wanglab/gogpt-training-data huggingface dataset:
Protein: LD28927p (Q8T049)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MPTEVYDDESDTDELDVSPSTGKVPSYSIYSEQEDYYMDLQQTTPSIQPNGFYEQVNNGYDYREDYFNEEDEYKYLEQQREQEEHNQPKNKKYLKQAKISKIQPPSLDFIDVGQDDDFIYDNYHSEDDSGNYLEGSSSGSVGPIEGSIIKVDSNIEASFASLNKKSDSFTPTNDSLQKHDTVIGESTTKLTRLRTEKMCPDVDEEDENLSDHVSDLTDLSKLISQKKKTLLRGETEEVVGGHMQVLRQTEITARQRWHWAYNKIIMQLNNGGGPGEVGLRTNGHPGDNPFYSNIDSMPDIRPRRKSIPLVSELTMAATKRNAGLTSAVPRATLNDEDLKMHVYKKALQALIYPISSTTPHNFLLWTATSPTYCYECEGLLWGIARQGVRCTECGVKCHEKCKDLLNADCLQRAAEKSSKHGAEDKANSIITAMKDRMKQREREKPEIFELIRMTFGVDPDTHIDSLEQAEHATVEGTSKWSCKLTITVICAQGLIAKDKSGTSDPYVTVQVSKVKKRTRTMPQELNPVWNEKFHFECHNSSDRIKVRVWDEDNDLKSKLRQKLTRESDDFLGQTIIEVRTLSGEMDVWYNLEKRTDKSAVSGAIRLHISVEIKGEEKVAPYHVQYTCLHENLFHYLCEENTGMVKLPTQKGDDAWKLYFDEIPEEIVDEFSMRYGIENIYQAMTHFHCLSAKYLCPGVPAVMSTLLANINAYYAHTTASSAVSASDRFAASNFGKEKFVKLLDQLHNSLRIDLSMYRNNFPASSPEKLMDLKSTVDLLTSITFFRMKVQELSSPPRASTVVKDCVKACLRSTYQFLFENCYELYNREFQVDPNEAKRAPDDHEPKLDSVDFWHKLIALIVSVIDEDKNSYGTVLNQFPQELNIGQLSASSMWHLFAVDMKYALEEHEQHRLCKSSAYMNLHFRVKWLYSNYVKEVPPYKGAVPDYPAWFEPFVMQWLNENDDVSLEYLHGAFKRDKKDGFQKSSEHALFSNSVVDVFTQLTQCFDVVSKLECPDPEIWKRYMRRFAKTIVKVLIAYADIVKLEFPEHMKDERIACILMNNIQQLRVQLEKMFESMGGDKLEEDAANILKELQQNLNSALDDLASQFAISLEPRITQSVRELGDMLLSIKGGSGTLAAGNLAAQRNAVAVEADEVLRPLMDLLDGSLTLYAQSCEKTVLKRLLKELWKIVMRILEKTIVLPPMTDKTMMFKHLTDNAKNLASNAKIEDMGRLFKSHMAGKQDVKSALSGVMDISKEVEKNLSPKQCAVLDVALDTIKQYFHAGGNGLKKTFLEKSPELQSLRYALSLYTQMTDTLIKTFISSQVHEVDLENSEEGVGEISVQIDLFSHPGTGEHKVNVKVVAANDLKWQIPSGMFRPFVDINLIGPHLQEKKRKFATKSKSNNWSPKYNESFSFTIGNEEQLDFFELHICVKDYCFARDDRLVGVAVIPLKDISEKGSVACWLPLMRRIEMDETGWTILRILSQRNNDEVAKEFVKLKSEIRQEPTMGT
Protein: Neutrophil cytosol factor 2 (NCF-2) (67 kDa neutrophil oxidase factor) (NADPH oxidase activator 2) (Neutrophil NADPH oxidase factor 2) (p67-phox) (O70145)
Organism: Mus musculus (Mouse)
Function: NCF2, NCF1, and a membrane bound cytochrome b558 are required for activation of the latent NADPH oxidase (necessary for superoxide production).
Subcellular location: Cytoplasm {ECO:0000305}.
Interaction partners:
- Cytochrome b-245 light chain
- Neutrophil cytosol factor 4
- NADPH oxidase organizer 1
- NADPH oxidase 1
- NADPH oxidase 2
- Ras-related C3 botulinum toxin substrate 2
- Neutrophil cytosol factor 1
- NADPH oxidase 4
- Ras-related C3 botulinum toxin substrate 1
- NADPH oxidase activator 1
Sequence:
MSLAEAIRLWNEGVLAADKKDWKGALEAFSEVQDPHSRICFNIGCVNTILENLQAAEQAFTKSINRDKHSAVAYFQRGMLYYRMEKYDLAIKDLKEALTQLRGNQLIDYKILGLQFKLFACEVLYNIALMHAKKEEWKKAEEQLALATNMKSEPRHSKIDKAMESIWKQKLFEPVVIPVGRLFRPNERQVAQLAKKDYLGKATVVASVVHQDNFSGFAPLQPQSAEPPPRPKTPEIFRALEGEAHRVLFGFVPETPEELQVMPGNIVFVLKKGSDNWATVMFNGQKGLVPCNYLEPVELRIHPQSQPQEDTSPESDIPPPPNSSPPGRLQLSPGHKQKEPKELKLSVPMPYMLKVHYKYTVVMETRLGLPYSQLRNMVSKKLALSPEHTKLSYRRRDSHELLLLSEESMKDAWGQVKNYCLTLWCEHTVGDQGLIDEPIQRENSDASKQTTEPQPKEGTQVVAIFSYEAAQPEDLEFVEGDVILVLSHVNEEWLEGECKGKVGIFPKAFVEGCAAKNLEGIPREV
Protein: Solute carrier family 30 member 10 (Zinc transporter 10) (A0A0R4IEQ2)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
- Metal cation symporter ZIP14
- Solute carrier family 39 member 8.
- Zinc transporter ZIP1
- Zinc-regulated GTPase metalloprotein activator 1
- Proton-coupled zinc antiporter SLC30A9, mitochondrial
- Zinc transporter 6
- Solute carrier family 39
- Glucose-6-phosphate exchanger SLC37A1
- Zinc transporter ZIP13
Sequence:
MGRYSGKTCRLILMLVITVIFFVAEIVAGYMGNSVALVSDSFNMLSDILSLCVGLTAARVSRRAGSGRFSFGLGRAEVVGALANAVFLIALCFSISMESLKRLAMPQAIDDAPLVLIVGSLGLAVNLVGLVIFQDCGRLCGRRGKEKKREEHREDREQELEQVETGLQEEKTEKDGAPLNIRGVLLHVLNDALGSVVVVVASALFYVWPLEPDQPCNWQCYVDPSLTLVMVIIILSSAAPLLKETTTILLQMSPEDLPVSAILESVCRLPGVSSVHEAHVWELAKGRNVASLHVKLQAPAGALWAQVSLQQQITQIFHRAGVHSLTLQLELADSDADSSCSAPCLSSSCQKLSCCPAGPVCVCAPPRDSSTEKHTPQACTHSSKL
Protein: Transthyretin-like family protein (O17345)
Organism: Caenorhabditis elegans
Subcellular location: Secreted {ECO:0000256|ARBA:ARBA00004613}.
Interaction partners:
- Fatty acid-binding protein homolog 2
- C-type lectin domain-containing protein
Sequence:
MRSVLIVCALFGVAASIEMFGRDQSSAVRGKLICDGRPASGVLVKLWDKDTLDSDDLLDSGTTDGNGDFHLAGWTKEYTPIDVKLNIYHDCNDGIKPCQRKFGIKIPDSYTSSGKVPKKVYDAGVIQLAGSYPGESRDCIH
Protein: Aspartate--tRNA ligase, cytoplasmic (EC 6.1.1.12) (Aspartyl-tRNA synthetase) (A0A140VJW5)
Organism: Homo sapiens (Human)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
Interaction partners:
Sequence:
MPSASASRKSQEKPREIMDAAEDYAKERYGISSMIQSQEKPDRVLVRVRDLTIQKADEVVWVRARVHTSRAKGKQCFLVLRQQQFNVQALVAVGDHASKQMVKFAANINKESIVDVEGVVRKVNQKIGSCTQQDVELHVQKIYVISLAEPRLPLQLDDAVRPEAEGEEEGRATVNQDTRLDNRVIDLRTSTSQAVFRLQSGICHLFRETLINKGFVEIQTPKIISAASEGGANVFTVSYFKNNAYLAQSPQLYKQMCICADFEKVFSIGPVFRAEDSNTHRHLTEFVGLDIEMAFNYHYHEVMEEIADTMVQIFKGLQERFQTEIQTVNKQFPCEPFKFLEPTLRLEYCEALAMLREAGVEMGDEDDLSTPNEKLLGHLVKEKYDTDFYILDKYPLAVRPFYTMPDPRNPKQSNSYDMFMRGEEILSGAQRIHDPQLLTERALHHGIDLEKIKAYIDSFRFGAPPHAGGGIGLERVTMLFLGLHNVRQTSMFPRDPKRLTP
Protein: LDLR chaperone boca (Q8T9B6)
Organism: Drosophila melanogaster (Fruit fly)
Function: Chaperone specifically assisting the folding of beta-propeller/EGF modules within the family of low-density lipoprotein receptors (LDLRs). Acts as a modulator of the Wg pathway, since some LDLRs are coreceptors for the canonical Wnt pathway.
Subcellular location: Endoplasmic reticulum {ECO:0000255|PROSITE-ProRule:PRU10138, ECO:0000269|PubMed:12581524}.
Interaction partners:
Sequence:
MQTRLVLLLLALTPLVLAKKFKEEEKPAWAKKDIRDYSEADLERLLDQWEEDEEPLEDDELPEHLRPQPKLDLSNLDSKSPEDLLKVSKKGRTLMTFVSVTGNPTREESDTITKLWQTSLWNNHIQAERYMVDDNRAIFLFKDGTQAWDAKDFLIEQERCKGVTIENKEYPGVNAKKDEL
Protein: Protein ZINC INDUCED FACILITATOR-LIKE 1 (Protein ZIF-LIKE 1) (Q94BZ1)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Major facilitator superfamily (MFS) transporter probably involved in 2,4-dichlorophenoxyacetic acid (2,4-D) export. K(+) may be the physiological substrate of the transporter.
Subcellular location: Cell membrane {ECO:0000269|PubMed:19440702}; Multi-pass membrane protein {ECO:0000269|PubMed:19440702}.; SUBCELLULAR LOCATION: [Isoform 1]: Vacuole membrane {ECO:0000269|PubMed:23524662}.; SUBCELLULAR LOCATION: [Isoform 3]: Cell membrane {ECO:0000269|PubMed:23524662}.
Interaction partners:
- Zinc transporter ZTP29
- Folate-biopterin transporter 1
- At5g23760
- Zinc transporter 4, chloroplastic
- GDSL esterase/lipase EXL1
Sequence:
MAEEYAECLLEKNFHEDCSGCKVDQMKRLRRGFPFWELFTVWIIVLCTALPISSLFPFLYFMIDDFNIAKKEEDIGFYAGFVGCSFMLGRAFTSVAWGLVADRYGRKPVILIGTASVVVFNTLFGLSLNFWMAIITRFCLGSFNGLLGPIKAYAMEIFRDEYQGLALSAVSTAWGIGLIIGPAIGGFLAQPAKQYPSLFSQDSIFGKFPFFLPCLAISVFAFLVTIVSSRIPETLHNHKFNDDESYDALKDLSDDPESNKVAERNGKSSLLNNWPLISSIIVYCVFSLHDMAYTEIFSLWANSPRKYGGLGYSTADVGSVLAFSGFGLLIFQLSLYSYAERLLGPIIVTRISGSLAMVVLSCYPLIAKLSGLALTVTVTSASVAKSVLGTSAITGLFILQNKAVRQDQRGAANGIAMTAMSLFKAIGPAAAGIIFSWSEKRQGAAFLPGTQMVFFILNVVLALGVVLTFKPFLAETQQ
Protein: Eukaryotic translation initiation factor 4E-4 (eIF-4E-4) (eIF4E-4) (eIF-4F 25 kDa subunit) (mRNA cap-binding protein) (Q22888)
Organism: Caenorhabditis elegans
Function: Recognizes and binds the 7-methylguanosine-containing mRNA cap during an early step in the initiation of protein synthesis and facilitates ribosome binding by inducing the unwinding of the mRNAs secondary structures. All 5 eIF4E proteins bind monomethyl cap structures. Only ife-1, ife-2 and ife-5 bind trimethyl cap structures which result from trans-splicing. Translation of trimethyl cap structure mRNAs may be regulated by intracellular redox state; disulfide bonds change the width and depth of the cap-binding cavity determining selectivity to mRNA caps.
Interaction partners:
- GYF domain-containing protein gyf-1
- MIF4G domain-containing protein
- Cytoplasmic FMR1-interacting protein homolog
- Translational repressor ifet-1
- mRNA cap guanine-N
- Eukaryotic initiation factor 4A
- Suppressor of aph-1
- SUI1 domain-containing protein
Sequence:
MEAETSTQEVVKQVKNLPILMEDAPVGSDDHQLQYSYTFSYFMRPTGKFDPEDYASYVQPVGIMKSVEQFWSIMVHFKRPTEMCDKADIHFFKTGVKPVWEDPANCKGGKWIIRLKKGLSTRIWENLLMAIIGEQFLVGDELCGAVCSIRNQEDIISLWNRNADDTPVTNRIRETLRSVLQLPQNTVLEYKRHDDCLRDQSSYRHTTKNICK
Protein: 6-phosphogluconate dehydrogenase, decarboxylating 1 (EC 1.1.1.44) (P38720)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Catalyzes the oxidative decarboxylation of 6-phosphogluconate to ribulose 5-phosphate and CO(2), with concomitant reduction of NADP to NADPH.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:14562095}.
Interaction partners:
- Glucose-6-phosphate 1-dehydrogenase
- 6-phosphogluconolactonase 3
- Ribulose-phosphate 3-epimerase
- Probable gluconokinase
- 6-phosphogluconolactonase 4
- 6-phosphogluconate dehydrogenase, decarboxylating 2
- Transketolase 1
- Ribose-5-phosphate isomerase
- 6-phosphogluconolactonase-like protein 1
- 6-phosphogluconolactonase-like protein 2
Sequence:
MSADFGLIGLAVMGQNLILNAADHGFTVCAYNRTQSKVDHFLANEAKGKSIIGATSIEDFISKLKRPRKVMLLVKAGAPVDALINQIVPLLEKGDIIIDGGNSHFPDSNRRYEELKKKGILFVGSGVSGGEEGARYGPSLMPGGSEEAWPHIKNIFQSISAKSDGEPCCEWVGPAGAGHYVKMVHNGIEYGDMQLICEAYDIMKRLGGFTDKEISDVFAKWNNGVLDSFLVEITRDILKFDDVDGKPLVEKIMDTAGQKGTGKWTAINALDLGMPVTLIGEAVFARCLSALKNERIRASKVLPGPEVPKDAVKDREQFVDDLEQALYASKIISYAQGFMLIREAAATYGWKLNNPAIALMWRGGCIIRSVFLGQITKAYREEPDLENLLFNKFFADAVTKAQSGWRKSIALATTYGIPTPAFSTALSFYDGYRSERLPANLLQAQRDYFGAHTFRVLPECASDNLPVDKDIHINWTGHGGNVSSSTYQA
Protein: Probable RNA helicase armi (EC 3.6.4.13) (Protein armitage) (Q6J5K9)
Organism: Drosophila melanogaster (Fruit fly)
Function: Probable RNA helicase required for axial polarization of the oocyte during early and mid oogenesis. Plays a central role in RNA interference (RNAi) process, a process that mediates mRNA destruction of translational repression. Required for the assembly of the RISC complex, a complex required for target RNA destruction or repression. May be required in the RISC assembly to unwind miRNAs, in the production of single-stranded miRNA from the double-stranded miRNA, a key step in RISC formation. Required both for the translational control of oskar (osk) mRNA and cytoskeletal polarization in the oocyte. Required for somatic primary piRNA biogenesis.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:15035984, ECO:0000269|PubMed:20966047}. Note=Component of Yb bodies, an electron dense structure containing Yb protein found in somatic cells of ovary and testis.
Interaction partners:
- Protein piwi
- Protein vreteno
- RNA helicase
- Mitochondrial cardiolipin hydrolase
- GH09064p
- Putative ATP-dependent RNA helicase SoYb
- Inactive peptidyl-prolyl cis-trans isomerase shutdown
- Probable ATP-dependent RNA helicase spindle-E
- Protein aubergine
- Tudor domain-containing protein krimp
Sequence:
MFTYVSKFFTNPDRNREDILESLDRENSFLDQKLMEEKMDQQLKANPNEINGVLSNKIAELTHGLSEMDVSKESSCTARKGVITSLDGDRGVIDKDVLFETKVAEDIILDLHVGCVVEYLTFTTGEAMRVVKVKSILEHSWEDTSQKEIEKAVDNLKNEKPTFFNTETRSVLGLISQRLASSIDVETEYGQLTVELDNIEMNFIPTNGDRVRLECNIQLDDGFVDKQGEILEVTKLFPTRIQEGEKCIVERVYVHMVVLGPETYILKTDLPTGTDLHLGDIVLADLIECQYSKFTRRAIKITPLEKNFGATKLTQQSSMGSSGSGKAVTVTGVNRFITAELWQKESVSLKLTNNLNRTLRLESITVCNDSESQLSVVSPLESKEISSGSEITVTFEIHTQFLGEAIEKYVLNFDLLKVRRVFTVIVCKTKEEVAEAEKRMIAAEALMAPGRNSQERSRFYANQVWCNKVDVIPGQQIVTKRRFVALRLGCFEVPKELRQICLTSERRQEMIKAIEQHYSFLTEPLSIKTYMHRFRLLLHLEEIECFVNFRNYDRDRAHFLRDGEFLTLQIENLAERRPSLVIGDTLRVINPWSDPDSQTTKSYEGIIHKVLFDRILLKFHSSFQEKYNGEDYRLEFYFSRYSFRKQHHAISKIVGVMGEDFLFPSKVTKRENPQLDVYMKDDDMYLYDSKLEWYNQSLNSIQKRAVFNILRGEAENIPYVLFGPPGSGKTMTLIETLLQLVRNLPGARILVGTPSNSSADLVTKRLIDSKALLQGDFIRLVSYNQVEKDLIPPEIMSYCATSDVGAVGSCEDKMMVTESGLKLRCQAKFIGTHRITISTCTTLGNFLQLGFPAGHFTHVLFDEAGQCTEPETMVPIVMLTKKRSQVVLSGDPRQLQSIVTSRIASKMGFSISFLERLLERSPYRKDLQRFPESSGYNPLVLTKLLYNYRALPSIMSIYSRLFYDDELIPVLSEKDSRESRLLSKLRCVFESEKDIPQAHGTFFYGIIGENRQNNDSPSWFNPQEVREVFLMTIALYRANVTADQIGIITPYQKQVKMLRSMFIGTDVVMPKIGSVEEFQGQERDIILISTVRSSEEILRMDARFSLGFVRCSKRLNVAVSRARAMMIIFGNPHLLAVDECWRQLILFCVKNNAYFGCDLPQMVINQKDEVPVCLETFVPSLNTTDDLN
Protein: Nucleoporin Nup37 (p37) (Nup107-160 subcomplex subunit Nup37) (Q8NFH4)
Organism: Homo sapiens (Human)
Function: Component of the Nup107-160 subcomplex of the nuclear pore complex (NPC). The Nup107-160 subcomplex is required for the assembly of a functional NPC. The Nup107-160 subcomplex is also required for normal kinetochore microtubule attachment, mitotic progression and chromosome segregation.
Subcellular location: Chromosome, centromere, kinetochore. Nucleus, nuclear pore complex.
Interaction partners:
- Nucleoporin SEH1
- Nuclear pore complex protein Nup133
- Nucleoporin Nup43
- Nuclear pore complex protein Nup98-Nup96
- Protein ELYS
- Nuclear pore complex protein Nup107
- Nuclear pore complex protein Nup160
- Nuclear pore complex protein Nup85
- Protein SEC13 homolog
- Nucleoporin NUP35
Sequence:
MKQDASRNAAYTVDCEDYVHVVEFNPFENGDSGNLIAYGGNNYVVIGTCTFQEEEADVEGIQYKTLRTFHHGVRVDGIAWSPETRLDSLPPVIKFCTSAADMKIRLFTSDLQDKNEYKVLEGHTDFINGLVFDPKEGQEIASVSDDHTCRIWNLEGVQTAHFVLHSPGMSVCWHPEETFKLMVAEKNGTIRFYDLLAQQAILSLESEQVPLMSAHWCLKNTFKVGAVAGNDWLIWDITRSSYPQNKRPVHMDRACLFRWSTISENLFATTGYPGKMASQFQIHHLGHPQPILMGSVAVGSGLSWHRTLPLCVIGGDHKLLFWVTEV
Protein: DDHD domain containing 2 (E9PK57)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MVVPGVEFEPMLIPHHKGRKRMHLELREGLTRMSMDLKNNLLGSLRMAWKSFTRAPYPALQASETPEETEAEPESTSEKPSDVNTEETSVAVKEEVLPINVGMLNGGQRIDYVLQEKPIESFNEYLFALQSHLCYWESEDTVLLVLKEIYQTQGIFLDQPLQ
Protein: Datilografo, isoform B (Q9V4C9)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MKLRCFNQAQTSHSWHPRSVFRVVSSCPPDRKKRPSPASWQICIGHLLTNYLGMFKMDSADFWQQARAPFGLQTALHQYSSPPNQQPISHHALHHSVPQENEQLAGVQPEGPAAGSGVVGNNSSMAISGTNSTVGSKAESSHIPQQHSEQQSYGSDSFRGTQSPQLSSHHLLFNAAAAAAAAVHLKSTAMQNNLSPIGDQVQNNLRNYGQGSLNALCGIKPKQEMDAKTPLQPLDECPHPLVQAQAQSQYGGDYYDVADPQAREISEGRALIIGLGAPSTVSTDDAQSSAPSHQLAGTGRALQTHQCKPMSPGTVGSSNLGAGRRSAPTTISKTFSQGQQSPQHSTTPSGGSTTPDIKYNNDKMANEIQLQLSRSSSAAAISERTLEECWSTLQRLFMHKSAMQQIQQQIPRVGLGTHGVTGSANLGGSITPSSDTKPHQCQQCMKSFSSNHQLVQHIRVHTGEKPYKCSYCDRRFKQLSHVQQHTRLHTGERPYKCHLPDCGRAFIQLSNLQQHLRNHDAQVERAKNRPFHCNICGKGFATESSLRTHTSKQHAALIGGPNATSCPVCHKLFLGTEALVDHMKHVHKEKSPPPGGSASSQFSELNQIVTGNGNGTGSSNEQIATQCTTESNSHQATVGSSLIDSFLGKRRTANHPCPVCGKHYVNEGSLRKHLACHAENSQLTNSLRMWPCSVCQAVFTHENGLLTHMESMRMDPKHQFAAQYVLSRAAAEQRERESLLAVTLAASSGASTRIGIADAGNVLPTGAHNSDGSNSKCPSPSANSECSSNGRLSSSTTSDQDQDIDHGLSENENSNQNNIGSSTNNNNNCTSNNNASSHKMAELRLPGTGQYTMDAELHVANRMSLMAAAAAAVAASRPQDGVDTSAVPSAAVQAAVVNLAAAMRMNNSSNGATPYQQHHADHTQAHQTHILQHAHPHHHQQQQAPQHQQQQLSHLLVHTHPSNSNSRSQSSPNINVPSLQNESTAASIAMNMNVHMMRGSLDPDPSLGGMHGIEVLHQHQQQHHHHHHHHTSNYPQHAVTPTNQHTHPHPQTHQTAHHHTSPETALRMHQAEAILRSHTEAAFRLATGSGPDTGVKCEADQNQLNSNNAGNAGGNSGGNSQQHRFHASSNHQENQRPSDS
Protein: Neutrophil cytosol factor 4 (NCF-4) (Neutrophil NADPH oxidase factor 4) (SH3 and PX domain-containing protein 4) (p40-phox) (p40phox) (Q15080)
Organism: Homo sapiens (Human)
Function: Component of the NADPH-oxidase, a multicomponent enzyme system responsible for the oxidative burst in which electrons are transported from NADPH to molecular oxygen, generating reactive oxidant intermediates. It may be important for the assembly and/or activation of the NADPH-oxidase complex.
Subcellular location: Cytoplasm, cytosol {ECO:0000269|PubMed:8280052}. Endosome membrane {ECO:0000269|PubMed:11684018}; Peripheral membrane protein {ECO:0000269|PubMed:11684018}; Cytoplasmic side {ECO:0000269|PubMed:11684018}. Membrane {ECO:0000269|PubMed:11684018, ECO:0000269|PubMed:8280052}; Peripheral membrane protein {ECO:0000269|PubMed:11684018}. Note=Translocates to the membrane upon activation by phorbol myristate acetate (PMA). {ECO:0000269|PubMed:8280052}.
Interaction partners:
- Neutrophil cytosol factor 2
- Cytochrome b-245 light chain
- Ras-related C3 botulinum toxin substrate 2
- NADPH oxidase 2
- Neutrophil cytosol factor 1
- NADPH oxidase 1
- NADPH oxidase activator 1
- NADPH oxidase organizer 1
- RAC-alpha serine/threonine-protein kinase
- NADPH oxidase 4
Sequence:
MAVAQQLRAESDFEQLPDDVAISANIADIEEKRGFTSHFVFVIEVKTKGGSKYLIYRRYRQFHALQSKLEERFGPDSKSSALACTLPTLPAKVYVGVKQEIAEMRIPALNAYMKSLLSLPVWVLMDEDVRIFFYQSPYDSEQVPQALRRLRPRTRKVKSVSPQGNSVDRMAAPRAEALFDFTGNSKLELNFKAGDVIFLLSRINKDWLEGTVRGATGIFPLSFVKILKDFPEEDDPTNWLRCYYYEDTISTIKDIAVEEDLSSTPLLKDLLELTRREFQREDIALNYRDAEGDLVRLLSDEDVALMVRQARGLPSQKRLFPWKLHITQKDNYRVYNTMP
Protein: Zinc finger-like gene 1g (B8A500)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
Sequence:
MAESARNYANGATLRTTSEKHGTEPPCVTIDQMLENLNAYLDKRLGLRKCCDDVSKKYSIKHSQSGLWALPDIKRAYGKTQRLCTTTKKDGLSVILVKQILQHEHMCETDKLERENKAEKAKVRALAEQLQNLKKDKERLENENNKLLTLISKQLESRSSSSFVDSEADLSINTCVHDHVNSKIRLAPVIVKHRRTNIEIDNEEGYEDNGERRTRTVTKVVKKYVPYRTYHPATPEQVDKWSKELPDVYKQPRKVWQFLQRLQKIYILHPLDGVMILNVTLRDSDQKRLTESVERRIGESQENIEDGWEAIKNFLFELKPAEVNWARITSCMQKTGESVAEFEERFRQIWTEHSGLNTSEDLDKDTGIPLKTAFVNGLNPEISKDLKIRYDDWDSTVTTFIQIVEWSAKLERAQDVRLRSLQSESLFYKNRTIEDEQKECVYMGYSKLRTKGRCRNCNEEGHWARECKLSLKHQSKDDDHLFKQFQQLTIQQKQTLLNAVQPQGN
Protein: Probable binding protein component of ABC transporter (Q9HUA1)
Organism: Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Interaction partners:
- RidA family protein
- D-amino acid dehydrogenase 2
- Amino acid ABC transporter membrane protein
- Glutamate/aspartate import permease protein GltK
- Amino acid ABC transporter ATP binding protein
- Probable permease of ABC transporter
- Probable amino acid permease
- Glutamate/aspartate import permease protein GltK
- Glutamate/aspartate import permease protein GltK
- Probable ATP-binding component of ABC transporter
Sequence:
MKTLVSSTFALSLSLAIGAAQAEELSGTLKKVADNGTITLGYRDASVPFSYLGDNSGQPMGYSVELAGKVVERLKSTLGKPELKVKYNLVTSQTRIPLVQNGTVDLECGSTGVTAERQKQVAFSYGFIYVKGQLLTRKDSGIAHFDDLKGKNVVTTAGTTNERYLKNYNAEHKLGMNVVSAKDHGEAFQMLQSGRAVAFYMDDALLYGERAKARQPHDWVVVGEPQSREIYSCMVRKDDPQFLALVNETLAGLYRSGEIQGIYQRWFQQPIPPKGLNLEFPMTAELKAILENPTSDPVQ
Protein: E3 ubiquitin-protein ligase Fancl (EC 2.3.2.27) (Fanconi anemia group L protein homolog) (Q8T913)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
- Fanconi anemia group I protein homolog
- Fanconi anemia group D2 protein homolog
- DEAD-box ATP-dependent DNA helicase Fancm
- BcDNA.LD22910
- DNA excision repair protein ERCC-1
- DNA repair endonuclease XPF
- WD repeat-containing protein 48 homolog
- Nuclear protein localization protein 4 homolog
- DNA repair protein RAD51 homolog 3
- Crossover junction endonuclease MUS81
Sequence:
MESNEDVERLLCQKYPGLAAELQPSGACIIRGVLGSEDTWRRLKLYLPHHPALHGFQLYVQESLEYKLYTSANLKLQDDWLLEDFLDHLPKILPAQKAPTVPKELCREGNIYYDILALYKSNEYCLQVDEACSMIRFSEFTDFEQHYLELKIPSLLLLDHSLPDCVSLGEMLTKSAGNLEEALNLFRKLLEDLRPFYDNFMDIDELCHVLQPSPISSKHKTRLFPLKDRVYLKLTIADPFACIASMSLKIIGPTEEVARLRHVLSDGLSNWDSEMNIHKNLLRMFDLCYFPMPDWSDGPKLDEEDNEELRCNICFAYRLDGGEVPLVSCDNAKCVLKCHAVCLEEWFKTLMDGKTFLEVSFGQCPFCKAKLSTSFAALLND
Protein: Excitatory amino acid transporter 1 (Glial glutamate transporter) (Sodium-dependent glutamate/aspartate transporter 1) (GLAST) (GLAST-1) (Solute carrier family 1 member 3) (P24942)
Organism: Rattus norvegicus (Rat)
Function: Sodium-dependent, high-affinity amino acid transporter that mediates the uptake of L-glutamate and also L-aspartate and D-aspartate. Functions as a symporter that transports one amino acid molecule together with two or three Na(+) ions and one proton, in parallel with the counter-transport of one K(+) ion (By similarity). Plays a redundant role in the rapid removal of released glutamate from the synaptic cleft, which is essential for terminating the postsynaptic action of glutamate (By similarity).
Subcellular location: Cell membrane {ECO:0000269|PubMed:1279699, ECO:0000269|PubMed:8387171}; Multi-pass membrane protein.
Interaction partners:
- Excitatory amino acid transporter 2
- Glutamine synthetase
- Glutamate receptor ionotropic, NMDA 2B
- Cytosolic 10-formyltetrahydrofolate dehydrogenase
- Nestin
- Glial fibrillary acidic protein
- Aquaporin-4
- Hexokinase-1
- ATP-sensitive inward rectifier potassium channel 10
- Fatty acid-binding protein, brain
Sequence:
MTKSNGEEPRMGSRMERFQQGVRKRTLLAKKKVQNITKEDVKSYLFRNAFVLLTVSAVIVGTILGFALRPYKMSYREVKYFSFPGELLMRMLQMLVLPLIISSLVTGMAALDSKASGKMGMRAVVYYMTTTIIAVVIGIIIVIIIHPGKGTKENMYREGKIVQVTAADAFLDLIRNMFPPNLVEACFKQFKTSYEKRSFKVPIQANETLLGAVINNVSEAMETLTRIREEMVPVPGSVNGVNALGLVVFSMCFGFVIGNMKEQGQALREFFDSLNEAIMRLVAVIMWYAPLGILFLIAGKILEMEDMGVIGGQLAMYTVTVIVGLLIHAVIVLPLLYFLVTRKNPWVFIGGLLQALITALGTSSSSATLPITFKCLEENNGVDKRITRFVLPVGATINMDGTALYEALAAIFIAQVNNFDLNFGQIITISITATAASIGAAGIPQAGLVTMVIVLTSVGLPTDDITLIIAVDWFLDRLRTTTNVLGDSLGAGIVEHLSRHELKNRDVEMGNSVIEENEMKKPYQLIAQDNEPEKPVADSETKM
Protein: Maf-like protein (F4K0M7)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
Sequence:
MTTKAMERGFKLILGSQSMARKRILAEMGYDYTIVTADIDEKAIRTEKPEDLVVALAEAKANEIISKLGGESQFAKDPQPTLLITADTVVVYKGVIREKPTTKEEAREFIKGYSGSHGGVVGSVLVRNLKTGVKKGGWDKAEVYFHEIPEQVIDGLIDDAITYKVAGGLTLEHPLISPFIDSVVGGVDTVMGLPKELTEKFINDVLL
Protein: Polyubiquitin 3 [Cleaved into: Ubiquitin] (Q1EC66)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Ubiquitin exists either covalently attached to another protein, or free (unanchored). When covalently bound, it is conjugated to target proteins via an isopeptide bond either as a monomer (monoubiquitin), a polymer linked via different Lys residues of the ubiquitin (polyubiquitin chains) or a linear polymer linked via the initiator Met of the ubiquitin (linear polyubiquitin chains). Polyubiquitin chains, when attached to a target protein, have different functions depending on the Lys residue of the ubiquitin that is linked: Lys-11-linked is involved in ERAD (endoplasmic reticulum-associated degradation) and in cell-cycle regulation; Lys-29-linked is involved in lysosomal degradation; Lys-33-linked is involved in kinase modification; Lys-48-linked is involved in protein degradation via the proteasome; Lys-63-linked is involved in endocytosis, and DNA-damage responses. Linear polymer chains formed via attachment by the initiator Met lead to cell signaling. Ubiquitin is usually conjugated to Lys residues of target proteins, however, in rare cases, conjugation to Cys or Ser residues has been observed. When polyubiquitin is free (unanchored-polyubiquitin), it also has distinct roles, such as in activation of protein kinases, and in signaling (By similarity).
Subcellular location: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
Interaction partners:
- Protein NBR1 homolog
- E3 ubiquitin-protein ligase PRT1
- E3 ubiquitin-protein ligase UPL4
- E3 ubiquitin-protein ligase UPL3
- 26S proteasome non-ATPase regulatory subunit 2 homolog A
- Small ribosomal subunit protein eS1z
- Small ribosomal subunit protein uS9x
- Large ribosomal subunit protein uL5z
- Proteasome subunit beta type-1
- Small ribosomal subunit protein eS7x
Sequence:
MQIFVKTLTGKTITLEVESSDTIDNVKAKIQDKEGIPPDQQRLIFAGKQLEDGRTLADYNIQKESTLHLVLRLRGGMQIFVKTLTGKTITLEVESSDTIDNVKAKIQDKEGIPPDQQRLIFAGKQLEDGRTLADYNIQKESTLHLVLRLRGGMQIFVKTLTGKTITLEVESSDTIDNVKAKIQDKEGIPPDQQRLIFAGKQLEDGRTLADYNIQKESTLHLVLRLRGGMQIFVKTLTGKTITLEVESSDTIDNVKAKIQDKEGIPPDQQRLIFAGKQLEDGRTLADYNIQKESTLHLVLRLRGGSF