wanglab/gogpt-training-data huggingface dataset:
Protein: Protocadherin beta 16 (Q91Y03)
Organism: Mus musculus (Mouse)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004162}; Single-pass membrane protein {ECO:0000256|ARBA:ARBA00004162}.
Interaction partners:
- Protocadherin beta 17
- Protocadherin beta 20
- Protocadherin beta 21
- Protocadherin beta-18
- Protocadherin beta 19
Sequence:
MEASRKLICRQRQVLFFFLLLGFPLTTAGELRRYSVVEEKEGRSFVTNLVKDLGLGQLELSRRGAKVISKGNKLHLQLDQETGDLLLNEKVDREKLCGHTEPCLLSFQVLLDNPLDIFQAELEVTDINDHSPEFLDKEIMLKISESSLPGATFPLKNAQDMDVGQNGIDKYLISSNSYFRVLTRKRSDGKKYPELVLDRALDREEEAELRLTLTAQDGGSLPRSGTTEVHIEVLDINDNAPQFEQLFYKAQIPEDSPIGFLIITVSATDKDIGVNGQISYSLFQVSDDISKTFSIHPLTGEVRLKEHLDFEKTQSYEINIEARDAGTFSGKCTILAQVLDVNDHAPEIILSAFTNSILENLPETMVAVFSVSDLDSGENGKVSCSIQDDLPFFLKPSGENFYTLLSQKPLDRESVAEYNITITVADMGSPILKTQVNLTVQVSDINDNAPIFTQTSYTMFIRENNSPALHIGTISATDSDSGSNAHITYSLLPPHDHQLALASFISINADNGQLFVLRALDYEALQAFEFHVGATDGGSPALSSQALVRMVVLDDNDNAPFVLYPMQNASAPYTELLPRAAEPGYLVTKVVAVDRDSGQNAWLSFQLLKATEPGLFSVWAHNGEVHTSRLLSERDVHKHRLILLVKDNGDPPRSASVTLHVLLVDGFSQPYLPLPEVARDPDHEDSELTLYLVIALASVSSLFLVSVLLFVGVRLCRRAREVSLGGCSVPEGHFPGHLVDVSGTGTLSQSYQYEVCLTGDSGTGEFKYLKPILPNFQDHSFRPEMGENPNSRNDWSFGIQLK
Protein: WW domain containing transcription regulator 1 (C9J038)
Organism: Homo sapiens (Human)
Subcellular location: Cell junction, tight junction {ECO:0000256|ARBA:ARBA00004435}. Cytoplasm {ECO:0000256|ARBA:ARBA00004496}. Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MNPASAPPPLPPPGQQVIHVTQDLDTDLEALFNSVMNPKPSSWRKKILPESFFKEPDSGSHSRQSSTDSSGGHPGPRLAGGAQHVRSHSSPASLQLGTGAGAAGSPAQQHAHLRQQSYDVTDELPLPPGWEMTFTATGQRYFLNHIEKITTWQDPRKAMNQPLNHMNLHPAVSSTPVPQRSMAVSQPNL
Protein: Ras-related protein Rab-3A (EC 3.6.5.2) (SMG P25A) (P11023)
Organism: Bos taurus (Bovine)
Function: Small GTP-binding protein that plays a central role in regulated exocytosis and secretion. Controls the recruitment, tethering and docking of secretory vesicles to the plasma membrane (By similarity). Upon stimulation, switches to its active GTP-bound form, cycles to vesicles and recruits effectors such as RIMS1, RIMS2, Rabphilin-3A/RPH3A, RPH3AL or SYTL4 to help the docking of vesicules onto the plasma membrane (By similarity). Upon GTP hydrolysis by GTPase-activating protein, dissociates from the vesicle membrane allowing the exocytosis to proceed (By similarity). Stimulates insulin secretion through interaction with RIMS2 or RPH3AL effectors in pancreatic beta cells (By similarity). Regulates calcium-dependent lysosome exocytosis and plasma membrane repair (PMR) via the interaction with 2 effectors, SYTL4 and myosin-9/MYH9 (By similarity). Acts as a positive regulator of acrosome content secretion in sperm cells by interacting with RIMS1 (By similarity). Also plays a role in the regulation of dopamine release by interacting with synaptotagmin I/SYT (By similarity).
Subcellular location: Cytoplasm, cytosol {ECO:0000250|UniProtKB:P63012}. Lysosome {ECO:0000250|UniProtKB:P20336}. Cytoplasmic vesicle, secretory vesicle {ECO:0000250|UniProtKB:P63012}. Cell projection, axon {ECO:0000250|UniProtKB:P63011}. Cell membrane {ECO:0000305}; Lipid-anchor {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Presynapse {ECO:0000250|UniProtKB:P63011}. Postsynapse {ECO:0000250|UniProtKB:P63011}. Note=Cycles between a vesicle-associated GTP-bound form and a cytosolic GDP-bound form. {ECO:0000250|UniProtKB:P63012}.
Interaction partners:
- Rabphilin-3A
- Vesicle-associated membrane protein 2
- RIMS2 protein
- Synaptotagmin-1
- Regulating synaptic membrane exocytosis 1
- DnaJ homolog subfamily C member 5
- Piccolo presynaptic cytomatrix protein
- Rab GDP dissociation inhibitor alpha
- Synaptosomal-associated protein 25
- Vesicular inhibitory amino acid transporter
Sequence:
MASATDARYGQKESSDQNFDYMFKILIIGNSSVGKTSFLFRYADDSFTPAFVSTVGIDFKVKTIYRNDKRIKLQIWDTAGQERYRTITTAYYRGAMGFILMYDITNEESFNAVQDWSTQIKTYSWDNAQVLLVGNKCDMEDERVVSSERGRQLADHLGFEFFEASAKDNINVKQTFERLVDVICEKMSESLDTADPAVTGAKQGPQLTDQQAPPHQDCAC
Protein: Cyclin-A2 (A0A0G2JVY9)
Organism: Rattus norvegicus (Rat)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MPGNSRQAGSALLSQQEDQENVNPEKVAPAQQPRAQAVLKAGKVRGPAPQQRLKTRRVAPLKDLPINDEHVPTVPSWKAVSKQPAFTIHVDEAEETQKRPAEQKETQCEDALAFSAAVSLPGARKPLVPLDYPMDGSFESPHAMDISIVLEDEKPVNVNEVPDYHEDIHTYLREMEVKCKPKVSYMKRQPDITNSMRAILVDWLVEVGEEYKLQNETLHLAVNYIDRFLSSMSVLRGKLQLVGTAAMLLASKFEEIYPPEVAEFVYITDDTYSKKQVLRMEHLVLKVLAFDLAAPTVNQFLTQYFLHLQPANCKVESLAMFLGELSLIDADPYLKYLPSLIAGAAFHLALYTVTGQSWPESLVQKTGYTLESLKPCLMDLHQTYLKAPQHAQQSIREKYKHSKYHSVSLLNPPETLNV
Protein: 2-oxoglutarate dehydrogenase complex component E1 (EC 1.2.4.2) (2-oxoglutarate dehydrogenase, mitochondrial) (Alpha-ketoglutarate dehydrogenase) (Thiamine diphosphate (ThDP)-dependent 2-oxoglutarate dehydrogenase) (B8JI08)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Mitochondrion {ECO:0000256|ARBA:ARBA00004173}. Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MHRLRTCAARLRPITASQTAKNLSQQGPAATPRTFQPLRCFSSPVAAEPFLNGTSSNYVEEMYYAWLENPKSVHKSWDIFFRNANAGAPPGTAYQSPPPLGVSLAGLAQAQSLVGAQPNVEKLVEDHLAVQSLIRAYQIRGHHVAQLDPLGIMDADLDSCVPTDIITSSDKLGFYGLEESDLDKVFRLPTTTFIGGDESALPLREIIRRLEMAYCQHIGVEFMFINDLDQCQWIRQKFERPGVMQFSLEEKRTLLARMVRSTRFEEFLQRKWSSEKRFGLEGCESLIPALKTIIDKSSENGVDTVIMGMPHRGRLNVLANVIRKELEQIFCQFDSKLEAADEGSGDVKYHLGMYHRRINRVTNRNITLSLVANPSHLEAVNPVVQGKTKAEQFYSGDTDGKRVMSILLHGDAAFAGQGIVYETFHLSDLPSYTTHGTVHVVANNQIGFTTDPRMARSSPYPTDVARVVNAPIFHVNADDPEAVMYVCNVAAEWRATFHKDVVVDLVCYRRNGHNEMDEPMFTQPLMYKQIKKQKGVLQKYAEKLIAEGAVTRQEYEEEIAKYDKICEEAHSRSKDEKILHIKHWLDSPWPGFFTLDGQPKSISCPSTGLPEEELAQIGQVASSVPVEDFTIHGGLSRILKGRGDMIKNRTVDWALGEYMAFGSLLKEGIHVRLSGQDVERGTFSHRHHVLHDQNVDKRICIPMNHMSPNQAPYTVCNSSLSEYGVLGFELGFAMASPNALVLWEAQFGDFHNTAQCIIDQFICPGQAKWVRQNGIVLLLPHGMEGMGPEHSSARPERFLQMCNDDPDFNPKITDDFDVRQLYDCNWIVVNCSNPANYFHVIRRQILLPFRKPLIVFTPKSLLRHPEAKSNFDQMLPGTHFQRVITDDGPPAQNPSEVKRIVFCTGKIYYELTRERKARNMENSVAITRIEQLSPFPFDLVRAETEKFPNADLVWCQEEHKNQGYYDYVKPRMRTTINRTKPVWYAGREPAAAPATGNKNTHLLELKRFLDTAFNLDAFKDHI
Protein: Meiotic expression up-regulated protein 6 (O94356)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Interaction partners:
- Meiotic PUF family protein 1
- Meiotically up-regulated protein PB17E12.09
- Meiotically up-regulated gene 131 protein
Sequence:
MSYEGREERPEQIAEPTFENVSEHNEHDSGSAEAQVETLEVPLSNETDNDDATENAVPAEVQAPEEPKEPETVDNIDPADDDPNSVAAPKVEEKKSKKKAKDEKPLTYTTGGYLYCRSNGLIPHVMKRYFYMLEGPMSMDLLDHYYKKHFHGTLQGNPTEPSLASEQMHDSDADSLFQSANDHLNRIAKATQDCRGLLFYSKSQSTSVPSGIINLTDAVSIEPGTGNKFTINFNNGKSETLEALDPESKNTWITDLKNAIAKKKETKDKIKELRAYNDTLKRLGKLAARSGPSASETFRYFLPMLSNGRDAKKSSSKSHGGKQNNSVAKDGLFDFFQNMIKGKTPQNDTASPIDNETSADPVDTTVEAQSVEVPENETNQIPTTEEHFPATTEEVAPASEEKPATGPAEESTSTQNVEQASTQNDNGTPIGQIADAIEEDVKGTAQSVEQAFIEETDIALPDIALPDVATPTADDQDPSTAATNEESVVSNEDRTSKKAGKKHHRHHKKKKGGNKRVFGFKLHKYAKPTKSVKTLQADPSLEFAKAGFEIFPSNLSKKLSGLVQKKVHKKFDKDGRLKEISQFSKTTIKPETPLTPTTTPTPRTAAQEDPAEETTDALASAEGENNQMPQVLETEAAPSIASEGRSITVNA
Protein: PABS domain-containing protein (Q389H0)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MHILKYTFLCVYIYSSLCVPSYTCKLSGVWWKHIGRKPTEMLDVSSPLFFFTFPCRSRMTQNLLHVLGTKPLLPYWVTLCPPIIQCTRGHIIYIYIYICYFLFGCLVTSSGGMYGAFWLIYLLNLCDMSTRWVSISPHFTPISVSFCFRVALADGEGVQAISSFLWLHSPLPTPVTVEVRARGLMFSC
Protein: Protein NrdI (P0A772)
Organism: Escherichia coli (strain K12)
Function: Probably involved in ribonucleotide reductase function.
Interaction partners:
- Ribonucleoside-diphosphate reductase 2 subunit alpha
- Glutaredoxin-like protein NrdH
- Ribonucleoside-diphosphate reductase 2 subunit beta
- Ribonucleoside-diphosphate reductase 1 subunit beta
- Transcriptional repressor NrdR
- Anaerobic ribonucleoside-triphosphate reductase
- Ribonucleoside-diphosphate reductase 1 subunit alpha
- Anaerobic ribonucleoside-triphosphate reductase-activating protein
Sequence:
MSQLVYFSSSSENTQRFIERLGLPAVRIPLNERERIQVDEPYILIVPSYGGGGTAGAVPRQVIRFLNDEHNRALLRGVIASGNRNFGEAYGRAGDVIARKCGVPWLYRFELMGTQSDIENVRKGVTEFWQRQPQNA
Protein: Redox- and pH-responsive transcriptional regulator WhiB3 (P9WF41)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: A redox-sensitive transcriptional regulator. Maintains intracellular redox homeostasis by regulating catabolic metabolism and polyketide biosynthesis. Regulates expression of the redox buffer ergothioneine (ERG) in a carbon-source-dependent manner; loss of ERG or mycothiol (MSH, the other major redox buffer in this bacteria) leads to respiratory alterations and bioenergetic deficiencies that negatively impact virulence. In response to low external pH (like that found in host macrophage phagosomes) alters endogenous gene expression leading to acid resistance; MSH and WhiB3 are probably part of a regulatory circuit that mediates gene expression upon acid stress. Regulates pathogenic lipid synthesis, coordinating proprionate flux (and other host-derived fatty acid oxidation intermediates) into methyl-branched fatty acids (polyacyltrehalose, phthiocerol dimycocerosates, sulfolipids) and the storage lipid triacylglycerol, functioning as reductive sink. During intracellular growth M.tuberculosis uses host fatty acids as an energy source, generating large quantities of proprionate and NADH/NADPH, which are toxic and highly reducing respectively. WhiB3 is thought to help dissipate proprionate and NADH/NADPH by switching to the in vivo carbon source and via lipid anabolism. Responds to NO and O(2). Regulates expression of genes encoding modular polyketide synthases such as pks2, pks3 and fbpA. The oxidized apo-form of WhiB3 binds DNA (with 2 intramolecular disulfide bonds); holo-WhiB3 (with the 4Fe-4S cluster) binds DNA considerably less well. Discriminates poorly between specific and non-specific DNA-binding. Plays a role in virulence and nutritional stress. In its apo-form can act as a protein disulfide reductase.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:Q9S426}.
Interaction partners:
- Possible two component system response transcriptional positive regulator PhoP
- RNA polymerase sigma factor SigA
Sequence:
MPQPEQLPGPNADIWNWQLQGLCRGMDSSMFFHPDGERGRARTQREQRAKEMCRRCPVIEACRSHALEVGEPYGVWGGLSESERDLLLKGTMGRTRGIRRTA
Protein: Proteasome subunit alpha type-5 (Q55G04)
Organism: Dictyostelium discoideum (Social amoeba)
Function: The proteasome is a multicatalytic proteinase complex which is characterized by its ability to cleave peptides with Arg, Phe, Tyr, Leu, and Glu adjacent to the leaving group at neutral or slightly basic pH. The proteasome has an ATP-dependent proteolytic activity (By similarity).
Subcellular location: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
Interaction partners:
- Proteasome subunit alpha type-3
- Proteasome subunit beta type-6
- Proteasome subunit beta type-2
- Proteasome subunit alpha type-4
- 26S proteasome regulatory subunit 7
- 26S proteasome regulatory subunit 6A homolog
- Proteasome subunit beta type-4
- Proteasome subunit alpha type-6
- Proteasome subunit alpha type-1
- Proteasome subunit beta type-3
Sequence:
MFLTRSEYDRGVNTFSPEGRLFQVEYALEAIKLGIGVQCEEGVVLAVEKRLTSPLLEPSSIQKVVEIDYHLICALSGLVADARTIIDHARIETQNHRFNYNEPMGVESCVQSICDLALRFGENRNSGEERMSRPFGVALLIAGIDEKGPSLYYSDPSGTFTQFHAKAIGAGSEGAQTTLQEKYSKTLTIAECQKLALTTLKQVMEEAITTTNVELAVITKADQKFKIYNKEELATVIQTLE
Protein: Patatin-like phospholipase domain-containing protein 2 (EC 3.1.1.3) (Adipose triglyceride lipase) (Calcium-independent phospholipase A2-zeta) (iPLA2-zeta) (EC 3.1.1.4) (Desnutrin) (Q8BJ56)
Organism: Mus musculus (Mouse)
Function: Catalyzes the initial step in triglyceride hydrolysis in adipocyte and non-adipocyte lipid droplets. Exhibits a strong preference for the hydrolysis of long-chain fatty acid esters at the sn-2 position of the glycerol backbone and acts coordinately with LIPE/HLS and DGAT2 within the lipolytic cascade. Also possesses acylglycerol transacylase and phospholipase A2 activities (By similarity). Transfers fatty acid from triglyceride to retinol, hydrolyzes retinylesters, and generates 1,3-diacylglycerol from triglycerides (By similarity). Regulates adiposome size and may be involved in the degradation of adiposomes (By similarity). May play an important role in energy homeostasis. May play a role in the response of the organism to starvation, enhancing hydrolysis of triglycerides and providing free fatty acids to other tissues to be oxidized in situations of energy depletion.
Subcellular location: Lipid droplet {ECO:0000269|PubMed:15550674, ECO:0000269|PubMed:16705060}. Cell membrane {ECO:0000250|UniProtKB:Q96AD5}; Multi-pass membrane protein {ECO:0000255}. Cytoplasm {ECO:0000269|PubMed:15337759}.
Interaction partners:
- 1-acylglycerol-3-phosphate O-acyltransferase ABHD5
- Perilipin-5
- Monoglyceride lipase
- Diacylglycerol O-acyltransferase 1
- Diacylglycerol O-acyltransferase 2
- Lipoprotein lipase
- G0/G1 switch protein 2
- Hormone-sensitive lipase
- Pancreatic triacylglycerol lipase
- Hepatic triacylglycerol lipase
Sequence:
MFPRETKWNISFAGCGFLGVYHIGVASCLREHAPFLVANATHIYGASAGALTATALVTGACLGEAGANIIEVSKEARKRFLGPLHPSFNLVKTIRGCLLKTLPADCHERANGRLGISLTRVSDGENVIISHFSSKDELIQANVCSTFIPVYCGLIPPTLQGVRYVDGGISDNLPLYELKNTITVSPFSGESDICPQDSSTNIHELRVTNTSIQFNLRNLYRLSKALFPPEPMVLREMCKQGYRDGLRFLRRNGLLNQPNPLLALPPVVPQEEDAEEAAVVEERAGEEDQLQPYRKDRILEHLPARLNEALLEACVEPKDLMTTLSNMLPVRLATAMMVPYTLPLESAVSFTIRLLEWLPDVPEDIRWMKEQTGSICQYLVMRAKRKLGDHLPSRLSEQVELRRAQSLPSVPLSCATYSEALPNWVRNNLSLGDALAKWEECQRQLLLGLFCTNVAFPPDALRMRAPASPTAADPATPQDPPGLPPC
Protein: Protein-L-isoaspartate(D-aspartate) O-methyltransferase (PIMT) (EC 2.1.1.77) (L-isoaspartyl protein carboxyl methyltransferase) (Protein L-isoaspartyl/D-aspartyl methyltransferase) (Protein-beta-aspartate methyltransferase) (P22062)
Organism: Rattus norvegicus (Rat)
Function: Initiates the repair of damaged proteins by catalyzing methyl esterification of L-isoaspartyl and D-aspartyl residues produced by spontaneous isomerization and racemization of L-aspartyl and L-asparaginyl residues in aging peptides and proteins (By similarity). Acts on EIF4EBP2, microtubule-associated protein 2, calreticulin, clathrin light chains a and b, Ubiquitin C-terminal hydrolase isozyme L1, phosphatidylethanolamine-binding protein 1, stathmin, beta-synuclein and alpha-synuclein (By similarity).
Subcellular location: Cytoplasm, cytosol {ECO:0000250|UniProtKB:P22061}.
Interaction partners:
- BLOC-1-related complex subunit 5
Sequence:
MAWKSGGASHSELIHNLRKNGIIKTDKVFEVMLATDRSHYAKSNPYMDSPQSIGFQATISAPHMHAYALELLFDQLHEGAKALDVGSGSGILTACFARMVGHSGKVIGIDHIKELVDDSITNVKKDDPMLLSSGRVRLVVGDGRMGFAEEAPYDAIHVGAAAPVVPQALIDQLKPGGRLILPVGPAGGNQMLEQYDKLQDGSVKMKPLMGVIYVPLTDKEKQWSRWK
Protein: Glycylpeptide N-tetradecanoyltransferase (EC 2.3.1.97) (A0A8I6A8X5)
Organism: Rattus norvegicus (Rat)
Interaction partners:
Sequence:
MMFSLLFLLSLISYRSPGGDLGAKKKKKKQKRKKEKPNSGGTKSDSASDSQEIKIQQSSKHNAIWQQISAGAAMGGDTMEGEWIDLRMYHKNPTIPIQKLQDIQRAMELLSACQGPARNIDEATKRRYQFWDTQPVPKLNEVITSHGAIEPDKDNIRQEPYSLPQGFMWDTLDLSNAEVLKELYTLLNENYVEDDDNMFRFDYSPEFLLWALRPPGWLLQWHCGVRVSSNKKLVGFISAIPANIRIYDSVKRMVEINFLCVHKKLRSKRVAPVLIREITRRVNLEGIFQAVYTAGVVLPKPVATCRYWHRSLNPRKLVEVKFSHLSRNMTLQRTMKLYRLPDVTKTSGLRPMEPKDIRAVRELINVYLKQFHLAPVMGDEEVAHWFLPREHIIDTFVVESPSGKLTDFLSFYTLPSTVMHHPAHKSLKAAYSFYNIHTETPLLDLMNDALIIAKLKGFDVFNALDLMENKTFLEKLKFGIGDGNLQYYLYNWRCPGTDSEKVGLVLQ
Protein: Sugar transport protein 11 (Hexose transporter 11) (Q9FMX3)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Mediates an active uptake of hexoses, probably by sugar/hydrogen symport. Can transport glucose, galactose, mannose, xylose and 3-O-methylglucose, but not fructose and ribose.
Subcellular location: Cell membrane {ECO:0000269|PubMed:15565288}; Multi-pass membrane protein {ECO:0000269|PubMed:15565288}.
Interaction partners:
- Cation/H
- Cysteine/Histidine-rich C1 domain family protein
- RNI-like superfamily protein
- Probable serine/threonine-protein kinase PBL25
- Transcription initiation factor IIE subunit beta
- Synaptotagmin-2
- Sucrose transport protein SUC8
- Lysine histidine transporter-like 7
Sequence:
MAGGAFIDESGHGGDYEGRVTAFVMITCIVAAMGGLLFGYDIGISGGVISMEDFLTKFFPDVLRQMQNKRGRETEYCKYDNELLTLFTSSLYLAALFASFLASTITRLFGRKVSMVIGSLAFLSGALLNGLAINLEMLIIGRLFLGVGVGFANQSVPLYLSEMAPAKIRGALNIGFQLAITIGILAANIVNYVTPKLQNGIGWRLSLGLAGVPAVMMLVGCFFLPDTPNSILERGNKEKAKEMLQKIRGTMEVEHEFNELCNACEAAKKVKHPWTNIMQARYRPQLTFCTFIPFFQQLTGINVIMFYAPVLFKTIGFGNDASLISAVITGLVNVLSTIVSIYSVDKFGRRALFLQGGFQMIVTQIAVGSMIGWKFGFNGEGNLSGVDADIILALICLYVAGFAWSWGPLGWLVPSEICPLEIRSAGQSLNVSVNMFFTFFIGQFFLTMLCHMKFGLFYFFAGMVLIMTIFIYFLLPETKGVPIEEMGKVWKEHRYWGKYSNNDDGDDVDDDAYF
Protein: BAG family molecular chaperone regulator 1B (BAG-1B) (O59739)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Inhibits the chaperone activity of HSP70/HSC70 by promoting substrate release.
Interaction partners:
- BAG family molecular chaperone regulator 1A
- E3 ubiquitin-protein ligase ubr11
- E3 ubiquitin-protein ligase ptr1
- Ribosome-associated molecular chaperone sks2
- Ornithine decarboxylase antizyme
- Ubiquitin-conjugating enzyme E2 4
- Large ribosomal subunit protein eL38B
Sequence:
MSFFTQLCSMDKKYWISLAVLSVTVLISALLKKRATETEDIVVVHYDGEKLNFVLRQPRLNMVSYTSFLRRVCNAFSVMPDKASLKLNGVTLKDGSLSDQNVQNGSELELELPKLSPAMQQIEAYIDELQQDLVPKIEAFCQSSPASAQDVQDLHTRLSETLLARMIKLDAVNVEDDPEARLKRKEAIRLSQQYLSKLDSTKNQNK
Protein: Uncharacterized protein (Q384F9)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MVADVVFVLVVEVFVCCWIESDNGSLLMVSFIYSCVSSRLMFASVKRAVGQYSCFHVICSPRFHSNYVVGVNKAPSWIASPTERRRKFGEECLAEGKERDGDMDVELVPVDVKKLALPLHLTDSIPQDIVDNIVARDRTLVFAPNMKILDLHRRLSRMKYRISVQPLGKVLHFRFFRLCKLSSGMPGDVTVETFRSIQQKLSEYTRFLVMDERWPLELSLEITPIIEHQRKQMLECQGECRVSTAEDVMELLSSVFSAELRVGAWCGLSCTPVLAKMACDECHRKHKLCRQDYSRGGVVGTVRYDIRSHKEAKEFVQNLSLGDIPVVGKPQARLLEDVYGITKCGGIADQEVRLGFSLSQSTMEFFLSVAYGTVRLPSEATTTLLRKPPRCKAAHIRRESQFGRVVSDEQFINTVMSVFDNVYTDLVEHDFVTGRVMIETRRTLPRTHWVVEESEDIAPRTNDRDLLREVTIRLARRFAPRRTEELRDIYSVGVHFGDVRSWSENERLQKKAVAVSEGGSPTTGGRKDGVIGAANGVPAPTVPKGSSSAGARQQKRKRTGTGPKPLRKGKMGAASGIRIVT
Protein: E3 ubiquitin-protein transferase MAEA (Macrophage erythroblast attacher) (D6RID6)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus matrix {ECO:0000256|ARBA:ARBA00004109}.
Interaction partners:
Sequence:
MVVAELEKTLSGCPAVDSVVSLLDGVVEKLSVLKRKAVESIQAEDESAKLCKRRIEHLKEHSSDQPAAASVWKRKRMDRMMVEHLLRCGYYNTAVKLARQSGIEDLVNIEMFLTA
Protein: Isocitrate dehydrogenase (NAD(+)), mitochondrial (OtIDH) (EC 1.1.1.41) (A0A096P8D3)
Organism: Ostreococcus tauri
Function: Performs an essential role in the oxidative function of the tricarboxylic acid cycle and respiration (Probable). Catalyzes the decarboxylation of isocitrate to produce 2-oxoglutarate and generate NADH to provide electrons for energy production (Probable).
Subcellular location: Mitochondrion {ECO:0000255}.
Interaction partners:
- Succinate--CoA ligase subunit beta, mitochondrial
- Citrate synthase
- Citrate synthase
- Succinate--CoA ligase subunit alpha, mitochondrial
- Succinate dehydrogenase iron-sulfur subunit, mitochondrial
- Malate dehydrogenase
- 4Fe-4S ferredoxin, iron-sulphur binding,conserved site
- fumarate hydratase
- malate dehydrogenase
- 3-isopropylmalate dehydrogenase
Sequence:
MTRVERGRVLARAIERAVAHRASARRWTTTTRTPAWMVTGWMGGRGVDRSTAMTRFERCGSTASSKITAAPMVYVRGEEMTAYVMDLIRSRWIEPRVDVGGWETFDLRAKNRDDTEDRVLRDVIEAGKRIKAIFKEPTVTPTADQVKRLGLRKSWGSPNGAMRRGWNGITISRDTIHIDGVELGYKKPVLFERHAVGGEYSAGYKNVGKGKLTTTFTPSEGPDAGKTVVVDEREIVDEEAAVVTYHNPYDNVHDLARFFFGRCLEAKVTPYVVTKKTVFKWQEPFWQIMRTVFDEEFKAQFVAAGVMKEGEELVHLLSDAATMKLVQWRQGGFGMAAHNYDGDVLTDELAQVHKSPGFITSNLVGVHEDGTLIKEFEASHGTVADMDEARLRGEETSLNPLGMVEGLIGAMNHAADVHNIDRDRTHAFTTKMRTVIHQLFREGKGTRDLCGPSGLTTEQFIDAVAERLDA
Protein: DNA-directed RNA polymerase subunit beta (EC 2.7.7.6) (Q583H5)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- DNA-direcetd RNA polymerase II, subunit 9, putative
- Transcription initiation protein, putative
- DNA-directed RNA polymerases I, II, and III subunit RPABC5
- RNA polymerase-like protein
- DNA-directed RNA polymerases I, II, and III subunit RPABC3
- DNA-directed RNA polymerase II, putative
- Plastid-encoded RNA polymerase subunit alpha
- Spt4/RpoE2 zinc finger domain-containing protein
- DNA excision repair protein, putative
- DNA repair and transcription factor protein, putative
Sequence:
MMDDELLLQLNEVEEITDDDVDDIHRVAGMENVNTADIDSEDIWEIISSFFREKGLVHQQVDSYNDFLLRIPRMARSLLEIVPRQDDQFDPGVHVESEPDQYRLSLEDVVVGNPSHEMSGFSRTEMHPLFPNECRLRDLTYDAVAQVTLAIRVYRSREEQPYRTFLQNMELGRIPIMLKSMRCNLLNKDEEELPRLNECPHDQGGYFIVNGTEKVLIAQERQAANHVYAFTRPKGLLCEIKSIVEGSLNKPRTLQILMPYKKSGPGHGYENLLCRVAQMDELIPLFVLFRALDMGSDKEILQTVVPDLKDVAMLEMLRGSMEDASTLEIFTRDEALWFIGKRLGKQDSRENLQREAQDLLMRDLLPHMGVDCAADRGKCLFIGYMVHRLLLLALGRREDTDRDFLGHKRIDVAGSLLTFQLNQFLVQVRREMAQTVHDYSTNRGGVVSFGRILHNRLITDGMRRCLATGNFGDLKSGNIKTGVSQTLNRLTYSSSLSNLRRIQNPISASSKATRPRNLHCTQWGYICPVETPEGGSIGLLKNLALMCLVSRGSDHTGVVQAVQSRITGFHSIALSDLADVRVARVFVNGTLIGVHGDPERLLRDLRARRRGGELSNEVSIVRDIRDREIRVFSDGGRCLRPLFVVEKSRIKLQKAGIGELLEPSTTLGGRREISWNKVMKKGYVELIDCEEEDSLLIAMVPSEVGKNYFYSHCEMDPSMILGICASIIPYPNHNQSPRNTYQSAMGKQAMGIYASNFNMRMDTTAHVLFYPQKPLVRTKAMSYMRSNDLPAGHNAIVAIACYSGYNQEDSIIMSRSAVERGFFRSVFWRSYKASEEKKREGREMFEIPDRKVCHVKRADYTKLDTDGLIKPGMPVIGGDIIVGKTIPVPKTLSEESPVSDTRILKRDCSISSRAAEKGVVDRVMLTENKGNRFTKVRIRTIKIPNIGDKFCSRHGQKGTNGIQFRQEDMPFNHDGISPDLIINPHAIPSRMTVAHLIETLAGKVACYKGGEVYATPFCSVVVEDFGKALTQLKLNRYGNERLYNGHTGLPLDHLIFFGPTYYQRLKHLSSDKIHARPRGPLQPLVRQPTEGRAHEGGLRFGEMERDCMLSYGASQWLRERLFRVSDYYSVHVCNMCGTICAADTDQNLYKCQGCDNDSHISQVLMPYACKLLFQELMSMAILPRLGTGPL
Protein: Xaa-Pro aminopeptidase 3 (X-Pro aminopeptidase 3) (EC 3.4.11.9) (Aminopeptidase P3) (APP3) (Q9NQH7)
Organism: Homo sapiens (Human)
Function: Catalyzes the removal of a penultimate prolyl residue from the N-termini of peptides, such as Leu-Pro-Ala. Also shows low activity towards peptides with Ala or Ser at the P1 position.
Subcellular location: [Isoform 1]: Mitochondrion {ECO:0000269|PubMed:20179356, ECO:0000269|PubMed:25609706}. Cytoplasm {ECO:0000269|PubMed:25609706}. Note=Mainly mitochondrial. Translocates to the cytoplasm following TNFRSF1B activation. {ECO:0000269|PubMed:25609706}.; SUBCELLULAR LOCATION: [Isoform 2]: Cytoplasm {ECO:0000269|PubMed:25609706}.
Interaction partners:
- Xaa-Pro aminopeptidase 2
- Xaa-Pro aminopeptidase 1
- Centrosome-associated protein ALMS1
- Dynein axonemal assembly factor 1
- Mitochondrial intermediate peptidase
- Centrosomal protein of 290 kDa
- Mitochondrial-processing peptidase subunit beta
Sequence:
MPWLLSAPKLVPAVANVRGLSGCMLCSQRRYSLQPVPERRIPNRYLGQPSPFTHPHLLRPGEVTPGLSQVEYALRRHKLMSLIQKEAQGQSGTDQTVVVLSNPTYYMSNDIPYTFHQDNNFLYLCGFQEPDSILVLQSLPGKQLPSHKAILFVPRRDPSRELWDGPRSGTDGAIALTGVDEAYTLEEFQHLLPKMKAETNMVWYDWMRPSHAQLHSDYMQPLTEAKAKSKNKVRGVQQLIQRLRLIKSPAEIERMQIAGKLTSQAFIETMFTSKAPVEEAFLYAKFEFECRARGADILAYPPVVAGGNRSNTLHYVKNNQLIKDGEMVLLDGGCESSCYVSDITRTWPVNGRFTAPQAELYEAVLEIQRDCLALCFPGTSLENIYSMMLTLIGQKLKDLGIMKNIKENNAFKAARKYCPHHVGHYLGMDVHDTPDMPRSLPLQPGMVITIEPGIYIPEDDKDAPEKFRGLGVRIEDDVVVTQDSPLILSADCPKEMNDIEQICSQAS