wanglab/gogpt-training-data huggingface dataset:
Protein: cAMP-dependent protein kinase regulatory subunit (EC 2.7.11.11) (Q7KQK0)
Organism: Plasmodium falciparum (isolate 3D7)
Interaction partners:
- cAMP-dependent protein kinase catalytic subunit
- Protein phosphatase PPM5, putative
- Aquaglyceroporin
- Glutamine synthetase, putative
- glutamate synthase
- NADPH:adrenodoxin oxidoreductase, mitochondrial
- DNA-directed RNA polymerases I, II, and III subunit RPABC2, putative
- Ribosomal protein L16, mitochondrial, putative
- cGMP-dependent protein kinase
- RAC-beta serine/threonine protein kinase
Sequence:
MGNVCTWRQGKEKAGDDNSQVIKDKELQNEFKTFEQKMRSNKKNAHEGDMNNDGEDDRYKFSRGFSLSKKPSKTKIPITKTDSEILDGLDYSEMSKQVLMTLNKKNILNDDGSSDGNDTDVHSMFDRKEIERKVLDLESIHFIQKKRLSVSAEAYGDWNKKIDNFIPKVYKKDEKEKAKIREALNESFLFNHLNKKEFEIIVNAFFDKNVEKGVNIINEGDYGDLLYVIDQGEVEIYKTKENNKKEVLTVLKSKDVFGELALLYNSKRAATATALTKCHLWALDRESFTYIIKDMVAKKRKMYEDILSHVNILKDMDPYERCKVADCLKSKSYNDGEIIIKEGEEGDTFFILIDGNAVASKDNKVIKTYTKGDYFGELALLKNKPRAATIKAQNFCQVVYLDRKSFKRLLGPIEDILHRNVENYKKVLNELGLDTTCIDEN
Protein: TATA-box-binding protein (TATA sequence-binding protein) (TBP) (TATA-binding factor) (CeTBP) (TATA-box factor) (Transcription initiation factor TFIID TBP subunit) (P32085)
Organism: Caenorhabditis elegans
Function: The TFIID basal transcription factor complex plays a major role in the initiation of RNA polymerase II (Pol II)-dependent transcription (By similarity). TFIID recognizes and binds promoters via its subunit tbp-1, a TATA-box-binding protein, and promotes assembly of the pre-initiation complex (PIC) (By similarity). The TFIID complex consists of tbp-1 and TBP-associated factors (TAFs) (By similarity). General transcription factor that functions at the core of the TFIID complex.
Subcellular location: Nucleus {ECO:0000269|PubMed:11030349}.
Interaction partners:
- Transcription initiation factor TFIID subunit 5
- Transcription initiation factor TFIID subunit 9
- Transcription initiation factor TFIID subunit 12
- Transcription initiation factor TFIID subunit 4
- Transcription initiation factor TFIID subunit 1
- Transcription initiation factor TFIID subunit 13
- Transcription initiation factor IIB
- Transcription initiation factor TFIID subunit 2
- Transcription initiation factor TFIID subunit 10
- Prion-like-
Sequence:
MNLNSPAVSMLGGDTPAHGGPNSVLGGQGPSSILTGHGPNSVMGPNSILGPGSVLNPQSIQPMQSQQMHSLQGSSMQMHSHLANSNLNLNINPASVGPDRNPGSVMHHNLDINPPSVAYQNLTVPMTPLAYSVYDRDALTHQAPASNIAATMVPATPASQLDIPMPALQNIVSTVNLGVQLDLKKIALHARNAEYNPKRFAAVIMRIREPRTTALIFSSGKMVCTGAKSEEASRLAARKYARIVQKLGFQAKFTEFMVQNMVGSCDVRFPIQLEGLCITHSQFSTYEPELFPGLIYRMVKPRVVLLIFVSGKVVITGAKTKRDIDEAFGQIYPILKGFKK
Protein: histone acetyltransferase (EC 2.3.1.48) (Q6DHD0)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- Transformation/transcription domain-associated protein
- DNA methyltransferase 1-associated protein 1.
- Cell division cycle 5-like protein
- Chromatin modification-related protein MEAF6
- YEATS domain-containing protein 4
- Mortality factor 4-like protein 1
- RuvB-like 1
- RuvB-like 2
- Male-specific lethal 1-like 1
- Actin-like 6A
Sequence:
MADHSVEITEGCRLPVLRRNQENEDEWPLAEILSVKDISGRKLYYVHYVDFNKRLDEWVTPDRLDIKKLQFPKKEAKTPMKNGLSGSRPSSPERDVKKSLDLHVQSASAPSRGKTVPTPKRKAESVSLATQVTAATPVPSLPASTEASQAALYTAIRDASFNIKSREEHEPLTSLTTNGTTSIQRHLIPPQPGRKRKNCGGTDEMVKVFQNNSPRCSTVYLLPGEDSQDSSDGIPSAPRMTGSLVSDRSHDDIVTRMKNIGCIELGRHRLKPWYFSPYPQELTSLPIIYLCEFCLKYLKSLKCLQRHLTKCNLRHPPGNEIYRKGTISFFEIDGRKNKAYSQNLCLLAKCFLDHKTLYYDTDPFLFYVMTEYDPKGFHIVGYFSKEKESTEDYNVACILTLPPYQRRGYGKLLIEFSYELSKVEGKTGTPEKPLSDLGLLSYRSYWSQTILEILMDLKSENGERPQITINEISEITSIKKEDVISTLQYLNLINYYKGQYILTLSEDIVEGHECAMQKRHLRIDPKCLHFTPKDWSKRGKW
Protein: Eyegone (Q8MTJ1)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123, ECO:0000256|PROSITE-ProRule:PRU00108, ECO:0000256|RuleBase:RU000682}.
Interaction partners:
Sequence:
MLIEPTLNRDLGSLTVANSGLSAAHWKMEPHPQRITLLAPHASSVAAASVAAAAAAAAAAAAAAAGAGSGAVAGGGGATSTSPTSVQIPPGFGGGGSTGGIPHGAGGPTGSTLNTLMSQHRLLEFSRFGGLRGYDIAQHMLTQQGAVSKLLGSLRPPGLIGGSKPKVATPTVVSKIEQYKRENPTIFAWEIRERLISEGVCTNATAPSVSSINRILRNRAAERVATEFARTAAYGLYPPPPHPYGSFTWHPAGNVPGGQGVPPPPPPSALWSVAAPTLANLPPSAASAVPVSTCGSLSSAHLMAGGAGGTPTNRAISPGSGSHDTLESADENRHIDSDYLDDDDEPKFRRNRTTFSPEQLEELEKEFDKSHYPCVSTRERLSSRTSLSEARVQVWFSNRRAKWRRHQRMNLLKRQRSSPANPLHSQQSNDAPASSPTPSNHSSASTSAPVAPVPPPQQPLPLCGDHSPQGPPPSVLLHPLHGPPGGHHHHHPLHLPTHPAALQLLSHYHQQQQQQQQQQHQQQQQQHHQQQQQLSPSGCNPAANHLSMGGERSAFRSLVSSPSAAAFLGLARQYAVAASLTVAEEQRSRLHYSAGGLGSGGEGTGPNTNTTQSGGSTMTVDNSSSDSDEEINVHDDSDGEIESSAATAAKVARLSSSDAPATLQFLKHDR
Protein: Glutamate decarboxylase 1b (A0A2R8QPB1)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
Sequence:
MASSAPSSSAGDMDPNTANLRQPATSFLQKNNSLDEKSRMVGSFKESAKNQMSCDNNERFTRDETDFSNLFARDLLPAKNGEEPTIQFLLEVVEILTNYVRKTFDRSTKVLDFHHPHQLLEGMEGFNLELSDQPESLEQILVDCRDTLKYGVRTGHPRFFNQLSSGLDIIGLAGEWLTSTANTNMFTYEIAPVFVLMEQLTLKKMREIIGWPNGDGDALFSPGGAISNMYSVMVARYKYFPEVKTKGMSAAPRLVLFTSEHSHYSIKKAGAVLGFGKENVILLKTDERGRVIPADLEAKVIDAKQKGYVPLFVNATAGTTVYGAFDPINDIADICEKYNLWLHVDGAWGGGLLMSRKHRHKLSGIERANSVTWNPHKMMGVPLQCSAILVREKGILQGCNSMCAGYLFQPDKQYDVTYDTGDKAIQCGRHVDIFKFWLMWKAKGTIGFEQHIDRCLELSEYLYNKIKNREGYEMVFEGQPQHTNVCFWYIPPSLRGMPNGDERREKLHRVAPKIKAMMMECGTTMVGYQPQGDKVNFFRMVVSNHAVTKSDIDFLIDEIERLGQDL
Protein: GM14349p (Uncharacterized protein, isoform A (EC 2.8.3.-, EC 2.8.3.8)) (Uncharacterized protein, isoform C) (Q9VAC1)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Probable citrate synthase, mitochondrial
- Enolase
- Probable hydroxyacid-oxoacid transhydrogenase, mitochondrial
- Glucose-6-phosphate isomerase
- Acetyl-coenzyme A synthetase
- transketolase
Sequence:
MSKQLARHVGQLNSLLKTAATASSVSAHNNYFTYVRELSHPIAREPPIVKPEEAVACVKSGDTVFAGGAAATPVALLNAMAKHGKSNNLECVTVCHMHTEGPGEYAKPEYKDHFRSNSFFMGANVRKAVADGRGDNVPIFLHEIPNLFYKQIVKPDVSFIHVSPPDNHGYCSLGTSVDCVRAALLNSKLIVAQINPKMPRTFGDAIIHKSHFDLAIEVTDDLPQHGTGKISEVEKKIGKLIAENLVKDGATLQMGIGSIPDAVLAALHNHKDLGIHSEMFANGVVELVRKGCVTNSKKKMHQGRIVGSFLIGDKALYDFVDNNPFIEMYAIDYVNNTSIVKQQPRMTAINSCIEVDLTGQVCSDSIGPRFYSGFGGQVDFIRGAAEGLDGLGVPIIAMPSTTNKGESKIVPTLKEGAGVVTSRAHVHYVVTEHGIASLFGKNVRQRMYELIQIADPKHRETLEKQAFERIKVMPSPN
Protein: ATP-dependent rRNA helicase SPB4 (EC 3.6.4.13) (Suppressor of PAB1 protein 4) (P25808)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: ATP-binding RNA helicase involved in the biogenesis of 60S ribosomal subunits. Binds 90S pre-ribosomal particles and dissociates from pre-60S ribosomal particles after processing of 27SB pre-rRNA. Required for the normal formation of 18S rRNA through the processing of pre-rRNAs at sites A0, A1 and A2, and the normal formation of 25S and 5.8S rRNAs through the processing of pre-rRNAs at sites C1 and C2. Also required for recruitment of NOG2 to pre-ribosomes.
Subcellular location: Nucleus, nucleolus {ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:9769101}.
Interaction partners:
- Ribosome biogenesis protein NSA2
- Nucleolar complex-associated protein 3
- Ribosome biogenesis protein RLP24
- Ribosome biogenesis protein YTM1
- 27S pre-rRNA
- rRNA-processing protein EBP2
- 25S rRNA
- Ribosome biogenesis protein RLP7
- Ribosome biogenesis protein 15
- Proteasome-interacting protein CIC1
Sequence:
MSKSLEWDNLGFSLLPWIRTGLDVMGFETMTPVQASTIPMLAGNKDVVVDSVTGSGKTAAFVIPVLEKVVKEEANTSKFKKAHFHSLIIAPTRELSRQIESVVLSFLEHYPSDLFPIKCQLLVGTNEATVRDDVSNFLRNRPQILIGTPGRVLDFLQMPAVKTSACSMVVMDEADRLLDMSFIKDTEKILRLLPKQRRTGLFSATMRSAGSDIFKTGLRNPVRITVNSKNQAPSSLKLNYCVVNPAEKLQLLVSILNNYKFKKCIVYFPTCVSVSYFYSFIQYLGKRNILVNEVEIFSLHGKLQTSARTKTLTAFTDSLSNSVLFTTDVAARGIDIPDVDLVIQLDPPTNTDMFMHRCGRTGRANRVGKAITFLNEGREEDFIPFMQVKNVELEELDLEVKGITTNFYEDFRNWILEDRDRFDKGVKAYVAFIKYYSNHSATSIFRLQSLDYVGIAKLYGLFRLPRMPEITKYLATEKQEGIFPGNWLVDPPVNMDEYKYKDKKREKERQETLKNISLINDKKKLKSELKKKNLAWSDKTLTKERKLERKEKMSLKRKAIEEELKAEELDENAEEERIKEDWKEIVLQNKRKKVSSKAIQGNFDDL
Protein: Tubulin polyglutamylase TTLL7 (EC 6.3.2.-) (Tubulin--tyrosine ligase-like protein 7) (F7E540)
Organism: Xenopus tropicalis (Western clawed frog) (Silurana tropicalis)
Function: Polyglutamylase which modifies tubulin, generating polyglutamate side chains of variable lengths on the gamma-carboxyl group of specific glutamate residues within the C-terminal tail of tubulin. Mediates both ATP-dependent initiation and elongation steps of the polyglutamylation reaction. Preferentially modifies the beta-tubulin tail over an alpha-tail. Competes with monoglycylase TTLL3 for modification site on beta-tubulin substrate, thereby creating an anticorrelation between glycylation and glutamylation reactions.
Subcellular location: Cell projection, cilium {ECO:0000250|UniProtKB:A4Q9F0}. Cytoplasm, cytoskeleton, cilium basal body {ECO:0000250|UniProtKB:A4Q9F0}. Cell projection, dendrite {ECO:0000250|UniProtKB:A4Q9F0}. Perikaryon {ECO:0000250|UniProtKB:A4Q9F0}. Note=In cells with primary cilia, found in both cilia and basal bodies. In neuronal cells, found in dendrites and perikaryon. {ECO:0000250|UniProtKB:A4Q9F0}.
Interaction partners:
Sequence:
MPSLPNESDHQATCSLSLHSDLPYQPSSSIKRKVRKKKKNGAITANVVGTKYEIVRLVTEEMMFTKARDDDETANLIWNDCAVQHEKIAELRNYQRINHFPGMGEICRKDCLARNMTKMIKCQPHEYNFIPRTWIFPAEYTQFQTYIKELKKKRRQKTFIIKPANGAMGHGISLTRNGEKLQAQDHLIVQEYLEKPFLLESYKFDLRIYILVTSCDPLRIFLYNDGLVRMGTEKYHPPSESNLSQLYMHLTNYSVNKHNENFERDETENRGSKRSIKWFTEFLRANDYDISKFWNDISDLVVKTLIVAEPHVLHAYRMCRPGQHPTSESVCFEVLGFDIILDRKLKPWLLEINRAPSFGTDQKIDHDVKKGVLLNALKLLNIRASDKKKNLAKQKAEAQKRLYGQGSMKRLSPASSDWEKQRHTLERRKEELKERLAQVRKQISREEYENRHLGNYRRIYPPEDKLLLEKYEGLLATAFQTFLAGRAASLQREMNNPLKRMKEEDILDLLEQCELDDEKLSGKPTRPKEPRTLSSMPESTQTLKKLKNYSSHSSSNSTGSSSDTEEEEDEKEGKEKKVSYDLEEHKYKSLERSSRIHWKPPLKAARPFSNSSSPSSAASMRRSVSCPRSITALNTQSPTTDQRPFSSRISSTITRPLSGNRTNSLNRSSSSNRVPQSGTSGSVYPSISESRLDHLTKEQEEELTKQTLYALRDMRIRIPGKGVEEITHSHIDEIMDNWTYHKSKVASYWLIKLDSVKQRKVLDIVRTNIRSVLQRIWKVSDVECLHIYRSFNRVFNRLLWNHGQGLWSCFSNSGTSWETIFCKSTEVVTPQQFQCCQRLVQLCKDCLLAVYKYATDSRVAGMSPDWDDSRYLFPVVPQFTMKSSSSGVNCSSSRLPRSSILFNPRHNHY
Protein: FRAS1-related extracellular matrix protein 1 (Protein QBRICK) (Q684R7)
Organism: Mus musculus (Mouse)
Function: Extracellular matrix protein that plays a role in epidermal differentiation and is required for epidermal adhesion during embryonic development.
Subcellular location: Secreted, extracellular space, extracellular matrix, basement membrane {ECO:0000269|PubMed:15878328}. Note=Localizes at the basement membrane zone of embryonic epidermis and hair follicles. {ECO:0000269|PubMed:15878328}.
Interaction partners:
- FRAS1-related extracellular matrix protein 2
- Extracellular matrix organizing protein FRAS1
- Integrin alpha-8
- Integrin beta-1
Sequence:
MHSPGCTGPKAQWFLLLQLLLLHLDRVSATFISINRGLRVMKGSSAFLSGDHLRVAVPKEKDACRLEVVMNEPVTQRVGKLSPQVFDCHFLPNEVKYVHNGCPILDEDSVKLRLYRFTETDTFMETFLLRVYLVEPDCNIIRMSSNVLEVTEFYGLSQAIDKNLLQFDYDRTASLDCTIRLDPLRTQLPAHGKLVVVNRKSEGPRGDQPHSFFSETELGAGLKCPDGSCALELKQVASLKVSCEEFLLTGFHYQHMQPPSPNIDYIPIQLDLTDRRSKTVYKSESAWLPVYIRVGIPNQVPRAAFMAMFVLEVDQFILTPLTTSVLDCEEDETPKPLLVFNITKAPLQGYVTHLLDHTRPISSFTWKDLSDMQVAYQPPNSSHPERRHYTMELEVYDFFFERSAPITVHISIRTADTNAPRVSWNTGLNLLEGQSRAITWEQFQIVDNDDIGAVQLVTIGGLQHGRLTVREGKGFLFTVTDLQAGVVRYHHDDSDTTKDFVAFRIFDGHHSSHHKFPINILPKDDSPPFLITNVVIELEEGKTILIQGSMLRASDMDSSDDYIFFNITKFPQAGEIMKKPGPRLIGYPVPGFLQRDLFSGIIYYRHFGGEIFEDSFEFVLWDSHEPPNLSVPQVVTIHITPVDDQLPKEAPGISRHLVVKETEVAYITKKHLHFLDMESRDGELIYTVTRPPCFSFSHRHLDAGKLFMVDSIPKLTKNPTAPGLSSFTQGLILISANQHTCSSQFASQHAVNHMKVAYMPPMQDIGPSPRHVQFTVSVSNQHGGALHGICFNITVLPVDNQVPEVFTNTLRVVEGGQCTISTEHILVSDVDTPLDSISLSLKERPLHGGVELDGFPLNPRGTFSWRDLNTLKVWYQHDGSEVLQDEIFLEVTDGTNSAAFVLHIEVFPVNDEPPILKADLIPMMHCSEGGEVTITPEYISATDADSDDLELLFLIAREPQHGVVRKAGLHVDRFSQGDVISGAVTYKHTGGEIGLEPCSDTVVLVVSDGEADPLMNGCCYDGPDSSVPLHKSFPTYQLNITVHPVDNQPPSIIIGRMLTVDEGFSAALTTHHLTVVDWDTAPDDLKFMLASQPQFGYLENALPSAGFEKSNIGIRIASFQWTDMKASHINYVQSRHLRVEPTADQFTVYATDGKHRSLETTFHVIINPTNDEAPDLAVQNITVYEGHMVELDSSIISATDRDIPKDPLLFSIALKPQHGLLVDAAISKDSHQIKQLQHEIHSFSVDLLKNGMKLVYAHDDSESSADNFVIQLSDGKHKILKTISVNITPVNDETPTLSKKAEISMAVGDTRVLSSAVLSATDKDSPREKIHYVFERLPQNGQLQLKIGRDWVPLSTGMQCTQEDVDLNLLRYTHAGKTDSQDGDSFTFYLWDEDNRSPAFDCHIIIEDMGKGDIVIHAKPLVVVKGDRGLLTTATLLAVDGADKPEELLYLITSPPRHGQVEYVHSPGVPIASFSQMDIAGQTVCYIHKSRTAVPTDSFRFTISNGLQTQRGVFEITLQTVDSALPVLTKNKRLRLAEGAMGLLSADHLQLTDPDTPPENLTFFLAQLPRHGYLFLRGKALQHNFTQRDVDSGGVAYQHSGGGAREDYFTFLATDRKNQGFVVDGKVQKEPVRFTIQVDQLDKAAPRITHLHSPTQVGLLKNGCYGIYITSRVLKASDPDTEDDQIIFKILRGPLYGRLENTTTGEFIHERFSQKDLSHKTILYIINPSLQVTSDILEFQAMDPTGNTATPQSLDLRWSYIEWAQTAYEVCENVGLLPLEVTRRGYPMDSAFVGVEVNQVSATVGKDFTVTPSKLLQFDPGMSTKMWNIAITYDGLEEDDEVFEVILNSPVNAVLGTQTKAAVKILDSKGGRCHPSNSFNQSKHSTWGKGPWHPLPSGSSSLTTSGSPLLERPPPSFTSGDALQGFGLTDLTQRKTMTQGNGKSVLPSSVCRNGTDTIYNYHGIVSLKLEGDRFSAHKRKAKISIVSQPQRTIKVAELPLADKVESTTDLHFLRQGLRPLFPKNCSVDLKGLFHFEESTHRLYQCDGISWKAWSPQTKGLEDRSCPGGWLLHSGYCHILVTRQKGTWTTATRACREQHQGDLVTVLSRRHMQWLWAMSGRKPFWIGLKNQPRTGHWEWIGGEPVAFTNWRRGAPLHPKPGKNCALVQKRGQWQTKNCSKGKAHNFVCSRKL
Protein: Cleavage and polyadenylation specificity factor subunit 2 (Cleavage and polyadenylation specificity factor 100 kDa subunit) (Q387M8)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123, ECO:0000256|RuleBase:RU365006}.
Interaction partners:
- Nucleic acid binding protein, putative
- Cleavage and polyadenylation specificity factor 30 kDa subunit
- Uncharacterized protein
- C3H1-type domain-containing protein
- Cleavage and polyadenylation specificity factor-like protein, putative
- Cleavage and polyadenylation specificity factor subunit, putative
- Cleavage stimulation factor 50 kDa subunit
- Uncharacterized protein
- Uncharacterized protein
- RNA-binding protein, putative
Sequence:
MLRASAGSIKLTNIYGAPSGDAYHPSIPMAYLLEIDGVRILMDCGWNDGFETSYLDALLPYLGDLHAVLFSTPELSSCGALPFVMEHITAETHVAAAGATAKMGLHGLLHPFLYLFPNTNTWKLQSGVEFEMTVDKIYSAFRSVREPYGGKVTIRHRDVEVECFPVFSGRMLGGCGWLIKYQIDELFYCPDFSLKPSYALNRFAPPTTATLLFIDGSPFHLLGNSGKKYEEQLNVFIREVLSTLRNGKDVLVPVSVPGRGLEVLTIIMHLLTEKGGDNYSIVLASVQAAEVIGKASTMTESLKDEVILSEHQLFANVITCKTAQEVMSVAGPKVCLADGETLDYGVAADLLEYFLQGSDEDREHLIVFPWTPKRDTTAFSVAAAAKGDAIKVQYTRRIPLSKEELEEYYLRLELELEEQRRALDGGAYEVAPLEDIASDSGDDGDEKQNGDAAQGSGGGAQKVQQCTPGLVLPSYMSFVSKHLQFPILETVGSLSSAVLKKMDCSYGLPIGDEMQALMRRKAPARIYSDEGPDNVQLHNDAQVEANIPSKTMVVDAVRIKNVRVFITDLSGFADAGTIRSLLKSRFTFAKKIVMIRGTTDDHHSMTQFCRSEKVMKCGENVFVPRPLGTHLELATHVYSYVVQLDPQLANALPSALRRVKETRSNGFWDVGWVEGSLVRAVVYKEKDEEKEEDDHEELHPSQRRRTEGGTSTEMRDSVYTLTALSSDKAQQCAREREMRGLQRGLYYLGETDLHKLRDAARNEQGIRGEFHKSAPMLIFDNGVCLRKSVSGNVSLSSMVSPSVFGLRKTVYKHFSQVL
Protein: Guanylate cyclase domain-containing protein (H2L2G5)
Organism: Caenorhabditis elegans
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004370}.
Interaction partners:
Sequence:
MCTPYDVVTLLNDLYLRFDRLVGLHDAYKVETIGDAYMIVGGVPERCENHAERVLNISIGMLMESKLVLSPITHKPIKIRLGVHCGPVVAGVVGIKMPRYCLFGDTVNVANKMESNGIQCKIHVSETGKLNGLKANPSYVFIDRGNTEIRGKGMMYTYFLERNDRKSVWELCSRPRSGEQTIDGYMELHDQSIYQEEGGQQENLTVENGNSAQNNHNNNNNTHHSGRKLMNGSSVDPGSHHIRSPTCTIS
Protein: HVA22-like protein c (AtHVA22c) (Q9S784)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
Sequence:
MPSNSGDDNVLQVLIKNFDVLALPLVTLVYPLYASVKAIETRSLPEDEQWLTYWVLYALISLFELTFSKPLEWFPIWPYMKLFGICWLVLPQFNGAEHIYKHFIRPFYRDPQRATTKIWYVPHKKFNFFPKRDDDDILTAAEKYMEQHGTEAFERMIVKKDSYERGRSSRGINNHMIFDDDYRY
Protein: Zinc finger protein 629 (Zinc finger protein 65) (Q9UEG4)
Organism: Homo sapiens (Human)
Function: May be involved in transcriptional regulation.
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
- Transcription intermediary factor 1-beta
- Zinc finger-containing ubiquitin peptidase 1
- Ubiquitin carboxyl-terminal hydrolase 5
- Polyubiquitin-C
- Ubiquitin thioesterase OTU1
- Ubiquitin carboxyl-terminal hydrolase 44
- OTU domain-containing protein 7A
- Histone-lysine N-methyltransferase SETDB1
Sequence:
MEPETALWGPDLQGPEQSPNDAHRGAESENEEESPRQESSGEEIIMGDPAQSPESKDSTEMSLERSSQDPSVPQNPPTPLGHSNPLDHQIPLDPPAPEVVPTPSDWTKACEASWQWGALTTWNSPPVVPANEPSLRELVQGRPAGAEKPYICNECGKSFSQWSKLLRHQRIHTGERPNTCSECGKSFTQSSHLVQHQRTHTGEKPYKCPDCGKCFSWSSNLVQHQRTHTGEKPYKCTECEKAFTQSTNLIKHQRSHTGEKPYKCGECRRAFYRSSDLIQHQATHTGEKPYKCPECGKRFGQNHNLLKHQKIHAGEKPYRCTECGKSFIQSSELTQHQRTHTGEKPYECLECGKSFGHSSTLIKHQRTHLREDPFKCPVCGKTFTLSATLLRHQRTHTGERPYKCPECGKSFSVSSNLINHQRIHRGERPYICADCGKSFIMSSTLIRHQRIHTGEKPYKCSDCGKSFIRSSHLIQHRRTHTGEKPYKCPECGKSFSQSSNLITHVRTHMDENLFVCSDCGKAFLEAHELEQHRVIHERGKTPARRAQGDSLLGLGDPSLLTPPPGAKPHKCLVCGKGFNDEGIFMQHQRIHIGENPYKNADGLIAHAAPKPPQLRSPRLPFRGNSYPGAAEGRAEAPGQPLKPPEGQEGFSQRRGLLSSKTYICSHCGESFLDRSVLLQHQLTHGNEKPFLFPDYRIGLGEGAGPSPFLSGKPFKCPECKQSFGLSSELLLHQKVHAGGKSSQKSPELGKSSSVLLEHLRSPLGARPYRCSDCRASFLDRVALTRHQETHTQEKPPNPEDPPPEAVTLSTDQEGEGETPTPTESSSHGEGQNPKTLVEEKPYLCPECGAGFTEVAALLLHRSCHPGVSL
Protein: Inorganic pyrophosphatase (EC 3.6.1.1) (Pyrophosphate phospho-hydrolase) (PPase) (Q9HWZ6)
Organism: Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Function: Catalyzes the hydrolysis of inorganic pyrophosphate (PPi) forming two phosphate ions.
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00209}.
Interaction partners:
- ATP synthase subunit b
- ATP synthase subunit delta
- Polyphosphate kinase
- ATP synthase subunit alpha
- ATP synthase subunit c
- ATP synthase gamma chain
- GDP-polyphosphate phosphotransferase
- ATP synthase subunit beta
- ATP synthase subunit a
- Elongation factor P
Sequence:
MSYSKIPAGKDLPNDIYVAIEIPANHAPIKYEIDKDTDCLFVDRFMATPMFYPANYGFIPNTLADDGDPLDVLVVTPYPVAPGSVIRARPVGVLHMTDEAGGDAKLIAVPHDKLSVLYKDVKEYTDLPALLLEQIKHFFENYKDLEKGKWVKVEGWGNADAARAEITKAVAAFQK
Protein: Collagen alpha-1(IX) chain (Q05722)
Organism: Mus musculus (Mouse)
Function: Structural component of hyaline cartilage and vitreous of the eye.
Subcellular location: Secreted, extracellular space, extracellular matrix {ECO:0000250}.
Interaction partners:
- Collagen, type IX, alpha 3
- Collagen alpha-2
- CD44 antigen
- Platelet glycoprotein VI
- Collagen alpha-1
- Integrin alpha-2
- Integrin alpha-3
- Matrilin-3
- Collagen alpha-2
- Collagen alpha-1
Sequence:
MKNFWKISVFFCVCSCLGPWVSATLKRRARFPANSISNGGSELCPKIRIGQDDLPGFDLISQFQIEKAASRRTIQRVVGSTALQVAYKLGSNVDFRIPTRHLYPSGLPEEYSFLTTFRMTGSTLEKHWNIWQIQDSAGREQVGVKINGQTKSVAFSYKGLDGSLQTAAFLNLPSLFDSRWHKLMIGVERTSATLFIDCIRIESLPIKPRGQIDADGFAVLGKLVDNPQVSVPFELQWMLIHCDPLRPRRETCHELPIRITTSQTTDERGPPGEQGPPGPPGPPGVPGIDGIDGDRGPKGPPGPPGPPGDPGKPGAPGKPGTPGADGLTGPDGSPGSVGPRGQKGEPGVPGSRGFPGRGIPGPPGPPGTTGLPGELGRVGPIGDPGKRGPPGPPGPPGPSGTIGFHDGDPLCPNSCPPGRSGYPGLPGMRGHKGAKGEIGEPGRQGHKGEEGDQGELGEVGAQGPPGPQGLRGITGIVGDKGEKGARGFDGEPGPQGIPGAAGDQGQRGPPGETGPKGDRGIQGSRGIPGSPGPKGDTGLPGVDGRDGIPGMPGTKGEAGKPGPPGDVGLQGLPGVPGIPGAKGVAGEKGNTGAPGKPGQLGSSGKPGQQGPPGEVGPRGPRGLPGSRGPVGPEGSPGIPGKLGSVGSPGLPGLPGPPGLPGMKGDRGVFGEPGPKGEQGASGEEGEAGARGDLGDMGQPGPKGSVGNPGEPGLRGPEGIRGLPGVEGPRGPPGPRGMQGEQGATGLPGIQGPPGRAPTDQHIKQVCMRVVQEHFVEMAASLKRPDTGASGLPGRPGPPGPPGPPGENGFPGQMGIRGLPGIKGPPGALGLRGPKGDLGEKGERGPPGRGPKGLPGAIGLPGDPGPASYGKNGRDGEQGPPGVAGIPGVPGPPGPPGPPGFCEPASCTLQSGQRAFSKGPDK
Protein: Forkhead box A2 (B0ZTD4)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123, ECO:0000256|PROSITE-ProRule:PRU00089}.
Interaction partners:
Sequence:
MHSASSMLGAVKMEGHEPSDWSSYYAEPEGYSSVSNMNAGLGMNGMNTYMSMSAAAMGSGSGNMSAGSMNMSSYVGAGMSPSLAGMSPGAGAMAGMGGSAGAAGVAGMGPHLSPSLSPLGGQAAGAMGGLAPYANMNSMSPMYGQAGLSRARDPKTYRRSYTHAKPPYSYISLITMAIQQSPNKMLTLSEIYQWIMDLFPFYRQNQQRWQNSIRHSLSFNDCFLKVPRSPDKPGKGSFWTLHPDSGNMFENGCYLRRQKRFKCEKQLALKEAAGAAGSGKKAAAGAQASQAQLGEAAGPASETPAGTESPHSSASPCQEHKRGGLGELKGTPAAALSPPEPAPSPGQQQQAAAHLLGPPHHPGLPPEAHLKPEHHYAFNHPFSINNLMSSEQQHHHSHHHHQPHKMDLKAYEQVMHYPGYGSPMPGSLAMGPVTNKTGLDASPLAADTSYYQGVYSRPIMNSS
Protein: 1-phosphatidylinositol 4-kinase (EC 2.7.1.67) (A0A1D8PTE0)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Interaction partners:
- 1-phosphatidylinositol-4-phosphate 5-kinase
- Phosphatidylinositol-3-phosphatase
- Protein EFR3
- Phosphatidylinositol 4-kinase
- Phosphatidylinositol 4-kinase PIK1a
- CDP-diacylglycerol--inositol 3-phosphatidyltransferase
- 1-phosphatidylinositol-3-phosphate 5-kinase
- phosphoinositide 5-phosphatase
- Phosphoinositide phospholipase C
- Phosphatidylinositol 3-kinase VPS34
Sequence:
MDYSGITRGSIRAEALKKLAELTVQNPSSNLKEVNTGIQKDDFSKLLSATPKLLNSRGKLNGSVSNGGGAGGSSGVRDRLSEVAIAKKEYEVIIALSDATKEPMKVDSQIQALINKFKAYLFELPDQKFAYSIVSNSATISPWNLLGEKLTTGLINLAMQNTKQYLDEVVDIFQEFIEKFFDNMNLHLTHFLTLAGVLDGFNQNAKFLSISSRTYKIFIALDSNIDDADFLNDVENYTDYLYDEPNEFQDLLTRDFVINFSPILYLESLSRLMCAIVNGIIDNKDQSLLHYILEKVANKYDQVDDKSNSAVFAKDNLDFSRAHMDIINNLTGLALRKLEFLDRGETYIVYSTYDRLKLGYLAKSHNLQILSCGMFTDNLDLKTSRKLFKSSIEIRDVMLDPDLGLTVFEFGSLLVYKDESIGPSLTRAFTSVIANPKLDPHYCLKASKAVGLGTKKLPQDTVVTTIYSLTNLLFVTNEGLLLPSKSTKRFNTGLSGGDNLLGREAFASPMSSRRTSFTSFSQAFSKGANSSEFDENDYRKVCENAVTGIIEVCEKCNDESVPALTCTILSQKVSKIDSPIGPLILKGLSSCAPFLPEREFVILIRLLNKISFDALEKKNMVLMGYLTESKMLLAEKLKVSNPLFTVYLHELLQTINSKGDVQQLEHHRSHNEISEVGDQIAIYLKPLAALLPDVHLGEKPLEIKSTVTINLFRNIWFNMVVHGYNINSKNTKTFRNELERIAYNSPPLASELSWDRTETSIELNTVLRRGSSNHNIKDHRHYLGNIFEVHRSLSYPKLMFLSAAVFVESLRVRNGNCSDSLLYFTDPTFKISGVDKYLGHISFKIVKDFIQLINTGANKQFSADHIAEQLTTMLIYCCYPVPEMQDAAMQCCDLLISRVPSSLCHKKSLFAVFDLLTLLFDSIADADVHEYEPTTVFRARCTGIKVSMSDDYHWRTSTFNRFHDKCKHWLKILLHKCNIDVKSLIQSYISANESLQFDSPVQFGLSFALEMAGAISSNDREWSAITYANSSNLNALPTIVSQLSWRSSFVTEIMNKLPLRTDEETDFAFQAIREKVYYIKARLVPGDNGGFDYPTNDEIMKLLSEIAGLTLLSDVNNAELIRYLVEIPFTMFVPSIMITASGVWFAVMKDKPQLSVLLLSEIAKKWEESIQLRKGVFSQEFDLVHPEFEKMEYAPSNRVLVNKEADNAQKNFAPHLEIIRLFASNFEATLNQSDHLLKIFTRFVEVGLENLKIASYHPLSRLVRFELVKFSFELLQYHIKLGSRSSKYLSELILDGALTWFRQRSTYPFGGNKLKFKSELILLKEVAKFVTGLNNFQSELIDMKAKILLYFMDDEICKFTVWLHSMNPSDTSGTYVNQQIGGQHLKFAYEIDPILAVNLAMRYKLKSLDELLQQLIIKDPLPAISYPDAVQFFIGINAGTHMPSYHLLFWAPLAPIDSITLFLPPFGSNSYILQYTMRSLESHDVNLTFFYVPQIVQSLRFDYKGYVERFIVETAKVSQLFAHQIIWNMLANSYKDEDSQEPDDLKPTLDRIQQTMLKSFSAHDLKFYEKEFGFFNEVTSISGKLKPYIKKSKAEKKEKIDEEMALIKVEPGVYLPSNPDGVVIDINRKSGRPLQSHAKAPFMATFKIKKELVDYDEQGHKQSFEIEKWQSAIFKVGDDCRQDVLALQLISMFRTIWSNAGLDLYVFPYRVTATAPGCGVIDVLPNSTSRDMLGREAVNGLYEYFITKFGPENSIEFQNARNNLIKSLAAYSIISYLLQFKDRHNGNIMYDEQGHILHIDFGFCFDIVPGGVRFEAAPFKLTHEMIMVLGGNDQTQSFKWFEELCVKGYLSCRPYMEFIVRSIIPMLESGLPCFKENTIKNLRQRFVPTKSEKEAALYFRKLIKKSMESFYTKGYDEFQRLTNGIPY
Protein: Thioredoxin reductase 2, mitochondrial (EC 1.8.1.9) (Thioredoxin reductase TR3) (Q9JLT4)
Organism: Mus musculus (Mouse)
Function: Involved in the control of reactive oxygen species levels and the regulation of mitochondrial redox homeostasis (By similarity). Maintains thioredoxin in a reduced state. May play a role in redox-regulated cell signaling (By similarity).
Subcellular location: Mitochondrion {ECO:0000269|PubMed:10721726}.
Interaction partners:
- Thioredoxin, mitochondrial
- Selenide, water dikinase 2
- Selenocysteine lyase
- Selenide, water dikinase 1
- Cystathionine gamma-lyase
- Kynurenine--oxoglutarate transaminase 3
- Kynurenine--oxoglutarate transaminase 1
- Thioredoxin reductase 3
- Thioredoxin reductase 1, cytoplasmic
- Thioredoxin
Sequence:
MVAAMVAALRGPSRRFRPRTRALTRGTRGAASAAGGQQSFDLLVIGGGSGGLACAKEAAQLGKKVAVADYVEPSPRGTKWGLGGTCVNVGCIPKKLMHQAALLGGMIRDAHHYGWEVAQPVQHNWKTMAEAVQNHVKSLNWGHRVQLQDRKVKYFNIKASFVDEHTVRGVDKGGKATLLSAEHIVIATGGRPRYPTQVKGALEYGITSDDIFWLKESPGKTLVVGASYVALECAGFLTGIGLDTTVMMRSIPLRGFDQQMSSLVTEHMESHGTQFLKGCVPSHIKKLPTNQLQVTWEDHASGKEDTGTFDTVLWAIGRVPETRTLNLEKAGISTNPKNQKIIVDAQEATSVPHIYAIGDVAEGRPELTPTAIKAGKLLAQRLFGKSSTLMDYSNVPTTVFTPLEYGCVGLSEEEAVALHGQEHVEVYHAYYKPLEFTVADRDASQCYIKMVCMREPPQLVLGLHFLGPNAGEVTQGFALGIKCGASYAQVMQTVGIHPTCSEEVVKLHISKRSGLEPTVTGCUG
Protein: NAD(P)H dehydrogenase subunit H (C5MRJ4)
Organism: Oryza sativa subsp. indica (Rice)
Interaction partners:
Sequence:
FCDYFLRGVIEYQQLITQNPIFLERVEGVGFISGEEAVNWGLSGPMLRASGIQWDLRKVDLYESYNQFDWKVQWQKEGDSLARYLVRIGEMRESIKIIQQAVEKIPGGPYENLEVRRFKKAKNSEWNDFEYRFLGKKPSPNFELSKQELYARVEAPKGELGIYLVGDDSLFPWRWKIRPPGFINLQILPQLVKKMKLADIMTILGSIDIIMGEVDR