wanglab/gogpt-training-data huggingface dataset:
Protein: tRNA (uracil(54)-C(5))-methyltransferase (EC 2.1.1.35) (Transfer RNA methyltransferase 2) (tRNA(m5U54)-methyltransferase) (P33753)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Catalyzes the formation of 5-methyl-uridine at position 54 (m5U54) in all tRNA. May also have a role in tRNA stabilization or maturation.
Interaction partners:
- Ribosome biogenesis protein ERB1
- tRNA
- tRNA
- tRNA
- tRNA
- tRNA
- U3 small nucleolar RNA-associated protein 13
- tRNA pseudouridine synthase 4
- Dimethyladenosine transferase
- Ribosome biogenesis protein RPF2
Sequence:
MYEQFEFSFFFFENSDNKVKYKAHLISSIKRWSIITCMRCFWTVQKSIFKARFFACRNFVKKHNYKLISTMTGSTEMVPPTMKHTVDNKRLSSPLTDSGNRRTKKPKLRKYKAKKVETTSPMGVLEFEVNDLLKSQNLSREQVLNDVTSILNDKSSTDGPIVLQYHREVKNVKVLEITSNGNGLALIDNPVETEKKQVVIIPFGLPGDVVNIKVFKTHPYYVESDLLDVVEKSPMRRDDLIRDKYFGKSSGSQLEFLTYDDQLELKRKTIMNAYKFFAPRLVAEKLLPPFDTTVASPLQFGYRTKITPHFDMPKRKQKELSVRPPLGFGQKGRPQWRKDTLDIGGHGSILDIDECVLATEVLNKGLTNERRKFEQEFKNYKKGATILLRENTTILDPSKPTLEQLTEEASRDENGDISYVEVEDKKNNVRLAKTCVTNPRQIVTEYVDGYTFNFSAGEFFQNNNSILPIVTKYVRDNLQAPAKGDDNKTKFLVDAYCGSGLFSICSSKGVDKVIGVEISADSVSFAEKNAKANGVENCRFIVGKAEKLFESIDTPSENTSVILDPPRKGCDELFLKQLAAYNPAKIIYISCNVHSQARDVEYFLKETENGSAHQIESIRGFDFFPQTHHVESVCIMKRI
Protein: 40S ribosomal protein S10, putative (Q38B67)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
Interaction partners:
- 40S ribosomal protein S5, putative
- 40S ribosomal protein S4
- 40S ribosomal protein S27, putative
- Small ribosomal subunit protein uS4
- 40S ribosomal protein S15, putative
- 40S ribosomal protein S14
- 40S ribosomal protein S23, putative
- 40S ribosomal protein S24
- 40S ribosomal protein S33, putative
- 40S ribosomal protein S25
Sequence:
MYTILLVCCFKNYCLCSFFVQITVTTSLPLPVGLLHLCLTTGQRISNMTTYVPKSSRDDVYRFFFTEGVVSCKKDPLGTWKGTLGGKTFKLPTLQVMQLMRSLKSRGLIKEQFAWRHFYWTLNDEGINYMRKYLYLGADAVPNTHKVDHKTFEREGGRGRGRGDGRGRGRGFGRGRGEGRGFGRGRGEGRGRGFHSERDQYRAGAAAQGEDAAPVAAVE
Protein: Keratin, type II cytoskeletal 74 (Cytokeratin-74) (CK-74) (Keratin-5c) (K5C) (Keratin-74) (K74) (Type II inner root sheath-specific keratin-K6irs4) (Type-II keratin Kb37) (Q7RTS7)
Organism: Homo sapiens (Human)
Function: Has a role in hair formation. Specific component of keratin intermediate filaments in the inner root sheath (IRS) of the hair follicle (Probable).
Interaction partners:
- Lysophosphatidic acid receptor 6
- Keratin, type I cytoskeletal 27
- Keratin, type II cytoskeletal 71
- Keratin, type I cytoskeletal 25
Sequence:
MSRQLNIKSSGDKGNFSVHSAVVPRKAVGSLASYCAAGRGAGAGFGSRSLYSLGGNRRISFNVAGGGVRAGGYGFRPGSGYGGGRASGFAGSMFGSVALGPACLSVCPPGGIHQVTVNKSLLAPLNVELDPEIQKVRAQEREQIKVLNDKFASFIDKVRFLEQQNQVLETKWELLQQLDLNNCKKNLEPILEGYISNLRKQLETLSGDRVRLDSELRSMRDLVEDYKKRYEVEINRRTTAENEFVVLKKDADAAYAVKVELQAKVDSLDKEIKFLKCLYDAEIAQIQTHASETSVILSMDNNRDLDLDSIIAEVRMHYEEIALKSKAEAEALYQTKIQELQLAASRHGDDLKHTRSEMVELNRLIQRIRCEIGNVKKQRASLETAIADAEQRGDNALKDAQAKLDELEGALHQAKEELARMLREYQELMSLKLALDMEIATYRKLLEGEECRMSGENPSSVSISVISSSSYSYHHPSSAGVDLGASAVAGSSGSTQSGQTKTTEARGGDLKDTQGKSTPASIPARKATR
Protein: Paired box protein Pax-6 (A0A1W2PQM7)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123, ECO:0000256|PROSITE-ProRule:PRU00108, ECO:0000256|RuleBase:RU000682}.
Interaction partners:
Sequence:
MQNSHSGVNQLGGVFVNGRPLPDSTRQKIVELAHSGARPCDISRILQVSNGCVSKILGRYYETGSIRPRAIGGSKPRVATPEVVSSINRVLRNLASEKQQMGADGMYDKLRMLNGQTGSWGTRPGWYPGTSVPGQPTQDGCQQQEGGGENTNSISSNGEDSDEAQMRLQLKRKLQRNRTSFTQEQIEALEKEFERTHYPDVFARERLAAKIDLPEARIQVWFSNRRAKWRREEKLRNQRRQASNTPSHIPISSSFSTSVYQPIPQPTTPVSSFTSGSMLGRTDTALTNTYSALPPMPSFTMANNLPMQPPVPSQTSSYSCMLPTSPSVNGRSYDTYTPPHMQTHMNSQPMGTSGTTSTGLISPGVSVPVQVPGSEPDMSQYWPRLQ
Protein: Methyl-CpG-binding domain protein 4 (EC 3.2.2.-) (A0A8I5ZTJ7)
Organism: Rattus norvegicus (Rat)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123, ECO:0000256|PIRNR:PIRNR038005}.
Interaction partners:
Sequence:
MESPSLGDNNVPSVTAGKSLVSDPPWDRCKEDVAVGLGGVGEDGKDLVISSECGSLLQEPAASTLPSCTTVAECHKPVPCGWERVVKQRLSGKTAGRVDVYFISPQGSKFRSKRSLANYLLKTGETCLKPEDFDFTVLSKGGINPGYKHQSLSAPASQQPNEADISKLNLRTRSKWKTDVLPLPGGNSESPDSNSLSNSNSARLLLKEHKGIQDADSGKSRKPKIKVTVLKGIASQRTKQRCRKSPSDSTGRNRKRLCTVQKADTDSELVPQESRLHRTVCPADACARATVSLVREAKGLGEEKSPSSDLRFTQVTSSITNKLYSTEAAGEATREATREQTFLESEEIRSKGEEEEAHLHIDILQSGSETPSCSQAKKHLTSETFREDSIPRTQVEKRKTSLYFSSKYNKEALSPPRRKAFKKWTPPRSPFNLVQETLFHDPWKLLISTIFLNRTSGLWVTVILSWLEGRDPNWLRGPSSGVGDLAQWQSTCLGSARPWVRSPAPKKRTKKKKRPKFKVHLKFVILDKAFPF
Protein: Gustatory receptor for bitter taste 66a (Q9VSH2)
Organism: Drosophila melanogaster (Fruit fly)
Function: Gustatory receptor required for response to the bitter in taste neurons. Gr66a cells respond to bitter compounds such as caffeine, theophylline, threonine or valine. Flies avoid bitter substances, suggesting that Gr66a neuron activity is sufficient to mediate avoidance behavior. Required for sensing and avoiding N,N-Diethyl-meta-toluamide (DEET), the most widely used insect repellent worldwide, as well as to L-canavanine, a plant-derived insecticide. Gr66a neurons are also involved in the sex-specific perception of molecules inducing male avoidance behavior, probably through sensing 7-tricosene (7-T), a male cuticular pheromone and leading to inhibition of male-male courtship. Finally, also plays a role in oviposition behavior, in which females evaluate their environment and choose to lay eggs on substrates they may find aversive in other contexts.
Subcellular location: Cell membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}.
Interaction partners:
- Gustatory receptor 5a for trehalose
- Gustatory and pheromone receptor 33a
- Gustatory and pheromone receptor 32a
- Gustatory receptor for sugar taste 64f
- Gustatory receptor for bitter taste 93a
- Pickpocket protein 28
- Gustatory receptor 8a
- Gustatory receptor
- Gustatory receptor for bitter taste 22e
- Pickpocket 23, isoform C
Sequence:
MAQAEDAVQPLLQQFQQLFFISKIAGILPQDLEKFRSRNLLEKSRNGMIYMLSTLILYVVLYNILIYSFGEEDRSLKASQSTLTFVIGLFLTYIGLIMMVSDQLTALRNQGRIGELYERIRLVDERLYKEGCVMDNSTIGRRIRIMLIMTVIFELSILVSTYVKLVDYSQWMSLLWIVSAIPTFINTLDKIWFAVSLYALKERFEAINATLEELVDTHEKHKLWLRGNQEVPPPLDSSQPPQYDSNLEYLYKELGGMDIGSIGKSSVSGSGKNKVAPVAHSMNSFGEAIDAASRKPPPPPLATNMVHESELGNAAKVEEKLNNLCQVHDEICEIGKALNELWSYPILSLMAYGFLIFTAQLYFLYCATQYQSIPSLFRSAKNPFITVIVLSYTSGKCVYLIYLSWKTSQASKRTGISLHKCGVVADDNLLYEIVNHLSLKLLNHSVDFSACGFFTLDMETLYGVSGGITSYLIILIQFNLAAQQAKEAIQTFNSLNDTAGLVGAATDMDNISSTLRDFVTTTMTPAV
Protein: Ubiquitin-ribosomal protein eS31B fusion protein [Cleaved into: Ubiquitin; Small ribosomal subunit protein eS31B (40S ribosomal protein S27b)] (P0C8R3)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Ubiquitin exists either covalently attached to another protein, or free (unanchored). When covalently bound, it is conjugated to target proteins via an isopeptide bond either as a monomer (monoubiquitin), a polymer linked via different Lys residues of the ubiquitin (polyubiquitin chains) or a linear polymer linked via the initiator Met of the ubiquitin (linear polyubiquitin chains). Polyubiquitin chains, when attached to a target protein, have different functions depending on the Lys residue of the ubiquitin that is linked: Lys-6-linked may be involved in DNA repair; Lys-11-linked is involved in ERAD (endoplasmic reticulum-associated degradation) and in cell-cycle regulation; Lys-29-linked is involved in lysosomal degradation; Lys-33-linked is involved in kinase modification; Lys-48-linked is involved in protein degradation via the proteasome; Lys-63-linked is involved in endocytosis, and DNA-damage responses. Linear polymer chains formed via attachment by the initiator Met lead to cell signaling. Ubiquitin is usually conjugated to Lys residues of target proteins, however, in rare cases, conjugation to Cys or Ser residues has been observed. When polyubiquitin is free (unanchored-polyubiquitin), it also has distinct roles, such as in activation of protein kinases, and in signaling (By similarity).
Subcellular location: [Ubiquitin]: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.; SUBCELLULAR LOCATION: [Small ribosomal subunit protein eS31B]: Cytoplasm {ECO:0000250|UniProtKB:P05759}. Nucleus, nucleolus {ECO:0000269|PubMed:16823372}.
Interaction partners:
- Ubiquitin-ribosomal protein eS31A fusion protein
- Elongation factor 3
- mRNA export factor elf1
- Small ribosomal subunit protein uS10
- Small ribosomal subunit protein eS27
- Small ribosomal subunit protein uS5
- Small ribosomal subunit protein eS7
- Small ribosomal subunit protein uS15
- Small ribosomal subunit protein uS3
- Ubiquitin-conjugating enzyme E2 15
Sequence:
MQIFVKTLTGKTITLEVESSDTIDNVKSKIQDKEGIPPDQQRLIFAGKQLEDGRTLSDYNIQKESTLHLVLRLRGGGKKRKKKTYTTPKKIKHKHKKVELAVLKYYKVEDDGSVKRLRRECPNCGASTFMANHKDRLYCGRCHLTLKLEA
Protein: COMM domain containing 10 (D6RJ90)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MKKAVSLINAIDTGRFPRLLTRILQKLHLKAESSFSEEEEEKLQAAFSLEKQDLHLVLETISFILEQAVYHNVKPAALQQQLENIHLRQDKAEAFVNTWSSMGQETVEKFRQRILAPCKLETVGWQLNLQMAHSAQAKLKSPQAVLQLGVNNEDSKSLEKVLVEFSHKELFDFYNKLETIQAQLDSLT
Protein: Malic acid transport protein (Malate permease) (P50537)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Permease for malate and other C4 dicarboxylic acids.
Subcellular location: Membrane; Multi-pass membrane protein.
Interaction partners:
- NAD-dependent malic enzyme
- Lysophospholipase NTE1
- Malate dehydrogenase, mitochondrial
Sequence:
MGELKEILKQRYHELLDWNVKAPHVPLSQRLKHFTWSWFACTMATGGVGLIIGSFPFRFYGLNTIGKIVYILQIFLFSLFGSCMLFRFIKYPSTIKDSWNHHLEKLFIATCLLSISTFIDMLAIYAYPDTGEWMVWVIRILYYIYVAVSFIYCVMAFFTIFNNHVYTIETASPAWILPIFPPMICGVIAGAVNSTQPAHQLKNMVIFGILFQGLGFWVYLLLFAVNVLRFFTVGLAKPQDRPGMFMFVGPPAFSGLALINIARGAMGSRPYIFVGANSSEYLGFVSTFMAIFIWGLAAWCYCLAMVSFLAGFFTRAPLKFACGWFAFIFPNVGFVNCTIEIGKMIDSKAFQMFGHIIGVILCIQWILLMYLMVRAFLVNDLCYPGKDEDAHPPPKPNTGVLNPTFPPEKAPASLEKVDTHVTSTGGESDPPSSEHESV
Protein: UDP-N-acetylglucosamine transporter (Golgi UDP-GlcNAc transporter) (Solute carrier family 35 member A3) (Q9Y2D2)
Organism: Homo sapiens (Human)
Function: Uridine diphosphate-N-acetylglucosamine (UDP-GlcNAc) transporter in the Golgi apparatus. May supply UDP-GlcNAc as substrate for Golgi-resident glycosyltransferases that generate branching of diantennary oligosaccharides.
Subcellular location: Golgi apparatus membrane {ECO:0000269|PubMed:10393322, ECO:0000269|PubMed:23766508, ECO:0000269|PubMed:28167211}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Nucleotide sugar transporter SLC35D2
- Solute carrier family 35 member D3
- Nucleotide sugar transporter SLC35D1
- Nucleotide sugar transporter SLC35B4
Sequence:
MFANLKYVSLGILVFQTTSLVLTMRYSRTLKEEGPRYLSSTAVVVAELLKIMACILLVYKDSKCSLRALNRVLHDEILNKPMETLKLAIPSGIYTLQNNLLYVALSNLDAATYQVTYQLKILTTALFSVSMLSKKLGVYQWLSLVILMTGVAFVQWPSDSQLDSKELSAGSQFVGLMAVLTACFSSGFAGVYFEKILKETKQSVWIRNIQLGFFGSIFGLMGVYIYDGELVSKNGFFQGYNRLTWIVVVLQALGGLVIAAVIKYADNILKGFATSLSIILSTLISYFWLQDFVPTSVFFLGAILVITATFLYGYDPKPAGNPTKA
Protein: Acid-sensing ion channel 4 (ASIC4) (Amiloride-sensitive cation channel 4) (Amiloride-sensitive cation channel 4, pituitary) (Q96FT7)
Organism: Homo sapiens (Human)
Function: Probable cation channel with high affinity for sodium. In vitro, has no proton-gated channel activity.
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:P78348}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Acid-sensing ion channel 3
- Bile acid-sensitive ion channel
- Probable thioesterase PNKD
- Hydroxyacylglutathione hydrolase, mitochondrial
- Acid-sensing ion channel 2
Sequence:
MPIEIVCKIKFAEEDAKPKEKEAGDEQSLLGAVAPGAAPRDLATFASTSTLHGLGRACGPGPHGLRRTLWALALLTSLAAFLYQAAGLARGYLTRPHLVAMDPAAPAPVAGFPAVTLCNINRFRHSALSDADIFHLANLTGLPPKDRDGHRAAGLRYPEPDMVDILNRTGHQLADMLKSCNFSGHHCSASNFSVVYTRYGKCYTFNADPRSSLPSRAGGMGSGLEIMLDIQQEEYLPIWRETNETSFEAGIRVQIHSQEEPPYIHQLGFGVSPGFQTFVSCQEQRLTYLPQPWGNCRAESELREPELQGYSAYSVSACRLRCEKEAVLQRCHCRMVHMPGNETICPPNIYIECADHTLDSLGGGPEGPCFCPTPCNLTRYGKEISMVRIPNRGSARYLARKYNRNETYIRENFLVLDVFFEALTSEAMEQRAAYGLSALLGDLGGQMGLFIGASILTLLEILDYIYEVSWDRLKRVWRRPKTPLRTSTGGISTLGLQELKEQSPCPSRGRVEGGGVSSLLPNHHHPHGPPGGLFEDFAC
Protein: Cytoadherence-linked asexual protein 3.1 (CLAG3) (RhopH1) (O77310)
Organism: Plasmodium falciparum (isolate 3D7)
Subcellular location: Host cell membrane {ECO:0000269|PubMed:29739907, ECO:0000269|PubMed:35393572}; Single-pass membrane protein {ECO:0000255}. Host cell membrane {ECO:0000269|PubMed:29739907, ECO:0000269|PubMed:35393572}; Peripheral membrane protein {ECO:0000250|UniProtKB:A0A1W6IZJ5}; Cytoplasmic side {ECO:0000250|UniProtKB:A0A1W6IZJ5}. Host cytoplasm {ECO:0000269|PubMed:35393572}. Cytoplasmic vesicle, secretory vesicle, rhoptry {ECO:0000269|PubMed:28252383, ECO:0000269|PubMed:29739907}.
Interaction partners:
- High molecular weight rhoptry protein 3
- High molecular weight rhoptry protein 2
Sequence:
MVSFFKTPIFILIIFLYLNEKVICSINENQNENDTISQNVNQHENINQNVNDNDNIEQLKSMIGNDELHKNLTILEKLILESLEKDKLKYPLLKQGTEQLIDISKFNKKNITDADDETYIIPTVQSTFHDIVKYEHLIKEQSIEIYNSDISDKIKKKIFIVRTLKTIKLMLIPLNSYKQNNDLKSALEELNNVFTNKEAQEESSPIGDHGTFFRKLLTHVRTIKENEDIENKGETLILGDNKIDVMNSNDFFFTTNSNVKFMENLDDITNQYGLGLINHLGPHLIALGHFTVLKLALKNYKNYFEAKSIKFFSWQKILEFSMSDRFKVLDMMCDHESVYYSEKKRRKTYLKVDRSNTSMECNILEYLLHYFNKYQLEIIKTTQDTDFDLHGMMEHKYIKDYFFSFMCNDPKECIIYHTNQFKKEANEENTFPEQEEPNRQISAFNLYLNYYYFMKRYSSYGVKKTLYVHLLNLTGLLNYDTRAYVTSLYLPGYYNAVEMSFTEEKEFSKLFESLIQCIEKCHSDQARQISKDSNLLNNITKCDLCKGAFLYANMKFDEVPSMLQKFYVYLTKGLKIQKVSSLIKTLDIYQDYSNYLSHDINWYTFLFLFRLTSFKEIAKKNVAEAMYLNIKDEDTFNKTVVTNYWYPSPIKKYYTLYVRKHIPNNLVDELEKLMKSGTLEKMKKSLTFLVHVNSFLQLDFFHQLNEPPLGLPRSYPLSLVLEHKFKEWMNSSPAGFYFSNYQNPYIRKDLHDKVLSQKFEPPKMNQWNKVLKSLIECAYDMYFEQRHVKNLYKYHNIYNINNKLMLMRDSIDLYKNNFDDVLFFADIFNMRKYMTATPVYKKVKDRVYHTLHSITGNSVNFYKYGIIYGFKVNKEILKEVVDELYSIYNFNTDIFTDTSFLQTVYLLFRRIEETYRTQRRDDKISVNNVFFMNVANNYSKLNKEEREIEIHNSMASRYYAKTMFAAFQMLFSTMLSNNVDNLDKAYGLSENIQVATSTSAFLTFAYVYNGSIMDSVTNSLLPPYAKKPITQLKYGKTFVFSNYFMLASKMYDMLNYKNLSLLCEYQAVASANFYSAKKVGQFLGRKFLPITTYFLVMRISWTHAFTTGQHLISAFGSPSSTANGKSNASGYKSPESFFFTHGLAAEASKYLFFYFFTNLYLDAYKSFPGGFGPAIKEQTQHVQEQTYERKPSVHSFNRNFFMELVNGFMYAFCFFAISQMYAYFENINFYITSNFRFLDRYYGVFNKYFINYAIIKLKEITSDLLIKYEREAYLSMKKYGYLGEVIAARLSPKDKIMNYVHETNEDIMSNLRRYDMENAFKNKMSTYVDDFAFFDDCGKNEQFLNERCDYCPVIEEVEETQLFTTTGDKNTNKTTEIKKQTSTYIDTEKMNEADSADSDDEKDSDTPDDELMISRFH
Protein: NADP-specific glutamate dehydrogenase (NADP-GDH) (EC 1.4.1.4) (P00370)
Organism: Escherichia coli (strain K12)
Function: Catalyzes the reversible oxidative deamination of glutamate to alpha-ketoglutarate and ammonia.
Interaction partners:
- Glutamate synthase large chain
- Glutamine synthetase
- Glutamate synthase small chain
- Isocitrate dehydrogenase
- Aspartate aminotransferase
- Bifunctional protein PutA
- Glutamate decarboxylase alpha
- Amino-acid acetyltransferase
- Citrate synthase
- Glutamate decarboxylase beta
Sequence:
MDQTYSLESFLNHVQKRDPNQTEFAQAVREVMTTLWPFLEQNPKYRQMSLLERLVEPERVIQFRVVWVDDRNQIQVNRAWRVQFSSAIGPYKGGMRFHPSVNLSILKFLGFEQTFKNALTTLPMGGGKGGSDFDPKGKSEGEVMRFCQALMTELYRHLGADTDVPAGDIGVGGREVGFMAGMMKKLSNNTACVFTGKGLSFGGSLIRPEATGYGLVYFTEAMLKRHGMGFEGMRVSVSGSGNVAQYAIEKAMEFGARVITASDSSGTVVDESGFTKEKLARLIEIKASRDGRVADYAKEFGLVYLEGQQPWSLPVDIALPCATQNELDVDAAHQLIANGVKAVAEGANMPTTIEATELFQQAGVLFAPGKAANAGGVATSGLEMAQNAARLGWKAEKVDARLHHIMLDIHHACVEHGGEGEQTNYVQGANIAGFVKVADAMLAQGVI
Protein: Importin subunit alpha-4 (IMPa-4) (O80480)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Binds to conventional NLS motifs and mediates nuclear protein import across the nuclear envelope. Acts as cellular receptor for the nuclear import of the virD2 protein of Agrobacterium and is essential for Agrobacterium-mediated root transformation.
Subcellular location: Nucleus envelope {ECO:0000250|UniProtKB:Q96321}.
Interaction partners:
- Importin subunit beta-1
- Transcription factor VIP1
- Nuclear cap-binding protein subunit 1
- Exportin-2
- Ran-binding protein 1 homolog c
- Nuclear pore complex protein NUP50A
- Transportin
- F-box protein VBF
- Nucleoporin
- Nuclear pore complex protein NUP96
Sequence:
MSLRPSTRAELRKKIYKTGVDADEARRRREDNLVEIRKNKREDSLLKKRREGMMLQQQLPLGAGLDGPQTAAAVEKRLEGIPMMVQGVYSDDPQAQLEATTQFRKLLSIERSPPIDEVIKAGVIPRFVEFLGRHDHPQLQFEAAWALTNVASGTSDHTRVVIEQGAVPIFVKLLTSASDDVREQAVWALGNVAGDSPNCRNLVLNYGALEPLLAQLNENSKLSMLRNATWTLSNFCRGKPPTPFEQVKPALPILRQLIYLNDEEVLTDACWALSYLSDGPNDKIQAVIEAGVCPRLVELLGHQSPTVLIPALRTVGNIVTGDDSQTQFIIESGVLPHLYNLLTQNHKKSIKKEACWTISNITAGNKLQIEAVVGAGIILPLVHLLQNAEFDIKKEAAWAISNATSGGSHEQIQYLVTQGCIKPLCDLLICPDPRIVTVCLEGLENILKVGEADKEMGLNSGVNLYAQIIEESDGLDKVENLQSHDNNEIYEKAVKILERYWAEEEEEQILQDGGNDNSQQAFNFGNNPAAPVGGFKFA
Protein: Carbonic anhydrase (EC 4.2.1.1) (Carbonate dehydratase) (A0A0B4LGX6)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MERILRGIMRYRNTTREQMVKEFQKVRDNPEPKAVFFTCMDSRMIPTRYTDTHVGDMFVGE
Protein: Cytoplasmic tRNA 2-thiolation protein 2 (Q9UUC7)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Plays a central role in 2-thiolation of mcm(5)S(2)U at tRNA wobble positions of tRNA(Lys), tRNA(Glu) and tRNA(Gln). May act by forming a heterodimer with ctu1 that ligates sulfur from thiocarboxylated urm1 onto the uridine of tRNAs at wobble position. Prior mcm(5) tRNA modification by the elongator complex is required for 2-thiolation. May also be involved in protein urmylation.
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03054, ECO:0000269|PubMed:16823372}. Nucleus {ECO:0000269|PubMed:16823372}.
Interaction partners:
- Cytoplasmic tRNA 2-thiolation protein 1
- Probable tRNA
- Ubiquitin-related modifier 1
- Elongator complex protein 3
- Adenylyltransferase and sulfurtransferase uba4
- Probable 3-mercaptopyruvate sulfurtransferase
- Putative tRNA pseudouridine synthase C25B8.05
- tRNA
- Elongator complex protein 1
- Cys-Gly metallodipeptidase dug1
Sequence:
MQNTALDNSADSKCSKCDNKATVLTKSDAVCDSCFVRRIENKIRRQFELVRPNLQGRKSKRAMLAISGGISSMAMLETANYLSKYRDDNYRPMFDELLAVHFQWGTDSAVAKTIEESISKNYPKCPFKVIGEAELLNRTIATDSRGNIEINADNEKFNPEVISSLASRQDLLYRIRDKLLVSYARKANCDTIVFGDSGTTIAARVLELVAEGRGFAIPWYTSVCSKLPNCDTFLLRPLREVLSSDLKSYMNIKGLAFCDSLIEARPNTIHGVTESYFSSLNDTFPSLVSTVVKMSSKLHVPSTEAICTICNLPMQEDAETWLQKTTVEHPDSVEGIKNQNVCYGCSVSLKSLKGTLHIPDIEKEGI
Protein: Protein Red (Cytokine IK) (IK factor) (Protein RER) (Q13123)
Organism: Homo sapiens (Human)
Function: Involved in pre-mRNA splicing as a component of the spliceosome. Auxiliary spliceosomal protein that regulates selection of alternative splice sites in a small set of target pre-mRNA species (Probable). Required for normal mitotic cell cycle progression. Recruits MAD1L1 and MAD2L1 to kinetochores, and is required to trigger the spindle assembly checkpoint. Required for normal accumulation of SMU1.
Subcellular location: Nucleus {ECO:0000269|PubMed:24945353, ECO:0000269|PubMed:28781166}. Nucleus, nucleoplasm {ECO:0000269|PubMed:24252166, ECO:0000269|PubMed:24945353}. Chromosome {ECO:0000269|PubMed:24252166}. Cytoplasm, cytoskeleton, spindle pole {ECO:0000269|PubMed:22351768}. Note=Predominantly present throughout the nucleoplasm during prometaphase, metaphase and anaphase. Is also detected in nuclear foci that are not identical with Cajal bodies. Starts to accumulate at chromosomes during telophase, and is nearly exclusively associated with chromosomes in newly divided cells (PubMed:24252166). Colocalizes with MAD1L1 at mitotic spindle poles during metaphase and anaphase (PubMed:22351768). {ECO:0000269|PubMed:24252166}.
Interaction partners:
- WD40 repeat-containing protein SMU1
- Microfibrillar-associated protein 1
- Pre-mRNA-processing factor 6
- 116 kDa U5 small nuclear ribonucleoprotein component
- Pre-mRNA-splicing factor 38A
- Splicing factor 3B subunit 3
- Pre-mRNA-processing-splicing factor 8
- U4/U6 small nuclear ribonucleoprotein Prp3
- U6 snRNA-associated Sm-like protein LSm4
- Splicing factor 3B subunit 1
Sequence:
MPERDSEPFSNPLAPDGHDVDDPHSFHQSKLTNEDFRKLLMTPRAAPTSAPPSKSRHHEMPREYNEDEDPAARRRKKKSYYAKLRQQEIERERELAEKYRDRAKERRDGVNKDYEETELISTTANYRAVGPTAEADKSAAEKRRQLIQESKFLGGDMEHTHLVKGLDFALLQKVRAEIASKEKEEEELMEKPQKETKKDEDPENKIEFKTRLGRNVYRMLFKSKAYERNELFLPGRMAYVVDLDDEYADTDIPTTLIRSKADCPTMEAQTTLTTNDIVISKLTQILSYLRQGTRNKKLKKKDKGKLEEKKPPEADMNIFEDIGDYVPSTTKTPRDKERERYRERERDRERDRDRDRERERERDRERERERDREREEEKKRHSYFEKPKVDDEPMDVDKGPGSTKELIKSINEKFAGSAGWEGTESLKKPEDKKQLGDFFGMSNSYAECYPATMDDMAVDSDEEVDYSKMDQGNKKGPLGRWDFDTQEEYSEYMNNKEALPKAAFQYGIKMSEGRKTRRFKETNDKAELDRQWKKISAIIEKRKKMEADGVEVKRPKY
Protein: m7GpppX diphosphatase (EC 3.6.1.59) (Decapping scavenger enzyme) (Scavenger mRNA-decapping enzyme DcpS) (D3K0N9)
Organism: Ascaris suum (Pig roundworm) (Ascaris lumbricoides)
Function: Decapping scavenger enzyme that catalyzes the cleavage of a residual cap structure following the degradation of mRNAs of the 3'->5' exosome-mediated mRNA decay pathway. Hydrolyzes cap analog structures like 7-methylguanosine nucleoside triphosphate (m7GpppG) and tri-methyl guanosine nucleoside triphosphate (m3(2,2,7)GpppG) with up to 2 nucleotide substrates (small capped oligoribonucleotides) and specifically releases 5'-phosphorylated RNA fragments and 7-methylguanosine monophosphate (m7GMP). Does not hydrolyze unmethylated cap analog (GpppG) and shows no decapping activity on intact m7GpppG-capped mRNA molecules. Does not hydrolyze 7-methylguanosine diphosphate (m7GDP) and tri-methylguanosine diphosphate (m3(2,2,7)GDP) to m(7)GMP and m3(2,2,7)GMP, respectively. May also play a role in the 5'->3 mRNA decay pathway; m7GDP, the downstream product released by the 5'->3' mRNA mediated decapping activity, may be also converted by dcs-1 to m7GMP. Binds to m7GpppG and strongly to m7GDP.
Subcellular location: Nucleus {ECO:0000250}.
Interaction partners:
Sequence:
MVDEVDANSTGDNSLVNMKGFSFKEVLGSDSARKSAFILLDSSNGENAILLADKNAFPVDKTSWSAILTGSTLKPIMKNDIYSSYTLCMPNEFSDVKSTLIYPCNEKHIAKYRDQKRFIINETPEDYRTITLPYIQRNQMSLEWVYNILDHKAEVDRIIYEETDPHDGFILAPDLKWSGEQLECLYVQALVRRKGIKSIRDLTANDLPLLEGIRDKGLNAIKEKYGLDKHQIRAYFHYQPSFYHLHVHFIHVSYEAPASGVAKAVLLDDVINNLKLIPDFYQRSTLTFTAKEQDPIYRREN
Protein: Transcription initiation factor TFIID subunit 7 (Transcription initiation factor TFIID 55 kDa subunit) (TAFII-55) (O13701)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: TAFs are components of the transcription factor IID (TFIID) complex that are essential for mediating regulation of RNA polymerase transcription. Also involved in the transport of mRNA from the nucleus to the cytoplasm.
Subcellular location: Nucleus {ECO:0000269|PubMed:10388808}.
Interaction partners:
- SAGA complex/transcription factor TFIID complex subunit Taf10
- Transcription initiation factor TFIID subunit 4
- Transcription initiation factor TFIID subunit 8
- Putative transcription initiation factor TFIID 111 kDa subunit
- TATA-box-binding protein
- Transcription initiation factor TFIID subunit 11
- SAGA complex/transcription factor TFIID complex subunit Taf6
- Transcription initiation factor TFIID subunit 13
- Transcription initiation factor TFIID subunit 2
- SAGA complex/transcription factor TFIID complex subunit Taf12
Sequence:
MVKLKIRAVQPPPNDSRSSTPATGPPPPIPKIKIKTREPKGPRLTKIRLKRVREPGLGYDSEASDREEDTYIEEQIILRLPPGEDCEYVRKAIENREVGRGADIWVKFKDQRRAVVHVNGHLYAAKLVDLPCIIESNKSFDKKVIFKAADICQMLIATERIEHENSVLNTQLKQADYIYPHGLTTPMHWVRQKRFRKRVSNRTIEAVENEVDRLLAMDERAESTSNELIDQAQLARDSSIALSEDTSFDGMAGLRGTSIDRDDQSVQTDMFDGMDEDDLAGQIEQGMLELSQDTRESTAEPRAAGEESASEEEEEEEEEEEEENEADDETRENKRQNRLVREFISELESSIQKRRKDADEATNPILRNRFLADVNRMVTELELKRTQLVDNPE