wanglab/gogpt-training-data huggingface dataset:
Protein: Protein regulator of cytokinesis 1 (O43663)
Organism: Homo sapiens (Human)
Function: Key regulator of cytokinesis that cross-links antiparrallel microtubules at an average distance of 35 nM. Essential for controlling the spatiotemporal formation of the midzone and successful cytokinesis. Required for KIF14 localization to the central spindle and midbody. Required to recruit PLK1 to the spindle. Stimulates PLK1 phosphorylation of RACGAP1 to allow recruitment of ECT2 to the central spindle. Acts as an oncogene for promoting bladder cancer cells proliferation, apoptosis inhibition and carcinogenic progression.
Subcellular location: Nucleus {ECO:0000269|PubMed:17409436}. Cytoplasm. Cytoplasm, cytoskeleton, spindle pole {ECO:0000269|PubMed:15297875, ECO:0000269|PubMed:15625105}. Midbody {ECO:0000269|PubMed:15297875, ECO:0000269|PubMed:15625105, ECO:0000269|PubMed:17409436, ECO:0000269|PubMed:35849559}. Chromosome {ECO:0000269|PubMed:15297875}. Note=Colocalized with KIF20B in the nucleus of bladder carcinoma cells at the interphase. Colocalized with KIF20B in bladder carcinoma cells at prophase, metaphase, early anaphase, at the midzone in late anaphase and at the contractile ring in telophase (PubMed:17409436). Predominantly localized to the nucleus of interphase cells. During mitosis becomes associated with the mitotic spindle poles and localizes with the cell midbody during cytokinesis. Co-localizes with PRC1 in early mitosis and at the spindle midzone from anaphase B to telophase (PubMed:15297875, PubMed:15625105). {ECO:0000269|PubMed:15297875, ECO:0000269|PubMed:15625105, ECO:0000269|PubMed:17409436}.
Interaction partners:
- Targeting protein for Xklp2
- Chromosome-associated kinesin KIF4A
- Kinesin-like protein KIF23
- Centromere-associated protein E
- Kinesin-like protein KIF14
- Rac GTPase-activating protein 1
- Kinesin-like protein KIF11
- Serine/threonine-protein kinase PLK1
- Cell division cycle protein 20 homolog
- Kinesin-like protein KIF2C
Sequence:
MRRSEVLAEESIVCLQKALNHLREIWELIGIPEDQRLQRTEVVKKHIKELLDMMIAEEESLKERLIKSISVCQKELNTLCSELHVEPFQEEGETTILQLEKDLRTQVELMRKQKKERKQELKLLQEQDQELCEILCMPHYDIDSASVPSLEELNQFRQHVTTLRETKASRREEFVSIKRQIILCMEALDHTPDTSFERDVVCEDEDAFCLSLENIATLQKLLRQLEMQKSQNEAVCEGLRTQIRELWDRLQIPEEEREAVATIMSGSKAKVRKALQLEVDRLEELKMQNMKKVIEAIRVELVQYWDQCFYSQEQRQAFAPFCAEDYTESLLQLHDAEIVRLKNYYEVHKELFEGVQKWEETWRLFLEFERKASDPNRFTNRGGNLLKEEKQRAKLQKMLPKLEEELKARIELWEQEHSKAFMVNGQKFMEYVAEQWEMHRLEKERAKQERQLKNKKQTETEMLYGSAPRTPSKRRGLAPNTPGKARKLNTTTMSNATANSSIRPIFGGTVYHSPVSRLPPSGSKPVAASTCSGKKTPRTGRHGANKENLELNGSILSGGYPGSAPLQRNFSINSVASTYSEFAKDPSLSDSSTVGLQRELSKASKSDATSGILNSTNIQS
Protein: Epstein-Barr nuclear antigen 2 (EBNA-2) (EBV nuclear antigen 2) (P12978)
Organism: Epstein-Barr virus (strain B95-8) (HHV-4) (Human herpesvirus 4)
Function: Plays a key role in the activation of the host resting B-cell and stimulation of B-cell proliferation. Acts by up-regulating the expression of viral EBNA1-6, LMP1, LMP2A and LMP2B genes, as well as several host genes including CD21, CD23 and MYC. Activates transcription by acting as an adapter molecule that binds to cellular sequence-specific DNA-binding proteins such as host CBF1, SMARCB1 and SPI1. Once EBNA2 is near promoter sites, its acidic activating domain recruits basal and activation-associated transcription factors TFIIB, TAF40, TFIIH components ERCC2 and ERCC3, and CBP in order to promote transcription. Alternatively, EBNA2 can affect activities of cell cycle regulators and retard cell cycle progression at G2/M phase. It also induces chromosomal instability, by disrupting mitotic checkpoints, multi-nucleation and formation of micronuclei in infected cells.
Subcellular location: Host nucleus matrix {ECO:0000269|PubMed:2161150}. Note=Associated with the nuclear matrix.
Interaction partners:
Sequence:
MPTFYLALHGGQTYHLIVDTDSLGNPSLSVIPSNPYQEQLSDTPLIPLTIFVGENTGVPPPLPPPPPPPPPPPPPPPPPPPPPPPPPPSPPPPPPPPPPPQRRDAWTQEPSPLDRDPLGYDVGHGPLASAMRMLWMANYIVRQSRGDRGLILPQGPQTAPQARLVQPHVPPLRPTAPTILSPLSQPRLTPPQPLMMPPRPTPPTPLPPATLTVPPRPTRPTTLPPTPLLTVLQRPTELQPTPSPPRMHLPVLHVPDQSMHPLTHQSTPNDPDSPEPRSPTVFYNIPPMPLPPSQLPPPAAPAQPPPGVINDQQLHHLPSGPPWWPPICDPPQPSKTQGQSRGQSRGRGRGRGRGRGKGKSRDKQRKPGGPWRPEPNTSSPSMPELSPVLGLHQGQGAGDSPTPGPSNAAPVCRNSHTATPNVSPIHEPESHNSPEAPILFPDDWYPPSIDPADLDESWDYIFETTESPSSDEDYVEGPSKRPRPSIQ
Protein: Multiplexin, isoform J (E1JI52)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MGPPGPPGPPGLPENYDESLMVNSMGAFRGTTQPGAKGVPGEKGDAGQKGERGDPGHKGAHGPSGAKGEPGEPGTPGLPGLPGQVGQPGGLDGLASANGTKGEKGEKGEKGMRGRRGGTGATGPIGPPGKPGPMGDIGHSGRPGMTGPKGEMGPKGPKGDSGGREGLKGDKGDRGQDGRDGLPGPPGLPSTGGGDGDSGGVQYIPMPGPPGPPGPPGLPGLSISGPKGEPGVDSRSSFFGDASYYGRPEPPRQPGHSHKHEETLGLVDGEEPYFSASSSNMNMKIVPGAVTFQNIDEMTKKSALNPPGTLAYITEEEALLVRVNKGWQYIALGTLVPIATPAPPTTVAPSMRFDLQSKNLLNSPPPLLNTPTLRVAALNEPSTGDLQGIRGADFACYRQGRRAGLLGTFKAFLSSRVQNLDTIVRPADRDLPVVNTRGDVLFNSWKGIFNGQGGFFSQAPRIYSFSGKNVMTDSTWPMKMVWHGSLPNGERSMDTYCDAWHSGDHLKGSFASNLDGHKLLEQKRQSCDSKLIILCVEALSQDRKRKKREIGDGSSHGESESREFKTADEYAAHLENLLL
Protein: PknH-like extracellular domain-containing protein (O69673)
Organism: Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh)
Interaction partners:
Sequence:
MRIAAAVVSIGLAVIAGFAVPVADAHPSEPGVVSYAVLGKGSVGNIVGAPMGWEAVFTRPFQAFWVELPACNNWVDIGLPEVYDDPDLASFNGATTQTSATDQTHLVKQAVGVFASNDAADRAFHRVVDRTVGCSGQTTAIHLDDGTTQVWSFAGGPSTGTDEAWTKQEAGTDRRCFVQTRLRENVLLQAKVCQSGNAGPAVNVLAGAMQNTLG
Protein: Reticulon-4 receptor (Nogo receptor) (NgR) (Nogo-66 receptor) (Q99M75)
Organism: Rattus norvegicus (Rat)
Function: Receptor for RTN4, OMG and MAG. Functions as receptor for the sialylated gangliosides GT1b and GM1. Besides, functions as receptor for chondroitin sulfate proteoglycans. Can also bind heparin. Intracellular signaling cascades are triggered via the coreceptor NGFR (By similarity). Signaling mediates activation of Rho and downstream reorganization of the actin cytoskeleton. Mediates axonal growth inhibition. May play a role in regulating axon regeneration and neuronal plasticity in the adult central nervous system. Plays a role in postnatal brain development. Required for normal axon migration across the brain midline and normal formation of the corpus callosum (By similarity). Protects motoneurons against apoptosis; protection against apoptosis is probably mediated via interaction with MAG. Acts in conjunction with RTN4 and LINGO1 in regulating neuronal precursor cell motility during cortical development. Like other family members, plays a role in restricting the number dendritic spines and the number of synapses that are formed during brain development.
Subcellular location: Cell membrane {ECO:0000269|PubMed:15673660, ECO:0000269|PubMed:19420245, ECO:0000269|PubMed:22325200}; Lipid-anchor, GPI-anchor {ECO:0000250|UniProtKB:Q99PI8}. Membrane raft {ECO:0000269|PubMed:15673660}. Cell projection, dendrite {ECO:0000250|UniProtKB:Q99PI8}. Perikaryon {ECO:0000269|PubMed:15673660}. Cell projection, axon {ECO:0000269|PubMed:12426574}. Note=Detected along dendrites and axons, close to synapses, but clearly excluded from synapses. {ECO:0000250|UniProtKB:Q99PI8}.
Interaction partners:
- Reticulon-4
- Myelin-associated glycoprotein
- Tumor necrosis factor receptor superfamily member 16
- Aminopeptidase N
- Leucine rich repeat and Ig domain containing 1
- Oligodendrocyte-myelin glycoprotein
- Ig gamma-1 chain C region
- Paired Ig-like receptor B
- Neutrophil immunoglobulin-like receptor 1
- TNF receptor superfamily member 19
Sequence:
MKRASSGGSRLLAWVLWLQAWRVATPCPGACVCYNEPKVTTSCPQQGLQAVPTGIPASSQRIFLHGNRISYVPAASFQSCRNLTILWLHSNALAGIDAAAFTGLTLLEQLDLSDNAQLRVVDPTTFRGLGHLHTLHLDRCGLQELGPGLFRGLAALQYLYLQDNNLQALPDNTFRDLGNLTHLFLHGNRIPSVPEHAFRGLHSLDRLLLHQNHVARVHPHAFRDLGRLMTLYLFANNLSMLPAEVLVPLRSLQYLRLNDNPWVCDCRARPLWAWLQKFRGSSSEVPCNLPQRLAGRDLKRLAASDLEGCAVASGPFRPFQTNQLTDEELLGLPKCCQPDAADKASVLEPGRPASAGNALKGRVPPGDTPPGNGSGPRHINDSPFGTLPGSAEPPLTALRPGGSEPPGLPTTGPRRRPGCSRKNRTRSHCRLGQAGSGSSGTGDAEGSGALPALACSLAPLGLALVLWTVLGPC
Protein: Envelope glycoprotein K (Q77CE8)
Organism: Bovine herpesvirus 1.1 (strain Cooper) (BoHV-1) (Infectious bovine rhinotracheitis virus)
Subcellular location: Host Golgi apparatus membrane {ECO:0000256|ARBA:ARBA00004252}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004252}. Host cell membrane {ECO:0000256|ARBA:ARBA00004598}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004598}. Host endosome membrane {ECO:0000256|ARBA:ARBA00004330}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004330}.
Interaction partners:
Sequence:
MLLGGRTVNLAALALLTAHLALALWVALAARCQRCACVRATARNGSLRWELRSPGAVYVWGGANNATLAADAPCRHAVVQHIPPGLLDGDEALHGRVRAVAGARDCRAYLWCAQARGGLLAWLLYVAFVYLRQERRMFGLCRNDADFLSPGGYTLNYAAAALAAVVGHGPYTKLARLMCELSARRRALAVDFRLDPLGCAWRPRAALPLLAEGFARLGARIAAAGSVGITHPCAAAYPLYLKIWAWVHVALFAGLELVSLLYRKPRRRGGTCAGDGGDGGESGIRKVCVNCCSTLLAGLLVKALYLAAIVGGVIALLHYEHNLRLRLLGAQT
Protein: non-specific serine/threonine protein kinase (EC 2.7.11.1) (M9PFS3)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MQKENNVTAENCQFVGPYRLEKTLGKGQTGLVKLGVHCVIGKKVAIKIINREKLSESVLMKVEREIAIMKLIDHPHVLGLSDVYENKKYLYLILEHVSGGELFDYLVKKGRLTPKEARKFFRQIISALDFCHSHSICHRDLKPENLLLDEKNNIKIADFGMASLQPAGSMLETSCGSPHYACPEVIRGEKYDGRKADVWSCGVILYALLVGALPFDDDNLRQLLEKVKRGVFHIPHFVPPDCQSLLRGMIEVNPDRRLTLAEINRHPWVTAGGKGELELELPMMEVVQTHVIPTATAVDPDVLNAICSLGCFKEKEKLIQELLSSSHNTEKVIYFLLLERKRRRPALEDDDEIAQKSRSELDAVDPPRKRLDTCRINGTNAPSYGQISEGSPLTPRRQAFNFRSYSSTRNHQRRSPTTVTSSVRSSSYHSPTRCNSPMSSAQQQANAISRPSSPAAGTRHSTYGDRDRSGHHSSVSRTPSHSSQKSIEGDVVVVREPRIERRDSLRQERGGGSPRDRGDCGIPPGSPGGNSSGSTSASPSVHHRANSVVNPNGSPMMNNSSPGMPGSPCNTPGGQLWKTRLTNIKNSFLGSPRFHRRKMQVSADEVHLTPESSPELTKRSWFGNLITTEKDETFTILVKGKPIATVKAHLIHAFLSMAELSHSVVSPTSFRVEYKRNGNGPVMFQRHVKFQVDISAICKQGDIADMLFALTFTLLSGNIRRFRRICEHIQSQVCSKRFPGPSSPPTVTSVTQAVSESSSCGSVSSERLSYKRQVIENDMENDSIFSYKSGNGRRASTTNNNNANPVDIPGSPIAVRSNSETAEHERNRELQSERQATTMSGSAIA
Protein: dTDP-4-keto-6-deoxy-D-glucose reductase (EC 1.1.1.-) (Novobiocin biosynthesis protein S) (Q9L9E9)
Organism: Streptomyces niveus (Streptomyces spheroides)
Function: Reduces the product formed from the reaction of NovW with dTDP-4-keto-6-deoxy-D-glucose to result in dTDP-5-methyl-L-rhamnose in the novobiocin biosynthesis pathway, an aminocoumarin family antibiotic that targets bacterial DNA gyrases.
Interaction partners:
Sequence:
MTDRWLVTGAAGMLGRDLVALLRGLNEPVVAITRHDLDITDRLSVRAVVDRHRPTTIVNCAAWTRFGEAEAGESAALLVNGGGARELAAVCRDRSIRLVHLSTDYVFDGTSRRPYAESAVTSPINAYGRTKQAGEQAVLDLLPDDGTIVRTAWLYGRHGMNFIRKMVRLEQLRETVDVVDDQWGQPTWTVDLAQQIVALVRHGASGVFHGTSAGEATWYDLARMTFRLLGADPGRVRPVPSDRIAGGELRPRYTVLGHDAWREAGLTPIRHWTTALTQAFPLLNADES
Protein: Odorant receptor 47a (P81921)
Organism: Drosophila melanogaster (Fruit fly)
Function: Odorant receptor which mediates acceptance or avoidance behavior, depending on its substrates. The odorant receptor repertoire encodes a large collection of odor stimuli that vary widely in identity, intensity, and duration. Complexes with Orco to form odorant-sensing units, providing sensitive and prolonged odorant signaling and calcium permeability. They are necessary and sufficient to promote functional reconstitution of odor-evoked signaling in sensory neurons that normally respond only to carbon dioxide. Involved in the behavioral responses to esters. Involved in the behavioral responses to pentyl acetate.
Subcellular location: Cell membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}.
Interaction partners:
- Odorant receptor 56a
- Odorant receptor 33a
- Odorant receptor 85a
- Odorant receptor 42b
- Odorant receptor 22a
- Odorant receptor 30a
- Odorant receptor 47b
- Odorant receptor 88a
- Odorant receptor 98a
- Odorant receptor 67b
Sequence:
MDSFLQVQKSTIALLGFDLFSENREMWKRPYRAMNVFSIAAIFPFILAAVLHNWKNVLLLADAMVALLITILGLFKFSMILYLRRDFKRLIDKFRLLMSNEAEQGEEYAEILNAANKQDQRMCTLFRTCFLLAWALNSVLPLVRMGLSYWLAGHAEPELPFPCLFPWNIHIIRNYVLSFIWSAFASTGVVLPAVSLDTIFCSFTSNLCAFFKIAQYKVVRFKGGSLKESQATLNKVFALYQTSLDMCNDLNQCYQPIICAQFFISSLQLCMLGYLFSITFAQTEGVYYASFIATIIIQAYIYCYCGENLKTESASFEWAIYDSPWHESLGAGGASTSICRSLLISMMRAHRGFRITGYFFEANMEAFSSIVRTAMSYITMLRSFS
Protein: Cocaine- and amphetamine-regulated transcript protein [Cleaved into: CART(1-52); CART(55-102); CART(62-102)] (P49192)
Organism: Rattus norvegicus (Rat)
Function: Satiety factor closely associated with the actions of leptin and neuropeptide y; this anorectic peptide inhibits both normal and starvation-induced feeding and completely blocks the feeding response induced by neuropeptide Y and regulated by leptin in the hypothalamus.
Subcellular location: Secreted {ECO:0000305}.
Interaction partners:
- Enoyl-CoA delta isomerase 2
- Hydroxymethylglutaryl-CoA synthase, mitochondrial
- Hydroxyacyl-coenzyme A dehydrogenase, mitochondrial
- Hydroxymethylglutaryl-CoA synthase, cytoplasmic
- Lambda-crystallin homolog
- Hydroxysteroid dehydrogenase-like protein 2
- Enoyl-CoA hydratase, mitochondrial
- Ethylmalonyl-CoA decarboxylase
Sequence:
MESSRLRLLPVLGAALLLLLPLLGAGAQEDAELQPRALDIYSAVDDASHEKELPRRQLRAPGAVLQIEALQEVLKKLKSKRIPIYEKKYGQVPMCDAGEQCAVRKGARIGKLCDCPRGTSCNSFLLKCL
Protein: Fe2OG dioxygenase domain-containing protein (Q5BG04)
Organism: Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Interaction partners:
Sequence:
MGSINETQTTSIPTVDIGPFLDGQAAQEAKDAVVAAMRHACSTFGFFYLVGHGIPEEDRLQILKCTKRYFDLPMEEKMETWIGKAIGRSFRGYEPPALQVHQEGLLPDTKEGFILGRETPADAPEAGTFHTGPNQWPKTLPDEEFRVPIMRYHAKMIEMVKVILKILALGLPAEWNCPSDVFDELTINPSAPLRLLYYAPQPVKHENQFGVGAHTDFGNVSVLLQEEDSEGLEVFYPPTQTWVPVPAKPHSYVINMGDMMQKWTAGYYRSALHRVVNSNTKPRYSAPFFMNGNLDVKCYALDGSGEVTTIGEHIRKRLMETIGGEEGKKLGL
Protein: Dolichol phosphate-mannose biosynthesis regulatory protein (A0A1D8PPC1)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Subcellular location: Endoplasmic reticulum membrane {ECO:0000256|ARBA:ARBA00004477, ECO:0000256|RuleBase:RU365084}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004477, ECO:0000256|RuleBase:RU365084}.
Interaction partners:
- Dolichol-phosphate mannosyltransferase subunit 3
- Dolichol-phosphate mannosyltransferase subunit 1
- Phosphatidylinositol N-acetylglucosaminyltransferase
- Phosphatidylinositol N-acetylglucosaminyltransferase
- Phosphatidylinositol N-acetylglucosaminyltransferase
- Phosphatidylinositol N-acetylglucosaminyltransferase GPI3 subunit
- Phosphatidylinositol N-acetylglucosaminyltransferase
- dolichyl-phosphate beta-glucosyltransferase
- dolichol kinase
- N-acetylglucosaminylphosphatidylinositol deacetylase
Sequence:
MGADKLIGFGMLGVAAFVFTYYTAWVFVLPFINEDNILNQFFLPRDYAIKLPILLLFIAALGVGTFVGKVLIKNQQKQKSKKKAQ
Protein: GMP synthase [glutamine-hydrolyzing] (EC 6.3.5.2) (GMP synthetase) (Glutamine amidotransferase) (P32073)
Organism: Dictyostelium discoideum (Social amoeba)
Interaction partners:
- Inosine-5'-monophosphate dehydrogenase
- Guanylate kinase
- Probable adenine phosphoribosyltransferase
- Hypoxanthine-guanine phosphoribosyltransferase
- Inosine triphosphate pyrophosphatase
- CTP synthase
- Bifunctional purine biosynthetic protein purD
- Asparagine synthetase
- Glutamyl-tRNA
- Protein transport protein got1 homolog
Sequence:
MTITSPVIKTPPLNSEIRLESNLTVESGDIEINEKDIVNASEVIVILDAGSQYSKVIDRRVRELNVASEIHPLNIDLLELIKIKSKSGSTIKGIIISGGPESVYGENAPKFDKSLFSEKLNLPIFGICYGMQLMNYIFGGKVESNSQREDGVHNIEILKDENQQLVSKLFKNLNQTEQVLLTHGDSVTKIADGFKIICKSDDGIVSGIENERLGYYGVQFHPEVDLTTNGKKMFSNFLIDICGCSANYTLDDREQQAITYIKSIVSNKKVLVLVSGGVDSTVCAALISKAIGPENVIALHIDNGFMRKDESLNVEKALSVLGLHLIVVDASQTFYNSTTTIKGHLTSSLKETISPEERRKIIGDTFMRVAENEVKKLGLQPEDVYLAQGTLRPDLIESSSKTVSGVADVIKTHHNDTELVRILRDSGRVVEPLKDYHKDEVRELGKSLGLSDSLVWRQPFPGPGLAIRIICADEPYLVNYDFTNNVVQYLVTGEASSELESEVKIKIDKQLTEMKCKRQDKITIKPVLLPIQTVGVQGDGRTYSYLLGLYSSENSTIDQIPWSYIFNLARTIPKICHNINRVVFIFSQNATKHTNIKVSNEPVKHITPTRLTPDVIKQLQHADSIVSEQLYKYNLIKSLSQVPVVSLPIDFGVTGNRSIAIRTFITNDFMTGVPAIPGKNISFDCLQEITNNILTSVNGISKVLFDCTSKPPGTTEFL
Protein: Sulfotransferase 2A8 (SULT2A8) (Glycochenodeoxycholate sulfotransferase 2A8) (EC 2.8.2.34) (Liver sulfotransferase-like protein) (L-STL) (Q8BGL3)
Organism: Mus musculus (Mouse)
Function: Hepatic sulfotransferase involved in the maintenance of bile acid homeostasis and energy balance. Catalyzes the transfer of sulfonate group from 3'-phosphoadenylyl sulfate (PAPS) to the 7-alpha hydroxy group of primary bile acids to form 7-monosulfate derivatives in the pathway of bile acid elimination. Displays high catalytic efficiency toward cholate, chenodeoxycholate and their glycine and taurine conjugates.
Subcellular location: Cytoplasm, cytosol {ECO:0000269|PubMed:28442498}.
Interaction partners:
- Cytochrome P450 1B1
- Cytochrome P450 1A1
Sequence:
MTDEFLWIEGIPFPTVYYSQEIIREVRDRFVVRDEDTIIVTYPKSGTHWLNEIVCLILTKGDPTWVQSTIANERTPWIEFENNYRILNSKEGPRLMASLLPIQLFPKSFFSSKAKVIYLIRNPRDVLVSGYHYFNALKQGKEQVPWKIYFENFLQGKSYFGSWFEHACGWISLRKRENILVLSYEQLKKDTRNTIKKICEFLGENLESGELELVLKNISFQIMKERMISQSCLSNIEKHEFIMRKGITGDWKNHFTVAQAEAFDKAFQEKAADFPQELFSWE
Protein: Transcription factor ast-1 (axon steering defect-1) (Q22355)
Organism: Caenorhabditis elegans
Function: Transcription factor. Probably binds to DNA sequences containing the consensus motif 5'-CGGA[AT][AG]-3'. Positively modulates expression of dopamine pathway genes, acting as a terminal selector for differentiation of dopaminergic neurons; may act in concert with homeobox proteins ceh-40, ceh-43 and ceh-20. Required for axon navigation in some interneurons, perhaps acting in the same pathways as basement membrane protein nid-1 and unc-6/netrin. Plays a role in the differentiation of the ventral cord pioneer neuron AVG. Required for morphogenesis of the pharynx.
Subcellular location: Nucleus {ECO:0000255|RuleBase:RU004019, ECO:0000269|PubMed:16584723, ECO:0000269|PubMed:22069471}. Cell projection, neuron projection {ECO:0000269|PubMed:16584723}. Note=Initially localized only in the nucleus, but later in development, at about the 3-fold stage, expressed elsewhere in the cell body and also in the neuronal projections. {ECO:0000269|PubMed:16584723}.
Interaction partners:
- Homeobox protein ceh-43
- ETS domain-containing transcription factor ets-5
- LIM/homeobox protein ttx-3
Sequence:
MQVVSSATLPPTVASADLAIVGGRSSDEDVIKYSAIQTIKQEQQQQQQQQSNTALPSYNFPFFNGMQNDFPPNRMLYNDNTMQKSENDHFTGMNLSTSASSSGNSTSSKDQSRRQFYTESSNSSGNGAAATSGSNGSSSSTESKSDVFNISMNAFAATPGSKSEDHNIPSFNMLSSYYTGALKLSNSTSFANPDPYQILGPTSKNLAHSGSGQTQLWQFLLELLSDKRYSEVITWEGTQGEFKLVDPDEVARKWGERKSKPNMNYDKMSRALRYYYDKNIMAKVHGKRYAYKFDFQGIAQALQPPTASHPQDYFNSHAMGRIAPDFSSWTSANYRSLNIAGFNNGSTIFNPSVNYSAFGATGTSNNLSAARAFPLYR
Protein: Glycerol kinase (EC 2.7.1.30) (ATP:glycerol 3-phosphotransferase) (Glycerokinase) (GK) (P0A6F3)
Organism: Escherichia coli (strain K12)
Function: Key enzyme in the regulation of glycerol uptake and metabolism. Catalyzes the phosphorylation of glycerol to yield sn-glycerol 3-phosphate. It also catalyzes the phosphorylation of dihydroxyacetone, L-glyceraldehyde and D-glyceraldehyde. It uses only ATP.
Interaction partners:
- Aerobic glycerol-3-phosphate dehydrogenase
- Glycerol uptake facilitator protein
- PTS system glucose-specific EIIA component
- Anaerobic glycerol-3-phosphate dehydrogenase subunit A
- Glycerol dehydrogenase
- Glycerophosphodiester phosphodiesterase, periplasmic
- Glycerol-3-phosphate transporter
- Probable glycerol-3-phosphate acyltransferase
- Glycerol-3-phosphate acyltransferase
- Fructose-1,6-bisphosphatase 1 class 2
Sequence:
MTEKKYIVALDQGTTSSRAVVMDHDANIISVSQREFEQIYPKPGWVEHDPMEIWATQSSTLVEVLAKADISSDQIAAIGITNQRETTIVWEKETGKPIYNAIVWQCRRTAEICEHLKRDGLEDYIRSNTGLVIDPYFSGTKVKWILDHVEGSRERARRGELLFGTVDTWLIWKMTQGRVHVTDYTNASRTMLFNIHTLDWDDKMLEVLDIPREMLPEVRRSSEVYGQTNIGGKGGTRIPISGIAGDQQAALFGQLCVKEGMAKNTYGTGCFMLMNTGEKAVKSENGLLTTIACGPTGEVNYALEGAVFMAGASIQWLRDEMKLINDAYDSEYFATKVQNTNGVYVVPAFTGLGAPYWDPYARGAIFGLTRGVNANHIIRATLESIAYQTRDVLEAMQADSGIRLHALRVDGGAVANNFLMQFQSDILGTRVERPEVREVTALGAAYLAGLAVGFWQNLDELQEKAVIEREFRPGIETTERNYRYAGWKKAVKRAMAWEEHDE
Protein: cystathionine gamma-lyase (EC 4.4.1.1) (Gamma-cystathionase) (C8VM61)
Organism: Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Interaction partners:
- Cystathionine beta-synthase
- 5-methyltetrahydropteroyltriglutamate--homocysteine S-methyltransferase
- Cysteine synthase 1
- cystathionine gamma-synthase
- Cysteine synthase 2
- Thiosulfate sulfurtransferase, putative
- Homocysteine S-methyltransferase
- Homocysteine synthase
- Serine O-succinyltransferase
- Aspartate aminotransferase
Sequence:
MTMMAGHPDLPSNGQNGDSNTHQQRQFATLAVHAGAPHDPTTGAVIAPISLSTTFAQESVGKPVGLYEYTRSSNPNRDNFEEAVASLEHAKYALAFSSGSATTATILHSLAPGSHVVSVSDVYGGTHRYFTKVAAAHGVNVSFSSCLELDVEKLIRPNETKLVWIETPSNPTLALVDIRKVAAVAHRHGVLVVVDNTFMSPYVQNPLDHGADVVIHSVTKYINGHSDVLMGVAAFNSDELKERFTFLQNAIGAVPSPFDCWLAHRGLKTLHLRAREATANATAVALALESSPHVISVNYPGLNSHPNREIAVKQHRKGMGGGMLSFRIKGGHKAAHLFCEYTKIFTLAESLGGVESLCEVPSSMTHAGIPKEEREAAGVYDDLVRMSCGIEDVEDLTADTMQALERAVAASQALENGSA
Protein: Homeobox protein knotted-1-like 2 (Protein ATK1) (Protein KNAT2) (P46640)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: May play a role in meristem function, and may be involved in maintaining cells in an undifferentiated, meristematic state. Probably binds to the DNA sequence 5'-TGAC-3'.
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
- Protein ASYMMETRIC LEAVES 2
- Transcription factor AS1
- Homeobox protein BEL1 homolog
- Protein KNATM
- BEL1-like homeodomain protein 2
- Axial regulator YABBY 1
- Protein WUSCHEL
- Protein LATERAL ORGAN BOUNDARIES
- Receptor-like protein kinase 5
- LRR receptor-like serine/threonine-protein kinase HSL2
Sequence:
MDRMCGFRSTEDYSEKATLMMPSDYQSLICSTTGDNQRLFGSDELATALSSELLPRIRKAEDNFSLSVIKSKIASHPLYPRLLQTYIDCQKVGAPMEIACILEEIQRENHVYKRDVAPLSCFGADPELDEFMETYCDILVKYKTDLARPFDEATTFINKIEMQLQNLCTGPASATALSDDGAVSSDEELREDDDIAADDSQQRSNDRDLKDQLLRKFGSHISSLKLEFSKKKKKGKLPREARQALLDWWNVHNKWPYPTEGDKISLAEETGLDQKQINNWFINQRKRHWKPSENMPFDMMDDSNETFFTE
Protein: Polycomb group RING finger protein 3 homolog mig-32 (RING-domain-containing protein mig-32) (Q19336)
Organism: Caenorhabditis elegans
Function: Component of a Polycomb group (PcG) multiprotein PRC1-like complex, a complex class required to maintain the transcriptionally repressive state of many genes, throughout development (By similarity). Required for ubiquitination of histone H2A. Plays a role in the formation of the male-specific genital sensilla (simple sense organs) known as rays. Required for normal migration of the hermaphrodite specific neurons (HSN) and for extension of some neuronal processes. Represses vulval fates in hypodermal cells that do not normally contribute to vulval development.
Subcellular location: Nucleus {ECO:0000269|PubMed:19211678}. Nucleus, nucleolus {ECO:0000269|PubMed:19211678}.
Interaction partners:
- E3 ubiquitin-protein ligase RING2 homolog spat-3
- Pre-mRNA polyadenylation factor Fip1 domain-containing protein
- Chromo domain-containing protein cec-1
- Probable cleavage and polyadenylation specificity factor subunit 1
- E3 ubiquitin-protein ligase RBBP6
- Cleavage and polyadenylation specificity factor subunit 5
- Suppressor of forked domain-containing protein
- DUF3453 domain-containing protein
- Histone-lysine N-methyltransferase mes-2
- pre-mRNA 3' end processing protein pfs-2
Sequence:
MTRKRPALAEPVSSSRSRVTRRSTTGAPSSKKKRSPEPESDADSEDDYDGPSTSQTKKLKRGNSSTNRGKAANKTKRGSFQVKQEIMDDDENEEKIDGEVENGITSREHSPDPSTFKKTAKLQTKKKKKKESPPETPPTSPSPSPSRSVSPSTTKSDISSKKGRKAVVNSVSKVKIEKESTPVKTNGRNLPPKRKKKPVEEETAEEIKLRERAERKARRIEEAKNRPKLTIEQKLAKLRKKKERRERRKEQEKEESMRQKYGQRKIKAEASKWNFGPISSINQRRRDEMMAYFPKANFLAEDGVPKVMNNFRRATVKYNMEVLNPFITCGICDGYIVDATTIIDCMHTFCKSCLLTYFESDNNTCPTCGTFIHGSHPTHYVTYDRAVNELVNQFVPKMENNELDVRKTFLRDCREALGIDTAAEDRERKERLERERITGTNRCYPLERPRFSHHRDDCQVTVNLLPGTANLPLITRPYVRCSEMTTMNTLKKFLSLQIWDDQSRYSDLDMFCDGQLMGKDFSVRFVWMMKRRGQPKSEPLIIRYHMTRT