wanglab/gogpt-training-data huggingface dataset:
Protein: Malic enzyme (A0A1W2PQH3)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MAFTLQERQMLGLQGLLPPKIETQDIQALRFHRNLKKMTSPLEKYIYIMGIQERNEKLFYRILQDDIESLMPIVYTPTVGLACSQYGHIFRRPKGLFISISDRGHVRSIVDNWPENHVKAVVVTDGERILGLGDLGVYGMGIPVGKLCLYTACAGIRPDRCLPVCIDVGTDNIALLKDPFYMGLYQKRDRTQQYDDLIDEFMKAITDRYGRNTLIQFEDFGNHNAFRFLRKYREKYCTFNDDIQGTAAVALAGLLAAQKVISKPISEHKILFLGAGEAALGIANLIVMSMVENGLSEQEAQKKIWMFDKYGLLVKGRKAKIDSYQEPFTHSAPESIPDTFEDAVNILKPSTIIGVAGAGRLFTPDVIRAMASINERPVIFALSNPTAQAECTAEEAYTLTEGRCLFASGSPFGPVKLTDGRVFTPGQGNNVYIFPGVALAVILCNTRHISDSVFLEAAKALTSQLTDEELAQGRLYPPLANIQEVSINIAIKVTEYLYANKMAFRYPEPEDKAKYVKERTWRSEYDSLLPDVYEWPESASSPPVITE
Protein: Putative meiotic phospholipase SPO1 (EC 3.1.1.-) (Sporulation-specific protein 1) (P53541)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Regulates spindle pole duplication in meiosis I, but not in mitosis. Required for meiosis I, meiosis II chromosome segregation and spore formation. Binds phosphatidylinositol (4)P mono- and polyphosphates.
Subcellular location: Endoplasmic reticulum membrane; Single-pass membrane protein. Nucleus membrane; Single-pass membrane protein.
Interaction partners:
- Prospore membrane adapter protein SPO71
- Sporulation protein 23
- Sporulation-specific protein 73
Sequence:
MQKLLFVFSVLLTVVLATAPFQVQCPSSPLIREAKHELCPEETLYLKKKKIKTKNKLIQFLKSLTEAKFSSKFYKRVLKDPPKIGIAISGGGYRSMLVGTGFISQMNDYGLFEYSDYIAGLSGGSWILMDLVVQNFEVKSLLQEWDLEEDLLLGIPEFDISEEEIVTNAKKEYNDNDLKMKKRQGGSLITSSSNFYEQIEEIMNSIEEIPEDYMITKRNLNPLARLKKIFFPNNTFTGTDAKIETFKKVLDFYKSLHLKIKPKKMEGFQISFTDYWGKAIVQRLKKNFDDDPNHSFSFSKLVNSSKKFKECSVPIPIFVANCKNGLLSNVIFEFTPFEFGSWENILRLFVKLPYLGSKIVSGKAEKCINNFDDLGFITATSSSIFNNVLIFIWNLASQSSREAMKALNMVMGIFGLGKEEIFSISKDSSRLETDYAVYQPNPFYLYPEKDNVLTNKNHLYLVDGGEDGENIPLRTLVIPERELDVIFVLDSSSDIDNYPNGSKLKRIFEKLDEENVHYQFPNNVKTFTHPIVIGCNATKRTGHDSFLPIIIYHANANHGNASNTSTFKITYNQSEVSSMLPTGRGVFSNDYDLYYKNCLGCILTKRTMDRLPRKKKFSPFCLQCFKDYCYS
Protein: Nicotinamide riboside kinase 2 (NRK 2) (NmR-K 2) (EC 2.7.1.22) (Integrin beta-1-binding protein 3) (Muscle integrin-binding protein) (MIBP) (Nicotinic acid riboside kinase 2) (EC 2.7.1.173) (Ribosylnicotinamide kinase 2) (RNK 2) (Ribosylnicotinic acid kinase 2) (Q9NPI5)
Organism: Homo sapiens (Human)
Function: Catalyzes the phosphorylation of nicotinamide riboside (NR) and nicotinic acid riboside (NaR) to form nicotinamide mononucleotide (NMN) and nicotinic acid mononucleotide (NaMN). Reduces laminin matrix deposition and cell adhesion to laminin, but not to fibronectin. Involved in the regulation of PXN at the protein level and of PXN tyrosine phosphorylation. May play a role in the regulation of terminal myogenesis.
Interaction partners:
- Nicotinate phosphoribosyltransferase
- Nicotinamide/nicotinic acid mononucleotide adenylyltransferase 1
- Nicotinate-nucleotide pyrophosphorylase [carboxylating]
- Nicotinamide/nicotinic acid mononucleotide adenylyltransferase 2
- Nicotinamide phosphoribosyltransferase
- Purine nucleoside phosphorylase
- Nicotinamide riboside kinase 1
- NAD-capped RNA hydrolase NUDT12
- Ectonucleotide pyrophosphatase/phosphodiesterase family member 1
- Ectonucleotide pyrophosphatase/phosphodiesterase family member 3
Sequence:
MKLIVGIGGMTNGGKTTLTNSLLRALPNCCVIHQDDFFKPQDQIAVGEDGFKQWDVLESLDMEAMLDTVQAWLSSPQKFARAHGVSVQPEASDTHILLLEGFLLYSYKPLVDLYSRRYFLTVPYEECKWRRSTRNYTVPDPPGLFDGHVWPMYQKYRQEMEANGVEVVYLDGMKSREELFREVLEDIQNSLLNRSQESAPSPARPARTQGPGRGCGHRTARPAASQQDSM
Protein: UPF0652 protein C22H10.08 (Q10301)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus {ECO:0000269|PubMed:16823372}.
Interaction partners:
Sequence:
MDAEALRNLYLSSILPNESKTGNESPEKKFSSPVLLQRAKVIPLRLEYEERKLLHLLTAALDVSDYTDSVDTLSFSSPAKRLAQQLKGITAVLSGIMVAYDYKVGQELLEHKNFEQHAEFFKKIFEIGRRYKVLNPNRLGSTYGKLMYFVQDSMRPEIQDALGFNLFKPILTVYEFLNERDALNALEDPYAEIATMEIVAENRSRSAIQKDIKAKERAVEHIAKKYYSSKITKEKVRWCLYSIADSNSYLRYNRDPIAKLIGLVEAYFSPDTVDDEFTLAIDAINGSRLKHSHYKQYHYVVQSLHLWLLIMGEIFSLWALSDLELTNPDMEYKLIDNNQGIHRMQPCPNIRIAMERILRTAQEQSETWIGSSTIHLGDTAVPNALLFIDKYMQVPRILTPLVLLFKELDSLNDHSLLNYIDTAFGGREYLKKTILTDFMRFGFDGSGADNWFDAGSCIDGRLTSAWNWANNIHTKDYYRVLLMSGFLSFNGE
Protein: Oligogalacturonate-specific porin KdgM (Q934G3)
Organism: Dickeya dadantii (strain 3937) (Erwinia chrysanthemi (strain 3937))
Function: Porin specific for oligogalacturonides. Also required for full virulence.
Subcellular location: Cell outer membrane.
Interaction partners:
- LPS-assembly lipoprotein LptE
Sequence:
MKIKLLTLAVASLVSVNALAVSIDYRHEMQDTAQAGHKDRLLISHRFANGFGLSSEVKWAQSSADKTPNKPFNEQVSNGTEVVASYVYKFNSVFSIEPGFSLESGSSNNNYRPYLRGRANVTDDLSVALRYRPYFKRNSGNIGKDNTMDKGYTLTGNIDYTFLKDYTIGYELEYKKGTSGKTILSDNDDYDITHNVKLSYKWDKNWKPYVEVGNVSGSETTDERQTRYRVGVQYSF
Protein: Phosphatidylinositol 3-kinase catalytic subunit type 3 (PI3-kinase type 3) (PI3K type 3) (PtdIns-3-kinase type 3) (EC 2.7.1.137) (Phosphatidylinositol 3-kinase p100 subunit) (Phosphoinositide-3-kinase class 3) (hVps34) (Q8NEB9)
Organism: Homo sapiens (Human)
Function: Catalytic subunit of the PI3K complex that mediates formation of phosphatidylinositol 3-phosphate; different complex forms are believed to play a role in multiple membrane trafficking pathways: PI3KC3-C1 is involved in initiation of autophagosomes and PI3KC3-C2 in maturation of autophagosomes and endocytosis. As part of PI3KC3-C1, promotes endoplasmic reticulum membrane curvature formation prior to vesicle budding. Involved in regulation of degradative endocytic trafficking and required for the abcission step in cytokinesis, probably in the context of PI3KC3-C2. Involved in the transport of lysosomal enzyme precursors to lysosomes (By similarity). Required for transport from early to late endosomes (By similarity).
Subcellular location: Midbody {ECO:0000269|PubMed:20208530}. Late endosome {ECO:0000269|PubMed:14617358}. Cytoplasmic vesicle, autophagosome {ECO:0000305|PubMed:14617358}. Note=As component of the PI3K complex I localized to pre-autophagosome structures. As component of the PI3K complex II localized predominantly to endosomes (PubMed:14617358). Also localizes to discrete punctae along the ciliary axoneme and to the base of the ciliary axoneme (By similarity). {ECO:0000250|UniProtKB:Q6PF93, ECO:0000305|PubMed:14617358}.
Interaction partners:
- Beclin-1
- Serine/threonine-protein kinase ULK1
- Ras-related protein Rab-5A
- Beclin-2
- UV radiation resistance-associated gene protein
- Beclin 1-associated autophagy-related key regulator
- Nuclear receptor-binding factor 2
- Activating molecule in BECN1-regulated autophagy protein 1
- Phosphoinositide 3-kinase regulatory subunit 4
- Serine/threonine-protein kinase ULK2
Sequence:
MGEAEKFHYIYSCDLDINVQLKIGSLEGKREQKSYKAVLEDPMLKFSGLYQETCSDLYVTCQVFAEGKPLALPVRTSYKAFSTRWNWNEWLKLPVKYPDLPRNAQVALTIWDVYGPGKAVPVGGTTVSLFGKYGMFRQGMHDLKVWPNVEADGSEPTKTPGRTSSTLSEDQMSRLAKLTKAHRQGHMVKVDWLDRLTFREIEMINESEKRSSNFMYLMVEFRCVKCDDKEYGIVYYEKDGDESSPILTSFELVKVPDPQMSMENLVESKHHKLARSLRSGPSDHDLKPNAATRDQLNIIVSYPPTKQLTYEEQDLVWKFRYYLTNQEKALTKFLKCVNWDLPQEAKQALELLGKWKPMDVEDSLELLSSHYTNPTVRRYAVARLRQADDEDLLMYLLQLVQALKYENFDDIKNGLEPTKKDSQSSVSENVSNSGINSAEIDSSQIITSPLPSVSSPPPASKTKEVPDGENLEQDLCTFLISRACKNSTLANYLYWYVIVECEDQDTQQRDPKTHEMYLNVMRRFSQALLKGDKSVRVMRSLLAAQQTFVDRLVHLMKAVQRESGNRKKKNERLQALLGDNEKMNLSDVELIPLPLEPQVKIRGIIPETATLFKSALMPAQLFFKTEDGGKYPVIFKHGDDLRQDQLILQIISLMDKLLRKENLDLKLTPYKVLATSTKHGFMQFIQSVPVAEVLDTEGSIQNFFRKYAPSENGPNGISAEVMDTYVKSCAGYCVITYILGVGDRHLDNLLLTKTGKLFHIDFGYILGRDPKPLPPPMKLNKEMVEGMGGTQSEQYQEFRKQCYTAFLHLRRYSNLILNLFSLMVDANIPDIALEPDKTVKKVQDKFRLDLSDEEAVHYMQSLIDESVHALFAAVVEQIHKFAQYWRK
Protein: RNA-editing complex protein MP42 (D6XMN0)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- MP18 RNA editing complex protein
- Protein farnesyltransferase subunit beta
- Peroxin 19
- Nucleoside diphosphate kinase-like domain-containing protein
Sequence:
MKRVTSHISRFLPLVLSQRGLSTYASPHVSSMRYYGATKCLLASTPDTPSFQCGECGKAFRLINALNHHIMTKHAGKAKAMMNKGGKLEEVNPEEIKNKPQGAMSQPTSPPPSSSTSGTEAASTSPTHSSFPGIPFSPVGGIGLVGTPVGAASHVVNTTTTAANSASGNALSDENADKKTFVCTICQKTFRLEAALQHHYQAKHNMEMPTSSSSSGGASAQPVLQGGATTAGVGSVGFSHTEEETGRSAMGTQYVHSQETILPQAPQYHLDVAPNAPEEGEVAAHWRCVNHCVMLGVVQNIQEGFVFEDKVLQFTLITDFEGPSPGDPDKDFHTVRVFDSDYSSRVKEQLRDGEWFLVTGRLRMVPQYDGSMRKYYHYPVIQVHPGCGSVLKV
Protein: Uncharacterized protein (Q54H50)
Organism: Dictyostelium discoideum (Social amoeba)
Interaction partners:
Sequence:
MNEKNFEVLFWKVIHNKFLFKLIFFHIESFEQQYDNFKQYHLENKKKFKEIYSLDWMIEQKQYQLLKCKLLANEYIRIDENGIRELFQIGVNDEEENKILIELIQLLFEKKFLEISEIDCLLIALGCTTNENFQFKKDLKFRKINISVIKMLVNQPPFSFKIYPSTLEWAIGNCDPNIVNYLINSPNIIISEKFKNKSLRIAFNNYKYKEEMIQFILERPKLYNSNLNQDQSISQIFTKKIKLINGHHSNKLSSSSFHPDLNEKDKIKIFDYNELFSIESNLIQNKLLNLNYLKLPIELDCSGSGSCSGNNGSCGDFKISKNKDEFNLKVLNILNGYNLNKIKELNKLLAIEYPNEFYEQYLFKFNEPIRELNGQDEIDQLLRWILSTFNFNGLKWFLNNFNNNFDNNINNQRNHIKNIQISSPSSSYYLTSTTNIENLNELIILQFIKLYTSLENHFENEDCDKLIIKYIFKSKNKEQYDRFLSCIKCNRFSNILPKKWNQIIIDLYNNSRNKNTIVIRDKETIDWILENVNNKFLLEKCNYLKTTEIFQFENLETIEYACLKFVENNLNLRFSKTTEQRLLYLPFIKAISECDIESLQYIDNNKIVLKNDLIGPYRQNMEENLSIQTTENLIKLTEYLGTSGYKNFKPDCFGFFVEIITNIQNPTYDLSLVKVNFNCYINKTIDLLIHSFNNSSFKIIKFILDNCNPIKTNTQSFIDQWNQSYRLNYIYVLDNSDKFYKIKYYTSNSSINDIQLCIKILLKFYKNNINNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNQLDLEYEIILKKLINYQFKRLIEINYLPIDLLNSIYQLINEIDENIIEHSFFHSFYYLTIKSKKFLKYIMGLPFITSVLKDFNNHRYDDDKNYNYIGFDIKKYLDPIIFNYQFIFQSDFDIILDKLIMNLSILPSINDQQMIQKEENYLFLTLNYNLQYFLEIKRIDLFLNQLDYIQFQMNNNNNNSIFNISNSTFQLIFKTISNSIDSILFQKIITFSSYNSIVNYLNNLYNQINQNNQNNRNNNDNQLDYIFNNFKLFNFILINYFNQQFELKIRNYNNNNKIQQQKDEKLLQLQSFISNYWNSVIESFKKQFTKHIVIKYNFHLLFIENNIILSPENLKLFYSLTSSSIVLFNSISKYNRNDPFLKITKSRLLDLIRNKKLNFLKYLYENRYITNQSVSNEEDDNLLDFLKFQFKNHPEYNLVNWLK
Protein: Ubiquitin-activating enzyme E1 C-terminal domain-containing protein (Q8BTN4)
Organism: Mus musculus (Mouse)
Interaction partners:
Sequence:
MDEELYSRQLYVLGLPAMQRIQEAKVLLCGLQGLGAEVAKNLVLTGVGSLTLHDPHPTCWADLAAQCFLSEESLGRNRAEASQAQLAQLNEAVQISVHSGDITEDLLQGFQVVVLTDSKLEDQLKVGPLCHKHGVRFLMAETRGLVGRLFCDFGEDFTVLDPTEVEPMTAAIQDISQGFPGIVTLRGDTKRHSFHDGDLVIFSDIEGMVELNSCSPQSVRVQKDGSLEIGDTTTFSRYLRGGVVTEVKRPKTVRHKPLDIALLQPHVVAQNTQEVQRAHCLHQAFHVLHKFQQLHGRLPKPWDPDDAETVVELAQDLEPLKGTEEESLDEALLRTIALSSAGTLSPMAAIMGGVAAQEVLKAISRKFMPLDQWLYFDALECLPEDETLLPSPEDCQPRNCRYDGQIAVFGTDLQEKLSDQHYLLVGAGAIGCEMLKVFALVGLGVRANGGVTVADMDYIERSNLSRQFLFRPKDVRRPKAEVAAAAAHRLNPDLRATPYTCPLDPTTEDIYDDSFFSRVNGVVAALDSFQARHYVAARCTHYLKPLLEAGTQGTWGSASVFVPYVTEAYRGPASDAASEDAPYQQTCTSLSATDRTETLALLQQVMGVLRTRPQTWQDCVVWALGHWQLCFHDKVLEGGTQFSSGSNKCPHPLQFDPNHDMHFLYVLAAANLYARMHGLPGSQSQPALRELLTRLLESDSRPQNLFSAEHGQEQLKELQETLDDWRKGPPLKPVLFVKDDDSNFHVDFVVAATDLRCQNYGILPVNHARIKQIVGRIIPAIATSTAVVAGLLGLELYKVVSGLRSHGTFRHSYLHLAENHFIRSAPSAPAVQSFRDLKWTCWDRLKVPAVQPERTLKSLLAHLQEEHGLKVEMLLHHQARWSTACSGPRINLRDSSDYLQNWFST
Protein: Sulfate adenylyltransferase (EC 2.7.7.4) (ATP-sulfurylase) (Sulfate adenylate transferase) (SAT) (P78937)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Catalyzes the first intracellular reaction of sulfate assimilation, forming adenosine-5'-phosphosulfate (APS) from inorganic sulfate and ATP. Plays an important role in sulfate activation as a component of the biosynthesis pathway of sulfur-containing amino acids.
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03106}.
Interaction partners:
- Adenylyl-sulfate kinase
- Probable phosphoadenosine phosphosulfate reductase
- Sulfite reductase subunit beta
- Probable sulfite reductase flavoprotein component
- 3'
- Pyruvate kinase
- Probable FAD synthase
- Probable uroporphyrinogen-III C-methyltransferase
- Probable cystathionine gamma-synthase
- Siroheme biosynthesis protein met8
Sequence:
MTKALLKDLNARDAPLREQLEQEATSLPKIVLSERQFCDVELILNGGFSPLDGFMNQKDYLNVVENLRLSTGEVFPIPITLDLNESQADSLKAGDRVALLDPRDGQTVIAILTVEDKYTPDKANEAEKVFGANDRAHPAVDYLFGRAGNVYVGGKLQAVTPIRHFDFVEYRYSPAQLRSDFQRNNWNRVVAFQTRNPMHRAHRELTVRAAKQHGARVLIHPVVGMTKPGDIDHFTRVRVYEAILQRYPKGSAKLSLLPLAMRMAGPREALWHAIIRKNYGASHFIIGRDHAGPGKNSQGEDFYGPYDAQYLVEQYAQEIGITIVPFQMMTYLPDEDIYKPVDKVEPGTRTLNISGTELRRRLRVGANIPEWFSYPEVVAILRQSYPPKYSQGFVLAVPATSDKLLPSALVSALNEDGRRHVTLLPRLDAISVFYAQELQRAGAAVVVSLADADASVKVPAEWTTVNIKPKDSVSEVTFAVLSQLSDEGYL
Protein: Ectodermal, isoform A (Ectodermal, isoform B) (LP09339p) (Q7K1N5)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MKFVILLCVLSALLLQIEASPLQRLSRSERAVSRQQTVNNEVAPAVAPASDDDDDDDDEDDDDEPDLGDLIDDDDDDDEEEDDDEDEEDDTPQGQAAPAATASDDDEEEDDDDDDYLDRLFDDILGDDEDEDDDDETPAATAQQSAVAAAPAQTLDEVAPAAASSVSAGISDGVDLPAESGNAAEVLAAGNAADESVSAAVAPAQNAAASSSNNEGIAGDDDEEADDDDDDDDDDIIGDDIIEARREARDLKNNVIDMSTDAFQARHNHFIDAIFSRINRIVSENYDPYVVNLTGRSVLPNAASGSNVKAANKKQSTSSKVGGHKKLKNTRSEPRSVNSNQEAREAAVKLQEQLTQLQSELAIKAVEKRPSPTSPATESESDSGSPKAETRTVSGSKTGQKKSSNKQNTKKASGLKSGNYNQPAGASKAGASSAGAVEKLQKAEGRLSGLASLKRVGNVKVISDAEGRNSTIKAKFTLGPLVLRVEKSFKKGSVRSVKSATARTNEMMGRIKFSVLDDRATLMSIKVQQPKQVEVESKDNHDRTREFVWRRTPKIAKLVNEKLKLAAESLFAPQGVEVVRL
Protein: Transcription termination factor MTERF15, mitochondrial (Mitochondrial transcription termination factor 15) (Q9C6A1)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Transcription termination factor required for mitochondrial NAD2 intron 3 splicing and normal membrane respiratory chain Complex I activity. Essential for normal plant growth and development. Binds to RNA but not to double-stranded DNA.
Subcellular location: Mitochondrion {ECO:0000269|PubMed:21464319, ECO:0000269|PubMed:25402171}.
Interaction partners:
- RCC1 domain-containing protein RUG3, mitochondrial
- Transcription termination factor MTERF6, chloroplastic/mitochondrial
- Transcription termination factor MTEF18, mitochondrial
- Nuclear intron maturase 2, mitochondrial
- Nuclear intron maturase 1, mitochondrial
- Nuclear intron maturase 4, mitochondrial
- DEAD-box ATP-dependent RNA helicase 53, mitochondrial
- Pentatricopeptide repeat-containing protein At3g48250
- NADH dehydrogenase subunit 2.
- Protein WHAT'S THIS FACTOR 9
Sequence:
MASKLKTFINLRDYPITLFNQIRSLSSRILTPINQSHYRKRILLANLLQRYGFPPSSLQHFLSRNNHLLNSDLVETEISLGILLSLKIPQKSLVSLISDCPNVLRSEFLRKWRVPLSNCGKHGVVSSSAIKSVLEHSSRIGIGPDKFNECVRVLKSLGFCDSTVSRILSSFPGVLLVNEIEIRRKIEFLVGIGIARDNIERFFHVFPEVLGIGTETRLKPLLDEFMKMGFSKDDVKKEIAREPRVLGLELGELPRCLELINTLKCREVIRVSIISEGAFRAGFEVKLRVDCLCKYGLIRRDAFKVVWKEPRVILYEIEDIEKKIEFLTNRMGFHINCLADVPEYLGVNLQKQIVPRYNVIDYLKLKGGLGCDIGLKGLIKPSMKRFYNLYVMPYPECERIFGKRKENVRVNKRHPAGLWKLMKPPSNLTTKEDVQNMKSFIESLA
Protein: Major facilitator superfamily (MFS) profile domain-containing protein (Q9GNP0)
Organism: Caenorhabditis elegans
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
- Ras-related protein Rab-3
Sequence:
MSYILDWISTYRNNRKILLLIVYIALFLDNMLLTTVVPIIPEYLLRMEHPNETDILFSHNSQKRVKRQWEDDDSWDVPLKLGNNADIDWDENPIGPVGRSERRKESDRKNHNSKNREYNDRRKYMSPAAKKPPVETEEPAVRTISEEERHKLLASENVHVGLMFGSKALVQLLVNPWIGPLTNRIGYTMPMFGGFVIMFCSTILFAFGDSYFTLWLARALQGVGSACTSTSGMGMLAQAYPDDLERGSAMGIALGGLALGVLVGPPYGGLLYQWSGKELPFVLLALLALFDGSIQFMVLQPKIDRGEPEGSSIKQLAKDPYIIVAAGAITIGNLGIAMLEPSLPLWMMESWGANSLERGAAFLPASISYLIGTNIFGPLAHRIGRWLSSFIGLVVIGFSLLSIPSATSVAGLIIPHALLGFSIGMIDASMFPLMGYLVDIRHVGVYGSIYAIADAAFCFAFALGPFFSGPLVKSLGFPTMMYIIAVISFLYAPLMFLLKNPPVLIEPTPQTQSVELRQNGDSRVTNENYERIEGMNIAGQLQQNNMYSATSAF
Protein: Vacuole membrane protein 1 homolog (Transmembrane protein 49 homolog) (Q54NL4)
Organism: Dictyostelium discoideum (Social amoeba)
Function: Phospholipid scramblase involved in lipid homeostasis and membrane dynamics processes (By similarity). Required for autophagosome formation: participates in early stages of autophagosome biogenesis at the endoplasmic reticulum (ER) membrane by reequilibrating the leaflets of the ER as lipids are extracted (By similarity). In addition to autophagy, involved in other processes in which phospholipid scramblase activity is required.
Subcellular location: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. Endoplasmic reticulum {ECO:0000269|PubMed:18550798}.
Interaction partners:
- Autophagy-related protein 9
- Autophagy-related protein 18
- Autophagy-related protein 8
- Ubiquitin-like protein atg12
- Autophagy protein 5
- WD repeat domain phosphoinositide-interacting protein 3
- Serine/threonine-protein kinase atg1
- Ubiquitin-like modifier-activating enzyme atg7
- Ubiquitin-like protein
Sequence:
MGKSNTIVLSNEKDIQLRIQQLEERKEKRKNVKLLFSPIKTTKYFLYILKDTLVSGIRYFQTRPFLLFFIALFASLTFIAVYVPGEHQKYMGKYSDLISDCIWWVGLGVLSSIGLGTGLHTFVLYLGPHIAKVTLAATEWNSVNFNVYGANSFIQPATAMIGGVSFWMILQKVQWAALFWGAGTAIGELPPYFVARTARLKGLKLEQEKKLKEQQEKPIDEKDQPKKGLLERLSEKVPALIGNLGFFGILAFASIPNPLFDLAGITCGHFLVPFWKFFGATFIGKAVVKAHIQACFVILAFNMETLTMVISFIEDKIPFLKNKIQPILEKERQKLNSTVSANSPKSLVGLAWDCVLFLMISYFLMSIVDSSVQEYLIEKDNKKIELLKSKLEKQQPKETKKTK
Protein: V-type proton ATPase subunit (B2R7M1)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MSFFPELYFNVDNGYLEGLVRGLKAGVLSQADYLNLVQCETLEDLKLHLQSTDYGNFLANEASPLTVSVIDDRLKEKMVVEFRHMRNHAYEPLASFLDFITYSYMIDNVILLITGTLHQRSIAELVPKCHPLGSFEQMEAVNIAQTPAELYNATLVDTPLAAFFQDCISEQDLDEMNIEIIRNTLYKAYLESFYKFCTLLGGTTADAMCPILEFEADRRAFIITINSFGTELSKEDRAKLFPHCGRLYPEGLAQLARADDYEQVKNVADYYPEYKLLFEGAGSNPGDKTLEDRFFEHEVKLNKLAFLNQFHFGVFYAFVKLKEQECRNIVWIAECIAQRHRAKIDNYIPIF
Protein: Regulator of chromosome condensation 1 (C9JMJ4)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MSPKRIAKRRSPPADAIPKSKKVKVSHRSHSTEPGLVLTLGQGDVGQLGLGENVMERKKPALVSIPEDVVQAEAGGMHTVCLSKSGQVYSFGCNDEGALGRDTSVEGSEMVPGKVELQEKVVQVSAGDSHTAALTDDGRVFLWGSFRDNNGVIGLLEPMKKSMVPVQVQLDVPVVKVASGNDHLVMLTADGDLYTLGCGEQGQLGRVPELFANRGGRQGLERLLVPKCVMLKSRGSRGHVRFQDAFCGAYFTFAISHEGHVYGFGLSNYHQL
Protein: Dihydroxyacetone phosphate transaminase Cj1437c (EC 2.6.1.-) (Capsule polysaccharide biosynthesis protein Cj1437c) (PLP-dependent transaminase Cj1437) (Q0P8H7)
Organism: Campylobacter jejuni subsp. jejuni serotype O:2 (strain ATCC 700819 / NCTC 11168)
Function: Pyridoxal phosphate (PLP)-dependent transaminase involved in the biosynthesis of amidated D-glucuronic acid structures found on the capsular polysaccharide (CPS) of C.jejuni. Catalyzes the transamination of dihydroxyacetone phosphate (DHAP) to (S)-serinol phosphate in the presence of L-glutamate. Less active with L-aspartate. No activity with dihydroxyacetone or L-alanine.
Interaction partners:
- Histidine biosynthesis bifunctional protein HisB
- Histidine biosynthesis bifunctional protein HisIE
- Histidinol dehydrogenase
- UDP-galactopyranose mutase
- Para-aminobenzoate synthase component I
- Bifunctional chorismate mutase/prephenate dehydratase
- Phosphatase
- Sugar transferase
- Imidazole glycerol phosphate synthase subunit HisH 2
- Imidazole glycerol phosphate synthase subunit hisF1
Sequence:
MQANKNIQKLTPYLSIPHKIWNSSQSNILKLDWNEATIPPSPYVIESIKKFLVNGNLNWYPNTKNLYLLDKIAEYTKQINSSFVELFEGSDSAHECIIDVFLDKCDKIGIVSPTYDNFRSRANGVGIETISFTLDDNFNLDFDSLEYFIHEKRIKLLYLCNPNNPTGKSYNIQKIKSLIINNPNVMFIIDEAYYEFTSQSVCDLVEQCNNLIITRTFSKAFALASFRIGYIISHPENIESINKLRNPKSVPMLSQIAANAALEDLQYMRDYVDEVSCARMEFVKFLNTLTTGGGGIFNDSVANFVLIQNENISLFVGFLEKEGIFIRNYSHLISKNCRISIGTRNQMSYVAEKIQEFAKKQGGFHLV
Protein: 4-coumarate--CoA ligase-like 8 (EC 6.2.1.12) (4-coumarate--CoA ligase isoform 11) (At4CL11) (Q84P26)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Carboxylate--CoA ligase that may use 4-coumarate as substrate. Follows a two-step reaction mechanism, wherein the carboxylate substrate first undergoes adenylation by ATP, followed by a thioesterification in the presence of CoA to yield the final CoA thioester.
Subcellular location: Peroxisome {ECO:0000305}.
Interaction partners:
- 12-oxophytodienoate reductase 3
- Acyl-coenzyme A oxidase 4, peroxisomal
- Acyl-coenzyme A oxidase 2, peroxisomal
- Putative acyl-coenzyme A oxidase At3g06690
- Putative acyl-coenzyme A oxidase 3.2, peroxisomal
- Acyl-coenzyme A oxidase 3, peroxisomal
- Putative peroxisomal acyl-coenzyme A oxidase 1.2
- Peroxisomal acyl-coenzyme A oxidase 1
- Putative acyl-activating enzyme 19
Sequence:
MANSQRSSSLIDPRNGFCTSNSTFYSKRKPLALPSKESLDITTFISSQTYRGKTAFIDAATDHRISFSDLWMAVDRVADCLLHDVGIRRGDVVLVLSPNTISIPIVCLSVMSLGAVLTTANPLNTASEILRQIADSNPKLAFTTPELAPKIASSGISIVLERVEDTLRVPRGLKVVGNLTEMMKKEPSGQAVRNQVHKDDTAMLLYSSGTTGRSKGVNSSHGNLIAHVARYIAEPFEQPQQTFICTVPLFHTFGLLNFVLATLALGTTVVILPRFDLGEMMAAVEKYRATTLILVPPVLVTMINKADQIMKKYDVSFLRTVRCGGAPLSKEVTQGFMKKYPTVDVYQGYALTESNGAGASIESVEESRRYGAVGLLSCGVEARIVDPNTGQVMGLNQTGELWLKGPSIAKGYFRNEEEIITSEGWLKTGDLCYIDNDGFLFIVDRLKELIKYKGYQVPPAELEALLLNHPDILDAAVIPFPDKEAGQFPMAYVARKPESNLCEKKVIDFISKQVAPYKKIRKVAFIDSIPKTPSGKTLRKDLIKFAISKI
Protein: ATP-dependent Clp protease ATP-binding subunit ClpX (ATP-dependent unfoldase ClpX) (P0A6H1)
Organism: Escherichia coli (strain K12)
Function: ATP-dependent specificity component of the Clp protease. Uses cycles of ATP binding and hydrolysis to unfold proteins and translocate them to the ClpP protease. It directs the protease to specific substrates both with and without the help of adapter proteins such as SspB. Participates in the final steps of RseA-sigma-E degradation, liberating sigma-E to induce the extracytoplasmic-stress response. It may bind to the lambda O substrate protein and present it to the ClpP protease in a form that can be recognized and readily hydrolyzed by ClpP. Can perform chaperone functions in the absence of ClpP.
Interaction partners:
- ATP-dependent Clp protease proteolytic subunit
- Stringent starvation protein B
- ATP-dependent protease subunit HslV
- ATP-dependent zinc metalloprotease FtsH
- Cell division protein FtsZ
- ATP-dependent Clp protease ATP-binding subunit ClpA
- Lon protease
- Chaperone protein ClpB
- ATP-dependent protease ATPase subunit HslU
- Protein GrpE
Sequence:
MTDKRKDGSGKLLYCSFCGKSQHEVRKLIAGPSVYICDECVDLCNDIIREEIKEVAPHRERSALPTPHEIRNHLDDYVIGQEQAKKVLAVAVYNHYKRLRNGDTSNGVELGKSNILLIGPTGSGKTLLAETLARLLDVPFTMADATTLTEAGYVGEDVENIIQKLLQKCDYDVQKAQRGIVYIDEIDKISRKSDNPSITRDVSGEGVQQALLKLIEGTVAAVPPQGGRKHPQQEFLQVDTSKILFICGGAFAGLDKVISHRVETGSGIGFGATVKAKSDKASEGELLAQVEPEDLIKFGLIPEFIGRLPVVATLNELSEEALIQILKEPKNALTKQYQALFNLEGVDLEFRDEALDAIAKKAMARKTGARGLRSIVEAALLDTMYDLPSMEDVEKVVIDESVIDGQSKPLLIYGKPEAQQASGE
Protein: Oxidized low-density lipoprotein receptor 1 (Lectin-like oxidized LDL receptor 1) (Lectin-type oxidized LDL receptor 1) (F5H7N8)
Organism: Homo sapiens (Human)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004193}; Lipid-anchor {ECO:0000256|ARBA:ARBA00004193}. Cell membrane {ECO:0000256|ARBA:ARBA00004401}; Single-pass type II membrane protein {ECO:0000256|ARBA:ARBA00004401}. Membrane raft {ECO:0000256|ARBA:ARBA00004285}. Secreted {ECO:0000256|ARBA:ARBA00004613}.
Interaction partners:
Sequence:
MVLGMQLSQVSDLLTQEQANLTHQKKKLEGQISARQQAEEASQESENELKEMIETLARKLNEKSKEQMELHHQNLNLQETLKRVANCSAPCPQDWIWHGENCYLFSSGSFNWEKSQEKCLSLDAKLLKINSTADLDFIQQAISYSSFPFWMGLSRRNPSYPWLWEDGSPLMPHLFRVRGAVSQTYPSGTCAYIQRGAVYAENCILAAFSICQKK
Protein: Spermidine synthase, putative (EC 2.5.1.16) (Q38EH6)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- ornithine decarboxylase
- S-adenosylmethionine decarboxylase proenzyme
- S-adenosylmethionine decarboxylase proenzyme-like, putative
- S-methyl-5'-thioadenosine phosphorylase
- Arginase, putative
- Trypanothione synthetase, putative
Sequence:
MPGPGLLADGWFREENGQWPGQAMSFKVEEVLHDTPTKFQHLSIFETDPKGPWGTVMTLDGCIQLTDFDEFVYHEMLSHTPLCAHPDPVDVLIIGGGDGGVMREVLRHGTVKRCVLVDIDGDVIEASKKYFPQISSGFSDPRADVRVGDGVAFVREAASESFDVVIIDTTDPDGPAAELFGEKFYRDVLRILKPRGICCNQGESVWLNRNLIEGMADFIKNKVGFASVKYAMIYTPTYPCGSIGSLICSKVAGVDVTQPVRPVESMPFAGELKYYDSDVHKAAFVLPRFARHLNQNYS
Protein: tRNA-uridine aminocarboxypropyltransferase (EC 2.5.1.25) (Q9FFU2)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- tRNA-uridine aminocarboxypropyltransferase
- tRNA-uridine aminocarboxypropyltransferase A
- tRNA
- tRNA
- tRNA
- Phosphatidylinositol N-acetyglucosaminlytransferase subunit P-like protein
- tRNA-dihydrouridine synthase
- Probable protein phosphatase 2C 36
Sequence:
MLSSGQMMGHVVARTQMILSRSNFADCIRCQGVRVSKTLKMGTKRPTCPSCDKPSQLCLCKKMRSPCFDNQVSITILQHSLERKHALNSTRIARLGLKNVGVTTVFDVHDEAEFLIRVIGSGCSKIDTNHLDSEYRVENVASLELDDSFKLGSSGNVENLESEKNVVLVDHGSLEIAESLNLSQHLSEISYRDSRVRDKIGSYEEDLIKICMKKHGVISNVSHSLMLETNVKVLSFDHILASPAAMDVLAKGFMVTKFSEGKQEFELEVPPGSALLFPSEESVKINYLKEKEELKVRNLIVLDGTWSKARRIYLENPWLKLLRCHVKLEIEGTSLYKEVRRQPRAGCLSTIESIVYAMKEIGEDPEGLDNMLNVFESMVEDQRRCKDENFNKII