wanglab/gogpt-training-data huggingface dataset:
Protein: NFE2 like bZIP transcription factor 2 (K7EIW5)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MIVSFLRPPQTCGTDMDLIDILWRQDIDLGVSREVFDFSQRRKEYELEKQKKLEKERQEQLQKEQEKAFFAQLQLDEETGEFLPIQPAQHIQSETSGSANYSQVAHIPKSDALYFDDCMQLLAQTFPFVDDNEVSSATFQSLVPDIPGHIESPVFIATNQAQSPETSVAQVAPVDLDGMQQDIEQVWEELLSIPELQCLNIENDKLVETTMVPSPEAKLTEVDNYHFYSSIPSMEKEVGNCSPHFLNAFEDSFSSILSTEDPNQLTVNSLNSDATVNTDFGDEFYSAFIAEPSISNSMPSPATLSHSLSELLNGPIDVSDLSLCKAFNQNHPESTAEFNDSDSGISLNTSPSVASPEHSVESSSYGDTLLGLSDSEVEELDSAPGSVKQNGPKTPVHSSGDMVQPLSPSQGQSTHVHDAQCENTPEKELPVSPGHRKTPFTKDKHSSRLEAHLTRDELRAKALHIPFPVEKIINLPVVDFNEMMSKEQFNEAQLALIRDIRRRGKNKVAAQNCRKRKLENIVELEQDLDHLKDEKEKLLKEKGENDKSLHLLKKQLSTLYLEVFSMLRDEDGKPYSPSEYSLQQTRDGNVFLVPKSKKPDVKKN
Protein: 17-beta-hydroxysteroid dehydrogenase type 1 (17-beta-HSD 1) (EC 1.1.1.51) (Estradiol 17-beta-dehydrogenase 1) (EC 1.1.1.62) (P51656)
Organism: Mus musculus (Mouse)
Function: Favors the reduction of estrogens and androgens. Converts estrone (E1) to a more potent estrogen, 17beta-estradiol (E2). Also has 20-alpha-HSD activity. Uses preferentially NADH (By similarity).
Subcellular location: Cytoplasm.
Interaction partners:
- Dehydrogenase/reductase SDR family member 11
- Aromatase
- 3-keto-steroid reductase/17-beta-hydroxysteroid dehydrogenase 7
- Estradiol 17-beta-dehydrogenase 2
- Very-long-chain 3-oxoacyl-CoA reductase
- (3R)-3-hydroxyacyl-CoA dehydrogenase (17-beta-hydroxysteroid dehydrogenase 8) (17-beta-HSD 8) (KAR alpha subunit) (Estradiol 17-beta-dehydrogenase 8) (Protein Ke6) (Ke-6) (Testosterone 17-beta-dehydrogenase 8)
- Sulfotransferase 1E1
- Cytochrome P450 1B1
- 17-beta-hydroxysteroid dehydrogenase type 6
- Cytochrome P450 1A1
Sequence:
MDPTVVLITGCSSGIGMHLAVRLASDRSQSFKVYATLRDLKAQGPLLEAARTQGCPPGSLEILELDVRDSKSVAAAQACVTEGRVDVLVCNAGRGLFGPLEAHELNAVGAVLDVNVLGTIRMLQAFLPDMKRRHSGRVLVTASVGGLMGLPFHEVYCASKFALEGLCESLAILLPLFGVHVSLIECGAVHTAFYEKLVGGPGGALERADAQTRHLFAHYLRGYEQALSEAQDPEEVTELFLTAMRAPQPALRYFSTNRFLPLARMRTEDPSGSSYVAAMHQEAFSNLQTQENAKAGAQVPGVSDTASSALICLPECAIPRVASELGWSASDKPGQDNSCYQQKI
Protein: 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase gamma-1 (EC 3.1.4.11) (PLC-148) (Phosphoinositide phospholipase C-gamma-1) (Phospholipase C-II) (PLC-II) (Phospholipase C-gamma-1) (PLC-gamma-1) (P19174)
Organism: Homo sapiens (Human)
Function: Mediates the production of the second messenger molecules diacylglycerol (DAG) and inositol 1,4,5-trisphosphate (IP3). Plays an important role in the regulation of intracellular signaling cascades. Becomes activated in response to ligand-mediated activation of receptor-type tyrosine kinases, such as PDGFRA, PDGFRB, EGFR, FGFR1, FGFR2, FGFR3 and FGFR4 (By similarity). Plays a role in actin reorganization and cell migration.
Subcellular location: Cell projection, lamellipodium {ECO:0000269|PubMed:17229814}. Cell projection, ruffle {ECO:0000269|PubMed:17229814}. Note=Rapidly redistributed to ruffles and lamellipodia structures in response to epidermal growth factor (EGF) treatment. {ECO:0000269|PubMed:17229814}.
Interaction partners:
- Linker for activation of T-cells family member 1
- Lymphocyte cytosolic protein 2
- Platelet-derived growth factor receptor beta
- Growth factor receptor-bound protein 2
- Fibroblast growth factor receptor 1
- Fibroblast growth factor receptor 2
- Proto-oncogene vav
- GRB2-related adapter protein 2
- Tyrosine-protein kinase SYK
- Tyrosine-protein kinase ITK/TSK
Sequence:
MAGAASPCANGCGPGAPSDAEVLHLCRSLEVGTVMTLFYSKKSQRPERKTFQVKLETRQITWSRGADKIEGAIDIREIKEIRPGKTSRDFDRYQEDPAFRPDQSHCFVILYGMEFRLKTLSLQATSEDEVNMWIKGLTWLMEDTLQAPTPLQIERWLRKQFYSVDRNREDRISAKDLKNMLSQVNYRVPNMRFLRERLTDLEQRSGDITYGQFAQLYRSLMYSAQKTMDLPFLEASTLRAGERPELCRVSLPEFQQFLLDYQGELWAVDRLQVQEFMLSFLRDPLREIEEPYFFLDEFVTFLFSKENSVWNSQLDAVCPDTMNNPLSHYWISSSHNTYLTGDQFSSESSLEAYARCLRMGCRCIELDCWDGPDGMPVIYHGHTLTTKIKFSDVLHTIKEHAFVASEYPVILSIEDHCSIAQQRNMAQYFKKVLGDTLLTKPVEISADGLPSPNQLKRKILIKHKKLAEGSAYEEVPTSMMYSENDISNSIKNGILYLEDPVNHEWYPHYFVLTSSKIYYSEETSSDQGNEDEEEPKEVSSSTELHSNEKWFHGKLGAGRDGRHIAERLLTEYCIETGAPDGSFLVRESETFVGDYTLSFWRNGKVQHCRIHSRQDAGTPKFFLTDNLVFDSLYDLITHYQQVPLRCNEFEMRLSEPVPQTNAHESKEWYHASLTRAQAEHMLMRVPRDGAFLVRKRNEPNSYAISFRAEGKIKHCRVQQEGQTVMLGNSEFDSLVDLISYYEKHPLYRKMKLRYPINEEALEKIGTAEPDYGALYEGRNPGFYVEANPMPTFKCAVKALFDYKAQREDELTFIKSAIIQNVEKQEGGWWRGDYGGKKQLWFPSNYVEEMVNPVALEPEREHLDENSPLGDLLRGVLDVPACQIAIRPEGKNNRLFVFSISMASVAHWSLDVAADSQEELQDWVKKIREVAQTADARLTEGKIMERRKKIALELSELVVYCRPVPFDEEKIGTERACYRDMSSFPETKAEKYVNKAKGKKFLQYNRLQLSRIYPKGQRLDSSNYDPLPMWICGSQLVALNFQTPDKPMQMNQALFMTGRHCGYVLQPSTMRDEAFDPFDKSSLRGLEPCAISIEVLGARHLPKNGRGIVCPFVEIEVAGAEYDSTKQKTEFVVDNGLNPVWPAKPFHFQISNPEFAFLRFVVYEEDMFSDQNFLAQATFPVKGLKTGYRAVPLKNNYSEDLELASLLIKIDIFPAKENGDLSPFSGTSLRERGSDASGQLFHGRAREGSFESRYQQPFEDFRISQEHLADHFDSRERRAPRRTRVNGDNRL
Protein: Small ribosomal subunit protein uS15 (40S ribosomal protein S13) (S27a) (YS15) (P05756)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Component of the ribosome, a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell. The small ribosomal subunit (SSU) binds messenger RNAs (mRNAs) and translates the encoded message by selecting cognate aminoacyl-transfer RNA (tRNA) molecules. The large subunit (LSU) contains the ribosomal catalytic site termed the peptidyl transferase center (PTC), which catalyzes the formation of peptide bonds, thereby polymerizing the amino acids delivered by tRNAs into a polypeptide chain. The nascent polypeptides leave the ribosome through a tunnel in the LSU and interact with protein factors that function in enzymatic processing, targeting, and the membrane insertion of nascent chains at the exit of the ribosomal tunnel.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:22096102}.
Interaction partners:
- Large ribosomal subunit protein uL18
- Small ribosomal subunit protein uS5
- Large ribosomal subunit protein uL15
- Serine/threonine-protein kinase RIO2
- Small ribosomal subunit protein eS10B
- Small ribosomal subunit protein uS2A
- Small ribosomal subunit protein uS3
- Small ribosomal subunit protein eS26A
- Large ribosomal subunit protein eL8B
- Large ribosomal subunit protein uL6A
Sequence:
MGRMHSAGKGISSSAIPYSRNAPAWFKLSSESVIEQIVKYARKGLTPSQIGVLLRDAHGVTQARVITGNKIMRILKSNGLAPEIPEDLYYLIKKAVSVRKHLERNRKDKDAKFRLILIESRIHRLARYYRTVAVLPPNWKYESATASALVN
Protein: Short transient receptor potential channel 3 (TrpC3) (Trp-related protein 3) (Q9JMI9)
Organism: Rattus norvegicus (Rat)
Function: Forms a receptor-activated non-selective calcium permeant cation channel. May be operated by a phosphatidylinositol second messenger system activated by receptor tyrosine kinases or G-protein coupled receptors.
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:Q13507}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Short transient receptor potential channel 4
- Protein kinase C gamma type
- Inositol 1,4,5-trisphosphate-gated calcium channel ITPR1
- Protein kinase C beta type
- Transient receptor potential Ca2+ channel 6A
- Bone morphogenetic protein receptor type-2
- RAR-related orphan receptor A
- Transient receptor potential cation channel, subfamily C, member 5
- Histone acetyltransferase KAT5
- Short transient receptor potential channel 1
Sequence:
MSTKVKKCREPARVTLPAPEEEDGEAEGAEPQRRRRGWRGVNGGLEPPCPRAPPSPGPDASSEGSPSRWRTAGMRDKGRRQAVRGPAFMFGARGPSLTAEEERFLDAAEYGNIPVVRKMLEESRTLNVNCVDYMGQNALQLAVGNEHLEVTELLLKKENLARIGDALLLAISKGYVRIVEAILGHPGFAASRRLTLSPCEQELRDDDFYAYDEDGTRFSPDITPIILAAHCHKYEVVHLLLLKGARIERPHDYFCRCADCAEKQRLDAFSHSRSRINAYKGLASPAYLSLSSEDPVLTALELSNELAKLANIEKEFKNDYRKLSMQCKDFVVGVLDLCRDSEEVEAILNGDLESVEPLERHGHKASLSRVKLAIKYEVKKFVAHPNCQQQLLTIWYENLSGLREQTIAIKCLVVLVVALGLPFLAIGYWIAPCSRLGKILRSPFMKFVAHAASFIIFLGLLVFNASDRFEGITTLPNITVIDYPKQIFRVKTTQFTWTEMLIMVWVLGMMWSECKELWLEGPREYIVQLWNVLDFGMLSIFIAAFTARFLAFLQATKAQQYVDSHVQESDLSEVTLPPEVQYFTYARDKWLPSDPQIISEGLYAIAVVLSFSRIAYILPANESFGPLQISLGRTVKDIFKFMVLFIMVFLAFMIGMFILYSYYLGAKVNPAFTTVEESFKTLFWSIFGLSEVTSVVLKYDHKFIENIGYVLYGIYNVTMVVVLLNMLIAMINSSYQEIEDDSDVEWKFARSKLWLSYFDDGKTLPPPFSLVPSPKSFVYFIMRITNFSKCRRRRLQKDLELGMGNSKSRLNLFTQSNSRVFESHSFNSILNQPTRYQQIMKRLIKRYVLKAQVDKENDEVNEGELKEIKQDISSLRYELLEDKSQATEELAILIHKLSEKLNPSALRCE
Protein: Kinase suppressor of Ras B (G5EDA5)
Organism: Caenorhabditis elegans
Function: Probable inactive protein kinase which positively regulates Ras-mediated signaling probably acting at the level of let-60/ras or/and lin-45/raf. In the germline, regulates meiotic progression during oogenesis and mpk-1 (isoform b) phosphorylation. Plays a role in meiotic recombination events. Functions redundantly with ksr-1 in the Ras-mediated regulation of larval survival, the development of excretory canal, in determining vulval precursor cell fate during vulval induction and in mpk-1 phosphorylation in somatic cells.
Interaction partners:
- Dual specificity mitogen-activated protein kinase kinase mek-2
- mitogen-activated protein kinase kinase
- Mitogen-activated protein kinase mpk-1
- Raf homolog serine/threonine-protein kinase
- Ras protein let-60
- Nucleoside diphosphate kinase
- 14-3-3-like protein 1
- 14-3-3-like protein 2
- 14-3-3 domain-containing protein
Sequence:
MSDEKKKKRGFFRYSVLTTSSFSSWRRSSTSGSISQSSRTTSKTTTSSSVTSSNPINAPPPTATSSSSVLPSTSSEPPPPASAPPRISIYHKMVPSKSKFRQCDVCEHIFIFDFVRKQHLDDVYACNVCGIRVHKGCLDRVKNDCKITTQYMGGILENAVIQSNKKQWEKPTTASISKSLTTSPTCSTSTTMSPAGVEKNVHKTRKLISMTTSTLDDVTTFNSEINEEMDEETVLMTWEDVTIKLTDVDVMTKIGDGRFGSVYFGGYHGNAAVRFVNMNYLSQEDRRADVFATEIVSAYKNSRHDHIALFYGYVSDPVTNTYAIVTNFYQHNTLYHRIHEQLSEDFDQSWTFQISLQICQAMSYLHKKKILHRDLRTKNILLDNPNRVVVTDFALMKLERLENPRRNCTLLIPNHWIDYLSPEIAGNLMIDWRGDVLFQHELPFSQESDVYSFGTIFFELLLRRMPTGCDSWDQKLYAKMCGQKAALQRLDAQLQKIDGKLHELLLECWSSQPEKRPSFQQIVKRITVQMPRKESNKQKRRSTAHENPLF
Protein: Ion_trans_2 domain-containing protein (H9G2R4)
Organism: Caenorhabditis elegans
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
- Potassium voltage-gated channel protein shk-1
- BK channel Interacting Protein
- Voltage-dependent L-type calcium channel subunit alpha
- RRM domain-containing protein
- Voltage-dependent T-type calcium channel subunit alpha
- Voltage-dependent calcium channel type A subunit alpha-1
Sequence:
MSDDIQYTGLRRIPSMSNMSDQDVDDIARTDSEAEGTVYKNSYASLMNELQPTTSFDDFKQSITQLTDIFRADPARMQYGEKKNIKHKLQQWFIENPSISARIRSCNVLIKLLTCILYCIRVVNDERSYPDDFPFSEEEAGKQDVTLYKYLLWVDFDFKIWFLQTMFACISMVYTILVFYLSYSGSVVRLLINIHFLLELITSFPFIISIFIPSLTYLYVPVFLNCWLAKGALQAMMNDLNRKSFISSSALFRQLLLLFSVLACLIFTGMCSIEHLQRARGKRIDLFTSFYFVMVTFSTVGYGDWYPDYWASQLCVVILICVALGLIPKQLDELGQTWSERQKSGTDFSSWNGVESHVVVTITTLEVEFIRDFLEEFYAHPENQRIQIVLLSPAELDNQTRMLLKIPLWNNRVHYVRGSSLRDEDLERANVATSKACFILSARHVNRKVATDEHTILRSWAIKDFAPNVKQYVQIFRAETKMHIEHAEVLICEDEFKYALLANNCICPGISTFITLLMHTSRGEEGQKSTEPWHKVYGFHSGNEMYQIKVQDSKFFCEYVGKSFSSTSFHAHKEYGIGLIAVSPDGDTSRMKLNPGSSHIIQPTDTVYYMGLTNEESLTDFRKGIRSQQKRANVASTIANIGTVAVDVPRSDKTELVGRKKKKRKEKAADEIHLIEVGEHVQSSRRPSIAMVTEGKIDSSSDSDQEEICDKCRGPCIQHKLQRTYPQVRTYIGTSNTVCHMMKERRSLCCLKLDEKCAHKSATSAHEYQWRNRPIILAADRTSSGMYNLVIPLRAYYRPVHDLHPIIILLELEEQDSLNDAFLDAISYFPDVYWMKGKVGNLDCLLRAGVSSAEHVVVVKETAVMAEEHTADCNTIITVQKIHRMFPRLRMITELTHATNMRFVQFNPHNAYSLAQSRFEKKERKRGSHMPFMFRLPFAQGGVFSANMLDRLLYQAIIKPFVVDLVRLLLGIDQHSDGGYLTSFVITSDDLWIRNYGRLYQKLCSSVADIPIGIFRTKKMDTKTVSLDLQEQCKDFENTEMGRNKDMYDHVKNRMRLLNIKDTHTLLEGSDEKSQISYVIINPAQDLELESGDIVYVIRSPIRKDATNARINPRRGLRRSKNVSETIDSTNQVPTIVIDENNL
Protein: Mediator of RNA polymerase II transcription subunit 15 (Mediator complex subunit 15) (C9JM58)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus {ECO:0000256|RuleBase:RU364148}.
Interaction partners:
Sequence:
MRKAGVAHSKSSKDMESHVFLKAKTRDEYLSLVARLIIHFRDIHNKKSQASVSDPMNALQSLTGGPAAGAAGIGMPPRGPGQSLGGMGSLGAMGQPMSLSGQPPP
Protein: Capsid protein VP1 (CP) (Coat protein) (p59) [Cleaved into: Soluble capsid protein (Protein 30k) (p30)] (Q83884)
Organism: Norovirus (strain Human/NoV/United States/Norwalk/1968/GI) (Hu/NV/NV/1968/US)
Function: Capsid protein self assembles to form an icosahedral capsid with a T=3 symmetry, about 38 nm in diameter, and consisting of 180 capsid proteins. A smaller form of capsid with a diameter of 23 nm might be capsid proteins assembled as icosahedron with T=1 symmetry. The capsid encapsulate the genomic RNA and VP2 proteins. Attaches virion to target cells by binding histo-blood group antigens present on gastroduodenal epithelial cells.
Subcellular location: [Capsid protein VP1]: Virion. Host cytoplasm.
Interaction partners:
Sequence:
MMMASKDATSSVDGASGAGQLVPEVNASDPLAMDPVAGSSTAVATAGQVNPIDPWIINNFVQAPQGEFTISPNNTPGDVLFDLSLGPHLNPFLLHLSQMYNGWVGNMRVRIMLAGNAFTAGKIIVSCIPPGFGSHNLTIAQATLFPHVIADVRTLDPIEVPLEDVRNVLFHNNDRNQQTMRLVCMLYTPLRTGGGTGDSFVVAGRVMTCPSPDFNFLFLVPPTVEQKTRPFTLPNLPLSSLSNSRAPLPISSMGISPDNVQSVQFQNGRCTLDGRLVGTTPVSLSHVAKIRGTSNGTVINLTELDGTPFHPFEGPAPIGFPDLGGCDWHINMTQFGHSSQTQYDVDTTPDTFVPHLGSIQANGIGSGNYVGVLSWISPPSHPSGSQVDLWKIPNYGSSITEATHLAPSVYPPGFGEVLVFFMSKMPGPGAYNLPCLLPQEYISHLASEQAPTVGEAALLHYVDPDTGRNLGEFKAYPDGFLTCVPNGASSGPQQLPINGVFVFVSWVSRFYQLKPVGTASSARGRLGLRR
Protein: Transmembrane protein 132E (L7VG99)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Function: Required for normal inner ear hair cell function and hearing.
Subcellular location: Membrane {ECO:0000255}; Single-pass type I membrane protein {ECO:0000255}.
Interaction partners:
- Si:dkey-266f7.5
- Calpain 7
- WD repeat domain 27.
- Snail family zinc finger 3.
Sequence:
MGHFVVQGDLPWILCSLRLVIMIIAGKVSPTSSDALFSVPVPSATSSPPEVYLPATFKLSNTQLAFFLQENRAPSYGSQRGHPLQRSESFVVFQTKELPAVNISLGPFTQDQTLSKDLLQPSSPLDIPGRLTVNWKVRAFIVQSRVYASNPLVQVLFYIAGRDWDDFKIQDKLPCVRLHAFRDVREIKTSCRLQGNLAQCLAQLDLPSTWFNVNVAPLGRRKSSGTDGLELTGETLQVELYYTLHDPDSNDECGESYPRRGGPSRGESLSQQPLLRIGSISLYQPSQEQLVVDKQLDKNLFLRLPERPLKPGETLNIYLLLVPNSTVEQFTLKVKAKKGVNLLSTKSRSNQWRVEWDMQSGAKHSIATVEASKIKGVSGDMAGSIEIMQLDFEMENFTSQSVTRRINWNIDYRGQNPTSDAEKVVTELTVVQKDIQAIIPLSMDTEIINTAVLTGRTVAIPVKVVSIELNGAVTDVSSSVQCKSFNEDIVKVSMNCDYVFVNGKETRGSMNARVIFSYEHLSAPLELTVWVPKLPLKVELSDNRLSFIKGWRVPILPDRRTARDSDDDDDDDRKVSRGCTLQYQRAQIKVLTQFHTTSSEGTNQMITMLGPDWQVDVTELVQDSLKVVDGRVAELADRTVLVANELGSSTLKVESPLAVEAVLGETQFSVVDEKVSIVELRVHAISGLALNLQPSPGNSHTMVAKATGLQTLSTLKQEASFSIWVYYSDNTAAPLSMYDPKDYNLNGTSADDKVVTVAQQPQQRWPVIIAEGEGTGDIVHVEMTISETCQKTKRKSVIASSSVFVKVRFGTDEDSEEDMEMETEIDTRMPANTRRPAIDSNVGGAGYEPSNEQPASVPIDYTNFPTISNPEEPTEEDEEDDEFVHSPRSMTDLEIGMYALLGVFCLAILVFLINCIVFVLKYRHKRIPPEGQANMDHSHHWVFLGNGEPLRTQSDLSPQTVESPSNTLEGVQTCCHGDHHSSGSSQTSVQSQVHGRGDGSSGGSTKDHGEDASSPTSKRKRVKFTTFTLPTEDLPYNSIPIANEEDIQWVCQDMGFQDQEELHDYMRRIKEIA
Protein: Aryl hydrocarbon receptor nuclear translocator (ARNT protein) (Dioxin receptor, nuclear translocator) (Hypoxia-inducible factor 1-beta) (HIF-1-beta) (HIF1-beta) (P53762)
Organism: Mus musculus (Mouse)
Function: Required for activity of the Ah (dioxin) receptor. This protein is required for the ligand-binding subunit to translocate from the cytosol to the nucleus after ligand binding. The complex then initiates transcription of genes involved in the activation of PAH procarcinogens (By similarity). The heterodimer binds to core DNA sequence 5'-TACGTG-3' within the hypoxia response element (HRE) of target gene promoters and functions as a transcriptional regulator of the adaptive response to hypoxia. The heterodimer ARNT:AHR binds to core DNA sequence 5'-TGCGTG-3' within the dioxin response element (DRE) of target gene promoters and activates their transcription.
Subcellular location: Nucleus {ECO:0000250|UniProtKB:P27540}.
Interaction partners:
- Endothelial PAS domain-containing protein 1
- Hypoxia-inducible factor 1-alpha
- Histone lysine acetyltransferase CREBBP
- Hypoxia-inducible factor 3-alpha
- Aryl hydrocarbon receptor
- Histone acetyltransferase p300
- Neuronal PAS domain-containing protein 4
- Aryl hydrocarbon receptor nuclear translocator 2
- Neuronal PAS domain-containing protein 3
- Aryl hydrocarbon receptor repressor
Sequence:
MAATTANPEMTSDVPSLGPTIASGNPGPGIQGGGAVVQRAIKRRSGLDFDDEVEVNTKFLRCDDDQMCNDKERFARSDDEQSSADKERLARENHSEIERRRRNKMTAYITELSDMVPTCSALARKPDKLTILRMAVSHMKSLRGTGNTSTDGSYKPSFLTDQELKHLILEAADGFLFIVSCETGRVVYVSDSVTPVLNQPQSEWFGSTLYDQVHPDDVDKLREQLSTSENALTGRVLDLKTGTVKKEGQQSSMRMCMGSRRSFICRMRCGTSSVDPVSMNRLSFLRNRCRNGLGSVKEGEPHFVVVHCTGYIKAWPPAGVSLPDDDPEAGQGSKFCLVAIGRLQVTSSPNCTDMSNICQPTEFISRHNIEGIFTFVDHRCVATVGYQPQELLGKNIVEFCHPEDQQLLRDSFQQVVKLKGQVLSVMFRFRSKTREWLWMRTSSFTFQNPYSDEIEYIICTNTNVKNSSQEPRPTLSNTIPRSQLGPTANLSLEMGTGQLPSRQQQQQHTELDMVPGRDGLASYNHSQVSVQPVASAGSEHSKPLEKSEGLFAQDRDPRFPEIYPSITADQSKGISSSTVPATQQLFSQGSSFPPNPRPAENFRNSGLTPPVTIVQPSSSAGQILAQISRHSNPAQGSAPTWTSSSRPGFAAQQVPTQATAKTRSSQFGVNNFQTSSSFSAMSLPGAPTASSGTAAYPALPNRGSNFPPETGQTTGQFQARTAEGVGVWPQWQGQQPHHRSSSSEQHVQQTQAQAPSQPEVFQEMLSMLGDQSNTYNNEEFPDLTMFPPFSE
Protein: Oleosin 20.3 kDa (Oleosin type 4) (Q42431)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: May have a structural role to stabilize the lipid body during desiccation of the seed by preventing coalescence of the oil. Probably interacts with both lipid and phospholipid moieties of lipid bodies. May also provide recognition signals for specific lipase anchorage in lipolysis during seedling growth (By similarity).
Subcellular location: Lipid droplet {ECO:0000250}. Membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Note=Surface of oil bodies. Oleosins exist at a monolayer lipid/water interface (By similarity). {ECO:0000250}.
Interaction partners:
- MLO-like protein 2
- Bifunctional inhibitor/lipid-transfer protein/seed storage 2S albumin superfamily protein
- MLO-like protein 6
- MLO-like protein 12
- Bifunctional inhibitor/lipid-transfer protein/seed storage 2S albumin superfamily protein
Sequence:
MANVDRDRRVHVDRTDKRVHQPNYEDDVGFGGYGGYGAGSDYKSRGPSTNQILALIAGVPIGGTLLTLAGLTLAGSVIGLLVSIPLFLLFSPVIVPAALTIGLAVTGILASGLFGLTGLSSVSWVLNYLRGTSDTVPEQLDYAKRRMADAVGYAGMKGKEMGQYVQDKAHEARETEFMTETHEPGKARRGS
Protein: Acylglycerol kinase, mitochondrial (EC 2.7.1.107) (EC 2.7.1.138) (EC 2.7.1.94) (Multiple substrate lipid kinase) (A0A3B3ITD0)
Organism: Homo sapiens (Human)
Subcellular location: Mitochondrion inner membrane {ECO:0000256|ARBA:ARBA00004637}; Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004637}. Mitochondrion intermembrane space {ECO:0000256|ARBA:ARBA00004569}.
Interaction partners:
Sequence:
MPPSLANFCIFSRDGVSPCWSGWSRTPDLVIHSPWPPKVLQLQVFGNQLIPPNAQVKKATVFLNPAACKGKARTLFEKNAAPILHLSGMDVTIVKTDYEGQAKKLLELMENTDVIIVAGGDGTLQEVVTGVLRRTDEATFSKIPIGFIPLGETSSLSHTLFAESGNKVQHITDATLAIVKGETVPLDVLQIKGEKEQPVFAMTGLRWGSFRDAGVKVSKYWYLGPLKIKAAHFFSTLKEWPQTHQASISYTGPTERPPNEPEETPVQRPSLYRRILRRLASYWAQPQDALSQEVSPEVWKDVQLSTIELSITTRNNQLDPTSKEDFLNICIEPDTISKGDFITIGSRKVRNPKLHVEGTECLQASQCTLLIPEGAGGSFSIDSEEYEAMPVEVKLLPRKLQFFCDPRKREQMLTSPTQ
Protein: DUF155 domain-containing protein (A0A1D8PJF1)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Interaction partners:
Sequence:
MLRVNTLSRCLKEVRFTRPLPFYRFNSSSTTTTTTTSSPPSVSVTNIKRATKNIPKKKIGAQKLRRTDDSKFQHESASYILSLLNANRQETPSPKELEKYLSIVTSVTVGDSIDFDKLLTQIKGYEYQIVIPEEVINISTSTTNLMILSNGTLVGWNLTEEEIVQFLPILEDDCIENKFDAFESEEIDWIELKQQLPQDPLNQGTSYLHGEIMVIQGPTMEKRLLDMAAFAVGLSRSTRLSILETQLEDYLHLTKKNSEILANGKQITTTEHEFLKITGQLFLLRGKLNLYSELIDTPDLYWSEPTLEKIYYSISKILDINSRISILNRKLDYATEEQRAFLSVLNEKKGTRLEWIIIWLILIEVCFEIFHFYEKYEEKQNKRLNVKEDR
Protein: Profilin-4 (Pollen allergen Zea m 12) (ZmPRO4) (allergen Zea m 12) (O22655)
Organism: Zea mays (Maize)
Function: Binds to actin and affects the structure of the cytoskeleton. At high concentrations, profilin prevents the polymerization of actin, whereas it enhances it at low concentrations. By binding to PIP2, it inhibits the formation of IP3 and DG. Has a high affinity for poly-proline.
Subcellular location: Cytoplasm, cytoskeleton.
Interaction partners:
- Actin-1
- Actin-1
- Uncharacterized protein.
- Actin-depolymerizing factor
- Actin-depolymerizing factor
- Actin-depolymerizing factor 7
- Actin-depolymerizing factor
- Actin-depolymerizing factor 1
- Expansin-B10
- Expansin-B9
Sequence:
MSWQAYVDEHLMCEIEGQHLSAAAIVGHDGSVWAQSESFPELKPEEVAGIIKDFDEPGTLAPTGLFVGGTKYMVIQGEPGVVIRGKKGTGGITIKKTGMSLIIGVYDEPMTPGQCNMVVERLGDYLIEQGF
Protein: Synaptojanin (N-terminal domain), putative (EC 3.1.3.36) (Q385L9)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Subcellular location: Endomembrane system {ECO:0000256|ARBA:ARBA00004308}.
Interaction partners:
- Vacuolar protein 14 C-terminal Fig4-binding domain-containing protein
- Zinc finger protein, putative
- Non-specific serine/threonine protein kinase
- 1-phosphatidylinositol-3-phosphate 5-kinase
Sequence:
MIDSDLQGHRDSGQRCSPWVNCDAFLQPEITKPLRNIVVCDLPAQCYIIGTSSKKNIEQKEVLLFNKSDGGPLVYSYSRSYTADEVDSLTACASKEGRLLHVKALLGCVRFTSGYYLLLATRRQTVARIGFNRIFEALDIELVSLCLPKMIALTTVVATKAATVLGVKGPASSSIQKARLQEEEYCRQFLSSAHKQNLFYSRTYDLTNTLQSNMTIPSQRRLVRTKFVWNEFLLEPLFTLQETESVRCERESAQNGGQSYEAAPLCPKDLRRWFVYVAQGSIVQRAVWCGSRPLLFTLIARTSKNYAGARYFRRGVNGNGHVANHVEIEQIISDESTLHDYGRRGSFTSYVQVRGSVPLHWFQPPTQLPKPPIKLGMSNFYCVDTCRHFQELLGDYGAPVIVVNLLRKREKHLREGALGSEFKKAVETLIGYTKKDFLGGCESSSNVLIYREYDIRASAQDAWNKTTSLAEEVFAKNGFFVCGTDASTGVDTGCYGRCCIHSNGYDAERSVRLQQGVTRSNCLDCVDRTNLAQYFFGLHALGYQLHALGLLHSPIDLSLSPQVREQFLHMYLLMGDIIALHYGGSAQVGAGVLNRGTGWDKMMGIKRLYNNILGDREKQLFMNLFLGRFQPCPNRCSPSQNPVMRIPDGEQQGTGSDGKGNESNESTNSSKQVACLADLSEGASDYYLVVNGGPSLPDPTELVGWWKKPLQFFSSFFQPRQRSLLDENAPSSPVSFGFVPHEGGNGKGSADDEEEYIVREICIDERAAAIDPYTNRGLVGAGAGELKEEGSAVLLQRTTAATTSLNRKTRTLLTAAHTEPSPQILWFVQDSLCNEQHQEAEFPQSDVASNKRDIPTEKMPDDLLYHDHLTYPDYVLGSEFNNNIETARCMCDNCVPEDDLQRMQLEVMHKYGDPCDWGVETVIDALLDVEPGVKRETIDALRQMNVHGRTLLNMNTKSLEEKVLLQRFIRLVDKLFRSASSSPPQHVRDDEMSELWLLHQHGDALEKSNIFASCKFVSCPDATQRVLQPFFRDLLAPDIIAATLRTLISKMADPDSGVPRSDRIRYREGSGCQYVPPVVVAQQCFSSNELHEWLLTESPRLGLTLHEHVESHERAQACWQFVLWLVHAKIVVPISIELISGVLVPPVVTRADVTSSTRLFTLSTIQELHVLNESERHPCGDVDVLRVKINPIKSTPLLLTGASALACAETLVAVALDTLLYMQDMSSPTVPPDVSHNPTAWKLLETVSTSSAHLAAVNIRGLERRELFCFWANVFNALYIHAWMSTLGKRAQDFTCFYNTNGYNVGGCFFSLSDIKDGILRGNKPAYYAVLPPFSKSDPRLFMVIPPDPSDIEVELQMKSRNCFDDKHITTSSRRDLHTRILLALIDAYLVPENFEDMPSYNPRTLLFASSPTVASRSAEGSNSSFLEDDLEIDESYRSRTTVGLWHANSIPVVAATWLSSWFNQRHTNKSSTLANPCVPLTPEHLLQQIHAAESFVLRSLSRAPQPTVPLHGVHVPRALLPLFVNMDNASIDEFMQLLSVSPRSETSLRCDMWISNPPA
Protein: RELB proto-oncogene, NF-kB subunit (V-rel reticuloendotheliosis viral oncogene homolog B, nuclear factor of kappa light polypeptide gene enhancer in B-cells 3 (Avian)) (D6R992)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MLRSGPASGPSVPTGRAMPSRRVARPPAAPELGALGSPDLSSLSLAVSRSTEIIDEYIKENGFGLDGGQPGPGEGLPRLVSRGAASLSTVTLGPVAPPATPPPWGCPLGRLVSPAPGPGPQPHLVITEQPKQRGMRFRYECEGRSAGSILGESSTEASKTLPAIELRDCGGLREVEVTACLVWKDWPHRVHPHSLVGKDCTDGICRVRLRPHVSPRHSFNNLGIQCVRKKEIEAAIERKIQLGIDPYNAGSLKNHQEVDMNVVRICFQASYRDQQGQMRRMDPVLSEPVYDKKSTNTSELRICRINKESGPCTGGEELYLLCDKVQKEDISVVFSRASWEGRADFSQADVHRQIAIVFKTPPYEDLEIVEPVTVNVFLQRLTDGVCSEPLPFTYLPRDHDSYGVDKKRKRGMPDVLGELNSSDPHGIESKRRKKKPAILDHFLPNHGSGPFLPPSALLPDPDFFSGTVSLPGLEPPGGPDLLDDGFAYDPTAPTLFTMLDLLPPAPPHASAVVCSGGAGAVVGETPGPEPLTLDSYQAPGPGDGGTASLVGSNMFPNHYREAAFGGGLLSPGPEAT
Protein: Non-specific lipid-transfer protein (LTP) (GH3) (Q43129)
Organism: Gossypium hirsutum (Upland cotton) (Gossypium mexicanum)
Function: Plant non-specific lipid-transfer proteins transfer phospholipids as well as galactolipids across membranes. May play a role in wax or cutin deposition in the cell walls of expanding epidermal cells and certain secretory tissues.
Interaction partners:
Sequence:
MASSMSLKLACVVVLCMVVGAPLAQGAVTSGQVTNSLAPCINYLRGSGAGAVPPGCCTGIKSLNSAAQTTPVRQAACRCIKSAAAGITGINFGLASGLPGKCGVNIPYKISPSTDCNSVK