wanglab/gogpt-training-data huggingface dataset:
Protein: Interferon gamma receptor 1 (A0A2R8YFL3)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MNPIVYWEYQIMPQVPVFTVEVKNYGVKNSEWIDACINISHHYCNISDHVGDPSNSLWVRVKARVGQKESAYAKSEEFAVCRDGKIGPPKLDIRKEEKQIMIDIFHPSVFVNGDEQEVDYDPETTCYIRVYNVYVRMNGSEIQYKILTQKEDDCDEIQCQLAIPVSSLNSQYCVSAEGVLHVWGVTTEKSKEVCITIFNSSIKGSLWIPVVAALLLFLVLSLVFICFYIKKINPLKEKSIILPKSLISVVRSATLETKPESKYVSLITSYQPFSLEKEVVCEEPLSPATVPGMHTEDNPGKVEHTEELSSITEVVTTEENIPDVVPGSHLTPIERESSSPLSSNQSEPGSIALNSYHSRNCSESDHSRNGFDTDSSCLESHSSLSDSEFPPNNKGEIKTEGQELITVIKAPTSFGYDKPHVLVDLLVDDSGKESLIGYRPTEDSKEFS
Protein: Anion exchange protein (G5EC65)
Organism: Caenorhabditis elegans
Subcellular location: Basolateral cell membrane {ECO:0000256|ARBA:ARBA00004554}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004554}. Membrane {ECO:0000256|RuleBase:RU362035}; Multi-pass membrane protein {ECO:0000256|RuleBase:RU362035}.
Interaction partners:
Sequence:
MTHSVRRRMSKARRESQSIELSSLAPGTRVMFLLKEKENTPALFTEMGELNNEEWRETARWVKFEEDVEQGGNRWSKPHVATLSLHSLFQLRSCIMNGHFMNDLAETDIPSIFNAVIENLEKSGDLPSENREELREILLRKHVHQYEQAKKNGAGGEKGGFLSTVRSISDIGKSFSHGKNLSKIEEKPEGPVTSQTAGAPSGSSNQLTLPTVESVPKDISSEESSKGNLHFLKKLPAGVEASNVLIGEVDFLTRHICCFIRLKNANQLGDLTEVPVPTRFIFLLLGPTGHGQQYREIGRAIATLMADEIFHDVAYGARDVDDLLDGIDEFLDQVTVLPPGEWDPNIRIEPPSKLPSQEKRKQIGQELLVEPSSHKHVKKVVEEEEIHSHGDDPALKRTGKLFGGLILDIKRKAPHFVSDFTDAFNLQCLASICFMYFGLLAPIVTFGGLLEEATHQRMAAMENLFGGALCGVIYHFFAGQPLTIVGSTGPVLVFETIVFDFCHRFGIVYLSFRFWVHVWTAVIIFLMVVTDASALVSFITRFTEESFATLIAVIFIYEAIMKLVKIKGQLDMINYSRDFVEGGFCSCVPPIGKPSVSPDHARLVIKSTGLPIAFNDTFIDYTAANLTDCRTIGGSFDGTTCFPLYDKLLMSILLTVGTFFLATTLKKMRNSCYFPSSVRQLLSDFAVMIAIASMTFVDIFVGVNTPKLNVPSTFRPTWEGRGWFIPPFDANEWWTAPLAILPALLACILIFMDQQITTVIVNRKENKLKKGCGYHLDLLVLSVSILMVGFLGLPIYVAATVLSINHINSLKVESECKAPGEVAQFVGVREQRVTGIVTFLIIGLSVLATNILGRIPMPVLYGVFLYMGISALGGIQLFDRTLLLFMPMKYQPDTIYIRHVPIRKIHLFTAFQIGCLALLWVIKSIKSTSILFPIMLVVMVAIRKMMEKAFTTTDLKYLDDPMPDFHLRKKEDAKRRQSEGEAVEIEFDNENQATIHAVKTEAHLHIPMASGNVIKIPLAAIQEPSHSINLTKEVNNSGMWKHITSVDSKNSLVRDVPASSDPTSSRDAPIEQPEDDDDPIMIKVIRPSPHTSTSNLTTENTPLLKDEEPPKTNPDEPKV
Protein: Agglutinin-like protein 4 (Adhesin 4) (A0A1D8PQB9)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Function: Cell surface adhesion protein which mediates both yeast-to-host tissue adherence and yeast aggregation. Plays an important role in the pathogenesis of C.albicans infections.
Subcellular location: Cell membrane; Lipid-anchor, GPI-anchor {ECO:0000305|PubMed:12845604}. Secreted, cell wall {ECO:0000269|PubMed:22106872}. Note=Identified as covalently-linked GPI-modified cell wall protein (GPI-CWP) in the outer cell wall layer (Probable). Covers the surface of yeast-form cells (PubMed:22106872). {ECO:0000269|PubMed:22106872, ECO:0000305|PubMed:12845604}.
Interaction partners:
Sequence:
MLLQFLLLSLCVSVATAKVITGIFDSFNSLTWTNAASYSYRGPANPTWTAVIGWSLDGATASAGDTFTLDMPCVFKFITDQTSIDLVADGRTYATCNLNSAEEFTTFSSVSCTVTTTMTADTKAIGTVTLPFSFSVGGSGSDVDLANSQCFTAGINTVTFNDGDTSISTTVDFEKSTVASSDRILLSRILPSLSQAVSLFLPQECANGYTSGTMGFSTAGTGATIDCSTVHVGISNGLNDWNYPISSESFSYTKTCTSTSVLVTYQNVPAGYRPFVDAYVSATRVSSYAMRYTNIYACVGAASVDDSFTHTWSGYSNSQAGSNGITIVVTTRTVTDSTTAVTTLPFNSESDKTKTIEILQPIPTTTITTSYVGVTTSYSTKTAPIGETATVIVDVPYHTTTTVTSEWTGTITTTTTRTNPTDSIDTVVVQVPSPNPTVTTTEYWSQSYATTTTVTAPPGGTDSVIIREPPNPTVTTTEYWSQSYATTTTVTAPPGGTDSVIIREPPNPTVTTTEYWSQSYATTTTVTAPPGGTDSVIIREPPNPTVTTTEYWSQSYATTTTVTAPPGGTDSVIIREPPNPTVTTTEYWSQSYATTTTVTAPPGGTDSVIIREPPNPTVTTTEYWSQSFATTTTVTAPPGGTDSVIIREPPNPTVTTTEYWSQSFATTTTVTAPPGGTDSVIIREPPNPTVTTTEYWSQSYATTTTVTAPPGGTDSVIIREPPNPTVTTTEYWSQSFATTTTVTAPPGGTDSVIIREPPNPTVTTTEYWSQSFATTTTVTAPPGGTDSVIIREPPNPTVTTTEYWSQSYATTTTVTAPPGGTDTVIIREPPNYTVTTTEYWSQSYATTTTVTGPPGGTDTVIIREPPNPTVTTTEYWSQSYATTTTVTSPPGGTDIVIIREPPNPTVTTTEYWSQSYATTTTVTAPPGGTDSVIIREPPNPTVTTTEYWSQSYATTTTVTAPPGGTDSVIIREPPNPTVTTTEYWSQSYATTTTVTAPPGGTDSVIIREPPNPTVTTTEYWSQSFATTTTVTAPPGGTDSVIIREPPNPTVTTTEYWSQSYATTTTVTAPPGGTDTVIIREPPNYTVTTTEYWSQSYATTTTVTGPPGGTDTVIIREPPNPTVTTTEYWSQSYATTTTVTSPPGGTDIVIIREPPNPTVTTTEYWSQSFATTTTVTAPPGGTDSVIIREPPNPTVTTTEYWSQSYATTTTVTAPPGGTDSVIIREPPNPTVTTTEYWSQSYATTTTVTAPPGGTDTVIIREPPNPTVTTTEYWSQSYATTTTVTAPPGGTDSVIIREPPNPTVTTTEYWSQSYATTTTVTAPPGGTDTVIIREPPNYTVTTTEYWSQSYATTTTVTAPPGGTDTVIIREPPSPTVTTTEYWSQSYATTTTVTAPPGGTATVIIKEPPNYTVTTTEYWSQSYATTTTITAPPGGTDTVIIREPPNYTVTTTEYWSQSYATTTTVTAPPGGTDTVIIREPPNYTVTTTEYWSQSYATTTTVTGPPGGTDTVIIREPPSPTVTTTEYWSQSYATTTTVTAPPGGTATVIIREPPNYTVTTTEYWSQSYATTTTITAPPGGTDTVIIREPPNYTVTTTEYWSQSYATTTTVTGPPGGTDTVIIREPPNYTVTTTEYWSQSYATTTTVTGPPGGTDTVIIREPPNYTVTTTEYWSQSYATTTTVTGPPGGTDTVIIREPPNPTVTTTEYWSQSYATTLTITAPPGGTNSVIIRVHSSTNDESSESTFSTLSVPSFSGSISIVSTVSRPHYVNSTVTHLPSSSSKPVDIPSSDVVTSTNDNSLTSLTGSENGKTSVAISTTFCDDENGCQTSIPQGSVVRTTATTTATTTTIIGDNNGSGKSKSGELSSTGSVTTNTATPDVPSTKVPSNPGAPGTGVPPPLAPSTETQTTNNVPGSPNIPATGTTDIIRESTTVSHTVTGNGNTGVPMNPNPVLTTSTSLTGATNSATNPSHETSVNTGSGGSTNIVTPPSSATATVVIPGTDNGATTKGQDTAGGGNSNGSTATTNIQGGNNEPGNQPGTNTTGEPVGTTDTQSVESISQPTTLSQQTTSSLISTPLASTFDGSGSIVQHSGWLYVLLTAISIFF
Protein: Tripartite motif-containing protein 2 (EC 2.3.2.27) (E3 ubiquitin-protein ligase TRIM2) (RING-type E3 ubiquitin transferase TRIM2) (Q58ER5)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
Sequence:
MATDASTLPSPVVRQIDKQFLICSICLDRYNNPKVLPCLHTFCERCLQNYIPPHSLTLSCPVCRQTSILPEKGVAALQSNFFITNLMEVLKKSPNSNLSEDYTDAINGVATGQPLSCPNHGGNVMEFYCPPCETAMCEECTSGEHAEHATVPLKDVLEQHKASLQEQLDAVKNRLPEIESALEVLSEILQQLSSQKSSIEEMIHATFEELQKTLNVRKSVLLMELEVNYGLKQKVLQTQLESLLQGQDGIRSSCSFTEQALNHGSEAEVLLVKKQMSERLDELANQELPLRPEENNQLDFLVETDGLRKSIHNLGAIVTTNAVAAETVATGEGLRHCIVGQLTSVTVTTKDRDGGLCRTGNALLIADLSAIDGSIVGEGKVTDHKNGTYEFVYSVPCEGRFTLTLKLYDQHIRGSPFSIRANKPTDISLTADVDKKRLKSPGNSHVKQRAIKRPASMYSTGKRKENPIEDDLIFRIGTKGRNKGEFTNLQGVAASSVGKVLIADSNNQCVQIFLNDGQFKGRFGIRGRSPGQLQRPTGVAVHPSGDIIIADYDNKWVSIFSSDGKFKSKIGSGKLMGPKGVSVDRNGHIIVVDNKSCCVFIFQPNGKLVSKFGNRGNSDKQFAGPHFAAVNQNNEVIVTDFHNHSVKVFSPEGEFILKFGSNGEGNGQFNAPTGVAVDANGNIIVADWGNSRIQVFDSSGSFLSYINTSADPLYGPQGLALTSDGHVVVADSGNHCFKVYRYLQ
Protein: Delta-6 fatty acid desaturase, putative (Q38AQ3)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MSSVKSKGSSCSTADVVRIDGIYYDTAKLAAIHCGGPTMVNMANGTDCTRVFLSYHRRRFPHEKYKSLQVSPSDVLDGAVTDEPDTTNFDKYLDLCSLIRPVIAPTGGFAPWHYFIKTLFWCSLVFFLDIYAIFAFRSLYLTIIQSLAMAMVGLNVQHDANHGAISRYPLINTIFGLTQDILGGSRISWIIHHDFIHHVYTNEPHHDLDLDIPLLRLHRFVPKRLCYAFQHIYFLLLEAVFGPVHVISSMKFVWQGPTTKQRFLQREWTMSRILTLIPPLRLALNILHAPTLLHALISTFLQYAIGGMYLAFFFLISHNFHGVRKDGTEVGECFVKAQVETSSSVGGWWLAQLNGGLNYQIEHHLFPRVHHSYYHYLAPIVRDYCTKLGISYTRFDTVLDNVVSTSKHLAQFGKGIEDKRL
Protein: 6-hydroxytryprostatin B O-methyltransferase (EC 2.1.1.293) (Fumitremorgin biosynthesis protein D) (B9WZX2)
Organism: Aspergillus fumigatus (Neosartorya fumigata)
Function: 6-hydroxytryprostatin B O-methyltransferase; part of the gene cluster that mediates the biosynthesis of fumitremorgins, indole alkaloids that carry not only intriguing chemical structures, but also interesting biological and pharmacological activities. The biosynthesis of fumitremorgin-type alkaloids begins by condensation of the two amino acids L-tryptophan and L-proline to brevianamide F, catalyzed by the non-ribosomal peptide synthetase ftmA. Brevianamide F is then prenylated by the prenyltransferase ftmPT1/ftmB in the presence of dimethylallyl diphosphate, resulting in the formation of tryprostatin B. The three cytochrome P450 monooxygenases, ftmP450-1/ftmC, ftmP450-2/ftmE and ftmP450-3/FtmG, are responsible for the conversion of tryprostatin B to 6-hydroxytryprostatin B, tryprostatin A to fumitremorgin C and fumitremorgin C to 12,13-dihydroxyfumitremorgin C, respectively. The putative methyltransferase ftmMT/ftmD is expected for the conversion of 6-hydroxytryprostatin B to tryprostatin A (Probable). FtmPT2/FtmH catalyzes the prenylation of 12,13-dihydroxyfumitre-morgin C in the presence of dimethylallyl diphosphate, resulting in the formation of fumitremorgin B. Fumitremorgin B is further converted to verruculogen by ftmOx1/ftmF via the insertion of an endoperoxide bond between the two prenyl moieties. In some fungal species, verruculogen is further converted to fumitremorgin A, but the enzymes involved in this step have not been identified yet (Probable).
Interaction partners:
Sequence:
MTQAVDIGTIQTLIRLEVPDQVPLTGSIPYDALVKKLKTPVDPELLQRLIRFTRLVGFLDEDAEGAVKHSPMSAIFVNDPDTAGQARFMADFGIRPCSFIYESIKLDPSGEAARQGPLALMAREPGAREGPTFFEVLEKDPVNRKRWHDGMAVHNDSMVRHVAGAYDWGTVQSLVDIGGSEGHVAAVIVNAFPHIQITVQDRPEIIEKARQRGDRHPNIIFEEHDFFTPQPRIADAYFLRLILHDWNDADCTRIVRQISSALRPGARLLIMDAVLPEPGEGSLQSERRLRRSDIGMYTLFSAKERSLAQMRRLVEDCDSRLRFEKLYTPPGSHASMLSWICE
Protein: Pyruvate dehydrogenase E1 component subunit alpha, mitochondrial (PDHE1-A) (EC 1.2.4.1) (Q10489)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: The pyruvate dehydrogenase complex catalyzes the overall conversion of pyruvate to acetyl-CoA and CO(2). It contains multiple copies of three enzymatic components: pyruvate dehydrogenase (E1), dihydrolipoamide acetyltransferase (E2) and lipoamide dehydrogenase (E3).
Subcellular location: Mitochondrion matrix {ECO:0000250}.
Interaction partners:
- Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex, mitochondrial
- Pyruvate dehydrogenase E1 component subunit beta, mitochondrial
- Dihydrolipoyl dehydrogenase, mitochondrial
- Probable pyruvate dehydrogenase protein X component, mitochondrial
- Glucose-6-phosphate isomerase
- Pyruvate kinase
- Pyruvate carboxylase
- Putative pyruvate decarboxylase C13A11.06
- 2-oxoglutarate dehydrogenase, mitochondrial
- NAD-dependent malic enzyme
Sequence:
MFRTCTKIGTVPKVLVNQKGLIDGLRRVTTDATTSRANPAHVPEEHDKPFPVKLDDSVFEGYKIDVPSTEIEVTKGELLGLYEKMVTIRRLELACDALYKAKKIRGFCHLSIGQEAVAAGIEGAITLDDSIITSYRCHGFAYTRGLSIRSIIGELMGRQCGASKGKGGSMHIFAKNFYGGNGIVGAQIPLGAGIGFAQKYLEKPTTTFALYGDGASNQGQAFEAFNMAKLWGLPVIFACENNKYGMGTSAERSSAMTEFYKRGQYIPGLLVNGMDVLAVLQASKFAKKYTVENSQPLLMEFVTYRYGGHSMSDPGTTYRSREEVQKVRAARDPIEGLKKHIMEWGVANANELKNIEKRIRGMVDEEVRIAEESPFPDPIEESLFSDVYVAGTEPAYARGRNSLEYHQYK
Protein: Multiple organellar RNA editing factor 7, mitochondrial (RNA editing-interacting protein 7) (Q9CAH0)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Involved in organellar RNA editing. Required for the processing of few RNA editing sites in mitochondria.
Subcellular location: Mitochondrion {ECO:0000269|PubMed:25583991}.
Interaction partners:
- Protoporphyrinogen oxidase 1, chloroplastic
Sequence:
MARIIRRPLNLTAAVRFRLSPLSPFSGNSGSINSETTSWSELIRVPSLVEGCDYKHWLVLMKPPNGYPTRNHIVQSFVETLAMALGSEEEAKRSIYSVSTKYYYAFGCRIHEPLTYKIRSLPDVKWVLPDSFIVDGDNRYGGEPFVDGEVVPYDEKYHADWLRDQTDEDAKSGVVKKKHRRKRKKKLI
Protein: Tumor necrosis factor receptor superfamily member 1B (Tumor necrosis factor receptor 2) (TNF-R2) (Tumor necrosis factor receptor type II) (TNF-RII) (TNFR-II) (p75) (p80 TNF-alpha receptor) (CD antigen CD120b) (P25119)
Organism: Mus musculus (Mouse)
Function: Receptor with high affinity for TNFSF2/TNF-alpha and approximately 5-fold lower affinity for homotrimeric TNFSF1/lymphotoxin-alpha. The TRAF1/TRAF2 complex recruits the apoptotic suppressors BIRC2 and BIRC3 to TNFRSF1B/TNFR2 (By similarity).
Subcellular location: Membrane; Single-pass type I membrane protein.
Interaction partners:
- Lymphotoxin-alpha
- Tumor necrosis factor
- TNF receptor-associated factor 2
- Tumor necrosis factor receptor superfamily member 1A
- TNF receptor-associated factor 1
- Death domain-associated protein 6
- Disabled homolog 2-interacting protein
- Keratin, type I cytoskeletal 18
- Baculoviral IAP repeat-containing protein 3
- TNF receptor-associated factor 3
Sequence:
MAPAALWVALVFELQLWATGHTVPAQVVLTPYKPEPGYECQISQEYYDRKAQMCCAKCPPGQYVKHFCNKTSDTVCADCEASMYTQVWNQFRTCLSCSSSCTTDQVEIRACTKQQNRVCACEAGRYCALKTHSGSCRQCMRLSKCGPGFGVASSRAPNGNVLCKACAPGTFSDTTSSTDVCRPHRICSILAIPGNASTDAVCAPESPTLSAIPRTLYVSQPEPTRSQPLDQEPGPSQTPSILTSLGSTPIIEQSTKGGISLPIGLIVGVTSLGLLMLGLVNCIILVQRKKKPSCLQRDAKVPHVPDEKSQDAVGLEQQHLLTTAPSSSSSSLESSASAGDRRAPPGGHPQARVMAEAQGFQEARASSRISDSSHGSHGTHVNVTCIVNVCSSSDHSSQCSSQASATVGDPDAKPSASPKDEQVPFSQEECPSQSPCETTETLQSHEKPLPLGVPDMGMKPSQAGWFDQIAVKVA
Protein: Putrescine N-methyltransferase 4 (NtPMT4) (EC 2.1.1.53) (Q9SEH4)
Organism: Nicotiana tabacum (Common tobacco)
Function: Involved in the biosynthesis of pyridine alkaloid natural products, leading mainly to the production of anabasine, anatabine, nicotine and nornicotine, effective deterrents against herbivores with antiparasitic and pesticide properties (neurotoxins); nornicotine serves as the precursor in the synthesis of the carcinogen compound N'-nitrosonornicotine (NNN). Methyltransferase that mediates the conversion of putrescine to N-methylputrescine. Promotes leaves ripening.
Interaction partners:
- Uridine 5'-monophosphate synthase.
- Arginase 1
- Arginase 1, mitochondrial-like
- arginase
Sequence:
MEVISTNTNGSTIFKNGAIPMNGHQSGTSKHLNGYQNGTSKHQNGHHNGTSEHRNGHQNGISEHQNGHQNGTSEQQNGTISHDNGNELLGNSNSIKLGWFSEFSALWPGEAFSLKVEKLLFQGKSDYQDVMLFESATYGKVLTLDGAIQHTENGGFPYTEMIVHLPLGSIPNPKKVLIIGGGIGFTLFEMLRYPTIEKIDIVEIDDVVVDVSRKSFPYLAANFNDPRVTLVLGDGAAFVKAAQAGYYDAIIVDSSDPIGPAKDLFERPFFEAVAKALRPGGVVCTQAESIWLHMHIIKQIIANCRQVFKGSVNYAWTTVPTYPTGVIGYMLCSTEGPEVDFKNPINPIDKETTQVKSKLAPLKFYNSDIHKAAFILPSFARSMIES
Protein: non-specific serine/threonine protein kinase (EC 2.7.11.1) (Q8I3C3)
Organism: Plasmodium falciparum (isolate 3D7)
Interaction partners:
- Protein phosphatase PPM5, putative
Sequence:
MEFLYFIFQVLSLIRINQNTVFYRSLKKCRYLSEIIIENVTSTKLYSDDCYDKNGVINDNNYVLKNTYDEYESYKRIKKIKQCKNILKENKLSESILPESTLPESTLPESTLAESTLAESTLAESTLAESEFSKYKLSNDTINENLESHLYLNSSPSTSHSMYYHDSKCNENINESNNATNELMEKSVSIKYPIYNWELGKACLSKYLGHSNNYFLNGVKFDEWKLVSFRDRYYNERKGRVHKILKTKITGNDGNNKRELKLFIKRIPIDMWLKQFEMMDTYNGEYIICAENFVMEAIVLSFLSAYHPGIGPKFYKLLFNPDNYYIDENNSSMNNINDISLFNKLLSDRLRMNMSGYILMVSESFGEDLETYLCTVNNKKIFKSRKKNKKKLLFESLKLINKLHQAGICHLDFTLDNILISKNGDMRLCDFAKCTPMYSYYLRHTKKMDSLCLFQSCITTIGKYMYVPPECWDVEKRYVEVGTKFPFEYLQEITDEEERKKYYFDVSCADKYMLGIVFIAIWNNSYLWYISDPIIDINYLKYKKCNMNFNKIWTTLFWPKKLKRILRQLLDLDRRKNLNLNDLINDPWFTR
Protein: Transcription factor KUA1 (Myb-related protein H) (AtMYBH) (AtMYBS3) (MYBS3-homolog protein) (Protein KUODA1) (Q9LVS0)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Transcriptional repressor. Direct regulator of the transcription of peroxidase (Prxs) and reactive oxygen species (ROS)-related genes via the recognition of 5'-ATCACA-3' motif. Binds to 5'-TATCCA-3' motif (TA box) and represses the activity of corresponding promoters (e.g. sugar response genes). Regulates hypocotyl elongation in response to darkness by enhancing auxin accumulation in a phytochrome-interacting factor (PIF) proteins-dependent manner. Promotes lateral roots formation. Promotes cell expansion during leaves development via the modulation of cell wall-located Prxs. Plays a critical role in developmentally regulated and dark-induced onset of leaf senescence by repressing the transcription of several genes involved in chloroplast function and responses to light and auxin. Promotes responses to auxin, abscisic acid (ABA), and ethylene.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00625, ECO:0000269|PubMed:23888064, ECO:0000269|PubMed:24806884}.
Interaction partners:
- Protein REVEILLE 7
- Mediator of RNA polymerase II transcription subunit 7b
Sequence:
MTRRCSHCNHNGHNSRTCPNRGVKLFGVRLTEGSIRKSASMGNLSHYTGSGSGGHGTGSNTPGSPGDVPDHVAGDGYASEDFVAGSSSSRERKKGTPWTEEEHRMFLLGLQKLGKGDWRGISRNYVTTRTPTQVASHAQKYFIRQSNVSRRKRRSSLFDMVPDEVGDIPMDLQEPEEDNIPVETEMQGADSIHQTLAPSSLHAPSILEIEECESMDSTNSTTGEPTATAAAASSSSRLEETTQLQSQLQPQPQLPGSFPILYPTYFSPYYPFPFPIWPAGYVPEPPKKEETHEILRPTAVHSKAPINVDELLGMSKLSLAESNKHGESDQSLSLKLGGGSSSRQSAFHPNPSSDSSDIKSVIHAL
Protein: Protein transport protein SEC23 (Q38AJ0)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Subcellular location: Cytoplasmic vesicle, COPII-coated vesicle membrane {ECO:0000256|RuleBase:RU365030}; Peripheral membrane protein {ECO:0000256|RuleBase:RU365030}; Cytoplasmic side {ECO:0000256|RuleBase:RU365030}. Endoplasmic reticulum membrane {ECO:0000256|RuleBase:RU365030}; Peripheral membrane protein {ECO:0000256|RuleBase:RU365030}; Cytoplasmic side {ECO:0000256|RuleBase:RU365030}.
Interaction partners:
- Protein transport protein Sec31, putative
- Protein transport protein Sec24C, putative
- Protein transport protein Sec13, putative
- ADP-ribosylation factor, putative
- Protein transport protein Sec24A, putative
- Protein transport protein sec13, putative
- Sec16 Sec23-binding domain-containing protein
- Longin domain-containing protein
- Synaptobrevin-type vesicle transport protein, putative
- Golgi reassembly stacking protein
Sequence:
MDQYGIPQQMPEEQVFECDPIRWSWGLYPSNRIDAARMVVPLGCVYAPIETPCIELSSEPLRCVCGGIVNPYCSIDFRSKMWGCPLCGKENSFPPHYAYMAGNDLPQELLRGNETVEYVSFADRNPPTFAFVVDTCVDTELELFGLREFVGCAFNKIPEGAFVCLITYGATVQIHELSGVTDYPRSLVFRGSQEATVETLKGVITDAQRFYGTRASLQQTMDSIFQELQQDLWPVRKAHRPLRCTGAALSVASAFLEMVSPNTGSCILAFISGICTEGPGIAVETTREKFIRQHADIRDGTAAAAFWDSSCAFYDKLMQRIVKNGHSLSCFTASLDQTGVAEMKLCIQASGGVILNDESWRKETLRQSLDRFFERREDGSLKMALNVTMDIITSPSWKVMGVIGQCVGTGKKSSSVADSEIGMGGTCQWTACMMDSTTNFAIYFDTMTVPEAQKQPFRYVQFVTKYEIGRETRVRVCTRKHVVQQVTSMPELAASFDQETAAVLLAREALHRADTAPLFDVLRWLDRTIVRLVNRFGTYIKDQPSSLSLPQEFVFFPAFMFHLRRSGYLHVFNSSPDETTILRLMLLKSSVQDSIIQIQPTLYSYRMDAPPQPVSLDSAAIQPDNILLLDTFFEVLVHLGSTIAAWKKAGYAEQEEYANFKEFLQYPVDDAARLVGGRYPTPRFIYVCQDDPDARILRNRINPSRSYGSDGGRGYGGSEEELVYTDDASLSVFIDHLKRLAVSQ
Protein: OPT peptide transporter Mtd1, putative (Q4WAD5)
Organism: Aspergillus fumigatus (strain ATCC MYA-4609 / CBS 101355 / FGSC A1100 / Af293) (Neosartorya fumigata)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
Sequence:
MDDKNRSAVDQGIDAAEPYKIGVEKEAKDVAQETESPESPGSQPDHAEYVKGHPVIRKGTDVSRFIVSVRDDGDPALTFRSIVLGSAFTALSSVITMLYTFKPTQMQVSAIFIQLLVYVVGLAWALFTPRPDRFRWKWLRRTLEFLNFGQPFGIKEHVVASLIASSGNNGLSGVEVYAVERLFYNISVSATTAVLGTFSISLCGFVLAGVLRPLIVYPAEMVYWSTLPQVVLYQTLHFDQRANRGRLIKFGCALGLAAVWEIFPAYIITWFGGFSIFCLASMGAPQHTRKIFSRVFGGSSSNEGLGLLNFGFDWQYIQSSYLSLPLKQQLNSWIGYVIFYPAMLGLYYRNTWSAKSFPFMSTSLFTSNGKQFSTTSILSDRGTVDYNKLKEVGIPYLTSSTVWGYLTQNLAIGALITHVLIFYGKDMYTAWKQARSRTQPDPHFQAMLKYKEVPMWWYLALFVLAFFAGLIVNIKGETTLPAWGYIVSLLLGAFIAPFSCILYGLYGTGVATNQLSKMVAGAVHPGRPLANLYFASWSHQVILLSVNLANWLKVGQYTKVPHRIMFATQIYGTLLGAGLNYAVMTTIVTNQREILLDPAGNSVWSGSTVQSLNSQAITWALARDVYGVNGRYLIVPLGLVIGLALPVVHWGLNRVFPRMRSWPLNTAIIASYAGQTYYGITSWIWSSVAVGVFSQVWLRRRLPRIYNEYNYLIGAALDGGSQIVIFILSFAVFGASGKEHPFPTWWGNPAGNPDHCI
Protein: Uncharacterized protein P4H10.18c (Q9P7D1)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Subcellular location: Mitochondrion {ECO:0000269|PubMed:16823372}.
Interaction partners:
- Large ribosomal subunit protein uL4m
- NAD-dependent malic enzyme
- Small ribosomal subunit protein uS4m
- Uncharacterized protein C106.19
- Aconitase-ribosomal protein bL21m fusion protein
- ADP,ATP carrier protein
Sequence:
MVASLIKRAKATSLRSLFQKNEMNFQSIRFNIHQFSTQPALRSEGSELIFGGRSFDSLLSSIKETMEEKKKKSSSFEKRDKRRVQLKEKSPLRTPRNRTQIIDARSTRKDTENESLRKNNFKRRTQFAFTGRATKSNAGVMDVQSPSTMSTSKNNVRNAERPASKKPVFGSKKYFDVINDSNVENKEETKDRNLDRALSKFTQSREKNEQNLSSKASVLRNKKSILLKKRNQDETQLTTEEDFSANNDSTAKIETSIHDHRDISRITPFELPFVNPKLFASFTPMSVALPAGRLLLIKQLQEKSTQSSSMTGLK
Protein: Transcription factor HES-4-A (Hairy and enhancer of split 4-A) (Protein hairy-2) (Xhairy2) (Protein hairy-2a) (Xhairy2a) (Q90Z12)
Organism: Xenopus laevis (African clawed frog)
Function: Transcriptional repressor. Binds DNA on N-box motifs: 5'-CACNAG-3'. Plays a role in the patterning of tissue boundaries. Promotes floor plate development and prechordal plate development. Required for lens development as early as the stage of lens field formation, partly through regulation of gene expression of the cell cycle inhibitor cdknx/p27(xic1). A role in neural crest development is disputed.
Subcellular location: Nucleus {ECO:0000250|UniProtKB:P14003, ECO:0000255|PROSITE-ProRule:PRU00380, ECO:0000255|PROSITE-ProRule:PRU00981}.
Interaction partners:
Sequence:
MPADTMEKPTASPIAGAPANSAQTPDKPKSASEHRKSSKPIMEKRRRARINESLGQLKTLILDALKKDSSRHSKLEKADILEMTVKHLRNLQRVQMTAALTSDPSVLGKYRAGFNECTNEVTRFLSTCEGVNTEVRTRLLGHLSSCLGQIVAMNYQQPPSSQQPLHVQLPSSTPAPMPISCKVNPAEAISPKVFQGGFQLVPATDGQFAFLIPNPAYTSSPGPVIPLYANANVTSPGGRQSQSPVQGLTTFGHKMPHMAQAVSPLGGSTGADSAESVWRPW
Protein: Probable E3 ubiquitin-protein ligase ARI12 (EC 2.3.2.31) (ARIADNE-like protein ARI12) (Protein ariadne homolog 12) (RING-type E3 ubiquitin transferase ARI12) (Q84RQ9)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Might act as an E3 ubiquitin-protein ligase, or as part of E3 complex, which accepts ubiquitin from specific E2 ubiquitin-conjugating enzymes and then transfers it to substrates.
Interaction partners:
- Ubiquitin-conjugating enzyme E2 11
- Transcription factor HY5-like
- Tubulin beta-9 chain
Sequence:
MDNNSVIGSEVDAEADESYVNAALEDGQTGKKSVQRNYATVLTEEDIRALMEIDVQSVSDFTSLSKAEATLLLSHLRWNVDCICKQWSAGAQSVRDSVGLLELDPPSDDNEYFCGACGESHPHKNLASVSCGHRICTRCWTSHINKIISEKPAAEWNLWLKCPVRVGLHASCPASVGLDTIERFASKREKFNYNQYLLRSYVDNRETMKWHPIQGSRCAIDLSPGSGNASVSCHRLVRFCWNCREDAHSPVDCKTAAKWLLENAVPCPKCKLRIPRNQDNSLKMKCLPCNYVFCWFCHVDWIEDMEGTGGDLHFCTFDAVLSDQRGKMSESDSNRYEDCYENWDSNELLMQKEQANLPKLDTIIQELSNTQLENVSQLKFILEAGLQIIECRRVLEWTYVYGYYLREDEVGKQNLLKDTQERLKKFVENLKHCLETNLQPFRYEEEPSKDFNAFRIKLTELTSLTRNHYENVVKDVENGLASVVSEGEASGSGRNQ
Protein: Protein SPEAR3 (SPL-like, EAR-containing protein 3) (TCP interactor containing EAR motif protein 1) (Q6IDB0)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Transcriptional regulator of leaf development. Acts as an adapter-like transcriptional repressor recruiting TPL/TPR corepressors to inhibit the CIN-like TCP transcription factors.
Subcellular location: Nucleus {ECO:0000269|PubMed:23444332}.
Interaction partners:
- Protein SPEAR2
- Protein SPEAR4
- Protein TOPLESS
- ARMADILLO BTB ARABIDOPSIS PROTEIN 1
- Transcription factor TCP17
- Transcription factor TCP24
- Transcription factor TCP10
- Transcription factor TCP3
- Transcription factor TCP12
- Transcription factor TCP4
Sequence:
MGSSFFGRPKMGGSSSSSPTSSSSSPAKRGKNKNGSDKPKQPQRGLGVAQLEKIRLHGEYNCNSFNTYPSYHPSTYQEDVRIQGGYPSIPSSSPSFSYASSSPPPAPYGFHPNMMMNANNDQYERTTIRYGDSQPHRAPSWNPSYGILESQHFVEPNTTRHFLHEDQRNISLGSGIQNFETSEANELDLELRL
Protein: EG:114E2.2 protein (O46042)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MGNSVTPASNTTSLPTSTPSVTTSPPASTDFMLLAAAATSATSATPATATSAAATAASNPAKRKLGSIAEIPSKFLVVSDAKGVYSAHTHPNGFAADSLGVDNNETMIKKLMQNLQSQRQQQSLQQLRSLRPAEISLTPPPAATRKVDISNSRTRSYSLSNVSAARDQQDHPQHQQHANHMQIQQHYGYMRSNIGGVIYGLHKDSADSAASSACGAGAGAAAVGMSIASSAPAAGSQLSAHHHTGHGGRRRTTSSNSNGAGTREVHNKLEKERRAQLKECYDLLKKVLPMGDEDRKKTSNLTILDTAHKYVNSLSHEVCEQEAKIEKLAKQKIELQKRLKQLSLRRESPPTDQQIIPQADKVCLATTATTAPPTAASGHNGTTILFDAGNACATGQQLTTVINKTNGGATAAASSKHNGNHTGGATTTLTPAMGIMTIKNGNGSNGNMLAISPTGGHNHQLHQHHNGSPAGSPSGIGATTGATITRGSPTPSTPSPSPSSSSSGVSLSTSFMGGSSSSSSSSSSSSSSSSSSSSSSPTQQQQIITPTATARSVGLKFHGGAGAAVPAGGGSVNGKRGSTRFH
Protein: Prohibitin (Q4QEK4)
Organism: Leishmania major
Subcellular location: Mitochondrion inner membrane {ECO:0000256|RuleBase:RU366048}.
Interaction partners:
- Prohibitin
- Stomatin-like protein
- 14-3-3 protein I
- Metallo-peptidase, Clan MA
- Putative ATP-dependent zinc metallopeptidase
- Putative ATP-dependent zinc metallopeptidase
- Putative ATP-dependent zinc metallopeptidase
- Putative ATP-dependent zinc metallopeptidase
- 14-3-3 protein II
- Metallo-peptidase, Clan MA
Sequence:
MSKLLQKVAIGAMAAGLSVYSCCFVVYPGEACILYNKISGLKDSVYGEGLQGRIIGLDEILRFNVRVRPRTLHTMTGTKDLQMVNVRLRVLFRPMADRLPQIYRTFGLDYDERILPSVSNEILKAVVAEYKAEELIQKRDAVSARIYQLMQEKVNQFGLIIEDLSLVDIQFGADFMTAVEQKQVAQQEAERYRYVVMENEQKRRAAVVRAEGEAESARLISEAIQKSGSGLLELRRIEAAVEVANQIVPMQNVTFVPKDANMLMNMSR
Protein: Cyclin-dependent kinase inhibitor 1B (Cyclin-dependent kinase inhibitor p27) (p27Kip1) (Q96TE0)
Organism: Homo sapiens (Human)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}. Endosome {ECO:0000256|ARBA:ARBA00004177}. Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MSNVRVSNGSPSLERMDARQADHPKPSACRNLFGPVDHEELTRDLEKHCRDMEEASQRKWNFDFQNHKPLEGKYEWQEVEKGSLPEFYYRPPRPPKGACKVPAQESQDGSGSRPAAPLIGAPANSEDTHLVDPKTDPSDSQTGLAEQCAGIRKRPATDDSSTQNKRANRTEENVSDGSPNAGSVEQTPKKPGLRRRQT