wanglab/gogpt-training-data huggingface dataset:
Protein: PAST-1 (Q94919)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004413}; Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004413}; Cytoplasmic side {ECO:0000256|ARBA:ARBA00004413}. Recycling endosome membrane {ECO:0000256|ARBA:ARBA00004159}; Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004159}; Cytoplasmic side {ECO:0000256|ARBA:ARBA00004159}.
Interaction partners:
Sequence:
MFSFLKREKNTQEVVENVIGELKKIYRSKLLPLEEHYQFHDFHSPKLEDPDFDANPVILLVGLYSTGKTTFIRYLLERDFPGIRIGPEPTTDRFIAVMYDDKEGVIPGNALVVDPNKQFRPLSKYGNAFLNRFQCSSVASPVLNAISNVDTPGILSGEKQRIDRGYDFTGVLEWFAERVDRIILLFDAHKLDISDEFRRSIEALKGHDDKIRIILNKADMIDHQQLMRVYGALMWSLGKVLQDLLHLLDVGEVAGRNGVLALDAIVYLAEVLNQVLLLAVLAEHRGHVLAQLGNDEGMHLGQARPLDQIVQLAQGGVTRQGLQHQDFTKFHSLKPHLLDIVDNMLAKDIARLMEMIPQEEMTMVADPIVKGGAFEGVIDDHVSPFGYMKGEGIDAGYGEHEWICNKDKPRTDGIFNGLGPVDGKISGATAKQELIKSKLPNSVLSKIWKLSDVDGDGFLDSDEFALALHLINVKLEGCELPTVLPEHLVPPSKRYD
Protein: Alpha,alpha-trehalose-phosphate synthase [UDP-forming] 1 (EC 2.4.1.15) (Trehalose-6-phosphate synthase 1) (AtTPS1) (Q9SYM4)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Required for normal embryo development, vegetative growth and transition to flowering. Regulates embryo growth, cell wall deposition, starch and sucrose degradation, but not cell differentiation. Involved in the regulation of glucose sensing and signaling genes during plant development.
Subcellular location: Vacuole {ECO:0000269|PubMed:17111094}. Secreted, cell wall {ECO:0000269|PubMed:17111094}. Cytoplasm {ECO:0000269|PubMed:17111094}. Note=Determined in transgenic tobacco plants expressing TPS1.
Interaction partners:
- Trehalose-phosphate phosphatase A
- Trehalose-phosphate phosphatase B
- Probable trehalose-phosphate phosphatase J
- Trehalase
- Probable trehalose-phosphate phosphatase E
- Probable trehalose-phosphate phosphatase H
- Probable trehalose-phosphate phosphatase D
- Probable trehalose-phosphate phosphatase F
- Probable trehalose-phosphate phosphatase G
- Probable trehalose-phosphate phosphatase C
Sequence:
MPGNKYNCSSSHIPLSRTERLLRDRELREKRKSNRARNPNDVAGSSENSENDLRLEGDSSRQYVEQYLEGAAAAMAHDDACERQEVRPYNRQRLLVVANRLPVSAVRRGEDSWSLEISAGGLVSALLGVKEFEARWIGWAGVNVPDEVGQKALSKALAEKRCIPVFLDEEIVHQYYNGYCNNILWPLFHYLGLPQEDRLATTRSFQSQFAAYKKANQMFADVVNEHYEEGDVVWCHDYHLMFLPKCLKEYNSKMKVGWFLHTPFPSSEIHRTLPSRSELLRSVLAADLVGFHTYDYARHFVSACTRILGLEGTPEGVEDQGRLTRVAAFPIGIDSDRFIRALEVPEVIQHMKELKERFAGRKVMLGVDRLDMIKGIPQKILAFEKFLEENANWRDKVVLLQIAVPTRTDVPEYQKLTSQVHEIVGRINGRFGTLTAVPIHHLDRSLDFHALCALYAVTDVALVTSLRDGMNLVSYEFVACQEAKKGVLILSEFAGAAQSLGAGAILVNPWNITEVAASIGQALNMTAEEREKRHRHNFHHVKTHTAQEWAETFVSELNDTVIEAQLRISKVPPELPQHDAIQRYSKSNNRLLILGFNATLTEPVDNQGRRGDQIKEMDLNLHPELKGPLKALCSDPSTTIVVLSGSSRSVLDKNFGEYDMWLAAENGMFLRLTNGEWMTTMPEHLNMEWVDSVKHVFKYFTERTPRSHFETRDTSLIWNYKYADIEFGRLQARDLLQHLWTGPISNASVDVVQGSRSVEVRAVGVTKGAAIDRILGEIVHSKSMTTPIDYVLCIGHFLGKDEDVYTFFEPELPSDMPAIARSRPSSDSGAKSSSGDRRPPSKSTHNNNKSGSKSSSSSNSNNNNKSSQRSLQSERKSGSNHSLGNSRRPSPEKISWNVLDLKGENYFSCAVGRTRTNARYLLGSPDDVVCFLEKLADTTSSP
Protein: SRY (sex determining region Y)-box 2 (Sox2 protein) (Transcriptional factor SOX2) (Q60I23)
Organism: Mus musculus (Mouse)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MYNMMETELKPPGPQQASGGGGGGGNATAAATGGNQKNSPDRVKRPMNAFMVWSRGQRRKMAQENPKMHNSEISKRLGAEWKLLSETEKRPFIDEAKRLRALHMKEHPDYKYRPRRKTKTLMKKDKYTLPGGLLAPGGNSMASGVGVGAGLGAGVNQRMDSYAHMNGWSNGSYSMMQEQLGYPQHPGLNAHGAAQMQPMHRYDVSALQYNSMTSSQTYMNGSPTYSMSYSQQGTPGMALGSMGSVVKSEASSSPPVVTSSSHSRAPCQAGDLRDMISMYLPGAEVPEPAAPSRLHMAQHYQSGPVPGTAINGTLPLSHM
Protein: Uncharacterized protein (Q8C2Y7)
Organism: Mus musculus (Mouse)
Interaction partners:
Sequence:
NNLGRRWNQALGTLGTWWVRTRAATNWHPWESGTADHHPPAARCDGGWRESPAARPAAAAVGLPGRTAHPARTPGAAPGGRGTGCAWRRGGHHPRSPLSDHLCPFALTAYKERDRTELLPKPELLGLHRPAIPH
Protein: Histone H2A.6 (HTA1) (Protein RESISTANT TO AGROBACTERIUM TRANSFORMATION 5) (Q9LD28)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling. Required for the T-DNA integration step of plant transformation by Agrobacterium. May play an important role in illegitimate recombination.
Subcellular location: Nucleus {ECO:0000250}. Chromosome {ECO:0000250}.
Interaction partners:
- Histone H2B.1
- Histone H4
- Histone H2B.6
- Histone H2B.10
- NAP1-related protein 1
- Histone H2B.7
- Histone H2B.5
- Histone H2B.9
- Histone H2B.11
- Histone H2B.8
Sequence:
MAGRGKTLGSGGAKKATSRSSKAGLQFPVGRIARFLKAGKYAERVGAGAPVYLAAVLEYLAAEVLELAGNAARDNKKTRIVPRHIQLAVRNDEELSKLLGDVTIANGGVMPNIHNLLLPKKAGASKPQED
Protein: Uncharacterized protein (G8B8C4)
Organism: Candida parapsilosis (strain CDC 317 / ATCC MYA-4646) (Yeast) (Monilia parapsilosis)
Interaction partners:
- Small ribosomal subunit protein bS6m
- DNA topoisomerase
- Small ribosomal subunit protein uS10
- Small ribosomal subunit protein uS10 domain-containing protein
- Eukaryotic translation initiation factor 1A
- Ribosome assembly factor mrt4
- 60S acidic ribosomal protein P0
- Small ribosomal subunit protein uS7 domain-containing protein
- Small ribosomal subunit protein uS7m
- Ribosomal protein S2
Sequence:
MLRAFTRSFTSTIPKKNFANGQLFGRVGNVDFKESANGTKYVRYSLAVNKFRKGEDSITDWYNITIFDEGELQKAEKALRVGNKMIVDVTLRLDKFEDPETKKVQTRTSLIQKHAEIVQWGKRTDEDRAEATE
Protein: Protein unc-50 (Uncoordinated protein 50) (Q10045)
Organism: Caenorhabditis elegans
Function: Required for cell surface expression of acetylcholine receptors in body-wall muscles.
Subcellular location: Golgi apparatus membrane {ECO:0000269|PubMed:17853888}; Multi-pass membrane protein {ECO:0000269|PubMed:17853888}.
Interaction partners:
- Resistance to inhibitors of cholinesterase protein 3
- Acetylcholine receptor subunit alpha-type unc-38
- Acetylcholine receptor subunit beta-type unc-29
- Acetylcholine receptor subunit alpha-type unc-63
- AcetylCholine Receptor
- Acetylcholine receptor subunit beta-type lev-1
- AcetylCholine Receptor
- Acetylcholine receptor subunit alpha-type acr-16
- Uncharacterized protein
- CUB domain-containing protein
Sequence:
MSSQPRGSGTQPGPSQSPISQRNFRYEPARSGYTSPGQYSTYSTSTADRVGCLTAVRMSAFAKLSRFTRRLVHIRQMDFEFALWQMLYLLIQPSKVYKNFIYRKRTKDQFARDDPAFLVLLALSLLFSSIFYAYALGLEKIGFFTFFLWSVFVDCIGVGVVIATVLWWVSNRFLRKVRDQDVEWGYCFDVHLNAFFPMLILLHVIVPILYPTLIDSPAFLSILLGNTFWFLAACYYVYITFLGYTALPILHKTQYFLYPISFIFMFFVATLTGGWNISRTALNFYHSRAEPHKFAPQHGGL
Protein: Uncharacterized protein (Q57ZP7)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- aspartyl aminopeptidase
Sequence:
MSSVGIEWSALSLPVEGEVVFASFVSLICPLDGRREGDDVSKKCSAASVLCNECANAIVCVLKDREVAFFDLADESAGPREVRRIGATPPLLVSRFMRNADPSVATCATLLPKDVSFMCRVPPAAVERVSSSDPSAGPHDGGAGAAHSVRGTVYLCGAVGTSDGRVDVFSEEGYVFGFVASDGPVVAVSVIYSTSFSSGGCAGVKSWEQIQPSGVSLPAEGSDEERTLDRATANLGFVTTNADGVVSVWRQDGCGLKPAVFGSSALFSRVFCSRVVQPSSRDWLLSGTEVTRTPFIVHTSPGLTADLCARSAVTFEDVESRVRLPGNMLTRTTAIASDGDSALVARGRSVFHVTFSGSSCDLVCTADCNVDGLHLPGSGPQKEGGAALAAACDVKGTVYVLCGQPLSVLGRYSATGGGPIRSLSICAVSRLVTIVGGDGTVDVVLVPTDADSVPTATVHQALASLPR
Protein: Aspartate--tRNA ligase (EC 6.1.1.12) (Aspartyl-tRNA synthetase) (AspRS) (P21889)
Organism: Escherichia coli (strain K12)
Function: Catalyzes the attachment of L-aspartate to tRNA(Asp) in a two-step reaction: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp). Also mischarges tRNA(Asp) with D-aspartate, although it is a poor substrate.
Subcellular location: Cytoplasm.
Interaction partners:
- Histidine--tRNA ligase
- Dihydroneopterin triphosphate diphosphatase
- Probable transcriptional regulatory protein YebC
- Arginine--tRNA ligase
- Alanine--tRNA ligase
- Valine--tRNA ligase
- Glutamate--tRNA ligase
- Threonine--tRNA ligase
- Proline--tRNA ligase
- Tyrosine--tRNA ligase
Sequence:
MRTEYCGQLRLSHVGQQVTLCGWVNRRRDLGSLIFIDMRDREGIVQVFFDPDRADALKLASELRNEFCIQVTGTVRARDEKNINRDMATGEIEVLASSLTIINRADVLPLDSNHVNTEEARLKYRYLDLRRPEMAQRLKTRAKITSLVRRFMDDHGFLDIETPMLTKATPEGARDYLVPSRVHKGKFYALPQSPQLFKQLLMMSGFDRYYQIVKCFRDEDLRADRQPEFTQIDVETSFMTAPQVREVMEALVRHLWLEVKGVDLGDFPVMTFAEAERRYGSDKPDLRNPMELTDVADLLKSVEFAVFAGPANDPKGRVAALRVPGGASLTRKQIDEYGNFVKIYGAKGLAYIKVNERAKGLEGINSPVAKFLNAEIIEDILDRTAAQDGDMIFFGADNKKIVADAMGALRLKVGKDLGLTDESKWAPLWVIDFPMFEDDGEGGLTAMHHPFTSPKDMTAAELKAAPENAVANAYDMVINGYEVGGGSVRIHNGDMQQTVFGILGINEEEQREKFGFLLDALKYGTPPHAGLAFGLDRLTMLLTGTDNIRDVIAFPKTTAAACLMTEAPSFANPTALAELSIQVVKKAENN
Protein: Glutathione reductase (GR) (GRase) (EC 1.8.1.7) (P78965)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Maintains high levels of reduced glutathione in the cytosol.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16950927}. Mitochondrion {ECO:0000269|PubMed:16950927}.
Interaction partners:
- Pyruvate dehydrogenase E1 component subunit beta, mitochondrial
- Glutathione synthetase large chain
- Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex, mitochondrial
- 2-oxoglutarate dehydrogenase, mitochondrial
- Glutathione S-transferase 3
- Glutathione S-transferase 2
- Glutathione hydrolase proenzyme 1
- Glutathione hydrolase proenzyme 2
- Glutathione S-transferase 1
- Thioredoxin-1
Sequence:
MAPISKVFDYLVIGGGSGGLASARRAAKHGAKVALIEASGRLGGTCVNYGCVPKKIMWNIADLVAKMKTAKQNGFPNSQLGSFDWGMIKRKRDAYIGRLNGIYERNVNKDGVAYISGHASFVSPTEVAVDMNDGSGTQVFSAKYILIAVGGHPIWPSHIPGAEYGIDSDGFFELESQPKRVAIVGAGYIAVELAGVFAALGTETHMFIRQSKFLRKFDPIISDGIMDHFQHIGINVHTNSLEFKKVEKLPSGELCIHQQDGSTFNVDTLLWAIGRAPKIQGLRLEKAGVKTLPNGIIIADTYQRTNVPTVLSLGDVCGKLELTPVAIAAGRRLSDRLFGGIKDAHLDYEEVPSVVFAHPEAGTIGLTEQEAIDKYGESQIKVYNTKFNGLNYSMVEQEDKVPTTYKLVCAGPLQKVVGLHLVGDFSAEILQGFGVAIKMGATKSDFDSCVAIHPTSAEELVTLV
Protein: ORF-3 (O75798)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MLGSWPARTFHPGACVSRRPSAPWKHTASGKDSPDLRFSEHGVSQEFWAGGLVAVLEMTPSPSPWGTQEDPAGMCSLWVVGWCPCRGAGVRDLVLVHAGVWCKHVCAVQRDACGESRTPAPPRKGGAVTSVLCLFLIKTFPLFSYKFASCKQVHKDPPLVKSGFE
Protein: Serine/arginine-rich splicing factor 1 (Alternative-splicing factor 1) (ASF-1) (Splicing factor, arginine/serine-rich 1) (pre-mRNA-splicing factor SF2, P33 subunit) (Q07955)
Organism: Homo sapiens (Human)
Function: Plays a role in preventing exon skipping, ensuring the accuracy of splicing and regulating alternative splicing. Interacts with other spliceosomal components, via the RS domains, to form a bridge between the 5'- and 3'-splice site binding components, U1 snRNP and U2AF. Can stimulate binding of U1 snRNP to a 5'-splice site-containing pre-mRNA. Binds to purine-rich RNA sequences, either the octamer, 5'-RGAAGAAC-3' (r=A or G) or the decamers, AGGACAGAGC/AGGACGAAGC. Binds preferentially to the 5'-CGAGGCG-3' motif in vitro. Three copies of the octamer constitute a powerful splicing enhancer in vitro, the ASF/SF2 splicing enhancer (ASE) which can specifically activate ASE-dependent splicing. Isoform ASF-2 and isoform ASF-3 act as splicing repressors. May function as export adapter involved in mRNA nuclear export through the TAP/NXF1 pathway.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:12215544, ECO:0000269|PubMed:20308322, ECO:0000269|PubMed:24449914, ECO:0000269|PubMed:9420331}. Nucleus speckle {ECO:0000269|PubMed:12215544, ECO:0000269|PubMed:20308322, ECO:0000269|PubMed:24449914, ECO:0000269|PubMed:24644279, ECO:0000269|PubMed:9420331}. Note=In nuclear speckles. Shuttles between the nucleus and the cytoplasm (PubMed:12215544, PubMed:20308322, PubMed:24449914, PubMed:9420331). Nuclear import is mediated via interaction with TNPO3 (PubMed:24449914). {ECO:0000269|PubMed:12215544, ECO:0000269|PubMed:20308322, ECO:0000269|PubMed:24449914, ECO:0000269|PubMed:9420331}.
Interaction partners:
- SRSF protein kinase 1
- Protein mago nashi homolog
- Eukaryotic initiation factor 4A-III
- Serine/arginine-rich splicing factor 10
- RNA-binding protein 8A
- Splicing factor U2AF 65 kDa subunit
- U1 small nuclear ribonucleoprotein 70 kDa
- Serine/arginine-rich splicing factor 7
- Splicing factor U2AF 35 kDa subunit
- Transformer-2 protein homolog beta
Sequence:
MSGGGVIRGPAGNNDCRIYVGNLPPDIRTKDIEDVFYKYGAIRDIDLKNRRGGPPFAFVEFEDPRDAEDAVYGRDGYDYDGYRLRVEFPRSGRGTGRGGGGGGGGGAPRGRYGPPSRRSENRVVVSGLPPSGSWQDLKDHMREAGDVCYADVYRDGTGVVEFVRKEDMTYAVRKLDNTKFRSHEGETAYIRVKVDGPRSPSYGRSRSRSRSRSRSRSRSNSRSRSYSPRRSRGSPRYSPRHSRSRSRT
Protein: Protein SSXT (Protein SYT) (Synovial sarcoma translocated to X chromosome protein) (Q15532)
Organism: Homo sapiens (Human)
Function: Appears to function synergistically with RBM14 as a transcriptional coactivator. Isoform 1 and isoform 2 function in nuclear receptor coactivation. Isoform 1 and isoform 2 function in general transcriptional coactivation. Component of SWI/SNF chromatin remodeling subcomplex GBAF that carries out key enzymatic activities, changing chromatin structure by altering DNA-histone contacts within a nucleosome in an ATP-dependent manner.
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
- SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily E member 1
- B-cell CLL/lymphoma 7 protein family member C
- SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily A member 4
- SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily A member 2
- SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily B member 1
- AT-rich interactive domain-containing protein 1A
- SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily D member 2
- SWI/SNF complex subunit SMARCC1
- SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily D member 1
- Actin-like protein 6A
Sequence:
MSVAFAAPRQRGKGEITPAAIQKMLDDNNHLIQCIMDSQNKGKTSECSQYQQMLHTNLVYLATIADSNQNMQSLLPAPPTQNMPMGPGGMNQSGPPPPPRSHNMPSDGMVGGGPPAPHMQNQMNGQMPGPNHMPMQGPGPNQLNMTNSSMNMPSSSHGSMGGYNHSVPSSQSMPVQNQMTMSQGQPMGNYGPRPNMSMQPNQGPMMHQQPPSQQYNMPQGGGQHYQGQQPPMGMMGQVNQGNHMMGQRQIPPYRPPQQGPPQQYSGQEDYYGDQYSHGGQGPPEGMNQQYYPDGHNDYGYQQPSYPEQGYDRPYEDSSQHYYEGGNSQYGQQQDAYQGPPPQQGYPPQQQQYPGQQGYPGQQQGYGPSQGGPGPQYPNYPQGQGQQYGGYRPTQPGPPQPPQQRPYGYDQGQYGNYQQ
Protein: NEDD8-conjugating enzyme Ubc12 (EC 2.3.2.34) (NEDD8 carrier protein) (Ubiquitin-conjugating enzyme E2 M) (P61081)
Organism: Homo sapiens (Human)
Function: Accepts the ubiquitin-like protein NEDD8 from the UBA3-NAE1 E1 complex and catalyzes its covalent attachment to other proteins. The specific interaction with the E3 ubiquitin ligase RBX1, but not RBX2, suggests that the RBX1-UBE2M complex neddylates specific target proteins, such as CUL1, CUL2, CUL3 and CUL4. Involved in cell proliferation.
Interaction partners:
- NEDD8-activating enzyme E1 regulatory subunit
- NEDD8-activating enzyme E1 catalytic subunit
- Ubiquitin-like protein NEDD8
- E3 ubiquitin-protein ligase RBX1
- DCN1-like protein 1
- Cullin-1
- Ubiquitin-like modifier-activating enzyme 1
- DCN1-like protein 3
- DCN1-like protein 2
- Cullin-3
Sequence:
MIKLFSLKQQKKEEESAGGTKGSSKKASAAQLRIQKDINELNLPKTCDISFSDPDDLLNFKLVICPDEGFYKSGKFVFSFKVGQGYPHDPPKVKCETMVYHPNIDLEGNVCLNILREDWKPVLTINSIIYGLQYLFLEPNPEDPLNKEAAEVLQNNRRLFEQNVQRSMRGGYIGSTYFERCLK
Protein: T. brucei spp.-specific protein (Q389L1)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MVARFLWTFPYASVKHPHIGCVSVVFPRSGTDPRVSFVFGRHAGGEPLGGWWGVSGFAAGASPPGREVLEFSTTVSTYLVCLCSVRGLGDRAYFRFRWVSYPCKGKRYWPSVGSPWPEAPLSTIWSCCAPTVPRPLTPVVHDRQLLC
Protein: Potassium channel toxin alpha-KTx 11.2 (Parabutoxin-2) (PBTx2) (P60165)
Organism: Parabuthus villosus (Black hairy thick-tailed scorpion)
Function: Binds and inhibits voltage-sensitive potassium channels. Inhibits the vertebrate potassium channel Kv1.1/KCNA1 with low affinity.
Subcellular location: Secreted {ECO:0000269|PubMed:10542442}.
Interaction partners:
Sequence:
DEEPKETCSDEMCVIYCKGEEYSTGVCDGPQKCKCSD
Protein: Vacuolar fusion protein MON1 homolog (Dmon1) (Q9VR38)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cytoplasm, cytosol {ECO:0000269|PubMed:23418349}. Note=There is no evidence of association with endosomal membranes, however this association may be transient (Probable). Binds phospholipids with a preference for phosphatidylinositol monophosphates, including phosphatidylinositol 3-phosphate (PtdIns[3]P) that is enriched in early endosomal and autophagosomal membranes (PubMed:27559127). {ECO:0000269|PubMed:27559127, ECO:0000305|PubMed:23418349}.
Interaction partners:
- Vacuolar fusion protein CCZ1 homolog
- Ras-related protein Rab7
- Vacuolar protein sorting-associated protein 41 homolog
- Ras-related protein Rab5
- Vacuolar protein sorting-associated protein 39 homolog
- Rabaptin-5-associated exchange factor for Rab5
- Regulator of MON1-CCZ1 complex
- Vacuolar protein sorting-associated protein 11 homolog
- Vacuolar protein sorting-associated protein 16 homolog
- Guanine nucleotide exchange factor MSS4 homolog
Sequence:
MEVEQTSVRSDTNSTCEYLDAEGDPESPNLYQEADPDQEAEQQNHSIISELRDGLGTMRDNSALSPEPGQENKGLAASVESLALSTSTSAKTEDSIGGGLEEEYDYQHDSLWQGQKKHIFILSEAGKPIFSLHGNEDKLATLFGVIQALVSFVQMGQDAITSIHAGGIKFAFMQRSSLILVAASRSNMSVQQLQLQLGDVYNQILSILTYSHMTKIFERRKNFDLRRLLSGSERLFYNLLANDSSSAKVSNNIFTFLTNSIRVFPLPTTIRSQITSAIQSNCSKIKNLVFAVLIANNKLIALVRMKKYSIHPADLRLIFNLVECSESFKSSENWSPICLPKFDMNGYLHAHVSYLADDCQACLLLLSVDRDAFFTLAEAKAKITEKLRKSHCLEAINEELQQPFNAKLYQQVVGIPELRHFLYKPKSTAQLLCPMLRHPYKSLTELERLEAIYCDLLHRIHNSSRPLKLIYEMKEREVVLAWATGTYELYAIFEPVVDKATVIKYVDKLIKWIEKEYDVYFIRNHATF
Protein: Rubicon autophagy regulator (H0Y6E6)
Organism: Homo sapiens (Human)
Subcellular location: Late endosome {ECO:0000256|ARBA:ARBA00004603}.
Interaction partners:
Sequence:
XREHWQLLGNLKTTVEGLVSTNSPNVWSKYGGLERLCRDMQSILYHGLIRDQACRRQTDYWQFVKDIRWLSPHSALHVEKFISVHENDQSSADGASERAVAELWLQHSLQYHCLSAQLRPLLGDRQYIRKFYTDAAFLLSDAHVTAMLQCLEAVEQNNPRLLAQIDASMFARKHESPLLVTKSQSLTALPSSTYTPPNSYAQHSYFGSFSSLHQSVPNNGSERRSTSFPLSGPPRKPQESRGHVSPAEDQTIQAPPVSVSALARDSPLTPNEMSSSTLTSPIEASWVSSQNDSPGDASEGPEYLAIGNLDPRGRTASCQSHSSNAESSSSNLFSSSSSQKPDSAASSLGDQEGGGESQLSSVLRRSSFSEGQTLTVTSGAKKSHIRSHSDTSIASRGAPGGPRNITIIVEDPIAEGGRYLCSGEGMFRRPSEGQSLISYLSEQDFGSCADLEKENAHFSISESLIAAIELMKCNMMSQCLEEEEVEEEDSDREIQELKQKIRLRRQQIRTKNLLPMYQEAEHGSFRVTSSSSQFSSRDSAQLSDSGSADEVDEFEIQDADIRRNTASSSKSFVSSQSFSHCFLHSTSAEAVAMGLLKQFEGMQLPAASELEWLVPEHDAPQKLLPIPDSLPISPDDGQHADIYKLRIRVRGNLEWAPPRPQIIFNVHPAPTRKIAVAKQNYRCAGCGIRTDPDYIKRLRYCEYLGKYFCQCCHENAQMAIPSRVLRKWDFSKYYVSNFSKDLLIKIWNDPLFNVQDINSALYRKVKLLNQVRLLRVQLCHMKNMFKTCRLAKELLDSFDTVPGHLTEDLHLYSLNDLTATRKGELGPRLAELTRAGATHVERCMLCQAKGFICEFCQNEDDIIFPFELHKCRTCEECKACYHKACFKSGSCPRCERLQARREALARQSLESYLSDYEEEPAEALALEAAVLEAT
Protein: Origin recognition complex subunit 4 (Uncharacterized protein ORC4L) (Q53SE3)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MSSRKSKSNSLIHTECLSQVQRILRERFCRQSPHSNLFGVQVQYKHLSELLKRTALHGESNSVLIIGPRGSGKTMLINHALKELMEIEEVSENVLQVHLNGLLQINDKIALKEITRQLNLENVVGDKVFGSFAENLSFLLEALKK
Protein: Mucolipin TRP cation channel 1a (Mucolipin-1a) (A2BGV1)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004651}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}. Endosome membrane {ECO:0000256|ARBA:ARBA00004337}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004337}.
Interaction partners:
- Mucolipin 1.2
- Zgc:66433.
- Transcription factor EB
- Mucin-4
Sequence:
MAAVDPNKLDHISSEEDRLLYPVAHYGSNDCMDEYSKPRPTPVTDGWIGADPEEEELRRKLKYFFMSPCEKYQAKGRKPFKLILQILKIVIVTAQLVLFGLSNEMAVMFKEENTASFKHLFLKDYADSDDALAVYTQSDVYDHMFYAVEQYLSLADTTVGQYAYVYGVGVNGSALSLCQQYYKKGRIDPANDTFIIDPLVVTDCIGVNPLSTPTAAGTGRDYRNFTLKFHKLINVTIQFQLKAINLQTIIHNEIPDCYTFLITILLDNKAHSGKVRISLDNKASIKECRDPSVSGHPDSNARVLFDLAVALVCVFSLLLCGRSIIRGIILQNEFVKYFKTSLKRHVCWGDRMEFINGWYILLIISDLLTITGSIIKIGIELKNLSSYDECGILLGTSTLLVWVGVIRYLTFFQKYNILIVTLQAAFPNVIRFCCCVAVIYLGYCFCGWIVLGPYHVKFRSLSSVSECLFSLINGDDMFVTFSGMQESSMLVWVFSQVYLYTFISLFIYMVLSLFIALITGAYETIKHQTQEPIHITDLHAFIAECTDTPCSGKFRGIETSPCSFFCCCDRTTTYEDVLLVN
Protein: RAS guanyl-releasing protein 4 (Si:dkey-12o15.1) (Q1L9A0)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
- RAS guanyl releasing protein 2.
- RAS guanyl-releasing protein 3
- GTPase NRas
- Muscle RAS oncogene homolog
- HRas proto-oncogene, GTPase a.
- RAS-related
- RAS-related 2
- small monomeric GTPase
- Ras-related protein M-Ras
- small monomeric GTPase
Sequence:
MGFDTMNRKESKSSRKSRQEGGIKSRRPVQRRMTCPSAQEISRALQSPPAHASFRSASLDELILRCLHCFDSDGKLNRGTQLVSMTLMMHNWVVPSHIFAHKLLSLYKDCPAEKRGQRRPQICHFIRQWISQFRLMFEMDPLLEKAMGDLWALVSAEGTNSHHQLINTPYINPPVNISQTPSPLVKKRKVSLLFDHMEPDEMAEHLSYLEFKNFCNVSFLDYRSYVVHGSVRDNPALERSVMLCNGVSQWVQLMILNRHTSQQRAEVFTKFIHVAQKLRSLQNFNTLMAVIGGLCHSSISRLKDTASLLSSDVTKTLSELTELLSSYSNYSNYRRVYSECTGFKVPILGVHLKDLISLNEALPDYLEDDKINLGKLQHLYSNISDLLAIHDCTPPFEANKDLLHLLTLSLDLYYTEDEIYELSYAKEPKNPKIQPVAPVKPPVVAEWGSGVTPRLDPATISKHVKQMVDSIMKNYDLNMDGYISLEEFEKIAANFPFSFCTHESDREGEISREEITSYFMRGMSVCAKLGFNLHNLHNFHETTYKRPTFCDTCGGFLWGVIKQGYHCKDCGVNCHKHCKDVVGMECLKRLQVNSSSCPCTPGPVSGLHTKGNSWTFQSGSEEEAFVFPNGNESEHSKGQTSSDSDAEAATLSDRSTQTEPGVWTPVAKRKDRLHSQKQHPPLEKVLP
Protein: cGMP-dependent 3',5'-cyclic phosphodiesterase (EC 3.1.4.17) (Cyclic GMP-stimulated phosphodiesterase) (CGS-PDE) (cGSPDE) (O00408)
Organism: Homo sapiens (Human)
Function: cGMP-activated cyclic nucleotide phosphodiesterase with a dual-specificity for the second messengers cAMP and cGMP, which are key regulators of many important physiological processes. Has a higher efficiency with cGMP compared to cAMP. Plays a role in cell growth and migration.
Subcellular location: [Isoform PDE2A3]: Cell membrane {ECO:0000269|PubMed:19632989, ECO:0000269|PubMed:28463107}; Lipid-anchor {ECO:0000269|PubMed:19632989}.; SUBCELLULAR LOCATION: [Isoform PDE2A2]: Mitochondrion matrix {ECO:0000250|UniProtKB:Q922S4}. Mitochondrion inner membrane {ECO:0000269|PubMed:28463107}. Mitochondrion outer membrane {ECO:0000269|PubMed:28463107}.; SUBCELLULAR LOCATION: [Isoform PDE2A1]: Cytoplasm {ECO:0000269|PubMed:19632989, ECO:0000269|PubMed:28463107}.; SUBCELLULAR LOCATION: [Isoform 5]: Mitochondrion {ECO:0000305}.
Interaction partners:
- cGMP-specific 3',5'-cyclic phosphodiesterase
- Adenosine kinase
- Ectonucleotide pyrophosphatase/phosphodiesterase family member 1
- Ectonucleotide pyrophosphatase/phosphodiesterase family member 3
- Inosine triphosphate pyrophosphatase
- Adenine phosphoribosyltransferase
- Deoxycytidine kinase
- GMP reductase 1
- Guanylate kinase
- GTP:AMP phosphotransferase AK3, mitochondrial
Sequence:
MGQACGHSILCRSQQYPAARPAEPRGQQVFLKPDEPPPPPQPCADSLQDALLSLGSVIDISGLQRAVKEALSAVLPRVETVYTYLLDGESQLVCEDPPHELPQEGKVREAIISQKRLGCNGLGFSDLPGKPLARLVAPLAPDTQVLVMPLADKEAGAVAAVILVHCGQLSDNEEWSLQAVEKHTLVALRRVQVLQQRGPREAPRAVQNPPEGTAEDQKGGAAYTDRDRKILQLCGELYDLDASSLQLKVLQYLQQETRASRCCLLLVSEDNLQLSCKVIGDKVLGEEVSFPLTGCLGQVVEDKKSIQLKDLTSEDVQQLQSMLGCELQAMLCVPVISRATDQVVALACAFNKLEGDLFTDEDEHVIQHCFHYTSTVLTSTLAFQKEQKLKCECQALLQVAKNLFTHLDDVSVLLQEIITEARNLSNAEICSVFLLDQNELVAKVFDGGVVDDESYEIRIPADQGIAGHVATTGQILNIPDAYAHPLFYRGVDDSTGFRTRNILCFPIKNENQEVIGVAELVNKINGPWFSKFDEDLATAFSIYCGISIAHSLLYKKVNEAQYRSHLANEMMMYHMKVSDDEYTKLLHDGIQPVAAIDSNFASFTYTPRSLPEDDTSMAILSMLQDMNFINNYKIDCPTLARFCLMVKKGYRDPPYHNWMHAFSVSHFCYLLYKNLELTNYLEDIEIFALFISCMCHDLDHRGTNNSFQVASKSVLAALYSSEGSVMERHHFAQAIAILNTHGCNIFDHFSRKDYQRMLDLMRDIILATDLAHHLRIFKDLQKMAEVGYDRNNKQHHRLLLCLLMTSCDLSDQTKGWKTTRKIAELIYKEFFSQGDLEKAMGNRPMEMMDREKAYIPELQISFMEHIAMPIYKLLQDLFPKAAELYERVASNREHWTKVSHKFTIRGLPSNNSLDFLDEEYEVPDLDGTRAPINGCCSLDAE
Protein: F-box only protein 44 (F-box only protein 6a) (Q8BK26)
Organism: Mus musculus (Mouse)
Function: Substrate-recognition component of the SCF (SKP1-CUL1-F-box protein)-type E3 ubiquitin ligase complex.
Interaction partners:
- S-phase kinase-associated protein 1
- Cullin-4B
- Cullin-1
- DNA damage-binding protein 1
Sequence:
MAVGNINELPENILLELFIHIPARQLLLRCRPVCSLWRDLIDLVTLWKRKCLQEGFITEDWDQPVADWKIFYFLRSLQRNLLHNPCAEEGFEFWSLDVNGGDEWKVEDLSKDQRKEFPNDQVKKYFVTSYYTCLKSQVVDLKAEGYWEELMDTTRPDIEVKDWFAARPDCGSKYQLCVQLLSSAHAPLGTFQPDPVMIQQKSDAKWSEVSHTFSNYPPGVRYIWFQHGGVDTHYWAGWYGPRVTNSSITIGPPLP