wanglab/gogpt-training-data huggingface dataset:
Protein: 4-coumarate--CoA ligase 2 (4CL 2) (Os4CL2) (EC 6.2.1.12) ((E)-ferulate--CoA ligase) (EC 6.2.1.34) (4-coumaroyl-CoA synthase 2) (Q42982)
Organism: Oryza sativa subsp. japonica (Rice)
Function: Involved in the phenylpropanoid metabolism by mediating the activation of a number of hydroxycinnamates for the biosynthesis of monolignols and other phenolic secondary metabolites. Catalyzes the formation of CoA esters of cinnamate, 4-coumarate, caffeate and ferulate. Is more efficient with substrates in the following order: ferulate > 4-coumarate > caffeate > cinnamate. Cannot convert sinapate to its corresponding CoA ester. Follows a two-step reaction mechanism, wherein the carboxylate substrate first undergoes adenylation by ATP, followed by a thioesterification in the presence of CoA to yield the final CoA thioester (By similarity).
Interaction partners:
- Phenylalanine ammonia-lyase
- tricin synthase
- Phenylalanine ammonia-lyase
- Chalcone synthase 1
- Aldehyde dehydrogenase 1
- Phenylalanine ammonia-lyase
- Os06g0592400 protein
- Hydroxycinnamoyltransferase 1
- Hydroxycinnamoyltransferase 2
- Aldehyde dehydrogenase 1
Sequence:
MITVAAPEAQPQVAAAVDEAPPEAVTVFRSKLPDIDIPSHLPLHEYCFARAAELPDAPCLIAAATGRTYTFAETRLLCRRAAAALHRLGVGHGDRVMVLLQNCVEFAVAFFAASFLGAVTTAANPFCTPQEIHKQFKASGVKLILTQSVYVDKLRQHEAFPRIDACTVGDDTLTVITIDDDEATPEGCLPFWDLIADADEGSVPEVAISPDDPVALPFSSGTTGLPKGVVLTHRSVVSGVAQQVDGENPNLHMGAGDVALCVLPLFHIFSLNSVLLCAVRAGAAVALMPRFEMGAMLGAIERWRVTVAAVVPPLVLALAKNPFVERHDLSSIRIVLSGAAPLGKELEDALRARLPQAIFGQGYGMTEAGPVLSMCPAFAKEPTPAKSGSCGTVVRNAELKVVDPDTGFSLGRNLPGEICIRGPQIMKGYLNDPEATAATIDVEGWLHTGDIGYVDDDDEVFIVDRVKELIKFKGFQVPPAELESLLIAHPSIADAAVVPQKDDVAGEVPVAFVVRAADSDITEESIKEFISKQVVFYKRLHKVHFIHAIPKSASGKILRRELRAKLAAC
Protein: Slit homolog 1b precursor (Slit1b) (Q3Y6S4)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
Sequence:
MPDTERSRPSSGLWIWALLLSLFLSGRSGACPPHCSCTGSTVDCHGLAFKSVPRNIPKTTERLDLNANNLTHIGKDDFAGLKHLRILHLMDNQIVSIDRGAFSDLKELDRLRLNRNRLQQLPELLFLKNPALSRLDLSENNIQMIPRRAFRGATDIKNLQLDKNHISCIEDGAFRAMRVLEVLTLNNNNISAIPISSFNHMPKLRTFRLHWNSLRCDCQLSWLSQWLRQRPALGLYTQCSSPAHLHGLNLAELQKKDFTCAGALDSSPQPCGLASGSCPPMCSCTNNIVDCRGKGLTAIPANMPESMTEIRLEQNGIKSVPPGAFSSYKRLRRIDLSNNQISEIAPDAFHGLRSLNSLVLYGNKITDLPRGVFDGLSALELLLLNANKIHCVRVNVFQDLENLSLLSLYDNKIQTLAKGTFAPLKSIQTLHLAQNPFVCDCGLKWLADFLRSNPIETSGARCSSPRRLANKRISQIKSKKFRCSAAKEQYYIPGSEDTRMNKDCNSKPVCPPKCRCEATVVDCSNLRLTKFPEHLPLSTTELRLNNNDLSILEATGLFRPLTHLKKINLSNNKITEIEDGAFEGASSVVELHLTANLLVSVRGGMFRGMDGLRMLMLRNNHIRCVHNSSFSGLQNVRLLSLYDNQLSTIMPGAFDSLPNLSTLNLLANPFSCDCRLSWLGEWLRSRQIVTGNPRCQNPAFLREIPLQDVAKPDFICDKDVLEQDVSCIPKPQCPEQCTCVDSVVRCSNKHLSALPRGVPLNVTELYLDGNVFVSIPQELSAFRQLQLLDLSNNKISSLTNTSFTNMSQLTTLILSYNALRCIPPLVFGGLSSLRLLSLHGNNISELHQQIFRDAASLSHLAIGANPLYCDCRLRWLSDWVKSGYKEPGIARCAGPQGMEGKLLLTTPGNTFQCTGPVDASVSGKCSPCSSNPCQNQGRCHNDPLHQYKCSCPQGYKGRNCELSISACEANPCVNGGTCRPEESRRGFRCVCPLGFEGLFCELDVDDCVDHQCVNGTICVDGVGNYSCVCAQPFSGQKCEEYEEDLCYPGQNPCQRGSTCIPTVSGPKCICPPGFVGDDCSVDYNECEGHYCQNGARCVDHVAGYTCVCPAGYSGRLCEASVSACDLLQCVNGAPCEEISGTAVCQCLPGFNGLRCEKLLSVNFIDRDSYLLLLRDATQSTHNNITLQVSTAEDNGILLYNGVNEHIAVELHDGHVKVTYDAGRQPGSTIYSSEIVNDGQFHTVELVTYERMVNLSIDGGLPTTLDSSGHIQPLTRDAPLYVGGMPENAKSLSSNHWPPVNGSSFQGCIRNLYINNELQDFTQTQMKPGVVPGCQACQELLCVNGLCQPDSAIGPVCHCQPGWGGKHCDQILLTAAAATNPCQKHKCVHGVCVAVDLQSYRCECVEGFHGQLCSQQDPCTALSCQHGLCQISPTGQPQCVCDSGYSGQLCDIVSPCQGEPVRDFHRVQRGDVQCRSTLPMSWTECRGGCRADSGLCCVGLRVRRRRYGFECDDGTTFTQEVEKTVECGCGKCV
Protein: Histone-lysine N-methyltransferase, putative (EC 2.1.1.43) (Q8I5R3)
Organism: Plasmodium falciparum (isolate 3D7)
Interaction partners:
Sequence:
MILFKRNFHNYFANNFIKDLFKKSQHISFNDIQKKIYIGKSSLGGLGVFSLEGIKKNEIIEICPTVSICNEEIPRNLVDYLYEGKEPSKNKAIVDIIINRKKETSNYKLLPLGYGILYNHSDIPNAYVEIHKINKNQIKQKQDVTVSNNVMIVYAYNNIQKDDEILISYGHSWWKVSS
Protein: tRNA-dihydrouridine(16/17) synthase [NAD(P)(+)] (EC 1.3.1.88) (mRNA-dihydrouridine synthase DUS1) (EC 1.3.1.-) (tRNA-dihydrouridine synthase 1) (P53759)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Catalyzes the synthesis of dihydrouridine, a modified base found in the D-loop of most tRNAs. Specifically modifies U16 and U17 in cytoplasmic tRNAs. Also able to mediate dihydrouridylation of some mRNAs, thereby affecting their translation (By similarity).
Interaction partners:
- tRNA
- tRNA
- tRNA
- tRNA
- tRNA
- tRNA
- U3 small nucleolar RNA-associated protein 21
- Cytoplasmic 60S subunit biogenesis factor REI1
- tRNA
- Regulator of ribosome biosynthesis
Sequence:
MTEPALSSANNALMQKLTGRQLFDKIGRPTRIVAPMVDQSELAWRILSRRYGATLAYTPMLHAKLFATSKKYREDNWSSLDGSSVDRPLVVQFCANDPEYLLAAAKLVEDKCDAVDLNLGCPQGIAKKGHYGSFLMEEWDLIHNLINTLHKNLKVPVTAKIRIFDDCEKSLNYAKMVLDAGAQFLTVHGRVREQKGQKTGLANWETIKYLRDNLPKETVFFANGNILYPEDISRCMEHIGADAVMSAEGNLYNPGVFNVGQTKNKEKIFPRVDKIIREYFQIVKECQESKASKTAMKSHFFKILRPFLPHHTDIRSTLATMNAKATWEEWEEQVVKPVEKVVQEIFEQPDIAIKDEITIGEKQSWGGSYRTVPYWRCQPYFRPVNGITGDKRVMQGLIDESVNKKRKADVPLESADKKKDVKA
Protein: Low-density lipoprotein receptor (LDL receptor) (P35951)
Organism: Mus musculus (Mouse)
Function: Binds LDL, the major cholesterol-carrying lipoprotein of plasma, and transports it into cells by endocytosis. In order to be internalized, the receptor-ligand complexes must first cluster into clathrin-coated pits.
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:P01130}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:P01131}. Membrane, clathrin-coated pit {ECO:0000269|PubMed:11247302}. Golgi apparatus {ECO:0000250|UniProtKB:P01130}. Early endosome {ECO:0000250|UniProtKB:P01130}. Late endosome {ECO:0000250|UniProtKB:P01130}. Lysosome {ECO:0000250|UniProtKB:P01130}. Note=Rapidly endocytosed upon ligand binding. {ECO:0000269|PubMed:12169628}.
Interaction partners:
- Low density lipoprotein receptor adapter protein 1
- E3 ubiquitin-protein ligase MYLIP
- Proprotein convertase subtilisin/kexin type 9
- Apolipoprotein B-100
- Disabled homolog 2
Sequence:
MSTADLMRRWVIALLLAAAGVAAEDSCSRNEFQCRDGKCIASKWVCDGSPECPDGSDESPETCMSVTCQSNQFSCGGRVSRCIPDSWRCDGQVDCENDSDEQGCPPKTCSQDDFRCQDGKCISPQFVCDGDRDCLDGSDEAHCQATTCGPAHFRCNSSICIPSLWACDGDVDCVDGSDEWPQNCQGRDTASKGVSSPCSSLEFHCGSSECIHRSWVCDGEADCKDKSDEEHCAVATCRPDEFQCADGSCIHGSRQCDREHDCKDMSDELGCVNVTQCDGPNKFKCHSGECISLDKVCDSARDCQDWSDEPIKECKTNECLDNNGGCSHICKDLKIGSECLCPSGFRLVDLHRCEDIDECQEPDTCSQLCVNLEGSYKCECQAGFHMDPHTRVCKAVGSIGYLLFTNRHEVRKMTLDRSEYTSLLPNLKNVVALDTEVTNNRIYWSDLSQKKIYSALMDQAPNLSYDTIISEDLHAPDGLAVDWIHRNIYWTDSVPGSVSVADTKGVKRRTLFQEAGSRPRAIVVDPVHGFMYWTDWGTPAKIKKGGLNGVDIHSLVTENIQWPNGITLDLSSGRLYWVDSKLHSISSIDVNGGNRKTILEDENRLAHPFSLAIYEDKVYWTDVINEAIFSANRLTGSDVNLVAENLLSPEDIVLFHKVTQPRGVNWCETTALLPNGGCQYLCLPAPQIGPHSPKFTCACPDGMLLAKDMRSCLTEVDTVLTTQGTSAVRPVVTASATRPPKHSEDLSAPSTPRQPVDTPGLSTVASVTVSHQVQGDMAGRGNEEQPHGMRFLSIFFPIALVALLVLGAVLLWRNWRLKNINSINFDNPVYQKTTEDELHICRSQDGYTYPSRQMVSLEDDVA
Protein: Zinc finger protein C11D3.17 (Q10096)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
Sequence:
MVDHVSENSTNVLSAKRKLTEPSLIDSKRVFPCDQCAKRFTRHENLTRHKACHSKAEPIPCPYCEIKCKRKDLLKRHIQRFHNDKSVIEEGSKDVLDVKAAASQQEDNMKIVLPSFDAIDVPKAYHPSLRPYFTILPLIPSDFLEHYIEGYFEWFHPVFPFIHQASFNSENVAASFLRSLVVIACLCTGIESDFSMALLFWDSGFHVLQLYLQGDPERVKKAWVFQSRLLFCTASLFEKTACFSGIGHVLLKDLVHESRTFGWTKLNWSVEGDTDISNLIDLECIRRSVFCLYILEWFLALIFNKPPSLSVLELQMPLPISSALWSSKELLSKDYWRPNPLNPRDALSILVNGPLLLEETNISGFVLLFAIFEFIRDEAKLSMIGLPRQPNRSYEIMLQHLKVSMELSNPCAKTSSIFLCLWHLVLTYYYLPDPLFLRSITLTDLESATSYFKDDSWMDDDYISPCMTTYNLTMGWENVIWGLRYAETELTKFKFDLPVPHLTLFRIFLQGLYALRDFDQISTSSLQTFTMLWKKLSTSLNMKEDAQNTAPSTCVKEFSAFVASALDVEGGWGIGPLLTKAFRPT
Protein: Cilia- and flagella-associated protein 157 (Q5JU67)
Organism: Homo sapiens (Human)
Function: Specifically required during spermatogenesis for flagellum morphogenesis and sperm motility. May be required to suppress the formation of supernumerary axonemes and ensure a correct ultrastructure.
Subcellular location: Cytoplasm, cytoskeleton, cilium basal body {ECO:0000250|UniProtKB:Q0VFX2}.
Interaction partners:
Sequence:
MAPKKSVSKAGKELEVKKKGGKKEPVVAVEPPLAKEMKEFYHIQIRDLEDRLARYQRKWDELAVQEKMFRQEFEQLANNKKEIVAFLKRTLNQQVDEITDLNEQLQNLQLAKEMEKDAFEAQLAQVRHEFQETKDQLTTENIILGGKLAALEEFRLQKEEVTDKFTLLEEQVRKQENEFRDYAYNLEKKSVLDKDRLRKEIIQRVNLVANEFHKVTTNRMWETTKRAIKENNGITLQMARVSQQGMKLLQENEQLKGRQNNLCKQLELLENTQKVMARHKRGHQKIILMLTKKCQEQQQDTKEAEELRLLLSQLEQRSLQLQVDNQALKSQRDQLSLQLEQQQVDLQRLQQELANEQKVRASLEAALVQATSFLQNILQMHRDEEDSDVDVTFQPWHKEMLQQLLVMLSSTVATRPQKAACPHQESQSHGPPKESRPSIQLPRTGSLLPQLSDITPYQPGDLGLVPRQVHIPPNPQDLRLLSYITRVGTFRAHSSPEMRAPGSLKRLEKFSLPEVPLRPK
Protein: Tyrosine--tRNA ligase (EC 6.1.1.1) (Tyrosyl-tRNA synthetase) (Q8IIJ2)
Organism: Plasmodium falciparum (isolate 3D7)
Interaction partners:
- tyrosine--tRNA ligase
- glycine--tRNA ligase
- D-aminoacyl-tRNA deacylase
- Isoleucine--tRNA ligase, putative
- isoleucine--tRNA ligase
- leucine--tRNA ligase
- leucine--tRNA ligase
- threonine--tRNA ligase
- Proline--tRNA ligase
- Proline--tRNA ligase, putative
Sequence:
MIILKVLFIYNGLIQIIRCYKKFAPHRLNNIIHENNKNNIGTYDIKSKALKKLYERKLIHYVSDIRNIDKILYHNENEKEKKNRKSVYAGIDLTCKYLHLGNLVPLITLDILRNHNTDVIILLGNSTTQIGDPSFQKVERQKTLEKDILENEENIRRTIIELFLQREICEEDMNELIKKSNIERDKEFIYESDNKGSLIILKNSLWYDKMNIIDFLKYGEYFSINKLLRKECFLNKIKKNLTLKDLNYITLQSFDFLHLFNKFKTCIQIGGSDQWGNIQSGIELAQYISNTQLYGLTTNLLVYKNNIKYSKSQFNENKRLPIWIDKNYNSPYLFWNFLRNVEDQKVQSYIDMLTNLKININQEIETVYNPMDTNLNEILDETLDDSNKKKKNNDNNNNNNNVKDINITTEHNNYSNDISLEKSYEEKINQAKKQLSDSVTSYIFGEHTVKKIHKMKDVLKNNEFHKINNIDDIKVFPYVEITMEHINKKQINISDLLKKFDIASTNKEAKEKISQNCIYLNELLINDSKYSLNINNFIKLHNNYYAILRLGKRTSYSIIIK
Protein: SNARE associated Golgi protein family (F4IBM1)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
Sequence:
MAPTRILTRDEELGVISDDDDSPSGKRSKLDRFPLSRWELAVSLGVFLVFSSGLCCIYMTMPAAEFGKLKLPRSLADLRLLKDNLANYANEYPAQFVLGYCATYIFMQTFMIPGTIFMSLLAGALFGVFKGVVLVVFNATAGATSCFFLSKLIGRPLITWLWPDKLRFFQAEISKRRDKLLNYMLFLRITPTLPNLFINLASPIVDVPFHVFFLATLIGLIPAAYITVRAGLAIGDLKSVKDLYDFKTFQGEASLQYTWPNIQCHTENKNTLNLFRGHNRTKLLIRLLVTCQITEIIQFFVQDERP
Protein: DNA-binding heavy metal response regulator (Q87Z28)
Organism: Pseudomonas syringae pv. tomato (strain ATCC BAA-871 / DC3000)
Interaction partners:
- Sensor protein
- Sensor protein
- Sensor protein
- DNA-binding heavy metal response regulator
- DNA-binding heavy metal response regulator
- histidine kinase
- histidine kinase
- histidine kinase
- histidine kinase
- histidine kinase
Sequence:
MHILLIEDDTKTGEYLKKGLGESGYKVDWTQHGADGLHLALENRYDLIVLDVMLPGIDGWQIIEVLRARQDVPVLFLTARDQLQDRIRGLELGADDYLVKPFSFTELLLRIRTILRRGVVREADHFHLADLELDLLRRRVTRQQQVIVLTNKEFALLHLLLRREGDVLSRAQIASEVWDMNFDSDTNVVDVAIKRLRSKVDLPYPVKLIHTVRGIGYVCEVRPCDASLP
Protein: Uncharacterized protein (Q38AS4)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- PTHB1 N-terminal domain-containing protein
- Bardet-Biedl syndrome 8 protein
- FG-GAP repeat protein, putative
- FG-GAP repeat protein, putative
- BBSome complex member BBS5 PH domain-containing protein
- Uncharacterized protein
- Telomerase-associated protein, putative
Sequence:
MEKKGSGRGAGARESKSSAVAATCKHQHPLPPSKPGGVEGTGAVETGTIKEEVASRDKIRERRNWLIYELYVRQEYSQCCAVIDAQLAECNGTCEYALFVKGLLTRRSGDLTISFQHFQKALTLNPGSPACLQQLAQTSLLLGKFYEAIESFQRAEEARAARGFRKDWSLQYGVGLCYEYMREYRKAEEAFVSSMQIQRFDCTVLRLSKVLVLQKQHSRAISLLEEAVLGSPDNPDMLTVLGLLYLRVDRPAKAFNYLGRCLILNSSDSRATMAAASIMQENGEFGVALNKYRVAVPKLPSSACLWSNIGMCFFGQKNMHAAVACLRRAASLSPFEWRIAYNLGLVFLHLKQYASAFHYLSASTHLHGKYALAFMHIGVCLALMSDSDNACAAYNRAISIQDDPLIRLNYCITLVHCGKDAEARDQLDKFIQMRERGKENSQQHPQLDVGPVVPRALTLLTAKLRK
Protein: Leucine-rich repeat and fibronectin type-III domain-containing protein 5 (D4A1J9)
Organism: Rattus norvegicus (Rat)
Function: Cell adhesion molecule that mediates homophilic cell-cell adhesion in a Ca(2+)-independent manner. Promotes neurite outgrowth in hippocampal neurons (By similarity).
Subcellular location: Membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}.
Interaction partners:
- Interleukin-1 receptor accessory protein-like 1
- Adhesion G protein-coupled receptor L3
- Adhesion G protein-coupled receptor L1
- Adhesion G protein-coupled receptor L2
Sequence:
MEKFLFYLFLIGIAVRAQICPKRCVCQILSPNLATLCAKKGLLFVPPNIDRRTVELRLADNFVTNIKRKDFANMTSLVDLTLSRNTISFITPHAFADLRNLRALHLNSNRLTKITNDMFSGLSNLHHLILNNNQLTLISSTAFDDVFALEELDLSYNNLETIPWDAVEKMVSLHTLSLDHNMIDNIPKGTFSHLHKMTRLDVTSNKLQKLPPDPLFQRAQVLATSGIISPSTFALSFGGNPLHCNCELLWLRRLSREDDLETCASPALLTGRYFWSIPEEEFLCEPPLITRHTHEMRVLEGQRATLRCKARGDPEPAIHWISPEGKLISNATRSLVYDNGTLDILITTVKDTGAFTCIASNPAGEATQTMDLHIIKLPHLLNSTNNIHEPDPGSSDISTSTKSGSNASSSNGDTKMSQDKIVVAEASSSTALLKFNFQRNIPGIRMFQIQYNGTYDDTLVYRMIPPTSKTFLVNNLASGTMYDLCVLAIYDDGITSLTATRVVGCIQFTTEQDYVRCHFMQSQFLGGTMIIIIGGIIVASVLVFIIILMIRYKVCNNNGQHKVTKVSNVYSQTNGAQMQGCSVTLPQSMSKQAMGHEENAQCCKVASDSAIQSSETCSSQDSSTTTSALPPTWTSSAPVSQKQKRKTGTKPSAEPQSEAVTNVESQNTNRNNSTALQLASCPPDSVTEGPTSQRAHTKPNALLTNVDQNVQETQRLESI
Protein: Malate dehydrogenase (EC 1.1.1.37) (Q383F3)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- Citrate synthase
- fumarate hydratase
- Malic enzyme
- Malic enzyme
- fumarate hydratase
- Aspartate aminotransferase
- aspartate transaminase
- phosphoenolpyruvate carboxykinase
- NAD-specific glutamate dehydrogenase
- Malate dehydrogenase
Sequence:
MSNTCKRVAVTGAAGQIGYSLLPLIAAGRMLGFDQRVQLQLLDISPALKALEGIRAELMDCSFPLLDGVVITDEPKVAFDKADIAILCGAFPRKPGMERRDLLQTNAKIFSEQGRVLGEVASPNCRVCVVGNPANTNALILLRESKGKLNPRFVTALTRLDHNRATAQVAERARARVEEVKNCIIWGNHSGTQVPDVNSATVGGKPARAAVDNGAFFDNEFITIVQERGAEIMKLRGLSSALSAAKAIVDHVHDWMLGTPSGTHVSMAVYSDGNPYGVPGGLIFSFPVTCSGGEWQIVSGLNVTPAISERIKATTTELEEERREVSTA
Protein: Calcium/calmodulin-dependent protein kinase II inhibitor 2 (CaM-KII inhibitory protein) (CaM-KIIN) (Q78WH7)
Organism: Mus musculus (Mouse)
Function: Potent and specific cellular inhibitor of CaM-kinase II (CAMK2) (By similarity). Traps Ca(2+)/calmodulin on CAMK2 (By similarity).
Subcellular location: Nucleus {ECO:0000250|UniProtKB:Q9Z2N6}. Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q9Z2N6}. Synapse {ECO:0000269|PubMed:28642476}. Note=Excluded from nucleus when coexpressed with activated CAMK2. {ECO:0000250|UniProtKB:Q9Z2N6}.
Interaction partners:
Sequence:
MSEILPYGEDKMGRFGADPEGSDLSFSCRLQDTNSFFAGNQAKRPPKLGQIGRAKRVVIEDDRIDDVLKGMGEKPPSGV
Protein: Metabotropic glutamate receptor-like protein C (Q54SH7)
Organism: Dictyostelium discoideum (Social amoeba)
Subcellular location: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
- Cytoplasmic dynein 1 light intermediate chain 1
Sequence:
MKMKIIFLILILIFSINIIKCDKEFKMLTLLTAQVDDLGFNNMINQGRIEVAKGMNIEDSRLLVVEGFNETFKHLLPIVQNDDIDLVICSSSGHLQACRAIAEMYINSTTIKTQFLVRGSSSPTRNLIYISYNYASANYISGYFAALFSKTGKIGFVSPGQAANNNDSFVYAFWVGARQVNPDIKFYYYNIGNYLDVDKTVAATNDLLDMGCDVVGNTLDDFSTGDASIARGFPAIGTNGFPQRHVYGENVIYSYSYNWTKFFLPIAESVKSGNTNNSQWYADFDFDENKNFYHLDYGFEVNQSILDKMNTEIDYLKSTDRMSHPYYCNELIPQYAKENNLKLANVTGITLPIGCVTHQTFLSINKPFPGMTYLGNYKIKLVEVEFSQSLQYGFSITTGVLIAITIIMMLGIVRYKSTPSIRSASPIFLNFILAGGIIVYIGIIVWVGPANDHQCNARLWLVTLGFSTLIGSLVVKNFRIWLIFDNPELKSISITNYQLFPWVGACLVINIILMSILTSVGDLREIDAQGIDSLGKYEFMKVCKMNSSGASTLYTILAYFAALLLVGVFVSWKIRIVDIQEFNESKAIANTLYAISFCLFVIVPLMISPQDKQSETIVLCTAGLFITTAALLIIFTPKFWRVFTLGDGGTNDMFRKKQSNVATARAESSKSSSGPKLNRRGNLVSDDFTDTETSISEKKVNVVAGAVLAEFTDDTISEFDDNNIEQDNDNDNDNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNTNTSQPNDEKVEEKQQNDTEEEDKNQ
Protein: Phosphopantothenoylcysteine decarboxylase subunit VHS3 (Viable in a HAL3 SIT4 background protein 3) (Q08438)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Component of the phosphopantothenoylcysteine decarboxylase (PPCDC) involved in the coenzyme A synthesis. Acts as an inhibitory subunit of protein phosphatase PPZ1, which is involved in many cellular processes such as G1-S transition or salt tolerance.
Interaction partners:
- Coenzyme A biosynthesis protein 3
- Phosphopantothenoylcysteine decarboxylase subunit SIS2
- Serine/threonine-protein phosphatase PP-Z1
- Dephospho-CoA kinase CAB5
- Phosphopantothenate--cysteine ligase CAB2
- Phosphopantetheine adenylyltransferase
- Serine/threonine-protein phosphatase PP-Z2
- Serine/threonine-protein phosphatase PP1-1
- Pantothenate kinase CAB1
Sequence:
MTNKSSLKNNRKGVASNTLSGAEQANIGSSAMPDTNSTGPFSSVSSLDTPVVRKSTSPTGSQTKSIMNASGTSGAVVSNTPEPGLKRIPTVTFSDPKLGSLRSDVEQTPPNQVARQSSEKKATSVHIAAEGANQGRNLKDINTKVPKDGEASASSFSTPTSILSNADMGNNISSLLAKKLSFTGGTDSILNSDNSSDSPRKEHPHFYVEDPLHTPSVRSRSNSTSPRPSVVVNTFNPINIEREGSISKTGEPTLLESVLEEAMSPNAVSNPLKRENIMTNMDPRLPQDDGKLHVLFGATGSLSVFKLKHMIRKLEEIYGRDKICIQVILTNSATKFFAMKYMRKNKKQHNSIDTSFNSTNSNAGNITGNKKKVASLEKFSIQKTSSNSAASQTNNKQEEEKQMASTTGFPSTLGGSRTYSNSSNVVSQHPQIELPAHIQFWTDQDEWDVWRQRTDPVLHIELRRWADILVVAPLTANTLAKIALGLCDNLLTSVIRAWNPTFPIFLAPSMGSGTFNSIMTKKHFRIIQEEMPWVTVFKPSEKVMGINGDIGLSGMMDANEIVGKIVVKLGGYPDVSAGKEEEEDEDNDEEDDNKKNDTGGKDEDNDDDDDDDDDDDDDDDDDDDDDDDDDDDDDDDDDDDDDDDDDDDDDEDDEDEDEDDEGKKKEDKGGLQRS
Protein: NAD(P)-binding Rossmann-fold superfamily protein (Q949S7)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- Ubiquinone biosynthesis protein
- Ubiquinone biosynthesis protein COQ4 homolog, mitochondrial
- 4-hydroxybenzoate polyprenyltransferase, mitochondrial
- Polyketide cyclase / dehydrase and lipid transport protein
- NADH dehydrogenase iron-sulfur protein 1, mitochondrial
- NADH dehydrogenase flavoprotein 1, mitochondrial
- Probable NADH dehydrogenase 1 alpha subcomplex subunit 12
- NADH dehydrogenase 1 beta subcomplex subunit 9
- Protein ABC transporter 1, mitochondrial
- NADH dehydrogenase iron-sulfur protein 4, mitochondrial
Sequence:
MLRSLIWKRSQAYSSVVTMSSISQRGNERLLSEVAGSHSRDNKILVLGGNGYVGSHICKEALRQGFSVSSLSRSGRSSLHDSWVDDVTWHQGDLLSPDSLKPALEGITSVISCVGGFGSNSQMVRINGTANINAVKAAAEQGVKRFVYISAADFGVINNLIRGYFEGKRATEAEILDKFGNRGSVLRPGFIHGTRQVGSIKLPLSLIGAPLEMVLKLLPKEVTKIPVIGPLLIPPVNVKSVAATAVKAAVDPEFASGVIDVYRILQHGH
Protein: Citrate synthase (Q80X68)
Organism: Mus musculus (Mouse)
Subcellular location: Mitochondrion matrix {ECO:0000256|ARBA:ARBA00004305}.
Interaction partners:
- Aconitate hydratase, mitochondrial
- ATP-citrate synthase
- Cytoplasmic aconitate hydratase
- Malate dehydrogenase, mitochondrial
- Pyruvate carboxylase, mitochondrial
- Malate dehydrogenase, cytoplasmic
- Fumarate hydratase, mitochondrial
- Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex, mitochondrial
- Acetyl-coenzyme A synthetase 2-like, mitochondrial
- Acetyl-coenzyme A synthetase, cytoplasmic
Sequence:
MALLTAAAWFLGTKNPPCLVLAARHASASSTNLKDVLRNLIPKEQARIKTFRKKHGKTVVGQITVDMMYGGMRGMKGLVYETSVLDPDEGIRFRGYSIPECQKLLPKAKGGKEPLPEGLFWLLVTGQMPTEEQVSWLSQEWVKRAALPSHVVTMLDNFPTKLHPMSQLSAAITVLNNESNFARAYAQGMNRTKYWELTYEDCMDLLAKLPCVAAKIYRNLYREDRNIEAIDSKLDWSHNFTNMLGYTDPQFTELMRLYLTIHSDHEGGNVSAHTSHLVGSALSDPYLSFAAALNGLAGPLHGLANQEVLVWLTQLQKEVGEDASDEKLKNYIWNTLNSGRVVPGYGHAVLRKTDPRYSCQREFALKHLPKDPMFKLVGQLYKIVPDILLEQGKAKNPWPNVDAHSGVLLQYYGMREMNYYTVLFGVSRALGVLSQLIWSRALGFPLERPKSMSTDALMKFVNSESG
Protein: R2D2 (Q2Q0K9)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MDNKSAVSALQEFCARTQINLPTYSFIPGEDGGYVCKVELLEIEAIGNGRSKRDAKHLAASNILRKIQLLPGIHGLMKDSTVGDLGEELTNLNRDMVKELRDYCVRREMPLPSIEIVQQSGTPSAPEFVACCSVASIVRYGKSDKKKDARQRAAIEMLALISSNSDNLRPDQMQVASTSKLKVVDMEESMEELEALRRKKFTTYWELKEAGSVDHTGMRLCDRHNYFKNFYPTLKKEAIEAINSDEYESSKDKAMDVMSSLKITPKISEVESSSLVPLLSVELNCAFDVVLMAKETDIYDHIIDYFRTMLI
Protein: 3-phosphoshikimate 1-carboxyvinyltransferase, chloroplastic (EC 2.5.1.19) (5-enolpyruvylshikimate-3-phosphate synthase) (EPSP synthase) (EPSPs) (P05466)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Catalyzes the transfer of the enolpyruvyl moiety of phosphoenolpyruvate (PEP) to the 5-hydroxyl of shikimate-3-phosphate (S3P) to produce enolpyruvyl shikimate-3-phosphate and inorganic phosphate.
Subcellular location: Plastid, chloroplast {ECO:0000255}.
Interaction partners:
- Chorismate synthase, chloroplastic
- Shikimate kinase 1, chloroplastic
- Shikimate kinase 2, chloroplastic
- 3-dehydroquinate synthase, chloroplastic
- Bifunctional 3-dehydroquinate dehydratase/shikimate dehydrogenase, chloroplastic
- Chorismate mutase 1, chloroplastic
- Chorismate mutase 2
- Chorismate mutase 3, chloroplastic
- Phospho-2-dehydro-3-deoxyheptonate aldolase 2, chloroplastic
- 3-phosphoshikimate 1-carboxyvinyltransferase
Sequence:
MAQVSRICNGVQNPSLISNLSKSSQRKSPLSVSLKTQQHPRAYPISSSWGLKKSGMTLIGSELRPLKVMSSVSTAEKASEIVLQPIREISGLIKLPGSKSLSNRILLLAALSEGTTVVDNLLNSDDINYMLDALKRLGLNVETDSENNRAVVEGCGGIFPASIDSKSDIELYLGNAGTAMRPLTAAVTAAGGNASYVLDGVPRMRERPIGDLVVGLKQLGADVECTLGTNCPPVRVNANGGLPGGKVKLSGSISSQYLTALLMSAPLALGDVEIEIVDKLISVPYVEMTLKLMERFGVSVEHSDSWDRFFVKGGQKYKSPGNAYVEGDASSASYFLAGAAITGETVTVEGCGTTSLQGDVKFAEVLEKMGCKVSWTENSVTVTGPPRDAFGMRHLRAIDVNMNKMPDVAMTLAVVALFADGPTTIRDVASWRVKETERMIAICTELRKLGATVEEGSDYCVITPPKKVKTAEIDTYDDHRMAMAFSLAACADVPITINDPGCTRKTFPDYFQVLERITKH
Protein: Caldesmon 1b (E7EZ62)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
- Mitogen-activated protein kinase
- Mitogen-activated protein kinase
- Lymphocyte specific protein 1.
- Rho guanine nucleotide exchange factor
- Ankyrin repeat and death domain-containing 1A.
- Sosondowah ankyrin repeat domain family d.
- Transmembrane protein 151A.
- Transmembrane protein 151A.
- Si:ch211-250g4.3.
- Ras association domain family member 4.
Sequence:
MDEDFDFERRRELRRQKREEMQREAEKMNSYDDDEEAARERRRRARQERLRNMENEESSNITTESNSTETSSLINSSEPAEDDDDQALLERIAKREERRQKRMKEALERQKELDPTITNGTESTSAATENEPNTRRDDQESSRNDLTSTETNSWKEKEELKVEEKLQERNVDVEETVPVQEETVPEEPKASLEEINKPDDEDRPTRSYLREQESMEEKPKEPTNKVVEEKSKPSFLRDRLKVSTKPQDLPDSTAKAKKQESTLSPSRLRSPETEKQDPIAKLEAERKLQELKRRRNETDSEALEKMKQKQQTAEAELEELRKKREERKKVLEEEEKQKKQQQADKRAKEEEERRKMKEEIERRRAEAAEKKKQKEESKEGSKVAFIAPKGASAKIGEKAEFLNKSALKSPIKTSHTPLVCKIGNRLEQYTSAVQTKEVTKSPKSPVDVPVAEGLRSIKSMWEKGNVVNPTPSPASPPVATKETAGLNIGVAGRINSWKTKTPEPKPAEPKPAPEPEKTPAKTEQKPAEVTKPRGSWETKGSTPAKVFAAKSKFVTNGTRK
Protein: Anthranilate synthase alpha subunit 2, chloroplastic (OsASA2) (EC 4.1.3.27) (Q9XJ29)
Organism: Oryza sativa subsp. japonica (Rice)
Function: Part of a heterotetrameric complex that catalyzes the two-step biosynthesis of anthranilate, an intermediate in the biosynthesis of L-tryptophan. In the first step, the glutamine-binding beta subunit of anthranilate synthase (AS) provides the glutamine amidotransferase activity which generates ammonia as a substrate that, along with chorismate, is used in the second step, catalyzed by the large alpha subunit of AS to produce anthranilate.
Subcellular location: Plastid, chloroplast {ECO:0000255}.
Interaction partners:
- Anthranilate synthase beta subunit 1, chloroplastic
- Anthranilate synthase beta subunit 2, chloroplastic
- anthranilate phosphoribosyltransferase
- indole-3-glycerol-phosphate synthase
- Os02g0131200 protein
- indole-3-glycerol-phosphate synthase
- indole-3-glycerol-phosphate synthase
- phosphoribosylanthranilate isomerase
- Anthranilate synthase alpha subunit 1, chloroplastic
- Tryptophan synthase
Sequence:
MESIAAATFTPSRLAARPATPAAAAAPVRARAAVAAGGRRRTSRRGGVRCSAGKPEASAVINGSAAARAAEEDRRRFFEAAERGSGKGNLVPMWECIVSDHLTPVLAYRCLVPEDNMETPSFLFESVEQGPEGTTNVGRYSMVGAHPVMEVVAKEHKVTIMDHEKGKVTEQVVDDPMQIPRSMMEGWHPQQIDQLPDSFTGGWVGFFSYDTVRYVEKKKLPFSGAPQDDRNLPDVHLGLYDDVLVFDNVEKKVYVIHWVNLDRHATTEDAFQDGKSRLNLLLSKVHNSNVPKLSPGFVKLHTRQFGTPLNKSTMTSDEYKNAVMQAKEHIMAGDIFQIVLSQRFERRTYANPFEVYRALRIVNPSPYMAYVQARGCVLVASSPEILTRVRKGKIINRPLAGTVRRGKTEKEDEMQEQQLLSDEKQCAEHIMLVDLGRNDVGKVSKPGSVKVEKLMNIERYSHVMHISSTVSGELDDHLQSWDALRAALPVGTVSGAPKVKAMELIDELEVTRRGPYSGGLGGISFDGDMLIALALRTIVFSTAPSHNTMYSYKDTERRREWVAHLQAGAGIVADSSPDDEQRECENKAAALARAIDLAESAFVDKE