wanglab/gogpt-training-data huggingface dataset:
Protein: FCP1 homology domain-containing protein (Q389J5)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MNIFSFGRESMCSFSATEGKESVPLTARSYERSRSELFEGLTTTRAVALQATTSSNFPSSSNAKQVPDGEGLFSMGSCSVSTDKVEENSTICETSRSAGGKQRKQKGQQKPRKAKTNNSRDDNKKKNATNTKTPQRTSRKKSGKRKKRRSSCRSMGEASVRSNGTPAEGEIESSNAESSVQLPRPFNTPKGVPAVVHVVAHNIAEMQGRKRESCVQSLSRPFEMFDRIVSRPECGKDAQETPSTAASHSDLHTSISVLKGQSSTTIDLPERSNSVVGVFATATTPALPSSPPLYGRSSRREHTARAGDGTAYLSSLTFSSLLGSFQKEQEKTERPPAKSPSTLEGLTRHSLTDMVEGKVPSKTEPVVERLLARTLSSTSEKERTATIVFDLDETLCNNRVNGPAILRPGAIDILGKLRSLYPRCIAPGDGGSPVRDASASAESVGNSGSRSGLVPTDVTAGNGPLLQLEIVLWTASVESVARPVVDRLDPDGTIFDCVICRDARWYDESGYTKDLRLLGRYIERSVIVENSPLCVKLNRRNAILVSDFVRNRMDRQLYVVCVILLEWLDNVNNLLLRKHMMRVNMERRRGCGMSDGGESPEPEMPPSEAQLRGSKTPGLTKPHKADMLGSTLPLHELERRASAIYFVGSHPFISPSTRLVRSSACQQAVRYLCGEGFASGKMKIISRRRPAAKHAAVTPNTPKGRSSSLTSISPAPVPGRAPSREVSCS
Protein: NADPH--cytochrome P450 reductase (CPR) (P450R) (EC 1.6.2.4) (Q09590)
Organism: Caenorhabditis elegans
Subcellular location: Endoplasmic reticulum membrane {ECO:0000256|HAMAP-Rule:MF_03212}; Single-pass membrane protein {ECO:0000256|HAMAP-Rule:MF_03212}; Cytoplasmic side {ECO:0000256|HAMAP-Rule:MF_03212}.
Interaction partners:
- CYtochrome P450 family
- CYtochrome P450 family
- Cytochrome P450
- Probable FAD synthase
- Cytochrome P450
- Putative cytochrome P450 cyp-13B1
- N-acetyltransferase 9-like protein
- Cytochrome P450 4V2
- Bifunctional 3'-phosphoadenosine 5'-phosphosulfate synthase pps-1
- 3beta-hydroxysteroid dehydrogenase/Delta
Sequence:
MLAWIVSGLDTSDLVVLTLLAGGAIIFLFMKVFNQQPSSSRYSPTVASVTTSAAASKSNQSFIDRMKNENRQVLIMYGSQTGTAEEMSGRLAKDLTRYTKKAVVVDPEDIECEDLNRLSEVEDALLVLCIATYGEGDPTDNAVTLVEYLNAGDCDLSGVRFAVFGLGNKTYEHFNEIGIQMDKQLEKLGAKRIFHLGLGDDDANLEEDFMIWREAFLPKVAEEFGWELNTEAETMRQYQLEPVEEGKALFKGEFGRLGAYERPRPPFDVKNPYLATVAINDELHTEHSDRSCRHIEFSVEGSRIRYEAGDHLAVFPTNDPVLVDRLINMLQFDPDHAFRLVNVDEDASKRHPFPCPTTFRTALSHYVDICAPVKSHVLKAISEYCTDDTEKEFLNKLSTANEEGLKEYARYIVKERRSIVDVLTDQKTCKPPIEYLLELLPRLQARYYSIASSPRLNEEKIAICAVVTKYSIGDRDINGVCTRYLTTKDAGSKSPVFVRKSTMRLPHRTTTQVIMIGPGTGFAPFRGFLQDRQFHKNAGKEIGAMHLYYGCRHPDHDYIYKDELAKFQEDEVLTHLVCAFSRAQEHKIYVQDRLWETRDRIWDAINVGAHVYICGDARNMARDVQATLQKIFREIGGKSETEAVAYFKDMEKTKRYQADVWS
Protein: Glutathione S-transferase kappa 1 (EC 2.5.1.18) (GST 13-13) (GST class-kappa) (GSTK1-1) (rGSTK1) (Glutathione S-transferase subunit 13) (P24473)
Organism: Rattus norvegicus (Rat)
Function: Glutathione S-transferase that catalyzes the conjugation of glutathione to exogenous and endogenous compounds.
Subcellular location: Mitochondrion matrix {ECO:0000269|PubMed:1883325}.
Interaction partners:
- Glutathione S-transferase omega-1
- Glutathione S-transferase theta-2
- Glutathione S-transferase P
- Glutathione S-transferase Mu 7
- Glutathione S-transferase theta-1
- Hematopoietic prostaglandin D synthase
- Glutathione S-transferase alpha-4
- Glutathione S-transferase omega-2
- Glutathione S-transferase
- Glutathione S-transferase Mu 5
Sequence:
MGPAPRVLELFYDVLSPYSWLGFEVLCRYQHLWNIKLKLRPALLAGIMKDSGNQPPAMVPHKGQYILKEIPLLKQLFQVPMSVPKDFFGEHVKKGTVNAMRFLTAVSMEQPEMLEKVSRELWMRIWSRDEDITESQNILSAAEKAGMATAQAQHLLNKISTELVKSKLRETTGAACKYGAFGLPTTVAHVDGKTYMLFGSDRMELLAYLLGEKWMGPVPPTLNARL
Protein: Lipid droplet-associated hydrolase (EC 3.1.1.13) (Lipid droplet-associated serine hydrolase) (Q9W0H3)
Organism: Drosophila melanogaster (Fruit fly)
Function: Probable serine lipid hydrolase associated with lipid droplets (By similarity). Appears to lack cholesterol esterase activity. Appears to lack triglyceride lipase activity. Involved in negatively regulating juvenile hormone (JH) and possibly, insulin signaling activities such as triacylglycerols (TAG) storage, and thereby plays a role in the endocrine regulation of organismal growth and survival. Likely functions by enhancing the activity of the JH hydrolase enzymes Jheh1 and Jheh2. Required for lipid droplet positioning and fat storage.
Subcellular location: Lipid droplet {ECO:0000269|PubMed:23525007, ECO:0000269|PubMed:27836991}. Endoplasmic reticulum membrane {ECO:0000269|PubMed:23525007}; Multi-pass membrane protein {ECO:0000255}. Note=Localizes to the endoplasmic reticulum in absence of lipid droplets and translocates to lipid droplets upon lipid storage induction. {ECO:0000269|PubMed:23525007}.
Interaction partners:
- Epoxide hydrolase
- Short-chain dehydrogenase/reductase 3
Sequence:
MQEAYVNINSIPTHIFTWGRWIEETITEKEIVICITGNPGLPGFYTEFAGTLQKELGDLPVWVIGHAGHDDPPEASIREVPQLSGNEELFNLDGQIRHKIAFIEKYVPSDVKIHLIGHSIGAWMILQLLENERIRSRIQKCYMLFPTVERMMESPNGWVFTKVAMPLYSVFGYIFFSFFNFLPVWLRLMLIQIYFLIFSIPRQFLGTALKYSKPSVAEKVVFLADDEMARVRGIQREIVEQNLDLLKFYYGTTDGWVPISYYDQLKKDYPKVDAQLDTKKIDHAFVLRHSQPMAVIVRDMIQQHRRV
Protein: AraC-type transcriptional regulator HrpX (Q3BW17)
Organism: Xanthomonas euvesicatoria pv. vesicatoria (strain 85-10) (Xanthomonas campestris pv. vesicatoria)
Interaction partners:
Sequence:
MILSTYFAAISALSYAERLPTYTSRMLVGAWPQGLQHLQQRRDGQGAADGADDEVSLFGASGDALLILEYQEEAEDAYRQALKAMRGHQRQLRLLSCRNTAWLMLRQRRLSAALNCFAQLAMDRETPPSLCGESLLGKSLTHFHLGQSTLALQTLERAREVLADLESGASDWLRIATALRLDMIAQLRIRRSDRMSDHVFWQATLRQEDATHAFEPSDLRACIADLAESMPVLAQRMRHVRSLLRIAGGDTFGFDAQIDALPAAATGCPPCARQDAQVELALAALAVGRADLAERALAGAGRHHAPRWNLEFEYCQAKISQAMGRTEQALLLYNRYALGAVQCLRSEVQAPRLLESGTPAHVSDDISARLPAKYRRAYSYMITNAHRSDLSINEVAAQIGVTGRALQQAFKSATGLSPTQVLRRYRMQSIRDELLAEGGCGSVLQAASRWGVGSRSALAKGYRQHFNEAPMETLQR
Protein: Rho guanine nucleotide exchange factor 4, isoform B (Q8IQ85)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MLDSNNSSPIGSPNPDAGKRLGFRRQAIQEIISSEKSYLEQLELLMNFFVRPLKEQAIIDCSNHTLLFGQIEMIHNLNGEFLRELEANMENVAHAFLKMAPFFKLYSVYAFDYRGALFIIQDLISKNPVFRKFLEQTESRPEVQRKLNSLMIVPIQRVPRYKLLLEQVLLYTSPADADYKLLKESVKEIEATASHINTCVEEQEITQYLIHLQNSLVNRTPNIVKPSRRVIKEGVLQKITHKGTEIKRYCVLMSDIFMYCKMIKERAPNTVVENSLECCCIFPLKKCKVYEMLPGNFKLTCQSDGIIFGSGDVQLSRTWVGFIRDAIDLHVQCRKTLRKDSSKRTPIRKKDMKKFGADYVLSPNKRKCEYDTVFRNKNRSTDSEEETEDSACFSRKRKVASGILRAPNGNPMGKASSSSSSSVSMKRVAPPPPAPPPPPAVQMRHQPGRPGELATASKENRISKLYKKIAAGDKVANVRGILKRSNVPAPNNDHDPSYGFASRYSDSKSYFRAHNVDNTIPTFVKREDLFNGDNMFPVHLKSHEEICTPPQKKRVKFDDTLDAVSPVLVEKPFAFSSESSSALKPTSLRERIYDFFANLF
Protein: SsrA-binding protein (Small protein B) (P9WGD3)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: Required for rescue of stalled ribosomes mediated by trans-translation. Binds to transfer-messenger RNA (tmRNA), required for stable association of tmRNA with ribosomes. tmRNA and SmpB together mimic tRNA shape, replacing the anticodon stem-loop with SmpB. tmRNA is encoded by the ssrA gene; the 2 termini fold to resemble tRNA(Ala) and it encodes a 'tag peptide', a short internal open reading frame. During trans-translation Ala-aminoacylated tmRNA acts like a tRNA, entering the A-site of stalled ribosomes, displacing the stalled mRNA. The ribosome then switches to translate the ORF on the tmRNA; the nascent peptide is terminated with the 'tag peptide' encoded by the tmRNA and targeted for degradation. The ribosome is freed to recommence translation, which seems to be the essential function of trans-translation.
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00023}. Note=The tmRNA-SmpB complex associates with stalled 70S ribosomes. {ECO:0000255|HAMAP-Rule:MF_00023}.
Interaction partners:
- Large ribosomal subunit protein uL16
- Large ribosomal subunit protein bL19
- Cell division ATP-binding protein FtsE
- Large ribosomal subunit protein bL20
- Small ribosomal subunit protein uS2
- Small ribosomal subunit protein uS3
- Large ribosomal subunit protein uL3
- Large ribosomal subunit protein uL13
- Large ribosomal subunit protein bL27
- Large ribosomal subunit protein uL2
Sequence:
MSKSSRGGRQIVASNRKARHNYSIIEVFEAGVALQGTEVKSLREGQASLADSFATIDDGEVWLRNAHIPEYRHGSWTNHEPRRNRKLLLHRRQIDTLVGKIREGNFALVPLSLYFAEGKVKVELALARGKQARDKRQDMARRDAQREVLRELGRRAKGMT
Protein: ORF K8 (P88939)
Organism: Human herpesvirus 8 type M
Interaction partners:
Sequence:
MPRMKDIPTKSSPGTDNSEKDEAVIEEDLSLNGQPFFTDNTDGGENEVSWTSSLLSTYVGCQPPAIPVCETVIDLTAPSQSGAPGDEHLPCSLNAETKFHIPDPSWTLSHTPPRGPHISQQLPTRRSKRRLHRKFEEERLCTKAKQGAGRPVPASVVKVGNITPHYGEELTRGDAVPAAPITPPSPRVQRPAQPTHVLFSPVFVSLKAEVCDQSHSPTRKQGRYGRVSSKAYTRQLQQV
Protein: ABC transporter C family member 2 (ABC transporter ABCC.2) (AtABCC2) (EC 7.6.2.2) (ATP-energized glutathione S-conjugate pump 2) (Glutathione S-conjugate-transporting ATPase 2) (Multidrug resistance-associated protein 2) (Q42093)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Pump for glutathione S-conjugates. Mediates the transport of S-conjugates such as GSH, S-(2,4-dinitrophenyl)-glutathione (DNP-GS), GSSG, cyanidin 3-glucoside-GS (C3G-GS) and metolachlor-GS (MOC-GS), glucuronides such as 17-beta-estradiol 17-(beta-D-glucuronide) (E(2)17betaG), and of the chlorophyll catabolite such as B.napus nonfluorescent chlorophyll catabolite (Bn-NCC-1).
Subcellular location: Vacuole membrane {ECO:0000269|PubMed:17151019}; Multi-pass membrane protein {ECO:0000255|PROSITE-ProRule:PRU00441}. Note=Tonoplast. {ECO:0000269|PubMed:11115509}.
Interaction partners:
- Glutathione gamma-glutamylcysteinyltransferase 1
- ABC transporter G family member 36
- Vacuolar cation/proton exchanger 4
- Oligopeptide transporter 6
- ABC transporter G family member 40
- ACT domain-containing protein ACR3
- Cytochrome P450, family 76, subfamily C, polypeptide 5
- Cytochrome P450 monooxygenase-like protein
- Cytochrome P450, family 86, subfamily C, polypeptide 4
- Cytochrome P450, family 76, subfamily C, polypeptide 6
Sequence:
MGFEFIEWYCKPVPNGVWTKQVANAFGAYTPCATDSFVLGISQLVLLVLCLYRIWLALKDHKVERFCLRSRLYNYFLALLAAYATAEPLFRLIMGISVLDFDGPGLPPFEAFGLGVKAFAWGAVMVMILMETKIYIRELRWYVRFAVIYALVGDMVLLNLVLSVKEYYSSYVLYLYTSEVGAQVLFGILLFMHLPNLDTYPGYMPVRSETVDDYEYEEISDGQQICPEKHANIFDKIFFSWMNPLMTLGSKRPLTEKDVWYLDTWDQTETLFTSFQHSWDKELQKPQPWLLRALNNSLGGRFWWGGFWKIGNDCSQFVGPLLLNQLLKSMQEDAPAWMGYIYAFSIFVGVVFGVLCEAQYFQNVMRVGYRLRSALIAAVFRKSLRLTNEGRRKFQTGKITNLMTTDAESLQQICQSLHTMWSAPFRIIIALILLYQQLGVASLIGALLLVLMFPLQTVIISKMQKLTKEGLQRTDKRIGLMNEVLAAMDTVKCYAWENSFQSKVQTVRDDELSWFRKSQLLGALNMFILNSIPVLVTIVSFGVFTLLGGDLTPARAFTSLSLFAVLRFPLFMLPNIITQVVNANVSLKRLEEVLATEERILLPNPPIEPGEPAISIRNGYFSWDSKGDRPTLSNINLDVPLGSLVAVVGSTGEGKTSLISAILGELPATSDAIVTLRGSVAYVPQVSWIFNATVRDNILFGSPFDREKYERAIDVTSLKHDLELLPGGDLTEIGERGVNISGGQKQRVSMARAVYSNSDVYIFDDPLSALDAHVGQQVFEKCIKRELGQKTRVLVTNQLHFLSQVDRIVLVHEGTVKEEGTYEELSSNGPLFQRLMENAGKVEEYSEENGEAEADQTAEQPVANGNTNGLQMDGSDDKKSKEGNKKGGKSVLIKQEERETGVVSWRVLKRYQDALGGAWVVMMLLLCYVLTEVFRVTSSTWLSEWTDAGTPKSHGPLFYNLIYALLSFGQVLVTLTNSYWLIMSSLYAAKKLHDNMLHSILRAPMSFFHTNPLGRIINRFAKDLGDIDRTVAVFVNMFMGQVSQLLSTVVLIGIVSTLSLWAIMPLLVLFYGAYLYYQNTAREVKRMDSISRSPVYAQFGEALNGLSTIRAYKAYDRMADINGRSMDNNIRFTLVNMGANRWLGIRLETLGGLMIWLTASFAVMQNGRAENQQAFASTMGLLLSYALNITSLLTGVLRLASLAENSLNAVERVGNYIEIPPEAPPVIENNRPPPGWPSSGSIKFEDVVLRYRPQLPPVLHGVSFFIHPTDKVGIVGRTGAGKSSLLNALFRIVEVEKGRILIDDCDVGKFGLMDLRKVLGIIPQSPVLFSGTVRFNLDPFGEHNDADLWESLERAHLKDTIRRNPLGLDAEVSEAGENFSVGQRQLLSLSRALLRRSKILVLDEATAAVDVRTDALIQKTIREEFKSCTMLIIAHRLNTIIDCDKILVLDSGRVQEFSSPENLLSNEGSSFSKMVQSTGAANAEYLRSLVLDNKRAKDDSHHLQGQRKWLASSRWAAAAQFALAASLTSSHNDLQSLEIEDDSSILKRTNDAVVTLRSVLEGKHDKEIAESLEEHNISREGWLSSLYRMVEGLAVMSRLARNRMQQPDYNFEGNTFDWDNVEM
Protein: Protein YciF (P21362)
Organism: Escherichia coli (strain K12)
Interaction partners:
- Protein YciE
- Uncharacterized protein YciG
- Catalase HPII
- Potassium binding protein Kbp
- UPF0702 transmembrane protein YcaP
Sequence:
MNMKTIEDVFIHLLSDTYSAEKQLTRALAKLARATSNEKLSQAFHAHLEETHGQIERIDQVVESESNLKIKRMKCVAMEGLIEEANEVIESTEKNEVRDAALIAAAQKVEHYEIASYGTLATLAEQLGYRKAAKLLKETLEEEKATDIKLTDLAINNVNKKAENKA
Protein: tRNA-dihydrouridine(47) synthase [NAD(P)(+)]-like (EC 1.3.1.89) (mRNA-dihydrouridine synthase DUS3L) (EC 1.3.1.-) (tRNA-dihydrouridine synthase 3-like) (Q96G46)
Organism: Homo sapiens (Human)
Function: Catalyzes the synthesis of dihydrouridine, a modified base, in various RNAs, such as tRNAs, mRNAs and some long non-coding RNAs (lncRNAs). Mainly modifies the uridine in position 47 (U47) in the D-loop of most cytoplasmic tRNAs. Also able to mediate the formation of dihydrouridine in some mRNAs, thereby regulating their translation.
Interaction partners:
- Pseudouridylate synthase 1 homolog
- tRNA
- tRNA
- Ribosome biogenesis protein BOP1
- tRNA
- tRNA
Sequence:
MAEGTAEAPLENGGGGDSGAGALERGVAPIKRQYLTTKEQFHQFLEAKGQEKTCRETEVGDPAGNELAEPEAKRIRLEDGQTADGQTEEAAEPGEQLQTQKRARGQNKGRPHVKPTNYDKNRLCPSLIQESAAKCFFGDRCRFLHDVGRYLETKPADLGPRCVLFETFGRCPYGVTCRFAGAHLRPEGQNLVQEELAARGTQPPSIRNGLDKALQQQLRKREVRFERAEQALRRFSQGPTPAAAVPEGTAAEGAPRQENCGAQQVPAGPGTSTPPSSPVRTCGPLTDEDVVRLRPCEKKRLDIRGKLYLAPLTTCGNLPFRRICKRFGADVTCGEMAVCTNLLQGQMSEWALLKRHQCEDIFGVQLEGAFPDTMTKCAELLSRTVEVDFVDINVGCPIDLVYKKGGGCALMNRSTKFQQIVRGMNQVLDVPLTVKIRTGVQERVNLAHRLLPELRDWGVALVTLHGRSREQRYTKLADWQYIEECVQAASPMPLFGNGDILSFEDANRAMQTGVTGIMIARGALLKPWLFTEIKEQRHWDISSSERLDILRDFTNYGLEHWGSDTQGVEKTRRFLLEWLSFLCRYVPVGLLERLPQRINERPPYYLGRDYLETLMASQKAADWIRISEMLLGPVPPSFAFLPKHKANAYK
Protein: Putative GPI-anchor transamidase (GPI transamidase) (EC 3.-.-.-) (Phosphatidylinositol glycan anchor biosynthesis protein class K) (Q8T4E1)
Organism: Drosophila melanogaster (Fruit fly)
Function: Mediates GPI anchoring in the endoplasmic reticulum, by replacing a protein's C-terminal GPI attachment signal peptide with a pre-assembled GPI. During this transamidation reaction, the GPI transamidase forms a carbonyl intermediate with the substrate protein (By similarity).
Interaction partners:
- Glycosylphosphatidylinositol anchor attachment 1
- LD37974p
- Phosphatidylinositol glycan anchor biosynthesis class T
- Phosphatidylinositol glycan anchor biosynthesis class S
- GPI ethanolamine phosphate transferase 3
- Phosphatidylinositol glycan anchor biosynthesis class F
- GPI inositol-deacylase
- GPI mannosyltransferase 1
- Prolyl 3-hydroxylase sudestada1
- N-acetylglucosaminyl-phosphatidylinositol de-N-acetylase
Sequence:
MFNIMLVKFVVIFALILASCRVEADNTSVLPEGFVDAAQRSTHTNNWAVLVDASRFWFNYRHVANVLSIYRSVKRLGIPDSQIILMIADDMACNARNPRPGQVYNNANQHINVYGDDVEVDYRGYEVTVENFVRLLTGRTQNGTARSKKLLSDAGSNVLIYLTGHGGDGFLKFQDSEEITSQELADGIQQMWEKKRYNELFFMVDTCQAASLYEKFTSPNVLAVASSLVGEDSLSHHVDPSIGVYMIDRYTYYALEFLEKVQPFSKRTIGEFLQVCPKRVCISTVGVRKDLYPRDPHKVPITDFFGAIRPTRVSTDRINVTLANEDDFIFDKDKMVTKKPFKIVMESQFPSELFK
Protein: Target of rapamycin complex 2 subunit AVO1 (TORC2 subunit AVO1) (Adheres voraciously to TOR2 protein 1) (Q08236)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Component of TORC2, which regulates cell cycle-dependent polarization of the actin-cytoskeleton and cell wall integrity. TORC2 controls polarity of the actin cytoskeleton, which is required for orienting the secretory pathway toward discrete growth sites, via the RHO1/PKC1/MAPK cell integrity pathway.
Subcellular location: Cell membrane {ECO:0000269|PubMed:12631735}; Peripheral membrane protein {ECO:0000269|PubMed:12631735}; Cytoplasmic side {ECO:0000269|PubMed:12631735}. Vacuole membrane {ECO:0000269|PubMed:12631735}; Peripheral membrane protein {ECO:0000269|PubMed:12631735}; Cytoplasmic side {ECO:0000269|PubMed:12631735}.
Interaction partners:
- Target of rapamycin complex 2 subunit AVO2
- Target of rapamycin complex 2 subunit BIT61
- Serine/threonine-protein kinase TOR2
- Target of rapamycin complex subunit LST8
- Target of rapamycin complex 2 subunit TSC11
- Probable target of rapamycin complex 2 subunit BIT2
- Serine/threonine-protein kinase TOR1
- Phosphatidylinositol 4,5-bisphosphate-binding protein SLM1
- Target of rapamycin complex 1 subunit KOG1
- Target of rapamycin complex 1 subunit TCO89
Sequence:
MDTVTVLNELRAQFLRVCPEKDQMKRIIKPYIPVDEFNTEQCLDSSIRELYMNSDGVSLLPELESPPVSKDFMENYASLGKMRIMRENEGQKGKANQNLIGAEKTERDEEETRNLQDKSAKNTLIVEENGTLRYNPLNSSASNSLLNDDDHTSGKHHKTSSKEDSYLNSSMEMQKKSSKRSSLPFVRIFKSRRDHSNTSGNKNVMNTTNTRAKSSTLHPPGARHNKKGSKFDMNFDFDENLEEEDDDDDDDEEGDDIHSQFFQLDDDFDAKGSGASPAHKGINGMSNNKNNTYTNNRNSISILDDRESSNGNIGSASRLKSHFPTSQKGKIFLTDNKNDGQKSDSLNANKGIHGDGSSASGNGSVSRDGLTETESNNISDMESYINEKDLDDLNFDTVTSNINKTVSDLGGHESTNDGTAVMNRDSKDSRSNSNEFNAQNRDRITPGSSYGKSLLGSEYSEERYSNNDSSTMESGEMSLDSDMQTNTIPSHSIPMSMQKYGIYHGDDDSTLNNVFDKAVLTMNSSRHPKERRDTVISGKEPTSLTSSNRKFSVSSNLTSTRSPLLRGHGRTSSTASSEHMKAPKVSDSVLHRARKSTLTLKQDHSQPSVPSSVHKSSKEGNILIEKTTDYLVSKPKASQLSNMFNKKKKRTNTNSVDVLEYFSFVCGDKVPNYESMGLEIYIQASKKYKRNSFTTKVRKSSTIFEVIGFALFLYSTEKKPDNFEEDGLTVEDISNPNNFSLKIVDEDGEPFEDNFGKLDRKSTIQSISDSEVVLCKVDDAEKSQNEIETPLPFETGGGLMDASTLDANSSHDTTDGTINQLSFYKPIIGNEDDIDKTNGSKIIDVTVYLYPNVNPKFNYTTISVLVTSHINDILVKYCKMKNMDPNEYALKVLGKNYILDLNDTVLRLDGINKVELISKKDARELHLEKMKPDLKKPVLPTIQSNDLTPLTLEPLNSYLKADAGGAVAAIPENTKVTSKAKKISTKYKLGLAKQHSSSSVASGSVSTAGGLANGNGFFKNKNSSKSSLHGTLQFHNINRSQSTMEHTPDTPNGVGDNFQDLFTGAYHKYKVWRRQQMSFINKHERTLAIDGDYIYIVPPEGRIHWHDNVKTKSLHISQVVLVKKSKRVPEHFKIFVRREGQDDIKRYYFEAVSGQECTEIVTRLQNLLSAYRMNHK
Protein: Photosystem II reaction center protein L (PSII-L) (Q2LII8)
Organism: Oryza meyeriana var. granulata
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004167}; Single-pass membrane protein {ECO:0000256|ARBA:ARBA00004167}. Plastid, chloroplast thylakoid membrane {ECO:0000256|HAMAP-Rule:MF_01317}; Single-pass membrane protein {ECO:0000256|HAMAP-Rule:MF_01317}.
Interaction partners:
Sequence:
MTQSNPNEQNVELNRTSLYWGLLLIFVLAVLFSNYFFN
Protein: Aminopeptidase (EC 3.4.11.-) (Q9W2S8)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Glutamate--cysteine ligase
- GCS light chain
- glutathione-specific gamma-glutamylcyclotransferase
- glutathione-specific gamma-glutamylcyclotransferase
- Aspartate aminotransferase, cytoplasmic
- Aspartate aminotransferase
- cystathionine gamma-lyase
- FI04487p
- Cysteine dioxygenase
- Jonah 74E
Sequence:
MIKLPWYLIVLHLCLPIGGTGATASNLRPLHYNLSLLTEVEPLKLSGNFSGEVIIRLRVWRETRTIILSNNGLQVGENVLLVRRNTGGRVTVRKMWQASSVHQLGIVFNSMLWLGEEYTLVVQFSGQLSRASGYFVGGYMDSKHHPQWIAVTQLAPNLANTVFPCFENRTFLAPFILNLAHPRGTNAVSNMRVLKTSDHEKDDYVWTTFQQTPAMSVQKLAFSINRFTNRTSAEIPKGPALTTWLRPKIADQGDYAISITPQIIVFFISLFGKPYPAMKIDQLVLPDTAYQSHEHLGLVSYPEAAFLYSAQRSTTRAKQQVASHVAQEFAHHWLSDLENAALYWLHNGLSDYVSGFAVDNVEPAWRFHELSMVRQALAVLVEDSKSSAYPMSLAYASKSSDTQANQKSALLFRMLHSLIGTQAFLNALRLYLQRSHKGSSSNQAFLWHTLQEESDNQMSLRQDIKVSQLMDSWTMQPGYPLIRVVRNYDTNEVTVTQERFLRNPGKLMQKRQQCWWVPLTFATAGIDSFVSTLPSEWLTCQGRQTASPLILNEVAQPDKWVVFNLRLATPCRITYDERNWQLIGNALSGTNASSIDRFTRAQLISDVLNLAGAGVVTYDLALNFLGHLRNEDEFIVWQAADTYLEWLHRTLRQTTIISTFKGFMRDLLQTKFDELFKRDGSAAENANITELMVIVLQLSCRTDLESCADFALKEFAGLTLETNRIPVDLSETIYCTAIQFGTEADWTLLRRLYTRSNVSEERRILLSAMACSRENWALDKLLNLAFAGRYMPKDDVLLIFSAVAQNPLGYNIAKKYLVDNIKAIIKLYGSNTDELAQLVTVLMKEVTTEEELNALRMFMRTDLQNLPGFEIAFRRILELGEDNISWHNRQYHNLLAAVCNITGSIEPQCIY
Protein: Probable 4-aminobutyrate aminotransferase (EC 2.6.1.19) ((S)-3-amino-2-methylpropionate transaminase) (EC 2.6.1.22) (GABA aminotransferase) (GABA-AT) (Gamma-amino-N-butyrate transaminase) (GABA transaminase) (Glutamate:succinic semialdehyde transaminase) (L-AIBAT) (P94427)
Organism: Bacillus subtilis (strain 168)
Interaction partners:
- Succinate-semialdehyde dehydrogenase [NADP
- HTH-type transcriptional regulatory protein GabR
- Malonate-semialdehyde dehydrogenase
- Putative aldehyde dehydrogenase YwdH
- Putative aldehyde dehydrogenase AldX
- Putative aldehyde dehydrogenase DhaS
- Putative aldehyde dehydrogenase AldY
- Aspartate 1-decarboxylase
- Pantothenate synthetase
- Acetyl-coenzyme A synthetase
Sequence:
MSQTTASITTAQWQQKRDQFVSKGVSNGNRSLAVKGEGAELYDLDGRRFIDFAGAIGTLNVGHSHPKVVEAVKRQAEELIHPGFNVMMYPTYIELAEKLCGIAPGSHEKKAIFLNSGAEAVENAVKIARKYTKRQGVVSFTRGFHGRTNMTMSMTSKVKPYKFGFGPFAPEVYQAPFPYYYQKPAGMSDESYDDMVIQAFNDFFIASVAPETVACVVMEPVQGEGGFIIPSKRFVQHVASFCKEHGIVFVADEIQTGFARTGTYFAIEHFDVVPDLITVSKSLAAGLPLSGVIGRAEMLDAAAPGELGGTYAGSPLGCAAALAVLDIIEEEGLNERSEEIGKIIEDKAYEWKQEFPFIGDIRRLGAMAAIEIVKDPDTREPDKTKAAAIAAYANQNGLLLLTAGINGNIIRFLTPLVISDSLLNEGLSILEAGLRA
Protein: von Willebrand factor A domain-containing protein 5A (Q8C1D4)
Organism: Mus musculus (Mouse)
Interaction partners:
Sequence:
MVRSGGLLTSIRDPVALKSIAVTLSINDFVAGVSATLNYENEEKSPLEAFFVFPMDEDSAVYSFEAFVDGKKIVAELQDKYQAHKRYEEALSGGYQAYLLEEDKCSRDVFCCNVGNLQPGSKVSLTLRYVQELPLEDDGALRYVLPAILNPRYHLSDGREDSNLDMKTPIVPLEELPYTLSMVATISSQLGISTIQSNCPLNPIEYTGDNKTSAQVSLAEGHKFDRDVELLIFYRKVHSPSVAVEMGMSGRPSDSLMGAPSAMVSFYPDIPEVETTTKCGEFVFLMDRSRSMNSPMSSKDKSQLRIDAAKETLILLLKSLPMGCYFNIYGFGATHEEFFPDSVMYNQETMQIAVKKVKRLLADLGGTELLTPLRKIFRKPPIPGHPLQVFVFTDGEVVETFSVIREVMFQSKKHRCFSFGIGEGASTSLIKNLARVSGGTAEFITGNDRMQSKALRSLRRSLQSVVEDVSLSWNLPPKMFAPMLSPEQTSIFRGQRLIIYSLLIGKIPKEEATGEVCLSYKLHGKSYEEKVTFSLQPKPDDNLTIHRLAAKSMIQSKDFGFKETSLMYKRDVLDISLESGVMSSFTAFVAINKELNEPIQGPLVHRDIPRPILLGAGPNRPSDGGYPKTLFCASAPVTLPPWLKGSGKCVGTILMPNGTPQQRQNSQKKKCVVHTDTRPELPHLAKYDSYPQGSKEHSIAQLIYLQNADGSWDMNEDLAKILSTSLEDITAACPTEVLEPSAWATMLAVIWLHANGKELKDEWELLERKAVVWLHNNSVRGFNKLIRTANKLLKTSLSPSIFKL
Protein: 3-hydroxydecanoyl-[acyl-carrier-protein] dehydratase (EC 4.2.1.59) (3-hydroxyacyl-[acyl-carrier-protein] dehydratase FabA) (Beta-hydroxydecanoyl thioester dehydrase) (Trans-2-decenoyl-[acyl-carrier-protein] isomerase) (EC 5.3.3.14) (O33877)
Organism: Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Function: Necessary for the introduction of cis unsaturation into fatty acids. Catalyzes the dehydration of (3R)-3-hydroxydecanoyl-ACP to E-(2)-decenoyl-ACP and then its isomerization to Z-(3)-decenoyl-ACP. Can catalyze the dehydratase reaction for beta-hydroxyacyl-ACPs with saturated chain lengths up to 16:0, being most active on intermediate chain length (By similarity).
Subcellular location: Cytoplasm {ECO:0000250}.
Interaction partners:
- 3-oxoacyl-[acyl-carrier-protein] synthase 1
- 3-hydroxyacyl-[acyl-carrier-protein] dehydratase FabZ
- Enoyl-[acyl-carrier-protein] reductase FabI
- Enoyl-[acyl-carrier-protein] reductase
- 3-oxoacyl-[acyl-carrier-protein] reductase FabG
- Malonyl CoA-acyl carrier protein transacylase
- Beta-ketoacyl-[acyl-carrier-protein] synthase FabY
- 2,3-dihydroxy-2,3-dihydro-p-cumate dehydrogenase
- Probable short-chain dehydrogenase
- Probable short-chain dehydrogenase
Sequence:
MTKQHAFTREDLLRCSRGELFGPGNAQLPAPNMLMIDRIVHISDVGGKYGKGELVAELDINPDLWFFACHFEGDPVMPGCLGLDAMWQLVGFYLGWQGNPGRGRALGSGEVKFFGQVLPTAKKVTYNIHIKRTINRSLVLAIADGTVSVDGREIYSAEGLRVGLFTSTDSF
Protein: PAK4-inhibitor INKA1 (Induced in neural crest by AP2-alpha protein homolog) (Inca) (Inka-box actin regulator 1) (Q9CX62)
Organism: Mus musculus (Mouse)
Function: Inhibitor of the serine/threonine-protein kinase PAK4. Acts by binding PAK4 in a substrate-like manner, inhibiting the protein kinase activity.
Subcellular location: Nucleus {ECO:0000250|UniProtKB:Q96EL1}. Cytoplasm {ECO:0000250|UniProtKB:Q96EL1}. Note=Mainly nuclear. Relocalizes to the cytoplasm following interaction with PAK4. {ECO:0000250|UniProtKB:Q96EL1}.
Interaction partners:
- Serine/threonine-protein kinase PAK 4
- Serine/threonine-protein kinase PAK 5
Sequence:
MHSARLDSFLSQLRWELLCARDTGSPPMSGPLQPKPRTDQNVQPKRQFRASDVLEEDSVCCVEEEEEEGLVAEDKGLPLGCPREHALDWDSGFSEVSGSTWREEEPSVPQRQAPRERPPHSQRFSVSDIPMRSRAAVTNIPPAHRPRPKSTPDACLEHWQGLEAEDWTAALLNRGRSRQPLVLGDNCFADLVHNWMELPEATSEGSDGDVPRARARPPQFLLGLSEQLRRRLARARRTAMASKRLSCPPRSEPDLPADISRFAALMNCRSRQPIIYNDVSYL
Protein: RIC3 acetylcholine receptor chaperone, isoform I (E1JGP7)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Endoplasmic reticulum membrane {ECO:0000256|ARBA:ARBA00004586}.
Interaction partners:
Sequence:
MPATATSKPRAPLVEEGMTPKKTALIIVTVIGCIAILWPKVFHPMMFGGVPPSQPNFKDPRAAPGGLRQERPAHLHPESIYQAMRERGRAIPATPTVPILERKTSPSNPPPRIVDGRPGPIPGMRPPMGAGALHQPQQRGSSMGFLMPLYTIGIVVFFGYTLMKIMFKKQVPNDPYGAAPPNPAFRQEVFGSQNHSQVEDLGGSKLGWREHQTIVTAIQGLIDAADEQLNGQDKQRATSDTETDSNKKNDNEKTREQPLDKQNLSNGHASSTDQNPEQETVAKGARKRRDLSAEQELTVLGMELTASCEGGHKWTGRPPTPVFRAPSEHSKLEDNLPEPQSIYLEGALAHESQILVADSQIKREEVYDSELNGSAEEPAIILSSRMTLSLINLDANQQNGNAGKSAVESPLADDIEIIGHDEQ