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
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