wanglab/gogpt-training-data huggingface dataset:
Protein: Prostaglandin-H2 D-isomerase (EC 5.3.99.2) (Glutathione-independent PGD synthase) (Lipocalin-type prostaglandin-D synthase) (Prostaglandin-D2 synthase) (PGD2 synthase) (PGDS) (PGDS2) (O02853)
Organism: Bos taurus (Bovine)
Function: Catalyzes the conversion of PGH2 to PGD2, a prostaglandin involved in smooth muscle contraction/relaxation and a potent inhibitor of platelet aggregation. Involved in a variety of CNS functions, such as sedation, NREM sleep and PGE2-induced allodynia, and may have an anti-apoptotic role in oligodendrocytes. Binds small non-substrate lipophilic molecules, including biliverdin, bilirubin, retinal, retinoic acid and thyroid hormone, and may act as a scavenger for harmful hydrophobic molecules and as a secretory retinoid and thyroid hormone transporter. Possibly involved in development and maintenance of the blood-brain, blood-retina, blood-aqueous humor and blood-testis barrier. It is likely to play important roles in both maturation and maintenance of the central nervous system and male reproductive system (By similarity). Involved in PLA2G3-dependent maturation of mast cells. PLA2G3 is secreted by immature mast cells and acts on nearby fibroblasts upstream to PTDGS to synthesize PGD2, which in turn promotes mast cell maturation and degranulation via PTGDR (By similarity).
Subcellular location: Rough endoplasmic reticulum {ECO:0000250|UniProtKB:P41222}. Nucleus membrane {ECO:0000250|UniProtKB:P41222}. Golgi apparatus {ECO:0000250|UniProtKB:P41222}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:P41222}. Secreted {ECO:0000250|UniProtKB:P41222}. Note=Detected on rough endoplasmic reticulum of arachnoid and menigioma cells. Localized to the nuclear envelope, Golgi apparatus, secretory vesicles and spherical cytoplasmic structures in arachnoid trabecular cells, and to circular cytoplasmic structures in meningeal macrophages and perivascular microglial cells. In oligodendrocytes, localized to the rough endoplasmic reticulum and nuclear envelope. In retinal pigment epithelial cells, localized to distinct cytoplasmic domains including the perinuclear region. Also secreted. {ECO:0000250|UniProtKB:P41222}.
Interaction partners:
- Hematopoietic prostaglandin D synthase
- Prostaglandin E synthase
- Prostaglandin E synthase 2
- Prostacyclin synthase
- Prostaglandin G/H synthase 1
- Prostaglandin G/H synthase 2
- Prostaglandin E synthase 3
- NADP-dependent oxidoreductase domain-containing protein
- Aldo_ket_red domain-containing protein.
- NADP-dependent oxidoreductase domain-containing protein
Sequence:
MATPNRLWMALLLLGVLGVLQTPAPAQAALQPNFEEDKFLGRWFTSGLASNSSWFLEKKKVLSMCKSVVAPAADGGLNLTSTFLRKDQCETRTLLLRPAGPPGCYSYTSPHWSSTHEVSVAETDYETYALLYTEGVRGPGQDFRMATLYSRSQNPRAEVKEHFTTFAKSLGFTEEGIVFLPKTDKCMEEHP
Protein: Wnt ligand secretion mediator (E9PJW4)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MDVSLAYRDDAFAEWTEMAHERVPRKLKCTFTSPKTPEHEGRYYECDVLPFMEIGSVAHKFYLLNIRLPVNEKKKINVGIGEIKDIRLVGIHQNGGFTKVWFAMKTFLTPSIFIIMVWYWRRITMMSRPPVLLE
Protein: Carbonic anhydrase (EC 4.2.1.1) (Carbonate dehydratase) (Q2YS41)
Organism: Caenorhabditis elegans
Interaction partners:
Sequence:
MPGLERILNGVIRFRQTVRKDLVKQFERIRDNPHPTAVFFTCMDSRMLPARITSSQVGDMFVVRNSGNMIPHANNYGPSGYEVSVTTEPAALELAVKRGKINHVIVCGHSDCKAINTLYNLHKCPKSFDPESPMDHWLRRHGFNSIRKLEKRLADKNAGPIEFVSDNPLFSFSAVIDPEDKLNVEDKLSQINTLQQLENVASHGFLKEFLVSQTVDLHAMWFDIYTGEMHMFSKPNKQFVLVDESNVEELIDEVEKHQT
Protein: Phospholipid phosphatase 2 (EC 3.1.3.-) (EC 3.1.3.4) (Lipid phosphate phosphohydrolase 2) (PAP2-gamma) (PAP2-G) (Phosphatidate phosphohydrolase type 2c) (Phosphatidic acid phosphatase 2c) (PAP-2c) (PAP2c) (O43688)
Organism: Homo sapiens (Human)
Function: Magnesium-independent phospholipid phosphatase that catalyzes the dephosphorylation of a variety of glycerolipid and sphingolipid phosphate esters including phosphatidate/PA, lysophosphatidate/LPA, sphingosine 1-phosphate/S1P and ceramide 1-phosphate/C1P. Has no apparent extracellular phosphatase activity and therefore most probably acts intracellularly. Also acts on N-oleoyl ethanolamine phosphate/N-(9Z-octadecenoyl)-ethanolamine phosphate, a potential physiological compound. Through dephosphorylation of these bioactive lipid mediators produces new bioactive compounds and may regulate signal transduction in different cellular processes (Probable). Indirectly regulates, for instance, cell cycle G1/S phase transition through its phospholipid phosphatase activity (By similarity).
Subcellular location: Membrane {ECO:0000269|PubMed:16467304, ECO:0000269|PubMed:9705349}; Multi-pass membrane protein {ECO:0000255}. Cell membrane {ECO:0000269|PubMed:16467304, ECO:0000269|PubMed:9705349}; Multi-pass membrane protein {ECO:0000255}. Early endosome membrane {ECO:0000269|PubMed:16467304}; Multi-pass membrane protein {ECO:0000255}. Endoplasmic reticulum membrane {ECO:0000269|PubMed:16467304}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Phosphatidate phosphatase LPIN1
- Diacylglycerol O-acyltransferase 1
- Phosphatidate phosphatase LPIN2
- Diacylglycerol O-acyltransferase 2
- 1-acyl-sn-glycerol-3-phosphate acyltransferase beta
- Phosphatidate phosphatase LPIN3
- Sphingosine-1-phosphate phosphatase 2
- 1-acyl-sn-glycerol-3-phosphate acyltransferase alpha
- Cholinephosphotransferase 1
- Phospholipid phosphatase 3
Sequence:
MQRRWVFVLLDVLCLLVASLPFAILTLVNAPYKRGFYCGDDSIRYPYRPDTITHGLMAGVTITATVILVSAGEAYLVYTDRLYSRSDFNNYVAAVYKVLGTFLFGAAVSQSLTDLAKYMIGRLRPNFLAVCDPDWSRVNCSVYVQLEKVCRGNPADVTEARLSFYSGHSSFGMYCMVFLALYVQARLCWKWARLLRPTVQFFLVAFALYVGYTRVSDYKHHWSDVLVGLLQGALVAALTVCYISDFFKARPPQHCLKEEELERKPSLSLTLTLGEADHNHYGYPHSSS
Protein: RNA-binding protein 47 (RNA-binding motif protein 47) (A0A8M1NHK4)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Function: Single-stranded RNA-binding protein that functions in a variety of RNA processes, including alternative splicing, RNA stabilization, and RNA editing (By similarity). Independently of its RNA-binding activity, could negatively regulate MAVS by promoting its lysosomal degradation.
Subcellular location: Nucleus {ECO:0000250|UniProtKB:A0AV96}. Cytoplasm {ECO:0000250|UniProtKB:A0AV96}.
Interaction partners:
Sequence:
MTAEDSASAVAMSNPSPSSSSKSSSGHPQHHCTVPEGVAGAPNEAALVSLMERSGYGMVQENGQRKYGPPPGWQGTSPPRGCEIFVGKIPRDVYEDELVPVFESVGRIYEMRLMMDFDGKNRGYAFVMYTQKHEAKRAVRELNNFEIRPGRLLGVCSSVDNCRLFIGGIPKTKKREEILEEVSKVTEGVLDVIVYASAADKMKNRGFAFVEYESHRAAAMARRKLMPGRIQLWGHQIAVDWAEPEIDVDEDVMETVKILYVRNLMIETSEEILRQTFGQFNPGCVERVKKIRDYAFVHFASRDDAVVAMDNLNGTEIEGSRIEVTLAKPVDKEQYTRYQKASKGTAAATTVESTQQSYVYQCDPYTLAYYGYPYNTLIGPNRDYFIKGTVRGRGRAGASSRGPGPRGSYLGGYSAGRGIYSRYHEGKTKLPDKPYEIMSNLELAAVNPVGIKPGTMALPALGAQYPTVFSAAPATKLMEEGKIHPVEHLINPLALQHDPTAASATAAVIPAVSTPPPFQGRPITPVYAMAHNIQRIPAAAASLYGAGYMPIAAHANTATLAALQKNAAVAAAYGGYAGYMPQAFPAATFQMPIHDVYQTY
Protein: LP04941p (Uncharacterized protein, isoform A) (Uncharacterized protein, isoform B) (Q9W375)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Kelch-like protein diablo
Sequence:
MSRSLSRVLGTIWAPSLSISHTVHRGSNRLNDLLSTKVTNTAIIPVARYSKRNGPPSDAGGYFKTVKSRDLDDDDELNSLESEPNWELTAERGNRFYLPNGIGPAWQGDSTTVGLLEPLGHLVNFHKGPNTDKSRLEFTCCKCPLLIRVPLLEIFPVPVVAQQCINITMLVLSHEGDIEMGAAKFVLAAREMCDRLLSYGYWADFMNPFSGRPFFLPREGANLYRLDSRFRGLNMRLSEQNRCTVISAEKNDSTRFSGTIYSTAPNHYGQLMKLLVPPPHKVAH
Protein: bZIP transcription factor 2 (AtbZIP2) (G-box-binding factor 5) (Protein FLORAL TRANSITION AT THE MERISTEM 3) (Q9SI15)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Transcription factor that binds to specific DNA sequences in target gene promoters. BZIP2-BZIP63-KIN10 complex binds to the ETFQO promoter to up-regulate its transcription.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00978}.
Interaction partners:
- Basic leucine zipper 19
- Basic leucine zipper 23
- Basic leucine zipper 25
- bZIP transcription factor 53
- Basic leucine zipper 63
- At5g04840
- SNF1-related protein kinase catalytic subunit alpha KIN10
- Basic leucine zipper 24
Sequence:
MASSSSTYRSSSSSDGGNNNPSDSVVTVDERKRKRMLSNRESARRSRMRKQKHVDDLTAQINQLSNDNRQILNSLTVTSQLYMKIQAENSVLTAQMEELSTRLQSLNEIVDLVQSNGAGFGVDQIDGCGFDDRTVGIDGYYDDMNMMSNVNHWGGSVYTNQPIMANDINMY
Protein: Syntaxin-2 (Epimorphin) (P50279)
Organism: Rattus norvegicus (Rat)
Function: Essential for epithelial morphogenesis. May mediate Ca(2+)-regulation of exocytosis acrosomal reaction in sperm.
Subcellular location: Membrane; Single-pass type IV membrane protein.
Interaction partners:
- Vesicle-associated membrane protein 3
- Vesicle-associated membrane protein 2
- Syntaxin-binding protein 1
- Vesicle-associated membrane protein 1
- Vesicle-associated membrane protein 4
- Synaptosomal-associated protein 23
- Syntaxin-binding protein 2
- Vesicle-associated membrane protein 8
- Alpha-soluble NSF attachment protein
- Multifunctional fusion protein
Sequence:
MRDRLPDLTACRKSDDGDNAVIITVEKDHFMDAFFHQVEEIRSSIARIAQHVEDVKKNHSIILSAPNPEGKIKEELEDLNKEIKKTANRIRGKLKAIEQSCDQDENGNRTSVDLRIRRTQHSVLSRKFVDVMTEYNEAQILFRERSKGRIQRQLEITGRTTTDEELEEMLESGKPSIFISDIISDSQITRQALNEIESRHKDIMKLETSIRELHEMFMDMAMFVETQGEMVNNIERNVVNSVDYVEHAKEETKKAIKYQSKARRKKWIIAAVVVAVIAVLALIIGLTVGK
Protein: Growth factor receptor-bound protein 2-A (Adapter protein GRB2-A) (SH2/SH3 adapter GRB2-A) (P87379)
Organism: Xenopus laevis (African clawed frog)
Function: Adapter protein that provides a critical link between cell surface growth factor receptors and the Ras signaling pathway (By similarity). Promotes meiotic reinitiation during oocyte maturation.
Subcellular location: Nucleus {ECO:0000250}. Cytoplasm {ECO:0000250}. Endosome {ECO:0000250}. Golgi apparatus {ECO:0000250}.
Interaction partners:
Sequence:
MEAIAKYDFKATADDELSFKRGDVLKVLNEECDQNWYKAELNGKDGFIPKNYIEMKAHPWFFGKIPRAKAEEMLGKQRHDGAFLIRESESAPGDFSLSVKFGNDVQHFKVLRDGAGKYFLWVVKFNSLNELVDYHRSTSVSRNQQIFLRDIEQVPQVHGGDRATSLPQQPTYVQALFDFDPQEDGELGFRRGDFIQVVDNSDPNWWKGTCLSQTGMFPRNYVTPVNRNM
Protein: Long-chain-fatty-acid--CoA ligase 1 (EC 6.2.1.3) (Arachidonate--CoA ligase) (EC 6.2.1.15) (Long-chain acyl-CoA synthetase 1) (LACS 1) (Phytanate--CoA ligase) (EC 6.2.1.24) (P41216)
Organism: Mus musculus (Mouse)
Function: Catalyzes the conversion of long-chain fatty acids to their active form acyl-CoAs for both synthesis of cellular lipids, and degradation via beta-oxidation (By similarity). Preferentially uses palmitoleate, oleate and linoleate (By similarity). Preferentially activates arachidonate than epoxyeicosatrienoic acids (EETs) or hydroxyeicosatrienoic acids (HETEs).
Subcellular location: Mitochondrion outer membrane {ECO:0000250}; Single-pass type III membrane protein {ECO:0000250}. Peroxisome membrane {ECO:0000250}; Single-pass type III membrane protein {ECO:0000250}. Microsome membrane {ECO:0000250}; Single-pass type III membrane protein {ECO:0000250}. Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P33121}; Single-pass type III membrane protein {ECO:0000250}.
Interaction partners:
- Fatty acid synthase
- Carnitine O-palmitoyltransferase 1, liver isoform
- Lipoprotein lipase
- Monoglyceride lipase
- Carnitine O-palmitoyltransferase 1, muscle isoform
- Patatin-like phospholipase domain-containing protein 2
- Palmitoyl thioesterase CPT1C
- Palmitoyl-protein thioesterase 1
- Lysosomal thioesterase PPT2
- Fatty acid CoA ligase Acsl3
Sequence:
MEVHELFRYFRMPELIDIRQYVRTLPTNTLMGFGAFAALTTFWYATRPKALKPPCDLSMQSVEIAGTTDGIRRSAVLEDDKLLVYYYDDVRTMYDGFQRGIQVSNNGPCLGSRKPNQPYEWISYKEVAELAECIGSGLIQKGFKPCSEQFIGLFSQNRPEWVIVEQGCFSYSMVVVPLYDTLGADAITYIVNKAELSVIFADKPEKAKLLLEGVENKLTPCLKIIVIMDSYGSDLVERGKKCGVEIISLKALEDLGRVNRVKPKPPEPEDLAIICFTSGTTGNPKGAMITHQNIINDCSGFIKATESAFIASTDDVLISFLPLAHMFETVVECVMLCHGAKIGFFQGDIRLLMDDLKVLQPTIFPVVPRLLNRMFDRIFGQANTSLKRWLLDFASKRKEAELRSGIVRNNSLWDKLIFHKIQSSLGGKVRLMITGAAPVSATVLTFLRTALGCQFYEGYGQTECTAGCCLSLPGDWTAGHVGAPMPCNYVKLVDVEEMNYLASKGEGEVCVKGANVFKGYLKDPARTAEALDKDGWLHTGDIGKWLPNGTLKIIDRKKHIFKLAQGEYIAPEKIENIYLRSEAVAQVFVHGESLQAFLIAVVVPDVESLPSWAQKRGLQGSFEELCRNKDINKAILDDLLKLGKEAGLKPFEQVKGIAVHPELFSIDNGLLTPTLKAKRPELRNYFRSQIDELYATIKI
Protein: G-protein coupled receptors family 1 profile domain-containing protein (A0A060X727)
Organism: Oncorhynchus mykiss (Rainbow trout) (Salmo gairdneri)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004651}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}.
Interaction partners:
- Ig-like domain-containing protein
- Guanine nucleotide-binding protein subunit gamma
- Guanine nucleotide-binding protein subunit gamma
- Endothelin-3
- Neuropeptide Y
- Endothelin-1
- Endothelin-1
- Guanine nucleotide-binding protein subunit gamma
- Guanine nucleotide-binding protein subunit gamma
Sequence:
MDVAKFTTVTNTSQDTNTSSAPRPLPQTGVGSALIILVVTVIILVTIVGNALVIVAVLTSRALRAPQNLFLVSLACADILVATLVIPFSLANEVMGYWYFGSTWCAFYLALDVLFCTSSIVHLCAISLDRYWSVTKAVSYNLKRTPKRIKSMIAVVWVISAVISFPPLIMTKHNEHECLLNNETWYILSSCLVSFFAPGLIMILVYCKIYKVAKQRSSTVKERMEMESPSSQSSEDHHRQEELDYIDLEESCCASDNKPRNHRFSKRRKSCRLSWASARASQLFQEPQNATNATLTKVAQMREKRFTFVLAVVMGVFVLCWFPFFFTYSLHAICRESCYIPGALFNAFFWIGYCNSSVNPMIYTIFNRDFRKAFKKIVCRTSKRTNTT
Protein: Anthranilate synthase beta subunit 1, chloroplastic (EC 4.1.3.27) (Anthranilate synthase component 2-1) (Anthranilate synthase, glutamine amidotransferase component 2-1) (Protein TRYPTOPHAN BIOSYNTHESIS 4) (Protein WEAK ETHYLENE INSENSITIVE 7) (Q42565)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Part of a heterotetrameric complex that catalyzes the two-step biosynthesis of anthranilate, an intermediate in the biosynthesis of L-tryptophan. In the first step, the glutamine-binding beta subunit of anthranilate synthase (AS) provides the glutamine amidotransferase activity which generates ammonia as a substrate that, along with chorismate, is used in the second step, catalyzed by the large alpha subunit of AS to produce anthranilate. Plays an important regulatory role in auxin production via the tryptophan-dependent biosynthetic pathway.
Subcellular location: Plastid, chloroplast {ECO:0000305}.
Interaction partners:
- Anthranilate synthase alpha subunit 1, chloroplastic
- Anthranilate synthase alpha subunit 2, chloroplastic
- Anthranilate phosphoribosyltransferase, chloroplastic
- anthranilate synthase
- Aminodeoxychorismate synthase, chloroplastic
- Chorismate synthase, chloroplastic
- Isochorismate synthase 2, chloroplastic
- Isochorismate synthase 1, chloroplastic
- Tryptophan synthase beta chain 1, chloroplastic
- Protein PHYLLO
Sequence:
MAASTLYKSCLLQPKSGSTTRRLNPSLVNPLTNPTRVSVLGKSRRDVFAKASIEMAESNSIPSVVVNSSKQHGPIIVIDNYDSFTYNLCQYMGELGCHFEVYRNDELTVEELKKKNPRGVLISPGPGTPQDSGISLQTVLELGPLVPLFGVCMGLQCIGEAFGGKIVRSPFGVMHGKSSMVHYDEKGEEGLFSGLSNPFIVGRYHSLVIEKDTFPSDELEVTAWTEDGLVMAARHRKYKHIQGVQFHPESIITTEGKTIVRNFIKIVEKKESEKLT
Protein: Thrombospondin type-1 domain-containing protein 1 (Transmembrane molecule with thrombospondin module) (Q9JM61)
Organism: Mus musculus (Mouse)
Function: Is a positive regulator of nascent focal adhesion assembly, involved in the modulation of endothelial cell attachment to the extracellular matrix.
Subcellular location: Endosome membrane {ECO:0000250|UniProtKB:Q9NS62}; Single-pass type I membrane protein {ECO:0000305}. Cell junction, focal adhesion {ECO:0000250|UniProtKB:Q9NS62}. Note=Localizes to nascent focal adhesions. {ECO:0000250|UniProtKB:Q9NS62}.
Interaction partners:
Sequence:
MKPMLKDFSNLLLVVLCDYVLGEAEYLLLQEPVHVALSDRTVSVGFHYLSDVNGTLRNVSVMLWEANTNRTLTTKYLLTNQAQGTLQFECFYFKEAGDYWFVMIPEVTDNGTQVPLWEKSAFLKVEWPVFHIDLNRTAKAAEGTFQVGVFTTQPLCLFPVDKPDMLVDVIFTDRLPEARASLGQPLEIRASKRTKLTQGQWVEFGCAPVGVEAYVTVMLRLLGQDSVIASTGPIDLAQKFGYKLMMAPEVTCESVLEVMVLPPPCVFVQGVLAVYKEAPKRPEERTFQVAENRLPLGERRTVFNCTLFDVGKNKYCFNFGIVKKGHFSAKECMLIQRNIETWGPWQPWSPCSTTCGDAVRERRRLCVTSFPSRPSCSGMSSETSPCSLEECAVFRPPGPSPVSPQDPVKSNNVVTVTGISLCLFIIFATVLITLWRRFGRAPKCSTPVRHNSIHSPGFRKNSDEENICELSEPRGSFSDAGDGPRGSPGDTGIPLTYRCSASAPPEDEASGSESFQSNAQKIIPPLFSYRLAQQQLKEMKKKGLTETTKVYHVSQSPLTDTVVDATASPPLDLECPEEAAASKFRIKSPFLDQPGAGTGERPPSRLDGIVPPPGCAVSPSQTLIQKSQIRSTGGRDGSSERCHSRSSLFRRTASFHETKQSRPFRERSLSALTPRQVPAYSSRMRTWDQMEDRCRPPSRSTHLLPERPEHFQGAGRTSSPLGPLSKSYTVGHPRRKPDPGDRQAGLVAGAEKMEPHRAHRGPSPSHRSASRKQSSPIFLKDSYQKVSQLSPSHFRKDKCQSFPIHPEFAFYDNTSFRLTEAEQRMLDLPGYFGSNEEDETTSTLSVEKLVI
Protein: Candida glabrata strain CBS138 chromosome J complete sequence (Q6FP09)
Organism: Candida glabrata (strain ATCC 2001 / BCRC 20586 / JCM 3761 / NBRC 0622 / NRRL Y-65 / CBS 138) (Yeast) (Nakaseomyces glabratus)
Interaction partners:
- Pheromone-processing carboxypeptidase KEX1
Sequence:
MKWWNKGCIYLAYIALISKNSNAELIPAKNFTSRDYFAVESHLSAAELSKLHPDWTFEHLVRGLDNHYVFSVAKSENEDDIDSGNSLRKRAIENEDHILSSEFLTPSNKLQKRMPVPAPPLDSSMLPIQEIKDKIGINDPLFPKQWHLINPAFPGNDINVKDVWLQNITGKGVVAAIIDDGVDYTSPDLKDNFCKEGSWDFNENQQLPMPLLSDDNHGTRCAGEIAAIRNNNYCGVGVAYDAKVSGIRILSGPLTAEDEAASLVHALDVNDIYSCSWGPTDDGKHLQGPSPLVKKAMKKGVTEGRGNKGAIYVFASGNGGMHGDNCNYDGYTNSIYSITVGAIDHKGLHPPYSESCSAVLVVTYSSGSGEYIHSTDINGGCYDRHGGTSAAAPIAAGIYALVLEANPNITWRDMQYLSILSSETIENNLEDGDWQTTKLEKKYSHKYGYGKLNAHNIVALAKDWENVNPQVEFATDIKEVNEETDKEDKPIESTIEITASDLEKAKFRSVEHVTINVDISTENRGTTTIDLISPFGVVSHLGVVRRKDDSNEGFRDWTFMSVAHWGELGSGEWKLIVKTTSDDDKVEFHSWSITLFGLSEYSEQKLKEGDIPSENDDDNRKEDGPETDNNNVTEETGSDQQPETENPENDGDNGTDKNTGHHMTPTIPTGVHLIVSIFIIGCVFLLLHFMFFVRTRRRIKRVRASNYDYDVIDTDAEYDSTNESSSTPLPDTFRLSDIDDNEFDISDEENTQYNHLFNNDESLDQRLLDSDNPEQNPTGEQAQTHSSDT
Protein: CCCTC-binding factor (Transcriptional repressor CTCF) (Q6JAA4)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MEGGPTEAVVEDAGDAFKAKECKTYQRRREDEEVGAELLQAAVIEQAQAEVEPVVEAQQQLVESVVSVNSSVDMMMMETLDPALLQMKTEVMEAAVGAPVAVAGAAHEATVTTVDDTQIITLQVVNMEEQQLGLGELQLVQVPVSAVPVTAATVEELQGTLVDATAMPKDGEPVICHTLPLPEGFQVVKVGANGEVETVEQDELQPQDDQPPHQEEEEEMAEPQNEDPAWSKDPDYTPPVKKVKKTKKSKLRYNTEGDKDMDVSVYDFEEEQQEGLLSEVNAEKVVGNMKPPKPTKIKKKGVKKTFQCELCSYTCPRRSNLDRHMKSHTDERPHKCHLCGRAFRTVTLLRNHLNTHTGTRPHKCTDCDMAFVTSGELVRHRRYKHTHEKPFKCSMCDYASVEVSKLKRHIRSHTGERPFQCSLCSYASRDTYKLKRHMRTHSGEKPYECYICHARFTQSGTMKMHILQKHTENVAKFHCPHCDTVIARKSDLGVHLRKQHSYIEQGRKCRYCDAVFHERYALIQHQKSHKNEKRFKCDQCDYACRQERHMVMHKRTHTGEKPYACSQCEKTFRQKQLLDMHFRRYHDPNFVPTSFVCTKCGKTFTRRNTMARHAENCTGMDSADGENGTPPKRGRGGRKRKMRSRKDDDDDDDSDEHGEPDLDDIDEEDEDDLLDEDQMGLLDQAPPSVPIPAPAEPPIKRKRGRPPKNAPKVSPTKSITKTTTAAAIIQVEDESTGAIENIIVKKEPEGTDAVVAAQPIIEEVEAVEADVETVQLTVPEAAPNGDLTPEMILSMMDR
Protein: Inactive selenide, water dikinase-like protein (Protein patufet) (Selenophosphate synthetase 1) (O18373)
Organism: Drosophila melanogaster (Fruit fly)
Function: Plays a role in apoptosis and consequently a role in imaginal disk patterning and growth.
Interaction partners:
- O-phosphoseryl-tRNA
- Eukaryotic translation elongation factor, selenocysteine-specific
- Thioredoxin reductase 1, mitochondrial
- Thioredoxin reductase 2, mitochondrial
- Selenide, water dikinase 2
- Cysteine desulfurase, mitochondrial
- Phosphoseryl tRNA kinase, isoform A
- GH01354p
Sequence:
MSYAADVLNSAHLELHGGGDAELRRPFDPTAHDLDASFRLTRFADLKGRGCKVPQDVLSKLVSALQQDYSAQDQEPQFLNVAIPRIGIGLDCSVIPLRHGGLCLVQTTDFFYPIVDDPYMMGKIACANVLSDLYAMGVTDCDNMLMLLAVSTKMTEKERDVVIPLIMRGFKDSALEAGTTVTGGQSVVNPWCTIGGVASTICQPNEYIVPDNAVVGDVLVLTKPLGTQVAVNAHQWIDQPERWNRIKLVVSEEDVRKAYHRAMNSMARLNRVAARLMHKYNAHGATDITGFGLLGHAQTLAAHQKKDVSFVIHNLPVIAKMAAVAKACGNMFQLLQGHSAETSGGLLICLPREQAAAYCKDIEKQEGYQAWIIGIVEKGNKTARIIDKPRVIEVPAKD
Protein: Selenide, water dikinase (EC 2.7.9.3) (LmselD) (Selenophosphate synthetase 2) (Q4Q0M0)
Organism: Leishmania major
Function: Synthesizes selenophosphate from selenide and ATP.
Interaction partners:
- O-phosphoseryl-tRNA
- cysteine desulfurase
- Putative mitotic spindle checkpoint component
Sequence:
MSHKRPQSSAGESNGAVDLKTPRFDPVSLGLPAEFQLTDYTRLKGCSCKLPQPKLLALLQELSATPGQKDVGMDCSIVPLHHTNSKGEALFLVSTTDFFFPSVSDPFLQGQIGAANVLSDLYSMGIPDCDTMLMLLAASTEMDEHERLITTREIMKGFAERARLATTTVTGGQTVMNPWPLIGGVAMAVVSEAEMVRPTGLLCAGDILVLTKPLGCQVAVNLKQWLLRPSPLYEEAIAGHISPEEIEELYNMATDSMRRLNREGARLMRKHGAHGATDVTGFGILGHANNFGAAQAVGDAPRSLCLVLERLPMFKTAVAASKQMNDKYRLLEGYSAETSGGLLVAFPSTTAAAAFCAELTAVDGGCPSWIVGHVEDRATNAVDGVYARLKDGYEIVEV
Protein: Interleukin-3 receptor class 2 subunit beta (IL-3 receptor class 2 subunit beta) (IL-3R class 2 subunit beta) (Colony-stimulating factor 2 receptor subunit beta-2) (Interleukin-3 receptor class II beta chain) (P26954)
Organism: Mus musculus (Mouse)
Function: In mouse, there are two classes of high-affinity IL3 receptors. One contains this IL3-specific beta subunit and the other contains the beta subunit also shared by high-affinity IL5 and GM-CSF receptors.
Subcellular location: Membrane; Single-pass type I membrane protein.
Interaction partners:
- Interleukin-3
- Granulocyte-macrophage colony-stimulating factor
- Interleukin-3 receptor subunit alpha
- Granulocyte-macrophage colony-stimulating factor receptor subunit alpha
- Cytokine receptor common subunit beta
- Interleukin-5
- Interleukin-5 receptor subunit alpha
- GTPase KRas
- GTPase HRas
- GTPase NRas
Sequence:
MDQQMALTWGLCYMALVALCWGHEVTEEEETVPLKTLECYNDYTNRIICSWADTEDAQGLINMTLLYHQLDKIQSVSCELSEKLMWSECPSSHRCVPRRCVIPYTRFSNGDNDYYSFQPDRDLGIQLMVPLAQHVQPPPPKDIHISPSGDHFLLEWSVSLGDSQVSWLSSKDIEFEVAYKRLQDSWEDASSLHTSNFQVNLEPKLFLPNSIYAARVRTRLSAGSSLSGRPSRWSPEVHWDSQPGDKAQPQNLQCFFDGIQSLHCSWEVWTQTTGSVSFGLFYRPSPAAPEEKCSPVVKEPQASVYTRYRCSLPVPEPSAHSQYTVSVKHLEQGKFIMSYYHIQMEPPILNQTKNRDSYSLHWETQKIPKYIDHTFQVQYKKKSESWKDSKTENLGRVNSMDLPQLEPDTSYCARVRVKPISDYDGIWSEWSNEYTWTTDWVMPTLWIVLILVFLIFTLLLALHFGRVYGYRTYRKWKEKIPNPSKSLLFQDGGKGLWPPGSMAAFATKNPALQGPQSRLLAEQQGVSYEHLEDNNVSPLTIEDPNIIRDPPSRPDTTPAASSESTEQLPNVQVEGPIPSSRPRKQLPSFDFNGPYLGPPQSHSLPDLPGQLGSPQVGGSLKPALPGSLEYMCLPPGGQVQLVPLSQVMGQGQAMDVQCGSSLETTGSPSVEPKENPPVELSVEKQEARDNPMTLPISSGGPEGSMMASDYVTPGDPVLTLPTGPLSTSLGPSLGLPSAQSPSLCLKLPRVPSGSPALGPPGFEDYVELPPSVSQAATSPPGHPAPPVASSPTVIPGEPREEVGPASPHPEGLLVLQQVGDYCFLPGLGPGSLSPHSKPPSPSLCSETEDLDQDLSVKKFPYQPLPQAPAIQFFKSLKY
Protein: Transcription factor HES-5 (Hairy and enhancer of split 5) (Q03062)
Organism: Rattus norvegicus (Rat)
Function: Transcriptional repressor of genes that require a bHLH protein for their transcription. Plays an important role as neurogenesis negative regulator (By similarity).
Subcellular location: Nucleus.
Interaction partners:
- Transcription factor HES-1
- Neurogenic locus notch homolog protein 1
- Achaete-scute homolog 1
- Transcription factor SOX-10
- Protein jagged-1
- Delta-like protein 1
- Neurogenic locus notch homolog protein 3
- Recombining binding protein suppressor of hairless
Sequence:
MAPSTVAVEMLSPKEKNRLRKPVVEKMRRDRINSSIEQLKLLLEQEFARHQPNSKLEKADILEMAVSYLKHSKAFAAAAGPKSLHQDYSEGYSWCLQEAVQFLTLHAASDTQMKLLYHFQRPPAPAAPVKETPTPGAAPQPARSSTKAAASVSTSRQSACGLWRPW
Protein: Histone deacetylase (EC 3.5.1.98) (Q9VYF3)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123, ECO:0000256|PIRNR:PIRNR037911}.
Interaction partners:
Sequence:
MSSPDDRIPIHDLPSEAGSDERLLHITPATLTLDFKPHPAVDIDQQIMELKKSQELQKQRLINSFQEQSKQMELEHKLQLEHKYQFAVNSHGAFQELRNESMVTAAAAAVAQEQHRQQLHQQQQQHQQQQQQQQHQQQQQQQQARGRDGMKLKQNCSANASPEVKQILNCFILSRKSQAAASNGTTTTSPYRNRGVVKSSSGESLPAGTVTSAHPYKIPQPPPSLLKYESDFPLRKTASEPNLLKIRLKQSVIERKARIGGPAGARRHERLLQAAQRRQQKNSVLTNCNSTPDSGPNSPPSAAALAVGVVGSRGSPTSAPIQEENEEGSQYQPGQRSSINDLPLFSSPSLPNISLGRPHLPNSAQAHAQVNAQVAAQAQAQAQAQAQAHAMFAALAAAQGGCGQPGYYNPLGMAFVGRQPAPLAMIPATGIAPQQPSPVVRSASATSTSSSQASLVGDVAPPQAHAASTILPSSSSYMQQLGSVAGSGVNLHAAAVAAAAAAAAAAGSLPPTNSHGHGHGSHAHPHPHAHGHGHGHGHGIYAGHQHNVPITDAQVAQVHLHKQGHRPLGRTQSAPLPLGHPMLTGAVQLNVVQTHYENSEAERQAYEHQVVNQKVRQTVLTRSGAAAAAAAAAGVSVVREAQLKEEDDDSAAEVMDLTDKKKPPKTVLTSTIATSTSQNLPEALAAAAAAAAYRAPHNASSNSASATKSGIKLRDQEYLQQQREQLLLLQQEEELAKSLMRPLSRTLSSPLVPLGPHGLSQIPDTGQQPAPIATSSSADHIPPVNLSLPHRQHRQLMSTLYASQLRNHQPSASGSPPHKVTTGLAYDPLMLKHSCICGDNAQHPEHSGRLQSVWARLNETDLVKRCDRLRARKATQEELQTVHTEAHAMLFGSNQCQLSRPKLENTLSASFVRLSCGGLGVDLDTTWNEHHTATAARMAAGCVIDLALKTAKGDLRNGFAVVRPPGHHAEANLAMGFCFFNSIAIAAKLLRQRMPEVRRILIVDWDVHHGNGTQQAFYQSPDILYLSIHRHDDGNFFPGTGGPTECGSGAGLGFNVNISWSGALNPPLGDAEYIAAFRTVVMPIARSFNPDIVLVSSGFDAATGHPAPLGGYHVSPACFGFMTRELLQLANGKVVLALEGGYDLAAICDSAQECVRALLGDPAAPIAKAELERPPCQNAINTLQKTIAIQQTHWPCVRMLEHTVGLSALETLKVEHDESETINAMAGLSMQSMHRTLSRDDSEEPMDQDETK