wanglab/gogpt-training-data huggingface dataset:
Protein: Myc target protein 1 (Myc target in myeloid cells protein 1) (Q8R411)
Organism: Mus musculus (Mouse)
Function: May regulate certain MYC target genes, MYC seems to be a direct upstream transcriptional activator. Does not seem to significantly affect growth cell capacity. Overexpression seems to mediate many of the known phenotypic features associated with MYC, including promotion of apoptosis, alteration of morphology, enhancement of anchorage-independent growth, tumorigenic conversion, promotion of genomic instability and inhibition of hematopoietic differentiation.
Subcellular location: Nucleus membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}.
Interaction partners:
Sequence:
MANNTTSLGSPWPENFWEDLIMSFTVSVAIGLAIGGFLWALFVFLSRRRRASAPISQWSPTRRPRSSYNHGLNRTGFYRHSGYERRSNLSLASLTFQRQASMELVNSFPRKSSFRASTFHPFLQCPPLPVETESQLMTLSASTTPSTLSTAHSPSRPDFRWSSNSLRMGLSTPPPPAYESIIKAFPDS
Protein: Acetylcholine receptor subunit delta (Q07001)
Organism: Homo sapiens (Human)
Function: After binding acetylcholine, the AChR responds by an extensive change in conformation that affects all subunits and leads to opening of an ion-conducting channel across the plasma membrane.
Subcellular location: Postsynaptic cell membrane; Multi-pass membrane protein. Cell membrane; Multi-pass membrane protein.
Interaction partners:
- Acetylcholine receptor subunit alpha
- 43 kDa receptor-associated protein of the synapse
- Acetylcholine receptor subunit beta
- Acetylcholine receptor subunit epsilon
- Neuronal acetylcholine receptor subunit alpha-9
- Acetylcholine receptor subunit gamma
- Intestinal-type alkaline phosphatase
- Neuronal acetylcholine receptor subunit alpha-4
- Neuronal acetylcholine receptor subunit beta-3
- Neuronal acetylcholine receptor subunit alpha-2
Sequence:
MEGPVLTLGLLAALAVCGSWGLNEEERLIRHLFQEKGYNKELRPVAHKEESVDVALALTLSNLISLKEVEETLTTNVWIEHGWTDNRLKWNAEEFGNISVLRLPPDMVWLPEIVLENNNDGSFQISYSCNVLVYHYGFVYWLPPAIFRSSCPISVTYFPFDWQNCSLKFSSLKYTAKEITLSLKQDAKENRTYPVEWIIIDPEGFTENGEWEIVHRPARVNVDPRAPLDSPSRQDITFYLIIRRKPLFYIINILVPCVLISFMVNLVFYLPADSGEKTSVAISVLLAQSVFLLLISKRLPATSMAIPLIGKFLLFGMVLVTMVVVICVIVLNIHFRTPSTHVLSEGVKKLFLETLPELLHMSRPAEDGPSPGALVRRSSSLGYISKAEEYFLLKSRSDLMFEKQSERHGLARRLTTARRPPASSEQAQQELFNELKPAVDGANFIVNHMRDQNNYNEEKDSWNRVARTVDRLCLFVVTPVMVVGTAWIFLQGVYNQPPPQPFPGDPYSYNVQDKRFI
Protein: CTD kinase subunit gamma (CTDK-I gamma subunit) (CTD kinase 32 kDa subunit) (CTD kinase subunit 3) (P46963)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Gamma subunit of the CTDK-I complex, which hyperphosphorylates the C-terminal heptapeptide repeat domain (CTD) of the largest RNA polymerase II subunit. CTDK-I phosphorylates 'Ser-5' if the CTD substrate is not phosphorylated at 'Ser-5', but will phosphorylate 'Ser-2' of a CTD substrate if 'Ser-5' is already phosphorylated. CTDK-I is also more reactive toward substrates that are prephosphorylated at 'Ser-2' or 'Ser-5' compared with an unphosphorylated CTD substrate, therefore efficiently creating doubly phosphorylated CTD repeats. Involved in RNA polymerase I transcription and RNA polymerase II transcriptional elongation, and as part of the CTDK-I complex, pre-mRNA 3'-end processing and SET2 mediated H3K36 methylation. Together with CTK2, required for CTK1 CTD kinase activation. Required for DNA damage induced transcription. Involved in the adaptation to alternative carbon sources, including galactose, glycerol and ethanol, but not raffinose. Required for the integrity of the rDNA locus.
Subcellular location: Nucleus, nucleolus. Cytoplasm.
Interaction partners:
- CTD kinase subunit beta
- CTD kinase subunit alpha
- DNA-directed RNA polymerase II subunit RPB1
- FACT complex subunit POB3
- RNA polymerase II holoenzyme cyclin-like subunit
- Serine/threonine-protein kinase KIN28
- Cyclin CCL1
- Protein BUR2
- RNA polymerase II transcription factor B subunit 3
- Transcription elongation factor 1
Sequence:
MDSLEARLQFIQVLKNLQKTLHKTRDSITSSSTTTPPSSQQKLNNDPIQFYLRNYRHHYEDFHQCLFDTTMKMDPLDRLDVVIYYVRIIRNLYPHSHSNTNVTKVLNEVLLMDIDLVFELCLPCQDWKSLTNQATCKELFLDLSKLIHYDATSVTHTPSDTTLIDATTWYSVKTERTTKDYKESLQRTESLLKDRDLKKLAFFQQFNSDTTAINPDLQTQPTNANILLHRMEADRELHKRSKETSWYIERPSNDILDESEFKSLWTHFETTDSGFDKDDYKNIKALNDIAKASYIY
Protein: Endocytosis protein RME-8 (J domain-containing protein) (G5ED36)
Organism: Caenorhabditis elegans
Interaction partners:
- PX domain-containing protein
- Vacuolar protein sorting-associated protein 35
- Vacuolar protein sorting-associated protein 29
- Auxilin
- Vacuolar protein sorting-associated protein 26
- small monomeric GTPase
- CUP-5L
- Receptor-mediated endocytosis protein 6
- Vacuolar protein sorting-associated protein 13
- Dynamin-type G domain-containing protein
Sequence:
MAQFCSENRDIACYLVTKHSWKGKYKRVFSIGTLAITTYNPNTLEITNQWLYEDFLSVKPLRNGGSNDSKQDEYKIHVRNRGKNNDMRFSSDYTTDILTHCLQFSTKFADKNFEPLTVTAFKQSWSDRRIPVTLRANASCLEQIDNRGVVVQSYPYKNIRSIGKVSDCPGGFVVDVGEHRRRHMFASSNNEELVKEIRRLASDNIGIIVPIAKEQLTLEDFMRTRLGLCSRDEELTSYAEFKISKITRRNEMPVRRLLCLSETCIIERDLATYAVICATPLKHIVCLVRSEKDPQQFIVEYENGDGRAYVAAERDLILASLLDGIRASGNNEVFVCGHRFERNLRVIPFSTNLDEDSESQCMKHIIAPPPGLRRCDLIRRFNANVPYSGLRFSKSHEGFFSENKGKVIVNAIEAVLMENYTKDDKEYKHKTEAQLQCLRRLFASKSGFQAFTEVNGVREKLGSLVVRVLSWKSESIDHSTVEALCALMYPMHDQYELRIEQLNKQSLMSSPKFVENLLDLIVLHVDRSTGWLVIASMLNFLTFSVCSPYSETTAGDTFDHILKLVSLRGRSFFRLFQCPSMTIVKGAGMVMRAIIEEADVETSKSMQMLALSEGAFLTHLFMSLLSTGKDLRVMTNKQLSGHLISLWIADNQQANDLLIRCLPRGLLNYMESDEKVPVNEKDLLIVRNNFDAASNETKQNAMKEKFDQLRVTAEAGLERFVQHWDLEQKLNFLPKRVIDEKQQQRQQPVVLRKRRNRVRPNVNWKLFAYQFSKDHSQADLIWNEKTREEFRHAMDTETRALISEKEQAPTGLPIAWNHTEFQIRYPSLLEEIKIGDYYLRLLLIEADENATPIHNPLEFFNNVYHRFLLSTKVDMKCLCLRAMAITYSRHHMTIGAFQDSKYFVEMLQKCINPLERDHLVLLLSKLALNKDNVRELIISNILPLLVDLCVLAHLHVQRAKVQNQTNVIEASAEQMAEGGSEEWYYHDKDAKQVGPLSFEKMKSLYTEKTIFEKSQIWAAGMDKWMSLAAVPQFRWTVCQQKDQPNEINTGKGPFQATVMNFTDLSVLCLDTILQMCEFFPSRDSHDCVVRPMPSVKKQLTEPVLLYQLVQLLLTYEPQIVQRVALLLYLVMQDNPFLPRLYLSGVFYFILMYNGSNVLPIARFLHYTHMKQAFRSTLPQFEGQRQSVLATLLPEAATFYLEQYGPEKYAEVFLGEFDNPEIIWNTAMRRHLIERIAVHVADFSHRLTSNVRALYQFCPIPLIDYPELAQELFCHVYYLRHLCNKQRFPDWEIRDPIPFLRCCLATWYNELEKKPATMSVDLAREILSVDLTNEEHRKPAFIRRQYYKLAAKYHPDKNPEGREMFERINAAYELLSSETANNSGMPDSHRIVLCLQAQSIIYSRYSQELSEYKYAGYSQLIKTIDLEAKDEALFIKGGGDLLSAAIELANYTLISSALNAEQLRRDNGLEALVTAFDRCVPMVTMSSLPDDMAVRVCIHVCDCFATAATFEACRQRLMEMPSIFGALTRLLQFSNLPRLSTAAAQCIRAMAVDTLLQFQLFQTGVLWQLVPHLFHFDYTLDEGGVQHSEDSNKQSLANSLARSSCEALAALAGFRENTPDNDGVQASLRALLTPYICRCMKLETNDMVLKTLNSNMENPYMIWDNGTRAEVLEFVERHRTSNEPTSELYGAEFELSVHKNELIVGDIFIRIYNEQPTFALHEPKKVAIDLLDYIKKHSAELTGAPKPKAISDDLIEIDWGNGSQANGNSLDTETKVLMTMTALANLVSANPGALFANKKGVEILLIGNFPLLITYLRCRKHPKLQIAALQVILLAAANKECVTDLATCNVTTTLFTLLRDQPKMIARVLDVLIALSSNGQIGKEMLEHGGLMYILSILCLTNSDQGQRLQAAELLAKLQADKLTGPRWTRFIIKFLPEIFADSLRDSPNTALQMFDSSSENPELIWNEVTRQKVKGIIDTEVGKLYEQHIKDPTVKWNTTSLADKSCAYGDSINGELVVGGVFVRLYVENPGFNVRHPKLFSTELIEKVLELMSRPTPELDLVTKAFVELVRHHPNTADQLPSQGYLPQFCTAMCLQNTSASRSAILILQELSENQFCCDALSQLPCIDGIMKSMKNQPSLMRESAHALKCLMKRNTGELAQQMLSCGMVPYLLQVLDSSMNGVSNGAAARAEIVDALKSAILDLKVGQKIAEILDKSPVWAQFKDQRHDLFLPEARTQAITGGPTGVAGYLTEGMFNPPPMSNQPPPMHQTSGDFQPPL
Protein: Adenylate cyclase type 5 (EC 4.6.1.1) (ATP pyrophosphate-lyase 5) (Adenylate cyclase type V) (Adenylyl cyclase 5) (C9JRT8)
Organism: Homo sapiens (Human)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004651}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}. Cell projection, cilium {ECO:0000256|ARBA:ARBA00004138}.
Interaction partners:
Sequence:
MEMKADINAKQEDMMFHKIYIQKHDNVSILFADIEGFTSLASQCTAQELVMTLNELFARFDKLAAENHCLRIKILGDCYYCVSGLPEARADHAHCCVEMGMDMIEAISLVREVTGVNVNMRVGIHSGRVHCGVLGLRKWQFDVWSNDVTLANHMEAGGKAGRIHITKATLNYLNGDYEVEPGCGGERNAYLKEHSIETFLILRCTQKRKEEKAMIAKMNRQRTNSIGHNPPHWGAERPFYNHLGGNQVSKEMKRMGFEDPKDKNAQESANPEDEVDEFLGRAIDARSIDRLRSEHVRKFLLTFREPDLEKKYSKQVDDRFGAYVACASLVFLFICFVQITIVPHSIFMLSFYLTCSLLLTLVVFVSVIYSCVKLFPSPLQTLSRKIVRSKMNSTLVGVFTITLVFLAAFVNMFTCNSRDLLGCLAQEHNISASQVNACHVAESAVNYSLGDEQGFCGSPWPNCNFPEYFTYSVLLSLLACSVFLQISCIGKLVLMLAIELIYVLIVEVPGVTLFDNADLLVTANAIDFFNNGTSQCPEHATKVALKVVTPIIISVFVLALYLHAQQVESTARLDFLWKLQATEEKEEMEELQAYNRRLLHNILPKDVAAHFLARERRNDELYYQSCECVAVMFASIANFSEFYVELEANNEGVECLRLLNEIIADFDEIISEDRFRQLEKIKTIGSTYMAASGLNDSTYDKVGKTHIKALADFAMKLMDQMKYINEHSFNNFQMKIGLNIGPVVAGVIGARKPQYDIWGNTVNVASRMDSTGVPDRIQVTTDMYQVLAANTYQLECRGVVKVKGKGEMMTYFLNGGPPLS
Protein: CYC2-like cyclin, putative (Q57XT7)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- Protein artemis
Sequence:
MNPHACGVSNSWKPLSPQRDNIHTDMLDNINDNDGEDDACDYHRNHEMHKKVKRARTGTAHDVTTVAHINSNCSSCTSNGNDDKGRHVALIGSSDDNRNNTEVVCNKGVKNNNNSDTSAASGAVDERGAVNGLSPSCGQEEEARDELGQKCGHENNEVAGGRDTTKGSGFIAPDGDGRPADGHDSNGVVNGDDNADGEKRAVTLPIELDTVCRGLVLFLESLCEENSSEPLLTTDFHSSSIPGTSIAAYTQRFRLRGSFSGETLLVSLIMLLKYSFTISHPVTYYNVHRLMITSAMLSAKMREDRFFDNRYYSFLGGIKLSEMNKLELRFCSVLGWDLWIDDEDYETLARLMRRLVKELAEVEVSSNNDCVGEDVSAQNEVALREFGARFWAEHLRPWKCGLESNLARRAQRMEQSDRIFLNRIRERSRQFYLSESNGINGYGCSAVLVPTIYGRQMYQMTTPVMINRSGEACMDKKVDFRQQQQQQQQQFGIANRNSRELGTDHSVAAAAASSSVTAASACATMVGASGTVANGFSSFGNSVRMDGGSLVTTKGQYVVDGSSSSAPRPHNFDHTNGQSCVDPFKKDLKTSVTGSVGGAGVSCDTVGNGVNNGHRYASGTSVGNGTTGSAVKQQRRGNVSENHNNNNTNDIVVVNGSSGTDASNTGSNKWFSRTVRSKIQHASAIAVSDEQQQQPPAEKGLPWQRGERGVGAKRRKPDHYRDYR
Protein: FAD-linked sulfhydryl oxidase ALR (EC 1.8.3.2) (Augmenter of liver regeneration) (P56213)
Organism: Mus musculus (Mouse)
Function: FAD-dependent sulfhydryl oxidase that regenerates the redox-active disulfide bonds in CHCHD4/MIA40, a chaperone essential for disulfide bond formation and protein folding in the mitochondrial intermembrane space. The reduced form of CHCHD4/MIA40 forms a transient intermolecular disulfide bridge with GFER/ERV1, resulting in regeneration of the essential disulfide bonds in CHCHD4/MIA40, while GFER/ERV1 becomes re-oxidized by donating electrons to cytochrome c or molecular oxygen (By similarity).
Subcellular location: Mitochondrion intermembrane space {ECO:0000250|UniProtKB:P55789}. Mitochondrion {ECO:0000250|UniProtKB:P55789}.
Interaction partners:
- Mitochondrial intermembrane space import and assembly protein 40
- Mitochondrial import inner membrane translocase subunit Tim10
- Mitochondrial intermembrane space import and assembly protein 40
- Mitochondrial import inner membrane translocase subunit TIM50
- Cytochrome c oxidase copper chaperone
- Cytochrome c oxidase assembly factor 5
Sequence:
MAAPSEPAGFPRGSRFSFLPGGARSEMTDDLVTDARGRGARHRDDTTPAAAPAPQGLEHGKRPCRACVDFKSWMRTQQKRDIKFREDCPQDREELGRHTWAFLHTLAAYYPDRPTPEQQQDMAQFIHIFSKFYPCEECAEDIRKRIGRNQPDTSTRVSFSQWLCRLHNEVNRKLGKPDFDCSRVDERWRDGWKDGSCD
Protein: Nuclear factor of activated T-cells 2 (D4A0I8)
Organism: Rattus norvegicus (Rat)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}. Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- Transcription factor Jun
- Protein c-Fos
- Nuclear factor of activated T-cells 1
- Calcineurin subunit B type 1
- Protein phosphatase 3 catalytic subunit alpha
- Serine/threonine-protein phosphatase 2B catalytic subunit beta isoform
- Calcineurin subunit B type 2
- Forkhead box P3
- Serine/threonine-protein phosphatase
- Myocyte-specific enhancer factor 2D
Sequence:
MDAPEPQSDPDGGDGPGHEPGGSSQDELDFSILFDYDYLNPIEEEPIAHKAISSPSGLAYPDDVLDYGLKPCNPLASLSGEPPGRFGESDSIGFQNFLSPAKPAGASGPSPRIEITPSHELMQAGGALRGRDAGLSPEQPALALAGMAASPRFTLPVPGFEGYREPLCLSPASSGSSASFISDTFSPYTSPCVSPNNAGPDDLCPQFQNIPAHYSPRTSPIMSPRTSLAEDSCLGRHSPVPRPASRSSSPGAKRRHSCAEALVAPLPAASPQRSRSPSPQPSPHVAPQDDGIPAGYPPTAGSAVLMDALNSLATDSPCGIPSKIWKTSPDPTPVSTAPSKAGLARHIYPAVEFLGPCEQEERRNSAPESILLVPPTWPKQLVPAIPICSIPVTASLPPLEWPLSNQSGSYELRIEVQPKPHHRAHYETEGSRGAVKAPTGGHPVVQLHGYMENKPLGLQIFIGTADERILKPHAFYQVHRITGKTVTTTSYEKIVGNTKVLEIPLEPKNNMRATIDCAGILKLRNADIELRKGETDIGRKNTRVRLVFRVHIPEPSGRIVSLQAASNPIECSQRSAHELPMVERQDMDSCLVYGGQQMILTGQNFTAESKVVFMEKTTDGQQIWEMEATVDKDKSQPNMLFVEIPEYRNKHIRVPVKVNFYVINGKRKRSQPQHFTYHPVPAIKTEPSDEYEPSLICSPAHGGLGSQPYYPQHPMLAESPSCLVATMAPCQQFRSGLSSPDARYQQQSPAAALYQRSKSLSPGLLGYQQPSLLAAPLGLADAHRSVLVHAGSQGQGQGQGSTLPHTSSASQQASPVIHYSPTNQQLRGGGHQEFQHIMYCENFGPSSVRPGLPPVNQGQRLSPGSYPTVIQQQTAPSQRAAKNGPPVSDQKEALPSGVTVKQEQNLDQTYLDDVNEIIRKEFSGPPSRNQT
Protein: COMM domain-containing protein 9 (Q9P000)
Organism: Homo sapiens (Human)
Function: May modulate activity of cullin-RING E3 ubiquitin ligase (CRL) complexes. May down-regulate activation of NF-kappa-B. Modulates Na(+) transport in epithelial cells by regulation of apical cell surface expression of amiloride-sensitive sodium channel (ENaC) subunits.
Subcellular location: Nucleus {ECO:0000269|PubMed:21778237}. Cytoplasmic vesicle {ECO:0000269|PubMed:21778237}.
Interaction partners:
- COMM domain-containing protein 6
- COMM domain-containing protein 1
- COMM domain-containing protein 10
- COMM domain-containing protein 4
- COMM domain-containing protein 2
- Coiled-coil domain-containing protein 22
- COMM domain-containing protein 3
- Coiled-coil domain-containing protein 93
- COMM domain-containing protein 8
- COMM domain-containing protein 5
Sequence:
MAALTAEHFAALQSLLKASSKDVVRQLCQESFSSSALGLKKLLDVTCSSLSVTQEEAEELLQALHRLTRLVAFRDLSSAEAILALFPENFHQNLKNLLTKIILEHVSTWRTEAQANQISLPRLVDLDWRVDIKTSSDSISRMAVPTCLLQMKIQEDPSLCGDKPSISAVTVELSKETLDTMLDGLGRIRDQLSAVASK
Protein: Cell division cycle 34, ubiqiutin conjugating enzyme (A0A8I6AJQ8)
Organism: Rattus norvegicus (Rat)
Interaction partners:
Sequence:
MARPLVPSSQKALLLELKGLQEEPVEGFRVTLVDEGDLYNWEVAIFGPPNTYYEGGYFKARLKFPIDYPYSPPAFRFLTKMWHPNIYETGDVCISILHPPVDDPQSGELPSERWNPTQNVRKQVLGTKVDAERDGVKVPTTLAEYCVKTKAPAPDEGSDLFYDDYYEDGEVEEADSCFGDEEDDSGTEES
Protein: Uncharacterized monooxygenase Rv0892 (EC 1.14.13.-) (P9WNG1)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Interaction partners:
- Uncharacterized protein Rv0049
- Small ribosomal subunit protein uS2
Sequence:
MTGRCPTVAVVGAGMSGMCVAITLLSAGITDVCIYEKADDVGGTWRDNTYPGLTCDVPSRLYQYSFAKNPNWTQMFSRGGEIQDYLRGIAERYGLRHRIRFGATVVSARFDDGRWVLRTDSGTESTVDFLISATGVLHHPRIPPIAGLDDFRGTVFHSARWDHTVPLLGRRIAVIGTGSTGVQLVCGLAGVAGKVTMFQRTAQWVLPWPNPRYSKLARVFHRAFPCLGSLAYKAYSLSFETFAVALSNPGLHRKLVGAVCRASLRRVRDPRLRRALTPDYEPMCKRLVMSGGFYRAIQRDDVELVTAGIDHVEHRGIVTDDGVLHEVDVIVLATGFDSHAFFRPMQLTGRDGIRIDDVWQDGPHAHQTVAIPGFPNFFMMLGPHSPVGNFPLTAVAESQAEHIVQWIKRWRHGEFDTMEPKSAATEAYNTVLRAAMPNTVWTTGCDSWYLNKDGIPEVWPFAPAKHRAMLANLHPEEYDLRRYAAVRATSRPQSA
Protein: Serine and arginine rich splicing factor 3 (A0A8I6A2P1)
Organism: Rattus norvegicus (Rat)
Interaction partners:
Sequence:
MHRDSCPLDCKVYVGNLGNNGNKTELERAFGYYGPLRSVWVARNPPGFAFVEFEDPRDAADAVRELDGRTLCGCRVRVELSNGEKRSRNRGPPPSWGRRPRDDYRRRSPPPRRRYLREHLLEKDIGLFLEIGEEKGLCLVREITSRLDPSLGLVADLGQMKGNRRPVGKSGVQEITSFDRSMYRKLKFCLRLHKLGAFLRCFSCSNLFCLLEQ
Protein: Butyrophilin-like protein 8 (Q6UX41)
Organism: Homo sapiens (Human)
Function: May stimulate primary immune response. Acts on T-cell stimulated sub-optimally through the TCR/CD3 complex stimulating their proliferation and cytokine production.
Subcellular location: Membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}.
Interaction partners:
- Xanthine dehydrogenase/oxidase
- Perilipin-2
- Lactadherin
Sequence:
MALMLSLVLSLLKLGSGQWQVFGPDKPVQALVGEDAAFSCFLSPKTNAEAMEVRFFRGQFSSVVHLYRDGKDQPFMQMPQYQGRTKLVKDSIAEGRISLRLENITVLDAGLYGCRISSQSYYQKAIWELQVSALGSVPLISITGYVDRDIQLLCQSSGWFPRPTAKWKGPQGQDLSTDSRTNRDMHGLFDVEISLTVQENAGSISCSMRHAHLSREVESRVQIGDTFFEPISWHLATKVLGILCCGLFFGIVGLKIFFSKFQWKIQAELDWRRKHGQAELRDARKHAVEVTLDPETAHPKLCVSDLKTVTHRKAPQEVPHSEKRFTRKSVVASQSFQAGKHYWEVDGGHNKRWRVGVCRDDVDRRKEYVTLSPDHGYWVLRLNGEHLYFTLNPRFISVFPRTPPTKIGVFLDYECGTISFFNINDQSLIYTLTCRFEGLLRPYIEYPSYNEQNGTPIVICPVTQESEKEASWQRASAIPETSNSESSSQATTPFLPRGEM
Protein: Hemolytic phospholipase C (EC 3.1.4.3) (Heat-labile hemolysin) (PLC-H) (Phosphatidylcholine cholinephosphohydrolase) (P06200)
Organism: Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Function: Hydrolyzes sphingomyelin in addition to phosphatidylcholine.
Interaction partners:
- Phospholipase C accessory protein PlcR
- Non-hemolytic phospholipase C
- Cardiolipin synthase A
- Cardiolipin synthase B
- PLD phosphodiesterase domain-containing protein
- Nus factor SuhB
- Phosphatidylserine decarboxylase proenzyme
- Diacylglycerol kinase
- Phosphatidylglycerophosphatase A
- Phosphatidylcholine synthase
Sequence:
MTENWKFRRRTFLKHGAQAATLAGLSGLFPETLRRALAVEPDIRTGTIQDVQHVVILMQENRSFDHYFGHLNGVRGFNDPRALKRQDGKPVWYQNYKYEFSPYHWDTKVTSAQWVSSQNHEWSAFHAIWNQGRNDKWMAVQYPEAMGYFKRGDIPYYYALADAFTLCEAYHQSMMGPTNPNRLYHMSGRAAPSGDGKDVHIGNDMGDGTIGASGTVDWTTYPERLSAAGVDWRVYQEGGYRSSSLWYLYVDAYWKYRLQEQNNYDCNALAWFRNFKNAPRDSDLWQRAMLARGVDQLRKDVQENTLPQVSWIVAPYCYCEHPWWGPSFGEYYVTRVLEALTSNPEVWARTVFILNYDEGDGFYDHASAPVPPWKDGVGLSTVSTAGEIEVSSGLPIGLGHRVPLIAISPWSKGGKVSAEVFDHTSVLRFLERRFGVVEENISPWRRAVCGDLTSLFDFQGAGDTQVAPDLTNVPQSDARKEDAYWQQFYRPSPKYWSYEPKSLPGQEKGQRPTLAVPYQLHATLALDIAAGKLRLTLGNDGMSLPGNPQGHSAAVFQVQPREVGNPRFYTVTSYPVVQESGEELGRTLNDELDDLLDANGRYAFEVHGPNGFFREFHGNLHLAAQMARPEVSVTYQRNGNLQLNIRNLGRLPCSVTVTPNPAYTREGSRRYELEPNQAISEVWLLRSSQGWYDLSVTASNTEANYLRRLAGHVETGKPSRSDPLLDIAAT
Protein: Uncharacterized oxidoreductase YKL107W (EC 1.-.-.-) (P34251)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Subcellular location: Membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}.
Interaction partners:
- Putative uncharacterized oxidoreductase YGL039W
- Uncharacterized protein YGR153W
Sequence:
MFWKKDPTVSWERKNINDIDFSRFNVAIIGGTGGLGRAISRELAQRNARVTVVGQTFRDEDLKDKINFVKADLSLVSECKRISHSDEIPYEELTHLIFTTGIFASRQRQATSEGLEKDMAVSYLSRYIIFHDVAKRLGISRTKKDDLPKVFIAGFPGNGQVGDPDDLNSDEKKYSAYATHMNTVAANESLVIDAKDRYTNIDTFGLNPGLIKTNIRNNLLGSDTYLSRITEWIISWTCQSAETYAKTICTLIASPAIESRSGTMFSNKGDAILPSPGLTKDVVEKFMENSELLVEKALRNQSPFTSSNE
Protein: Autophagy protein 5 (Q6FJZ6)
Organism: Candida glabrata (strain ATCC 2001 / BCRC 20586 / JCM 3761 / NBRC 0622 / NRRL Y-65 / CBS 138) (Yeast) (Nakaseomyces glabratus)
Function: Involved in cytoplasm to vacuole transport (Cvt) and autophagic vesicle formation. Autophagy is essential for maintenance of amino acid levels and protein synthesis under nitrogen starvation. Required for selective autophagic degradation of the nucleus (nucleophagy). Also required for mitophagy, which eliminates defective or superfluous mitochondria in order to fulfill cellular energy requirements and prevent excess ROS production. Conjugation with ATG12, through a ubiquitin-like conjugating system involving ATG7 as an E1-like activating enzyme and ATG10 as an E2-like conjugating enzyme, is essential for its function. The ATG12-ATG5 conjugate acts as an E3-like enzyme which is required for lipidation of ATG8 and ATG8 association to the vesicle membranes (By similarity).
Subcellular location: Preautophagosomal structure membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}.
Interaction partners:
- Autophagy-related protein 3
- Ubiquitin-like protein ATG12
- Autophagy protein 16
- Serine/threonine-protein kinase ATG1
- Putative lipase ATG15
- Autophagy-related protein 18
- Autophagy-related protein 8
- Ubiquitin-like modifier-activating enzyme ATG7
- ATPase expression protein 3
- Phosphatidylinositol 3-kinase VPS34
Sequence:
MGDSKELVWNGSINVQIKLDSRLLVDGVPEGRRLVNIRVPRESHIAIYTPLVLERLRNVLRSDIEELLPKVWYSYKDISLPWSIPFGTLFDIYNGAHKGISGSRDNYINVWKLNLVTDEKFPINVIPIIEGQDQLRKFMMQSWKQCCFILNGSSKRVMSLSLQDSLEVWEGVTERDYAKYSGVIKRILPRTPRRIPVAIHAANGGPIVQTTEPTLTDTSFSQAVEGIVKADFVVCQGIVMYLRDFSDTSLYDVYDKLHSIDGYLHLIANL
Protein: CDT1 Geminin-binding domain-containing protein (Q86S68)
Organism: Caenorhabditis elegans
Interaction partners:
- DNA replication licensing factor mcm-5
- DNA replication licensing factor MCM7
- Cell division control protein
- ORC
- Origin recognition complex subunit 1
- DNA replication licensing factor MCM3
- DNA replication licensing factor MCM2
- DNA replication licensing factor mcm-6
- DNA replication licensing factor mcm-4
- Origin recognition complex subunit 5 C-terminal domain-containing protein
Sequence:
MSSRVTRSRSQTPQTAVTDFFKTTRKPRARGEKKIIDESITKTTTIKEVQIPAAPIVENKSSRTRARTPSRQAELSSSGTPPKKAREAEAEAPELPKIHEDIILENPAPQKSAIDKLMEASGPAKKKAGIRTVADLQARIAAKGAAKAIHEQNLKNKTKQVDDHVELLKSPKKPVIVEHHKSPQKSKAARNLFSPKKPVPDYIIPGFNVLKSAEKVRGEQDDAHEEEGKRMTAEFLKSSRLIDEVKESARQRIELPTAYEHLADTFKRIDQITAIFIGQNRSCVVPELIKNVKNTSGKDFSNEHLSQILHVYPQSYHIEMREQRKAFGQGGKYELEVRPNLVEDLRGYIYEKSPTDGDTEDLPLVCPSKLLSPKKSPRKQVQPALRKPEVDGRIRLDAARQRDRAHVFRYKLASIVTKCHTEFLESQGLCASSNIKRMHPLFRLDKHCPSLPQVKLPEPPLQKSSIHIGMKEALDKYMDQVSLPSFVQKAYQDLKSPLKSTTGASGTVPISPKKFSEMQKEQKSQGAMSLLERIRAKEAIKKAAEACIDKDLERRKQRLTLLRDRYVRIVCNHYTAKRAQTMEIDVICKFVQFSSSNSSSIPDIMDHLRLLCEVAPMYISEASLMNKKYFRFTDNNIEAINELLDEELQITQKKIDEQRNTQIAQMSHHHTPRPSKAARSLKFH
Protein: Probable protein phosphatase 2C 39 (AtPP2C39) (EC 3.1.3.16) (Q9LDA7)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
Sequence:
MTGREILHKMKESVKEKVGLGASASSADSGKGKSKMLKQITHGFHLVKGKAFHEMEDYVVAKFKEVDDNELGLFAIFDGHLSHEIPDYLCSHLFENILKEPNFWQEPEKAIKKAYYITDTTILDKADDLGKGGSTAVTAILINCQKLVVANVGDSRAVICQNGVAKPLSVDHEPNMEKDEIENRGGFVSNFPGDVPRVDGQLAVARAFGDKSLKMHLSSEPYVTVEIIDDDAEFLILASDGLWKVMSNQEAVDSIKGIKDAKAAAKHLAEEAVARKSSDDISVVVVKFQ
Protein: MltA-interacting protein (P0A908)
Organism: Escherichia coli (strain K12)
Function: May serve as a scaffold protein required for the formation of a complex with MrcB/PonB and MltA, this complex could play a role in enlargement and septation of the murein sacculus.
Subcellular location: Cell outer membrane {ECO:0000269|PubMed:16079137}.
Interaction partners:
- Adenylate kinase
Sequence:
MTKLKLLALGVLIATSAGVAHAEGKFSLGAGVGVVEHPYKDYDTDVYPVPVINYEGDNFWFRGLGGGYYLWNDATDKLSITAYWSPLYFKAKDSGDHQMRHLDDRKSTMMAGLSYAHFTQYGYLRTTLAGDTLDNSNGIVWDMAWLYRYTNGGLTVTPGIGVQWNSENQNEYYYGVSRKESARSGLRGYNPNDSWSPYLELSASYNFLGDWSVYGTARYTRLSDEVTDSPMVDKSWTGLISTGITYKF
Protein: Ferric/cupric reductase transmembrane component 2 (EC 1.16.1.9) (Ferric-chelate reductase 2) (O94727)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Metalloreductase responsible for reducing extracellular iron and copper prior to import (By similarity). Catalyzes the reductive uptake of Fe(3+)-salts and Fe(3+) bound to catecholate or hydroxamate siderophores (By similarity). Fe(3+) is reduced to Fe(2+), which then dissociates from the siderophore and can be imported by the high-affinity Fe(2+) transport complex in the plasma membrane (By similarity). Also participates in Cu(2+) reduction and Cu(+) uptake (By similarity).
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:P32791}; Multi-pass membrane protein {ECO:0000255}. Endoplasmic reticulum membrane {ECO:0000269|PubMed:16823372}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Iron transport multicopper oxidase fio1
- Plasma membrane iron permease
Sequence:
MILARDDKWTLGSIALIFVLLIGFALLFLLERFRVKEKSRTFKDCVNVYQCPSKGERVYLALRHWFIFLATHKAQMTLILSPLVMLVTIPFTGKETKNSIASYDWNLTGVAARLGYLSCGLFFVSYFFSLKNNPFCLMLFSSHEKMNYLHRWLSVYAVLISVLHGILFMIFSAQSYKPLLYDKISIYGYFITVVLFLMTVASLPSVRRKFFEWFFVLHHTCSVLIIFLIWLHHPRTIVYMKACIIIYAFDRGCRLFRSIWNRSNFRIYLLNEDMIYMVGRKPKRSFFALPWAAGSHVYINIPSLSYWQVHPFTLASAPFDDFIELFVAVHSGFTERLANRLYSMPHEYPNFSLAPGTPESLSNTYRELNSFKSYAVEIENTAQGHTYEPEDLYLETTVFMDGPYGTTSNVFKEYSYVLLIAGGVGFSYTLPILRDLILKECNVTSITFIWSCRSLSLLKVASKSLNSLLHQSNVRLKIINHFTGSISCKESSEFSNQTTENSEMEFFDDRPDLDMYIQKFFDYVGYQTAALAACGSQSFLKRIKNSVNKSISSTTDIYQHYEEL
Protein: Coactosin-like protein (Q9CQI6)
Organism: Mus musculus (Mouse)
Function: Binds to F-actin in a calcium-independent manner. Has no direct effect on actin depolymerization. Acts as a chaperone for ALOX5 (5LO), influencing both its stability and activity in leukotrienes synthesis (By similarity).
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:Q14019}. Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:Q14019}. Nucleus {ECO:0000250|UniProtKB:Q14019}.
Interaction partners:
- Arachidonate 12-lipoxygenase, 12R-type
- Actin, cytoplasmic 1
Sequence:
MATKIDKEACRAAYNLVRDDGSAVIWVTFRYDGATIVPGDQGADYQHFIQQCTDDVRLFAFVRFTTGDAMSKRSKFALITWIGEDVSGLQRAKTGTDKTLVKEVVQNFAKEFVISDRKELEEDFIRSELKKAGGANYDAQSE