wanglab/gogpt-training-data huggingface dataset:
Protein: Meiosis regulator and mRNA stability factor 1 (Limkain-b1) (Meiosis arrest female protein 1) (Q9Y4F3)
Organism: Homo sapiens (Human)
Function: Essential regulator of oogenesis required for female meiotic progression to repress transposable elements and preventing their mobilization, which is essential for the germline integrity. Probably acts via some RNA metabolic process, equivalent to the piRNA system in males, which mediates the repression of transposable elements during meiosis by forming complexes composed of RNAs and governs the methylation and subsequent repression of transposons. Also required to protect from DNA double-strand breaks (By similarity).
Subcellular location: Peroxisome {ECO:0000269|PubMed:15932519}.
Interaction partners:
- Enhancer of mRNA-decapping protein 4
- Centrosomal protein 20
- Tudor domain-containing protein 5
- mRNA-decapping enzyme 1A
- Nuclear distribution protein nudE homolog 1
Sequence:
MMEGNGTENSCSRTRGWLQQDNDAKPWLWKFSNCFSRPEQTLPHSPQTKEYMENKKVAVELKDVPSPLHAGSKLFPAVPLPDIRSLQQPKIQLSSVPKVSCCAHCPNEPSTSPMRFGGGGGGSGGTSSLIHPGALLDSQSTRTITCQVGSGFAFQSASSLQNASARNNLAGIASDFPSMCLESNLSSCKHLPCCGKLHFQSCHGNVHKLHQFPSLQGCTSAGYFPCSDFTSGAPGHLEEHISQSELTPHLCTNSLHLNVVPPVCLKGSLYCEDCLNKPARNSIIDAAKVWPNIPPPNTQPAPLAVPLCNGCGTKGTGKETTLLLATSLGKAASKFGSPEVAVAGQVLENLPPIGVFWDIENCSVPSGRSATAVVQRIREKFFKGHREAEFICVCDISKENKEVIQELNNCQVTVAHINATAKNAADDKLRQSLRRFANTHTAPATVVLVSTDVNFALELSDLRHRHGFHIILVHKNQASEALLHHANELIRFEEFISDLPPRLPLKMPQCHTLLYVYNLPANKDGKSVSNRLRRLSDNCGGKVLSITGCSAILRFINQDSAERAQKRMENEDVFGNRIIVSFTPKNRELCETKSSNAIADKVKSPKKLKNPKLCLIKDASEQSSSAKATPGKGSQANSGSATKNTNVKSLQELCRMESKTGHRNSEHQQGHLRLVVPTHGNSSAAVSTPKNSGVAEPVYKTSQKKENLSARSVTSSPVEKKDKEETVFQVSYPSAFSKLVASRQVSPLLASQSWSSRSMSPNLLNRASPLAFNIANSSSEADCPDPFANGADVQVSNIDYRLSRKELQQLLQEAFARHGKVKSVELSPHTDYQLKAVVQMENLQDAIGAVNSLHRYKIGSKKILVSLATGAASKSLSLLSAETMSVLQDAPACCLPLFKFTDIYEKKFGHKLNVSDLYKLTDTVAIREQGNGRLVCLLPSSQARQSPLGSSQSHDGSSTNCSPIIFEELEYHEPVCRQHCSNKDFSEHEFDPDSYKIPFVILSLKTFAPQVHSLLQTHEGTVPLLSFPDCYIAEFGDLEVVQENQGGVPLEHFITCVPGVNIATAQNGIKVVKWIHNKPPPPNTDPWLLRSKSPVGNPQLIQFSREVIDLLKSQPSCVIPISHFIPSYHHHFAKQCRVSDYGYSKLIELLEAVPHVLQILGMGSKRLLTLTHRAQVKRFTQDLLKLLKSQASKQVIVREFSQAYHWCFSKDWDVTEYGVCELIDIVSEIPDTTICLSQQDNEMVICIPKRERTQDEIERTKQFSKDVVDLLRHQPHFRMPFNKFIPSYHHHFGRQCKLAYYGFTKLLELFEAIPDTLQVLECGEEKILTLTEVERFKALAAQFVKLLRSQKDNCLMMTDLLTEYAKTFGYTFRLQDYDVSSISALTQKLCHVVKVADIESGRQIQLINRKSLRSLTAQLLVLLMSWEGTTHLSVEELKRHYESTHNTPLNPCEYGFMTLTELLKSLPYLVEVFTNDKMEECVKLTSLYLFAKNVRSLLHTYHYQQIFLHEFSMAYTKYVGETLQPKTYGHSSVEELLGAIPQVVWIKGHGHKRIVVLKNDMKSRLSSLSLSPANHENQPSEGERILEVPESHTASELKLGADGSGPSHTEQELLRLTDDSPVDLLCAPVPSCLPSPQLRPDPVILQSADLIQFEERPQEPSEIMILNQEEKMEIPIPGKSKTLTSDSSSSCISAAVPVPPCPSSETSESLLSKDPVESPAKKQPKNRVKLAANFSLAPITKL
Protein: Fasciculation and elongation protein zeta-1 (Zygin I) (Zygin-1) (Q99689)
Organism: Homo sapiens (Human)
Function: May be involved in axonal outgrowth as component of the network of molecules that regulate cellular morphology and axon guidance machinery. Able to restore partial locomotion and axonal fasciculation to C.elegans unc-76 mutants in germline transformation experiments. May participate in the transport of mitochondria and other cargos along microtubules.
Subcellular location: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000269|PubMed:18439996}. Cell membrane {ECO:0000250}. Note=Colocalizes with both, alpha- and gamma-tubulin. Translocated from the plasma membrane to the cytoplasm by activation of the PKC zeta (By similarity). {ECO:0000250}.
Interaction partners:
- Short coiled-coil protein
- Synaptotagmin-1
- Disrupted in schizophrenia 1 protein
- Kinesin-1 heavy chain
- Protein ZNF365
- Protein unc-119 homolog A
Sequence:
MEAPLVSLDEEFEDLRPSCSEDPEEKPQCFYGSSPHHLEDPSLSELENFSSEIISFKSMEDLVNEFDEKLNVCFRNYNAKTENLAPVKNQLQIQEEEETLQDEEVWDALTDNYIPSLSEDWRDPNIEALNGNCSDTEIHEKEEEEFNEKSENDSGINEEPLLTADQVIEEIEEMMQNSPDPEEEEEVLEEEDGGETSSQADSVLLQEMQALTQTFNNNWSYEGLRHMSGSELTELLDQVEGAIRDFSEELVQQLARRDELEFEKEVKNSFITVLIEVQNKQKEQRELMKKRRKEKGLSLQSSRIEKGNQMPLKRFSMEGISNILQSGIRQTFGSSGTDKQYLNTVIPYEKKASPPSVEDLQMLTNILFAMKEDNEKVPTLLTDYILKVLCPT
Protein: Large ribosomal subunit protein uL24m (39S ribosomal protein L24, mitochondrial) (L24mt) (MRP-L24) (Q9VMY1)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Mitochondrion {ECO:0000250|UniProtKB:Q96A35}.
Interaction partners:
- Large ribosomal subunit protein bL17m
- Large ribosomal subunit protein uL11m
- Large ribosomal subunit protein uL13m
- Large ribosomal subunit protein bL21m
- Large ribosomal subunit protein uL3m
- Large ribosomal subunit protein uL15m
- Mitochondrial ribosomal protein L2
- Large ribosomal subunit protein uL4m
- Large ribosomal subunit protein bL9m
- Small ribosomal subunit protein uS9m
Sequence:
MRLTQYLASKLKNFSNLPKEYIERSKKQVYWQTPKEINYLPRTVERKRFRYTTNRSWTGQFRQQNMPGTVRRKVLVEPIEDWSFFRGDRIEVLVGKDKGKQGIVTQVIPERNWVIVEGLNWHYRKVGGEKEFPGIIIKSEAPLHVTKDIRLVDPSDLQGTDFEWRFTEEGEKVRVSLRSGRIIPIPETNNQTHDYKTPNAYIEREKDTPGAVVGEITFQPKLSTFEMDIMEEMGIKEERTPVKSYWY
Protein: Muellerian-inhibiting factor (Anti-Muellerian hormone) (AMH) (Muellerian-inhibiting substance) (MIS) (P49000)
Organism: Rattus norvegicus (Rat)
Function: Plays an important role in several reproductive functions. Induces Muellerian duct regression during male fetal sexual differentiation and plays a role in Leydig cell differentiation and function (By similarity). In female acts as a negative regulator of the primordial to primary follicle transition and decreases FSH sensitivity of growing follicles. AMH signals by binding to a specific type-II receptor, AMHR2, that heterodimerizes with type-I receptors (ACVR1 and BMPR1A), and recruiting SMAD proteins that are translocated to the nucleus to regulate target gene expression (By similarity).
Subcellular location: Secreted {ECO:0000250|UniProtKB:P03971}.
Interaction partners:
- Anti-Muellerian hormone type-2 receptor
- Bone morphogenetic protein receptor type-1A
- Activin receptor type-1
- Chordin
- Follicle-stimulating hormone receptor
- Noggin
- Neuroblastoma suppressor of tumorigenicity 1
- Growth/differentiation factor 9
- Bone morphogenetic protein 15
- Steroid 17-alpha-hydroxylase/17,20 lyase
Sequence:
MQGPHLSLLLLLLATMGAVLQADTVEELTNTRGLIFLEDGVWPPSSPPEPLCLVAVRGEGDTSKASLTVVGGLHSYEHAFLEAVQESRWGPQDLATFGVCSTDSQTTLPALQRLGAWLGETGEQQLLVLHLAEVIWEPQLLLKFQEPPPGGASRWEQALLVLYPGPGPQVTVTGAGLQGTQSLCPTRDTRYLVLTVHFPAGAWSGSGLALTLQPSKEGATLTIAQLQAFLFGSDSRCFTRMTPTLVLLPPTGPTPQPAHGQLDTVPFPQPGLSLEPEDLPHSADPFLETLTRLVRALRGPLTRASNTRLALDPGALASFPQGLVNLSDPVALGRLLDGEEPLLLLLSPAAATVGEPMRLHSPTSAPWAAGLARRVAVELQAAASELRDLPGLPPTAPPLLSRLLALCPNDSRSAGDPLRALLLLKALQGLRAEWRGREGRGRAGRSKGTGTDGLCALRELSVDLRAERSVLIPETYQANNCQGACAWPQSDRNPRYGNHVVLLLKMQARGAALGRLPCCVPTAYTGKLLISLSEEHISAHHVPNMVATECGCR
Protein: Chloride channel protein 1 (ClC-1) (Chloride channel protein, skeletal muscle) (P35524)
Organism: Rattus norvegicus (Rat)
Function: Voltage-gated chloride channel. Plays an important role in membrane repolarization in skeletal muscle cells after muscle contraction (By similarity).
Subcellular location: Cell membrane {ECO:0000269|PubMed:1659664}; Multi-pass membrane protein {ECO:0000255}. Cell membrane, sarcolemma {ECO:0000250|UniProtKB:Q64347}; Multi-pass membrane protein {ECO:0000255}. Cell membrane, sarcolemma, T-tubule {ECO:0000250|UniProtKB:Q64347}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Sodium channel protein type 4 subunit alpha
- Muscleblind-like splicing regulator 1
- CUGBP Elav-like family member 1
- Barttin
- Muscleblind-like protein 2
- Osteoclastogenesis associated transmembrane protein 1
- Calcium-transporting ATPase
Sequence:
MERSQSQQHGGEQSWWGTAPQYQYMPFEHCTSYGLPSENGGLQHRPRKDLGPRHNAHPTQIYGHHKEQYSYQAQDRGIPKKTDSSSTVDSLDEDHYSKCQDCVHRLGRVLRRKLGEDWIFLVLLGLLMALVSWCMDYVSAKSLQAYKWTYAQMQPSLPLQYLAWVTFPLILILFSALFCQLISPQAVGSGIPEMKTILRGVVLKEYLTLKAFVAKVVALTAGLGSGIPVGKEGPFVHIASICAAVLSKFMSMFSGVYEQPYYYTDILTVGCAVGVGCCFGTPLGGVLFSIEVTSTYFAVRNYWRGFFAATFSAFVFRVLAVWNKDAVTITALFRTNFRMDFPFDLKELPAFAVIGICCGFLGAVFVYLHRQVMLGVRKHKALSQFLAKHRLLYPGIVTFVIASLTFPPGMGQFMAGELMPREAISTLFDNNTWVKHIGDPKSLGQSAVWIHPQVNVVIIILLFFVMKFWMSIVATTMPIPCGGFMPVFVLGAAFGRLVGEIMAMLFPEGILFDDIIYKILPGGYAVIGAAALTGAVSHTVSTAVICFELTGQIAHILPMMVAVILANMVAQSLQPSLYDSIIQVKKLPYLPDLGWNQLSKFTIFVEDIMVRDVKFVSASCTYGELRNLLQTTTVKTLPLVDSKDSMILLGSVERSELQSLLQRHLCAERRLKAAQDMARKLSELPYNGQAQLAGEWHPGGRPESFAFVDEDEDEDVSRKTELPQTPTPPPPPPPPLPPQFPIAPSYPEEPNGPLPSHKQPPEASDSADQRSSIFQRLLHCLLGKAHSTKKKITQDSTDLVDNMSPEEIEAWEREQLSQPVCFDFCCIDQSPFQLVEQTTLHKTHTLFSLLGLHLAYVTSMGKLRGVLALEELQKAIKGHTKSGVQLRPPLASFRNTTSIRKTPGGPPPPAESWNVPEGEDGAPEREVMVPTMPETPVPPPSPEVPSCLAPARVEGELEELEMVGNLGPEEDLADILHGPSLRSTDEEDEDELIL
Protein: WD repeat-containing protein 55 (Q6DRF9)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Function: Nucleolar protein that acts as a modulator of rRNA synthesis. Plays a central role during organogenesis (By similarity).
Subcellular location: Nucleus, nucleolus {ECO:0000250}.
Interaction partners:
- Lymphocyte cytosolic protein 2a.
- IK cytokine
- Zinc finger matrin-type protein 2
- Ribosome biogenesis protein wdr12
- Stem-loop-binding protein 2
- Protocadherin 2 alpha a 1.
- C-C motif chemokine 21
Sequence:
MATPTEHEDLSEQEVTEDEFKTPKIRETPEDIKLEAIVNTIAFHPKQDILAAGDIDGDIYLFSYSCTEGENKELWSSGHHLKSCRKVLFSSDGQKLFSVSKDKAIHIMDVEAGKLETRIPKAHKVPINAMLLIDENIFATGDDEGTLKVWDMRKGTSFMDLKHHEDYISDITIDQAKRTLLTSSGDGTLGVFNIKRRRFELLSEIQNGDLTSVSIMKRGRKVVCGSGEGTIYIFNWNGFGATSDRFAVQAESVDCIVPITDSILCAASTDGVIRAINILPNRVVGSIGQHVGEAIEEIARCRDTHFLASCAHDELIKFWDISSLPDEKVNDYRRRKKKDRRLKALSNKAFDTGQNFFAGLLDTTEENGKEGENDEDDDDEDSDSGSD
Protein: Protein arginine N-methyltransferase 9 (Protein arginine N-methyltransferase 10) (EC 2.1.1.320) (Q6P2P2)
Organism: Homo sapiens (Human)
Function: Arginine methyltransferase that can both catalyze the formation of omega-N monomethylarginine (MMA) and symmetrical dimethylarginine (sDMA). Specifically mediates the symmetrical dimethylation of SF3B2. Involved in the regulation of alternative splicing of pre-mRNA.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:25737013, ECO:0000269|PubMed:25979344}.
Interaction partners:
- Protein arginine N-methyltransferase 5
- Transmembrane protein 184C
- Splicing factor 3B subunit 2
- Splicing factor 3B subunit 4
Sequence:
MSNSRPRSRRDAGGGAGAAGRDELVSRSLQSAEHCLGVQDFGTAYAHYLLVLSLAPELKHDVKETFQYTLFRWAEELDALSRIQDLLGCYEQALELFPDDEVICNSMGEHLFRMGFRDEAAGYFHKAVKLNPDFSDAKENFYRVANWLVERWHFIMLNDTKRNTIYNAAIQKAVCLGSKSVLDIGAGTGILSMFAKKAGAHSVYACELSKTMYELACDVVAANKMEAGIKLLHTKSLDIEIPKHIPERVSLVVTETVDAGLFGEGIVESLIHAWEHLLLQPKTKGESANCEKYGKVIPASAVIFGMAVECAEIRRHHRVGIKDIAGIHLPTNVKFQSPAYSSVDTEETIEPYTTEKMSRVPGGYLALTECFEIMTVDFNNLQELKSLATKKPDKIGIPVIKEGILDAIMVWFVLQLDDEHSLSTSPSEETCWEQAVYPVQDLADYWIKPGDHVMMEVSCQDCYLRIQSISVLGLECEMDVAKSFTQNKDLLSLGNEAELCSALANLQTSKPDAVEQTCILESTEIALLNNIPYHEGFKMAMSKVLSSLTPEKLYQTMDTHCQNEMSSGTGQSNTVQNILEPFYVLDVSEGFSVLPVIAGTLGQVKPYSSVEKDQHRIALDLISEANHFPKETLEFWLRHVEDESAMLQRPKSDKLWSIIILDVIEPSGLIQQEIMEKAAISRCLLQSGGKIFPQYVLMFGLLVESQTLLEENAVQGTERTLGLNIAPFINQFQVPIRVFLDLSSLPCIPLSKPVELLRLDLMTPYLNTSNREVKVYVCKSGRLTAIPFWYHMYLDEEIRLDTSSEASHWKQAAVVLDNPIQVEMGEELVLSIQHHKSNVSITVKQ
Protein: Fido domain-containing protein (O69630)
Organism: Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh)
Interaction partners:
Sequence:
MTVDPLAPLMELPGVAAASDRVRDALSRVHRHRANLRGWPVAAAEASLRAARASSVLDGGPARLHDAGAPTSGKPALSDPVFAGALRVGQALEGGAGPVVGVWRRAPLQALARLHMLAAADQVDDDRLGRPRSDADVGPRLELLADVVTHPTLASAPVVAAVAHGELLTLRPFGCADGVVARAVSRLVTIATGLDPHGLGVPEVIWMRQPAEYHDAARRFAGGTPDGVAGWLLLCCGAMLDGAREALSIAESLSPG
Protein: Myomesin 1 (A0A8I6GFM8)
Organism: Rattus norvegicus (Rat)
Interaction partners:
Sequence:
MSLPFYQRSHQHYDLSYRNKDLHTTMSHYQQEKKRSAVYTHGSTAYSSRSSAAHRQESEALRQASAASYQQQASKAYSLGTSSSQHYQGSEVSRKTASSYDYGYSHGLTDSSLLLEDYSSRLSPQTKRAKRSLLSGEETGNLSGNYMVPIYSGRQVHISGIRDSEEERIKEAAAYIAQRTLLESEEAIMASKQSTASKQSTASKQSIASKQSTASKQSTASKQSTASKQATSTFQQEETFERKSRNISIREKAEELSLRKTLEETQAYHGKLNEDHLLHAPEFIIKPRSHTVWEKENVKLHCSVAGWPEPRLTWYKNQVPINVHANPEKYIIESRYGMHTLEISKCDFEDTAQYRASAMNVQGEVSAYASVVVKRYKGELDDSLLRGGVSMPLSFAVTPYGYASKFEIHFDDKFDVSFGREGETMSLGCRVVITPEIKHVQPEVQWYRNGAPVSPSKWVQPHWSGDRATLTFSHLNKEDEGLYTIRVRMGEYYEQYSAYVFVRDADAEIEGAPAAPLDVVSLDANKDYIIISWKQPAVDGGSPILGYFIDKCEVGTDTWSQCNDTPVKFARFPVTGLIEGRSYIFRVRAVNKTGIGLPSRVSEPVAALDPAEKARLKSRPSAPWTGQIIVTEEEPTEGVIPGPPTDLSVTEATRSYVVLSWKPPGQRGHEGIMYFVEKCDVGTENWQRVNTELPVKSPRFALFDLVEGKSYRFRVRCSNSAGVGEPSESTEVTVVGDKLDIPKAPGKIIPSRNTDTSVVVSWEESKDAKELVGYYIESSVVGSGQWEPCNNNPVKGSRFTCHGLTTGQSYIFRVRAVNAAGLSEYSQDSEAIEVKAAIAVPSPPYDITCLESFRDSMVLGWKQPDKTGGAEITGYYVNYREVVGGVPGKWREANIKAVSDAAYKISELKENTVYQFQVSAMNIAGLGAPSAVSECFKCEEWTIAVPGPPHSLKLSEVRKNSLVLQWKPPVYSGRTPVTGYFVDLKEASAKDDQWRGLNEAAIPNKYLRVQGLKEGISYVFRVRAINQAGVGKPSDLAGPVVAETRPGTKEVVVNVDDDGVISLNFECDQMTPKSEFVWSKDYVPSEDSPRLEVESKGNKTKMVFKDLGPDDLGTYSCDVTDTDGIASSYLIDEEEMKRLLALSQEHKFPTVPTKSELAVEILEKGQVRFWMQAEKLSGNAKVNYIFNEKEIFEGPKYKMHIDRNTGIIEMFMEKLQDEDEGTYTFQIQDGKATGHSTLVLIGDVYKKLQKEAEFQRQEWIRKQGPHFAEYLSWEVTGECNVLLKCKVANIKKETHIVWYKDEREISVDEKHDFKDGICTLLITEFSKKDAGFYEVILKDDRGKDKSRLKLVDEAFQDLMTEVCRKIALSATDLKIQSTAEGIRLYSFVCYYLDDLKVNWSHNGTGIKYTDRVKSGVTGEQIWLQINEPTQNDKGKYVMELFDGKTGHQKSVDLSGQAFDEAFAEFQRLKQAAIAEKNRARVLGGLPDVVTIQEGKALNLTCNVWGDPTPEVSWLKNEKPLTSDDHCSLKFEAGKTAFFTISGVSTADSGKYGLVVKNKYGSETSDFTVSVFIPEEEARKGASEPPKGNQKSK
Protein: Acetyl-CoA decarbonylase/synthase complex subunit gamma 1 (ACDS complex subunit gamma 1) (EC 2.1.1.245) (5-methyltetrahydrosarcinapterin:corrinoid/iron-sulfur protein Co-methyltransferase 1) (ACDS complex methyltransferase 1) (Corrinoid/iron-sulfur component large subunit 1) (Q50539)
Organism: Methanosarcina thermophila
Function: Part of a complex that catalyzes the reversible cleavage of acetyl-CoA, allowing growth on acetate as sole source of carbon and energy.
Interaction partners:
Sequence:
MKINSPLEAYKYLPQTNCGECGEPTCMAFASKLIDRSGKTSDCPPLVKEKKYAKKLAELDRLLAPEIRQVTIGVGEKAANIGGDDVLYRHKLTFFNKTKMFFDVSDNMEEDALIERVKKIADFKKFYVGRNLLLDGVAIKATSNDPAKFAAAVKKVAEIGLPMIFCSFNPAVLKAGLEVAKDKNPLLYAANKDNWKEVGELALEYKVPVVVSVFNDLDGLKSLAKTFAEAGIKDIVLDPGTYPSGKGLKDTFTNFLKIRRAGIMGDTEIAYPIMALPLTAWMAGISDPVSASYWETVIASVFTIRYGDIMILHSLEPYAALPEMHLAETIYTDPRTPVSVDGGMYKVGEPDKDSPVFFTTNFALTYYTVESDISANGIVCWLLAVDTDGIGVEAAVAGGQLTSAKVKDAFEKAGFDLKTDTNHNTLIIPGLSARLQGDLEDTLGANVKVGPMDSGRIPGWVEKNWPPK
Protein: 2-oxoglutarate (2OG) and Fe(II)-dependent oxygenase superfamily protein (Q8VYD7)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- GRR1-like protein 1
- Calcium-transporting ATPase 9, plasma membrane-type
Sequence:
MAETEILEPYQLSFSDLLLSSRNRSQWISKNVMDALGPTGPGLLCITGVLGSAFLRRKLLPMARKLALLDPDKRKLILMEHHLGSDVPLKNPERDVSSFAMQLNYERTTYKSSLGKLWFDEAGSKLDLQEDDDDAFTNLGGAFKELGFCMRELGLSIARLCDREIGGGLLEESLLDSCTAKGRLIHYHSAADKYALRESQRRNQSGNRVSSKRRVQNAAEQELNRRNGAGLSGSHFNLWQQWHYDYGIFTVLTDPMFLSPYSYQEFSLMSSHSYLQIYHPSKNKFYMVKTPQDSFLVQIGESADILSKGKLRSTLHCVCKPEKLDHVSRETFVVFLHPKWSQTFSVSEYTMEHLRSDEVVPRPDLQNIVPPLSSRLRDGMTFAEFSRETTKQYYGGNGLQSNR
Protein: Fibroblast growth factor 8 (FGF-8) (Heparin-binding growth factor 8) (HBGF-8) (Q90722)
Organism: Gallus gallus (Chicken)
Function: Plays an important role in the regulation of embryonic development, cell proliferation, cell differentiation and cell migration. Involved in initiation, outgrowth and patterning of the limbs.
Subcellular location: Secreted.
Interaction partners:
- Fibroblast growth factor receptor 1
- Fibroblast growth factor receptor 3
- Fibroblast growth factor receptor
- Fibroblast growth factor receptor 2
- Sonic hedgehog protein
- Uncharacterized protein.
- Fibroblast growth factor 10
- Platelet-derived growth factor receptor alpha
- Vascular endothelial growth factor receptor 2
- Bone morphogenetic protein 4
Sequence:
MDPCSSLFSYVFMHLFVLCLQAQVTVQSPPNFTQHVREQSLVTDQLSRRLVRTYQLYSRTSGKHVQILDNKKINAMAEDGDVHAKLIVETDTFGSRVRIKGAATGFYICMNKKGKLIGKSNGKGKDCVFTEIVLENNYTALQNAKYEGWYMAFTRKGRPRKGSKTRQHQREVHFMKRLPKGHQTTEPHRRFEFLNYPFNRRSKRTRNSSASLRP
Protein: Phosphoglucan phosphatase LSF1, chloroplastic (EC 3.1.3.-) (Phosphoglucan phosphatase like sex Four1) (Protein LIKE SEX4 1) (F4J117)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Starch granule-associated phosphoglucan phosphatase involved in the control of starch accumulation. Participates in the regulation of the initial steps of starch degradation at the granule surface. May release a different set of phosphate groups from those removed by DSP4.
Subcellular location: Plastid, chloroplast {ECO:0000269|PubMed:20018601}. Note=Located on the surface of starch granules.
Interaction partners:
- CBS domain-containing protein CBSCBSPB3
- Beta-amylase 3, chloroplastic
- Isoamylase 3, chloroplastic
- Beta-amylase 1, chloroplastic
- SNF1-related protein kinase regulatory subunit gamma-1-like
- Alpha-glucan water dikinase 1, chloroplastic
- Maltose excess protein 1, chloroplastic
- Phosphoglucan phosphatase
- Inositol diphosphatase DSP5
- Beta-amylase 2, chloroplastic
Sequence:
MAFLQQISGLGALERSCPSIMIGSSFRSGNGRVFDGRGIAYLGSREKFGFNRRRRVVLRVVAMSSSSTPFKMNLNEYMVTLEKPLGIRFALSADGKIFVHAIKKGSNAEKARIIMVGDTLKKASDSSGGTLVEIKDFGDTKKMLVEKTGSFSLVLERPFSPFPIQYLLHLSDLDLLYNRGRVSFVTWNKNLLSSNLRASSQGSGNSGYAAFSSKFFTPQGWKLLNRQSNSFQSGTKKNILSPPISPLVSVFSEDVPGDGEWGYGNFPLEEYIKALDRSKGELSYNHALGMRYSKITEQIYVGSCIQTEEDVENLSEAGITAILNFQGGTEAQNWGIDSQSINDACQKSEVLMINYPIKDADSFDLRKKLPLCVGLLLRLLKKNHRVFVTCTTGFDRSSACVIAYLHWMTDTSLHAAYSFVTGLHACKPDRPAIAWATWDLIAMVDDGKHDGTPTHSVTFVWNGHEGEEVLLVGDFTGNWKEPIKATHKGGPRFETEVRLTQGKYYYKYIINGDWRHSATSPTERDDRGNTNNIIVVGDVANVRPTIQQPRKDANIIKVIERVLTESERFRLAKAARCIAFSVCPIRLCPKS
Protein: Scarecrow-like protein 15 (AtSCL15) (GRAS family protein 25) (AtGRAS-25) (O23210)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Probable transcription factor involved in plant development.
Subcellular location: Nucleus {ECO:0000269|PubMed:18500650}.
Interaction partners:
- Histone deacetylase 19
- Scarecrow-like protein 29
- Scarecrow-like protein 9
- Protein PAT1 homolog
Sequence:
MKIPASSPQDTTNNNNNTNSTDSNHLSMDEHVMRSMDWDSIMKELELDDDSAPNSLKTGFTTTTTDSTILPLYAVDSNLPGFPDQIQPSDFESSSDVYPGQNQTTGYGFNSLDSVDNGGFDFIEDLIRVVDCVESDELQLAQVVLSRLNQRLRSPAGRPLQRAAFYFKEALGSFLTGSNRNPIRLSSWSEIVQRIRAIKEYSGISPIPLFSHFTANQAILDSLSSQSSSPFVHVVDFEIGFGGQYASLMREITEKSVSGGFLRVTAVVAEECAVETRLVKENLTQFAAEMKIRFQIEFVLMKTFEMLSFKAIRFVEGERTVVLISPAIFRRLSGITDFVNNLRRVSPKVVVFVDSEGWTEIAGSGSFRREFVSALEFYTMVLESLDAAAPPGDLVKKIVEAFVLRPKISAAVETAADRRHTGEMTWREAFCAAGMRPIQLSQFADFQAECLLEKAQVRGFHVAKRQGELVLCWHGRALVATSAWRF
Protein: Candida glabrata strain CBS138 chromosome F complete sequence (Q6FUA0)
Organism: Candida glabrata (strain ATCC 2001 / BCRC 20586 / JCM 3761 / NBRC 0622 / NRRL Y-65 / CBS 138) (Yeast) (Nakaseomyces glabratus)
Interaction partners:
Sequence:
MKFDKLLFTVTTVFAFTTFILIIIATAGSSSNYKPITNIKIGEADISHINVTKVVPQVGPILTILGSALTANASLDQIFDALKQVADTPALVPLLNLMSNSKSNVTGTIGALTNLAPLALQKSDNTTDAALNSINMVIGDATNVDLLLDGMKEVVNSAMESLTSPNFKNLTIMENEVFNLLLDSENVTATTEALIDMNQIPDADKQKLIPAFTLFKDSSNLNATIDSMASLMNYSSALSSIPTAELSTLFSTVSSLASSKSSLISTITALSSKLPSNLAPAVSSLTTLLNSTNEDSLNSTLNALQTLILKNNITASVDSAKTSINSIKIMNEYAQNKTLLLDSVEDLATQTSVPSNTTTAQLKALDDIFQGSGNASATLRTLMGLEQGLTANPSLIKYVPYIFELLDDSNNATLSFTSLLNLTSFAKSNPTTFVPIMSILGKANSITPVTQDQLRELTPAILEYLHIPIKFHLSIFTLCKADINDKIISCSKSHAVQNLDFRSIIYDSIAESDFKPYLEALKIGKQDLHLDGKMQNRQHEYVPAIRASLSMNLLAIIVSFFLMCYAIFLLVSKNAMTHMKWCILFFLTMNSALFSGLGGTIISAMINIIKSGTHDDKYGVVFDDNSSILGLLWCAFTVAFLSYVAATLSWFQFWRENKNKPVTYLSSGTSSENESVTSRVTEHANNKADEKESV
Protein: Flavin-dependent halogenase aclH (EC 1.14.14.-) (Aspirochlorine biosynthesis protein H) (Q2UPC7)
Organism: Aspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold)
Function: Flavin-dependent halogenase; part of the gene cluster that mediates the biosynthesis of aspirochlorine (or antibiotic A30641), an unusual halogenated spiro compound with distinctive antifungal properties due to selective inhibition of protein biosynthesis, and which is also active against bacteria, viruses, and murine tumor cells. The non-ribosomal peptide synthetase (NRPS) aclP is responsible the formation of the diketopiperazine (DKP) core from the condensation of 2 phenylalanine residues. One Phe residue is tailored into chlorotyrosine by hydroxylation and chlorination, whereas the second Phe undergoes an unprecedented C-C bond cleavage to be converted into glycine. After formation of the DKP, sulfur is incorporated into the DKP by conjugation with glutathione by aclG, followed by its stepwise degradation to the thiol by aclI, aclJ and aclK, and the dithiol oxidation by aclT. In addition, oxygenases (aclB, aclC, aclL and aclO) and O-methyltransferases (aclM and aclU) act as tailoring enzymes to produce the intermediate dechloroaspirochlorine. Ultimately, chlorination of dechloroaspirochlorine by the halogenase aclH is the last step in the aspirochlorine pathway.
Interaction partners:
- Cytochrome P450 monooxygenase aclL
- Cytochrome P450 monooxygenase aclO
- O-methyltransferase aclU
Sequence:
MSIPNRCTVLVVGGGPAGSYAAAALAREGVDTVLLEADVFPRYHIGESMLPSIRHFLRFIDLDSKFDSYGFVNKNGAAFKLNSKPEAYTDFIAAGGPGSHAWNVVRSEADHLMFKHAGENGAQVFDGVKVNSIEFEQIDGLTVDPSLSELGRPVSATWSCKATGGKGSITFEYLIDATGRAGLVSTKYMKNRRYNQGLKNVASWGYWSNAGSYGVGTPREGDPYFEAIEDGSGWVWLIPLHNGTTSIGVVMNQEAATAKKRETGATTKDLYLNTIKNTPGVWQLLDKAELQSDLKSASDWSYNASSYASPYLRIVGDAGCFIDPFFSSGVHLALASGLSAALTIRAAQRGDCDEQAAVSWHSKKVAEGYTRFLLVVMSALKQISDREKPVLTDFDEDSFNRAFDFFRPIIQGTADVDKNLTQAEIAQTIEFCVQAFQTASTDEQDAVMTKVAAINSQNGTEGALRELHASLSADERRTLTTIQARQIIRSEDQMNIDNFTIDVIDGMVPRLERSSLGLARFVPKAQTSREDGLRATLGLPEKQKSIFSY
Protein: Argininosuccinate synthase (EC 6.3.4.5) (Citrulline--aspartate ligase) (P0A6E4)
Organism: Escherichia coli (strain K12)
Subcellular location: Cytoplasm {ECO:0000305}.
Interaction partners:
- Acetylglutamate kinase
- N-acetyl-gamma-glutamyl-phosphate reductase
- Acetylornithine deacetylase
- Argininosuccinate lyase
- Amino-acid acetyltransferase
- Ornithine carbamoyltransferase subunit F
- Ornithine carbamoyltransferase subunit I
- Carbamoyl phosphate synthase large chain
- Carbamoyl phosphate synthase small chain
- Acetylornithine/succinyldiaminopimelate aminotransferase
Sequence:
MTTILKHLPVGQRIGIAFSGGLDTSAALLWMRQKGAVPYAYTANLGQPDEEDYDAIPRRAMEYGAENARLIDCRKQLVAEGIAAIQCGAFHNTTGGLTYFNTTPLGRAVTGTMLVAAMKEDGVNIWGDGSTYKGNDIERFYRYGLLTNAELQIYKPWLDTDFIDELGGRHEMSEFMIACGFDYKMSVEKAYSTDSNMLGATHEAKDLEYLNSSVKIVNPIMGVKFWDESVKIPAEEVTVRFEQGHPVALNGKTFSDDVEMMLEANRIGGRHGLGMSDQIENRIIEAKSRGIYEAPGMALLHIAYERLLTGIHNEDTIEQYHAHGRQLGRLLYQGRWFDSQALMLRDSLQRWVASQITGEVTLELRRGNDYSILNTVSENLTYKPERLTMEKGDSVFSPDDRIGQLTMRNLDITDTREKLFGYAKTGLLSSSAASGVPQVENLENKGQ