wanglab/gogpt-training-data huggingface dataset:
Protein: Free methionine-R-sulfoxide reductase (fRMsr) (EC 1.8.4.14) (GAF domain-containing protein YKL069W) (P36088)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Catalyzes the reversible oxidation-reduction of the R-enantiomer of free methionine sulfoxide to methionine. Does not act on S-enantiomer of free methionine sulfoxide or R-enantiomer of dabsylated methionine sulfoxide. Involved in protection against oxidative stress.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:14562095}. Nucleus {ECO:0000269|PubMed:14562095}.
Interaction partners:
- Peptide methionine sulfoxide reductase
- Peptide methionine sulfoxide reductase 2
- Homocysteine S-methyltransferase 1
- S-adenosylmethionine synthase 2
- 5-methyltetrahydropteroyltriglutamate--homocysteine methyltransferase
- Homocysteine S-methyltransferase 2
- S-adenosylmethionine synthase 1
- Aromatic/aminoadipate aminotransferase 1
- Uncharacterized protein YOL118C
- Uncharacterized protein YDL242W
Sequence:
MGSSTGFHHADHVNYSSNLNKEEILEQLLLSYEGLSDGQVNWVCNLSNASSLIWHAYKSLAVDINWAGFYVTQASEENTLILGPFQGKVACQMIQFGKGVCGTAASTKETQIVPDVNKYPGHIACDGETKSEIVVPIISNDGKTLGVIDIDCLDYEGFDHVDKEFLEKLAKLINKSCVFK
Protein: Ribonucleoside-diphosphate reductase small chain A (EC 1.17.4.1) (Ribonucleoside-diphosphate reductase R2A subunit) (AtRNR2) (Protein R2at) (Ribonucleotide reductase small subunit A) (P50651)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Provides the precursors necessary for DNA synthesis. Catalyzes the biosynthesis of deoxyribonucleotides from the corresponding ribonucleotides.
Subcellular location: Cytoplasm {ECO:0000250}.
Interaction partners:
- Ribonucleoside-diphosphate reductase large subunit
- Guanylate kinase 1
- Guanylate kinase 3, chloroplastic
- Guanylate kinase 2
- Nucleoside diphosphate kinase IV, chloroplastic/mitochondrial
- Nucleoside diphosphate kinase II, chloroplastic
- Nucleoside diphosphate kinase 1
- Nucleoside diphosphate kinase III, chloroplastic/mitochondrial
- Probable UMP-CMP kinase 1
- UMP-CMP kinase 3
Sequence:
MGSLKEGQGRDMEEGESEEPLLMAQNQRFTMFPIRYKSIWEMYKKAEASFWTAEEVDLSTDVQQWEALTDSEKHFISHILAFFAASDGIVLENLAARFLNDVQVPEARAFYGFQIAMENIHSEMYSLLLETFIKDSKEKDRLFNAIETIPCISKKAKWCLDWIQSPMSFAVRLVAFACVEGIFFSGSFCAIFWLKKRGLMPGLTFSNELISRDEGLHCDFACLLYSLLQKQLPLEKVYQIVHEAVEIETEFVCKALPCDLIGMNSNLMSQYIQFVADRLLVTLGCERTYKAENPFDWMEFISLQGKTNFFEKRVGEYQKASVMSNLQNGNQNYEFTTEEDF
Protein: Poly-ADP-ribosylation-amplifying and CtIP-maintaining micropeptide (PAR-amplifying and CtIP-maintaining micropeptide) (P0DW81)
Organism: Homo sapiens (Human)
Function: Micropeptide that acts as a regulator of DNA repair both by preventing KLHL15-mediated ubiquitination and degradation of RBBP8/CtIP, and by promoting the poly-ADP-ribosyltransferase activity of PARP1. Prevents KLHL15-mediated ubiquitination of RBBP8/CtIP by competitively blocking the association between KLHL15 and RBBP8/CtIP. Recruited to DNA damage sites via association with poly-ADP-ribose chains, and enhances the poly-ADP-ribosyltransferase activity of PARP1.
Subcellular location: Nucleus, nucleolus {ECO:0000269|PubMed:35219381}. Chromosome {ECO:0000269|PubMed:35219381}. Note=Recruited to DNA damage sites via interaction with poly-ADP-ribose chains. {ECO:0000269|PubMed:35219381}.
Interaction partners:
Sequence:
MAASGGTKKAQSGGRRLREPSSRPSRRARQRPRRGALRKAGRFL
Protein: Appetite-regulating hormone (Growth hormone secretagogue) (Growth hormone-releasing peptide) (Motilin-related peptide) (Q7T2V1)
Organism: Gallus gallus (Chicken)
Subcellular location: Secreted {ECO:0000256|ARBA:ARBA00004613}.
Interaction partners:
Sequence:
MFLRVILLGILLLSILGTETALAGSSFLSPTYKNIQQQKDTRKPTARLHRRGTESFWDTDETEGEDDNNSVDIKFNVPFEIGVKITEREYQEYGQALEKMLQDILAENAEETRTKS
Protein: YjeF domain-containing protein 1 (H3BPN4)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
XEIDTYERRSGTRSRGIPNERPTRYRHDENILESEPIVYRRIIVPHNVSKEFCTDSGLVVPSISYELHKKLLSVAEKHGLTLERRLEMTGVCASQMALTLLGGPNRLNPKNVHQRPTVALLCGPHVKGAQGISCGRHLANHDVQVILFLPNFVKMLESITNELSLFSKTQGQQVSSLKGEHLGRAGLKASSLLSSLMVSSCHPVATGGKALRV
Protein: Small ribosomal subunit protein uS11B (40S ribosomal protein S14b) (C0HKA1)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MAPRKAKVQKEEVQVQLGPQVRDGEIVFGVAHIYASFNDTFVHVTDLSGRETIARVTGGMKVKADRDEASPYAAMLAAQDVAEKCKTLGITALHIKLRATGGNKTKTPGPGAQSALRALARSSMKIGRIEDVTPIPSDSTRRKGGRRGRRL
Protein: Mitochondrial import inner membrane translocase subunit Tim10 (Q9W2D6)
Organism: Drosophila melanogaster (Fruit fly)
Function: Mitochondrial intermembrane chaperone that participates in the import and insertion of multi-pass transmembrane proteins into the mitochondrial inner membrane. May also be required for the transfer of beta-barrel precursors from the TOM complex to the sorting and assembly machinery (SAM complex) of the outer membrane. Acts as a chaperone-like protein that protects the hydrophobic precursors from aggregation and guide them through the mitochondrial intermembrane space (By similarity).
Subcellular location: Mitochondrion inner membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Intermembrane side {ECO:0000250}.
Interaction partners:
- Mitochondrial import inner membrane translocase subunit Tim9
- Mitochondrial import inner membrane translocase subunit Tim8
- Mitochondrial import inner membrane translocase subunit Tim10B
- Mitochondrial import inner membrane translocase subunit Tim22
- Mitochondrial import inner membrane translocase subunit Tim13
- Mitochondrial import inner membrane translocase subunit
- Mitochondrial import receptor subunit TOM7 homolog
- AT05822p
- GEO12235p1
- RE03721p
Sequence:
MALPQISTADQAKLQLMQEMEIEMMSDLYNRMTNACHKKCIPPRYSESELGKGEMVCIDRCVAKYLDIHEKIGKKLTAMSMQDEELMKKMSS
Protein: Ras-related protein Rab-3B (EC 3.6.5.2) (Q63941)
Organism: Rattus norvegicus (Rat)
Function: Protein transport. Probably involved in vesicular traffic (By similarity).
Subcellular location: Cell membrane {ECO:0000305}; Lipid-anchor {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Golgi apparatus {ECO:0000250|UniProtKB:Q9CZT8}. Note=Colocalizes with GAS8/DRC4 in the Golgi apparatus. {ECO:0000250|UniProtKB:Q9CZT8}.
Interaction partners:
- Polymeric immunoglobulin receptor
- Regulating synaptic membrane exocytosis protein 2
- Symplekin
Sequence:
MASVTDGNTGIRDASDQNFDYMFKLLIIGNSSVGKTSFLFRYADDTFTPAFVSTVGIDFKVKTVYRHEKRVKLQIWDTAGQERYRTITTAYYRGAMGFILMYDITNEESFNAVQDWATQIKTYSWDNAQVILVGNKCDMEEERVIPTEKGRLLAEQLGFDFFEASAKENISVRQAFERLVDAICDKMSDSMDTDPSVLGASKTTRLSDTPPLLQQNCSC
Protein: WD repeat-containing protein 48 (USP1-associated factor 1) (A0A024R2L1)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MAAHHRQNTAGRRKVQVSYVIRDEVEKYNRNGVNALQLDPALNRLFTAGRDSIIRIWSVNQHKQDPYIASMEHHTDWVNDIVLCCNGKTLISASSDTTVKVWNAHKGFCMSTLRTHKDYVKALAYAKDKELVASAGLDRQIFLWDVNTLTALTASNNTVTTSSLSGNKDSIYSLAMNQLGTIIVSGSTEKVLRVWDPRTCAKLMKLKGHTDNVKALLLNRDGTQCLSGSSDGTIRLWSLGQQRCIATYRVHDEGVWALQVNDAFTHVYSGGRDRKIYCTDLRNPDIRVLICEEKAPVLKMELDRSADPPPAIWVATTKSTVNKWTLKGIHNFRASGDYDNDCTNPITPLCTQPDQVIKGGASIIQCHILNDKRHILTKDTNNNVAYWDVLKACKVEDLGKVDFEDEIKKRFKMVYVPNWFSVDLKTGMLTITLDESDCFAAWVSAKDAGFSSPDGSDPKLNLGGLLLQALLEYWPRTHVNPMDEEENEVNHVNGEQENRVQKGNGYFQVPPHTPVIFGEAGGRTLFRLLCRDSGGETESMLLNETVPQWVIDITVDKNMPKFNKIPFYLQPHASSGAKTLKKDRLSASDMLQVRKVMEHVYEKIINLDNESQTTSSSNNEKPGEQEKEEDIAVLAEEKIELLCQDQVLDPNMDLRTVKHFIWKSGGDLTLHYRQKST
Protein: Down syndrome cell adhesion molecule 1, isoform BO (A0A0B4K7T6)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MNMPNERLKWLMLFAAVALIACGSQTLAANPPDADQKGPVFLKEPTNRIDFSNSTGAEIECKASGNPMPEIIWIRSDGTAVGDVPGLRQISSDGKLVFPPFRAEDYRQEVHAQVYACLARNQFGSIISRDVHVRAVVSQFYITEAENEYVIKGNAAVVKCKIPSFVADFVQVEAWVDEEGMELWRNNATDAYDGKYLVLPSGELHIREVGPEDGYKSYQCRTKHRLTGETRLSATKGRLVITEPVGAKAPTFSSDSKGSIFERSIKASFALLCQAQAFPVPIIRWYKFIEGTTRKQAVVLNDRVKQVSGTLIIKDAVVEDSGKYLCVVNNSVGGESVETVLTVTAPLSAKIDPPTQTVDFGRPAVFTCQYTGNPIKTVSWMKDGKAIGHSEPVLRIESVKKEDKGMYQCFVRNDQESAEASAELKLGGRFDPPVIRQAFQEETMEPGPSVFLKCVAGGNPTPEISWELDGKKIANNDRYQVGQYVTVNGDVVSYLNITSVHANDGGLYKCIAKSKVGVAEHSAKLNVYGLPYIRQMEKKAIVAGETLIVTCPVAGYPIDSIVWERDNRALPINRKQKVFPNGTLIIENVERNSDQATYTCVAKNQEGYSARGSLEVQVMVPPKITPFTFGDEPTNVEDSVSVTCLISSGDLPIDIEWLFNDYGISSFSGMTVYRGGKRTSMLTIDNVHARHAGKYSCRARNHASAVNFTTELIVNVPPRWILEPTDKAFAQGSDAKVECKADGFPKPQVTWKKAVGDTPGEYKDLKKSDNIRVEEGTLHVDNIQKTNEGYYLCEAINGIGSGLSAVIMISVQAPPEFTEKLRNQTARRGEPAVLQCEAKGEKPIGILWNMNNMRLDPKNDNRYTIREEILSTGVMSSLSIKRTERSDSALFTCVATNAFGSDDASINMIVQEVPEMPYALKVLDKSGRSVQLSWAQPYDGNSPLDRYIIEFKRSRASWSEIDRVIVPGHTTEAQVQKLSPATTYNIRIVAENAIGTSQSSEAVTIITAEEAPSGKPQNIKVEPVNQTTMRVTWKPPPRTEWNGEILGYYVGYKLSNTNSSYVFETINFITEEGKEHNLELQNLRVYTQYSVVIQAFNKIGAGPLSEEEKQFTAEGTPSQPPSDTACTTLTSQTIRVGWVSPPLESANGVIKTYKVVYAPSDEWYDETKRHYKKTASSDTVLHGLKKYTNYTMQVLATTAGGDGVRSVPIHCQTEPDVPEAPTDVKALVMGNAAILVSWRPPAQPNGIITQYTVYSKAEGAETETKTQKVPHYQMSFEATELEKNKPYEFWVTASTTIGEGQQSKSIVAMPSDQVPAKIASFDDTFTATFKEDAKMPCLAVGAPQPEITWKIKGVEFSANDRMRVLPDGSLLIKSVNRQDAGDYSCHAENSIAKDSITHKLIVLAPPQSPHVTLSATTTDALTVKLKPHEGDTAPLHGYTLHYKPEFGEWETSEVSVDSQKHNIEGLLCGSRYQVYATGFNNIGAGEASDILNTRTKGQKPKLPEKPRFIEVSSNSVSLHFKAWKDGGCPMSHFVVESKKRDQIEWNQISNNVKPDNNYVVLDLEPATWYNLRITAHNSAGFTVAEYDFATLTVTGGTIAPSRDLPELSAEDTIRIILSNLNLVVPVVAALLVIIIAIIVICILRSKGNHHKDDVVYNQTMGPGATLDKRRPDLRDELGYIAPPNRKLPPVPGSNYNTCDRIKRGRGGLRSNHSTWDPRRNPNLYEELKAPPVPMHGNHYGHAHGNAECHYRHPGMEDEICPYATFHLLGFREEMDPTKAMNFQTFPHQNGHAGPVPGHAGTMLPPGHPGHVHSRSGSQSMPRANRYQRKNSQGGQSSIYTPAPEYDDPANCAEEDQYRRYTRVNSQGGSLYSGPGPEYDDPANCAPEEDQYGSQYGGPYGQPYDHYGSRGSMGRRSIGSARNPGNGSPEPPPPPPRNHDMSNSSFNDSKESNEISEAECDRDHGPRGNYGAVKRSPQPKDQRTTEEMRKLIERNETGPKQLQLQQANGAGFTAYDTMAV
Protein: Valine--tRNA ligase, chloroplastic/mitochondrial 2 (EC 6.1.1.9) (Protein EMBRYO DEFECTIVE 2247) (Valyl-tRNA synthetase) (ValRS) (F4KE63)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Plastid, chloroplast {ECO:0000269|PubMed:16251277}. Mitochondrion {ECO:0000269|PubMed:16251277}.
Interaction partners:
- Cysteine--tRNA ligase, chloroplastic/mitochondrial
- Threonine--tRNA ligase, chloroplastic/mitochondrial 2
- Methionine--tRNA ligase, cytoplasmic
- Probable threonine--tRNA ligase, cytoplasmic
- Threonine--tRNA ligase, mitochondrial 1
- Histidine--tRNA ligase, cytoplasmic
- Cysteine--tRNA ligase 2, cytoplasmic
- Cysteine--tRNA ligase 1, cytoplasmic
- Histidine--tRNA ligase, chloroplastic/mitochondrial
- Probable elongation factor 1-gamma 2
Sequence:
MILKTAFSLPTPTTTLLSPSSPHQLNTLFFTRRRRRLISPSRLNSIFSQRRFSFSAAASGNNVFTSPETSKTFDFSSEEKIYKWWESQGYFKPNFDQGGSPFVIPMPPPNVTGSLHMGHAMFVTLEDIMVRYNRMNGRPTLWLPGTDHAGIATQLVVEKMLASEGIKRVDLGRDEFTKRVWEWKEKYGGTITNQIKRLGASCDWSRERFTLDEQLSRAVVEAFVKLHDKGLIYQGSYMVNWSPNLQTAVSDLEVEYSEEPGFLYHIKYRVAGSPDFLTIATTRPETLFGDVALAVHPEDDRYSKYVGQTAIVPMTYGRHVPIIADKYVDKDFGTGVLKISPGHDHNDYLLARKLGLPILNVMNKDATLNDVAGLFCGLDRFEVREKLWADLEEIGLAVKKEPHTLRVPRSQRGGEVIEPLVSKQWFVHMDPLAEKALLAVENKELTIIPERFEKIYNHWLTNIKDWCISRQLWWGHRIPVWYVVGKDCEEDYIVAKSAEEALEKALEKYGKDVEIYQDPDVLDTWFSSSLWPFSTLGWPDVAAKDFNNFYPTNMLETGHDILFFWVARMVMMGIEFTGTVPFSHVYLHGLIRDSQGRKMSKSLGNVIDPLDTIKDFGTDALRFTIALGTAGQDLNLSTERLTANKAFTNKLWNAGKFVLHSLPSLSDTSAWENLLDLKLDKEETLLSLPLPECWAVSKLHILIDSVTASYEKLFFGDVGRETYDFFWSDFADWYIEASKSRLYGSGGNSVSLASQAVLLYVFENILKLLHPFMPFVTEDLWQALPYRKEALIVSPWPQNSLPRNVESIKRFENLQALTRAIRNARAEYSVEPVKRISASVVGSAEVIEYISKEKEVLALLSRLDLNNVHFSNAPPGDANLSVHLVASEGLEAYLPLAAMVDISSEVQRISKRLSKMQTEYDALITRLSSPKFVEKAPEEVVRGVKEQVEELEEKIKLTKARLDFLKSTTSLVSQ
Protein: Lipoprotein lipase (LPL) (EC 3.1.1.34) (Phospholipase A1) (EC 3.1.1.32) (P11152)
Organism: Mus musculus (Mouse)
Function: Key enzyme in triglyceride metabolism. Catalyzes the hydrolysis of triglycerides from circulating chylomicrons and very low density lipoproteins (VLDL), and thereby plays an important role in lipid clearance from the blood stream, lipid utilization and storage. Although it has both phospholipase and triglyceride lipase activities it is primarily a triglyceride lipase with low but detectable phospholipase activity (By similarity). Mediates margination of triglyceride-rich lipoprotein particles in capillaries. Recruited to its site of action on vascular endothelium by binding to GPIHBP1 and cell surface heparan sulfate proteoglycans.
Subcellular location: Cell membrane {ECO:0000269|PubMed:20620994, ECO:0000269|PubMed:24726386, ECO:0000269|PubMed:27811232}; Peripheral membrane protein {ECO:0000269|PubMed:20620994, ECO:0000269|PubMed:24726386, ECO:0000269|PubMed:27811232}; Extracellular side {ECO:0000269|PubMed:20620994, ECO:0000269|PubMed:24726386, ECO:0000269|PubMed:27811232}. Secreted {ECO:0000269|PubMed:17403372, ECO:0000269|PubMed:25066055}. Secreted, extracellular space, extracellular matrix {ECO:0000269|PubMed:27811232}. Note=Newly synthesized LPL binds to cell surface heparan proteoglycans and is then released by heparanase. Subsequently, it becomes attached to heparan proteoglycan on endothelial cells (PubMed:27811232). Locates to the plasma membrane of microvilli of hepatocytes with triglyceride-rich lipoproteins (TRL). Some of the bound LPL is then internalized and located inside non-coated endocytic vesicles (By similarity). {ECO:0000250|UniProtKB:P11151, ECO:0000269|PubMed:27811232}.
Interaction partners:
- Glycosylphosphatidylinositol-anchored high density lipoprotein-binding protein 1
- Apolipoprotein C-II
- Angiopoietin-related protein 4
- Angiopoietin-related protein 3
- Prolow-density lipoprotein receptor-related protein 1
- Patatin-like phospholipase domain-containing protein 2
- Apolipoprotein C-III
- Monoglyceride lipase
- Apolipoprotein E
- Hepatic triacylglycerol lipase
Sequence:
MESKALLLVVLGVWLQSLTAFRGGVAAADAGRDFSDIESKFALRTPEDTAEDTCHLIPGLADSVSNCHFNHSSKTFVVIHGWTVTGMYESWVPKLVAALYKREPDSNVIVVDWLYRAQQHYPVSAGYTKLVGNDVARFINWMEEEFNYPLDNVHLLGYSLGAHAAGVAGSLTNKKVNRITGLDPAGPNFEYAEAPSRLSPDDADFVDVLHTFTRGSPGRSIGIQKPVGHVDIYPNGGTFQPGCNIGEAIRVIAERGLGDVDQLVKCSHERSIHLFIDSLLNEENPSKAYRCNSKEAFEKGLCLSCRKNRCNNLGYEINKVRAKRSSKMYLKTRSQMPYKVFHYQVKIHFSGTEDGKQHNQAFEISLYGTVAESENIPFTLPEVSTNKTYSFLIYTEVDIGELLMMKLKWISDSYFSWPDWWSSPSFVIERIRVKAGETQKKVIFCAREKVSHLQKGKDSAVFVKCHDKSLKKSG
Protein: Cyclin-dependent protein kinase inhibitor SMR1 (Protein LOSS OF GIANT CELLS FROM ORGANS) (Protein SIAMESE-RELATED 1) (Q9LPP4)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Probable cyclin-dependent protein kinase (CDK) inhibitor that functions as a repressor of mitosis in the endoreduplication cell cycle. Cooperates with SIM and SMR2 to promote endoreplication during leaf development. Specifically regulates endoreduplication in epidermal pavement cells to produce the cell size pattern. Is necessary for giant cell formation. Positive regulator of effector-triggered immunity (ETI).
Subcellular location: Nucleus {ECO:0000269|PubMed:17098811}.
Interaction partners:
- Cyclin-dependent protein kinase inhibitor SMR2
- Cyclin-dependent protein kinase inhibitor SMR11
- Protein CPR-5
- Cyclin-dependent kinase B1-1
- Cyclin-dependent protein kinase inhibitor SMR8
- Cyclin-dependent protein kinase inhibitor SMR3
- Transmembrane 9 superfamily member 4
- Transmembrane 9 superfamily member 1
- Cyclin-dependent kinase A-1
- Cyclin-dependent protein kinase inhibitor SMR5
Sequence:
MDLELLQDLSKFNFPTPIKIRSKTSKTKKDEGDDDEDDLRCSTPTSQEHKIPAVVDSPPPPPRKPRPPPSAPSATAALMIRSCKRKLLVSTCEIIMNREEIDRFFSSVYNETSTTAKRRRSYPYCSRR
Protein: DNA-binding protein SMUBP-2 (EC 3.6.4.12) (EC 3.6.4.13) (ATP-dependent helicase IGHMBP2) (Antifreeze enhancer-binding protein ortholog) (AEP) (Q9EQN5)
Organism: Rattus norvegicus (Rat)
Function: 5' to 3' helicase that unwinds RNA and DNA duplexes in an ATP-dependent reaction (By similarity). Specific to 5'-phosphorylated single-stranded guanine-rich sequences (By similarity). May play a role in RNA metabolism, ribosome biogenesis or initiation of translation (By similarity). May play a role in regulation of transcription. Interacts with tRNA-Tyr (By similarity).
Subcellular location: Nucleus {ECO:0000250|UniProtKB:P38935}. Cytoplasm {ECO:0000250|UniProtKB:P38935}. Cell projection, axon {ECO:0000250|UniProtKB:P40694}.
Interaction partners:
- GTP-binding protein
- Phosphatidylinositol 3-kinase regulatory subunit alpha
Sequence:
MASYTVESFVAQQLQLLELERDAEVEERRSWQEHSSLKELQSRGVCLLKLQVSGQRTGLYGQRLVTFEPRKFGPAVVLPSNSFTSGDIVGLYDTNESSQLATGVLTRITQKSVIVAFDESHDFQLNLDRENTYRLLKLANDVTYKRLKKALLTLKKYHSGPASSLIDVLLGGSTPSPATEIPPLTFYNTTLDPSQKEAVSFALAQKEVAIIHGPPGTGKTTTVVEIILQAVKQGLKVLCCAPSNIAVDNLVERLALCKKQILRLGHPARLLESVQQHSLDAVLARSDNAQIVADIRRDIDQVFGKNKKTQDKREKSNFRNEIKLLRKELKEREEAAIVQSLSAADVVLATNTGASTDGPLKLLPEDYFDVVVVDECAQALEASCWIPLLKAPKCILAGDHKQLPPTTVSHKAALAGLSRSLMERLAEKHGAAVVRMLAVQYRMHQAITRWASEAMYHGQLTAHPSVAGHLLKDLPGVADTEETSVPLLLIDTAGCGLLELEEEDSQSKGNPGEVRLVTLHIQALVDAGVQAGDIAVIAPYNLQVDLLRQSLSNKHPELEIKSVDGFQGREKEAVILTFVRSNRKGEVGFLAEDRRINVAVTRARRHVAVICDSHTVNNHAFLKTLVDYFTEHGEVRTAFEYLDDIVPENYTHEGSRSHSCAPKPKCPTTSVRKPASAQESRQEARAATGHSRRKPSEKPLGSQVQPQHSSKANGSDRTGGTDRTEHFRAMIEEFVASKEAQLEFPTSLSSHDRLRVHQLAEEFGLKHDSTGEGKARHITVSRRSPAGSGSATPQPPSPPSPAQAEPEPQVEQPVGQPHGSTQLDLKALHLERLQRQQGCQAQSQLGGGSRPQKAPQKKKKKEPKGPAMALPSEEDFDALVSAVVKADNTCSFTKCSASTTTLGQFCMHCSRRYCLSHHLPEIHGCGEKARAHARQRISREGVLYAGSGTKDRALDPAKRAQLQRKLDKKLGELSSQRTSKKKEKERGT
Protein: Cardiolipin synthase (CMP-forming) (CLS) (EC 2.7.8.41) (O01916)
Organism: Caenorhabditis elegans
Function: Catalyzes the synthesis of cardiolipin (CL) (diphosphatidylglycerol) by specifically transferring a phosphatidyl group from CDP-diacylglycerol to phosphatidylglycerol (PG). CL is a key phospholipid in mitochondrial membranes and plays important roles in maintaining the functional integrity and dynamics of mitochondria under both optimal and stress conditions.
Subcellular location: Mitochondrion inner membrane {ECO:0000250|UniProtKB:Q9UJA2}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Phosphatidate cytidylyltransferase
- Phosphatidylserine decarboxylase proenzyme, mitochondrial
- CDP-diacylglycerol--glycerol-3-phosphate 3-phosphatidyltransferase
- Tafazzin family protein
- CDP-diacylglycerol--inositol 3-phosphatidyltransferase
- Phospholipid/glycerol acyltransferase domain-containing protein
- Phospholipid/glycerol acyltransferase domain-containing protein
- Lysophosphatidylinositol acyltransferase 10
- Phospholipid/glycerol acyltransferase domain-containing protein
- Phosphoserine phosphatase
Sequence:
MIVTSMFRGIACRCELQLLLTPRRMLRNFSSLEQKQSPKIESLPPEERGKYKVATIPNAICTARIAATPLIGYLVVQHNFTPAFVLFTVAGATDLLDGFIARNVPGQKSLLGSVLDPVADKLLISTMFITMTYAGLIPLPLTSVVILRDICLIGGGFYKRYQVMSPPYSLSRFFNPQVSSMQVVPTMMSKINTVLQITLVALSLSSPVFDFSTGANDVIVGLGCITGFTTIYSGLQYASGKAIKKI
Protein: ATP-dependent kinase YFH7 (EC 2.7.1.-) (Altered inheritance of mitochondria protein 12) (P43591)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: ATP-dependent kinase that could be involved in endoplasmic reticulum membrane assembly.
Interaction partners:
- Pantoate--beta-alanine ligase
- mRNA-binding protein PUF3
- Cytidine deaminase
- Large ribosomal subunit protein mL61
Sequence:
MVDTHKLADDVLQLLDNRIEDNYRVCVILVGSPGSGKSTIAEELCQIINEKYHTFLSEHPNVIEVNDRLKPMVNLVDSLKTLQPNKVAEMIENQGLFKDHVEDVNFQPVKYSALTSNNEECTAVVARGGTANAIRIAAVDNPVNVNKLAQDSINIAQIVPMDGFHLSRRCLDLFKDPQTAHKRRGSPSTFDSNNFLQLCKILAKTSLCKVSSHHKFYSTSSVFEKLSKTFSQTIPDIFVPGFNHALKDPTPDQYCISKFTRIVILEGLYLLYDQENWKKIYKTLADTGALLVYKIDIDYEATEERVAKRHLQSGLVTTIAEGREKFRSNDLLNGRDIDNHLIKVDNIVHIRND
Protein: Probable serine/threonine-protein kinase roco6 (EC 2.7.11.1) (Ras of complex proteins and C-terminal of roc 6) (Q54WS5)
Organism: Dictyostelium discoideum (Social amoeba)
Function: May act as a serine/threonine-protein kinase and guanine-nucleotide releasing factor.
Subcellular location: Membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}.
Interaction partners:
- SAP DNA-binding domain-containing protein
- Uncharacterized protein
- Probable serine/threonine-protein kinase qkgA
- Probable serine/threonine-protein kinase roco11
- Uncharacterized protein
- Probable serine/threonine-protein kinase roco8
- Probable serine/threonine-protein kinase roco5
- Tubulin beta chain
- Latrophilin receptor-like protein A
- Tubulin alpha chain
Sequence:
MNSIHKQHYTINSNHYNESININSLLLNDLNDEKRTTSTNNKSNNNSNNNNNETLEDIIEFNNNNCNGDMKYLDLSKRMIYSLELMMIPEIENRFQGDFKSISILNLNDNLLGEIPESLKQLTQLISLSIRGNHILEIPLWFPEEFKLLRKLDVSHNAISSVPNTFNKFSILEDLNLSNNYISYIHPSLFPEGIMRLNLSNNLFREVELPPWFESLLTLDISGNKLKHLGNLPFHLVRVSIDDNHLESIDHKVILRNKDLALKFNQSFSDIVLERIYQCWYTGDPVLDLSGLGMCVVPPILGMLVHLTHLDLSGNCISVLPPELANLTELVRLDLSFNILTTLPLYIVSYKRLEHLDLQGTLDTLVSPPRRIAETGKLIDIQRYFHDLFQGEPSYRVKLMIVGQENVGKTSLVKCLKMKKKFSKNSDHLGTNVSTDGIDIDEIKFNLDIELPSNPSSNSLISNSLSNSSISSNNINSNNNINVHSNGGGINSNGVNSNSQININSSSGNIHSNGGGVGNVNSSGGIHSNNSSGGGGGSNSFLNNTNSNGTNNNSSNLNINTNSNNVNSSGGGNNYHPPVGTNTSMSNIQVIGSSGSNLGSGSNLSIGGSNGNNNNNSGGSGTMVNQRVTMSIWDCAGQELYYTSHQMFLTDSALYVVVWNLCKPEVNSRVEFWLHSIRSKAENAPILLIGTHLDDYLATHSESELDEILENIYSKYFRKFRLKGISILSCSTGVGFDNFLDLLKKTVVELPSLKQSLPELYLKLEKLIIKKRSTLVPPVLTWQSFSQMVLSNLDFHDEIHVKVATKALVPLGSISFFDEPGLDQYVFLDPQWLTGVFSSIITTKHKFIKDGVLKKSDLYQIWKPPHFIEDEGLHSLLINLLERFELMFPLDSDLVSLSSSNGNNGNSYVNNNNNNNNNSNNNNNGSNKSSPFKTTPSSPSTLRLVDSKSKGSHSSNPILSGNNSSSKNSTSTKRSISGSPLRSRSNSDLDLIGGGGGSPINGSSIDYSSKSNTLTPGLFNELNQKFIIPSQLPEIRPSFGLLWPSLDHSRVEFNRWIQLSFAPAGLFSRLLIRLLISKEFDMKPILYWRNGVVVESQSGKSFLSTSTALIEMVPSYANCSSTIKISVRGDRRTGRGLSAKLLRLIVEIADTLCTSWYHLETNQVIPCPHCINKPNCTLFSLSDCEAVASSGVWYLLCGDRKINFETFVPDVAMSDFWGSGSKKFNYDQIKMHKEKRILSIKPASFGNNQIQFEVRVPPSPPPPPVQQIINNGADDNITTTTLAVNNIKVLESGGSQPPSPRSGKDVTHELPIINRLEIIQPTSDESSLIQVEFDHNNQTLVISGTYKYGDLLEIEFESPKLIGRGASGKIYRANLNDTMVAVKQLEVVGEDAPRIFSEFRREIHVMSDLKHSNVVNLLGFTLSPFTMVMEYIDCGDLHKFLHSPIGDQLNGNWALILKLALDIAKGMEFLHSVTPPLLHRDLKSPNVLLSMKDGVYTAKVGDFGLSSRMFIQALKHKLRNFPVGNITWVAPEILREEEYTVKSDVYAFGLILHELLTRKHPYREFNYSMVSLQEDAIKNGLRPTISPSYTQTVTGHEYCGLIQDCWDSDIDRRPTFNKIVKRIKQIIGRDVNNILMVNGVSVVSGIQSPNSLADSQPFHYHQQQQPSLNSTNQLQQQQYSSVLTSPRSNLSDSSNSSQNIANKSLNNISATSLGDLGGNDENLGGQLQYSMRVPQPEAKVNQLVWEVNSRRVWGGCESGEIIVWNAENGNQIFREQKLHPGPIRSLALVNQEDIWSAGGIGPQQSTIRIWNAWRFNLDDQSGTKSDFITKKGRGGSTFGRKSWRLRWFVLSRFDKTLKYYSKQTDKEPSCSLILEGAWLEEISPPGYKVSLHLIHPEKRTMEMEFKSESEKSSWLTAINRVINQNIPLYEIALGKQMTSGSENDYITNLLSVGPNVWVSLKETPSILVYNVKSKELVTKISLNDDQSSDQWGKTGAVNMMLVNNFVWITGGSKLTQIDSQSYQLLEVHGNHYSKPITSMALVEKNVWISCEDESLSVWDGDTGSFIRKVGSPIGSPTKPTVYTKLLYFSGYVWACTQGSIHIYCIHSLTCKKKVESKNHPNSIVDLIKVFQQTVWSCCGTNNVCIWS
Protein: High mobility group protein B1 (Q8I616)
Organism: Plasmodium falciparum (isolate 3D7)
Interaction partners:
- DNA-directed RNA polymerase
- Histone H2A
- rRNA adenine N
Sequence:
MKNTGKEVRKRRKNKKDPHAPKRSLSAYMFFAKEKRAEIISKQPELSKDVATVGKMIGEAWNKLGEKEKAPFEKKAQEDKLRYEKEKAEYANMKMKA