wanglab/gogpt-training-data huggingface dataset:
Protein: Cytochrome c-type biogenesis ccda-like chloroplastic protein (Cytochrome b6f biogenesis protein CCDA) (Q9M5P3)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Required for the transfer of reducing equivalents from stroma to thylakoid lumen. Involved in the biogenesis of the plastid cytochrome b6f complex by probably transferring reducing equivalents from stromal m-type thioredoxin (Trx-m) to the lumenal thioredoxin HCF164.
Subcellular location: Plastid, chloroplast thylakoid membrane {ECO:0000269|PubMed:15159384, ECO:0000269|PubMed:20214498}; Multi-pass membrane protein {ECO:0000269|PubMed:15159384, ECO:0000269|PubMed:20214498}.
Interaction partners:
- Thioredoxin-like protein HCF164, chloroplastic
- Cytochrome c biogenesis protein CcsA
- Cytochrome c biogenesis protein CCS1, chloroplastic
- Thiol-disulfide oxidoreductase LTO1
- Cytochrome c-type biogenesis CcmH-like mitochondrial protein
- Protein SUPPRESSOR OF QUENCHING 1, chloroplastic
- AT4g31560
- NADPH-dependent thioredoxin reductase 3
- Thioredoxin-like 2-1, chloroplastic
- Serine/threonine-protein kinase STN7, chloroplastic
Sequence:
MNLSVNRCITGGFVGGFSSCRLNHEKRWVRAGKHCELERERSLVSDAVSLERLESKSIKLAMLASGLGVANLVTLSSAKAADLKMIVLDQATSIYILAEGSLGDSVGNFLYSANQQANEAVQDQLSALSVTSLAVIFGAGLVTSLSPCTLSVLPLTLGYIGAFGSGKSRGQVIGDTVAFALGLATTLALLGIVASFAGKAYGQIGQGLPVAASGLAIVMGLNLLEIIELQLPSFFNNFDPRAAAANFPSSVQAYLAGLTFALAASPCSTPVLATLLGYVATSRDPVIGGSLLLTYTTGYVAPLIVAASFAGALQSLLSLRKVSAWINPISGALLLGGGLYTFLDRLFPAATMVM
Protein: Peptidyl-prolyl cis-trans isomerase FKBP17-3, chloroplastic (PPIase FKBP17-3) (EC 5.2.1.8) (FK506-binding protein 17-3) (AtFKBP17-3) (Immunophilin FKBP17-3) (Rotamase) (Q8LB65)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides (By similarity).
Subcellular location: Plastid, chloroplast thylakoid lumen {ECO:0000250}.
Interaction partners:
- Peptidyl-prolyl cis-trans isomerase FKBP17-1, chloroplastic
- Peptidyl-prolyl cis-trans isomerase FKBP15-3
- Peptidyl-prolyl cis-trans isomerase FKBP43
- Peptidyl-prolyl cis-trans isomerase FKBP18, chloroplastic
- Peptidyl-prolyl cis-trans isomerase FKBP20-1
- Peptidyl-prolyl cis-trans isomerase FKBP53
- PsbP domain-containing protein 7, chloroplastic
- Thylakoid lumenal 19 kDa protein, chloroplastic
- PsbQ-like protein 3
- Peptidyl-prolyl cis-trans isomerase FKBP15-2
Sequence:
MATLFTATVPSHHRFVSPSQHPKQSLLSQSLSVTFTENPQPTAVVTLQEQQLTDWITSPVTRRFGIGAGFTWAGFLAFGVVSEQMKKSRLDVFQEEDNTRGLEKQEEIILPNGIRYYDLQVGSGATPSSGYLVVFDVKGQVHGTEQVFVDTFGGKGKSLAMVMDSRPYSKGLCQGIEHVLRSMKAGGKRRVIIPPSLGFGDRNVEFGQGLEIPPSATLDYIIEVDTVYCFQTIV
Protein: Centrosomal protein 112 (A0A8I5Y9N9)
Organism: Rattus norvegicus (Rat)
Interaction partners:
Sequence:
PLWLPQSFPICSGLCRNVRTAFLAIRVALFSLLALQDELETRSNQVRSAEKKLQHKELEAQEQMMYIRQEYETKFKGLMPASLRQELEDTISSLKSQVNFLQKRASILQEELTTYQSRR
Protein: Plasmepsin IX (PfPMIX) (EC 3.4.23.-) (Plasmepsin 9) (Q8ILG2)
Organism: Plasmodium falciparum (isolate 3D7)
Function: During the asexual blood stage, initiates the proteolytic maturation of several rhoptry proteins and thus, is required for merozoite invasion of host erythrocytes and probably the subsequent development of the ring-stage. Cleaves rhoptry associated protein 1 RAP1 and apical sushi protein ASP during schizont maturation. Also cleaves rhoptry protein RON3.
Subcellular location: Membrane {ECO:0000255}; Single-pass type II membrane protein {ECO:0000305}. Cytoplasmic vesicle, secretory vesicle, rhoptry {ECO:0000269|PubMed:29074775}. Note=In schizonts, localizes to the bulb of rhoptries. {ECO:0000269|PubMed:29074775}.
Interaction partners:
Sequence:
MFFINFKKIKKKQFPIYLTQHRIITVFLIFIYFINLKDCFHINNSRILSDVDKHRGLYYNIPKCNVCHKCSICTHENGEAQNVIPMVAIPSKRKHIQDINKEREENKYPLHIFEEKDIYNNKDNVVKKEDIYKLRKKKKQKKNCLNFLEKDTMFLSPSHDKETFHINHMNKIKDEKYKQEYEEEKEIYDNTNTSQEKNETNNEQNLNINLINNDKVTLPLQQLEDSQYVGYIQIGTPPQTIRPIFDTGSTNIWIVSTKCKDETCLKVHRYNHKLSSSFKYYEPHTNLDIMFGTGIIQGVIGVETFKIGPFEIKNQSFGLVKREKASDNKSNVFERINFEGIVGLAFPEMLSTGKSTLYENLMSSYKLQHNEFSIYIGKDSKYSALIFGGVDKNFFEGDIYMFPVVKEYYWEIHFDGLYIDHQKFCCGVNSIVYDLKKKDQENNKLFFTRKYFRKNKFKTHLRKYLLKKIKHQKKQKHSNHKKKKLNKKKNYLIFDSGTSFNSVPKDEIEYFFRVVPSKKCDDSNIDQVVSSYPNLTYVINKMPFTLTPSQYLVRKNDMCKPAFMEIEVSSEYGHAYILGNATFMRYYYTVYRRGNNNNSSYVGIAKAVHTEENEKYLSSLHNKINNL
Protein: Pyrophosphate--fructose 6-phosphate 1-phosphotransferase subunit beta 1 (PFP 1) (EC 2.7.1.90) (6-phosphofructokinase, pyrophosphate dependent 1) (PPi-PFK 1) (Pyrophosphate-dependent 6-phosphofructose-1-kinase 1) (Q8W4M5)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Catalytic subunit of pyrophosphate--fructose 6-phosphate 1-phosphotransferase. Catalyzes the phosphorylation of D-fructose 6-phosphate, the first committing step of glycolysis. Uses inorganic phosphate (PPi) as phosphoryl donor instead of ATP like common ATP-dependent phosphofructokinases (ATP-PFKs), which renders the reaction reversible, and can thus function both in glycolysis and gluconeogenesis.
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03185}.
Interaction partners:
- Glucose-6-phosphate isomerase, cytosolic
- Glucose-6-phosphate isomerase 1, chloroplastic
- Aldolase-type TIM barrel family protein
- transaldolase
- Transketolase-1, chloroplastic
- Transketolase-2, chloroplastic
- 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase
- Mannose-6-phosphate isomerase 1
- Mannose-6-phosphate isomerase 2
- Fructose-bisphosphate aldolase 3, chloroplastic
Sequence:
MAPALAVTRDLTAVGSPENAPAKGRASVYSEVQSSRINNTLPLPSVLKGAFKIVEGPASSAAGNPDEIAKLFPGLYGQPSVAVVPDQDAPSSAPKLKIGVVLSGGQAPGGHNVISGLFDYLQERAKGSTFYGFKGGPAGIMKCKYVELNAEYIQPYRNQGGFDMICSGRDKIETPDQFKQAEETAKKLDLDGLVVIGGDDSNTNACLLAENFRSKNLKTRVIGCPKTIDGDLKCKEVPTSFGFDTACKIYSEMIGNVMIDARSTGKYYHFVRLMGRAASHITLECALQTHPNITIIGEEVSAQKQTLKNVTDYMVDVICKRAELGYNYGVILIPEGLIDFIPEVQELIAELNEILANEVVDENGLWKKKLTEQSLKLFDLLPEAIQEQLMLERDPHGNVQVAKIETEKMLIQMVETELEKRKQAGAYKGQFMGQSHFFGYEGRCGLPTNFDATYCYALGYGAGVLLNSGKTGLISSVGNLAAPVEEWTVGGTALTALMDVERRHGKFKPVIKKAMVELEGAPFKKFASLREEWALKNRYISPGPIQFTGPGSDSLSHTLLLELGAQ
Protein: Corticostatin-3 (Antiadrenocorticotropin peptide III) (Corticostatin III) (CS-III) (Macrophage antibiotic peptide MCP-1) (NP-1) (P01376)
Organism: Oryctolagus cuniculus (Rabbit)
Function: This peptide has antibiotic, anti-fungi and antiviral activity. It also inhibits corticotropin (ACTH) stimulated corticosterone production.
Subcellular location: Secreted.
Interaction partners:
Sequence:
MRTLALLAAILLVALQAQAEHVSVSIDEVVDQQPPQAEDQDVAIYVKEHESSALEALGVKAGVVCACRRALCLPRERRAGFCRIRGRIHPLCCRR
Protein: Ribosomal protein L36, putative (Q38CY6)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- 60S ribosomal protein L13a, putative
- 60S ribosomal protein L39, putative
- 60S ribosomal protein L44
- 60S ribosomal protein L27, putative
- 60S ribosomal protein L27a
- 60S ribosomal protein L17, putative
- 60S ribosomal protein L29
- 60S ribosomal protein L5, putative
- 60S ribosomal protein L19, putative
- 60S ribosomal protein L6, putative
Sequence:
MAATKREAPVPRTGIIAGFNKGYKTTRRARRPSSNDRYALPHKKLRAVKAIISDLVGFSPMERRVQELLRVGKDKRALKFCKKRLGSIKAAKKRRAKVEEALRQQTKKK
Protein: Activin receptor type-2B (EC 2.7.11.30) (Activin receptor type IIB) (ACTR-IIB) (Q90670)
Organism: Gallus gallus (Chicken)
Function: On ligand binding, forms a receptor complex consisting of two type II and two type I transmembrane serine/threonine kinases. Type II receptors phosphorylate and activate type I receptors which autophosphorylate, then bind and activate SMAD transcriptional regulators. Receptor for activin A, activin B and inhibin A. May modulate neuropeptide expression in dorsal root ganglia (DRG) neurons and ovarian follicle development.
Subcellular location: Membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}.
Interaction partners:
- Growth/differentiation factor 8
- Growth differentiation factor 11.
- Bone morphogenetic protein 4
- Receptor protein serine/threonine kinase
- BMP5
- Bone morphogenetic protein 7.
- CVg1 protein
- Bone morphogenetic protein 6.
- Inhibin beta B chain
- Bone morphogenetic protein 2
Sequence:
MSASWLTLAVLCATLGAGPGHGEAETRECIYYNANWELEKTNQSGVERCEGEKDKRLHCYASWRNNSGSIELVKKGCWLDDFNCYDRQECVATEENPQVFFCCCEGNYCNEKFTHLPEVTGPEVIYEPPPPTPSLLNILVYSLLPIAVLSVAILLAFWMYRHRKPPYGHVDINEDPGPPPPSPLVGLKPLQLLEIKARGRFGCVWKAQLMNDYVAVKIFPIQDKQSWQSEREIFNTPGMKHENLLQFIAAEKRGTNLETELWLITAFHDKGSLTDYLKGNIISWNELCHVAETMARGLSYLHEDVPWCKGEGHKPAIAHRDFKSKNVLLKNDLTAVLADFGLAVRFEPGKPPGDTHGQVGTRRYMAPEVLEGAINFQRDAFLRIDMYAMGLVLWELVSRCRAVDGPVDEYMLPFEEEIGQHPSLEDLQEVVVHKKMRPVFKDHWLKHPGLAQLCVTIEECWDHDAEARLSAGCVEERIAQIRKSVNGTTSDCLVSIVTSVTNVDLPPKESSI
Protein: NADPH-dependent aldehyde reductase 1, chloroplastic (AtChlADR1) (EC 1.1.1.-) (Glucose and ribitol dehydrogenase homolog 1) (Q9FZ42)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Aldehyde reductase that catalyzes the reduction of the aldehyde carbonyl groups on saturated and alpha,beta-unsaturated aldehydes with more than 5 carbons. No activity on alpha,beta-unsaturated ketones. Can use propionaldehyde, butyraldehyde, methylglyoxal, (e)-2-pentenal, (E)-2-hexenal, (Z)-3-hexenal and (E)-2-nonenal as substrates, but not propenal (acrolein), crotonaldehyde, 2-butanone, 3-buten-2-one or 1-penten-3-one. May act as a short alcohol-polyol-sugar dehydrogenase possibly related to carbohydrate metabolism and the acquisition of desiccation tolerance (By similarity). May also be involved in signal transduction (By similarity).
Subcellular location: Plastid, chloroplast {ECO:0000269|PubMed:21169366}.
Interaction partners:
- Large ribosomal subunit protein uL29x
- 12S seed storage protein CRA1
- SEED MATURATION PROTEIN 1
- Nucleolin
- Probable aldo-keto reductase 1
- Large ribosomal subunit protein eL32y
- NADPH-dependent alkenal/one oxidoreductase, chloroplastic
- NADPH-dependent aldo-keto reductase, chloroplastic
- Small ribosomal subunit protein uS9x
- Multiprotein-bridging factor 1b
Sequence:
MASEKQKQHAQPGKEHVMESSPQFSSSDYQPSNKLRGKVALITGGDSGIGRAVGYCFASEGATVAFTYVKGQEEKDAQETLQMLKEVKTSDSKEPIAIPTDLGFDENCKRVVDEVVNAFGRIDVLINNAAEQYESSTIEEIDEPRLERVFRTNIFSYFFLTRHALKHMKEGSSIINTTSVNAYKGNASLLDYTATKGAIVAFTRGLALQLAEKGIRVNGVAPGPIWTPLIPASFNEEKIKNFGSEVPMKRAGQPIEVAPSYVFLACNHCSSYFTGQVLHPNGGAVVNA
Protein: Plasma membrane fusion protein PRM1 (Pheromone-regulated membrane protein 1) (P53835)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Involved in cell fusion during mating by stabilizing the plasma membrane fusion event.
Subcellular location: Cell membrane {ECO:0000269|PubMed:11062271, ECO:0000269|PubMed:12374868}; Multi-pass membrane protein {ECO:0000269|PubMed:11062271, ECO:0000269|PubMed:12374868}. Note=Localizes at sites of cell fusion during mating.
Interaction partners:
- Nuclear fusion protein FUS1
- Nuclear fusion protein FUS2
- Pheromone-regulated membrane protein 2
- Factor-induced gene 2 protein
Sequence:
MSGFKCYLQLGDRLSQIWLNKYTLVLLLAMLKLLFFSKSIQHAIEVSETYILSNCYSIDSLYSKMTDNTPHYLGIMGNYLIEKGMEETVKATLETLSLIVYASEGLVNFAIDLYLGTYACLIVSAVDGTVDVATNITEKLISLVNDTVSSVANELDTGLNDISKIINKVIKAASKVENFFTGDDDDSNMTSSIKSVNLTISALHNLYIPSSINDKLEELSAKTPDFAQVKNTTKNLISVPFNEVRKNIKAVNASNIIGDTSVLYVPPVSLDNSTGICSSNQSEILAFYSILGHVLKIATVVCITVLICFAVGAMAPVAWNEIKLWRRLCGMRDHYMLSRQDSYTSFSSENTHELKDPFRDPPIQNGQYDVIASYQQCFQTWNTRIAGWMTNLVTFGKSPENIDPKTKQKIEWVVAYMTSERALCVLGIGLLGILVCICQFVMIALLKHKISHSLTSNDGDGVQNLLKSSTAVDIENQMSLWSVQTNKYINTTETNINQEVFGWINTTTLSVNNTVATMISDIDTTLADVFNGTLLYNPMKTVVGCAIENKLYTIEKAMTWIHDKAQLHIPRINGTQIKQALAKQTDNSTIPTASSTSAATENLLENLVNDMREGLLKILRAYHRITLGELTVALVILAVWLVQLPIALVILRLRLRKATFD
Protein: Mitochondrial dicarboxylate transporter (DTP) (Dicarboxylate carrier 1) (Q06143)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Mitochondrial dicarboxylic transporter catalyzing the exchange of dicarboxylic acids like malate and succinate for inorganic phosphate. Required for growth on ethanol and acetate.
Subcellular location: Mitochondrion inner membrane {ECO:0000269|PubMed:10027973, ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:14576278}; Multi-pass membrane protein {ECO:0000269|PubMed:10027973, ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:14576278}.
Interaction partners:
Sequence:
MSTNAKESAGKNIKYPWWYGGAAGIFATMVTHPLDLAKVRLQAAPMPKPTLFRMLESILANEGVVGLYSGLSAAVLRQCTYTTVRFGAYDLLKENVIPREQLTNMAYLLPCSMFSGAIGGLAGNFADVVNIRMQNDSALEAAKRRNYKNAIDGVYKIYRYEGGLKTLFTGWKPNMVRGILMTASQVVTYDVFKNYLVTKLDFDASKNYTHLTASLLAGLVATTVCSPADVMKTRIMNGSGDHQPALKILADAVRKEGPSFMFRGWLPSFTRLGPFTMLIFFAIEQLKKHRVGMPKEDK
Protein: Sialic acid-binding Ig-like lectin 15 (Siglec-15) (CD33 antigen-like 3) (Q6ZMC9)
Organism: Homo sapiens (Human)
Function: Binds sialylated glycoproteins.
Subcellular location: Membrane; Single-pass type I membrane protein.
Interaction partners:
- TYRO protein tyrosine kinase-binding protein
- Elongation factor 1-alpha 2
- Sialoadhesin
- B-cell receptor CD22
Sequence:
MEKSIWLLACLAWVLPTGSFVRTKIDTTENLLNTEVHSSPAQRWSMQVPPEVSAEAGDAAVLPCTFTHPHRHYDGPLTAIWRAGEPYAGPQVFRCAAARGSELCQTALSLHGRFRLLGNPRRNDLSLRVERLALADDRRYFCRVEFAGDVHDRYESRHGVRLHVTAAPRIVNISVLPSPAHAFRALCTAEGEPPPALAWSGPALGNSLAAVRSPREGHGHLVTAELPALTHDGRYTCTAANSLGRSEASVYLFRFHGASGASTVALLLGALGFKALLLLGVLAARAARRRPEHLDTPDTPPRSQAQESNYENLSQMNPRSPPATMCSP
Protein: Eukaryotic translation initiation factor 3 subunit E (eIF3e) (Eukaryotic translation initiation factor 3 subunit 6) (eIF-3 p48) (B3KW56)
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:
MVDFAMDVYKNLYSDDIPHALREKRTTVVAQLKQLQAETEPIVKMFEDPETTRQMQSTRDGRMLFDYLADKHGFRQEYLDTLYRYAKFQYECGNYSGAAEYLYFFRVLVPATDRNALSSLWGKLASEILMQNWDAAMEDLTRLKETIDNNSVSSPLQSLQQRTWLIHWSLFVFFNHPKGRDNIIDLFLYQPQYLNAIQTMCPHILRYLTTAVITNKDVRKRRQVLKDLVKVIQQESYTYKDPITEFVECLYVNFDFDGAQKKLRECESVLVNDFFLVACLEDFIENARLFIFETFCRIHQCISINMLADKLNMTPEEAERWIVNLIRNARLDAKIDSKLGHVVMGNNAVSPYQQVIEKTKSLSFRSQMLAMNIEKKLNQNSRSEAPNWATQDSGFY
Protein: Nuclear pore complex protein NUP205 (Nucleoporin 205) (Protein EMBRYO DEFECTIVE 3142) (F4KBW6)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Nucleus envelope {ECO:0000269|PubMed:21189294}. Nucleus, nuclear pore complex {ECO:0000305|PubMed:21189294}.
Interaction partners:
- Nuclear pore complex protein NUP93B
- Protein SEH1
- Nuclear pore complex protein NUP35
- Nuclear pore complex protein NUP155
- Nuclear pore complex protein NUP107
- Nuclear pore complex protein NUP93A
- Nuclear pore complex protein NUP54
- Nuclear pore complex protein NUP88
- Nuclear pore complex protein NUP160
- Nucleoporin
Sequence:
MVSPKDLVAIVHSSLLGTSRPTPTQRIELTHAIRNSFPSLQNLLSFPPPKPSDRAQVQSKEIRLPDSLPISLDDQDIAISLKLSDELHLNEIDSVRLLVSSNQEWGLMGRDPLEIQRLATGLWYTGRRDLTSTLYTLLRAVVLDEGLEPDLIADIQGLLEELIEAGLRQRLITLIKELNREDPTGLGGPLCERYLIDSRGALVERRAVVQRERLILGHCLVLSILVDRPGSKDVKDIYYILKDNAAQLTEGNDTISSQITFSLLFSLIITFVSDAISRLSDKSSMISQDASFRTDFQDIVMASGSDPTADGFIGGIRLAWAVHLMLIHDGISGMDTISTASTTDMGHICSCLESIFSKNVFQFLLDNVLRTAAYQNDEEDIIYIYNAYLHKLASCFLSHPIARDKVKESKDMAMSVLNSYRTSDPLDGSMQTEESDRPLPFISLMEFKEPELLSGNDVLWTFVNFAGEDHTNFKTLVAFLEMLCTLASTQEGASKVYELLRGTSFRSIGWPTLFDCIRIYDEKFKQSLQTAGAMMPEFLEGDAKALVAYLNVLQKVVENGNPTERKNWFPDIEPFFKLLGYENIPPYLKGALRKTIAAFVNVFPEMRDSIWAFLEQYDLPVVVGSQVGKSDQSSQVYDMQFELNEVEARREQYPSTISFLNLINALIAGEKDVNDRGRRAYSDPCEKWQLVVACLQHFHMILSMYDIQEEDLDGFTEHPHFLVSLETSSLQTQLPIIELLKDFMSGKALYRNLMGILQVGVNSIISERLSKTYGKILEKAVQLSLEILLLVFEKDLLVSDVWRPLYQPLDIILSQDHNQIIALLEYVRYDSLPQIQRSSIKIMNILRCSRLVGLVPMLIKIDAANSLIEDYAACLEGRLEEGEVVENSCDDLGVLIMQLLVDNINRPAPSITHLLLKFDLDAPVEGTVLQPKFHYSCLKVILEMLEKLPNPDINFLLFEFGFQLLCELNLDPLTSGPTMDLLSSKKYQFFLQHLDTIGVATLPKRSGSQALRISSLHQRAWLLKLLAIALHTGSGSSSAHLEACQSILSHLFGREVTEAANEPFSSSTYPQDGLDYAGTSSISKSKALALLEILQFRSPDASMQLPQIVSSLKYDSLVEDILGNRDTSVSGSIYYYSERGDRLIDLSSFSNKLWQKLHSGFPLVDSFPNVAELSEVRETIQQLLKWGWKYNRNLEEQAAQLHMLAGWSQIVEVSACRRISSLDNRSEILYRILDASLSASASPDCSLKMAFVLTQVALTCIAKLRDDRFSFQGALSSDTVTCLDVMMVKHLSTGACHSVLFKLVMAILRHESSESLRRRQYALLLSYFQYCQHMIALDVPTSVVQFLLLNEQDGEDLDIQKIDKEQADLARANFFIIKKEAQGILDLVIKDASQGSEFGKTISLYVLEALVCIDHERYFLSQLQSRGFIRSCLGSISNISYQDGTHLLESQQRACTLEAELALLLRISHKYGKSGGQVLFSMGALEHIASCRAISFKGNMRRVDMKLQSDVGYNVQKQRTIITAVLRLVFALTSLVETSEFFEGRNKIVRDVVEFIKGHQSLFDQLLREDFTQADDLLMEQIILAVGILSKVWPFEENDGYGFVQGLFDMMSKLFIASPIKSILSQGSELKLSQLRFSLTSYLYFLVTKNSLRLQVSDDSLDSSTKLRQPTLLLLASLLSHVTDSLERAAEKKSLLLHKIRDINELSRQDVDAIIKICDSQEYVTPSDNIHKRRYIAMVEMCQIVGNRDQLITLLLQLAEHVLNIILIHLQDRSVSSNERGSYGSKSHIQQEVTDLCGKLSPTIDRLALLNEGKVGHNLKVFQRLATTVKEMAIQKCV
Protein: DesT (Q9HUS3)
Organism: Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Interaction partners:
- Acyl-CoA delta-9-desaturase, DesB
- Probable oxidoreductase
- 3-oxoacyl-[acyl-carrier-protein] synthase 1
- 3-hydroxydecanoyl-[acyl-carrier-protein] dehydratase
- Delta-9 fatty acid desaturase, DesA
- Glycerol-3-phosphate acyltransferase
- Probable transcriptional regulator
Sequence:
MSSPRAEQKQQTRHALMSAARHLMESGRGFGSLSLREVTRAAGIVPAGFYRHFSDMDQLGLALVAEVDETFRATLRAVRRNEFELGGLIDASVRIFLDAVGANRSQFLFLAREQYGGSLPIRQAIASLRQRITDDLAADLALLNKMPHLDGAALDVFADLVVKTVFATLPELIDPPAADLPPHLMPAAKITHQLRFIMIGGKHWHGLPG
Protein: non-specific serine/threonine protein kinase (EC 2.7.11.1) (Q8IIR9)
Organism: Plasmodium falciparum (isolate 3D7)
Interaction partners:
- Falcipain-3
- Raf kinase inhibitor
- Cysteine proteinase falcipain 1
- Uncharacterized protein
- Kelch domain-containing protein, putative
- ADP/ATP translocase
- Peptidyl-prolyl cis-trans isomerase
- Citrate synthase
- DNA polymerase II subunit 2
- Ribosome-interacting GTPase 1, putative
Sequence:
MSVSSINKKIYIPKFYADVNIHKPKEYYDYDNLELQWNKPNRYEIMKKIGRGKYSEVFNGYDTECNRPCAIKVLKPVKKKKIKREIKILQNLNGGPNIIKLLDIVKDPVTKTPSLIFEYINNIDFKTLYPKFTDKDIRYYIYQILKALDYCHSQGIMHRDVKPHNIMIDHENRQIRLIDWGLAEFYHPGQEYNVRVASRYYKGPELLIDLQLYDYSLDIWSLGCMLAGMIFKKEPFFCGHDNYDQLVKIAKVLGTEDLHAYLKKYNIKLKPHYLNILGEYERKPWSHFLTQSNIDIAKDEVIDLIDKMLIYDHAKRIAPKEAMEHPYFREVREES
Protein: WW domain-containing protein (Q57Z68)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MYTFKRPQQQQPQLQGANMGVTDAVDPPATGAPFVDGDNTAYPAVAAQASQEGVGEEAQQQQHQQPAGYLSEEATAEEALQYCQQMVLRNPVSPPPTWSGARQVLPATVPELHLIPSAPVQAQQPPHITPSASVVLQLDGVVPEGMTPKEYGRSLVKYIVELLAYQRATTAITSLRFVKMGTELMQLVVTFGRDVRLAMRVMEEFTNVGLCAGFVLEDDGDLNSGGSFGGNKRVVPPCATFQVTDYQFLLNGGRGITSEDIGSLFQPETGNGENDMNVISGFEPGVFYVAVKKPGTVYEWLWNPFCSFLVQYTLFQRCGVLITMADCMDEFSQSKGGPRVAVGRQKGSDVGENSRLRRDVKDDTGETNDYSNNGAKYEDDEAADDDDYLGKSSDIEEKRGGRWVRSGSPMWSRNAKEEVDIFGGLGTGVKPQKLSEEDFVDNDITELLQEVKADGQKDVRTAEQQQKPSARHRSGQSAPRAEAHAPPAAEVSVPHVAAAPPRATPAPIPHSGSQSCPPYGSYYGYAAPTAAWQQPPPPPPPRTDTPPPYQAAVMSNINEMKAPKTDYPELVEEEISNEDAEEGNTGDNNTTQQPPPQMMYWGSGGGPPGGAAGYYPPSTYAQYAAPPYGYPIPQHHHSHAVPSSMPSILGQSTFGSFVPTVRVEERVAVQVQPITINGAPCVSSITVDDVNSLAAKIVERVQLAFPLGALQNGNTNLLNSGETTTRVDGEYEGPIETAQAMPSNNEGEDRLRDKELMFPSIPCDFSVPPLSPEVEDIVSFLQQHSADIRIILTSTSEEFNDGRSRIVEALLVENSGSCNDEQAAWDQQYARPKDGETIASVEATTTAGKPATETEGTQPKKIKQLPTLLPYLLASKGAISILTALANCHAAKLLPLLCRCILPFLLDTTVVQSVGVVALRSDPTAANPLVLRLLRHWASLAMWLHEHIQSLAGESAQTSQAAAMGRLTSQVGSAIDALLTAMSSEQRESVAEFLAETKALETFFQSMPECPQSGKKEENLKGEVSRQSSFMLWDIEGAVYRSLLRLYLNADFFNGEEFANILYASKTSLTRDHFYFIRVALSKSNVSPTLSVETARLCGAFLRLMELMPRDIGKNKEVDKNSGVRCVFTDHDALNLLEAALRVQPSEEAYQSLRSAYFAKPASEERYEQIEKKLSSTVLPPPYPQQPANITTAILGTSSSYNPQPSSDAQQHVTTRRWLPEWTAAMRHYPRTGEPFTPLPTGWTSAMSRSYGYYYFRDGKSPATYKHPTDATEFMVAPQAFLLEARTAVTLDEVLEYANRMSQECRTDDASREQPPIITKEVAEEWINDQRIRLEALDLAALDLMKVSYHTVGSGGRRYGERNEHTDGDGGRRDRRRRHHSHRRHGRSRRKRSRSRSRSRSTRGSRERRHSDRSLSKTLKFSSYPPRGHPFPHLPYRWTCNLSASKGLYYFRAPTGSLVFTHPDTRREYRVTPQAFALHHNIQVAAIATTSRRPVEEVERWLSDQRNRDEDIDTAVVRMIPITYVWSSCDDEEGDDEGKRFHREEGSSRLHRKDSRR
Protein: Rop guanine nucleotide exchange factor 9 (AtRopGEF9) (Rho of plants guanine nucleotide exchange factor 9) (Q9SVQ3)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Guanine-nucleotide exchange factor (GEF) that acts as an activator of Rop (Rho of plants) GTPases by promoting the exchange of GDP for GTP.
Subcellular location: Cell membrane {ECO:0000269|PubMed:16415208}. Note=Localizes to the apical region of the pollen tube plasma membrane.
Interaction partners:
Sequence:
MVPSLERGISITSSFNLDRMFDSSPGKEQQQPHLAETTMPESQTQDSLGGSPVETSRPMTSRLISRRQDKQQSETEMMKDRFTKLLLGEDMSGGGKGVSSALALSNAITNLAASIFGEQTKLQPMAPDRRARWKKEIDWLLSVTDHIVEFVPSQQISKEGVCTEIMVTRQRGDLLMNIPALRKLDAMLIDTLDNFRGHNEFWYVSRDSEEGKQARNERTKDKWWLPPVKVPPNGLSESARRMLHFQKDSVSQVQKAAMAINAQVLSEMAIPDSYIESLPKNGRVSLGDSLYKSITEEWFDPEQFLSTLDLSTEHKVLDVKNRIEASIVIWKRKLHLKDNKSSWGSAVSLEKRELFEERAETILVLLKQKFPGLPQSSLDISKIQYNKDVGHAVLESYSRILESLGYTEMSRIDDVLYADSLARKQCTGEETSDGGKIATETDSASAGSSNYSGEEIEKLESQNSSKTTLLDFIGWSDNSSKGQSEKPPKSPRMTPKKLSYLEKLENLNGFRSPKDRH
Protein: Protein TIFY 6b (OsTIFY6b) (Jasmonate ZIM domain-containing protein 4) (OsJAZ4) (OsJAZ8) (Q6ES51)
Organism: Oryza sativa subsp. japonica (Rice)
Function: Repressor of jasmonate responses.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00768}.
Interaction partners:
- Transcription factor MYC2
- Os10g0506950 protein
- Coronatine-insensitive protein homolog 1a
- Protein TIFY 9
- Coronatine-insensitive protein homolog 1b
- Coronatine-insensitive protein homolog 2
- Protein TIFY
- Transcription factor
- Transcription factor
- Protein TIFY 11a
Sequence:
MERDFLGAIGKDEEQRRHAEERKESDYFGAGGGAAAAAMDWSFASRAALMSFRSSSSAAAAAAREETRELAFPHFSALDGAKMQQASHVLARQKSFGAESHGIPQYAAAAAVHGAHRGQPPHVLNGARVIPASSPFNPNNPMFRVQSSPNLPNAVGAGGGAFKQPPFAMGNAVAGSTVGVYGTRDMPKAKAAQLTIFYAGSVNVFNNVSPEKAQELMFLASRGSLPSAPTTVARMPEAHVFPPAKVTVPEVSPTKPMMLQKPQLVSSPVPAISKPISVVSQATSLPRSASSSNVDSNVTKSSGPLVVPPTSLPPPAQPETLATTTAAAIMPRAVPQARKASLARFLEKRKERVTTVAPYPLAKSPLESSDTMGSANDNKSSCTDIALSSNRDESLSLGQPRTISFCEESPSTKLQI
Protein: PHD finger protein 13 (Survival time-associated PHD finger protein in ovarian cancer 1) (SPOC1) (Q86YI8)
Organism: Homo sapiens (Human)
Function: Modulates chromatin structure. Required for normal chromosome condensation during the early stages of mitosis. Required for normal chromosome separation during mitosis.
Subcellular location: Nucleus {ECO:0000269|PubMed:19638409, ECO:0000269|PubMed:23034801}. Nucleus, nucleoplasm {ECO:0000269|PubMed:19638409}. Note=Predominantly bound to chromatin, but a minor proportion is also detected in the nucleoplasm.
Interaction partners:
- Deoxyribonuclease-1-like 2
- T-box transcription factor TBX20
Sequence:
MDSDSCAAAFHPEEYSPSCKRRRTVEDFNKFCTFVLAYAGYIPYPKEELPLRSSPSPANSTAGTIDSDGWDAGFSDIASSVPLPVSDRCFSHLQPTLLQRAKPSNFLLDRKKTDKLKKKKKRKRRDSDAPGKEGYRGGLLKLEAADPYVETPTSPTLQDIPQAPSDPCSGWDSDTPSSGSCATVSPDQVKEIKTEGKRTIVRQGKQVVFRDEDSTGNDEDIMVDSDDDSWDLVTCFCMKPFAGRPMIECNECHTWIHLSCAKIRKSNVPEVFVCQKCRDSKFDIRRSNRSRTGSRKLFLD
Protein: Arginase (EC 3.5.3.1) (E9AEX1)
Organism: Leishmania major
Interaction partners:
- ornithine decarboxylase
- Putative glutamamyl carboxypeptidase
- Acetylornithine deacetylase-like protein
- Spermidine synthase
- Putative S-adenosylmethionine decarboxylase proenzyme-like
- S-adenosylmethionine decarboxylase proenzyme
Sequence:
MEHVQQYKFYKEKKMSIVLAPFSGGQPHGGVELGPDYLLKQGLQQDMEKLGWNTRLERVFDGKAVEARKANDNGDRIGRVKRPRLTAECTEKIYKCVRRVAEQGRFPLTIGGDHSIALGTVAGVLSVYPDAGVIWVDAHADINTMSGTVSGNLHGCPLSILLGLDRENIPECFSWVPQVLKPNKIAYIGLRAVDEEEKKILHDLNIAAFSMHHVDRYGINKVVSMAIEAISPKGTEPVMVSYDVDTIDPLYVPATGTPVRGGLSFREALFLCELIAECGRLVALDVVECNPLLAATESHVKDTISVGCAIARCMMGETLLYTPRKDAKL