wanglab/gogpt-training-data huggingface dataset:
Protein: Tafazzin (Taz) (EC 2.3.1.-) (Q91WF0)
Organism: Mus musculus (Mouse)
Function: Acyltransferase required to remodel newly synthesized phospholipid cardiolipin (1',3'-bis-[1,2-diacyl-sn-glycero-3-phospho]-glycerol or CL), a key component of the mitochondrial inner membrane, with tissue specific acyl chains necessary for adequate mitochondrial function. Its role in cellular physiology is to improve mitochondrial performance (By similarity). CL is critical for the coassembly of lipids and proteins in mitochondrial membranes, for instance, remodeling of the acyl groups of CL in the mitochondrial inner membrane affects the assembly and stability of respiratory chain complex IV and its supercomplex forms (By similarity). Catalyzes the transacylacion between phospholipids and lysophospholipids, with the highest rate being between phosphatidylcholine (1,2-diacyl-sn-glycero-3-phosphocholine or PC) and CL. Catalyzes both 1-acyl-sn-glycero-3-phosphocholine (lysophosphatidylcholine or LPC) reacylation and PC-CL transacylation, that means, it exchanges acyl groups between CL and PC by a combination of forward and reverse transacylations. Also catalyzes transacylations between other phospholipids such as phosphatidylethanolamine (1,2-diacyl-sn-glycero-3-phosphoethanolamine or PE) and CL, between PC and PE, and between PC and phosphatidate (1,2-diacyl-sn-glycero-3-phosphate or PA), although at lower rate. Not regiospecific, it transfers acyl groups into any of the sn-1 and sn-2 positions of the monolysocardiolipin (MLCL), which is an important prerequisite for uniformity and symmetry in CL acyl distribution. Cannot transacylate dilysocardiolipin (DLCL), thus, the role of MLCL is limited to that of an acyl acceptor. CoA-independent, it can reshuffle molecular species within a single phospholipid class. Redistributes fatty acids between MLCL, CL, and other lipids, which prolongs the half-life of CL. Its action is completely reversible, which allows for cyclic changes, such as fission and fusion or bending and flattening of the membrane. Hence, by contributing to the flexibility of the lipid composition, it plays an important role in the dynamics of mitochondria membranes. Essential for the final stage of spermatogenesis, spermatid individualization (By similarity). Required for the initiation of mitophagy. Required to ensure progression of spermatocytes through meiosis.
Subcellular location: Mitochondrion outer membrane {ECO:0000250|UniProtKB:Q16635}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q16635}; Intermembrane side {ECO:0000250|UniProtKB:Q16635}. Mitochondrion inner membrane {ECO:0000250|UniProtKB:Q16635}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q16635}; Intermembrane side {ECO:0000250|UniProtKB:Q16635}.
Interaction partners:
Sequence:
MPLHVKWPFPAVPRLTWTLASSVVMGLVGTYSCFWTKYMNHLTVHNKEVLYELIENRGPATPLITVSNHQSCMDDPHLWGILKLRHIWNLKLMRWTPAAADICFTKELHSHFFSLGKCVPVCRGDGVYQKGMDFILEKLNHGDWVHIFPEGKVNMSSEFLRFKWGIGRLIAECHLNPIILPLWHVGMNDVLPNSPPYFPRFGQKITVLIGKPFSTLPVLERLRAENKSAVEMRKALTDFIQEEFQRLKMQAEQLHNHFQPGR
Protein: 4Cytl1 protein (Q6P536)
Organism: Mus musculus (Mouse)
Interaction partners:
Sequence:
TLPLLLLLVVVVIAWPLAVQSAPPTCYSRMLTLSREIMADFQSLQASEPEDSCVRYLPRLYLDIHNYCVLAKLRDFVASPQCWKMAEVDTLKDRVRKLYTIMNSFCRRDLVFLSDDCSALEDPIPEATGPPDWQS
Protein: Leucine-rich single-pass membrane protein 2 (Q8N112)
Organism: Homo sapiens (Human)
Subcellular location: Membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}.
Interaction partners:
Sequence:
MPSLAPDCPLLAMPEETQEDSVAPMMPSQRSRGPLAPNHVHEVCLHQVESISDLHSGAGTLRPYLTEEARPWDELLGVLPPSLCAQAGCSPVYRRGGFLLLLALLVLTCLVLALLAVYLSVLQSESLRILAHTLRTQEETLLKLRLASLSQLRRLNSSEAQAPS
Protein: Probable ATP-dependent RNA helicase DDX4 (EC 3.6.4.13) (DEAD box protein 4) (Vasa homolog) (Q9NQI0)
Organism: Homo sapiens (Human)
Function: ATP-dependent RNA helicase required during spermatogenesis. Required to repress transposable elements and preventing their mobilization, which is essential for the germline integrity (By similarity). Acts via the piRNA metabolic process, which mediates the repression of transposable elements during meiosis by forming complexes composed of piRNAs and Piwi proteins and governs the methylation and subsequent repression of transposons (By similarity). Involved in the secondary piRNAs metabolic process, the production of piRNAs in fetal male germ cells through a ping-pong amplification cycle (By similarity). Required for PIWIL2 slicing-triggered piRNA biogenesis: helicase activity enables utilization of one of the slice cleavage fragments generated by PIWIL2 and processing these pre-piRNAs into piRNAs (By similarity).
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:Q61496}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q61496}. Note=Component of the meiotic nuage, also named P granule, a germ-cell-specific organelle required to repress transposon activity during meiosis. {ECO:0000250|UniProtKB:Q61496}.
Interaction partners:
- Piwi-like protein 2
- Tudor domain-containing protein 1
- Protein maelstrom homolog
- Deleted in azoospermia-like
- RNA helicase Mov10l1
- Ran-binding protein 9
- Putative ATP-dependent RNA helicase TDRD12
- Ankyrin repeat, SAM and basic leucine zipper domain-containing protein 1
- Serine/threonine-protein phosphatase PP1-gamma catalytic subunit
- ATP-dependent RNA helicase TDRD9
Sequence:
MGDEDWEAEINPHMSSYVPIFEKDRYSGENGDNFNRTPASSSEMDDGPSRRDHFMKSGFASGRNFGNRDAGECNKRDNTSTMGGFGVGKSFGNRGFSNSRFEDGDSSGFWRESSNDCEDNPTRNRGFSKRGGYRDGNNSEASGPYRRGGRGSFRGCRGGFGLGSPNNDLDPDECMQRTGGLFGSRRPVLSGTGNGDTSQSRSGSGSERGGYKGLNEEVITGSGKNSWKSEAEGGESSDTQGPKVTYIPPPPPEDEDSIFAHYQTGINFDKYDTILVEVSGHDAPPAILTFEEANLCQTLNNNIAKAGYTKLTPVQKYSIPIILAGRDLMACAQTGSGKTAAFLLPILAHMMHDGITASRFKELQEPECIIVAPTRELVNQIYLEARKFSFGTCVRAVVIYGGTQLGHSIRQIVQGCNILCATPGRLMDIIGKEKIGLKQIKYLVLDEADRMLDMGFGPEMKKLISCPGMPSKEQRQTLMFSATFPEEIQRLAAEFLKSNYLFVAVGQVGGACRDVQQTVLQVGQFSKREKLVEILRNIGDERTMVFVETKKKADFIATFLCQEKISTTSIHGDREQREREQALGDFRFGKCPVLVATSVAARGLDIENVQHVINFDLPSTIDEYVHRIGRTGRCGNTGRAISFFDLESDNHLAQPLVKVLTDAQQDVPAWLEEIAFSTYIPGFSGSTRGNVFASVDTRKGKSTLNTAGFSSSQAPNPVDDESWD
Protein: Prolyl endopeptidase (PE) (EC 3.4.21.26) (POase) (Post-proline cleaving enzyme) (Q86AS5)
Organism: Dictyostelium discoideum (Social amoeba)
Function: Cleaves peptide bonds on the C-terminal side of prolyl residues within peptides that are up to approximately 30 amino acids long.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:10329620}.
Interaction partners:
- Multiple inositol polyphosphate phosphatase 1
- Inositol monophosphatase
- Inositol-3-phosphate synthase
Sequence:
MKFNYPETRRDDSVFDIFKSTEKGSVKVYDPYRHLEDQQSPETKKWVDEENKITRSFLDQDNTSEKISNEIMKMLNFERFDWFRRRGSKLFFSRNPNTLNQNIIYLIDIDQISISKDGKSSAKGFENAIEFLNPNTYSKDGTWSLKSFVISKSGDHVCFSYSKAGSDWEEIAVKKIITTNELKTNKDDEEEKEDLKKKNCLHYAVVDLPDSINWCKFTSIKWDENETGFIYNRYPKPEKVSDDDKGTETDTNLNNKVYYHKLGDANESFDRVVFECPENPQWIFGTEFSHDHSSLFISAFRDCNVEHNLYVIRNFQEAIANKSAFKVEALIDNFDACYYYITNTKQGEYFFLTNLSAPFNRLISIQLNDDQPIVPNSKSKLEFKEIIPEKDYVLESVSRSSQEKFYVSYQKHVQDIIEVYDFNGKYLKDIKLPGPGSASLSATEYHDHIFINFSNLVSPSVTYYMDSKNDELLLFKEPHIEGFKSSDYECKQVFYESPKDKTKIPMFIAYKKTTDITSGNAPTYMTGYGGFNISYTQSFSIRNIYFLNKFNGIFVIANIRGGGEYGKAWHEAGSKKNKQNCFDDFIGAAEYLIKENYTNQNKLAVRGGSNGGLLMGAISNQRPDLFKCVVADVGVMDMLRFHLHTIGSNWVSDYGRSDNPDDFDVLIKYSPLNNVPKDSNQYPSIMLCTGDHDDRVIPAHSYKFISELQYQLGKKVDTPLLIRVDKDSGHGAGKGLSKQNNEIADIFNFFSKVLNVKLNF
Protein: Paralemmin-1 (Paralemmin) (Q9Z0P4)
Organism: Mus musculus (Mouse)
Function: Involved in plasma membrane dynamics and cell process formation. Isoform 1 and isoform 2 are necessary for axonal and dendritic filopodia induction, for dendritic spine maturation and synapse formation in a palmitoylation-dependent manner.
Subcellular location: Cell membrane; Lipid-anchor; Cytoplasmic side. Cell projection, filopodium membrane; Lipid-anchor. Cell projection, axon {ECO:0000250}. Cell projection, dendrite {ECO:0000250}. Cell projection, dendritic spine. Basolateral cell membrane {ECO:0000250}; Lipid-anchor {ECO:0000250}. Apicolateral cell membrane {ECO:0000250}; Lipid-anchor {ECO:0000250}. Note=Translocation to the plasma membrane is enhanced upon stimulation of neuronal activity. {ECO:0000250}.
Interaction partners:
- PALM2-AKAP2 fusion protein
Sequence:
MEVLATDTASQQERLQAIAEKRRKQAEIESKRRQLEDDRRQLQYLKSKALRERWLLEGTPSSASEGDEDMRKQMQEDEQKARGLEESITRLEKEIDVLEFGESAPAASKENSAAPSPGRPQSASPAKEEQKSETLVNAQQTPLGTPKENRTSTPVRSPGGSTMMKAAMYSVEITVEKDKVTGETRVLSSTTVLPRDPLPQGVKVYEDETKVVHAVDGIAENGIQPLSSSEVDELIHKADEVTLSEAGSTAGPAEPRGLAEDVTRTTPSRREITGVEAQPGEATSGPPGIQPGQEPPVTMVFMGYQNVEDEAETKKVLGLQDTIKAELVVIEDAATPREPAPLNGSAAELPATKEENQTGPTTTPSDTQDLDMKKPRCRCCSVM
Protein: Large ribosomal subunit protein eL6 (60S ribosomal protein L6) (Q9V9W2)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MAPIEKAKKVAKSAKKGKKHPVNSYLKGGILRYSKAQMYKRRALYRLKDKKSPVVEKAKVPIKKSKASYPTKTFVKKRPSKANFSEHKRNTRRNLTPGTVLILLAGRHQGKRVVLLKVLASGLLLVTGPFALNSCPLRRVSQRYVIGTSSKVDLGAFKVPEHLNDAYFRRLKAKKDKKTGEADIFAAKKERFVPNEQRKKDQKEVDAALLKVIKAHPEGKFFAKYLQNMFALHSSQYPHRMRF
Protein: Sarcospan (K-ras oncogene-associated protein) (Kirsten-ras-associated protein) (Q14714)
Organism: Homo sapiens (Human)
Function: Component of the dystrophin-glycoprotein complex (DGC), a complex that spans the muscle plasma membrane and forms a link between the F-actin cytoskeleton and the extracellular matrix. Preferentially associates with the sarcoglycan subcomplex of the DGC.
Subcellular location: Cell membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Cell membrane, sarcolemma {ECO:0000250}. Postsynaptic cell membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Note=Also found in myotendinous junctions and in the postsynaptic membrane of neuromuscular junctions. {ECO:0000250}.
Interaction partners:
- Dystroglycan 1
- Dystrophin
- Delta-sarcoglycan
- Alpha-sarcoglycan
- Dystrobrevin alpha
- Gamma-sarcoglycan
- Epsilon-sarcoglycan
- Utrophin
- Alpha-1-syntrophin
- Beta-sarcoglycan
Sequence:
MGKNKQPRGQQRQGGPPAADAAGPDDMEPKKGTGAPKECGEEEPRTCCGCRFPLLLALLQLALGIAVTVVGFLMASISSSLLVRDTPFWAGIIVCLVAYLGLFMLCVSYQVDERTCIQFSMKLLYFLLSALGLTVCVLAVAFAAHHYSQLTQFTCETTLDSCQCKLPSSEPLSRTFVYRDVTDCTSVTGTFKLFLLIQMILNLVCGLVCLLACFVMWKHRYQVFYVGVRICSLTASEGPQQKI
Protein: Methanethiol oxidase (Q9XXF9)
Organism: Caenorhabditis elegans
Interaction partners:
- Cysteine synthase 1
- Bifunctional L-3-cyanoalanine synthase/cysteine synthase
- Cysteine synthase
- Cysteine synthase 3
- FAD/NAD
- Sulfide:quinone oxidoreductase, mitochondrial
- Probable calcium-binding mitochondrial carrier F17E5.2
- Probable methionine synthase
- Hcy-binding domain-containing protein
- Adenosylhomocysteinase
Sequence:
MSPNCGLKCHGGPGYASPADAIKGPREEVLFVTAPNAADGPDAIFTVDVNPESDTFCQVISRVDVPHIGDEVHHTGWNACSSCHDKPTEKRSHLIVPCLNSDRIYIINVENERKIYLEHTIEPSKLHSLNLSFPHTSHCLADGNIMISTLGEANGTPSGNFLLLDGKTFEPKGTWPADEKTVPFNYDFWYQPRRNVMISTEWGSPNHIKKGFNPAHVGEGLYGNSVHIFEWDSKKYLQTIDLPQPLGALPLEVRFLHEPTSEHAFVGCALGSGIFRIHPVEENSTTHAATLVAFIPSKKVSGWALPEMPALITDILISMDDRFLYVSCWLHGDIRQYDISDPLKVKLNSQVYIGGSVHTESNVKVLEGEKPIEALYVKGRKIEGGPQMLQLSLDGKRLYVTTSLYKKWDDQFYPEHVKSGATMVQVNIDPESGKMEINRDFLIDFGKIEGGPYLAHEMRYPGGDCTSDIWI
Protein: Saccharolysin (EC 3.4.24.37) (Oligopeptidase YSCD) (Protease D) (Proteinase yscD) (P25375)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Could be involved in late stage of protein degradation.
Subcellular location: Cytoplasm.
Interaction partners:
Sequence:
MRLLLCKNWFASPVISPLLYTRSLYSMANTTSFPIAPQAPPNWSFTPSDISGKTNEIINNSNNFYDSMSKVESPSVSNFVEPFMKFENELGPIINQLTFLQHVSSDKEIRDASVNSSMKLDELNIDLSLRHDIFLQFARVWQDVQSKADSVERETFKYVEKSYKDYIHSGLELDEGNRLKIKEIKKKISVNSINFSKNLGEQKEYITFTKEQLEGVPDSILTQFETIKSDKDSNETLYKVTFKYPDIFPVMKLASSAQTRKQAFLADQNKVPENEAILLDTLKLRDELASLLGYDTYANYNLYDKMAEDSTTVMNFLNDLKDKLIPLGRKELQVLQDMKAEDVKKLNQGADPNYYIWDHRYYDNKYLLENFNVDLEKISEYFPLEATITGMLEIYETLFNLKFIETKDSQNKSVWHDDVKQIAVWNMDDPKSPNFVGWIYFDLHPRDGKYGHAANFGLSSSFMIDDTTRSYPVTALVCNFSKSTKDKPSLLKHNEIVTFFHELGHGIHDLVGQNKESRFNGPGSVPWDFVEAPSQMLEFWTWNKNELINLSSHYKTGEKIPESLINSLIKTKHVNGALFTLRQLHFGLFDMKVHTCKDLQNLSICDTWNQLRQDISLISNGGTLSKGYDSFGHIMSDSYSAGYYGYLWAEVFATDMYHTKFAKDPLNAKNGIQYRDIVLARGGLYDINDNLKEFLGREPSKDAFLKELGLQN
Protein: Protein phosphatase Slingshot homolog 3 (EC 3.1.3.16) (EC 3.1.3.48) (SSH-like protein 3) (SSH-3L) (hSSH-3L) (Q8TE77)
Organism: Homo sapiens (Human)
Function: Protein phosphatase which may play a role in the regulation of actin filament dynamics. Can dephosphorylate and activate the actin binding/depolymerizing factor cofilin, which subsequently binds to actin filaments and stimulates their disassembly (By similarity).
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000250}. Nucleus {ECO:0000250}.
Interaction partners:
- Cofilin-1
- Cofilin-2
- LIM domain kinase 1
- Protein phosphatase Slingshot homolog 1
- Serine/threonine-protein phosphatase 2B catalytic subunit beta isoform
- Protein phosphatase 3 catalytic subunit alpha
- Protein phosphatase Slingshot homolog 2
- Serine/threonine-protein phosphatase 2B catalytic subunit gamma isoform
- Calcineurin subunit B type 1
- Calcineurin subunit B type 2
Sequence:
MALVTVSRSPPGSGASTPVGPWDQAVQRRSRLQRRQSFAVLRGAVLGLQDGGDNDDAAEASSEPTEKAPSEEELHGDQTDFGQGSQSPQKQEEQRQHLHLMVQLLRPQDDIRLAAQLEAPRPPRLRYLLVVSTREGEGLSQDETVLLGVDFPDSSSPSCTLGLVLPLWSDTQVYLDGDGGFSVTSGGQSRIFKPISIQTMWATLQVLHQACEAALGSGLVPGGSALTWASHYQERLNSEQSCLNEWTAMADLESLRPPSAEPGGSSEQEQMEQAIRAELWKVLDVSDLESVTSKEIRQALELRLGLPLQQYRDFIDNQMLLLVAQRDRASRIFPHLYLGSEWNAANLEELQRNRVTHILNMAREIDNFYPERFTYHNVRLWDEESAQLLPHWKETHRFIEAARAQGTHVLVHCKMGVSRSAATVLAYAMKQYECSLEQALRHVQELRPIARPNPGFLRQLQIYQGILTASRQSHVWEQKVGGVSPEEHPAPEVSTPFPPLPPEPEGGGEEKVVGMEESQAAPKEEPGPRPRINLRGVMRSISLLEPSLELESTSETSDMPEVFSSHESSHEEPLQPFPQLARTKGGQQVDRGPQPALKSRQSVVTLQGSAVVANRTQAFQEQEQGQGQGQGEPCISSTPRFRKVVRQASVHDSGEEGEA
Protein: Glutamyl-tRNA(Gln) amidotransferase subunit B, mitochondrial (Glu-AdT subunit B) (EC 6.3.5.-) (Q9UT77)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Allows the formation of correctly charged Gln-tRNA(Gln) through the transamidation of misacylated Glu-tRNA(Gln) in the mitochondria. The reaction takes place in the presence of glutamine and ATP through an activated gamma-phospho-Glu-tRNA(Gln).
Subcellular location: Mitochondrion {ECO:0000255|HAMAP-Rule:MF_03147, ECO:0000269|PubMed:16823372}.
Interaction partners:
- Glutamyl-tRNA
- Aspartate--tRNA ligase, mitochondrial
- Probable asparagine--tRNA ligase, cytoplasmic
- Asparagine--tRNA ligase, mitochondrial
- Aspartate--tRNA ligase, cytoplasmic
- Probable glutamine--tRNA ligase
- Putative amidase C869.01
- Putative polysaccharide deacetylase
- Restriction of telomere capping protein 5
- Putative amidase C550.07
Sequence:
MSFGRWAASIGLEIHLQLATVKKLFSPAKVNPLAQPNTCVAYFDVSLPGSMPILNPEALKFAVKGALALNCEVANVCKFDRKHYFYPDLPAGYQITQKEIPIGRNGFIPLSAGLDNVPDTQIPIQHIQLEQDTAKSTSAKNPSRILLDYNRAGTPLLEIVTKPCFHDVNTVSAFLFKLQSIVRFAGISEALMENGGMRCDVNVSIAPVISSENLNELHFKNNGVISVEKSISHFPQLGTQLARVELKNLSNVRNVVNSIRHEVDRQVSLANMGVSWPSETRGFDDITGKTFPLRNKTTSDDYLFLPETDIPPIILSRSYVNSVLKSLPALPDELFQKLTTGSHAISHKEARTLLSVKEYYHYYRNAYHHIDSISHVNQSLKEDALRTLPYWITVELVGKVREIDPSPNINIVPPLQLADIVLLVSKKKLTAASAKLFLRSLIKSPSSKPISTLIQEKNFGTIGDSEKIKACVESVLSKHSKQFEELKNGKTSLIKWFVGLTMRELRGQASPKDIEMEVQSSLRREK
Protein: Interferon-induced GTP-binding protein Mx1 (RBTMx1) (Interferon-inducible Mx protein 1) (Q91192)
Organism: Oncorhynchus mykiss (Rainbow trout) (Salmo gairdneri)
Function: Does not inhibit strain RB-1 of the fish pathogen, infectious hematopoietic necrosis virus (IHNV).
Subcellular location: Cytoplasm {ECO:0000269|PubMed:9188599}. Note=Exhibits cytoplasmic staining in a large globular pattern surrounding the nucleus.
Interaction partners:
Sequence:
MNNTLNQHYEEKVRPCIDLIDSLRSLGVEKDLALPAIAVIGDQSSGKSSVLEALSGVALPRGSGIVTRCPLELKMKRKKEGEEWHGKISYQDHEEEIEDPSDVEKKIREAQDEMAGVGVGISDDLISLEIGSPDVPDLTLIDLPGIARVAVKGQPENIGEQIKRLIRKFIMKQETISLVVVPCNVDIATTEALKMAQEVDPEGERTLGILTKPDLVDKGTEETVVDIVHNEVIHLTKGYMIVKCRGQKEIMERVSLTEATEREKAFFKEHAHLSTLYDEGHATIPKLAEKLTLELVHHIEKSLPRLEEQIEAKLSETHAELERYGTGPPEDSAERLYFLIDKVTAFTQDAINLSTGEEMKSGVRLNVFSTLRKEFGKWKLHLERSGEIFNQRIEGEVDDYEKTYRGRELPGFINYKTFEVMVKDQIKQLEGPAVKKLKEISDAVRKVFLLLAQSSFTGFPNLLKSAKTKIEAIKQVNESTAESMLRTQFKMELIVYTQDSTYSHSLCERKREEDEDQPLTEIRSTIFSTDNHATLQEMMLHLKSYYWISSQRLADQIPMVIRYLVLQEFASQLQREMLQTLQEKDNIEQLLKEDIDIGSKRAALQSKLKRLMKARSYLVEF
Protein: tRNA N(3)-methylcytidine methyltransferase (EC 2.1.1.-) (Q38DL9)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MPDKIENNTRKRPRELPFVEDYRPYTGGQLAQLKVRKTTHKEHWDQYYRNNTLNGYRDRHYILREFSELREALERLKKNNEATLEECVWMEAGCGVGNAVFPILKDYGDVSGWRVVGFDISTVAIKLLREKQNTLPHVEQEKFTAWVLNPVEQDIAPIITASVARQSRPRGDGLVDFVSMIFVLCSIPVEEHAVVLRRIAACMKEGGVFFFRDYCVDDHAEKRFSAHCRVEANTFSRTNGTLSHFFSVSELRDLFCSVGFELINVEVVEREVVNRREGMNLQRRFLQGRFRKIRRIGDNGIDIAGNGNLSRNMPQK
Protein: Peroxin-7 (Q5BF00)
Organism: Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Subcellular location: Cytoplasm, cytosol {ECO:0000256|ARBA:ARBA00004514}. Peroxisome matrix {ECO:0000256|ARBA:ARBA00004253}.
Interaction partners:
- Peroxisomal targeting signal receptor
- Peroxisomal membrane protein PEX14
- Peroxisomal membrane protein PEX13
- Peroxisomal membrane protein PEX14
- RING-type E3 ubiquitin transferase
- Peroxisome assembly protein 12
- acetyl-CoA C-acyltransferase
- 3-ketoacyl-CoA ketothiolase
- acetyl-CoA C-acyltransferase
- acetyl-CoA C-acyltransferase
Sequence:
MLHFRTEGYQGYAVKYSPFFDNRLAVASSANFGLVGNGRLYILELTPNGIVPAKWFTTQDALYDLAWSEANEHQVLTATGDGSIKLFDSTLNDFPIQNWKEHNREVFSVSWNLVAKDTFCSSSWDGTVRIWSPQRPHSLVTLPTHSCTYSASFSPHSPDILSCVSSDSYLRVYDLRTPASASNHLTLQIPIHAAPASPIPGNPGAPPAACPPSEALTHDWNKYRPSVVAVAGVDRTIRTFDIRAPQQGPQAIMIGHDYAVRRVAWSPHLSNVLLSASYDMTCRAWSDQSPPGVVGDTDLMRSGPSPVMGAELGRMNRHTEFVTGVDWCLFGSEGWCASVGWDESVYVWDVRAVMG
Protein: Putative zinc finger protein F44E2.7 (P34437)
Organism: Caenorhabditis elegans
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
Sequence:
MVKPTSSLLQRYKNNVRVDPSTLNHYLCYYCGKTLSDRLEYQQHMLKVHEVMSQSYQLWSDHTMDTLGLIWSESKRSYDRDTSCSLSVPASPMSRESRNRNSDDDYYDYVYEDEKPKRRRIDVEQSRRSVAAAAEKHRKLLEEQRRKAEAEYERKRKADEKKKEKAIKDEEKRKAEDLRKCLQLQQQKTAAAAQIRETAEKAAVARRMSTFEVGESSEQLAKPEGEKRKRRRTESRWREIESDSDKPEVTALVKKILEESKKKEASSQEVEDADLVPELSTRKPYDNTEHVSKLCKVCKKGPHYTFANLFEHYQDLHNATIKSLHYYGFNGNKLIGKKNLIERDHCQRCVIKFPRARDYFAHMIKHHVYESVRCQLDFENATNADVEARMMFRDRILTLGYNFKFEQVADPNLVSDVLEPGQEPSTSAEQEDPSSLKIVKLEEPELEEQKALKPESEAMEQQEDVHSLNPE
Protein: Trypanin (T lymphocyte-triggering factor) (TLTF) (O15697)
Organism: Trypanosoma brucei rhodesiense
Function: Cytoskeletal linker that plays a central role in the flagellum cell motility. Required for directional cell motility. Plays a role as part of a dynein regulatory system that regulates flagellar beat in response to signals from the central pair apparatus and radial spokes in procyclic cells. Also plays an essential role in the bloodstream form of the trypanosomes as its silencing is lethal for the circulating form.
Subcellular location: Cytoplasm. Cytoplasm, cytoskeleton. Cell projection, cilium, flagellum. Note=Associated with the cytoskeleton. Localized to the site of attachment of the flagellum to the subpellicular cytoskeleton. Also localized in the flagellum of the bloodstream form trypanosomes.
Interaction partners:
Sequence:
MPPRTAAERGGRRKSVKAPPPVDPLVELTTLESVHDALAKAERLRNYFQVERDKVNDFWTITKGEVETYRNRLFNAEASIEELERSHQVEMKVYKQRVRHLIYERKKKAQACQDESDRLLREAEDRHLQRMNEIQAKLQQQDQQLRAAAADHEMNVYEKRDSHSYMVTVTKTQSHEKELARLQVSCEAKLKVLRDELELRRRAEIHEIEERKNEHINALIKQHEEKFHEMKTYYNQITTNNLEIIHSLKEEIAQMKQNDEHNETLMYDIDRENQNLVAPLEEAQREVAELQQKRKQNEQNKRGLEVTRVKLRSLREEIRRQREEHQALEERYACVHREREELKGKFESALRQAVMVVEERNEVLQQKLIESHALVEERDVQLEGVLRAMNLEPKTLELIATEVDEWLQRKNQLIKDLHFELKKGEKLYSATLLEMERRCQTANIASLPRSNFE
Protein: U2 splicing auxiliary factor, putative (Q38BS6)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- RNA-binding protein, putative
- RNA-binding protein, putative
- Splicing factor TSR1
- U1 small nuclear ribonucleoprotein, putative
- Pre-mRNA splicing factor, putative
- Pre-mRNA-splicing factor SLU7
- RNA-binding protein, putative
- RNA-binding protein RBP14, putative
- RNA-binding protein, putative
- Nuclear cap-binding protein subunit 2
Sequence:
MYQDRCIFFSKMGACRHGDGCTKVHVRPTTSPTVLFPFMYPNPAAIEHIQDREWNFHFERKYLRRHFEHFYKETWRTFMELGRIAELRVVSNLGDHLLGNVYIRFEDSHDASRIVRELKAKKLNDIVLLPELSPVTNFAEACCKEDLEGKCERGPQCNYLHIMKVSRKLMEKLEKEQAKFWKKKEKHSSSSSSSRKRERSKERGGERSKERSKERGRDRQKSPRGYSSDMCHICGKSGHISRECPLK
Protein: Inner membrane transport protein YdiM (P76197)
Organism: Escherichia coli (strain K12)
Subcellular location: Cell inner membrane; Multi-pass membrane protein.
Interaction partners:
- Quinate/shikimate dehydrogenase
- 3-dehydroquinate dehydratase
- Uncharacterized protein YdiL
- Uncharacterized protein YehI
Sequence:
MKNPYFPTALGLYFNYLVHGMGVLLMSLNMASLETLWQTNAAGVSIVISSLGIGRLSVLLFAGLLSDRFGRRPFIMLGMCCYMAFFFGILQTNNIIIAYVFGFLAGMANSFLDAGTYPSLMEAFPRSPGTANILIKAFVSSGQFLLPLIISLLVWAELWFGWSFMIAAGIMFINALFLYRCTFPPHPGRRLPVIKKTTSSTEHRCSIIDLASYTLYGYISMATFYLVSQWLAQYGQFVAGMSYTMSIKLLSIYTVGSLLCVFITAPLIRNTVRPTTLLMLYTFISFIALFTVCLHPTFYVVIIFAFVIGFTSAGGVVQIGLTLMAERFPYAKGKATGIYYSAGSIATFTIPLITAHLSQRSIADIMWFDTAIAAIGFLLALFIGLRSRKKTRHHSLKENVAPGG
Protein: asparagine--tRNA ligase (EC 6.1.1.22) (O96198)
Organism: Plasmodium falciparum (isolate 3D7)
Interaction partners:
- asparagine--tRNA ligase
- Glutamyl-tRNA
- Glutamyl-tRNA
- Proline--tRNA ligase, putative
- Proline--tRNA ligase
- Isoleucine--tRNA ligase, putative
- isoleucine--tRNA ligase
- leucine--tRNA ligase
- leucine--tRNA ligase
- tRNA import protein tRIP
Sequence:
MCEKDDITVNEEILQKAQEFQVENEKDIKMKKLKPITEGLLKPEVDLLQISERGSRGRVKICNVLNVPRSEKEYNNNNSDKVENKYIGKIITVCGWSKAIRKQGGGRFCFVNLNDGSCHLNLQIVVNQCIENYEKLLKCGAGCCFRFTGELIISPVQNDNNKKGLLKENVELALNNNDIHNFEIYGENLDPQKYPLSKKNHGKEFLREVAHLRPRSYFISSVIRIRNSLSIATHLFFQSRGFLYIHTPLITTSDCEGGGEMFTVTTLLNENGDIRSIPRINLKNKKKEKREDILNEKNGKKDHMNDSLNNNTCNNNNNNGNSSSSNIVSSPQYEDNYLIDYKKDFFSKQAFLTVSGQLSLENLCSSMGDVYTFGPTFRAENSHTSRHLAEFWMIEPEIAFADLYDNMELAEAYIKYCIDYVLNNNFHDIYYFEENVETNLIKRLKNILNEDFAKITYTNAIEILQNYSDSFEVKVEWGMDLQSEHERFIAEKIFKKPVIVYNYPKDLKAFYMKLNEDNKTVAAMDVLVPKIGEVIGGSQREDNLERLDKMIKEKKLNIDSYWWYRQLRQYGSHPHAGFGLGFERLIMLVTGVDNIKDTIPFPRYPGHAEF
Protein: Cytochrome c oxidase subunit 4 isoform 2, mitochondrial (Cytochrome c oxidase subunit IV isoform 2) (COX IV-2) (Q91Y94)
Organism: Rattus norvegicus (Rat)
Function: Component of the cytochrome c oxidase, the last enzyme in the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII) and cytochrome c oxidase (complex IV, CIV), that cooperate to transfer electrons derived from NADH and succinate to molecular oxygen, creating an electrochemical gradient over the inner membrane that drives transmembrane transport and the ATP synthase. Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Electrons originating from reduced cytochrome c in the intermembrane space (IMS) are transferred via the dinuclear copper A center (CU(A)) of subunit 2 and heme A of subunit 1 to the active site in subunit 1, a binuclear center (BNC) formed by heme A3 and copper B (CU(B)). The BNC reduces molecular oxygen to 2 water molecules using 4 electrons from cytochrome c in the IMS and 4 protons from the mitochondrial matrix.
Subcellular location: Mitochondrion inner membrane {ECO:0000250|UniProtKB:P00423}; Single-pass membrane protein {ECO:0000250|UniProtKB:P00423}.
Interaction partners:
- Cytochrome c oxidase subunit 5A, mitochondrial
- Cytochrome c oxidase subunit 7C, mitochondrial
- Cytochrome c1, heme protein, mitochondrial
- Cytochrome c oxidase subunit 6A2, mitochondrial
- Cytochrome b-c1 complex subunit 8
- Cytochrome b-c1 complex subunit Rieske, mitochondrial
- Cytochrome b-c1 complex subunit 2, mitochondrial
- Cytochrome b-c1 complex subunit 6, mitochondrial
- Cytochrome c oxidase subunit 6A1, mitochondrial
- Cytochrome c oxidase subunit 5B, mitochondrial
Sequence:
MFSRATRSLVMKTGGLRTQGTHSPGSAASSSQRRMTPYVDCYAQRSYPMPDEPYCTELSEEQRALKEKEKGSWAQLSQAEKVALYRLQFHETFAEMNHRSNEWKTVMGCVFFFIGFTALVIWWQRVYVFPKKVVTLTEERKAQQLQRLLDMKSNPIQGLSAHWDYEKKEWKK