wanglab/gogpt-training-data huggingface dataset:
Protein: Plastid transcriptionally active 3 (F4J3M2)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- Protein PLASTID TRANSCRIPTIONALLY ACTIVE 10
- Protein PLASTID TRANSCRIPTIONALLY ACTIVE 12, chloroplastic
- Protein PLASTID TRANSCRIPTIONALLY ACTIVE 14
- Thioredoxin-like protein CITRX, chloroplastic
- PLASTID TRANSCRIPTIONALLY ACTIVE protein 6, chloroplastic
- Fructokinase-like 1, chloroplastic
- Fructokinase-like 2, chloroplastic
- UDP-N-acetylmuramoyl-L-alanyl-D-glutamate--2,6-diaminopimelate ligase MurE homolog, chloroplastic
- DNA-directed RNA polymerase subunit alpha
- Protein PLASTID TRANSCRIPTIONALLY ACTIVE 7
Sequence:
MSLLFLNPPFPSNSIHPIPRRAAGISSIRCSISAPEKKPRRRRKQKRGDGAENDDSLSFGSGEAVSALERSLRLTFMDELMERARNRDTSGVSEVIYDMIAAGLSPGPRSFHGLVVAHALNGDEQGAMHSLRKELGAGQRPLPETMIALVRLSGSKGNATRGLEILAAMEKLKYDIRQAWLILVEELMRINHLEDANKVFLKGARGGMRATDQLYDLMIEEDCKAGDHSNALDISYEMEAAGRMATTFHFNCLLSVQATCGIPEVAYATFENMEYGEVFMKPDTETYNWVIQAYTRAESYDRVQDVAELLGMMVEDHKRVQPNVKTYALLVECFTKYCVVKEAIRHFRALKNFEGGTVILHNAGNFEDPLSLYLRALCREGRIVELIDALDAMRKDNQPIPPRAMIMSRKYRTLVSSWIEPLQEEAELGYEIDYLARYIEEGGLTGERKRWVPRRGKTPLDPDASGFIYSNPIETSFKQRCLEDWKVHHRKLLRTLQSEGLPVLGDASESDYMRVVERLRNIIKGPALNLLKPKAASKMVVSELKEELEAQGLPIDGTRNVLYQRVQKARRINKSRGRPLWVPPIEEEEEEVDEEVDDLICRIKLHEGDTEFWKRRFLGEGLIETSVESKETTESVVTGESEKAIEDISKEADNEEDDDEEEQEGDEDDDENEEEEVVVPETENRAEGEDLVKNKAADAKKHLQMIGVQLLKESDEANRTKKRGKRASRMTLEDDADEDWFPEEPFEAFKEMRERKVFDVADMYTIADVWGWTWEKDFKNKTPRKWSQEWEVELAIVLMTKVIELGGIPTIGDCAVILRAALRAPMPSAFLKILQTTHSLGYSFGSPLYDEIITLCLDLGELDAAIAIVADMETTGITVPDQTLDKVISARQSNESPRSEPEEPASTVSS
Protein: Large ribosomal subunit protein uL29 (60S ribosomal protein L35) (P42766)
Organism: Homo sapiens (Human)
Function: Component of the large ribosomal subunit. The ribosome is a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:23636399}.
Interaction partners:
- Large ribosomal subunit protein P1
- Large ribosomal subunit protein uL4
- Small ribosomal subunit protein eS7
- Small ribosomal subunit protein eS4, X isoform
- Proliferation-associated protein 2G4
- Small ribosomal subunit protein eS28
- Small ribosomal subunit protein uS7
- Large ribosomal subunit protein eL30
- Small ribosomal subunit protein eS17
- Large ribosomal subunit protein bL36m
Sequence:
MAKIKARDLRGKKKEELLKQLDDLKVELSQLRVAKVTGGAASKLSKIRVVRKSIARVLTVINQTQKENLRKFYKGKKYKPLDLRPKKTRAMRRRLNKHEENLKTKKQQRKERLYPLRKYAVKA
Protein: Protein MC132 (Q98298)
Organism: Molluscum contagiosum virus subtype 1 (MOCV) (MCVI)
Function: Inhibits host NF-kappa-B activation stimulated by IL-1 and multiple PRR viral detection pathways. Targets host NF-kappa-B component RELA/p65 for ubiquitin-dependent proteasomal degradation.
Subcellular location: Host cytoplasm {ECO:0000269|PubMed:26041281}.
Interaction partners:
Sequence:
MMNFSDPCLLGPSACNEDFFEELAREILPTPEAKALAARLLRRLGWHPSEGQCSWCPEAYEYLYDLQFRYTGPVPLVRKHPGSALIVRWMLDGLGHFLFCRPRVQGNPLTYHLSCMGSAIRTLELFREQAHSHLWEQGNLVDCYWSCSSDYGYEGKWGQQAVVRGALSGPWPRPDPPSLQLQCLCAIWRTCLLRGQSQAQKYTNWICARHLQLRPDTSTRDSDLLLQRC
Protein: Prostaglandin E synthase 3 (EC 5.3.99.3) (Cytosolic prostaglandin E2 synthase) (cPGES) (Hsp90 co-chaperone) (Progesterone receptor complex p23) (Telomerase-binding protein p23) (P83868)
Organism: Rattus norvegicus (Rat)
Function: Cytosolic prostaglandin synthase that catalyzes the oxidoreduction of prostaglandin endoperoxide H2 (PGH2) to prostaglandin E2 (PGE2). Molecular chaperone that localizes to genomic response elements in a hormone-dependent manner and disrupts receptor-mediated transcriptional activation, by promoting disassembly of transcriptional regulatory complexes. Facilitates HIF alpha proteins hydroxylation via interaction with EGLN1/PHD2, leading to recruit EGLN1/PHD2 to the HSP90 pathway (By similarity).
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:Q3ZBF7}.
Interaction partners:
- Prostaglandin E synthase
- Prostaglandin E synthase 2
- peptidylprolyl isomerase
- Heat shock protein HSP 90-beta
- AH receptor-interacting protein
- Prostacyclin synthase
- Glucocorticoid receptor
- Peptidyl-prolyl cis-trans isomerase FKBP4
- Prostaglandin G/H synthase 1
- Prostaglandin G/H synthase 2
Sequence:
MQPASAKWYDRRDYVFIEFCVEDSKDVNVNFEKSKLTFSCLGGSDNFKHLNEIDLFHCIDPNDSKHKRTDRSILCCLRKGESGQSWPRLTKERAKLNWLSVDFNNWKDWEDDSDEDMSNFDRFSEMMDHMGGDEDVDLPEVDGADDDSQDSDDEKMPDLE
Protein: Trem-like transcript 1 protein (TLT-1) (Triggering receptor expressed on myeloid cells-like protein 1) (Q8K558)
Organism: Mus musculus (Mouse)
Function: Cell surface receptor that may play a role in the innate and adaptive immune response.
Subcellular location: Cell membrane {ECO:0000269|PubMed:15100151}; Single-pass type I membrane protein {ECO:0000269|PubMed:15100151}. Cytoplasm {ECO:0000269|PubMed:15100151}. Note=Sequestered in cytoplasmic vesicles in resting platelets. Transported to the cell surface after stimulation by thrombin. Soluble fragments can be released into the serum by proteolysis. {ECO:0000250|UniProtKB:Q86YW5}.
Interaction partners:
- Trem-like transcript 2 protein
- Trem-like transcript 4 protein
- Platelet glycoprotein IX
- Triggering receptor expressed on myeloid cells 1
- Triggering receptor expressed on myeloid cells 2
- TYRO protein tyrosine kinase-binding protein
Sequence:
MDCYLLLLLLLLGLAGQGSADSHPEVLQAPVGSSILVQCHYRLQDVRALKVWCQFLQEGCHPLVTSAVDRRAPGNGRIFLTDLGGGLLQVEMVTLQEEDTGEYGCVVEGAAGPQTLHRVSLLVLPPVPGPREGEEAEDEKETYRIGTGSLLEDPSLDPSASAGPHEFRRRENSIPLIWGAVLLLALVVVAVVIFAVMARKKGNRLVVCGPSQSTGVPGMDPPSAAHRSSDSGLPSDIPHVRLDSPPSFDSIYTGSSLDPPSSEPPAPPSQPPLPPKVLMSSKSVTYATVVFPGGDKGKIASCEPVQDPPNSQTPPSK
Protein: Cytochrome c oxidase subunit 5A, mitochondrial (Cytochrome c oxidase polypeptide Va) (P00426)
Organism: Bos taurus (Bovine)
Function: Component of the cytochrome c oxidase, the last enzyme in the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII) and cytochrome c oxidase (complex IV, CIV), that cooperate to transfer electrons derived from NADH and succinate to molecular oxygen, creating an electrochemical gradient over the inner membrane that drives transmembrane transport and the ATP synthase. Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Electrons originating from reduced cytochrome c in the intermembrane space (IMS) are transferred via the dinuclear copper A center (CU(A)) of subunit 2 and heme A of subunit 1 to the active site in subunit 1, a binuclear center (BNC) formed by heme A3 and copper B (CU(B)). The BNC reduces molecular oxygen to 2 water molecules using 4 electrons from cytochrome c in the IMS and 4 protons from the mitochondrial matrix.
Subcellular location: Mitochondrion inner membrane {ECO:0000269|PubMed:27605664, ECO:0000269|PubMed:31533957}; Peripheral membrane protein {ECO:0000269|PubMed:27605664, ECO:0000269|PubMed:31533957}; Matrix side {ECO:0000269|PubMed:27605664, ECO:0000269|PubMed:31533957}.
Interaction partners:
- Cytochrome c oxidase subunit 1
- Cytochrome b-c1 complex subunit Rieske, mitochondrial
- Cytochrome c oxidase subunit 7A1, mitochondrial
- Cytochrome b-c1 complex subunit 10
- Cytochrome c oxidase subunit 4 isoform 1, mitochondrial
- Cytochrome c oxidase subunit 6B1
- Cytochrome b-c1 complex subunit 9
- Cytochrome b
- Cytochrome b-c1 complex subunit 1, mitochondrial
- Cytochrome c oxidase subunit 5B, mitochondrial
Sequence:
MLGAAVRRCSVAAAAVARASPRGLLHPTPAPGQAAAVQSLRCYSHGSHETDEEFDARWVTYFNKPDIDAWELRKGMNTLVGYDLVPEPKIIDAALRACRRLNDFASAVRILEVVKDKAGPHKEIYPYVIQELRPTLNELGISTPEELGLDKV
Protein: Mannosylfructose-phosphate synthase (EC 2.4.1.246) (A7TZT2)
Organism: Agrobacterium fabrum (strain C58 / ATCC 33970) (Agrobacterium tumefaciens (strain C58))
Interaction partners:
- Mannosylfructose-phosphate phosphatase
Sequence:
MEKFTKMGPMTTTSETERYPRIALISTHGYVAAHPPLGAADTGGQVVYVLELARKLGQLGYTVDLYTRRFEDQPEFDEVDERVRVVRIPCGGRDFIPKEYLHRHLMEWCENALRFIKKNDLNYSFINSHYWDAGVAGQRLSEALKIPHLHTPHSLGIWKKRQMETDYPEKADTFELEFNFKERIQHELIIYRSCDMVIATTPVQLDVLIEDYGLKRKHIHMIPPGYDDNRFFPVSDATRQMIRQRFGFEGKVVLALGRLATNKGYDLLIDGFSVLAEREPEARLHLAVGGENMDEQETTILNQLKERVKSLGLEDKVAFSGYVADEDLPDIYRAADLFVLSSRYEPFGMTAIEAMASGTPTVVTIHGGLFRAISYGRHALFADPFDKEDLGITMMKPFKHERLYGRLSRMGAHKARSLFTWTGIAQQLLALVEGRTMMPVLEEADWAEPWNDGD
Protein: Cytochrome c oxidase subunit (Q6FY72)
Organism: Candida glabrata (strain ATCC 2001 / BCRC 20586 / JCM 3761 / NBRC 0622 / NRRL Y-65 / CBS 138) (Yeast) (Nakaseomyces glabratus)
Subcellular location: Mitochondrion {ECO:0000256|ARBA:ARBA00004173}.
Interaction partners:
- Cytochrome b-c1 complex subunit 7
- Cytochrome c oxidase subunit 6, mitochondrial
- Complex III subunit 9
- Cytochrome c oxidase subunit 13, mitochondrial
- Cytochrome c oxidase subunit 8, mitochondrial
- Cytochrome c oxidase subunit 1
- Cytochrome c oxidase subunit 4, mitochondrial
- Cytochrome c oxidase subunit 9, mitochondrial
- quinol--cytochrome-c reductase
- Cytochrome b-c1 complex subunit 2, mitochondrial
Sequence:
MSDSPLHTVGFDPRFPNQNQTRHCWQAYVDYHKCINLKGEDFAPCKVFWKTYSSLCPVEWVEKWDDQREKGIFAGDISPEESK
Protein: Uncharacterized protein (Q4GZ89)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MTEIVSDNYFPPNDKLGETPSVPNEATPPLESPSSTTENATSLKREENTSALHSNSLLDTSSSICAFEFNFVIEQDETVRGAIETINALMQAGDINGAVAVAEASQLTIDMLALNGTQLATAMNMTLKYAVRPICGAFLFLFDTAFGVWAMVPSLEGILRKTAHKVENNNTTATSYVATREKPFLWGITGGMDVTNRVYAEVTMLVVCVILCLLIFSIRRLFRHYSASIDTLEAWKQKSWHVQANGAYSPAPLLPLAVNHTHVETLAWEDGLQFANKSKSLHNISPTSSGANLVEDNMSPISLSRTM
Protein: Uncharacterized protein (Q4GZ72)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- Telomerase-associated protein, putative
Sequence:
MGGIPSRDAPTTLFCLRYGTHEVGLIPLVYRYFHSDNKELREQFVRVRNDPSIRYSFMRSPEYRMDEIPKKVYTEKTLDKFLDVIDESLYDSTSAMLADEDAPFRPVPCAVCFVYVNGREGSDCFSFYGRRINIIGHFGCYESEDRVSEGPCLHARKTILKAAGDRTLERVVTLAAMMLKGEFFRAVQTVCPTRDPLAMLKRRLNPLILVASTPWNSYPTLKFVYDTAVIAWAYGKEVVEADPPRLSMYEIEQSGEGGLCMRVSGSVLLWAVMRVCETLTLSAVRGSWEQYVLDDFEMQQKEKIVSQWLSTSPHVNSFLGSETFTDLVQKRLATLLREVVRARETPTEDTTLWGESQEYSHDGKLYRIFNSPTCGPFLATVKKKVPKRGSSANTGNASITSATGGDSASDRRSSGVHLTDSPSSGGENKSRSSGQGNPRSKNNGNQPSGFPAHNNAGQPPQYKDAVNSVLQSQFATAAQRVVYQMPPPVGKTSQGQVSVSPQMSPQFVPMFQTAPPPPMQQFSVPYVVMAPPESQPQPQPQPQPQPQPQMGMVFPSTVANYVLLPDGRVGMINAPAPPTMGFWGQ
Protein: SWI/SNF related, matrix associated, actin dependent regulator of chromatin, subfamily a, member 2 (A0A1B0GWA8)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MSTPTDPGAMPHPGPSPGPGPSPGPILGPSPGPGPSPGSVHSMMGPSPGPPSVSHPMPTMGSTDFPQEGMHQMHKPIDGIHDKGIVEDIHCGSMKGTGMRPPHPGMGPPQSPMDQHSQGYMSPHPSPLGAPEHVSSPMSGGGPTPPQMPPSQPGALIPGDPQAMSQPNRGPSPFSPVQLHQLRAQILAYKMLARGQPLPETLQLAVQGKRTLPGLQQQQQQQQQQQQQQQQQQQQQQQPQQQPPQPQTQQQQQPALVNYNRPSGRLIRNQMNNAMVQLG
Protein: Proenkephalin-A [Cleaved into: Synenkephalin; Met-enkephalin (Opioid growth factor) (OGF); PENK(114-133); PENK(143-184); Met-enkephalin-Arg-Ser-Leu; Leu-enkephalin; PENK(238-259); Met-enkephalin-Arg-Phe] (P22005)
Organism: Mus musculus (Mouse)
Function: Neuropeptide that competes with and mimic the effects of opiate drugs. They play a role in a number of physiologic functions, including pain perception and responses to stress.
Subcellular location: Cytoplasmic vesicle, secretory vesicle, chromaffin granule lumen {ECO:0000250|UniProtKB:P01211}. Secreted {ECO:0000250|UniProtKB:P01211}.
Interaction partners:
- Mu-type opioid receptor
- Delta-type opioid receptor
- Nociceptin receptor
- Pro-opiomelanocortin
- Kappa-type opioid receptor
- Proenkephalin-B
- Somatostatin
- Protachykinin-1
- Prepronociceptin
- Opioid growth factor receptor
Sequence:
MARFLRLCTWLLALGSCLLATVQAECSQDCAKCSYRLVRPGDINFLACTLECEGQLPSFKIWETCKDLLQVSRPEFPWDNIDMYKDSSKQDESHLLAKKYGGFMKRYGGFMKKMDELYPMEPEEEANGGEILAKRYGGFMKKDADEGDTLANSSDLLKELLGTGDNRAKDSHQQESTNNDEDMSKRYGGFMRSLKRSPQLEDEAKELQKRYGGFMRRVGRPEWWMDYQKRYGGFLKRFAESLPSDEEGENYSKEVPEIEKRYGGFMRF
Protein: DnaJ homolog subfamily C member 7 (Tetratricopeptide repeat protein 2) (TPR repeat protein 2) (Q99615)
Organism: Homo sapiens (Human)
Function: Acts as co-chaperone regulating the molecular chaperones HSP70 and HSP90 in folding of steroid receptors, such as the glucocorticoid receptor and the progesterone receptor. Proposed to act as a recycling chaperone by facilitating the return of chaperone substrates to early stages of chaperoning if further folding is required. In vitro, induces ATP-independent dissociation of HSP90 but not of HSP70 from the chaperone-substrate complexes. Recruits NR1I3 to the cytoplasm (By similarity).
Subcellular location: Cytoplasm {ECO:0000269|PubMed:11573955, ECO:0000269|PubMed:12853476}. Nucleus {ECO:0000269|PubMed:11573955}. Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:Q9QYI3}. Note=Colocalizes with NR1I3 to microtubules. {ECO:0000250|UniProtKB:Q9QYI3}.
Interaction partners:
- Heat shock 70 kDa protein 4
- Heat shock protein HSP 90-alpha
- Heat shock cognate 71 kDa protein
- Heat shock 70 kDa protein 1A
- Heat shock 70 kDa protein 1-like
- Heat shock protein HSP 90-beta
- Mitochondrial import receptor subunit TOM34
- Heat shock-related 70 kDa protein 2
- BAG family molecular chaperone regulator 2
- BAG family molecular chaperone regulator 5
Sequence:
MAAAAECDVVMAATEPELLDDQEAKREAETFKEQGNAYYAKKDYNEAYNYYTKAIDMCPKNASYYGNRAATLMMLGRFREALGDAQQSVRLDDSFVRGHLREGKCHLSLGNAMAACRSFQRALELDHKNAQAQQEFKNANAVMEYEKIAETDFEKRDFRKVVFCMDRALEFAPACHRFKILKAECLAMLGRYPEAQSVASDILRMDSTNADALYVRGLCLYYEDCIEKAVQFFVQALRMAPDHEKACIACRNAKALKAKKEDGNKAFKEGNYKLAYELYTEALGIDPNNIKTNAKLYCNRGTVNSKLRKLDDAIEDCTNAVKLDDTYIKAYLRRAQCYMDTEQYEEAVRDYEKVYQTEKTKEHKQLLKNAQLELKKSKRKDYYKILGVDKNASEDEIKKAYRKRALMHHPDRHSGASAEVQKEEEKKFKEVGEAFTILSDPKKKTRYDSGQDLDEEGMNMGDFDPNNIFKAFFGGPGGFSFEASGPGNFFFQFG
Protein: Prolyl 4-hydroxylase subunit alpha-1 (4-PH alpha-1) (EC 1.14.11.2) (Procollagen-proline,2-oxoglutarate-4-dioxygenase subunit alpha-1) (P13674)
Organism: Homo sapiens (Human)
Function: Catalyzes the post-translational formation of 4-hydroxyproline in -Xaa-Pro-Gly- sequences in collagens and other proteins.
Subcellular location: Endoplasmic reticulum lumen.
Interaction partners:
- Protein disulfide-isomerase
- Prolyl 4-hydroxylase subunit alpha-2
- Proline dehydrogenase 1, mitochondrial
- Hydroxyproline dehydrogenase
- Proline dehydrogenase
- Pyrroline-5-carboxylate reductase 1, mitochondrial
- Pyrroline-5-carboxylate reductase 3
- Pyrroline-5-carboxylate reductase 2
- Cytosol aminopeptidase
- Procollagen-lysine,2-oxoglutarate 5-dioxygenase 1
Sequence:
MIWYILIIGILLPQSLAHPGFFTSIGQMTDLIHTEKDLVTSLKDYIKAEEDKLEQIKKWAEKLDRLTSTATKDPEGFVGHPVNAFKLMKRLNTEWSELENLVLKDMSDGFISNLTIQRQYFPNDEDQVGAAKALLRLQDTYNLDTDTISKGNLPGVKHKSFLTAEDCFELGKVAYTEADYYHTELWMEQALRQLDEGEISTIDKVSVLDYLSYAVYQQGDLDKALLLTKKLLELDPEHQRANGNLKYFEYIMAKEKDVNKSASDDQSDQKTTPKKKGVAVDYLPERQKYEMLCRGEGIKMTPRRQKKLFCRYHDGNRNPKFILAPAKQEDEWDKPRIIRFHDIISDAEIEIVKDLAKPRLRRATISNPITGDLETVHYRISKSAWLSGYENPVVSRINMRIQDLTGLDVSTAEELQVANYGVGGQYEPHFDFARKDEPDAFKELGTGNRIATWLFYMSDVSAGGATVFPEVGASVWPKKGTAVFWYNLFASGEGDYSTRHAACPVLVGNKWVSNKWLHERGQEFRRPCTLSELE
Protein: Secretoglobin, family 3A, member 1 (E9PU36)
Organism: Rattus norvegicus (Rat)
Interaction partners:
- Uteroglobin
- BPI fold-containing family A member 1
- Pneumo secretory protein 1
- BPI fold-containing family B member 1
Sequence:
MKLTAIFLVFCVALLSDSGVAFFVESLAKPVVEPVAALAPAAEAVAGAVPSLPLSHLAILRFILASLGIPLDPLIDGSRKCVTELGPEAVGAVKSLLGALTTFG
Protein: Actin, aortic smooth muscle (EC 3.6.4.-) (Alpha-actin-2) (Cell growth-inhibiting gene 46 protein) [Cleaved into: Actin, aortic smooth muscle, intermediate form] (P62736)
Organism: Homo sapiens (Human)
Function: Actins are highly conserved proteins that are involved in various types of cell motility and are ubiquitously expressed in all eukaryotic cells.
Subcellular location: Cytoplasm, cytoskeleton.
Interaction partners:
- Myosin-11
- Actin, gamma-enteric smooth muscle
- Vitamin D-binding protein
- Myosin regulatory light polypeptide 9
- Actin, alpha cardiac muscle 1
- Myosin-10
- Transgelin
- Myosin-9
- Myosin light polypeptide 6
- Myosin light chain 6B
Sequence:
MCEEEDSTALVCDNGSGLCKAGFAGDDAPRAVFPSIVGRPRHQGVMVGMGQKDSYVGDEAQSKRGILTLKYPIEHGIITNWDDMEKIWHHSFYNELRVAPEEHPTLLTEAPLNPKANREKMTQIMFETFNVPAMYVAIQAVLSLYASGRTTGIVLDSGDGVTHNVPIYEGYALPHAIMRLDLAGRDLTDYLMKILTERGYSFVTTAEREIVRDIKEKLCYVALDFENEMATAASSSSLEKSYELPDGQVITIGNERFRCPETLFQPSFIGMESAGIHETTYNSIMKCDIDIRKDLYANNVLSGGTTMYPGIADRMQKEITALAPSTMKIKIIAPPERKYSVWIGGSILASLSTFQQMWISKQEYDEAGPSIVHRKCF
Protein: DExH-box ATP-dependent RNA helicase DExH9 (EC 3.6.4.13) (Protein MTR4 homolog) (AtMTR4) (Q9XIF2)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: ATP-dependent RNA helicase that associates with the RNA exosome complex. Required for proper rRNA biogenesis and development. Involved in the 3'-processing of the 7S pre-RNA to the mature 5.8S rRNA and also in the removal of rRNA maturation by-products.
Subcellular location: Nucleus, nucleolus {ECO:0000269|PubMed:21682783, ECO:0000269|PubMed:25144737}.
Interaction partners:
- Protein RRP6-like 2
- Exosome complex component RRP41 homolog
- Exosome complex component RRP4 homolog
- Exosome complex exonuclease RRP46 homolog
- rRNA biogenesis protein RRP5
- Protein RRP6-like 3
- Bystin
- Protein RRP6-like 1
- Transducin family protein / WD-40 repeat family protein
- Periodic tryptophan protein 2
Sequence:
MGSVKRKSVEESSDSAPPQKVQREDDSTQIINEELVGCVHDVSFPENYVPLAPSVHNKPPAKDFPFTLDSFQSEAIKCLDNGESVMVSAHTSAGKTVVASYAIAMSLKENQRVIYTSPIKALSNQKYRDFKEEFSDVGLMTGDVTIDPNASCLVMTTEILRSMQYKGSEIMREVAWIIFDEVHYMRDSERGVVWEESIVMAPKNSRFVFLSATVPNAKEFADWVAKVHQQPCHIVYTDYRPTPLQHYVFPAGGNGLYLVVDEKSKFHEDSFQKSLNALVPTNESDKKRDNGKFQKGLVIGKLGEESDIFKLVKMIIQRQYDPVILFSFSKKECEALAMQMSKMVLNSDDEKDAVETIFASAIDMLSDDDKKLPQVSNILPILKRGIGVHHSGLLPILKEVIEILFQEGLIKCLFATETFSIGLNMPAKTVVFTNVRKFDGDKFRWLSSGEYIQMSGRAGRRGIDKRGICILMVDEKMEPAVAKSMLKGSADSLNSAFHLSYNMLLNQLRCEEGDPENLLRNSFFQFQADRAIPDLEKQIKSLEEERDSLVIEEEESLKNYYNLILQYKSLKKDIREIVFTPKYCLPFLLPNRAVCLDCTNDDEEPQSFSIEDQDTWGVIMKFNKVKSLSEDDDSRRPEDANYTVDVLTRCMVSKDGVGKKKVKAVPIKERGEPVVVTVPLSQIKSLSSAIMNIPKDLVPLEARENALKKVSELLSRHPDGIPLDPEVDMKIKSSSYKKTVRRLEALENLFEKHKIAKSPLITEKLKVLQMKEELIAKIKSLKKTVRSSTALAFKDELKARKRVLRRLGYITSDNVVELKGKVACEISSAEELTLTELMFSGIFKDAKVEELVSLLSCFVWRERLPDAAKPREELDLLFIQLQDTARRVAEVQLDCKVEIDVESFVQSFRPDIMEAVYAWAKGSKFYEVMEIARVFEGSLIRAIRRMEEVLQQLIVAAKSIGETQLEAKLEEAVSKIKRDIVFAASLYL
Protein: Aconitate hydratase (Aconitase) (EC 4.2.1.3) (Q388J9)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- Citrate synthase
- Isocitrate dehydrogenase
- Isocitrate dehydrogenase
- 50S ribosomal protein L17, putative
- Small ribosomal subunit protein mS29
- Succinate--CoA ligase subunit alpha, mitochondrial
- Large ribosomal subunit protein mL46
- Large ribosomal subunit protein mL43
- Large ribosomal subunit protein uL29m
- Large ribosomal subunit protein uL5
Sequence:
MLSTMKLLKASLPSNNPFLKYIATLSVDGGQAQYFKLHEIDPRYDGLPFSIRVLLESAVRNCDEFDITSKAVENILSWSENCHKSIEIPFKPARVVLQDFTGVPCVVDLAAMRDATKRLGGDVDKINPQIPVELVVDHSVQVDSYGTPEAAKLNQDIEMQRNRERFEFLKWGSEAFHNLLIVPPGSGIVHQVNLEYLARVVFNNDGVLYPDSVVGTDSHTTMVNGVGVIGWGVGGIEAEAGMLGQSLSMVLPEVVGYRFTGKLSEGCTATDLVLTVVRNLRKLGVVGKFVEFYGPGVDTLSLPDRATLANMAPEYGATTGFFPIDQETLNYLRCTGRDAEHLARIEKYTKATKMFRTGDEKISYSQNIELDLSTVEPSLAGPKRPHDHILLRNMKQDFEACLGAKTGFKGFGIPDGEHKKEVKYTVDGKEAVMRHGSVVIAAITSCTNTSNPNVLIAAGLLAKKAVEKGLKVPAGVKTSLSPGSHVVTKYLENSGLQSFLDELRFHTTGYGCMTCIGNAGDVDPAVSKCINDNNFVAAAVLSGNRNFEARIHPQTAANYLASPPLVVAYALAGRVNIDFATEPIANDVYLRDIWPTNDEVSAVVREHVTPDLFKTVYKSITTLNEQWNGLKVKGGTQYEWQESTYIHKPPYFEKMTMEVTPNVVFKNAACLAVFGDSITTDHISPAGNIAKDSPAAQFLQGLGVARKDFNTYGARRGNDMVMVRGTFANTRLGNRIVGEGQTGPFTIHWPTNEKVYIFDAAMRYAEENTPLVILAGKEYGSGSSRDWAAKGPFLQGVKVVIAESFERIHRSNLVGMGIVPLQFRQGESVESLGLTGRERFNFDFSGGIHPGQEVTVQKDDGSSFSAILRIDTEMEVKYVEHGGILQYVLREKIKGNL
Protein: Cytochrome P450 71B2 (EC 1.14.-.-) (O65788)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}.
Interaction partners:
- Protein indeterminate-domain 4
Sequence:
MTILLCFFLVSLLTIVSSIFLKQNKTSKFNLPPSPSSLPIIGNLHHLAGLPHRCFHKLSIKYGPLVFLRLGSVPVVVISSSEAAEAVLKTNDLECCSRPKTVGSGKLSYGFKDITFAPYGEYWREVRKLAVIELFSSKKVQSFRYIREEEVDFVVKKVSESALKQSPVDLSKTFFSLTASIICRVALGQNFNESGFVIDQDRIEELVTESAEALGTFTFSDFFPGGLGRFVDWLFQRHKKINKVFKELDAFYQHVIDDHLKPEGRKNQDIVTLILDMIDKQEDSDSFKLNMDNLKAIVMDVFLAGIDTSAVTMIWAMTELIRNPRVMKKAQESIRTTLGLKKERITEEDLGKVEYLNHILKETFRLHPALPFVVPRETMSHIKIQGYDIPPKTQIQLNVWTIGRDPKRWNDPEEFNPERFANSSVDFRGQHFDLLPFGSGRRICPGMPMAIASVELALMNLLYYFDWSMPDGTKGEDIDMEEAGNISIVKKIPLQLVPVQRY
Protein: D-ribulose kinase (D-ribulokinase) (EC 2.7.1.47) (Probable sugar kinase) (SePSK) (Q31KC7)
Organism: Synechococcus elongatus (strain ATCC 33912 / PCC 7942 / FACHB-805) (Anacystis nidulans R2)
Function: Exhibits ATP hydrolysis without substrate. Phosphorylates D-ribulose.
Interaction partners:
- Ribulose-phosphate 3-epimerase
- 6-phosphogluconate dehydrogenase, decarboxylating
- Ribose-5-phosphate isomerase A
- Small ribosomal subunit protein uS15
- Ribonuclease H
- Threonine--tRNA ligase
- S-adenosylmethionine synthase
Sequence:
MVVALGLDFGTSGARAIACDFDSDRSVSVSVTFPKTSQNWPQVWREALWQLLTQIPADWRSRIERIAIDGTSGTVLLCDREGQPQTEPLLYNQACPIDLADLADWVPADHAALSSTSSLAKLWFWQQQFGALPPDWQILAQADWLSLQLHGCSQQSDYHNALKLGYSPDRERFSKNLLDSELGALLPVVHEPGVAIGPILPAIAQEFGLSPDCQICAGTTDSIAAFLASGAHQPGEAVTSLGSTIVLKLLSQVAVSDRLTGVYSHKLGGYWLTGGASNCGGATLRQFFPDTELESLSCQIDPTKKSGLDYYPLPSRGERFPIADPDRLPQLEPRPENPVQFLQGLLEGLTQVETLGYQRLQDLGATPLKRIWTAGGGAKNAVWQQLRQQAIGVPIAIAPNTEAAFGTARLAAFGLAAFHSAGLKRT
Protein: Endoglucanase (EC 3.2.1.4) (Q9RAI8)
Organism: Myxobacter sp. AL-1
Interaction partners:
Sequence:
MKAFFFVLLLTFAMLFMPASGKADIASAKESQNYAELLQKSILFYEAQRSGKLPESSRLNWRGDSALEDGKDVGHDLTGGWYDAGDHVKFGLPMAYSAAVLSWSVYEYRDAYEAAGQLDAILDNIRWATDYFIKAHTDRYEFWGQVGNGAQDHAWWGPAEVMPMKRPAYKIDAACPGSDLAGGTAAALASASRLRSTDAVNRDSFVRRASSSCAHAKELYDFADRYRGKYSDCITDAHEYYNSWSGYKDELTWGAVWLYLATGDQKYLDKALASVSDWGDPANWPYRWTLSWDDVSYGAQLLLARLTNESRFTASVERNLDYWSTGYNHNGSTERITYTPGGLAWLEQWGSLRYASNAAFLAFVYSDWVKDAGKAKRYRDFAVQQMNYMLGDNPQQRSFIVGYGTNPPKHPHHRTAHGSWADHMNVPENHRHTLYGALVGGPGKDDSYRDETNDYVSNEVAIDYNAAFTGNAAKMFQTVWCRAITAAHFPEKETPEDEFFAEASINSSGNNYSEIRVQLNNRSGWPAKKTDKLSFRYYVDLTEAVNAGFSSEDIKISTGYNEGASVSQLKPYHIGEHIYYTEVSFSGVMIYPGGQSAHKKEVQFRLAAPAGTSFWNPKNDHSYRGLSHTLAKTRYIPVYDEGRLVFGNEPD
Protein: Fibronectin type-III domain-containing protein (D3DEL8)
Organism: Caenorhabditis elegans
Subcellular location: Cell junction {ECO:0000256|ARBA:ARBA00004282}.
Interaction partners:
Sequence:
MIVGRHVELAEHHHQSYAVVDEEVTNLTSHEVQFRVSAYGRTGFGPASNPSLPVKIPISETDLATSAGAPLAPGRPTVIAVDGQGVLLEWTPPVADVHSSPPQGYQVEYRVYGSRDWIVANEQLVQENVFTVESLRPNGVYEFRVRGKNQDGLGHPSMSSGGVAIRPAAPQRHVPARKVSESVQPPGQPQMVEVGDDVVKLEWAPSVQNARYIVEYREVGDPEWHTANYDPIVQNGIQVEGLHRNSTYEFCVISIVDNIASQPSETSDIIHLRPTCNTSALRPAPNILEAPEFLEVDGDKITICWLPAQSQLPVMGYDVEFRDLQQDDRWYKVNDQPVFACKMTVGDLIMDHDYQFRVLAHNASGCSQPSPPSDFVHIEPSTNRFSSDTMESPHLGHHDVVKYVEAERFGAVPLLQEEMVRESPPLPERDDSPPPLRRANNNVQWRDPSLKEVIEYLSSADKDKQLNASGYLQHLTYTDNQIKEETREYGGIPKLIALLRSDTPRIQKNACACLKNLSFGKENDANKLAVMEADGVRLIAEVLRTTHDASVKEEAAAALWNLSSADMLKPVILESATEILSQQVIAPVLAVGTSDPTRHFGSTLFKNSTGVLRNVSAASQQARRRLRDIPNLIEALVHFLTHAIQKSQVDSPTVENAVCLLRNLSYRIQEVVDPNYDPAAAHSSSSKNMKHVASPKPEKKKKDKEKKKDKNPKNIVTGPSVLWQPHVVKLYLKLLQDSSNIETLEASAGAIQNLAACQFPPSAEVRAAVRVEKGLPVLVELIRLPEDFVVCAVATALRNLAIDPRNRELIGKYALRDFLDKLPEPGSPRRSAISDQTIGAVLGILFEIVRSSAAYTKDVHELKGTDKLRALSRSYPTYSHRVCKYASQVLYVMWQHKELHDGFKRSGLKEADFYSGTARRGDSSTLARPISSQGRERPSMHQLDETLSSGGGYGTMESNNRAGTLRPASATSQTIQRRYDQVPRDGPVYSSVQKPSPRGGGGGGNIDDSWV