wanglab/gogpt-training-data huggingface dataset:
Protein: DNA (cytosine-5)-methyltransferase 3-like (Q9UJW3)
Organism: Homo sapiens (Human)
Function: Catalytically inactive regulatory factor of DNA methyltransferases that can either promote or inhibit DNA methylation depending on the context (By similarity). Essential for the function of DNMT3A and DNMT3B: activates DNMT3A and DNMT3B by binding to their catalytic domain. Acts by accelerating the binding of DNA and S-adenosyl-L-methionine (AdoMet) to the methyltransferases and dissociates from the complex after DNA binding to the methyltransferases. Recognizes unmethylated histone H3 lysine 4 (H3K4me0) and induces de novo DNA methylation by recruitment or activation of DNMT3. Plays a key role in embryonic stem cells and germ cells (By similarity). In germ cells, required for the methylation of imprinted loci together with DNMT3A (By similarity). In male germ cells, specifically required to methylate retrotransposons, preventing their mobilization (By similarity). Plays a key role in embryonic stem cells (ESCs) by acting both as an positive and negative regulator of DNA methylation (By similarity). While it promotes DNA methylation of housekeeping genes together with DNMT3A and DNMT3B, it also acts as an inhibitor of DNA methylation at the promoter of bivalent genes (By similarity). Interacts with the EZH2 component of the PRC2/EED-EZH2 complex, preventing interaction of DNMT3A and DNMT3B with the PRC2/EED-EZH2 complex, leading to maintain low methylation levels at the promoters of bivalent genes (By similarity). Promotes differentiation of ESCs into primordial germ cells by inhibiting DNA methylation at the promoter of RHOX5, thereby activating its expression (By similarity).
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
- DNA
- DNA
- Histone H3.1
- Histone H3.2
- Histone H3.3
- Histone H3.3C
- Histone H3-7
- Histone H3.1t
- Histone deacetylase 1
- Transcriptional regulator ATRX
Sequence:
MAAIPALDPEAEPSMDVILVGSSELSSSVSPGTGRDLIAYEVKANQRNIEDICICCGSLQVHTQHPLFEGGICAPCKDKFLDALFLYDDDGYQSYCSICCSGETLLICGNPDCTRCYCFECVDSLVGPGTSGKVHAMSNWVCYLCLPSSRSGLLQRRRKWRSQLKAFYDRESENPLEMFETVPVWRRQPVRVLSLFEDIKKELTSLGFLESGSDPGQLKHVVDVTDTVRKDVEEWGPFDLVYGATPPLGHTCDRPPSWYLFQFHRLLQYARPKPGSPRPFFWMFVDNLVLNKEDLDVASRFLEMEPVTIPDVHGGSLQNAVRVWSNIPAIRSRHWALVSEEELSLLAQNKQSSKLAAKWPTKLVKNCFLPLREYFKYFSTELTSSL
Protein: Rifin (C6KTF6)
Organism: Plasmodium falciparum (isolate 3D7)
Interaction partners:
Sequence:
MKVHYINILLFALPLNILIYNQRNHKSTTHHTLKIPTTRLLCECDLYIPNYDNDPQMKKIMENFDRQTSQRFHEYDERMKTTRQKCKDKCDKEIQKIILKDKIDKELTEKFATLQTDIQNDAIPTCVCEKSLADKVEKTCLKCGGVLGGGVTPAWGLISGIVYTGWKAAALAAAKKLAAEAGAAEGASQGAAAGATRLIELIQSTFQVQNIAGQSLESIFTAQTYTDVSNITKALFNEYAEICLPIFTDSVPVRGVRYNISSPICTFVEEGILATSRDKGGSPITFIEKKVETMVSKAEGVATARAADVAAAKTAEFEATKVGAVEATYAGYHTTIIASIIAILIIVLIMVIIYLILRYRRKKKMKKKLQYIKLLEE
Protein: Prostaglandin G/H synthase 1 (EC 1.14.99.1) (Cyclooxygenase-1) (COX-1) (Prostaglandin H2 synthase 1) (PGH synthase 1) (PGHS-1) (PHS 1) (Prostaglandin-endoperoxide synthase 1) (P23219)
Organism: Homo sapiens (Human)
Function: Dual cyclooxygenase and peroxidase in the biosynthesis pathway of prostanoids, a class of C20 oxylipins mainly derived from arachidonate, with a particular role in the inflammatory response. The cyclooxygenase activity oxygenates arachidonate (AA, C20:4(n-6)) to the hydroperoxy endoperoxide prostaglandin G2 (PGG2), and the peroxidase activity reduces PGG2 to the hydroxy endoperoxide PGH2, the precursor of all 2-series prostaglandins and thromboxanes. This complex transformation is initiated by abstraction of hydrogen at carbon 13 (with S-stereochemistry), followed by insertion of molecular O2 to form the endoperoxide bridge between carbon 9 and 11 that defines prostaglandins. The insertion of a second molecule of O2 (bis-oxygenase activity) yields a hydroperoxy group in PGG2 that is then reduced to PGH2 by two electrons. Involved in the constitutive production of prostanoids in particular in the stomach and platelets. In gastric epithelial cells, it is a key step in the generation of prostaglandins, such as prostaglandin E2 (PGE2), which plays an important role in cytoprotection. In platelets, it is involved in the generation of thromboxane A2 (TXA2), which promotes platelet activation and aggregation, vasoconstriction and proliferation of vascular smooth muscle cells (Probable).
Subcellular location: Microsome membrane; Peripheral membrane protein. Endoplasmic reticulum membrane; Peripheral membrane protein.
Interaction partners:
- Prostacyclin synthase
- Prostaglandin E synthase
- Polyunsaturated fatty acid 5-lipoxygenase
- Prostaglandin E synthase 2
- Polyunsaturated fatty acid lipoxygenase ALOX15
- Polyunsaturated fatty acid lipoxygenase ALOX12
- Prostaglandin E synthase 3
- Prostaglandin-H2 D-isomerase
- Hematopoietic prostaglandin D synthase
- Prostaglandin G/H synthase 2
Sequence:
MSRSLLLWFLLFLLLLPPLPVLLADPGAPTPVNPCCYYPCQHQGICVRFGLDRYQCDCTRTGYSGPNCTIPGLWTWLRNSLRPSPSFTHFLLTHGRWFWEFVNATFIREMLMRLVLTVRSNLIPSPPTYNSAHDYISWESFSNVSYYTRILPSVPKDCPTPMGTKGKKQLPDAQLLARRFLLRRKFIPDPQGTNLMFAFFAQHFTHQFFKTSGKMGPGFTKALGHGVDLGHIYGDNLERQYQLRLFKDGKLKYQVLDGEMYPPSVEEAPVLMHYPRGIPPQSQMAVGQEVFGLLPGLMLYATLWLREHNRVCDLLKAEHPTWGDEQLFQTTRLILIGETIKIVIEEYVQQLSGYFLQLKFDPELLFGVQFQYRNRIAMEFNHLYHWHPLMPDSFKVGSQEYSYEQFLFNTSMLVDYGVEALVDAFSRQIAGRIGGGRNMDHHILHVAVDVIRESREMRLQPFNEYRKRFGMKPYTSFQELVGEKEMAAELEELYGDIDALEFYPGLLLEKCHPNSIFGESMIEIGAPFSLKGLLGNPICSPEYWKPSTFGGEVGFNIVKTATLKKLVCLNTKTCPYVSFRVPDASQDDGPAVERPSTEL
Protein: Mcf.2 transforming sequence (Q8BLE2)
Organism: Mus musculus (Mouse)
Interaction partners:
Sequence:
MAMALHRVRIAEKYGKNYLCLLQAVFLAETGLLLQLKDINHFLMQDIAFLSGGRGKDNAWIITFPENCNFRCIPEEVIAKVLNYLTSIARQSGSDSRFTIILDRRLDTWASLKISLQKISASFPGSLHLVLVLRPTSFLQRTFTDIGFRFSQEDFMLKLPVVMLSSVSDLLTYIDDKQLTPELGGTLQYCHSEWIIFRNAIEKFAVTVKEMAQMLQSFGTELAETELPQDILSIEEILAGRAERYHLLKNDLTAVTKEGKVLLMNLQVPATEETVSSSLECTQHINGDWQTIKKLLAQVHDMETAFDGFWEKHQLKMEQYLQLWKFEQDFQEAVTQVEFLLSQQRELGDITGNLAQVKQRLKKLEILDDKSQELLTKARIVILRGHKLASNHHYALDLICQRCNELRYLSDILVNEIRTKRVQLSRTFKVHRLLQQARQCCDQGECLLASQGMDKFQTKEDAQKALQDVDNFLQMAMPFINYDIESLQYEFDVLLSPELKAQMQNIQLKLENIRSAFQNQQAGCKSLKEVPEGAFQNLVPASENVMRSRMIFFSPKHVKKSWRQIHAQSNVKVEAVEDSQEKNSDQSPKLDNSLDILKNHVLNELIQTERAYVRELFTVLLGYRSEMDNPQMFDLMPPLLRNKKDVLFGNMAEIYEFHNNIFMSRLEDCSDAPERVGPCFLERKDDFQMYAKYCQNKPRSELIWRKYSECAFFQECQRKLKHRLGLDSYLLKPVQRITKYQLLLKELLKYSKEGEGTTKLKEALDSMLELLKSVNDSMHQTAINGYVGNINELGKMVLQGSFNVWLGHRKGATKMKDFARFKPMQRHLFLYEKAVMFCKRRFESGEGADRYPSYSFKHCLKMEDVGITEHVKGDNRKFEIRYSEKEEIYIVQAPNVDVKMLWLKEIRKILVQQKELMTAKTQQDQALDQDQLFPQQQNAELCKSSPFCVCEETLFNATEAGAEVEQAGALIKVREAAVLAQAEASSAAWNGMLPSAEGAAAIAEHSYNYFSSNNDHGEDRTQMRHMSEVTF
Protein: Caspase b (EC 3.4.22.58) (Caspase 19a) [Cleaved into: Caspase b subunit p20; Caspase b subunit p10] (Q504J1)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Function: Thiol protease which cleaves IL-1 beta (il1b), releasing the mature cytokine which is involved in a variety of inflammatory processes, and mediates apoptosis. Component of the NLRP1 inflammasome, which plays a crucial role in innate immunity and inflammation. In response to pathogens and other damage-associated signals, recruited to the NLRP1 inflammasome in its precursor form following the recruitment of caspase caspa. Its subsequent activation causes the cleavage of the midformed pro-il1b and results in il1b maturation and secretion in the extracellular milieu. Activated by direct binding to bacterial lipopolysaccharides (LPS), which causes non-canonical inflammasome activation and results in the pyroptosis of infected cells and their extrusion into the gut lumen, as well as in cytokine secretion. Plays a crucial role in the restriction of bacterial infection to intestinal sites. Pyroptosis limits bacterial replication, while cytokine secretion promotes the recruitment and activation of immune cells and triggers mucosal inflammation (By similarity). Promotes pyroptosis by bacterial infection by E.piscicida.
Subcellular location: Inflammasome {ECO:0000269|PubMed:30150286}. Cytoplasm {ECO:0000269|PubMed:30150286}. Note=Co-localizes with pycard, caspa and nlrp1 in the cytoplasm (PubMed:30150286). Co-localizes with pycard at large cytoplasmic aggregates, known as specks (PubMed:30150286). {ECO:0000269|PubMed:30150286}.
Interaction partners:
- Apoptosis-associated speck-like protein containing a CARD
- Gasdermin Ea
- Deafness, autosomal dominant 5
- NACHT, LRR and PYD domains-containing protein 1 homolog
- Pejvakin.
- Interleukin-1.
Sequence:
MEDITQLLSDVLEDLVESELKQFTRQLWIGVKPGVEPIPRGKLENKDRQDVVDSMVQQYSEDAGTITVQTLRKIKQNERAKRLESNLLKVQSQGQENKQNSEEPQPIPQIISQPIQQIISQPINNAGSEDLQPIQADWQRPRQIIPCSQETKNTLLKAHGDDIYTPRSGTQRKGLALLITNIQFANTQHNRNGADRDEENAEWLLRSLGFAVIKYRNLSGKDIRRAVENFSKRREHEDADSTFIVIMSHGTRIDNKDAIVGVSDDVYFIEETFSHLNSVNCPALIDKPKVILIQACRGGQSSGVLAQDSVFASDSWVHMEKDFVCFMSTMPNTFAYRNPIEGSFFISYIVDVFCSSAHRDDIMELFRKVTLRMEKDQRFQGQAKLLPCIERTSISKRFYLFPGL
Protein: Serine/threonine-protein kinase SRK2J (EC 2.7.11.1) (OST1-kinase-like 10) (SNF1-related kinase 2.9) (SnRK2.9) (O64812)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- Probable protein phosphatase 2C 78
- Protein phosphatase 2C 3
- Probable protein phosphatase 2C 24
- Protein phosphatase 2C 37
- Probable protein phosphatase 2C 75
- Protein phosphatase 2C 7
- Protein phosphatase 2C 16
- Protein phosphatase 2C 77
- Protein phosphatase 2C 56
- ABSCISIC ACID-INSENSITIVE 5-like protein 5
Sequence:
MEKYEMVKDLGFGNFGLARLMRNKQTNELVAVKFIDRGYKIDENVAREIINHRALNHPNIVRFKEVVLTPTHLGIVMEYAAGGELFERISSVGRFSEAEARYFFQQLICGVHYLHALQICHRDLKLENTLLDGSPAPRLKICDFGYSKSSVLHSNPKSTVGTPAYIAPEVFCRSEYDGKSVDVWSCGVALYVMLVGAYPFEDPKDPRNFRKTVQKIMAVNYKIPGYVHISEDCRKLLSRIFVANPLHRSTLKEIKSHAWFLKNLPRELKEPAQAIYYQRNVNLINFSPQRVEEIMKIVGEARTIPNLSRPVESLGSDKKDDDEEEYLDANDEEWYDDYA
Protein: Adaptor related protein complex 3 subunit delta 1 (A0A8I6GAS3)
Organism: Rattus norvegicus (Rat)
Subcellular location: Endomembrane system {ECO:0000256|ARBA:ARBA00004184}; Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004184}.
Interaction partners:
Sequence:
MALKMVKGSIDRMFDKNLQDLVRGIRNHKEDEAKYISQCIDEIKQELKQDNIAVKANAVCKLTYLQMLGYDISWAAFNIIEVMSASKFTFKRVGYLAASQCFHEGTDVIMLTTNQIRKDLSSPSQYDTGVALTGLSCFVTPDLARDLANDIMTLMSHTKPYIRKKAVLIMYKVFLKYPESLRPAFPRLKEKLEDPDPGVQSAAVNVICELARRNPKNYLSLAPLFFKLMTSSTNNWVLIKIIKLFGALTPLEPRLGKKLIEPLTNLIHSTSAMSLLYECVNTVIAGEPVWLSSFQLCVQKLRILIEDSDQNLKYLGLLAMSKILKTHPKSVQSHKDLILQCLDDKDESIRLRALDLLYGMVSKKNLMEIVKKLMTHVDKAEGTTYRDELLTKIIDICSQSNYQHITNFEWYISILVELTRLEGTRHGHLIAAQMLDVAIRVKAIRKFAVSQMSSLLDSAHLVASSTQRNGICEVLYAAAWICGEFSEHLQGPQQTLEAMLRPKVTTLPGHIQAVYVQNVVKLYASILQQKEQAADTEGAQEVTQLLVERLPQFVQSADLEVQERASCILQLVKHVQKLQAKGVPVAEEVSALFAGELNPVAPKAQKKVPVPEGLDLDAWINEPPSDSESEDEKPKAIFHEEEPRHTRRRQPEEDEEELARRREARKQEQANNPFYIKSSPSPQKASSDMMGFLVSLTCGHPCSPTGMPMSDQYVKLEEQRRHRQRLEKDKKRKKKEKGKRRHSSLPTESDEDIAPAQRVDIITEEMPENALPSDEDDKDPNDPYRALDIDLDKPLADSEKLPVQKHRNAETVKSPEKEGVPGVEKKSKKPKKKEKKPKEREREKKDKKGEDLDFWLSTTPPPAAAPVPAPSTEGLAASIVTPPKGECEVLKGEEPQDEEDHMDHDQERKSSRHKKKKHRKEKEERPRDKKKAKRKQVVQLENGAPAEEEEEEEEPIPPMSSYCLLAENPYIKVTYDVQASLQKDSQVTVSIILENQSSSFLKNMELNVLDSLNTKMARPEGSSVHDGVPVPFQLPPGVSNEAQFVFTIQSIVMAQKLKGTLSFIAKDDEGATHEKLDFRLHFSCSSYLITTPCYSDAFAKLLESGDLSMNSIKVDGISISFQNLLAKICFYHHFSVVERVDSCASMYSRSIQGHHVCLLVKKGESSVSVDGKCSDATLLSSLLEEMKTTLSQC
Protein: NADH:ubiquinone oxidoreductase subunit M (EC 1.6.99.5) (Q5F628)
Organism: Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090)
Subcellular location: Endomembrane system {ECO:0000256|ARBA:ARBA00004127}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004127}. Membrane {ECO:0000256|RuleBase:RU000320}; Multi-pass membrane protein {ECO:0000256|RuleBase:RU000320}.
Interaction partners:
- NADH-quinone oxidoreductase subunit F
- NADH-quinone oxidoreductase subunit H
- NADH-quinone oxidoreductase subunit D
- NADH-quinone oxidoreductase subunit A
- NADH-quinone oxidoreductase subunit K
- NADH:ubiquinone oxidoreductase subunit L
- NADH dehydrogenase
- NADH-quinone oxidoreductase subunit C
- NADH-quinone oxidoreductase subunit I
- NADH-quinone oxidoreductase subunit N
Sequence:
MFSNYLLSLAIWIPIAAGVLVLATGKDSRAPLARVLAFMGALAGFLVTLPLFTGFDRLSGGYQFTEFHEWIPLLKINYALGVDGISVLFIILNAFITLLVVLAGWEVIQKRPAQYMAAFLMMSGLINGAFAAQDAILFYVFFEGMLIPLYLIIGVWGGPRRVYASVKLFLYTLTGSLLMLVAMVYLYYQTGSFSIVDFQNIKQIPLGVQQLLFVAFFLSFAVKVPMFPVHTWLPDAHVEAPTGGSMVLAAITLKLGAYGFLRFILPIMPDAARYFAPVIIVLSLIAVIYIGMVALVQTDMKKLVAYSSISHMGFVTLGMFLFVDGQLDDWALKGAVIQMISHGFVSAAMFMCIGVMYDRLHTRNIADYGGVVNVMPKFAAFMMLFGMANAGLPATSGFVGEFMVVMGAVKVNFWVGALAAMTLIYGASYTLWMYKRVIFGAIHNPHVAEMKDINCREFAILAVLAVAVLGMGLYPNAFIEVVHQAANDLIAHVAQSKI
Protein: Galectin-10 (Gal-10) (Charcot-Leyden crystal protein) (CLC) (Eosinophil lysophospholipase) (Lysolecithin acylhydrolase) (Q05315)
Organism: Homo sapiens (Human)
Function: Regulates immune responses through the recognition of cell-surface glycans. Essential for the anergy and suppressive function of CD25-positive regulatory T-cells (Treg).
Subcellular location: Cytoplasm, cytosol {ECO:0000269|PubMed:17502455}. Cytoplasmic granule {ECO:0000269|PubMed:17502455}. Note=Localized in granules from where it may be secreted or transported to other locations in the cell.
Interaction partners:
- UDP-glucose 4-epimerase
- Immunoglobulin lambda-like polypeptide 5
- Immunoglobulin heavy variable 3-43D
- Probable non-functional immunoglobulin heavy variable 3-16
- C-C chemokine receptor type 3
- Non-secretory ribonuclease
- Galectin-2
- Eosinophil cationic protein
Sequence:
MSLLPVPYTEAASLSTGSTVTIKGRPLACFLNEPYLQVDFHTEMKEESDIVFHFQVCFGRRVVMNSREYGAWKQQVESKNMPFQDGQEFELSISVLPDKYQVMVNGQSSYTFDHRIKPEAVKMVQVWRDISLTKFNVSYLKR
Protein: Transmembrane protein 70, mitochondrial (Q921N7)
Organism: Mus musculus (Mouse)
Function: Scaffold protein that participates in the c-ring assembly of mitochondrial ATP synthase (F(1)F(0) ATP synthase or complex V) by facilitating the membrane insertion and oligomer formation of the subunit c/ATP5MC1 through its interaction (By similarity). Therefore, participates in the early stage of mitochondrial ATP synthase biogenesis and also protects subunit c/ATP5MC1 against intramitochondrial proteolysis. In addition, binds the mitochondrial proton-transporting ATP synthase complexes I and may play a role in the stability of its membrane-bound subassemblies (By similarity).
Subcellular location: Mitochondrion inner membrane {ECO:0000250|UniProtKB:Q9BUB7}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q9BUB7}. Note=Mostly located within the inner cristae membrane. {ECO:0000250|UniProtKB:Q9BUB7}.
Interaction partners:
- Evolutionarily conserved signaling intermediate in Toll pathway, mitochondrial
- NADH dehydrogenase iron-sulfur protein 5
- FAD-dependent oxidoreductase domain-containing protein 1
- ATP synthase mitochondrial F1 complex assembly factor 2
- Distal membrane-arm assembly complex protein 2
- Transmembrane protein 186
- Transmembrane protein 242
- Complex I intermediate-associated protein 30, mitochondrial
Sequence:
MLLGLGGRWAAGLWPGRTRTTWCVAAALRGSGIAFWRAASLAEPERLRSGGHLALAESCGPPGRAQIPVCWEQCVRCFHTQVDKPENGRLIYTGNLARTIFGVKCFSYSTSVVSLAFLPYLLSQNNMMFGSLPLQVLFYGVMGSFTVITPTLLHLLTKGYVIRLYHEATSDTYRAVTYNVMLSETSTVFHQDDVTIPESAHIFTSFYAKTKSLLVNPALFLNPEDYNHLMGYDKPFTFDMEEVDEKKLHEGEK
Protein: Vicianin hydrolase (VH) (EC 3.2.1.119) (A2SY66)
Organism: Vicia sativa subsp. nigra (Common vetch) (Vicia angustifolia)
Function: Hydrolyzes the disaccharide glycosides vicianin, pNP beta-primeveroside, 2-phenylethyl beta-primeveroside and furcatin.
Interaction partners:
Sequence:
ISPSLLYLFSLATLLAVVTGTGTPSQEVHPSHYATTFNKSLFPKDFLFGIGSSAYQVEGASNIDGRGPSIWDTFTKQHPEKIWDHSSGNIGADFYHRYKSDIKIVKEIGLDSYRFSISWSRIFPKGKGEVNPLGVKFYNNVINEILANGLIPFVTLFHWDLPQSLEDEYKGFLSSKVVKDFENYADFVFKTYGDRVKHWVTLNEPFSYALYGYNGGTFAPGRCSKYAGNCEYGDSSTEPYIVAHNLILSHAAAAKLYKTKYQAHQKGNIGATLVTHYFEPHSNSAADRVAASRALDFFFGWFAHPLTYGHYPQSMISSLGNRLPKFSKEEVELTKGSYDFLGVNYYSTYYAQSAPLTTVNRTFYTDIQANVSPLKNGAPIGPATDLNWLYVYPKGIHSLVTHMKDVYKNPIVYITENGVAQSRNDSIPISEARKDGIRISYHDNHLKFLLQGIKDGANVKGYYAWSFSDSYEWDAGYTLRFGIIYVDFKDNLRRYPKYSALWLQKFLLK
Protein: Protein CHROMATIN REMODELING 20 (AtCHR20) (EC 3.6.4.-) (ATP-dependent helicase ATRX) (Transcriptional regulator ATRX) (X-linked helicase II) (F4HW51)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Involved in transcriptional regulation and chromatin remodeling. Facilitates DNA replication in multiple cellular environments and is required for efficient replication of a subset of genomic loci. Binds to DNA tandem repeat sequences in both telomeres and euchromatin and in vitro binds DNA quadruplex structures. May help stabilizing G-rich regions into regular chromatin structures by remodeling G4 DNA and incorporating H3.3-containing nucleosomes (By similarity). Involved in DNA repair of gamma-irradiation-mediated damages.
Subcellular location: Nucleus {ECO:0000250|UniProtKB:Q61687}. Chromosome, telomere {ECO:0000250|UniProtKB:Q61687}.
Interaction partners:
- Histone H3.3
- Histone H3-like 5
- Histone H3.1
- Histone H3-like 2
- Histone H3-like 3
- Histone H3-like 1
- Histone H3-like centromeric protein CENH3
- Histone H3-like 4
- Chromatin structure-remodeling complex protein SYD
- Histone H4
Sequence:
MEANEESLKGKIEKLEGKEVIVESKEDEMDIIIEENREAEQEVMEVKARDGRGEQNDVLMEENNNQGEQKDEEMQDASSRSESSDFNSDEDEQILSRRDDELDLEKPLSEEEIDELISDLLAVESKAAEAQEALEKESLSKVESEVREELAQALRGDELDEAVAAEMMTFKDEWEATLDELETESATLLEQLDGAGIELPKLYEMIESQAPNGCYTEAWKQRAHWVGTQVTKETVESLANAERFLHTHRPVRKRHGKLLEEGASGFLEKKLADGAVKESLAGTSELDWSSLNKVFSEKRDESVSFGSKQWASVYLASTPHQAAAMGLEFPGVNEVEEIEEIDASLADPFLADAIDNERELALTEEQKTNYIRVKEEDDITCDRVLQLRLKRKRRKKRSKQVIRCAAENMDDDSVYLDGNNTTPNFAKDQVKSPETSTQVHNSEVNIEENGNFSNSDVDKMTPSTHINVDAKRDDSQNPANNFRCTACNKVAVEVHSHPLLEVIVCMDCKRSIEDRVSKVDDSLERHCEWCGHIADLIDCRTCEKLFCASCIKRNIGEEYMSEAQSSGWDCCCCSPIPLQRLTLELEKAMRDKKSIELSSDSSSDSSSDNNSVDTDADVNVTISSKKKSKKKIRRIIDDAELGKDTRTKIAIEKARQERLRSLQFSARYKTISSMGDVKSIPEGAEVEVLGDAHSGYIVNVVREIGEEAVRVPRSISAKLKVHQVTGIRFMWENIIQSISRVKSGDKGLGCILAHTMGLGKTFQVIAFLYTAMRCVDLGLKTALIVTPVNVLHNWRSEFEKWMPSEVKPLRIFMLGDVSRERRFDLLTKWRKKGGVFLMGYTNFRNLSLGRGVKDLNAARGICNALRDGPDILVCDEAHIIKNTKADTTQALKQVKCQRRIALTGSPLQNNLMEYYCMVDFVREGFLGSSPEFRNRFQNPIENGQHMNSTAEDVKIMNQRSHILYEQLKGFVQRMDMNVVKKDLPPKTVFVISVKLSPLQRILYQRFLELYGFSDGRTDERMRKNFFAAYQVLAQILNHPGIPQLRSEDSKNGRRGSIVDIPDDCSSDENIDYNMVTGEKQRTMNDLQDKVDGYLQKDWWVDLLQKNNYKVSDFSGKMILLLDILSMSADVGDKALVFSQSIPTLDLIELYLSRVPRHGKQGKFWKKGKDWYRIDGKTESSERQKLVDRFNEPDNKRVKCTLISTRAGSLGINLYAANRVIIVDGSWNPTYDLQAIFRAWRYGQKKPVFAYRLMARGTIEEKIYKRQVTKEGLAARVVDRQQVHRTISKEEMLHLFEFDDDDEKSEAVTEISKQNEAGHSNLVEQAILWTKKATLSRVGGDKLMENLLQRHGPNWISSFHEHETLLQENEEERLTKEEKDMAWEVYRRALEWEEVQRVPFSESPVVPKPSPSTQTEPLPQPKGFNRSRFVNRNCTRIAHQLTLISQGLKVGSSTVCGECGRVIRWEDVIPASKLSAVIVN
Protein: NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 6 (Complex I-B14) (CI-B14) (NADH-ubiquinone oxidoreductase B14 subunit) (Q9CQZ5)
Organism: Mus musculus (Mouse)
Function: Accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), that is believed to be not involved in catalysis. Required for proper complex I assembly. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone.
Subcellular location: Mitochondrion inner membrane {ECO:0000269|PubMed:38575788}; Peripheral membrane protein {ECO:0000269|PubMed:38575788}; Matrix side {ECO:0000269|PubMed:38575788}.
Interaction partners:
- NADH dehydrogenase 1 alpha subcomplex subunit 1
- NADH dehydrogenase flavoprotein 2, mitochondrial
- NADH dehydrogenase iron-sulfur protein 5
- NADH dehydrogenase 1 alpha subcomplex subunit 13
- NADH dehydrogenase iron-sulfur protein 3, mitochondrial
- NADH dehydrogenase flavoprotein 1, mitochondrial
- NADH-ubiquinone oxidoreductase 75 kDa subunit, mitochondrial
- NADH dehydrogenase 1 alpha subcomplex subunit 3
- NADH dehydrogenase 1 alpha subcomplex subunit 5
- NADH dehydrogenase 1 beta subcomplex subunit 1
Sequence:
MAAAATGLRQAAAAAASTSVKPIFSRDLNEAKRRVRELYRAWYREVPNTVHLMQLDITVKQGRDKVREMFMKNAHVTDPRVVDLLVIKGKMELQETIKVWKQRTHVMRFFHETETPRPKDFLSKFYMGHDP
Protein: DNA polymerase III subunit alpha (EC 2.7.7.7) (P10443)
Organism: Escherichia coli (strain K12)
Function: DNA polymerase III is a complex, multichain enzyme responsible for most of the replicative synthesis in bacteria. This DNA polymerase also exhibits 3' to 5' exonuclease activity. The alpha chain is the DNA polymerase catalytic subunit. It is tethered to replicating DNA by the beta sliding clamp (dnaN), which confers extremely high processivity to the catalytic subunit, copying a 5.4 kb genome in 11 seconds, a speed of at least 500 nucleotides/second at 30 degrees Celsius.
Subcellular location: Cytoplasm.
Interaction partners:
- DNA polymerase III subunit psi
- DNA polymerase III subunit epsilon
- DNA polymerase III subunit tau
- Single-stranded DNA-binding protein
- DNA polymerase III subunit theta
- DNA polymerase III subunit delta
- DNA polymerase III subunit chi
- Beta sliding clamp
- DNA polymerase III subunit delta'
- Replicative DNA helicase DnaB
Sequence:
MSEPRFVHLRVHSDYSMIDGLAKTAPLVKKAAALGMPALAITDFTNLCGLVKFYGAGHGAGIKPIVGADFNVQCDLLGDELTHLTVLAANNTGYQNLTLLISKAYQRGYGAAGPIIDRDWLIELNEGLILLSGGRMGDVGRSLLRGNSALVDECVAFYEEHFPDRYFLELIRTGRPDEESYLHAAVELAEARGLPVVATNDVRFIDSSDFDAHEIRVAIHDGFTLDDPKRPRNYSPQQYMRSEEEMCELFADIPEALANTVEIAKRCNVTVRLGEYFLPQFPTGDMSTEDYLVKRAKEGLEERLAFLFPDEEERLKRRPEYDERLETELQVINQMGFPGYFLIVMEFIQWSKDNGVPVGPGRGSGAGSLVAYALKITDLDPLEFDLLFERFLNPERVSMPDFDVDFCMEKRDQVIEHVADMYGRDAVSQIITFGTMAAKAVIRDVGRVLGHPYGFVDRISKLIPPDPGMTLAKAFEAEPQLPEIYEADEEVKALIDMARKLEGVTRNAGKHAGGVVIAPTKITDFAPLYCDEEGKHPVTQFDKSDVEYAGLVKFDFLGLRTLTIINWALEMINKRRAKNGEPPLDIAAIPLDDKKSFDMLQRSETTAVFQLESRGMKDLIKRLQPDCFEDMIALVALFRPGPLQSGMVDNFIDRKHGREEISYPDVQWQHESLKPVLEPTYGIILYQEQVMQIAQVLSGYTLGGADMLRRAMGKKKPEEMAKQRSVFAEGAEKNGINAELAMKIFDLVEKFAGYGFNKSHSAAYALVSYQTLWLKAHYPAEFMAAVMTADMDNTEKVVGLVDECWRMGLKILPPDINSGLYHFHVNDDGEIVYGIGAIKGVGEGPIEAIIEARNKGGYFRELFDLCARTDTKKLNRRVLEKLIMSGAFDRLGPHRAALMNSLGDALKAADQHAKAEAIGQADMFGVLAEEPEQIEQSYASCQPWPEQVVLDGERETLGLYLTGHPINQYLKEIERYVGGVRLKDMHPTERGKVITAAGLVVAARVMVTKRGNRIGICTLDDRSGRLEVMLFTDALDKYQQLLEKDRILIVSGQVSFDDFSGGLKMTAREVMDIDEAREKYARGLAISLTDRQIDDQLLNRLRQSLEPHRSGTIPVHLYYQRADARARLRFGATWRVSPSDRLLNDLRGLIGSEQVELEFD
Protein: cAMP/cGMP dual specificity phosphodiesterase Rv0805 (EC 3.1.4.16) (EC 3.1.4.17) (2',3'-cyclic-nucleotide phosphodiesterase) (3',5'-cyclic-nucleotide phosphodiesterase) (Cyclic nucleotide phosphodiesterase) (P9WP65)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: Cyclic nucleotide phosphodiesterase with a dual-specificity for the second messengers cAMP and cGMP. Can use 2',3'-cAMP, 2',3'-cGMP, 3',5'-cAMP, 3',5'-cGMP and 3',5'-cUMP. Hydrolysis of 2',3'-cAMP produces a mixture of 3'-AMP (major product) and 2'-AMP (minor product). In vitro, is 150-fold more active in hydrolyzing 2',3'-cAMP than 3',5'-cAMP. Can also hydrolyze the model substrates p-nitrophenyl phosphate (pNPP), bis-(p-nitrophenyl phosphate) (bis(pNPP)) and p-nitrophenyl phenylphosphonate (pNPPP). Plays an important regulatory role in modulating the intracellular concentration of cAMP, thereby influencing cAMP-dependent processes. May play a role in pathogenicity, not only by hydrolyzing cAMP, but also by altering properties of the cell wall.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:19801656, ECO:0000269|PubMed:24970891}. Cell membrane {ECO:0000269|PubMed:19801656, ECO:0000269|PubMed:24970891}. Secreted, cell wall {ECO:0000269|PubMed:19801656, ECO:0000269|PubMed:24970891, ECO:0000269|PubMed:26904001}. Cell envelope {ECO:0000269|PubMed:24970891}. Note=The C-terminal extension (CTE) is necessary for the localization to the cell wall and cell envelope (PubMed:19801656, PubMed:24970891). Phosphorylation at Thr-309 promotes cell wall localization (PubMed:26904001). {ECO:0000269|PubMed:19801656, ECO:0000269|PubMed:24970891, ECO:0000269|PubMed:26904001}.
Interaction partners:
- Adenylate cyclase
- Uncharacterized protein Rv1318c
- Uncharacterized protein Rv1320c
- Uncharacterized protein Rv1319c
- Probable conserved transmembrane protein
- Adenine phosphoribosyltransferase
- pH-sensitive adenylate cyclase Rv1264
- Adenylate kinase
- Adenosine kinase
- Adenylosuccinate lyase
Sequence:
MHRLRAAEHPRPDYVLLHISDTHLIGGDRRLYGAVDADDRLGELLEQLNQSGLRPDAIVFTGDLADKGEPAAYRKLRGLVEPFAAQLGAELVWVMGNHDDRAELRKFLLDEAPSMAPLDRVCMIDGLRIIVLDTSVPGHHHGEIRASQLGWLAEELATPAPDGTILALHHPPIPSVLDMAVTVELRDQAALGRVLRGTDVRAILAGHLHYSTNATFVGIPVSVASATCYTQDLTVAAGGTRGRDGAQGCNLVHVYPDTVVHSVIPLGGGETVGTFVSPGQARRKIAESGIFIEPSRRDSLFKHPPMVLTSSAPRSPVD