wanglab/gogpt-training-data huggingface dataset:
Protein: Transcription factor S (Transcription elongation factor IIS/RNA polymerase subunit homolog) (TFIIS/RPSU homolog) (Q9P9I8)
Organism: Methanothermococcus thermolithotrophicus (Methanococcus thermolithotrophicus)
Function: Induces RNA cleavage activity in the RNA polymerase. In its presence, the cleavage activity of the RNA polymerase truncates the RNA back to position +15 in a stepwise manner by releasing mainly dinucleotides from the 3'-end of the nascent RNA. The truncated RNAs are able to continue elongation. Involved in transcriptional proofreading and fidelity. Misincorporation of nucleotides during elongation of transcription leads to arrested elongation complexes which are rescued by TFS-promoted removal of a dinucleotide from the 3'-end. TFS is able to induce a cleavage resynthesis cycle in stalled elongation complexes (resulting from the next missing nucleotide or a reduced incorporation rate of a wrong nucleotide) preventing misincorporation and enabling proofreading in a post-incorporation manner. Pausing of elongation complexes is the main determinant of TFS-induced RNA cleavage.
Interaction partners:
Sequence:
MVEFCPKCNNIMLPKNGRLKCTVCGFEEELGNRTEEYELKEKIEAKKQEVTVIEDVDTLPTTRIECPSCGNMEASWWLQQTRCADEPETRFYKCKKCGHTWREYD
Protein: PelC (Q9HZE6)
Organism: Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Interaction partners:
- PelD
- PelF
- PelG
- PelE
- PelB
- PelA
- Beta-monoglucosyldiacylglycerol synthase
Sequence:
MQSIRCLALAAVALFMAGCSSFTSESATPLARGAQWGLVPLLNYSQAPQAGERAEQILLSVLAEEGVRPRLYPAQPQGDLQLVDDRERQQRALDWARQQKLAYVVTGSVEEWQYKNGLDGEPAVGVSLQVLEPASGRVLWSTSGARAGWSRESLAGAAQKVLRELVGDLRLE
Protein: Acetate kinase (EC 2.7.2.1) (Acetokinase) (P71104)
Organism: Clostridium acetobutylicum (strain ATCC 824 / DSM 792 / JCM 1419 / IAM 19013 / LMG 5710 / NBRC 13948 / NRRL B-527 / VKM B-1787 / 2291 / W)
Function: Catalyzes the formation of acetyl phosphate from acetate and ATP. Can also catalyze the reverse reaction.
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00020}.
Interaction partners:
- Phosphate acetyltransferase
- Phosphate butyryltransferase
- Pyruvate:ferredoxin oxidoreductase
- Acylphosphatase
- Acyl-CoA dehydrogenase, short-chain specific
- Pyruvate:ferredoxin oxidoreductase
- 3-hydroxybutyryl-CoA dehydrogenase
- Acetyl-CoA acetyltransferase
- L-lactate dehydrogenase 1
- Short-chain-enoyl-CoA hydratase
Sequence:
MKNLVINCGSSSIKYQFIDMKDETVLAKGLVERIGIKGSVITHKVNGEKYVTETPMEDHKKAIKLVLDALLNDEYGVIKNIDEISAVGHRIVHGGEKYANSVLIDEDVMKSIEDCVSLAPLHNPPHIIGINACKELMPNVPMVAVFDTAFHQTIPDYAYMYAIPYEYYDKYKIRKYGFHGTSHKYVSRTAAEFIGKKVEDLKMVVCHMGNGASITAVENGKSVDTSMGFTPLGGLAMGTRSGDMDPAVVTFLMDKLNINASEVNNLLNKKSGIEGLSGISSDMRDIKKGNYVDKDPKAMLAYSVFNYKIKQFIGSYTAVMNGLDCLVFTGGIGENSFENRREICKNMDYLGIKIDDKKNDETMGIPMDISAEGSKVRVLVIPTNEELMIARDTKDIVGKLK
Protein: Glypican-3 (I6QTG3)
Organism: Homo sapiens (Human)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004471}; Lipid-anchor, GPI-anchor {ECO:0000256|ARBA:ARBA00004471}; Extracellular side {ECO:0000256|ARBA:ARBA00004471}.
Interaction partners:
Sequence:
MAGTVRTACLVVAMLLSLDFPGQAQPPPPPPDATCHQVRSFFQRLQPGLKWVPETPVPGSDLQVCLPKGPTCCSRKMEEKYQLTARLNMEQLLQSASMELKFLIIQNAAVFQEAFEIVVRHAKNYTNAMFKNNYPSLTPQAFEFVGEFFTDVSLYILGSDINVDDMVNELFDSLFPVIYTQLMNPGLPDSALDINECLRGARRDLKVFGNFPKLIMTQVSKSLQVTRIFLQALNLGIEVINTTDHLKFSKDCGRMLTRMWYCSYCQGLMMVKPCGGYCNVVMQGCMAGVVEIDKYWREYILSLEELVNGMYRIYDMENVLLGLFSTIHDSIQYVQKNAGKLTTTIGKLCAHSQQRQYRSAYYPEDLFIDKKVLKVAHVEHEETLSSRRRELIQKLKSFISFYSALPGYICSHSPVAENDTLCWNGQELVERYSQKAARNGMKNQFNLHELKMKGPEPVVSQIIDKLKHINQLLRTMSMPKGRVLDKNLDEEGFESGDCGDDEDECIGGSGDGMIKVKNQLRFLAELAYDLDVDDAPGNSQQATPKDNEISTFHNLGNVHSPLKLLTSMAISVVCFFFLVH
Protein: Cytochrome P450 2A6 (EC 1.14.14.-) (1,4-cineole 2-exo-monooxygenase) (CYPIIA6) (Coumarin 7-hydroxylase) (Cytochrome P450 IIA3) (Cytochrome P450(I)) (P11509)
Organism: Homo sapiens (Human)
Function: Exhibits a high coumarin 7-hydroxylase activity. Can act in the hydroxylation of the anti-cancer drugs cyclophosphamide and ifosphamide. Competent in the metabolic activation of aflatoxin B1. Constitutes the major nicotine C-oxidase. Acts as a 1,4-cineole 2-exo-monooxygenase. Possesses low phenacetin O-deethylation activity.
Subcellular location: Endoplasmic reticulum membrane; Peripheral membrane protein. Microsome membrane; Peripheral membrane protein.
Interaction partners:
- Cytochrome P450 2A7
- Cytochrome P450 3A4)
- UDP-glucuronosyltransferase 2B7
- UDP-glucuronosyltransferase 1A4
- Cytochrome P450 4A11
- Cytochrome P450 1A2
- UDP-glucuronosyltransferase 1A6
- UDP-glucuronosyltransferase 2B10
- UDP-glucuronosyltransferase 1A10
- UDP-glucuronosyltransferase 1A7
Sequence:
MLASGMLLVALLVCLTVMVLMSVWQQRKSKGKLPPGPTPLPFIGNYLQLNTEQMYNSLMKISERYGPVFTIHLGPRRVVVLCGHDAVREALVDQAEEFSGRGEQATFDWVFKGYGVVFSNGERAKQLRRFSIATLRDFGVGKRGIEERIQEEAGFLIDALRGTGGANIDPTFFLSRTVSNVISSIVFGDRFDYKDKEFLSLLRMMLGIFQFTSTSTGQLYEMFSSVMKHLPGPQQQAFQLLQGLEDFIAKKVEHNQRTLDPNSPRDFIDSFLIRMQEEEKNPNTEFYLKNLVMTTLNLFIGGTETVSTTLRYGFLLLMKHPEVEAKVHEEIDRVIGKNRQPKFEDRAKMPYMEAVIHEIQRFGDVIPMSLARRVKKDTKFRDFFLPKGTEVYPMLGSVLRDPSFFSNPQDFNPQHFLNEKGQFKKSDAFVPFSIGKRNCFGEGLARMELFLFFTTVMQNFRLKSSQSPKDIDVSPKHVGFATIPRNYTMSFLPR
Protein: Mediator of RNA polymerase II transcription subunit 8 (Mediator complex subunit 8) (A1ZBT5)
Organism: Drosophila melanogaster (Fruit fly)
Function: Component of the Mediator complex, a coactivator involved in the regulated transcription of nearly all RNA polymerase II-dependent genes. Mediator functions as a bridge to convey information from gene-specific regulatory proteins to the basal RNA polymerase II transcription machinery. Mediator is recruited to promoters by direct interactions with regulatory proteins and serves as a scaffold for the assembly of a functional preinitiation complex with RNA polymerase II and the general transcription factors (By similarity). Required for activated transcription of the MtnA and MtnB genes.
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
- Mediator of RNA polymerase II transcription subunit 22
- Mediator of RNA polymerase II transcription subunit 18
- Mediator of RNA polymerase II transcription subunit 20
- Mediator of RNA polymerase II transcription subunit 6
- Mediator of RNA polymerase II transcription subunit 11
- Mediator of RNA polymerase II transcription subunit 17
- Mediator of RNA polymerase II transcription subunit 14
- Mediator of RNA polymerase II transcription subunit 4
- Mediator of RNA polymerase II transcription subunit 30
- Mediator of RNA polymerase II transcription subunit 31
Sequence:
MQRDEKLFELTLDTVLQRLNDLKLAVLSMIQKLELEYETINWPTFLDNFAIISSHLTGLTKILAKEQCPPLRNRTVLPLLVSMDRDDTLINITEGRVPVFSHDIVPDYLRTRPDPITEQKMLQNEQKAANLTNDAAMKQVTQYNKVVSHVLDMVSKAREEWEIESSSRTGIQQTSSMADTQLLVAAVGMGKGLKLTNYGPGPGMMVPPSIRAPSPMGGPAMSPGNVQQQLGKAPSAVKTNIKSANQVHPFSR
Protein: Exosome complex component Rrp42 (Q9UXC0)
Organism: Saccharolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2) (Sulfolobus solfataricus)
Function: Non-catalytic component of the exosome, which is a complex involved in RNA degradation. Contributes to the structuring of the Rrp41 active site.
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00622}.
Interaction partners:
- Exosome complex component Rrp4
- Exosome complex component Csl4
- Exosome complex component Rrp41
- DNA primase DnaG
- K Homology domain-containing protein
- Ribosomal RNA small subunit methyltransferase Nep1
- Pre mRNA splicing protein
- RNA 3'-terminal phosphate cyclase
- Small ribosomal subunit protein eS6
- Ribosome assembly factor SBDS
Sequence:
MSSTPSNQNIIPIIKKESIVSLFEKGIRQDGRKLTDYRPLSITLDYAKKADGSALVKLGTTMVLAGTKLEIDKPYEDTPNQGNLIVNVELLPLAYETFEPGPPDENAIELARVVDRSLRDSKALDLTKLVIEPGKSVWTVWLDVYVLDYGGNVLDACTLASVAALYNTKVYKVEQHSNGISVNKNEVVGKLPLNYPVVTISVAKVDKYLVVDPDLDEESIMDAKISFSYTPDLKIVGIQKSGKGSMSLQDIDQAENTARSTAVKLLEELKKHLGI
Protein: Hydroxymethylglutaryl-CoA synthase, mitochondrial (HMG-CoA synthase) (EC 2.3.3.10) (3-hydroxy-3-methylglutaryl coenzyme A synthase) (P54868)
Organism: Homo sapiens (Human)
Function: Catalyzes the first irreversible step in ketogenesis, condensing acetyl-CoA to acetoacetyl-CoA to form HMG-CoA, which is converted by HMG-CoA reductase (HMGCR) into mevalonate.
Subcellular location: Mitochondrion {ECO:0000250|UniProtKB:P22791}.
Interaction partners:
- 3-hydroxy-3-methylglutaryl-coenzyme A reductase
- Acetyl-CoA acetyltransferase, mitochondrial
- 3-ketoacyl-CoA thiolase, mitochondrial
- Trifunctional enzyme subunit beta, mitochondrial
- Acetyl-CoA acetyltransferase, cytosolic
- Hydroxymethylglutaryl-CoA lyase, mitochondrial
- 3-ketoacyl-CoA thiolase, peroxisomal
- Farnesyl pyrophosphate synthase
- 3-hydroxy-3-methylglutaryl-CoA lyase, cytoplasmic
- Peroxisomal bifunctional enzyme
Sequence:
MQRLLTPVKRILQLTRAVQETSLTPARLLPVAHQRFSTASAVPLAKTDTWPKDVGILALEVYFPAQYVDQTDLEKYNNVEAGKYTVGLGQTRMGFCSVQEDINSLCLTVVQRLMERIQLPWDSVGRLEVGTETIIDKSKAVKTVLMELFQDSGNTDIEGIDTTNACYGGTASLFNAANWMESSSWDGRYAMVVCGDIAVYPSGNARPTGGAGAVAMLIGPKAPLALERGLRGTHMENVYDFYKPNLASEYPIVDGKLSIQCYLRALDRCYTSYRKKIQNQWKQAGSDRPFTLDDLQYMIFHTPFCKMVQKSLARLMFNDFLSASSDTQTSLYKGLEAFGGLKLEDTYTNKDLDKALLKASQDMFDKKTKASLYLSTHNGNMYTSSLYGCLASLLSHHSAQELAGSRIGAFSYGSGLAASFFSFRVSQDAAPGSPLDKLVSSTSDLPKRLASRKCVSPEEFTEIMNQREQFYHKVNFSPPGDTNSLFPGTWYLERVDEQHRRKYARRPV
Protein: Thiamine thiazole synthase, chloroplastic (EC 2.4.2.60) (Thiazole biosynthetic enzyme) (Q38814)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Involved in biosynthesis of the thiamine precursor thiazole. Catalyzes the conversion of NAD and glycine to adenosine diphosphate 5-(2-hydroxyethyl)-4-methylthiazole-2-carboxylic acid (ADT), an adenylated thiazole intermediate. The reaction includes an iron-dependent sulfide transfer from a conserved cysteine residue of the protein to a thiazole intermediate. The enzyme can only undergo a single turnover, which suggests it is a suicide enzyme. May have additional roles in adaptation to various stress conditions and in DNA damage tolerance. Acts as a positive regulator for the abscisic acid-induced activation of slow type anion channels during stomatal closure by repressing CPK33 kinase activity.
Subcellular location: Plastid, chloroplast {ECO:0000269|PubMed:12482914, ECO:0000269|PubMed:18431481, ECO:0000269|PubMed:26662273}. Mitochondrion {ECO:0000269|PubMed:12482914}. Cell membrane {ECO:0000269|PubMed:26662273}.
Interaction partners:
- Bifunctional TH2 protein, mitochondrial
- Phosphomethylpyrimidine synthase, chloroplastic
- Thiamine biosynthetic bifunctional enzyme TH1
- Hydroxyethylthiazole kinase
- Thiamine pyrophosphokinase 1
- Thiamine pyrophosphokinase 2
- Calcium-dependent protein kinase 33
- At1g09850
- Purine-uracil permease NCS1
- Thiol protease aleurain
Sequence:
MAAIASTLSLSSTKPQRLFDSSFHGSAISAAPISIGLKPRSFSVRATTAGYDLNAFTFDPIKESIVSREMTRRYMTDMITYAETDVVVVGAGSAGLSAAYEISKNPNVQVAIIEQSVSPGGGAWLGGQLFSAMIVRKPAHLFLDEIGVAYDEQDTYVVVKHAALFTSTIMSKLLARPNVKLFNAVAAEDLIVKGNRVGGVVTNWALVAQNHHTQSCMDPNVMEAKIVVSSCGHDGPFGATGVKRLKSIGMIDHVPGMKALDMNTAEDAIVRLTREVVPGMIVTGMEVAEIDGAPRMGPTFGAMMISGQKAGQLALKALGLPNAIDGTLVGNLSPELVLAAADSAETVDA
Protein: Coiled-coil domain-containing protein 77 (Q9BR77)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MNFTPTHTPVCRKRTVVSKRGVAVSGPTKRRGMADSLESTPLPSPEDRLAKLHPSKELLEYYQKKMAECEAENEDLLKKLELYKEACEGQHKLECDLQQREEEIAELQKALSDMQVCLFQEREHVLRLYSENDRLRIRELEDKKKIQNLLALVGTDAGEVTYFCKEPPHKVTILQKTIQAVGECEQSESSAFKADPKISKRRPSRERKESSEHYQRDIQTLILQVEALQAQLGEQTKLSREQIEGLIEDRRIHLEEIQVQHQRNQNKIKELTKNLHHTQELLYESTKDFLQLRSENQNKEKSWMLEKDNLMSKIKQYRVQCKKKEDKIGKVLPVMHESHHAQSEYIKSLKDKLVQEKKLSNMYQEQCISLEEELARIREEEGMRREIFKDRTNKMGKRLQIMTKRYEALERRRILEVEGFKTDIKVLRQKLKDLEQMLYKATVNARANQDLALLCEVRDSNRRAHKIQGELKNLKSKVFGLENELRLC
Protein: Structural polyprotein (PP) [Cleaved into: Precursor of VP2 (Pre-VP2); Capsid protein VP2; Structural peptide 1 (p1) (pep46); Structural peptide 2 (p2) (pep7a); Structural peptide 3 (p3) (pep7b); Protease VP4 (EC 3.4.21.-) (Non-structural protein VP4) (NS); Capsid protein VP3] (Q9WR38)
Organism: Avian infectious bursal disease virus (IBDV) (Gumboro disease virus)
Subcellular location: Virion {ECO:0000256|ARBA:ARBA00004328}.; SUBCELLULAR LOCATION: [Structural peptide 2]: Virion {ECO:0000256|RuleBase:RU363030}. Host cytoplasm {ECO:0000256|RuleBase:RU363030}.; SUBCELLULAR LOCATION: [Structural peptide 3]: Virion {ECO:0000256|RuleBase:RU363030}. Host cytoplasm {ECO:0000256|RuleBase:RU363030}.; SUBCELLULAR LOCATION: [Capsid protein VP3]: Virion {ECO:0000256|RuleBase:RU363030}. Host cytoplasm {ECO:0000256|RuleBase:RU363030}.; SUBCELLULAR LOCATION: [Capsid protein VP2]: Virion {ECO:0000256|RuleBase:RU363030}. Host cytoplasm {ECO:0000256|RuleBase:RU363030}.; SUBCELLULAR LOCATION: [Structural peptide 1]: Virion {ECO:0000256|RuleBase:RU363030}. Host cytoplasm {ECO:0000256|RuleBase:RU363030}.
Interaction partners:
Sequence:
MTNLTDQTQQIVPFIRSLLMPTTGPASIPDDTLEKHTLRSETSTYNLTVGDTGSGLIVFFPGFPGSIVGAHYTLQSNGNYKFDQMLLTAQNLPASYNYCRLVSRSLTVRSSTLPGGVYALNGTINAVTFQGSLSDLTDVSYNGLMSATANINDKIGNVLVGEGVTVLSLPTSYDLGYVRLGDPIPAIGLDPKMVATCDSSDRPRVYTITAADDYQFSSQYQSGGVTITLFSANIDAITSLSIGGELVFHTSVHGLALDATIYLIGFDGTTVITRAVASDNGLTTGIDNLMPFNLVIPTNEITQPITSIKLEIVTSKSGGQAGDQMSWSAMWSLAVTIHGGNYPGALRPVTLVAYERVATGSVVTVAGVSNFELIPNPELAKNLVTEYGRFDPGAMNYTKLILSERERLGIKTVWPTREYTDFREYFMEVADLNSPLKIAGAFGFKDIIRAIRRIAVPVVSTLFPPAAPLALAIGEGVNYLLGDEAQAASGTARAASGKARAASGRIRQLTLAADKGYEVVANLFQVPQNPVVDGILASPGVLRGAHNLDCVLREGATLFPVVITTVEDAMTPKALNSKMFAVIEGVREDLQPPSQRGSFIRTLSGHRVYGYAPDGVLPLETGRDYTVVPIDDVWDDSIMLSKDPIPPIVGNSGNLAIAYMDVFRPKVPIHVAMTGALNACGEIEKVSFRSTKLATAHRLGLKLAGPGAFDVNTGPNWATFIKRFPHNPRDWDRLPYLNLPYLPPNAGRQYHLAMAASEFKETPELESAVRAMEAAASVDPLFQSAISVFMWLEENGIVTDMANFALSDPNAHRMRNFLANAPQAGSKSQRAKYGTAGYGVEARSPTPEEAQREKDTRISKKMETMGIYFATPEWVALNGHRGPSPGQLKYWQNTREIPDPNEDYLDYVHAEKSRLASEEQIQRAATSIYGAPGQAEPPQAFIDEVAKVYEINHGRGPNQEQMKDLLLTAMEMKHRNPRRAPPKPKPKPNAPTPRPPGRLGRWIRTVSDEDLE
Protein: CHCH domain-containing protein (Q38EG3)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MGSGLLGNVASVAAGSVIGHGITHMLFDRNAPPAQPTELQQVAQQVCNGACAAHVQTYAKCLEANEGNAAPCKWAWETFTQCQSEQQPTQ
Protein: Large ribosomal subunit protein uL6B (60S ribosomal protein L9-B) (O74905)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus {ECO:0000269|PubMed:16823372}. Nucleus, nucleolus {ECO:0000269|PubMed:16823372}.
Interaction partners:
- Elongation factor 3
- Small ribosomal subunit protein uS15
- mRNA export factor elf1
- Large ribosomal subunit protein uL10
- Small ribosomal subunit protein uS10
- Small ribosomal subunit protein uS3
- Large ribosomal subunit protein eL6
- Large ribosomal subunit protein uL24
- Large ribosomal subunit protein uL30B
- Large ribosomal subunit protein uL29
Sequence:
MGRDIYKDETLTIPEGVSVDIKARLVTVKGPRGVLKQNLRRVDIELKKQGNTIKFIVWHGSRKHNACIRTAYSIINNMIIGVTQGFRYKMRLVYAHFPININLTENGTVVEIRNFLGERITRVIKCLPGVTVSISSAVKDEIIIEGNSLENVSQSAANIKQICNVRNKDIRKFLDGIYVSERGNIEELE
Protein: Syntaxin-3 (Q64704)
Organism: Mus musculus (Mouse)
Function: Potentially involved in docking of synaptic vesicles at presynaptic active zones. Apical receptor involved in membrane fusion of apical vesicles (By similarity). Essential for survival of retinal photoreceetors.
Subcellular location: Membrane {ECO:0000305}; Single-pass type IV membrane protein {ECO:0000305}. Note=Localized to the inner and outer plexiform layers, the cell body and the inner segments of photoreceptors. {ECO:0000269|PubMed:28369466}.; SUBCELLULAR LOCATION: [Isoform 3B]: Photoreceptor inner segment {ECO:0000269|PubMed:26406599}. Cell projection, cilium, photoreceptor outer segment {ECO:0000269|PubMed:26406599}. Note=Colocalizes with SNAP25 and ROM1 in the inner segment and outer nuclear layer of the retina (at protein level) (PubMed:26406599). Partially colocalizes with PRPH2 in the inner segment of the retina (at protein level) (PubMed:26406599). {ECO:0000269|PubMed:26406599}.
Interaction partners:
- Synaptosomal-associated protein 23
- Vesicle-associated membrane protein 8
- Vesicle-associated membrane protein 2
- Vesicle-associated membrane protein 3
- Synaptosomal-associated protein 25
- Synaptosomal-associated protein 29
- Vesicle-associated membrane protein 4
- Syntaxin-binding protein 1
- Syntaxin-4
- Vesicle-trafficking protein SEC22b
Sequence:
MKDRLEQLKAKQLTQDDDTDEVEIAIDNTAFMDEFFSEIEETRLNIDKISEHVEEAKKLYSIILSAPIPEPKTKDDLEQLTTEIKKRANNVRNKLKSMEKHIEEDEVRSSADLRIRKSQHSVLSRKFVEVMTKYNEAQVDFRERSKGRIQRQLEITGKKTTDEELEEMLESGNPAIFTSGIIDSQISKQALSEIEGRHKDIVRLESSIKELHDMFMDIAMLVENQGEMLDNIELNVMHTVDHVEKARDETKRAMKYQGQARKKLIIIIVVVVVLLGILALIIGLSVGLK
Protein: Quercetin 2,3-dioxygenase (Quercetinase) (EC 1.13.11.24) (Pirin-like protein YhhW) (P46852)
Organism: Escherichia coli (strain K12)
Function: Has quercetin 2,3-dioxygenase activity in vitro. Its physiological role is unknown; however, may provide a mechanism that would avoid inhibition of key cellular proteins, such as DNA gyrase, by quercetin.
Interaction partners:
- 4,5-DOPA dioxygenase extradiol
- Inner membrane protein YqjF
- Probable HTH-type transcriptional regulator YhaJ
Sequence:
MIYLRKANERGHANHGWLDSWHTFSFANYYDPNFMGFSALRVINDDVIEAGQGFGTHPHKDMEILTYVLEGTVEHQDSMGNKEQVPAGEFQIMSAGTGIRHSEYNPSSTERLHLYQIWIMPEENGITPRYEQRRFDAVQGKQLVLSPDARDGSLKVHQDMELYRWALLKDEQSVHQIAAERRVWIQVVKGNVTINGVKASTSDGLAIWDEQAISIHADSDSEVLLFDLPPV
Protein: PVR cell adhesion molecule-related 2-like (Si:dkey-225e11.1) (B0CLW6)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004167}; Single-pass membrane protein {ECO:0000256|ARBA:ARBA00004167}.
Interaction partners:
- CD226 molecule.
- Nectin-3-like protein
- Nectin cell adhesion molecule 3
- Afadin, adherens junction formation factor a.
- Nectin cell adhesion molecule 3
- Si:ch211-222f23.6
- Par-3 family cell polarity regulator.
- Par-3 family cell polarity regulator alpha, b.
- Mitochondrial import receptor subunit TOM22 homolog
- Translocase of outer mitochondrial membrane 7 homolog
Sequence:
MSDFTMINCCLVLAACLLSSQAVWSQRVRVEYEVTAYPNGSVNLRCEFTNSGTTKLTQVSWMFERAENDRQNIAVFHPQYGASFPNKDFEGRVKFTQGSLENPSIRIDKLRMADAGRYICEYATYPSGNEQGTTTLIMLAKPKNSATAIPVRAGTSEVVVATCAAAQGKPEATISWITTITGRYNHTSVPESDGTVTVKSEYRMIPTPVENGKEITCVVNQRTQMEDKVFNLKLVVEYPPTVTIDGYDNNWYMGRTDVYLTCEADANPEPSEISWTVATGQMPSSVRVEENRLLVRKVDETVNTTFVCEVKNRLGTGKKELVALVIGE
Protein: Branched-chain-amino-acid aminotransferase, mitochondrial (BCAT(m)) (EC 2.6.1.42) (Placental protein 18) (PP18) (O15382)
Organism: Homo sapiens (Human)
Function: Catalyzes the first reaction in the catabolism of the essential branched chain amino acids leucine, isoleucine, and valine. May also function as a transporter of branched chain alpha-keto acids (By similarity).
Subcellular location: Mitochondrion {ECO:0000250|UniProtKB:O35854}.
Interaction partners:
- 2-oxoisovalerate dehydrogenase subunit alpha, mitochondrial
- 2-oxoisovalerate dehydrogenase subunit beta, mitochondrial
- Cystathionine gamma-lyase
- Alanine--glyoxylate aminotransferase 2, mitochondrial
- L-amino-acid oxidase
- Glutamate--cysteine ligase regulatory subunit
- Branched-chain-amino-acid aminotransferase, cytosolic
- L-serine dehydratase/L-threonine deaminase
- Glutamate--cysteine ligase catalytic subunit
- Serine dehydratase-like
Sequence:
MAAAALGQIWARKLLSVPWLLCGPRRYASSSFKAADLQLEMTQKPHKKPGPGEPLVFGKTFTDHMLMVEWNDKGWGQPRIQPFQNLTLHPASSSLHYSLQLFEGMKAFKGKDQQVRLFRPWLNMDRMLRSAMRLCLPSFDKLELLECIRRLIEVDKDWVPDAAGTSLYVRPVLIGNEPSLGVSQPTRALLFVILCPVGAYFPGGSVTPVSLLADPAFIRAWVGGVGNYKLGGNYGPTVLVQQEALKRGCEQVLWLYGPDHQLTEVGTMNIFVYWTHEDGVLELVTPPLNGVILPGVVRQSLLDMAQTWGEFRVVERTITMKQLLRALEEGRVREVFGSGTACQVCPVHRILYKDRNLHIPTMENGPELILRFQKELKEIQYGIRAHEWMFPV
Protein: Serine/threonine protein phosphatase PstP (EC 3.1.3.16) (Mycobacterial Ser/Thr phosphatase) (Mstp) (PP2C-family Ser/Thr phosphatase) (P9WHW5)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: Plays an important role in regulating cell division and growth by reversible phosphorylation signaling. May play important roles in regulating cellular metabolism and signaling pathways, which could mediate the growth and development of the cell. Plays a role in establishing and maintaining infection. Dephosphorylates several proteins, including the kinases PknA, PknB, PknD, PknE, PknF, PknH, PknJ and Pyk, the transcriptional regulatory proteins EmbR and EthR, the osmosensory protein OprA and the dimycocerosyl transferase PapA5. In vitro, dephosphorylates the phosphorylated Ser/Thr residues of myelin basic protein (MBP), histone and casein phosphorylated at Ser/Thr residues, but fails to dephosphorylate phosphotyrosine residue of these substrates.
Subcellular location: Cell membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000255}.
Interaction partners:
- Serine/threonine-protein kinase PknB
- Serine/threonine-protein kinase PknA
- Peptidoglycan D,D-transpeptidase PbpA
- FHA domain-containing protein FhaB
- Peptidoglycan glycosyltransferase RodA
- FHA domain-containing protein FhaA
- Serine/threonine-protein kinase PknL
- Putative methyltransferase Rv1407
- Serine/threonine-protein kinase PknD
- Serine/threonine-protein kinase PknE
Sequence:
MARVTLVLRYAARSDRGLVRANNEDSVYAGARLLALADGMGGHAAGEVASQLVIAALAHLDDDEPGGDLLAKLDAAVRAGNSAIAAQVEMEPDLEGMGTTLTAILFAGNRLGLVHIGDSRGYLLRDGELTQITKDDTFVQTLVDEGRITPEEAHSHPQRSLIMRALTGHEVEPTLTMREARAGDRYLLCSDGLSDPVSDETILEALQIPEVAESAHRLIELALRGGGPDNVTVVVADVVDYDYGQTQPILAGAVSGDDDQLTLPNTAAGRASAISQRKEIVKRVPPQADTFSRPRWSGRRLAFVVALVTVLMTAGLLIGRAIIRSNYYVADYAGSVSIMRGIQGSLLGMSLHQPYLMGCLSPRNELSQISYGQSGGPLDCHLMKLEDLRPPERAQVRAGLPAGTLDDAIGQLRELAANSLLPPCPAPRATSPPGRPAPPTTSETTEPNVTSSPASPSPTTSAPAPTGTTPAIPTSASPAAPASPPTPWPVTSSPTMAALPPPPPQPGIDCRAAA
Protein: N-acetylmuramoyl-L-alanine amidase (EC 3.5.1.28) (N-acetylmuramoyl-L-alanine amidase) (J9PU17)
Organism: Bacillus phage BPS13
Interaction partners:
Sequence:
MNINTQYLVTDPERLKVIGPNWMNPTEITFHNTYNDASASAEVRNVRNNSTGTSFHTAVDDFEVQQVVPFDRNAWHAGDGTYGAGNRNSIGVEICYSMSGGERYRKAELNAIEHISDLMVRFNIPISKVKTHQERNGKYCPHRMLDEGRVGWFKEQCERRANEKRNGGGGAPIEQPKPKPEPTPTPKPPTGDYDSSWFTKETGTFVTNTTIKLRTAPFTSAGVIATLPAGSTVNYNGFGIEYDGYVWIRQPRSNGYGYLATGESRNGKRVNYWGTFK
Protein: Ribosome maturation protein SBDS (A0A0S2Z5I7)
Organism: Homo sapiens (Human)
Subcellular location: Cytoplasm, cytoskeleton, spindle {ECO:0000256|ARBA:ARBA00004186}. Nucleus, nucleolus {ECO:0000256|ARBA:ARBA00004604}. Nucleus, nucleoplasm {ECO:0000256|ARBA:ARBA00004642}.
Interaction partners:
Sequence:
MSIFTPTNQIRLTNVAVVRMKRAGKRFEIACYKNKVVGWRSGVEKDLDEVLQTHSVFVNVSKGQVAKKEDLISAFGTDDQTEICKQILTKGEVQVSDKERHTQLEQMFRDIATIVADKCVNPETKRPYTVILIERAMKDIHYSVKTNKSTKQQALEVIKQLKEKMKIERAHMRLRFILPVNEGKKLKEKLKPLIKVIESEDYGQQLEIVCLIDPGCFREIDELIKKETKGKGSLEVLNLKDVEEGDEKFE