSSSKH SSPSGTVAAR VTPFNYNPSP RKSSADSTSA RPSQIPTPVN NNTKKRDSKT
     DSTESSGTQS PKRHSGSYLV TSV
//
   

     



For VSL2B cite
Obradovic Z, Peng K, Vucetic S, Radivojac P, Dunker AK. "Exploiting heterogeneous sequence properties improves prediction of protein disorder." Proteins. 2005;61 Suppl 7:176-82, PMID: 16187360
For VL3 and cite
Obradovic Z, Peng K, Vucetic S, Radivojac P, Brown CJ, Dunker AK. "Predicting intrinsic disorder from amino acid sequence." Proteins. 2003;53 Suppl 6:566-72, PMID: 14579347
For PONDR-FIT cite
Xue, B., R. L. DunBrack, R.W. Williams, A.K. Dunker, and V. N. Uversky (2010) "PONDR-Fit: A meta-predictor of intrinsically disordered amino acids," Biochim. Biophys. Acta (in press) doi:10.1016/j.bbapap.2010.01.011

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