wanglab/gogpt-training-data huggingface dataset:
Protein: Uncharacterized protein C14G10.02 (O74415)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Interaction partners:
- rRNA biogenesis protein rrp5
- Probable nucleolar pre-ribosomal-associated protein 2
- Probable metalloprotease arx1
- U3 small nucleolar RNA-associated protein 20
- DNA-directed RNA polymerase I subunit rpa1
- U3 small nucleolar RNA-associated protein 10
- RNA cytidine acetyltransferase
- ATP-dependent RNA helicase dbp6
- ATP-dependent RNA helicase mak5
- Periodic tryptophan protein 2 homolog
Sequence:
MESGSIDLDKEIDELSRVLLEHPAHVEKVLKTVEFDKSALRYIDAILDHHLKQIYRNLTSNSPLHTLSLLQKMASWNNGLACVRVFQAIDWNSKIFIKMLQLPNQIQNSRKGNKRLKITISKKRSSLLLLFITFLRLGTPEIRLEILNSRKLTTPLFKGIYNDEPSVLKELLQCWLTYVLLDHDVSRATKLSYFNEWSLSCLASLYSRDDEIDGISLCNLVHKFFVDACTVPGEGLCFVSNGWHLQKKVDGQSKTIFNRVLQSFVFSLHVHTSTLQRELVLKILKACPDITASFIERNSLTSEPVLSYQWISFVSLLQAILGMGIPFPFYDAETRTVPPTNIIIENILPSSFSKPVVLKALNGNDKFVCFLTVNTLLASFKRLESVLDEIKRSELSEDNKVELVSKISDAILLRLPDSQTFVQLYSSTESDLLKEGLSRILLYFFTYFPENILKLKIDTSIFLRLDLSPGMLDRPFSRLHVENIIQILRYLPEVKWFDVVRSPFVFLCLMYLQTSHSKLRDAIISTLNDVFSQTIIFCPSLAVPPILTILASLQHTSPTQHKAVLEFLNSCINRCISRVFAYLDVCVDCFKKHSVNSQKKTAPEVSPISVTLIEQIPFFLQKRDISDDSKDAVLSWLSDLFSNLVCTGEDANCLFHLLENVNVTAFDSDYTLKPFNQLMSFIESLAVQKLPDYVNQIGSLSQYLLYSTNDELSNSGIQKFGMNLDFLPLYVVIITKRIAIMLQSGDMRVKKFLELIRELVEFSKEETMATSQSPIRTLLSACINLRPFLLQEQYISFNMDFAEFLIDTNASIKGSVVNTCVLDFLYKSFSDKVQENYNLIRIAAKFMLLWTQEEFIGFSKALDSFLSENDDLIYKNLDYVAPLLFECMQFTSTTNANMFSNNSISVLLKAAILKPTKLTHGMFDALNTMKPIISDFTVFEPALHTVENFDLTDCADEQILLLSSFVNFVPLFRKVIWNLLLNNKEALIQKYELLAILCCDLAKQYVAEQSQYDLERIRSFCSEVVENNLDLVLQKSHLIELLFPLMKLSDPKIQYYVKVSNALSEKYLPQGVLELLVLLQKRIDIPSSLRVQTIMRIFAILTRVLSDSPQIGLSLEKFLTNFEALIKMNVDILRDEIDKSTLNSFLESAIVHVTSFSNLRLCLTLAFTMTAEQCDSSRFLQMILAHEKNPLAGEDSSDEIKATMSAIICKLTIIGKNYTLSVLDQILKLFKGRYTLHDSLLCELLAYFETLDDISVASRYKGWVITDEYDMMLLARKDGSGVLEPKIAANTVNQYPSEWEKIDLKVFDDLETTEGLLSSYCSNEWNREVYHPLYALGITASLLHSNQQVSNIQVIVQQNFLGMIVMGLSLFKEEARFACLNFLRNFIPILDEQKFREKHLIKLVLASIIVNVPSSENRLSTLMANFYAFSLTVMMKPTHPLFVGINRYYLQRQHVDVTDIPMYYELLYPSTDYTKSVYWLLTLLHAGLQTNQDLKIYLRRHVFEMICTLYNSCVVNSEIRTLIEKILLKVVALGGGPMLVKYNAIYPMLQMVIPSFQETKENTVVSTT
Protein: Small ribosomal subunit protein eS1 (Q6NXR8)
Organism: Homo sapiens (Human)
Subcellular location: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03122}. Nucleus {ECO:0000256|HAMAP-Rule:MF_03122}. Nucleus, nucleolus {ECO:0000256|ARBA:ARBA00004604}. Note=Localized in cytoplasmic mRNP granules containing untranslated mRNAs. {ECO:0000256|HAMAP-Rule:MF_03122}.
Interaction partners:
Sequence:
MAVSKNKRLTKGGKKGAKKKVVDPFSKKDWYDVKAPAMFNIRNIGKTLVTRTQGTKIASDGLKGRVFEVSLADLQNDEVAFRKFKLITEDVQGKNCLTNFHGMDLTRDKMCSMVKKWQTMIEAHVDVKTTDGYLLRLFCVGFTKKRNNQIRKTSYAQHQQVRQIRKKMMEIMTREVQTNDLKEVVNKLIPDSIGKDIEKACQSIYPLHDVFVRKVKMLKKPKFELGKLMELHGEGSSSGKATGDETGAKVERADGYEPPVQESV
Protein: Ribose import ATP-binding protein RbsA (EC 7.5.2.7) (P04983)
Organism: Escherichia coli (strain K12)
Function: Part of the ABC transporter complex RbsABC involved in ribose import. Responsible for energy coupling to the transport system.
Subcellular location: Cell inner membrane {ECO:0000255|HAMAP-Rule:MF_01716, ECO:0000305|PubMed:25533465}; Peripheral membrane protein {ECO:0000255|HAMAP-Rule:MF_01716, ECO:0000305|PubMed:25533465}.
Interaction partners:
- Ribose import permease protein RbsC
- Ribose import binding protein RbsB
- D-ribose pyranase
- Probable ABC transporter permease protein YphD
- Autoinducer 2 import system permease protein LsrC
- Ribokinase
- L-arabinose transport system permease protein AraH
- D-allose transport system permease protein AlsC
- Autoinducer 2 import system permease protein LsrD
- High-affinity branched-chain amino acid transport system permease protein LivM
Sequence:
MEALLQLKGIDKAFPGVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGTLLWLGKETTFTGPKSSQEAGIGIIHQELNLIPQLTIAENIFLGREFVNRFGKIDWKTMYAEADKLLAKLNLRFKSDKLVGDLSIGDQQMVEIAKVLSFESKVIIMDEPTDALTDTETESLFRVIRELKSQGRGIVYISHRMKEIFEICDDVTVFRDGQFIAEREVASLTEDSLIEMMVGRKLEDQYPHLDKAPGDIRLKVDNLCGPGVNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVTRSPQDGLANGIVYISEDRKRDGLVLGMSVKENMSLTALRYFSRAGGSLKHADEQQAVSDFIRLFNVKTPSMEQAIGLLSGGNQQKVAIARGLMTRPKVLILDEPTRGVDVGAKKEIYQLINQFKADGLSIILVSSEMPEVLGMSDRIIVMHEGHLSGEFTREQATQEVLMAAAVGKLNRVNQE
Protein: Caffeine dehydrogenase subunit beta (EC 1.17.5.2) (Caffeine dehydrogenase medium subunit) (D7REY4)
Organism: Pseudomonas sp. (strain CBB1)
Function: Catalyzes the hydrolitical oxidation of 1,3,7-trimethylxanthine (caffeine) by incorporation of an oxygen atom originating from a water molecule into position C-8 to produce 1,3,7-trimethyluric acid (TMU). Coenzyme Q0 is the preferred electron acceptor and coenzyme Q2 can also be used, but oxygen and NADP cannot.
Interaction partners:
Sequence:
MKPTAFDYIRPTSLPEALAILAEHSDDVAILAGGQSLMPLLNFRMSRPALVLDINDISELQQVRCENDTLYVGSMVRHCRVEQEEIFRSTIPLMSEAMTSVAHIQIKTRGTLGGNLCNAHPASEMPAVITALGASMVCKSEKRGERVLTPEEFFEGALQNGLQSDELLCEIRIPVPSQYVGWAFEEVARRHGDFAQCGAAVLIGAEDRKIDYARIALCSIGETPIRFHALEQWLIGRPVGNDLPADVKLHCREILDVAEDSTMTAENRAKLASAVTSRAIARAADRIVHLDVKRG
Protein: LD32410p (SAGA factor-like TAF6, isoform A) (Q9VPT4)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Transcription initiation factor TFIID subunit 12
- SAGA complex subunit Spt3
- Transcriptional adapter 1-2
- SAGA-associated factor 11 homolog
- Enhancer of yellow 2 transcription factor
- Transcriptional adapter 2b
- SAGA complex subunit Spt7
- Transcription initiation factor TFIID subunit 9
- Transcription initiation factor TFIID subunit 10b
- Protein will decrease acetylation
Sequence:
MKTSGASNTDELNKSSHSKVSKKSTKSRSKSAKLELTGKNSLSASASSSIASAVSGGVAVGSLPATPTHLNMVTTPTTPTSSLGNYNLFDASFAVAGSGGHGLAGGIAGAEASGNSSRMGHQKSYAGFDPRSIKIFWEQHDQTDVELSQDVCARLAEDASYKVWELINNVKIYSRHSGGVVTYDLVNEVLKDADVPPMLGAMDSDWDRIDYDGSFYFHSDKIFELSAEFQKEVNLCTPDDADFQSICPVEDKHMDQLRQCVQSLVTAALFADSKSQTAAVCHAFQTPLMGSIYRVIVSKMVQLLAFKQQDHLSQRCWRLLRACNYNATANHNACRPEYFNLAEVLVSQLMAPYETIKAPHVDPDPGQTTSIKMEFEEELKVEPDQCHNPETQENPEVMGVEKQEQEPQMFPGESTMEHTIYKLQSEEEELNPQPEAEHLSSYFACPVGNGLVDELCETIGQLASQSGYLHAECLFLIKRRLARFFEGRHVSSERDFRYISRAVRGLIALGEYAFREFIPYIYKLRVEEIPDSLWPDLAPAAIFLGGHDDVYLYEWLEYGCGAALQPFLVHYARAYEKMVTRRYVKAKQPAYRIESVPGVRRLEWSTLAAAMCHGDDPSKALKPKPTLCEAFPDLQSPNLQLNCAGNIRFKFAGCRPVLLKPKVATVPHSEDSPSSAANGGGGGGASSDILIAKRKLFKPLTNVRKWSPISGYHYLRI
Protein: Glutaredoxin domain-containing cysteine-rich protein 1 (Q50H32)
Organism: Mus musculus (Mouse)
Function: May play a role in actin filament architecture in developing stereocilia of sensory cells.
Subcellular location: Cell projection, stereocilium {ECO:0000269|PubMed:20137774}. Cell projection, microvillus {ECO:0000269|PubMed:20137774}. Cell projection, kinocilium {ECO:0000269|PubMed:20137774}. Note=In the inner ear, localized to stereocilia, apical microvilli of sensory cells and kinocilia.
Interaction partners:
- Taperin
- Unconventional myosin-VIIa
- Fascin-2
- Rho family-interacting cell polarization regulator 2
- Glutaredoxin domain-containing cysteine-rich protein 2
- Chloride intracellular channel protein 5
- Xin actin-binding repeat-containing protein 2
- Myosin-9
- Plastin-1
- Twinfilin-1
Sequence:
MLRRETKPESDRPRKVRFRIASSHSGRVLKEVYEDGQAPGSLDSECASICAIDGLSDSEGQQNGHIGSEDNEQEKDQDNLLVLARTASEKAFGTRRVNILSKNGTVRGVKYKVSAGQALFNNLTKVLQQPSADLEFDRVVIYTTCLRVVRTTFERCELVRKIFQNHRVKFEEKNIALNGDYGKELDERCRRVSEAPSLPVVFIDGHYLGGAEKILSMNESGELQDLLTKIERVQHPHECPSCGGFGFLPCSVCHGSKMSVFRNCFTDAFKALKCTACNENGLQRCKNCTC
Protein: M-zodatoxin-Lt8g (M-ZDTX-Lt8g) (Cytoinsectotoxin-1g) (CIT-1g) (P85259)
Organism: Lachesana tarabaevi (Spider)
Function: Insecticidal, cytolytic and antimicrobial peptide. Has insecticidal activity against the flesh fly S.carnaria. Has antibacterial activity against the Gram-negative bacteria E.coli. Forms voltage-dependent, ion-permeable channels in membranes. At high concentration causes cell membrane lysis.
Subcellular location: Secreted {ECO:0000269|PubMed:18215128, ECO:0000269|PubMed:27287558}.
Interaction partners:
Sequence:
MKYFVVALALVAAFACIAESKPAESEHELAEVEEENELADLEDAVWLEHLADLSDLEEARGFFGNTWKKIKGKADKIMLKKAVKIMVKKEGISKEEAQAKVDAMSKKQIRLYVLKHYGKKALQKASEKL
Protein: ATP-dependent Clp protease proteolytic subunit 1 (EC 3.4.21.92) (Endopeptidase Clp 1) (Q9I2U1)
Organism: Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Function: Cleaves peptides in various proteins in a process that requires ATP hydrolysis. Has a chymotrypsin-like activity. Plays a major role in the degradation of misfolded proteins.
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00444}.
Interaction partners:
- ATP-dependent Clp protease ATP-binding subunit ClpX
- ATP-binding protease component ClpA
- Chaperonin GroEL
- Co-chaperonin GroES
- Chaperone protein DnaK
- Chaperone protein ClpB
- Lon protease
- ATP-dependent Clp protease adapter protein ClpS
- ATP-dependent protease ATPase subunit HslU
- Lon protease
Sequence:
MSRNSFIPHVPDIQAAGGLVPMVVEQSARGERAYDIYSRLLKERIIFLVGQVEDYMANLVVAQLLFLEAENPEKDIHLYINSPGGSVTAGMSIYDTMQFIKPNVSTTCIGQACSMGALLLAGGAAGKRYCLPHSRMMIHQPLGGFQGQASDIEIHAKEILFIKERLNQILAHHTGQPLDVIARDTDRDRFMSGDEAVKYGLIDKVMTQRDLAV
Protein: Dihydropyrimidine dehydrogenase [NADP(+)] (DHPDHase) (DPD) (EC 1.3.1.2) (Dihydrothymine dehydrogenase) (Dihydrouracil dehydrogenase) (Q28007)
Organism: Bos taurus (Bovine)
Function: Involved in pyrimidine base degradation. Catalyzes the reduction of uracil and thymine. Also involved the degradation of the chemotherapeutic drug 5-fluorouracil.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:Q12882}.
Interaction partners:
- Uridine 5'-monophosphate synthase
- Dihydropyrimidinase
- Uridine phosphorylase
- Uridine phosphorylase
- Beta-ureidopropionase 1
- Uracil phosphoribosyltransferase homolog
- Purine nucleoside phosphorylase
- Cytochrome b5 reductase 4
- NADH-cytochrome b5 reductase
- Oxidoreductase NAD-binding domain-containing protein 1
Sequence:
MAPVLSKDVADIESILALNPRTQSRATLRSTLAKKLDKKHWKRNPDKNCFNCEKLENNFDDIKHTTLGERGALREAMRCLKCADAPCQKSCPTNLDIKSFITSISNKNYYGAAKMIFSDNPLGLTCGMVCPTSDLCVGGCNLYATEEGPINIGGLQQYATEVFKAMNIPQIRNPSLPPPEKMPEAYSAKIALLGAGPASISCASFLARLGYNDITIFEKQEYVGGISTSEIPQFRLPYDVVNFEIELMKDLGVKIICGKSLSVNDITLSTLKEEGYKAAFIGIGLPEPKKDHIFQGLTQDQGFYTSKDFLPLVAKSSKAGMCACHSPLLSIRGTVIVLGAGDTAFDCATSALRCGARRVFIVFRKGFVNIRAVPEEVELAREEKCEFLPFLSPRKVIVKGGRIVAMQFVRTEQDETGKWNEDGDQIACLKADVVISAFGSVLSDPKVKEALSPIKFNRWDLPEVDPETMQTSEPWVFAGGDVVGIANTTVEAVNDGKQASWYIHRYIQSQYGASVSAKPELPLFYTPIDLVDISVEMAALKFTNPFGLASATPTTSSSMIRRAFEAGWAFALTKTFSLDKDIVTNVSPRIIRGTTSGPMYGPGQSSFLNIELISEKTAAYWCQSVTELKADFPDNIVIASIMCSYNRNDWMELSRKAEASGADALELNLSCPHGMGERGMGLACGQDPELVRNICRWVRQAVRIPFFAKLTPNVTDIVSIARAAKEGGANGVTATNTVSGLMGLKADGTPWPAVGREKRTTYGGVSGTAIRPIALRAVTTIARALPEFPILATGGIDSAESGLQFLHGGASVLQVCSAIQNQDFTIIQDYCTGLKALLYLKSIEELQDWDGQSPATKSHQKGKPVPCIAELVGKKLPSFGPYLEKCKKIIAEEKLRLKKENVTVLPLERNHFIPKKPIPSVKDVIGKALQYLGTYGELNNTEQVVAVIDEEMCINCGKCYMTCNDSGYQAIQFDPETHLPTVTDTCTGCTLCLSVCPIIDCIKMVSRTTPYEPKRGLPLAVNPVS
Protein: Very long-chain specific acyl-CoA dehydrogenase, mitochondrial (VLCAD) (EC 1.3.8.9) (P49748)
Organism: Homo sapiens (Human)
Function: Very long-chain specific acyl-CoA dehydrogenase is one of the acyl-CoA dehydrogenases that catalyze the first step of mitochondrial fatty acid beta-oxidation, an aerobic process breaking down fatty acids into acetyl-CoA and allowing the production of energy from fats. The first step of fatty acid beta-oxidation consists in the removal of one hydrogen from C-2 and C-3 of the straight-chain fatty acyl-CoA thioester, resulting in the formation of trans-2-enoyl-CoA. Among the different mitochondrial acyl-CoA dehydrogenases, very long-chain specific acyl-CoA dehydrogenase acts specifically on acyl-CoAs with saturated 12 to 24 carbons long primary chains.
Subcellular location: Mitochondrion inner membrane {ECO:0000269|PubMed:9461620, ECO:0000269|PubMed:9599005}; Peripheral membrane protein {ECO:0000269|PubMed:9599005}.; SUBCELLULAR LOCATION: [Isoform 2]: Mitochondrion inner membrane {ECO:0000269|PubMed:17374501}; Peripheral membrane protein {ECO:0000269|PubMed:17374501}.
Interaction partners:
- Trifunctional enzyme subunit alpha, mitochondrial
- Carnitine O-palmitoyltransferase 2, mitochondrial
- Trifunctional enzyme subunit beta, mitochondrial
- 3-ketoacyl-CoA thiolase, mitochondrial
- Enoyl-CoA hydratase, mitochondrial
- 3-ketoacyl-CoA thiolase, peroxisomal
- Peroxisomal bifunctional enzyme
- Peroxisomal acyl-coenzyme A oxidase 1
- Long-chain specific acyl-CoA dehydrogenase, mitochondrial
- Peroxisomal acyl-coenzyme A oxidase 3
Sequence:
MQAARMAASLGRQLLRLGGGSSRLTALLGQPRPGPARRPYAGGAAQLALDKSDSHPSDALTRKKPAKAESKSFAVGMFKGQLTTDQVFPYPSVLNEEQTQFLKELVEPVSRFFEEVNDPAKNDALEMVEETTWQGLKELGAFGLQVPSELGGVGLCNTQYARLVEIVGMHDLGVGITLGAHQSIGFKGILLFGTKAQKEKYLPKLASGETVAAFCLTEPSSGSDAASIRTSAVPSPCGKYYTLNGSKLWISNGGLADIFTVFAKTPVTDPATGAVKEKITAFVVERGFGGITHGPPEKKMGIKASNTAEVFFDGVRVPSENVLGEVGSGFKVAMHILNNGRFGMAAALAGTMRGIIAKAVDHATNRTQFGEKIHNFGLIQEKLARMVMLQYVTESMAYMVSANMDQGATDFQIEAAISKIFGSEAAWKVTDECIQIMGGMGFMKEPGVERVLRDLRIFRIFEGTNDILRLFVALQGCMDKGKELSGLGSALKNPFGNAGLLLGEAGKQLRRRAGLGSGLSLSGLVHPELSRSGELAVRALEQFATVVEAKLIKHKKGIVNEQFLLQRLADGAIDLYAMVVVLSRASRSLSEGHPTAQHEKMLCDTWCIEAAARIREGMAALQSDPWQQELYRNFKSISKALVERGGVVTSNPLGF
Protein: Nuclear matrix constituent protein 1b (OsNMCP1b) (Nuclear matrix constituent protein 1) (OsNMCP1) (Q0JJ05)
Organism: Oryza sativa subsp. japonica (Rice)
Function: Architectural component of nuclear structure that plays different roles in controlling nuclear size and morphology (Probable). Involved in the modification of chromatin accessibility by interacting with SWI3C, a component of the chromatin-remodeling complex, to thus reduce the suppression effect of the complex. Acts as positive regulator of drought resistance and modulates root growth. Positively regulates the expression of genes related to root growth and drought resistance.
Subcellular location: Nucleus matrix {ECO:0000269|PubMed:32129897}. Nucleus lamina {ECO:0000269|PubMed:32129897}. Note=Localizes predominantly at the nuclear periphery. {ECO:0000269|PubMed:32129897}.
Interaction partners:
Sequence:
MASPRSAGGVGGGGGGGGGSGGAAAGDDAIWSKLREAGFDEESLKRRDKAALIAYISRLESEIYQYQHNLGLVLMERKELTSKHEQLRAASESAEIMHKRERAAQQSALAEARKKEENLKKSLGIQKECVANLEKALHDMRGETAETKVSYESKLAEALQLMEAAHKKFDEAEEKLLLAKSLEAESIRTHNAALRSLHDIDDREDQLRRDRISCELENEAKEKEISLQRKSLNDMKKILHEKEEVLLKEQALLNQRDENILERLAYVTHSEKRVEEEKNILEAERKVLLEEKYKLELKMEAIVSREEALIQKESLLDKRESELLILQETIASKERAEIERLNQEQAIALERRKHDFESEMANKQMSFDAAMEVTRNALHQRECALSEQESVVVQRSQNLDLQLAELASKEKALAGRSDELKEEEEKLLLHREAIHNELQKEREEIQRIKSDLEKEKAFFEEEKREAIQAQQDLAITQADRDELLTLQMKLKEEIDSLRAQKRELMADADRLQAEKERFEIEWELIDEKKEELQKEAIRIAEERRAITEYLKNESDIIKQEKDNLRVQFKSNSETLSREHKEFMSKMQQEHASWLSKIQQERQDLKRDIDIQRVELLNSAKARQMEIDSYLREREEEFEQKKAKELEHINSQKEMINTKLEHVAVELQKLKDERKEATLERERREQELSEIKGTIEALNNQREKLQEQRKLLHSDREAITVQIQQLNVLEELKIDSENKQLSLLQHDKSKLGSDINVKDNHHDNSHSSPKQRFGRKLDLSPVSTPISWVRKCAQVIFKRSPEKSASHDQFVQNGVPKKVGDSVDVEDVNLDFAKVGQKRLNHLVSCDQTEVLEPKRKHRRSTIQKVNGGEITSNCLSALEEKCSKNEHDEAPLGLSNTCKEHEYGDKGPENLTKPGEPASSVDVPYVNGIVDNSDSVQEEPSVEATVSATETSNVDGPEDNNDSDEEDEEEEEEKTSSAKKLWRFLIT
Protein: Peroxisomal ATPase PEX1 (Peroxin-1) (Q9VUC7)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004370}.
Interaction partners:
- Peroxisomal ATPase PEX6
- Peroxisomal membrane protein PEX13
- Peroxisomal targeting signal 1 receptor
- Peroxisome assembly protein 12
- RING-type E3 ubiquitin transferase
- Peroxisomal membrane protein PEX14
- Peroxin-19
- Peroxisomal biogenesis factor 3
- Peroxisome biogenesis factor 2
- Peroxin-7
Sequence:
MFKRTFKVVYRPIRSNFVLLPDQYYGVVSTYDTGCLSLQYNGRTHYASWAPQKGGGGIKDTEIGINARAAKEIGLHENDLVKCALIADVLNLRSVHVTPVSSKDWEIIELSTEKISGSVLEQTRIVNSTQILIVWINKSMQVALTVDRLKPHMNYGRIDHNTELVVAPNLYKGLTNGTSNGVIEENTKLSRSKTTAQVKDELTEKLTPLTHSSTVSNVKNTIQRNKRQDHMERLKKDLRRESSRSFEFRVIRGLWREQAQESDVFVNGKHLPEFFDLDLFYCMHTAADKDYYVRVRTVEDDIEDDLPETIHPSIELNANLMKLLGIKELERVVLRPKTTVVNFVEKIELFANKKTHYKIMENAFKRFVIERTQHKPMLFNQEEVVRLEDDLLVTVGILPEHFRYCVVDAQFLKESKIYAADLVRPVGEIIKEETPPTSPLSVQDLIQLPEYDKIVDQVVQELRMNLCLSADNSVMRQCNVLLAGASGTGKTVLVERILDQLSRKPDYCHFEFFHGSRSKGRKTESIQKDLRNIFTSCLQHAPAIVVLENLDVLAHAAGEQSSQDGEYYNRMADTVYQLIVQYTTNNAIAVIATVNELQTLNKRLSSPRGRHVFQTVARLPNLERADREIILRELCSHINVAKDLDLVKFSNLTEGYRKCDLVQFVERAIFYAYRISKTQPLLTNDQLIESLEHTNSYCLQGIQSNQRTGNDADANEMRVEELPGLESVVGVLEEVLMWPSRYPTIFNASPLRNQAGVLLYGPPGTGKTYLVSQLATSWNLRIISVKGPELLAKYIGQSEENVRNLFNRARSARPCVLFFDEFDSLAPKRGHDSTGVTDRVVNQLLTELDGVEGLQGVTVIAATSRPELLDPALLRSGRIDRLVECPLPDAPARVRIFEALSSTLSLDECVDFDWFAGKTANYTGADIQSILTSANMAAVKEALAQFGHEKLAKKISLKQKHLIESFQTTRPSLSASDVAKYHRTYARFTNKEKTSREFVAKRATLA
Protein: Male gametocyte surface protein P230p (O96175)
Organism: Plasmodium falciparum (isolate 3D7)
Function: Plays an essential role in male gamete fertility (By similarity). Required for the binding to erythrocytes and thus, for the formation of exflagellation centers (By similarity).
Subcellular location: Cell surface {ECO:0000269|PubMed:12106866}. Cell membrane {ECO:0000269|PubMed:12106866, ECO:0000269|PubMed:30297725}; Peripheral membrane protein {ECO:0000305}. Note=Present on the surface of male gametocytes. {ECO:0000269|PubMed:12106866, ECO:0000269|PubMed:30297725}.
Interaction partners:
Sequence:
MFIYLFIYLFFKMDKKRTFYYLFFFFTFLVYVLYFDNIKSVLRSSTKKKKKKKICKSTFYVHEESEEIKSWLRNSNERDKGKKFFIFERLIKERKYICVNKYKRNNKLKWIYKNTYEKTKNICDDYNILFKCIKGIIYDKNKETFFETFFENFWDNIFYMNKYIFNIYYYMFDYTKKVKKKIEGIKENMNIRHNNNYNNIFYVHKFFLFNDDEEKKKRNDDIKINIKLHNNTRKLSVSEENVELKPYIKQGERNETVVNLYEYFTGGVKRSNNNNEIVVTSTEQFHRIVIICFKPTVKHSHIITSPHDALNHIVEENDKIKLSEEIYSIPFYPIYGNLGLKNVITTGIVEFMIPYFSRTQMNFTVTCANGEMNDLYKFEDLIKIRIRIPRNTKKILGLSTNEKDKTVFERIVDNTSNEYRFKSYNNKIVGIKLENSILDPPGCFKTVYEDDKILQLEVFLQYVKCINLDRDNYKIRFFFLPEDFGDEEIEFSCKFTYKKKTSKIIFGLGETSVDKDIFYLEDEHVKLNINQDISGDEPYYSHLNYNGIPYNICNFQYKSEYDSQVCERTIHEFSLFIYNCDTLVGTQIQTTEPITSVKYLNSTYPINKFSDITLLSKDIDIEGLEEAFRNSKFFLTSYINHGPFPLIIECVISNSNKDYQNVYILLHLRTSIKNRSVSFCDFEKVQGYNYLNNYIDGKICNINITSNSVFGFRCPSNSIKEPKDCFSQVYIDKKVYKLNDKLSNKLILYSMKQENLAIAGFNNYISNSFSFECYCIDKNQTYSSYERTSGEDIFNHIVKRIHVHYKNYDELYDYNIHDKITYEPIMKNPPITYLCDFLNKKQILQPLNNKTKNYICTIWYPKPLNYIALNCPTNRRDEQNDQTISEVYNSLQKDLLKPTGIEQQIDQKKKELNLLFNKRNIYSNLYHLPKNAPKRTINKNGLNIVNIDEIIPGILIKDVINMKLEDVIKPDLLTPTSFLHKTYNTNKSYLFSTRNKSTSVFNTPSIYTPLTHTSFSISPKSVPLTKSRIEETHSSSNTYEQYIGKRNSIENGFFIFQLPPYLKKNQTIEFACINDSTIKNKNVGNNGIMTIHLKSFGNPIEGCYFYKNSAKYNYLKKSIKIDDLKKEECTIRSDGEIEFVGIMCPYENNLYLTPSSCFLKTYDNTDNLVELLDINENFEYYSNDKGISYLKIPQEFLNHVHLFCYCNVDKDSVSDTNVLVKKENKISLELNYSNKGFNIIKTIDYQYEADILIGYSYYFKRVTPIYRKKHICDFTTEDNSLEPESEDKMIYSCYLSLENNLNFIEVKCPKNKKSSNSEWLFKYGTFDKSSEIMEDDENIKKYEHMKYMPEDKDEIIYLFKKQKLEDILPGVIIFDKNRYFFEKGNFSFVTPLIVKEDVTIKLLCDNSETKIDDKIGKKGIILIKIPQHITDKKFYGCDFSGDSNKKSSFYYTSVYDLKTQNQYCEVKLKENIIISLNCPNGNINPNNCFNNVFLKTNMNEQIHEKIQNIFDQVKVINTKSHVLLNSSSTFLIISKITKKELNFFCTCHHNETKNVGTIYIKNEDIINFSKAYNKESSILQYIDVTPYYLKDTYICDFTQNHYSISFDTSVNVQNVLERYLKILSDLYNTHEEFTYFSIHLKLKKEIMKKKYIDYLKKKINEYKEKETSDKIKRVTLSTNDNINTILVYRCNIDLGSFDKFKIKCPSKLNEEEVENNKLYPNLIYSSNLGLDETDMLNGLTKLLYGSVLINKTEKNVSFFEKGELELIISPYTDSSKNIIFSCENVPRNLSKGIIGSASIFIKKNDNKILGCDFIDTPSTLSSASTLESSYGSHASSPLSSSHHVLHNDNQGHDVHMINHIDISNKKNSFEFEIELIEGKNTYCNIEAIENDIVGFSCPYNFLTTPSDCFESIQIEGVDKELETHKLEKLLKGVKILNNDIYKYNFTPSYIILPKKIKKSLKIFCRCNSVKLIKTGIIQINIVGDDLNNWFKKEITHNIFAYQKMDYFYDFSKGPTNISSENVLGISTMSLMSSNKKVSRKKNHKEENRTQQNVYKEIENDHKNINENVNKYDNLPVTLLSSDEGDGYQADEDIGGEDDAEDVDGEGDDEDDNILNPLRTKQVYDIIVAASEFSKIEVVCPLRNSSQFRQSKISPENFFEYVYVLEDKNDDKRKRSIEENEKLVKAILEGKKNIDGHIINIEDINNKKSSKNASVEYDDMGNKIFISIISEKPKAVIGDNISSSRSSVHISNNIMNSSFQSNIHPDPITSDTTTSEYEQYNSYFKDILVIKNINEVISFANIKIDINEQTYSSSLHIPPLILKDAEFLISCDNSLTLNENTRGKTATVKIKVKSNFLKIYGCDFVGEFSTHFLFSKKWDDIPKNYICKINIQDDMLIGLACPSFTKLHPPDCFENIIVNQNVYKKNIIMETKNMFFYKQNDKPILSFVHVKKILVETFLCKCYQVTKADYKEVTIQILYEPYVMGTPKYTLEKSIIQYRYANLKPPLHI
Protein: Peptidyl-prolyl cis-trans isomerase F, mitochondrial (PPIase F) (EC 5.2.1.8) (Cyclophilin D) (CyP-D) (CypD) (Cyclophilin F) (Rotamase F) (P30404)
Organism: Bos taurus (Bovine)
Function: PPIase that catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides and may therefore assist protein folding. Involved in regulation of the mitochondrial permeability transition pore (mPTP). It is proposed that its association with the mPTP is masking a binding site for inhibiting inorganic phosphate (Pi) and promotes the open probability of the mPTP leading to apoptosis or necrosis; the requirement of the PPIase activity for this function is debated. In cooperation with mitochondrial p53/TP53 is involved in activating oxidative stress-induced necrosis (By similarity). Involved in modulation of mitochondrial membrane F(1)F(0) ATP synthase activity and regulation of mitochondrial matrix adenine nucleotide levels (By similarity). Has anti-apoptotic activity independently of mPTP and in cooperation with BCL2 inhibits cytochrome c-dependent apoptosis (By similarity).
Subcellular location: Mitochondrion matrix {ECO:0000250|UniProtKB:P29117}.
Interaction partners:
- Non-selective voltage-gated ion channel VDAC1
- ADP/ATP translocase 1
- ADP/ATP translocase 3
- Cytochrome c
- Cytochrome c 2
- ADP/ATP translocase 4
- ADP/ATP translocase 2
- Non-selective voltage-gated ion channel VDAC3
- Hexokinase-2
- Non-selective voltage-gated ion channel VDAC2
Sequence:
MMLALRCGPRLLGLLSGPRSAHLRLPAVRACSSGSGSHGSSSSSGNPLVYLDVGADGQPLGRVVLELKADVVPKTAENFRALCTGEKGFGYKGSTFHRVIPSFMCQAGDFTNHNGTGGKSIYGSRFPDENFKLKHEGPGVLSMANAGPNTNGSQFFICTIKTDWLDGKHVVFGHVKEGMDVVKKIESFGSKSGKTSKKIVITDCGQLS
Protein: Defensin ARD1 (P84156)
Organism: Archaeoprepona demophon (One-spotted leafwing butterfly)
Function: Possesses potent anti-fungal activity.
Subcellular location: Secreted {ECO:0000255|PROSITE-ProRule:PRU00710, ECO:0000269|PubMed:14978308}.
Interaction partners:
Sequence:
DKLIGSCVWGAVNYTSNCNAECKRRGYKGGHCGSFANVNCWCET
Protein: Conserved protein (O53448)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Interaction partners:
- Fructose-1,6-bisphosphatase class 2
- Uncharacterized protein Rv0738
- UPF0301 protein Rv0038
- Probable transcriptional regulatory protein
- Uncharacterized protein Rv1488
- Probable conserved transmembrane protein
- Fumarate hydratase class II
- Possible conserved membrane protein
- Carboxylesterase/lipase Culp6
- Conserved protein
Sequence:
MVGDCPRSRTVRWSWDTGHVTAEPQPTPRPAKPRLLQDGRDMFWSLAPLVVGCILLAGLVGMCSFQLGGTKRGPIPSYDAAQALRADAKTLGFPIRLPQLPGGWTPNSGGRGGIENGRADPATGQRRNAATSIVGFISPTGRYLSLTQSNADEDKLVGSIHPSMYPTGTVDVGGTRWVVYEGSDENGAVEPVWTTRLTGPGGATQLAITGAGSIDQFRTLASATQSQPPLPAR
Protein: Lipoyl synthase, mitochondrial (EC 2.8.1.8) (Lipoate synthase) (LS) (Lip-syn) (Lipoic acid synthase) (O43766)
Organism: Homo sapiens (Human)
Function: Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
Subcellular location: Mitochondrion {ECO:0000255|HAMAP-Rule:MF_03123}.
Interaction partners:
- Lipoyl amidotransferase LIPT1, mitochondrial
- Octanoyl-[acyl-carrier-protein]:protein N-octanoyltransferase LIPT2, mitochondrial
- Ankyrin repeat domain-containing protein 54
- Glycine cleavage system H protein, mitochondrial
- NFU1 iron-sulfur cluster scaffold homolog, mitochondrial
- BolA-like protein 3
- Iron-sulfur cluster assembly factor IBA57, mitochondrial
- Iron-sulfur cluster assembly 2 homolog, mitochondrial
- Iron-sulfur cluster assembly 1 homolog, mitochondrial
- Iron-sulfur cluster assembly enzyme ISCU
Sequence:
MSLRCGDAARTLGPRVFGRYFCSPVRPLSSLPDKKKELLQNGPDLQDFVSGDLADRSTWDEYKGNLKRQKGERLRLPPWLKTEIPMGKNYNKLKNTLRNLNLHTVCEEARCPNIGECWGGGEYATATATIMLMGDTCTRGCRFCSVKTARNPPPLDASEPYNTAKAIAEWGLDYVVLTSVDRDDMPDGGAEHIAKTVSYLKERNPKILVECLTPDFRGDLKAIEKVALSGLDVYAHNVETVPELQSKVRDPRANFDQSLRVLKHAKKVQPDVISKTSIMLGLGENDEQVYATMKALREADVDCLTLGQYMQPTRRHLKVEEYITPEKFKYWEKVGNELGFHYTASGPLVRSSYKAGEFFLKNLVAKRKTKDL