wanglab/gogpt-training-data huggingface dataset:
Protein: 2,4-dinitrotoluene dioxygenase system, ferredoxin component (Q45694)
Organism: Burkholderia sp. (strain RASC)
Function: Component of the 2,4-dinitrotoluene dioxygenase (DNTDO) multicomponent enzyme system which catalyzes the incorporation of both atoms of molecular oxygen into 2,4-dinitrotoluene (DNT) to form 4-methyl-5-nitrocatechol (MNC) and nitrite. Functions as an intermediate electron transfer protein via a specific interaction with iron sulfur protein components (ISP)(DntAc and DntAd). Also able to convert naphthalene to cis-(1R,2S)-dihydroxy-1,2-dihydronaphthalene.
Interaction partners:
Sequence:
MSENWIDAAARDEVPRGRRDRHQYRRQGDCLYEVAGEIYATDNTCTHGAARMSDGFLEGREIECPLHQGRFDVCTGKALCTPLTQDIKTYPVKIENMRVMLKLD
Protein: Pituitary adenylate cyclase-activating polypeptide type I receptor (PACAP type I receptor) (PACAP-R-1) (PACAP-R1) (P32215)
Organism: Rattus norvegicus (Rat)
Function: This is a receptor for PACAP-27 and PACAP-38. The activity of this receptor is mediated by G proteins which activate adenylyl cyclase. May regulate the release of adrenocorticotropin, luteinizing hormone, growth hormone, prolactin, epinephrine, and catecholamine. May play a role in spermatogenesis and sperm motility. Causes smooth muscle relaxation and secretion in the gastrointestinal tract.
Subcellular location: Cell membrane; Multi-pass membrane protein {ECO:0000250|UniProtKB:P41586}.
Interaction partners:
- Pituitary adenylate cyclase-activating polypeptide
- Guanine nucleotide-binding protein G
- VIP peptides
- Pro-glucagon
- Guanine nucleotide-binding protein subunit gamma
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein G
- Pro-opiomelanocortin
Sequence:
MARVLQLSLTALLLPVAIAMHSDCIFKKEQAMCLERIQRANDLMGLNESSPGCPGMWDNITCWKPAQVGEMVLVSCPEVFRIFNPDQVWMTETIGDSGFADSNSLEITDMGVVGRNCTEDGWSEPFPHYFDACGFDDYEPESGDQDYYYLSVKALYTVGYSTSLATLTTAMVILCRFRKLHCTRNFIHMNLFVSFMLRAISVFIKDWILYAEQDSSHCFVSTVECKAVMVFFHYCVVSNYFWLFIEGLYLFTLLVETFFPERRYFYWYTIIGWGTPTVCVTVWAVLRLYFDDAGCWDMNDSTALWWVIKGPVVGSIMVNFVLFIGIIIILVQKLQSPDMGGNESSIYLTNLRLRVPKKTREDPLPVPSDQHSPPFLSCVQKCYCKPQRAQQHSCKMSELSTITLRLARSTLLLIPLFGIHYTVFAFSPENVSKRERLVFELGLGSFQGFVVAVLYCFLNGEVQAEIKRKWRSWKVNRYFTMDFKHRHPSLASSGVNGGTQLSILSKSSSQLRMSSLPADNLAT
Protein: Ral GTPase-activating protein subunit alpha-1 (GAP-related-interacting partner to E12) (GRIPE) (GTPase-activating Rap/Ran-GAP domain-like 1) (Tuberin-like protein 1) (p240) (P86409)
Organism: Sus scrofa (Pig)
Function: Catalytic subunit of the heterodimeric RalGAP1 complex which acts as a GTPase activator for the Ras-like small GTPases RALA and RALB.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:Q6GYP7}. Nucleus {ECO:0000250|UniProtKB:Q6GYP7}. Note=Translocated to the nucleus, when associated with TCF3/E12. {ECO:0000250|UniProtKB:Q6GYP7}.
Interaction partners:
Sequence:
MFSKKPHGDVKKSTQKVLDTKKDALTRLKHLRIVIENAESIDLKQFFDQHFSHIYYVFFENFVTIEASLKQKGHKSQREELDAILFIFEKILQLLPERIHQRWQFHSIGLILKKLLHTGNSLKIRREGVRLFLLWLQALQNNCSREQLWMFSCLIPGFSAPQSEYGPRTLDNLINPPLNLQETQVTIEEITPLVPPQSGDKGQEDLTSYFLEALLKYIVIQVKSLEWKNKENQERGFSFLFSHFKKYYLPYIFPNICKENSLYHPVLDIPQMRPKPHYVMIKKDAETNEAIYCTKEPFIKARVIVIRWLVSFWLEPKPHTGPHIPGMEGEVLPKNIQ
Protein: KH domain-containing RNA-binding protein QKI (Protein quaking) (MqkI) (Q9QYS9)
Organism: Mus musculus (Mouse)
Function: RNA-binding protein that plays a central role in myelinization. Also required for visceral endoderm function and blood vessel development. Binds to the 5'-NACUAAY-N(1,20)-UAAY-3' RNA core sequence. Acts by regulating pre-mRNA splicing, mRNA export, mRNA stability and protein translation, as well as cellular processes including apoptosis, cell cycle, glial cell fate and development. Required to protect and promote stability of mRNAs such as MBP and CDKN1B which promotes oligodendrocyte differentiation. Participates in mRNA transport by regulating the nuclear export of MBP mRNA. May also play a role in smooth muscle development.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:29021242, ECO:0000269|PubMed:8987822}. Nucleus {ECO:0000269|PubMed:29021242, ECO:0000269|PubMed:31868295, ECO:0000269|PubMed:8987822}.; SUBCELLULAR LOCATION: [Isoform QKI5]: Nucleus {ECO:0000269|PubMed:10506177, ECO:0000269|PubMed:29021242}. Cytoplasm {ECO:0000269|PubMed:10506177}. Note=Localizes predominantly in the nucleus and at lower levels in cytoplasm (PubMed:10506177, PubMed:29021242). It shuttles between the cytoplasm and the nucleus (PubMed:10506177). {ECO:0000269|PubMed:10506177, ECO:0000269|PubMed:29021242}.; SUBCELLULAR LOCATION: [Isoform QKI6]: Cytoplasm, cytosol {ECO:0000269|PubMed:11297509, ECO:0000269|PubMed:20956316, ECO:0000269|PubMed:29021242}. Nucleus {ECO:0000269|PubMed:11297509}. Note=Localizes predominantly in the cytoplasm and at lower levels in nucleus. {ECO:0000269|PubMed:11297509, ECO:0000269|PubMed:29021242}.; SUBCELLULAR LOCATION: [Isoform QKI7]: Cytoplasm, cytosol {ECO:0000269|PubMed:11297509, ECO:0000269|PubMed:29021242}. Cytoplasm, Stress granule {ECO:0000250|UniProtKB:Q96PU8}. Nucleus {ECO:0000269|PubMed:11297509}. Note=Localizes predominantly in the cytoplasm and at much lower levels in nucleus (PubMed:11297509, PubMed:29021242). Shuttles between the cytosol and stress granules in response to stress (By similarity). {ECO:0000250|UniProtKB:Q96PU8, ECO:0000269|PubMed:11297509, ECO:0000269|PubMed:29021242}.
Interaction partners:
- Mediator of RNA polymerase II transcription subunit 13
- Mediator of RNA polymerase II transcription subunit 15
- Mediator of RNA polymerase II transcription subunit 25
- Mediator of RNA polymerase II transcription subunit 4
- Mediator of RNA polymerase II transcription subunit 1
- Mediator of RNA polymerase II transcription subunit 29
- Mediator of RNA polymerase II transcription subunit 17
- Mediator of RNA polymerase II transcription subunit 14
- Mediator of RNA polymerase II transcription subunit 23
- Mediator of RNA polymerase II transcription subunit 12
Sequence:
MVGEMETKEKPKPTPDYLMQLMNDKKLMSSLPNFCGIFNHLERLLDEEISRVRKDMYNDTLNGSTEKRSAELPDAVGPIVQLQEKLYVPVKEYPDFNFVGRILGPRGLTAKQLEAETGCKIMVRGKGSMRDKKKEEQNRGKPNWEHLNEDLHVLITVEDAQNRAEIKLKRAVEEVKKLLVPAAEGEDSLKKMQLMELAILNGTYRDANIKSPALAFSLAATAQAAPRIITGPAPVLPPAALRTPTPAGPTIMPLIRQIQTAVMPNGTPHPTAAIVPPGPEAGLIYTPYEYPYTLAPATSILEYPIEPSGVLGAVATKVRRHDMRVHPYQRIVTADRAATGN
Protein: Mucin-7 (MUC-7) (Apo-MG2) (Salivary mucin-7) (Q8TAX7)
Organism: Homo sapiens (Human)
Function: May function in a protective capacity by promoting the clearance of bacteria in the oral cavity and aiding in mastication, speech, and swallowing. Binds P.aeruginosa pili.
Subcellular location: Secreted {ECO:0000269|PubMed:7690757}.
Interaction partners:
- Mucin-5B
- Mucin-2
- Mucin-1
- Statherin
- Mucin-5AC
- Histatin-1
- Mucin-6
- Mucin-13
- Polypeptide N-acetylgalactosaminyltransferase 14
- Mucin-3A
Sequence:
MKTLPLFVCICALSACFSFSEGRERDHELRHRRHHHQSPKSHFELPHYPGLLAHQKPFIRKSYKCLHKRCRPKLPPSPNNPPKFPNPHQPPKHPDKNSSVVNPTLVATTQIPSVTFPSASTKITTLPNVTFLPQNATTISSRENVNTSSSVATLAPVNSPAPQDTTAAPPTPSATTPAPPSSSAPPETTAAPPTPSATTQAPPSSSAPPETTAAPPTPPATTPAPPSSSAPPETTAAPPTPSATTPAPLSSSAPPETTAVPPTPSATTLDPSSASAPPETTAAPPTPSATTPAPPSSPAPQETTAAPITTPNSSPTTLAPDTSETSAAPTHQTTTSVTTQTTTTKQPTSAPGQNKISRFLLYMKNLLNRIIDDMVEQ
Protein: Tau tubulin kinase 1 (A0A0G2JTK1)
Organism: Rattus norvegicus (Rat)
Interaction partners:
Sequence:
MQCLAAALKDETNMSGGGEQADILPANYVVKDRWKVLKKIGGGGFGEIYEAMDLLTRENVALKVESAQQPKQVLKMEVAVLKKLQGKDHVCRFIGCGRNEKFNYVVMQLQGRNLADLRRSQPRGTFTLSTTLRLGKQILESIEAIHSVGFLHRDIKPSNFAMGRLPSTYRKCYMLDFGLARQYTNTTGDVRPPRNVAGFRGTVRYASVNAHKNREMGRHDDLWSLFYMLVEFAVGQLPWRKIKDKEQVGMIKEKYEHRMLLKHMPSEFHLFLDHIASLDYFTKPDYQLIMSVFENSMKERGIAENEAFDWEKAGTDALLSTSTSTPPQQNTRQTAAMFGVVNVTPVPGDLLRENTEDVLQGEHLSDQENAPPILPGRPPEGLGPGPHLVPHPGGPEAEVWEETDVNRNKLRINIGKTPCVEEEQSRGVGVPSSPVRAPPDSPTTPVRSLRYRRVNSPESERLSTAADGRAELQERRSRMDLPGSPSRQACSSQPAQMLSVDTGHADRQASGRMDVSASVEQEALSNAFRSVPLAEEEDFDSKEWVIIDKETELKDFPPGAEPSTSGTTDEEPEELRPLPEEGEERRRLGTEPTVRPRGRGMQTLAEEDPRQMLPQPAPPQLSQADGRSETSQPPTPGSPSHSPLHSGPRPRRRESDPTGPQRQVFSVAPPFEVNGLPRAVPLGLPYQDFKRDLSDYRERARLLNRVRRVGFSHMLLTTPQVPLAPFQPQANGKEGEEEEEEDEEEEEEEEEEDEEDEEEEDEEDEDEEEEEAGALGEVLGPRSGSSSEGSERSQEGAPSTLLADDQKEARGRASMADGDLEPEEGSKTLVLVSPGDMKKSPVTAELAPDPDLGTLAALTPQHERPQPTGSQLDVSEPGTLSSILKSEPKPSGPGAGVGVGLVAPGAGVTAVTSPFTKVERTFVHIAEKSHLNVMSSGGQAPRPEELSTGGELGLEMLSEVGAAEEGAPQPLENGMALVGPDGTEMESCALSGPPGETPSEVVTDSLPDGPALADEPAPASPQEPITKKGTIISPSRHAMPGSRPRSRIPVLLSEEDTGSEPSGSLSAKERWSKRARPQQDLARLVMEKRQGRLLLRLASGASSSSSEEQRRASETLSGTGSEEDTPASEPAAALPRKAGRAATTRSRIPRPISVSMPAEGQQLPGRPHGAASATDSAITSRLQLQKPPGLATAADHRPKQPASRASGPGRAQVSKPAAPRSPGLPTSTARHSSGSPRSQSLSRKESSSPSHQARPGFPPSRGVLQVRSQSEASPGGPKKGPKGKQLQTLRAATKGRPAVSEGRPGNR
Protein: X-linked lymphocyte regulated gene 4 (X-linked lymphocyte-regulated 4B) (Xlr4b protein) (Q9JJQ7)
Organism: Mus musculus (Mouse)
Interaction partners:
- X-linked lymphocyte-regulated protein PM1
- X-linked lymphocyte-regulated 4A
- X-linked lymphocyte-regulated 4C
Sequence:
MASKIKGRPPKQPKVTPALPSNDSQQLHENNPGNNLALETCGESSSSHGTGGPKPGPSKKTLNERKRKYGVSVNKTVQNIEWNVDHFLKVQHERRQELYKDYSHQFLTLVMMWNIDVDQIKKQAGKLSDILDEQQKLFQQFQSIHMQKIEEFKELCDRHLKNLQAIKCCRRKAIIEEARKLMDYLEKRVTEETVHVNKQEAKDGVQSSLLSLLIS
Protein: Chromosomal passenger protein (Q381V1)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- Chromosomal passenger protein
- Kinesin motor domain-containing protein
- Kinesin-like protein
- DNA ligase, putative
- PUF nine target 1
- Aurora kinase
Sequence:
MQWKKDDLFEGLRKLPRTPGELFGHRNKLNFILQKRFFIAPDMVELALNRQNGEQFNRCYAKLVMQAVAKFNNTTRSQLKVRVDPRLPKGLQLIQPDDKDTGANLKSKKSEKAASGRLNAFSNTTSGQQRKPQQRQQSRYCSPQSGGVSPRVVMPIDPAERDCLYATYLRARTPQSGTPDYSDMMLQSPSCATDGKTTMFSEDGSSALRSATRRSAGDVHFATPPVFKGFERTLELTPADSPTESLPLHF
Protein: WRKY transcription factor WRKY76 (OsWRKY76) (Q6IEK5)
Organism: Oryza sativa subsp. indica (Rice)
Function: Transcription repressor. Interacts specifically with the W box (5'-(T)TGAC[CT]-3'), a frequently occurring elicitor-responsive cis-acting element. Regulates, probably indirectly, the activation of defense-related genes during defense response (By similarity). Modulates plant innate immunity against X.oryzae pv. oryzae (Xoo) (By similarity).
Subcellular location: Nucleus {ECO:0000250|UniProtKB:Q6QHD1, ECO:0000255|PROSITE-ProRule:PRU00223}.
Interaction partners:
Sequence:
MDAAWRGGVGCSPVCLDLCVGLSPVREPSAARHELLDRPAGCRGGGDSKSMTNDEAKILEAKVTQMSEENRRLTEVIARLYGGQIARLGLDGSASPPRPVSPLSGKKRSRESMETANSCDANSNRHQGGDADHAESFAADDGTCRRIKVSRVCRRIDPSDTSLVVKDGYQWRKYGQKVTRDNPSPRAYFRCAFAPSCPVKKKVQRSAEDSSLLVATYEGEHNHPHPSPRAGELPAAVGGAGGSLPCSISINSSGPTITLDLTKNGGAVQVVEAAHPPPPPDLKEVCREVASPEFRTALVEQMASALTSDPKFTGALAAAILQKLPEF
Protein: EG:100G10.5 protein (UDP-galactose transporter, isoform B) (O76865)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
- Probable galactose-1-phosphate uridylyltransferase
- Protein Mo25
- UDP-glucose 4-epimerase
- GH11113p
- Hexosyltransferase
- Lysosomal dipeptide transporter MFSD1
Sequence:
MALLPAPVTYSYSHRTVNANTLKYISLLTLTLQNAILGLSMRYARTRPGDIFLSSTAVLMAEFAKLITCLFLVFNEEGKDAQKFVRSLHKTIIANPMDTLKVCVPSLVYIVQNNLLYVSASHLDAATYQVTYQLKILTTAMFAVVILRRKLLNTQWGALLLLVMGIVLVQLAQTEGPTSGSAGGAAAAATAASSGGAPEQNRMLGLWAALGACFLSGFAGIYFEKILKGAEISVWMRNVQLSLLSIPFGLLTCFVNDGSRIFDQGFFKGYDLFVWYLVLLQAGGGLIVAVVVKYADNILKGFATSLAIIISCVASIYIFDFNLTLQFSFGAGLVIASIFLYGYDPARSAPKPTMHGPGGDEEKLLPRV
Protein: Serine/threonine-protein kinase KIN2 (EC 2.7.11.1) (P13186)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Serine/threonine protein kinase involved in the regulation of exocytosis. Induces phosphorylation of SEC9 and its release from the plasma membrane to the cytosol.
Subcellular location: Cytoplasm. Cell membrane; Peripheral membrane protein; Cytoplasmic side.
Interaction partners:
- 5'-AMP-activated protein kinase subunit gamma
- Serine/threonine protein kinase KIN1
- SNF1 protein kinase subunit beta-1
- SNF1 protein kinase subunit beta-2
- SNF1 protein kinase subunit beta-3
- Protein transport protein SEC9
- Bud site selection protein 14
Sequence:
MPNPNTADYLVNPNFRTSKGGSLSPTPEAFNDTRVAAPATLRMMGKQSGPRNDQQQAPLMPPADIKQGKEQAAQRQNDASRPNGAVELRQFHRRSLGDWEFLETVGAGSMGKVKLVKHRQTKEICVIKIVNRASKAYLHKQHSLPSPKNESEILERQKRLEKEIARDKRTVREASLGQILYHPHICRLFEMCTMSNHFYMLFEYVSGGQLLDYIIQHGSLKEHHARKFARGIASALQYLHANNIVHRDLKIENIMISSSGEIKIIDFGLSNIFDYRKQLHTFCGSLYFAAPELLKAQPYTGPEVDIWSFGIVLYVLVCGKVPFDDENSSILHEKIKKGKVDYPSHLSIEVISLLTRMIVVDPLRRATLKNVVEHPWMNRGYDFKAPSYVPNRVPLTPEMIDSQVLKEMYRLEFIDDIEDTRRSLIRLVTEKEYIQLSQEYWDKLSNAKGLSSSLNNNYLNSTAQQTLIQNHITSNPSQSGYNEPDSNFEDPTLAYHPLLSIYHLVSEMVARKLAKLQRRQALALQAQAQQRQQQQQVALGTKVALNNNSPDIMTKMRSPQKEVVPNPGIFQVPAIGTSGTSNNTNTSNKPPLHVMVPPKLTIPEQAHTSPTSRKSSDIHTELNGVLKSTPVPVSGEYQQRSASPVVGEHQEKNTIGGIFRRISQSGQSQHPTRQQEPLPEREPPTYMSKSNEISIKVPKSHSRTISDYIPSARRYPSYVPNSVDVKQKPAKNTTIAPPIRSVSQKQNSDLPALPQNAELIVQKQRQKLLQENLDKLQINDNDNNNVNAVVDGINNDNSDHYLSVPKGRKLHPSARAKSVGHARRESLKFTRPPIPAALPPSDMTNDNGFLGEANKERYNPVSSNFSTVPEDSTTYSNDTNNRLTSVYSQELTEKQILEEASKAPPGSMPSIDYPKSMFLKGFFSVQTTSSKPLPIVRHNIISVLTRMNIDFKEVKGGFICVQQRPSIETAAVPVITTTGVGLDSGKAMDLQNSLDSQLSSSYHSTASSASRNSSIKRQGSYKRGQNNIPLTPLATNTHQRNSSIPMSPNYGNQSNGTSGELSSMSLDYVQQQDDILTTSRAQNINNVNGQTEQTNTSGIKERPPIKFEIHIVKVRIVGLAGVHFKKVSGNTWLYKELASYILKELNL
Protein: Acyl-CoA synthetase short-chain family member 3, mitochondrial (EC 6.2.1.1) (Acetate--CoA ligase 3) (Acyl-CoA synthetase short-chain family member 3) (Propionate--CoA ligase) (EC 6.2.1.17) (Q9H6R3)
Organism: Homo sapiens (Human)
Function: Catalyzes the synthesis of acetyl-CoA from short-chain fatty acids. Propionate is the preferred substrate. Can utilize acetate and butyrate with a much lower affinity (By similarity).
Subcellular location: Mitochondrion matrix {ECO:0000269|PubMed:28003429}.
Interaction partners:
- Peroxisomal acyl-coenzyme A oxidase 1
- Ethylmalonyl-CoA decarboxylase
- Propionyl-CoA carboxylase beta chain, mitochondrial
- Propionyl-CoA carboxylase alpha chain, mitochondrial
- Short-chain specific acyl-CoA dehydrogenase, mitochondrial
- Peroxisomal acyl-coenzyme A oxidase 3
- Methylmalonate-semialdehyde/malonate-semialdehyde dehydrogenase [acylating], mitochondrial
- Lipoamide acyltransferase component of branched-chain alpha-keto acid dehydrogenase complex, mitochondrial
- 3-ketoacyl-CoA thiolase, mitochondrial
- Acetyl-coenzyme A synthetase, cytoplasmic
Sequence:
MKPSWLQCRKVTSAGGLGGPLPGSSPARGAGAALRALVVPGPRGGLGGRGCRALSSGSGSEYKTHFAASVTDPERFWGKAAEQISWYKPWTKTLENKHSPSTRWFVEGMLNICYNAVDRHIENGKGDKIAIIYDSPVTNTKATFTYKEVLEQVSKLAGVLVKHGIKKGDTVVIYMPMIPQAMYTMLACARIGAIHSLIFGGFASKELSSRIDHVKPKVVVTASFGIEPGRRVEYVPLVEEALKIGQHKPDKILIYNRPNMEAVPLAPGRDLDWDEEMAKAQSHDCVPVLSEHPLYILYTSGTTGLPKGVIRPTGGYAVMLHWSMSSIYGLQPGEVWWAASDLGWVVGHSYICYGPLLHGNTTVLYEGKPVGTPDAGAYFRVLAEHGVAALFTAPTAIRAIRQQDPGAALGKQYSLTRFKTLFVAGERCDVETLEWSKNVFRVPVLDHWWQTETGSPITASCVGLGNSKTPPPGQAGKSVPGYNVMILDDNMQKLKARCLGNIVVKLPLPPGAFSGLWKNQEAFKHLYFEKFPGYYDTMDAGYMDEEGYLYVMSRVDDVINVAGHRISAGAIEESILSHGTVADCAVVGKEDPLKGHVPLALCVLRKDINATEEQVLEEIVKHVRQNIGPVAAFRNAVFVKQLPKTRSGKIPRSALSAIVNGKPYKITSTIEDPSIFGHVEEMLKQA
Protein: Muscarinic acetylcholine receptor M2 (P08172)
Organism: Homo sapiens (Human)
Function: The muscarinic acetylcholine receptor mediates various cellular responses, including inhibition of adenylate cyclase, breakdown of phosphoinositides and modulation of potassium channels through the action of G proteins. Primary transducing effect is adenylate cyclase inhibition. Signaling promotes phospholipase C activity, leading to the release of inositol trisphosphate (IP3); this then triggers calcium ion release into the cytosol.
Subcellular location: Cell membrane {ECO:0000269|PubMed:22278061, ECO:0000269|PubMed:24256733, ECO:0000269|PubMed:3443095}; Multi-pass membrane protein {ECO:0000269|PubMed:22278061, ECO:0000269|PubMed:24256733}. Postsynaptic cell membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. Note=Phosphorylation in response to agonist binding promotes receptor internalization. {ECO:0000250|UniProtKB:P06199}.
Interaction partners:
- Beta-arrestin-1
- Proteinase-activated receptor 1
- Guanine nucleotide-binding protein G
- Lysophosphatidic acid receptor 1
- Muscarinic acetylcholine receptor M1
- Lysophosphatidic acid receptor 5
- Kininogen-1
- Lysophosphatidic acid receptor 4
- Lysophosphatidic acid receptor 6
- Lysophosphatidic acid receptor 2
Sequence:
MNNSTNSSNNSLALTSPYKTFEVVFIVLVAGSLSLVTIIGNILVMVSIKVNRHLQTVNNYFLFSLACADLIIGVFSMNLYTLYTVIGYWPLGPVVCDLWLALDYVVSNASVMNLLIISFDRYFCVTKPLTYPVKRTTKMAGMMIAAAWVLSFILWAPAILFWQFIVGVRTVEDGECYIQFFSNAAVTFGTAIAAFYLPVIIMTVLYWHISRASKSRIKKDKKEPVANQDPVSPSLVQGRIVKPNNNNMPSSDDGLEHNKIQNGKAPRDPVTENCVQGEEKESSNDSTSVSAVASNMRDDEITQDENTVSTSLGHSKDENSKQTCIRIGTKTPKSDSCTPTNTTVEVVGSSGQNGDEKQNIVARKIVKMTKQPAKKKPPPSREKKVTRTILAILLAFIITWAPYNVMVLINTFCAPCIPNTVWTIGYWLCYINSTINPACYALCNATFKKTFKHLLMCHYKNIGATR
Protein: Cdc42 effector protein 3 (Binder of Rho GTPases 2) (MSE55-related Cdc42-binding protein) (Q9UKI2)
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.
Subcellular location: Endomembrane system {ECO:0000269|PubMed:11035016}; Peripheral membrane protein {ECO:0000269|PubMed:11035016}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:11035016}.
Interaction partners:
- Rho-related GTP-binding protein RhoQ
- S-phase kinase-associated protein 1
- Cdc42 effector protein 5
- Cell division control protein 42 homolog
- Septin-7
Sequence:
MPAKTPIYLKAANNKKGKKFKLRDILSPDMISPPLGDFRHTIHIGKEGQHDVFGDISFLQGNYELLPGNQEKAHLGQFPGHNEFFRANSTSDSVFTETPSPVLKNAISLPTIGGSQALMLPLLSPVTFNSKQESFGPAKLPRLSCEPVMEEKAQEKSSLLENGTVHQGDTSWGSSGSASQSSQGRDSHSSSLSEQYPDWPAEDMFDHPTPCELIKGKTKSEESLSDLTGSLLSLQLDLGPSLLDEVLNVMDKNK
Protein: dextransucrase (EC 2.4.1.5) (Q5SBN1)
Organism: Limosilactobacillus reuteri (Lactobacillus reuteri)
Interaction partners:
Sequence:
MEIKKHFKLYKSGKQWVTASIATFAVSTGLVLGGGVVHAADNHPTTTSASVTNTVNNLKPQNDPEQQNNTQESNTVEFPKKDSQDNAVQPLKETAVMPNATNKDGAKASITNNAHTDNTIYGNIDPTTINDKELHVTGWNATNQAINKNESRYVIAYDDTTNSELGRTKITNQIARPDVEKVHKDIYNAQNSGFNVNISLDFNKMNNYRDAIKIISRYSGVPNGNSDYVDFVSQPIIFDENNYAYLDDFSVQNGRLHVSGRNATNKAIQRPNHFLILFDRTVNREVARQKVTAGINRSDVEKVYPQVVNANVSGFDATFDTINLNPNHEYQILSRYSNNGDGEGDYVTYWFNPQRIAPVNQFNNGHLDNFDISKAGKVTVSGWQATNLSNIQNNRYIILFDTTANCQIASMKVTGVDRPDVAKVYPQILNANKSGYNVTFDLTQAQIAQLFPNHSYSIVSRYSADPNGNGNDKQHTDFWSAPIVLNKTASYIDDISLNGDVLNVKGWMASDASATQANPYIIILNNGKEVTRQKLTLNDRPDVAKVYPDVYNSLASGFDTTIKLTNSQLNALNGNMQILLRYSAAADGNPINNGGFTDQYSKNYATNGGSFDFVKVDNNQVAFSGWHVSDQATDKPYQWIIVLVNGKEVGRQLISSTTNGLVSYNRPDVYNVNPAISNSSTSGFQGIMTLKDNIKNANVQLVHRFSDDGQNGEGNRVDYWSEVMPVTNTFQKGTDQLMRNLVAKPNKNQLKIYNGNTLVKTLGPGTWENMAFAQDSSAINNIDGYLSYTGWYRPYGTSQDGKTWYETTAMDWRPLLMYIWPSKDVQAQFIKYFVNNGYENANYGLTESSVASFSKDTNANLLDVTAQNLRYVIEQSIAANKGTSKLANDINSFAATVPELSASSELSLQSMPNYRPDESGTVDSDQVIFVNNNSKDPRKGNTGYADSNYRLMNRTINNQAGNNNSDNSPELLVGNDIDNSNPVVQAENLNWEYFLLNYGKLMGYNPDGNFDGFRVDAADNIDADVLDQMGQLMNDMYHTKGNPQNANDHLSYNEGYHSGAAQMLNEKGNPQLYMDSGEFYTLENVLGRANNRDSIGNLITNSVVNRQNDTTENEATPNWSFVTNHDQRKNLINRLIIKGHPNIPDIMGSAYKAEYANQAWQEFYADQKKTNKQYDQYNVPAQYAILLSNKDTVPQVYYGDLYNETAQYMQEKSIYYDTITTLMKARKQFVSGGQTMTKLNNNLLASVRYGKGVADSNSNGTDKLSRTSGIAVLVGNDSNMAQQTVAINMGRAHANQQYRNLIDTTENGLTYDGENSENPAILTTDSNGILKVTVKGYSNPYVSGYLGVWVPVISGDQDVTTSASDVVADKEKTFESNAALDSHMIYEDFSLFQPEPTNVENHAYNVIAKNANLFNDLGITDFWMAPAYTPFGMSRYNEGYSMTDRYNLGTTANPTKYGSGEELANTIAALHKVGLKVQEDIVMNQMIGFSGQEAVTVTRTNNRGMQIHVNGQTYANQIYFAYTTGGGNGQETYGGKYLAELQKNYPDLFTTKAISTEVVPDPTVRINKWSAKYENGTSLQNIGIGLAVKLANGDYAYLNSGDNKAFNTLLPTAISLNFNN
Protein: Fructose-1,6-bisphosphatase (FBPase) (EC 3.1.3.11) (D-fructose-1,6-bisphosphate 1-phosphohydrolase) (Q6RYT0)
Organism: Dictyostelium discoideum (Social amoeba)
Interaction partners:
- Fructose-bisphosphate aldolase
- Transketolase
- ATP-dependent 6-phosphofructokinase
- Glucose-6-phosphate isomerase
- Probable transaldolase
- Probable mannose-6-phosphate isomerase
- fructokinase
- Enolase-phosphatase E1
- isocitrate lyase
- malate synthase
Sequence:
MSSNNLITLHRWLLSDTHKNMENKLEMANLFSGIALACKITNNAIKRAGFESNFGLAGITNVHSEDVKKLDVIANDAFKMALKSTREVFCMVSEEEDSIIPVSQSQAGKYVVAFDPLDGSSNLDCNVSVGSIFSIWPKASKDHNYSNDDVLRKGRDMTAAGYALYGSATMLVLTFGQGVYGFTLDNHIGEFVLTHVEMRIRTKGSIYSINEGNSVFWDKATQEYVKAIKSGADGRAPYSSRYIGSMVSDIHRTLLYGGIFMYPGDTKSPNGKLRYLYEVAPLSFIMEQAAGKSTNGSSPCLDMIPKSIHERVPVFMGSPACIDELLAFQKKFNHNHSTTSQHEKDN
Protein: FAD-dependent monooxygenase mdpD (EC 1.-.-.-) (Monodictyphenone synthesis protein D) (Q5BH33)
Organism: Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Function: FAD-dependent monooxygenase; part of the gene cluster that mediates the biosynthesis of monodictyphenone, a prenyl xanthone derivative. The pathway begins with the synthesis of atrochrysone thioester by the polyketide synthase (PKS) mdpG. The atrochrysone carboxyl ACP thioesterase mdpF then breaks the thioester bond and releases the atrochrysone carboxylic acid from mdpG. The atrochrysone carboxylic acid is then converted to atrochrysone which is further transformed into emodin anthrone. The next step is performed by the anthrone oxygenase mdpH that catalyzes the oxidation of emodinanthrone to emodin (By similarity). Emodin is further modified to yield monodictyphenone via several steps involving mdpB, mdpC mdpJ, mdpK and mdpL. These enzymes with xptA, xptB and xptC are also proposed to be involved in the synthesis of shamixanthone from emodin. Especially, direct reduction of emodin by the short chain dehydrogenase mdpC followed by dehydration catalyzed by the scytalone dehydratase-like protein mdpB gives loss of oxygen and formation of chrysophanol intermediate in two simple steps.
Interaction partners:
Sequence:
MTHFPVNIASDKQEFDPERWAKTPTTESSVNGENGTAPTSGLPSRHPSTGISVLIVGAGMGGLMTALECWRKGHDVAGILERSEGPVYSGDIIVMQPSAVSIIRHWPDMLHDMKAEQVHAVVSYETHDGRHIYGPTVPSFNDPEHLETRKGPFVAPAQVRRKFYRMLLRQVARCGLRVEYGKTVKSYFEDEKDGKGGVIIATTGEAEVRVADIVVAADGLKSPSEILIAGQHVPPRSSGLSIYRTAFPKDLAMQNELVRKRWSDSPPIWEYWLGPGMYLGVFVGDDIISFGFTPRDDIVEGTATESWEPDTDPETVAQAMLSGAGDWDPAVLALIRSAPKGAIVHWPLLWRDLRREWTSPAGRVVQVGDSAHSFIPTSGNGGSQALEDAITLATCLQLAGSSQRAYLGTKIYNLLRYERVSCAQKMSFVNSQLKTGTDWDAIWKDPAKIRTRFPKWIFQHDPEAYAYEKFGEAFAHLLDGREFVNTNYPPGHEFRAWTVEEVWRNIADGKRVEDLLDGDWS
Protein: PAP-associated domain-containing protein (Q585X9)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MVNSVFFSFSQHKHVQLVICLNACLFFSAFYICISLALFGNIHRILEAPGVALVRMFGPVDDAERVANSGSQQHGRQASISSPVPSGYAQPSDRREQFTPVSFGGSQANIGSLGTPNMFRKMRRPSSSTSSRRSTLRSTPACTVSHEQAIDTTNVVLVATRPLLKTLARTCRPHPPWCIGMSVPDTVTEEVRLFSSFLRPTALELYCYEAVVTSVTAMLRELWPTAELHPMSTTAAGLPPLKDMTLHFYAKNTVVTPDAKQYTQMHLQSITNNAGFQLEFCYDYRNVMCLLLTDSRSGLRMNVRYGAEACRVEVASRLFASAVASNEACRQTFLLLDALLRQNKILDDTGTNPEALNSEAVATMLVAIFNSYDANDTPDTGRLLMDFFLTYGFCANFDMFSHSVTARGLREPTSKVHPNAQISVLDPSNEGHNLTYRLEKAAHLQAVFNYCYTAISQFAQVEERQLRAQSVLSTIIGGESYWSRVLQLYHEGISPYFEVVNEKKIFLIRAL
Protein: Alanine/arginine aminopeptidase (EC 3.4.11.-) (P37898)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Positive effector of glycogen accumulation. May be involved in nutrient-sensing.
Interaction partners:
- Mitogen-activated protein kinase SLT2/MPK1
Sequence:
MSREVLPNNVTPLHYDITLEPNFRAFTFEGSLKIDLQINDHSINSVQINYLEIDFHSARIEGVNAIEVNKNENQQKATLVFPNGTFENLGPSAKLEIIFSGILNDQMAGFYRAKYTDKVTGETKYMATTQMEATDARRAFPCFDEPNLKATFAVTLVSESFLTHLSNMDVRNETIKEGKKYTTFNTTPKMSTYLVAFIVADLRYVESNNFRIPVRVYSTPGDEKFGQFAANLAARTLRFFEDTFNIEYPLPKMDMVAVHEFSAGAMENWGLVTYRVIDLLLDIENSSLDRIQRVAEVIQHELAHQWFGNLVTMDWWEGLWLNEGFATWMSWYSCNKFQPEWKVWEQYVTDNLQRALNLDSLRSSHPIEVPVNNADEINQIFDAISYSKGSSLLRMISKWLGEETFIKGVSQYLNKFKYGNAKTGDLWDALADASGKDVCSVMNIWTKRVGFPVLSVKEHKNKITLTQHRYLSTGDVKEEEDTTIYPILLALKDSTGIDNTLVLNEKSATFELKNEEFFKINGDQSGIFITSYSDERWAKLSKQANLLSVEDRVGLVADAKALSASGYTSTTNFLNLISNWKNEDSFVVWEQIINSLSALKSTWVFEPEDILNALDKFTLDLVLNKLSELGWNIGEDDSFAIQRLKVTLFSAACTSGNEKMQSIAVEMFEEYANGNKQAIPALFKAVVFNTVARLGGENNYEKIFNIYQNPVSSEEKIIALRALGRFEDKELLERTLSYLLDGTVLNQDFYIPMQGIRVHKKGIERLWAWMQEHWDEIAKRLQPGSPVLGGVLTLGLTNFTSFEALEKISAFYSRKVTKGFDQTLAQALDTIRSKAQWVSRDREIVATYLREHEYDQ