wanglab/gogpt-training-data huggingface dataset:
Protein: RNA 2'-O-methyltransferase FBLL1 (EC 2.1.1.-) (Fibrillarin like 1) (A6NHQ2)
Organism: Homo sapiens (Human)
Function: S-adenosyl-L-methionine-dependent methyltransferase that has the ability to methylate both RNAs and proteins. Involved in pre-rRNA processing by catalyzing the site-specific 2'-hydroxyl methylation of ribose moieties in pre-ribosomal RNA. Also acts as a protein methyltransferase by mediating methylation of glutamine residues (By similarity).
Subcellular location: Nucleus, nucleolus {ECO:0000269|PubMed:39570315}.
Interaction partners:
- Nucleolar protein 58
- Nucleolar protein 56
- H/ACA ribonucleoprotein complex subunit DKC1
- NHP2-like protein 1
- Nucleolar protein 6
- H/ACA ribonucleoprotein complex subunit 2
- WD repeat-containing protein 36
- WD repeat-containing protein 46
- H/ACA ribonucleoprotein complex subunit 1
- U3 small nucleolar RNA-interacting protein 2
Sequence:
MKSAASSRGGGGGGRGGGGWGSWGGGRGGGGGAGKGGGGDGGGQGGKGGFGARARGFGGGGRGRGRGGGDGKDRGGGGQRRGGVAKSKSRRRKGAMVVSVEPHRHEGVFIYRGAEDALVTLNMVPGQSVYGERRVTVTEGGVKQEYRTWNPFRSKLAAAILGGVDQIHIKPKSKVLYLGAASGTTVSHVSDIIGPDGLVYAVEFSHRAGRDLVNVAKKRTNIIPVLEDARHPLKYRMLIGMVDVIFADVAQPDQSRIVALNAHTFLRNGGHFLISIKANCIDSTASAEAVFASEVRKLQQENLKPQEQLTLEPYERDHAVVVGVYRPLPKSSSK
Protein: Tubulin beta chain (Beta-tubulin) (P05219)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Tubulin is the major constituent of microtubules, a cylinder consisting of laterally associated linear protofilaments composed of alpha- and beta-tubulin heterodimers. Microtubules grow by the addition of GTP-tubulin dimers to the microtubule end, where a stabilizing cap forms. Below the cap, tubulin dimers are in GDP-bound state, owing to GTPase activity of alpha-tubulin.
Subcellular location: Cytoplasm, cytoskeleton.
Interaction partners:
- Tubulin alpha-1 chain
- Microtubule integrity protein mal3
- Tubulin alpha-2 chain
- Kinesin-like protein cut7
- Dynein heavy chain, cytoplasmic
- Spindle pole body component alp14
- Dynein intermediate chain 1
- Actin
- Tubulin-specific chaperone A
- Tubulin-folding cofactor D
Sequence:
MREIVHIQAGQCGNQVGAAFWSTIADEHGLDSAGIYHGTSEAQHERLNVYFNEAAGGKYVPRAVLVDLEPGTMDAVKSGKFGNLFRPDNIIYGQSGAGNIWAKGHYTEGAELADAVLDVVRREAEACDALQGFQLTHSLGGGTGSGMGTLLLSKIREEYPDRMMATFSVAPAPKSSDTVVEPYNATLSMHQLVENSDETFCIDNEALSSIFANTLKIKSPSYDDLNHLVSAVMAGVTTSFRFPGELNSDLRKLAVNMVPFPRLHFFMVGFAPLAAIGSSSFQAVSVPELTQQMFDANNMMVAADPRHGRYLTVAALFRGKVSMKEVDEQIRSVQTKNSAYFVEWIPDNVLKAVCSVPPKDLKMSATFIGNSTSIQEIFRRLGDQFSAMFRRKAFLHWYTGEGMDEMEFTEAESNMNDLVSEYQQYQEAGIDEGDEDYEIEEEKEPLEY
Protein: Acetyltransferase PA2271 (EC 2.3.1.-) (GCN5-related N-acetyltransferase) (GNAT) (Q9I1K2)
Organism: Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Function: Catalyzes the transfer of an acetyl group from acetyl coenzyme A (AcCoA) to an acceptor substrate and releases both CoA and the acetylated product. It can use a variety of substrates including spermidine, spermine and N(8)-acetylspermidine, 7-aminocephalosporanic acid, colistin and thiamine.
Interaction partners:
- Probable transcriptional regulator
Sequence:
MDYRIRTSRDEDAALLPAIERSAGESFRLLPELAWIADAGVAGVDFHRRLIERGSHWLAEDADGQPVGFLAAERCADELHIAELSIAQAHQQQGLGRRLLERAVTYAHASHCRALTLTTFCDVPWNAPFYARLGFQRLTWQEAGERLRAILGHEQEIGFAADSRCAMRLVL
Protein: D-beta-hydroxybutyrate dehydrogenase, mitochondrial (EC 1.1.1.30) (3-hydroxybutyrate dehydrogenase) (C9JM78)
Organism: Homo sapiens (Human)
Subcellular location: Mitochondrion inner membrane {ECO:0000256|ARBA:ARBA00004273}. Mitochondrion matrix {ECO:0000256|ARBA:ARBA00004305}.
Interaction partners:
Sequence:
MASNGIQKRRPLLLGSTSFIPIGRRTYASAAEPVGSKAVLVTGCDSGFGFSLAKHLHSKGFLVFAGCLMKDKGHDGVKELDSLNSDRLRTVQLNVCSSEEVEKVVEIVRSSLKDPEKGMWGLVNNAGISTFGEVEFTSLETYKQVAEVNLWGTVRMTKSFLPLIRRAK
Protein: Enhancer of polycomb-like protein (O96542)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123, ECO:0000256|RuleBase:RU361124}.
Interaction partners:
Sequence:
MSKLSFRARHLDPSKQMPIYLAEELPDLPEYSAINRAVPQMPSGMEKEEESEHHLQRAICTGLIIPTPEVLQTDQPFYDAYYPPDYKMPRQMIHMQPLGLDTEVPDYDMDSADEDWLSQQQRLELTELKFEQMMDRLEKSSGQTVVTLNEAKSLLNQDDETSISVYDYWLNKRLKMQHPLILTVKTESRPGASSNNPYLAFRRRTEKMQTRKNRKNDEASYEKMLKLRRDLQRATTILEMVRRREETKRDHLKMTVNIFEKRVEMRDFNGAVYSELNSQYKNTRPAYNPLYTNQYSQGAAAVGTAGAILAALPTGLLPGGAGAAGNANVFGSASQYLNSSNLTMDAISGSGNGNSSRKEKRPYKKRKHKLPRDKQQHQQQQTQQHQQQQYLPASGGAGVSPAHHLPHHLHHLSRQQSASPAANDSIADSEEEDYFGAGAQNGNKLGSESEEETPFAFRRRSSCVYLPTRQRDGRYPWDSADEDMAPSGACSDAKYRYTLTSLNYPRPRCIGFARRRLGRGGRILLDRATTNFDDFWSQLDYTVMESVTVNKCRDKIKPGDPDQLCKPSSPPTVVDLVPAGKPVDGEHPVPELIKEEPSSDTEKPVAATESGRESKERELEEKFENDVDDEFVASDDENVSRLGIYSSAVTLPQSCADLRQKRRRLRRKKQQLRELNAAKRLKRSSEAVATAEDVQLEDEDTKPDLRPLPRAYLQRLALILGQKLKVEEDDNTEVSENVAPELLEMNDPEQLQPPRANHQQHHRSNHNNNNNTVLNNNNSSSSNVMNKDVSISEKINVIKQEAEELVGGKCEDQPVASTSAAAAAARAAEAAAAAEAASSTTTLAAPNPGPSLEEVAKTIKREMIDADDSNEPLSSIRTAAVMLSTQTSVSELMDDEAEDDVNLAQLSSIIRHTAVKKELEAQQHQQQVQHEQMQAARKMEEDEAAPCLNQLPDVIRLRNIRNSQVHARPKDLFVQAPVDEEFNADYMGGLSPTSSQRLDICNELLSEIRRDWLHFRPKTPTDELSDSQDCEVGKTCDSHAVDWTQGTPISVELNRLGKREAEESDSSSYFLSSGFKYRDLESDAQLLQTVQAQDYARGSSKSPNCSGSGSGSALEFNLSGGDSLNDINNLLGCDDEDDNHEHMLDNILQECAMDDPKALNQATNFWNGILDGEAAVDEVEMADQLLDCIDEKKSKVGAADTSKRAGRNRKARLIQAPVGSSAFTVCPTAETLKERELFFSQAPPVEVPPKEKTPAEVELPEVVVKETANLPVKVEAVEKPQSEVLPVAPQPQQLQPQAITLPTTQLINIPAQISTQKQHQQPQVTQLLNQFANAGPQIIARTEYGGGAAVGDIVTITPHTGSSPLPTLTAQQQLQHQLAQAQLRNVTVQQRQATPQNPNQNQNPQQQLLFQMQRDPSRSLTPLQAAGAGATGNHLIYTTSCGEIVTAGAAASASQKVTYAIQKAGVSSGGATTASIGPNTVITLSNVKVQNDDISSGGSGNSGSSVNIINTASGQQLAVHSIAGMQQQGQQQVQQVTTSTPLLVATPTRNNVQQQQQQLVQQQPIVWRQVSGTNTAVATTAVLSTTVDSSPKAVTNQILWTSRATQKRQLNGPENTDINKLLLNRKLPRKQQIQQQHQQIQLTKQQLQQLVQHEELDDLVATSTGNSGDQMETGDGLQQQQQQQQQQQQLQKLSKVIKMSQFPLLVSDVSLQQQQSVSGQAQQQQLKPNSAAAIAANHNYSLHPASTAIITAQATPQQANKIFLTSSNSGGGGSAGNFTIATASELQAAAAGQKLHYKELPNSNLKLNFVSSAGTGEQTQQVGATTVLLNKSQQQQQQQQHQKLKTLATTGNSQTGQGDKRVLYTSLLNVKPLQKNNSGQMQMQLGPGGLQQVLRGRLNNSAIITRTLPLGTTVNSTGGAVGPTTTTIRQLVTTNANNVSSQDGNLLSAKEVGKALTVEQVIASANNGGVVLPTSNNNNNNNGSGAGGNGGPLNSGVNATGAGGGGSTGAGVGGAGVTSTINR
Protein: Zinc transporter ZIP6 (Estrogen-regulated protein LIV-1) (Solute carrier family 39 member 6) (Zrt- and Irt-like protein 6) (ZIP-6) (Q6L8F3)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:Q13433}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
Sequence:
MMTFLCTRSGRRASGVECRIAAERAYFRVRGLPVANMIGWWPRLCPVMSLALLWACSVGAGSDCKSVAIETDSRIAEQTQQRHLQALFDKYGQNGSISLEGLFNLLKGVGLDRIRKVMVHHPGNAHNHTHTHDHTHTHVDKLTAHTHPVTTKKGDMDHSVEKSDPVPKAQPDPASGKKSQSDAHHNLYMKMNQESTTALTTPSYVTRSRRTNRSADYDFTQDHASFSPSQPNVTHSNHTHHDEDTPTHQHDDHDEHEHARASLGCQNASTILQTHGMRKEASLSVKDFSFLCPALLMQIDSKSCIVHEDEDEHSDHSHHHKHHHHHHDHQHLQHPHNHTNGRGQRNTPVYIAWLGGFLSITLISLLALVGVVLIPLMNRVCFNFLLSFLVALAVGTLSGDALLHLIPHSQGHHHHGHSEEHAEEEDSLRPVWTGLTALSGVYIMFLIEHFLTLGKMYKDKNQKVQKRVDLTTEVLESEKLPSLEENDVKIEAAETNGGRALAEEEEVMLGAELYNDIDCENKCHSHFHDTVGQSDEQHHHHHDYHHILHHHHSQNHHPHTHTHRHTHSYSQQHFEQAGVATLAWMVIMGDGLHNFSDGLAIGAAFTEGLSSGLSTSVAVFCHELPHELGDFAVLLKAGMSVRQAMLYNLLSALMGYLGMIIGILIGHYAENVATWIFALTAGLFMYVALVDMVPEMLHNDASEAGFSHYGFFLLQNAGILLGFGIMLIIAVFEDRIQLDLGY
Protein: Regulator of G-protein signaling 3 (RGS3) (SRB-RGS) (P49797)
Organism: Rattus norvegicus (Rat)
Function: Down-regulates signaling from heterotrimeric G-proteins by increasing the GTPase activity of the alpha subunits, thereby driving them into their inactive GDP-bound form. Down-regulates G-protein-mediated release of inositol phosphates and activation of MAP kinases.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:P49796}. Membrane {ECO:0000250|UniProtKB:P49796}; Peripheral membrane protein {ECO:0000250|UniProtKB:P49796}. Nucleus {ECO:0000250|UniProtKB:P49796}. Note=Long isoforms are cytoplasmic and associated with the plasma membrane. Short isoforms are nuclear. {ECO:0000250|UniProtKB:P49796}.
Interaction partners:
- Ephrin-B1
- Ephrin B2
- Ephrin-B3
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein G
- Regulator of G-protein signaling 12
Sequence:
MNRFNGLCKVCSERRYRQITIRRGKDGFGFTICCDSPVRVQAVDSGGPAERAGLQQLDTVLQLNERPVEHWKCVELAHEIRSCPSEIILLVWRVVPQIKPGPDGGVLRRASCKSTHDLLSPPNKREKNCTHGAPTRPEQRHSCHLVCDSSDGLLLGGWERYTEVGKRSGQHTLPALSRATTPTDPNYIILAPLNPGSQLLRPVYQEDAIPEEPGTTTKGKSYTGLGKKSRLMKTVQTMKGHSNYQDCSALRPHIPHSSYGTYVTLAPKVLVFPVFVQPLDLCNPARTLLLSEELLLYEGRNKTSQVTLFAYSDLLLFTKEEEPGRCDVLRNPLYLQSVKLQEGSSEDLKFCVLYLAEKAECLFTLEAHSQEQKKRVCWCLSENIAKQQQLAATPTERKMFETEADEKEMPLVEGKGPGAEERTPSKDPSPSQELPPGQELPPSKDPSPSQELPPGQELPPSKDPSPSQELPPGQELPSSKNPSPSQELPAGQDLPPRKESFSGQEAAPGPESPSSEDIATCQNPPQSPETSTSKDSPPGQGSSPTTEVPSCQGLPAGQESTSQDPLLSQEPPAIPESSASDQNVLPSQESPPSQGSLSEKALAEQTISPGELPAATAGEPSASRPNFVIPEVRLDSAYSQQDGAHGGSSGEDEDAEEGEEGEEGEEDEEDDTNDDNYGDRNEAKRSSLIETGQGAEGGLSLRVQNSLRRRTHSEGSLLQEARGPCFASDTTLHCSDGEGTTSTWAIPSPRTLKKELGRNGGSMHHLSLFFTGHRKMSGTDLADDVEASRKRKSKNIAKDMKNKLAIFRRRNESPGAQPAGKADKTTKSFKPTSEEALKWSESLEKLLLHKYGLEVFQAFLRTEFSEENLEFWLACEDFKKVKSQSKMAAKAKKIFAEFIAIQACKEVNLDSYTREHTKENLQSITRGCFDLAQKRIFGLMEKDSYPRFLRSDLYLDLINQKKMSPPL
Protein: Deoxyribonuclease (Q6DH05)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
- CUB domain-containing protein 2.
- Photoreceptor cilium actin regulator 2
- Cholinergic receptor, nicotinic, beta 5a.
- Gap junction protein
- Guanine nucleotide-binding protein subunit alpha
- deoxyribonuclease II
- Biogenesis of lysosome-related organelles complex 1 subunit 3
- 3-oxo-5alpha-steroid 4-dehydrogenase
- Cytochrome c oxidase assembly factor 6
- Sulfotransferase 6B1
Sequence:
MRPPLLLCFIGLCLWTCVISLKICAFNIQSYGEAKASNTRVMEILTKIISRCDLSLIQEVRDSRGEAISALLMSLNRFDKSHIYAHLESKRLGKKTYKEQYVYIYRKDMLQVQEQYEHPEVNESASEVFSREPFIILVHSPTTLVKNFVLIGQHTSPKSAMKEMDSLYEVFQTVKKKWKTENVMFLGDLNAACNYVTNKGLRNVRLRSDPKFHWLIRDEQDTTVREKTRCAYDRIIIHGKELISGIVPESAQPFNFKQEFNLSEEEALEVSDHFPVEVDLKANHRYLLRHEL
Protein: Protein Rev (ART/TRS) (Anti-repression transactivator) (Regulator of expression of viral proteins) (P04618)
Organism: Human immunodeficiency virus type 1 group M subtype B (isolate HXB2) (HIV-1)
Function: Escorts unspliced or incompletely spliced viral pre-mRNAs (late transcripts) out of the nucleus of infected cells. These pre-mRNAs carry a recognition sequence called Rev responsive element (RRE) located in the env gene, that is not present in fully spliced viral mRNAs (early transcripts). This function is essential since most viral proteins are translated from unspliced or partially spliced pre-mRNAs which cannot exit the nucleus by the pathway used by fully processed cellular mRNAs. Rev itself is translated from a fully spliced mRNA that readily exits the nucleus. Rev's nuclear localization signal (NLS) binds directly to KPNB1/Importin beta-1 without previous binding to KPNA1/Importin alpha-1. KPNB1 binds to the GDP bound form of RAN (Ran-GDP) and targets Rev to the nucleus. In the nucleus, the conversion from Ran-GDP to Ran-GTP dissociates Rev from KPNB1 and allows Rev's binding to the RRE in viral pre-mRNAs. Rev multimerization on the RRE via cooperative assembly exposes its nuclear export signal (NES) to the surface. Rev can then form a complex with XPO1/CRM1 and Ran-GTP, leading to nuclear export of the complex. Conversion from Ran-GTP to Ran-GDP mediates dissociation of the Rev/RRE/XPO1/RAN complex, so that Rev can return to the nucleus for a subsequent round of export. Beside KPNB1, also seems to interact with TNPO1/Transportin-1, RANBP5/IPO5 and IPO7/RANBP7 for nuclear import. The nucleoporin-like HRB/RIP is an essential cofactor that probably indirectly interacts with Rev to release HIV RNAs from the perinuclear region to the cytoplasm.
Subcellular location: Host nucleus, host nucleolus {ECO:0000255|HAMAP-Rule:MF_04077}. Host cytoplasm {ECO:0000255|HAMAP-Rule:MF_04077}. Note=The presence of both nuclear import and nuclear export signals leads to continuous shuttling between the nucleus and cytoplasm. {ECO:0000255|HAMAP-Rule:MF_04077}.
Interaction partners:
Sequence:
MAGRSGDSDEELIRTVRLIKLLYQSNPPPNPEGTRQARRNRRRRWRERQRQIHSISERILGTYLGRSAEPVPLQLPPLERLTLDCNEDCGTSGTQGVGSPQILVESPTVLESGTKE
Protein: Zinc finger CCHC domain-containing protein 7 (TRAMP-like complex RNA-binding factor ZCCHC7) (Q960D5)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MDATDVKMGLSCITEPEGTSVVASSTTPPMHSPSCSVMSSDDFIVQKDTTRLLTECENANDEDLLVLTETAIREAIGEEPKDKEVVENASEEQEHDHAADTSSEYEFVPPSRLEEIKKNYRVDDQQFRALDVYESESDLTESGIYSKAKSKTTPTIIRNVDSSSGSSSVEEVVEPSVQKTKRLRKRSCSTNNHSQSDPNNDDGLDDSDSDDGVHATGVPGIARGMAVERCKRKIRRISTRHSSDDNSKKAATRIQKPKVAAVHHASSESASEDELPSARDIAERLLNQQKGQGKEQVQKGDGDDDAISIGSDEDSHAEAEFRDAMTDRLAAVFERLDAKAKKMEEDEEQVNASGYISDEEDSRDKSADTTVRSDEDIDASNDLEETNPDKNDRDVTNEEQHVHVEHNLQELRDESLPKSGDLIGWNEEMRSFYNDSWNGENFSVHKVQRMMTGHRHEWRINTADRCPVARPRSHAKCSNCFEMGHVRSKCPRPRKPLVCFICGTMGHAEPRCPNAICFGCGSKQEIYVQQCNKCSFHSRLVCQLCKMRGHGVDHCPDKWRRYHSTTRSNTELDSRVQYRSVQCSYCAGRHSFENCRQRIGDFRSTNYTSQIVSHQKIYKNRGGPIGNLGDLKSFFAIETPFHFKWNNPSMPKNCYYSRFLVNANLAKVQSVKRKSTTAVSQIPEKIYTHEYVPNAQVKAARGEVSTGTAKKPLTKQMPVVESIAENRTAEEPIGKLNREDEKSKDILPLPEVPPEVKQTQDEKLVEGQPNQNQPDEELPMKDDDQEEPSSSVQREEITTNFDNPPTEPGLSRTPLAPHELDSDSNYSFSEHFELPSSTTSDGQPNTQLPLVRTMGTLPDVIPLSKDDFELSSNVQGISMCVNSSSTSLRTDETPDPDSSEELPDVPSEGKIIMAREESEYLFSAEGRTFLAAAAKQCHVSVRMDFKDYGYVLVIYGLKKHQEELQVKLLRRSQEVKRKSIEFQSQKPPKRIDVLIRFLRDGINSLNTNLGNAKSHYVRIKELEGMNTKNGFKMAEKKRRQLNMILVGQAGLLNGKTHLDQLLVLLRRLIDDFSPDEHATPQLRNEIEEHWRMIFSSYPHPNYDSLLNSYGRLDQKNRLPSLHIDPVLLGLQQKKTQSQPQSPSKGPPSPTPLPPVRQDMAPPPPPKMSKKKQRQALDQQTQNQQRQQQQQQQRLQQQHQNQQQRLQQQQKQQQQSLQQQHQQQRVQQQRMQQQQQHQQQDNNQYQQNLRRPQIDQMPYNNLQQRSRSDLQLRHTLNPECDRLLSEMDHNQPGSINKDANKPSMFWSRESLKYLDDLFKMTSNTETVERLKRVLQRSQRGLLSHNDYRAVIRLHSLMCN
Protein: F-box only protein 3 (Q9UK99)
Organism: Homo sapiens (Human)
Function: Substrate recognition component of the SCF (SKP1-CUL1-F-box protein)-type E3 ubiquitin ligase complex, SCF(FBXO3), which mediates the ubiquitination and subsequent proteasomal degradation of target proteins. Mediates the ubiquitination of HIPK2 and probably that of EP300, leading to rapid degradation by the proteasome. In the presence of PML, HIPK2 ubiquitination still occurs, but degradation is prevented. PML, HIPK2 and FBXO3 may act synergically to activate p53/TP53-dependent transactivation. The SCF(FBXO3) also acts as a regulator of inflammation by mediating ubiquitination and degradation of FBXL2 in response to lipopolysaccharide (LPS). The SCF(FBXO3) complex specifically recognizes FBXL2 phosphorylated at 'Thr-404' and promotes its ubiquitination (By similarity).
Subcellular location: Nucleus {ECO:0000269|PubMed:18809579}. Note=Colocalizes with PML at the peripheries of nuclear bodies. {ECO:0000269|PubMed:18809579}.
Interaction partners:
- S-phase kinase-associated protein 1
- Cullin-1
- UPF0606 protein KIAA1549L
- F-box/LRR-repeat protein 2
- E3 ubiquitin-protein ligase RBX1
Sequence:
MAAMETETAPLTLESLPTDPLLLILSFLDYRDLINCCYVSRRLSQLSSHDPLWRRHCKKYWLISEEEKTQKNQCWKSLFIDTYSDVGRYIDHYAAIKKAWDDLKKYLEPRCPRMVLSLKEGAREEDLDAVEAQIGCKLPDDYRCSYRIHNGQKLVVPGLLGSMALSNHYRSEDLLDVDTAAGGFQQRQGLKYCLPLTFCIHTGLSQYIAVEAAEGRNKNEVFYQCPDQMARNPAAIDMFIIGATFTDWFTSYVKNVVSGGFPIIRDQIFRYVHDPECVATTGDITVSVSTSFLPELSSVHPPHYFFTYRIRIEMSKDALPEKACQLDSRYWRITNAKGDVEEVQGPGVVGEFPIISPGRVYEYTSCTTFSTTSGYMEGYYTFHFLYFKDKIFNVAIPRFHMACPTFRVSIARLEMGPDEYEEMEEEEEEEEEEDEDDDSADMDESDEDDEEERRRRVFDVPIRRRRCSRLF
Protein: Carbon monoxide dehydrogenase medium chain (CO dehydrogenase subunit M) (CO-DH M) (EC 1.2.5.3) (P19914)
Organism: Hydrogenophaga pseudoflava (Pseudomonas carboxydoflava)
Function: Catalyzes the oxidation of carbon monoxide to carbon dioxide.
Interaction partners:
Sequence:
MIPPRFEYHAPKSVGEAVALLGQLGSDAKLLAGGHSLLPMMKLRFAQPEHLIDINRIPELRGIREEGSTVVIGAMTVENDLISSPIVQARLPLLAEAAKLIADPQVRNRGTIGGDIAHGHPGNDHPALSIAVEAHFVLEGPNGRRTVPADGFFLGTYMTLLEENEVMVEIRVPAFAQGTGWAYEKLKRKTGDWATAGCAVVMRKSGNTVSHIRIALTNVAPTALRREGGRSRLLGKAFTKEAVQAAADAAIAICEPAEDLRGDADYKTAMAGQMVKRALNAAWARCA
Protein: Serine/threonine-protein kinase VIK (EC 2.7.11.1) (VH1-interacting kinase) (Q9XI87)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Serine/threonine protein kinase which may function as an adapter protein for BRL2. Required during vascular development for the establishment of vein pattern in foliar organs. Mediates MSSP1/TMT1 phosphorylation and activation to enhance its carrier activity and consequently vacuolar sugar accumulation, particularly in response to cold.
Subcellular location: Vacuole {ECO:0000269|PubMed:21838775}.
Interaction partners:
- MND1-interacting protein 1
- At3g12955
- Inactive TPR repeat-containing thioredoxin TTL3
- Auxin-responsive family protein
Sequence:
MSSDSPAAGDGGEQAAAGTSVPSPSYDKQKEKARVSRTSLILWHAHQNDAAAVRKLLEEDPTLVHARDYDKRTPLHVASLHGWIDVVKCLLEFGADVNAQDRWKNTPLADAEGARKQKMIELLKSHGGLSYGQNGSHFEPKPVPPPIPKKCDWEIEPAELDFSNAAMIGKGSFGEIVKAYWRGTPVAVKRILPSLSDDRLVIQDFRHEVDLLVKLRHPNIVQFLGAVTERKPLMLITEYLRGGDLHQYLKEKGGLTPTTAVNFALDIARGMTYLHNEPNVIIHRDLKPRNVLLVNSSADHLKVGDFGLSKLIKVQNSHDVYKMTGETGSYRYMAPEVFKHRRYDKKVDVFSFAMILYEMLEGEPPFANHEPYEAAKHVSDGHRPTFRSKGCTPDLRELIVKCWDADMNQRPSFLDILKRLEKIKETLPSDHHWGLFTS
Protein: Galactofuranose transporter permease protein YtfT (P39328)
Organism: Escherichia coli (strain K12)
Function: Part of the ABC transporter complex YtfQRT-YjfF involved in galactofuranose transport (Probable). Probably responsible for the translocation of the substrate across the membrane (Probable).
Subcellular location: Cell inner membrane {ECO:0000269|PubMed:15919996}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Galactofuranose transporter ATP-binding protein YtfR
- Galactofuranose-binding protein YtfQ
- Inner membrane ABC transporter permease protein YjfF
- Ribose import binding protein RbsB
- D-allose-binding periplasmic protein
- Xylose import ATP-binding protein XylG
- Arabinose import ATP-binding protein AraG
- D-allose import ATP-binding protein AlsA
- Ribose import ATP-binding protein RbsA
- ABC transporter periplasmic-binding protein YphF
Sequence:
MMPQSLPDTTTPKRRFRWPTGMPQLVALLLVLLVDSLVAPHFWQVVLQDGRLFGSPIDILNRAAPVALLAIGMTLVIATGGIDLSVGAVMAIAGATTAAMTVAGFSLPIVLLSALGTGILAGLWNGILVAILKIQPFVATLILMVAGRGVAQLITAGQIVTFNSPDLSWFGSGSLLFLPTPVIIAVLTLILFWLLTRKTALGMFIEAVGINIRAAKNAGVNTRIIVMLTYVLSGLCAAIAGIIVAADIRGADANNAGLWLELDAILAVVIGGGSLMGGRFNLLLSVVGALIIQGMNTGILLSGFPPEMNQVVKAVVVLCVLIVQSQRFISLIKGVRSRDKT
Protein: Mitochondrial nuclease (EC 3.1.30.-) (P08466)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: This enzyme has both RNase and DNase activity.
Subcellular location: Mitochondrion inner membrane.
Interaction partners:
- Ribonuclease Z
- Apoptosis-inducing factor 1
- Metacaspase-1
- Pro-apoptotic serine protease NMA111
- Glucose-6-phosphate 1-epimerase
- Chromosomal passenger complex protein BIR1
- DNA damage-inducible protein DIN7
- Bax inhibitor 1
- mRNA-binding protein PUF3
Sequence:
MCSRILLSGLVGLGAGTGLTYLLLNKHSPTQIIETPYPPTQKPNSNIQSHSFNVDPSGFFKYGFPGPIHDLQNREEFISCYNRQTQNPYWVLEHITPESLAARNADRKNSFFKEDEVIPEKFRGKLRDYFRSGYDRGHQAPAADAKFSQQAMDDTFYLSNMCPQVGEGFNRDYWAHLEYFCRGLTKKYKSVRIVTGPLYLPKKDPIDNKFRVNYEVIGNPPSIAVPTHFFKLIVAEAPTANPAREDIAVAAFVLPNEPISNETKLTDFEVPIDALERSTGLELLQKVPPSKKKALCKEVNCQIVVRDFSNAAIKQSKDVKLLPPPKKRN
Protein: dITP/XTP pyrophosphatase (EC 3.6.1.66) (Hypoxanthine/xanthine dNTP pyrophosphatase) (Non-canonical purine NTP pyrophosphatase) (Non-standard purine NTP pyrophosphatase) (Nucleoside-triphosphate diphosphatase) (Nucleoside-triphosphate pyrophosphatase) (NTPase) (Nucleotide triphosphatase) (Q57679)
Organism: Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440) (Methanococcus jannaschii)
Function: Pyrophosphatase that catalyzes the hydrolysis of nucleoside triphosphates to their monophosphate derivatives, with a high preference for the non-canonical purine nucleotides xanthosine triphosphate (XTP), deoxyinosine triphosphate (dITP) and ITP. Probably functions as a house-cleaning enzyme that removes non-canonical purine nucleotides from the nucleotide pool, thus preventing their incorporation into DNA/RNA and avoiding chromosomal lesions. Shows very low activity on GTP or dGTP, both of which are hydrolyzed more than 100-fold less efficiently than XTP, and has nearly no activity toward the canonical nucleotides ATP, CTP, and TTP, and toward 6-N-hydroxylaminopurine deoxynucleoside triphosphate (dHAPTP). Displays neither endonuclease nor 3'-exonuclease activities.
Interaction partners:
- Inosine-5'-monophosphate dehydrogenase
- Nucleoside diphosphate kinase
- GMP synthase subunit B
- GMP synthase subunit A
- 5'-nucleotidase SurE
- Probable inosine/xanthosine triphosphatase
- Universal stress protein MJ0577
- Probable bifunctional tRNA threonylcarbamoyladenosine biosynthesis protein
- Probable metallophosphoesterase MJ0623
- Phosphodiesterase MJ0936
Sequence:
MKIYFATGNPNKIKEANIILKDLKDVEIEQIKISYPEIQGTLEEVAEFGAKWVYNILKKPVIVEDSGFFVEALNGFPGTYSKFVQETIGNEGILKLLEGKDNRNAYFKTVIGYCDENGVRLFKGIVKGRVSEEIRSKGYGFAYDSIFIPEEEERTFAEMTTEEKSQISHRKKAFEEFKKFLLDRI
Protein: Caspase-10 (CASP-10) (EC 3.4.22.63) (Apoptotic protease Mch-4) (FAS-associated death domain protein interleukin-1B-converting enzyme 2) (FLICE2) (ICE-like apoptotic protease 4) [Cleaved into: Caspase-10 subunit p23/17; Caspase-10 subunit p12] (Q92851)
Organism: Homo sapiens (Human)
Function: Involved in the activation cascade of caspases responsible for apoptosis execution. Recruited to both Fas- and TNFR-1 receptors in a FADD dependent manner. May participate in the granzyme B apoptotic pathways. Cleaves and activates effector caspases CASP3, CASP4, CASP6, CASP7, CASP8 and CASP9. Hydrolyzes the small- molecule substrates, Tyr-Val-Ala-Asp-|-AMC and Asp-Glu-Val-Asp-|-AMC.
Interaction partners:
- Caspase-8
- FAS-associated death domain protein
- CASP8 and FADD-like apoptosis regulator
- Receptor-interacting serine/threonine-protein kinase 1
- Tumor necrosis factor receptor type 1-associated DEATH domain protein
- Tumor necrosis factor receptor superfamily member 6
- Tumor necrosis factor ligand superfamily member 6
- BH3-interacting domain death agonist
- Caspase-3
- Caspase-7
Sequence:
MKSQGQHWYSSSDKNCKVSFREKLLIIDSNLGVQDVENLKFLCIGLVPNKKLEKSSSASDVFEHLLAEDLLSEEDPFFLAELLYIIRQKKLLQHLNCTKEEVERLLPTRQRVSLFRNLLYELSEGIDSENLKDMIFLLKDSLPKTEMTSLSFLAFLEKQGKIDEDNLTCLEDLCKTVVPKLLRNIEKYKREKAIQIVTPPVDKEAESYQGEEELVSQTDVKTFLEALPQESWQNKHAGSNGNRATNGAPSLVSRGMQGASANTLNSETSTKRAAVYRMNRNHRGLCVIVNNHSFTSLKDRQGTHKDAEILSHVFQWLGFTVHIHNNVTKVEMEMVLQKQKCNPAHADGDCFVFCILTHGRFGAVYSSDEALIPIREIMSHFTALQCPRLAEKPKLFFIQACQGEEIQPSVSIEADALNPEQAPTSLQDSIPAEADFLLGLATVPGYVSFRHVEEGSWYIQSLCNHLKKLVPRMLKFLEKTMEIRGRKRTVWGAKQISATSLPTAISAQTPRPPMRRWSSVS
Protein: snRNA-activating protein complex subunit 3 (SNAPc subunit 3) (Proximal sequence element-binding transcription factor subunit beta) (PSE-binding factor subunit beta) (PTF subunit beta) (Small nuclear RNA-activating complex polypeptide 3) (snRNA-activating protein complex 50 kDa subunit) (SNAPc 50 kDa subunit) (Q92966)
Organism: Homo sapiens (Human)
Function: Part of the SNAPc complex required for the transcription of both RNA polymerase II and III small-nuclear RNA genes. Binds to the proximal sequence element (PSE), a non-TATA-box basal promoter element common to these 2 types of genes. Recruits TBP and BRF2 to the U6 snRNA TATA box.
Subcellular location: Nucleus.
Interaction partners:
- snRNA-activating protein complex subunit 4
- snRNA-activating protein complex subunit 2
- snRNA-activating protein complex subunit 1
- snRNA-activating protein complex subunit 5
- TATA-box-binding protein
- Transcription initiation factor IIA subunit 2
- Transcription initiation factor IIB
- Transcription initiation factor IIA subunit 1
- DNA-directed RNA polymerases I, II, and III subunit RPABC4
- DNA-directed RNA polymerases I, II, and III subunit RPABC3
Sequence:
MAEGSRGGPTCSGVGGRQDPVSGSGGCNFPEYELPELNTRAFHVGAFGELWRGRLRGAGDLSLREPPASALPGSQAADSDREDAAVARDLDCSLEAAAELRAVCGLDKLKCLEDGEDPEVIPENTDLVTLGVRKRFLEHREETITIDRACRQETFVYEMESHAIGKKPENSADMIEEGELILSVNILYPVIFHKHKEHKPYQTMLVLGSQKLTQLRDSIRCVSDLQIGGEFSNTPDQAPEHISKDLYKSAFFYFEGTFYNDKRYPECRDLSRTIIEWSESHDRGYGKFQTARMEDFTFNDLCIKLGFPYLYCHQGDCEHVIVITDIRLVHHDDCLDRTLYPLLIKKHWLWTRKCFVCKMYTARWVTNNDSFAPEDPCFFCDVCFRMLHYDSEGNKLGEFLAYPYVDPGTFN