wanglab/gogpt-training-data huggingface dataset:
Protein: Zinc finger protein 22 (Zinc finger protein KOX15) (Zinc finger protein Krox-26) (P17026)
Organism: Homo sapiens (Human)
Function: Binds DNA through the consensus sequence 5'-CAATG-3'. May be involved in transcriptional regulation and may play a role in tooth formation (By similarity).
Subcellular location: Nucleus {ECO:0000250}.
Interaction partners:
Sequence:
MRLAKPKAGISRSSSQGKAYENKRKTGRQRQKWGMTIRFDSSFSRLRRSLDDKPYKCTECEKSFSQSSTLFQHQKIHTGKKSHKCADCGKSFFQSSNLIQHRRIHTGEKPYKCDECGESFKQSSNLIQHQRIHTGEKPYQCDECGRCFSQSSHLIQHQRTHTGEKPYQCSECGKCFSQSSHLRQHMKVHKEEKPRKTRGKNIRVKTHLPSWKAGTGRKSVAGLR
Protein: 16.9 kDa class I heat shock protein 1 (HSP 16.9) (Heat shock protein 16.9A) (Heat shock protein 17) (Low molecular weight heat shock protein) (P12810)
Organism: Triticum aestivum (Wheat)
Subcellular location: Cytoplasm {ECO:0000305}.
Interaction partners:
Sequence:
MSIVRRSNVFDPFADLWADPFDTFRSIVPAISGGSSETAAFANARVDWKETPEAHVFKVDLPGVKKEEVKVEVEDGNVLVVSGERSREKEDKNDKWHRVERSSGKFVRRFRLPEDAKVEEVKAGLENGVLTVTVPKAEVKKPEVKAIEISG
Protein: Seed linoleate 13S-lipoxygenase-1 (EC 1.13.11.12) (Lipoxygenase-1) (L-1) (P08170)
Organism: Glycine max (Soybean) (Glycine hispida)
Function: Plant lipoxygenase may be involved in a number of diverse aspects of plant physiology including growth and development, pest resistance, and senescence or responses to wounding. With linoleate as substrate, L-1 shows a preference for carbon 13 as the site for hydroperoxidation (in contrast to L-2 and L-3, which utilize either carbon 9 or 13). At pH above 8.5, only (9Z,11E,13S)-13-hydroperoxyoctadeca-9,11-dienoate is produced, but as the pH decreases, the proportion of (9S)-hydroperoxide increases linearly until at pH 6.0 it represents about 25 % of the products.
Subcellular location: Cytoplasm.
Interaction partners:
- Uncharacterized protein
- Caleosin
- Uncharacterized protein
- Lipoxygenase
Sequence:
MFSAGHKIKGTVVLMPKNELEVNPDGSAVDNLNAFLGRSVSLQLISATKADAHGKGKVGKDTFLEGINTSLPTLGAGESAFNIHFEWDGSMGIPGAFYIKNYMQVEFFLKSLTLEAISNQGTIRFVCNSWVYNTKLYKSVRIFFANHTYVPSETPAPLVSYREEELKSLRGNGTGERKEYDRIYDYDVYNDLGNPDKSEKLARPVLGGSSTFPYPRRGRTGRGPTVTDPNTEKQGEVFYVPRDENLGHLKSKDALEIGTKSLSQIVQPAFESAFDLKSTPIEFHSFQDVHDLYEGGIKLPRDVISTIIPLPVIKELYRTDGQHILKFPQPHVVQVSQSAWMTDEEFAREMIAGVNPCVIRGLEEFPPKSNLDPAIYGDQSSKITADSLDLDGYTMDEALGSRRLFMLDYHDIFMPYVRQINQLNSAKTYATRTILFLREDGTLKPVAIELSLPHSAGDLSAAVSQVVLPAKEGVESTIWLLAKAYVIVNDSCYHQLMSHWLNTHAAMEPFVIATHRHLSVLHPIYKLLTPHYRNNMNINALARQSLINANGIIETTFLPSKYSVEMSSAVYKNWVFTDQALPADLIKRGVAIKDPSTPHGVRLLIEDYPYAADGLEIWAAIKTWVQEYVPLYYARDDDVKNDSELQHWWKEAVEKGHGDLKDKPWWPKLQTLEDLVEVCLIIIWIASALHAAVNFGQYPYGGLIMNRPTASRRLLPEKGTPEYEEMINNHEKAYLRTITSKLPTLISLSVIEILSTHASDEVYLGQRDNPHWTSDSKALQAFQKFGNKLKEIEEKLVRRNNDPSLQGNRLGPVQLPYTLLYPSSEEGLTFRGIPNSISI
Protein: D-aspartate oxidase (EC 1.4.3.1) (C9K4X7)
Organism: Homo sapiens (Human)
Subcellular location: Peroxisome matrix {ECO:0000256|ARBA:ARBA00004253}.
Interaction partners:
Sequence:
MDTARIAVVGAGVVGLSTAVCISKLVPRCSVTIISDKFTPDTTSDVAAGMLIPHTYPDTPIHTQKQWFRETFNHLFAIANSAEAGDAGVHLVSGWQIFQSTPTEEVPFWADVVLGFRKMTEAELKKFPQYVFGQAFTTLKCECPAYLPWLEKRIKGSGGWTLTRRIEDLWELHPSFDIVVNCSGLGSRQLAGDSKIFPVRGQVLQVQAPWVEHFIRDGSGLTYIYPGTSHVTLGGTRQKGDWNLSPDAENSREILSRCCALEPSLHGACNIREKVGLRPYRPGVRLQTELLARDGQRLPVVHHYGHGSGGISVHWGTALEAARLVSECVHALRTPIPKSNL
Protein: Sulfiredoxin (EC 1.8.98.2) (Sulphiredoxin) (P36077)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Contributes to oxidative stress resistance by reducing cysteine-sulfinic acid formed under exposure to oxidants in the peroxiredoxin TSA1. May catalyze the reduction in a multi-step process by acting both as a specific phosphotransferase and as thioltransferase.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:14562095}. Nucleus {ECO:0000269|PubMed:14562095}.
Interaction partners:
- Peroxiredoxin TSA1
- Peroxiredoxin TSA2
- Peroxiredoxin PRX1, mitochondrial
- Glutathione peroxidase-like peroxiredoxin 1
- Thioredoxin-2
- Glutathione peroxidase-like peroxiredoxin 2
- Peroxiredoxin AHP1
- Thioredoxin-1
- Glutathione peroxidase-like peroxiredoxin HYR1
- Catalase T
Sequence:
MSLQSNSVKPTEIPLSEIRRPLAPVLDPQKIDAMVATMKGIPTASKTCSLEQAEAAASAGELPPVDVLGVRVKGQTLYYAFGGCHRLQAYDRRARETQNAAFPVRCRVLPATPRQIRMYLGSSLDIE
Protein: Neuroepithelial cell-transforming gene 1 protein (Rho guanine nucleotide exchange factor 8) (Q9Z206)
Organism: Mus musculus (Mouse)
Function: Acts as guanine nucleotide exchange factor (GEF) for RhoA GTPase. May be involved in activation of the SAPK/JNK pathway. Stimulates genotoxic stress-induced RHOB activity in breast cancer cells leading to their cell death.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:11839749}. Nucleus {ECO:0000269|PubMed:11839749}.
Interaction partners:
- Transforming protein RhoA
- Rho-related GTP-binding protein RhoC
- Rho-related GTP-binding protein RhoB
Sequence:
MEPEPAAQKQPRPRRRSRRVSMLSEEPAAGLPADTPGPAANERCSLRRGSSFTFLTPGPHWDFTLKRKRREKDDDAVSLSSLDLKEPSNKRVRPLARVTSLANLISPVRNGAVRRFGQTIQSFTLRGDHRSPASAQKSFSRSTVPTPTKRRSSALWSEMLDINMKESLTTREIKRQEAIYELSRGEQDLIEDLKLARKAYHDPMLKLSIMSEEELTHIFGDLDAYIPLHEDLLARIGEATKPDGTVEQIGHILVNWLPGLNAYRGYCSNQLAAKALLDQKKQDPRVQDFLQRCLESPFSRKLDLWSFLDIPRSRLVKYPLLLKEILRHTPKDHRDVQLLEEAILIIQGVLSDINLKKGESECQYYINKLEYLDEKQKDPRIEASKVLLCHGELKNKSGHKLYIFLFQDILVLTRPVTRNERHLYQVYRQPIPVQELVLEDLQDGDVRMGGSFRGAFGNSDKAKNIFRVRFQDPSPGHSHTLQANDVFHKQQWFNCIRAAIAPFQRAASPLELQGLPDLHEECEENNPSAGNLRAQRRSCVVPGVMQIDEESALDCGSSVQTVEDTRNMKAQRPQPGLRRARDKAQSGGKKKETLV
Protein: RasGRP3 (Q2PHE9)
Organism: Mus musculus (Mouse)
Subcellular location: Cytoplasm, cytosol {ECO:0000256|ARBA:ARBA00004514}.
Interaction partners:
Sequence:
MGSNGLGKAATLDELLSTCIEMFDDNGDLNDSYLPRIVLLMHRWYLSSTELAGKLLCMYRNASGESCDEFRLKICYFMRYWILKFPAEFNLDLGLIRMTEEFREVASQLGHEKHISLMDISSVPSYDWMRRVTQRKKVSKRGKACLLFDHLEPIELAEHLTFLEHKSFRRISFTDYQSYVIHGCLENNPTLERSIALFNGISKWVQLMVLSKPSAQQRAEVITKFINVAQKLLQLKNFNTLMAVVGGLSHSSISRLXDTHSHLSSEVTKKLDEMTELVSSNGNYCNYRKAFADCDGFKIPILGVHLKDLIAVHVIFPDWMEENKVNVVKMHQLSVTLSELVSLQNASHHLEPNMDLINLLTLSLDLYHTEDDIYKLSLVLEPRNSKSQPTSPTTPNKPVVPLEWASEVVPKPDPTIINKHIRKLVESVFRNYDHDHDGYISQEDFESIAANFPFLDSFCVLDKDQDGLISKDEMMAYFLRAKSQLHCKMGPGFIHNFQEMNYLKPTFCEHCAGFLWGIIKQGYKCKDCGANCHKQCKDLLVLACRRLARAPSLSSNPGSLPGSPALPPVQDEVFEFPGVTAGHRDLDSRAITLVTGSSRKISVRLQRATTSQATQTEPVWSEAVWGDSGSHTFPKMKSKFHDKAAKDKGFAKWENEKPTVQAGVDVVDRGTAFEPDQDDGQDEAKQGGEDG
Protein: At1g18720/F6A14_17 (ER membrane protein, putative (DUF962)) (F6A14.17 protein) (Q9M9U3)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
Sequence:
MSRIMGLFDLEKHFAFYGAYHSNPINILIHIIFVWPIFFSVLLLLHSSTPIFDPSQLGFSQSLTLDGVLRFNVGFIFALIYALFYIGLDKKSGFVAALMCFSCWVGSSFLAVRLGSSLALKVGLASQLLCWTGQFVGHGVFEKRAPALLDNLLQAFLMAPFFVLLEVLQSVFGYEPYPGFQARVNAKVESDIKEYRAKKQKKNKIT
Protein: Glycerophosphoinositol permease 1 (Glycerophosphodiester transporter GIT1) (Q59Q30)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Function: Glycerophosphodiester transporter that mediates uptake of glycerophosphoinositol (GroPIns) as a source of inositol and phosphate. Does not possess detectable glycerophosphocholine (GroPCho) transport activity. Although no glycerophosphoinositol transport activity occurs in the absence of GIT1, C.albicans is still able to use glycerophosphoinositol as a phosphate source at pH 7.5, albeit slowly. Thus, a second, GIT1-independent, mechanism must exist for utilizing glycerophosphoinositol as a phosphate source at physiological pH. The expanded ability to utilize GroPIns and GroPCho results from the organism's pathogenic nature and its need to occupy a variety of environments within its host organism. This possibility is buttressed by the fact that GroPIns and GroPCho are present and abundant in human fluids.
Subcellular location: Cell membrane {ECO:0000305|PubMed:21984707}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Pho100p
- Glycerophosphocholine phosphodiesterase GDE1
Sequence:
MSDLVKSSEVIETTEVPPHNNNNNKRHFKYDSEQRKQRLAGGVKLKDALMILCAGFALISDGYQNNVMSMMNKVFALEYPKEYTASLSTQVSNASLVGTIFGQVIIGLTADYIGRKWSIVTATCFLIFGTMMCAASHGKTVNGMFWMLTIFRGVTGFGIGAEYPSSSVTASEAANESVKRRGGAFILATNLPLSFGGPFALCIFLIVRRICGNHLDAIWRTMFAIGCFWPLSVFYFRLKMVTSELYTKSAIKQRAPYWLALKYYWPRLIGTCVAWFLYDFVTFPNGIFSAGIISNVIPKSEKNNLEKIAEWNLLLGAIALPGVFVGAYVVDILGRKYTMMIGFCGYIVFGLIVGCGYHQIKPITGLFIVFYGLMMSCGNFGPGNNMGLTSSESFATPIRGTAYGISAAIGKVGAVVGTKTFSPIQKNLGDKWTFIIAAICGLAGVLVTFIFIPHLKDEDLLEEDVKFKNYLIDNGWKGKFGIQEYDEEEDLEGSSEDSSDGEIVKNNTKNDVEKVDALK
Protein: Flagellar calcium-binding protein TB-1.7G (17 kDa calcimedin) (17 kDa calflagin) (Q26677)
Organism: Trypanosoma brucei brucei
Function: May contribute to the rapid motility of the trypanosomes, playing a role either in flagellar structure or in calcium metabolism. Could alternate between a GDP-bound inactive form to a calcium/GTP-bound active form.
Subcellular location: Cell projection, cilium, flagellum.
Interaction partners:
Sequence:
GSKNASNPKDGAASKGGKDGKTTADRKVAWERIRCAIPRDKDAESKSRRIELFKQFDTNGTGKLGFREVLDGCYGILKLDEFTTHLPDIVQRAFDKAKDLGNKVKGVGEEDLVEFLEFRLMLCYIYDIFELTVMFDTMDKDGSLLLELQEFKEALPKLKEWGVDITDATTVFNEIDTNGSGVVTFDEFSCWAVTKKLQVCGDPDDEENGANEGDGANAGDGVPAAEGSA
Protein: Uncharacterized protein (Q38FY7)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- Calmodulin, putative
- BRCT domain-containing protein
- Dynein assembly factor 3, axonemal
- Transcription factor CBF/NF-Y/archaeal histone domain-containing protein
- BTB domain-containing protein
Sequence:
MEASGHCDVDNGPTAQQPVKAIQIVQSTEEADALVKRVKQLERENKSLTDVLTKVCDENAKLSGTVAEMQVRCETYSTNIFSETPVLKALYERDKFKLFGSSKTATPENLQKLLDNLCKEFTDFRAQHTSSNGEVQKLLMEVQQGHANVQKLSAVVRDQQEVISRSPLAVTVRIAQDEDESKNVMFRDLRSEVDRHRIREDELRDQLQRLQAELQAKTAELTQQQWELQASREECDSASVAEQKQQELHDKITRYEQELEDLRENLATESSMHKDVEAENRALTEKLRELEDRIRQNESCSAEAKLTAPSYDVDTLLTASMNEPKSCKNCEDAQHQHEAAMEKISILESRLAQVTEENGKLTDLSSAMKEEATYFATTKEHDEERLRGLEAQCETLTTDINNLRVERDQLSRDYEAAQLELDRARMQAEKIPQFETSVAELQQEVSTLRERLSCAEESEKALLKAREEITQLEEAQRQNTGSDTEARCTALEFSLQAVKVQLGETQADLQRVGSERASLQDTVDNQRQTLKSREDEVAALVKESAELRVEVCRLMEENNKLCGQNTTLEGQLNELQLRMEELEANSLVFNDLRSEVDRHRIREDELRDQLQRLQAELQAKTAELTQQQWELQASREECDSASVAEQKQQELHDKITRYEQELEDLRENLATESSMHKDVEAENRALTEKLRELEDRIRQNESCSAEAKLTAPSYDVDTLLTASMNEPKSCKNCEDAQHQHEAAMEKISILESRLAQVTEENGKLTDLSSAMKEEATYFATTKEHDEERLRGLEAQCETLTTDINNLRVERDQLSRDYEAAQLELDRARMQAEKIPQFETSVAELQQEVSTLRERLSCAEESEKALLKAREEITQLEEAQRQNTGSDTEARCTALEFSLQAVKVQLGETQADLQRVGSERASLQDTVDNQRQTLKSREDEVAALVKESAELRVEVCRLMEENNKLCGQNTTLEGQLNELQLRMEEVMRQCGGANDTKGVGACVEQRTSVGGVECERAVASEGTVAAQLESNSFVPDDIRSVMVENTRLVSENQQMVSDIDRLTSELLVYRQTIDELEAENEEQLRQNEQIRSAHSAELGLIAERLASETAMCTNTNEKMAKLTDEYRALELERNKYQCLVEEKSNQEEKLLSTIVATSSELEAVKEELRRVMVTVNDQLEAVRHEKELEMEVRIAEERQRYENESGRLCAQLHQVEEERLHIESELDKLRQSTEAAGGVAARASSAAAEDSDVTALRVQVDQLRVTLKEAHRQLEEQERSSAEVNERFEEERKKLDDDAAAMRRRIEQLEEKLQTARAEQIVSGAVTLPVRRKKKKQPNTDLLSLVRFDDGPAVDVLAHGADSPSYRSVGNEREAESLAAQLKESNDKLSVLQEENGKLKESIADLTEKLRIMQDYTTNDLERQVEELQEKIQQLEQQLESAAEPVASILPVDEKTVNGDGADKKLQLLTTENKRLRSKLRQAREALRKKEGGDDASVEQLKAELQMLAGEVVPMKNKLAEYMAMADRIGIQYPFSEEMEKAALLNLNAVQTKMSHKKSRNSATKIEIGADEKDRGSSGHTKKRTSSKKIKDRHSHTVAEVSEDLR
Protein: Venom prothrombin activator pseutarin-C catalytic subunit (PCCS) (vPA) (EC 3.4.21.6) (Venom coagulation factor Xa-like protease) [Cleaved into: Pseutarin-C catalytic subunit light chain; Pseutarin-C catalytic subunit heavy chain] (Q56VR3)
Organism: Pseudonaja textilis (Eastern brown snake)
Function: Snake prothrombin activator that attacks the hemostatic system of prey. This non-catalytic subunit is functionally similar to blood coagulation factor V. It serves as a critical cofactor for the prothrombinase activity of the catalytic subunit, which is similar to the blood coagulation factor X. The complex converts prothrombin to thrombin by sequential cleavage at two positions, Arg-320 followed by Arg-271. Cleavage at Arg-320 produces an active intermediate known as meizothrombin. Meizothrombin is the 'second' substrate for prothrombinase, and it docks in an altered manner to present the second cleavage site (271). Cleavage at Arg-271 releases active thrombin from its pro-fragment. This order of events is reversed if the protease component of prothrombinase is used on its own, suggesting that the 271 site is inherently more accessible to proteolysis. The complex converts prothrombin to thrombin in presence but also in the absence of membrane.
Subcellular location: Secreted {ECO:0000269|PubMed:12362232, ECO:0000269|PubMed:3075905}.
Interaction partners:
Sequence:
MAPQLLLCLILTFLWSLPEAESNVFLKSKVANRFLQRTKRANSLVEEFKSGNIERECIEERCSKEEAREVFEDDEKTETFWNVYVDGDQCSSNPCHYRGICKDGIGSYTCTCLSGYEGKNCERVLYKSCRVDNGNCWHFCKSVQNDIQCSCAEGYLLGEDGHSCVAGGNFSCGRNIKTRNKREASLPDFVQSHNATLLKKSDNPSPDIRIVNGMDCKLGECPWQAALVDDKKGVFCGGTILSPIYVLTAAHCINETETISVVVGEIDRSRAETGPLLSVDKVYVHKKFVPPKKSQEFYEKFDLVSYDYDIAIIQMKTPIQFSENVVPACLPTADFANQVLMKQDFGIVSGFGGIFERGPNSKTLKVLKVPYVDRHTCMLSSNFPITPTMFCAGYDTLPQDACQGDSGGPHITAYRDTHFITGIVSWGEGCARKGRYGIYTKLSKFIPWIKRIMRQKLPSTESSTGRL
Protein: Bifunctional aldehyde-alcohol dehydrogenase AdhE (Alcohol dehydrogenase E) [Includes: Acetaldehyde dehydrogenase [acetylating] (ACDH) (EC 1.2.1.10); Alcohol dehydrogenase (ADH) (EC 1.1.1.1)] (P0A9Q7)
Organism: Escherichia coli (strain K12)
Function: Under fermentative conditions, catalyzes the sequential NADH-dependent reduction of acetyl-CoA to acetaldehyde and then to ethanol. Under aerobic conditions, despite the reversibility of the two NADH-coupled reactions, wild-type E.coli cannot grow on ethanol as the sole carbon and energy source due to the down-regulation of adhE transcription and the inactivation of the enzyme by metal-catalyzed oxidation (MCO). Nevertheless, in the presence of oxygen, AdhE may act as a hydrogen peroxide scavenger and have a protective role against oxidative stress.
Interaction partners:
- Formate acetyltransferase 1
- PFL-like enzyme TdcE
- Phosphate acetyltransferase
- Aldehyde dehydrogenase B
- Acetaldehyde dehydrogenase
- Alcohol dehydrogenase, propanol-preferring
- Aldehyde reductase Ahr
- S-
- Phosphate acetyltransferase EutD
- Acetyl-CoA acetyltransferase
Sequence:
MAVTNVAELNALVERVKKAQREYASFTQEQVDKIFRAAALAAADARIPLAKMAVAESGMGIVEDKVIKNHFASEYIYNAYKDEKTCGVLSEDDTFGTITIAEPIGIICGIVPTTNPTSTAIFKSLISLKTRNAIIFSPHPRAKDATNKAADIVLQAAIAAGAPKDLIGWIDQPSVELSNALMHHPDINLILATGGPGMVKAAYSSGKPAIGVGAGNTPVVIDETADIKRAVASVLMSKTFDNGVICASEQSVVVVDSVYDAVRERFATHGGYLLQGKELKAVQDVILKNGALNAAIVGQPAYKIAELAGFSVPENTKILIGEVTVVDESEPFAHEKLSPTLAMYRAKDFEDAVEKAEKLVAMGGIGHTSCLYTDQDNQPARVSYFGQKMKTARILINTPASQGGIGDLYNFKLAPSLTLGCGSWGGNSISENVGPKHLINKKTVAKRAENMLWHKLPKSIYFRRGSLPIALDEVITDGHKRALIVTDRFLFNNGYADQITSVLKAAGVETEVFFEVEADPTLSIVRKGAELANSFKPDVIIALGGGSPMDAAKIMWVMYEHPETHFEELALRFMDIRKRIYKFPKMGVKAKMIAVTTTSGTGSEVTPFAVVTDDATGQKYPLADYALTPDMAIVDANLVMDMPKSLCAFGGLDAVTHAMEAYVSVLASEFSDGQALQALKLLKEYLPASYHEGSKNPVARERVHSAATIAGIAFANAFLGVCHSMAHKLGSQFHIPHGLANALLICNVIRYNANDNPTKQTAFSQYDRPQARRRYAEIADHLGLSAPGDRTAAKIEKLLAWLETLKAELGIPKSIREAGVQEADFLANVDKLSEDAFDDQCTGANPRYPLISELKQILLDTYYGRDYVEGETAAKKEAAPAKAEKKAKKSA
Protein: Stress-associated endoplasmic reticulum protein 2 (Ribosome-associated membrane protein RAMP4-2) (Q8N6R1)
Organism: Homo sapiens (Human)
Function: May interact with target proteins during translocation into the lumen of the endoplasmic reticulum. May protect unfolded target proteins against degradation and facilitate correct glycosylation (Potential).
Subcellular location: Membrane {ECO:0000250|UniProtKB:Q9R2C1}; Single-pass membrane protein {ECO:0000250|UniProtKB:Q9R2C1}. Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q9R2C1}; Single-pass membrane protein {ECO:0000250|UniProtKB:Q9R2C1}.
Interaction partners:
Sequence:
MVAKQRIRMANEKHSKNITQRGNVAKTLRPQEEKYPVGPWLLALFVFVVCGSAIFQIIQSIRMGM
Protein: Large ribosomal subunit protein bL36m (39S ribosomal protein L36, mitochondrial) (L36mt) (MRP-L36) (BRCA1-interacting protein 1) (Q9P0J6)
Organism: Homo sapiens (Human)
Subcellular location: Mitochondrion {ECO:0000269|PubMed:25278503, ECO:0000269|PubMed:25838379}.
Interaction partners:
- Large ribosomal subunit protein bL20m
- Small ribosomal subunit protein uS5m
- Large ribosomal subunit protein uL22m
- Small ribosomal subunit protein uS3
- Small ribosomal subunit protein uS17
- Large ribosomal subunit protein bL27m
- Large ribosomal subunit protein bL19m
- Small ribosomal subunit protein uS10m
- Small ribosomal subunit protein uS14m
- Large ribosomal subunit protein bL33m
Sequence:
MANLFIRKMVNPLLYLSRHTVKPRALSTFLFGSIRGAAPVAVEPGAAVRSLLSPGLLPHLLPALGFKNKTVLKKRCKDCYLVKRRGRWYVYCKTHPRHKQRQM
Protein: Prostaglandin E2 receptor EP1 subtype (PGE receptor EP1 subtype) (PGE2 receptor EP1 subtype) (Prostanoid EP1 receptor) (P70597)
Organism: Rattus norvegicus (Rat)
Function: Receptor for prostaglandin E2 (PGE2). The activity of this receptor is mediated by G(q) proteins which activate a phosphatidylinositol-calcium second messenger system. May play a role as an important modulator of renal function (By similarity). Implicated the smooth muscle contractile response to PGE2 in various tissues. Isoform 1 and isoform 2 have identical ligand binding properties, but isoform 2 lacks coupling to calcium mobilization and may therefore attenuate the action of PGE2 on tissues.
Subcellular location: Cell membrane; Multi-pass membrane protein.
Interaction partners:
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein G
- Neuroendocrine secretory protein 55
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein subunit alpha-11
- Guanine nucleotide-binding protein subunit alpha
Sequence:
MSPYGLNLSLVDEATTCVTPRVPNTSVVLPTGGNGTSPALPIFSMTLGAVSNVLALALLAQVAGRLRRRRSTATFLLFVASLLAIDLAGHVIPGALVLRLYTAGRAPAGGACHFLGGCMVFFGLCPLLLGCGMAVERCVGVTQPLIHAARVSVARARLALALLAAMALAVALLPLVHVGHYELQYPGTWCFISLGPPGGWRQALLAGLFAGLGLAALLAALVCNTLSGLALLRARWRRRRSRRFRENAGPDDRRRWGSRGLRLASASSASSITSTTAALRSSRGGGSARRVHAHDVEMVGQLVGIMVVSCICWSPLLVLVVLAIGGWNSNSLQRPLFLAVRLASWNQILDPWVYILLRQAMLRQLLRLLPLRVSAKGGPTELSLTKSAWEASSLRSSRHSGFSHL
Protein: Chondrosarcoma-associated gene 2/3 protein (Cancer/testis antigen 24.2) (CT24.2) (Taxol-resistant-associated gene 3 protein) (TRAG-3) (Q9Y5P2)
Organism: Homo sapiens (Human)
Function: Drug-resistance related protein, its expression is associated with the chemotherapy resistant and neoplastic phenotype. May also be linked to the malignant phenotype.
Interaction partners:
- Melanoma-associated antigen 3
Sequence:
MWMGLIQLVEGVKRKDQGFLEKEFYHKTNIKMRCEFLACWPAFTVLGEAWRDQVDWSRLLRDAGLVKMSRKPRASSPLSNNHPPTPKRRGSGRHPLNPGPEALSKFPRQPGREKGPIKEVPGTKGSP
Protein: Protein IQ-DOMAIN 31 (AtIQD31) (Q8L4D8)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: May be involved in cooperative interactions with calmodulins or calmodulin-like proteins (By similarity). Recruits calmodulin proteins to microtubules, thus being a potential scaffold in cellular signaling and trafficking (By similarity). May associate with nucleic acids and regulate gene expression at the transcriptional or post-transcriptional level (By similarity).
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00768}. Nucleus envelope {ECO:0000269|PubMed:28115582}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:24134884, ECO:0000269|PubMed:28115582}. Cell membrane {ECO:0000269|PubMed:28115582}. Note=Associates to cortical microtubules (MTs). {ECO:0000269|PubMed:24134884}.
Interaction partners:
- Protein IQ-DOMAIN 9
- Protein IQ-DOMAIN 33
- Photosystem I assembly factor PSA3, chloroplastic
- Protein IQ-DOMAIN 10
Sequence:
MGKSTKWLKNVLLGKKTSKSSGSKDKERVVSGKEVLVTSKVEESDVVSDLPSFEVAETNTVDRSGGMLETQNVGPEEISDDEIELPEGKSTDSQNVAPVQDHSLSDAERIQREIAATSVQAAFRGYLARRAFWALKGIIRLQALIRGHLVRRQAVATLFSVMGIVRLQAFARGREIRKSDIGVQVYRKCRLQLLQGNKLANPTDAYLGIKKLTANAFAQKLLASSPKVLPVHAYDTSNPNSNLIWLENWSASCFWKPVPQPKKTISRKPQNRLLVEAESAKPKKSVRKVPASNFESSSVQTSFEFEKPKRSFRKVSSQSIEPPAVEDPQIELEKVKRSLRKVHNPVVESSIQPQRSPRKEVEKPKLGVEKTRESSYPLVHETAEEPVNVCDEKKKQEISEQPEEEVHALEMEVHTPGPLETNEALDSSLVNQIDSNEKAMVEEKPSMEKDTKEEKTPKPNNKENSAGKENQKSRKKGSATSKTEREESNGHHETSPSIPSYMQATKSAKAKLRLQGSPKSAEQDGTEKATVPRRHSLPSPGNGRITSHSPRTTRLANSGDKTGNKKEKPLLSSREGNAKTTPAERKR
Protein: Cathepsin S (EC 3.4.22.27) (P25774)
Organism: Homo sapiens (Human)
Function: Thiol protease. Key protease responsible for the removal of the invariant chain from MHC class II molecules and MHC class II antigen presentation. The bond-specificity of this proteinase is in part similar to the specificities of cathepsin L.
Subcellular location: Lysosome {ECO:0000269|PubMed:1377692}. Secreted {ECO:0000269|PubMed:9524075}. Cytoplasmic vesicle, phagosome {ECO:0000269|PubMed:30612035}.
Interaction partners:
- HLA class II histocompatibility antigen gamma chain
- Myeloperoxidase
- Cathepsin B
- BH3-interacting domain death agonist
- Cystatin-C
- Interleukin-10 receptor subunit alpha
- Apoptosis regulator Bcl-2
- Bcl-2-like protein 1
- Legumain
- Interleukin-10 receptor subunit beta
Sequence:
MKRLVCVLLVCSSAVAQLHKDPTLDHHWHLWKKTYGKQYKEKNEEAVRRLIWEKNLKFVMLHNLEHSMGMHSYDLGMNHLGDMTSEEVMSLMSSLRVPSQWQRNITYKSNPNRILPDSVDWREKGCVTEVKYQGSCGACWAFSAVGALEAQLKLKTGKLVSLSAQNLVDCSTEKYGNKGCNGGFMTTAFQYIIDNKGIDSDASYPYKAMDQKCQYDSKYRAATCSKYTELPYGREDVLKEAVANKGPVSVGVDARHPSFFLYRSGVYYEPSCTQNVNHGVLVVGYGDLNGKEYWLVKNSWGHNFGEEGYIRMARNKGNHCGIASFPSYPEI
Protein: DNA repair and recombination protein RAD54, putative (Q385M5)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- DNA repair protein RAD51 homolog
- Replication protein A subunit
- DNA polymerase
- DNA repair protein RAD50
- Protein artemis
- DNA 3'-5' helicase
- Exonuclease, putative
Sequence:
MPVFRNSTGFVTPFRIPSAVSREDSSSTTTTPRSSTVLQRQKREVVYPDSRGSSGNEVVAARLAKRANIDYHQPIKENKTFPNHGGPNTEVHDDNASEKTTEEGPVSSKPSVPPTSGVQQQQPQETAPVSTDAAGADEGSVEKSTEIVSLYPVSPHGCLYFQVETEAATRHDSVGIIVINTELLGVMMYDCAGRQYGNRPEPGYPISEEDMKSAKAGAKLKVGQKSVLLVTALLEESFRSGEFFLRSEHLSRKREEDKKAKEEAAAAAAPRRVVPKMTLGETLLGNMFASPIFRKRPREGQTGFVVPIAGRVKPGTSGIGAELKSLHDPDREGAVVLFHAHYKRDVNGRLQVSVVVDPIIGDKLRPHQRIGVKFLFDCITGQRMPGYHGAILADEMGLGKTIQTVATVYTCLKQGRYGVPTARKCLIVTPSSLVKNWCNEFDKWLGVGAVKYLSISESTPKGDRIISRFDGDGDVLVISYDQLRKYISRISTLKSVELVVCDEGHKLKNAEVKTTKAVDMLPTRNRIILSGTPIQNDLSEFHAMVGFVNPGILGTRDVFGRVFEEPVTLGRDPDCPEHLRMLGADRAHYLSTLTQRFILRRTQSINESYLPPKVDLTVFVRLGEKQREAYEKISAIVESSQCTPLVLISSLRKLCNHMDLFHEAVVSSNGDQKGKGGGIPKSVLPKGYKVGTLSQEVGSKMQFVSLMLDELCSNGDHDKLVIVSNFTQTLDVIAAMCKTKKISFFQLDGSMPIKRRQEVVDRFNVPNSQEIVFLLSSKAGGVGLNLIGANRLILFDPDWNPANDAQAMGRVWRDGQKKRVFIYRLLSTGSIEEKIYQRQVSKQGLSANVVDMQTDSKQHFTLEELRSLFRFRSDTDSETHDLLHCTSCEAVMNSGGGRASGRARLKEQEAPMKFRPVTVKKSGPRMDELKGWRHFSQCATFPLDKVIRAIATAAPGICSFIFADERDNTATTASKDGKGGKSGGAKVEPVMKVERAFAEDEEAIICMSQTEEMVRESQLEIEIHEDDDDDDYPSGDD
Protein: NADH-ubiquinone oxidoreductase chain 4 (EC 7.1.1.2) (NADH dehydrogenase subunit 4) (P03911)
Organism: Mus musculus (Mouse)
Function: Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) which catalyzes electron transfer from NADH through the respiratory chain, using ubiquinone as an electron acceptor. Essential for the catalytic activity and assembly of complex I.
Subcellular location: Mitochondrion inner membrane {ECO:0000269|PubMed:38575788}; Multi-pass membrane protein {ECO:0000269|PubMed:38575788}.
Interaction partners:
- Acyl carrier protein, mitochondrial
- NADH dehydrogenase 1 alpha subcomplex subunit 6
- NADH dehydrogenase 1 alpha subcomplex subunit 9, mitochondrial
- NADH-ubiquinone oxidoreductase chain 3
- NADH-ubiquinone oxidoreductase chain 6
- NADH dehydrogenase 1 alpha subcomplex subunit 8
- Cytochrome c oxidase subunit 1
- NADH dehydrogenase 1 alpha subcomplex subunit 2
- NADH-ubiquinone oxidoreductase chain 2
- NADH dehydrogenase 1 alpha subcomplex subunit 12
Sequence:
MLKIILPSLMLLPLTWLSSPKKTWTNVTSYSFLISLTSLTLLWQTDENYKNFSNMFSSDPLSTPLIILTAWLLPLMLMASQNHLKKDNNVLQKLYISMLISLQILLIMTFSATELIMFYILFEATLIPTLIIITRWGNQTERLNAGIYFLFYTLIGSIPLLIALILIQNHVGTLNLMILSFTTHTLDASWSNNLLWLACMMAFLIKMPLYGVHLWLPKAHVEAPIAGSMILAAILLKLGSYGMIRISIILDPLTKYMAYPFILLSLWGMIMTSSICLRQTDLKSLIAYSSVSHMALVIASIMIQTPWSFMGATMLMIAHGLTSSLLFCLANSNYERIHSRTMIMARGLQMVFPLMATWWLMASLANLALPPSINLMGELFITMSLFSWSNFTIILMGINIIITGMYSMYMIITTQRGKLTNHMINLQPSHTRELTLMALHMIPLILLTTSPKLITGLTM