wanglab/gogpt-training-data huggingface dataset:
Protein: Fanconi anemia protein FANCL (Q3MUH5)
Organism: Gallus gallus (Chicken)
Interaction partners:
- Fanconi anemia group F protein
- Uncharacterized protein.
- Uncharacterized protein.
- Ubiquitin conjugating enzyme E2 T
- Uncharacterized protein.
- Fanconi anemia group M protein
- Uncharacterized protein.
- Fanconi anemia group C protein homolog
- Uncharacterized protein.
- Fanconi_A_N domain-containing protein.
Sequence:
MAGRGSLLRQCPLLLPQNREGTAYEGFVSAQGRDFHIRILLPTDSQLKNARIECSWHLKKILHGYQHILKQRLHSCPDLVSFVVELKTILEIALKNTQELHVPWPPEYYSCLIRDLEILGWNKVAYVDTGLTTVKLKAEDSRGRQHLITLKLNAKYPTEPPDCVVDFPVQFAISWMPQDSLIDIHNQFLAALESLKEFWDTMDEIDGKTWVLEPENPARCATSRRIAIGNNVSVNIEVDPRHPKMLPECYFLGADHAVNPLRTKLNNNMHLWDPEISLLQNLKDLLEIDFPSRAALEKSDFTKDCGICYAYRLNGTTPDQVCNEPRCGQPFHQACLYEWLQGLPSSRQSFNVIFGECPYCNKPLTVKSSMKKP
Protein: Adrenodoxin, mitochondrial (Adrenal ferredoxin) (Ferredoxin-1) (Hepato-ferredoxin) (P00257)
Organism: Bos taurus (Bovine)
Function: Essential for the synthesis of various steroid hormones. Participates in the reduction of mitochondrial cytochrome P450 for steroidogenesis. Transfers electrons from adrenodoxin reductase to CYP11A1, a cytochrome P450 that catalyzes cholesterol side-chain cleavage to produce pregnenolone, the precursor of most steroid hormones. Does not form a ternary complex with adrenodoxin reductase and CYP11A1 but shuttles between the two enzymes to transfer electrons.
Subcellular location: Mitochondrion matrix.
Interaction partners:
- NADPH:adrenodoxin oxidoreductase, mitochondrial
- Cysteine desulfurase
- Cholesterol side-chain cleavage enzyme, mitochondrial
- Iron-sulfur cluster assembly enzyme ISCU
- NADH dehydrogenase iron-sulfur protein 2, mitochondrial
- NADH dehydrogenase iron-sulfur protein 8, mitochondrial
- NADH-ubiquinone oxidoreductase chain 3
- NADH-ubiquinone oxidoreductase chain 4
- NADH dehydrogenase iron-sulfur protein 3, mitochondrial
- LYR motif-containing protein 4
Sequence:
MAARLLRVASAALGDTAGRWRLLARPRAGAGGLRGSRGPGLGGGAVATRTLSVSGRAQSSSEDKITVHFINRDGETLTTKGKIGDSLLDVVVQNNLDIDGFGACEGTLACSTCHLIFEQHIFEKLEAITDEENDMLDLAYGLTDRSRLGCQICLTKAMDNMTVRVPDAVSDARESIDMGMNSSKIE
Protein: REPTOR-binding partner (Q9VL14)
Organism: Drosophila melanogaster (Fruit fly)
Function: Transcriptional regulator that acts in the TORC1 signaling pathway to regulate energy homeostasis and promote survival during nutrient deprivation. Interacts with REPTOR to form a transcriptional activator complex that functions downstream of TORC1 to up-regulate the expression of most target genes induced by TORC1 inhibition. In the complex, acts to enhance the binding of the transcriptional activator REPTOR to the regulatory sequences of target genes. Under normal conditions TORC1 is active, inhibiting the formation of the REPTOR/REPTOR-BP complex by phosphorylating REPTOR and mediates its cytoplasmic retention by forming a docking site for 14-3-3 proteins. Upon TORC1 inhibition resulting from nutrient stress, REPTOR is recruited into the nucleus where it interacts with REPTOR-BP and together they maintain organismal metabolism by activating the expression of target stress response genes including those involved in glycogenesis and triglyceride biosynthesis. The complex also appears to negatively regulate some aspects of TORC1-dependent larval growth.
Subcellular location: Nucleus {ECO:0000269|PubMed:25920570}. Chromosome {ECO:0000269|PubMed:25920570}. Note=Binds chromatin. {ECO:0000269|PubMed:25920570}.
Interaction partners:
- Protein CREBRF homolog
Sequence:
MADMEIQSNKMSITEETQVQTRKECGKRGRKPGRKTSTEKLDMKAKLERSRQSARECRARKKLRYQYLEELVADREKAVVALRTELERLIQWNNQLSESNTPTNNDQLLQELGILKQE
Protein: Pectinesterase inhibitor 12 (Pectin methylesterase inhibitor 12) (AtPMEI12) (Q9FJR5)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Pectin methylesterase (PME) inhibitor involved in the maintenance of cell wall integrity in response to necrotrophic pathogens. Modulates PME activity and pectin methylesterification during infection by Botrytis cinerea and contributes to resistance against the pathogen.
Subcellular location: Secreted, extracellular space, apoplast {ECO:0000269|PubMed:28082716}.
Interaction partners:
- Pectinesterase inhibitor 10
- Pectinesterase inhibitor 11
- Pectinesterase inhibitor 5
- Pectinesterase inhibitor 2
- Pectinesterase inhibitor 1
- Plant invertase/pectin methylesterase inhibitor superfamily protein
- Probable pectinesterase/pectinesterase inhibitor 17
- AT4g29480/F17A13_300
- Probable pectinesterase 66
- Pectinesterase inhibitor 6
Sequence:
MKFLVSLVIFSLFLNGFATAQTLIQDSCKKAFAKDPQLSYDFCVNSLTQDPQSKAATTLESLVLASTKTAAAKITNLKGIVAQDLKDQRYQDIVEDLKLCLGFYNDANDDLTTALANIKSRDYQGANINLSAALDVPGNCEDDFKEAKKTSPITNENSILFKTILIPLAFTNML
Protein: AT04516p (Q8IHG0)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MEALIPVINKLQDVFNTVGSDSIQLPQIVVLGSQSSGKSSVIESVVGRSFLPRGTGIVTRRPLVLQLIYSPLDDRENRSAENGTSNAEEWGRFLHTKKCFTDFDEIRKEIENETERAAGSNKGICPEPINLKIFSTHVVNLTLVDLPGITKVPVGDQPEDIEAQIKELVLKYIENPNSIILAVTAANTDMATSEALKLAKDVDPDGRRTLAVVTKLDLMDAGTDAIDILCGRVIPVKLGIIGVMNRSQKDIMDQKHIDDQMKDEAAFLQRKYPTLATRNGTPYLAKTLNRLLMHHIRDCLPDLKTRVNIMATQFQSLLNSYGEDVSDKSQTLLQIITKFSSAYCCTIEGTARNIETTELCGGARMGYIFHETFGRTLDSIHPLAGLSKMDILTAIRNATGPRPALFVPEVSFELLVKRQIRRLEEPSLRCVELIHEEMQRIVQHCGNEVQQEMLRFPKLHEKIVDVVTQLLRRRLPHTNVMVENIVAIELAYINTKHPDFHKDAALVPSLLKTDSDPYSQINLGQRRANTPRNHMSPQISSHSAGSQQPQQQQPPQPSSSQQQYSQVHEQNHVAENSTPSMASTWLSNILPPAPTRPDSIENSTNNTPVHNNIVSPVKPVNLLPDVPANHNPRRLTDKEQKDCDVIEHLIKSYFYIVRKSIQDSVPKAIMHFLVNYVKDNLQSELVTHLYKSDKAETLLNESDHIAVRRKEAADMLKALTRANHIISEIRETHMW
Protein: Uncharacterized protein Rv1128c (P9WM57)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Interaction partners:
- Conserved 13E12 repeat family protein
- Uncharacterized protein Rv2100
- Conserved 13E12 repeat family protein
- HNH nuclease domain-containing protein
- Uncharacterized protein Rv3776
Sequence:
MCSTREEITEAFASLATALSRVLGLTFDALTTPERLALLEHCETARRQLPSVEHTLINQIGEQSTEEELGGKLGLTLADRLRITRSEAKRRVAEAADLGQRRALTGEPLPPLLTATAKAQRHGLIGDGHVEVIRAFVHRLPSWVDLKTLEKAERDLAKQATQYRPDQLAKLAARIMDCLNPDGDYTDEDRARRRGLTLGKQDVDGMSRLSGYVTPELRATIEAVWAKLAAPGMCNPEQKAPCVNGAPSKEQARRDTRSCPQRNHDALNAELRSLLTSGNLGQHNGLPASIIVTTTLKDLEAAAGAGLTGGGTILPISDVIRLARHANHYLAIFDRGKALALYHTKRLASPAQRIMLYAKDSGCSAPGCDVPGYYCEVHHVTPYAQCRNTDVNDLTLGCGGHHPLAERGWTTRKNAHGDTEWLPPPHLDHGQPRVNTFHHPEKLLADDEGDP
Protein: Stimulator of interferon genes protein (A0A494C0W5)
Organism: Homo sapiens (Human)
Subcellular location: Cytoplasm, perinuclear region {ECO:0000256|ARBA:ARBA00004556}. Cytoplasmic vesicle, autophagosome membrane {ECO:0000256|ARBA:ARBA00004542}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004542}. Endoplasmic reticulum-Golgi intermediate compartment membrane {ECO:0000256|ARBA:ARBA00004457}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004457}. Mitochondrion outer membrane {ECO:0000256|ARBA:ARBA00004374}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004374}.
Interaction partners:
Sequence:
MLALLGLSQALNILLGLKGLAPAEISAVCEKGNFNVAHGLAWSYYIGYLRLILPELQARIRTYNQHYNNLLRGAVSQRLYILLPLDCGVPDNLSMADPNIRFLDKLPQQTGDHAGIKDRVYSNSIYELLENGQRAGTCVLEYATPLQTLFAMSQYSQAGFSREDRLEQAKLFCRTLEDILADAPESQNNCRLIAYQEPADDSSFSLSQEVLRHLRQEEKEEVTVGSLKTSAVPSTSTMSQEPELLISGMEKPLPLRTDFS
Protein: Prostaglandin E2 receptor EP2 subtype (PGE receptor EP2 subtype) (PGE2 receptor EP2 subtype) (Prostanoid EP2 receptor) (P43116)
Organism: Homo sapiens (Human)
Function: Receptor for prostaglandin E2 (PGE2). The activity of this receptor is mediated by G(s) proteins that stimulate adenylate cyclase. The subsequent raise in intracellular cAMP is responsible for the relaxing effect of this receptor on smooth muscle.
Subcellular location: Cell membrane; Multi-pass membrane protein.
Interaction partners:
- Guanine nucleotide-binding protein G
- Prostaglandin E2 receptor EP4 subtype
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein G
- Pro-opiomelanocortin
- Pro-glucagon
- Gastric inhibitory polypeptide
- VIP peptides
- Thyrotropin subunit beta
Sequence:
MGNASNDSQSEDCETRQWLPPGESPAISSVMFSAGVLGNLIALALLARRWRGDVGCSAGRRSSLSLFHVLVTELVFTDLLGTCLISPVVLASYARNQTLVALAPESRACTYFAFAMTFFSLATMLMLFAMALERYLSIGHPYFYQRRVSRSGGLAVLPVIYAVSLLFCSLPLLDYGQYVQYCPGTWCFIRHGRTAYLQLYATLLLLLIVSVLACNFSVILNLIRMHRRSRRSRCGPSLGSGRGGPGARRRGERVSMAEETDHLILLAIMTITFAVCSLPFTIFAYMNETSSRKEKWDLQALRFLSINSIIDPWVFAILRPPVLRLMRSVLCCRISLRTQDATQTSCSTQSDASKQADL
Protein: BES1/BZR1 homolog protein 4 (Q9ZV88)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- Protein BRASSINOSTEROID INSENSITIVE 1
Sequence:
MTSGTRMPTWRERENNKRRERRRRAIAAKIFTGLRMYGNYELPKHCDNNEVLKALCNEAGWIVEPDGTTYRKGCSRPVERMEIGGGSATASPCSSYQPSPCASYNPSPGSSNFMSPASSSFANLTSGDGQSLIPWLKHLSTTSSSSASSSSRLPNYLYIPGGSISAPVTPPLSSPTARTPRMNTDWQQLNNSFFVSSTPPSPTRQIIPDSEWFSGIQLAQSVPASPTFSLVSQNPFGFKEEAASAAGGGGGSRMWTPGQSGTCSPAIPPGADQTADVPMSEAVAPPEFAFGSNTNGLVKAWEGERIHEESGSDDLELTLGNSSTR
Protein: Photosystem II D2 protein (PSII D2 protein) (EC 1.10.3.9) (Photosystem Q(A) protein) (P0C437)
Organism: Oryza sativa subsp. japonica (Rice)
Function: Photosystem II (PSII) is a light-driven water:plastoquinone oxidoreductase that uses light energy to abstract electrons from H(2)O, generating O(2) and a proton gradient subsequently used for ATP formation. It consists of a core antenna complex that captures photons, and an electron transfer chain that converts photonic excitation into a charge separation. The D1/D2 (PsbA/PsbA) reaction center heterodimer binds P680, the primary electron donor of PSII as well as several subsequent electron acceptors. D2 is needed for assembly of a stable PSII complex.
Subcellular location: Plastid, chloroplast thylakoid membrane {ECO:0000255|HAMAP-Rule:MF_01383}; Multi-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_01383}.
Interaction partners:
- Photosystem II CP47 reaction center protein
- Photosystem II protein D1
- Cytochrome b559 subunit beta
- Photosystem II CP43 reaction center protein
- Cytochrome b559 subunit alpha
- Photosystem II reaction center protein H
- Photosystem II reaction center protein K
- Cytochrome b6-f complex subunit 4
- Photosystem II reaction center protein L
- Photosystem II reaction center protein J
Sequence:
MTIALGRVTKEENDLFDIMDDWLRRDRFVFVGWSGLLLFPCAYFALGGWFTGTTFVTSWYTHGLASSYLEGCNFLTAAVSTPANSLAHSLLLLWGPEAQGDFTRWCQLGGLWTFVALHGAFALIGFMLRQFELARSVQLRPYNAISFSGPIAVFVSVFLIYPLGQSGWFFAPSFGVAAIFRFILFFQGFHNWTLNPFHMMGVAGVLGAALLCAIHGATVENTLFEDGDGANTFRAFNPTQAEETYSMVTANRFWSQIFGVAFSNKRWLHFFMLFVPVTGLWMSAIGVVGLALNLRAYDFVSQEIRAAEDPEFETFYTKNILLNEGIRAWMAAQDQPHENLIFPEEVLPRGNAL
Protein: Isocitrate dehydrogenase [NADP] (IDH) (EC 1.1.1.42) (IDP) (NADP(+)-specific ICDH) (Oxalosuccinate decarboxylase) (P53982)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: May function in the production of NADPH for fatty acid and sterol synthesis.
Interaction partners:
- Aconitate hydratase, mitochondrial
- 2-oxoglutarate dehydrogenase, mitochondrial
- Isocitrate dehydrogenase cytoplasmic
- Citrate synthase 3, mitochondrial
- Citrate synthase, peroxisomal
- Isocitrate dehydrogenase subunit 1, mitochondrial
- Isocitrate dehydrogenase subunit 2, mitochondrial
- Citrate synthase, mitochondrial
- Glutamate synthase
- NADP-specific glutamate dehydrogenase 1
Sequence:
MSKIKVVHPIVEMDGDEQTRVIWKLIKEKLILPYLDVDLKYYDLSIQERDRTNDQVTKDSSYATLKYGVAVKCATITPDEARMKEFNLKEMWKSPNGTIRNILGGTVFREPIIIPKIPRLVPHWEKPIIIGRHAFGDQYRATDIKIKKAGKLRLQFSSDDGKENIDLKVYEFPKSGGIAMAMFNTNDSIKGFAKASFELALKRKLPLFFTTKNTILKNYDNQFKQIFDNLFDKEYKEKFQALKITYEHRLIDDMVAQMLKSKGGFIIAMKNYDGDVQSDIVAQGFGSLGLMTSILITPDGKTFESEAAHGTVTRHFRKHQRGEETSTNSIASIFAWTRAIIQRGKLDNTDDVIKFGNLLEKATLDTVQVGGKMTKDLALMLGKTNRSSYVTTEEFIDEVAKRLQNMMLSSNEDKKGMCKL
Protein: Sciellin (Q9EQG3)
Organism: Mus musculus (Mouse)
Function: May function in the assembly or regulation of proteins in the cornified envelope. The LIM domain may be involved in homotypic or heterotypic associations and may function to localize sciellin to the cornified envelope (By similarity).
Subcellular location: Cytoplasm. Membrane. Note=May become cross-linked to membrane proteins by transglutaminase.
Interaction partners:
Sequence:
MSNFSSRKKSPTGNDLKSARGAELRQQGFQDVNKRRAFLQDNSWIKKPPEEEQDGNYGRVVLNRHNSHDALDRKLIERDEPKATISRYRSEDMLDRTLSSFRTPQSTKTPAVSSFNANTTATASTPATTPVKKKRQSWFPPPPPGHNASPSTAASRRDPALHPPLPPKPCSPIASPKPLGRTNRQIHAATAGACGETERHAERNIRTEDLDDIIRVAAALQKTDKGEELDNLIRMNKSLNRNQGLDGLFRANLKAQQLDKRAQSLESLIYMNTQTDRDGKGNQAFGSLKKINQRADPDRRSQDLRSVIRTHATAERIGRRKQDLDGLIKVNPDTNKNMKRGKSLDNLIKVTPEVNRSNKGGPSLDNFTKGVPARSRANQRDQDLDSLIKVTPSANRSSQHSLDELINTSPQTIKTTARHQDLDKFIKVNPDVLTNNQRNHDVDSTIRGNPTGTRCEQSEELDNLIKVKPSALRNTNGGQDLESLTEVNSHVAEKNGRIDGQANGLTNSLFKESTRASVYSYEARNSLSSNSGNKNGGPKDTVVYTRTYVENSKSPKDGYQENISGKYIQTVYSTSDRSVIERDMCTYCRKPLGVETKMILDELQICCHSTCFKCEICKRPLENLQAGDSIWIYRQTIHCEPCYSKVMAKWIQ
Protein: Serine/threonine-protein kinase 38-like (EC 2.7.11.1) (NDR2 protein kinase) (Nuclear Dbf2-related kinase 2) (Q7TSE6)
Organism: Mus musculus (Mouse)
Function: Involved in the regulation of structural processes in differentiating and mature neuronal cells.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:15308672}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:15308672}. Membrane {ECO:0000269|PubMed:15308672}. Note=Associated with the actin cytoskeleton. Co-localizes with STK24/MST3 in the membrane.
Interaction partners:
- MOB kinase activator 1A
- MOB kinase activator 2
- Dual specificity protein phosphatase CDC14A
- Dual specificity protein phosphatase CDC14B
- MOB kinase activator 1B
Sequence:
MAMTAGATTTFPMSNHTRERVTVAKLTLENFYSNLILQHEERETRQKKLEVAMEEEGLADEEKKLRRSQHARKETEFLRLKRTRLGLDDFESLKVIGRGAFGEVRLVQKKDTGHIYAMKILRKADMLEKEQVAHIRAERDILVEADGAWVVKMFYSFQDKRNLYLIMEFLPGGDMMTLLMKKDTLTEEETQFYISETVLAIDAIHQLGFIHRDVKPDNLLLDAKGHVKLSDFGLCTGLKKAHRTEFYRNLTHNPPSDFSFQNMNSKRKAETWKKNRRQLAYSTVGTPDYIAPEVFMQTGYNKLCDWWSLGVIMYEMLIGFPPFCSETPQETYRKVMSWKETLAFPPEVPVSEKAKDLILRFCTDSENRIGNGGVEEIKGHPFFEGVDWGHIRERPAAIPIEIRSIDDTSNFDDFPESDILQPVPNTTEPDYKSKDWVFLNYTYKRFEGLTQRGSIPTYMKAGKL
Protein: Achaete-scute homolog 3 (ASH-3) (hASH3) (Class A basic helix-loop-helix protein 42) (bHLHa42) (bHLH transcriptional regulator Sgn-1) (Q9NQ33)
Organism: Homo sapiens (Human)
Function: Transcriptional repressor. Inhibits myogenesis (By similarity).
Subcellular location: Nucleus.
Interaction partners:
- Transcription factor 4
- Transcription factor E2-alpha
Sequence:
MMDNRGNSSLPDKLPIFPDSARLPLTRSFYLEPMVTFHVHPEAPVSSPYSEELPRLPFPSDSLILGNYSEPCPFSFPMPYPNYRGCEYSYGPAFTRKRNERERQRVKCVNEGYAQLRHHLPEEYLEKRLSKVETLRAAIKYINYLQSLLYPDKAETKNNPGKVSSMIATTSHHADPMFRIV
Protein: Protein salvador homolog 1 (45 kDa WW domain protein) (mWW45) (Q8VEB2)
Organism: Mus musculus (Mouse)
Function: Regulator of STK3/MST2 and STK4/MST1 in the Hippo signaling pathway which plays a pivotal role in organ size control and tumor suppression by restricting proliferation and promoting apoptosis. The core of this pathway is composed of a kinase cascade wherein STK3/MST2 and STK4/MST1, in complex with its regulatory protein SAV1, phosphorylates and activates LATS1/2 in complex with its regulatory protein MOB1, which in turn phosphorylates and inactivates YAP1 oncoprotein and WWTR1/TAZ. Phosphorylation of YAP1 by LATS1/2 inhibits its translocation into the nucleus to regulate cellular genes important for cell proliferation, cell death, and cell migration. SAV1 is required for STK3/MST2 and STK4/MST1 activation and promotes cell-cycle exit and terminal differentiation in developing epithelial tissues. Plays a role in centrosome disjunction by regulating the localization of NEK2 to centrosomes, and its ability to phosphorylate CROCC and CEP250. In conjunction with STK3/MST2, activates the transcriptional activity of ESR1 through the modulation of its phosphorylation (By similarity).
Subcellular location: Nucleus {ECO:0000250}. Cytoplasm {ECO:0000250}.
Interaction partners:
- Serine/threonine-protein kinase LATS1
- Serine/threonine-protein kinase 4
- Serine/threonine-protein kinase LATS2
- Serine/threonine-protein kinase 3
- Wilms tumor protein 1-interacting protein
- LIM domain-containing protein 1
- MOB kinase activator 1A
- Merlin
- LIM domain-containing protein ajuba
- Ras association domain-containing protein 1
Sequence:
MLSRKKTKNEVSKPAEVQGKYVKKETSPLLRNLMPSFIRHGPTIPRRTDLCLPDSSATAFSASGDGVVSRNQSFLRTAIQRTPHEVMRRESHRLSAPSYLVRSLADVPRECGSSQSFLTEVNFAVENGDSGSRYFFSDNFFDGQRRRPLGDRAQEDYRYYEYNHDLFQRMPQSQGRHTSGIGRVTATSLGNLTNHGSEDLPLPPGWSVDWTMRGRKYYIDHNTNTTHWSHPLEREGLPPGWERVESSEFGTYYVDHTNKRAQYRHPCAPSVPRYDQPPPITYQPQQTERNQSLLVPANPYHTAEIPDWLQVYARAPVKYDHILKWELFQLADLDTYQGMLKLLFMKELEQIVKLYEAYRQALLTELENRKQRQQWYAQQHGKTFLS
Protein: Serine/threonine-protein kinase PRP4 homolog (EC 2.7.11.1) (PRP4 pre-mRNA-processing factor 4 homolog) (Pre-mRNA protein kinase) (Q61136)
Organism: Mus musculus (Mouse)
Function: Has a role in pre-mRNA splicing. Phosphorylates SF2/ASF.
Subcellular location: Nucleus {ECO:0000269|PubMed:12077342}. Chromosome, centromere, kinetochore {ECO:0000250|UniProtKB:Q13523}. Note=Located throughout the nucleus, excluding the nucleolus but enriched in multiple speckles. {ECO:0000269|PubMed:12077342}.
Interaction partners:
- RNA-binding protein 25
- Transcription elongation regulator 1
- Pre-mRNA-processing factor 6
- Pinin
- U4/U6 small nuclear ribonucleoprotein Prp31
- Pre-mRNA-processing factor 40 homolog A
- Serine/arginine repetitive matrix protein 2
- Pre-mRNA-processing-splicing factor 8
- RNA-binding protein 39
- 116 kDa U5 small nuclear ribonucleoprotein component
Sequence:
MAATEPPSLREQAEMDDADNSEKSVNEENGEVSEDQSQNKHSRHKKKKHKHRSKHKKHKHSSEEDRDKKHKHKHKHKKHKRKEVIEASDKEGLSPAKRTKLDDLALLEDLEKQRALIKAELDNELMEGKVQSGMGLILQGYESGSEEEGEIHEKARNGNRSSTRSSSTRGKLEITDNKNSAKKRSKSRSKERTRHRSDKRKSKGAGEMLREKANRSKSKERRKSKSPSKRSKSQDQARKSKSPPLRRRSQEKVGKARSPAEEKMKSEEKGKIKDRKKSPIVNERSRDRSKKSKSPVDLRDKSKDRRSRSKERKSKRSEIDKEKKPIKSPSKDASSGKENRSPSRRPGRSPKRRSLSPKLRDKSRRSRSPLLNDRRSKQSKSPSRTLSPGRRAKSRSLERKRREPERRRLSSPRTRPRDDILGRCERSKDASPINRWSPTRRRSRSPIRRRSRSPLRRSRSPRRRSRSPRRRDRSRRSRSRLRRRSRSRGGHRRRSRSKVKEDKFKGSLSEGMKVEQESSSDDNLEDFDVEEEDEEALIEQRRIQRQAIVQKYKYLAEDSNISVPSEPSSPQSSTRSRSPSPDDILERVAADVKEYERENVDTFEASVKAKHNLMTVEQNNGSSQKKILAPDMFTESDDMFAAYFDSARLRAAGIGKDFKENPNLRDNWTDAEGYYRVNIGEVLDKRYNVYGYTGQGVFSNVVRARDNARANQEVAVKIIRNNELMQKTGLKELEFLKKLNDADPDDKFHCLRLFRHFYHKQHLCLVFEPLSMNLREVLKKYGKDVGLHIKAVRSYSQQLFLALKLLKRCNILHADIKPDNILVNESKTILKLCDFGSASHVADNDITPYLVSRFYRAPEIIIGKSYDYGIDMWSVGCTLYELYTGKILFPGKTNNHMLKLAMDLKGKMPNKMIRKGVFKDQHFDQNLNFMYIEVDKVTEREKVTVMSTINPTKDLLADLIGCQRLPEDQRKKVHQLKDLLDQILMLDPAKRISINQALQHAFIQEKI
Protein: Pro-neuropeptide Y [Cleaved into: Neuropeptide Y (Neuropeptide tyrosine) (NPY); C-flanking peptide of NPY (CPON)] (P01304)
Organism: Sus scrofa (Pig)
Function: NPY is implicated in the control of feeding and in secretion of gonadotrophin-release hormone.
Subcellular location: Secreted. Cytoplasmic vesicle, secretory vesicle, neuronal dense core vesicle {ECO:0000250|UniProtKB:P07808}.
Interaction partners:
- Neuropeptide Y receptor type 2
- Neuropeptide Y receptor type 1
- Leptin
- Neuropeptide Y receptor type 5
- Cholecystokinin
- Pro-opiomelanocortin
- Somatostatin
- Peptide YY
- Neuropeptide Y receptor type 1
- Agouti-related protein
Sequence:
VCLCALAEAYPSKPDNPGEDAPAEDLARYYSALRHYINLITRQRYGKRSSPETLISDLLMREGTENVPRTRLEDPS
Protein: 2-hydroxy-palmitic acid dioxygenase MPO1 (EC 1.14.18.12) (Metabolism of phytosphingosine to odd-numbered fatty acids protein 1) (Metabolism of PHS to odd-numbered FA protein 1) (P25338)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Dioxygenase that catalyzes the alpha-oxidation of 2-hydroxy fatty acids in an iron-dependent manner. Involved in metabolism of phytosphingosine and is required for proper endoplasmic reticulum stress response.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:25345524}; Multi-pass membrane protein {ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:25345524}.
Interaction partners:
Sequence:
MGEGLLDLRSQLGFYKFYHHNPKNVLIHSIFVPTILFSGSCMLHRVKIYQSISLTAVLSVLFSIFYCLLYLPTGLLAGVLLLLLNLALIDHRVDLTFKQELGLFTIGWIFQFVGHGVFEKRRPALIDNLVQSLVLAPYFIMFEFLFKLGFMPRLKATLEHDLEIKQRNLRMQRQ
Protein: LD22662p (Loechrig isoform I) (SNF4/AMP-activated protein kinase gamma subunit, isoform F) (SNF4/AMP-activated protein kinase gamma subunit, isoform R) (SNF4/AMP-activated protein kinase gamma subunit, isoform S) (Q9VDD2)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- non-specific serine/threonine protein kinase
- 5'-AMP-activated protein kinase subunit beta-1
- Serine/threonine-protein kinase STK11
- Raptor, isoform B
- Forkhead box protein O
- Serine/threonine-protein kinase mTor
- Cystathionine beta-synthase
- calcium/calmodulin-dependent protein kinase
- Tribbles
- LD44138p
Sequence:
MATNCDFIEQPVKQQPLANAPVMGVQEDKAQEPKELPDEPAKQPDGQPYQHFAGEDSFECAFESTMDDLEQGVLDGYESDSEASANDQITDSASSGSLGQLAQQQQREERLRGLPGPLHGQHIDSEMLKCMPRSNSFDFHSSSGSSSDDEDDPDDDDDDQVHHSLGLSLSGKFVKVDLYSGHQRPGYLLPPYIERRRLSQCKEEDDEDEGDRTQLGGGSSSTGESTKSEKASKAPPRPPTPQDEASKEKFKDLERLRQQFMHKIDRINTRNIEESEAPPPPPPPPPPIPATILPKALKALLHTQEPVAPPSRPSPVGPPSPAPTSSVIVAKETPVPVTPEPVSPLPLPTEPPLIIKGKFKVTLAQETPELRVEAQKLSKLNASSNAHTISFPSSFGGYSSVQGLFSQRYGSNRFPTAAPHMSKQFFEPSLVEIRTPAQSNVALNTTGLANSNHQSLTCDTNSLANKPRTPSERELDEIWIRRQDGGLSGTAAPGAPGAPLPLLQQQQQQQRPVSLGGASTMPRLLRSESSASTTSPSRQLTNSGSVSVSVSDDEQDGSLGGAGRMPGSRPSSAPAEPNAKAAKKAYKKMEKEQRRQEKEQSRREKEARKLERETARRNEREAAKLEKINRHSEKISRSTERMAMAGVGSRSGSLERRRSGEDSPVLNQSTVHGIASPNRRPTIFDVFRPRAKSDAKRQKEKHLLDPSSADSSATSSTYSVSGGTGPATSSAAGGAGGAAAAAGQGAAGGAGGLMNSMKVAMQNFSHRQHPAVTITSADGTQSTAKSKYKDGSAHPHQGSDAQYYHTVTAVRPNSSQRSPMTKVMDLFRHRSSSVVSEADKRKARAAAHQQQLAVQSAHMRRASADLEKRRASVGAAGRGLRGDGTLDPHHAAILFRDSRGLPVADPFLEKVNLSDLEEDDSQIFVKFFRFHKCYDLIPTSAKLVVFDTQLLVKKAFYALVYNGVRAAPLWDSEKQQFVGMLTITDFIKILQMYYKSPNASMEQLEEHKLDTWRSVLHNQVMPLVSIGPDASLYDAIKILIHSRIHRLPVIDPATGNVLYILTHKRILRFLFLYINELPKPAYMQKSLRELKIGTYNNIETADETTSIITALKKFVERRVSALPLVDSDGRLVDIYAKFDVINLAAEKTYNDLDVSLRKANEHRNEWFEGVQKCNLDESLYTIMERIVRAEVHRLVVVDENRKVIGIISLSDILLYLVLRPSGEGVGGSESSLRASDPVLLRKVAEVEIPATAAAATTTTPPRSPSAGSGNRSLIEDIPEEETAPARSDDADSDNNKSASEDKANNNQHDQTTTAATANGDSNNSPVEVSFADEAQEEEAADQVERSNCDDDDQPALAEIERKNASMDDDEDDGMSSAVSAASALGQSLTPAAQEMALVSE
Protein: Riboflavin transporter (Q9V9S9)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004651, ECO:0000256|RuleBase:RU368035}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651, ECO:0000256|RuleBase:RU368035}.
Interaction partners:
Sequence:
MSRYHRGRGAGSPTNPAGPVYGVISTLDDATPSPADFARCSSLEAKKSELSLFLNWGGPQKNMEISSKLRNRSWLVDVLAIFFGIGTWLGVNGTFIQLPLLVDEAPEGWSLPSYLSVMVQIGNLGPLLYTAIQKYSPKKLNDGWTIHGVLLVGAISCLLTAFFYNQTASVAGTDHSLALFLLTCFTALNACTSSVLFMPYMGRFKEQYMVTYFIGEGLSGLLPSVTALIQGIGESGDCVLVNVTESGEEVYALRKTPPRFDTRVFFLILFALMVLAYVGYALLNSLPLARREYAQVTVSEGNKYVYGEADNQPKAEKLSKGQYTYLLLLIGAISLFSNGMFGSIQSYSSAPYGSQAYHLAATLSVIANPVACFMAMFLHFTSLRIITVLSILAGLLTSYVFTTAALSPLPPLHDQTVGAVLVVTAWTLLVGIVSYTKLGITTVMRAQGGQSLVWVGAITQLGSAIGAVAIFFAINYSDLFQAAESNC