wanglab/gogpt-training-data huggingface dataset:
Protein: Serine/threonine-protein kinase max-2 (EC 2.7.11.1) (Motor axon guidance protein 2) (p21-activated kinase) (G5EGQ3)
Organism: Caenorhabditis elegans
Function: Serine/threonine-protein kinase, which phosphorylates mlk-1. Involved in the stress response to heavy metals by activating the mlk-1/mek-1/kgb-1 pathway. In ventral cord commissural motoneurons, required for dorsal axon guidance downstream of unc-6/netrin repulsion receptor unc-5 and probably of Rho GTPases ced-10 and mig-2. Plays a redundant role with mig-10 in orientating axonal growth of HSN neurons. Plays a redundant role with pak-1 in P neuroblast migration and in distal tip cell (DTC)-mediated guidance of gonad elongation probably downstream of Rho GTPases. In association with pak-2, plays a role in embryogenesis. In association with pak-1, may be involved in spermatogenesis.
Subcellular location: Perikaryon {ECO:0000269|PubMed:17050621}. Cell projection, dendrite {ECO:0000269|PubMed:17050621}. Cytoplasm {ECO:0000269|PubMed:19023419}.
Interaction partners:
- Cell division control protein 42 homolog
- Ras-related protein ced-10
- Arf-GAP domain-containing protein
- SH3 domain-containing protein
- Ras-related protein rac-2
- Ras-like GTP-binding protein rhoA
- Rac-like GTPase
- CHp/Wrch Rho-like protein homolog
- Actin
- Serine/threonine-protein kinase pak-1
Sequence:
MSTSKSSKVRIRNFIGRIFSPSDKDKDRDDEMKPSSSAMDISQPYNTVHRVHVGYDGQKFSGLPQPWMDILLRDISLADQKKDPNAVVTALKFYAQSMKENEKTKFMTTNSVFTNSDDDDVDVQLTGQVTEHLRNLQCSNGSATSPSTSVSASSSSARPLTNGNNHLSTASSTDTSLSLSERNNVPSPAPVPYSESAPQLKTFTGETPKLHPRSPFPPQPPVLPQRSKTASAVATTTTNPTTSNGAPPPVPGSKGPPVPPKPSHLKIASSTVSSGCSSPQQYSSARSVGNSLSNGSVVSTTSSDGDVQLSNKENSNDKSVGDKNGNTTTNKTTVEPPPPEEPPVRVRASHREKLSDSEVLNQLREIVNPSNPLGKYEMKKQIGVGASGTVFVANVAGSTDVVAVKRMAFKTQPKKEMLLTEIKVMKQYRHPNLVNYIESYLVDADDLWVVMDYLEGGNLTDVVVKTELDEGQIAAVLQECLKALHFLHRHSIVHRDIKSDNVLLGMNGEVKLTDMGFCAQIQPGSKRDTVVGTPYWMSPEILNKKQYNYKVDIWSLGIMALEMIDGEPPYLRETPLKAIYLIAQNGKPEIKQRDRLSSEFNNFLDKCLVVDPDQRADTTELLAHPFLKKAKPLSSLIPYIRAVREK
Protein: Actin-related protein 10 (Actin-related protein 11) (Q9QZB7)
Organism: Mus musculus (Mouse)
Function: Part of the dynactin complex that activates the molecular motor dynein for ultra-processive transport along microtubules.
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:I3LHK5}.
Interaction partners:
- Dynactin subunit 6
- Dynactin subunit 4
- Dynactin subunit 2
- Dynactin subunit 5
- Dynactin subunit 1
- Alpha-centractin
- Dynactin subunit 3
- Beta-centractin
- Actin, cytoplasmic 1
- Cytoplasmic dynein 1 intermediate chain 2
Sequence:
MPLYEGLGSGGEKTAVVIDLGEAFTKCGFAGETGPRCIIPSVIKRAGMSKPIKVVQYNINTEELYSYLKEFIHILYFRHLLVNPRDRRVVVIESVLCPSHFRETLTRVLFKYFEVPSVLLAPSHLMALLTLGINSAMVLDCGYRESLVLPIYEGIPILNCWGALPLGGKALHKELETQLLEQCTVDTGAAKGQSLPSVMGSVPEGVLEDIKVRTCFVSDLKRGLQIQAAKFNIDGNNERPTPPPNVDYPLDGEKILHVLGSIRDSVVEILFEQDNEEKSVATLILDSLLQCPIDTRKQLAENLVIIGGTSMLPGFLHRLLAEIRYLVEKPKYKKTLGTKNFRIHTPPAKANCVAWLGGAVFGALQDILGSRSISKEYYNQTGRIPDWCSLNNPPLEMMFDVGKAQPPLMKRAFSTEK
Protein: Transcription cofactor vestigial-like protein 2 (Vgl-2) (Protein VITO1) (Q8BGW8)
Organism: Mus musculus (Mouse)
Function: May act as a specific coactivator for the mammalian TEFs. May play a role in the development of skeletal muscles.
Subcellular location: Nucleus {ECO:0000269|PubMed:12376544}.
Interaction partners:
Sequence:
MSCLDVMYQVYGPPQPYFAAAYTPYHQKLAYYSKMQEAQECASPGSSASGSSSFSNPTPASVKEEEGSPEKERPPEAEYINSRCVLFTYFQGDISSVVDEHFSRALSHPSSYTPSCTSSKAHRSSGPWRAEGTFPMSQRSFPASFWNSAYQAPVPAPLGSPLAAAHSELPFATDPYSPATLHGHLHQGAADWHHAHPHHAHPHHPYALGGALGAQASAYPRPAVHEVYAPHFDPRYGPLLMPAATGRPGRLAPASAPAPGSPPCELAAKGEPAGSAWAAPGGPFVSPTGDVAQSLGLSVDSGKRRRECSLPSAPPALYPTLG
Protein: 1,4-alpha-glucan-branching enzyme (EC 2.4.1.18) (Brancher enzyme) (Glycogen-branching enzyme) (Q04446)
Organism: Homo sapiens (Human)
Function: Required for normal glycogen accumulation. The alpha 1-6 branches of glycogen play an important role in increasing the solubility of the molecule (Probable).
Interaction partners:
- Glycogen [starch] synthase, muscle
- Glycogen phosphorylase, liver form
- Glycogen phosphorylase, muscle form
- Glycogen phosphorylase, brain form
- Glycogen [starch] synthase, liver
- Glycogenin-1
- Glycogen debranching enzyme
- Ornithine transcarbamylase, mitochondrial
- Alpha-amylase 2B
- demerged
Sequence:
MAAPMTPAARPEDYEAALNAALADVPELARLLEIDPYLKPYAVDFQRRYKQFSQILKNIGENEGGIDKFSRGYESFGVHRCADGGLYCKEWAPGAEGVFLTGDFNGWNPFSYPYKKLDYGKWELYIPPKQNKSVLVPHGSKLKVVITSKSGEILYRISPWAKYVVREGDNVNYDWIHWDPEHSYEFKHSRPKKPRSLRIYESHVGISSHEGKVASYKHFTCNVLPRIKGLGYNCIQLMAIMEHAYYASFGYQITSFFAASSRYGTPEELQELVDTAHSMGIIVLLDVVHSHASKNSADGLNMFDGTDSCYFHSGPRGTHDLWDSRLFAYSSWEILRFLLSNIRWWLEEYRFDGFRFDGVTSMLYHHHGVGQGFSGDYSEYFGLQVDEDALTYLMLANHLVHTLCPDSITIAEDVSGMPALCSPISQGGGGFDYRLAMAIPDKWIQLLKEFKDEDWNMGDIVYTLTNRRYLEKCIAYAESHDQALVGDKSLAFWLMDAEMYTNMSVLTPFTPVIDRGIQLHKMIRLITHGLGGEGYLNFMGNEFGHPEWLDFPRKGNNESYHYARRQFHLTDDDLLRYKFLNNFDRDMNRLEERYGWLAAPQAYVSEKHEGNKIIAFERAGLLFIFNFHPSKSYTDYRVGTALPGKFKIVLDSDAAEYGGHQRLDHSTDFFSEAFEHNGRPYSLLVYIPSRVALILQNVDLPN
Protein: N-lysine methyltransferase SMYD2 (EC 2.1.1.-) (HSKM-B) (Histone methyltransferase SMYD2) (EC 2.1.1.354) (Lysine N-methyltransferase 3C) (SET and MYND domain-containing protein 2) (Q9NRG4)
Organism: Homo sapiens (Human)
Function: Protein-lysine N-methyltransferase that methylates both histones and non-histone proteins, including p53/TP53 and RB1. Specifically trimethylates histone H3 'Lys-4' (H3K4me3) in vivo. The activity requires interaction with HSP90alpha. Shows even higher methyltransferase activity on p53/TP53. Monomethylates 'Lys-370' of p53/TP53, leading to decreased DNA-binding activity and subsequent transcriptional regulation activity of p53/TP53. Monomethylates RB1 at 'Lys-860'.
Subcellular location: Cytoplasm, cytosol {ECO:0000250}. Nucleus {ECO:0000250}.
Interaction partners:
- Cellular tumor antigen p53
- Heat shock protein HSP 90-alpha
- Histone-lysine N-methyltransferase SETD7
- Heat shock protein HSP 90-beta
- Calmodulin-lysine N-methyltransferase
- N-lysine methyltransferase KMT5A
- Histone H3.1
- Histone H3.2
- Actin-histidine N-methyltransferase
- Lysine-specific histone demethylase 1A FAD-dependent demethylase 1A)
Sequence:
MRAEGLGGLERFCSPGKGRGLRALQPFQVGDLLFSCPAYAYVLTVNERGNHCEYCFTRKEGLSKCGRCKQAFYCNVECQKEDWPMHKLECSPMVVFGENWNPSETVRLTARILAKQKIHPERTPSEKLLAVKEFESHLDKLDNEKKDLIQSDIAALHHFYSKHLGFPDNDSLVVLFAQVNCNGFTIEDEELSHLGSAIFPDVALMNHSCCPNVIVTYKGTLAEVRAVQEIKPGEEVFTSYIDLLYPTEDRNDRLRDSYFFTCECQECTTKDKDKAKVEIRKLSDPPKAEAIRDMVRYARNVIEEFRRAKHYKSPSELLEICELSQEKMSSVFEDSNVYMLHMMYQAMGVCLYMQDWEGALQYGQKIIKPYSKHYPLYSLNVASMWLKLGRLYMGLEHKAAGEKALKKAIAIMEVAHGKDHPYISEIKQEIESH
Protein: Leukocyte cell derived chemotaxin 2, tandem duplicate 1 precursor (Leukocyte cell-derived chemotaxin 2) (Q0H0R9)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
Sequence:
MHLDILFSFLLLAVLSSSCVDAQVKFGPLCSGNSSNQKRGCDKNYGCGNFGASRGRRTHMGLDIVCTDGATVYAPFDVKINGRAKPYGNNNAIDDGISLSGGGLCFKLFYIKPDRLSGNLKKGDKIGSLLPMQKVYPGITSHVHVQMCDKSDPTKYF
Protein: Adhesion G protein-coupled receptor L3 (Calcium-independent alpha-latrotoxin receptor 3) (CIRL-3) (Latrophilin-3) (Lectomedin-3) (Q9HAR2)
Organism: Homo sapiens (Human)
Function: Plays a role in cell-cell adhesion and neuron guidance via its interactions with FLRT2 and FLRT3 that are expressed at the surface of adjacent cells. Plays a role in the development of glutamatergic synapses in the cortex. Important in determining the connectivity rates between the principal neurons in the cortex.
Subcellular location: Cell membrane {ECO:0000269|PubMed:26235030}; Multi-pass membrane protein {ECO:0000305}. Cell projection, axon {ECO:0000250|UniProtKB:Q80TS3}. Cell junction {ECO:0000250|UniProtKB:Q80TS3}.
Interaction partners:
- Leucine-rich repeat transmembrane protein FLRT3
- Teneurin-2
- Teneurin-1
- Netrin receptor UNC5D
- Teneurin-4
- Teneurin-3
- Netrin receptor UNC5C
- Netrin receptor UNC5A
- SUZ RNA-binding domain-containing
- UNC5C-like protein
Sequence:
MWPSQLLIFMMLLAPIIHAFSRAPIPMAVVRRELSCESYPIELRCPGTDVIMIESANYGRTDDKICDSDPAQMENIRCYLPDAYKIMSQRCNNRTQCAVVAGPDVFPDPCPGTYKYLEVQYECVPYKVEQKVFLCPGLLKGVYQSEHLFESDHQSGAWCKDPLQASDKIYYMPWTPYRTDTLTEYSSKDDFIAGRPTTTYKLPHRVDGTGFVVYDGALFFNKERTRNIVKFDLRTRIKSGEAIIANANYHDTSPYRWGGKSDIDLAVDENGLWVIYATEQNNGKIVISQLNPYTLRIEGTWDTAYDKRSASNAFMICGILYVVKSVYEDDDNEATGNKIDYIYNTDQSKDSLVDVPFPNSYQYIAAVDYNPRDNLLYVWNNYHVVKYSLDFGPLDSRSGQAHHGQVSYISPPIHLDSELERPSVKDISTTGPLGMGSTTTSTTLRTTTLSPGRSTTPSVSGRRNRSTSTPSPAVEVLDDMTTHLPSASSQIPALEESCEAVEAREIMWFKTRQGQIAKQPCPAGTIGVSTYLCLAPDGIWDPQGPDLSNCSSPWVNHITQKLKSGETAANIARELAEQTRNHLNAGDITYSVRAMDQLVGLLDVQLRNLTPGGKDSAARSLNKAMVETVNNLLQPQALNAWRDLTTSDQLRAATMLLHTVEESAFVLADNLLKTDIVRENTDNIKLEVARLSTEGNLEDLKFPENMGHGSTIQLSANTLKQNGRNGEIRVAFVLYNNLGPYLSTENASMKLGTEALSTNHSVIVNSPVITAAINKEFSNKVYLADPVVFTVKHIKQSEENFNPNCSFWSYSKRTMTGYWSTQGCRLLTTNKTHTTCSCNHLTNFAVLMAHVEVKHSDAVHDLLLDVITWVGILLSLVCLLICIFTFCFFRGLQSDRNTIHKNLCISLFVAELLFLIGINRTDQPIACAVFAALLHFFFLAAFTWMFLEGVQLYIMLVEVFESEHSRRKYFYLVGYGMPALIVAVSAAVDYRSYGTDKVCWLRLDTYFIWSFIGPATLIIMLNVIFLGIALYKMFHHTAILKPESGCLDNIKSWVIGAIALLCLLGLTWAFGLMYINESTVIMAYLFTIFNSLQGMFIFIFHCVLQKKVRKEYGKCLRTHCCSGKSTESSIGSGKTSGSRTPGRYSTGSQSRIRRMWNDTVRKQSESSFITGDINSSASLNREGLLNNARDTSVMDTLPLNGNHGNSYSIASGEYLSNCVQIIDRGYNHNETALEKKILKELTSNYIPSYLNNHERSSEQNRNLMNKLVNNLGSGREDDAIVLDDATSFNHEESLGLELIHEESDAPLLPPRVYSTENHQPHHYTRRRIPQDHSESFFPLLTNEHTEDLQSPHRDSLYTSMPTLAGVAATESVTTSTQTEPPPAKCGDAEDVYYKSMPNLGSRNHVHQLHTYYQLGRGSSDGFIVPPNKDGTPPEGSSKGPAHLVTSL
Protein: Autophagy-related 18a, isoform E (M9PER1)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Autophagy-related protein 2
- Autophagy-related 16, isoform F
- Autophagy-related 1, isoform B
- Autophagy-related protein 9
- Autophagy protein 12-like
- Autophagy protein 5
- Autophagy-related 8a, isoform A
- Autophagy-related 8b, isoform A
- Ubiquitin-like modifier-activating enzyme ATG7
- Ubiquitin-like-conjugating enzyme ATG3
Sequence:
MMSLLGRTDVDAGEVFVNFNQNITSLAVATSGGYSLYSLGSVDSTLDKIYHTKSDELFLIERLFESSLVAIVSQRAPRKLKVCHFKKQSEICNYSYANTILAVKLNRERLIVCLEESLYIHNIQDMKVVHTIRDTPCNPQGLCALSSSSEHCYLAYPGSVTAGEVQIFDAINLHAKTMIPAHDTPLAALAFSPSGTEIATASERGTVIRVFSSQDGSRLFELRRGLKRCVSIVSLSFSTCAEYLVSSSNTETVHIFRLDRSATETAEGHGSKQSSDDWMGYSFFRFLSKTVTSYLPTQVTDVFSQGRAFASVTLPEAGVRRMCAIATIQKQLRLLIASQDGYLYVYSIPTVEGAECQLIKRHDLRLEDHYAMDIKVDSPQTLGLNSGVSIGGAAGVPPSSASAAGAGTGGSGGDGKSAVSVTGGVDKPSSSYASAVKGDDPVGPSSA
Protein: Fatty acid synthase (EC 1.1.1.100) (EC 1.3.1.39) (EC 2.3.1.38) (EC 2.3.1.39) (EC 2.3.1.41) (EC 2.3.1.85) (EC 3.1.2.14) (EC 4.2.1.59) (A0A060XQE7)
Organism: Oncorhynchus mykiss (Rainbow trout) (Salmo gairdneri)
Interaction partners:
- Carrier domain-containing protein
- L-aminoadipate-semialdehyde dehydrogenase-phosphopantetheinyl transferase
- Malonyl-CoA-acyl carrier protein transacylase, mitochondrial
- Uncharacterized protein
- Malonyl-CoA:ACP transacylase
- Hydroxysteroid dehydrogenase-like protein 2
- acetyl-CoA carboxylase
- acetyl-CoA carboxylase
- ATP citrate synthase
- ATP citrate synthase
Sequence:
MEEIVVAGISGRLPESNNLEEFWENLFNGVDMVTEDDRRWKPGLYGLPKRNGKLKDISRFDAAFFGVHPKQAHTMDPQLRLMLEIAYEAIVDGGLNPTELRGSRTGVYIGVSGSEAGEAFSRDPEELLGYSMTGCQRAMFANRLSYFFDFNGPSTAIDTACSSSLLALENAFNAIRHGHCDAALVGGVNLLLKPNTSVQFMKLGMLSPEGTCKSFDSSGNGYCRSEAAVAVLLTRRSMAKRVYATVLNAGNNTDGYKEQGVTFPSGEMQQRLVRSLYQEVNITPDQVEYIEAHGTGTKVGDPQEVNGIVSVFCHSKRDPLLIGSTKSNMGHPEPASGLAALAKVVLSLERGVWAPNIHYNSPNTDIPALSDGRLRVVNEPIPVRGGIVGINSFGFGGSNVHVILRPPGFNTPKSFKVPPNTPSVSSQVPRLLQACGRTEEAVSALLSKGKEHSGDDNFLCLLNDVSGVPTAGMPYRGYTLIGSQDDVTEVQKTEATPRPLWYICSGMGTQWGGMGRSLMQLPEFRESILRSDIALKDTGMCVSSLLMEADESTFEDTVQAFVGLAAIQIAQIDLLQKLGLQPDGIVGHSVGELACGYADGSLSHSEAILAAYWRGRSIKEANLPPGGMAAVGLTWAECKAQCPQGVVPACHNAEDTVTISGPAEAVSKFVSELKESGVFAKEVRSAGVAFHSYYMASIAPALLAALKRVIKEPKQRSARWISTSIPQKDWDSPLALYSSADYHCNNLVSPVLFQEGLSLVPDNAVVVEIAPHALLQAILKRSLKPTCSILPLMRRGHANNLEFFLSHIGKVYMNGINVDSKQLYPCVEYPVPAGTPLISPLVQWDHTQTWDVPKAEDFPAGSGGSTSATIYNIDMNPESPDYYMIGHCIDGRVLYPATGYLVLAWRTLMRSLGVVMETTPVTFEDVTIHRATILPKTGSVQLEVRLMPATSRFEVSENGNLAVSGKVSILEDAALDAFHSEIGKPVTGDDGDPNLRLTAHDIYKELRLRGYDYGKTFQGILESNNAGDSGKLQWTGNWVTFLDTMLQMIVVGLSGRSLRLPTRIRSVCVDPTVHQERVTEYGEAKKAVVVHVNRCLDNIVAGGVQICGLHATVAPRRQQQQSPPTLEEFLFVPYLETECLSANEKLGNQLKNCKGLIHKLQKKLAPQGVKLSIPGLGGVSGPAVPSPESAEPGLLRLLSLLCGLELNGNLRSELEQTVEKERGCLLQDPLLHGLLDGPALRHCLDTALENTTPGKIKVLEALSNDGHLFSRAVPLLNIQPMLRLDYVATAATLDLLTPHQTTLDAMGVTSAQWDPQQGPVPGGAVGGADLVVCNHAWGPLGAGAEVVVGNLASGAKEGGFVMLHTLLKGETLGEMVAFLTSKDSQNNQQRLLSQTEWEKAFSDASLNLVAVRKSFYGSALFLCRRRLPSKLPIFLPVDSLDYQWVETLKTTLAEPSDSPVWLTATQGHSGVVGMVNCLRQEPGGSRIRCAFVSNLCESSAVPTLQPAHNSMRSVLEGDLCMNVFRDGHWGVFRHQLISQDLSEELTEQAYVNVLTRGDLSSLRWIASPLRHFVASSPHVQLCRVYYSSLNFRDIMLATGKLPPDAIPGDLALQQCMLGMEFSGRDPSGRRVMGLLPAKGLATCVDADTRFLWDIPDGWTLEQAASVPVVYATAYYSLVVRGRLRPGESVLIHSGSGGVGQAAISIALSQRCRVFTTVGSAEKRAYLQERFPQLTSESFANSRDATFEQHVLLHTQGKGVDMVLNSLAEEKLQASLRCLARHGRFLEIGKYDLSNNSPLGMALFLKNVAFHGILLDALFEEGNREWEEVSQLLKGGIVGGVVKPLRTTVFERDQVEEAFRYMAQGKHIGKVLLQVRSEEKGGGTQAVGSPLSLPAICRTFCPASHSYIITGGLGGFGLELAHWLTERGARKLVLTSRSGIRNGYQAKRVREWQGMGVQVLVSTSDVSTLEGAERLINEACRLGPVGGVFHLAMVLKDGMLENLTPQLFLDVNKPKYNGTLHLDRVTRKLCPDLSYFVAFSSVSCGRGNAGQSNYGYANSAMERVCEQRRHDGLPGLAVQWGAIGDVGVVLETMGGNDVVVGGTLPQRITSCLEVLDRFLCERRPVMSSFVLAERSVVKSEGTGQRDLVEAVAHILGVRDVSSLNADASLADLGLDSLMGVEVRQTLERDYDIVMAMREIRQLTINKLRELSSQPAGTAESCQSPVKKGGVRSLLESDLSLMLVNPDGPTVSRLNEVQSAERPLFLVHPIEGSIAAFHTLTAKLSVPCYGLQCTKAAPLDSIQSLATYYVECIRQVQSEGPYRIAGYSFGACVAFEMCSQLQAQGRTVDYLFLFDGSHSYVAAYTQSYKSKLTPGKESEAETEALCAFIQQFTGIEYNKLLETLLPLSDLKARVNMAVDLITSSHKNVSKESLRFAAATFYYKLKAADGYVPATKYHGNVTLLRAKASSDYGDNLGADYKLSEVCDGKVSVHVIEGDHRSFLEGEGVESISSIIHSSLAEPRVTAREG
Protein: DNA N6-methyl adenine demethylase (EC 1.14.11.51) (N6-methyl adenine demethylase 1) (Q8MNT9)
Organism: Caenorhabditis elegans
Function: Dioxygenase that specifically demethylates DNA methylated on the 6th position of adenine (N(6)-methyladenosine) DNA. N(6)-methyladenosine (m6A) DNA is involved in epigenetic transgenerational inheritance. Plays an essential role in DNA replication and repair in the germline during meiosis. Binds to components of the DNA replication machinery such as top-2, and directs their localization to DNA to control DNA replication.
Subcellular location: Nucleus {ECO:0000305|PubMed:31283754}. Note=May co-localize with top-2 on DNA. {ECO:0000305|PubMed:31283754}.
Interaction partners:
- DNA N6-methyl methyltransferase
- Alpha-ketoglutarate-dependent dioxygenase AlkB-like domain-containing protein
- Lysine-specific histone demethylase 1
- Fe2OG dioxygenase domain-containing protein
- Fe2OG dioxygenase domain-containing protein
- Single-stranded DNA-binding protein
Sequence:
MGSAEQACGCKGARFCALCETTERVKKLRVVEDKHVNYKVFIYDHIRQIAIPTTNLNSQSSLEDIIDESTSCQSVSTDGSIEIDGLTLIHNFLSESEESKILNMIDTVEWAQSQSGRRKQDYGPKVNFKHKKVKTDTFVGMPEYADMLLNKMSEYDVKKLGNYQPFEMCNLEYEEVKKSAIEMHQDDMWIWGNRLISINLINGSVMTLSNDNKSFLCYVHMPHRSLLCMADECRYDWKHGVLAHHIRGRRIALTMREAAKDFAEGGELYEKYGAELIRLGNIRVPLSKTSV
Protein: 2-oxoadipate dehydrogenase complex component E1 (E1a) (OADC-E1) (OADH-E1) (EC 1.2.4.-) (2-oxoadipate dehydrogenase, mitochondrial) (Alpha-ketoadipate dehydrogenase) (Alpha-KADH-E1) (Dehydrogenase E1 and transketolase domain-containing protein 1) (Probable 2-oxoglutarate dehydrogenase E1 component DHKTD1, mitochondrial) (Q96HY7)
Organism: Homo sapiens (Human)
Function: 2-oxoadipate dehydrogenase (E1a) component of the 2-oxoadipate dehydrogenase complex (OADHC). Participates in the first step, rate limiting for the overall conversion of 2-oxoadipate (alpha-ketoadipate) to glutaryl-CoA and CO(2) catalyzed by the whole OADHC. Catalyzes the irreversible decarboxylation of 2-oxoadipate via the thiamine diphosphate (ThDP) cofactor and subsequent transfer of the decarboxylated acyl intermediate on an oxidized dihydrolipoyl group that is covalently amidated to the E2 enzyme (dihydrolipoyllysine-residue succinyltransferase or DLST) (Probable). Can catalyze the decarboxylation of 2-oxoglutarate in vitro, but at a much lower rate than 2-oxoadipate. Responsible for the last step of L-lysine, L-hydroxylysine and L-tryptophan catabolism with the common product being 2-oxoadipate (Probable).
Subcellular location: Mitochondrion {ECO:0000269|PubMed:23141294}.
Interaction partners:
- Dihydrolipoyllysine-residue succinyltransferase component of 2-oxoglutarate dehydrogenase complex, mitochondrial
- Dihydrolipoyl dehydrogenase, mitochondrial
- Glutaryl-CoA dehydrogenase, mitochondrial
- Succinate--CoA ligase subunit alpha, mitochondrial
- Kynurenine/alpha-aminoadipate aminotransferase, mitochondrial
- Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex, mitochondrial
- Pyruvate dehydrogenase protein X component, mitochondrial
- Lipoamide acyltransferase component of branched-chain alpha-keto acid dehydrogenase complex, mitochondrial
- Citrate synthase, mitochondrial
- Succinate dehydrogenase flavoprotein subunit, mitochondrial
Sequence:
MASATAAAARRGLGRALPLFWRGYQTERGVYGYRPRKPESREPQGALERPPVDHGLARLVTVYCEHGHKAAKINPLFTGQALLENVPEIQALVQTLQGPFHTAGLLNMGKEEASLEEVLVYLNQIYCGQISIETSQLQSQDEKDWFAKRFEELQKETFTTEERKHLSKLMLESQEFDHFLATKFSTVKRYGGEGAESMMGFFHELLKMSAYSGITDVIIGMPHRGRLNLLTGLLQFPPELMFRKMRGLSEFPENFSATGDVLSHLTSSVDLYFGAHHPLHVTMLPNPSHLEAVNPVAVGKTRGRQQSRQDGDYSPDNSAQPGDRVICLQVHGDASFCGQGIVPETFTLSNLPHFRIGGSVHLIVNNQLGYTTPAERGRSSLYCSDIGKLVGCAIIHVNGDSPEEVVRATRLAFEYQRQFRKDVIIDLLCYRQWGHNELDEPFYTNPIMYKIIRARKSIPDTYAEHLIAGGLMTQEEVSEIKSSYYAKLNDHLNNMAHYRPPALNLQAHWQGLAQPEAQITTWSTGVPLDLLRFVGMKSVEVPRELQMHSHLLKTHVQSRMEKMMDGIKLDWATAEALALGSLLAQGFNVRLSGQDVGRGTFSQRHAIVVCQETDDTYIPLNHMDPNQKGFLEVSNSPLSEEAVLGFEYGMSIESPKLLPLWEAQFGDFFNGAQIIFDTFISGGEAKWLLQSGIVILLPHGYDGAGPDHSSCRIERFLQMCDSAEEGVDGDTVNMFVVHPTTPAQYFHLLRRQMVRNFRKPLIVASPKMLLRLPAAVSTLQEMAPGTTFNPVIGDSSVDPKKVKTLVFCSGKHFYSLVKQRESLGAKKHDFAIIRVEELCPFPLDSLQQEMSKYKHVKDHIWSQEEPQNMGPWSFVSPRFEKQLACKLRLVGRPPLPVPAVGIGTVHLHQHEDILAKTFA
Protein: Australin, isoform A (Australin, isoform B) (IP08034p1) (Q9VLD7)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Chromosome, centromere {ECO:0000256|ARBA:ARBA00004584}. Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- Deterin
- Inner centromere protein, isoform A
- Aurora kinase B
- ATP synthase subunit alpha, mitochondrial
- ATP synthase subunit gamma, mitochondrial
- ATP synthase subunit a
- ATP synthase F
- Borealin
- ATPase protein 9
- FI05611p
Sequence:
MPRTKITARRQAQRQKADREEKVRLSQIKMDSALEKIDEMSKRYKQEVDNQIKVIRGRTDKQLLQMKMPEFLALGFKTFAEFQRAAIKPPTTRSLSISRGRTRTPQNALPPRLQAHSVDRALSGDTMSFVRWPRAGEMVLSKAGSPLAVQMRPDRYADVHIPTRGGVITVKPHKINTVKREVLMQLDENTLNQVKTLNANLGLIVDMANKLGKLKP
Protein: CAP, isoform Q (B7YZD8)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MPNNRNRNRNRNRNKRNRNQNQNQNPSQNQNENHQQQAEGAEDREEQQDFQTQIAVAQSSSFVDDNGNSGSVSNGPTENSEEVTNTLEKTEKKEEIFEQPATVIQKEADSDAEMGAKNSKHRKEKSDKQASNGKSEEQVRPPPTIIRRPPGSPRQAKVIVHRIVREEDTANGKAQSPEPPKAVESKEQHMEVEDSKKEKPEAQQEIETKEERENEPSPKELPESSHLSEDAQQKHVEVEENQQVYDEVDYSKDETTDNNPQQEQHDSKEPEQYVLQLEKAMEFVENAHQQHVAAVQSYQKQRDTEQNAQQQEQNEAQHLQESTKAHQQNIAVPQILVDPKKREEGLAQQLHHDVKEEPILNNAQQQNDDTAPKSPKEVTIKVQFQTEDPYSQQPPPQKPTSKVIIHQIHVETTDEEQNAKPTFEEVSSTTGSLAGTLSPPPRYLVESPKNVSSGQFSNFSRNVQIQEMELNSDFSSGEFNSLQSPLVCEVDSESEGSVVLGPERSPSDQQVPSSSRVEQHEQVRQKRAQYRNALESHFMPQLLNPRYLDSILEENEWRNSTASSGGSDQTGIRTPKLNETFPRSQLDFSRRHKRREEAPSPLKLETKLLEESTDLESCTRLQSALSPQSEDAELVYLSSSASSSVSDLMELELEQAAALAERALVDLDTDASRLIARPDDEMSSTSTTTADRSETEAETETETEREGEQSRESTPVNANPTLASSQSSLLSAATPTPTPTPTPADREQLAKDTNVSGGSTVSFGAASPLAATREEFVRNMDKVRELIEMTRREQEQGELPRSPSPPPVPPPPASVPPYSPESSSFHLASLQLKRQESNDSHCSDSTTHSQCTAINLASPPPPPTAQPPTPPLRQKPAPPPVPQPVSPPAPPTPQSEPELSVADSVANANADVDADADTDTEAIKKLRLLCTEQLASMPYGEQVLEELASVAQNISDQSQNKMPYPMPQLPHIKELQLNANESKSSSAWLGLPTQSDPKLLVCLSPGQRDLVNNQTQPDDLLDAHQKFVERRGYHELSKAQVLEQDHQQQQSEMLKTAAMMRELRKSLSPPAPPVPPPPVPVKSAETAAKATAHENAKRDDASEQKQKIAACESSSLENKPRRAADLGAQQSAEQRQSSSTTTSSHKATTETMSSDTAKFPTLDSMESELARMFPQHKGDIFEEQRKRFSNIEFPSHQPVSQTKRYSNIETSSYESKKRMENGQVVYDVSTSSHEKKEQGDPPKDQPVPPVPPPPIMSATKLNGNTFIDGDVAPKNSQPSRESGSGSGNGTYEEFRQRAKAAADAFGEQREQQNGLDQDRVFKDFDRLSQQMHAELQSTREKREKSASMYDLSGFTRPASGHPRLDELQQRRHAHMQELEREIERSAKSRQERMSSVPRQMEATPPRTHEIPIELEPRSRRAESLCNLNEPPPRPHTTVGHYNHPVVQDDWSRYANDLGYSENIARPFAREVEICYQRQNQRTPHCIRAPRLSASTNDLSSSSQYSYDTFNAYGGRRTHAPMLNQAQQQQRPHYGSCYSMIERDPNPRYISTTSRRGVSPAPPPVATPQQQQVPPPAYDRQQRRSSLPRELHEQQLKYILSKEEELKFEVERLQQERRRLMEEMQRAPVLPAPQRRESYRPAAKLPTLSEDEVFRQQMAEEWMNKVAEREERRQHKIIRISKIEDEHDHSAVDKATISDEFLDRVKERRHKLSMPADSDWESGAESQPQPAAQSQPESDVEAPPVRILEGQAEANLRQLPRHLREFAKFSTSEQLPDGAQMERHEEQERREEATDNAHSSATKKTSIVKTYKVSRLPPSVQDRAIASEEANSAATGMGVRLRPRPPKQTRFLLNAQQLQQQRQRRSWSESDLLKEIDSELQLAKGFLYANARPSYKSNGYVSEPEPNYDSDYSTVRYRTQNPHRVQSVSSAVNVRNLNQDEKLYGTMPNPIKSAQNSYKNQPGRIENYTTGHSSVSEKEKKEWWDEVMDIFNGNLEQSKLSPLYTEGNLSRALAKESGYTSDSNLVFRKKEVPVSSPLSPVEQKQAYKSLQAGGEPPLLGFRKPAPEKPRDVNIHFKTPIRHEQRQNLSEEELAIRQAEHMQKLYHEERRRKYLQELQDMNSRRHTDNFTPSQKSPIALNRYDDFPTDVTLKSLVGPKTVARALFNFQGQTSKELSFRKGDTIYIRRQIDANWYEGEHNAMIGLLPASYVEIVSRDGARTPSKRPSEGQARAKYNFQAQSGIELSLNKGELVTLTRRVDGNWFEGKIANRKGIFPCSYVEVLTDIGAEDIAARTTTVITSQSTTNLRPNLDVLRTNINNEFNTLTQNGAQPPNGILKETRTLHKTDALHVDTSSEPLAYRALYKYRPQNSDELELLEGDVVHVLEKCDDGWFVGTSQRTGCFGTFPGNYVERA
Protein: 4-hydroxyphenylpyruvate dioxygenase (EC 1.13.11.27) (4-hydroxyphenylpyruvic acid oxidase) (4HPPD) (HPD) (HPPDase) (F Alloantigen) (F protein) (P49429)
Organism: Mus musculus (Mouse)
Function: Catalyzes the conversion of 4-hydroxyphenylpyruvic acid to homogentisic acid, one of the steps in tyrosine catabolism.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:P32755}. Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P32755}; Peripheral membrane protein {ECO:0000250|UniProtKB:P32755}. Golgi apparatus membrane {ECO:0000250|UniProtKB:P32755}; Peripheral membrane protein {ECO:0000250|UniProtKB:P32755}.
Interaction partners:
- Homogentisate 1,2-dioxygenase
- Toll-like receptor 4
- Nucleolin
- Tyrosine aminotransferase
- Aspartate aminotransferase, mitochondrial
- Aspartate aminotransferase, cytoplasmic
- Putative aspartate aminotransferase, cytoplasmic 2
- Fumarylacetoacetase
- Macrophage migration inhibitory factor
- L-amino-acid oxidase
Sequence:
MTTYNNKGPKPERGRFLHFHSVTFWVGNAKQAASFYCNKMGFEPLAYRGLETGSREVVSHVIKQGKIVFVLCSALNPWNKEMGDHLVKHGDGVKDIAFEVEDCDHIVQKARERGAKIVREPWVEQDKFGKVKFAVLQTYGDTTHTLVEKINYTGRFLPGFEAPTYKDTLLPKLPRCNLEIIDHIVGNQPDQEMQSASEWYLKNLQFHRFWSVDDTQVHTEYSSLRSIVVTNYEESIKMPINEPAPGRKKSQIQEYVDYNGGAGVQHIALKTEDIITAIRHLRERGTEFLAAPSSYYKLLRENLKSAKIQVKESMDVLEELHILVDYDEKGYLLQIFTKPMQDRPTLFLEVIQRHNHQGFGAGNFNSLFKAFEEEQALRGNLTDLEPNGVRSGM
Protein: Ankyrin repeat domain-containing protein 1 (Cardiac ankyrin repeat protein) (Q865U8)
Organism: Sus scrofa (Pig)
Function: May play an important role in endothelial cell activation. May act as a nuclear transcription factor that negatively regulates the expression of cardiac genes (By similarity).
Subcellular location: Nucleus {ECO:0000250}.
Interaction partners:
- Ankyrin repeat and SOCS box containing 2
Sequence:
MMVLKVEELVTGKKNGGGDAGEFLPEDFRDGEYEAAVTLEKQEDLKTLPAHFVSLGEQQWKIEKEREAELKKKKLEQRSKLENLEDLEIIIQLKKRKKYRKTKVPVVKEPEPEVITEPVDVPRFLKAALENKLPVVEKFLSDKNNPDVCDEYKRTALHRACLEGHLAIVEKLIEAGAQIEFRDMLESTAIHWASRGGNLDVLKLLLNKGAKISARDKLLSTALHVAVRTGHYECAEHLIACEADLNAKDREGDTPLHDAVRLNRYKMIRLLITYGADLNVKNCAGKTPMDLVLNWQNGTKAIFDSLKENSYKASRIATF
Protein: 5-deoxyribose 1-phosphate isomerase (EC 5.3.1.-) (5-deoxyribose disposal isomerase) (Methylthioribose-1-phosphate isomerase) (M1Pi) (MTR-1-P isomerase) (EC 5.3.1.23) (S-methyl-5-thioribose-1-phosphate isomerase) (P0DTQ1)
Organism: Bacillus thuringiensis serovar kurstaki (strain ATCC 35866 / NRRL B-4488 / HD73)
Function: Catalyzes the isomerization of 5-deoxy-alpha-D-ribose 1-phosphate to 5-deoxy-D-ribulose 1-phosphate, as part of a 5-deoxyribose salvage pathway that recycles this toxic radical SAM enzyme by-product to mainstream metabolites. Also seems to be able to catalyze the conversion of methylthioribose-1-phosphate (MTR-1-P) into methylthioribulose-1-phosphate (MTRu-1-P). However this enzyme may not function in methionine salvage in B.thuringiensis since it exists a paralog (MtnA) present in the methionine salvage pathway cluster.
Interaction partners:
Sequence:
MMEEQLIPIQWKDDALVLLDQTLLPNEIVYESFKTAESVWDAIQVMKVRGAPVIGVSAAYGVYLGVKEFAESTEEGFMDEVRKVCTYLATSRPTAVNLFWALERMESVAADNIHLSISQLKDRLLEEAKEIHREDEEINRQIGEHALTLFHDGMGVLTHCNAGALATTKYGTATAPMYLAKEKGWDLKIFSDETRPRLQGSTLTALELQRAGIDVTVITDNMAAMVMSQGKIDAVIVGCDRVAANGDIANKIGTLGVSILAKYYNIPFYVAAPTPTIDLKTPTGKEIPIEERDASEVINRFGQYSAPKESKVYNPAFDVTPHENVTAIITEKGIVKAPFTENLKKIFQ