wanglab/gogpt-training-data huggingface dataset:
Protein: Secretory carrier-associated membrane protein (Secretory carrier membrane protein) (G5EED5)
Organism: Caenorhabditis elegans
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141, ECO:0000256|RuleBase:RU363122}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141, ECO:0000256|RuleBase:RU363122}.
Interaction partners:
- Apical junction molecule ajm-1
- Uncharacterized protein R10E11.6
Sequence:
MSDNPFADPFSAPPPPPAAAAAASKPTSGGTIETEDFNPFANRAGGSNAQPTTHQSTGSLGNKSAGMDDELFRKQQDLERRAQELRMREEELDRRQRSAAGGNNLNTNAQNNAPRPHNWPPLPTIIPIEPCFYQDIEVEIPVQFQKTVTFAYYVFLMYVLALVVNVLASLFYMIFAGGSIGQLFLACIQLALFSPCSFLFWFRPVYKAFRNDSSFNFMVFFFVLFFHCIFTFVQTLGLSNYACGWINALDTFNVSVPIALLMLISAITFTVALTGMVTALVKVHRLYRGAGFSIDKARQEFTNGVMSDAGVQRATQAATQAAAGAAFNQATQGRF
Protein: Protein-tyrosine-phosphatase (Q95Y26)
Organism: Caenorhabditis elegans
Interaction partners:
Sequence:
MSDDTSASVWNDGGPPEIQEQKPKSPPPPLPTSNPVVKDTPNVVPTGDLIQFESEEERAATTVPNGNPVIFEKNPAMDGLLREFLKEEEAYTPQDYLRRFYQIRVEQEKLRMEAEYRSECAVAPQHYARNRYRDILPYDKNRVEIQKDSENPEGYMNASLIQLPGGKTEFIAAQAPLPATLDEWWKMIDEHRVSLVVILCKLVELNKIKCERYWPEQVGESELFGDYEITLEEEKLFDDDEYLMRCLKMENQTTGECRKVHQLHYREWPDHGCPSGEKQLLNMIDLMENIHEEVSPQDSSPILVHCSAGVGRTGTIIAINFIREQMKAETLHSIDIFGLVMTLRKQRASMVQTQDQFQFVHRCIASYCRRHLGIIEEPKLDLAPPVATADLPVGSSGSVRLIAPPTPTTGPSTDQTATIANYNQLHHHQSSSNHMDEDTSTEEAASVPDFPEEPPAPMGPEDLGSSAAF
Protein: Septin-5 (Cell division control-related protein 1) (CDCrel-1) (Peanut-like protein 1) (Q9JJM9)
Organism: Rattus norvegicus (Rat)
Function: Filament-forming cytoskeletal GTPase (By similarity). May play a role in cytokinesis (Potential). May play a role in platelet secretion (By similarity).
Subcellular location: Cytoplasm {ECO:0000250}. Cytoplasm, cytoskeleton {ECO:0000250}.
Interaction partners:
- Septin-11
- E3 ubiquitin-protein ligase parkin
- Septin-8
- Septin
- Neuronal-specific septin-3
- Septin-12
- Septin-2
- Septin-7
- Septin-10
- Septin-1
Sequence:
MSTGLRYKSKLATPEDKQDIDKQYVGFATLPNQVHRKSVKKGFDFTLMVAGESGLGKSTLVHSLFLTDLYKDRKLLSAEERINQTVEILKHTVDIEEKGVKLKLTIVDTPGFGDAVNNFECWKPITDYVDQQFEQYFRDESGLNRKNIQDNRVHCCLYFISPFGHGLRPVDVGFMKALHEKVNIVPLIAKADCLVPSEIRKLKDRIREEIDKFGIHVYQFPECDSDEDEDFKQQDRELKESAPFAVIGSNTVVEAKGQRVRGRLYPWGIVEVENQAHCDFVKLRNMLIRTHMHDLKDVTCDVHYENYRAHCIQQMTSKLTQDSRMESPIPILPLPTPDSETEKLIRMKDEELRRMQEMLQKMKQRMQDQ
Protein: Fumarate hydratase, mitochondrial (Fumarase) (EC 4.2.1.2) (P08417)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Catalyzes the reversible stereospecific interconversion of fumarate to L-malate. In mitochondrion, catalyzes the hydration of fumarate to L-malate in the tricarboxylic acid (TCA) cycle to facilitate a transition step in the production of energy in the form of NADH. In cytoplasm and nucleus, involved in DNA repair in response to DNA damage: following DNA double-strand breaks (DSBs), translocates from the cytosol to the nucleus and promotes DNA repair by catalyzing the dehydration of L-malate to fumarate.
Subcellular location: Mitochondrion matrix {ECO:0000269|PubMed:11502169, ECO:0000269|PubMed:11585823, ECO:0000269|PubMed:20231875, ECO:0000269|PubMed:3040736}. Cytoplasm {ECO:0000269|PubMed:11502169, ECO:0000269|PubMed:11585823, ECO:0000269|PubMed:20231875, ECO:0000269|PubMed:3040736}. Nucleus {ECO:0000269|PubMed:20231875}. Note=Mitochondrial, cytoplasmic and nuclear forms are derived from a single translation product and not by alternative initiation of the transcript (PubMed:11585823). The mitochondrial transit peptide is cleaved by the mitochondrial processing peptidase, promoting mitochondrial targeting of around 70% of the proteins (PubMed:11585823). The remaining 30% of the processed proteins localize in the cytosol: they probably undergo rapid folding into an import-incompetent state, leading to retrograde movement of the processed proteins back to the cytosol through the translocation pore (PubMed:11585823). Translocates from the cytosol to the nucleus in response to DNA damage (PubMed:20231875). {ECO:0000269|PubMed:11585823, ECO:0000269|PubMed:20231875}.
Interaction partners:
- NAD-dependent malic enzyme, mitochondrial
- Malate dehydrogenase, mitochondrial
- Succinate dehydrogenase flavoprotein subunit, mitochondrial
- Malate dehydrogenase, peroxisomal
- Succinate dehydrogenase iron-sulfur subunit, mitochondrial
- Succinate dehydrogenase cytochrome b small subunit, mitochondrial
- Succinate dehydrogenase cytochrome b subunit
- Malate dehydrogenase, cytoplasmic
- Succinate dehydrogenase flavoprotein subunit 2, mitochondrial
- Citrate synthase, mitochondrial
Sequence:
MLRFTNCSCKTFVKSSYKLNIRRMNSSFRTETDAFGEIHVPADKYWGAQTQRSFQNFKIGGARERMPLPLVHAFGVLKKSAAIVNESLGGLDPKISKAIQQAADEVASGKLDDHFPLVVFQTGSGTQSNMNANEVISNRAIEILGGKIGSKQVHPNNHCNQSQSSNDTFPTVMHIAASLQIQNELIPELTNLKNALEAKSKEFDHIVKIGRTHLQDATPLTLGQEFSGYVQQVENGIQRVAHSLKTLSFLAQGGTAVGTGLNTKPGFDVKIAEQISKETGLKFQTAPNKFEALAAHDAIVECSGALNTLACSLFKIAQDIRYLGSGPRCGYHELMLPENEPGSSIMPGKVNPTQNEALTQVCVQVMGNNAAITFAGSQGQFELNVFKPVMIANLLNSIRLITDAAYSFRVHCVEGIKANEPRIHELLTKSLMLVTALNPKIGYDAASKVAKNAHKKGITLKESALELGVLTEKEFDEWVVPEHMLGPK
Protein: VopF (C5IZN1)
Organism: Vibrio cholerae
Interaction partners:
Sequence:
MFKISVSQQANVMSTSDTAQRSSLKISIKSICNKSLSKKLHTLAEKCRRFSQELKEHTASKKQIVEQATTTVRESSLTKSDSELGSSRSLLTSDVLSSSSSHEDLTAVNLEDNDSVFVTIESSSELIVKQDGSIPPAPPLPGNIPPAPPLPSAGNIPTAPGLPKQKATTESVAQTSDNRSKLMEEIRQGVKLRATPKSSSTEKSASDPHSKLMKELINHGAKLKKVSTSDIPVPPPLPAAFASKPTDGRSALLSEIAGFSKDRLRKAGSSETLNVSQPTVAESSIPEAYDLLLSDEMFNLSPKLSETELNTLADSLADYLFKAADIDWMQVIAEQTKGSTQATSLKSQLEQAPEYVKAFCDEILKFPDCYKSADVASPESPKAGPSSVIDVALKRLQAGRNRLFSTIDAKGTNELKKGEAILESAINAARSVMTAEQKSALLSSNVKSATFKVFSELPCMEGFAEQNGKAAFNALRLAFYSSIQSGDTAQQDIARFMKENLATGFSGYSYLGLTSRVAQLEAQLAALTTK
Protein: Phytoene synthase 1, chloroplastic (OsPSY1) (EC 2.5.1.32) (Q5Z5B7)
Organism: Oryza sativa subsp. japonica (Rice)
Function: Catalyzes the conversion of geranylgeranyl diphosphate to phytoene. Mediates the first committed step in carotenoid biosynthesis.
Subcellular location: Plastid, chloroplast membrane {ECO:0000269|PubMed:18326788}; Peripheral membrane protein {ECO:0000305}. Plastid, chloroplast, plastoglobule {ECO:0000269|PubMed:23023170}.
Interaction partners:
- 15-cis-phytoene desaturase, chloroplastic/chromoplastic
- aldehyde oxygenase
- Probable solanesyl-diphosphate synthase 3, chloroplastic
- Solanesyl-diphosphate synthase 2, chloroplastic
- Os07g0580900 protein
- prolycopene isomerase
- Os02g0668100 protein
- Geranylgeranyl diphosphate reductase, chloroplastic
- Phytoene synthase 3, chloroplastic
- Phytoene synthase 2, chloroplastic
Sequence:
MAAITLLRSASLPGLSDALARDAAAVQHVCSSYLPNNKEKKRRWILCSLKYACLGVDPAPGEIARTSPVYSSLTVTPAGEAVISSEQKVYDVVLKQAALLKRHLRPQPHTIPIVPKDLDLPRNGLKQAYHRCGEICEEYAKTFYLGTMLMTEDRRRAIWAIYVWCRRTDELVDGPNASHITPSALDRWEKRLDDLFTGRPYDMLDAALSDTISKFPIDIQPFRDMIEGMRSDLRKTRYKNFDELYMYCYYVAGTVGLMSVPVMGIAPESKATTESVYSAALALGIANQLTNILRDVGEDARRGRIYLPQDELAEAGLSDEDIFNGVVTNKWRSFMKRQIKRARMFFEEAERGVTELSQASRWPVWASLLLYRQILDEIEANDYNNFTKRAYVGKAKKLLALPVAYGRSLLMPYSLRNSQK
Protein: Zinc finger protein SNAI1 (Protein snail homolog 1) (Protein sna) (Q02085)
Organism: Mus musculus (Mouse)
Function: Involved in induction of the epithelial to mesenchymal transition (EMT), formation and maintenance of embryonic mesoderm, growth arrest, survival and cell migration. Binds to 3 E-boxes of the E-cadherin gene promoter and to the promoters of CLDN7 and KRT8 and, in association with histone demethylase KDM1A which it recruits to the promoters, causes a decrease in dimethylated H3K4 levels and represses transcription. Involved in induction of the epithelial to mesenchymal transition (EMT), formation and maintenance of embryonic mesoderm, growth arrest, survival and cell migration. Binds to 3 E-boxes of the E-cadherin/CDH1 gene promoter and to the promoters of CLDN7 and KRT8 and, in association with histone demethylase KDM1A which it recruits to the promoters, causes a decrease in dimethylated H3K4 levels and represses transcription. The N-terminal SNAG domain competes with histone H3 for the same binding site on the histone demethylase complex formed by KDM1A and RCOR1, and thereby inhibits demethylation of histone H3 at 'Lys-4' (in vitro) (By similarity). During EMT, involved with LOXL2 in negatively regulating pericentromeric heterochromatin transcription. SNAI1 recruits LOXL2 to pericentromeric regions to oxidize histone H3 and repress transcription which leads to release of heterochromatin component CBX5/HP1A, enabling chromatin reorganization and acquisition of mesenchymal traits. Associates with EGR1 and SP1 to mediate 12-O-tetradecanoylphorbol-13-acetate (TPA)-induced up-regulation of CDKN2B, possibly by binding to the CDKN2B promoter region 5'-TCACA-3'. In addition, may also activate the CDKN2B promoter by itself.
Subcellular location: Nucleus {ECO:0000269|PubMed:12832491}. Cytoplasm {ECO:0000269|PubMed:12832491}. Note=Once phosphorylated (probably on Ser-107, Ser-111, Ser-115 and Ser-119) it is exported from the nucleus to the cytoplasm where subsequent phosphorylation of the destruction motif and ubiquitination involving BTRC occurs. {ECO:0000250|UniProtKB:O95863}.
Interaction partners:
- Mothers against decapentaplegic homolog 3
- Histone deacetylase 1
- Histone-lysine N-methyltransferase EZH2
- Lysine-specific histone demethylase 1A
- DNA
- Histone-lysine N-methyltransferase EHMT2
- Histone deacetylase 2
- Mothers against decapentaplegic homolog 4
- Lysyl oxidase homolog 3
- Lysyl oxidase homolog 2
Sequence:
MPRSFLVRKPSDPRRKPNYSELQDACVEFTFQQPYDQAHLLAAIPPPEVLNPAASLPTLIWDSLLVPQVRPVAWATLPLRESPKAVELTSLSDEDSGKSSQPPSPPSPAPSSFSSTSASSLEAEAFIAFPGLGQLPKQLARLSVAKDPQSRKIFNCKYCNKEYLSLGALKMHIRSHTLPCVCTTCGKAFSRPWLLQGHVRTHTGEKPFSCSHCNRAFADRSNLRAHLQTHSDVKRYQCQACARTFSRMSLLHKHQESGCSGGPR
Protein: CASP-like protein 2A1 (AtCASPL2A1) (Q8VZQ3)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Cell membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}.
Interaction partners:
- Receptor-like protein 31
- Receptor-like protein 3
- Wall-associated receptor kinase-like 22
Sequence:
MEKSNDHDKASHGGSGGGATEKWEETSLGIRTAETMLRLAPVGLCVAALVVMLKDSETNEFGSISYSNLTAFRYLVHANGICAGYSLLSAAIAAMPRSSSTMPRVWTFFCLDQLLTYLVLAAGAVSAEVLYLAYNGDSAITWSDACSSYGGFCHRATASVIITFFVVCFYIVLSLISSYKLFTRFDPPSIVDSAKNLEVAVFGS
Protein: Tubby-related protein 1 (Tubby-like protein 1) (Q9Z273)
Organism: Mus musculus (Mouse)
Function: Required for normal development of photoreceptor synapses. Required for normal photoreceptor function and for long-term survival of photoreceptor cells. Interacts with cytoskeleton proteins and may play a role in protein transport in photoreceptor cells. Binds lipids, especially phosphatidylinositol 3-phosphate, phosphatidylinositol 4-phosphate, phosphatidylinositol 5-phosphate, phosphatidylinositol 3,4-bisphosphate, phosphatidylinositol 4,5-bisphosphate, phosphatidylinositol 3,4,5-bisphosphate, phosphatidylserine and phosphatidic acid (in vitro) (By similarity). Contribute to stimulation of phagocytosis of apoptotic retinal pigment epithelium (RPE) cells and macrophages.
Subcellular location: Cytoplasm. Cell membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Secreted. Synapse. Note=Detected at synapses between photoreceptor cells and second-order neurons. Does not have a cleavable signal peptide and is secreted by an alternative pathway.
Interaction partners:
- Tyrosine-protein kinase Mer
- Growth arrest-specific protein 6
- Aryl-hydrocarbon-interacting protein-like 1
- Tyrosine-protein kinase receptor TYRO3
- Retinoid isomerohydrolase
- Lecithin retinol acyltransferase
- X-linked retinitis pigmentosa GTPase regulator-interacting protein 1
- Retinol dehydrogenase 12
- Spermatogenesis-associated protein 7 homolog
- Vitamin K-dependent protein S
Sequence:
MPLQEETLREVWASDSGHEEDCLSPEPPLRPKQRPAQGQKLRKKKPETPDSLESKPRKAGAGRRKHEEPPADSAEPRAAQTVYAKFLRDPEAKKRDPRENFLVARAPDLGGEENSEEDSDDDDNDDDEEEEEKKEGKKEKSSLPPKKAPKEREKKAKALGPRGDVGSPDAPRKPLRTKKKEVGEGTKLRKAKKKGPGETDKDPAGSPAALRKEFPAAMFLVGEGGAAEKGVKKKGPPKGSEEEKKEEEEEVEEEVASAVMKNSNQKGRAKGKGKKKVKEERASSPPVEVGEPREFVLQPAPQGRAVRCRLTRDKKGMDRGMYPSYFLHLDTEKKVFLLAGRKRKRSKTANYLISSDPTNLSRGGENFIGKLRSNLLGNRFTVFDNGQNPQRGGGGDVGSLRQELAAVVYETNVLGFRGPRRMTVIIPGMNSDNERVPIRPRNASDGLLVRWQNKTLESLIELHNKPPIWNEDSGSYTLNFQGRVTQASVKNFQIVHADDPDYIVLQFGRVAEDAFTLDYRYPLCALQAFAIALSSFDGKLACE
Protein: RhoGAP18B-PC (Q00IM9)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MPQQAKDINDNVGMEAHIYENLPGLTSTPKGHLNAELRKYFPREAIYENLCRGCGYGVFAAQGRYCHFCQCIVSGGVVSTPPPPPPPPLSTISGESSNIYENICDLCRGIYSDNERCRCQRSETPAKAPAPSTPTTPPTPPTKVKSRSLLGYSKSSAATLTRLFGSLKQLNRSSSLQRRIFPRTPTTGSSSAGSLEIIHNVDEVFRTQETFDLQRICELKLEQQQLKGSQSDQHIYGRVREPEESQSHKRERKRPRVSRIRLLQDESTSGSSSLYLNESICQWMTSLRRQVHHYDEGPWQQPKSVPARDPSSSAEESTVTLRRSTEESAKCADEQAKLVKDFKRKLQQKRAHNVEPEREQRRCAITANFVNDYLSALGEEKEAVQHQQVAAIEEHVAVVAIAIQPQVSVSLLRLMQSLALSASLHVSVRGFLTAYDKSFSLWLWHQQQQQRQQPPINGYRRRRARDSVVGVVGDWRRRLPLFAFSFAGGNDRSVASASVSVSPAISESVDVCAAAASRRRANRSTRRRGTAIVREEGVCGGESSTSSNNSKKNNNNNSNNNSGALMAAPKPNGEAERPSTNSNNNTINCSSNNNNDNISNNNNNHHTVDNESGINNNKNNDGNANCNVNEQQQQQQQQPITQNCVIKVRRPAPKVPVRNPNTSLSNPRQIEEEQTKPNGGKKDNLRGNSFAAENSSPEEQEEESIYQPIWQFKTIEPVDQEIIEALPVEGEDEEDEDEEDDDVEDEEEDLGDYDESLPSDADPDVMALQAAAVFAAGVRHKLSTSTLTKRSKMMMPTPLPSPTASMDHGAWETDMEFMYSRESKEEADETLSLGSTVTNSTATLGSISSTGSSVTGQPKDTPKDLPADQQPSVVVHPILRNICIFYSQKDPKKYSAIFYDYHLSLVHQRFMTRIRRPAPPPPAQLATSNTTSLAPRSDDSGCSCEAEDSYNHQHNPTPAIPKPLKEEWERAVLAAGAVAGKRGVAPRTGRKLRVRSNARLLLTDSVLAWRETLQDVNCCEDEEDMIVPVTDILRAQQIQEDNEVQQTQQSTILQRYKSVSIGNLLDLPGEDDKKSIKNRMRMKFAVNSNVFRINRSPKSEKKSRSRRGQVNSLYLDEQKYPLFAAPLSALELNMTDHPNVPRFVVDVCAYIEQPECIEQDGLYRASGNKVLVDELRKKLTHVYDPRWLKTDDIHTLTSLHKQFFRELTSPLITQEAYERLGRSLNDDAAIERMSLAFDDMPEPNRSTLRFLIRHLTRVAAASASNRMPSTNLAIVWGPCLLSANQIQLDIGRMNMLAKVLIENYDRIFHPDNERLVC
Protein: Acetolactate synthase isozyme 3 small subunit (EC 2.2.1.6) (ALS-III) (Acetohydroxy-acid synthase III small subunit) (AHAS-III) (P00894)
Organism: Escherichia coli (strain K12)
Interaction partners:
- Acetolactate synthase isozyme 1 large subunit
- Acetolactate synthase isozyme 3 large subunit
- Ketol-acid reductoisomerase
- 3-isopropylmalate dehydrogenase
- L-threonine dehydratase biosynthetic IlvA
- Acetolactate synthase isozyme 2 small subunit
- 2-isopropylmalate synthase
- D-malate dehydrogenase [decarboxylating]
- L-threonine dehydratase catabolic TdcB
- Pyruvate dehydrogenase
Sequence:
MRRILSVLLENESGALSRVIGLFSQRGYNIESLTVAPTDDPTLSRMTIQTVGDEKVLEQIEKQLHKLVDVLRVSELGQGAHVEREIMLVKIQASGYGRDEVKRNTEIFRGQIIDVTPSLYTVQLAGTSGKLDAFLASIRDVAKIVEVARSGVVGLSRGDKIMR
Protein: Neurogenic differentiation factor 1 (NeuroD) (P46581)
Organism: Caenorhabditis elegans
Function: Acts as a transcriptional regulator whose activity is required for several aspects of motor neuron fate specification, including cell division patterns, proper spatiotemporal expression of fate-specific markers, and normal axonal morphology and pathfinding. Involved in regulating glial specification.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00981}.
Interaction partners:
- Transcription factor sox-2
- Helix-loop-helix protein hlh-2
Sequence:
MRPTDTSNFAPAEISKRKVRRVKANGRERARMHGLNNALDMLREYIPITTQHQKLSKIETLRLARNYIDALQRMLQTNEQPTPLEYAHTLANGLSQTTTNMLANLLQVQPRQLLPPSQFDIFSDPSHHQLHPSHPPPHSSFSSSSPSSSCSPPQYYYSPTQPSAAPLQGSCDPQYQQMYHQHSHQNTFNYSP
Protein: Germacrene D synthase 2 (EC 4.2.3.75) (PatTpsBF2) (Q49SP6)
Organism: Pogostemon cablin (Patchouli) (Mentha cablin)
Function: Sesquiterpene synthase involved in germacrene D biosynthesis.
Subcellular location: Cytoplasm, cytosol {ECO:0000250}.
Interaction partners:
Sequence:
MELKNQSVAIISSNASRPLAHYHPDVWGDRFLLYKPNPSSEAGQKPVIEELKQQVRSELKEASNDYMRQLKMVDAIQRLGIESLFEEDIDNALKNLSENFDDYCKDKHDLYAIALSFRLLRQHGYRISCDVFDKLKDGEDGFKVPPSDEALAVVELLEATHLRIHGEVVLDRAFVFARIHLESIEANLNNPVAKQVHNALYGYSNRRGMQQVEARKYIPIYEQYASHHQGLLKLATLNFNLQQTMHKRELSELSRWYRDLEVPTMLPFARQRLVETYFWDAGVVFEPENDVARMILVKVQCLISFLDDTFDAYGSFEELQLFTDAINTWDVSCLDQLPDYMKIIYKALLGVFEVIEKLMIKQGTLYRLNYAKEAMKIVVGGYFVEAKWREEKSKPTTQEYMQVATKSAGYMTLIITSFLGMEANIATKEAFDWVLSEPDVMKAAITLARLTNDIVGIELEKERKHIATAVEVYEDEHKLSMQEAMVEIKNQIESGWKTINEAFLRPTKFPTPILYRILNYCRVLEVIYDKSDRYTHVDPALQDIIKQLYIHPIP
Protein: Cytochrome c (Q4QEN5)
Organism: Leishmania major
Subcellular location: Mitochondrion intermembrane space {ECO:0000256|ARBA:ARBA00004569}.
Interaction partners:
- Putative reiske iron-sulfur protein
- Putative cytochrome c1, heme protein,mitochondrial
- Putative elongation factor Tu
- Cytochrome c peroxidase, mitochondrial
- Acyl-lipid
- Metallo-peptidase, Clan ME, Family M16
- Putative mitochondrial processing peptide beta subunit
- MYND-type domain-containing protein
- Thioredoxin domain-containing protein
- TROVE domain-containing protein
Sequence:
MPPKARAPLPPGDVERGEKLFKGRAAQCHTATKGGSNGVGPNLFGIVNRPSGKVEGFTYSKANAESGVIWTPEVLDVYLENPKKFMPGTKMSFAGIKKPQERADVIAYLETLK
Protein: Large ribosomal subunit protein eL24 (60S ribosomal protein L24) (V9HW01)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MKVELCSFSGYKIYPGHGRRYARTDGKVFQFLNAKCESAFLSKRNPRQINWTVLYRRKHKKGQSEEIQKKRTRRAVKFQRAITGASLADIMAKRNQKPEVRKAQREQAIRAAKEAKKAKQASKKTAMAAAKAPTKAAPKQKIVKPVKVSAPRVGGKR
Protein: Uncharacterized protein (Q57UU1)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MRLTSRGSHNSSQVVYLLDTREFITDCSTVRQVTHFAHVHRLGSPLWLSCELASALGLTLRYMCSPLNIWSPLTGESFVQLASSPALARDTLYKFPINKEFLAPGGVLPHNSGEGSLMALSAAASSDGKPRWYNIPKDVSHLFVLPKNLCQLSVPVHRGGFRPRPFNLWVSTVIAVRMGGLAEAVKTVRTPSSFMTLVNADQMYPSALLAEKELECVLLMRKEGRLGEM
Protein: RE56519p (Q8SXH0)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MRAIAMDSLKKKSENISLKEKLTNMELELTQLKTDLIEQQEKNAENIQKYTEINKKYTHCEQHYDKELEIIKVCVEKKNSELRDAQSRMALQAQELNNMQQTNRELAGACENYKKDLEEAEVAKSMILHELTDLKELHEDLQLQFEDVSAQKEKFEANILQLSSDLNAKMLDCAQLEDRIEQLPIEANKALSKLQRDLEASELQFVDQQRLTDQATRELELVRNEINTFKTLIEEKERRHVSLSDELTQMTERLSELADINESYINELTETKLKHSQEIKDQADAYEIVVQELKESLNKASVDFTQLKSNSEKLHKETLLQVSELQEKLIEMVSHRSNQEELIKRLGNEIQEKTHNFEEELKRQQEQLANQMQMKATEVESENKRNAVEIQKLKSELEERNKAFKAQQDKLEYLISDHDTLKSAIINLQAEKKEIESELSTAKVKFSEELQSQKDNLMKKVSELELEIKRKETELIELEREKNNEMAVLQFKMNRINCLIDQPVTTIKQLKDSKGPTRTESIPTKVQPENTDEFSSTARKRNARRQKITTYSSDFDSGDDIPIVGNSLSGKRAKLCAPIKPQNNIDMFDMLKNSK
Protein: Actobindin-B/C (Q55DU1)
Organism: Dictyostelium discoideum (Social amoeba)
Function: Is able to bind two actin monomers at high concentrations of G-actin. Inhibits actin polymerization by sequestering G-actin and stabilizing actin dimers (By similarity).
Interaction partners:
Sequence:
MSTTANPLLAEINKGTDLKHAETQDKSAPIIENVPIKKNDHSSLLGEVEKGAQLKHVETQDRSAPVTEGATVKSNNHSALLGEIKSKAQE
Protein: L-lysine 6-oxidase (EC 1.4.3.20) (L-lysine-epsilon-oxidase) (Marinocine) (F2JXJ3)
Organism: Marinomonas mediterranea (strain ATCC 700492 / JCM 21426 / NBRC 103028 / MMB-1)
Function: Has antibacterial activity against a wide spectrum of Gram-positive and Gram-negative bacteria including nosocomial isolates of S.aureus and Pseudomonas sp. The antimicrobial activity is due to hydrogen peroxide generated by its lysine oxidase activity. Also has autotoxic activity. Involved in biofilm differentiation; responsible for cell death within microcolonies during biofilm development which is linked to the generation of a phenotypically diverse dispersal population and thus may play a role in colonization.
Subcellular location: Secreted {ECO:0000269|PubMed:15652194, ECO:0000269|PubMed:20025674}.
Interaction partners:
- Putative FAD-dependent oxidoreductase LodB
- Fumarate reductase/succinate dehydrogenase flavoprotein domain protein
- FAD dependent oxidoreductase
Sequence:
MALSVHPSIGVARLGNANTDNFVLNPMEIGGLPYEHDVDLKPTTTVVNFKDEAGCIRRQGQVFKVFGASNEELTLDSPNVKNIEWTVHLANKKAAWYEFRELNGNLLYGRDNSYSARGVPWRNASKTASSERQSLIIDLGPRSVSGVMATVEISINNIPETYLHPSYPSGELLQGSKHFESLGTLRTDSQGRLIVLGGYGFAGGNTDLSGYGGGDDWYDDISDGSVTCVVTYSDDSSETSTAWMVVGSPDFAPEIVNISTLSDTCFDVGVRNFDLVPDMYDSATGHYKSDYVANFDRDILPIIQRISQYQWVSNVQSMSGFFSFQFDYRDGSAANKANRMKYYNYFRQLDNKVIGDYDQPQQVLMSSEVEGDILPLMPMNSGSNSVSSSNFYDLTDNVVEKFLALDATQLFLLGQWAEGEFTAGPADDYPVSDMDTASIGNCVGLPMCPGIEMTWSLQNPVIYKDAYQIKHYQDKAYFDVNGLTPERDECEEETGCEPGDLTKRMACPWQADFFNCTIQTVNFSEPSVNKASQTETVTSRTHYEWGNLPAGVSVPDQSSVSATKNVDEKVPLPPAYYSYWWPPQSPWDVLTGELDTEGQLHSHLPAGQQINYARGINSYSQMVEHWSALAFIRDRNQNNDGFPFFTETERNHELFDFKEVLVGQVTGNSEDNETSLPVFFINANKESLEGKGTKKGKLMASYFEERAFSKVRSSNIRPRSGTRMRG
Protein: Acyl-coenzyme A diphosphatase NUDT19 (EC 3.6.1.-) (EC 3.6.1.77) (Nucleoside diphosphate-linked moiety X motif 19) (Nudix motif 19) (A8MXV4)
Organism: Homo sapiens (Human)
Function: Fatty acyl-coenzyme A (CoA) diphosphatase that hydrolyzes fatty acyl-CoA to yield acyl-4'-phosphopantetheine and adenosine 3',5'-bisphosphate (By similarity). Mediates the hydrolysis of a wide range of CoA esters, including choloyl-CoA and branched-chain fatty-acyl-CoA esters and at low substrate concentrations medium and long-chain fatty-acyl-CoA esters are the primary substrates (By similarity). Highest activity seen with medium-chain acyl-CoA esters and higher rates of activity seen with the unsaturated acyl-CoA esters compared with the saturated esters (By similarity). Exhibits decapping activity towards dpCoA-capped RNAs in vitro (By similarity).
Subcellular location: Peroxisome {ECO:0000250|UniProtKB:P11930}.
Interaction partners:
- NAD-capped RNA hydrolase NUDT12
- m7GpppN-mRNA hydrolase NUDT17
- Peroxisomal coenzyme A diphosphatase NUDT7
- NPC intracellular cholesterol transporter 2
- Peroxisomal leader peptide-processing protease
- Nucleotide triphosphate diphosphatase NUDT15
Sequence:
MSSSLRPGPSRWRRAASIVLAAGWSRPETATPPSRPPPAEGFRLLLLQRSPHQGFMPGAHVFSGGVLDAADRSADWLGLFAPHHGPPRFGLGPAPFSRTAFPSLPDTDDHKTDNTGTLPEDVAFRICAVREAFEEAGVLLLRPRTSPPGPAPGPGLALEPPPGLASWRDRVRQDPRHFLRLCAHLDCTPDIWALHNWSAWLTPFLRGTTRRFDTAFFLCCLREPPPVYPDLAEVVGYQWSSPSEATESFLSKEIWLPPPQFYEVRRLANFASLSDLHKFCLGRALEGLERWLPIILLTADGMVHLLPGDELYLEDSDFLENLMSTEKKTEEIMKEGKQFHRIVTYHRHLYDIHVTVQPKYKHVYPKNSVVRKSHL
Protein: Calpastatin (Calpain inhibitor) (B7Z574)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MEGPHLPNKKKHKKQAVKTEPEKKSQSTKLSVVHEKKSQEGKPKEHTEPKSLPKQASDTGSNDAHNKKAVSRSAEQQPSEKSTEPKTKPQDMISAGGESVAGITAISGKPGDKKKEKKSLTPAVPVESKPDKPSGKSGMDAALDDLIDTLGGPEETEEENTTYTGPEVSDPMSSTYIEELGKREVTIPPKYRELLAKKEGITGPPADSSKPIGPDDAIDALSSDFTCGSPTAAGKKTEKEESTEVLKAQSAGTVRSAAPPQEKKRKVEKDTMSDQALEALSASLGTRQAEPELDLRSIKEVDEAKAKEEKLEKCGEDDETIPSEYRLKPATDKDGKPLLPEPEEKPKPRSESELIDELSEDFDRSECKEKPSKPTEKTEESKAAAPAPVSEAVCRTSMCSIQSAPPEPATLKGTVPDDAVEALADSLGKKEADPEDGKPVMDKVKEKAKEEDREKLGEKEETIPPDYRLEEVKDKDGKPLLPKESKEQLPPMSEDFLLDALSEDFSGPQNASSLKFEDAKLAAAISEVVSQTPASTTQAGAPPRDTSQSDKDLDDALDKLSDSLGQRQPDPDENKPMEDKVKEKAKAEHRDKLGERDDTIPPEYRHLLDDNGQDKPVKPPTKKSEDSKKPADDQDPIDALSGDLDSCPSTTETSQNTAKDKCKKAASSSKAPKNGGKAKDSAKTTEETSKPKDD
Protein: ATP-dependent DNA helicase Q-like 3 (EC 5.6.2.4) (DNA 3'-5' helicase RecQ3) (RecQ-like protein 3) (AtRecQ3) (AtRecQl3) (Q9FT72)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: 3'-5' DNA helicase that may play a role in the repair of DNA. Exhibits an ATP or dATP-dependent DNA-helicase activity. Cannot use GTP/dGTP, CTP/dCTP or UTP/dUTP as nucleotide cofactors. Catalyzes DNA strand annealing. On nicked Holliday junctions, unwinds the lagging strand. Cannot act on intact Holliday junctions.
Subcellular location: Nucleus {ECO:0000250}.
Interaction partners:
- Exonuclease 1
- Crossover junction endonuclease MUS81
- AT5G19950 protein
- Serine/threonine-protein kinase ATR
- ATP-dependent DNA helicase Q-like 4B
- ATP-dependent DNA helicase Q-like 4A
- Exonuclease 1
- DNA topoisomerase 3-alpha
- BRCT domain-containing protein At4g02110
- ATP-dependent DNA helicase 2 subunit KU70
Sequence:
MKKSPLPVQNVQSSDKNVAGKEALVKLLRWHFGHADFRGKQLEAIQAVVSGRDCFCLMPTGGGKSICYQIPALAKPGIVLVVSPLIALMENQVMALKEKGIAAEYLSSTQATHVKNKIHEDLDSGKPSVRLLYVTPELIATKGFMLKLRKLHSRGLLNLIAIDEAHCISSWGHDFRPSYRQLSTLRDSLADVPVLALTATAAPKVQKDVIDSLNLRNPLVLKSSFNRPNIFYEVRYKDLLDNAYTDLGNLLKSCGNICAIIYCLERTTCDDLSVHLSSIGISSAAYHAGLNSKMRSTVLDDWLSSKKQIIVATVAFGMGIDKKDVRMVCHFNIPKSMESFYQESGRAGRDQLPSRSVLYYGVDDRKKMEYLLRNSENKKSSSSKKPTSDFEQIVTYCEGSGCRRKKILESFGEEFPVQQCKKTCDACKHPNQVAHCLEELMTTASRRHNSSRIFITSSNNKTNEGQYSEFWNRNEDGSNSNEEISDSDDATEAANSVTGPKLSKKLGLDEKLVLLEQAEEKYYERNKQVKKSEKNAISEALRDSSKQRLLDALTRVLQLLACVEEIDSQKGSEFLENECYRKYSKAGKSFYYSQIASTVRWLGTASRDELMTRLSSVVSLAREQEPLEEPLLATEPVENIEEEDDGKTNTVESRVDEPTQELVVSPILSPIRLPQVPSFSEFVNRRKIKQNTLIDKSSEGFDDKKPAKIMKLQ