wanglab/gogpt-training-data huggingface dataset:
Protein: Membrane protein (M) (E1 glycoprotein) (Matrix glycoprotein) (Membrane glycoprotein) (P0DTC5)
Organism: Severe acute respiratory syndrome coronavirus 2 (2019-nCoV) (SARS-CoV-2)
Function: Component of the viral envelope that plays a central role in virus morphogenesis and assembly via its interactions with other viral proteins (By similarity). Regulates the localization of S protein at cis-Golgi, the place of virus budding. May act by binding cytoplasmic c-terminus of S.
Subcellular location: Virion membrane {ECO:0000255|HAMAP-Rule:MF_04202}; Multi-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_04202}. Host Golgi apparatus membrane {ECO:0000255|HAMAP-Rule:MF_04202, ECO:0000269|PubMed:33060197}; Multi-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_04202}. Host membrane {ECO:0000269|PubMed:33060197}; Multi-pass membrane protein. Note=Largely embedded in the lipid bilayer. {ECO:0000255|HAMAP-Rule:MF_04202}.
Interaction partners:
Sequence:
MADSNGTITVEELKKLLEQWNLVIGFLFLTWICLLQFAYANRNRFLYIIKLIFLWLLWPVTLACFVLAAVYRINWITGGIAIAMACLVGLMWLSYFIASFRLFARTRSMWSFNPETNILLNVPLHGTILTRPLLESELVIGAVILRGHLRIAGHHLGRCDIKDLPKEITVATSRTLSYYKLGASQRVAGDSGFAAYSRYRIGNYKLNTDHSSSSDNIALLVQ
Protein: Bifunctional glutamate/proline--tRNA ligase (Bifunctional aminoacyl-tRNA synthetase) [Includes: Glutamate--tRNA ligase (EC 6.1.1.17) (Glutamyl-tRNA synthetase); Proline--tRNA ligase (EC 6.1.1.15) (Prolyl-tRNA synthetase) (ProRS)] (P28668)
Organism: Drosophila melanogaster (Fruit fly)
Function: Catalyzes the attachment of the cognate amino acid to the corresponding tRNA in a two-step reaction: the amino acid is first activated by ATP to form a covalent intermediate with AMP and is then transferred to the acceptor end of the cognate tRNA.
Interaction partners:
- leucine--tRNA ligase
- Probable glutamine--tRNA ligase
- Methionine--tRNA ligase, cytoplasmic
- Probable aminoacyl tRNA synthase complex-interacting multifunctional protein 2
- Asparagine--tRNA ligase, cytoplasmic
- AaRS-interacting multifunctional protein 1
- isoleucine--tRNA ligase
- Isoleucine--tRNA ligase, cytoplasmic
- Tyrosine--tRNA ligase
- Elongation factor 1-gamma
Sequence:
MSIKLKANLNNPPISGLATAHLINGTVPVEIVWSKEETSLQFPDNRLLVCHSNNDVLRALARAAPDYKLYGETAIERTQIDHWLSFSLTCEDDISWALSFLDKSIAPVTYLVANKLTIADFALFNEMHSRYEFLAAKGIPQHVQRWYDLITAQPLIQKVLQSLPEDAKVKRSPQSSKEQTPAKTGERKQEGKFVDLPGAEMGKVVVRFPPEASGYLHIGHAKAALLNQYYALAFQGTLIMRFDDTNPAKETVEFENVILGDLEQLQIKPDVFTHTSNYFDLMLDYCVRLIKESKAYVDDTPPEQMKLEREQRVESANRSNSVEKNLSLWEEMVKGSEKGQKYCVRAKIDMSSPNGCMRDPTIYRCKNEPHPRTGTKYKVYPTYDFACPIVDAIENVTHTLRTTEYHDRDDQFYWFIDALKLRKPYIWSYSRLNMTNTVLSKRKLTWFVDSGLVDGWDDPRFPTVRGIIRRGMTVEGLKEFIIAQGSSKSVVFMNWDKIWAFNKKVIDPIAPRYTALEKEKRVIVNVAGAKVERIQVSVHPKDESLGKKTVLLGPRIYIDYVDAEALKEGENATFINWGNILIRKVNKDASGNITSVDAALNLENKDFKKTLKLTWLAVEDDPSAYPPTFCVYFDNIISKAVLGKDEDFKQFIGHKTRDEVPMLGDPELKKCKKGDIIQLQRRGFFKVDVAYAPPSGYTNVPSPIVLFSIPDGHTKDVPTSGLKVNAPDAKATKKASSPVSSSGQASELDSQISQQGDLVRDLKSKKAAKDQIDVAVKKLLALKADYKSATGKDWKPGQTSASSAPVPAASSSSANDAVSVNASIVKQGDLVRDLKGKKASKPEIDAAVKTLLELKAQYKTLTGQDWKPGTVPTTAAPSASAAPSVGVNDSVAQILSQITAQGDKVRELKSAKADKATVDAAVKTLLSLKADYKAATGSDWKPGTTAPAPAAAPVKVKQEKNPDPASVLTVNTLLNKIAQQGDKIRQLKSAKSEKSLVEAEVKLLLALKTDYKSLTGQEWKPGTVAPAPTTVNVIDLTGGDSGSDVGSVLSKIQAQGDKIRKLKSEKAAKNVIDPEVKTLLALKGEYKTLSGKDWTPDAKSEPAVVKKEASPVSMASPAKDELTQEINAQGEKVRAAKGNKAAKEVIDAEVAKLLALKAKYKEVTGTDFPVAGRGGGGGGGSAKKAPKEAQPKPAKPVKKEPAADASGAVKKQTRLGLEATKEDNLPDWYSQVITKGEMIEYYDVSGCYILRQWSFAIWKAIKTWFDAEITRMGVKECYFPIFVSKAVLEKEKTHIADFAPEVAWVTKSGDSDLAEPIAVRPTSETVMYPAYAKWVQSYRDLPIRLNQWNNVVRWEFKQPTPFLRTREFLWQEGHTAFADKEEAAKEVLDILDLYALVYTHLLAIPVVKGRKTEKEKFAGGDYTTTVEAFISASGRAIQGATSHHLGQNFSKMFEIVYEDPETQQKKYVYQNSWGITTRTIGVMIMVHADNQGLVLPPHVACIQAIVVPCGITVNTKDDERAQLLDACKALEKRLVGGGVRCEGDYRDNYSPGWKFNHWELKGVPLRLEVGPKDLKAQQLVAVRRDTVEKITIPLADVEKKIPALLETIHESMLNKAQEDMTSHTKKVTNWTDFCGFLEQKNILLAPFCGEISCEDKIKADSARGEEAEPGAPAMGAKSLCIPFDQPAPIAASDKCINPSCTNKPKFYTLFGRSY
Protein: Protein SERAC1 (Serine active site-containing protein 1) (Q3U213)
Organism: Mus musculus (Mouse)
Function: Plays an important role in the phosphatidylglycerol remodeling that is essential for both mitochondrial function and intracellular cholesterol trafficking. May catalyze the remodeling of phosphatidylglycerol and be involved in the transacylation-acylation reaction to produce phosphatidylglycerol-36:1. May be involved in bis(monoacylglycerol)phosphate biosynthetic pathway (By similarity).
Subcellular location: Membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}. Endoplasmic reticulum {ECO:0000250}. Mitochondrion {ECO:0000250}. Note=Localizes at the endoplasmic reticulum and at the endoplasmic reticulum-mitochondria interface. {ECO:0000250}.
Interaction partners:
- Transmembrane protein 242
- Tubby-related protein 4
- General transcription factor IIH subunit 5
Sequence:
MSLAAYCVICCRRIGSFAPRSKSRTPWRNIRNIIRFTGSLIVGGSLFITYEVLALKKSLMLDTQVVEREKMKSYIYVHKAPVDRLDNRGIVWQARKELHRAVRKLLAAAAKVLRSPFADSFSTVDIEDHDCAVWLLLRKSREDDLAARLQAVREMSEAHHWHDYQYRIIAQACDPRTLIGLARSKESDLRFFLPPPPLPSLKEDSSTEEELRHLLASLPQTELDECLQYFTSLALSESSQSLAAQKGGLWCFGGNGLPYAESFGKVPSATVEMFCLEAIVKHSEIPSHCDHIEAGGGLQLLQRLYQLHKDCPKVQRNVMRIIGNMALNEHLHPAIVHSGWVSLMAEALKSSHIMEASHAARTLANLDRETVGEKYQDGVYVLHPQCRTSQPIKADVLFIHGLMGAAFKTWRQHDSQRALTESAVVDEDRYTTCWPKTWLAKDCPSLRIISVEYDTSLSDWRARCPMERKSIAFRSNELLSKLRAAGVGDRPMIWISHSMGGLLVKKMLLEASKKPELNALINNTRGIIFYSVPHHGSRLAEYSVNIRYLLFPSLEVKELSKDSPALKTLQDDFLEFAKDKNFQVLNFVETQPTFIGSMIKLHVVPVESADLGIGDLIPVDVNHLNICKPKTKDAFLYQRTLQFICETLARDLEN
Protein: Probable bifunctional methylthioribulose-1-phosphate dehydratase/enolase-phosphatase E1 [Includes: Methylthioribulose-1-phosphate dehydratase (MTRu-1-P dehydratase) (EC 4.2.1.109); Enolase-phosphatase E1 (EC 3.1.3.77) (2,3-diketo-5-methylthio-1-phosphopentane phosphatase)] (Q9FN41)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- Methylthioribose-1-phosphate isomerase
- Acireductone dioxygenase 2-requiring) 2)
- Acireductone dioxygenase 3-requiring) 3)
- Acireductone dioxygenase 4-requiring) 4)
- Acireductone dioxygenase 1-requiring) 1)
- Methylthioribose kinase
- Xylulose kinase 2
- 5'-methylthioadenosine/S-adenosylhomocysteine nucleosidase
- 5'-methylthioadenosine nucleosidase
- fructose-bisphosphatase
Sequence:
MAVAAAAMIGLPQAYLEGKEVKETSSLVTELCRHFYTQGWVSGTGGSITMKVHDASIPKPEQLIVMSPSGVQKERMQPEDMYILSANGSIISTPSPKPYPNKPPKCTDCAPLFMKAYEMRNAGAVIHSHGMESCLVTMLNPQAKEFRITHMEMIKGIQGHGYYDELVVPIIENTAYENELTDSLTKAIEAYPKATAVLVRNHGVYIWGDSWIHAKTQAECYHYLFDAAIKLHQLGLDAATPDHGPIRRTIHSQIKDSQYEREWPRRWIVLDIEGTTTPITFVTDVLFPYARENVGKHLNLTYHTAETQEDIKLLRAQVEEDLREGVTGAVPIPHADEGKEKVIAAMVSNVEAMIRADRKITALKELQGHIWRTGFECDELKAIVFEDVADALEKWHSSGIKVYIYSSGSRLAQKLLFGNTDYGDLRKYISGFFDTTIGNKKESRSYKEIKETLGVDDPAEIMFVTDVYQEAVAAKAAGLEAIISIRPGNAPLPENHGFKTVTSFSQI
Protein: Aminoacyl tRNA synthetase complex-interacting multifunctional protein 1 (A0A8I6A263)
Organism: Rattus norvegicus (Rat)
Interaction partners:
Sequence:
MMRVRKRIFCRFWGKMATNDAVLKRLEQKGAEADQIIEYLKQQVALLKEKAILQATLREEKKLQVENAKLKKEIEELKQELIQAEIHNGVKQVPVPSSSSLETHCSVSESVTRSASVTTTTMTGGGGEEKKVKEKTEKKGEKKEKKQQSAAASADSKPVDVSRLDLRIGCIVTAKKHPDADSLYVEEVDVGEAAPRTVVSGLVNHVPLEQMQNRMVVLLCNLKPAKMRGVLSQAMVMCASSPEKVEILAPPNGSVPGDRITFDAFPGEPDKELNPKKKIWEQIQPDLHTNDECVATYKGAPFEVKGKGVCRAQTMANSGIK
Protein: Lethal(3)malignant brain tumor-like protein 3 (L(3)mbt-like protein 3) (MBT-1) (Q8BLB7)
Organism: Mus musculus (Mouse)
Function: Is a negative regulator of Notch target genes expression, required for RBPJ-mediated transcriptional repression. It recruits KDM1A to Notch-responsive elements and promotes KDM1A-mediated H3K4me demethylation (By similarity). Involved in the regulation of ubiquitin-dependent degradation of a set of methylated non-histone proteins, including SOX2. It acts as an adapter recruiting the CRL4-DCAF5 E3 ubiquitin ligase complex to methylated target proteins. Also involved in the regulation of ubiquitin-dependent degradation of methylated DNMT1 and E2F1 (By similarity). Required for normal maturation of myeloid progenitor cells.
Subcellular location: Nucleus {ECO:0000269|PubMed:15889154, ECO:0000269|PubMed:33980486}.
Interaction partners:
- Recombining binding protein suppressor of hairless
- DDB1- and CUL4-associated factor 5
Sequence:
MTESASSTSGQEFDVFSVMDWKDGVGTLPGSDLKFRVNEFGALEVITDESEMESVKKATATTTWMVPTAQDAPTSPPSSRPVFPPAYWTSPPGCPTVFSEKTGVPFRLKEQSKADGLQFCENCCQYGNGDECLSGGKYCSQNCARHAKDKDQKDERDGGEDNDEEDPKCSRKKKPKLSLKADSKDDGEERDDEMENKQDGRILRGSQRARRKRRGDSAVLKQGLPPKGKKTWCWASYLEEEKAVAVPTKLFKEHQSFPYNKNGFKVGMKLEGVDPDHQAMYCVLTVAEVCGYRIKLHFDGYSDCYDFWVNADALDIHPVGWCEKTGHKLRPPKGYKEEEFNWQSYLKTCKAQAAPKSLFENQNITVIPSGFRVGMKLEAADKKSPSVICVATVTDMVDNRFLVHFDNWDESYDYWCESNSPHIHPVGWCKEHRRTLITPPGYSHVKHFSWDKYLEETNSLPAPARAFKVKPPHGFQKKMKLEAVDKRNPLFIRVATVADTDDHRIKVHFDGWSSCYDYWIDADSPDIHPVGWCSKTGHPLQAPLSPAELMEPSETGGCPTLGCRGVGHFKKSRYLGTQSGANCPYSEINLSKERIFPDRLSGDTSPPTTPSFPRSKRMDTRESSSSPETREKHANNFKEDSEKKKENEVKTSAEAKVVREEPTPSVQQSQPPQQVQQVQHAQPPQQAQKAPQAQQAQQAQQAQQAPQAPQTPQPQQAPQVQQAQQAPQAQQAQQPQQAQQPQQAPPVQQPQQVQQAQPTQQQAQTQQQAQRRSAVFLSFKPPIPCLPLRWEQQSKLLPTVAGIPASRVSKWSTDEVSEFIQSLPGCEEHGKVFKDEQIDGEAFLLMTQTDIVKIMSIKLGPALKIFNSILMFKAAEKNSHNEL
Protein: ADP ribosylation factor-like GTPase 3, like 1 (ADP-ribosylation factor-like 3, like 1) (Q6PC92)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000256|ARBA:ARBA00004300}.
Interaction partners:
- Protein unc-119 homolog B
- Sulfotransferase
- Protein unc-119 homolog A
- Protein XRP2
- Transporter
Sequence:
MGEVQKGLFSVIEKLKGTTEQELRIVLLGLDNAGKTTLLKQLASEDVNTITPTQGFNIKSVTCDGMKLNVWDIGGQRKIRPFWKKYLENTDLLIYVIDSADKKRFEETGLELSELIDEENLKGVPLLIFANKQDLATASPASEIAEGLNLHTYRDREWQIQACSAVSGEGVQDGMNWISNNIVNKKK
Protein: Nuclear cap-binding protein subunit 3 (Protein ELG) (Q53F19)
Organism: Homo sapiens (Human)
Function: Associates with NCBP1/CBP80 to form an alternative cap-binding complex (CBC) which plays a key role in mRNA export. NCBP3 serves as adapter protein linking the capped RNAs (m7GpppG-capped RNA) to NCBP1/CBP80. Unlike the conventional CBC with NCBP2 which binds both small nuclear RNA (snRNA) and messenger (mRNA) and is involved in their export from the nucleus, the alternative CBC with NCBP3 does not bind snRNA and associates only with mRNA thereby playing a role in only mRNA export. The alternative CBC is particularly important in cellular stress situations such as virus infections and the NCBP3 activity is critical to inhibit virus growth.
Subcellular location: Nucleus {ECO:0000269|PubMed:26382858}. Cytoplasm {ECO:0000269|PubMed:26382858}.
Interaction partners:
- Nuclear cap-binding protein subunit 1
- Nuclear cap-binding protein subunit 2
- Eukaryotic translation initiation factor 4E
- THO complex subunit 2
- Protein argonaute-2
- Zinc finger CCCH domain-containing protein 11A
- Eukaryotic translation initiation factor 4E type 2
- RNA guanine-N7 methyltransferase activating subunit
- mRNA cap guanine-N
- Spliceosome RNA helicase DDX39B
Sequence:
MAAVRGLRVSVKAEAPAGPALGLPSPEAESGVDRGEPEPMEVEEGELEIVPVRRSLKELIPDTSRRYENKAGSFITGIDVTSKEAIEKKEQRAKRFHFRSEVNLAQRNVALDRDMMKKAIPKVRLETIYICGVDEMSTQDVFSYFKEYPPAHIEWLDDTSCNVVWLDEMTATRALINMSSLPAQDKIRSRDASEDKSAEKRKKDKQEDSSDDDEAEEGEVEDENSSDVELDTLSQVEEESLLRNDLRPANKLAKGNRLFMRFATKDDKKELGAARRSQYYMKYGNPNYGGMKGILSNSWKRRYHSRRIQRDVIKKRALIGDDVGLTSYKHRHSGLVNVPEEPIEEEEEEEEEEEEEEEEDQDMDADDRVVVEYHEELPALKQPRERSASRRSSASSSDSDEMDYDLELKMISTPSPKKSMKMTMYADEVESQLKNIRNSMRADSVSSSNIKNRIGNKLPPEKFADVRHLLDEKRQHSRPRPPVSSTKSDIRQRLGKRPHSPEKAFSSNPVVRREPSSDVHSRLGVPRQDSKGLYADTREKKSGNLWTRLGSAPKTKEKNTKKVDHRAPGAEEDDSELQRAWGALIKEKEQSRQKKSRLDNLPSLQIEVSRESSSGSEAES
Protein: Probable high-affinity hexose transporter ght8, mitochondrial (Hexose transporter 8) (Q9P3U7)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Subcellular location: Mitochondrion membrane {ECO:0000269|PubMed:16823372}; Multi-pass membrane protein {ECO:0000269|PubMed:16823372}.
Interaction partners:
- SNF1-like protein kinase ssp2
- Zinc finger protein rsv1
- Uncharacterized transporter C794.04c
Sequence:
MGKTLTIVMLVFVSMAGWMFGADTGSIGGITNMRDFQSRFADRYNPVTDTYSYSSARQGLITGMVNVGSMTGCILSSPLMDRIGKRVSIMFWTIVYLIGIILQVTAVPSWVQIMVAKIWTGLAIGALSVLAPGFQSEVAPATLRGTIVTTYQLAVTGGIFIAACINMGTHKLHKTAQWRVSMGINLLWGIIMFIGISFLPESPRYLIAIGKDEEALDIMCKNNVLPREHEIIQTEYHVIKTDCEAEMAGGPATWGDILGADIRYRTFLGLGVMSLQQLTGDNYYFYYGFEVFEGTGMNSPYLSALILDAVNFGCTFGGLFVLEFFGRRMPLIIGGVWQSITFFIYAAVGNRALTRKNGTSNHRAGAVMIVFSCLFIFSFAQTWGPAAYVIVGESYPIRYRSKCAAVATTGNWLWGFLITFFTPFISDSIGFKYGYIFAACNLCAACIIFLFAHETKGLTLEEINELYLSGAKPWMPRPENLGQAAKQQQEVLEKSRGVQGESAAHLENVDNEGMEDTSSNDITSSTSSSEGRAKPESNYVDEQDRYA
Protein: Protein FD (bZIP transcription factor 14) (AtbZIP14) (Q84JK2)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Transcription factor required for the transition to flowering promoted by FT.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00978, ECO:0000269|PubMed:16099979, ECO:0000269|PubMed:25661797}.
Interaction partners:
- Protein FLOWERING LOCUS T
- Protein TERMINAL FLOWER 1
- Zinc finger protein CONSTANS
- Protein LEAFY
- Basic leucine zipper 8
- Transcription factor PERIANTHIA
Sequence:
MLSSAKHQRNHRLSATNKNQTLTKVSSISSSSPSSSSSSSSTSSSSPLPSQDSQAQKRSLVTMEEVWNDINLASIHHLNRHSPHPQHNHEPRFRGQNHHNQNPNSIFQDFLKGSLNQEPAPTSQTTGSAPNGDSTTVTVLYSSPFPPPATVLSLNSGAGFEFLDNQDPLVTSNSNLHTHHHLSNAHAFNTSFEALVPSSSFGKKRGQDSNEGSGNRRHKRMIKNRESAARSRARKQAYTNELELEVAHLQAENARLKRQQDQLKMAAAIQQPKKNTLQRSSTAPF
Protein: non-specific serine/threonine protein kinase (EC 2.7.11.1) (A0A8I5ZZ88)
Organism: Rattus norvegicus (Rat)
Interaction partners:
Sequence:
MELRVGNKYRLGRKIGSGSFGDIYLGANIASGEEVAIKLECVKTKHPQLHIESKFYKMMQGGVGIPSIKWCGAEGDYNVMVMELLGPSLEDLFNFCSRKFSLKTVLLLADQMISRIEYIHSKNFIHRDVKPDNFLMGLGKKGNLVYIIDFGLAKKYRDARTHQHIPYRENKNLTGTARYASINTHLGIEQSRRDDLESLGYVLMYFNLGSLPWQGLKAATKRQKYERISEKKMSTPIEVLCKGYPSEFSTYLNFCRSLRFDDKPDYSYLRQLFRNLFHRQGFSYDYVFDWNMLKFMRPPALPCGRPQDQLGCSPESRGRRPGETRARTGREDGTVARVRDQSPAPWPTNRGYRQPTPKCSRACGFHPGLPHPASWQYFSQSDLTGRPREEGEHETPQRCACQCLILRPHWATRGLPNCSLTDKRAI
Protein: protein-tyrosine-phosphatase (EC 3.1.3.48) (A0A0G2K561)
Organism: Rattus norvegicus (Rat)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004479}; Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004479}.
Interaction partners:
Sequence:
TFGVSCGGSHQSPIDILDHHARVGEEYQELQLDGFDNESSNKTWMKNTGKTVAILLKDDYFVSGAGLPGRFKAEKVEFHWGHSNGSAGSEHSVNGRRFPVEMQIFFYNPDDFDSFQTAISENRIIGAMAIFFQVSPRDNSALDPIIHGLKGVVHHEKETFLDPFVLRDLLPASLGSYYRYTGSLTTPPCSEIVEWIVFRRPVPISYHQLEAFYSIFTTEQQDHVKSVEYLRNNFRPQQALNDRVVSKSAVRDAWNHDLADFLDNPLGTEASKVCSSPPIHMKVQPLNQTALQVSWSQPETIYHPPIMNYMISYSWTKNEDEKEKTFTKDSDKDLKATISHISPDSLYLFRVQAVCRNDMRSDFSQTMLFQANTTRIFQGTRIVKTGVPTASPASSADMAPISSGSSTWTSSGIPFSFVSMATGMGPSSSGSQATVASVVTSTLLAGLGFGGGGISSFPSTVWPTRLPTASAASKQAGRPVLATTEALASPGPDGDSAPTKDGEGAEEGEKEEKSESEDGEREQEEEEKDSEKKEKSEATHTAAESDQTAPAPTPSSPHRTAQEGGHQTIPGHRQDHSAPVTDQPGHVDPGLDTLVDTATQVPPTATEEHYSGSDPKRPEMPSKKPISRGDRFSEDSKFITVNPAEKNTSGMISRPSPGRMEWIIPLIVVSALTFVCLVLLIAVLVYWRKCFQTAHFYVEDSSSPRVVPNESIPIIPIPDDMEAIPVKQFGKHIGELYSNSQHGFSGDFEEVQRCTADMNITAEHSNHPDNKHKNRYINILAYDHSRVKLRPLPGKDSKHSDYINANYVDGYNKAKAYIATQGPLKSTFEDFWRMIWEQNTGIIIMITNLVEKGRRKCDQYWPTENTEEYGNIIVTLKSTEVHACYTVRRFSVRNTKVKKGQKGNPKGRQNERTVIQYHYTQWPDMGVPEYALPVLTFVRRSSAARMPDMGPVLVHCSAGVGRTGTYIVIDSMLQQIKDKSTVNVLGFLKHIRTQRNYLVQTEEQYIFIHDALLEAILGKETEVSSSQLHSYVNSILIPGVGGKTRLEKQFKLITQCNAKYVECFSAQKECNKEKNRNSSVVPAERARVGLAPLPGMKGTDYINASYIMGYYRSNEFIITQHPLPHTTKDFWRMIWDHNAQIIVMLPDNQSLAEDEFVYWPSREESMNCEAFTVTLISKDRLCLSNEEQIIIHDFILEATQDDYVLEVRHFQCPKWPNPDAPISSTFELINVIKEEALARDGPTIVHDEYGAVSAGMLCALTTLSQQLENENAVDVFQVAKMINLMRPGVFTDIEQYQFVYKAMLSLVSTKENGNGPMTGDKNGAVLTAEESDPAESMESLV
Protein: Flavin-dependent trigonelline monooxygenase, reductase component (EC 1.5.1.36) (Flavin:NADH reductase) (Q6F9F5)
Organism: Acinetobacter baylyi (strain ATCC 33305 / BD413 / ADP1)
Function: Involved in the degradation of the pyridine ring of trigonelline (TG; N-methylnicotinate) into succinate and methylamine as carbon and nitrogen sources, respectively. TgnA catalyzes the reduction of flavin (FMN or FAD) by NADH and supplies the reduced flavin to the oxygenase component TgnB.
Interaction partners:
- Flavin-dependent trigonelline monooxygenase, oxygenase component
- (E)-2-((N-methylformamido)methylene)succinate hydrolase (MFMS hydrolase)
- p-hydroxyphenylacetate hydroxylase C1:reductase component
- NADH-dependent FMN reductase
- Riboflavin biosynthesis protein
- Peptide synthetase
- (Z)-2-((N-methylformamido)methylene)-5-hydroxybutyrolactone dehydrogenase (MFMB dehydrogenase)
Sequence:
MSEMDAVNKIRELRDAFGSFMTGVTVVTTCKDDGTPLGFTANSFASVSLDPALLLVSIAKTSSNYHNFADASHFAINILAEEQKDVSNIFARPSDDRFAQLVWAKSEYQNPLIDGVSAWFDCTTYQVVDAGDHAILIGKVENFTSAGFAGLGYYRGAYFTPAKSSTDVISSMKVMMMALIGHENKILLEQTADHKWALPHLMVEKDGAEKALEKIFATYQPEASPSFIYSVYDDVTTQQQYIAFLCNTPVPTAHKGQFVDLNDLEKLTFTDSALQSMLMRYRKENYLKTYGVYYGNHTSGTVRQIVKEGV
Protein: APETALA2-like protein 5 (Protein SHATTERING ABORTION 1) (A0A0N7KJT8)
Organism: Oryza sativa subsp. japonica (Rice)
Function: Transcription factor. Involved in spikelet transition and development (Probable). Prevents lemma and palea elongation as well as grain growth. Required for seed shattering through specifying abscission zone (AZ) development.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00366, ECO:0000269|PubMed:22408071}.
Interaction partners:
Sequence:
MWDLNDSPAAEAAPPPLSPSADDSGASSSSAAAVVEIPDDADDDSAAVVVVTRQFFPPAVPGGGGDPAPGNARAGWLRLAGAAPPVAATGPAASAAVSKKSRRGPRSRSSQYRGVTFYRRTGRWESHIWDCGKQVYLGGFDTAHAAARAYDRAAIKFRGVEADINFSLEDYEDDLKQMSNLTKEEFVHVLRRQSTGFPRGSSKYRGVTLHKCGRWEARMGQFLGKKYVYLGLFDTEEEAARAYDRAAIKCNGKDAVTNFDPSIYAGEFEPPAAATGDAAEHNLDLSLGSSAGSKRGNVDGGGDDEITGGGGGGAGSDQRVPMAFDLDWQTAAARSTKAKFDQNSNHPQMPPVLQVTHLPFSPRHHHQFLSNGDPGTAGGLSLTIGAGMAGHWPPQQQQGWGNAGGMSWPHPPHPPPPPTNAAAAATATAAAASSRFPPYIATQASTWLQKNGFHSLTRPT
Protein: Transcription initiation factor TFIID subunit 8 (Protein taube nuss) (TBP-associated factor 43 kDa) (TBP-associated factor 8) (Transcription initiation factor TFIID 43 kDa subunit) (TAFII-43) (TAFII43) (hTAFII43) (Q7Z7C8)
Organism: Homo sapiens (Human)
Function: The TFIID basal transcription factor complex plays a major role in the initiation of RNA polymerase II (Pol II)-dependent transcription. TFIID recognizes and binds promoters with or without a TATA box via its subunit TBP, a TATA-box-binding protein, and promotes assembly of the pre-initiation complex (PIC). The TFIID complex consists of TBP and TBP-associated factors (TAFs), including TAF1, TAF2, TAF3, TAF4, TAF5, TAF6, TAF7, TAF8, TAF9, TAF10, TAF11, TAF12 and TAF13. The TFIID complex structure can be divided into 3 modules TFIID-A, TFIID-B, and TFIID-C. TAF8 is involved in forming the TFIID-B module, together with TAF5. Mediates both basal and activator-dependent transcription. Plays a role in the differentiation of preadipocyte fibroblasts to adipocytes, however, does not seem to play a role in differentiation of myoblasts. Required for the integration of TAF10 in the TAF complex. May be important for survival of cells of the inner cell mass which constitute the pluripotent cell population of the early embryo (By similarity).
Subcellular location: Nucleus {ECO:0000269|PubMed:14580349, ECO:0000269|PubMed:35759269}. Cytoplasm {ECO:0000269|PubMed:35759269}. Note=Predominantly nuclear. {ECO:0000269|PubMed:35759269}.
Interaction partners:
- Transcription initiation factor TFIID subunit 12
- Transcription initiation factor TFIID subunit 10
- Transcription initiation factor TFIID subunit 5
- Transcription initiation factor TFIID subunit 4
- TATA-box-binding protein
- Transcription initiation factor TFIID subunit 11
- Transcription initiation factor TFIID subunit 13
- Transcription initiation factor TFIID subunit 1
- Transcription initiation factor TFIID subunit 7
- Transcription initiation factor TFIID subunit 6
Sequence:
MADAAATAGAGGSGTRSGSKQSTNPADNYHLARRRTLQVVVSSLLTEAGFESAEKASVETLTEMLQSYISEIGRSAKSYCEHTARTQPTLSDIVVTLVEMGFNVDTLPAYAKRSQRMVITAPPVTNQPVTPKALTAGQNRPHPPHIPSHFPEFPDPHTYIKTPTYREPVSDYQVLREKAASQRRDVERALTRFMAKTGETQSLFKDDVSTFPLIAARPFTIPYLTALLPSELEMQQMEETDSSEQDEQTDTENLALHISMEDSGAEKENTSVLQQNPSLSGSRNGEENIIDNPYLRPVKKPKIRRKKSLS
Protein: Uncharacterized protein (Q559I6)
Organism: Dictyostelium discoideum (Social amoeba)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141, ECO:0000256|RuleBase:RU003755}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141, ECO:0000256|RuleBase:RU003755}.
Interaction partners:
- Transmembrane protein
- CBS domain-containing protein
- Uncharacterized protein
- Peptidase M14 family protein
Sequence:
MEGIDNEVFVYGGDENHFPSSIKYIMGNEICERYSYYALRGILTNYLISFMGYSEKNASSIGHGFNAGAYIFSLVGAYVADGVLGKYKTILYFSILYCFGAAIFSITAIPGITGDSPGERSPWGLIVGLTCIAIGTGGIKPVVSSFCGDQFGPHQKKLLQNLFQVFYWCVNLGSFFSSILSPILRTNVGYWCAFVIPAGILIISILIYLVGNKQYVKRKPQGSVLSTAFCIVGTGISESVKKTFRGSKYNDHYYNNSFLDRAKLKYSPRIVEQVKLVLRVLTVFVPLPFFWALYDQTGTRWTIQANSMDRHLGSWEIDSEIINCINPLLVMIFVPIFEYGIYRPLERKKINFTLLRRMGTGMFLSVIAFYISAIIQVHIDNSPPESVHIALQIPQYVVLTAAEVLLSITGLEFAYANSPRSMKSLVIAGWLICVSIGNMFDAFVIELIELPEYVLSLLFGSVMFVFIFIFIIIAYRFKEIDQSVLDELNGDTPMTDDNANANSKELDVVTQKDLSSSSNPIINNNNNNNNSTLGNSIDYGYDHEKSN
Protein: Kinesin-like protein KIF20A (GG10_2) (Mitotic kinesin-like protein 2) (MKlp2) (Rab6-interacting kinesin-like protein) (Rabkinesin-6) (O95235)
Organism: Homo sapiens (Human)
Function: Mitotic kinesin required for chromosome passenger complex (CPC)-mediated cytokinesis. Following phosphorylation by PLK1, involved in recruitment of PLK1 to the central spindle. Interacts with guanosine triphosphate (GTP)-bound forms of RAB6A and RAB6B. May act as a motor required for the retrograde RAB6 regulated transport of Golgi membranes and associated vesicles along microtubules. Has a microtubule plus end-directed motility.
Subcellular location: Golgi apparatus {ECO:0000250}. Cytoplasm, cytoskeleton, spindle {ECO:0000269|PubMed:12939256, ECO:0000269|PubMed:29357359}. Note=Localizes to the spindle midzone during anaphase and telophase. {ECO:0000269|PubMed:29357359}.
Interaction partners:
- Rac GTPase-activating protein 1
- Ras-related protein Rab-6A
- Inner centromere protein
- Chromosome-associated kinesin KIF4A
- Serine/threonine-protein kinase PLK1
- Aurora kinase B
- Cell division cycle protein 20 homolog
- Borealin
- Kinesin-like protein KIF11
- Mitotic checkpoint serine/threonine-protein kinase BUB1 beta
Sequence:
MSQGILSPPAGLLSDDDVVVSPMFESTAADLGSVVRKNLLSDCSVVSTSLEDKQQVPSEDSMEKVKVYLRVRPLLPSELERQEDQGCVRIENVETLVLQAPKDSFALKSNERGIGQATHRFTFSQIFGPEVGQASFFNLTVKEMVKDVLKGQNWLIYTYGVTNSGKTHTIQGTIKDGGILPRSLALIFNSLQGQLHPTPDLKPLLSNEVIWLDSKQIRQEEMKKLSLLNGGLQEEELSTSLKRSVYIESRIGTSTSFDSGIAGLSSISQCTSSSQLDETSHRWAQPDTAPLPVPANIRFSIWISFFEIYNELLYDLLEPPSQQRKRQTLRLCEDQNGNPYVKDLNWIHVQDAEEAWKLLKVGRKNQSFASTHLNQNSSRSHSIFSIRILHLQGEGDIVPKISELSLCDLAGSERCKDQKSGERLKEAGNINTSLHTLGRCIAALRQNQQNRSKQNLVPFRDSKLTRVFQGFFTGRGRSCMIVNVNPCASTYDETLHVAKFSAIASQLVHAPPMQLGFPSLHSFIKEHSLQVSPSLEKGAKADTGLDDDIENEADISMYGKEELLQVVEAMKTLLLKERQEKLQLEMHLRDEICNEMVEQMQQREQWCSEHLDTQKELLEEMYEEKLNILKESLTSFYQEEIQERDEKIEELEALLQEARQQSVAHQQSGSELALRRSQRLAASASTQQLQEVKAKLQQCKAELNSTTEELHKYQKMLEPPPSAKPFTIDVDKKLEEGQKNIRLLRTELQKLGESLQSAERACCHSTGAGKLRQALTTCDDILIKQDQTLAELQNNMVLVKLDLRKKAACIAEQYHTVLKLQGQVSAKKRLGTNQENQQPNQQPPGKKPFLRNLLPRTPTCQSSTDCSPYARILRSRRSPLLKSGPFGKKY
Protein: UPS-like protein C36.10 (O59707)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Required for mitochondrial morphology. May control phospholipid metabolism in the mitochondrial intermembrane space (By similarity).
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16823372}. Mitochondrion inner membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Intermembrane side {ECO:0000250}. Mitochondrion intermembrane space {ECO:0000250}.
Interaction partners:
- Uncharacterized protein C119.18
- Uncharacterized protein C36.11
- Mitochondrial inner membrane protease atp23
- Protein ups1 homolog
Sequence:
MKIFESCHLFQYPFEQVSAAHWQKYPNEHATHVIAVDTLDRKVLDNGVLYTERLITCHQALPRWILKLIDGAQDCYIRETSYVDLKARTLTLLTSNLTFSDRLRVDETVTYSPHPELEATVFQQEARIEALACMKRLSNLIEQWSVDGFGKKASRGKEGFESVLEKINMSVFQTRPFGSSEATA