wanglab/gogpt-training-data huggingface dataset:
Protein: Mitochondrial distribution and morphology protein 38 (Q08179)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Involved in mitochondrial potassium homeostasis through the mitochondrial K(+)/H(+) exchange regulation. With MBA1, plays a role in ribosomal translation and protein insertion into the inner membrane.
Subcellular location: Mitochondrion inner membrane {ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:14576278, ECO:0000269|PubMed:15138253}; Single-pass membrane protein {ECO:0000255}.
Interaction partners:
- Inner membrane mitoribosome receptor MBA1, mitochondrial
- Mitochondrial inner membrane protein OXA1
- Magnesium transporter MRS2, mitochondrial
- mRNA-binding protein PUF3
- K
- Low affinity vacuolar monovalent cation/H
- Large ribosomal subunit protein uL22m
- Mitochondrial inner membrane magnesium transporter MFM1
Sequence:
MLNFASRASCVTRRQASLYFVKNQGPRLIASTIPSCHWPLRAQGVQPNYPLSLRFYSTDKSKSVTKPVAPTSTDAPAKPKETLMVKVKHALKHYANGTKLLGYEIKVSTKLLIKFAQGYELSRRERNQLRRTMGDVFRLIPFSAFLIIPFAELFLPFALKLFPNLLPSTYESGKDKQAKRNKLIEIRKKTSEFLHETLEESNLITYNTIENAEKKQKFLNFFRKLYSAKEGKIMTFQHDEISAIAQMFKNDSVLDNLSRPQLAAMSKFMSLRPFGNDNMLRYQIRSKLKDIMNDDKTIDYEGVESLSQEELYQACVSRGMKAYGVSKEDLVDNLKVWLELRLRQKIPSVLMVLSSTFTFGGLPKENYSKAFSPLAEKKETKSKYDDLLDLYYDGILQVLSSIPDPVYNVAKLDVSESKSSAAETEAEKQVAEKKIKTEEKPEETAIPKEEATAKESVIATTASAVTPKLVVVNEKAETAKTEEISQEKENAEPTDSAEATEAEEKKTSDDNEFKLNVLKEQEELIKKEEEEAKQRASREHVPDDINLDEEEEAKSVPPIPADQAAKTFVIKKD
Protein: Bacterial microcompartment shell protein PduJ (Bacterial microcompartment protein homohexamer) (BMC-H) (Propanediol utilization protein PduJ) (H9L478)
Organism: Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Function: One of the major shell proteins of the bacterial microcompartment (BMC) dedicated to 1,2-propanediol (1,2-PD) degradation. The isolated BMC shell component protein ratio for J:A:B':B:K:T:U is approximately 15:10:7:6:1:1:2. At least one of PduA or PduJ is required for BMC assembly; it must be encoded as the first gene in the pdu operon. Required for structural integrity of BMCs and to mitigate propionaldehyde toxicity, probably joins facets responsible for BMC closure. Edge residues (particularly Lys-25) are important for function and assembly of the BMC. 80% identical to PduA; although their pore regions appear structurally identical, unlike PduA plays no role in 1,2-PD diffusion into or out of the BMC shell. If pduJ is cloned in the chromosomal position of pduA it is able to complement a pduA deletion; it then has a functional pore as it assumes the transport functions of PduA. Overexpression of this protein leads to aberrant filaments that extend the length of the cell, cross the cleavage furrow and impair division. The filaments form nanotubes with a hollow center. Modeling suggests PduJ is probably the hub for binding multiple enzymes to the interior of the BMC; modeling suggests PduC, PduD, PduG and PduM are targeted to PduJ (Probable).
Subcellular location: Bacterial microcompartment {ECO:0000269|PubMed:12923081, ECO:0000269|PubMed:24747050}.
Interaction partners:
- Bacterial microcompartment shell vertex protein PduN
- Bacterial microcompartment shell protein PduT
- Propanal dehydrogenase
- Bacterial microcompartment shell protein PduU
- Bacterial microcompartment shell protein PduB
- Phosphate propanoyltransferase
- Bacterial microcompartment assembly protein PduM
- Propanediol dehydratase medium subunit
- Bacterial microcompartment shell vertex protein EutN
- Propanediol dehydratase small subunit
Sequence:
MNNALGLVETKGLVGAIEAADAMVKSANVQLVGYEKIGSGLVTVMVRGDVGAVKAAVDAGSAAASVVGEVKSCHVIPRPHSDVEAILPKSA
Protein: SP2 protein (Q9BRW5)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MAATAAVSPSDYLQPAASTTQDSQPSPLALLAATCSKIGPPAVEAAVTPPAPPQPTPRKLVPIKPAPLPLSPGKNSFGILSSKGNILQIQGSQLSASYPGGQLVFAIQNPTMINKGTRSNANIQYQAVPQIQASNSQTIQVQPNLTNQIQIIPGTNQAIITPSPSSHKPVPIKPAPIQKSSTTTTPVQSGANVVKLTGGGGNVTLTLPVNNLVNASDTGAPTQLLTASCQTGMLNSTRMFLFLAFINVL
Protein: Glutathione S-transferase (EC 2.5.1.18) (Q5T8R1)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MPMTLGYWDIRGLAHAIRLLLEYTDSSYVEKKYTLGDAPDYDRSQWLNEKFKLGLDFPNLPYLIDGAHKITQSNAILRYIARKHNLCGETEEEKIRVDILENQTTDNWMQLVMICYHPEFEKLKPKYLEELPEKLKLYSEFLGKRPWFAGDKITFVDFLAYDVLDMKRIFEPKCLDAFLNLKDFISRFEGLKKISAYMKSSQFLRGLLFGKSATWNSK
Protein: MutL homolog 1 (A0A669KAW3)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MSFVAGVIRRLDETVVNRIAAGEVIQRPANAIKEMIENCLDAKSTSIQVIVKEGGLKLIQIQDNGTGIRKEDLDIVCERFTTSKLQSFEDLASISTYGFRGEALASISHVAHVTITTKTADGKCAYRASYSDGKLKAPPKPCAGNQGTQITVEDLFYNIATRRKALKNPSEEYGKILEVVGRYSVHNAGISFSVKKQGETVADVRTLPNASTVDNIRSIFGNAVSRELIEIGCEDKTLAFKMNGYISNANYSVKKCIFLLFINHRLVESTSLRKAIETVYAAYLPKNTHPFLYLSLEISPQNVDVNVHPTKHEVHFLHEESILERVQQHIESKLLGSNSSRMYFTQTLLPGLAGPSGEMVKSTTSLTSSSTSGSSDKVYAHQMVRTDSREQKLDAFLQPLSKPLSSQPQAIVTEDKTDISSGRARQQDEEMLELPAPAEVAAKNQSLEGDTTKGTSEMSEKRGPTSSNPRKRHREDSDVEMVEDDSRKEMTAACTPRRRIINLTSVLSLQEEINEQGHEVLREMLHNHSFVGCVNPQWALAQHQTKLYLLNTTKLSEELFYQILIYDFANFGVLRLSEGNLIGLPLLIDNYVPPLEGLPIFILRLATEVNWDEEKECFESLSKECAMFYSIRKQYISEESTLSGQQSEVPGSIPNSWKWTVEHIVYKALRSHILPPKHFTEDGNILQLANLPDLYKVFERC
Protein: Small ArfGAP2 (A0A087WV97)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MGKVGRARFAQKDVLQIEEIGPVKLFVRDWPRWASWNIGVFICIRCAGIHRNLGVHISRVKSVNLDQWTQEQIQCMQEMGNGKANRLYEAYLPETFRRPQIDPAVEGFIRDKYEKKKYMDRSLDINAFRKEKDDKWKRGSEPVPEKKLEPVVFEKVKMPQKKEDPQLPRKSSPKSTAPVMDLLGLDAPVACSIANSKTSNTLEKDLDLLASVPSPSSSGSRKVVGSMPTAGSAGSVPENLNLFPEPGSKSEEIGKKQLSKDSILSLYGSQTPQMPTQAMFMAPAQMAYPTAYPSFPGVTPPNSIMGSMMPPPVGMVAQPGASGMVAPMAMPAGYMGGMQASMMGVPNGMMTTQQAGYMAGMAAMPQTVYGVQPAQQLQWNLTQMTQQMAGMNFYGANGMMNYGQSMSGGNGQAANQTLSPQMWK
Protein: Down syndrome cell adhesion molecule 1, isoform I (Q0E9I0)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MNMPNERLKWLMLFAAVALIACGSQTLAANPPDADQKGPVFLKEPTNRIDFSNSTGAEIECKASGNPMPEIIWIRSDGTAVGDVPGLRQISSDGKLVFPPFRAEDYRQEVHAQVYACLARNQFGSIISRDVHVRAVVAQYYEADVNKEHVIRGNSAVIKCLIPSFVADFVEVVSWHTDEEENYFPGAEYDGKYLVLPSGELHIREVGPEDGYKSYQCRTKHRLTGETRLSATKGRLVITEPVGGKAPTLLSNDIKRSWIERMLSTNLALFCPAQGFPVPAFRWYKFIEGTTRKQAVVLNDRVKQVSGTLIIKDAVVEDSGKYLCVVNNSVGGESVETVLTVTAPLSAKIDPPTQTVDFGRPAVFTCQYTGNPIKTVSWMKDGKAIGHSEPVLRIESVKKEDKGMYQCFVRNDQESAEASAELKLGGRFDPPVIRQAFQEETMEPGPSVFLKCVAGGNPTPEISWELDGKKIANNDRYQVGQYVTVNGDVVSYLNITSVHANDGGLYKCIAKSKVGVAEHSAKLNVYGLPYIRQMEKKAIVAGETLIVTCPVAGYPIDSIVWERDNRALPINRKQKVFPNGTLIIENVERNSDQATYTCVAKNQEGYSARGSLEVQVMVPPKITPFDFGDEPTNFEDSVSVTCLISSGDLPIDIEWFFNEYGISSYSGISVVKGGKRNSVLSIDSVQARHAGNYSCRAKNHAAAVNYTTSLIVNVPPRWILEPTDKAFAQGSDAKVECKADGFPKPQVTWKKAVGDTPGEYKDLKKSDNIRVEEGTLHVDNIQKTNEGYYLCEAINGIGSGLSAVIMISVQAPPEFTEKLRNQTARRGEPAVLQCEAKGEKPIGILWNMNNMRLDPKNDNRYTIREEILSTGVMSSLSIKRTERSDSALFTCVATNAFGSDDASINMIVQEVPEMPYALKVLDKSGRSVQLSWAQPYDGNSPLDRYIIEFKRSRASWSEIDRVIVPGHTTEAQVQKLSPATTYNIRIVAENAIGTSQSSEAVTIITAEEAPSGKPQNIKVEPVNQTTMRVTWKPPPRTEWNGEILGYYVGYKLSNTNSSYVFETINFITEEGKEHNLELQNLRVYTQYSVVIQAFNKIGAGPLSEEEKQFTAEGTPSQPPSDTACTTLTSQTIRVGWVSPPLESANGVIKTYKVVYAPSDEWYDETKRHYKKTASSDTVLHGLKKYTNYTMQVLATTAGGDGVRSVPIHCQTEPDVPEAPTDVKALVMGNAAILVSWRPPAQPNGIITQYTVYSKAEGAETETKTQKVPHYQMSFEATELEKNKPYEFWVTASTTIGEGQQSKSIVAMPSDQVPAKIASFDDTFTATFKEDAKMPCLAVGAPQPEITWKIKGVEFSANDRMRVLPDGSLLIKSVNRQDAGDYSCHAENSIAKDSITHKLIVLAPPQSPHVTLSATTTDALTVKLKPHEGDTAPLHGYTLHYKPEFGEWETSEVSVDSQKHNIEGLLCGSRYQVYATGFNNIGAGEASDILNTRTKGQKPKLPEKPRFIEVSSNSVSLHFKAWKDGGCPMSHFVVESKKRDQIEWNQISNNVKPDNNYVVLDLEPATWYNLRITAHNSAGFTVAEYDFATLTVTGGTIAPSRDLPELSAEDTIRIILSNLNLVVPVVAALLVIIIAIIVICILRSKGNHHKDDVVYNQTMGPGATLDKRRPDLRDELGYIAPPNRKLPPVPGSNYNTCDRIKRGRGGLRSNHSTWDPRRNPNLYEELKAPPVPMHGNHYGHAHGNAECHYRHPGMEDEICPYATFHLLGFREEMDPTKAMNFQTFPHQNGHAGPVPGHAGTMLPPGHPGHVHSRSGSQSMPRANRYQRKNSQGGQSSIYTPAPEYDDPANCAEEDQYRRYTRVNSQGGSLYSGPGPEYDDPANCAPEEDQYGSQYGGPYGQPYDHYGSRGSMGRRSIGSARNPGNGSPEPPPPPPRNHDMSNSSFNDSKESNEISEAECDRDHGPRGNYGAVKRSPQPKDQRTTEEMRKLIERNETGPKQLQLQQANGAGFTAYDTMAV
Protein: Cuticular protein 49Ac, isoform F (Cuticular protein 49Ac, isoform G) (A0A0B4LG85)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MFTKSMLSFSLVVALFVVCHASPVPDNNGKYTVPQQSSNDGKYRPSDDGKYHGNSQNEGRYHHMPIPYRHVSDQRELGKYHHIPYPYDGGYGPYAGSNIPYVHDDRPYNHDLYTSTTTKKPTTTTKRTTTSTTTTTTTPRNILFNYDDEGRHKILHKEEVRKQDKYDHSYLTENGIYGEEQAKLHHTGGTHAKGFYEYTGDDGKLYRVNYASNDGGFMPQGDHIHPIPDAIVRALKYVEEQHKINGGAQFDHRGFRINHMTKDLKAQIKAIHLEEMPKELTEQIHMLEHEVELAEEEEREEQAALERLRQAAKSH
Protein: Liprin-alpha-3 (Protein tyrosine phosphatase receptor type f polypeptide-interacting protein alpha-3) (PTPRF-interacting protein alpha-3) (O75145)
Organism: Homo sapiens (Human)
Function: May regulate the disassembly of focal adhesions. May localize receptor-like tyrosine phosphatases type 2A at specific sites on the plasma membrane, possibly regulating their interaction with the extracellular environment and their association with substrates.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:Q91Z79}. Cytoplasmic vesicle, secretory vesicle, acrosome {ECO:0000269|PubMed:23124857}. Note=Also detected in epididymosome. {ECO:0000250|UniProtKB:Q91Z79}.
Interaction partners:
- Receptor-type tyrosine-protein phosphatase F
- Serine/threonine-protein phosphatase 2A catalytic subunit alpha isoform
- Receptor-type tyrosine-protein phosphatase delta
- ELKS/Rab6-interacting/CAST family member 1
- Protein unc-13 homolog B
- Receptor-type tyrosine-protein phosphatase S
- ARF GTPase-activating protein GIT1
- Liprin-beta-1
- Regulating synaptic membrane exocytosis protein 1
- Liprin-beta-2
Sequence:
MMCEVMPTISEDGRRGSALGPDEAGGELERLMVTMLTERERLLETLREAQDGLATAQLRLRELGHEKDSLQRQLSIALPQEFAALTKELNLCREQLLEREEEIAELKAERNNTRLLLEHLECLVSRHERSLRMTVVKRQAQSPGGVSSEVEVLKALKSLFEHHKALDEKVRERLRMALERVAVLEEELELSNQETLNLREQLSRRRSGLEEPGKDGDGQTLANGLGPGGDSNRRTAELEEALERQRAEVCQLRERLAVLCRQMSQLEEELGTAHRELGKAEEANSKLQRDLKEALAQREDMEERITTLEKRYLSAQREATSLHDANDKLENELASKESLYRQSEEKSRQLAEWLDDAKQKLQQTLQKAETLPEIEAQLAQRVAALNKAEERHGNFEERLRQLEAQLEEKNQELQRARQREKMNDDHNKRLSETVDKLLSESNERLQLHLKERMGALEEKNSLSEEIANMKKLQDELLLNKEQLLAEMERMQMEIDQLRGRPPSSYSRSLPGSALELRYSQAPTLPSGAHLDPYVAGSGRAGKRGRWSGVKEEPSKDWERSAPAGSIPPPFPGELDGSDEEEAEGMFGAELLSPSGQADVQTLAIMLQEQLEAINKEIKLIQEEKETTEQRAEELESRVSSSGLDSLGRYRSSCSLPPSLTTSTLASPSPPSSGHSTPRLAPPSPAREGTDKANHVPKEEAGAPRGEGPAIPGDTPPPTPRSARLERMTQALALQAGSLEDGGPPRGSEGTPDSLHKAPKKKSIKSSIGRLFGKKEKGRMGPPGRDSSSLAGTPSDETLATDPLGLAKLTGPGDKDRRNKRKHELLEEACRQGLPFAAWDGPTVVSWLELWVGMPAWYVAACRANVKSGAIMANLSDTEIQREIGISNPLHRLKLRLAIQEMVSLTSPSAPASSRTSTGNVWMTHEEMESLTATTKPETKEISWEQILAYGDMNHEWVGNDWLPSLGLPQYRSYFMESLVDARMLDHLNKKELRGQLKMVDSFHRVSLHYGIMCLKRLNYDRKDLERRREESQTQIRDVMVWSNERVMGWVSGLGLKEFATNLTESGVHGALLALDETFDYSDLALLLQIPTQNAQARQLLEKEFSNLISLGTDRRLDEDSAKSFSRSPSWRKMFREKDLRGVTPDSAEMLPPNFRSAAAGALGSPGLPLRKLQPEGQTSGSSRADGVSVRTYSC
Protein: RAB30, member RAS oncogene family, isoform CRA_a (cDNA FLJ78283, highly similar to Homo sapiens RAB30, member RAS oncogene family (RAB30), mRNA) (cDNA, FLJ92634, Homo sapiens RAB30, member RAS oncogene family (RAB30), mRNA) (A8K5R1)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MSMEDYDFLFKIVLIGNAGVGKTCLVRRFTQGLFPPGQGATIGVDFMIKTVEINGEKVKLQIWDTAGQERFRSITQSYYRSANALILTYDITCEESFRCLPEWLREIEQYASNKVITVLVGNKIDLAERREVSQQRAEEFSEAQDMYYLETSAKESDNVEKLFLDLACRLISEARQNTLVNNVSSPLPGEGKSISYLTCCNFN
Protein: non-specific serine/threonine protein kinase (EC 2.7.11.1) (Q9M1P3)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
Sequence:
MEPWIDELTDDLQSVSFTSAGTTVNRSTSSGSRSSSSAAALTPAPSAHGSFSSSKLPPSLRSSLSLSDLRFRLRLGSGDIGSVFLAEFKSLTAVTETTAVKLPLLAAKVMDKKELASRSKEGRAKTEREILESLDHPFLPTLYAAIDSPKWLCLLTEFCPGGDLHVLRQKQTHKRFHESAVRFYVSEVIVAIEYLHMLGIVYRDLKPENVLVRSDGHIMLTDFDLSLKCDESTSTPQIVLNRNNLPNGSSDQNENQGMDHRQTTSSSCMIPNCIVPAVSCFHPRIRRRKKKTDHRNNGPELVAEPVDVRSMSFVGTHEYLAPEIVSVYIMYNFPMWYPNMKRKMWMAGEGHGSAVDWWTLGIFMFELFYGTTPFKGMDHELTLANIVARALEFPKEPTIPSAAKDLISQLLAKDPSRRLGSSLGATAVKRHPFFQGVNWALLMCTRPPFLPPPFRKELLSDDICPETHVDYY
Protein: Steroidogenic acute regulatory protein, mitochondrial (StAR) (START domain-containing protein 1) (StARD1) (P97826)
Organism: Rattus norvegicus (Rat)
Function: Plays a key role in steroid hormone synthesis by enhancing the metabolism of cholesterol into pregnenolone. Mediates the transfer of cholesterol from the outer mitochondrial membrane to the inner mitochondrial membrane where it is cleaved to pregnenolone (By similarity).
Subcellular location: Mitochondrion {ECO:0000250|UniProtKB:P51557}.
Interaction partners:
- Translocator protein
- Non-selective voltage-gated ion channel VDAC1
- Cholesterol side-chain cleavage enzyme, mitochondrial
- Non-selective voltage-gated ion channel VDAC2
- Non-selective voltage-gated ion channel VDAC3
- Steroid 17-alpha-hydroxylase/17,20 lyase
- Cytochrome P450 11B3, mitochondrial
- Aromatase
- cAMP-dependent protein kinase catalytic subunit beta
- cAMP-dependent protein kinase catalytic subunit alpha
Sequence:
MLLATFKLCAGSSYRHMRNMKGLRHQAVLAIGQELNRRALGDPSPGWMGQVRRRSSLLGSQLEATLYSDQELSYIQQGEEAMQKALGILNNQEGWKKESQQENGDEVLSKVVPGVGKVFRLEVLLDQPMDRLYEELVDRMEAMGEWNPNVKEIKVLKKIGKDTVITHELAAAAAGNLVGPRDFVSVRCTKRRGSTCVLAGMATHFGEMPEQSGVIRAEHGPTCMVLHPLAGSPSKTKLTWLLSIDLKGWLPKTIINQVLSQTQIEFASHLRKRLESSPASEAQC
Protein: Integrin alpha-8 [Cleaved into: Integrin alpha-8 heavy chain; Integrin alpha-8 light chain] (A2ARA8)
Organism: Mus musculus (Mouse)
Function: Integrin alpha-8/beta-1 functions in the genesis of kidney and probably of other organs by regulating the recruitment of mesenchymal cells into epithelial structures. It recognizes the sequence R-G-D in a wide array of ligands including TNC, FN1, SPP1 TGFB1, TGFB3 and VTN. NPNT is probably its functional ligand in kidney genesis. Neuronal receptor for TNC it mediates cell-cell interactions and regulates neurite outgrowth of sensory and motor neurons.
Subcellular location: Membrane {ECO:0000269|PubMed:10742111}; Single-pass type I membrane protein {ECO:0000269|PubMed:10742111}. Cell membrane {ECO:0000250}.
Interaction partners:
- Integrin beta-1
- Vitronectin
- Nephronectin
- Fibronectin
- Extracellular matrix organizing protein FRAS1
- FRAS1-related extracellular matrix protein 1
- FRAS1-related extracellular matrix protein 2
- Tenascin
- Tenascin XB
- Tenascin-N
Sequence:
MSAGTHCGPPGNRAPPFARLCCVSAALGMLWSPACLAFNLDVDKLTVYSGPEGSYFGYSLDFYIPDARTASVLVGAPKANTSQPDIVEGGAVYYCPWPSERSAQCKQIPFDTTNNRKIRVNGTKEPIEFKSNQWFGATVRAHKGKVVACAPLYHWRTLKPNPAKDPVGTCYVAIQNFSAYAEHSPCRNSNADPEGQGYCQAGFSLDFYKNGDLIVGGPGSFYWQGQVITVSIADIIANYSFKDILRKLAAEKQTDVAPASYDDSYLGYSVAAGEFTGDSQQELVAGIPRGAQNFGYVSIINSTDMTFIQNFTGEQMASYFGYTVVVSDVNNDGMDDILVGAPLFMEREFESNPREVGQVYLYLQASALLFQDPQVLTGTETFGRFGSSVAHLGDLNQDGYNDIAIGVPFAGKDQRGKVLIYNGNPRGLHSKPSQVLQGIWGSQTIPSGFGFSLRGDADIDKNDYPDLLVGAFGKGKVAVYRARPVVTVDAQLLLHPMIINLENKTCQIPEFPTPVACFSVRVCASIAGQSISNTIALLAEVQLDFLKQKGAIKRTLFLHNHQSHFTFPFVMKQQKSLHCQDFMVYLRDETEFRDKLSPINISLNYSLDDSTFKDSLEVKPILNHYRDNVVTEQAHILVDCGEDNLCVPDLKLSARPDKHQIIIGDENHLMLIINARNEGEGAYEAELFVIIPEEADYVGIERNNKGLRPLSCEYKMENVTRMVVCDLGNPMVTGTNFSLGLRFAVPRLEKTNMSINFDLQIRSSNKDNPDSNFERVQINITAIAQVEIRGVSHPPQIVLPIHNWEPEKKPHKEEEVGPLVEHIYELHNIGPSTISDSILDVGWPFSARDEFLLYIFHLQTLGPLQCQTNPEINPQDIKPAASPEDTPELSAFLRNATIPHLVRKRDVPVVQLHRQSPARILNCTNIDCLQISCAVGRLGGGESAVLKVRSRLWAHTFLKRKNDHYALASLVSFEVKKMPYKEQPAKLPAGSTAVKTSVIWATPNVSFSIPLWVIILAILLGLLVLAILTLALWKCGFFDRARPPQDEMTDREQLTSDKTPEA
Protein: Arf-GAP with Rho-GAP domain, ANK repeat and PH domain-containing protein 2 (Centaurin-delta-1) (Cnt-d1) (Protein PARX) (Q8WZ64)
Organism: Homo sapiens (Human)
Function: Phosphatidylinositol 3,4,5-trisphosphate-dependent GTPase-activating protein that modulates actin cytoskeleton remodeling by regulating ARF and RHO family members. Is activated by phosphatidylinositol 3,4,5-trisphosphate (PtdIns(3,4,5)P3) binding. Can be activated by phosphatidylinositol 3,4-bisphosphate (PtdIns(3,4,5)P2) binding, albeit with lower efficiency (By similarity).
Subcellular location: Cytoplasm {ECO:0000250}.
Interaction partners:
- Ras-related protein Rab-13
Sequence:
MSSVSEVNVDIKDFLMSINLEQYLLHFHESGFTTVKDCAAINDSLLQKIGISPTGHRRRILKQLQIILSKMQDIPIYANVHKTKKNDDPSKDYHVPSSDQNICIELSNSGSVQTSSPPQLETVRKNLEDSDASVERSQYPQSDDKLSPPKRDFPTAEEPHLNLGSLNDSLFGSDNIKIESLITKKTVDHTVEEQQTEKVKLITENLSKLPNADSECLSFVGCSTSGTNSGNGTNGLLEGSPPSPFFKFQGEMIVNDLYVPSSPILAPVRSRSKLVSRPSRSFLLRHRPVPEIPGSTKGVSGSYFRERRNVATSTEKSVAWQNSNEENSSSIFPYGETFLFQRLENSKKRSIKNEFLTQGEALKGEAATATNSFIIKSSIYDNRKEKISEDKVEDIWIPREDKNNFLIDTASESEYSTVEECFQSLRRKNSKASKSRTQKALILDSVNRHSYPLSSTSGNADSSAVSSQAISPYACFYGASAKKVKSGWLDKLSPQGKRMFQKRWVKFDGLSISYYNNEKEMYSKGIIPLSAISTVRVQGDNKFEVVTTQRTFVFRVEKEEERNDWISILLNALKSQSLTSQSQAVVTPEKCGYLELRGYKAKIFTVLSGNSVWLCKNEQDFKSGLGITIIPMNVANVKQVDRTVKQSFEIITPYRSFSFTAETEKEKQDWIEAVQQSIAETLSDYEVAEKIWFNESNRSCADCKAPDPDWASINLCVVICKKCAGQHRSLGPKDSKVRSLKMDASIWSNELIELFIVIGNKRANDFWAGNLQKDEELHMDSPVEKRKNFITQKYKEGKFRKTLLASLTKEELNKALCAAVVKPDVLETMALLFSGADVMCATGDPVHSTPYLLAKKAGQSLQMEFLYHNKFSDFPQHDIHSEGVLSQESSQSTFLCDFLYQAPSAASKLSSEKKLLEETNKKWCVLEGGFLSYYENDKSTTPNGTININEVICLAIHKEDFYLNTGPIFIFEIYLPSERVFLFGAETSQAQRKWTEAIAKHFVPLFAENLTEADYDLIGQLFYKDCHALDQWRKGWFAMDKSSLHFCLQMQEVQGDRMHLRRLQELTISTMVQNGEKLDVLLLVEKGRTLYIHGHTKLDFTVWHTAIEKAAGTDGNALQDQQLSKNDVPIIVNSCIAFVTQYGLGCKYIYQKNGDPLHISELLESFKKDARSFKLRAGKHQLEDVTAVLKSFLSDIDDALLTKELYPYWISALDTQDDKERIKKYGAFIRSLPGVNRATLAAIIEHLYRVQKCSEINHMNAHNLALVFSSCLFQTKGQTSEEVNVIEDLINNYVEIFEVKEDQVKQMDIENSFITKWKDTQVSQAGDLLIEVYVERKEPDCSIIIRISPVMEAEELTNDILAIKNIIPTKGDIWATFEVIENEELERPLHYKENVLEQVLRWSSLAEPGSAYLVVKRFLTADTIKHCSDRSTLGSIKEGILKIKEEPSKILSGNKFQDRYFVLRDGFLFLYKDVKSSKHDKMFSLSSMKFYRGVKKKMKPPTSWGLTAYSEKHHWHLCCDSSRTQTEWMTSIFIAQHEYDIWPPAGKERKRSITKNPKIGGLPLIPIQHEGNATLARKNIESARAELERLRLSEKCDKESVDSSLKERASMVAHCLEHKDDKLRNRPRKHRSFNCLEDTEPEAPLGQPKGHKGLKTLRKTEDRNSKATLDSDHKLPSRVIEELNVVLQRSRTLPKELQDEQILK
Protein: Ferredoxin-thioredoxin reductase, variable chain (FTR-V) (Ferredoxin-thioredoxin reductase subunit A) (FTR-A) (Q55781)
Organism: Synechocystis sp. (strain ATCC 27184 / PCC 6803 / Kazusa)
Function: Variable subunit of the ferredoxin-thioredoxin reductase (FTR), which catalyzes the two-electron reduction of thioredoxins by the electrons provided by reduced ferredoxin.
Interaction partners:
- Ferredoxin-thioredoxin reductase, catalytic chain
- Ferredoxin-1
- Thioredoxin
- Sll1390 protein
- Ssl2781 protein
- Sll0372 protein
- Slr1052 protein
- Slr0600 protein
- Sll1372 protein
- Sll1155 protein
Sequence:
MNVGDRVRVTSSVVVYHHPEHKKTAFDLQGMEGEVAAVLTEWQGRPISANLPVLVKFEQRFKAHFRPDEVTLIED
Protein: Probable serine protease PepA (Serine proteinase) (MTB32A) (O07175)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Interaction partners:
- Proteasome-associated ATPase
- Trehalose synthase/amylase TreS
- PPE family protein PPE18
- Glycerol kinase
- Proteasome subunit beta
- CysO-cysteine peptidase
- Maltokinase
Sequence:
MSNSRRRSLRWSWLLSVLAAVGLGLATAPAQAAPPALSQDRFADFPALPLDPSAMVAQVGPQVVNINTKLGYNNAVGAGTGIVIDPNGVVLTNNHVIAGATDINAFSVGSGQTYGVDVVGYDRTQDVAVLQLRGAGGLPSAAIGGGVAVGEPVVAMGNSGGQGGTPRAVPGRVVALGQTVQASDSLTGAEETLNGLIQFDAAIQPGDSGGPVVNGLGQVVGMNTAASDNFQLSQGGQGFAIPIGQAMAIAGQIRSGGGSPTVHIGPTAFLGLGVVDNNGNGARVQRVVGSAPAASLGISTGDVITAVDGAPINSATAMADALNGHHPGDVISVTWQTKSGGTRTGNVTLAEGPPA
Protein: Toll-interacting protein (Q9H0E2)
Organism: Homo sapiens (Human)
Function: Component of the signaling pathway of IL-1 and Toll-like receptors. Inhibits cell activation by microbial products. Recruits IRAK1 to the IL-1 receptor complex. Inhibits IRAK1 phosphorylation and kinase activity. Connects the ubiquitin pathway to autophagy by functioning as a ubiquitin-ATG8 family adapter and thus mediating autophagic clearance of ubiquitin conjugates. The TOLLIP-dependent selective autophagy pathway plays an important role in clearance of cytotoxic polyQ proteins aggregates. In a complex with TOM1, recruits ubiquitin-conjugated proteins onto early endosomes. Binds to phosphatidylinositol 3-phosphate (PtdIns(3)P).
Subcellular location: Cytoplasm {ECO:0000269|PubMed:31263572}. Endosome {ECO:0000269|PubMed:15047686, ECO:0000269|PubMed:31263572}. Early endosome {ECO:0000269|PubMed:15047686, ECO:0000269|PubMed:26320582}. Note=Localized to endo/exosomal vesicles. {ECO:0000269|PubMed:31263572}.
Interaction partners:
- Interleukin-1 receptor-associated kinase 1
- Myeloid differentiation primary response protein MyD88
- Target of Myb1 membrane trafficking protein
- Toll-like receptor 2
- Toll-like receptor 4
- Interleukin-1 receptor-associated kinase 4
- Interleukin-1 receptor type 1
- TNF receptor-associated factor 6
- TOM1-like protein 2
- Toll/interleukin-1 receptor domain-containing adapter protein
Sequence:
MATTVSTQRGPVYIGELPQDFLRITPTQQQRQVQLDAQAAQQLQYGGAVGTVGRLNITVVQAKLAKNYGMTRMDPYCRLRLGYAVYETPTAHNGAKNPRWNKVIHCTVPPGVDSFYLEIFDERAFSMDDRIAWTHITIPESLRQGKVEDKWYSLSGRQGDDKEGMINLVMSYALLPAAMVMPPQPVVLMPTVYQQGVGYVPITGMPAVCSPGMVPVALPPAAVNAQPRCSEEDLKAIQDMFPNMDQEVIRSVLEAQRGNKDAAINSLLQMGEEP
Protein: HTH-type transcriptional regulator AscG (Cryptic asc operon repressor) (P24242)
Organism: Escherichia coli (strain K12)
Function: Repressor of the asc operon. The cryptic operon is activated by the insertion of IS186 into the ascG gene.
Interaction partners:
- PTS system arbutin-, cellobiose-, and salicin-specific EIIBC component
- 6-phospho-beta-glucosidase AscB
Sequence:
MTTMLEVAKRAGVSKATVSRVLSGNGYVSQETKDRVFQAVEESGYRPNLLARNLSAKSTQTLGLVVTNTLYHGIYFSELLFHAARMAEEKGRQLLLADGKHSAEEERQAIQYLLDLRCDAIMIYPRFLSVDEIDDIIDAHSQPIMVLNRRLRKNSSHSVWCDHKQTSFNAVAELINAGHQEIAFLTGSMDSPTSIERLAGYKDALAQHGIALNEKLIANGKWTPASGAEGVEMLLERGAKFSALVASNDDMAIGAMKALHERGVAVPEQVSVIGFDDIAIAPYTVPALSSVKIPVTEMIQEIIGRLIFMLDGGDFSPPKTFSGKLIRRDSLIAPSR
Protein: Hairy-related 4, tandem duplicate 3 (B0V3D2)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MTPTITGSISSRETLLTNKLRKPMVEKIRRERINSSIEKLKTLLAQEFIKQQPDSRQEKADILEMTLDFLRRSQKSSAAGDGRSRCVQEAVSFLSQCPVQTQSHTRLMKLFLHMQTPADQHTRVDNPQTTETHANSSAKQHTPVRSHIWRPW
Protein: Zinc phosphodiesterase ELAC protein 2 (EC 3.1.26.11) (ElaC homolog protein 2) (Ribonuclease Z 2) (RNase Z 2) (tRNA 3 endonuclease 2) (tRNase Z 2) (Q80Y81)
Organism: Mus musculus (Mouse)
Function: Zinc phosphodiesterase, which displays mitochondrial tRNA 3'-processing endonuclease activity. Involved in tRNA maturation, by removing a 3'-trailer from precursor tRNA. Associates with mitochondrial DNA complexes at the nucleoids to initiate RNA processing and ribosome assembly.
Subcellular location: Mitochondrion {ECO:0000250|UniProtKB:Q9BQ52}. Mitochondrion matrix, mitochondrion nucleoid {ECO:0000250|UniProtKB:Q9BQ52}. Nucleus {ECO:0000250|UniProtKB:Q9BQ52}. Note=Mainly mitochondrial. {ECO:0000250|UniProtKB:Q9BQ52}.
Interaction partners:
- Zinc phosphodiesterase ELAC protein 1
- ATP-dependent RNA helicase SUPV3L1, mitochondrial
- tRNA methyltransferase 10 homolog C
- Endonuclease G, mitochondrial
- Nuclease EXOG, mitochondrial
- RNA cytosine C
- CCA tRNA nucleotidyltransferase 1, mitochondrial
- Periodic tryptophan protein 2 homolog
- Mitochondrial ribonuclease P catalytic subunit
- tRNA
Sequence:
MWALRSLLRPLGLRTMSQGSARRPRPSKDPLRHLRTREKRGPGPGGPNTVYLQVVAAGGRDAGAALYVFSEYNRYLFNCGEGVQRLMQEHKLKVARLDNIFLTRMHWSNVGGLCGMILTLKETGLPKCVLSGPPQLEKYLEAIKIFSGPLKGIELAVRPHSAPEYKDETMTVYQVPIHSERRCGKQQPSQSPRTSPNRLSPKQSSDSGSAENGQCPPEDSSAGANRKAWGRDPSLVVAFVCKLHLRKGNFLVLKAKELGLPVGTAAIAPIIAAVKDGKSITYEGREIAAEELCTPPDPGLVFIVVECPDEGFILPICENDTFKRYQAEADAPVALVVHIAPESVLIDSRYQQWMERFGPDTQHLILNENCPSVHNLRSHKIQTQLSLIHPDIFPQLTSFYSKEEGSTLSVPTVRGECLLKYQLRPKREWQRDTTLDCNTDEFIAEALELPSFQESVEEYRKNVQENPAPAEKRSQYPEIVFLGTGSAIPMKIRNVSSTLVNLSPDKSVLLDCGEGTFGQLCRHYGQQIDRVLCSLTAVFVSHLHADHHTGLLNILLQREHALASLGKPFQPLLVVAPTQLRAWLQQYHNHCQEILHHVSMIPAKCLQKGAEVSNTTLERLISLLLETCDLEEFQTCLVRHCKHAFGCALVHSSGWKVVYSGDTMPCEALVQMGKDATLLIHEATLEDGLEEEAVEKTHSTTSQAINVGMRMNAEFIMLNHFSQRYAKIPLFSPDFNEKVGIAFDHMKVCFGDFPTVPKLIPPLKALFAGDIEEMVERREKRELRLVRAALLTQQADSPEDREPQQKRAHTDEPHSPQSKKESVANTLGARV