Q24742 · TRX_DROVI
- ProteinHistone-lysine N-methyltransferase trithorax
- Genetrx
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids3828 (go to sequence)
- Protein existenceInferred from homology
- Annotation score5/5
Function
function
Histone methyltransferase that methylates 'Lys-4' of histone H3 (H3K4me). H3K4me represents a specific tag for epigenetic transcriptional activation. Functions in segment determination through interaction with genes of bithorax (BX-C) and antennapedia (ANT-C) complexes. Acts as an activator of BX-C. Involved in the very early regulation of homeotic genes expressed only in the posterior region of the embryo.
Catalytic activity
- L-lysyl9-[histone H3] + 3 S-adenosyl-L-methionine = N6,N6,N6-trimethyl-L-lysyl9-[histone H3] + 3 S-adenosyl-L-homocysteine + 3 H+
Features
Showing features for dna binding, binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
DNA binding | 725-839 | Nuclear receptor | ||||
Sequence: ASTCAVCSAPVNNKDAPLARKYGVIACEVCRKFNSRMTKISKLSTPMHSNPSTSTAQSGQQLKCTDGGNCSILSLKSQLKNFKKLYKERCKACWLKKCLATLQLPAGHRSRLSAI | ||||||
Binding site | 3700 | S-adenosyl-L-methionine (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 3702 | S-adenosyl-L-methionine (UniProtKB | ChEBI) | ||||
Sequence: R | ||||||
Binding site | 3744 | S-adenosyl-L-methionine (UniProtKB | ChEBI) | ||||
Sequence: Y | ||||||
Binding site | 3767-3768 | S-adenosyl-L-methionine (UniProtKB | ChEBI) | ||||
Sequence: NH | ||||||
Binding site | 3770 | Zn2+ (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 3816 | Zn2+ (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 3818 | Zn2+ (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 3823 | Zn2+ (UniProtKB | ChEBI) | ||||
Sequence: C |
GO annotations
all annotations | all molecular function | virus receptor activity | dna binding | rna binding | cytoskeletal motor activity | catalytic activity | gtpase activity | structural molecule activity | transporter activity | cytoskeletal protein binding | lipid binding | cyclase activity | antioxidant activity | oxidoreductase activity | transferase activity | hydrolase activity | lyase activity | isomerase activity | ligase activity | protein tag activity | cargo receptor activity | histone binding | protein folding chaperone | translation regulator activity | nutrient reservoir activity | receptor ligand activity | molecular transducer activity | molecular adaptor activity | toxin activity | cell adhesion mediator activity | molecular function regulator activity | virus coreceptor activity | catalytic activity, acting on a protein | catalytic activity, acting on dna | catalytic activity, acting on rna | molecular carrier activity | transcription regulator activity | general transcription initiation factor activity | molecular sensor activity | molecular sequestering activity | atp-dependent activity | other molecular function | all biological process | mitotic cell cycle | cytokinesis | cytoplasmic translation | immune system process | muscle system process | circulatory system process | renal system process | respiratory system process | carbohydrate metabolic process | generation of precursor metabolites and energy | dna replication | dna repair | dna recombination | chromatin organization | dna-templated transcription | regulation of dna-templated transcription | trna metabolic process | protein folding | protein glycosylation | amino acid metabolic process | modified amino acid metabolic process | lipid metabolic process | vitamin metabolic process | sulfur compound metabolic process | intracellular protein transport | nucleocytoplasmic transport | autophagy | inflammatory response | mitochondrion organization | cytoskeleton organization | microtubule-based movement | peroxisome organization | lysosome organization | chromosome segregation | cell adhesion | establishment or maintenance of cell polarity | programmed cell death | photosynthesis | mrna metabolic process | snrna metabolic process | vesicle-mediated transport | reproductive process | digestive system process | signaling | cell differentiation | protein catabolic process | extracellular matrix organization | regulatory ncrna-mediated gene silencing | telomere organization | cell junction organization | wound healing | ribosome biogenesis | cilium organization | anatomical structure development | cell motility | nervous system process | endocrine process | protein maturation | transmembrane transport | nucleobase-containing small molecule metabolic process | hepaticobiliary system process | membrane organization | protein-containing complex assembly | cell wall organization or biogenesis | nitrogen cycle metabolic process | protein localization to plasma membrane | defense response to other organism | detoxification | meiotic nuclear division | mitotic nuclear division | mitochondrial gene expression | carbohydrate derivative metabolic process | other biological process | all cellular component | nuclear chromosome | extracellular region | extracellular space | cell wall | nucleus | nuclear envelope | nucleoplasm | chromosome | nucleolus | mitochondrion | lysosome | endosome | vacuole | peroxisome | endoplasmic reticulum | golgi apparatus | lipid droplet | microtubule organizing center | cytosol | ribosome | cytoskeleton | plasma membrane | cilium | plastid | thylakoid | external encapsulating structure | extracellular matrix | cytoplasmic vesicle | organelle | other cellular component | |||
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Aspect | Term | |
---|---|---|
Cellular Component | histone acetyltransferase complex | |
Cellular Component | MLL1/2 complex | |
Cellular Component | polytene chromosome band | |
Cellular Component | transcription elongation factor complex | |
Molecular Function | chromatin binding | |
Molecular Function | DNA-binding transcription factor activity | |
Molecular Function | histone H3K4 methyltransferase activity | |
Molecular Function | histone H3K9 trimethyltransferase activity | |
Molecular Function | protein homodimerization activity | |
Molecular Function | protein phosphatase 1 binding | |
Molecular Function | protein-cysteine methyltransferase activity | |
Molecular Function | sequence-specific DNA binding | |
Molecular Function | zinc ion binding | |
Biological Process | eye development | |
Biological Process | germ cell migration | |
Biological Process | haltere development | |
Biological Process | heart development | |
Biological Process | methylation | |
Biological Process | positive regulation of transcription elongation by RNA polymerase II |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameHistone-lysine N-methyltransferase trithorax
- EC number
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Ecdysozoa > Arthropoda > Hexapoda > Insecta > Pterygota > Neoptera > Endopterygota > Diptera > Brachycera > Muscomorpha > Ephydroidea > Drosophilidae > Drosophila
Accessions
- Primary accessionQ24742
Subcellular Location
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000124875 | 1-3828 | Histone-lysine N-methyltransferase trithorax | |||
Sequence: MGRSKFPGNPSKSINRKRISVLQLEDEAASAAAAAAAATAATTEQHQQSEQSAGSSASREKGNNCDNDDDDNAPSGAATSGNRGASSGASDAAPEGGNSYGNGSSTGSKTTNGGNVNGGSHHKSATAPAELKECKNQGNQIEPNNCIAAEPDGTEDTNNDDDDDSSNDKKPTAAAAAAAAAAFVPGPSALQRARKGGNKKFKNLNLARPEVMLPSTSKLKQQQQQQLQLNCPSASASSLSSSAAAAAAAAAPTTTTTTASASATLTATATSTSTSSLPGTPLSVIAGGGGGAAAAALLLANPFASVETKVVEVNAAATAAATAAATAAAGAGEDVGMLKASIEMANEAGLEAPAVAVKSSGSSPNPNHNPNAVAGSTSAAAPGAPTATKQKKTVTFKNILETSDDKSVVKRFYNPDNRVPLVSIMKKDSLNRPLNYCRGSEFIVRPSILSKILNKNSNIDKLNSLKFRSVHASSNSIQESSSSTTNLFGSGLSRAFGAPIDDEDAVSGGVTFRKQEPQHKTPEDNDDDGSASSDAIEDDEDIDDDDAEENEEAASEKSAETTASVDEKEADDRQLVMDKHFVLPKRSTRSSRIIKPNKRLLEVGGICSKRSPSDANGKPKPKNYFGLATLPAKCTPRRRRSAATALSQKLGKETFASFATAKVNSSFVLRQPRLQFQTDKSRSFVSAKPTLPTTTVLPASSSAITSANVLSFGALNNANSAVAAASTCAVCSAPVNNKDAPLARKYGVIACEVCRKFNSRMTKISKLSTPMHSNPSTSTAQSGQQLKCTDGGNCSILSLKSQLKNFKKLYKERCKACWLKKCLATLQLPAGHRSRLSAILPASMREEVAPKDDKCPELLSPTASLRFTAPTSSASSGTTIKWKSSAETAVNSIKSNPLAENNVTFGGTPLLRPAILEKPLFLKIGSDNKKAKESKEALGLSPVPSTSEAAVAPGKTTRKAKQDKEKARELEAEKPLSPNAKKTTEANTPETQKDEQPASTTTTVSAASSSTSHTSSAATNSSQLETTEAANASAVPDNLKRQRIDLKGPRVKHVCRSASIVLGQPLATFGDEEEELAAAEAGPAPTTTTTTTSPEVIIKKPKSPQPMQMIIDENDNCASCILTPTEATAEAQPAVKSVLESRSSKSNTQTEAKKTPATSGSSKGKVTTRNATATVTSVASSLVATKKQRNIEVSSSISSSQAAATQSRRALAKEVNRLKALISIDFWENYDPAEVCQTGFGLIVTETVAQRALCFLCGSTGLDPLIFCACCCEPYHQYCVLDEYNLKHSSFEDTLMTSLLETSNNACAISAATNTALNQLTQRLNWLCPRCTVCYTCNMSSGSKVKCQKCQKNYHSTCLGTSKRLLGADRPLICVNCLKCKSCATTKVSKFVGNLPMCTACFKLRKKGNFCPICQKCYDDNDFDLKMMECGDCNQWVHSKCEGLSDEQYNLLSTLPESIEFICKKCARRCDVSRNKADEWRQAVMEEFKSSLYSVLKLLSKSRQACALLKLSPRKNWRCCSAGAQPAKAHSQGKLQPKALQFTYNGLGSDGESQNSDDIYEFKEQHSTNRKPSTPVPCSCLQPLSQSPSFSLVDIKQKIASNAYVSLAEFNYDMSQVIQQSNCDELDIAYKELLSEQFPWFQNETKACTDALEEDMFESCGYEELKESPTTYAEHHTASQAPRTGLLDIPLDDVDDLGGCAVKTRLDTRVCLFCRKSGEGLSGEEARLLYCGHDCWVHINCAMWSAEVFEEIDGSLQNVHSAVARGRMIKCTVCGNRGATVGCNVKSCGEHYHYPCARTIDCAFLTDKSMYCPAHARNALKANGSPSVTYESNFEVSRPVYVELERKRKKLIVPAKVQFHIGSVAVRQLGSIVPRFSDSFEAIVPINFLCSRLYWSSKEPWKIVEYTVRTTIQNSYSSTLTLDAGRNFTVDHTNPNCSLVQLGLAQIARWHSSLARSDLLDTDWAEFPNSYVPADENTEEEPQQNADLLPPEIKDAIFEDLPHELLDGISMLDIFMYEDLGDKTELFAMSEQSKDGTTATSQAGGASVIICDEDTRNSNSLNKHLVLSNCCTASNPVDDAMLCAARSSSQEKECGDVLKKTDTAPTRSWPKLDGGSVAAFKRRKLSKNIAEGVLLSLNQRSKKEMATVAGITRRQSVCGSSELPAEGSATMRTKSFTWSAAKCLFEKNESREEPAKLTIMQMDGVDDSITEYRIIGSDGNLSTAQFTGQVKCERCQCTYRNYDSFQRHLGSCEPMSTSESESETATGTAQLSAESLNELQKQALAAATLSNTGGLNYLQTSFPQVQNLATLGQFGVQGLQGLQTLQLQPQSLGNGFFLSQPNAAQATSNGNDVLQLYANSLQNLAANLGGGFTLTQPTMSTQAQPQLIALSTNPDGTQQFIQLPQSNGATTQLLQTAAPLRCNATYQTLQATNSDKKIVLLFLEAGDPLQEVVTQAAQQATAAAHQKQLKSGHGVKPIQAKLQGQQQQQRHQQHQQHQQHQQQQQQQQQQQQQQQTPITVAQHGGTTQLLGQNLLQPQLLFQSNAQPQTQQLLLPQTQAQNIISFVTGDGSQNQPLQYISIPTTNDFKPQQTTSTPTFLTAPGGGATFLQTDASGNLMLTTAPANSGLQMLTGQLQTQPQVIGTLIQPQTLQLTTGADGTQTATAQQPLILGGATGGGTTGLEFATAPQVILATQPMYYGLETIVQNTVMSSQQFVSTAMPGVLSQNSSFSATTTQVFQASKIEPIVDLPAGYVVLNNAVDASGNTSWLQQSQTQATDDATAQLLQNAGFQFQTTPTTSTQQTMSTDYAPPLVVTAKVPPVAQMKRNTNANKSPISVLSKVQPQPQQSQVVNKVLPTNVIQQQQQQQQQQQQQQQQMQPKQQLAGNANLKLTSQFQRQQQANELKNKQAAGQQTGSTCGAPPSIASKPLQKKTNLIRPIHKVEVKPKIMKQAPKLATSAASMQHHQQQQSPAAINQVAKVALLQQRLAPAPQPQQQEPQEEQQHLHQQQQQQQQQQQHMQQHQQQQQQLSMPQLLRAQQPIISIVNTAEPQAATQFVIRPALQAQAQPIQLQEQQSQQQQQQPAEQLINGKAARLQRYASNSLPTNVVNPLQQQRCASANNSSNSNVTQQNSTITINSRPTNRVLPMQQRQEPTPLSNDVVVQSPTPPKPIEEPVPAGASTQKPIVKCYAQLEQKSPGYETELKTNITLDNLEQTNSITTMQLQQPQQGPIYGEQIFEKQSEAQVQLEKPKHNDLMLLEATSCQQQQQQQQHMEMVVDNGFQLTSNESCLLEKHGFNVEAVPMDTEDHYASMKNGSGGGAAEGIGQVDDAEEDEDDDDDFSLKMATSACNDHEMSDSEEPAVKEKISKILDNLTNDDCSDSIATATTVEASAGYQQMVEDVLATTAAGSVSTDDETFTATAEAVEAAASYINEMAEAHELQLKQLQAGVELDLKKPKLDVPQQQPDTVPPNVVPTAAAPQQPPPMRDPKKISGPHLLYEIQSEDGFTYKSSSIAEIWEKVFEAVQVARRAHGLTPLPEGPLADMSGVQMIGLKTNALKYLIEQLPGVEKCVKYTPKYHKRNGNVSTAAGGGHARTAGSNPAALAAGAESLIDYGSDQEELQENAYECARCEPYVSRSEYDMFSWLASRHRKQPIQVFVQPSDNELVPRRGTGSNLPMAMKYRTLKETYKDYVGVFRSHIHGRGLYCTKDIEAGEMVIEYAGELIRSTLTDKRERYYDSRGIGCYMFKIDDNLVVDATMRGNAARFINHSCEPNCYSKVVDILGHKHIIIFALRRIVQGEELTYDYKFPFEDEKIPCSCGSKRCRKYLN |
Interaction
Subunit
Interacts with ash1 via its SET domain.
Family & Domains
Features
Showing features for region, compositional bias, zinc finger, domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 25-179 | Disordered | ||||
Sequence: EDEAASAAAAAAAATAATTEQHQQSEQSAGSSASREKGNNCDNDDDDNAPSGAATSGNRGASSGASDAAPEGGNSYGNGSSTGSKTTNGGNVNGGSHHKSATAPAELKECKNQGNQIEPNNCIAAEPDGTEDTNNDDDDDSSNDKKPTAAAAAAA | ||||||
Compositional bias | 40-61 | Polar residues | ||||
Sequence: AATTEQHQQSEQSAGSSASREK | ||||||
Compositional bias | 69-87 | Polar residues | ||||
Sequence: DDDNAPSGAATSGNRGASS | ||||||
Compositional bias | 97-122 | Polar residues | ||||
Sequence: GNSYGNGSSTGSKTTNGGNVNGGSHH | ||||||
Region | 356-390 | Disordered | ||||
Sequence: AVKSSGSSPNPNHNPNAVAGSTSAAAPGAPTATKQ | ||||||
Compositional bias | 358-390 | Polar residues | ||||
Sequence: KSSGSSPNPNHNPNAVAGSTSAAAPGAPTATKQ | ||||||
Region | 512-589 | Disordered | ||||
Sequence: FRKQEPQHKTPEDNDDDGSASSDAIEDDEDIDDDDAEENEEAASEKSAETTASVDEKEADDRQLVMDKHFVLPKRSTR | ||||||
Compositional bias | 528-553 | Acidic residues | ||||
Sequence: DGSASSDAIEDDEDIDDDDAEENEEA | ||||||
Compositional bias | 561-585 | Basic and acidic residues | ||||
Sequence: TTASVDEKEADDRQLVMDKHFVLPK | ||||||
Region | 933-1036 | Disordered | ||||
Sequence: ESKEALGLSPVPSTSEAAVAPGKTTRKAKQDKEKARELEAEKPLSPNAKKTTEANTPETQKDEQPASTTTTVSAASSSTSHTSSAATNSSQLETTEAANASAVP | ||||||
Compositional bias | 957-978 | Basic and acidic residues | ||||
Sequence: TRKAKQDKEKARELEAEKPLSP | ||||||
Compositional bias | 980-1033 | Polar residues | ||||
Sequence: AKKTTEANTPETQKDEQPASTTTTVSAASSSTSHTSSAATNSSQLETTEAANAS | ||||||
Region | 1075-1094 | Disordered | ||||
Sequence: ELAAAEAGPAPTTTTTTTSP | ||||||
Region | 1131-1170 | Disordered | ||||
Sequence: AQPAVKSVLESRSSKSNTQTEAKKTPATSGSSKGKVTTRN | ||||||
Compositional bias | 1137-1170 | Polar residues | ||||
Sequence: SVLESRSSKSNTQTEAKKTPATSGSSKGKVTTRN | ||||||
Zinc finger | 1251-1334 | PHD-type 1 | ||||
Sequence: RALCFLCGSTGLDPLIFCACCCEPYHQYCVLDEYNLKHSSFEDTLMTSLLETSNNACAISAATNTALNQLTQRLNWLCPRCTVC | ||||||
Zinc finger | 1335-1380 | PHD-type 2 | ||||
Sequence: YTCNMSSGSKVKCQKCQKNYHSTCLGTSKRLLGADRPLICVNCLKC | ||||||
Zinc finger | 1408-1469 | PHD-type 3 | ||||
Sequence: GNFCPICQKCYDDNDFDLKMMECGDCNQWVHSKCEGLSDEQYNLLSTLPESIEFICKKCARR | ||||||
Zinc finger | 1708-1748 | C2HC pre-PHD-type | ||||
Sequence: TRVCLFCRKSGEGLSGEEARLLYCGHDCWVHINCAMWSAEV | ||||||
Zinc finger | 1769-1816 | PHD-type 4 | ||||
Sequence: IKCTVCGNRGATVGCNVKSCGEHYHYPCARTIDCAFLTDKSMYCPAHA | ||||||
Domain | 1856-1913 | FYR N-terminal | ||||
Sequence: KVQFHIGSVAVRQLGSIVPRFSDSFEAIVPINFLCSRLYWSSKEPWKIVEYTVRTTIQ | ||||||
Region | 2252-2272 | Disordered | ||||
Sequence: CEPMSTSESESETATGTAQLS | ||||||
Region | 2464-2510 | Disordered | ||||
Sequence: AHQKQLKSGHGVKPIQAKLQGQQQQQRHQQHQQHQQHQQQQQQQQQQ | ||||||
Compositional bias | 2480-2510 | Polar residues | ||||
Sequence: AKLQGQQQQQRHQQHQQHQQHQQQQQQQQQQ | ||||||
Region | 2826-2848 | Disordered | ||||
Sequence: RNTNANKSPISVLSKVQPQPQQS | ||||||
Compositional bias | 2897-2930 | Polar residues | ||||
Sequence: RQQQANELKNKQAAGQQTGSTCGAPPSIASKPLQ | ||||||
Region | 2897-2973 | Disordered | ||||
Sequence: RQQQANELKNKQAAGQQTGSTCGAPPSIASKPLQKKTNLIRPIHKVEVKPKIMKQAPKLATSAASMQHHQQQQSPAA | ||||||
Compositional bias | 2956-2973 | Polar residues | ||||
Sequence: ATSAASMQHHQQQQSPAA | ||||||
Region | 2988-3031 | Disordered | ||||
Sequence: APAPQPQQQEPQEEQQHLHQQQQQQQQQQQHMQQHQQQQQQLSM | ||||||
Compositional bias | 3117-3164 | Polar residues | ||||
Sequence: ASANNSSNSNVTQQNSTITINSRPTNRVLPMQQRQEPTPLSNDVVVQS | ||||||
Region | 3117-3178 | Disordered | ||||
Sequence: ASANNSSNSNVTQQNSTITINSRPTNRVLPMQQRQEPTPLSNDVVVQSPTPPKPIEEPVPAG | ||||||
Region | 3314-3338 | Disordered | ||||
Sequence: NGSGGGAAEGIGQVDDAEEDEDDDD | ||||||
Region | 3457-3487 | Disordered | ||||
Sequence: KLDVPQQQPDTVPPNVVPTAAAPQQPPPMRD | ||||||
Domain | 3493-3577 | FYR C-terminal | ||||
Sequence: GPHLLYEIQSEDGFTYKSSSIAEIWEKVFEAVQVARRAHGLTPLPEGPLADMSGVQMIGLKTNALKYLIEQLPGVEKCVKYTPKY | ||||||
Domain | 3690-3806 | SET | ||||
Sequence: DYVGVFRSHIHGRGLYCTKDIEAGEMVIEYAGELIRSTLTDKRERYYDSRGIGCYMFKIDDNLVVDATMRGNAARFINHSCEPNCYSKVVDILGHKHIIIFALRRIVQGEELTYDYK | ||||||
Domain | 3812-3828 | Post-SET | ||||
Sequence: EKIPCSCGSKRCRKYLN |
Sequence similarities
Belongs to the class V-like SAM-binding methyltransferase superfamily. Histone-lysine methyltransferase family. TRX/MLL subfamily.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length3,828
- Mass (Da)413,724
- Last updated1996-11-01 v1
- Checksum32059CF303A3C504
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 40-61 | Polar residues | ||||
Sequence: AATTEQHQQSEQSAGSSASREK | ||||||
Compositional bias | 69-87 | Polar residues | ||||
Sequence: DDDNAPSGAATSGNRGASS | ||||||
Compositional bias | 97-122 | Polar residues | ||||
Sequence: GNSYGNGSSTGSKTTNGGNVNGGSHH | ||||||
Compositional bias | 358-390 | Polar residues | ||||
Sequence: KSSGSSPNPNHNPNAVAGSTSAAAPGAPTATKQ | ||||||
Compositional bias | 528-553 | Acidic residues | ||||
Sequence: DGSASSDAIEDDEDIDDDDAEENEEA | ||||||
Compositional bias | 561-585 | Basic and acidic residues | ||||
Sequence: TTASVDEKEADDRQLVMDKHFVLPK | ||||||
Compositional bias | 957-978 | Basic and acidic residues | ||||
Sequence: TRKAKQDKEKARELEAEKPLSP | ||||||
Compositional bias | 980-1033 | Polar residues | ||||
Sequence: AKKTTEANTPETQKDEQPASTTTTVSAASSSTSHTSSAATNSSQLETTEAANAS | ||||||
Compositional bias | 1137-1170 | Polar residues | ||||
Sequence: SVLESRSSKSNTQTEAKKTPATSGSSKGKVTTRN | ||||||
Compositional bias | 2480-2510 | Polar residues | ||||
Sequence: AKLQGQQQQQRHQQHQQHQQHQQQQQQQQQQ | ||||||
Compositional bias | 2897-2930 | Polar residues | ||||
Sequence: RQQQANELKNKQAAGQQTGSTCGAPPSIASKPLQ | ||||||
Compositional bias | 2956-2973 | Polar residues | ||||
Sequence: ATSAASMQHHQQQQSPAA | ||||||
Compositional bias | 3117-3164 | Polar residues | ||||
Sequence: ASANNSSNSNVTQQNSTITINSRPTNRVLPMQQRQEPTPLSNDVVVQS |