wanglab/gogpt-training-data huggingface dataset:
Protein: Hemolysin, plasmid (P08715)
Organism: Escherichia coli
Function: Bacterial hemolysins are exotoxins that attack blood cell membranes and cause cell rupture by forming a pore.
Subcellular location: Secreted {ECO:0000250|UniProtKB:P09983}. Host cell membrane {ECO:0000305|PubMed:12598051, ECO:0000305|PubMed:2121650}; Multi-pass membrane protein {ECO:0000305|PubMed:2121650}.
Interaction partners:
Sequence:
MTTITTAQIKSTLQSAKQSAANKLHSAGQSTKDALKKAAEQTRNAGNRLILLIPKDYKGQGSSLNDLVRTADELGIEVQYDEKNGTAITKQVFGTAEKLIGLTERGVTIFAPQLDKLLQKYQKAGNILGGGAENIGDNLGKAGGILSTFQNFLGTALSSMKIDELIKKQKSGGNVSSSELAKASIELINQLVDTVASLNNNVNSFSQQLNTLGSVLSNTKHLNGVGNKLQNLPNLDNIGAGLDTVSGILSAISASFILSNADADTRTKAAAGVELTTKVLGNVGKGISQYIIAQRAAQGLSTSAAAAGLIASAVTLAISPLSFLSIADKFKRANKIEEYSQRFKKLGYDGDSLLAAFHKETGAIDASLTTISTVLASVSSGISAAATTSLVGAPVSALVGAVTGIISGILEASKQAMFEHVASKMADVIAEWEKKHGKNYFENGYDARHAAFLEDNFKILSQYNKEYSVERSVLITQQHWDTLIGELAGVTRNGDKTLSGKSYIDYYEEGKRLEKKXDEFQKQVFDPLKGNIDLSDSKSSTLLKFVTPLLTPGEEIRERRQSGKYEYITELLVKGVDKWTVKGVQDKGAVYDYSNLIQHASVGNNQYREIRIESHLGDGDDKVFLSAGSANIYAGKGHDVVYYDKTDTGYLTIDGTKATEAGNYTVTRVLGGDVKVLQEVVKEQEVSVGKRTEKTQYRSYEFTHINGKNLTETDNLYSVEELIGTTRADKFFGSKFTDIFHGADGDDLIEGNDGNDRLYGDKGNDTLSGGNGDDQLYGGDGNDKLIGVAGNNYLNGGDGDDEFQVQGNSLAKNVLFGGKGNDKLYGSEGADLLDGGEGDDLLKGGYGNDIYRYLSGYGHHIIDDDGGKEDKLSLADIDFRDVAFKREGNDLIMYKGEGNVLSIGHKNGITFRNWFEKESGDISNHEIEQIFDKSGRIITPDSLKKALEYQQRNNKASYVYGNDALAYGSQGDLNPLINEISKIISAAGSFDVKEERTAASLLQLSGNASDFSYGRNSITLTTSA
Protein: Proteasome subunit alpha type-3 (20S proteasome subunit alpha-7) (Q9V5C6)
Organism: Drosophila melanogaster (Fruit fly)
Function: The proteasome is a multicatalytic proteinase complex which is characterized by its ability to cleave peptides with Arg, Phe, Tyr, Leu, and Glu adjacent to the leaving group at neutral or slightly basic pH. The proteasome has an ATP-dependent proteolytic activity (By similarity).
Subcellular location: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
Interaction partners:
- Proteasome subunit beta type-1
- 26S proteasome non-ATPase regulatory subunit 14
- Proteasome subunit beta
- Proteasome subunit beta type-3
- Proteasome subunit alpha type-7-1
- Proteasome subunit alpha type-4
- Proteasome subunit alpha type-2
- Proteasome subunit beta
- Proteasome subunit alpha type-5
- Proteasome subunit alpha type-1
Sequence:
MSTIGTGYDLSASQFSPDGRVFQIDYASKAVEKSGTVIGIRGKDAVVLAVEKIITSKLYEPDAGGRIFTIEKNIGMAVAGLVADGNFVADIARQEAANYRQQFEQAIPLKHLCHRVAGYVHAYTLYSAVRPFGLSIILASWDEVEGPQLYKIEPSGSSFGYFACASGKAKQLAKTEMEKLKMDMRTDELVESAGEIIYKVHDELKDKDFRFEMGLVGRVTGGLHLINPSELTEKARKAGDAANKDEDSDNETH
Protein: L-allo-isoleucine:holo-[CmaA peptidyl-carrier protein] ligase (EC 6.2.1.46) (Adenylation activation enzyme) (Coronamic acid synthetase CmaA) (Q6TNA5)
Organism: Pseudomonas savastanoi pv. glycinea (Pseudomonas syringae pv. glycinea)
Function: Involved in the biosynthesis of the phytotoxin coronatine (COR) which mimics the plant hormone jasmonic acid isoleucine and promotes opening of stomata for bacterial entry, bacterial growth in the apoplast, systemic susceptibility, and disease symptoms. CmaA catalyzes the adenylation of L-allo-isoleucine (via the A domain) and the attachment of L-allo-isoleucine to the 4'-phosphopantetheine arm located within the T domain of CmaA. It can also use L-isoleucine, L-leucine and L-valine as substrates.
Interaction partners:
Sequence:
MTSYHSHPPKAYRRFESVCTQAPNAIAVVHEGKPVTYQQLQTQVLERSEALIRQGLADHPYMPLMANRCLEYLITMLACCKLGITYVSIEPSTPSKRLIAVLEQLGCNHLLLLGQPTDLRPDPTLTCFRLDDCGTLCSDGPALRQPIRRRLDDASVITVMFTSGTTGVPKGVRISQDGLLNLVDNVQQQVQGKPRSYVHHSSIGFDAALFEVWVPLLTGACVTLQPSEFNIDALDHCVRAASCDVLLLTTSLFHLVAQHRLSMLEAVRVLYVGGEVLKPVHARALLLANPRITLVNGYGPTENTVFSTWYSLNKPEDAERDVIPIGQFLHQVHGKIVDAKLQEVEVGTPGELLLTGANLALGYLDEALTPTRFLQLPEGTYYRTGDYVIQDEHGMLFYQGRIDEQVKIKGFRVEIAEVEHALTQLPGVAQAVVQAHVMNDLENSLHAFIVFRHGSPTIEESKLMSLLGDRLPHYMVPRRIHYLAELPLTANGKVDKRSLQPPEKAAVVSPQAGSAVLEIWSGILGTRNLQLEHSIYGYGASSLSVVMAHSRINEILGRTTPFDEVARLSTFQEWVQYYATHADPVTSLRSQHGNH
Protein: Glycoprotein C (C7EYC8)
Organism: Suid herpesvirus 1 (SuHV-1) (Pseudorabies virus)
Subcellular location: Virion membrane {ECO:0000256|ARBA:ARBA00004381}; Single-pass membrane protein {ECO:0000256|ARBA:ARBA00004381}.
Interaction partners:
Sequence:
MASLARAMLALLALYAAAIAAAPSTTTALGTTPNGGGGGNSSAGELSPSPPPTPAPASPEAGAVSTPRAPPPSVSRRKPPRNNNRTRVHGDKATAHGRKRIVCRERLFSARVGDAVSFGCAVFPRAGETFEVRFYRRGRFRSPDADPEYFDEPPRSELPRERLLFSSANASLAHADALTPVVEDEGGRATVANVSGEVSVRVAAADAETEGVYTWRVLSANGTEVRSANVSLLLYSQPEFGLSAPPVLFGEPFRAACVVRDYYPRRSVRLRWFADEHPVDAAFVTNSTVADELGRRTRVSVVNVTRADVPGLAAADDADALAPSLRCEAVWYRDSVASQRFSEALRPHVYHPAAVSVRFVEGFAVCDGLCVPPEARLAWSDHAADTVYHLGACAEHPGLLNVRSARPLSDLDGPVDYTCRLEGLPSQLPVFEDTQRYDASPASVSWPVVSSMIVVIAGIGILAIVLVIMATCVYYRRAGP
Protein: UDP-N-acetylglucosamine--peptide N-acetylglucosaminyltransferase stabilizing protein GtfB (Glycosyltransferase stabilizing protein GtfB) (A0A0H2UR90)
Organism: Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4)
Function: Required for the polymorphic O-glycosylation of the serine-rich repeat protein PsrP. A stabilizing protein that is part of the accessory SecA2/SecY2 system specifically required to export serine-rich repeat cell wall proteins encoded upstream in the same operon. The GtfA-GtfB complex adds GlcNAc from UDP-GlcNAc to PsrP, attaching the first sugar residue. Stabilizes the glycosylation activity of GtfA (By similarity). Has no N-acetylglucosaminyl transferase activity on its own.
Subcellular location: Cell membrane {ECO:0000255|HAMAP-Rule:MF_01473}; Peripheral membrane protein {ECO:0000255|HAMAP-Rule:MF_01473}.
Interaction partners:
Sequence:
MIELYDSYSQESRDLHESLGATGLSQLGVVIDADGFLPDGLLSPFTYYLGYEDGKPLYFNQVPVSDFWEILGDNQSACIEDVTQERAVIHYADGMQARLVKQVDWKDLEGRVRQVDHYNRFGACFATTTYSADSEPIMTVYQDVNGQQVLLENHVTGDILLTLPGQSMRYFANKVEFITFFLQDLEIDTSQLIFNTLATPFLVSFHHPDKSGSDVLVWQEPLYDAIPGNMQLILESDNVRTKKIIIPNKATYERALELTDEKYHDQFVHLGYHYQFKRDNFLRRDALILTNSDQIEQVEAIAGALPDVTFRIAAVTEMSSKLLDMLCYPNVALYQNASPQKIQELYQLSDIYLDINHSNELLQAVRQAFEHNLLILGFNQTVHNRLYIAPDHLFESSEVAALVETIKLALSDVDQMRQALGKQGQHANYVDLVRYQETMQTVLGG
Protein: Mitochondrial poly(A) polymerase (Q5T852)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MQNERREQAQRTVLIHCPEKISENKFLKYLSQFGPINNHFFYESFGLYAVVEFCQKESIGSLQNGTHTPSTAMETAIPFRSRFFNLKLKNQTSERSRVRSSNQLPRSNKQLFELLCYAESIDDQLNTLLKEFQLTEENTKLRYLTCSLIEDMAAAYFPDCIVRPFGSSVNTFGKLGCDLDMFLDLDETRNLSAHKISGNFLMEFQVKNVPSERIATQKI
Protein: Catalase isozyme 2 (EC 1.11.1.6) (P30567)
Organism: Gossypium hirsutum (Upland cotton) (Gossypium mexicanum)
Function: Occurs in almost all aerobically respiring organisms and serves to protect cells from the toxic effects of hydrogen peroxide.
Subcellular location: Peroxisome.
Interaction partners:
- (R)-specific enoyl-CoA hydratase-like
- (R)-specific enoyl-CoA hydratase-like
- Enoyl-CoA hydratase 2, peroxisomal-like
- NAD
- Peroxiredoxin
- Peroxiredoxin
- L-arabinolactonase-like
- 2-Cys peroxiredoxin BAS1-like
- thioredoxin-dependent peroxiredoxin
- thioredoxin-dependent peroxiredoxin
Sequence:
MDPYKFRPSSSFDSPFWTTNSGAPVWNNNSSLTVGARGPILLEDYHLVEKLANFDRERIPERVVHARGASAKGFFEVTHDISQLTCADFLRAPGVQTPLIVRFSTVIHERGSPETLRDPRGFAVKFYTREGNFDLVGNNFPVFFIRDGMKFPDMVHALKPNPKSHIQENWRILDFFSHHPESLHMFTFLFDDIGVPQDYRHMDGSGVHTYTLINKAGKSHYVKFHWKPTCGVKSLLEDEAIRVGGANHSHATQDLYDSIAAGNYPEWKLFIQIMDPLHEDRFDFDPLDVTKTWPEDIFPLQPMGRMVLNKNIDNFFAENEQLAFCPSLIVPGIYYSDDKLLQTRIFSYSDTQRHRLGPNYLQLPANAPKCAHHNNHHEGFMNFMHRDEEVNYFPSRYDPVRHAEKHPIPSTVLSGKREKCIIGKENNFKQPGERYRSFSADRQERFINRWIDALSDPRVTHEIRSIWISYWSQADKSLGQKIASRLNVRPSI
Protein: RNA-binding protein ZC3H11 (CCCH zinc finger protein ZC3H11) (Q57W26)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Function: RNA-binding protein involved in regulation of mRNA stability. Binds AU-rich regions in the 3'-UTR of mRNAs and promotes their stabilization by recruiting a MKT1-containing complex. Stabilizes chaperone mRNAs during stress that causes an accumulation of misfolded or unfolded proteins in the cytoplasm.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:23592996}.
Interaction partners:
- Ribosomal RNA-processing protein 43
- 5'-3' exoribonuclease 2
Sequence:
MSTATSAPVVESMSDTVVCPQLSRHSTSLEELYTIGYNRSHSPSCFSSAGCEEEEGQKNVLAERYKTKLCKNFVQYGTCPYDIRCMFAHGEEELRTAEMNIMDGLVTKDAITSFQKLWHRAVSASSGSKHHSSHVANRRGVMTTATTTTTAGGSTDAAMHICRRMQRVVAAAAAAVPCGGRRVVSGSIRIRGCVRHNPYCHNILPTVSRYYSTMPDVFTRPYSKSDSCGNEAITEGNAWTYANEEGNEKETPAMISSGVPELTAWKRFNYVAERSQCTSVPEQNLPCADFAAIKESNNTGGNASGVDVENVDDAEHSTCSSVGNESGYFCRASRSASCGEQSQSHLKREGNEGRGEGLHMFLSL
Protein: TRAF-interacting protein with FHA domain-containing protein B (TIFA-like protein) (Q6ZNK6)
Organism: Homo sapiens (Human)
Function: Inhibits TIFA-mediated TRAF6 activation possibly by inducing a conformational change in TIFA.
Interaction partners:
Sequence:
MEKPLTVLRVSLYHPTLGPSAFANVPPRLQHDTSPLLLGRGQDAHLQLQLPRLSRRHLSLEPYLEKGSALLAFCLKALSRKGCVWVNGLTLRYLEQVPLSTVNRVSFSGIQMLVRVEEGTSLEAFVCYFHVSPSPLIYRPEAEETDEWEGISQGQPPPGSG
Protein: Tripartite motif-containing protein 72 (EC 2.3.2.27) (Mitsugumin-53) (Mg53) (Q6ZMU5)
Organism: Homo sapiens (Human)
Function: Muscle-specific protein that plays a central role in cell membrane repair by nucleating the assembly of the repair machinery at injury sites. Specifically binds phosphatidylserine. Acts as a sensor of oxidation: upon membrane damage, entry of extracellular oxidative environment results in disulfide bond formation and homooligomerization at the injury site. This oligomerization acts as a nucleation site for recruitment of TRIM72-containing vesicles to the injury site, leading to membrane patch formation. Probably acts upstream of the Ca(2+)-dependent membrane resealing process. Required for transport of DYSF to sites of cell injury during repair patch formation. Regulates membrane budding and exocytosis. May be involved in the regulation of the mobility of KCNB1-containing endocytic vesicles (By similarity).
Subcellular location: Cell membrane, sarcolemma {ECO:0000269|PubMed:36944613}. Cytoplasmic vesicle membrane {ECO:0000269|PubMed:36944613, ECO:0000269|PubMed:37770719}. Note=Tethered to plasma membrane and cytoplasmic vesicles via its interaction with phosphatidylserine. {ECO:0000250, ECO:0000269|PubMed:36944613, ECO:0000269|PubMed:37770719}.
Interaction partners:
- Caveolin-3
- Dysferlin
- Annexin A1
- Annexin A6
- Gamma-butyrobetaine dioxygenase
- Annexin A2
- Caveolae-associated protein 1
- Ubiquitin-conjugating enzyme E2 H
- Insulin receptor substrate 1
- T-cell receptor-associated transmembrane adapter 1
Sequence:
MSAAPGLLHQELSCPLCLQLFDAPVTAECGHSFCRACLGRVAGEPAADGTVLCPCCQAPTRPQALSTNLQLARLVEGLAQVPQGHCEEHLDPLSIYCEQDRALVCGVCASLGSHRGHRLLPAAEAHARLKTQLPQQKLQLQEACMRKEKSVAVLEHQLVEVEETVRQFRGAVGEQLGKMRVFLAALEGSLDREAERVRGEAGVALRRELGSLNSYLEQLRQMEKVLEEVADKPQTEFLMKYCLVTSRLQKILAESPPPARLDIQLPIISDDFKFQVWRKMFRALMPALEELTFDPSSAHPSLVVSSSGRRVECSEQKAPPAGEDPRQFDKAVAVVAHQQLSEGEHYWEVDVGDKPRWALGVIAAEAPRRGRLHAVPSQGLWLLGLREGKILEAHVEAKEPRALRSPERRPTRIGLYLSFGDGVLSFYDASDADALVPLFAFHERLPRPVYPFFDVCWHDKGKNAQPLLLVGPEGAEA
Protein: tRNA N(3)-methylcytidine methyltransferase trm141 (EC 2.1.1.-) (O74386)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: S-adenosyl-L-methionine-dependent methyltransferase that mediates N(3)-methylcytidine modification of residue 32 of the tRNA anticodon loop of tRNA(Ser). N(3)-methylcytidine methylation by trm141 requires the formation of N(6)-dimethylallyladenosine(37) (i6A37) by tit1 as prerequisite. Does not catalyze N(3)-methylcytidine modification of tRNA(Thr).
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus {ECO:0000269|PubMed:16823372}.
Interaction partners:
- 18S rRNA aminocarboxypropyltransferase
- tRNA dimethylallyltransferase
- Serine--tRNA ligase, cytoplasmic
- Serine--tRNA ligase, mitochondrial
- tRNA
- tRNA-specific adenosine deaminase subunit tad2
- tRNA-specific adenosine deaminase subunit tad3
Sequence:
MSGISKLSDFWVEKYKKESKKSWDKFYKRNETRFFKDRHWLDREFDCYFGLPDKLPLTILEVGCGVGNLVYPLLEVQPNLKIYCCDFSPRAIDFVKKHSCYNENRVFPFVNDITEDSLLEVLGSACIDTLTAIFVLSAIPREKQLRSIKNLASVIKPGGHLVFRDYCDGDFAQEKFMTSGDPSMIDEQTFVRQDGTLSLFFREEDIAEWMKSAGFGLVTLDRVNRTVDNRKRNLNMKRTFLQGVWKKL
Protein: Iron (III) ABC transporter, periplasmic iron-bindin gprotein (B5Z9J2)
Organism: Helicobacter pylori (strain G27)
Interaction partners:
Sequence:
MLIARFKKALISYSLGALIVSSLLGVANASNQEVKVKDYFGEQTIKLPVSKIIYLGSFAEVPAMFHTWDRVVGISDYAFKSDIVKATLKDPERIKPMSSDHVAALNVELLKKLSPDLVVTFVGNPKAVEHAKKFGISFLSFQEKTIAEVMEDIDTQAKALEVDASKKLAKMQETLDFIAERLKGVKKKKGVELFHKANKISGHQALDSDILEKGGIDNFGLKYVKFGRADISVEKIVKENPEIIFIWWISPLSPEDVLNNPKFATIKAIKNKQVYKLPTMDIGGPRAPLISLFIALKAHPEAFKGVDINAIVKDYYKVVFDLNDAEVEPFLWH
Protein: Lysine-specific histone demethylase 1, putative (EC 1.14.11.27) (Q8I5T5)
Organism: Plasmodium falciparum (isolate 3D7)
Interaction partners:
Sequence:
MGTEKEDDEQDIVNRSNDLKKKKENNKCDNMSNDISDSISNNISDSISTNISNNISNNISNNISNNLSNNISNNISNNLSNNISNNTSNNTSHNISHNICHNISQNNHDIIKKVHIKNLNIMNTHKDNNYKYKNNGLNIYNKKKKDYNGDENLKINTRESYDIFYSYLKLSEKKSLKQSDMIKDNMSEQDFFINVFSQKLKKHNIDLIMINNKLYIYIKFSQDIDHLIPYFKREFFFKTLIGNNIILLLAKKYEVTEVLIKSLYLKETIQKFFTSNFTIEDFLVHNNFMNKYEIYRNIVINNFFPIQMNNKNGDHKKKKINNNNNNKKKYIDHEDINNFVEYVHDLEENQKYSSLPFEKKCYKENIKCMKNFEKSHNMNKIQYVEDFQKENTENGKILYLKEKKGINKYNNEKDMMCNHSAFDNNMVQNNNVLDNNMCNKKNIKKKMKKNNVIKFMVDNYVINDVSNKMNHHNESLQENNNYSVLQIPNNNKQINNNIRANVILNNEFNLDVQKFRNTEETMNKIESNKNDKEERLQFEKEKKQILKREKKLRENQEKKRKQNQEKENKKQEKIIKKKELLILEKEIRKKLKEEKKLKEKEEKKKEKEKFLKNEKEIKKKIKEDKKRQKEEFLRKIKEEKKKLKEEKKKLKQEIINSIKEERKKFKELKSKFKKISKKDNHLNKDKKKTKQNKIDKSNQSNMNKKEYNNNDKKKDDINYQFLTDQINNNTVDKKKRKKTHDISLSIKKKKKCTKNNLLLNSINDIKSDSLSFISTFPTFNNIEKEQEDRNEINDILKLIEIKKVVNTQEKNDYIECLHKSKSKNVKRNKDKIKQNQLLSKGNNKIITKNGEHMNDQSDPLNQINSDLLNIDDFLINNMNTIIKKYKKGDTSNVDMSNVDMSNVDISNVDFSNKDISNKDISYVDISKKNVVHTNNSLHNIDNIHYNKNMNNSERHNESEINELILKGLKSFGDIKNLKSLQKILRIKESKGKNKIETVVHIPNNVIERSVAKKIVLNKHEGIKNKDGVKEKVKTKKKISLFGIVKPEDIIKRGINNVYHNIEDNQKLYTDVLIIGAGISGLAASYYLNKCNAKFLVIEGRNRIGGRAFSTILPERIINNKVLPETVVDLGANYLHCCDNADLTNDKKGKTKHEFANCTEFNNEKSMRKEDDIDYEDNFIWNMKKKKTKKKKYKVIVKKRKYNYNKDNGNDKNKMGNFSIYDVQKEYVTNINLFKEEYSKLINDFAYLPYFEYLNNSLQSEHNQDDENKTGDKNKISGGNKNIYRYLNSNKNISCNSNIYNNQRYYSDEDYFYSRRIKNRRKIKLRNNMLFMIKNNIDNIRNYFKIYNKEKKDNILNFFKSLDEDIHFYNNLSDSCVHTSSVLYPKNNCTNKSNKLLKILSFNKDTRRRREYDKSVTQLAEKLKPRVSLVCGKDNWESTFYAHWYNNENGKKIKSFKIYRVNLLCDKIRVRAARKMRNFLFIGDSCNDEYQKDIKSEDQQKSNNNYVSDDTNEKDSDYFYNNDILKEDKQINNNILIDDTYHKEILFNNNHVKNIKPNENNIIRNENFEASVLYNNKDDMKLENEENGKNAENGKNEENGENGKNAENGKNEQNEQNGKNGKNEENEENGKNEENGKNEENGKNGKNEQNKNNEKTSKKHIISSKKKMSKVDMNNILSYDNHAIIYNNYYDYGDLYNKVVRNVSSTNRNIDDEERKEKKKKEDISKTELYYNNKKRRSMWDLLMECTEEIFTEMNINEENFTMEEWKMLMVTLQSRYGYGSDLRETSIAMSRLPFSNYLDIDMCPKYGSNNYILKNIKYYDKIKKNEQTPYISSFKDLNTSDKIVVDGWKWLINYLSEEVQNKIFLNTVAELVYIKDKHQDKKIYHLDNDNCQINKQKSSSFLNTKKKNNNNNNNNNNIESVENNSINSDHVINQDNNSFVPQNEVSSKNKKKYINENFLINNVIKDDYKLGENNEDDYKVMIKCKCYDTKFKNINKHFHGTSDLNNCNYKNVTIYAKYVIVALPLGCLIENDKKRKLKTCLKFEPELHPLKLRALQNYKMGNHNKIILRFYPYNFTWPFDSLQINCIDQKFQFLNLHAYGKIGCILVHCFPPWSCTYGYIKKEHYIINECLYTLNKMFEKSGKKLPILVDYIITKWQDDNFSFGSYAYPYINCNDNDLIYLRSPHPINNPRVVFCGEYLSKSYFQCVDGAYDTGIRAAEDIAHIGLHLKNNDTKNYKTDVYIFPQNKCPFTNIPLPPIKKKFLGFYITDGSDEALTDYESSSDENMNTNVDINIDINSNTNIDINNNTNSNTSSNNNNTNKYNYCNNNIPISVMKKEYEFLLYSLQSIQNIFRFLKKQNTHKNFKQDKNINHIKNETDALKCSSYKKEIKSNTYESFTNNSLINFEDKKSNDVKSNISTLLLNLYEYNNKSTDQIHYFDRIKSIDSYKSKYKNGSYLLELHSKDSENDSNKNDANNICTIETFNNVDKNNKGDHINDVHNDVYNDVYNDKYTSNYNIETYSHITNNHFEYINNISNLYINKYMIKLNDAVFYNYNEIENTILNKQHNAEYNKSYFVLLQTFSNIFKKYSDFTYFIQKELFLKIQAMKHILFNDNNFQSLQDMNVVLSQAEHKNDHIVSHNNHMNDVDRKKAYEQNTDIINEDDKEISYFHEKMEEVNNMNKMKLSLNLIKSNMVGNNNDDDNNNNNGHIQKSNISTDELDINKINLNSKTKNNNITNKKDVMIQTNLNIYNNIDLQNKIKNIYINNRKICYLNDYLKYVLIHLSISKNILDEQIMSSNNNKWNSCGFLFFLCYILQYILKHLKYDLFNSTVNTKVVIQLLCDYIYYLIFCKHDILCYKCMNGGELNMCDSYNCNNSWHTYCLSSSEHNMNNKNDKFWLCPSCSNIDISKHVQRGCYNQNEIMENYWKRRIYIYKIKFFLSRTRKIRKRLDLLKAHLSRSVA
Protein: Dopamine D2-like receptor (DD2R) (Q8IS44)
Organism: Drosophila melanogaster (Fruit fly)
Function: Receptor for dopamine. The activity of this receptor is mediated by G proteins which inhibit adenylyl cyclase.
Subcellular location: Cell membrane {ECO:0000269|PubMed:12391323}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Dopamine receptor 2
- Dopamine receptor 1
- G protein alpha i subunit subunit alpha 65A)
- G protein beta subunit 5
- G protein alpha s subunit subunit alpha)
- Guanine nucleotide-binding protein subunit beta-1
- IP03705p
Sequence:
MLSPFDWRRGISSSGTGGTMAAQPLSSTAATTAAATGATAATAATAATTSATLSTAAASTSTTAAPSAGATWINHHLAVEADSSQPANGSDAQAGVEGPTMPAGYLPLYEDVETAAEDAGYALIDDISEWLLGSVGSEAAVGGPENSTNLAVTGANGTLAWLEALNSTQPAQSNSSAEDGERGRYSLRSFVEQQLAGGGAAGAGDGGDAGIALIDSGEEAALDNVADAETDYGMLGGFGDAELLQRTATVARETLGNRTAPSTTSYDGGGSGDVGVAGGLAGTAGGGVGGAGGSGGSTFMLLLENFNDYFPNYNGSTVSGTSTIAPGVAITGSRGSGLLLEQNLTGLYLDGYRLNCTNETLNLTDSCGELRVVDHNYWALILILFPILTLFGNILVILSVCRERSLQTVTNYFIVSLAIADLLVAVVVMPFAVYFLVNGAWALPDVVCDFYIAMDVICSTSSIFNLVAISIDRYIAVTQPIKYAKHKNSRRVCLTILLVWAISAAIGSPIVLGLNNTPNREPDVCAFYNADFILYSSLSSFYIPCIIMVFLYWNIFKALRSRARKQRAARKPHLSELTGGSVIENIAQTRRLAETALDSSRHASRILPDEAATNTASGSNEEEDENAISPDIDDCHVIVNDKSTEFMLATVVEETGNSVVAQITTQPQLVVADPNGNHDSGYAASNVDDVLAGVAPASASAATSAAPRSSGSPPDSPLPSGATLQRSSVSSQRRPTGDDSPKRGEPALRSVGVDNSSVAMKPLSFVRYGVQEAMTLARNDSTLSTTSKTSSRKDKKNSQASRFTIYKVHKASKKKREKSSAKKERKATKTLAIVLGVFLFCWLPFFSCNIMDAMCAKFKKDCRPGLTAYMMTTWLGYINSFVNPVIYTIFNPEFRKAFKKIMHMG
Protein: NBR1 autophagy cargo receptor (cDNA FLJ55359, highly similar to Next to BRCA1 gene 1 protein) (B7Z5R6)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MEPQVTLNVTFKNEIQSFLVSDPENTTWADIEAMVSINSQGEYEEALKMAVKQGNQLQMQVHEGHHVVDEAPPPVVGAKRLAARAGKKPLAHYSSLVRVLGSDMKTPEDPAVQSFPLVPCDTDQPQDKPPDWFTSYLETFREQVVNETVEKLEQKLHEKLVLQNPSLGSCPSEVSMPTSEETLFLPENQFSWHIACNNCQRRIVGVRYQCSLCPSYNICEDCEAGPYGHDTNHVLLKLRRPVVGSSEPFCHSKYSTPRLPAALEQVRLQKQVDKNFLKAEKQRLRAEKKQRKAEVKELKKQLKLHRKIHLWNSIHGLQSPKSPLGRPESLLQSNTLMLPLQPCTSVMPMLSAAFVDENLPDGTHLQPGTKFIKHWRMKNTGNVKWSADTKLKFMWGNLTLASTEKKDVLVPCLKAGHVGVVSVEFIAPALEGTYTSHWRLSHKGQQFGPRVWCSIIVDPFPSEESPDNIEKGMISSSKTDDLTCQQEETFLLAKEERQLGEVTEQTEGTAACIPQKAKNVASERELYIPSVDLLTAQDLLSFELLDINIVQELERVPHNTPVDVTPCMSPLPHDSPLIEKPGLGQIEEENEGAGFKALPDSMVSVKRKAENIASVEEAEEDLSGTQFVCETVIRSLTLDAAPDHNPPCRQKSLQMTFALPEGPLGNEKEEIIHIAEEEAVMEEEEDEEDEEEEDELKDEVQSQSSASSEDYIIILPECFDTSRPLGDSMYSSALSQPGLERGAEGKPGVEAGQEPAEAGERLPGGENQPQEHSISDILTTSQTLETVPLIPEVVELPPSLPRSSPCVHHHGSPGVDLPVTIPEVSSVPDQIRGANNF
Protein: Putative RNA polymerase II transcriptional coactivator (Q94045)
Organism: Caenorhabditis elegans
Function: General coactivator that functions cooperatively with TAFs and mediates functional interactions between upstream activators and the general transcriptional machinery. Binds single-stranded DNA (By similarity).
Subcellular location: Nucleus {ECO:0000250}.
Interaction partners:
- DUF3453 domain-containing protein
- Translation machinery-associated protein 7 homolog
Sequence:
MSSSSSSEDELEKKVTKEQKKKETKSKKRQSEAVEEEKQEVKKAKNEEEVSGRLKDSDGNEMFEIGNLRYATVSKFKGKEYVNIREYYIDRDSQKMMPSRKGISLSKAQWANLKDLIPEIDKKF
Protein: Hydroxyethylthiazole kinase (EC 2.7.1.50) (4-methyl-5-beta-hydroxyethylthiazole kinase) (TH kinase) (Thz kinase) (P76423)
Organism: Escherichia coli (strain K12)
Function: Catalyzes the phosphorylation of the hydroxyl group of 4-methyl-5-beta-hydroxyethylthiazole (THZ).
Interaction partners:
- Hydroxymethylpyrimidine/phosphomethylpyrimidine kinase
- Thiamine-phosphate synthase
- Phosphomethylpyrimidine synthase
- Thiazole synthase
- Sulfur carrier protein ThiS adenylyltransferase
- 2-iminoacetate synthase
- HTH-type transcriptional regulator GgaR
- Thiamine-binding periplasmic protein
- Sulfur carrier protein ThiS
Sequence:
MQVDLLGSAQSAHALHLFHQHSPLVHCMTNDVVQTFTANTLLALGASPAMVIETEEASQFAAIASALLINVGTLTQPRAQAMRAAVEQAKSSQTPWTLDPVAVGALDYRRHFCHELLSFKPAAIRGNASEIMALAGIANGGRGVDTTDAAANAIPAAQTLARETGAIVVVTGEMDYVTDGHRIIGIHGGDPLMTKVVGTGCALSAVVAACCALPGDTLENVASACHWMKQAGERAVARSEGPGSFVPHFLDALWQLTQEVQA
Protein: Uracil-DNA glycosylase (UDG) (EC 3.2.2.27) (Q7ZVD1)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Mitochondrion {ECO:0000256|HAMAP-Rule:MF_03166}. Nucleus {ECO:0000256|HAMAP-Rule:MF_03166}.
Interaction partners:
Sequence:
MIGQKSIKSFFSPASKKRNLDEIKTGETRDDVKKQKLESGNEAPLSPEQLERIAKNKKAALERLQSAAPDGIGESWLKALSAEFGKSYFKSLMSFVGEERKKHTIYPPPHAVFTWTQTCDIKDVKVVILGQDPYHGPNQAHGLCFSVQRPVPPPPSLVNIFKELASDIEGFVQPDHGDLTGWANQGVLLLNAVLTVRAHQANSHKDKGWETFTDAVVHWLSSNMQGLVFILWGSYAQKKGAAINKKQHHVLQAVHPSPLSAHRGFFGCKHFSKANELLKKSGKKPIDWKAL
Protein: ODF2L protein (Q96GC1)
Organism: Homo sapiens (Human)
Subcellular location: Cell projection, cilium {ECO:0000256|ARBA:ARBA00004138}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole {ECO:0000256|ARBA:ARBA00004114}.
Interaction partners:
Sequence:
MLLENLTDNESENTNLKKKVFEKEAHIQELSCLFQSEKSLETKIAKWNLQSRMNKNEAIVMKEASRQKTVALKKGI
Protein: U3 small nucleolar RNA-associated protein 22 (U3 snoRNA-associated protein 22) (O94676)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Involved in nucleolar processing of pre-18S ribosomal RNA and ribosome assembly.
Subcellular location: Nucleus, nucleolus {ECO:0000269|PubMed:16823372}.
Interaction partners:
- U3 small nucleolar RNA-associated protein 17
- Periodic tryptophan protein 2 homolog
- Probable U3 small nucleolar RNA-associated protein 13
- RNA cytidine acetyltransferase
- Probable U3 small nucleolar RNA-associated protein 18
- Probable nucleolar complex protein 14
- U3 small nucleolar RNA-associated protein 21 homolog
- U3 small nucleolar RNA-associated protein 20
- U3 small nucleolar RNA-associated protein 10
- rRNA biogenesis protein rrp5
Sequence:
MNGLKREHESSSSQDGSKTPETEYDSHVDSIEDIHSLASKRKKLNEKKENLEDLTLLKTSAFELKLNELIREISVRGKYFRHANTFVEKIKDLIFKTPVIPETNFWSACKNLEKDKKVIVPLAEPLSAKDTNLRASFVPPKTVTPGIFSCSNKFFLNPDGWSYDLFLEIPESIFTQKDYLNGRYFRKRAFYLTCIAKHLLENLGNEVKLEFVAFNDDIRRPILAILPESKGFAATGKRFTVFLIPTVRQIFPVSKLLPHKNAIRDFMEHEELKPTPFYNNSVLEEQNLLFYRDLVKKYSVNPQFLDACGLGSTWLNMRGFSSSIHSNGFGLLEWYVLMALLMSSTGLPAGNVLNTYLTAAQFFKSMLQFLSSKNLTSTLFKLNADSSNLKIGNGHLPTLIDCNTGFNLLGKMKQSFFEYFQASCRHTLNLLDENANYNFSKIFITHVNVPALEFDVSGCIPLEPKELEDPNFCRKTDLDSPYSLYLEYTWDLLQHALGDRVCQIILYSSICTSCSINESLKTKLPKLISFGLLLNPDALLRLVDIGPSPDDTVGSQKFREFWGEVSELRKFKNGSIAESVYWECSSPDERIRIPQRIIRHILNRHLGNNVGDRVSFRNEKFRVYVHSKISPNTDTYNEYVPVMEAYNEAVKSLINLSDIPLSIAEILPADESLRYSSSSVPFYESSTCAPIDVVFQFESSSKWPDELEGIQRTKIAFLLKIAELLEALDNVERASVGLENTDNPTHNCCFLQVLFSNNFTFRYRLRNDREIFFWKSLERNPSTKLSAQKGLYAYEHMFQFIPRHTLAIQAICQAHRSYSMAVRLAKHWFYSHLLTDHVTDEVIELLVASVYINSSSWRTTSSGETSFCRMLHFLAHWDWRFDPLIINSNGKLPHDVRHQATEKLESIRKQDVAIAHNAYYIITDYDFDGNHIGYYKPSKIIANRITSLARASLSELLKDTPNYKSIFKSSLDIYHVVIDVNINKLPMYRESNLTKYKNLQNMSSERPGFEPITEFVKELHRCFEDTISFFYNKKNPKVVTGVFNPRILANRPYRTNIDYPFKVVDKDTVVLDADVVCEEIRQVGGDLIRSIQLQLKA
Protein: anthranilate synthase (EC 4.1.3.27) (G3XCK6)
Organism: Pseudomonas aeruginosa
Interaction partners:
Sequence:
MNALPTSLLQRLLERPAPFALLYRPESNGPGLLDVIRGEALELHGLADLPLDEPGPGLPRHDLLALIPYRQIAERGFEALDDGTPLLALKVLEQELLPLEQALALLPNQALELSEEGFDLDDEAYAEVVGRVIADEIGRGEGANFVIKRRFQARIDGYATASALSFFRQLLLREKGAYWTFIVHTGERTLVGASPERHISVRDGLAVMNPISGTYRYPPAGPNLAEVMEFLDNRKEADELYMVVDEELKMMARICEDGGRVLGPYLKEMAHLAHTEYFIEGQTSRDVREVLRETLFAPTVTGSPLESACRVIRRYEPQGRGYYSGVAALIGGDGQGGRTLDSAILIRTAEIEGDGRLRIGVGSTIVRHSDPLGEAAESRAKASGLIAALKSQAPQRLGSHPHVVAALASRNAPIADFWLRGASERQQLQADLSGREVLIVDAEDTFTSMIAKQLKSLGLTVTVRGFQEPYSFDGYDLVIMGPGPGNPTEIGQPKIGHLHLAIRSLLSERRPFLAVCLSHQVLSLCLGLDLQRRQEPNQGVQKQIDLFGAAERVGFYNTFAARALQDRIEIPEVGPIEISRDRETGEVHALRGPRFASMQFHPESVLTREGPRIIADLLRHALVERRP
Protein: 5', 3'-nucleotidase, cytosolic (J3KRC4)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MARSVRVLVDMDGVLADFEAGLLRGFRRRFPEEPHVPLEQRRGFLAREQYRALRPDLADKVASVYEAPGFFLDLEPIPGALDAVREMNDLPDTQVFICTSPLLKYHHCVGEKYRWVEQHLGPQFVERIILTRDKTVVLGDLLIDDKDTVRGGDPKLGAHLVHLLPQSAPGPAPDKETAALLE