wanglab/gogpt-training-data huggingface dataset:
Protein: Otoconin-90 precursor (PLA2-like otoconin) (A0JL26)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Secreted {ECO:0000256|ARBA:ARBA00004613, ECO:0000256|RuleBase:RU361236}.
Interaction partners:
Sequence:
MRMLYLIFLFVLQKVHSTAVFCPETDDLNSDKLLIGCLGVRLTWLYAVFEDLRSVLEFAVSLRCETGLCPADIQDHGHYCSNANTRDLQQIQPVDALDGCCFTHLRCSQELKERNCSRRAPSNNNYTCSYNSSCDMLDFCDEGFCRCDRMVIDCISFNRPITKQDRDNQLITSQTVSPFVTDLLENDTYISDVVNVTESVDLPLSDIDMETMFYEVNGTLNETMSNFTNELVPVNDSLSSNFQSTEYPGIYQSGREEEENEAGEKELGRNPDRESTLEREEEPVEYEDGLSNVTAVLTTEEPAGDNVEAPTTNNPVQWNKLDWTNNEPTVSMALTESQNVTDLPDKNTPHMTPPTTYVQTHSQPDHHPFDEDDYESDEDKLQLFTSNTLKPTTHTFEHTTLTQTHTTTNYTHGITKPHVDTHVITEEESEESGEEGEEEVQSTQSPYMVLMTTPTKLTTNQSSHHKTTSSVVTSKNTAASVQFPSMKESEEKYISDESKPESKEDEETEKERDLLADPPNESLESSTEQNYKLSTTKPTTPTQKMDKEESKEDLQSHEEDDKSTTSQTTTIPYRVSQISPFSWVIPAPIPKPVVHSVSPAPTVVKPTTNHKSTTVVPQKPISTRTTSSGRATVETISHPQKPPHPITDRSPSLTTTERQESAEEEEEEEEEEKEPSDSSQESKKIESLRVRGRALPFFTLSLLEAAGLTDLQQQKDSEECSMSFLQYSASGRVWRDMSALGEMLHCLTGRCPHEYQHYGCYCGQQGTGQPVDRLDRCCFLQQCCLEQLSVFGCRTNRKLNAHISCHKAKPQCFGVSVCDRLQCVCDRSTAECMAASHFNSSASSSCSGPRPLCLRTAHSSAQSTNQESSEESDEMSQSQPQINTQSDTVDRKPTQSKPQQDVREEEEDEEGKEKEEEEEEEKEQEEEEEEKEQEEEEEQ
Protein: Rho-GTPase-activating protein 5 (O74335)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: GTPase-activating protein for Rho1. Has a role in the negative regulation of (1-3)beta-D-glucan synthase activity and cell integrity.
Subcellular location: Membrane {ECO:0000269|PubMed:12519200}. Note=Membrane-associated. Localizes to the cell poles and septum.
Interaction partners:
- GTP-binding protein rho1
- Protein kinase C-like 1
- Rho-type GTPase-activating protein 1
- Rho-GTPase-activating protein 8
- Rho1 guanine nucleotide exchange factor 2
Sequence:
MTVVVGVLQIDDMGKKSSFASWWKQLRVKKSDDNKLFGLSLTRALEVSKVAIFLTRRDGEKVFYGYIPAVVAKCGFFLKQNATQVKGIFRVNGSSKRIQILQKAFSTGPDYGRSFDWEGYTVHDAANVFRRFINLMPEHVIPLEYYERFREPMTIPNLTDNERVEMYRRRIDELPIPNRQLLLYLLDLLSVFAMNSSKNLMTADNLAAIFQPGILSHPDHEVYSKDYQISQTALLFLINHQGSFIKTIPLSSLPPLVAAPTSPNTSSTLITQSAAPTPIASTSIRINSFNPRNGSIKRWRSFSRHSSATYSNSPSSNFSNMKSSEVDPGSPPRIKSRSYSLSRSSSMKLFHTLDRRRENRM
Protein: chitin synthase (EC 2.4.1.16) (Q8IPN4)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
- UDP-N-acetylglucosamine diphosphorylase
- chitin synthase
- Chitinase 7
- BcDNA.GH02976
- Knickkopf
- Chitin deacetylase-like 4
- FI03450p
- Vermiform, isoform I
- UPAR/Ly6 domain-containing protein rtv
Sequence:
MSAMRHRPMAPPGQGPGAGTAGEHVDSDDNNFTDDESSPLTHDIYGGSQRTIQETKGWDVFRDPPIKIETGSTANQECLELTVKILKIFAYVITFIIVLTGGVIAKGTMLFMTSQVRKDKKMEYCNKDLGRDKSFVVRLPEEERVAWIWALLIAYALPEIGALIRSARICFFKTFKVPKTGHFLFVWLMESLSAVGMALLMFVVLPQIDAIQGAMLTNCLCVVPGIFGLLSRTSKEGKRFVKVIIDLAAVAAQVTGLVIWPLLENRRELWVIPVACVMISCGWWENYVSPQSPLGLVRALGRIKEEMKYTRYFCHIFLSIWKILLFFTVTLLIYWAQGEEPGNLFAMYGDAFGPHKIIVYELPAGLGGVLPDTLESANIDTVDVDAAYNTVVYVLLLQIFGAYLCYIFGKFACKILIQGFSYAFPVSLTVPLSVTFLIAACGIRIDDPCFFHDTIPDYLFFTSPSNFRFNNFVTEQMAWAWILWLLSQTWIALHIWTPKCERLATTEKLFVQPMYSSLLIDQSMALNRRRDDQADVKTEDLSEIEKEKGDEYYETISVHTDRSSAPNKPSIKSSDNITRIYSCATMWHETKDEMIEFLKSIMRMDEDQCARRVAQKYLRVLDPDYYEFETHIFFDDAFEISDHSDDDIQCNRFVKLLIATMDEAASEIHQTTIRLRPPKKYPTPYGGRLVWTLPGKTKFITHLKDKDRIRHRKRWSQVMYMYYLLGHRLMELPISVDRKDAIAENTYLLTLDGDIDFKPNAVTLLVDLMKKNKNLGAACGRIHPVGSGPMVWYQLFEYAIGHWLQKATEHMIGCVLCSPGCFSLFRGKALMDDNVMKKYTTRSDEARHYVQYDQGEDRWLCTLLLQRGYRVEYSAASDAYTHCPEGFNEFYNQRRRWVPSTIANIMDLLADAKRTIKINDNISLLYIFYQMMLMGGTILGPGTIFLMLVGAFVAAFRIDNWTSFHYNIVPILAFMFICFTCKSNIQLFVAQVLSTAYALIMMAVIVGTALQLGEDGIGSPSAIFLISMVGSFFIAACLHPQEFWCITCGLIYLLSIPSMYLLLILYSIINLNVVSWGTREVVAKKTKKELEAEKKAAEEAKKRVKQKSMLSFLQSGIGDNGDEEGSVEFSLAGLFRCIFCTHGKTSDEKQQLTSIAESLDTIKHRMDTIESAVDPHGHHASRHGRRRTTSSGSKDHHLLTSVAEKSGDESDESDSDTSAEPKQERDFLTNPYWIEDPDVRKGEVDFLSSTEIQFWKDLIDQYLYPIDNDPVEQARIAKDLKELRDSSVFAFFMINALFVLIVFLLQLNKDNIHVKWPFGVRTNITYDESTQEVHISKEYLQLEPIGLVFVFFFALILIIQFTAMLFHRFGTISHILASTELNFCKKKSEDLTQDQLIDKHAVEIVKNLQRLQGIDGDYDNDSGSGPDRIARRKTIQNLEKARQPRRQIGTLDVAFKKRFLKLTADAENNPATPILTRRLTMRAETIRALEVRKNSVMAERRKSAMQTLGAKNEYGITTGAPINNNGALPNQRSGRVSNAGISIKDVFNVNGGGAEQIYGSNGGGTINQGYEHVIDEDGDGNSLRLTTRNPHPHPHHQVSWGQNTNGGGGNGTGRL
Protein: Bb in a boxcar, isoform C (EC 2.7.8.-, EC 2.7.8.1, EC 2.7.8.2) (A0A0B4K7Y4)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004370}.
Interaction partners:
Sequence:
MALLAYRDKHILSAQQLRKLSEHKYSCFSVSLLDPLLQPWWNWLVAQTPLWLAPNLITIVGLILNVVTTLILICYSPNGVEAPPRWTCLLCALGLFIYQSLDSIDGKQARRTNTSSPLGELFDHGCDSISTVFVALSACISCQLGHYPNWLFFQCFCAIALFYCAHWQTYVSGTMRFGRIDVTEAQFSIIAIHLVSAALGPEIWLTKLPHFNCESRFLPIYVACGVDLILALRYTKCILTEGCGKNGSSVAGTSVLSPSIPLTLVVLPALMIAQKSPQNLFTEHASVYIMAFGMVAAKVTNKLVIAHMTKAEMEYLDWSLLGPSLLFLNQYFNCIVPEIWLLWFTLIWGTQDLLRYCAQVCLEICQHLRIDLFRIPYTPKGATPHPATASVSSQSNFGSSADKNGGSAHRKSKSKPH
Protein: Serine/threonine-protein kinase PLK2 (EC 2.7.11.21) (Polo-like kinase 2) (PLK-2) (Serine/threonine-protein kinase SNK) (Serum-inducible kinase) (Q9R012)
Organism: Rattus norvegicus (Rat)
Function: Tumor suppressor serine/threonine-protein kinase involved in synaptic plasticity, centriole duplication and G1/S phase transition. Polo-like kinases act by binding and phosphorylating proteins are that already phosphorylated on a specific motif recognized by the POLO box domains. Phosphorylates CENPJ, NPM1, RAPGEF2, RASGRF1, SNCA, SIPA1L1 and SYNGAP1. Plays a key role in synaptic plasticity and memory by regulating the Ras and Rap protein signaling: required for overactivity-dependent spine remodeling by phosphorylating the Ras activator RASGRF1 and the Rap inhibitor SIPA1L1 leading to their degradation by the proteasome. Conversely, phosphorylates the Rap activator RAPGEF2 and the Ras inhibitor SYNGAP1, promoting their activity. Also regulates synaptic plasticity independently of kinase activity, via its interaction with NSF that disrupts the interaction between NSF and the GRIA2 subunit of AMPARs, leading to a rapid rundown of AMPAR-mediated current that occludes long term depression. Required for procentriole formation and centriole duplication by phosphorylating CENPJ and NPM1, respectively. Its induction by p53/TP53 suggests that it may participate in the mitotic checkpoint following stress.
Subcellular location: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole {ECO:0000250}. Cell projection, dendrite {ECO:0000269|PubMed:10523297}. Note=Localizes to centrosomes during early G1 phase where it only associates to the mother centriole and then distributes equally to both mother and daughter centrioles at the onset of S phase. {ECO:0000250}.
Interaction partners:
- Serine/threonine-protein kinase PLK1
- Serine/threonine-protein kinase PLK3
- Centrosomal P4.1-associated protein
- separase
- Nucleophosmin
- G2/mitotic-specific cyclin-B1
- Fizzy-related protein homolog
- Serine/threonine-protein phosphatase 4 catalytic subunit
- Cell division cycle protein 20 homolog
- Cyclin B3
Sequence:
MELLRTITYQPAAGTKMCEQALGKACGGDSKKKRPQQPSEDGQSQAQVTPAAPHHHHHHSHSGPEISRIIVDPTTGKRYCRGKVLGKGGFAKCYEMTDLTNNKVYAAKIIPHSRVAKPHQREKIDKEIELHRILHHKHVVQFYHYFEDKENIYILLEYCSRRSMAHILKARKVLTEPEVRYYLRQIVSGLKYLHEQEILHRDLKLGNFFINEAMELKVGDFGLAARLEPLEHRRRTICGTPNYLSPEVLNKQGHGCESDIWALGCVMYTMLLGRPPFETTNLKETYRCIREARYTMPSSLLAPAKHLIASMLSKNPEDRPSLDDIIRHDFFLQGFTPDRLSSSCCHTVPDFHLSSPAKNFFKKAAAALFGGKKDKARYNDTHNKVSKEDEDIYKLRHDLKKTSITQQPSKHRTDEELQPPPTTFAKSGTSAVENKQQIGDAIRMIVRGTLGSCSSSSECLEDSTMGSVADTVARVLRGCLENMPEADCIPKEQLSTSFQWVTKWVDYSNKYGFGYQLSDHTVGVLFNNGAHMSLLPDKKTVHYYAELGQCSVFPATDAPEQFISQVTVLKYFSHYMEENLMDGGDLPSVTDIRRPRLYLLQWLKSDKALMMLFNDGTFQVNFYHDHTKIIICNQNEEYLLTYINEDRISTTFRLTTLLMSGCSLELKHRMEYALNMLLQRCN
Protein: DafA protein (Q72AW5)
Organism: Nitratidesulfovibrio vulgaris (strain ATCC 29579 / DSM 644 / CCUG 34227 / NCIMB 8303 / VKM B-1760 / Hildenborough) (Desulfovibrio vulgaris)
Interaction partners:
- DnaJ protein, putative
- Chaperone protein ClpB
- Peptidase, M16 family
- Chaperone protein DnaJ
- histidine kinase
- DNA-directed RNA polymerase subunit beta
Sequence:
MEGKHSVAGLPIRSELIARAEFLELAAILPARLNELIELGWIEPVMTPVEAMLFRQIDVYRIRKLERICADFELPSVGGIIIVDLLDRIDTLNSRIRELEVSIRR
Protein: 14-3-3 protein gamma (Protein kinase C inhibitor protein 1) (KCIP-1) [Cleaved into: 14-3-3 protein gamma, N-terminally processed] (P61981)
Organism: Homo sapiens (Human)
Function: Adapter protein implicated in the regulation of a large spectrum of both general and specialized signaling pathways. Binds to a large number of partners, usually by recognition of a phosphoserine or phosphothreonine motif. Binding generally results in the modulation of the activity of the binding partner.
Subcellular location: Cytoplasm, cytosol {ECO:0000269|PubMed:22532927}. Mitochondrion matrix {ECO:0000269|PubMed:22532927}. Note=Translocates to the mitochondrial matrix following induction of MALM (mitochondrial protein catabolic process). {ECO:0000269|PubMed:22532927}.
Interaction partners:
- Serine/threonine-protein kinase B-raf
- RAF proto-oncogene serine/threonine-protein kinase
- Histone deacetylase 4
- 14-3-3 protein epsilon
- M-phase inducer phosphatase 2
- 14-3-3 protein zeta/delta
- Serine/threonine-protein kinase A-Raf
- M-phase inducer phosphatase 3
- Transcriptional coactivator YAP1
- 14-3-3 protein eta
Sequence:
MVDREQLVQKARLAEQAERYDDMAAAMKNVTELNEPLSNEERNLLSVAYKNVVGARRSSWRVISSIEQKTSADGNEKKIEMVRAYREKIEKELEAVCQDVLSLLDNYLIKNCSETQYESKVFYLKMKGDYYRYLAEVATGEKRATVVESSEKAYSEAHEISKEHMQPTHPIRLGLALNYSVFYYEIQNAPEQACHLAKTAFDDAIAELDTLNEDSYKDSTLIMQLLRDNLTLWTSDQQDDDGGEGNN
Protein: Actin interacting protein 3-like C-terminal domain-containing protein (H2L0S5)
Organism: Caenorhabditis elegans
Interaction partners:
Sequence:
MPLFSWRPRILGGGRKTPEATQAVQITIAPEPPELPEPAASSKPRNVRFDEPKSGSFNQERAAPVDWATNNYGGEARIIGTVRPEKNLTSGSSGRIPPEENVGSDWRYADDVKVRIDPVDHQRPIDSQPSRFGQHPSRATSVLQNLREQKSNLEYDERRREVSTLPSSYSSNRPDIYGNVQRFDTVSRTESHLSSDSQATRHLDDMNVVFLQANDEVKRILLPRNIHSMHQVKMSFVRTFPNVNRSFVEQPHVKIYIQEPTKGAIFYELEDPGDIKNKSVLRLREKTRVMSPVGGGYLDQPDYHSETEQDDGRRVGMMPMMRPASAMAAPSVDYMHRNTLPLKPQPPPPQVYDIYSDPYNSDTSSHDSRSVTRSGSATPVIDRESRVRMETMERQLAGLSNLVHTALVSKGMSETTQKDMAELRREILSMHPDTARESSEKPASSLSDSISSHTAYQLSVFRSKLKDTHNELKQLKNSAQVNAQTGNTLLREAGDKIGRLVADRMRGGVSVMPIEIPATEMSNESQRNEHASQLAELLHSLTSFETNVETVRGSVLANQKKLRMSEVEDMTEKLTNIGRLAANLKTDFPPIQMAIEQQIKRDMERVVREEKFIRDQSIAVDQSLRRCKALANIMVTMKKLAMVQDPSIQRRKKHVERADSAGAPGSPRLPPKPSVAQTIAMHSAPPSPLTAPIPPPPPPPPPMLPPQQSQLAQSLQLAATSSNVVKVAPMYEYKESPKSPVSDLDNVLEEVGDPGSIPRPPSRYSVQDVRQKFSKPPELPDQLRNLIEDVARRASPGPEQMNDRRQDLEERQERLAEKQRQLRSQFQQLQQLAPLP
Protein: Kinesin-like kinetochore motor protein CENP-meta (Q9NCG0)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000256|ARBA:ARBA00004245}.
Interaction partners:
Sequence:
MSAKNASSIQVCIKVRPCEPGLTSLWQVKEGRSIHLADSHAEPYVFDYVFDEGASNQEVFDRMARHIVHACMQGFNGTIFAYGQTSSGKTYTMMGDEQNPGVMVLAAKEIFQQISSETERDFLLRVGYIEIYNEKIYDLLNKKNQDLKIHESGNGIVNVNCEECIITSEVDLLRLLCLGNKERTVGETNMNERSSRSHAIFKIIIESRKSDHSDDDAVIQSVLNLVDLAGSERADQTGARGARLKEGGHINKSLLFLSNVIKSLSENADNRFTNYRDSKLTRILQASLGGNAFTSIICTIKPSIMEESQSTLSFATRAKKIRIKPQVNEMVSDATMMKRLEREIKVLKDKLAEEERKNENQQKVEHLERQIKHDMHKIICGHSLSDKGQQKRRRTWCPTASGSHLELAETGTTEDRIDQFPKVSHLPKPVFFHTSNAGKRWDNIPKTINILGSLDIGTESNSISEEFLPAECIDFGSPRPDVLKPMLTIRQLPDLPLTPKGPLTTDKIKKEIQDLQMFTSLEKHFEVECEEVQGLKEKLAEVTAQRDNLEQESLAEKERYDALEKEVTSLRADNEAANSKISELEEKLSTLKQTMRIMEVENQVAVGLEFEFEAHKKSSKLRVDDLLSALLEKESTIESLQKSLDNLTRDVLRNSKEGHMLSIAPEQEDVAGDSICNKCEELEKLIADLESKKNSCECDQLRLEIVSVRDKLESVESAFNLASSGIIQKATDCERLSKELSTSQNAFGQLQERYDALDQQWQAQQAGITTLHNEHEHVQEIYQKLQEEYEQLESRARSASSAEFQRLQNDNTKFQADIASLNERLEEAQNMLTEVQNSESTVEKLRIQNHELTAKIKELETNFEEMQREYDCLFNQLMESVQENDALREEIKQRPTSHVEESMRSSGISSDFDEQKQDINLLHQFVQLSESVQQIELQHHSGISRLFRANQMKLDQSEPGLKLCLESAEYIEEDNRQSDATEPICLKGFLKRHRFQIKRLSQEHVDMGEEKRLLDIISQLEQEIEEKSALMEATEATINEMREQMTNLESALLEKSVIINKVEDYQRQIESLEKQNAEMTMVYEELQDRVTRESSMSESLLRVPPDEDTLPGCPTSPSRREQEVATLKTSITELQSQVSDLNAELENHLRQIQLKDGNIARLQTDFEEMSERCLSMEVRLAELDEDTKQKQELLDRQAQKLSDDLCLIDQLQKKNAQLVEQYHKATESLSLADAKPDQILLSSQYDSQIEKLNQLLNAAKDELHDVRRIKDDEISALRMEFLLQIETNEKENQAKFYAELQETKDRYESNVAELKEKLLQVEETLSSVTVRCQAELEALKSAHKENISQAVEERNNLIVQHQAEMETIRETLKNKLAEASTQQSKMEDAFRAEINEVRATLMEQLNQTKEDRDKGASKLEEVKKTLEQMINGGRVMSDTIAELEKTKAEQDLAVNKLTKDNIELEKQCSKTQEQLQMESLTRDQISFEIEAHIKKLELIVASSKKRIIELEEKCDQQVLELDKCRLEKLSLESEIQKANSEHSCTMEKLQELQAEMKVLSNRNEKEKCDFETKLETFTFKITDLEEVLKEAQHKVILYDDLVSQHERLKICLAEANELSSNLQKKVMSLHTELIDSQKGISSRDVEINELREELKAAMDAKATASAEQMTLVTQLKDVEERMANQAEKFTREAANLKGSINELLLKLNSMQETKDMLESGNEELKEQLRNSQNLRNMLDEESKMCISLKEKLVKLEDAKTSLEQQLRDNKSEIYQRHTELTKEVELGRNRIGELTKKCEELCSDLENSDQIRLDLQETKEQLKKTLENNLGWQQKVDEVTRECEKLRFDMQSKEVQNESKVQELISECEELRSTLKSKEASFQSEKESMDRTISSLLEDKRNLEEKLCSANDIVAKLETEIAALRPRKSLDRNPVPRKSITFESEIRKNRRISVHDERRQSYWNDVREFGIMTDPVGMSSCSVFPLVFPLNESNFRQHNCNCAELNSKLQDCQRELFIRESQVTALKMELDHHPLKDENAQLTKRVIEEQDKAKVEQKRLKMKLQDLNARINDLTTASAKEPESNQMAQAAKPATVAAQTQTESDLETILEKTNVKYEEAVRMLRYRYNLIQELKEKLRQNENSDTSNITSLSAGQTSALKVAISNRYSSSSYIKYCFCRHSVSPKRRKFWQSNISMKPPSEFWRFEMMIWMLCGKNSRNMKQLHQINKSLGIIFVYICVCVWA
Protein: Vacuolar protein-sorting-associated protein 46 (Charged multivesicular body protein 1) (Doa4-independent degradation protein 2) (O60074)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Class E VPS protein implicated in concentration and sorting of cargo proteins of the multivesicular body (MVB) for incorporation into intralumenal vesicles. The lumenal sequestrated membrane proteins will be targeted into the vacuole after fusion of the endosome with the vacuole (By similarity).
Subcellular location: Endosome membrane; Peripheral membrane protein. Endomembrane system {ECO:0000250}; Peripheral membrane protein {ECO:0000250}.
Interaction partners:
- ESCRT-III complex subunit did4
- Vacuolar protein sorting-associated protein vts1
- Suppressor protein of bem1/bed5 double mutants
- Vacuolar protein sorting-associated protein 24
- Vacuolar protein sorting-associated protein ist1
- Uncharacterized protein C162.06c
- Vacuolar-sorting protein snf7
- Vacuolar protein sorting-associated protein 20
- Vacuolar protein-sorting-associated protein 25
- Charged multivesicular body protein 7
Sequence:
MSNLEASLFQLKFAAKSLNKQSLKAAKEERAEREKVKKAITKGNSEIARIYASNAIRKQQESLNLLKLSSRIDAVSSRLQTAVTMRAVSGNMAGVVRGMDRAMKTMNLEMISQVMDKFEAQFDDVNVQTGYMNKAMGSVTAVDTPQEDVDLLMQTVADEAGLEFNQNMNNNLSVPAASVPTPAAPVEDDNLQERLRALRS
Protein: SR-related CTD associated factor 8 (A0A0A0MT33)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MPQPLLPALPPLSSPSGAGSCGPSGGEVKQEPVGGRGRREWRVAPSSRPRSSPRLALPTQCSGRRLFRRRARGLRSDNMEAVKTFNSELYSLNDYKPPISKAKMTQITKAAIKAIKFYKHVVQSVEKFIQKCKPEYKVPGLYVIDSIVRQSRHQFGQEKDVFAPRFSNNIISTFQNLYRCPGDDKSKIVRVLNLWQKNNVFKSEIIQPLLDMAAGIPPPVVTPVLASTTTAMSNTPGTPVTPVTPANVVQGLPDPWVSQITNTDTLAAVAQILQSPQGQQLQQLIQTLQIQQQKPQPSILQALDAGLVVQLQALTAQLTAAAAAANTLTPLEQGVSFNKKLMDRFDFGEDSEHSEEPKKEIPASQLSHVSESVNNSIFHQIAEQLQQQNLEHLRQQLLEQQQPQKATPQDSQEGTFGSEHSASPSQGSSQQHFLEPEVNLDDSIDIQQQDMDIDEGQDGVEEEVFEQEAKKVAVRSRSRTHSRSRSRSPRKRRSRSRSGSRKRKHRKRSRSRSRERKRKSSRSYSSERRAREREKERQKKGLPPIRSKTLSVCSTTLWVGQVDKKATQQDLTNLFEEFGQIESINMIPPRGCAYVCMVHRQDAFRALQKLSSGSYKIGSKVIKIAWALNKGVKTEYKQFWDVDLGVTYIPWEKVKVDDLEGFAEGGMIDQETVNTEWETVKSSEPVKETVQTTQSPTPVEKETVVTTQAEVFPPPVAMLQIPVAPAVPTVSLVPPAFPVSMPVPPPGFSPIPPPPFLRASFNPSQPPPGFMPPPVPPPVVPPPTIPPVVPTSLVQPSLSMTPETVKDVGFGSLVIPGGSVASNLATSALPAGNVFNAPTKQAEPEEKVPHLIDHQISSGENTRSVIPNDISSNAAILGGQPPNVTSNSGILGVQRPNVSSNSEILGVRPSNVSSSSGIIAAQPPNILNNSGILGIQPPSVSNSSGLLGVLPPNIPNNSGLVGVQPPNVPNTPGLLGTQPPAGPQNLPPLSIPNQRMPTMPMLDIRPGLIPQAPGPRFPLIQPGIPPQRGIPPPSVLDSALHPPPRGPFPPGDIFSQPERPFLAPGRQSVDNVTNPEKRIPLGNDNIQQEGDRDYRFPPIETRESISRPPPVDVRDVVGRPIDPREGPGRPPLDGRDHFGRPPVDIRENLVRPGIDHLGRRDHFGFNPEKPWGHRGDFDEREHRVLPVYGGPKGLHEERGRFRSGNYRFDPRSGPWNRGFGQEVHRDFDDRRRPWERQRDRDDRDFDFCREMNGNRLGRDRIQNTWVPPPHARVFDYFEGATSQRKGDNVPQVNGENTERHAQPPPIPVQNDPELYEKLTSSNEINKEKSDTVADIESEPVVESTETEGT
Protein: Liquid facets, isoform F (A8JNM3)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
Interaction partners:
Sequence:
MQVNVAGLRRNIKNLAHNYSDAQVKVREATSNDPWGPSAAIMSEIAELTYNVVAFSEIMQMIWKRLNDHGKNWRHVYKALILLEYLIKTGSEKVAQQCKENIFAIQTLREFVYFEEGKDQGTHVREKAKQLVTLLKDDERLKNERVKAQKAKERFAQNPSGFGSDGYIDGPSQRDLPPGWQEEPPKSVSELEMVRPQTAGEEELQLQLAMAMSREEAEQEEAKRRSDDVRLQLALSQSEQDFKDPNGRPIPAPKKEEQQSHLLDLLDISLGATSISSPPLGAAGGAPTAVVDPWAMPGPRAPSQLSDPWSGTSSPQVDPWNPSAAPRTILGAGVPMTSAPLGAGNDAWGARTQSPSVASGSSNEGWLQSNGNANQNGRGATPAGPPAEGWLIKSTAVGALGAAPINHAANNGSSSSDPWLAEPAASAAGGAAAVGLADPWAPGAASQTGAGALDDPWKALGTGAIKKQSPEFDEFDLITNRNKSEHSNSNASNNNNASLLDDMDPLSANYGNGGINSSMHPSTGATAKKSIKDAHSFLGENSALVNLDNLIKPIAPQTQTGNQPAYNPFSDNVVPPKTNLFQQQQPAVPSINQLKQQAPFSVSMNQDPWAPVMGGVSTTSQQNNNMPWIKPEAATNPFLS
Protein: phosphatidylinositol-3,4,5-trisphosphate 5-phosphatase (EC 3.1.3.86) (W5U6G9)
Organism: Ictalurus punctatus (Channel catfish) (Silurus punctatus)
Subcellular location: Cell projection, filopodium {ECO:0000256|ARBA:ARBA00004486}. Cell projection, lamellipodium {ECO:0000256|ARBA:ARBA00004510}. Cytoplasm, cytoskeleton {ECO:0000256|ARBA:ARBA00004245}. Cytoplasm, cytosol {ECO:0000256|ARBA:ARBA00004514}. Membrane {ECO:0000256|ARBA:ARBA00004170}; Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004170}. Nucleus speckle {ECO:0000256|ARBA:ARBA00004324}.
Interaction partners:
Sequence:
MAGGGGAAPPLWYHRDLSRAAAEELLARAGRDGSFLVRDSESVSGAYALCVLYQKHVHTYRILPDEDNFLAVQTSQGVQPKRFKTLPELIQLYLQPNQGLVTTLLLPVEREECMDERDYSDGEDDKPPLPPRTGSCSSALVSIETPTESLSVGNGLSTVSHEYLKGSYALDLEAVKQGASTLPHLNKTLVSSCKRLHGEVDKVLSGLEILSKVFDQQSASMVSRMIQQSVSQGGDQELENLVTKLAILKDLLSSIEKKALKALQDMSVSSPLTPLTRHSKAIPVQAFEVKPDMYLAELAKIGKSQKNTLSVDVEAGKLVVMKKVKDTQEDWTTFTHDKIRQLIKSQRMPNKLGIVFEKEKDKSQRKDFIFPSAKKREAFCQLLQLMKNKHSNQDEPDMISIFIGTWNMGSVPAPKAVVSWLLSRGLGKTLDEMTVTIPHDIYVFGTQENSVCDKEWVENLRAALKDYTEIDYKPVAVQTLWNIKIVVLVKPEHENRISHVGMSSVKTGIANTLGNKGAVGVSFMFNGTSFGFVNCHLTSGNEKIHRRNQNYLDILRQLSLGDKQLNSFDISLRFTHLFWFGDLNYRLDMDIQEILNYINRKEFEPLLKVDQLNLEREKNKVFLRFVEEEITYPPTYRYERGSRDTYVWQKQKATGMRTNVPSWCDRILWKSYPETHIVCNSYGCTDDIVTSDHSPVFATFEVGVTSQFVSKKGLPKSSEQAYIEFENIEAIVKTASRTKFFIEFYSTCLEEFKKSYENDSQSSDNINFLRVSWSSKQLTTLKPILSDIEYLQDQHLLLTVKSLDGYESYGECVLALKSMIGSTAQQFHTYLSHRGEETGNIRGSMRVRVPSERMGTRERLYEWISVDKDETGGPKGKTLPSRAGHDYIKPTPSRKELSKVSEEGERNTTGRPAYTHTTAKEDNTQTRSKQTDSADGDATTCKNSFNNPAYYILEGVPNQSAALAADLLPGSAFSLPSASKSPPPAGGAGKGKGSVQARKQTGGRPPRPISEEGGSSEEDGSSGLTRPPPDFPPPPLPKSALEVSDASFFPKESKPRMHPEMADIKIPVTVSSKPLPSPSFAPPPTGSGAFCLDPSPGPSAFRRGGGTSGADDQSCSVLHLAKKLSEVEYVSGAGGVGGTGLKGGGVIHGRGLGFGESCRTFPPRSIPEEIMAEDLPEEALWQGGSSSSSLSVDSSVGEWLQRLGLERYEEGLLRNGWDDLEFLSDITEEDLEEAGILDPTHKMILLASLRQQQQQK
Protein: HTH-type transcriptional regulator PrtR (Pyocin repressor protein) (Q06553)
Organism: Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Function: Represses the promoter activity of the prtN gene.
Interaction partners:
- Transcription regulatory protein PrtN
- Protein RecA
- Repressor, PtrB
Sequence:
MDKSTQIPPDSFAARLKQAMAMRNLKQETLAEAAGVSQNTIHKLTSGKAQSTRKLIEIAAALGVSPVWLQTGEGAPAARSAVSVADGSPLVLEPLHPWDSDTPLDEDEVELPLYKEVEMSAGAGRTAVREIEGRKLRFSYATLRASGVDPSAAICAQLTGNSMEPLIMDGSTIGVDTATTHITDGEIYALEHDGMLRVKFVYRLPGGGIRLRSFNREEYPDEEYSPEDMRSRQISMIGWVFWWSTVRHRRGPSLVR
Protein: Glycogen phosphorylase, liver form (EC 2.4.1.1) (Q9ET01)
Organism: Mus musculus (Mouse)
Function: Allosteric enzyme that catalyzes the rate-limiting step in glycogen catabolism, the phosphorolytic cleavage of glycogen to produce glucose-1-phosphate, and plays a central role in maintaining cellular and organismal glucose homeostasis.
Subcellular location: Cytoplasm, cytosol {ECO:0000250|UniProtKB:P06737}.
Interaction partners:
- 1,4-alpha-glucan-branching enzyme
- Glycogen debranching enzyme
- Phosphoglucomutase-1
- UTP--glucose-1-phosphate uridylyltransferase
- Receptor-interacting serine/threonine-protein kinase 3
- Alpha-amylase 1
- Pancreatic alpha-amylase 2a5
- Glycogen phosphorylase, brain form
- Glucose 1,6-bisphosphate synthase
- Glycogen phosphorylase, muscle form
Sequence:
MAKPLTDQEKRRQISIRGIVGVENVAELKKGFNRHLHFTLVKDRNVATPRDYYFALAHTVRDHLVGRWIRTQQHYYDKCPKRVYYLSLEFYMGRTLQNTMINLGLQNACDEAIYQLGLDMEELEEIEEDAGLGNGGLGRLAACFLDSMATLGLAAYGYGIRYEYGIFNQKIREGWQVEEADDWLRHGNPWEKARPEFMLPVHFYGRVEHTQTGTKWVDTQVVLALPYDTPVPGYMNNTVNTMRLWSARAPNDFNLQDFNVGDYIQAVLDRNLAENISRVLYPNDNFFEGKELRLKQEYFVVAATLQDVIRRFKASKFGSKDGMGTVFDAFPDQVAIQLNDTHPALAIPELMRIFVDIEKLPWAKAWEITKKTFAYTNHTVLPEALERWPVELVEKLLPRHLEIIYEINQKHLDRIVALFPKDISRMRRMSLIEEEGGKRINMAHLCIVGCHAVNGVAKIHSDIVKTQVFKDFSELEPDKFQNKTNGITPRRWLLLCNPGLADLIAEKIGEDYVKDLSQLTKLHSFVSDDIFLREIAKVKQENKLKFSQFLEKEYKVKINPSSMFDVHVKRIHEYKRQLLNCLHVITMYNRIKKDPKKFFVPRTVIIGGKAAPGYHMAKMIIKLITSVAEVVNNDPMVGSKLKVIFLENYRVSLAEKVIPATDLSEQISTAGTEASGTGNMKFMLNGALTIGTMDGANVEMAEEAGEENLFIFGMRVDDVAALDKKGYEAKEYYEALPELKLVIDQIDNGFFSPNQPDLFKDIINMLFYHDRFKVFADYEAYVKCQEKVSQLYMNQKAWNTMVLKNIAASGKFSSDRTIKEYAKDIWNMEPSDLKISLSNESSNGVSANGK
Protein: Protein mu-NS (MuNS) (Q9PY83)
Organism: Reovirus type 1 (strain Lang) (T1L) (Mammalian orthoreovirus 1)
Function: Non-structural protein with ssRNA-binding activity. Is probably involved in the formation of viral inclusions, where the assembly of cores and the replication of viral RNA are thought to occur. Together with mu-2, recruits the other core proteins to these inclusions.
Subcellular location: Host cytoplasm {ECO:0000269|PubMed:28794026}. Note=Localizes to the viral factories formed by mu-NS and sigma-NS (PubMed:28794026). Localizes to the host stress granules (By similarity). {ECO:0000250|UniProtKB:Q9PY82, ECO:0000269|PubMed:28794026}.
Interaction partners:
Sequence:
MASFKGFSVNTVPVSKAKRDISSLAATPGIRSQPFTPSVDMSQSREFLTKAIEQGSMSIPYQHVNVPKVDRKVVSLVVRPFSSGAFSISGVISPAHAYLLDCLPQLEQAMAFVASPESFQASDVAKRFAIKPGMSLQDAITAFINFVSAMLKMTVTRQNFDVIVAEIERLASTSVSVRTEEAKVADEELMLFGLDHRGPQQLDISNAKGIMKAADIQATHDVHLAPGVGNIDPEIYNEGRFMFMQHKPLAADQSYFTLETADYFKIYPTYDEHDSRMADQKQSGLILCTKDEVLAEQTIFKLDAPDDKTVHLLDRDDDHVVARFTKVFIEDVAPGHHAAQRSGQRSVLDDLYANTQVVSITSAALKWVVKHGVSDGIVNRKNVKVCVGFDPLYTLSTHNGVSLCALLMDEKLSVLNSACRMTLRSLMKTGRDADAHRAFQRVLSQGYASLMCYYHPSRKLAYGEVLFLERSSDMVDGIKLQLDASRQCHECPVLQQKVVELEKQIIMQKSIQSDPTPMALQPLLSQLRELSSEVTRLQMELSRTQSLNAQLEADAKSAQACSLDMYLRHHTCINGHTKEDELLDAVRVAPDVRKEIMEKRGEVRRGWCERISKEAAAKCQTVIDDLTQMNGKQAREITELRESAENYEKQIAELVGTITQNQMTYQQELQALVAKNVELDTMNQRQAKSLRITPSLLSATPIDSVDGAADLIDFSVPTDEL
Protein: SET domain-containing protein (Q4GYU9)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MFRLSFAAFTSVAAGSRSVGCSTTFSTTTSAAASSSSSAAAATGKEAYEALMKFLTSSGATFEGVAVRPSAEQCRGLIATQTFREGTTILSVPMTTLSITADRLLNTDFIRSLNPPTRDDVRRLLMARGVNDPVLCDQVHLALLVAGERINVHSPFAPYFDVLPYPAIDDTAVIQRYKDVLDPTQLLEWDDHQRDWVTVLRALTDQWGNAGPPVEVCYWAWRTVLSRMHMLPDRGLAPADVGSSLHYSALATYGRAERQTRIMKRLRATIGAVFGSDGVAEDYRLVPTLLPLLDMVDHLPSSNVSVEVQPRGDRGSCGELQALREIQAGEHIGFSFNRSQGIPFTLYRFGFLPL
Protein: Acetylcholinesterase (AChE) (EC 3.1.1.7) [Cleaved into: Acetylcholinesterase 16 kDa subunit; Acetylcholinesterase 55 kDa subunit] (P07140)
Organism: Drosophila melanogaster (Fruit fly)
Function: Rapidly hydrolyzes choline released into the synapse. It can hydrolyze butyrylthiocholine.
Subcellular location: Synapse. Cell membrane; Lipid-anchor, GPI-anchor. Note=Attached to the membrane of the neuronal cholinergic synapses by a GPI-anchor.
Interaction partners:
- Carboxylic ester hydrolase
- LD22655p
- RE24176p
- Vesicular acetylcholine transporter
- Gamma-aminobutyric acid receptor subunit beta
Sequence:
MAISCRQSRVLPMSLPLPLTIPLPLVLVLSLHLSGVCGVIDRLVVQTSSGPVRGRSVTVQGREVHVYTGIPYAKPPVEDLRFRKPVPAEPWHGVLDATGLSATCVQERYEYFPGFSGEEIWNPNTNVSEDCLYINVWAPAKARLRHGRGANGGEHPNGKQADTDHLIHNGNPQNTTNGLPILIWIYGGGFMTGSATLDIYNADIMAAVGNVIVASFQYRVGAFGFLHLAPEMPSEFAEEAPGNVGLWDQALAIRWLKDNAHAFGGNPEWMTLFGESAGSSSVNAQLMSPVTRGLVKRGMMQSGTMNAPWSHMTSEKAVEIGKALINDCNCNASMLKTNPAHVMSCMRSVDAKTISVQQWNSYSGILSFPSAPTIDGAFLPADPMTLMKTADLKDYDILMGNVRDEGTYFLLYDFIDYFDKDDATALPRDKYLEIMNNIFGKATQAEREAIIFQYTSWEGNPGYQNQQQIGRAVGDHFFTCPTNEYAQALAERGASVHYYYFTHRTSTSLWGEWMGVLHGDEIEYFFGQPLNNSLQYRPVERELGKRMLSAVIEFAKTGNPAQDGEEWPNFSKEDPVYYIFSTDDKIEKLARGPLAARCSFWNDYLPKVRSWAGTCDGDSGSASISPRLQLLGIAALIYICAALRTKRVF