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Protein

Neuroblast differentiation-associated protein AHNAK

Gene

AHNAK

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

May be required for neuronal cell differentiation.

GO - Molecular functioni

  • cadherin binding involved in cell-cell adhesion Source: BHF-UCL
  • poly(A) RNA binding Source: UniProtKB
  • S100 protein binding Source: UniProtKB
  • structural molecule activity conferring elasticity Source: UniProtKB

GO - Biological processi

  • protein oligomerization Source: UniProtKB
  • regulation of RNA splicing Source: UniProtKB
  • regulation of voltage-gated calcium channel activity Source: UniProtKB
Complete GO annotation...

Names & Taxonomyi

Protein namesi
Recommended name:
Neuroblast differentiation-associated protein AHNAK
Alternative name(s):
Desmoyokin
Gene namesi
Name:AHNAK
Synonyms:PM227
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 11

Organism-specific databases

HGNCiHGNC:347. AHNAK.

Subcellular locationi

GO - Cellular componenti

  • actin cytoskeleton Source: UniProtKB
  • cell-cell adherens junction Source: BHF-UCL
  • cell-cell contact zone Source: UniProtKB
  • costamere Source: UniProtKB
  • cytoplasm Source: UniProtKB
  • cytosol Source: UniProtKB
  • extracellular exosome Source: UniProtKB
  • focal adhesion Source: UniProtKB
  • lysosomal membrane Source: UniProtKB
  • membrane Source: UniProtKB
  • nucleus Source: UniProtKB
  • plasma membrane Source: UniProtKB
  • sarcolemma Source: UniProtKB
  • T-tubule Source: UniProtKB
  • vesicle Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA24640.

Polymorphism and mutation databases

DMDMi160332335.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 58905890Neuroblast differentiation-associated protein AHNAKPRO_0000064504Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionineCombined sources
Modified residuei41 – 411PhosphoserineCombined sources
Modified residuei93 – 931PhosphoserineCombined sources
Modified residuei101 – 1011PhosphothreonineCombined sources
Modified residuei115 – 1151PhosphoserineCombined sources
Cross-linki134 – 134Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1)Combined sources
Cross-linki134 – 134Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residuei135 – 1351PhosphoserineCombined sources
Modified residuei158 – 1581PhosphothreonineCombined sources
Modified residuei177 – 1771PhosphoserineCombined sources
Modified residuei210 – 2101PhosphoserineCombined sources
Modified residuei212 – 2121PhosphoserineCombined sources
Modified residuei216 – 2161PhosphoserineCombined sources
Modified residuei218 – 2181PhosphothreonineCombined sources
Modified residuei220 – 2201PhosphoserineCombined sources
Modified residuei256 – 2561PhosphoserineCombined sources
Modified residuei332 – 3321PhosphoserineCombined sources
Modified residuei337 – 3371PhosphoserineCombined sources
Modified residuei379 – 3791PhosphoserineCombined sources
Modified residuei470 – 4701PhosphoserineCombined sources
Modified residuei490 – 4901PhosphothreonineCombined sources
Modified residuei511 – 5111PhosphoserineCombined sources
Modified residuei551 – 5511PhosphothreonineCombined sources
Modified residuei553 – 5531PhosphothreonineCombined sources
Modified residuei559 – 5591PhosphoserineCombined sources
Modified residuei570 – 5701PhosphoserineCombined sources
Modified residuei572 – 5721PhosphoserineCombined sources
Modified residuei658 – 6581PhosphoserineCombined sources
Cross-linki712 – 712Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residuei793 – 7931PhosphoserineCombined sources
Modified residuei819 – 8191PhosphoserineCombined sources
Cross-linki942 – 942Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1)Combined sources
Cross-linki961 – 961Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1)Combined sources
Cross-linki961 – 961Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residuei1010 – 10101PhosphoserineCombined sources
Modified residuei1042 – 10421PhosphoserineCombined sources
Modified residuei1068 – 10681PhosphoserineCombined sources
Modified residuei1170 – 11701PhosphoserineCombined sources
Modified residuei1192 – 11921PhosphothreonineCombined sources
Modified residuei1196 – 11961PhosphoserineCombined sources
Modified residuei1286 – 12861PhosphoserineCombined sources
Modified residuei1298 – 12981PhosphoserineCombined sources
Modified residuei1580 – 15801PhosphoserineCombined sources
Modified residuei1654 – 16541PhosphoserineCombined sources
Modified residuei1856 – 18561PhosphoserineCombined sources
Modified residuei1923 – 19231PhosphoserineCombined sources
Modified residuei1986 – 19861PhosphothreonineCombined sources
Modified residuei1990 – 19901PhosphoserineCombined sources
Modified residuei2092 – 20921PhosphoserineCombined sources
Modified residuei2118 – 21181PhosphoserineCombined sources
Cross-linki2132 – 2132Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1)Combined sources
Modified residuei2138 – 21381PhosphoserineCombined sources
Modified residuei2181 – 21811PhosphothreonineCombined sources
Modified residuei2287 – 22871PhosphoserineCombined sources
Modified residuei2309 – 23091PhosphothreonineCombined sources
Modified residuei2397 – 23971PhosphoserineCombined sources
Cross-linki2575 – 2575Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1)Combined sources
Modified residuei2580 – 25801PhosphoserineCombined sources
Cross-linki2594 – 2594Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1)Combined sources
Modified residuei2600 – 26001PhosphoserineCombined sources
Modified residuei2670 – 26701PhosphoserineCombined sources
Cross-linki2703 – 2703Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1)Combined sources
Modified residuei2708 – 27081PhosphoserineCombined sources
Cross-linki2722 – 2722Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1)Combined sources
Modified residuei2728 – 27281PhosphoserineCombined sources
Modified residuei2798 – 27981PhosphoserineCombined sources
Modified residuei2832 – 28321PhosphothreonineCombined sources
Modified residuei2845 – 28451PhosphothreonineCombined sources
Cross-linki2959 – 2959Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1)Combined sources
Modified residuei3054 – 30541PhosphoserineCombined sources
Cross-linki3087 – 3087Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1)Combined sources
Modified residuei3092 – 30921PhosphoserineCombined sources
Modified residuei3182 – 31821PhosphoserineCombined sources
Cross-linki3215 – 3215Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1)Combined sources
Modified residuei3220 – 32201PhosphoserineCombined sources
Modified residuei3362 – 33621PhosphoserineCombined sources
Modified residuei3409 – 34091PhosphoserineCombined sources
Modified residuei3412 – 34121PhosphoserineCombined sources
Modified residuei3426 – 34261PhosphoserineCombined sources
Modified residuei3544 – 35441PhosphoserineCombined sources
Cross-linki3667 – 3667Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1)Combined sources
Modified residuei3716 – 37161PhosphothreonineCombined sources
Modified residuei3746 – 37461PhosphoserineCombined sources
Cross-linki3760 – 3760Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1)Combined sources
Modified residuei3766 – 37661PhosphoserineCombined sources
Modified residuei3836 – 38361PhosphoserineCombined sources
Cross-linki3869 – 3869Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1)Combined sources
Modified residuei3874 – 38741PhosphoserineCombined sources
Modified residuei3964 – 39641PhosphoserineCombined sources
Cross-linki3997 – 3997Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1)Combined sources
Modified residuei4002 – 40021PhosphoserineCombined sources
Cross-linki4016 – 4016Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1)Combined sources
Modified residuei4022 – 40221PhosphoserineCombined sources
Modified residuei4092 – 40921PhosphoserineCombined sources
Modified residuei4100 – 41001PhosphothreonineCombined sources
Modified residuei4150 – 41501PhosphoserineCombined sources
Modified residuei4220 – 42201PhosphoserineCombined sources
Cross-linki4253 – 4253Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1)Combined sources
Modified residuei4258 – 42581PhosphoserineCombined sources
Cross-linki4272 – 4272Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1)Combined sources
Modified residuei4278 – 42781PhosphoserineCombined sources
Modified residuei4360 – 43601PhosphoserineCombined sources
Cross-linki4381 – 4381Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1)Combined sources
Cross-linki4400 – 4400Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1)Combined sources
Modified residuei4406 – 44061PhosphoserineCombined sources
Modified residuei4425 – 44251PhosphoserineCombined sources
Modified residuei4430 – 44301PhosphothreonineCombined sources
Cross-linki4455 – 4455Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1)Combined sources
Modified residuei4460 – 44601PhosphoserineCombined sources
Cross-linki4474 – 4474Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1)Combined sources
Modified residuei4480 – 44801PhosphoserineCombined sources
Modified residuei4486 – 44861PhosphoserineCombined sources
Modified residuei4516 – 45161PhosphoserineCombined sources
Modified residuei4520 – 45201PhosphoserineCombined sources
Modified residuei4564 – 45641PhosphothreonineCombined sources
Modified residuei4684 – 46841PhosphoserineCombined sources
Modified residuei4722 – 47221PhosphoserineCombined sources
Modified residuei4766 – 47661PhosphothreonineCombined sources
Modified residuei4812 – 48121PhosphoserineCombined sources
Modified residuei4900 – 49001PhosphoserineCombined sources
Modified residuei4903 – 49031PhosphoserineCombined sources
Modified residuei4908 – 49081PhosphoserineCombined sources
Modified residuei4953 – 49531PhosphoserineCombined sources
Modified residuei4960 – 49601PhosphoserineCombined sources
Modified residuei4986 – 49861PhosphoserineCombined sources
Modified residuei4993 – 49931PhosphoserineCombined sources
Modified residuei5009 – 50091PhosphothreonineCombined sources
Modified residuei5077 – 50771PhosphoserineCombined sources
Modified residuei5099 – 50991PhosphoserineCombined sources
Modified residuei5110 – 51101PhosphoserineCombined sources
Modified residuei5125 – 51251PhosphoserineCombined sources
Modified residuei5261 – 52611PhosphoserineCombined sources
Modified residuei5318 – 53181PhosphoserineCombined sources
Modified residuei5332 – 53321PhosphoserineCombined sources
Modified residuei5369 – 53691PhosphoserineCombined sources
Modified residuei5386 – 53861PhosphoserineCombined sources
Modified residuei5393 – 53931PhosphoserineCombined sources
Modified residuei5400 – 54001PhosphoserineCombined sources
Modified residuei5415 – 54151PhosphothreonineCombined sources
Modified residuei5448 – 54481PhosphoserineCombined sources
Modified residuei5519 – 55191PhosphoserineCombined sources
Modified residuei5530 – 55301PhosphoserineCombined sources
Modified residuei5552 – 55521PhosphoserineCombined sources
Modified residuei5577 – 55771PhosphoserineCombined sources
Modified residuei5620 – 56201PhosphoserineCombined sources
Modified residuei5641 – 56411PhosphoserineCombined sources
Modified residuei5731 – 57311PhosphoserineCombined sources
Modified residuei5739 – 57391PhosphoserineCombined sources
Modified residuei5749 – 57491PhosphoserineCombined sources
Modified residuei5752 – 57521PhosphoserineCombined sources
Modified residuei5762 – 57621PhosphoserineCombined sources
Modified residuei5763 – 57631PhosphoserineCombined sources
Modified residuei5780 – 57801PhosphoserineCombined sources
Modified residuei5782 – 57821PhosphoserineCombined sources
Modified residuei5790 – 57901PhosphoserineCombined sources
Modified residuei5793 – 57931PhosphoserineCombined sources
Modified residuei5794 – 57941PhosphothreonineCombined sources
Modified residuei5824 – 58241PhosphothreonineCombined sources
Modified residuei5830 – 58301PhosphoserineCombined sources
Modified residuei5841 – 58411PhosphoserineCombined sources
Modified residuei5845 – 58451PhosphothreonineCombined sources
Modified residuei5851 – 58511PhosphoserineCombined sources
Modified residuei5857 – 58571PhosphoserineCombined sources
Modified residuei5863 – 58631PhosphoserineCombined sources

Keywords - PTMi

Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiQ09666.
MaxQBiQ09666.
PaxDbiQ09666.
PeptideAtlasiQ09666.
PRIDEiQ09666.

PTM databases

iPTMnetiQ09666.
PhosphoSiteiQ09666.
SwissPalmiQ09666.

Expressioni

Gene expression databases

BgeeiENSG00000124942.
CleanExiHS_AHNAK.
ExpressionAtlasiQ09666. baseline and differential.
GenevisibleiQ09666. HS.

Organism-specific databases

HPAiHPA019010.
HPA019070.
HPA026643.

Interactioni

Subunit structurei

Interacts with DYSF; the interaction is direct and Ca2+-independent.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
EGFRP005333EBI-2555881,EBI-297353
NOL9Q5SY163EBI-10245106,EBI-1055462

GO - Molecular functioni

  • cadherin binding involved in cell-cell adhesion Source: BHF-UCL
  • S100 protein binding Source: UniProtKB

Protein-protein interaction databases

BioGridi122494. 103 interactions.
IntActiQ09666. 42 interactions.
MINTiMINT-4998803.
STRINGi9606.ENSP00000367263.

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4DRWX-ray3.50E/F5654-5673[»]
4FTGX-ray2.51E5654-5673[»]
4HRGX-ray2.00C/D5655-5668[»]
ProteinModelPortaliQ09666.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini9 – 9082PDZPROSITE-ProRule annotationAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi4971 – 49799Nuclear localization signalSequence analysis
Motifi5019 – 50279Nuclear localization signalSequence analysis
Motifi5034 – 50396Nuclear localization signalSequence analysis
Motifi5706 – 571611Nuclear localization signalSequence analysisAdd
BLAST
Motifi5772 – 57798Nuclear localization signalSequence analysis

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi5458 – 5654197Gly-richAdd
BLAST

Sequence similaritiesi

Contains 1 PDZ (DHR) domain.PROSITE-ProRule annotation

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiENOG410JR2V. Eukaryota.
ENOG410ZVP4. LUCA.
GeneTreeiENSGT00530000063716.
HOGENOMiHOG000033865.
HOVERGENiHBG104864.
InParanoidiQ09666.
OMAiFKMPNIK.
OrthoDBiEOG091G01FG.
PhylomeDBiQ09666.
TreeFamiTF350595.

Family and domain databases

Gene3Di2.30.42.10. 1 hit.
InterProiIPR001478. PDZ.
[Graphical view]
SMARTiSM00228. PDZ. 1 hit.
[Graphical view]
SUPFAMiSSF50156. SSF50156. 1 hit.
PROSITEiPS50106. PDZ. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q09666-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MEKEETTREL LLPNWQGSGS HGLTIAQRDD GVFVQEVTQN SPAARTGVVK
60 70 80 90 100
EGDQIVGATI YFDNLQSGEV TQLLNTMGHH TVGLKLHRKG DRSPEPGQTW
110 120 130 140 150
TREVFSSCSS EVVLSGDDEE YQRIYTTKIK PRLKSEDGVE GDLGETQSRT
160 170 180 190 200
ITVTRRVTAY TVDVTGREGA KDIDISSPEF KIKIPRHELT EISNVDVETQ
210 220 230 240 250
SGKTVIRLPS GSGAASPTGS AVDIRAGAIS ASGPELQGAG HSKLQVTMPG
260 270 280 290 300
IKVGGSGVNV NAKGLDLGGR GGVQVPAVDI SSSLGGRAVE VQGPSLESGD
310 320 330 340 350
HGKIKFPTMK VPKFGVSTGR EGQTPKAGLR VSAPEVSVGH KGGKPGLTIQ
360 370 380 390 400
APQLEVSVPS ANIEGLEGKL KGPQITGPSL EGDLGLKGAK PQGHIGVDAS
410 420 430 440 450
APQIGGSITG PSVEVQAPDI DVQGPGSKLN VPKMKVPKFS VSGAKGEETG
460 470 480 490 500
IDVTLPTGEV TVPGVSGDVS LPEIATGGLE GKMKGTKVKT PEMIIQKPKI
510 520 530 540 550
SMQDVDLSLG SPKLKGDIKV SAPGVQGDVK GPQVALKGSR VDIETPNLEG
560 570 580 590 600
TLTGPRLGSP SGKTGTCRIS MSEVDLNVAA PKVKGGVDVT LPRVEGKVKV
610 620 630 640 650
PEVDVRGPKV DVSAPDVEAH GPEWNLKMPK MKMPTFSTPG AKGEGPDVHM
660 670 680 690 700
TLPKGDISIS GPKVNVEAPD VNLEGLGGKL KGPDVKLPDM SVKTPKISMP
710 720 730 740 750
DVDLHVKGTK VKGEYDVTVP KLEGELKGPK VDIDAPDVDV HGPDWHLKMP
760 770 780 790 800
KMKMPKFSVP GFKAEGPEVD VNLPKADVDI SGPKIDVTAP DVSIEEPEGK
810 820 830 840 850
LKGPKFKMPE MNIKVPKISM PDVDLHLKGP NVKGEYDVTM PKVESEIKVP
860 870 880 890 900
DVELKSAKMD IDVPDVEVQG PDWHLKMPKM KMPKFSMPGF KAEGPEVDVN
910 920 930 940 950
LPKADVDISG PKVGVEVPDV NIEGPEGKLK GPKFKMPEMN IKAPKISMPD
960 970 980 990 1000
VDLHMKGPKV KGEYDMTVPK LEGDLKGPKV DVSAPDVEMQ GPDWNLKMPK
1010 1020 1030 1040 1050
IKMPKFSMPS LKGEGPEFDV NLSKANVDIS APKVDTNAPD LSLEGPEGKL
1060 1070 1080 1090 1100
KGPKFKMPEM HFRAPKMSLP DVDLDLKGPK MKGNVDISAP KIEGEMQVPD
1110 1120 1130 1140 1150
VDIRGPKVDI KAPDVEGQGL DWSLKIPKMK MPKFSMPSLK GEGPEVDVNL
1160 1170 1180 1190 1200
PKADVVVSGP KVDIEAPDVS LEGPEGKLKG PKFKMPEMHF KTPKISMPDV
1210 1220 1230 1240 1250
DLHLKGPKVK GDVDVSVPKV EGEMKVPDVE IKGPKMDIDA PDVEVQGPDW
1260 1270 1280 1290 1300
HLKMPKMKMP KFSMPGFKGE GREVDVNLPK ADIDVSGPKV DVEVPDVSLE
1310 1320 1330 1340 1350
GPEGKLKGPK FKMPEMHFKA PKISMPDVDL NLKGPKLKGD VDVSLPEVEG
1360 1370 1380 1390 1400
EMKVPDVDIK GPKVDISAPD VDVHGPDWHL KMPKVKMPKF SMPGFKGEGP
1410 1420 1430 1440 1450
EVDVKLPKAD VDVSGPKMDA EVPDVNIEGP DAKLKGPKFK MPEMSIKPQK
1460 1470 1480 1490 1500
ISIPDVGLHL KGPKMKGDYD VTVPKVEGEI KAPDVDIKGP KVDINAPDVE
1510 1520 1530 1540 1550
VHGPDWHLKM PKVKMPKFSM PGFKGEGPEV DMNLPKADLG VSGPKVDIDV
1560 1570 1580 1590 1600
PDVNLEAPEG KLKGPKFKMP SMNIQTHKIS MPDVGLNLKA PKLKTDVDVS
1610 1620 1630 1640 1650
LPKVEGDLKG PEIDVKAPKM DVNVGDIDIE GPEGKLKGPK FKMPEMHFKA
1660 1670 1680 1690 1700
PKISMPDVDL HLKGPKVKGD MDVSVPKVEG EMKVPDVDIK GPKVDIDAPD
1710 1720 1730 1740 1750
VEVHDPDWHL KMPKMKMPKF SMPGFKAEGP EVDVNLPKAD IDVSGPSVDT
1760 1770 1780 1790 1800
DAPDLDIEGP EGKLKGSKFK MPKLNIKAPK VSMPDVDLNL KGPKLKGEID
1810 1820 1830 1840 1850
ASVPELEGDL RGPQVDVKGP FVEAEVPDVD LECPDAKLKG PKFKMPEMHF
1860 1870 1880 1890 1900
KAPKISMPDV DLHLKGPKVK GDADVSVPKL EGDLTGPSVG VEVPDVELEC
1910 1920 1930 1940 1950
PDAKLKGPKF KMPDMHFKAP KISMPDVDLH LKGPKVKGDV DVSVPKLEGD
1960 1970 1980 1990 2000
LTGPSVGVEV PDVELECPDA KLKGPKFKMP EMHFKTPKIS MPDVDLHLKG
2010 2020 2030 2040 2050
PKVKGDMDVS VPKVEGEMKV PDVDIKGPKM DIDAPDVDVH GPDWHLKMPK
2060 2070 2080 2090 2100
MKMPKFSMPG FKAEGPEVDV NLPKADVVVS GPKVDVEVPD VSLEGPEGKL
2110 2120 2130 2140 2150
KGPKLKMPEM HFKAPKISMP DVDLHLKGPK VKGDVDVSLP KLEGDLTGPS
2160 2170 2180 2190 2200
VDVEVPDVEL ECPDAKLKGP KFKMPEMHFK TPKISMPDVN LNLKGPKVKG
2210 2220 2230 2240 2250
DMDVSVPKVE GEMKVPDVDI RGPKVDIDAP DVDVHGPDWH LKMPKMKMPK
2260 2270 2280 2290 2300
FSMPGFKGEG PEVDVNLPKA DVDVSGPKVD VEVPDVSLEG PEGKLKGPKF
2310 2320 2330 2340 2350
KMPEMHFKTP KISMPDVDFN LKGPKIKGDV DVSAPKLEGE LKGPELDVKG
2360 2370 2380 2390 2400
PKLDADMPEV AVEGPNGKWK TPKFKMPDMH FKAPKISMPD LDLHLKSPKA
2410 2420 2430 2440 2450
KGEVDVDVPK LEGDLKGPHV DVSGPDIDIE GPEGKLKGPK FKMPDMHFKA
2460 2470 2480 2490 2500
PNISMPDVDL NLKGPKIKGD VDVSVPEVEG KLEVPDMNIR GPKVDVNAPD
2510 2520 2530 2540 2550
VQAPDWHLKM PKMKMPKFSM PGFKAEGPEV DVNLPKADVD ISGPKVDIEG
2560 2570 2580 2590 2600
PDVNIEGPEG KLKGPKLKMP EMNIKAPKIS MPDFDLHLKG PKVKGDVDVS
2610 2620 2630 2640 2650
LPKVEGDLKG PEVDIKGPKV DINAPDVGVQ GPDWHLKMPK VKMPKFSMPG
2660 2670 2680 2690 2700
FKGEGPDGDV KLPKADIDVS GPKVDIEGPD VNIEGPEGKL KGPKFKMPEM
2710 2720 2730 2740 2750
NIKAPKISMP DIDLNLKGPK VKGDVDVSLP KVEGDLKGPE VDIKGPKVDI
2760 2770 2780 2790 2800
DAPDVDVHGP DWHLKMPKIK MPKISMPGFK GEGPDVDVNL PKADIDVSGP
2810 2820 2830 2840 2850
KVDVECPDVN IEGPEGKWKS PKFKMPEMHF KTPKISMPDI DLNLTGPKIK
2860 2870 2880 2890 2900
GDVDVTGPKV EGDLKGPEVD LKGPKVDIDV PDVNVQGPDW HLKMPKMKMP
2910 2920 2930 2940 2950
KFSMPGFKAE GPEVDVNLPK ADVDVSGPKV DVEGPDVNIE GPEGKLKGPK
2960 2970 2980 2990 3000
FKMPEMNIKA PKIPMPDFDL HLKGPKVKGD VDISLPKVEG DLKGPEVDIR
3010 3020 3030 3040 3050
GPQVDIDVPD VGVQGPDWHL KMPKVKMPKF SMPGFKGEGP DVDVNLPKAD
3060 3070 3080 3090 3100
LDVSGPKVDI DVPDVNIEGP EGKLKGPKFK MPEMNIKAPK ISMPDIDLNL
3110 3120 3130 3140 3150
KGPKVKGDMD VSLPKVEGDM KVPDVDIKGP KVDINAPDVD VQGPDWHLKM
3160 3170 3180 3190 3200
PKIKMPKISM PGFKGEGPEV DVNLPKADLD VSGPKVDVDV PDVNIEGPDA
3210 3220 3230 3240 3250
KLKGPKFKMP EMNIKAPKIS MPDLDLNLKG PKMKGEVDVS LANVEGDLKG
3260 3270 3280 3290 3300
PALDIKGPKI DVDAPDIDIH GPDAKLKGPK LKMPDMHVNM PKISMPEIDL
3310 3320 3330 3340 3350
NLKGSKLKGD VDVSGPKLEG DIKAPSLDIK GPEVDVSGPK LNIEGKSKKS
3360 3370 3380 3390 3400
RFKLPKFNFS GSKVQTPEVD VKGKKPDIDI TGPKVDINAP DVEVQGKVKG
3410 3420 3430 3440 3450
SKFKMPFLSI SSPKVSMPDV ELNLKSPKVK GDLDIAGPNL EGDFKGPKVD
3460 3470 3480 3490 3500
IKAPEVNLNA PDVDVHGPDW NLKMPKMKMP KFSVSGLKAE GPDVAVDLPK
3510 3520 3530 3540 3550
GDINIEGPSM NIEGPDLNVE GPEGGLKGPK FKMPDMNIKA PKISMPDIDL
3560 3570 3580 3590 3600
NLKGPKVKGD VDISLPKLEG DLKGPEVDIK GPKVDINAPD VDVHGPDWHL
3610 3620 3630 3640 3650
KMPKVKMPKF SMPGFKGEGP EVDVTLPKAD IDISGPNVDV DVPDVNIEGP
3660 3670 3680 3690 3700
DAKLKGPKFK MPEMNIKAPK ISMPDFDLNL KGPKMKGDVV VSLPKVEGDL
3710 3720 3730 3740 3750
KGPEVDIKGP KVDIDTPDIN IEGSEGKFKG PKFKIPEMHL KAPKISMPDI
3760 3770 3780 3790 3800
DLNLKGPKVK GDVDVSLPKM EGDLKGPEVD IKGPKVDINA PDVDVQGPDW
3810 3820 3830 3840 3850
HLKMPKVKMP KFSMPGFKGE GPDVDVNLPK ADLDVSGPKV DIDVPDVNIE
3860 3870 3880 3890 3900
GPEGKLKGPK FKMPEMNIKA PKISMPDIDL NLKGPKVKGD MDVSLPKVEG
3910 3920 3930 3940 3950
DMQVPDLDIK GPKVDINAPD VDVRGPDWHL KMPKIKMPKI SMPGFKGEGP
3960 3970 3980 3990 4000
EVDVNLPKAD LDVSGPKVDV DVPDVNIEGP DAKLKGPKFK MPEMNIKAPK
4010 4020 4030 4040 4050
ISMPDFDLHL KGPKVKGDVD VSLPKMEGDL KAPEVDIKGP KVDIDAPDVD
4060 4070 4080 4090 4100
VHGPDWHLKM PKVKMPKFSM PGFKGEGPEV DVNLPKADID VSGPKVDIDT
4110 4120 4130 4140 4150
PDIDIHGPEG KLKGPKFKMP DLHLKAPKIS MPEVDLNLKG PKMKGDVDVS
4160 4170 4180 4190 4200
LPKVEGDLKG PEVDIKGPKV DIDVPDVDVQ GPDWHLKMPK VKMPKFSMPG
4210 4220 4230 4240 4250
FKGEGPDVDV NLPKADLDVS GPKVDIDVPD VNIEGPDAKL KGPKFKMPEM
4260 4270 4280 4290 4300
NIKAPKISMP DFDLHLKGPK VKGDVDVSLP KVEGDLKGPE VDIKGPKVDI
4310 4320 4330 4340 4350
DAPDVDVHGP DWHLKMPKVK MPKFSMPGFK GEGPDVDVTL PKADIEISGP
4360 4370 4380 4390 4400
KVDIDAPDVS IEGPDAKLKG PKFKMPEMNI KAPKISMPDI DFNLKGPKVK
4410 4420 4430 4440 4450
GDVDVSLPKV EGDLKGPEID IKGPSLDIDT PDVNIEGPEG KLKGPKFKMP
4460 4470 4480 4490 4500
EMNIKAPKIS MPDFDLHLKG PKVKGDVDVS LPKVESDLKG PEVDIEGPEG
4510 4520 4530 4540 4550
KLKGPKFKMP DVHFKSPQIS MSDIDLNLKG PKIKGDMDIS VPKLEGDLKG
4560 4570 4580 4590 4600
PKVDVKGPKV GIDTPDIDIH GPEGKLKGPK FKMPDLHLKA PKISMPEVDL
4610 4620 4630 4640 4650
NLKGPKVKGD MDISLPKVEG DLKGPEVDIR DPKVDIDVPD VDVQGPDWHL
4660 4670 4680 4690 4700
KMPKVKMPKF SMPGFKGEGP DVDVNLPKAD IDVSGPKVDV DVPDVNIEGP
4710 4720 4730 4740 4750
DAKLKGPKFK MPEMSIKAPK ISMPDIDLNL KGPKVKGDVD VTLPKVEGDL
4760 4770 4780 4790 4800
KGPEADIKGP KVDINTPDVD VHGPDWHLKM PKVKMPKFSM PGFKGEGPDV
4810 4820 4830 4840 4850
DVSLPKADID VSGPKVDVDI PDVNIEGPDA KLKGPKFKMP EINIKAPKIS
4860 4870 4880 4890 4900
IPDVDLDLKG PKVKGDFDVS VPKVEGTLKG PEVDLKGPRL DFEGPDAKLS
4910 4920 4930 4940 4950
GPSLKMPSLE ISAPKVTAPD VDLHLKAPKI GFSGPKLEGG EVDLKGPKVE
4960 4970 4980 4990 5000
APSLDVHMDS PDINIEGPDV KIPKFKKPKF GFGAKSPKAD IKSPSLDVTV
5010 5020 5030 5040 5050
PEAELNLETP EISVGGKGKK SKFKMPKIHM SGPKIKAKKQ GFDLNVPGGE
5060 5070 5080 5090 5100
IDASLKAPDV DVNIAGPDAA LKVDVKSPKT KKTMFGKMYF PDVEFDIKSP
5110 5120 5130 5140 5150
KFKAEAPLPS PKLEGELQAP DLELSLPAIH VEGLDIKAKA PKVKMPDVDI
5160 5170 5180 5190 5200
SVPKIEGDLK GPKVQANLGA PDINIEGLDA KVKTPSFGIS APQVSIPDVN
5210 5220 5230 5240 5250
VNLKGPKIKG DVPSVGLEGP DVDLQGPEAK IKFPK