wanglab/gogpt-training-data huggingface dataset:
Protein: Carbamoyl phosphate synthase arginine-specific large chain (CPS) (CPSase) (CPSase-arg) (EC 6.3.4.16) (EC 6.3.5.5) (Ammonium-dependent carbamoyl phosphate synthetase) (Arginine-specific carbamoyl phosphate synthetase, ammonia chain) (Carbamoyl phosphate synthase A) (CPS-A) (Glutamine-dependent carbamoyl phosphate synthetase) (P03965)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Subcellular location: Cytoplasm {ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:200419, ECO:0000269|PubMed:205532}.
Interaction partners:
- Argininosuccinate synthase
- Carbamoyl phosphate synthase arginine-specific small chain
- Ornithine carbamoyltransferase
- Protein ARG5,6
- Amidophosphoribosyltransferase
- Argininosuccinate lyase
- Glutamine synthetase
- Glutamate synthase
- Multifunctional protein URA2
- Glutamine--fructose-6-phosphate aminotransferase
Sequence:
MTSIYTSTEPTNSAFTTEDYKPQLVEGVNSVLVIGSGGLSIGQAGEFDYSGSQAIKALKEDNKFTILVNPNIATNQTSHSLADKIYYLPVTPEYITYIIELERPDAILLTFGGQTGLNCGVALDESGVLAKYNVKVLGTPIKTLITSEDRDLFASALKDINIPIAESFACETVDEALEAAERVKYPVIVRSAYALGGLGSGFANNASEMKELAAQSLSLAPQILVEKSLKGWKEVEYEVVRDRVGNCITVCNMENFDPLGVHTGDSMVFAPSQTLSDEEFHMLRSAAIKIIRHLGVIGECNVQYALQPDGLDYRVIEVNARLSRSSALASKATGYPLAYTAAKIGLGYTLPELPNPITKTTVANFEPSLDYIVAKIPKWDLSKFQYVDRSIGSSMKSVGEVMAIGRNYEEAFQKALRQVDPSLLGFQGSTEFGDQLDEALRTPTDRRVLAIGQALIHENYTVERVNELSKIDKWFLYKCMNIVNIYKELESVKSLSDLSKDLLQRAKKLGFSDKQIAVTINKHASTNINELEIRSLRKTLGIIPFVKRIDTLAAEFPAQTNYLYTTYNATKNDVEFNENGMLVLGSGVYRIGSSVEFDWCAVNTAKTLRDQGKKTIMINYNPETVSTDFDEVDRLYFEELSYERVMDIYELEQSEGCIISVGGQLPQNIALKLYDNGCNIMGTNPNDIDRAENRHKFSSILDSIDVDQPEWSELTSVEEAKLFASKVNYPVLIRPSYVLSGAAMSVVNNEEELKAKLTLASDVSPDHPVVMSKFIEGAQEIDVDAVAYNGNVLVHAISEHVENAGVHSGDASLVLPPQHLSDDVKIALKDIADKVAKAWKITGPFNMQIIKDGEHTLKVIECNIRASRSFPFVSKVLGVNFIEIAVKAFLGGDIVPKPVDLMLNKKYDYVATKVPQFSFTRLAGADPFLGVEMASTGEVASFGRDLIESYWTAIQSTMNFHVPLPPSGILFGGDTSREYLGQVASIVATIGYRIYTTNETTKTYLQEHIKEKNAKVSLIKFPKNDKRKLRELFQEYDIKAVFNLASKRAESTDDVDYIMRRNAIDFAIPLFNEPQTALLFAKCLKAKIAEKIKILESHDVIVPPEVRSWDEFIGFKAY
Protein: Acyl-coenzyme A thioesterase 9, mitochondrial (Acyl-CoA thioesterase 9) (EC 3.1.2.-) (EC 3.1.2.2) (Acyl coenzyme A thioester hydrolase 2) (MTE-2) (Acyl-CoA thioester hydrolase 9) (Mitochondrial 48 kDa acyl-CoA thioester hydrolase 1) (MT-ACT48.1) (Protein U8) (p48) (Q9R0X4)
Organism: Mus musculus (Mouse)
Function: Acyl-CoA thioesterases are a group of enzymes that catalyze the hydrolysis of acyl-CoAs to the free fatty acid and coenzyme A (CoASH), providing the potential to regulate intracellular levels of acyl-CoAs, free fatty acids and CoASH. Active on long chain acyl-CoAs.
Subcellular location: Mitochondrion {ECO:0000305|PubMed:10383425}. Mitochondrion matrix {ECO:0000269|PubMed:31676684}. Mitochondrion inner membrane {ECO:0000269|PubMed:32498134}.
Interaction partners:
- Acyl-coenzyme A thioesterase 2, mitochondrial
- Acyl-coenzyme A thioesterase 3
- Acyl-coenzyme A thioesterase 8
- Acyl-coenzyme A thioesterase 5
- Acyl-coenzyme A thioesterase 13
Sequence:
MKRAAIRLWTLNKGLLTHGRGLSQGSQYKISEPLHIHQVRDKLREIVGVSTVWRDHVKAMEERKLLHSFLPKSQKVLPPRKMRDSYIEVLLPLGTDPELRDKYVTVQNTVRFGRILEDLDSLGVLVCYMHNHNHSTKMSPLSIVTVLVDKIDMCKHSLSPEQDIKFTGHVSWVGNTSMEVKMKMFQLHNDEKYWPVLDATFVMVARDSENKGPAFVNPLIPENKEEEELFKQGELNKSRRIAFSTSSLLKVAPSSEERNIIHELFLTTLDPKTISFQSRILPPKAVWMEDTKLKSLDICHPQERNVFNRIFGGFLMRKAYELAWATACSFGGSRPYVVTVDDIMFQKPVEVGSLLFLSSQVCFTQDNYIQVRVHSEVSSLDSREHMTTNVFHFTFMSEKEVPLIFPKTYGESMLYLDGQRHFKSMSTPVTLKKDYPVEP
Protein: RING-type E3 ubiquitin transferase (EC 2.3.2.27) (Q94F54)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
Sequence:
MRQRNMMTGSDMEQNSQSFVPHPEPRIGTNYLYPDIPPVNTVPHLEAHSLQEPYDNNSMFYGPPQYHHQHASNLGSGMSTAPNFYVPYVNYEAPPSFLLSHGSNDAVVGVTSTEHERNAHFMDHGFKRKSSEVIPGNSQYPVAPCSFPQLNTSETAPFSFPHFGTYPQPLDQRSVRNRAGAATMDPLLSHGHNNFSQGNYAAHPFPPLGSIWYDQHCNGNRSDGSSSLWSQAPAVPYMHGNIATGSIESGNVCFPRYHETSSSRNPTPSVYQRNHYISHHPVPPPPIVYPHMPSASYAETLHPASYSHMGQVQSTGFRINQYPGEDFVPAAILRHRELPHFRAMPANENAFWEVGDFYNAVNYVDHHQDMRLDIEDMSYEELLALSDQIGTVKTGLSSEDVKELLKRRTSTRINLEEGPSTDLETDSCTICQENYKNEDKIATLDCMHKYHAECLKKWLVIKNVCPICKSEALVIEKKKKLRLSSR
Protein: N-alpha-acetyltransferase 38, NatC auxiliary subunit (I3L3Z2)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MAGAGPTMLLREENGCCSRRQSSSSAGDSDGEREDSAAERARQQLEALLNKTMRIRMTDGRTLVGCFLCTDRDCNVILGSAQEFLKPSGQCPGNAHPPDSFSAGEPRVLGLAMVPGHHIVSIEVQRESLTGPPYL
Protein: Proteasome subunit beta type-1 (Proteasome subunit beta 6) (P34286)
Organism: Caenorhabditis elegans
Function: Non-catalytic component of the proteasome, a multicatalytic proteinase complex which is characterized by its ability to cleave peptides with Arg, Phe, Tyr, Leu, and Glu adjacent to the leaving group at neutral or slightly basic pH. The proteasome has an ATP-dependent proteolytic activity (By similarity).
Subcellular location: Cytoplasm {ECO:0000255|PROSITE-ProRule:PRU00809}. Nucleus {ECO:0000250}.
Interaction partners:
- Proteasome subunit pbs-5
- Proteasome subunit alpha type-6
- Proteasome subunit alpha type-5
- Proteasome subunit beta type-3
- Proteasome subunit beta
- Proteasome subunit beta
- Proteasome subunit alpha type-4
- Proteasome subunit beta
- Proteasome subunit beta type-2
- Proteasome subunit alpha type-1
Sequence:
MTSFTGITAVANATNEMAMFKQAMKEVAAHPEWMSSRQIERQRWNPYSMEGGSTCAISGENFAIVASDTRMTQNDINILTRDAEKIQILNDNIILTTSGFYGDVLQLKKVLQSRLHKYRFDYRSDMSVDLCAELLSRNLYYRRFFPYYTGAILAGIDEHGKGAVFSYDPIGCIERLGYSASGAAEPMIIPFLDCQIGHVTLSEGYERPELTLDRAISLMKDSFRGAAEREISTGDKIHLVIAEAGKPVVVKFLPLRED
Protein: Uncharacterized protein (U5H305)
Organism: Microbotryum lychnidis-dioicae (strain p1A1 Lamole / MvSl-1064) (Anther smut fungus)
Interaction partners:
Sequence:
MLLKLTITLIVALLVLNVSALQEAGDTKAEFRLIKRAAAQKSNLTQPTENASFLLHHPIPFELNYDPKIVYAVDVELLSEHDKSIPLAVQMAGDHTGAISTTFSTPYFAENSVKYRNVTLRVTEWSLPSHNTAPKKKSSTIDRKIVCRNFSGKIHA
Protein: isoleucine--tRNA ligase (EC 6.1.1.5) (Isoleucyl-tRNA synthetase) (Q38A55)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- Tyrosyl/methionyl-tRNA synthetase, putative
- glutamate--tRNA ligase
- proline--tRNA ligase
- arginine--tRNA ligase
- glutamine--tRNA ligase
- leucine--tRNA ligase
- methionine--tRNA ligase
- phenylalanine--tRNA ligase
- Valine--tRNA ligase, mitochondrial
- serine--tRNA ligase
Sequence:
MNRCYSLLCSVLNSGKRAQTSFPSTRRTVIHSRVLPSESITSSFSPPETTTASKDKSRGEAASKTTMTGPLQNFGDELNFPKMEEEVLKHWEDIDAFKECLKQSEGKKPYTFYDGPPFATGLPHYGHLLAGTIKDIVCRYAHQTGHHVDRRFGWDCHGLPIEFEIDKEYGIKSSHDVKKMGIENYNNACRAIVMRFSEEWRKTVTRMGRWIDFDNDYKTMYLSYMESVWWVFKSLWDKGLVYRGFKVMPFSTACTTPLSNFEANLNYKDVSDPSLMVTFRTKDDPNTFLIAWTTTPWTLPSNLALCVHPDIDYVKVLDSKTKRHYIFGEPRLGEVYPKKKGDGKKGTEASPYTIVSRMKGKELVGTKYEPLFPYFEEKYGATAYRVLCDAYVATDSGTCVVHQAPGFGEEDNRICIDSGVITKEDMLCPVDENGSFTPDVVDFQGRYVKEADSDIIKYLESKGLVHSKGSIVHSYPFCWRSEAPLIYKAVDTWFVKVESLREQLLSANEETEWVPDFVKVRRFSNWLADAKDWNVSRNRYWGTPLPIWHSEDWEEVVCVGSVAELEELSGTKGITDIHRHFVDQLTIPSKRPGMPPLRRVEVVFDCWFESGSMPYAQIHYPFAAKDSFVGEKFPADFVAEGLDQTRGWFYTMLVLGVALFGRAPFKNVVVNGLILAEDGKKMSKRLKNYPEPGIIINTHGADALRMYMINSPVVRAEPLRFREQGVKGIVRDVMLPLFNAAKFFIANANYCVELGGNVATDVVSSNEMDRWILASTQTLQQYVKREMEKYHLYNVVPGVLRFVVDLSNWYVRMNRRRMKDTVDLEDRSRALSTMLNVLFAVSRIIAPIAPFVAEMLYLRIKPLLPQEQQLKSVHFHMFPEDDISKHDEVLERAMTRMVTIVELARVLRDRMVIPMKRPVRQVVVVHPDEAYLDDVRKVVTYIKEEVSAFEVVLSSSDEYVTTQLDASMENLGKLYRNEAPQIRKAIQALGPAAVTEFLKTGEVEVLGKKISRDDVKVIRKVKDGITDFESNTDNDVVVLLDKRDDQTLVDSWRAREFVNRVQQLRKKAKLIVKDIIEVYFETEDPELTTSILNCSEQVNKTIRGKWETMDKLPKGAKLIAEEDNSISGVGIRIVFTQPSAGES
Protein: Protein phosphatase PTC7 homolog fig (Fos intronic gene protein) (EC 3.1.3.16) (Q9VAH4)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MITCLRNWPLLLKRFSVHQIHQFTQLSGRFERPPQSGKSSRDPYLVTVVQGRSKKPRFPGERSNQRFGEDSWFVSSTPLAEVMGVADGVGGWRDLGVDAGRFAKELMSCCSGQTQLSDFDGRSPRNMLIAGFQELSHREHPVVGSSTACLATMHRKDCTLYTANLGDSGFLVVRNGRVLHRSVEQTHDFNTPYQLTVPPEDRKESYYCDKPEMAVSTRHSLLPGDLVLLATDGLFDNMPESMLLSILNGLKERGEHDLLVGASRVVEKARELSMNASFQSPFAIKARQHNVSYSGGGKPDDITLILSSVEVPNA
Protein: Ornithine decarboxylase, chloroplastic (EC 4.1.1.17) (E0WN94)
Organism: Nicotiana glauca (Glaucous tobacco) (Tree tobacco)
Function: Involved in the biosynthesis of pyridine alkaloid natural products, leading mainly to the production of anabasine, anatabine, nicotine and nornicotine, effective deterrents against herbivores with antiparasitic and pesticide properties (neurotoxins); nornicotine serves as the precursor in the synthesis of the carcinogen compound N'-nitrosonornicotine (NNN). Catalyzes the first and rate-limiting step of polyamine biosynthesis that converts ornithine into putrescine, which is the precursor for the polyamines, spermidine and spermine (By similarity). Polyamines are essential for cell proliferation and are implicated in cellular processes, ranging from DNA replication to apoptosis (By similarity).
Subcellular location: Plastid, chloroplast {ECO:0000255}.
Interaction partners:
Sequence:
MAGQTIIVSGLNPAAILQSTIGGGASPTAAAAAENGTRKVIPLSRDALQDFMLSIITQKLQDEKQPFYVLDLGEVVSLMDQWKSALPNIRPFYAVKCNPEPSFLSILSAMGSNFDCASRAEIEYVLALGISPDRIVFANPCKPESDIIFAAKVGVNLTTYDSEDEVYKIRKHHPKSELLLRIKPMFDGNARCPMGPKYGALPEEVEPLLRAAQAARLTVSGVSFHIGSGDADSNAYLGAIAAAKEVFETAAKLGMSKMTVLDVGGGFTSGHQFTAAAVAVKSALKQRFDDEPELTIIAEPGRFFAETAFTLATTIIGKRVRGELREYWINDGLYGSMNCVLYDHATVNATPLAVQSNRSNVTCGGSKTFPTTVFGPTCDALDTVLRDYQLPELQVNDWLVFPNMGAYTKAAGSNFNGFNTSAIVTHLAYAYPS
Protein: Malate dehydrogenase, mitochondrial (EC 1.1.1.37) (O02640)
Organism: Caenorhabditis elegans
Function: Catalyzes the reversible conversion of (S)-malate to oxaloacetate in the citric acid cycle.
Subcellular location: Mitochondrion matrix {ECO:0000250|UniProtKB:P04636}.
Interaction partners:
- Bifunctional glyoxylate cycle protein
- Probable citrate synthase, mitochondrial
- Probable fumarate hydratase, mitochondrial
- Aspartate aminotransferase
- Aspartate aminotransferase
- Malate dehydrogenase, cytoplasmic
- Pyruvate carboxylase 1
- Malic enzyme
- Phosphoenolpyruvate carboxykinase
- Aspartate aminotransferase, cytoplasmic
Sequence:
MSLPAKTLVQAAANSGLRAVSVRHSSQAPKVALLGAAGGIGQPLGLLLKQDPLVAHLALYDVVNTPGVAADLSHIDSNAKVTAHTGPKELYAAVENADVIVIPAGVPRKPGMTRDDLFNTNAGIVRDLAAVIAKASPKALIAIITNPVNSTVPIASEVLKKAGVYDPKRVFGVTTLDVVRSQAFVSELKGHDASKTVVPVVGGHAGITIIPLLSQVKPSTKFSEEEISKLTPRIQDAGTEVVNAKAGAGSATLSMALAGARFANALVRGIKGEKNVQCAYVASDAVKGVEYFSTPVELGPNGVEKILGVGKVSAYEQKLIDASVPELNKNIAKGVAFVKGN
Protein: Histone H4 (P62806)
Organism: Mus musculus (Mouse)
Function: Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling.
Subcellular location: Nucleus {ECO:0000269|PubMed:32726616}. Chromosome {ECO:0000250}. Note=Localized to the nucleus when acetylated in step 11 spermatids. {ECO:0000269|PubMed:32726616}.
Interaction partners:
- Histone H3.2
- Histone H3.3
- Histone H3.1
- Bromodomain testis-specific protein
- Histone-binding protein RBBP7
- H2B.U histone 2
- Histone H2B type 2-B
- Histone H2A type 1-B
- Bromodomain-containing protein 4
- Histone H2B type 1-C/E/G
Sequence:
MSGRGKGGKGLGKGGAKRHRKVLRDNIQGITKPAIRRLARRGGVKRISGLIYEETRGVLKVFLENVIRDAVTYTEHAKRKTVTAMDVVYALKRQGRTLYGFGG
Protein: Kinesin-like protein (A8K932)
Organism: Homo sapiens (Human)
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000256|ARBA:ARBA00004245}.
Interaction partners:
Sequence:
MGTRKKVHAFVRVKPTDDFAHEMIRYGDDKRSIDIHLKKDIRRGVVNNQQTDWSFKLDGVLHDASQDLVYETVAKDVVSQALDGYNGTIMCYGQTGAGKTYTMMGATENYKHRGILPRALQQVFRMIEERPAHAITVRVSYLEIYNESLFDLLSTLPYVGPSVTPMTIVENPQGVFIKGLSVHLTSQEEDAFSLLFEGETNRIIASHTMNKNSSRSHCIFTIYLEAHSRTLSEEKYITSKINLVDLAGSERLGKSGSEGQVLKEATYINKSLSFLEQAIIALGDQKRDHIPFRQCKLTHALKDSLGGNCNMVLVTNIYGEAAQLEETLSSLRFASRMKLVTTEPAINEKYDAERMVKNLEKELALLKQELAIHDSLTNRTFVTYDPMDEIQIAEINSQVRRYLEGTLDEIDIISLRQIKEVFNQFRVVLSQQEQEVESTLRRKYTLIDRNDFAAISAIQKAGLVDVDGHLVGEPEGQNFGLGVAPFSTKPGKKAKSKKTFKEPLSSLARKEGASSPVNGKDLDYVSTSKTQLVPSSKDGDVKDMLSRDRETSSIEPLPSDSPKEELRPIRPDTPPSKPVAFEEFKNEQGSEINRIFKENKSILNERRKRASETTQHINAIKREIDVTKEALNFQKSLWEKQGKYENKGLMIIDEEEFLLILKLKDLKKQYRSEYQDLRDLRAEIQYCQHLVDQCRHRLLMEFDIWYNESFVIPEDMQMALKPGGSIRPGMVPVNRIVSLGEDDQDKFSQLQQRVLPEGPDSISFYNAKVKIEQKHNYLKTMMGLQQAHRK
Protein: Syntaxin-1A (Neuron-specific antigen HPC-1) (Synaptotagmin-associated 35 kDa protein) (P35A) (P32850)
Organism: Bos taurus (Bovine)
Function: Plays an essential role in hormone and neurotransmitter calcium-dependent exocytosis and endocytosis. Part of the SNARE (Soluble NSF Attachment Receptor) complex composed of SNAP25, STX1A and VAMP2 which mediates the fusion of synaptic vesicles with the presynaptic plasma membrane. STX1A and SNAP25 are localized on the plasma membrane while VAMP2 resides in synaptic vesicles. The pairing of the three SNAREs from the N-terminal SNARE motifs to the C-terminal anchors leads to the formation of the SNARE complex, which brings membranes into close proximity and results in final fusion (By similarity). Participates in the calcium-dependent regulation of acrosomal exocytosis in sperm. Also plays an important role in the exocytosis of hormones such as insulin or glucagon-like peptide 1 (GLP-1) (By similarity).
Subcellular location: Cytoplasmic vesicle, secretory vesicle, synaptic vesicle membrane {ECO:0000250|UniProtKB:O35526}; Single-pass type IV membrane protein {ECO:0000250|UniProtKB:O35526}. Synapse, synaptosome {ECO:0000250|UniProtKB:O35526}. Cell membrane {ECO:0000250|UniProtKB:P32851}. Note=Colocalizes with KCNB1 at the cell membrane. {ECO:0000250|UniProtKB:P32851}.
Interaction partners:
- Synaptosomal-associated protein 25
- Syntaxin-binding protein 1
- Vesicle-associated membrane protein 2
- Alpha-soluble NSF attachment protein
- Vesicle-associated membrane protein 1
- Vesicle-associated membrane protein 4
- Synaptosomal-associated protein
- Synaptotagmin-1
- Vesicle-associated membrane protein 8
- Amyloid beta precursor protein binding family A member 1.
Sequence:
MKDRTQELRTAKDSDDDDDVTVTVDRDRFMDEFFEQVEEIRGFIDKISENVEEVKRKHSAILASPNPDEKTKEELEELMSDIKKTANKVRSKLKSIEQSIEQEEGLNRSSADLRIRKTQHSTLSRKFVEVMSEYNATQSDYRERCKGRIQRQLEITGRTTTSEELEDMLESGNPAIFASGIIMDSSISKQALSEIETRHSEIIKLENSIRELHDMFMDMAMLVESQGEMIDRIEYNVEHSVDYVERAVSDTKKAVKYQSKARRKKIMIVICCVVLGIVIASTFGGIFG
Protein: Sigma factor-binding protein Crl (Q7CR52)
Organism: Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Function: Binds to the sigma-S subunit of RNA polymerase, activating expression of sigma-S-regulated genes, such as the csgBAC operon encoding the subunits of curli proteins, and BcsA, involved in cellulose biosynthesis.
Subcellular location: Cytoplasm {ECO:0000250}.
Interaction partners:
- Esterase FrsA
- RNA polymerase sigma factor RpoS
Sequence:
MTLPSGHPKSRLIKKFTALGPYIREGQCEDNRFFFDCLAVCVNVKPAPEKREFWGWWMELEAQEKRFTYRYQFGLFDKEGNWTVVPINETEVVERLEYTLREFHEKLRDLLISMELALEPSDDFNDEPVKLSA
Protein: Bifunctional phosphoribosylaminoimidazole carboxylase/phosphoribosylaminoimidazole succinocarboxamide synthetase (PAICS) (Protein adenosine-5) [Includes: Phosphoribosylaminoimidazole-succinocarboxamide synthase (EC 6.3.2.6) (SAICAR synthetase); Phosphoribosylaminoimidazole carboxylase (EC 4.1.1.21) (AIR carboxylase) (AIRC)] (Q9I7S8)
Organism: Drosophila melanogaster (Fruit fly)
Function: Bifunctional phosphoribosylaminoimidazole carboxylase and phosphoribosylaminoimidazole succinocarboxamide synthetase catalyzing two reactions of the de novo purine biosynthetic pathway.
Interaction partners:
- Trifunctional purine biosynthetic protein adenosine-3
- Adenylosuccinate lyase
Sequence:
MSTTTTASIEGYKLGKVIIEGKTKQVYDLPEQPGLCLLLSKDRITAGDGVKAHDLAGKAEISNTTNGQVFRLLNEAGIRTAYVKQCGAKAFIARKCQMIPIEWVTRRLATGSFLKRNVGVPEGYRFSPPKQETFFKDDANHDPQWSEEQIVSAKFELNGLVIGQDEVDIMRRTTLLVFEILERAWQTKNCALIDMKVEFGICDDGNIVLADIIDSDSWRLWPAGDKRLMVDKQVYRNLASVTASDLDTVKRNFIWVAEQLADIVPKKDHLVVILMGSASDISHSEKIATSCRSLGLNVELRVSSAHKGPEETLRIVREYESVMSNLIFVAVAGRSNGLGPVVSGSTNYPVINCPPVKSDNMQVDVWSSLNLPSGLGCATVLYPEAAALHAATILGLGNFMVWSKLRVKALNNFITLKKADKELRGVRNA
Protein: Lysin (EC 3.5.1.28) (Cell wall hydrolase) (Lytic amidase) (N-acetylmuramoyl-L-alanine amidase) (O03979)
Organism: Pneumococcus phage Dp-1 (Bacteriophage Dp-1)
Function: Lysis of bacterial host cell wall.
Subcellular location: Host cell wall. Note=Binds to the choline residues present in the cell wall substrate.
Interaction partners:
Sequence:
MGVDIEKGVAWMQARKGRVSYSMDFRDGPDSYDCSSSMYYALRSAGASSAGWAVNTEYMHAWLIENGYELISENAPWDAKRGDIFIWGRKGASAGAGGHTGMFIDSDNIIHCNYAYDGISVNDHDERWYYAGQPYYYVYRLTNANAQPAEKKLGWQKDATGFWYARANGTYPKDEFEYIEENKSWFYFDDQGYMLAEKWLKHTDGNWYWFDRDGYMATSWKRIGESWYYFNRDGSMVTGWIKYYDNWYYCDATNGDMKSNAFIRYNDGWYLLLPDGRLADKPQFTVEPDGLITAKV
Protein: B-cell CLL/lymphoma 7 protein family member A (Q4VC05)
Organism: Homo sapiens (Human)
Interaction partners:
- SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily A member 4
- SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily B member 1
- AT-rich interactive domain-containing protein 1A
- SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily D member 1
- Actin-like protein 6A
- SWI/SNF complex subunit SMARCC1
- SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily A member 2
- SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily E member 1
- Bromodomain-containing protein 9
- SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily D member 2
Sequence:
MSGRSVRAETRSRAKDDIKRVMAAIEKVRKWEKKWVTVGDTSLRIYKWVPVTEPKVDDKNKNKKKGKDEKCGSEVTTPENSSSPGMMDMHDDNSNQSSIADASPIKQENSSNSSPAPEPNSAVPSDGTEAKVDEAQADGKEHPGAEDASDEQNSQSSMEHSMNSSEKVDRQPSGDSGLAAETSAISQDLEGVPPSKKMKLEASQQNSEEM
Protein: Tubulin-specific chaperone D (A0A0R4IXD9)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
- Tubulin-specific chaperone E
- ADP-ribosylation factor-like 2
- Tubulin-specific chaperone C
- Tubulin folding cofactor B.
- UDP-GlcNAc:betaGal beta-1,3-N-acetylglucosaminyltransferase-like 1.
- protein-ribulosamine 3-kinase
- Protein XRP2
- Kinetochore scaffold 1.
- Alcohol dehydrogenase iron-containing 1.
- CDP-diacylglycerol--glycerol-3-phosphate 3-phosphatidyltransferase
Sequence:
MSVMEGACNGEDAEVLAQACVLSEFTESTETRALISSLPDIHHDTVSREATIEKFVVIMDRYQEQPHLLDPHLEWMLNMLLEMIRSEKSPPLLVHLCFKFLYIISKVRGYKIFMQLFPHEVSDVQPVLDLLCRQDQKDTETWETRYILLLWLSMTCLIPFDLSRLDGHLSTVPGTNRESTMDRILEVAKSFLRVSDKSRDAASVLVSKFVTRPDVKQKRLGDFLDWCLTTISQSSEMTMEGTVILDGALQSLAQLFKHGKRDDFLQYAPTVLECLNQKKIAESNQATLRKLGVKVVQRLGLTFLKPRLAKWRYQRGSRSLAVNLAQSSVTESVEATKPDLESVSQEEDYDIPQEVENVIEQLLLGLKDKETIVRWSSAKGIGRVTGRLPKELADDVVESVLDCFSFQETDNAWHGGCLALAELGRRGLLLPSRLSDVVPLILKALTYDEKRGACSLGSNVRDAGCYVCWAFARAYEPTELKPYVNQIASSLVIATVFDRNVTCRKAASAAFQENVGRQGTFPHGIDIITAADYFTVGNLNNCYLTISVYIAGFEEYTKPLIDHLVAMKINHWDGAIRELATKALHNLTIQAPEYMANTVLPQLLPMATGMDLHSRHGAILACAEITHALYKLAAQNNRSVTDLMSSDTIEGLKDIHQKLSDRKQYRGFGGELMRPAVCSLIEKLSLSKMPFKDEPVIAGWQWLIDDSLKNLHLFSSGVRRGIQDAAVSALAALCWQYYQVEPGVADVKMQEELVSQYLSALQSPEVLTRCGCALALGSLPPFMIHNKLQQILSGLQATCRVAQKGESLTEARRDAATAMSQVCVAVGVCAQGRSDQVLCEDNIRPVYEALLGCMNDYSTDSRGDVGAWVRAAAMSSLMDVTLLVVASAPELLSSDLVLRMMCCLAQQAAEKIDRYRAHAGTVFLRLLHGTDPAVPHIPHHEELLSIFPPETGNSLNWNAASQAFPHITQLLRLPQYQYHTLLGLCVSVGGLTESTVRFSSQSLFDYLKGIQQDFTMLQQFGDTLLRIFRDNLRNDRVSVPLLKMVDQILANGCFDLFTRQESHPFCVELLSLCKEEIKKSKDVQKLLSCIAVFCGLVQFPGDVRKKVLVQLLMLLCHPFPLIRKTTASQVYEMLLTYDDVIEDEQVLADVMASLSDTNWESDIATVRSHRNQLCDWLGVPKPTLVAKTSPQ
Protein: Insulin-degrading enzyme (EC 3.4.24.56) (A0A0R4IL71)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
- Insulin
- Membrane metallo-endopeptidase-like 1
- Ubiquitin-ribosomal protein eS31 fusion protein
- Amyloid beta
- Insulin-like growth factor 2
- Amyloid beta
- Natriuretic peptide A
- Protransforming growth factor alpha precursor
- Natriuretic peptide B
- Ubiquitin-ribosomal protein eL40 fusion protein
Sequence:
MILSTVFGRSIRRVSTLSIRMSDPAVKRVVSDIIRSPEDKREYRGLEFTNGLKAILISDPTTDKSSAALDVHMGSLSDPENISGLAHFCEHMLFLGTEKYPKENEYSQFLSEHAGSSNAFTSGEHTNYYFDVSHEHLQGALDRFAQFFLCPLFDESCKDREVNAVDSEHEKNLMNDAWRLFQLEKATGNPKHPFSKFGTGNKLTLETRPSQQGIDIREELLKFHSTYYSSNLMGLCVLGRETLDELTSMVVKLFGEVENKNVPVPEFPTHPFQEEHLRQFYKVVPIKDIRNLYVTFPIPDLQKYYKSNPGHYLGHLIGHEGPGSLLSELKSKGWVNTLVGGQKEGARGFMFFIINVDLTEEGLLHVEDIIFHMFQYIQKLRTEGPQEWVFQECKDLNTVAFRFKDKERPRGYTSKVAGLLHYYPLEEILAAEYLLEEFRPDLIEMVLDKLRPENVRVAVVSKSFEGQTDRTEEWYGTQYKQEAITDEAIKKWDNADLNGKFKLPMKNEFIPTNFEIYPLEKDSPSAPTLIKDTAMSKVWFKQDDKFFLPKACLNFEFFSPFAYVDPLHCNMAYLYLELLKDSLNEYAYAAELAGLSYDLQNTVYGMYLSVKGYNDKQHILLKKIIEKMATFEIDEKRFDIIKEAYMRSLNNFRAEQPHQHAMYYLRLLMTEVAWTKDELRDALDDVTLPRLKAFIPQLLSRLHIEALLHGNITKQSALEMMQMLEDTLIEHAHTKPLLPSQLIRYREVQVPDGGWYVYQQRNEVHNNCGIEIYYQTDMQNTHENMLLELFCQIISEPCFNTLRTKEQLGYIVFSGPRRANGVQGLRFIIQSEKAPHYLESRVEAFLKTMEKSVEEMGDEAFQKHIQALAIRRLDKPKKLAAECAKYWGEIISQQYNFDRDNIEVAYLKTLTKEHIMQFYRDLLAIDAPRRHKVSVHVLSREMDSCPLVGEFPAQNDVNLAPAPSLPQPSLVQDMTEFKRSLPLFPLTKPHINFMAAKL
Protein: Splicing factor U2AF 65 kDa subunit (U2 auxiliary factor 65 kDa subunit) (hU2AF(65)) (hU2AF65) (U2 snRNP auxiliary factor large subunit) (P26368)
Organism: Homo sapiens (Human)
Function: Plays a role in pre-mRNA splicing and 3'-end processing. By recruiting PRPF19 and the PRP19C/Prp19 complex/NTC/Nineteen complex to the RNA polymerase II C-terminal domain (CTD), and thereby pre-mRNA, may couple transcription to splicing. Induces cardiac troponin-T (TNNT2) pre-mRNA exon inclusion in muscle. Regulates the TNNT2 exon 5 inclusion through competition with MBNL1. Binds preferentially to a single-stranded structure within the polypyrimidine tract of TNNT2 intron 4 during spliceosome assembly. Required for the export of mRNA out of the nucleus, even if the mRNA is encoded by an intron-less gene. Represses the splicing of MAPT/Tau exon 10. Positively regulates pre-mRNA 3'-end processing by recruiting the CFIm complex to cleavage and polyadenylation signals.
Subcellular location: Nucleus.
Interaction partners:
- Splicing factor U2AF 35 kDa subunit
- Splicing factor 3B subunit 1
- Splicing factor 3B subunit 4
- Splicing factor 1
- Splicing factor 3B subunit 6
- Splicing factor 3B subunit 3
- PHD finger-like domain-containing protein 5A
- Splicing factor 3B subunit 2
- Serine/arginine-rich splicing factor 1
- Splicing factor 3B subunit 5
Sequence:
MSDFDEFERQLNENKQERDKENRHRKRSHSRSRSRDRKRRSRSRDRRNRDQRSASRDRRRRSKPLTRGAKEEHGGLIRSPRHEKKKKVRKYWDVPPPGFEHITPMQYKAMQAAGQIPATALLPTMTPDGLAVTPTPVPVVGSQMTRQARRLYVGNIPFGITEEAMMDFFNAQMRLGGLTQAPGNPVLAVQINQDKNFAFLEFRSVDETTQAMAFDGIIFQGQSLKIRRPHDYQPLPGMSENPSVYVPGVVSTVVPDSAHKLFIGGLPNYLNDDQVKELLTSFGPLKAFNLVKDSATGLSKGYAFCEYVDINVTDQAIAGLNGMQLGDKKLLVQRASVGAKNATLVSPPSTINQTPVTLQVPGLMSSQVQMGGHPTEVLCLMNMVLPEELLDDEEYEEIVEDVRDECSKYGLVKSIEIPRPVDGVEVPGCGKIFVEFTSVFDCQKAMQGLTGRKFANRVVVTKYCDPDSYHRRDFW