wanglab/gogpt-training-data huggingface dataset:
Protein: Erythrocyte membrane protein 1, PfEMP1 (Q8IIZ5)
Organism: Plasmodium falciparum (isolate 3D7)
Interaction partners:
Sequence:
MEPHGGSGGGGDVIDHQSAKHLLDSIGKIVHDQVEKEAADYRSSLQGRLKDATYSKKPDNQEKPSDPCELKHEYRTNATNGTSYPCRAGKEERFSDTLGGQCTDQQIEGNDRNNGGACAPYRRLHLCNKNMVKMDTNNDDSSKAKHNLLLDVCMAAKYEGYSINTHYPKHQEKYKDTGTASQLCTVLARSFADIGDIVRGRDLFRGNKKKSENKREKEKLEENFKKYFQQIHEDVTSTSGKNRKALRDRYHKDGPDYYQLREDWWNNNRKMVWIAMTCEAGGSQYFRRTCSNGISETNNKCRCTIETVPTYFDYVPQYLRWFEEWAEDFCRKKKHKLKDAIDKCRGQYQDADRYCDLNGYDCEKTKRGINMYRWDHKCTGCFLSCSHFRTWIDNQKEQFHKQKKIYDKEITRGGSDHKGYEKKFYGKLKGTDYKDVGKFLEKLSDEDVCTKFREDEGIIDFKNVNSSSGSGGGEGSNKTFSHTEYCQACPLCGVEKESNGGGGNTKWKRKEDMDKCPPINLYKPIDDKGGITINFLYSGDEPTEIGKKLNAFCLTHSGNSVVSSSSARGNGASRDKNGGSDSQDLYQKWTCYEIDELEKDEKEDGVDDPQYEKDVKTGGGLCILEKTNGKEKVNKQKTSHEMQKTFNPFFYYWVVHMLKDSIHWRTKKLDKCINNSNESKACKNNKKCNKECECFQRWITQKQQEWEQIKKHFRKQKNIDNVGGFFKLSHDDVLQQVLDKDLLLKSLQEAYGKPEDIKHIKDLLEKEAAAVAVVLGGKDNTTIDKLLNHEDKDAKDCLKKQEECKEQERGGVARSGTGPRPPSAGDTVHEVEEKEEEEQEEEEEDEGDDGDGDGKGDVDQDNTVDVGAKEAPKVVEGPTTTQNEVNPCQIVDNLFSNPEQFKDACGLKYGPKAPTSWKCVTPSGKPGEAPSGDSTATGSSGSICVPPRRRRLYVTPLTRLAGDNTAASVSPQVRGETPLASTSASTPSGSHRDPLLAAFVESAAIETFFLWDRYKKEWEAQKKAEQEQSGLLLGESSEALGMTAITSGAGAPKTPLTQQPVASSDDPQSKLQKSGDIPPPFLRQMFYTIADYKDILYSGSNDDNTKSSTYNDILKGDKEMKAKEEKIKEAIQKFFENGDKKPDGGTTPSSWWNNNAKHIWNGMICALTYTDNTNGGPPTQDGEVKNALLDDNNKPKTNAGPKSNPHDYTYEKVVLKEDEENGPKTGSSTQPLTLKNFVERPPYFRYLEEWGEEFCRKQKHKLYIIEKECKVEANGRDGKKNPKCSCYGENCNDNLIADPSIFPDFNCPKCGKHCSSYRKWINTKKTQYEKQKEAYGEQQKKCQKENNGAQGNNGGNGVCGTLEATYTEAKDFLQKLGSCKNNSEEANIDFGDKTKTFGPSENCKPCSEFKINCRNGNCGSDPKVECNGKNKNSISANHIIDDKNGNGNIEMLVSDDSTTEFEVDELKVCKGAGIFEGIRKDVWKCGNVCGYNVCKPKNVKGEKGNGNQIIIIRALFKRWLEYFLQDYNKINAKISYCKENGGTNICIKNCADKWIRKKKEEWKKIKDHYLEKKHENGDNNMKSLVTDILRSLQPQTELNKAIKPCGSLDAFESFCGLNGDENSKKNNDNQDAIDCMITNLQKKIGECKKNHAKTSGSDCNTAPTSDTTLDDEDLSLEEENTVEQPKFCPKPPEPKAEEKGACDPAPTTPKETASPADSGEGTKEHPSPPPTPDPAAPTSPPLPPLTTALVTSTLAWSVGIGFAAFTYFFLKKKTKASVGNLFQILQIPKSDYDIPTKLSPNRYIPYTSGKYRGKRYIYLEGDSGTDSGYTDHYSDITSSSESEYEEMDINDIYAPRAPKYKTLIEVVLEPSKRDIPSDDIPNNDTPSSKITDNEWNTLKHDFISNMLQNTQNTEPNMLGYNVDNNTHPTMSRHNVEEKPFIMSIHDRNLLNGEEYSYNVNMVNSMNDIPMSGKNDVYSGIDLINDSLSGGEPIDIYDEVLKRKENELFGTNHVKQTSIHSVAKPISDDPIHNQLELFHTWLDRHRDMCEKWENHHERLAKLKEEWENETHSGNTHPSDSNKTLNTDVSIQIHMDNPKPINEFTNMDTYPENSTMDTILDDLDKYKEPYYDVQDDIYYDVNDDNDISTVDSNNMDIPSKVQIEMDVNTKLVKEKYPIADVWDI
Protein: ATP-binding cassette sub-family G member 8 (EC 7.6.2.-) (Sterolin-2) (Q9DBM0)
Organism: Mus musculus (Mouse)
Function: ABCG5 and ABCG8 form an obligate heterodimer that mediates Mg(2+)- and ATP-dependent sterol transport across the cell membrane. Plays an essential role in the selective transport of the dietary cholesterol in and out of the enterocytes and in the selective sterol excretion by the liver into bile. Plays an important role in preventing the accumulation of dietary plant sterols in the body. Required for normal sterol homeostasis. The heterodimer with ABCG5 has ATPase activity.
Subcellular location: Cell membrane {ECO:0000269|PubMed:12208867, ECO:0000269|PubMed:18402465, ECO:0000305|PubMed:16352607}; Multi-pass membrane protein {ECO:0000305}. Apical cell membrane {ECO:0000269|PubMed:12208867, ECO:0000269|PubMed:14504269, ECO:0000269|PubMed:16867993, ECO:0000269|PubMed:18402465}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
- ATP-binding cassette sub-family G member 5
- Cytochrome P450 7A1
- NPC1-like intracellular cholesterol transporter 1
- 3-hydroxy-3-methylglutaryl-coenzyme A reductase
- Oxysterols receptor LXR-alpha
- Sterol regulatory element-binding protein 2
- Bile acid receptor
- Oxysterols receptor LXR-beta
- Sarcoplasmic/endoplasmic reticulum calcium ATPase 2
- Sodium/potassium-transporting ATPase subunit alpha-2
Sequence:
MAEKTKEETQLWNGTVLQDASQGLQDSLFSSESDNSLYFTYSGQSNTLEVRDLTYQVDIASQVPWFEQLAQFKIPWRSHSSQDSCELGIRNLSFKVRSGQMLAIIGSSGCGRASLLDVITGRGHGGKMKSGQIWINGQPSTPQLVRKCVAHVRQHDQLLPNLTVRETLAFIAQMRLPRTFSQAQRDKRVEDVIAELRLRQCANTRVGNTYVRGVSGGERRRVSIGVQLLWNPGILILDEPTSGLDSFTAHNLVTTLSRLAKGNRLVLISLHQPRSDIFRLFDLVLLMTSGTPIYLGAAQQMVQYFTSIGHPCPRYSNPADFYVDLTSIDRRSKEREVATVEKAQSLAALFLEKVQGFDDFLWKAEAKELNTSTHTVSLTLTQDTDCGTAVELPGMIEQFSTLIRRQISNDFRDLPTLLIHGSEACLMSLIIGFLYYGHGAKQLSFMDTAALLFMIGALIPFNVILDVVSKCHSERSMLYYELEDGLYTAGPYFFAKILGELPEHCAYVIIYAMPIYWLTNLRPVPELFLLHFLLVWLVVFCCRTMALAASAMLPTFHMSSFFCNALYNSFYLTAGFMINLDNLWIVPAWISKLSFLRWCFSGLMQIQFNGHLYTTQIGNFTFSILGDTMISAMDLNSHPLYAIYLIVIGISYGFLFLYYLSLKLIKQKSIQDW
Protein: Replication protein A 14 kDa subunit (RP-A p14) (Replication factor A protein 3) (RF-A protein 3) (Q9CQ71)
Organism: Mus musculus (Mouse)
Function: As part of the heterotrimeric replication protein A complex (RPA/RP-A), binds and stabilizes single-stranded DNA intermediates, that form during DNA replication or upon DNA stress. It prevents their reannealing and in parallel, recruits and activates different proteins and complexes involved in DNA metabolism. Thereby, it plays an essential role both in DNA replication and the cellular response to DNA damage. In the cellular response to DNA damage, the RPA complex controls DNA repair and DNA damage checkpoint activation. Through recruitment of ATRIP activates the ATR kinase a master regulator of the DNA damage response. It is required for the recruitment of the DNA double-strand break repair factors RAD51 and RAD52 to chromatin, in response to DNA damage. Also recruits to sites of DNA damage proteins like XPA and XPG that are involved in nucleotide excision repair and is required for this mechanism of DNA repair. Also plays a role in base excision repair (BER), probably through interaction with UNG. Also recruits SMARCAL1/HARP, which is involved in replication fork restart, to sites of DNA damage. May also play a role in telomere maintenance. RPA3 has its own single-stranded DNA-binding activity and may be responsible for polarity of the binding of the complex to DNA.
Subcellular location: Nucleus {ECO:0000250}.
Interaction partners:
- Replication protein A 70 kDa DNA-binding subunit
- Replication protein A 32 kDa subunit
- RecQ-like DNA helicase BLM
- RecQ-mediated genome instability protein 1
- DNA topoisomerase 3-alpha
- Bifunctional 3'-5' exonuclease/ATP-dependent helicase WRN
- SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily A-like protein 1
- DNA repair protein RAD52 homolog
- Claspin
- TIMELESS-interacting protein
Sequence:
MEDIMQLPKARVNASMLPQYIDRPVCFVGKLEKIHPTGKMFILSDGEGKNGTIELMEPLDEEISGIVEVVGKVTAKATVLCASYTLFKEDTNRFDLELYNEAVKIINELPQFFPVGLPQHE
Protein: Bidirectional sugar transporter SWEET8 (AtSWEET8) (Protein RUPTURED POLLEN GRAIN 1) (Protein SUGARS WILL EVENTUALLY BE EXPORTED TRANSPORTERS 8) (Q8LFH5)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Mediates both low-affinity uptake and efflux of sugar across the plasma membrane. Required, in pollen, for microspore cell integrity and primexine pattern formation.
Subcellular location: Cell membrane {ECO:0000269|PubMed:18434608, ECO:0000269|PubMed:24027245}; Multi-pass membrane protein {ECO:0000269|PubMed:18434608}.
Interaction partners:
- Protein DEFECTIVE IN EXINE FORMATION 1
- ATP-dependent helicase/deoxyribonuclease subunit B
- No exine formation 1
- Cytochrome P450 703A2
- Type III polyketide synthase B
- Callose synthase 5
- Disease resistance protein RPM1
- Cytochrome P450 704B1
- Type III polyketide synthase A
- Serine/arginine-rich SC35-like splicing factor SCL33
Sequence:
MVDAKQVRFIIGVIGNVISFGLFAAPAKTFWRIFKKKSVEEFSYVPYVATVMNCMLWVFYGLPVVHKDSILVSTINGVGLVIELFYVGVYLMYCGHKKNHRRNILGFLALEVILVVAIILITLFALKGDFVKQTFVGVICDVFNIAMYGAPSLAIIKVVKTKSVEYMPFLLSLVCFVNAGIWTTYSLIFKIDYYVLASNGIGTFLALSQLIVYFMYYKSTPKEKTVKPSEVEISATERV
Protein: Inorganic phosphate transporter 1-4 (AtPht1;4) (H(+)/Pi cotransporter) (Q96303)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: High-affinity transporter for external inorganic phosphate. Acts as a H(+):phosphate symporter in both low- and high-Pi conditions. Confers sensitivity to arsenate.
Subcellular location: Cell membrane {ECO:0000269|PubMed:15060130, ECO:0000269|PubMed:24122828, ECO:0000305|PubMed:15308754}; Multi-pass membrane protein {ECO:0000305|PubMed:15308754}. Note=Localizes at the plasma membrane, where it interacts with NLA. {ECO:0000269|PubMed:24122828}.
Interaction partners:
- Inorganic phosphate transporter 2-1, chloroplastic
- SPX domain-containing protein 1
- SEC12-like protein 1
- Probable ubiquitin-conjugating enzyme E2 24
- Phosphate transporter PHO1
- Ascorbate transporter, chloroplastic
- Probable anion transporter 5
- SPX domain-containing protein 3
- Sodium-dependent phosphate transport protein 1, chloroplastic
- Protein PHOSPHATE STARVATION RESPONSE 1
Sequence:
MAREQLQVLNALDVAKTQWYHFTAIIIAGMGFFTDAYDLFCISLVTKLLGRIYYHVEGAQKPGTLPPNVAAAVNGVAFCGTLAGQLFFGWLGDKLGRKKVYGMTLMVMVLCSIASGLSFGHEPKAVMATLCFFRFWLGFGIGGDYPLSATIMSEYANKKTRGAFVSAVFAMQGFGIMAGGIFAIIISSAFEAKFPSPAYADDALGSTIPQADLVWRIILMAGAIPAAMTYYSRSKMPETARYTALVAKDAKQAASDMSKVLQVEIEPEQQKLEEISKEKSKAFGLFSKEFMSRHGLHLLGTTSTWFLLDIAFYSQNLFQKDIFSAIGWIPPAQSMNAIQEVFKIARAQTLIALCSTVPGYWFTVAFIDVIGRFAIQMMGFFFMTVFMFALAIPYNHWTHKENRIGFVIMYSLTFFFANFGPNATTFVVPAEIFPARFRSTCHGISAASGKLGAMVGAFGFLYLAQNPDKDKTDAGYPPGIGVRNSLIVLGVVNFLGILFTFLVPESKGKSLEEMSGENEDNENSNNDSRTVPIV
Protein: Endo-1,4-beta-xylanase Y (Xylanase Y) (EC 3.2.1.8) (1,4-beta-D-xylan xylanohydrolase Y) (XylY) (P51584)
Organism: Acetivibrio thermocellus (Hungateiclostridium thermocellum) (Clostridium thermocellum)
Interaction partners:
Sequence:
MKNKRVLAKITALVVLLGVFFVLPSNISQLYADYEVVHDTFEVNFDGWCNLGVDTYLTAVENEGNNGTRGMMVINRSSASDGAYSEKGFYLDGGVEYKYSVFVKHNGTGTETFKLSVSYLDSETEEENKEVIATKDVVAGEWTEISAKYKAPKTAVNITLSITTDSTVDFIFDDVTITRKGMAEANTVYAANAVLKDMYANYFRVGSVLNSGTVNNSSIKALILREFNSITCENEMKPDATLVQSGSTNTNIRVSLNRAASILNFCAQNNIAVRGHTLVWHSQTPQWFFKDNFQDNGNWVSQSVMDQRLESYIKNMFAEIQRQYPSLNLYAYDVVNEAVSDDANRTRYYGGAREPGYGNGRSPWVQIYGDNKFIEKAFTYARKYAPANCKLYYNDYNEYWDHKRDCIASICANLYNKGLLDGVGMQSHINADMNGFSGIQNYKAALQKYINIGCDVQITELDISTENGKFSLQQQADKYKAVFQAAVDINRTSSKGKVTAVCVWGPNDANTWLGSQNAPLLFNANNQPKPAYNAVASIIPQSEWGDGNNPAGGGGGGKPEEPDANGYYYHDTFEGSVGQWTARGPAEVLLSGRTAYKGSESLLVRNRTAAWNGAQRALNPRTFVPGNTYCFSVVASFIEGASSTTFCMKLQYVDGSGTQRYDTIDMKTVGPNQWVHLYNPQYRIPSDATDMYVYVETADDTINFYIDEAIGAVAGTVIEGPAPQPTQPPVLLGDVNGDGTINSTDLTMLKRSVLRAITLTDDAKARADVDKNGSINSTDVLLLSRYLLRVIDKFPVAENPSSSFKYESAVQYRPAPDSYLNPCPQAGRIVKETYTGINGTKSLNVYLPYGYDPNKKYNIFYLMHGGGENENTIFSNDVKLQNILDHAIMNGELEPLIVVTPTFNGGNCTAQNFYQEFRQNVIPFVESKYSTYAESTTPQGIAASRMHRGFGGFSMGGLTTWYVMVNCLDYVAYFMPLSGDYWYGNSPQDKANSIAEAINRSGLSKREYFVFAATGSDHIAYANMNPQIEAMKALPHFDYTSDFSKGNFYFLVAPGATHWWGYVRHYIYDALPYFFHE
Protein: Casein kinase I isoform delta (CKI-delta) (CKId) (EC 2.7.11.1) (Tau-protein kinase CSNK1D) (EC 2.7.11.26) (P48730)
Organism: Homo sapiens (Human)
Function: Essential serine/threonine-protein kinase that regulates diverse cellular growth and survival processes including Wnt signaling, DNA repair and circadian rhythms. It can phosphorylate a large number of proteins. Casein kinases are operationally defined by their preferential utilization of acidic proteins such as caseins as substrates. Phosphorylates connexin-43/GJA1, MAP1A, SNAPIN, MAPT/TAU, TOP2A, DCK, HIF1A, EIF6, p53/TP53, DVL2, DVL3, ESR1, AIB1/NCOA3, DNMT1, PKD2, YAP1, PER1 and PER2. Central component of the circadian clock. In balance with PP1, determines the circadian period length through the regulation of the speed and rhythmicity of PER1 and PER2 phosphorylation. Controls PER1 and PER2 nuclear transport and degradation. YAP1 phosphorylation promotes its SCF(beta-TRCP) E3 ubiquitin ligase-mediated ubiquitination and subsequent degradation. DNMT1 phosphorylation reduces its DNA-binding activity. Phosphorylation of ESR1 and AIB1/NCOA3 stimulates their activity and coactivation. Phosphorylation of DVL2 and DVL3 regulates WNT3A signaling pathway that controls neurite outgrowth. Phosphorylates NEDD9/HEF1 (By similarity). EIF6 phosphorylation promotes its nuclear export. Triggers down-regulation of dopamine receptors in the forebrain. Activates DCK in vitro by phosphorylation. TOP2A phosphorylation favors DNA cleavable complex formation. May regulate the formation of the mitotic spindle apparatus in extravillous trophoblast. Modulates connexin-43/GJA1 gap junction assembly by phosphorylation. Probably involved in lymphocyte physiology. Regulates fast synaptic transmission mediated by glutamate.
Subcellular location: Cytoplasm. Nucleus. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000269|PubMed:14654843}. Cytoplasm, perinuclear region. Cell membrane. Cytoplasm, cytoskeleton, spindle. Golgi apparatus. Note=Localized at mitotic spindle microtubules, and at the centrosomes and interphase in interphase cells. Recruited to the spindle apparatus and the centrosomes in response to DNA-damage. Correct subcellular localization requires kinase activity.
Interaction partners:
- Period circadian protein homolog 2
- Cryptochrome-1
- Casein kinase I isoform epsilon
- Period circadian protein homolog 3
- Cryptochrome-2
- Period circadian protein homolog 1
- Protein LTV1 homolog
- Basic helix-loop-helix ARNT-like protein 1
- Circadian locomoter output cycles protein kaput
- Neuronal PAS domain-containing protein 2
Sequence:
MELRVGNRYRLGRKIGSGSFGDIYLGTDIAAGEEVAIKLECVKTKHPQLHIESKIYKMMQGGVGIPTIRWCGAEGDYNVMVMELLGPSLEDLFNFCSRKFSLKTVLLLADQMISRIEYIHSKNFIHRDVKPDNFLMGLGKKGNLVYIIDFGLAKKYRDARTHQHIPYRENKNLTGTARYASINTHLGIEQSRRDDLESLGYVLMYFNLGSLPWQGLKAATKRQKYERISEKKMSTPIEVLCKGYPSEFATYLNFCRSLRFDDKPDYSYLRQLFRNLFHRQGFSYDYVFDWNMLKFGASRAADDAERERRDREERLRHSRNPATRGLPSTASGRLRGTQEVAPPTPLTPTSHTANTSPRPVSGMERERKVSMRLHRGAPVNISSSDLTGRQDTSRMSTSQIPGRVASSGLQSVVHR
Protein: Major capsid protein (Capsid protein pb8) (Major head protein) [Cleaved into: Scaffolding domain delta] (Q6QGD8)
Organism: Escherichia phage T5 (Enterobacteria phage T5)
Function: Major capsid protein that self-associates to form 120 hexamers and 11 pentamers, building the T=13 icosahedral capsid which about 860 Angstroms in diameter. Responsible for its self-assembly into a procapsid. The phage does not need to encode a separate scaffolfing protein because its capsid protein contains the delta domain that carries that function. The capsid gains its final stability through the reorganization of the subunits that takes place upon expansion. DNA encapsidation through the portal triggers capsid expansion and the binding of the decoration protein to the capsid exterior. Might play a role in counteracting the host Pycsar defense system that is mediated by pyrimidine cyclases and leads to abortive infection.
Subcellular location: [Major capsid protein]: Virion {ECO:0000269|PubMed:24198424, ECO:0000269|PubMed:4571380}. Note=Forms the icosahedral capsid shell which contains 775 major capsid proteins. {ECO:0000269|PubMed:4571380}.
Interaction partners:
Sequence:
MTIDINKLKEELGLGDLAKSLEGLTAAQKAQEAERMRKEQEEKELARMNDLVSKAVGEDRKRLEEALELVKSLDEKSKKSNELFAQTVEKQQETIVGLQDEIKSLLTAREGRSFVGDSVAKALYGTQENFEDEVEKLVLLSYVMEKGVFETEHGQRHLKAVNQSSSVEVSSESYETIFSQRIIRDLQKELVVGALFEELPMSSKILTMLVEPDAGKATWVAASTYGTDTTTGEEVKGALKEIHFSTYKLAAKSFITDETEEDAIFSLLPLLRKRLIEAHAVSIEEAFMTGDGSGKPKGLLTLASEDSAKVVTEAKADGSVLVTAKTISKLRRKLGRHGLKLSKLVLIVSMDAYYDLLEDEEWQDVAQVGNDSVKLQGQVGRIYGLPVVVSEYFPAKANSAEFAVIVYKDNFVMPRQRAVTVERERQAGKQRDAYYVTQRVNLQRYFANGVVSGTYAAS
Protein: Ethylene-responsive transcription factor RAP2-12 (Protein RELATED TO APETALA2 12) (Q9SSA8)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Transcription factor involved in the activation of hypoxic gene expression and in ethylene response. Partially redundant with RAP2-2. Acts as a downstream regulator in the ethylene signaling pathway.
Subcellular location: Cell membrane {ECO:0000269|PubMed:22020282}. Nucleus {ECO:0000255|PROSITE-ProRule:PRU00366, ECO:0000269|PubMed:22020282}. Note=Localizes to the plasma membrane under aerobic conditions, but accumulates in the nucleus upon hypoxia.
Interaction partners:
- Acyl-CoA-binding domain-containing protein 1
- Acyl-CoA-binding domain-containing protein 2
- Sequence-specific DNA binding transcription factor
- E3 ubiquitin-protein ligase PRT6
- Acyl-CoA-binding domain-containing protein 6
- Plant cysteine oxidase 1
- Alcohol dehydrogenase class-P
- Pyruvate decarboxylase 1
- Arginyl-tRNA--protein transferase 2
- Cysteine proteinase inhibitor 2
Sequence:
MCGGAIISDFIPPPRSRRVTSEFIWPDLKKNLKGSKKSSKNRSNFFDFDAEFEADFQGFKDDSSIDCDDDFDVGDVFADVKPFVFTSTPKPAVSAAAEGSVFGKKVTGLDGDAEKSANRKRKNQYRGIRQRPWGKWAAEIRDPREGARIWLGTFKTAEEAARAYDAAARRIRGSKAKVNFPEENMKANSQKRSVKANLQKPVAKPNPNPSPALVQNSNISFENMCFMEEKHQVSNNNNNQFGMTNSVDAGCNGYQYFSSDQGSNSFDCSEFGWSDQAPITPDISSAVINNNNSALFFEEANPAKKLKSMDFETPYNNTEWDASLDFLNEDAVTTQDNGANPMDLWSIDEIHSMIGGVF
Protein: Peroxygenase (EC 1.11.2.3) (Caleosin) (A8B479)
Organism: Lilium longiflorum (Trumpet lily)
Function: Calcium-binding peroxygenase involved in the degradation of storage lipid in oil bodies.
Subcellular location: Lipid droplet {ECO:0000269|PubMed:18632804}. Microsome membrane {ECO:0000250|UniProtKB:Q9SQ57}.
Interaction partners:
Sequence:
MGSTSDPSPSIITVAAEAPVTAERKQNLHLQEQLAKPYVARALAAVDPAHPNGTEGHEHHNMSVLQQRAAFFDRNNDGIVYPWETYQGFRAVGFGVLTSILGGFLINLGLSYRSQPSWIPSPVLSIHIKNIHRCKHGSDTESYDTEGRFEPSKFDAIFSKYALTQPDALTSEEISTMLQVNRNLLDFIGWVASIAEWRLLYQIGKDEDGLLHKETIRGAFDGSLFERLEKDRASRTKIV
Protein: N-acyl-phosphatidylethanolamine-hydrolyzing phospholipase D (N-acyl phosphatidylethanolamine phospholipase D) (NAPE-PLD) (NAPE-hydrolyzing phospholipase D) (EC 3.1.4.54) (Q769K2)
Organism: Rattus norvegicus (Rat)
Function: D-type phospholipase that hydrolyzes N-acyl-phosphatidylethanolamines (NAPEs) to produce bioactive N-acylethanolamines/fatty acid ethanolamides (NAEs/FAEs) and phosphatidic acid. Cleaves the terminal phosphodiester bond of diacyl- and alkenylacyl-NAPEs, primarily playing a role in the generation of long-chain saturated and monounsaturated NAEs in the brain (By similarity). May control NAPE homeostasis in dopaminergic neuron membranes and regulate neuron survival, partly through RAC1 activation (By similarity). As a regulator of lipid metabolism in the adipose tissue, mediates the crosstalk between adipocytes, gut microbiota and immune cells to control body temperature and weight. In particular, regulates energy homeostasis by promoting cold-induced brown or beige adipocyte differentiation program to generate heat from fatty acids and glucose. Has limited D-type phospholipase activity toward N-acyl lyso-NAPEs (By similarity).
Subcellular location: Golgi apparatus membrane {ECO:0000250|UniProtKB:Q6IQ20}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q6IQ20}. Early endosome membrane {ECO:0000250|UniProtKB:Q6IQ20}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q6IQ20}. Nucleus envelope {ECO:0000250|UniProtKB:Q6IQ20}. Nucleus, nucleoplasm {ECO:0000250|UniProtKB:Q6IQ20}. Note=Localized in the proximity of the cellular membranes likely through interaction with membrane phospholipids. {ECO:0000250|UniProtKB:Q6IQ20}.
Interaction partners:
- Fatty-acid amide hydrolase 1
- Monoglyceride lipase
- Glycerophosphodiester phosphodiesterase 1
- 
- N-acylethanolamine-hydrolyzing acid amidase
- G protein-coupled receptor 55
- Monoacylglycerol lipase ABHD6
- Lysophosphatidylserine lipase ABHD12
- Diacylglycerol lipase-beta
- Diacylglycerol lipase-alpha
Sequence:
MDENENSQSPAPSHQYPKETLRKRQNSVQNSGGSESSRLSRKSFKLDYRLEEDVTKSKKGKDGRFVNPWPTWKNVSIPNVLRWLIMEKDHSSVPGSKEELDKELPVLKPYFISDPEEAGVREAGLRVTWLGHATLMVEMDELILLTDPMFSSRASPSQYMGPKRFRRPPCTISELPPIDAVLISHNHYDHLDYGSVLALNERFGSELRWFVPLGLLDWMQKCGCENVIELDWWEENCVPGHDKVTFVFTPSQHWCKRTLLDDNKVLWGSWSVLGPWNRFFFAGDTGYCPAFEEIGKRFGPFDLAAIPIGAYEPRWFMKYQHADPEDAVRIHIDVQAKRSVAIHWGTFALANEHYLEPPVKLNEALERYGLKSEDFFILKHGESRYLNTDDKAFEET
Protein: Small ribosomal subunit protein mS43 (37S ribosomal protein MRP1, mitochondrial) (P10662)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Component of the mitochondrial ribosome (mitoribosome), a dedicated translation machinery responsible for the synthesis of mitochondrial genome-encoded proteins, including at least some of the essential transmembrane subunits of the mitochondrial respiratory chain. The mitoribosomes are attached to the mitochondrial inner membrane and translation products are cotranslationally integrated into the membrane.
Subcellular location: Mitochondrion {ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:14576278, ECO:0000269|PubMed:2185247}. Note=Mitoribosomes are tethered to the mitochondrial inner membrane and spatially aligned with the membrane insertion machinery through two distinct membrane contact sites, formed by the 21S rRNA expansion segment 96-ES1 and the inner membrane protein MBA1. {ECO:0000269|PubMed:25609543}.
Interaction partners:
- Small ribosomal subunit protein mS23
- Small ribosomal subunit protein uS5m
- Small ribosomal subunit protein bS1m
- Small ribosomal subunit protein mS29
- Small ribosomal subunit protein uS2m
- Small ribosomal subunit protein uS17m
- Small ribosomal subunit protein mS47
- Small ribosomal subunit protein mS42
- Small ribosomal subunit protein mS26
- Small ribosomal subunit protein uS10m
Sequence:
MLRFTGARAIRKYSTRYALEHLKEGAPLKGLFSIEGLQKAWFDRVKYLDAKLNDCTNEAQQKPLETLIHENSKSASKKHIVNYASSLYNLKFSMSSLQGCIRTPPEECPRLGPEALLQTPDFNRTISNEPLTTGNERLQAALISSFGSLMEFRTLLINSNLAISGDGFTWLVARRQLDKRAMRNDMPNRDIEYDKLFILNTYNAGTPFNFSTSGVMNELNNQYTNMEKQRAKEAGNLEDSEMTAKQAKTKFIYETQQKGFSGKEVSYIPLLAIDASPKTWLTDYGVFGKREYLERVWDSIEWKIVESRLPQRTKIQAFNTL
Protein: Serine/threonine protein phosphatase 2A 57 kDa regulatory subunit B' epsilon isoform (AtB' epsilon) (PP2A, B' subunit, epsilon isoform) (Q9SV41)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: The B regulatory subunit may modulate substrate selectivity and catalytic activity, and may also direct the localization of the catalytic enzyme to a particular subcellular compartment.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:26517938}.
Interaction partners:
- Serine/threonine-protein phosphatase 2A 65 kDa regulatory subunit A alpha isoform
- Serine/threonine protein phosphatase 2A 55 kDa regulatory subunit B beta isoform
- Serine/threonine protein phosphatase 2A 55 kDa regulatory subunit B alpha isoform
- Serine/threonine-protein phosphatase 2A 65 kDa regulatory subunit A beta isoform
- Probable serine/threonine protein phosphatase 2A regulatory subunit B''epsilon
- Probable serine/threonine protein phosphatase 2A regulatory subunit B''delta
- Serine/threonine protein phosphatase 2A regulatory subunit B''beta
- Serine/threonine protein phosphatase 2A regulatory subunit B''alpha
- Probable serine/threonine protein phosphatase 2A regulatory subunit B''gamma
- Serine/threonine-protein phosphatase 2A 65 kDa regulatory subunit A gamma isoform
Sequence:
MFNKIIKLGQKKFNKSDQHHQDNNNNNNNTSTNTVVRGSRTTTPAPSSVSNGESQTTAQSPSQTPNHPMFTTTPILEVLPLLKDVSSSDRPLLFMKKAHMCSCHCDFSDTLIMPREKEIKRQTLLELVDFLHSSSGKVNETMQSELIRMVSANIFRCLPPAYHENTGAPPEGNDPEEEEPYLEPWWPHLQLVYELLLRYVVSSEIEPKTAKKFINHTFVSRLLDLFDSEDPREREYLKTVLHRIYGKFIFHRPFIRCSIYNIFYKFLYETERCIGIGELLEILGSVINGFTVPMREEHRLYLVKAILPLHKSKGISIYHQQLAYCVTQFVEKDYKLADTVIRGLLKFWPLTNCQKEVLFLGELEEVLDATEPSEFQQCVVPLFTQIGKCLNSAHFQVAERALFLWNNEHIVGLIAQNKDVIFPIIFEALERNMKGHWNQAVHGLSENVRRMFLEMDTELFEECEKQYLENEAKACELLEQRELTWKRLEEAASLAAN