wanglab/gogpt-training-data huggingface dataset:
Protein: Probable D-serine/alanine/glycine transporter protein CycA (O33203)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004651}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}.
Interaction partners:
- D-alanine--D-alanine ligase
- Alanine racemase
- Uncharacterized PPE family protein PPE22
Sequence:
MPDDIAAADPTDTQPHLRRDLANRHIQLIAIGGAIGTGLFMGSGRTISLAGPAVMVVYGIIGFFVFFVLRAMGELLLSNLNYKSFVDFAADLRGPAAGFFVGWSYWFAWVVTGIADLVAITGYARFWWPGLPIWVPALVTVALILAVNLFSVRHFGELEFWFALIKVAAIVCLIAVGAILVATNFVSPHGVHATIENLWNDNGFFPTGFLGVVSGFQIAFFAYIGVELVGTAAAETADPRRTLPRAINAVPLRVAVFYIGALLAILAVVPWRQFASGESPFVTMFSLAGLAAAASVVNFVVVTAAASSANSGFFSTGRMLFGLADEGHAPAAFHQLNRGGVPAPALLLTAPLLLTSIPLLYAGRSVIGAFTLVTTVSSLLFMFVWAMIIISYLVYRRRHPQRHTDSVYKMPGGVVMCWAVLVFFAFVIWTLTTETETATALAWFPLWFVLLAVGWLVTQRRQSRRSFGFHCQVVGVRQQLGRGMARLAMKIHARPKLRSAVVVEPVSAGEPGARRSAKSVRKLASDDSQSAHCPVAVVGLADGGRDPQYHHDGPDR
Protein: Seventh homolog of septin 1 (Septation protein 7) (Q07657)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Septins are GTPases involved in cytokinesis that assemble early in the cell cycle as a patch at the incipient bud site and form a ring approximate 15 min before bud emergence, which transforms into an hour-glass shaped collar of cortical filaments that spans both sides of the mother-bud neck. This collar persists until just before cytokinesis, when it splits into two rings that occupy opposite sides of the neck. The septins at the bud neck serve as a structural scaffold that recruits different components involved in diverse processes at specific stages during the cell cycle. Many proteins bind asymmetrically to the septin collar. The septin assembly is regulated by protein kinases GIN4 and/or CLA4. May act by recruiting MYO1 and HOF1, a protein involved in septation, to the site of cleavage. Septins are also involved in cell morphogenesis, bud site selection, chitin deposition, cell cycle regulation, cell compartmentalization and spore wall formation.
Subcellular location: Membrane {ECO:0000305}; Peripheral membrane protein {ECO:0000305}. Bud neck {ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:25971666, ECO:0000269|PubMed:9790978}. Note=Present at the bud neck during cell division. Probably interacts with phosphoinosides such as phosphatidylinositol 4-phosphate or phosphatidylinositol 5-phosphate. {ECO:0000250|UniProtKB:P32458}.
Interaction partners:
- Cell division control protein 3
- Cell division control protein 11
- Cell division control protein 12
- Cell division control protein 10
- Serine/threonine-protein kinase GIN4
- Uncharacterized protein YMR124W
- Bud site selection protein 4
- Probable serine/threonine-protein kinase KCC4
- Bud neck protein 5
- Vesicle-associated membrane protein-associated protein SCS2
Sequence:
MSTASTPPINLFRRKKEHKRGITYTMLLCGPAGTGKTAFANNLLETKIFPHKYQYGKSNASISSNPEVKVIAPTKVVSFNSKNGIPSYVSEFDPMRANLEPGITITSTSLELGGNKDQGKPEMNEDDTVFFNLIMTHGIGENLDDSLCSEEVMSYLEQQFDIVLAEETRIKRNPRFEDTRVHVALYFIEPTGHGLREVDVELMKSISKYTNVLPIITRADSFTKEELTQFRKNIMFDVERYNVPIYKFEVDPEDDDLESMEENQALASLQPFAIITSDTRDSEGRYVREYPWGIISIDDDKISDLKVLKNVLFGSHLQEFKDTTQNLLYENYRSEKLSSVANAEEIGPNSTKRQSNAPSLSNFASLISTGQFNSSQTLANNLRADTPRNQVSGNFKENEYEDNGEHDSAENEQEMSPVRQLGREIKQENENLIRSIKTESSPKFLNSPDLPERTKLRNISETVPYVLRHERILARQQKLEELEAQSAKELQKRIQELERKAHELKLREKLINQNKLNGSSSSINSLQQSTRSQIKKNDTYTDLASIASGRD
Protein: Cecropin-P3 (Q5H7N5)
Organism: Ascaris suum (Pig roundworm) (Ascaris lumbricoides)
Function: Has antibacterial activity against several Gram-positive and Gram-negative bacteria. Is weakly active against yeasts. Acts by a nonpore mechanism.
Subcellular location: Secreted {ECO:0000250}.
Interaction partners:
Sequence:
MFLIYLLVQTAESSWLSKTAKKLENSAKKRISEGIAIAIKGGSRRRRSVGEEDAIPSHIEVNKFFLRKPAKEHI
Protein: Btz domain-containing protein (Q8IL16)
Organism: Plasmodium falciparum (isolate 3D7)
Interaction partners:
Sequence:
MATKIRYSVHTTNKFSVFDSDDNSEEEIENKDLNESPKNEPDIVYEEKTIDNSNEVNKIIEVHDNIPSPIIKDYYNKRVNVHYNDRYKYPVTSINDVNENTYRSYRDNYHIRGNNLRNKFTRKRGGGYSNASTNILGGSNFYRGSRNYDYKMNMDRRNYNPSYNYNKFDFREKMYNDYNDNTSKYDSMKRDNLIDFKNKNYEDSSKAGRKYKSVTIDYDLYRRQQEKKLNSNKSAESNDKKKKKNEENNTEKVNKVTTNVPKRNDTLEEDLKSDHPKRKAINVYQYILEEGGRVDRLPGFRRSYRSFKKVDEGNWNNKYEKSKMQIDEKIFKKRDPPNINDTRAFPSLTSK
Protein: Adenylyl-sulfate kinase (EC 2.7.1.25) (ATP adenosine-5'-phosphosulfate 3'-phosphotransferase) (Adenosine-5'-phosphosulfate kinase) (APS kinase) (Q12657)
Organism: Penicillium chrysogenum (Penicillium notatum)
Function: Catalyzes the synthesis of activated sulfate.
Interaction partners:
Sequence:
MSTNITFHASALTRSERTELRNQRGLTIWLTGLSASGKSTLAVELEHQLVRDRRVHAYRLDGDNIRFGLNKDLGFSEADRNENIRRIAEVAKLFADSNSIAITSFISPYRKDRDTARQLHEVATPGEETGLPFVEVYVDVPVEVAEQRDPKGLYKKAREGVIKEFTGISAPYEAPANPEVHVKNYELPVQDAVKQIIDYLDTKGYLPAKKE
Protein: Uncharacterized protein (Q57YL1)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MEKLQLERNELLLYVLQNPPPYVTIVLPEGVRSAAELDLTHTQSPLAVYAAATASNPIEVRVSAPPTLLGDSAEKKKKKCGLGTTGSGINSPSKGKRPRFRWKDLSNYFMSHLRGDSQTMCSPEKTPPATPSRLDAAMSNPERKHSLHAYVTEPSKSEGGHVIQLSKCTSARREPLPLEGKQGYSLAEYVTPFLSQTQVSVQNPLERPVLPVIELCPVLNSAMLPEFDEDERQLLFYEHVVLAASILLPARGAWFDSKVGSRYRKAMGISNEQHVRVLSNISPAIKEGQDTLNMPINLQTIERLVETSSDGDFTQRMNKILCMCSQYPEDPQQRRYPLCLRAFIYAGALSPLYGSNSSADTVLFEEEVRDVITAVRNRLEIPKSIEPFCRVHARLLSIDDDDDVERRTAFLMGVASALHELSKSTGSLSREPLTPEVKYMLYLLQETFEMSTAPISLLGVVRSDYAFLCVFDLFLESCLSLPTEFLSVYVQVNGRDLLPPMRPVKDFLLSLLLVFITCGVLRSFCNLKLEINPRNAPRDLLASVRHLGRSTREYCDLLSRSVQHAPALMLPGVTTVASHLLATHWADTLSCERLPSDFSEGLRTMLSLLLTYSSPGMENDEDVSHTILACAGNLSWVVPVMERHNCAAKGRVLARLQAAKAVAKAGVPVQRLMLNRIEELMEELESFISPPPLVPAAANVVRQRLSLVVDTLSDIFADMKAPYTRLSSRSGSLATKAGGYFEEYKAQLELQEKVFSLSLSTEDAVARLKCLSVIDERLRKIAIQSQRDYQLVRQVTGAPAAGFEDLLGTLTNPLSESINMFRDVVAATIVRVELAGLLFDKFMKTDMRLYKVLKSDKAAVPDRRHIQLEFPEVTMVSVLKRLESVIVSVSAVINDPFVDAEVWSMTMLHFVSALYYVYFEESDCRFFCPEDWKCILQDLRIVDMFMKESFPYPPRGEPARGVTERAVELLRWLQQIVLHCFPYSSTALVNGADGAPPFAQLPPSSDTTPWSKHVVRRVLRRRKDKVAKSASGLGGFFRWDTSQ
Protein: Homeobox A9 (A0A669K9T0)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123, ECO:0000256|PROSITE-ProRule:PRU00108, ECO:0000256|RuleBase:RU000682}.
Interaction partners:
Sequence:
MATTGALGNYYVDSFLLGADAADELSVGRYAPGTLGQPPRQAATLAEHPDFSPCSFQSKATVFGASWNPVHAAGANAVPAAVYHHHHHHPYVHPQAPVAAAAPDGRYMRSWLEPTPVDREKQPSEGAFSENNAENESGGDKPPIDPNNPAANWLHARSTRKKRCPYTKHQTLELEKEFLFNMYLTRDRRYEVARLLNLTERQVKIWFQNRRMKMKKINKDRAKDE
Protein: Transketolase (TK) (EC 2.2.1.1) (P29401)
Organism: Homo sapiens (Human)
Function: Catalyzes the transfer of a two-carbon ketol group from a ketose donor to an aldose acceptor, via a covalent intermediate with the cofactor thiamine pyrophosphate.
Interaction partners:
- Transaldolase
- Glucose-6-phosphate isomerase
- Ribose-5-phosphate isomerase
- Ribulose-phosphate 3-epimerase-like protein 1
- Ribulose-phosphate 3-epimerase
- Fructose-1,6-bisphosphatase 1
- Triosephosphate isomerase
- Glyceraldehyde-3-phosphate dehydrogenase
- 6-phosphogluconate dehydrogenase, decarboxylating
- Fructose-1,6-bisphosphatase isozyme 2
Sequence:
MESYHKPDQQKLQALKDTANRLRISSIQATTAAGSGHPTSCCSAAEIMAVLFFHTMRYKSQDPRNPHNDRFVLSKGHAAPILYAVWAEAGFLAEAELLNLRKISSDLDGHPVPKQAFTDVATGSLGQGLGAACGMAYTGKYFDKASYRVYCLLGDGELSEGSVWEAMAFASIYKLDNLVAILDINRLGQSDPAPLQHQMDIYQKRCEAFGWHAIIVDGHSVEELCKAFGQAKHQPTAIIAKTFKGRGITGVEDKESWHGKPLPKNMAEQIIQEIYSQIQSKKKILATPPQEDAPSVDIANIRMPSLPSYKVGDKIATRKAYGQALAKLGHASDRIIALDGDTKNSTFSEIFKKEHPDRFIECYIAEQNMVSIAVGCATRNRTVPFCSTFAAFFTRAFDQIRMAAISESNINLCGSHCGVSIGEDGPSQMALEDLAMFRSVPTSTVFYPSDGVATEKAVELAANTKGICFIRTSRPENAIIYNNNEDFQVGQAKVVLKSKDDQVTVIGAGVTLHEALAAAELLKKEKINIRVLDPFTIKPLDRKLILDSARATKGRILTVEDHYYEGGIGEAVSSAVVGEPGITVTHLAVNRVPRSGKPAELLKMFGIDRDAIAQAVRGLITKA
Protein: Synaptotagmin-10 (Synaptotagmin X) (SytX) (Q9R0N4)
Organism: Mus musculus (Mouse)
Function: Ca(2+) sensor specifically required for the Ca(2+)-dependent exocytosis of secretory vesicles containing IGF1 in neurons of the olfactory bulb. Exocytosis of IGF1 is required for sensory perception of smell. Not involved in Ca(2+)-dependent synaptic vesicle exocytosis. Acts through Ca(2+) and phospholipid binding to the C2 domain: Ca(2+) induces binding of the C2-domains to phospholipid membranes and to assembled SNARE-complexes; both actions contribute to triggering exocytosis (By similarity).
Subcellular location: Cytoplasmic vesicle, secretory vesicle membrane {ECO:0000269|PubMed:21496647, ECO:0000269|PubMed:23345244}; Single-pass membrane protein {ECO:0000255}. Note=Localizes to neuronal vesicles containing IGF1 that are not enriched at synapses (PubMed:21496647, PubMed:23345244). Does not colocalize with synaptic vesicles or with the Golgi apparatus (PubMed:21496647, PubMed:23345244). {ECO:0000269|PubMed:21496647, ECO:0000269|PubMed:23345244}.
Interaction partners:
Sequence:
MSFRKEDGVSSLCQKALHIITELCFAGQVEWDKCSGIFPADRSGQGGGGTDISVSLLAVVVSFCGLALLVVSLFVFWKLCWPCWKSKLVAPNLSVLPQSISSAPTEVFETEEKKEVEENEKPAPKAIEPAIKISHTSPDIPAEVQTALKEHLIKHARVQRQTTEPTSSSRHNSFRRHLPRQMNVSSVDFSVGTEPILQRGETRTSIGRIKPELYKQKSVDSEGNRKDDVKTCGKLNFALQYDYENELLVVKIIKALDLPAKDFTGTSDPYVKIYLLPDRKKKFQTRVHRKTLNPLFDELFQFPVVYDQLSNRKLHFSIYDFDRFSRHDMIGEVILDNLFEVSDLSREATVWKDIHCATTESIDLGEIMFSLCYLPTAGRMTLTVIKCRNLKAMDITGSSDPYVKVSLMCEGRRLKKRKTTTKKNTLNPVYNEAIIFDIPPENVDQVSLCIAVMDYDRVGHNEVIGVCRTGLDAEGLGRDHWNEMLAYHRKPITHWHPLLELPGRATSFDSQGSCSSPRPPSTP
Protein: UTP--glucose-1-phosphate uridylyltransferase (EC 2.7.7.9) (Q8WQE5)
Organism: Caenorhabditis elegans
Interaction partners:
Sequence:
MNVSFSTSSLSVSNSRTRLISFRETEHGDQKSSEEWKTSTKLEALGSMEGELAHLLSTCKPETLNHNKTELSGFRNLFARFLRAKPTVDWSKIEPLPEGAIRPYKSLGTSMGCKGPKSVISVRNDLTFLDLTMQQIQTLNKTYGVDVPLVLMNSFNTNEDTQKVLKKYANVKVSVHTFSQSQYPRINRETLLPIVKSLEADDNECWYPPGHGNFYEAFHNSGLLDKFLADGKEYCFLSNIDNMGATVDLSILNFVLNPSPDQTAPEFLMEVTDKTRADVKGGTLIQYEGRLMLLEIAQVPKDYVDEFKSISKFRIFNTNNLWAKLDAMRKIVVENKLEMEVIVNPKHLDRGLDVIQLETAAGAAIKSFSGAVGVNVPRSRFLPVKKTSDLLLLMSNLYDIDNGSLTLSHQRSFPTTPLVKLGSSFDKVKDYLGRFNGIPDLLELDHLTVSGDVWFGKDVSLKGTVIIIANHGDRIDIPPGSILENKIVSGNLRILEH
Protein: Vertebrate ancient long opsin (Vertebrate ancient opsin) (D0E2W5)
Organism: Gallus gallus (Chicken)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141, ECO:0000256|RuleBase:RU004951}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141, ECO:0000256|RuleBase:RU004951}.
Interaction partners:
- Tyrosinase
Sequence:
MDVFRALGNESLLSNSSGPARWDPFHHPLDSIQPWHFRLVAAVMFVVTSLSLAENLAVILVTFKFKQLRQPVNYVIVNLSVADFLVSLTGGTISFLANLKGYFYMGHWACVLEGFAVTFFGIVALWSLALLAFERYIVICRPVGNMRLRGKHAAQGIAFVWTFSFIWTIPPTMGWSSYTTSKIGTTCEPNWYSGAYNDRSYIIAFFTTCFIVPLLVILVSYGKLLQKLRKVSNTQGRLRTARKPERQVTRMVVVMIIAFLICWMPYAVFSILATAYPSIELDPHLAAIPAFFSKTATVYNPIIYVFMNKQFRMCLIQMFKCSAIETAESNMNPTSERATLTQDKRDSQLSVMAVRSTIS
Protein: LD28079p (Q95RI6)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MIRQRLPAKRYPNFTMQRIHFALPQTIVPLSTESLYNLQLKLIEGINNDVVVSAVLSGSHIFIQHPLHPSHPSLPLLQKQLYDSYSTMEAPLLPSLELSAVCVIPINDVWYRVQIVDTDPEDEERCVIKFLDFGGYMNVGFNTLRQIRTDFMNVPFQSTECILSNIEPIGGTWSIEAAEILNKLTKGIVLQAQVAGYNSHNLPEIFLFASLGPNNVIFINKELVGRKLAKWVEMSD
Protein: Dihydrolipoamide acetyltransferase component of pyruvate dehydrogenase complex (EC 2.3.1.-) (Q383B2)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- 2-oxoglutarate dehydrogenase subunit, putative
- oxoglutarate dehydrogenase
- Dihydrolipoamide dehydrogenase, point mutation
- Dihydrolipoamide dehydrogenase, putative
- Dihydrolipoamide dehydrogenase, putative
- Dihydrolipoyl dehydrogenase
- Succinate--CoA ligase subunit beta, mitochondrial
- Succinate--CoA ligase subunit alpha, mitochondrial
- Pyruvate dehydrogenase E1 component subunit beta
- 3-methyl-2-oxobutanoate dehydrogenase
Sequence:
MLRRLATHGLQATCLTSEKLAYRYCLSICVPTIAESISSGKVVGWTKKVGDAVAEDEIICQIESDKLNVDVRAPAAGVITKINFEEGTVVDVGAELSTMKEGEAPAAKAETADKPKQNAPAAAAPPKASPTEAAPKPAPAAAPVTSRGADPRVRSVRISSMRQRIADRLKASQNTCAMLTTFNEIDMTPLIELRNRYKDDFFKKNGVKLGFMSPFVKACAIALQDVPIVNASFGTDCIEYHDYVDISVAVSTPKGLVVPVLRDVQNSNFAQIEKQIADFGERARSNKLTMAEMTGGTFTISNGGVFGSWMGTPIVNPPQSAILGMHATKKKPWVVGNSVVPRDIMAVALTYDHRLIDGSDAVTFLVKVKNLIEDPARIVLDLA
Protein: Forkhead box protein D1 (Forkhead-related protein FKHL8) (Forkhead-related transcription factor 4) (FREAC-4) (Q16676)
Organism: Homo sapiens (Human)
Function: Transcription factor involved in regulation of gene expression in a variety of processes, including formation of positional identity in the developing retina, regionalization of the optic chiasm, morphogenesis of the kidney, and neuralization of ectodermal cells (By similarity). Involved in transcriptional activation of PGF and C3 genes.
Subcellular location: Nucleus.
Interaction partners:
- Wilms tumor protein
- Homeobox protein SIX2
Sequence:
MTLSTEMSDASGLAEETDIDVVGEGEDEEDEEEEDDDEGGGGGPRLAVPAQRRRRRRSYAGEDELEDLEEEEDDDDILLAPPAGGSPAPPGPAPAAGAGAGGGGGGGGAGGGGSAGSGAKNPLVKPPYSYIALITMAILQSPKKRLTLSEICEFISGRFPYYREKFPAWQNSIRHNLSLNDCFVKIPREPGNPGKGNYWTLDPESADMFDNGSFLRRRKRFKRQPLLPPNAAAAESLLLRGAGAAGGAGDPAAAAALFPPAPPPPPHAYGYGPYGCGYGLQLPPYAPPSALFAAAAAAAAAAAFHPHSPPPPPPPHGAAAELARTAFGYRPHPLGAALPGPLPASAAKAGGPGASALARSPFSIESIIGGSLGPAAAAAAAAQAAAAAQASPSPSPVAAPPAPGSSGGGCAAQAAVGPAAALTRSLVAAAAAAASSVSSSAALGTLHQGTALSSVENFTARISNC
Protein: Fumarate hydratase 2 (AtFUM2) (Fumarase 2) (EC 4.2.1.2) (Q9FI53)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Cytosolic fumarate hydratase that catalyzes the reversible stereospecific interconversion of fumarate to L-malate. Catalyzes the dehydration of L-malate to fumarate in the cytosol: required for the massive fumarate accumulation during the day in plants grown under high nitrogen. Also required for acclimation of photosynthesis to cold: acts by mediating accumulation of fumarate at low temperature, leading to reduce accumulation of phosphorylated sugars.
Subcellular location: Cytoplasm, cytosol {ECO:0000269|PubMed:20202172}.
Interaction partners:
- Succinate dehydrogenase iron-sulfur subunit 2, mitochondrial
- Succinate dehydrogenase flavoprotein subunit 1, mitochondrial
- Succinate dehydrogenase flavoprotein subunit 2, mitochondrial
- Succinate dehydrogenase iron-sulfur subunit 1, mitochondrial
- Malate dehydrogenase 2, mitochondrial
- Succinate dehydrogenase iron-sulfur subunit 3, mitochondrial
- Malate dehydrogenase 1, cytoplasmic
- Malate dehydrogenase 1, mitochondrial
- Malate dehydrogenase 2, peroxisomal
- Malate dehydrogenase, chloroplastic
Sequence:
MAALTMQFEGEKKNVSEVADVTLKQEDEQQERRSYSTPFREERDTFGPIQVPSDKLWGAQTQRSLQNFEIGGDRERMPEPIVRAFGVLKKCAAKVNMEYGLDPMIGEAIMEAAQEVAEGKLNDHFPLVVWQTGSGTQSNMNANEVIANRAAEILGHKRGEKIVHPNDHVNRSQSSNDTFPTVMHIAAATEITSRLIPSLKNLHSSLESKSFEFKDIVKIGRTHTQDATPLTLGQEFGGYATQVEYGLNRVACTLPRIYQLAQGGTAVGTGLNTKKGFDVKIAAAVAEETNLPFVTAENKFEALAAHDACVETSGSLNTIATSLMKIANDIRFLGSGPRCGLGELSLPENEPGSSIMPGKVNPTQCEALTMVCAQVMGNHVAVTIGGSNGHFELNVFKPVIASALLHSIRLIADASASFEKNCVRGIEANRERISKLLHESLMLVTSLNPKIGYDNAAAVAKRAHKEGCTLKHAAMKLGVLTSEEFDTLVVPEKMIGPSD
Protein: Protein AATF (Apoptosis-antagonizing transcription factor) (Rb-binding protein Che-1) (Q9NY61)
Organism: Homo sapiens (Human)
Function: May function as a general inhibitor of the histone deacetylase HDAC1. Binding to the pocket region of RB1 may displace HDAC1 from RB1/E2F complexes, leading to activation of E2F target genes and cell cycle progression. Conversely, displacement of HDAC1 from SP1 bound to the CDKN1A promoter leads to increased expression of this CDK inhibitor and blocks cell cycle progression. Also antagonizes PAWR mediated induction of aberrant amyloid peptide production in Alzheimer disease (presenile and senile dementia), although the molecular basis for this phenomenon has not been described to date.
Subcellular location: Nucleus, nucleolus {ECO:0000269|PubMed:12429849, ECO:0000269|PubMed:34516797}.
Interaction partners:
- Nucleolar protein 10
- RNA cytidine acetyltransferase
- Neuroguidin
- Probable U3 small nucleolar RNA-associated protein 11
- WD repeat-containing protein 36
- Transducin beta-like protein 3
- Ribosome biogenesis protein BMS1 homolog
- Nucleolar protein 6
- WD repeat-containing protein 43
- WD repeat-containing protein 3
Sequence:
MAGPQPLALQLEQLLNPRPSEADPEADPEEATAARVIDRFDEGEDGEGDFLVVGSIRKLASASLLDTDKRYCGKTTSRKAWNEDHWEQTLPGSSDEEISDEEGSGDEDSEGLGLEEYDEDDLGAAEEQECGDHRESKKSRSHSAKTPGFSVQSISDFEKFTKGMDDLGSSEEEEDEESGMEEGDDAEDSQGESEEDRAGDRNSEDDGVVMTFSSVKVSEEVEKGRAVKNQIALWDQLLEGRIKLQKALLTTNQLPQPDVFPLFKDKGGPEFSSALKNSHKALKALLRSLVGLQEELLFQYPDTRYLVDGTKPNAGSEEISSEDDELVEEKKQQRRRVPAKRKLEMEDYPSFMAKRFADFTVYRNRTLQKWHDKTKLASGKLGKGFGAFERSILTQIDHILMDKERLLRRTQTKRSVYRVLGKPEPAAQPVPESLPGEPEILPQAPANAHLKDLDEEIFDDDDFYHQLLRELIERKTSSLDPNDQVAMGRQWLAIQKLRSKIHKKVDRKASKGRKLRFHVLSKLLSFMAPIDHTTMNDDARTELYRSLFGQLHPPDEGHGD
Protein: MamJ paralog LimJ (Q2W8L8)
Organism: Paramagnetospirillum magneticum (strain ATCC 700264 / AMB-1) (Magnetospirillum magneticum)
Function: Regulates the dynamic behavior of MamK filaments; paralog MamJ also promotes MamK turnover. At least one other protein besides MamJ and LimJ is required for MamK turnover. Might connect magnetosomes to MamK filaments (Probable).
Subcellular location: Magnetosome {ECO:0000269|PubMed:16303747, ECO:0000305|PubMed:21883528}. Note=Tagged protein extends in a line from one pole to the other. {ECO:0000250|UniProtKB:Q2W8Q7, ECO:0000305|PubMed:21883528}.
Interaction partners:
Sequence:
MMMEHEMATNRRPRAKRTPGDKLGKGGGDAALAPAADAEIPASSAPEPAAPISAPPAPVIKPVGGDAWASLLSGSPWSSPGAASPTEAALKPVMPSALAEAVANAPPEAAPFTELVSHWSPPFRRQPDREYEEINPAEAAIPVTAAAPEPEPEPVPEPEPEPEPEAAHDHAATETEGVTEMMTSDVELEIEIASDVEVVEAPAVIEPSPRPQAFSHSTAYAYPAEPAPAVETAAEAAPAGPAENPVKEVPVEDLFTGIFNVADSAVRGAIGASTDLLRDPKSLGGKLSVAGQSLVHSIKGRFNALLAPRHGAKSNGDEF
Protein: Aspartyl/glutamyl-tRNA(Asn/Gln) amidotransferase subunit B (Asp/Glu-ADT subunit B) (EC 6.3.5.-) (P9WN61)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: Allows the formation of correctly charged Asn-tRNA(Asn) or Gln-tRNA(Gln) through the transamidation of misacylated Asp-tRNA(Asn) or Glu-tRNA(Gln) in organisms which lack either or both of asparaginyl-tRNA or glutaminyl-tRNA synthetases. The reaction takes place in the presence of glutamine and ATP through an activated phospho-Asp-tRNA(Asn) or phospho-Glu-tRNA(Gln) (By similarity).
Interaction partners:
- Glutamyl-tRNA
- Glutamyl-tRNA
- Aspartate--tRNA
- Putative amidase AmiD
- Putative amidase AmiA2
- Putative amidase AmiB2
- Possible amidase
- Putative amidase AmiC
- Glutamate--tRNA ligase
- GMP synthase
Sequence:
MTVAAGAAKAAGAELLDYDEVVARFQPVLGLEVHVELSTATKMFCGCTTTFGGEPNTQVCPVCLGLPGSLPVLNRAAVESAIRIGLALNCEIVPWCRFARKNYFYPDMPKNYQISQYDEPIAINGYLDAPLEDGTTWRVEIERAHMEEDTGKLTHIGSETGRIHGATGSLIDYNRAGVPLIEIVTKPIVGAGARAPQIARSYVTALRDLLRALDVSDVRMDQGSMRCDANVSLKPAGTTEFGTRTETKNVNSLKSVEVAVRYEMQRQGAILASGGRITQETRHFHEAGYTSAGRTKETAEDYRYFPEPDLEPVAPSRELVERLRQTIPELPWLSRRRIQQEWGVSDEVMRDLVNAGAVELVAATVEHGASSEAARAWWGNFLAQKANEAGIGLDELAITPAQVAAVVALVDEGKLSNSLARQVVEGVLAGEGEPEQVMTARGLALVRDDSLTQAAVDEALAANPDVADKIRGGKVAAAGAIVGAVMKATRGQADAARVRELVLEACGQG
Protein: ATP synthase subunit beta, chloroplastic (EC 7.1.2.2) (ATP synthase F1 sector subunit beta) (F-ATPase subunit beta) (P0C2Z8)
Organism: Oryza sativa subsp. indica (Rice)
Function: Produces ATP from ADP in the presence of a proton gradient across the membrane. The catalytic sites are hosted primarily by the beta subunits.
Subcellular location: Plastid, chloroplast thylakoid membrane {ECO:0000255|HAMAP-Rule:MF_01347}; Peripheral membrane protein {ECO:0000255|HAMAP-Rule:MF_01347}.
Interaction partners:
- ATP synthase subunit alpha
- ATP synthase epsilon chain, chloroplastic
- ATP synthase subunit alpha, chloroplastic
- ATP synthase subunit a, chloroplastic
- ATP synthase subunit d
- Uncharacterized protein
- F-ATPase gamma subunit
- ATP synthase subunit b, chloroplastic
- ATP synthase subunit c, chloroplastic
- ATP synthase CF0 subunit I
Sequence:
MRTNPTTSRPGVSTIEEKSTGRIDQIIGPVLDVTFPPGKLPYIYNALVVKSRDTDGKQINVTCEVQQLLGNNRVRAVAMSATDGLMRGMEVIDTGAPLSVPVGGATLGRIFNVLGEPVDNLGPVDTSATFPIHRSAPAFIELDTKLSIFETGIKVVDLLAPYRRGGKIGLFGGAGVGKTVLIMELINNIAKAHGGVSVFGGVGERTREGNDLYMEMKESGVINEKNLEESKVALVYGQMNEPPGARMRVGLTALTMAEYFRDVNKQDVLLFIDNIFRFVQAGSEVSALLGRMPSAVGYQPTLSTEMGSLQERITSTKKGSITSIQAVYVPADDLTDPAPATTFAHLDATTVLSRGLASKGIYPAVDPLDSTSTMLQPRIVGNEHYETAQRVKQTLQRYKELQDIIAILGLDELSEEDRLTVARARKIERFLSQPFFVAEVFTGSPGKYVGLAETIRGFQLILSGELDGLPEQAFYLVGNIDEASTKAINLEEENKLKK
Protein: Transcription initiation factor TFIID subunit (A0A8I6A7M0)
Organism: Rattus norvegicus (Rat)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123, ECO:0000256|PIRNR:PIRNR003047}.
Interaction partners:
Sequence:
MGPGWAGLLPEDGSGSPSAVMSDTDSDEDSAGGGPFSLTGFLFGNINGAGQLEGESVLDDECKKHLAGLGALGLGSLITELTANEELSGTDGTLVNDEGWIRSREDAVDYSDINEVAEDESRRYQQTMGSLQPLCHTDYDEDDYDADCEDIDCKLMPPPPPPPGPVKKERDQDGITGVSEDGEGIILPSIIAPSSLASEKVDFSSSSDSESEMGPQEATQSESKDGKLTLPLAGIMQHDATKLLPSVTELFPEFRPGKVLRFLRLFGPGKNVPSVWRSARRKRKKKHRELIQEEQIQEEECSVELEVNQKSLWNYDYAPPPLPEQCLSDDEITMMAPVESKFSQSTGDTDKVMDTKPRVAEWRYGPARLWYDMLGVPEDGSGFDYGFKMKKTEHDSTMKYNIMKKLRKLEENNGVDLLADENFLMVTQLHWEDDIIWDGEDVKHKGTKPQRASLAGWLPSSMTRNAMAYNVQQGFTATLDDDKPWYSIFPIDNEDLVYGRWEDNIIWDAQNMPRILEPPVLTLDPNDENLILEIPDEKEEATSNSPSKENKKESSLKKSRILLGKTGVIKEEPQQNMSQPEVKDPWNLSNDEYYYPKQQGLRGTFGGNIIQHSIPAVELRQPFFPTHMGPIKLRQFHRPPLKKYSFGALSQPGPHSVQPLLKHIKKKAKMREQERQASGGGEMFFMRTPQDLTGKDGDLILAEYSEENGPLMMQVGMATKIKNYYKRKPGKDPGAPDCKYGETVYCHTSPFLGSLHPGQLLQAFENNLFRAPIYLHKMPESDFLIIRTRQGYYIRELVDIFVVGQQCPLFEVPGPNSKRANTHIRDFLQVFIYRLFWKSKDRPRRIRMEDIKKAFPSHSESSIRKRLKLCADFKRTGMDSNWWVLKSDFRLPTEEEIRAMVSPEQCCAYYSMIAAEQRLKDAGYGEKSFFAPEEENEEDFQMKIDDEVRTAPWNTTRAFIAAMKGKCLLEVTGVADPTGCGEGFSYVKIPNKPTQQKDDKEPQPVKKTVTGTDADLRRLSLKNAKQLLRKFGVPEEEIKKLSRWEVIDVVRTMSTEQARSGEGPMSKFARGSRFSVAEHQERYKEECQRIFDLQNKVLSSTEVLSTDTDSSSAEDSDFEEMGKNIENMLQNKKTSSQLSREREEQERKELQRMLLAAGSAAGGNNHRDDDTASVTSLNSSATGRCLKIYRTFRDEEGKEYVRCETVRKAAVIDAYVRIRTTKDEEFIRKFALFDEQHREEMRKERRRIQEQLRRLKRNQEKEKLKGPPEKKPKKMKERPDLKLKCGACGAIGHMRTNKFCPLYYQTNAPPSNPVAMTEEQEEELEKTVIHNDNEELIKVEGTKIVLGKQLIESADEVRRKSLVLKFPKQQLPPKKKRRVGTTVHCDYLNRPHKSIHRRRTDPMVTLSSILESIINDMRDLPNTYPFHTPVNAKVVKDYYKIITRPMDLQTLRENVRKRLYPSREEFREHLELIVKNSATYNGPKHSLTQISQSMLDLCDEKLKEKEDKLARLEKAINPLLDDDDQVAFSFILDNIVTQKMMAVPDSWPFHHPVNKKFVPDYYKVIVNPMDLETIRKNISKHKYQSRESFLDDVNLILANSVKYNGPESQYTKTAQEIVNVCHQTLTEYDEHLTQLEKDICTAKEAALEEAELESLDPMTPGPYTPQAKPPDLYDNSTSLSVSRDASVYQDESNLSVLDIPSATSEKQLTQEGGDGDGDLADEEEGTVQQPQASVLYEDLLMSEGEDDEEDAGSDEEGDNPFSAIQLSESGSDSDVESGSIRPKQPRMLQENTRMGMENEESMMSYEGDGGEASRGLEDSNISYGSYEEPDPKSNTQDTSFSSIGGYEVSEEEEDEEEQRSGPSVLSQVQLSEDEEDSEDLHSIAGDSDLDSDE
Protein: ADP-ribosylation factor 3 (P40994)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: GTP-binding protein involved in protein trafficking; may modulate vesicle budding and uncoating within the Golgi apparatus.
Subcellular location: Golgi apparatus.
Interaction partners:
- ARF guanine-nucleotide exchange factor 2
- ARF guanine-nucleotide exchange factor 1
- Guanine-nucleotide exchange factor YEL1
- ADP-ribosylation factor guanine nucleotide-exchange factor SEC7
- LAS seventeen-binding protein 5
- ADP-ribosylation factor 1
- ADP-ribosylation factor 2
- ADP-ribosylation factor GTPase-activating protein GCS1
- Protein GTS1
- ADP-ribosylation factor GTPase-activating protein GLO3
Sequence:
MGNSISKVLGKLFGSKEMKILMLGLDKAGKTTILYKLKLNKIKTSTPTVGFNVETVTYKNVKFNMWDVGGQQRLRPLWRHYFPATTALIFVIDSSARNRMEEAKEELYSIIGEKEMENVVLLVWANKQDLKDAMKPQEVSDFLELEKNLKNQPWCVIGSNALSGQGLVEGLSWISNNTNVPKK