wanglab/gogpt-training-data huggingface dataset:
Protein: Uncharacterized protein (Q22A77)
Organism: Tetrahymena thermophila (strain SB210)
Interaction partners:
Sequence:
MQSFVNLIQLEENYNLSLLSYSNSIRQYLLDNKVHEDKYIQLMKDIKDLFSSPTFLMPNFSDKRKQFFSQLCLIAFDFANNQVTEQQSLSEFRKKFKFPFVIIAIIYTKLLEIKEALPEDFLTLVDCHFKNKGPQSIFASLTLISLFLNEVDQYEIDCDHIESSNTLSSCSEAAESNIPKKVNITVKTVQNFFDKQGLQMIAFPLNVIKNIHCVAHDQQSIIQLLLKIVVIIIKNMSNKIKQEFFYFHQKDLNVILSCFIGFLQQNNQAREDRDVALANIFEFCELLAKSTSPAQLYVAFKDFLVYISQNFSFANDSIEYFDFNSKCVDFLVSITPCFIQQSENLSAYPLIIQLLKQSAKINLVNLEDQIGCLHIWSHYSDQFIQAYDNNNNSIKAETINNLAILNSTFIESLQFDIELLFNLQIKDHDSEDVNQFVDQLSRLVIHSNLIDNQLFVEVIKSLSLLYQKNMLLYYTFQKCLMKQYLNSKDTLSQIYQVFGKSNDFLQITELLFESFSQAQKQFANLDLNTIAAIEKFTQFMSQIGAKLFNTQISHLEQSQILGIFQKYILNPIKMFNLNIFSQLPENFIQLNEVQFSQVCTMMESVHYFIFSDNKSNSDQVFETEVDVSMIKKILLFNQSVNQDMAYWINPQLKNERKKIKQFYQSTIYWVIFASINLENAANIFESYFFQKEFNIWVLNSTIKKLKGRILPNTFLLYLCYYLKSLTDSDSFSKIVQKSEYEEKFRKLMVNISKSVPSEIYVDYSKIQYYLQLYINEECQMFRFQILSDQTVSLLTLENRFSHVYKVFIILEDLFTIVQRFPKFYYENTFMGLKRNFFLNRVFWIIVKCFTIVPKQELLENSQIYKTISLYLNLAIRFKMDFLEKEETQSENSHYFNFILEILDHMYFTNKKIVLDFCQKILNYFDQDCYNQNIIQLAQSSQTFQNITLQLFTNIWEQIFNFCSSSNEKAEEFKEKDISQSIDFILKFSKCLQGNLSIIQDRIMLVIKAHPIYSSNSQIIYSTIIENLVIKEIDGVKVLQNVFLKSIIKDLQIWAKSICPQRLQS
Protein: Multifunctional fusion protein [Includes: Interleukin-1; Interleukin-1 beta] (M4WG34)
Organism: Ovis aries (Sheep)
Subcellular location: Cytoplasm, cytosol {ECO:0000256|RuleBase:RU364119}. Secreted {ECO:0000256|RuleBase:RU364119}. Lysosome {ECO:0000256|ARBA:ARBA00004371, ECO:0000256|RuleBase:RU364119}. Secreted, extracellular exosome {ECO:0000256|ARBA:ARBA00004550, ECO:0000256|RuleBase:RU364119}. Note=The precursor is cytosolic. In response to inflammasome-activating signals, such as ATP for NLRP3 inflammasome or bacterial flagellin for NLRC4 inflammasome, cleaved and secreted. Mature form is secreted and released in the extracellular milieu by passing through the gasdermin-D (GSDMD) pore. In contrast, the precursor form is not released, due to the presence of an acidic region that is proteolytically removed by CASP1 during maturation. The secretion is dependent on protein unfolding and facilitated by the cargo receptor TMED10. {ECO:0000256|RuleBase:RU364119}.
Interaction partners:
Sequence:
MATVPEPINEVMAYYSDANELLFEVDGPKQMKSCTQHLDLGSMGDGNIQLQISHQLYNKSFRQVVSVIVAMEKLRSRAYEHVFRDDDLRSILSFIFEEEPVIFETSSDELLCDAAVQSVKCKLQDREQKSLVLDSPCVLKALHLLSQEMSREVVFCMSFVQGEERDNKIPVALGIRDKNLYLSCVKKGDTPTLQLEEVDPKVYPKRNMEKRFVFYKTEIKNTVEFESVLYPNWYISTSQIEEKPVFLGRFRGGQDITDFRMETLSP
Protein: Bone morphogenetic protein 10 (BMP-10) (O95393)
Organism: Homo sapiens (Human)
Function: Required for maintaining the proliferative activity of embryonic cardiomyocytes by preventing premature activation of the negative cell cycle regulator CDKN1C/p57KIP and maintaining the required expression levels of cardiogenic factors such as MEF2C and NKX2-5. Acts as a ligand for ACVRL1/ALK1, BMPR1A/ALK3 and BMPR1B/ALK6, leading to activation of SMAD1, SMAD5 and SMAD8 transcription factors. Inhibits endothelial cell migration and growth. May reduce cell migration and cell matrix adhesion in breast cancer cell lines.
Subcellular location: Secreted {ECO:0000250}.
Interaction partners:
- Bone morphogenetic protein receptor type-2
- Activin receptor type-1-like
- Activin receptor type-2A
- Endoglin
- Growth/differentiation factor 2
- Activin receptor type-2B
- Activin receptor type-1
- Myosin-6
- Myosin-7
- Cyclin-dependent kinase inhibitor 1C
Sequence:
MGSLVLTLCALFCLAAYLVSGSPIMNLEQSPLEEDMSLFGDVFSEQDGVDFNTLLQSMKDEFLKTLNLSDIPTQDSAKVDPPEYMLELYNKFATDRTSMPSANIIRSFKNEDLFSQPVSFNGLRKYPLLFNVSIPHHEEVIMAELRLYTLVQRDRMIYDGVDRKITIFEVLESKGDNEGERNMLVLVSGEIYGTNSEWETFDVTDAIRRWQKSGSSTHQLEVHIESKHDEAEDASSGRLEIDTSAQNKHNPLLIVFSDDQSSDKERKEELNEMISHEQLPELDNLGLDSFSSGPGEEALLQMRSNIIYDSTARIRRNAKGNYCKRTPLYIDFKEIGWDSWIIAPPGYEAYECRGVCNYPLAEHLTPTKHAIIQALVHLKNSQKASKACCVPTKLEPISILYLDKGVVTYKFKYEGMAVSECGCR
Protein: Golgi-associated plant pathogenesis-related protein 1 (GAPR-1) (Golgi-associated PR-1 protein) (Glioma pathogenesis-related protein 2) (GliPR 2) (Q9H4G4)
Organism: Homo sapiens (Human)
Subcellular location: Golgi apparatus membrane {ECO:0000269|PubMed:11865038}; Lipid-anchor {ECO:0000269|PubMed:11865038}. Note=Binds lipid-enriched microdomains of Golgi membranes not only by ionic interactions but also through the myristate.
Interaction partners:
- Beclin-1
- Trifunctional purine biosynthetic protein adenosine-3
- Glioma pathogenesis-related protein 1
Sequence:
MGKSASKQFHNEVLKAHNEYRQKHGVPPLKLCKNLNREAQQYSEALASTRILKHSPESSRGQCGENLAWASYDQTGKEVADRWYSEIKNYNFQQPGFTSGTGHFTAMVWKNTKKMGVGKASASDGSSFVVARYFPAGNVVNEGFFEENVLPPKK
Protein: Acidic protein MsyB (P25738)
Organism: Escherichia coli (strain K12)
Function: Could participate in the normal pathway of protein export.
Interaction partners:
- Uncharacterized acetyltransferase YdcK
- Uncharacterized protein YdiZ
- Probable hydrolase YcaC
- Transaldolase A
- UPF0339 protein YegP
- Serine/threonine kinase YeaG
- Uncharacterized HTH-type transcriptional regulator YiaG
- NAD
- Uncharacterized protein YqjD
- Protein/nucleic acid deglycase 1
Sequence:
MTMYATLEEAIDAAREEFLADNPGIDAEDANVQQFNAQKYVLQDGDIMWQVEFFADEGEEGECLPMLSGEAAQSVFDGDYDEIEIRQEWQEENTLHEWDEGEFQLEPPLDTEEGRAAADEWDER
Protein: Eukaryotic translation initiation factor 4 gamma 1 (E9PGM1)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MMIPSQISYPASQGAYYIPGQGRSTYVVPTQQYPVQPGAPGFYPGASPTEFGTYAGAYYPAQGVQQFPTGVAPTPVLMNQPPQIAPKRERKTIRIRDPNQGGKDITEEIMSGARTASTPTPPQTGGGLEPQANGETPQVAVIVRPDDRSQGAIIADRPGLPGPEHSPSESQPSSPSPTPSPSPVLEPGSEPNLAVLSIPGDTMTTIQMSVEESTPISRETGEPYRLSPEPTPLAEPILEVEVTLSKPVPESEFSSSPLQAPTPLASHTVEIHEPNGMVPSEDLEPEVESSPELAPPPACPSESPVPIAPTAQPEELLNGAPSPPAVDLSPVSEPEEQAKEVTASMAPPTIPSATPATAPSATSPAQEEEMEEEEEEEEGEAGEAGEAESEKGGEELLPPESTPIPANLSQNLEAAAATQVAVSVPKRRRKIKELNKKEAVGDLLDAFKEANPAVPEVENQPPAGSNPGPESEGSGVPPRPEEADETWDSKEDKIHNAENIQPGEQKYEYKSDQWKPLNLEEKKRYDREFLLGFQFIFASMQKPEGLPHISDVVLDKANKTPLRPLDPTRLQGINCGPDFTPSFANLGRTTLSTRGPPRGGPGGELPRGPQAGLGPRRSQQGPRKEPRKIIATVLMTEDIKLNKAEKAWKPSSKRTAADKDRGEEDADGSKTQDLFRRVRSILNKLTPQMFQQLMKQVTQLAIDTEERLKGVIDLIFEKAISEPNFSVAYANMCRCLMALKVPTTEKPTVTVNFRKLLLNRCQKEFEKDKDDDEVFEKKQKEMDEAATAEERGRLKEELEEARDIARRRSLGNIKFIGELFKLKMLTEAIMHDCVVKLLKNHDEESLECLCRLLTTIGKDLDFEKAKPRMDQYFNQMEKIIKEKKTSSRIRFMLQDVLDLRGSNWVPRRGDQGPKTIDQIHKEAEMEEHREHIKVQQLMAKGSDKRRGGPPGPPISRGLPLVDDGGWNTVPISKGSRPIDTSRLTKITKPGSIDSNNQLFAPGGRLSWGKGSSGGSGAKPSDAASEAARPATSTLNRFSALQQAVPTESTDNRRVVQRSSLSRERGEKAGDRGDRLERSERGGDRGDRLDRARTPATKRSFSKEVEERSRERPSQPEGLRKAASLTEDRDRGRDAVKREAALPPVSPLKAALSEEELEKKSKAIIEEYLHLNDMKEAVQCVQELASPSLLFIFVRHGVESTLERSAIAREHMGQLLHQLLCAGHLSTAQYYQGLYEILELAEDMEIDIPHVWLYLAELVTPILQEGGVPMGELFREITKPLRPLGKAASLLLEILGLLCKSMGPKKVGTLWREAGLSWKEFLPEGQDIGAFVAEQKVEYTLGEESEAPGQRALPSEELNRQLEKLLKEGSSNQRVFDWIEANLSEQQIVSNTLVRALMTAVCYSAIIFETPLRVDVAVLKARAKLLQKYLCDEQKELQALYALQALVVTLEQPPNLLRMFFDALYDEDVVKEDAFYSWESSKDPAEQQGKGVALKSVTAFFKWLREAEEESDHN
Protein: AP complex subunit beta (Q24253)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Endomembrane system {ECO:0000256|ARBA:ARBA00029433}; Peripheral membrane protein {ECO:0000256|ARBA:ARBA00029433}; Cytoplasmic side {ECO:0000256|ARBA:ARBA00029433}.
Interaction partners:
- Adaptor protein complex 2, mu subunit, isoform A
- AP-1 complex subunit gamma
- Adaptor protein complex 1, mu subunit
- AP complex subunit sigma
- Clathrin heavy chain
- AP complex subunit sigma
- AP-2 complex subunit alpha
- Clathrin light chain
- AP-3 complex subunit delta
- Epidermal growth factor receptor pathway substrate clone 15, isoform A
Sequence:
MTDSKYFTTTKKGEIFELKSELNNDKKEKKKEAVKKVIASMTVGKDVSALFPDVVNCMQTDNLELKKLVYLYLMNYAKSQPDMAIMAVNTFVKDCEDSNPLIRALAVRTMGCIRVDKITEYLCEPLRKCLKDEDPYVRKTAAVCVAKLYDISATMVEDQGFLDQLKDLLSDSNPMVVANAVAALSEINEASQSGQPLVEMNSVTINKLLTALNECTEWGQVFILDSLANYSPKDEREAQSICERITPRLAHANAAVVLSAVKVLMKLLEMLSSDSDFCATLTKKLAPPLVTLLSSEPEVQYVALRNINLIVQKRPDILKHEMKVFFVKYNDPIYVKLEKLDIMIRLANQSNIAQVLSELKEYATEVDVDFVRKAVRAIGRCAIKVEPSAERCVSTLLDLIQTKVNYVVQEAIVVIKDIFRKYPNKYESIISTLCENLDTLDEPEARASMVWIIGEYAERIDNADELLDSFLEGFQDENAQVQLQLLTAVVKLFLKRPSDTQELVQHVLSLATQDSDNPDLRDRGFIYWRLLSTDPAAAKEVVLADKPLISEETDLLEPTLLDELICHISSLASVYHKPPTAFVEGRGAGVRKSLPNRAAGSAAGAEQAENAAGSEAMVIPNQESLIGDLLSMDINAPAMPSAPAATSNVDLLGGGLDILLGGPPAEAAPGGATSLLGDIFGLGGATLSVGVQIPKVTWLPAEKGKGLEIQGTFSRRNGEVFMDMTLTNKAMQPMTNFAIQLNKNSFGLVPASPMQAAPLPPNQSIEVSMALGTNGPIQRMEPLNNLQVAVKNNIDIFYFACLVHGNVLFAEDGQLDKRVFLNTWKEIPAANELQYTLSGVIGTTDGIASKMTTNNIFTIAKRNVEGQDMLYQSLKLTNNIWVLLELKLQPGNPEATLSLKSRSVEVANIIFAAYEAIIRSP
Protein: Peroxygenase (EC 1.11.2.3) (Caleosin) (A0A060LAL9)
Organism: Pinus massoniana (Chinese red pine)
Function: Calcium-binding peroxygenase involved in the degradation of storage lipid in oil bodies.
Subcellular location: Lipid droplet {ECO:0000269|PubMed:24954070}. Microsome membrane {ECO:0000250|UniProtKB:Q9SQ57}.
Interaction partners:
Sequence:
MASNESLQTTAAMAPVTIERRVNPNLDDELPKPFLPRALVAVDTEHPSGTPGHQHGDMSVLQQHVAFSNRNNDGIVYPWETFLGFRAVGFNIIISFFGCLIINIFLSYPTLPGWIPSPFFPIYIDRIHRAKHGSDSEVYDTEGRFVPAKFEEIFTKNAKTHPDKLSFSELWNLTEHNRNALDPLGWIAAKLEWFLLYSLAKDPHGFVPKEAARGVFDGSLFEFCEKSRKVKQATVKSLTFKI
Protein: Alpha-amylase A (EC 3.2.1.1) (1,4-alpha-D-glucan glucanohydrolase) (P08144)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MFLAKSIVCLALLAVANAQFDTNYASGRSGMVHLFEWKWDDIAAECENFLGPNGYAGVQVSPVNENAVKDSRPWWERYQPISYKLETRSGNEEQFASMVKRCNAVGVRTYVDVVFNHMAADGGTYGTGGSTASPSSKSYPGVPYSSLDFNPTCAISNYNDANEVRNCELVGLRDLNQGNSYVQDKVVEFLDHLIDLGVAGFRVDAAKHMWPADLAVIYGRLKNLNTDHGFASGSKAYIVQEVIDMGGEAISKSEYTGLGAITEFRHSDSIGKVFRGKDQLQYLTNWGTAWGFAASDRSLVFVDNHDNQRGHGAGGADVLTYKVPKQYKMASAFMLAHPFGTPRVMSSFSFTDTDQGPPTTDGHNIASPIFNSDNSCSGGWVCEHRWRQIYNMVAFRNTVGSDEIQNWWDNGSNQISFSRGSRGFVAFNNDNYDLNSSLQTGLPAGTYCDVISGSKSGSSCTGKTVTVGSDGRASINIGSSEDDGVLAIHVNAKL
Protein: E3 SUMO-protein ligase nse2 (EC 2.3.2.-) (E3 SUMO-protein transferase nse2) (Non-structural maintenance of chromosomes element 2) (Non-SMC element 2) (Q4PIR3)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Acts as an E3 ligase mediating SUMO/Smt3 attachment to other proteins. Acts in a DNA repair pathway for removal of UV-induced DNA damage that is distinct from classical nucleotide excision repair and in repair of ionizing radiation damage. Functions in homologous recombination repair of DNA double strand breaks and in recovery of stalled replication forks. Plays a critical role in meiosis.
Subcellular location: Nucleus {ECO:0000269|PubMed:12966087, ECO:0000269|PubMed:16823372}.
Interaction partners:
- Structural maintenance of chromosomes protein 5
- Non-structural maintenance of chromosome element 4
- Non-structural maintenance of chromosomes element 1
- Structural maintenance of chromosomes protein 6
- Non-structural maintenance of chromosome element 3
- Non-structural maintenance of chromosome element 5
- SUMO-conjugating enzyme ubc9
- Non-structural maintenance of chromosome element 6
- E3 SUMO-protein ligase pli1
- Ubiquitin-like protein pmt3/smt3
Sequence:
MSEAQLKTSLEALSQNLLPGNQNHCSFDFQLKEIDDSIKQVIKCALVAAEIKNNECLDMLDSGIRELLDAKQRLLLMQQSVDTLANKTSENISDFENKSLLDIYTQIFKELIQEYEEKSDYGKYGTQGEYIEFKKTIWHEQNTDGSDFPSMKTFFNVMNTEEQEADEVMVYSATFDNRCPLTLQPIVHPILSTACNHFYEKDAILSLLNPTCVCPVVGCEARLQRSLLKEDEILERRLRRAQEISNLKEA
Protein: Vomeronasal type-1 receptor (Q9EQ41)
Organism: Mus musculus (Mouse)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004651, ECO:0000256|RuleBase:RU364061}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651, ECO:0000256|RuleBase:RU364061}.
Interaction partners:
- Vomeronasal 2, receptor 54
Sequence:
MSLFKNVLYFQAGLGVLANMFLLFFYIFIILGHRPKPTDLISCQLTFVHIMMFLAGGDIWLTDIFETLNIENDFKCKTIFYISRVMRGLSICNTCLLSVVQAVTISPSTSLLAKFKPRLKMYLIYAFFCIWSFNLLYSSNQILYVGGFTNLSETNQMKVTKSCTLLPKNYIIKGLILTVSISRDVFLVGVMLTTSTYMLNILFRHQRQCKHLHSISYLRASPEKRATQTILLLVVFFVVMYWVDFIISSTSVMLWMYDPVVLTVQKFVMCAYPTITPLVQITSDNRIIIMLENMQSKHRQNFF
Protein: Protein SEY1 homolog (EC 3.6.5.-) (Q388F1)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Function: Probable GTP-binding protein that may be involved in cell development.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000255|HAMAP-Rule:MF_03109}; Multi-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_03109}.
Interaction partners:
Sequence:
MAAFSGETAVKGIHLINDDGELLPEADINDFLISALAGKGSSDILYRTGVNYHVVGVFGGQSSGKSTLLNSLFQTEFMTMDEAHHRGQTTKGAFMTRAILDAQTHRKEREEGEGADLLKREKPQPLFVLDFEGTDGIERGEDQNFERQLSLFALSVADILIINMWAVDVGRFNAANMNLLRTVFEVNLQLFSHGSYVKEEKPTLLVVLRDFTENDPAPSFETVRKSFDKIWGNIQKPESFTDATIDVVFDLRYRVLPHYKLQRPEFDSAVSEFREWFVSPKNSNFLFSNCSMFRGVPADGMPSYLSNCWNAICSSKDLDIPTQRDMLARHRCADAKHAAIEEFKEVCEEYTKKIQRGDVIPQFTRALEETIERLLKNFSDQTKLYKVSVVHETAEALEEELGDMELHLLKQYAKSIAVTVLAALDGVIGSSVDEAVRWLQNEARSVLLLEGKDNKGDRIDGGGLAQGVLDTAEGLVDNKRCRLFVEEFWKRICLSLQGAFDMLNGCSKSHQAALSSLYGKFATAIMDDQAVREGVAHAAMEGAQHKLRNRFVAMAENAAETVHQVFEQALTSKTDGTVRFFRTTDGLLGAEKQARQAGLVLLGCLLYYRLKLVPVEVDAGEVEGEGTTRALQRLVRDRCRFQVRDNRTEKNFFLHFTNISDVPRYPLDAPTSVVDSGDTTADTVNADNVLLSHNALQCAFHLYKQKADFTLQMQLRNIESGKQSLPPWVLPVMLLLGWNELYYLLTSPILLIAIIVIAVLFFKTFLKSQLEVLEEKCPVWLVVSVKALLQQAQALQNAYAPTEAVRGGGGGAQFRDPTQATSVSGASAGVSSESSSAASPRRRVCRESRDKGED
Protein: tRNA (guanine(9)-/adenine(9)-N1)-methyltransferase (EC 2.1.1.218) (EC 2.1.1.221) (tRNA(m1G9/m1A9)-methyltransferase) (tRNA(m1G9/m1A9)MTase) (Q5JD38)
Organism: Thermococcus kodakarensis (strain ATCC BAA-918 / JCM 12380 / KOD1) (Pyrococcus kodakaraensis (strain KOD1))
Function: Catalyzes the S-adenosyl-L-methionine-dependent formation of either N(1)-methyladenine or N(1)-methylguanine at position 9 (m1A9 or m1G9) in tRNA.
Subcellular location: Cytoplasm {ECO:0000305}.
Interaction partners:
- Phosphodiesterase
- RNA-free ribonuclease P
Sequence:
MKTLADVFREALKEKGISSIGTLSKRFRKSKNKLQDIAIEIVHGKGAVFRVPEKTAVAWDLNGNRVDGSYYAYAPLCMREKFEPVLTPEELREKLPDWPYFIIDLYHWDKHTQKEKGKICLQVNQSYGLLRDYFTGSELAVTWANEEFREMFHGPLDRITTYGGPTSEFLKENGINEVVLLDPWAEEVLSEKDFDVKAFIIGGIVDTGGNKKKTTPKIGEELESAGIKVRRRKIVLRGDVVGVPDRINRILGIILKMMVEGKSMDEAVYEMQEPLHARWRLRKELPKRATRYMVEGKVYRVVEKELFDEYSKWLKIRWEDFVKVLRELDLVALERKRIHHLNKISNARIINGKLHRVILLKRAAMLCYNC
Protein: BZIP domain-containing protein (A0A1I6CMA8)
Organism: Caenorhabditis elegans
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MIMDASRPRMVPPCSILLNSPTSSSNEDKHNLFNYQHHQHNHQTYSSPISQPIFDHASPSLYTSEHSEYSPAEIYSPNSASSSLPSTSPFPYTTSPFTATEEIYPDIPFIDSMIAEVRQEIINEDIPVPSPSTSSDISSVSRKSSASSSSSLRDVFVSPGQTLVIRGDDGQEYKVIVERVEGSEAHATPALTKRKLSDDSDIAPKRARAPPVSLVNLSDEEIAERKKQQNRAAALRYRQKLRESRVMSVSVKETLTQRNAYLRDEAERLSKECEVIRRLIFDKLGKNAPLF
Protein: Ketol-acid reductoisomerase (NADP(+)) (KARI) (EC 1.1.1.86) (Acetohydroxy-acid isomeroreductase) (AHIR) (Alpha-keto-beta-hydroxylacyl reductoisomerase) (Ketol-acid reductoisomerase type 2) (Ketol-acid reductoisomerase type II) (P05793)
Organism: Escherichia coli (strain K12)
Function: Involved in the biosynthesis of branched-chain amino acids (BCAA). Catalyzes an alkyl-migration followed by a ketol-acid reduction of (S)-2-acetolactate (S2AL) to yield (R)-2,3-dihydroxy-isovalerate. In the isomerase reaction, S2AL is rearranged via a Mg-dependent methyl migration to produce 3-hydroxy-3-methyl-2-ketobutyrate (HMKB). In the reductase reaction, this 2-ketoacid undergoes a metal-dependent reduction by NADPH to yield (R)-2,3-dihydroxy-isovalerate. Also able to use 2-ketopantoate, 2-ketoisovalerate, 2-ketovalerate, 2-ketobutyrate, 3-hydroxypyruvate, 3-hydroxy-2-ketobutyrate and pyruvate.
Subcellular location: Cytoplasm {ECO:0000305|PubMed:2653423}.
Interaction partners:
- Acetolactate synthase isozyme 1 large subunit
- Dihydroxy-acid dehydratase
- Acetolactate synthase isozyme 3 small subunit
- Acetolactate synthase isozyme 1 small subunit
- Acetolactate synthase isozyme 3 large subunit
- 3-isopropylmalate dehydrogenase
- 3-isopropylmalate dehydratase small subunit
- 3-isopropylmalate dehydratase large subunit
- Acetolactate synthase isozyme 2 small subunit
- 2-isopropylmalate synthase
Sequence:
MANYFNTLNLRQQLAQLGKCRFMGRDEFADGASYLQGKKVVIVGCGAQGLNQGLNMRDSGLDISYALRKEAIAEKRASWRKATENGFKVGTYEELIPQADLVINLTPDKQHSDVVRTVQPLMKDGAALGYSHGFNIVEVGEQIRKDITVVMVAPKCPGTEVREEYKRGFGVPTLIAVHPENDPKGEGMAIAKAWAAATGGHRAGVLESSFVAEVKSDLMGEQTILCGMLQAGSLLCFDKLVEEGTDPAYAEKLIQFGWETITEALKQGGITLMMDRLSNPAKLRAYALSEQLKEIMAPLFQKHMDDIISGEFSSGMMADWANDDKKLLTWREETGKTAFETAPQYEGKIGEQEYFDKGVLMIAMVKAGVELAFETMVDSGIIEESAYYESLHELPLIANTIARKRLYEMNVVISDTAEYGNYLFSYACVPLLKPFMAELQPGDLGKAIPEGAVDNGQLRDVNEAIRSHAIEQVGKKLRGYMTDMKRIAVAG
Protein: Biorientation defective 1, isoform E (A0A0B4KHZ9)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MDDFIKTLIAEVKSQGVFDEFRFNCCLADVDTKPAYQNVRTQVETAVNDFLAKQQWTPETNKVQLRERLRKHLMDSDVLDKGVDQIVDQVVNPKVATIFEPKIESIVYKYLGITPPARPTMLSAPPLPPFGAHLNGSSLLNVETTVGLLPTDLEQISPDSDRATVKSESRDDELPPGVDDEDTSPSYELVSERKTLAIKEELNNVSLNNSDSVNGVSQASQLSQVSSDSRLTMASSTESMVDSHQHTAAHNSGEPENICEEAQMPKFSENSWDASAGTGRSEGRQLHFDIKQDAITFEGTERKNSVSETTSTGLQILSIEDEIMSEVKANIDDANNASIESIAPEPVQVPAPPKVNPPPPPRPASPKVEPPPPAPPGVESPPGPQPPASPRFDPPPPHTIEPPPPPAPPTLVPPPPPAPPTIKPPPPPAPPTVEPPPPPPPAPPTVEPPPPPPPAPTKVEPPPPPAPAEVEPPPPPAPTELEPPPPPAPPKVELPPPPAPPKAEAAITPRRAKGSNGFITELAVTPKESETRDKPHNVNTDVKEDEQPATTEDKQDKPLELGLDAPKDAVSTASESTESPTSTSSQSKSHSKSRDKEKEKDRRHHRHSDDKHRRRSTDRDRDRSRDKSHSKHSSSSSSKHSSSNSSSSKHKSSSSKNDKSSSSSSSRSNRESSSSKRSGTTSSSRHESSSHKKHKSSSSSSRSERDKGKEKDKEREKDSQSRSHHSSSSSSSSSRRKDHDRGRDRDRNKSNTSGSAENKAIHDDHSESKEKYKQRRGSDSNDEGKPPSSGGPAKNSQPEDSAATMKSDAPVENANGTNGNSNGSTNGACDNVSGVVIVSDILQQSTSSFVELTAGSQSHDRAESSKHEPEDIDGKEADNQPEKTELEARQDECASQNEVPTVEPQTLADSVPDLPAKESMDTLEDEKVETNVEENKSEEESKPENPPEECVDEPAQVGDVEDPPQDADKPATPVPISNEQSDEFSADFVTHFEENTDEFRTRLQLINQLIEDRKNLLNRLSEDGTQEEAVDIRALRRSLSKRRRSSMQEQHRVERETTPPQPRSPSSSSTAGSPAKRLRQDEPKSSPTPSDASINSKENEALEKQEHADALSARRLSKKLCQQQRYTNDDLYKPRPILSQRSRRRGLDSIL
Protein: Peptidyl-prolyl cis-trans isomerase PASTICCINO1 (EC 5.2.1.8) (70 kDa peptidyl-prolyl isomerase) (FK506-binding protein 72) (AtFKBP72) (Immunophilin FKBP72) (Peptidyl-prolyl cis-trans isomerase FKBP72) (PPIase FKBP72) (Rotamase) (Q7DMA9)
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). Essential protein regulating cell division, adhesion and elongation throughout the plant development and embryogenesis. Required for the spatial organization of apical meristems. Involved in the hormonal control of cell division and differentiation mediated by cytokinins and auxin. Regulates the function of NAC089 transcription factor by controlling its targeting to the nucleus upon plant cell division. Interacts with enzymes of the fatty acid elongase complex and favors the generation of very-long-chain fatty acids (VLCFAs) required for polar auxin transport and tissue patterning during plant development.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000305}; Single-pass type IV membrane protein {ECO:0000305}. Cytoplasm {ECO:0000305}. Nucleus {ECO:0000269|PubMed:16803883, ECO:0000269|Ref.6}. Note=Relocalization from the cytoplasm into the nucleus is induced by auxin treatment and in association with NAC089.
Interaction partners:
- Very-long-chain
- Very-long-chain 3-oxoacyl-CoA reductase 1
- Very-long-chain enoyl-CoA reductase
- Uncharacterized protein At1g21580
- Peptidyl-prolyl cis-trans isomerase FKBP15-3
- Protein ECERIFERUM 26-like
- Protein ROOT HAIR DEFECTIVE 3 homolog 1
- Protein ECERIFERUM 26
- Peptidyl-prolyl cis-trans isomerase FKBP17-3, chloroplastic
Sequence:
MAVGDQTEQNYLPKKKKSETEDDKRRKKIVPGSLLKAVVRPGGGDSSPVDGDQVIYHCTVRTLDGVVVESTRSESGGRGVPIRDVLGNSKMILGLLEGIPTMHKGEIAMFKMKPEMHYAEIDCPVSAPENFPKDDELHFEIELLDFSKAKIASDDLGVIKKILNEGEGWESPREPYEVKARISAKSGDGHVIFSHTEEPYFFTFGKSEVPKGLEIGIGTMARKEKAVIYVRKQYLTESPLLHIDQDLEEVHFEVELVHFIQVRDMLGDGRLIKRRIRDGRGEFPMDCPLQDSRLSVHYKGMLLNEEKTVFYDSKIDNNDQPLEFSSGEGLVPEGFEMCTRLMLPGEIALVTCPPDYAYDKFPRPPGVSEGAHVQWEIELLGFETPRDWTGLNFQSIMDEADKIRSTGNRLFKEGKFELAKAKYEKVLREFNHVNPQDEDEGKIFGDTRNMLHLNVAACLLKMGEWRKSIETCNKVLEAKPGHVKGLYRRGMAYIAGGEYDDARNDFNMMIKVDKSSEADATAALLKLKQKEQEAESKARKQFKGLFDKRPGEITEVGSEIREESKTIEEVDETKDNDDDETLEEEGATTVSTERKRKWSEKAWPFLKNVMLQIGIQLGVVLIGILIFQFVSAKFT
Protein: P-type DNA transfer ATPase VirB11 (VirB11-like protein) (Q6VRM0)
Organism: Helicobacter pylori (Campylobacter pylori)
Interaction partners:
Sequence:
MAEDRLSAEDKKFLEVERALKEAALNPLRHATEELFGDFLKMENITEICYNGNKVVWVLKNNGEWQPFDVRDRKAFSLSRLMHFARCCASFKKKTIDNYENPILSSNLANGERVQIVLSPVTVNDETISISIRIPSKTTYPHSFFEEQGFYNLLDNKEQAISAIKDGIAIGKNVIVCGGTGSGKTTYIKSIMEFIPKEERIISIEDTEEIVFKHHKNYTQLFFGGNITSADCLKSCLRMRPDRIILGELRSSEAYDFYNVLCSGHKGTLTTLHAGSSEEAFIRLANMSSSNSAARNIKFESLIEGFKDLIDMIVHINHHKQCDEFYIKHR
Protein: Serine/threonine-protein phosphatase (EC 3.1.3.16) (Q8IKH5)
Organism: Plasmodium falciparum (isolate 3D7)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- Protein phosphatase inhibitor 3
Sequence:
MNNGSFKETSVCRKEKQKGDIPAPRFGHTATYLGNNKVAIFGGAIGDAGKYNITDDIYLYDLTQNKWKKLITENTPSARAAHAAACVDEQQLVIYGGATGGGSLSLDDLYILDLRKEQKYTWMTVPTKGVTPGRRYGHVMVYSKPNLIVFGGNDGQNTLNDVWYMHVEMPPFEWVRVIIPNTCKVPPQRVYHSADMCKEGPASGMIVIFGGRSAENKSLDDTWGLRQHRDGRWDWVEAPIKKGSPPEARYQHTSVFIGSKIFILGGRNDNGCAVPLSTALYNTETIEWVTLPSISKFRHTSWVYKYTIYTFGGFSHQTQQYPTNELECLECFNLLSSLNSLDSEKKKSIKQSSLKQKQLTNDNLKHSSSDLRNVNSYNLNSQDVINTQQHNISTNNQFNVSNELYDLKNNASICNTLANVPIVPNVQNVPNVPNVPNTHYRNMFDTSSNSSVFRLSNRPMSNKIRLSAHAHAVQENGSDFAFLVRKISIDKLEEEGRKINNGVLCTPVNYISEFKNTVYDKIITTLLNPNITQFEIQYNHNSESIFIIPWANISVLCSIVIDIFKQEDMVLKLRAPIKIYGDIHGQYYDLMRMFQLYKCPVEEDLGEKLNAIGDIDSNDYLFLGDYVDRGSNSLEVICLLFALKCKYPKQIHLIRGNHEDVAINSLYGFQEECKRRLKEDVTDKDSCWYQINQVFEWLPIGAIVEDKILCVHGGIGKSINQISDISQLKRPLVVSQVPQNLNEQKVTDLLWSDPTDNDSILGTIPNDIRDPDGTGHIVKYGPDRVHKFLEENDLQLIIRAHECVMDGFERFAGGKLITLFSATNYCNSHKNAGALLFIRRDLTVIPKLIYPAKDEVRFFNTWDTKMTELRPPTPPRNQPKMRELNFGAP
Protein: Succinate dehydrogenase subunit 7A, mitochondrial (Q9C5E8)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Mitochondrion inner membrane {ECO:0000305}; Peripheral membrane protein {ECO:0000305}.
Interaction partners:
- Succinate dehydrogenase subunit 8
- Succinate dehydrogenase subunit 5
- Succinate dehydrogenase subunit 4
- Succinate dehydrogenase subunit 7B
- Succinate dehydrogenase subunit 6
- Succinate dehydrogenase iron-sulfur subunit 2, mitochondrial
- Succinate dehydrogenase iron-sulfur subunit 1, mitochondrial
- Succinate dehydrogenase flavoprotein subunit 1, mitochondrial
- Succinate dehydrogenase subunit 3-1
- Succinate dehydrogenase iron-sulfur subunit 3, mitochondrial
Sequence:
MAFLLNTSISSHLRSSSQKTDGALAQSRRGFHVELGAREKALLAEDASLRRFKSHKKGVHRLKRIGDVLTVVVVAGCCYEIYARVMRKEAQAA
Protein: Inner kinetochore subunit MCM16 (CENP-H homolog) (Constitutive centromere-associated network protein MCM16) (Minichromosome maintenance protein 16) (Q12262)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Component of the kinetochore, a multiprotein complex that assembles on centromeric DNA and attaches chromosomes to spindle microtubules, mediating chromosome segregation and sister chromatid segregation during meiosis and mitosis. Component of the inner kinetochore constitutive centromere-associated network (CCAN), which serves as a structural platform for outer kinetochore assembly.
Subcellular location: Nucleus. Chromosome, centromere, kinetochore. Note=Associated with kinetochores.
Interaction partners:
- Inner kinetochore subunit MCM22
- Inner kinetochore subunit OKP1
- Inner kinetochore subunit CTF3
- Inner kinetochore subunit NKP1
- Inner kinetochore subunit MCM21
- Inner kinetochore subunit IML3
- Inner kinetochore subunit CHL4
- Inner kinetochore subunit CTF19
- Inner kinetochore subunit AME1
- Inner kinetochore subunit NKP2
Sequence:
MTNSSEKQWERIQQLEKEHVEVYRELLITLDRLYLIRKHNHAVILSHTQQRLLEIRHQLQINLEKTALLIRLLEKPDNTNVLFTKLQNLLEESNSLDYELLQSLGAQSSLHKQLIESRAERDELMSKLIELSSKFPKPTIPPDDSDTAGKQVEVEKENETIQELMIALQIHSGYTNISYTI