wanglab/gogpt-training-data huggingface dataset:
Protein: Protein dispatched homolog 1 (Mdispa) (Q3TDN0)
Organism: Mus musculus (Mouse)
Function: Functions in hedgehog (Hh) signaling. Regulates the release and extracellular accumulation of cholesterol-modified hedgehog proteins and is hence required for effective production of the Hh signal. Synergizes with SCUBE2 to cause an increase in SHH secretion.
Subcellular location: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
- Sonic hedgehog protein
- Desert hedgehog protein
- Indian hedgehog protein
Sequence:
MAVISGSDSVLLSNGSISTSTSNPSPLSPSDGDLPAQHLGPRETPRTKASPNGCLQLNGTVKSSFLPLDNQRTPQTPTQCCHPCPYHHPVSSHSNHQECHPEAGLAASPALASCRMQPHSEYSASLCPNHSPVYQAAHCLQPSPSFCLHHPWPDHFQHQPVRQHLTIIRPSRPFKFPRSYAALLADWPVVVLGMCTLLIVVCALVGVLVPELPDFSDPLLGFEPRGTTIGQRLVTWNNMMRNTGYKATLANYPYKYAEEQARSHRDDRWSDDHHERERREVDWNFQKDSFFCDVPSDGYSRVVFASAGGETLWNLPAIKSMCDVDNSRIRSHPQFSDLCQRTTAVSCCPSWTLGNYIAILNNRSSCQKIVERDVSHTLKLLRTCAKHYQNGTLGPDCWDKAARRKDQLKCTNVPRKCTKYNAVYQILHYLVDKDFMTPKTADYAVPALKYSMLFSPTEKGESMMNIYLDNFENWNSSDGITTVTGIEFGIKHSLFQDYLLMDTVYPAIAIAIVLLIMCVYTKSMFITLMTMFAIISSLIVSYFLYRVVFNFEFFPFMNLTALIILVGIGADDAFVLCDVWNYTKFDKPRAETSEAVSVTLQHAALSMFVTSFTTAAAFYANYVSNITAIRCFGVYAGTAILVNYVLMVTWLPAVIVLHERYLLNIFTCFRKPQPQAYDKSCWAVLCQKCRRVLFAVSEASRIFFEKVLPCIVIKFRYLWLIWFLALTVGGAYIVCVNPKMKLPSLELSEFQVFRSSHPFERYDAEFKKLFMFERVHHGEELHMPITVIWGVSPEDSGDPLNPKSKGELTLDSTFNIASPASQAWILHFCQKLRNQTFFHQTEQQDFTSCFIETFKQWMENQDCDEPALYPCCSHCSFPYKQEVFELCIKKAIMELDRSTGYHLNNKTPGPRFDINDTIRAVVLEFQSTFLFTLAYEKMQQFYKEVDSWISHELSSAPEGLSRGWFVSNLEFYDLQDSLSDGTLIAMGLSVAVAFSVMLLTTWNIIISLYAIVSIAGTIFVTVGSLVLLGWELNVLESVTISVAVGLSVDFAVHYGVAYRLAPDPDREGKVIFSLSRMGSAIAMAALTTFVAGAMMMPSTVLAYTQLGTFMMLVMCVSWAFATFFFQCLCRCLGPQGTCGQIPFPTKLQCSPFSHTLSARPGDRGPSKTHAASAYSVDARGQKSQLEHEFYELQPLASHSCTSSEKTTYEEPHTCSEFFNGQAKNLRMPVPAAYSSELTKSPSSEPGSALLQSCLEQDTVCHFSLNPRCNCRDAYTHLQYGLPEIHCQQMGDSLCHKCASTAGGFVQIQSSVAPLKASHQAAEGLLHPAQHMLPPGMQNSRPRNFFLHSVQHFQAQENLGRTSTHSTDERLPRTAELSPPPSDSRSTESFQRACCHPENNQRRLCKSRDPGDTEGSGGTKSKVSGLPNQTDKEEKQVEPSLLQTDETVNSEHLNHNESNFTFSHLPGEAGCRSCPNSPQSCRSIMRSKCGTEDCQTPNLEANVPAVPTHSDLSGESLLIKTL
Protein: Rhamnogalacturonan I rhamnosyltransferase 4 (EC 2.4.1.351) (O-fucosyltransferase 18) (O-FucT-18) (O-fucosyltransferase family protein) (Q6E279)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Glycosyltransferase involved in the formation of rhamnogalacturonan I (RG-I) oligosaccharides in the seed coat mucilage, which is a specialized cell wall with abundant RG-I (By similarity). Transfers the rhamnose residue from UDP-beta-L-rhamnose to RG-I oligosaccharides.
Subcellular location: Golgi apparatus membrane {ECO:0000250|UniProtKB:Q4V398}; Single-pass type II membrane protein {ECO:0000255}.
Interaction partners:
- Glucuronoxylan 4-O-methyltransferase-like protein
- AT3g56750/T8M16_80
- At1g61240
- At3g26950
- At4g12700
- At1g71690)
- O-fucosyltransferase 36
- O-fucosyltransferase 23
- Probable xyloglucan galactosyltransferase GT11
- Galactan beta-1,4-galactosyltransferase GALS1
Sequence:
MSVVVGDRSESTLMRSDYKAPPSQAIPKARLQVWFFRVCSCILVWTCLIQLFWHSQIFTGLTNHISRFSLPVQSVPLPPPLPPRNYTSNGILLVSCNGGLNQMRAAICDMVTVARLLNLTLVVPELDKKSFWADTSDFEDIFDIKHFIDSLRDEVRIIRRLPKRYSKKYGFKLFEMPPVSWSNDKYYLQQVLPRFSKRKVIHFVRSDTRLANNGLSLDLQRLRCRVNFQGLRFTPRIEALGSKLVRILQQRGSFVALHLRYEMDMLAFSGCTHGCTDEEAEELKKMRYAYPWWREKEIVSEERRVQGLCPLTPEEAVLVLKALGFQKDTQIYIAAGEIFGGAKRLALLKESFPRIVKKEMLLDPTELQQFQNHSSQMAALDFIVSVASNTFIPTYYGNMAKVVEGHRRYLGFKKTILLDRKRLVELLDLHNNKTLSWDQFAVAVKDAHQGRRMGEPTHRKVISVRPKEEDYFYANPQECIS
Protein: Protein ATP1B4 (X,K-ATPase subunit beta-m) (X/potassium-transporting ATPase subunit beta-m) (Q9UN42)
Organism: Homo sapiens (Human)
Function: May act as a transcriptional coregulator during muscle development through its interaction with SNW1. Has lost its ancestral function as a Na,K-ATPase beta-subunit.
Subcellular location: Nucleus inner membrane {ECO:0000250}; Single-pass type II membrane protein {ECO:0000250}. Note=Detected in nuclear envelops. {ECO:0000269|PubMed:14656723, ECO:0000269|PubMed:17592128}.
Interaction partners:
- Sodium/potassium-transporting ATPase subunit alpha-4
- Sodium/potassium-transporting ATPase subunit alpha-3
- Sodium/potassium-transporting ATPase subunit gamma
- Sodium/potassium-transporting ATPase subunit alpha-2
- Sodium/potassium-transporting ATPase subunit alpha-1
- SNW domain-containing protein 1
- Sodium/potassium-transporting ATPase subunit beta-1
- Sodium/potassium-transporting ATPase subunit beta-3
- cGMP-dependent protein kinase 1
- Sodium/potassium-transporting ATPase subunit beta-2
Sequence:
MRRQLRSRRAPSFPYSYRYRLDDPDEANQNYLADEEEEAEEEARVTVVPKSEEEEEEEEKEEEEEEEKEEEEGQGQPTGNAWWQKLQIMSEYLWDPERRMFLARTGQSWSLILLIYFFFYASLAAVITLCMYTLFLTISPYIPTFTERVKPPGVMIRPFAHSLNFNFNVSEPDTWQHYVISLNGFLQGYNDSLQEEMNVDCPPGQYFIQDGNEDEDKKACQFKRSFLKNCSGLEDPTFGYSTGQPCILLKMNRIVGFRPELGDPVKVSCKVQRGDENDIRSISYYPESASFDLRYYPYYGKLTHVNYTSPLVAMHFTDVVKNQAVPVQCQLKGKGVINDVINDRFVGRVIFTLNIET
Protein: RING/FYVE/PHD zinc finger superfamily protein (Q9SN83)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- CHP-rich zinc finger protein-like protein
- D-galactoside/L-rhamnose binding SUEL lectin protein
- Adrenodoxin-like protein 1, mitochondrial
- B-box zinc finger protein 32
- CAP superfamily protein
Sequence:
MADHLSLCTDRLITSESLDSEKDSDSSGESSYRPQGTDLASSSVNETEVPREYYAVADEEEPLLQSVECRICQEEDSTKNLEAPCACNGSLKYAHRKCVQRWCNEKGDITCEICHQPYQHGYTAPPPPPPDETIIHIGDDWENGVPLDLTDPRILAMAAAERHFLEADYDEYSENNSSGAAFCRSAALILMALLLLRDALNLTTNPDDEDDPTAFFSLFLLRAAGFLLPCYIMAWAIGILQRRRQRQEAAALAAAEVTFMIHGGGPQRRGLHFAVAPQPPISNVPTPV
Protein: adenylate cyclase (EC 4.6.1.1) (ATP pyrophosphate-lyase) (Adenylyl cyclase) (D6XEJ9)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
- Phosphodiesterase
- Phosphodiesterase
- 3', 5'-cyclic nucleotide phosphodiesterase, putative
Sequence:
MVTFMRELYVRDGAFTYLVFSLLLQVLTASSLANDKIQVKVYNMLYSNKISAKIYDPITAGFNASITNGNTPSGANVEVVYVPPMDDSKYADYLGKHMTTHDGKELPVILGPVGDKNTLGLLKYFKEKNVISFSPLTGSSKVRSWNPNLYFLTASPAAEMLALLRYAITQLRLHRLGFMYLKDVSYGDDEYELAVELTTRMDRKLCGVFALKSQIGKESDDSSFSAEWNKFANTRPQGVIVFGSPINDTKKFLMKSLEDERTKGGYLLIPSTLQYVIENKWEKELGRDRFVPDKIIITGTNPLAKDDGYDAIKRFKGDMAKYLKEKKDILSGTGQWNVNLNVDESNFTEQDTEAELMVDGWIAGEVLKQALSCREWLTSRDAFITSLYNQRRYVIDDIVVGDFGGECRGMAGERGASCLCNQGGNVVYMKKMGKDLRLYPMKEGVLALTSSRCYRDLSQLYAPLSGIMFKLTDDPKALRTAEAIYDGAFYVVGKGQLGHSDRFFLHWLSSKSHDTSTALYDEVEKRVVTAVFGVVDDSLLSTKGMAFIDPITLTPQLSNPRRNVIHLSPTLEQQLFVIVEHIIQNGAGKMHAIVRSGDTRGVRKVLQKTLDFFESSLSSFVASGEGSTLRDKLPTAGEVLVAGLISDDIPIILSHLGKHHNVRIFVPFFDVALLYDELVSAFRDKPFADRLLFATNLPHWGDKNTKSDMVREFHRVVRDESKWKPLSLLGYVTARAMINILQRMGHVTPEELVDAIFSQSVITVDDMRYGPFDDKCTNGASFEEKHCAVNYGATHISVWSMSRVLNPSVSPVVTHVTPSMKYGDTEGFRLKRGHIAAIAVSCVVVLALFVTVLVLVSASRRNARDNNNAPKEPTDPVTLIFTDIESSTAQWAAHPEQMPDLVATHHRLIRSLITRYECYEVKTVGDSFMIACKSPFAAAQLACDLQRDFLNHDWKTTELDESYREFERKRAEDDSDYTPPTASLDPEVYRQLWNGLRVRVGIHTGLCDIRHDEVTKGYDYYGRTSNMAARTESVGNGGQVLMTRSTYLSLSGEEREQLNVTPLGDVPLRGVPKPVEMYQLNAVPGRTFAALRLDREFEEEEDNVTGSITSGSGSPERGLTATAQQVAGCIDALLGTFPATQRQKMLATFCERWRVKKPPGMDAWNEASCRCVTRRIAAKVGCVMDFGTRNTSGSVPSFERGGSFFSLGGVAAAIMLSSSSNSFCGEGDCSGVQLIDLDNVSAAS
Protein: Cdc42 effector protein 2 (Binder of Rho GTPases 1) (O14613)
Organism: Homo sapiens (Human)
Function: Probably involved in the organization of the actin cytoskeleton. May act downstream of CDC42 to induce actin filament assembly leading to cell shape changes. Induces pseudopodia formation in fibroblasts in a CDC42-dependent manner.
Subcellular location: Endomembrane system {ECO:0000269|PubMed:11035016}; Peripheral membrane protein {ECO:0000269|PubMed:11035016}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:11035016}.
Interaction partners:
- Cdc42 effector protein 5
- Rho-related GTP-binding protein RhoQ
- Cell division control protein 42 homolog
- Rho GTPase-activating protein 26
- Septin-7
Sequence:
MSTKVPIYLKRGSRKGKKEKLRDLLSSDMISPPLGDFRHTIHIGSGGGSDMFGDISFLQGKFHLLPGTMVEGPEEDGTFDLPFQFTRTATVCGRELPDGPSPLLKNAISLPVIGGPQALTLPTAQAPPKPPRLHLETPQPSPQEGGSVDIWRIPETGSPNSGLTPESGAEEPFLSNASSLLSLHVDLGPSILDDVLQIMDQDLDSMQIPT
Protein: Adenylate cyclase (EC 4.6.1.1) (ATP pyrophosphate-lyase) (Adenylyl cyclase) (P14605)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Plays essential roles in regulation of cellular metabolism by catalyzing the synthesis of a second messenger, cAMP.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16489217}.
Interaction partners:
- Guanine nucleotide-binding protein alpha-2 subunit
- Ras-like protein 1
- cAMP-dependent protein kinase catalytic subunit
- 3',5'-cyclic-nucleotide phosphodiesterase
- Glucose receptor protein git3
- cAMP-dependent protein kinase regulatory subunit
- Adenylyl cyclase-associated protein
- Glucose-insensitive transcription protein 7
- Guanine nucleotide-binding protein subunit beta
- Nucleoside diphosphate kinase
Sequence:
MDQSKRLLKSAVPNPPEHFKTGISWLDDLDEKDDDSATSVNYDIPEITEANLCNDSHEALSPCTQPVGNSGRPVEAFKTYPSTPAVPSKSVLFHFYEPDENFSLSDTGRTKSDTALAARESSEKSEVPRDTRSAGIKPYKENNSSNCAISKEAGLRRLIDKDRESFDKNLNQSFTNLTFPEPISDDSDSVEFQRDSLNNNWPASLEGSIHELPRNSDDDGIPASAAHILDLDYHRDSYDSPWKKFLPYPSILSDDSWKAPESWGTSLPTEAIPKQVFTTRFFARPSLGNRKKEFFLRVYRDDRTSVSFICPIGIQTHEVIKLLARLFFLPSSANFYLLLIQFNTERILLPHEQPCIIFERLLSLFGCKVTSDEEINEEDNYSVARLVFTTMDIGADVLRKFSEKKITANLDISRSNLEVIPVKIYPYAHELISLNVSHNLSLDLPLDFMERCVKLKRLDISNNLRSPRGKPITALRQLEVLNMSRNDIYELDPLIFSGLSRNSLKELNIANNKLFFLPHSTRYLVNLTYLDLSYNNFVTFPLIITELSQLETLNFSHNLLSQISSKIGSLVKLKHLYLQFNDLSNRLPQEIGLLKNLETIDLSYNAITNIASLSECPKLNSINVACNLLSFYEYSNPSATFIDFSFCPLTTIDPAFSYSNLVYFDISHAKLIGLKDSVIETLVNVETVKVNYNHFTSISDAISAMQNLKYLSCTNCEMSYVSPNLGKLKHLVHLDLHANNIKIFPEEVWQVSSLKVVNLSSNILEKIKLPVATSKKLTRTISQLKIMRTLSGNPVSSLSSQEFVMPTVEELYLVDNRLGNDCFTALEYFKCLKVLNLSYNYLTEIPSKFFQNFSDLKHLFVSGNELANLSISSTAQVLLETLYANGNRLSSFPKNEALSKSLRFLDISTNNLQNLAVEKAEKKSLTKLPQLEYLNLSGNTWFRFSEHEDTNFTKSYLKNLKFLSIMDLNTKFSNAPSDVLNHFIQRNSPQPNILRYGVCGYLSRSIPVISACELVVNNFLHPQSSLYCVLDSDISAGKNNRVLKFVYDNLASCLAHEINAADSSSEQICNALRRGFLRLNKKLGNVIHYDLRKSSEGDVDSNYVTTMNISEKGYSMDSSCLDIGVSIILVYVRDTRAFVANVGTSMAIMSTRNDSEPTTLSVMHDVYNRDEIRRIVDSCGFISGEIKSTTTRAIGRLSQFPGVQAVPYVNVQYLSELNEFIILANQEFWSVLSKRTVIDVVRANRHSPLLASTKLRDYAIAYGAEKNVLVVIVELNGLFEENSLNFNQLRGDEKTLAISEKNDNMSFVQDLPDDSSLARMNREVSPPKGCIAMVFTDIKNSTLLWERHPIAMRSAIKTHNTIMRRQLRATGGYEVKTEGDAFMVCFQTVPAALLWCFSVQLQLLSADWPNEIVESVQGRLVLGSKNEVLYRGLSVRIGVNYGVTVSELDPITRRMDYYGPVVNRTSRVVSVADGGQIAVSAEVVSVLNQLDSETMSSEKTNVNEMEVRALKQIGYIIHNLGEFKLKGLDTTEMISLVYPVQLQGRLERLIKSRSLGTPTALPETQTYTPVRSRSNSLRPMLARLSDSKSVHGEEGGSGKRSVSSLRNVSPSESTGGYEGCIFDDQQYQLLYELCERLEDHAAILHGFPEPPPCDTGLAAPVNQAEEYSLFYRLTLRIENTIYCVSQMLGHTG
Protein: Uncharacterized GPI-anchored protein At5g19250 (P59833)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Cell membrane; Lipid-anchor, GPI-anchor.
Interaction partners:
- At1g65720/F1E22_13
- CHCH domain protein
- Translocation protein SEC62
- soluble epoxide hydrolase
- Zinc finger CCCH domain-containing protein 52
- Proline-rich extensin-like family protein
- Protein DA1-related 7
- Bifunctional TENA-E protein
- Expansin-A13
- LIM domain-containing protein PLIM2b
Sequence:
MAISKLHLLFLLSVFLSLHPLVLSDTADEEDVLLTGINSYRASLNLTTLIHNHNAECLADEIADQFKNQPCTNTTGSASVPGTTPGFPNLPNLLSKCRLNPTVTRDGAILPACVPNLDPSLVLTNFTMSQYSKDLNDSKFTGIGIGSDDNWIVVVLTTSTPEGSYSPASNSGAFAFGVNGLVSSSLMFLLFCFFMF
Protein: Cytochrome P450 71D15 (EC 1.14.14.99) ((-)-(4S)-Limonene-3-hydroxylase) (Cytochrome P450 isoform PM2) (Q9XHE6)
Organism: Mentha piperita (Peppermint) (Mentha aquatica x Mentha spicata)
Function: Hydroxylates (-)-(4S)-limonene to (-)-trans-isopiperitenol, a precursor of (-)-menthol, responsible for the cooling sensation of peppermint. Fluorinated substrate analogs are hydroxylated with the same regio- and stereochemistry.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000305}; Single-pass type II membrane protein {ECO:0000305}.
Interaction partners:
Sequence:
MELLQLWSALIILVVTYTISLLINQWRKPKPQGKFPPGPPKLPLIGHLHLLWGKLPQHALASVAKEYGPVAHVQLGEVFSVVLSSREATKEAMKLVDPACANRFESIGTRIMWYDNEDIIFSPYSEHWRQMRKICVSELLSSRNVRSFGFIRQDEVSRLLRHLRSSAGAAVDMTERIETLTCSIICRAAFGSVIRDNAELVGLVKDALSMASGFELADMFPSSKLLNLLCWNKSKLWRMRRRVDTILEAIVDEHKFKKSGEFGGEDIIDVLFRMQKDTQIKVPITTNSIKAFIFDTFSAGTETSSTTTLWVLAELMRNPAVMAKAQAEVRAALKEKTNWDVDDVQELKYMKSVVKETMRMHPPIPLIPRSCREECVVNGYTIPNKARIMINVWSMGRNPLYWEKPDTFWPERFDQVSKDFMGNDFEFVPFGAGRRICPGLNFGLANVEVPLAQLLYHFDWKLAEGMKPSDMDMSEAEGLTGILKNNLLLVPTPYDPSS
Protein: RT03134p (TipE homolog 3) (TipE-like protein 3) (Q9VZG8)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- TipE homolog 1, isoform B
- Protein tipE
- IP20336p
- Sodium channel protein para
Sequence:
MGKKKVPVEDLVVPPQDTRICGTICICQMTLVLSSVALVYLTVAIYMPSTRAFKSGIDPTPVMCTTTRAVNKDNCEWGSCGEWCLSKTSGACIQIYVNLRSNGSNLIFQNCTNSANKTCYGIDQDRADKARCINDECKNLTGTFNCTAGQCLNITDAFECIFHNSDAPVKCSGRRGKINCMDISGLYSCSRGTCRKIRTPYNCDRRCVDIPTRNKNVVVLSGDKVYLSQCQNAINAETLEEVWNESSENVAMTSCYFIRHTSDQVDAVDCINGSTLETNMLSDLTNFTYLSHLHVSVATPVPEIAPPDVDLTISNESKLMINLEGCVNTLMDECKEFLKDFGRDGSDHNARARFPCFYSPGKKDVVVARFDLEVTYRQFVFASVVPSVLFVVSCSILIMCQTTVYVGDDAKMRFKGCVDTETVLNKNNVGAPTNGDMGGGGGDEVMAL
Protein: Glutathione S-transferase omega-2 (GSTO-2) (EC 2.5.1.18) (Glutathione S-transferase omega 2-2) (GSTO 2-2) (Glutathione-dependent dehydroascorbate reductase) (EC 1.8.5.1) (Monomethylarsonic acid reductase) (MMA(V) reductase) (EC 1.20.4.2) (Q9H4Y5)
Organism: Homo sapiens (Human)
Function: Exhibits glutathione-dependent thiol transferase activity. Has high dehydroascorbate reductase activity and may contribute to the recycling of ascorbic acid. Participates in the biotransformation of inorganic arsenic and reduces monomethylarsonic acid (MMA).
Interaction partners:
- Glutathione reductase, mitochondrial
- Phospholipid hydroperoxide glutathione peroxidase GPX4
- Hematopoietic prostaglandin D synthase
- Glutathione synthetase
- Peroxiredoxin-6
- Epoxide hydrolase 1
- Glutathione S-transferase P
- Cytochrome P450 1A1
- Cytochrome P450 1B1
- Cytochrome P450 2E1
Sequence:
MSGDATRTLGKGSQPPGPVPEGLIRIYSMRFCPYSHRTRLVLKAKDIRHEVVNINLRNKPEWYYTKHPFGHIPVLETSQCQLIYESVIACEYLDDAYPGRKLFPYDPYERARQKMLLELFCKVPHLTKECLVALRCGRECTNLKAALRQEFSNLEEILEYQNTTFFGGTCISMIDYLLWPWFERLDVYGILDCVSHTPALRLWISAMKWDPTVCALLMDKSIFQGFLNLYFQNNPNAFDFGLC
Protein: Two-component response regulator ORR4 (Type A response regulator 4) (OsRR4) (Q4GZK7)
Organism: Oryza sativa subsp. indica (Rice)
Function: Functions as response regulator involved in His-to-Asp phosphorelay signal transduction system. Phosphorylation of the Asp residue in the receiver domain activates the ability of the protein to promote the transcription of target genes. Type-A response regulators seem to act as negative regulators of the cytokinin signaling.
Interaction partners:
Sequence:
MTVVDAESRFHVLAVDDSLIDRKLIEMLLKNSSYQVTTVDSGSKALELLGLRDEGDDSSSSPSSSSPDHQEIDVNLIITDYCMPGMTGYDLLKRVKGSSSLKDIPVVIMSSENVPARINRCLEDGAEEFFLKPVKLADMKKLKSHLLKRKQQLPMAAAAPDKPPHKPDEAAASAAAIAEAATAQTDGIISDCSCSGSSKRKAAAMEQEVISSPDQRTKPRLSSTSSGLAVET
Protein: Phosphatidylinositol 3-kinase regulatory subunit beta (PI3-kinase regulatory subunit beta) (PI3K regulatory subunit beta) (PtdIns-3-kinase regulatory subunit beta) (Phosphatidylinositol 3-kinase 85 kDa regulatory subunit beta) (PI3-kinase subunit p85-beta) (PtdIns-3-kinase regulatory subunit p85-beta) (O00459)
Organism: Homo sapiens (Human)
Function: Regulatory subunit of phosphoinositide-3-kinase (PI3K), a kinase that phosphorylates PtdIns(4,5)P2 (Phosphatidylinositol 4,5-bisphosphate) to generate phosphatidylinositol 3,4,5-trisphosphate (PIP3). PIP3 plays a key role by recruiting PH domain-containing proteins to the membrane, including AKT1 and PDPK1, activating signaling cascades involved in cell growth, survival, proliferation, motility and morphology. Binds to activated (phosphorylated) protein-tyrosine kinases, through its SH2 domain, and acts as an adapter, mediating the association of the p110 catalytic unit to the plasma membrane. Indirectly regulates autophagy. Promotes nuclear translocation of XBP1 isoform 2 in a ER stress- and/or insulin-dependent manner during metabolic overloading in the liver and hence plays a role in glucose tolerance improvement (By similarity).
Interaction partners:
- Phosphatidylinositol 3-kinase regulatory subunit gamma
- Phosphatidylinositol 3-kinase regulatory subunit alpha
- Phosphatidylinositol 4,5-bisphosphate 3-kinase catalytic subunit beta isoform
- Phosphatidylinositol 4,5-bisphosphate 3-kinase catalytic subunit delta isoform
- Phosphatidylinositol 4,5-bisphosphate 3-kinase catalytic subunit alpha isoform
- Phosphatidylinositol 4,5-bisphosphate 3-kinase catalytic subunit gamma isoform
- Epidermal growth factor receptor
- Insulin receptor substrate 1
- Receptor tyrosine-protein kinase erbB-3
- Insulin receptor substrate 4
Sequence:
MAGPEGFQYRALYPFRRERPEDLELLPGDVLVVSRAALQALGVAEGGERCPQSVGWMPGLNERTRQRGDFPGTYVEFLGPVALARPGPRPRGPRPLPARPRDGAPEPGLTLPDLPEQFSPPDVAPPLLVKLVEAIERTGLDSESHYRPELPAPRTDWSLSDVDQWDTAALADGIKSFLLALPAPLVTPEASAEARRALREAAGPVGPALEPPTLPLHRALTLRFLLQHLGRVASRAPALGPAVRALGATFGPLLLRAPPPPSSPPPGGAPDGSEPSPDFPALLVEKLLQEHLEEQEVAPPALPPKPPKAKPASTVLANGGSPPSLQDAEWYWGDISREEVNEKLRDTPDGTFLVRDASSKIQGEYTLTLRKGGNNKLIKVFHRDGHYGFSEPLTFCSVVDLINHYRHESLAQYNAKLDTRLLYPVSKYQQDQIVKEDSVEAVGAQLKVYHQQYQDKSREYDQLYEEYTRTSQELQMKRTAIEAFNETIKIFEEQGQTQEKCSKEYLERFRREGNEKEMQRILLNSERLKSRIAEIHESRTKLEQQLRAQASDNREIDKRMNSLKPDLMQLRKIRDQYLVWLTQKGARQKKINEWLGIKNETEDQYALMEDEDDLPHHEERTWYVGKINRTQAEEMLSGKRDGTFLIRESSQRGCYACSVVVDGDTKHCVIYRTATGFGFAEPYNLYGSLKELVLHYQHASLVQHNDALTVTLAHPVRAPGPGPPPAAR
Protein: Host protease inhibitor (Protein pin) (P07068)
Organism: Enterobacteria phage T4 (Bacteriophage T4)
Function: Plays a role in the inhibition of bacterial toxin-antitoxin system by blocking the action of host Lon protease.
Interaction partners:
Sequence:
MITVDKWFRINRADTGLCNYWPELSAGTVFKVRELVKECEDDIEPDTGIIEIELSDGKIINIYDKPITYWCLWNTESVENGEIEEVVERTNQVVQKPKADFQGERISYALAKLAAQENNDGYEGNLMQAAAEYIEWLETQISFSDRMIQQYKRLHQMFYNT
Protein: Mitochondrial transcription factor A, isoform B (Q86BR8)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- DNA-directed RNA polymerase
- Single-stranded DNA-binding protein, mitochondrial
- DNA polymerase subunit gamma-1, mitochondrial
- DNA-binding protein Ewg
- FI18188p1
- NAD-dependent histone deacetylase sirtuin-1
- Dimethyladenosine transferase 1, mitochondrial dimethyltransferase 1)
- Mitochondrial DNA helicase
- E3 ubiquitin-protein ligase parkin
- Dimethyladenosine transferase 2, mitochondrial dimethyltransferase 2)
Sequence:
MIYTTTLMSSRGGLIGSLINKVRQVVAKDWPPSDPSRANDTDHRPLTPPRPLAAASISNTPAVPSKTLEEQLGLPPRPKKPLTPYFRFMREQRPKLKAANPQITTVEVVRQLSKNWSDADAQLKERLQAEFKRDQQIYVEERTKYDATLTEEQRAEIKQLKQDLVDAKERRQLRKRVKELGRPKKPASAFLRFIASERINTPQGDKQTYREWHQKTTAKWTRLSDSEKEVYMQESRKEMELYRKAISVWEEKMIRLGHIDVVRHGNLIDPPEPKPRKTLASKDI
Protein: Multifunctional virulence effector protein DrrA (Defects in Rab1 recruitment protein A) [Includes: Protein adenylyltransferase (AMPylator) (EC 2.7.7.108) (Protein guanylyltransferase) (GMPylator) (EC 2.7.7.n6); Rab1 guanine nucleotide exchange factor] (Q5ZSQ3)
Organism: Legionella pneumophila subsp. pneumophila (strain Philadelphia 1 / ATCC 33152 / DSM 7513)
Function: Virulence effector that plays a key role in hijacking the host vesicular trafficking by recruiting the small guanosine triphosphatase (GTPase) Rab1 to the cytosolic face of the Legionella-containing vacuole (LCVs). Acts as a GDP-GTP exchange factor (GEF) for the small GTPase Rab1 (RAB1A, RAB1B or RAB1C), thereby converting Rab1 to an active GTP-bound state, leading to the incorporation of Rab1 into LCVs. Also shows RabGDI displacement factor (GDF) activity; however, this probably represents a passive activity following the GEF activity. Also acts as an adenylyltransferase by mediating the addition of adenosine 5'-monophosphate (AMP) to 'Tyr-77' of host RAB1B, thereby rendering RAB1B constitutively active. Also has adenylyltransferase activity towards Rab6 and Rab35. Also displays guanylyltransferase activity by mediating the addition of guanosine 5'-monophosphate (GMP) to host RAB1B in vitro; however such activity remains uncertain in vivo. Specifically binds phosphatidylinositol 4-phosphate (PtdIns(4)P) lipids on the cytosolic surface of the phagosomal membrane shortly after infection.
Subcellular location: Secreted {ECO:0000269|PubMed:16824952}. Host cytoplasmic vesicle membrane {ECO:0000269|PubMed:16824952}; Peripheral membrane protein {ECO:0000269|PubMed:16824952}. Note=Translocated into the host cell via the type IV secretion system (T4SS). Membrane association is mediated by PtdIns(4)P-binding.
Interaction partners:
Sequence:
MSIMGRIKMSVNEEQFGSLYSDERDKPLLSPTAQKKFEEYQNKLANLSKIIRENEGNEVSPWQEWENGLRQIYKEMIYDAFDALGVEMPKDMEVHFAGSLAKAQATEYSDLDAFVIVKNDEDIKKVKPVFDALNNLCQRIFTASNQIYPDPIGINPSRLIGTPDDLFGMLKDGMVADVEATAMSILTSKPVLPRYELGEELRDKIKQEPSFSNMVSAKKFYNKAIKDFTAPKEGAEVVSVKTHIMRPIDFMLMGLREEFNLYSEDGAHLSAPGTIRLLREKNLLPEEQIARIESVYNQAMSKRFELHAEHKKEHDEMPYSDAKAMLDEVAKIRELGVQRVTRIENLENAKKLWDNANSMLEKGNISGYLKAANELHKFMKEKNLKEDDLRPELSDKTISPKGYAILQSLWGAASDYSRAAATLTESTVEPGLVSAVNKMSAFFMDCKLSPNERATPDPDFKVGKSKILVGIMQFIKDVADPTSKIWMHNTKALMNHKIAAIQKLERSNNVNDETLESVLSSKGENLSEYLSYKYATKDEGREHRYTASTENFKNVKEKYQQMRGDALKTEILADFKDKLAEATDEQSLKQIVAELKSKDEYRILAKGQGLTTQLLGLKTSSVSSFEKMVEETRESIKSQERQTIKIK
Protein: Cadherin domain-containing protein (Q8BRR0)
Organism: Mus musculus (Mouse)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004251}; Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004251}.
Interaction partners:
Sequence:
MLSFQRRGSCTLPPLRWLLLLAAWEAGSGQLHYSIPEEAKHGTFVGRIAQDLGLELTELVPRLFRVASKDRGDLLEVNLQNGILFVNSRIDREELCGRSAECSIHLEVIVDRPLQVFHVEVEVRDINDNPPVFPLREQRLLISESKQPDSRFPLEGASDADIGENAVLVYRLSQNEYFSLEPPINSKQTKRPSLILKKVLDREKTPELNLLLTATDGGKPELTGTVQLWVRVLDVNDNDPVFDHLEYKVRIMENAAKETLVITLNATDLDEGANGQLVYSLMSIKPTGRHLFTLDEKNGELRVNGTLDYEENKLYEIEVLATDKGTPPMVGHCVVLVEILDTNDNSPEVTLTSLSLPVREDAQPNTVIALISVSDLDSGINGQVTCSLTPNVPFKIVSTFKNYYSLVLDSSLDRERVSTYDLVVIARDGGSPSLSATVSVSVEVADVNDNAPVFAQPEYTVFVKENNPPGAHIFTVSAMDADAQENALVSYSLVERRVGERLLSSYVSVHAESGKVFALQPLDHEELELLQFQVSARDAGVPALGSNVTLQVFVLDENDNAPTLLPHGAVGAGGAVSGLVSRSVGSGHVVTKVRAVDADSGYNAWLSYEVQLGTGGVRSPFRVGLYTGEISTTRALDEVDSPRQTLLVLVKDHGEPALTATATVLVSLVESGQAPKSFSQASGRASAPEASLVDVNVYLIIAICAVSSLLVLTLLLYTALRCSALPMVNEATGGPGKPMLVCSSEVGSWSYSQQRRQRVCSGEVLPKTDLMAFSPSLPPNLGRDERERQESESSHPGQPRQTNPDWRYSASLRAGMHSSVHLEEAGILRAGPGGPDQQWPTVSSATPEPEAGEVSPPVGAGVNSNSWTFKYGPGNPKQSGPGELPDKFIIPGSPAIISIRQEPANNQIDKSDFITFGKKEETK
Protein: Probable WRKY transcription factor 39 (WRKY DNA-binding protein 39) (Q9SR07)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Transcription factor. Interacts specifically with the W box (5'-(T)TGAC[CT]-3'), a frequently occurring elicitor-responsive cis-acting element (By similarity).
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00223}.
Interaction partners:
Sequence:
MEEVEAANRSAIESCHGVLNLLSQRTSDPKSLTVETGEVVSKFKRVASLLTRGLGHGKFRSTNKFRSSFPQHIFLESPICCGNDLSGDYTQVLAPEPLQMVPASAVYNEMEPKHQLGHPSLMLSHKMCVDKSFLELKPPPFRAPYQLIHNHQQIAYSRSNSGVNLKFDGSGSSCYTPSVSNGSRSFVSSLSMDASVTDYDRNSFHLTGLSRGSDQQHTRKMCSGSLKCGSRSKCHCSKKRKLRVKRSIKVPAISNKIADIPPDEYSWRKYGQKPIKGSPHPRGYYKCSSVRGCPARKHVERCIDETSMLIVTYEGEHNHSRILSSQSAHT
Protein: Triosephosphate isomerase (TIM) (EC 5.3.1.1) (Methylglyoxal synthase) (EC 4.2.3.3) (Triose-phosphate isomerase) (Q10657)
Organism: Caenorhabditis elegans
Function: Triosephosphate isomerase is an extremely efficient metabolic enzyme that catalyzes the interconversion between dihydroxyacetone phosphate (DHAP) and D-glyceraldehyde-3-phosphate (G3P) in glycolysis and gluconeogenesis.
Subcellular location: Cytoplasm {ECO:0000255|PROSITE-ProRule:PRU10127}.
Interaction partners:
- Glyceraldehyde-3-phosphate dehydrogenase 1
- Glyceraldehyde-3-phosphate dehydrogenase 4
- Probable phosphoglycerate kinase
- Glyceraldehyde-3-phosphate dehydrogenase 3
- Glyceraldehyde-3-phosphate dehydrogenase 2
- Enolase
- Glucose-6-phosphate isomerase
- Transaldolase
- Triokinase/FMN cyclase)
- Fructose-bisphosphate aldolase 2
Sequence:
MTRKFFVGGNWKMNGDYASVDGIVTFLNASADNSSVDVVVAPPAPYLAYAKSKLKAGVLVAAQNCYKVPKGAFTGEISPAMIKDLGLEWVILGHSERRHVFGESDALIAEKTVHALEAGIKVVFCIGEKLEEREAGHTKDVNFRQLQAIVDKGVSWENIVIAYEPVWAIGTGKTASGEQAQEVHEWIRAFLKEKVSPAVADATRIIYGGSVTADNAAELGKKPDIDGFLVGGASLKPDFVKIINARS