wanglab/gogpt-training-data huggingface dataset:
Protein: Phosphatidylcholine-sterol acyltransferase (EC 2.3.1.43) (1-alkyl-2-acetylglycerophosphocholine esterase) (EC 3.1.1.47) (Lecithin-cholesterol acyltransferase) (Phospholipid-cholesterol acyltransferase) (Platelet-activating factor acetylhydrolase) (PAF acetylhydrolase) (P16301)
Organism: Mus musculus (Mouse)
Function: Central enzyme in the extracellular metabolism of plasma lipoproteins. Synthesized mainly in the liver and secreted into plasma where it converts cholesterol and phosphatidylcholines (lecithins) to cholesteryl esters and lysophosphatidylcholines on the surface of high and low density lipoproteins (HDLs and LDLs). The cholesterol ester is then transported back to the liver. Also produced in the brain by primary astrocytes, and esterifies free cholesterol on nascent APOE-containing lipoproteins secreted from glia and influences cerebral spinal fluid (CSF) APOE- and APOA1 levels. Together with APOE and the cholesterol transporter ABCA1, plays a key role in the maturation of glial-derived, nascent lipoproteins. Required for remodeling high-density lipoprotein particles into their spherical forms. Has a preference for plasma 16:0-18:2 or 18:O-18:2 phosphatidylcholines. Catalyzes the hydrolysis of 1-O-alkyl-2-acetyl-sn-glycero-3-phosphocholine (platelet-activating factor or PAF) to 1-O-alkyl-sn-glycero-3-phosphocholine (lyso-PAF). Also catalyzes the transfer of the acetate group from PAF to 1-hexadecanoyl-sn-glycero-3-phosphocholine forming lyso-PAF (By similarity). Catalyzes the esterification of (24S)-hydroxycholesterol (24(S)OH-C), also known as cerebrosterol to produce 24(S)OH-C monoesters (By similarity).
Subcellular location: Secreted {ECO:0000269|PubMed:19065001, ECO:0000269|PubMed:8820107}. Note=Secreted into blood plasma (PubMed:8820107). Produced in astrocytes and secreted into cerebral spinal fluid (CSF) (By similarity). {ECO:0000250|UniProtKB:P04180, ECO:0000269|PubMed:8820107}.
Interaction partners:
- Apolipoprotein A-I
- Apolipoprotein C-I
- Apolipoprotein A-IV
- Apolipoprotein B-100
- Apolipoprotein A-II
- Phosphatidylethanolamine N-methyltransferase
- Apolipoprotein C-III
- Apolipoprotein E
- Serum paraoxonase/arylesterase 1
- Patatin-like phospholipase domain-containing protein 7
Sequence:
MGLPGSPWQRVLLLLGLLLPPATPFWLLNVLFPPHTTPKAELSNHTRPVILVPGCLGNRLEAKLDKPDVVNWMCYRKTEDFFTIWLDFNLFLPLGVDCWIDNTRIVYNHSSGRVSNAPGVQIRVPGFGKTESVEYVDDNKLAGYLHTLVQNLVNNGYVRDETVRAAPYDWRLAPHQQDEYYKKLAGLVEEMYAAYGKPVFLIGHSLGCLHVLHFLLRQPQSWKDHFIDGFISLGAPWGGSIKAMRILASGDNQGIPILSNIKLKEEQRITTTSPWMLPAPHVWPEDHVFISTPNFNYTVQDFERFFTDLHFEEGWHMFLQSRDLLERLPAPGVEVYCLYGVGRPTPHTYIYDHNFPYKDPVAALYEDGDDTVATRSTELCGQWQGRQSQPVHLLPMNETDHLNMVFSNKTLEHINAILLGAYRTPKSPAASPSPPPPE
Protein: Low affinity inorganic phosphate transporter 4 (MtPT4) (MtPht1;4) (Arbuscular mycorrhiza-induced phosphate transporter PT4) (AM-induced phosphate transporter PT4) (H(+)/Pi cotransporter PT4) (Q8GSG4)
Organism: Medicago truncatula (Barrel medic) (Medicago tribuloides)
Function: Low-affinity transporter for external inorganic phosphate (Pi) probably involved in the acquisition of phosphate released by arbuscular mycorrhizal (AM) fungi (e.g. Gigaspora gigantea, Glomus versiforme and G.intraradices) during AM symbiosis; required for propper mycorrhizal arbuscule morphology. Acts as a Pi-sensing machinery at the root tip level, independently of AM fungi, involved in the regulation of early root branching and lateral roots formation.
Subcellular location: Cell membrane {ECO:0000269|PubMed:12368495}; Multi-pass membrane protein {ECO:0000255}. Note=Present on the periarbuscular membrane in cells containing arbuscules during arbuscular mycorrhizal (AM) symbiosis with AM fungi (e.g. Gigaspora gigantea, Glomus versiforme and G.intraradices). {ECO:0000269|PubMed:12368495}.
Interaction partners:
Sequence:
MGLEVLEALDSARTQWYHVTAIVIAGMGFFTDAYDLFCISTVSKLLGRLYYFDPSTNKPGKLPPSVNNVVTGVALVGTLSGQLVFGWLGDKLGRKKVYGVTLIIMVACAICSGLSFGSSAKSVMITLCFFRFWLGFGIGGDYPLSATIMSEYANKRTRGAFIAAVFAMQGVGIIFAGLVSMVFSGIFKAYYQAPRFNEDPILSTQPEGDLLWRLILMIGAVPAAMTYYWRMKMPETGRYTAIVEGNAKQAAADMARVLDIEIIAEQDKLAEFKAANDYPLWSSEFFNRHGRHLIGTMSCWFLLDIAFYSQNLTQKDIYPAMGLIRQDKEMNAIDEVFQTSRAMFVVALFGTFPGYWFTVFFIEKLGRFKIQLVGFFMMSFFMFVIGVKYEYLKDENKNLFALLYGLTFFFANFGPNSTTFVLPAELFPTRVRSTCHAFSAASGKAGAMVGAFGIQYYTLDGTPRKIRRAMMILAFTNLIGFFCTFLVTETKGRSLEEISGEDGRESELTATPNDRAPGIRQDSRTEKM
Protein: Anthocyanin synthase (AcANS) (EC 1.14.20.4) (Leucoanthocyanidin dioxygenase) (AcLDOX) (Leucocyanidin oxygenase) (A0A2R6PI27)
Organism: Actinidia chinensis var. chinensis (Chinese soft-hair kiwi)
Function: Involved in anthocyanin biosynthesis by catalyzing the oxidation of leucoanthocyanidins into anthocyanidins. Required for the accumulation of anthocyanin in red-fleshed kiwifruit varieties.
Interaction partners:
- Dihydroflavonol 4-reductase
- Dihydroflavonol 4-reductase
- Dihydroflavonol 4-reductase
- Dihydroflavonol 4-reductase
- Dihydroflavonol 4-reductase
- Naringenin,2-oxoglutarate 3-dioxygenase
- Naringenin,2-oxoglutarate 3-dioxygenase
- Dihydroflavonol 4-reductase
- Dihydroflavonol 4-reductase
- Anthocyanidin 3-O-galactosyltransferase F3GT1
Sequence:
MVATVVGTRVESLASSGIEAIPKEYVRPQEELTSIGNIFEEEKKENGPQVPTIDLEDLVSEDEEKRVRCHEELKRAATEWGVMQVVNHGIPIELMERVRAAGAEFFNQSVEEKEKYANDHASGNIQGYGSKLANNASGQLEWEDYFFHLVYPEDKRDMSIWPKTPSDYIPATSAYAEHLRGLATKILSALSLGLGLEEGRLEKEVGGMEELLLQMKINYYPKCPQPELALGVEAHTDVSALTFILHNMVPGLQLFYEGKWVTAKCVPDSLVMHIGDTIEILSNGKYKSILHRGLVNKEKVRISWAVFCEPPKEKIILKPLPETVSEAEPPLYPPRTFAQHIHHKLFRKTQELGAK
Protein: Dihydropteridine reductase (EC 1.5.1.34) (Quinoid dihydropteridine reductase) (A7YT77)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
- Pterin-4-alpha-carbinolamine dehydratase
- Dihydrofolate reductase.
- Zgc:153031.
- Tyrosine 3-monooxygenase
- Tryptophan hydroxylase 2
- Phenylalanine hydroxylase.
- Tryptophan hydroxylase 1b.
- Tyrosine hydroxylase 2.
- Tryptophan hydroxylase 1
- Sepiapterin reductase
Sequence:
MAAANRVLVYGGKGALGSACVHYFKSKGWWVASIDIGANEEANANVLVKLSESFTDQAAQVTSDVSKLLGEHKVEAIVCVAGGWAGGNCSSKDLYKNSDMMWKQSVWTSTISSHLASLHLKPGGLLTLAGAKASLDATPGMVGYGMAKAAVHQLCKSLAGENSGLPSGAVAVAILPVTLDTPMNRKFMPDADFGSWTPLEYIAETFHSWATGSGRPASGSLIQLETTGGKTEATAVQ
Protein: Catenin alpha-1 (Q5U302)
Organism: Rattus norvegicus (Rat)
Subcellular location: Cell junction, adherens junction {ECO:0000256|ARBA:ARBA00004536}. Cell membrane {ECO:0000256|ARBA:ARBA00004413}; Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004413}; Cytoplasmic side {ECO:0000256|ARBA:ARBA00004413}. Cytoplasm, cytoskeleton {ECO:0000256|ARBA:ARBA00004245}. Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- Catenin beta-1
- Cadherin-1
- Tight junction protein ZO-1
- Catenin delta 1
- Actin, cytoplasmic 1
- Alpha-actinin-1
- Alpha-actinin-4
- Cadherin-2
- Junction plakoglobin
- Actin, cytoplasmic 2
Sequence:
MTAVHTGNINFKWDPKSLEIRTLAVERLLEPLVTQVTTLVNTNSKGPSNKKRGRSKKAHVLAASVEQATENFLEKGDKIAKESQFLKEELVAAVDDVRKQGDLMKSAAGEFADDPCSSVKRGNMVRAARALLSAVTRLLILADMADVYKLLVQLKVVEDGILKLRNAGNEQDLGIQYRALKPEVDKLNIMAAKRQQELKDVGHRDQMAAARGILQKNVPILYTASQACLQHPDVAAYKANRDLIYKQLQQAVTGISNAAQATASDDASQQQGGGGGGGELAYALNNFDKQIIVDPLSFSEERFRPSLEERLESIISGAALMADSSCTRDDRRERIVAECNAVRQALQDLLSEYMGNAGRKERSDALNSAIDKMTKKTRDLRRQLRKAVMDHVSDSFLETNVPLLVLIEAAKNGNEKEVKEYAQVFREHANKLIEVANLACSISNNEEGVKLVRMSASQLEALCPQVINAALALAAKPQSKLAQENMDLFKEQWEKQVRVLTDAVDDITSIDDFLAVSENHILEDVNKCVIALQEKDVDGLDRTAGAIRGRAARVIHVVTSEMDNYEPGVYTEKVLEATKLLSNTVMPRFTEQVEAAVEALSSDPAQPMDENEFIDASRLVYDGIRDIRKAVLMIRTPEELDDSDFETEDFDVRSRTSVQTEDDQLIAGQSARAIMAQLPQEQKAKIAEQVASFQEEKSKLDAEVSKWDDSGNDIIVLAKQMCMIMMEMTDFTRGKGPLKNTSDVISAAKKIAEAGSRMDKLGRTIADHCPDSACKQDLLAYLQRIALYCHQLNICSKVKAEVQNLGGELVVSGVDSAMSLIQAAKNLMNAVVQTVKASYVASTKYQKSQGMASLNLPAVSWKMKAPEKKPLVKREKQDETQTKIKRASQKKHVNPVQALSEFKAMDSI
Protein: Lysophosphatidic acid receptor 1 (Q6DHQ8)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004651}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}. Cell surface {ECO:0000256|ARBA:ARBA00004241}. Endosome {ECO:0000256|ARBA:ARBA00004177}.
Interaction partners:
Sequence:
MDDRQCYYNETIAFFYNRSQKYLATEWNAVSKLVMGLGITVCIFIMLANLLVMVAIYINRRFHFPIYYLMANLAAADFFAGLAYFYLMFNTGPNTRRLTVSTWLLRQGLIDTSLTASVANLLAIAIERHITVFRMQLHTRMSNRRVVVVIVIIWTMSIVMGAIPSVGWNCICAIDTCSNMAPLYSNSYLGFWAIFNLVTFVVMVVLYAHIFMYVRQRTMRMSRHSSGQRRNRDTMMSLLKTVVIVLGAFIVCWTPGLVILLLDVVCANCNVLTYEKFFLLLAEFNSAMNPIIYSYRDKEMSITFKQILCCQRQENVNGTAEGSDRSASSINHTVLSGAHHNDHSVV
Protein: At5g12880 (Proline-rich family protein) (Q9LXV1)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- At5g49280
- At1g23040
- GDSL esterase/lipase At1g28660
- UPF0496 protein At3g49070
- Uncharacterized protein
- Glycine-rich protein homolog
- Uncharacterized protein
- Transmembrane protein
- STAY-GREEN-like protein
- Uncharacterized protein
Sequence:
MRRSWPTRLILLMVLTVVITMIAAAYGYSSVSSSKHKFPHYKYKAPSPPTTYSPYRYFSPPPVTDSDSAAYVR
Protein: Heterogeneous nuclear ribonucleoprotein A1 (hnRNP A1) (HDP-1) (Helix-destabilizing protein) (Single-strand-binding protein) (Topoisomerase-inhibitor suppressed) (hnRNP core protein A1) [Cleaved into: Heterogeneous nuclear ribonucleoprotein A1, N-terminally processed] (P49312)
Organism: Mus musculus (Mouse)
Function: Involved in the packaging of pre-mRNA into hnRNP particles, transport of poly(A) mRNA from the nucleus to the cytoplasm and modulation of splice site selection. Plays a role in the splicing of pyruvate kinase PKM by binding repressively to sequences flanking PKM exon 9, inhibiting exon 9 inclusion and resulting in exon 10 inclusion and production of the PKM M2 isoform. Binds to the IRES and thereby inhibits the translation of the apoptosis protease activating factor APAF1. May bind to specific miRNA hairpins.
Subcellular location: Nucleus {ECO:0000250|UniProtKB:P09651}. Cytoplasm {ECO:0000250|UniProtKB:P09651}. Note=Localized in cytoplasmic mRNP granules containing untranslated mRNAs. Shuttles continuously between the nucleus and the cytoplasm along with mRNA. Component of ribonucleosomes. {ECO:0000250|UniProtKB:P09651}.
Interaction partners:
- Heterogeneous nuclear ribonucleoprotein K
- Heterogeneous nuclear ribonucleoprotein M
- Heterogeneous nuclear ribonucleoproteins C1/C2
- Transportin-1
- Heterogeneous nuclear ribonucleoprotein U
- Heterogeneous nuclear ribonucleoproteins A2/B1
- Polypyrimidine tract-binding protein 1
- Poly
- RNA binding motif protein, X-linked-like-1
- Serine/arginine-rich splicing factor 1
Sequence:
MSKSESPKEPEQLRKLFIGGLSFETTDESLRSHFEQWGTLTDCVVMRDPNTKRSRGFGFVTYATVEEVDAAMNARPHKVDGRVVEPKRAVSREDSQRPGAHLTVKKIFVGGIKEDTEEHHLRDYFEQYGKIEVIEIMTDRGSGKKRGFAFVTFDDHDSVDKIVIQKYHTVNGHNCEVRKALSKQEMASASSSQRGRSGSGNFGGGRGGGFGGNDNFGRGGNFSGRGGFGGSRGGGGYGGSGDGYNGFGNDGSNFGGGGSYNDFGNYNNQSSNFGPMKGGNFGGRSSGPYGGGGQYFAKPRNQGGYGGSSSSSSYGSGRRF
Protein: Germacrene D synthase (LaGERDS) (EC 4.2.3.75) ((-)-germacrene D synthase) (Bicyclogermacrene synthase) (EC 4.2.3.100) (U3LVL5)
Organism: Lavandula angustifolia (Lavender)
Function: Sesquiterpene synthase that catalyzes the formation of sesquiterpenes and sesquiterpenoid alcohols. Converts farnesyl diphosphate (FPP) to germacrene D. Converts FPP to bicyclogermacrene. Germacrene D is the major product.
Interaction partners:
Sequence:
MEIHSSVVPAITNVKSLDEIRRSAKFHPTVWGDYFLAYNSDNTEITAAEHEEHAKQKEMVKKLLTLAPNDPTDKMQLIDAIQRLGLQYHFEKEIQEILQSIHANFKADKDLHTVALRFRLLRQHGYNVACDVFNNFLNKEGDFMESITNDFEGLLSLYEAAYLGTHGEEILDKAIEFCSFHLQSSLPQISNVSLSKRVEEALYIPTHKSLTRFGARKFIPIYEEDESHKKVLLNLAKLDFNIVQKIHQKELSDLTRWWTKLEVPKNMPYSRDRLVELFFWIVGVYFEPQFTTARRILVKAISMASLIDDTYEHATLDELKVLTDVIERWDTNAVIKDWPPYTQMCYKYLFDTYAEIEDEVEERESYRVQYAKKEMQKLVRAYFDEAKWLYKNYLPTWEEYMKVSTVTGAYMMLSTTSLVGMGDLVTKQDFDWVVREPLIVRASSVISRLMDDLVGDEDEQKPSGALCYMKQYGVSKEEACAEVRKHVKNAWKDMNQECLEPRPASMQVLTRVVNLGRVINLLYTGDDWYGNPLGSKEWVKMVFVEPLTI
Protein: glucan 1,3-beta-glucosidase (EC 3.2.1.58) (Exo-1,3-beta-glucanase) (G8BI93)
Organism: Candida parapsilosis (strain CDC 317 / ATCC MYA-4646) (Yeast) (Monilia parapsilosis)
Subcellular location: Secreted, cell wall {ECO:0000256|ARBA:ARBA00004191}.
Interaction partners:
- Glucan 1,3-beta-glucosidase
- glucan 1,3-beta-glucosidase
- glucan 1,3-beta-glucosidase
- 1,3-beta-glucan synthase
- 1,3-beta-glucan synthase
- 1,3-beta-glucan synthase
- Uncharacterized protein
- beta-glucosidase
- SWIRM domain-containing protein
- SWI/SNF complex subunit SWI3
Sequence:
MQFKLLSALVAGLATANAIGDLAFNLGVKDNNGNCKTVDEFKSDLEVIKGSSSIIKTYAVSDCNTLQNLGPAAEAEGFQIMLGIWPNDDAHFEEEKQALQQYLTQISTSTIKIFLVGSEALYREDLTADQLSEKINEIKDLVKNIKDKDGNSYSGIPVGTVDSWNVLVDGGSKPAIETADVVYANAFSYWQGQTNQNASYSFFDDIMQALQTIQTVKGSTDIEFWVGETGWPTDGSNFESSQPGVENAKNFWQNAICAMRGWGVNVAVFEAIDEAWKPDTSGISDVEKHWGVWDANYKLKYNINCDFD
Protein: Prolyl 3-hydroxylase sudestada1 (EC 1.14.11.-) (2-oxoglutarate and iron-dependent oxygenase domain-containing protein 1 homolog) (uS12 prolyl 3-hydroxylase) (Q9I7H9)
Organism: Drosophila melanogaster (Fruit fly)
Function: Prolyl 3-hydroxylase that catalyzes 3-hydroxylation of 'Pro-62' of small ribosomal subunit uS12 (RpS23), thereby regulating protein translation termination efficiency.
Subcellular location: Nucleus {ECO:0000269|PubMed:24550463}. Cytoplasm {ECO:0000269|PubMed:24550463}. Note=Localizes predominantly to the nucleus. Present at lower levels are also detected in the cytoplasm.
Interaction partners:
- Phosphatidylinositol glycan anchor biosynthesis class S
- Glycosylphosphatidylinositol anchor attachment 1
- Phosphatidylinositol glycan anchor biosynthesis class T
- Putative GPI-anchor transamidase
- LD37974p
- Uncharacterized protein, isoform B
- Peptidoglycan-recognition protein SA
Sequence:
METSSSSPVKPRRKDKDEDGRAEQEDSADQVGEPHRKLLRLGDILETNEVLLNEAYQQPELTKWLQTAWTEEKSQGTKETQTGAQVFSDPFQICLLPGMLEKGQSQALVAEIIQKVQWSRKQMDLYEFYQSADLSNMPACRLLTNFLQVLRKQVRPWLEKVTNLKLDYVSASCSMYTCGDYLLVHDDLLKDRQVAFIYYLSPWEGAEEWTDEQGGCLEIFGSDDQCFPQFPVQRKIAPKDNQFAFFKVGSRSFHQVGEVTTFDYPRLTINGWFHGDTNEAFVADSLRAFPRLNYLQPDGLNRPPLGLFLNNVYLKGATRRSIQKRIEENSEICLYEFFKREKFELARSQLLADSDTLKWRRQGPANAHNYEVLDLTTARGTILELLQLFRSHAMFDLLRDFTDLDLAGTDAESPTCSVELQRWSHGNYTVLGDGLTSEENTLDLVYYLNAAEGAAVITYLAPDAEMPTAKAPTDGRRSDYDDEEEDDSVLLTITPVDNALNIVYRCEGTTKFTKYVSRNTPLEKGPVFVISCSYKE
Protein: NAD(P)-linked oxidoreductase superfamily protein (Putative NADPH-dependent mannose 6-phosphate reductase) (Q9SJV2)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- NAD
- At2g27680/F15K20.22
- L-galactose dehydrogenase
Sequence:
MEITLNSGFKMPIVGLGVWRMEKEGIRDLILNAIKIGYRHLDCAADYRNETEVGDALTEAFKTGLVKREDLFITTKLWNSDHGHVIEACKDSLKKLQLDYLDLFLVHFPVATKHTGVGTTDSALGDDGVLDIDTTISLETTWHDMEKLVSMGLVRSIGISNYDVFLTRDCLAYSKIKPAVNQIETHPYFQRDSLVKFCQKHGICVTAHTPLGGATANAEWFGTVSCLDDPVLKDVAEKYKKTVAQVVLRWGIQRKTVVIPKTSKPARLEENFQVFDFELSKEDMEVIKSMERKYRTNQPAKFWNIDLYA
Protein: Uncharacterized protein (Q5ARV0)
Organism: Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Interaction partners:
Sequence:
MDDPLLRAWTTQYTNSPITTPRSATPGECRLRPPRDERVEKPRHPKNPPTPPSMSMPYAVSSVPQGNMCNVDRGNGALEYINPSLLLFPQDYASQESNNYASARRVSDRRIGQSPYTRPNTPNVEGVSNVSSSDQRSSLSGRNGREEQSNPPVDIFEGILAKMLAFDVVRPPSTNELGNDEPPREVEAKQPTVHHGFAISVGWSSTFFPDDIQEGSGHSRNTVDTVGHF
Protein: PDGF- and VEGF-receptor related, isoform M (EC 2.7.10.1) (M9PCX2)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004167}; Single-pass membrane protein {ECO:0000256|ARBA:ARBA00004167}.
Interaction partners:
Sequence:
MAMLPRLILLPLLLILRISWSDAVPLQQFSPDPDDSIENCGGENGAPLMTPCKSAIILDAQTSTTLKCEDDEPMSWWTSQSQYVHVKSFDNTEDPARPFGTSLHLIEVTADYVAAYYCVKTSKFSQIAKEEQSDEAMIELVNQGYASSIYVYVNDPDTKLVDSHNVVTARQYTDVVIPCKPAMPDTEVLLETSNGEMHSSKSVGRYDPQRGFTIEIRSIVDGGDYYCRPNPPFPHNEEEMTSIEVRFIATGLDIPRTQTTNMVYTYAPGVTDGDDEVLTVTNQSTGNLALIRGGDGTLSRERARRSPARLAPMNASPSPRPGQDGKPLPKPVIRSSVEHHVFTDTNFTLDCEQSAYVESVYGMEWFTPSRDENRIFASQSRTDPKTRNSTHQTGRSTLTVLNAQPSDTGLYKCVTTDNSNQNVQRATYRIKVLKQNESYLNVGEPSGHYNVQEYANRTIQMTANFEGFPTPSFSWFKPDGTEVRQSENNFKILSTELSTMLQVLNAQLQDSGTYVLRGSNSFGVVQREYNVSVMDAPALKMSDAYVQVGSVARLECTVRSYPPAIVTFFFRPCSLEPQWPTCSVLNQNFSFQTRPRPGKLSVERIYEVSFLPTEPGILTCIAQNIIDGKERRTLTKAHVLLGNISENMTIYGFDKDHKIAKEDNVNFTCEALAYHFDGNLKWFINGEDLKESDSVHIETSHTKYSYKSTVHITTISDRDRGTYECRAYHNDKDAVYSSREIDLYVHDPSAPQWTNGGQEGHSKIKRKLSQTLELECASTAVPVAIVRWFKDDKEVTESKLRHIIEKESKLLITHLYPGDEGVYKCVVENRLDRIERSFTVVISDLPGISMAWVWFGVILFLILIGLCVFLAVRYQKEHKRHLALKAAGLANFEEGAVGHINPDLTLDEQAELLPYNREFEFPRENLKLGKQLGAGAFGVVLKGEAKGIRREEPTTTVAVKMVKATADNEVVRALVSELKIMVHLGQHLNVVNLLGAVTKNIAKRELMVIVEYCRFGNIQNFLLRNRKCFINQINPDTDHIDPSIMTQRMSDNYELHRDTNGGGLKYANVGFPIHSYINEPHNNNTQPPTHRRNSDNDPRSGTRAGRTGSGTATYSYDRQMDTCATVMTTVPEDDQIMSNNSVQPAWRSNYKTDSTEAMTVTTVDLISWAFQVARGMDYLSSKKVLHGDLAARNILLCEDNVVKICDFGLARSMYRGDNYKKSENGKLPIKWLALESLSDHVFSTYSDVWSYGIVLWEMFSLAKVPYPGIDPNQELFNKLNDGYRMEKPKFANQELYEIMLECWRKNPESRPLFAELEKRFANMLGEDVASHYLDLNNPYMQSNIEYMKKQSTDYLALMGSPDELAPAAPRYVNGHIVPDIRIEELPDDYMEMSRDSDPDACTAIFSPTRLEGESSDFPDFSSETTFNFPGARQSPTLSNNLNSGSSKPLRKKNGMPTVDVADQAPEEIPMLHRSSTGSDGSPEQGRRFNQALKQQYVTPTPSPRHHVETKLNGEPSENYVNMKPPRKNIPGKTTTGGGGAAAGASTEAFSNPSYQPLSTVNEKEQRRY
Protein: Thioesterase domain-containing protein (Q38AF5)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MQRGFCRVGTVTVSQAQKRAAELINSSDGFCSNVMRTVQFTPTGVKACDGESMGFSWRANQRALNGFRSTHGGALAILADTFTQIHLGAARPAAEFRSVSFEINYLEAIPENAECTCITRIVGDGESDIHHVEYSFQDERRRKVFSRGTHVLSCTK
Protein: LOC553366 protein (Q568F5)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004651}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}. Early endosome {ECO:0000256|ARBA:ARBA00004412}.
Interaction partners:
Sequence:
KHCESDHREREDDRQQLICITNTFFSQTKKKLRGSMMNVTELITSLTPQTSEYEEYGDFSTTSDYGDTDDGFCPKSKVREFRMYYEPMLYWMIVILGAIGNTLVVWIYTHFKNRLKAMTDVYLLNLALADLFFLCTLPFWAADSIYGWAFGSGLCKVVSAVYKINFFSSMFLLTCISVDRYIVIVQTTKAQNSKRSRLLYSKLICVLVWLLAALMSIPECLFARSKEDDESNTFCTMVYWNNENNRTKILVLALQICMGFCIPLVVMIFCYTNIIRTLLKTRNFQKHKALRVILAVVAVFVLSQLPYNGMLVFEATQAANMTVTNCTESIRFDIAGQVMKSIAYMHSCLNPFLYAFVGVRFRKDVIRIFQNIGCVSNLKNSKLAGIPHRSSVMSDTDTTNALSL
Protein: Ribosome maturation factor RimP (P9WH17)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: Required for maturation of 30S ribosomal subunits.
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01077}.
Interaction partners:
- Transcription termination/antitermination protein NusA
- Small ribosomal subunit protein uS12
- YlxR domain-containing protein
- Translation initiation factor IF-2
- Ribosome-binding factor A
- Small ribosomal subunit protein uS10
- Ribosome maturation factor RimM
- Small ribosomal subunit protein bS16
- Large ribosomal subunit protein uL13
- tRNA pseudouridine synthase B
Sequence:
MTTGLPSQRQVIELLGADFACAGYEIEDVVIDARARPPRIAVIADGDAPLDLDTIAALSRRASALLDGLDGANKIRGRYLLEVSSPGVERPLTSEKHFRRARGRKVELVLSDGSRLTGRVGEMRAGTVALVIREDRGWAVREIPLAEIVKAVVQVEFSPPAPAELELAQSSEMGLARGTEAGA
Protein: non-specific serine/threonine protein kinase (EC 2.7.11.1) (Q9FK52)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- At3g49990
- Serine/threonine-protein kinase MPS1
- Leucine-rich repeat protein kinase family protein
- Kinase superfamily with octicosapeptide/Phox/Bem1p domain-containing protein
- Protein kinase superfamily protein
- Expressed protein
- G-type lectin S-receptor-like serine/threonine-protein kinase At1g61440
- Protein AE7-like 2
- Protein AE7-like 1
- Bystin
Sequence:
MPELRSGARRLRQPSPQVTGQADNIELPPQPVTRRRGGGGRGRGNAKGAAPPRPAGGVGRGRGIRLIDLEAEPCEVRPAVGEPAFNQVEAVAEKDIAMEGGSAEKVVGVEEDSSTAPVPERVQVGNSPVYKTERKLGKGGFGQVFVGRRVSGGSDRIGADAIEVALKFEHRNSKGCNFGPPYEWQVYNTLNGCYGVPAVHHKGRQGDFYILVMDMLGPSLWDVWNSSGQSMSPNMVACIAVESISILEKLHMKGFVHGDVKPENFLLGQPGTADEKKLYLIDLGLASKWKDSHSGQHVEYDQRPDVFRGTIRYASVHAHLGRTGSRRDDLESLAYTLIFLLKGRLPWQGYQGDNKSFLVCKKKMSTSPELMCCFCPPPFKLFLEAVTNMKFDEEPNYAKLISIFDSLIEQCALSRPIKIDGALKVGQKRGRMLLNLDEDEQPKKKIRIGSPACQWISVYNARRPMKQRYHYNVADSRLHQHVQKGNEDGLLISCVASAANLWALIMDAGTGFTSQVYELSTVFLHKDWIMEQWEKNYYISSIAGSDNGNSLVVMSKGTSYTQQSYKVSDSFPFKWINKKWKEDFHVTSMTTAGNRWGVVMSRNSGYSDQVVELDFLYPSDGIHRRWESGYRITSMAATADQAAFILSVPKRKMMDETQETLRTTAFPSTHVKEKWAKNLYIASICFGRTVC
Protein: Peptidyl-prolyl cis-trans isomerase FKBP10 (PPIase FKBP10) (EC 5.2.1.8) (65 kDa FK506-binding protein) (65 kDa FKBP) (FKBP-65) (FK506-binding protein 10) (FKBP-10) (Immunophilin FKBP65) (Rotamase) (Q96AY3)
Organism: Homo sapiens (Human)
Function: PPIases accelerate the folding of proteins during protein synthesis.
Subcellular location: Endoplasmic reticulum lumen {ECO:0000255|PROSITE-ProRule:PRU10138}.
Interaction partners:
- Serpin H1
- Procollagen-lysine,2-oxoglutarate 5-dioxygenase 2
- Elastin
- Cartilage-associated protein
- Collagen alpha-2
- Prolyl 3-hydroxylase 1
- Peptidyl-prolyl cis-trans isomerase B
- General transcription factor II-I repeat domain-containing protein 1
- Trimeric intracellular cation channel type B
- Collagen alpha-1
Sequence:
MFPAGPPSHSLLRLPLLQLLLLVVQAVGRGLGRASPAGGPLEDVVIERYHIPRACPREVQMGDFVRYHYNGTFEDGKKFDSSYDRNTLVAIVVGVGRLITGMDRGLMGMCVNERRRLIVPPHLGYGSIGLAGLIPPDATLYFDVVLLDVWNKEDTVQVSTLLRPPHCPRMVQDGDFVRYHYNGTLLDGTSFDTSYSKGGTYDTYVGSGWLIKGMDQGLLGMCPGERRKIIIPPFLAYGEKGYGTVIPPQASLVFHVLLIDVHNPKDAVQLETLELPPGCVRRAGAGDFMRYHYNGSLMDGTLFDSSYSRNHTYNTYIGQGYIIPGMDQGLQGACMGERRRITIPPHLAYGENGTGDKIPGSAVLIFNVHVIDFHNPADVVEIRTLSRPSETCNETTKLGDFVRYHYNCSLLDGTQLFTSHDYGAPQEATLGANKVIEGLDTGLQGMCVGERRQLIVPPHLAHGESGARGVPGSAVLLFEVELVSREDGLPTGYLFVWHKDPPANLFEDMDLNKDGEVPPEEFSTFIKAQVSEGKGRLMPGQDPEKTIGDMFQNQDRNQDGKITVDELKLKSDEDEERVHEEL
Protein: ATP synthase subunit beta, mitochondrial (EC 7.1.2.2) (Q05825)
Organism: Drosophila melanogaster (Fruit fly)
Function: Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramembraneous catalytic core, and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Subunits alpha and beta form the catalytic core in F(1). Rotation of the central stalk against the surrounding alpha(3)beta(3) subunits leads to hydrolysis of ATP in three separate catalytic sites on the beta subunits.
Subcellular location: Mitochondrion. Mitochondrion inner membrane. Note=Peripheral membrane protein.
Interaction partners:
- ATP synthase subunit O, mitochondrial
- ATP synthase F
- ATP synthase subunit g
- Protein stunted
- ATP synthase-coupling factor 6, mitochondrial
- ATP synthase F
- ATP synthase subunit gamma, mitochondrial
- ATP synthase subunit b, mitochondrial
- ATP synthase subunit d, mitochondrial
- Putative ATP synthase subunit f
Sequence:
MFALRAASKADKNLLPFLGQLSRSHAAKAAKAAAAANGKIVAVIGAVVDVQFDDNLPPILNALEVDNRSPRLVLEVAQHLGENTVRTIAMDGTEGLVRGQKVLDTGYPIRIPVGAETLGRIINVIGEPIDERGPIDTDKTAAIHAEAPEFVQMSVEQEILVTGIKVVDLLAPYAKGGKIGLFGGAGVGKTVLIMELINNVAKAHGGYSVFAGVGERTREGNDLYNEMIEGGVISLKDKTSKVALVYGQMNEPPGARARVALTGLTVAEYFRDQEGQDVLLFIDNIFRFTQAGSEVSALLGRIPSAVGYQPTLATDMGSMQERITTTKKGSITSVQAIYVPADDLTDPAPATTFAHLDATTVLSRAIAELGIYPAVDPLDSTSRIMDPNIIGQEHYNVARGVQKILQDYKSLQDIIAILGMDELSEEDKLTVARARKIQRFLSQPFQVAEVFTGHAGKLVPLEQTIKGFSAILAGDYDHLPEVAFYMVGPIEEVVEKADRLAKEAA
Protein: Probable ribose-5-phosphate isomerase 3, chloroplastic (EC 5.3.1.6) (Phosphoriboisomerase 3) (Protein EMBRYO DEFECTIVE 3119) (Q9S726)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Catalyzes the reversible conversion of ribose-5-phosphate to ribulose 5-phosphate.
Subcellular location: Plastid, chloroplast {ECO:0000305}.
Interaction partners:
- Ribulose-5-phosphate-3-epimerase, chloroplastic
- Ribulose-phosphate 3-epimerase
- Ribulose-phosphate 3-epimerase
- Transketolase-1, chloroplastic
- 6-phosphogluconate dehydrogenase, decarboxylating 2
- 6-phosphogluconate dehydrogenase, decarboxylating 1, chloroplastic
- 6-phosphogluconate dehydrogenase, decarboxylating 3, chloroplastic
- Transketolase-2, chloroplastic
- Phosphoribulokinase, chloroplastic
- Ribose-phosphate pyrophosphokinase 1, chloroplastic
Sequence:
MASLSFVSSSHLTLRTPSIALRSTGSSPRTSVSFSVKAQSVALSQDDLKKLAAEKAVEAIKPGMVLGLGTGSTAAFAVDQIGKLLSSGELYDIVGIPTSKRTEEQARSLGIPLVGLDTHPRIDLAIDGADEVDPNLDLVKGRGGALLREKMVEAVADKFIVVADDTKLVTGLGGSGLAMPVEVVQFCWNFNLIRLQDLFKEFGCESKLRVDGDGKPYVTDNSNYIIDLYFKTPLKDGFAAAKEIGKFQGVVEHGLFLGMATSVIIAGKNGVEVMTK