wanglab/gogpt-training-data huggingface dataset:
Protein: Aquaporin (Q18352)
Organism: Caenorhabditis elegans
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
Sequence:
MVEDEKDYTIYSKCAAEFIAVLLFVYIGSMQAAGVFLHDGVLHAAFAHGVAIFVLAATFGGVSGAHINPAVTFGIALVGRISPIHAVCYVVSQLLGSVFGALLVRISLPYKMYNVISAGATLCGKGYNWQEGLTAEIVTTYILVQTVLLCAVDTDKNRLAPLAIGFSLIIEILAAGAISGASMNPARSFGPNIMGQVFLKPEHLDAQYMYWNYHWIYYIGPIIGAFIAAGVYRMFFARDYRVLA
Protein: Taz1-interacting factor 1 (Protein taf1) (Autophagy-related protein 11) (Cytoplasm to vacuole targeting protein 9) (O14261)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Involved in cytoplasm to vacuole transport (Cvt), pexophagy, mitophagy and nucleophagy. Recruits mitochondria for their selective degradation via autophagy (mitophagy) during starvation. Works as scaffold proteins that recruit ATG proteins to the preautophagosome (PAS), the site of vesicle/autophagosome formation. Required for atg9 anterograde transport from the mitochondria to the PAS (By similarity). Required for nitrogen starvation-induced sexual development and for entering the dormant G0 state (By similarity).
Subcellular location: Preautophagosomal structure membrane {ECO:0000269|PubMed:23950735}; Peripheral membrane protein {ECO:0000269|PubMed:23950735}. Vacuole membrane {ECO:0000269|PubMed:23950735}; Peripheral membrane protein {ECO:0000269|PubMed:23950735}.
Interaction partners:
- Serine/threonine-protein kinase atg1
- Autophagy protein 13
- Autophagy-related protein 17
- Autophagy-related protein 9
- Autophagy-related protein 101
- Autophagy-related protein 8
- Dynamin-related protein dnm1
- Vacuolar protein sorting-associated protein atg6
- Ubiquitin-like protein ATG12
- Ubiquitin-like modifier-activating enzyme atg7
Sequence:
MRFRLNDSFSGKSWTIDNVQWTPQNLVAWIMELNIGLSDEAKLLLPNGMSLNETVLNSESDVVIYVLDQNLLTFTYDGDKIPSIPSLKGQPISNVLTGIIADSSSDQWKDKISKCLSLLSDILESSSKIHNQLSVCHDEYSTSIVSPEVAMNYLQRRQSGMKDLLFVFYERLDRVSVSDLLHDFLALPTGSLPITPLKILSTNWTKLDSWLNSISARYAEAQKRVQQCIGAANSIIVSPFKEVPSIKEGDDAYYHLRSVAQDAANILQEILKIESTSTTSQIKPKCNYETEITDCMEKLQSNLSELKSSRKSSLISLKSFWLSFYKVSLRYDALYEYLRQIAEELDRSKFVLSQSRNIFSLYIDILMEALRRTEWQESYNVSHDSSLPLDQEKELSLRKSWLSHFSNLLFNHGQLKYLPVLTRDEISNYLLNIQAHPNYQTFHQMLSNRLSEYLGFPGSPREAVSNTVQANNSLHEKLAMYQNRCNNLEAMLSHQNGFNYNINNDGLSPNAPHPPINEQSNSSQPFYRVSPSIVPLNVIRKLTNRKTSFTDSHILRLQDEVNQLRNELDLVNKRNEDLLIELQGKEEKIQYLETENEEVLQKYENLQEELSSTRKLLTKNEAAVAEQQSNEEMHSNEPNILNLYSVFEGKVDSLQELYNAFKLQLTSLKQKGEYATLAKDAEAVQHIIEERDYALAEKADLLKLSENRKEQCKILTQKLYTIVFRCNELQSVLRECVTQPGFDSDNERDGHASIPDRQIEFNSKDLQYLYWMDGEDADRNFQEFLNRMSSLDFDSFHNFVVSVLTQAHNHELRWKREFQSNRDKALKAILDSQSKVSLRNFKQGSLVLFLPTRRTAGNKKVWAAFNVNAPHYYLNTQPHLKLESRDWMLGRVTSIEDRTADDSTDKWLRLPSGTIWHLVEAIDERF
Protein: Protein GPR15LG (Protein GPR15 ligand) (Protein GPR15L) (A0A0B4J1N3)
Organism: Mus musculus (Mouse)
Function: Highly cationic protein that has multiple functions. Acts as a chemotactic factor that mediates lymphocytes recruitment to epithelia through binding and activation of the G-protein coupled receptor GPR15. May be a tumor suppressor; together with SUSD2 has a growth inhibitory effect on colon cancer cells which includes G1 cell cycle arrest (By similarity). May regulate keratinocyte proliferation. In addition, through activation of Mas-related G protein-coupled receptors (MRGPRs) contributes to pruritogenesis by activating itch-selective sensory neurons and mast cells degranulation.
Subcellular location: Secreted {ECO:0000250|UniProtKB:Q6UWK7}.
Interaction partners:
- G-protein coupled receptor 15
Sequence:
MRLLALSGLLCMLLLCFCIFSSEGRRHPAKSLKLRRCCHLSPRSKLTTWKGNHTRPCRLCRNKLPVKSWVVPGALPQI
Protein: Putative amastin-like surface protein (Q4Q335)
Organism: Leishmania major
Interaction partners:
Sequence:
MKCSIPLVVYVVVQFVAFLLVLVGTPLDMFRAHNRPGVAQCLTLFGFKLDCKGLQYDQTVDMQWIECPARITLFRLAQGCAIISILVYGAAFVLGLVLLYGCTIHRWVCLALNIVGAVTLFIVWVAIVVTYNKDDGQKCPKVRDTGYRLGTGFALLVAAWILDILNIIFLLLPCTVPATKANEKPESPTAQE
Protein: Transcription factor Sp8 (Q6P0J3)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Function: Transcription factor which plays a key role in limb development. Positively regulates FGF8 expression in the apical ectodermal ridge (AER) and contributes to limb outgrowth in embryos.
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
- Rh50-like protein
Sequence:
MLAATCNKIGSPSPSPSSISDNSSSFGKGFHPWKRATASSCSLGSSLSSFTRNGGGLSDSFGTNTSTGSSAFSLTSGTSSNSHFGNDYSVFQTSVSNNSQEPSHQPMFISKVHTSVDSLQSIYPRMSVAHPYESWFKSSHPGIPTGDVGTTGASAWWDVGAGWIDVQNPNGAALQTSLHSGGLQTSLHSPLGGYNSDYSSLSHSAFSTSASPHLLTTGQHLMDGFKPVLSSYPDSSPSPLGGAGGSMLTGGPTASLAGSPRSSARRYSGRATCDCPNCQEAERLGPAGASLRRKGLHSCHIPGCGKVYGKTSHLKAHLRWHTGERPFVCNWLFCGKRFTRSDELQRHLRTHTGEKRFACPVCNKRFMRSDHLSKHVKTHSAGGSSGSGSGASGGKRGSDTDSEHSVPGSPSCHSPDLLQAPESVPTTGMNGRASSLD
Protein: Argininosuccinate synthase (EC 6.3.4.5) (Citrulline--aspartate ligase) (Q5ZJ23)
Organism: Gallus gallus (Chicken)
Function: One of the enzymes of the urea cycle, the metabolic pathway transforming neurotoxic amonia produced by protein catabolism into inocuous urea in the liver of ureotelic animals. Catalyzes the formation of arginosuccinate from aspartate, citrulline and ATP and together with ASL it is responsible for the biosynthesis of arginine in most body tissues.
Subcellular location: Cytoplasm, cytosol {ECO:0000250|UniProtKB:P00966}.
Interaction partners:
- Ornithine transcarbamylase, mitochondrial
- Argininosuccinate lyase
- Uncharacterized protein.
- Ornithine aminotransferase
- Delta-1 crystallin
- Asparagine synthetase
- Adenylosuccinate synthetase isozyme 2
- Adenylosuccinate synthetase isozyme 1
- Nitric oxide synthase, inducible
- Nitric oxide synthase
Sequence:
MAEPRDTVVLAYSGGLDTSCILVWLKEQGYTVIAFLANIGQTEDFDAAQKKALALGAKKVYIQDVCREFVEDFIWPAVRANALYEDRYMLGSALARPCIARHLVLIAQEEGARYIAHGATGKGNDQVRFELGCYALCPSIKVIAPWRMPEFYQRFPGRRELMEYAQKHGIPVPVTPKAPWSMDENLMHISYEAGILENPKNRAPLDLYTKTCNPTTSPDVPDELEIEFEKGVPVKVTNTRNGVTHRSALELFVYLNDIASKHGVGRVDIVENRFVGMKSRGIYETPAGTILYHAHLDIEAFTMDREVRKIKQGLSLKFSELVYNGFWYSPECEFLKHCIARSQQAVAGTVHVSVFKGQVYVLGRESPHSLYNEELVSMDVQGDYEPADATGFININALRLKEYHRLQSKVSTKQDE
Protein: Serine/threonine-protein phosphatase 4 catalytic subunit (PP4C) (Pp4) (EC 3.1.3.16) (A6H772)
Organism: Bos taurus (Bovine)
Function: Protein phosphatase that is involved in many processes such as microtubule organization at centrosomes, maturation of spliceosomal snRNPs, apoptosis, DNA repair, tumor necrosis factor (TNF)-alpha signaling, activation of c-Jun N-terminal kinase MAPK8, regulation of histone acetylation, DNA damage checkpoint signaling, NF-kappa-B activation and cell migration. The PPP4C-PPP4R1 PP4 complex may play a role in dephosphorylation and regulation of HDAC3. The PPP4C-PPP4R2-PPP4R3A PP4 complex specifically dephosphorylates H2AX phosphorylated on Ser-140 (gamma-H2AX) generated during DNA replication and required for DNA double strand break repair. Dephosphorylates NDEL1 at CDK1 phosphorylation sites and negatively regulates CDK1 activity in interphase. In response to DNA damage, catalyzes RPA2 dephosphorylation, an essential step for DNA repair since it allows the efficient RPA2-mediated recruitment of RAD51 to chromatin.
Subcellular location: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250}.
Interaction partners:
- Protein phosphatase 4 regulatory subunit 2
- SMEK homolog 1
- Serine/threonine-protein phosphatase 4 regulatory subunit 1
- Protein phosphatase 4 regulatory subunit 3C
- Serine/threonine-protein phosphatase 2A activator
- Protein phosphatase 4 regulatory subunit 3B
- Calcineurin subunit B type 1
- IGBP1 protein
- IGBP1 protein
- CREB-regulated transcription coactivator 2
Sequence:
MAEISDLDRQIEQLRRCELIKESEVKALCAKAREILVEESNVQRVDSPVTVCGDIHGQFYDLKELFRVGGDVPETNYLFMGDFVDRGFYSVETFLLLLALKVRYPDRITLIRGNHESRQITQVYGFYDECLRKYGSVTVWRYCTEIFDYLSLSAIIDGKIFCVHGGLSPSIQTLDQIRTIDRKQEVPHDGPMCDLLWSDPEDTTGWGVSPRGAGYLFGSDVVAQFNAANDIDMICRAHQLVMEGYKWHFNETVLTVWSAPNYCYRCGNVAAILELDEHLQKDFIIFEAAPQETRGIPSKKPVADYFL
Protein: FI18412p1 (Prestin) (Q9VVM6)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
- Tetraspanin
- Anion exchange protein
- Misfire, isoform F
Sequence:
MPSDKESPETKPLNNNNTNGNGGSVPSKPKIQPKYSIHRDVLTHEVVIKQTGYAARDKSIPSSLRNCWRSWNFFALFTGVIPILQWLPQYSPRRDLPGDIIAGFTVAIMNIPHGMAYGILAGVSAGNGLYMAVFPVLAYMFLGTSKHISIGTFAVASMMTAKVVDTYANVDDHHQILPINAFGLQSNGTATASPLLLINSSALADSVSSTTISPFQLLNSTLNADPITKIEVATSLALTVGIVNLLMAFLRLGTLSSLLSEPLVNGFTTAAACHVVTAQLKDVLGISVPRHKGAFKIIYTVIDVIKGVPQTNLVNFGFCMAVIAFMMICNEILKPRLSKKCRFPLPAELIMVIGGTLISKWFNLYVDYNVNPVGKIPSGLPEPVLPRLDLVPKVAVDSIAIAIVTYSIIMSMGLTFAKKHGYEVRPNQELFAMGIGNMVGGCFSCIPMACSLSRSVIQDQTGGVSQIASLVSASLVVVTLMWIGPFFSSLPRCVLAGVIIVALKPMFMQAKELKKFSKQGKLEMFTWISTFLCVVIIDIDIGLLIGICISLLALYIKGLKPYSCLLGYMPEAPGIYMDLNQHRNAMQVPEVRIFRYSGSLNFATSLFFRRALYEAVGLDKIPLTKVSSSNSNSPSKGSKSSYSPVSQNGGKAINGKLEETSGAFKVLVLDFSMLGHIDVAGCRTLTDLSKELKVRGARLLLASPVDRVYDTLVHSMALSEGPFEIFPTLHDCVEYANACRTA
Protein: RNA polymerase II subunit A C-terminal domain phosphatase SSU72 (CTD phosphatase SSU72) (EC 3.1.3.16) (Q9NP77)
Organism: Homo sapiens (Human)
Function: Protein phosphatase that catalyzes the dephosphorylation of the C-terminal domain of RNA polymerase II. Plays a role in RNA processing and termination. Plays a role in pre-mRNA polyadenylation via its interaction with SYMPK.
Subcellular location: Nucleus. Cytoplasm. Note=Predominantly in the cytosol.
Interaction partners:
- WD repeat-containing protein 82
- Symplekin
- Cleavage and polyadenylation specificity factor subunit 3
- Pre-mRNA cleavage complex 2 protein Pcf11
- Transcription initiation factor IIB
- pre-mRNA 3' end processing protein WDR33
- Cleavage and polyadenylation specificity factor subunit 2
- Cleavage stimulation factor subunit 2
- DNA-directed RNA polymerase II subunit RPB1
- Cleavage and polyadenylation specificity factor subunit 1
Sequence:
MPSSPLRVAVVCSSNQNRSMEAHNILSKRGFSVRSFGTGTHVKLPGPAPDKPNVYDFKTTYDQMYNDLLRKDKELYTQNGILHMLDRNKRIKPRPERFQNCKDLFDLILTCEERVYDQVVEDLNSREQETCQPVHVVNVDIQDNHEEATLGAFLICELCQCIQHTEDMENEIDELLQEFEEKSGRTFLHTVCFY
Protein: Growth hormone (Q0QBC0)
Organism: Ovis aries (Sheep)
Subcellular location: Secreted {ECO:0000256|ARBA:ARBA00004613, ECO:0000256|RuleBase:RU003618}.
Interaction partners:
Sequence:
MMAAGPRTSLLLAFTLLCLPWTQVVGAFPAMSLSGLFANAVLRAQHLHQLAADTFKEFERTYIPEGQRYSIQNTQVALCFSETIPAPTGKNEAQQKSDLELLRISLLLIQSWLGPLQFLSRVFTNSLVFGTSDRVYEKLKDLEEGILALMRLEDVTPRAGQILKQTYDKFDTNMRSDDALLKNYGLLSCFRKDLHKTETYLRVMKCRRFGEASSAF
Protein: Guanine nucleotide-binding protein subunit alpha (G5EGU1)
Organism: Caenorhabditis elegans
Interaction partners:
- 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase beta egl-8
- Guanine nucleotide-binding protein subunit beta-1
- Guanine nucleotide-binding protein subunit beta-2
- Guanine nucleotide-binding protein subunit gamma
- G-protein coupled receptors family 1 profile domain-containing protein
- G-protein coupled receptors family 1 profile domain-containing protein
- G protein gamma domain-containing protein
- Muscarinic acetylcholine receptor gar-3
- Muscarinic acetylcholine receptor gar-2
- CRAL-TRIO domain-containing protein
Sequence:
MACCLSEEAREQKRINQEIEKQLQRDKRNARRELKLLLLGTGESGKSTFIKQMRIIHGQGYSEEDKRAHIRLVYQNVFMAIQSMIRAMDTLDIKFGNESEELQEKAAVVREVDFESVTSFEEPYVSYIKELWEDSGIQECYDRRREYQLTDSAKYYLSDLRRLAVPDYLPTEQDILRVRVPTTGIIEYPFDLEQIIFRMVDVGGQRSERRKWIHCFENVTSIMFLVALSEYDQVLVECDNENRMEESKALFRTIITYPWFTNSSVILFLNKKDLLEEKILYSHLADYFPEYDGPPRDPIAAREFILKMFVDLNPDADKIIYSHFTCATDTENIRFVFAAVKDTILQHNLKEYNLV
Protein: KiSS-1 receptor (KiSS-1R) (G-protein coupled receptor 54) (G-protein coupled receptor OT7T175) (rOT7T175) (Kisspeptins receptor) (Metastin receptor) (Q924U1)
Organism: Rattus norvegicus (Rat)
Function: Receptor for metastin, a C-terminally amidated peptide of KiSS1. KiSS1 is a metastasis suppressor protein. Activation of the receptor inhibits cell proliferation and cell migration, key characteristics of tumor metastasis. The receptor is essential for normal gonadotropin-released hormone physiology and for puberty. The hypothalamic KiSS1/KISS1R system is a pivotal factor in central regulation of the gonadotropic axis at puberty and in adulthood. Analysis of the transduction pathways activated by the receptor identifies coupling to phospholipase C and intracellular calcium release through pertussis toxin-insensitive G(q) proteins.
Subcellular location: Cell membrane; Multi-pass membrane protein.
Interaction partners:
- Metastasis-suppressor KiSS-1
- Guanine nucleotide-binding protein G
- Tachykinin-3
- Pro-FMRFamide-related neuropeptide VF
- Beta-arrestin-1
- Beta-arrestin-2
- Guanine nucleotide-binding protein subunit alpha-11
- Phosphatidylinositol 3-kinase regulatory subunit alpha
- Phosphatidylinositol 4,5-bisphosphate 3-kinase catalytic subunit beta isoform
- Phosphatidylinositol 3-kinase regulatory subunit beta
Sequence:
MAAEATLGPNVSWWAPSNASGCPGCGVNASDGPGSAPRPLDAWLVPLFFAALMLLGLVGNSLVIFVICRHKHMQTVTNFYIANLAATDVTFLLCCVPFTALLYPLPTWVLGDFMCKFVNYIQQVSVQATCATLTAMSVDRWYVTVFPLRALHRRTPRLALTVSLSIWVGSAAVSAPVLALHRLSPGPHTYCSEAFPSRALERAFALYNLLALYLLPLLATCACYGAMLRHLGRAAVRPAPTDGALQGQLLAQRAGAVRTKVSRLVAAVVLLFAACWGPIQLFLVLQALGPSGAWHPRSYAAYALKIWAHCMSYSNSALNPLLYAFLGSHFRQAFCRVCPCGPQRQRRPHASAHSDRAAPHSVPHSRAAHPVRVRTPEPGNPVRRSPSVQDEHTAPL
Protein: Myotrophin (G9BZS8)
Organism: Sus scrofa (Pig)
Interaction partners:
Sequence:
MCNKEFMWALKNGDLDEVKDYVAKGEDVNRTLEGGRKPLHYAADCGQLEILEFLLLKGADINAPDEHHITPLLSAVYEGHVSCVKLLLSKGADKTVKGPDGLTAFEATDNQTIKALLQ
Protein: Protein transport protein SEC23 (Q9U2Z1)
Organism: Caenorhabditis elegans
Subcellular location: Cytoplasmic vesicle, COPII-coated vesicle membrane {ECO:0000256|RuleBase:RU365030}; Peripheral membrane protein {ECO:0000256|RuleBase:RU365030}; Cytoplasmic side {ECO:0000256|RuleBase:RU365030}. Endoplasmic reticulum membrane {ECO:0000256|RuleBase:RU365030}; Peripheral membrane protein {ECO:0000256|RuleBase:RU365030}; Cytoplasmic side {ECO:0000256|RuleBase:RU365030}.
Interaction partners:
- Protein transport protein Sec24C
- WD_REPEATS_REGION domain-containing protein
- Yeast SEC homolog
- Small COPII coat GTPase SAR1
- Protein SEC13 homolog
- Protein transport protein sec-16A.1
- Vesicle-trafficking protein SEC22b
- Protein transport protein sec16
- ANK_REP_REGION domain-containing protein
- WD_REPEATS_REGION domain-containing protein
Sequence:
MATWEEYLGAQQANDGVQFTWNMWPHSRVDSQKLVVPLTCFFTPLKERPSTEVAQPPLEYDPVLCQKASCKAILNPLCAVDYRAKIWMCPFCNNRNPFPAHYAAIAEDNRPPELYPQFTTIEYTLRKATTMPPIFVFVVDTCMTAEELKSLKECLQTALSLLPADALVGLITYGRMVQLHELNTQGISRSYVFKGTKEVTAKQIKDVMAGGGLSQRPAAGAPGAPAGAPGAPMAMGSGAAPLGQLPGSGLPGGLPRGGGPPLPGAAQGIVAPGGGAPVPHAPANKFLQPISECDESINDLIDQISIDRWPVPQGHRPLRATGAALAVAVTLLESCFPSTGARIMSFIGGACTHGPGAVVGEELKNPIRSWNSIKEDAAPYMKKAIKFYDGLAARIVKNGHAVDVYSCALDQTGLLEMKNMFNSSGGHVVMGDSFNSSLFKQTYQRSFDKDSAGNLKMGFNATMEVKVGAGLKIEGVLGCCASGNVRNANVSDQEMGIGGTCQWKFGAISPRTTIGVVFEIAAQHGSAIPQGGRGMVQFVTQYQHADGRKRIRVTTTCRTWADMATQQPNIAYGFDQEAAAVAIARLASFRASNENDTPEALRWLDRSLIRLCQKFGEYSKDDPNSFRLSDKFSLFPQFMFHLRRSQFLQVFNNSPDETAYYRHILFSENVLESTTMIQPVLFSYSFNGPPEPVLLDTSSILADRILLMDDYFHVLIYHGQTIAQWRKQNFHENPQYATFKQLLEAPVADATSILQERFPMPRYIVTEHEGSQARFLLSKVNPSLTHNNPYANEAGSAVFTDDVSLQVFMEHLKKLSSSSST
Protein: RNA demethylase ALKBH9B (AtALKBH9B) (EC 1.14.11.53) (Alkylated DNA repair protein alkB homolog 9B) (Alpha-ketoglutarate-dependent dioxygenase alkB homolog 9B) (Q9SL49)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Dioxygenase that demethylates RNA by oxidative demethylation: specifically demethylates N(6)-methyladenosine (m6A) RNA, the most prevalent internal modification of messenger RNA (mRNA) in higher eukaryotes. Modulates viral infection of the alfalfa mosaic virus (AMV) and the m6A abundance in its genomic RNAs.
Subcellular location: Cytoplasm, P-body {ECO:0000269|PubMed:28923956}. Cytoplasmic granule {ECO:0000269|PubMed:28923956}.
Interaction partners:
- FKBP12-interacting protein of 37 kDa
- E3 ubiquitin-protein ligase HAKAI homolog
- YTH domain-containing protein ECT4
- YTH domain-containing protein ECT2
- 30-kDa cleavage and polyadenylation specificity factor 30
- N
- YTH domain-containing protein ECT3
- YTH domain-containing protein ECT1
- YTH domain-containing family protein
- Protein virilizer homolog
Sequence:
MENDPFLRQYQPSELKIASEFLTNWLPFLSKDLCKDCNHLLSNRIRSLDPAHCSNNTDKVDGECKTGSCSVVENMGSERASNNVDDNYDEKSENGEDCDNHSLGSWKGSEIVFGSFPEDFSSVLQSRPAVVETASPRMRWADMAQEDEFDEEEEEEEEERDSSRKGFDASSMKTPEKPKLSRDQRENLRLINVKRKKDFICLERVKGKIVNVLDGLELHTGVFSAVEQKRIVDQVYQLQEKGRRGELKKRTFTAPHKWMRGKGRETIQFGCCYNYAPDRAGNPPGILQREEVDPLPHLFKVIIRKLIKWHVLPPTCVPDSCIVNIYDEGDCIPPHIDNHDFLRPFCTISFLSECDILFGSNLKVEGPGDFSGSYSIPLPVGSVLVLNGNGADVAKHCVPAVPTKRISITFRKMDESKRPVWFTPEPDLQGIEPLPLDLNRSGSTSRFSRLNNHNGTNQRGHGRRGGGNGYDSRGYYNPERSSEHNDSGDWPSSQRRGMPRPSRRNYG
Protein: Probable ATP-citrate synthase subunit 1 (EC 2.3.3.8) (ATP-citrate (pro-S-)-lyase 1) (Citrate cleavage enzyme subunit 1) (Q9P7W3)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Catalyzes the formation of cytosolic acetyl-CoA, which is mainly used for the biosynthesis of fatty acids and sterols.
Subcellular location: Cytoplasm {ECO:0000250}.
Interaction partners:
- Probable ATP-citrate synthase subunit 2
- Probable citrate synthase, mitochondrial
- Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex, mitochondrial
- Succinate--CoA ligase subunit alpha, mitochondrial
- Malate dehydrogenase, mitochondrial
- Aconitate hydratase, mitochondrial
- Pyruvate carboxylase
- Acetyl-CoA carboxylase
- NADP-specific glutamate dehydrogenase
- 2-oxoglutarate dehydrogenase, mitochondrial
Sequence:
MAGSVDKPSYELFSKDTRAFVYGMQTKAVQGMLDFDYMCGRTVPSVAAIIYTFGSQSISKLYWGTKEILLPVYRTIEEACTKHPEVDVVVNFASSRSAYASTMELMEFPQIRCIAIIAEGVPERRAREILVTSKEKNVVIIGPATVGGIKPGCFKIGNTGGMMDNIVASKLYRPGSVAYVSKSGGMSNELNNIISHTTDGVYEGIAIGGDRYPGTTFIDHLIRFEADPACKLMVLLGEVGGVEEYRVIEAVKNGTIKKPIVAWAIGTCSSMFKTEVQFGHAGSFANSELETAVAKNQAMREAGIYVPETFEKLPALLQEVYEGLVKKGVIVPQPEVAPPNIPLDYAWAKELGLVRKPSSFICTISNDRGSELTYNNVPISKVFEEELGIGGVISLLWLRRRLPSYATKFLEMVLQLTADHGPCVSGAMNTIITTRAGKDLISSLVAGLLTIGTRFGGALDGAAQEFSKAYDAGLSPRAFVDSCRKANKLIPGIGHRIKSRNNPDLRVELVKGYVKKNFPSTKLLDYALAVENVTTSKKDNLILNVDGCIAVCFVDLLRNCGAFTLEEANEYINLGILNGMFVLGRSIGLIGHHLDQKRLRAPLYRHPWDDFLYLS
Protein: Enhancer of mRNA-decapping protein 3 (A0A1D8PM93)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Subcellular location: Cytoplasm, P-body {ECO:0000256|ARBA:ARBA00004201}.
Interaction partners:
- Decapping enzyme complex catalytic subunit
- ATP-dependent RNA helicase DHH1
- mRNA-decapping enzyme subunit 1
- mRNA decay factor PAT1 domain-containing protein
- 5'-3' exoribonuclease 1
- U6 snRNA-associated Sm-like protein LSm1
- U6 snRNA-associated Sm-like protein LSm4
- Tubulin tyrosine ligase
- Protein SCD6
- U6 snRNA-associated Sm-like protein LSm2
Sequence:
MTEFLNYKVDLTLKDGTKSTGLISQVDSQQIRLSNAIQSIQPKQTIPYLDIKSSEIADLKVIQLPPDFKQQQKKKQKPRNGELIDDAIVFASKPGTPRVHTPKLKTQKPHAVSAGSEQPDWDTSSDVQDIKSSNEFDFQANLAMFDKKSVFADFQKRDHTNIGDRLVGHNKIENVNKLKKEKYDNDEMVLDQNRTDNWDNIGTATTSKTGTPVVNQNGYKDSQHQHLKLINANNLGNVALASPVQMLEIERLATDSFGITQAMMAEVCATNLSQLIMESILGGASRLSNKKNHNLPPLVLLLIGSARGGSRAFATGRHLTNHGVRVLAFMINTVEVDADLQQQWKLFESSGGKVVISNIIELLDIINNQLDTPVEIIIDALQGYDDHLEDTFYQDEDQATLRKLMKWCNEPQQQNKIMSLDIPSGVDGGSGTLSDDSLKLNCRWCISMGIPLSGIILAYKNGNMSLRDGDIVHYLVDVGIPNKVYSSKGNLRKFDKFWYCSEASIKLEVSEK
Protein: POU domain, class 5, transcription factor 1.2 (POU class V protein oct-91) (XlPOU91) (Xoct-91) (B7ZQA9)
Organism: Xenopus laevis (African clawed frog)
Function: Transcription factor that binds to the octamer motif (5'-ATTTGCAT-3'). Antagonizes the activity of nodal/activin signaling during gastrulation to suppress mesendoderm formation.
Subcellular location: Nucleus {ECO:0000250|UniProtKB:Q01860, ECO:0000255|PROSITE-ProRule:PRU00108, ECO:0000255|PROSITE-ProRule:PRU00530}.
Interaction partners:
Sequence:
MYNQQTYPSFTHNPALMPDGSGQYNLGTYTGMARHPHQAQAFFPFSGVKSDYGDLGGQTTSVGDTSAWNPLTSLDSANQLGISGQGNPFKNLKREREDDEEKSESPEPKCSPPSLPPAYYTHAWNPTTTFWSQVSSSGTTVVSKPLPTPLQPGDKCDPVEANKIFTSSPDKSGESGISSLDNSRCSSATSSSSGGTNVGTPRSLSRGASDGLSSDSEEEAPNSGEMEQFAKDLKHKRITMGYTQADVGYALGVLFGKTFSQTTICRFESLQLSFKNMCKLKPLLRSWLHEVENNENLQEIISRGQIIPQVQKRKHRTSIENNVKCTLENYFMQCSKPSAQEIAQIARELNMEKDVVRVWFCNRRQKGKRQVYPYIRENGGEPYDAPQTLTPPSQGPFPLPQVMPSQVFPTVPLGANPTIYVPTYHKNDMFPQAMHHGIGMGNQGN
Protein: Opsin Rh2 (Ocellar opsin) (P08099)
Organism: Drosophila melanogaster (Fruit fly)
Function: Visual pigments are the light-absorbing molecules that mediate vision. They consist of an apoprotein, opsin, covalently linked to cis-retinal.
Subcellular location: Membrane; Multi-pass membrane protein.
Interaction partners:
- Phosrestin-1
- Inactivation-no-after-potential D protein
- Guanine nucleotide-binding protein subunit beta-2
Sequence:
MERSHLPETPFDLAHSGPRFQAQSSGNGSVLDNVLPDMAHLVNPYWSRFAPMDPMMSKILGLFTLAIMIISCCGNGVVVYIFGGTKSLRTPANLLVLNLAFSDFCMMASQSPVMIINFYYETWVLGPLWCDIYAGCGSLFGCVSIWSMCMIAFDRYNVIVKGINGTPMTIKTSIMKILFIWMMAVFWTVMPLIGWSAYVPEGNLTACSIDYMTRMWNPRSYLITYSLFVYYTPLFLICYSYWFIIAAVAAHEKAMREQAKKMNVKSLRSSEDCDKSAEGKLAKVALTTISLWFMAWTPYLVICYFGLFKIDGLTPLTTIWGATFAKTSAVYNPIVYGISHPKYRIVLKEKCPMCVFGNTDEPKPDAPASDTETTSEADSKA
Protein: Protein SUPPRESSOR OF FRI 4 (Q9C5G0)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Sequence-specific DNA binding factor that recognizes the 5'-CCAAATTTTAAGTTT-3' sequence. Recruits the FRI-C complex to the FLC promoter. Required for FRI-mediated FLC activation, but has no effect on the expression of MAF1, MAF2, MAF3, MAF5, UFC and CO. Dispensable for the reactivation of FLC in early embryogenesis, but required to maintain high levels of FLC expression in later embryonic and vegetative development.
Subcellular location: Nucleus {ECO:0000269|PubMed:17079264, ECO:0000269|PubMed:17138694, ECO:0000269|PubMed:24451981}.
Interaction partners:
- FRIGIDA-like protein 1
- Protein FRIGIDA-ESSENTIAL 1
- Inactive protein FRIGIDA
- Mitotic checkpoint protein BUB3.1
- Mitotic checkpoint protein BUB3.3
- Mitotic checkpoint protein BUB3.2
- Inactive FRIGIDA-like protein 2
- Protein FLX-like 4
- Protein FLC EXPRESSOR
- Protein VERNALIZATION INSENSITIVE 3
Sequence:
MGKKKKRATEKVWCYYCDREFDDEKILVQHQKAKHFKCHVCHKKLSTASGMVIHVLQVHKENVTKVPNAKDGRDSTDIEIYGMQGIPPHVLTAHYGEEEDEPPAKVAKVEIPSAPLGGVVPRPYGMVYPPQQVPGAVPARPMYYPGPPMRHPAPVWQMPPPRPQQWYPQNPALSVPPAAHLGYRPQPLFPVQNMGMTPTPTSAPAIQPSPVTGVTPPGIPTSSPAMPVPQPLFPVVNNSIPSQAPPFSAPLPVGGAQQPSHADALGSADAYPPNNSIPGGTNAHSYASGPNTSGPSIGPPPVIANKAPSNQPNEVYLVWDDEAMSMEERRMSLPKYKVHDETSQMNSINAAIDRRISESRLAGRMAF
Protein: 4-hydroxybenzaldehyde dehydrogenase (NADP(+)) (PHBDD) (EC 1.2.1.96) (Q59702)
Organism: Pseudomonas putida (Arthrobacter siderocapsulatus)
Function: Involved in p-cresol and 2,4-xylenol catabolism. Catalyzes the oxidation of 4-hydroxybenzaldehyde and 4-hydroxy-3-methylbenzaldehyde to yield 4-hydroxybenzoic acid and 4-hydroxy-3-methylbenzoic acid, respectively.
Interaction partners:
Sequence:
MSQRLAAYENMSLQLIAGEWRVGKAGRDLDVLDPFTQEKLLQIPLANREDLDEAYRSARQAQVAWAACGPSERAQVMLNAVRIFDERRDEIIDWIIRESGSTRIKAQIEWGAARAITQESASLPSRVHGRILASDVPGKESRVYREPLGVIGIISPWNFPLHLTARSLAPALALGNACVIKPASDTPVTGGLLLAHIFEEAGLPKGVLSVVVGSGSEIGDAFVEHEVPGFISFTGSTQVGRNIGRIAAGGEHLKHVALELGGNSPFVVLADADLDQAVNAAVVGKFLHQGQICMAINRIIVEDSVYDEFVNRYAERVKSLPYGDPSKPETVVGPVINAKQLAGLQDKIATAKSEGARVMVEGEAQGNVLPPHVFADVTADMEIAREEIFGPLVGIQRARDEAHALELANSSEYGLSSAVFTSSLERGVKFARGIRAGMTHINDIPVNDEPNAPFGGEKNSGLGRFNGDWAIEEFTTDHWITVQHAPRRYPF