wanglab/gogpt-training-data huggingface dataset:
Protein: Eukaryotic translation initiation factor 3 subunit E (eIF3e) (Eukaryotic translation initiation factor 3 subunit 6) (eIF-3 p48) (E5RGA2)
Organism: Homo sapiens (Human)
Subcellular location: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03004}. Nucleus {ECO:0000256|HAMAP-Rule:MF_03004}. Nucleus, PML body {ECO:0000256|HAMAP-Rule:MF_03004}.
Interaction partners:
Sequence:
MFEDPETTRQMQSTRDGRMLFDYLADKHGFRQEYLDTLYRYAKFQYECGNYSGAAEYLYFFRVLVPATDRNALSSLWGKLASEILMQNWDAAMEDLTRLKETIDNNSVSSPLQSLQQRTWLIHWSLFVFFNHPKGRDNIIDLFLYQPQYLNAIQTMCPHILRYLTTAVITNKDVRKRRQVLKDLVKVIQQESYTYKDPITEFVECLYVNFDFDGAQKKLRECESVLVNDFFLVACLEDFIENARLFIFETFCRIHQCISINMLADKLNMTPEEAERWIVNLIRNARLDAKIDSKLGHVVMGNNAVSPYQQVIEKTKSLSFRSQMLAMNIEKKLNQNSRSEAPNWATQDSGFY
Protein: Phosphoribomutase (PRM) (EC 5.4.2.7) (Phosphoglucomutase 3) (PGM 3) (Q03262)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Major phosphoribomutase that converts ribose 1-phosphate to ribose 5-phosphate. Involved in ribose salvage via the pentose phosphate pathway.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:14562095}. Nucleus {ECO:0000269|PubMed:14562095}.
Interaction partners:
- Phosphoglucomutase 1
- Phosphoglucomutase 2
- Glycogen phosphorylase
- Glucose-6-phosphate isomerase
- Probable UTP--glucose-1-phosphate uridylyltransferase
- UTP--glucose-1-phosphate uridylyltransferase
- Hexokinase-1
- Glucokinase-1
- Hexokinase-2
- Putative glucokinase-2
Sequence:
MLQGILETVPSDLKDPISLWFKQDRNPKTIEEVTALCKKSDWNELHKRFDSRIQFGTAGLRSQMQAGFSRMNTLVVIQASQGLATYVRQQFPDNLVAVVGHDHRFHSKEFARATAAAFLLKGFKVHYLNPDHEFVHTPLVPFAVDKLKASVGVMITASHNPKMDNGYKVYYSNGCQIIPPHDHAISDSIDANLEPWANVWDFDDVLNKALKQGKLMYSREEMLKLYLEEVSKNLVEINPLKLEVKAKPWFVYTPMHGVGFDIFSTIVKKTLCLVEGKDYLCVPEQQNPDPSFPTVGFPNPEEKGALDIGINLAEKHDIDLLVANDPDADRFSVAVKDMQSGEWRQLTGNEIGFLFAFYEYQKYKSMDKEFQHVHPLAMLNSTVSSQMIKKMAEIEGFHYEDTLTGFKWIGNRAILLEKKGYYVPFGFEEAIGYMFPAMEHDKDGISASIVFLQAYCKWKIDHNLDPLNVLENGFKKYGVFKEYNGYYVVPNPTVTKDIFDYIRNVYTPEGASYPSSIGEEIEVLYYRDLTTGYQSDTINHKPTLPVDPTSQMITVSARPSNGSENEHIRFTIRGSGTEPKLKVYIEACANEEQRASFLAKLTWNVLRREWFRPDEMNIVTKF
Protein: Gamma-aminobutyric acid receptor subunit alpha-6 (GABA(A) receptor subunit alpha-6) (GABAAR subunit alpha-6) (P16305)
Organism: Mus musculus (Mouse)
Function: GABA, the major inhibitory neurotransmitter in the vertebrate brain, mediates neuronal inhibition by binding to the GABA/benzodiazepine receptor and opening an integral chloride channel.
Subcellular location: Postsynaptic cell membrane {ECO:0000250|UniProtKB:P30191}; Multi-pass membrane protein {ECO:0000255}. Cell membrane {ECO:0000250|UniProtKB:P30191}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Class E basic helix-loop-helix protein 23
- Integrin beta-1
- Integrin beta-4
- Neuronal acetylcholine receptor subunit alpha-3
- CD151 antigen
- Integrin alpha-6
- Fibronectin
- Integrin alpha-3
- Inactive phospholipase C-like protein 1
- Vesicle-fusing ATPase
Sequence:
MVLLLPWLFIILWLENAQAQLEDEGNFYSENVSRILDNLLEGYDNRLRPGFGGAVTEVKTDIYVTSFGPVSDVEMEYTMDVFFRQTWTDERLKFKGPAEILSLNNLMVSKIWTPDTFFRNGKKSIAHNMTTPNKLFRLMQNGTILYTMRLTINADCPMRLVNFPMDGHACPLKFGSYAYPKTEIIYTWKKGPLYSVEVPEESSSLLQYDLIGQTVSSETIKSNTGEYVIMTVYFHLQRKMGYFMIQIYTPCIMTVILSQVSFWINKESVPARTVFGITTVLTMTTLSISARHSLPKVSYATAMDWFIAVCFAFVFSALIEFAAVNYFTNLQSQKAERQAQTAATPPVAKSKASESLQAEIVVHSDSKYHLKKRISSLTLPIVPSSEASKALSRTPILKSTPVSPPLLLPATGGTSKIDQYSRILFPVAFAGFNLVYWIVYLSKDTMEVSSTVE
Protein: Erythroid transcription factor (Eryf1) (GATA-binding factor 1) (GATA-1) (GF-1) (NF-E1 DNA-binding protein) (P15976)
Organism: Homo sapiens (Human)
Function: Transcriptional activator or repressor which serves as a general switch factor for erythroid development. It binds to DNA sites with the consensus sequence 5'-[AT]GATA[AG]-3' within regulatory regions of globin genes and of other genes expressed in erythroid cells. Activates the transcription of genes involved in erythroid differentiation of K562 erythroleukemia cells, including HBB, HBG1/2, ALAS2 and HMBS.
Subcellular location: Nucleus {ECO:0000269|PubMed:35030251}.
Interaction partners:
- Zinc finger protein ZFPM1
- T-cell acute lymphocytic leukemia protein 1
- Rhombotin-2
- LIM domain-binding protein 1
- Krueppel-like factor 1
- Transcription factor PU.1
- Transcription factor E2-alpha
- LIM domain-binding protein 2
- Runt-related transcription factor 1
- Bromodomain-containing protein 3
Sequence:
MEFPGLGSLGTSEPLPQFVDPALVSSTPESGVFFPSGPEGLDAAASSTAPSTATAAAAALAYYRDAEAYRHSPVFQVYPLLNCMEGIPGGSPYAGWAYGKTGLYPASTVCPTREDSPPQAVEDLDGKGSTSFLETLKTERLSPDLLTLGPALPSSLPVPNSAYGGPDFSSTFFSPTGSPLNSAAYSSPKLRGTLPLPPCEARECVNCGATATPLWRRDRTGHYLCNACGLYHKMNGQNRPLIRPKKRLIVSKRAGTQCTNCQTTTTTLWRRNASGDPVCNACGLYYKLHQVNRPLTMRKDGIQTRNRKASGKGKKKRGSSLGGTGAAEGPAGGFMVVAGGSGSGNCGEVASGLTLGPPGTAHLYQGLGPVVLSGPVSHLMPFPGPLLGSPTGSFPTGPMPPTTSTTVVAPLSS
Protein: ER-Golgi SNARE complex subunit Sed5 (Eurofung) (Q5AQA4)
Organism: Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004211}; Single-pass type IV membrane protein {ECO:0000256|ARBA:ARBA00004211}.
Interaction partners:
- Synaptobrevin homolog YKT6
- ER-golgi SNARE complex subunit Bet1
- Golgi SNAP receptor complex member 1
- Golgi transport protein Sly1, putative
- Vesicle transport v-SNARE protein vti1
- Synaptobrevin homologue SNC1/2
- Uncharacterized protein
- Vesicular-fusion protein sec17
- MYB DNA-binding domain protein
- Uncharacterized protein
Sequence:
MTGPTIQDRTSEFQAILGQAQKRAASSKVGSQRQALLTDSQRQQANGSPNGTAAGGKRRSEFARRAAEIGRGITATTAKLRRLAELAKRKTLFDDRPVEISELTYVIKQDLASLNQQIASLQALTLSQHPKSNRSKTDQEGEHNDNVVVMLQGKLADVGANFKDVLEVRTKNIQASRSRTENFVSSVSSKSQAALDPQRSDSPLYPSGRRTPQPGGSSDLLTLEPSNPSPLGRPSMQSDQQLLMMEEAESSNSYIQSRGEAIDAIERTINELGGIFGQLAQMVSEQSEMIQRIDANTEDVVDNVQGAQRELMKYWTRVSGNRWLIAKMFGVLMIFFLLWVLISG
Protein: PDZ domain-containing protein 11 (ATPase-interacting PDZ protein) (Plasma membrane calcium ATPase-interacting single-PDZ protein) (PMCA-interacting single-PDZ protein) (Q5EBL8)
Organism: Homo sapiens (Human)
Function: Mediates docking of ADAM10 to zonula adherens by interacting with PLEKHA7 which is required for PLEKHA7 to interact with the ADAM10-binding protein TSPAN33.
Subcellular location: [Isoform 2]: Secreted {ECO:0000305}.; SUBCELLULAR LOCATION: [Isoform 1]: Cytoplasm {ECO:0000269|PubMed:12763866}. Cell junction, adherens junction {ECO:0000269|PubMed:30463011}. Cell membrane {ECO:0000269|PubMed:30463011}.
Interaction partners:
- Copper-transporting ATPase 1
- Sodium-dependent multivitamin transporter
- Tetraspanin-33
- Pleckstrin homology domain-containing family A member 7
- Afadin
- Chromosome-associated kinesin KIF4A
- Pleckstrin homology domain-containing family A member 5
- Disintegrin and metalloproteinase domain-containing protein 10
- Copper transport protein ATOX1
- ADP/ATP translocase 2
Sequence:
MDSRIPYDDYPVVFLPAYENPPAWIPPHERVHHPDYNNELTQFLPRTITLKKPPGAQLGFNIRGGKASQLGIFISKVIPDSDAHRAGLQEGDQVLAVNDVDFQDIEHSKAVEILKTAREISMRVRFFPYNYHRQKERTVH
Protein: Replication factor C, subunit 2, putative (Q585Y7)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- Replication factor C, subunit 3, putative
- Proliferating cell nuclear antigen
- Replication factor C, subunit 5, putative
- Replication factor C, subunit 4, putative
- Checkpoint protein HUS1
- DNA polymerase eta
- Chromosome transmission fidelity protein 18 homolog
- Replication factor C, subunit 1, putative
- DNA primase large subunit
- BRCT domain-containing protein
Sequence:
MLPDPPLKKHRVEPSVDLRPWIEKYRPKSLDEVKSQEEVVQALRSTLRQGASMPHFLFHGPPGTGKTTAILAVAHELFGPDYIKSRVRELNASDDRGIQVIREKVKSFAQTAVGNVVQKVQSDGKIYPVPPFKVIILDEADALLPDAQAALRRMMEDFSDVTRFCILCNYVTRIIDPIASRCAKYRFKPLIKEALYERISEVASRENIQISRSSIDALDHVSGGDLRLAIMYLQYAQRANGNDLQKEDFVEVSGSVPASMMQTYLAALMMKSFDEVRSVTKRLVQQGYPACQILAQLQDYIVSAACPLNSAQRGSIALKLCDIEKRLSDGCDDFVQLLELGSFICSV
Protein: Cation transporter, putative (Q384C5)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
Sequence:
MANVNNETTECGALLSNITSLQTTLTSMGCQVPALHHHHRDNHTHGVVDDGIDGDTHGGCESGHGTYSIGLHVVAIFVVLIASFLGTLIPIIGKYVPALRLPPFALVLGKCIAAGVLLSVSTIHMINESILQLQEDCVPESFRESYEAYAFLFAVAGALLLHMVDVLSGFCVRRDEMVYSDTSAVVPHEVIDAEEAQAAPAALDAYDGHHCHYAVGMPQSRTKRLFSAMFMEFAVTVHSVFVGLAVGIARDAETKTLLVALVFHQMLEGLALGARLVDAELSLKLEMLFALLFSVSAPLGTAIAVGTIAIWNVSMVGTAFVITQAVTSAVCGGMLLYLAFCLMLSDFPSDMQKHAGKDKVRRFFRCFGMFAALWLGAALMAFIGKWI
Protein: Phosphate transporter PHO1 homolog 3 (Protein PHO1 homolog 3) (AtPHO1;H3) (Q6R8G7)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: May transport inorganic phosphate (Pi).
Subcellular location: Cell membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
- Inorganic phosphate transporter 1-1
- SPX domain-containing protein 1
- Protein PHOSPHATE STARVATION RESPONSE 1
- Endoglucanase 16
- SPX domain-containing protein 3
- SPX domain-containing protein 2
- Leucine-rich repeat receptor protein kinase EMS1
- Probable ubiquitin-conjugating enzyme E2 24
Sequence:
MKFGKEFSSQMVPEWQQAYMDYDFLKTLLKEIITFKRRTNNAPSHGGAKTGGGLNRKLTLYRAFSGLVSTPRHKRSNSSHDVEEGVQLTGSMRSGPILVNTTASHGYETTFLMAAEEGGEYELVFFRRLDDEFNKVDKFYRKKVEEVLKEAAMLNKQMDALIAFRVKVENPDGWRWEERTVEMTRLASDIATSAAALSASTPAGAKSMKVRSQEHMEAIQEGGSSRAGLMEDDEEDEDEQNETSVVSTGAIDNETTTSRMRGARPSPIDVLGRVKINNTKETPRSTIKGVLKVSKQTDLKFSRENLMKVEESLKRAFIEFYQKLRLLKSYSFLNVLAFSKILKKYDKITSRDATKPYMKVVDSSYLGSSDEVMRLMERVEATFIKHFANANRAKAMNILRPKAKRERHRITFSTGFSAGCVFSLIVALVAIIRTRNLLEMEGQKEYMNTMFPLYSLFGFIVLHIIVYAANIYYWRRYRVNYSFIFGFKQGTELGYRQVLLVGFSIGVLALLCVLANLDMEADPKTKAYQARTEILPLILLAAMFIVLVLPFNYFYRSSRFFFLTCLFHCLAAPLYKVTLPDFFLGDQLTSQVQAIRSIEFYICYYGWGDFRHRKSTCKESDVYNTFFFIVAVIPYVSRLLQCLRRLFEEKNPEQGYNGLKYFLTIVAVCLRTAYSIQKGQVAWRVLAAVFSFIAAIFCTYWDFVHDWGLLNRTSKNRWLRDKLLVPQKKVYFIAMVLNVLLRFAWIQTVLDFNFSFMHRQTMVAIVASLEIIRRGIWNFFRLENEHLNNVGKYRAFKSVPLPFNYDEDDDKDN
Protein: Vacuolar protein sorting-associated protein 51 homolog (Another new gene 2 protein) (Protein fat-free homolog) (Q9UID3)
Organism: Homo sapiens (Human)
Function: Acts as component of the GARP complex that is involved in retrograde transport from early and late endosomes to the trans-Golgi network (TGN). The GARP complex is required for the maintenance of protein retrieval from endosomes to the TGN, acid hydrolase sorting, lysosome function, endosomal cholesterol traffic and autophagy. VPS51 participates in retrograde transport of acid hydrolase receptors, likely by promoting tethering and SNARE-dependent fusion of endosome-derived carriers to the TGN. Acts as component of the EARP complex that is involved in endocytic recycling. The EARP complex associates with Rab4-positive endosomes and promotes recycling of internalized transferrin receptor (TFRC) to the plasma membrane.
Subcellular location: Golgi apparatus, trans-Golgi network {ECO:0000269|PubMed:20685960}. Recycling endosome {ECO:0000269|PubMed:25799061}. Note=Localizes to the trans-Golgi network as part of the GARP complex, while it localizes to recycling endosomes as part of the EARP complex (PubMed:25799061). {ECO:0000269|PubMed:25799061}.
Interaction partners:
- Vacuolar protein sorting-associated protein 53 homolog
- Syndetin
- Vacuolar protein sorting-associated protein 52 homolog
- Vacuolar protein sorting-associated protein 54
- Syntaxin-6
- EARP and GARP complex-interacting protein 1
- Syntaxin-16
- Conserved oligomeric Golgi complex subunit 8
- Conserved oligomeric Golgi complex subunit 1
- Syntaxin-10
Sequence:
MAAAAAAGPSPGSGPGDSPEGPEGEAPERRRKAHGMLKLYYGLSEGEAAGRPAGPDPLDPTDLNGAHFDPEVYLDKLRRECPLAQLMDSETDMVRQIRALDSDMQTLVYENYNKFISATDTIRKMKNDFRKMEDEMDRLATNMAVITDFSARISATLQDRHERITKLAGVHALLRKLQFLFELPSRLTKCVELGAYGQAVRYQGRAQAVLQQYQHLPSFRAIQDDCQVITARLAQQLRQRFREGGSGAPEQAECVELLLALGEPAEELCEEFLAHARGRLEKELRNLEAELGPSPPAPDVLEFTDHGGSGFVGGLCQVAAAYQELFAAQGPAGAEKLAAFARQLGSRYFALVERRLAQEQGGGDNSLLVRALDRFHRRLRAPGALLAAAGLADAATEIVERVARERLGHHLQGLRAAFLGCLTDVRQALAAPRVAGKEGPGLAELLANVASSILSHIKASLAAVHLFTAKEVSFSNKPYFRGEFCSQGVREGLIVGFVHSMCQTAQSFCDSPGEKGGATPPALLLLLSRLCLDYETATISYILTLTDEQFLVQDQFPVTPVSTLCAEARETARRLLTHYVKVQGLVISQMLRKSVETRDWLSTLEPRNVRAVMKRVVEDTTAIDVQVGLLYEEGVRKAQSSDSSKRTFSVYSSSRQQGRYAPSYTPSAPMDTNLLSNIQKLFSERIDVFSPVEFNKVSVLTGIIKISLKTLLECVRLRTFGRFGLQQVQVDCHFLQLYLWRFVADEELVHLLLDEVVASAALRCPDPVPMEPSVVEVICERG
Protein: SRR1-like domain-containing protein (Q381Q5)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MWTVVQQRQQPSRRRREANAAKSAGGGKGVSSLVTTIPSRSTAAEVKHLRKAARFLRGLAFVRRDVISPLRHFLNAHSNGLTGIKLVALGIGPFTYEESRAGFLQMALFIVLQSECESFVRHLIRSKLSSVPSNNGDGLQPSTPTVRACFFDPVATEVHTKCCDKLGVVMEECNLYGAYIPGHPHALLIAYLPHSPWVLLRNLFVSNLTKISECPAGGEGGVNKVDSLVLRRTLVIGNDVKKGPCVSDTFLEKLGAYLHIGELHVRGRRKQCVESFVECVSDTCDDVGDVGEVTVFDGLTGISRHDIVQAFSETSVMQLNERSELLLLDELKRIRIPPLTCVGLDMV
Protein: RCC1 and BTB domain-containing protein 1 (Chronic lymphocytic leukemia deletion region gene 7 protein) (CLL deletion region gene 7 protein) (Regulator of chromosome condensation and BTB domain-containing protein 1) (Q8NDN9)
Organism: Homo sapiens (Human)
Function: May be involved in cell cycle regulation by chromatin remodeling.
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
- Cullin-3
Sequence:
MVDVGKWPIFTLLSPQEIASIRKACVFGTSASEALYVTDNDEVFVFGLNYSNCLGTGDNQSTLVPKKLEGLCGKKIKSLSYGSGPHVLLSTEDGVVYAWGHNGYSQLGNGTTNQGIAPVQVCTNLLIKQVVEVACGSHHSMALAADGEVFAWGYNNCGQVGSGSTANQPTPRKVTNCLHIKRVVGIACGQTSSMAVLDNGEVYGWGYNGNGQLGLGNNGNQLTPVRVAALHSVCVNQIVCGYAHTLALTDEGLLYAWGANTYGQLGTGNKNNLLSPAHIMVEKERVVEIAACHSAHTSAAKTQGGHVYMWGQCRGQSVILPHLTHFSCTDDVFACFATPAVSWRLLSVEHEDFLTVAESLKKEFDSPETADLKFRIDGKYIHVHKAVLKIRCEHFRSMFQSYWNEDMKEVIEIDQFSYPVYRAFLQYLYTDTVDLPPEDAIGLLDLATSYCENRLKKLCQHIIKRGITVENAFSLFSAAVRYDAEDLEEFCFKFCINHLTEVTQTAAFWQMDGPLLKEFIAKASKCGAFKN
Protein: NAD kinase (EC 2.7.1.23) (ATP-dependent NAD kinase) (Poly(P)-dependent NAD kinase) (PPNK) (O58801)
Organism: Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3)
Function: Involved in the regulation of the intracellular balance of NAD and NADP, and is a key enzyme in the biosynthesis of NADP. Catalyzes specifically the phosphorylation on 2'-hydroxyl of the adenosine moiety of NAD to yield NADP. It can use ATP and other nucleoside triphosphates (GTP,UTP) as well as inorganic polyphosphate (poly(P)) as a source of phosphorus. NAD is the preferred substrate for the kinase, but NADH can also be used as phosphoryl acceptor.
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00361}.
Interaction partners:
- NAD-dependent protein deacylase
- NH
- fructose-bisphosphatase
- Nicotinamide-nucleotide adenylyltransferase
- L-aspartate oxidase
- nicotinate phosphoribosyltransferase
Sequence:
MKFGIVARRDKEEALKLAYRVYDFLKVHGYEVVVDKETYEHFPHFKEGDVIPLDEFDVDFIVAIGGDGTILRIEHMTKKDIPILSINMGTLGFLTEVEPSDTFFALNRLIEGEYYIDERIKVRTYIDGENRVPDALNEVAILTGIPGKIIHMKYYVDGGLADEVRADGLVVSTPTGSTGYAMSAGGPFIDPRLDVILIAPLLPLPKTSVPMVIPGSSRIDIRMLTDREIILAIDGQYYEHLPPNVEITVVKSPRKTKFIRFTREIYPKYTIRIKERH
Protein: Outer membrane protein 40 (Omp40) (PG33) (Q9S3R8)
Organism: Porphyromonas gingivalis (strain ATCC BAA-308 / W83)
Function: May have porin activity and function in peptidoglycan binding.
Subcellular location: Cell outer membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
- Lipoprotein, putative
- Outer membrane protein 41
- 60 kDa protein
- Lipoprotein, putative
- DUF3078 domain-containing protein
- Outer membrane protein beta-barrel domain-containing protein
Sequence:
MKAKSLLLALAGLACTFSATAQEATTQNKAGMHTAFQRDKASDHWFIDIAGGAGMALSGWNNDVDFVDRLSIVPTFGIGKWHEPYFGTRLQFTGFDIYGFPQGSKERNHNYFGNAHLDFMFDLTNYFGVYRPNRVFHIIPWAGIGFGYKFHSENANGEKVGSKDDMTGTVNVGLMLKFRLSRVVDFNIEGQAFAGKMNFIGTKRGKADFPVMATAGLTFNLGKTEWTEIVPMDYALVNDLNNQINSLRGQVEELSRRPVSCPECPEPTQPTVTRVVVDNVVYFRINSAKIDRNQEINVYNTAEYAKTNNAPIKVVGYADEKTGTAAYNMKLSERRAKAVAKMLEKYGVSADRITIEWKGSSEQIYEENAWNRIVVMTAAE
Protein: Rifin (O96290)
Organism: Plasmodium falciparum (isolate 3D7)
Interaction partners:
Sequence:
MKLHYTKILLFFFPLNILLTSYHAHNKNKPYITSRHRQTSTSRVLSESDPYMLNYDNDDDMKSVKENFDRQTSQRFEEYEGRMKDKRRKCKEQCDKDIQEIILKDKMEKSLAEKVEIGCLRCGCGLGGVAASVGIFGTVAVKELAKTATAAAVAAAQEAVKDAAMAATIKAVGAAAGKEFVIAGLKQMGVSTLDGKELGTYITATNYTNVKNIAHAINTQYEPSSCLITVPVDSKPICTWVRAKEGAARVIQGKQFSTQETIKVAVTSIVSDAENVAAAAEQQATKDAIKASTLAVDSKYAICQNAIIASVVALLIIVLIMIIIYLVLRYRRKKKMKKKAEYTKLLNQ
Protein: Thymine dioxygenase JBP1 (EC 1.14.11.6) (J-binding protein 1) (Thymidine hydroxylase JBP1) (P86938)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Function: Dioxygenase that catalyzes the first step of DNA base J (beta-d-glucosyl-HOMedU) biosynthesis by converting thymine to 5-hydroxymethyluracil (HOMedU). DNA base J is a hypermodified thymidine residue found in the genome of kinetoplastid parasites, which is localized primarily to repetitive DNA, namely the telomeres, and is implicated in the regulation of antigenic variation. Also specifically binds to base J-containing DNA (J-DNA). Involved in propagation and maintenance of DNA base J synthesis initiated by JBP2 by specifically binding already synthesized DNA base J and propagating J synthesis. Thymine dioxygenase activity and J-DNA-binding are independent functions.
Subcellular location: Nucleus {ECO:0000269|PubMed:15694344, ECO:0000269|PubMed:17389644}.
Interaction partners:
- thymidine kinase
Sequence:
MRRQVKKVLREKADDSMKPGWDVYQPSNDVVYAFNHYMQGSQIDAEAREKAEKAFQEAVKKHPFHNNADHTVDFHGTTVFRNAKGKVCGVLIPKALPSFATSMAADVLECAVARTSLRSALFGGVSPNSGIAGYFDYRGTPVELKCRKTSFTYEHTKEWRSVFPMIDYTSAIYKAALPDHWKAQDAAVPDVVRIHGSPFSTLTVNERFRTASHTDNGDFDNGYGVLAVLKGEYSGLSLALDDYGVCFNMQPTDVLLFDTHLFHSNTELEAKEANATWNRLSCVFYYRAALGEQPCVEEYRRRLKKAKEEKSTSLSFNHIEQKDNGENTNKPAPVYPVSLTPFSCAASAWALRGCAAAMLTRLHGLVRENASLMTELFGEPVEVADGLPRRAPEEIIPVHKHTNVQMHYLGGFSEKGDILNEAMNKRHYLDKENLQKMFGEEFVNIWTQSRTHWLQLVKKEWEHQKETNPTRTRFSWNNTSAMNFAFFDLCDVAKQLMCGAFGDREVNKKEEQSFWGMFAAHLDNACINEIGMLQGSMGMHKLNVKLKDYNFGGTRYLKDMPPEEQERRRRRRLEIEQARRRAPICDSESGDWLRNEAFDYQTEDVAVNYEREQWITPENNAKRFGFPERGVYGAEGAATGTISVLIVLPKPTNHRQKTCELPTSREADRIMKNPAAQRLLCAKPCNIGLSTSSNKSRTVLCGNIRIDKVFDGGSVGGKMYDFVIMRHLLAATTGEREPLECLVRWTSLARYCTFVVEVDLLDRHHYILKSEIGEEYSAVSEICFSALYSATYARDKVNLRTTPCLLSFIDKSGNMLESRFKFNGSPLNTVAFVVRRREK
Protein: Eukaryotic translation initiation factor 5A-2 (eIF-5A-2) (Initiation factor five protein 2) (Q20751)
Organism: Caenorhabditis elegans
Function: mRNA-binding protein involved in translation elongation. Has an important function at the level of mRNA turnover, probably acting downstream of decapping. Critical for the efficient synthesis of peptide bonds between consecutive proline residues. Can resolve ribosomal stalling caused by consecutive prolines during translation (By similarity). Involved in actin dynamics and cell cycle progression, mRNA decay and probably in a pathway involved in stress response and maintenance of cell wall integrity. Functions as a regulator of apoptosis (By similarity). Acts in somatic tissues and its function in the soma is essential for normal growth and reproduction.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:P23301}.
Interaction partners:
- Ubiquitin-like domain-containing protein
- Small ribosomal subunit protein uS19
- Small ribosomal subunit protein uS17
- Small ribosomal subunit protein uS13
- Large ribosomal subunit protein uL14
- Small ribosomal subunit protein uS3
- Deoxyhypusine synthase
- Large ribosomal subunit protein uL18
- Large ribosomal subunit protein uL29
- Small ribosomal subunit protein RACK1
Sequence:
MSDDHHDDEHFHTGDSGAAATFPKQCSALRKNEHVMIKGRPCKIVEMSTSKTGKHGHAKVHMVAIDIFTSKKLEDICPSTHNMDVPVVKRREYLLMAIDDGYCSLMDPESCEQKDDLKLPDTELGQQIRDAYEKDEGSVLVQVVSAIGEEAILGWKVSTKE
Protein: Bromo domain-containing protein (Q8C473)
Organism: Mus musculus (Mouse)
Interaction partners:
Sequence:
MAWPFLEPVDPNDAPDYYGVIKEPMDLATMEERIQKRYYEKLTEFVADMTKIFDNCRYYNPRDTPFYQCAEVLESFFVQKLKGFKASRSHNNKLQSTAP
Protein: Sporulation-specific with a leucine zipper motif protein 1 (P40167)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Component of the MIS complex, a complex that mediates N6-methyladenosine (m6A) methylation on some mRNAs during meiosis and is required for sporulation. In the complex, mediates the entry of the MIS complex in nucleolus, where methylation takes place.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:24269006}. Nucleus, nucleolus {ECO:0000269|PubMed:24269006}. Note=Mediates localization of the MIS complex to the nucleolus during the period of m6A mRNA accumulation. {ECO:0000269|PubMed:24269006}.
Interaction partners:
- Protein MUM2
- N
Sequence:
MMNKVDQIIGYKKYEVKLPKDRQVKKNKSKGGNVDQIDTKREKDKMRAFGEERKKFLDKMAKNKKKNTSRKDREKPKEVEKENYKREDKRLKEQKKLSLAKEFRFKEPNSEAINQNTAAENGKPKPQTGLDFDIDHQTVSKIMIDQAIQTSSPLNVQLTELFNDNVLDVSKDSQFVLQDMEFTSWERRWSNCSTTSNATTVSSVPDPKYNINYNDITSFNSVALITEDLNISASSNGLHERGKKLLQQEMEYSNKVKNVTIGLERLCMDEKPVPDAGITMQQASRWSEFPTCCDQAAI
Protein: Ciliogenesis-associated TTC17-interacting protein (Q7Z7H3)
Organism: Homo sapiens (Human)
Function: Plays a role in primary ciliogenesis by modulating actin polymerization.
Subcellular location: Nucleus {ECO:0000269|PubMed:24475127, ECO:0000269|PubMed:32503832}. Cytoplasm {ECO:0000269|PubMed:24475127, ECO:0000269|PubMed:32503832}. Cell membrane {ECO:0000269|PubMed:24475127}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:24475127}. Note=Colocalized with TTC17 at F-actin rich zones and at dynamic plasma membrane protrusions.
Interaction partners:
Sequence:
MSSKVYSTGSRAKDHQPSGPECLPLPEANAEAIDFLSSLHKEELQMLFFSETLAMVSDTGEPQGELTIEVQRGKYQEKLGMLTYCLFVHASSRGFLDKMLCGNSLLGYLSEKLELMEQHSQDFIKFLILPMERKMSLLKQDDQLAVTRSIKEGEEVKTGVTSFPWSSIKGFISEAANLVLLRVMAWRRMVPSNARFLTLDTEGKLCYLTYQNLGFQTIQVDHQQAEVFIVEQTVHAEEGIPMSCQYYLLSDGHLAKRIQVGSPGCCIITKMPILREEDEIEPRPVFEKKPLVWEEDMELYSKFLDRKEELRLGHASYLRQHPEAHALISDFLLFLLLRQPEDVVTFAAEFFGPFDPWRPSSPALGSSHRPNPFRSLEPEGDARSGAA
Protein: Protein CYCLOPS (MtCYCLOPS) (DMI3-interacting protein IPD3) (Interacting protein of DMI3) (MtIPD3) (MtSYM1) (A7TUE1)
Organism: Medicago truncatula (Barrel medic) (Medicago tribuloides)
Function: Involved symbiotic signaling. Required for root infection by symbiotic rhizobia, infection thread (IT) formation, and nodule development. Required for proper induction of early nodulin gene expression. Probably not involved in nodule organogenesis. Involved in arbuscular mycorrhizal (AM) symbiosis. Required for fungal infection of the outer cortical cell layers, and for arbuscule development during the AM symbiosis. Acts downstream of CCAMK. Required for symbiosome formation (i.e. the release of the bacteria from the ITs) and subsequent symbiosome development. Required for the expression of the nodule-specific RPG gene, which controls proper IT growth and is essential for symbiosome formation. Acts upstream of ERN1, a transcriptional regulator required for nodulation.
Subcellular location: Nucleus {ECO:0000269|PubMed:17722695, ECO:0000269|PubMed:21787150}.
Interaction partners:
- Pre-mRNA-splicing factor ISY1
- Putative transcription factor C3H family
- Calcium and calcium/calmodulin-dependent serine/threonine-protein kinase DMI-3
- P-loop nucleoside triphosphate hydrolase superfamily protein
- Cwf15/cwc15 cell cycle control protein
- Putative transcription factor C2H2 family
- SNU114 homolog
- Pre-mRNA-splicing factor SYF2
- Small nuclear ribonucleoprotein E
- Protein NODULATION SIGNALING PATHWAY 2
Sequence:
MEGRGFSGLYKNSSEELFLKTVMESPIGMPVPTMEMLGFKTVSQSFRTDSEELFKRWLTNDQEGYNSSSMGLNSRLSKRISTEIANMSNQQHIGVASEGRNNDKSCLQNNFLANDVSSDFNFPIRDPVDRELQSSNLFLAKAWFITDQRMTRSRSSELRRRYTEMQNSQAPQGLDSMFMVPEHDTNTIKEELANFNGFDYLSMCELPSQKGTFMSPSNSSSSTFNTHQLVDVDKVSSCVSMLKGTLQRKKLECQVEKEAAEDGLNEIFCIREPLFQSAFNEEESWNQQKLVNVQGDFTDQVNDPGVMQTLEGTTNFVLDGFANQTNQIQGRTASGEPSQSESSAAAPVISSGLDACEGPSNSNQTLGDSSWKQVGESTQNKVRGVREQIMDNLKDDRKRKSLERYGSVTSAVSDGKMDNTKKRRVERSRKMAEAKERNLTPTIPSDMQAILKRCENLEKEVRSLKLNLSFMNRKDSEQTKQIEDLQKQNEDLADEKERLLEEIERILSETGKI