wanglab/gogpt-training-data huggingface dataset:
Protein: Large ribosomal subunit protein uL22 (60S ribosomal protein L17-B) (Q59TE0)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (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:0000305|PubMed:35613268}.
Interaction partners:
- Large ribosomal subunit protein eL24
- Small ribosomal subunit protein uS5
- Large ribosomal subunit protein eL39
- Small ribosomal subunit protein uS12
- Small ribosomal subunit protein uS7
- Small ribosomal subunit protein uS14
- Large ribosomal subunit protein eL8B
- Small ribosomal subunit protein eS17
- Small ribosomal subunit protein eS12
- Large ribosomal subunit protein eL34
Sequence:
MVRYAATPANPAKSASARGSYLRVSFKNTRETAQAINGWKLEKAQKYLDQVLDHQRAIPFRRYNSSIGRTGQGKEFGVTKARWPAKSVNFVKDLLRNAQANAEAKGLDSSKLVISHIQVNHAPKQRRRTYRAHGRINAYQSTPSHIELTLTEEDEIVEKPVEQKQIRLNSRQRGRLASQKRLTAA
Protein: Adenylate kinase 9 (J3KP89)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MTSQEKTEEYPFADIFDEDETERNFLLSKPVCFVVFGKPGVGKTTLARYITQAWKCIRVEALPILEEQIAAETESGVMLQSMLISGQSIPDELVIKLMLEKLNSPEVCHFGYIITEIPSLSQDAMTTLQQIELIKNLNLKPDVIINIKCPDYDLCQRISGQRQHNNTGYIYSRDQWDPEVIENHRKKKKEAQKDGKGEEEEEEEEQEEEEAFIAEMQMVAEILHHLVQRPEDYLENVENIVKLYKETILQTLEEVMAEHNPQYLIELNGNKPAEELFMIVMDRLKYLNLKRAAILTKLQGAEEEINDTMENDELFRTLASYKLIAPRYRWQRSKWGRTCPVNLKDGNIYSGLPDYSVSFLGKIYCLSSEEALKPFLLNPRPYLLPPMPGPPCKVFILGPQYSGKTTLCNMLAENYKGKVVDYAQLVQPRFDKARETLVENTIAEATAAAIKVVKEKLLRELQARKQAETALREFQRQYEKMEFGVFPMEATHSSIDEEGYIQGSQRDRGSSLVDTEEAKTKSENVLHDQAAKVDKDDGKETGETFTFKRHSQDASQDVKLYSDTAPTEDLIEEVTADHPEVVTMIEETIKMSQDINFEQPYEKHAEILQEVLGEVMEENKDRFPGAPKYGGWIVDNCPIVKELWMALIKKGIIPDLVIYLSDTENNGKCLFNRIYLQKKSEIDSKILERLLEELQKKKKEEEEARKATEEELRLEEENRRLLELMKVKAKGKHRLL
Protein: Delta-1-pyrroline-5-carboxylate synthase [Includes: Glutamate 5-kinase (GK) (EC 2.7.2.11) (Gamma-glutamyl kinase); Gamma-glutamyl phosphate reductase (GPR) (EC 1.2.1.41) (Glutamate-5-semialdehyde dehydrogenase) (Glutamyl-gamma-semialdehyde dehydrogenase)] (Q9VNW6)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Multifunctional fusion protein
- Ornithine aminotransferase, mitochondrial
- GH20963p
- Pyrroline-5-carboxylate reductase
- Glutamine synthetase 2 cytoplasmic
- Glutamine synthetase 1, mitochondrial
- Glutamate dehydrogenase, mitochondrial
- Glutamate synthase
- Glutamate dehydrogenase
- Chaperone Ric-8
Sequence:
MLQNSFKLAQSLRNGFYRNAWRAFSSHGPRQPLVSPERRLEKAHPTFTERSQLKYARRLVVKLGSAVITREDNHGLALGRLASIVEQVAECHLEGREVMMVTSGAVAFGKQKLAQELLMSLSMRETLNPKDSKEFDGATLEPRAAAAVGQSGLMSLYDAMFAQYGVKIAQVLVTKPDFYNEETRNNLFCTLSELISLNIVPIINTNDAVSPPMFIRDDEPAGGARRGIPIKDNDSLSAMLAAEVQADLLILMSDVDGIYNKPPWEDGAKLMHTYTSDDSNSIEFGKKSKVGTGGMDSKVKAATWALDRGVSVVICNGMQEKAIKTIIGGRKVGTFFTEATESANAVPVEVMAENARTGSRQMQALTPAQRASAVNTLADLLVSREKFILDANAKDLAEAQKSGLAKPLLSRLSLNPAKLKNLSVGLKQIAEDSHKNVGRVLRRTRLADQLELKQVTVPIGVLLVIFESRPDSLPQVAALAMASANGLLLKGGKEAAHSNKALMELVKEALATVGAEHAVSLVSTREEISDLLSMENHIDLIIPRGSSDLVRSIQQQSLHIPVLGHAEGVCHVYIDRDADLEKALRIARDAKCDYPAACNAMETLLIHEDLMSGAIFGDVCNMLKREGVKIYAGPRLNQQLTFGPPAAKSLKHEYGALECCIEVVPSLDEAINHIHTYGSSHTDVIVTENDAAARQFLGSVDSACVFHNASSRFADGFRFGLGAEVGISTARIHARGPVGVEGLLTTKWILEGQDHAAADFAEGGGRTWLHETLPLD
Protein: alpha-amylase (EC 3.2.1.1) (Q8N0Q8)
Organism: Drosophila kikkawai (Fruit fly)
Interaction partners:
Sequence:
MFLTKSIVCLAILALASAQFDTNYASGRSGMVHLFEWKWDDIAAECENFLGPNGFAGVQVSPVNENAVKDSRPWWERYQPISYKLVTRSGNEEQFASMTRRCNAVGVRIYVDVIFNHMAANGGTYGTGGSTASPSSKSYPGVPYSSLDFNPTCAISNYNDANQVRNCELVGLRDLNQGNSYVQEKIAEFLNHLIDLGVAGFRVDAAKHMWPADLGVIYGRLKNLNTDHGFSSGSKAYIVQEVIDMGGEAISKSEYTGLGAITEFRHSDSIGKAFRGKNQLRYLSNWGTAWGFAASDRSLVFVDNHDNQRGHGAGGADVLTYKVPKQYKMASAFMLAHPFGTPRVMSSFSFSDTDQGPPTTDGHNIASPSFNSDNSCSGGWVCEHRWRQIYNMVAFRNAVGSDAIQNWWDNGSNQIAFSRGSRGFVAFNNDNYDLNSSLQTGLPAGTYCDVISGTKNGSSCTGKTVTVGSDGRASIYLGNSEDDGVLAIHVNAML
Protein: ALS2 C-terminal-like protein (Q60I26)
Organism: Mus musculus (Mouse)
Function: Acts as a guanine nucleotide exchange factor (GEF) for Rab5 GTPase. Regulates the ALS2-mediated endosome dynamics (By similarity).
Subcellular location: Cytoplasm {ECO:0000269|PubMed:15388334, ECO:0000269|PubMed:17239822}. Note=Distributed onto the vesicular compartments in the cytoplasm with strong punctated staining. Colocalizes with RAB5A onto the vesicular/membranous compartments in the cytoplasm, particularly to the leading edges of the cells (By similarity). {ECO:0000250}.
Interaction partners:
- GTPase-activating protein and VPS9 domain-containing protein 1
Sequence:
MSSSEEADLLRLEEVFSTTLARTISLILQPLLLADPEPSDPCGKECLRLLQQLHESAQRLWYVTEQSLLSLRQRLYHPPSKGLEAVLLLSNADHVLQAHMEYIKSYTDCVVAQAFQKVSKKRSEFWRSQRKALRQLLSSGSSEGSVGTTMCQALRQPLSQHVQKYLLLLLSLRDTLDESHPAQELVMHAITLFGNLQSFMGQALDQAVATQALWHSLSSRLRDVLCSPAHRLLQDSQDIPVVVTPLRAERVLLFDDSLVLLQGHNTHTFDLKLVWVKPGQDKCVLHILTPEEEISFCTRDPQGQVVWQWKVTQAVCQALCGKKDFPVLGSGRETSVPPECRCVAYTFCREGRLCQATYDGEWCRAKPHGKGTLKWPDGRNHVGTFYQGLEHGFGICLVPQASEDKFDCYKCHWREGRMCEYGICEYGTDEVYKGYFQAGLRHGFGILESAPQAPQPFRYTGHWERGQRSGYGIEEDRDRGERYIGMWQADQRHGPGVVVTQAGVCYQGTFQGDKMAGPGILLCEDDSLYEGTFTRDLTLLGKGKVTFPNGFTLDGSFSSGTDKGLYTQGVLDTAALPPDPSSTRKRQLGLGTFPVESRWQGVYSPFRDFLRLGCPGEQQEALLGFHTQSSRELRKSQECLCCERSHPEDCVGSMEDTLKELLQHRKPKALQQYLRKALSNSRHPLGQLLRTLMLTFQATYSGIGANKHLQEMAQEEVKQHARELWAAYRGLLKVALQHQGQTLEEENMETRDLQVHGLLLPLILPSFYSELFTLYLLLHEREDGLYSRGITNLSLFPDTKLLEFLDVQKHLWPLKDLKLTSNQRYSLVRDKCFLTATECLQKIITTVHPREKLEVLEKTYGEIEATVSRVLGCKYKLPMDDLLPLLIYVVSRARIQHLGAEIHLIRDMMDPVHTGGLHDFLLTALESCYEHIQKEDMRPHHLPGHWDARDLW
Protein: Arginine biosynthesis bifunctional protein ArgJ [Cleaved into: Arginine biosynthesis bifunctional protein ArgJ alpha chain; Arginine biosynthesis bifunctional protein ArgJ beta chain] [Includes: Glutamate N-acetyltransferase (EC 2.3.1.35) (Ornithine acetyltransferase) (OATase) (Ornithine transacetylase); Amino-acid acetyltransferase (EC 2.3.1.1) (N-acetylglutamate synthase) (AGSase)] (P9WPZ3)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: Catalyzes two activities which are involved in the cyclic version of arginine biosynthesis: the synthesis of N-acetylglutamate from glutamate and acetyl-CoA as the acetyl donor, and of ornithine by transacetylation between N(2)-acetylornithine and glutamate.
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01106, ECO:0000305}.
Interaction partners:
- N-acetyl-gamma-glutamyl-phosphate reductase
- Arginine repressor
- Acetylglutamate kinase
- Acetylornithine aminotransferase
- Ornithine carbamoyltransferase
- Argininosuccinate synthase
- Argininosuccinate lyase
- Amino-acid acetyltransferase
- Probable histone acetyltransferase Rv0428c
- Alanine aminotransferase
Sequence:
MTDLAGTTRLLRAQGVTAPAGFRAAGVAAGIKASGALDLALVFNEGPDYAAAGVFTRNQVKAAPVLWTQQVLTTGRLRAVILNSGGANACTGPAGFADTHATAEAVAAALSDWGTETGAIEVAVCSTGLIGDRLPMDKLLAGVAHVVHEMHGGLVGGDEAAHAIMTTDNVPKQVALHHHDNWTVGGMAKGAGMLAPSLATMLCVLTTDAAAEPAALERALRRAAAATFDRLDIDGSCSTNDTVLLLSSGASEIPPAQADLDEAVLRVCDDLCAQLQADAEGVTKRVTVTVTGAATEDDALVAARQIARDSLVKTALFGSDPNWGRVLAAVGMAPITLDPDRISVSFNGAAVCVHGVGAPGAREVDLSDADIDITVDLGVGDGQARIRTTDLSHAYVEENSAYSS
Protein: GEO05038p1 (LD03247p) (Pomp) (Q9VIJ5)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Proteasome subunit alpha type-3
- Proteasome subunit beta type-1
- Proteasome subunit beta type-4
- Proteasome subunit beta type-3
- Proteasome subunit alpha type-2
- Proteasome subunit beta
- Proteasome assembly chaperone 2
- Proteasome subunit alpha type-4
- Proteasome subunit alpha type-6
- Proteasome subunit alpha type-5
Sequence:
MYQPSLKVQPAEVSVLNATGRVGMPTEANCLNQLAHVHRLRDSELNYNEHQYNRNMQMLRNHEGLGVPLKMGMERFAARQVGRLPFLSSSNFMDDVLTGRCDSIGFEDFMNLPENSEHMRQPHAVVEKSLGIYQ
Protein: histidine kinase (EC 2.7.13.3) (Q1CYI5)
Organism: Myxococcus xanthus (strain DK1622)
Interaction partners:
- DNA-binding response regulator PhoP3
- DNA-binding response regulator PhoP2
- DNA-binding response regulator
- histidine kinase
- Response regulator
- Response regulator
- Response regulator
- DNA-binding response regulator
- Response regulator
- DNA-binding response regulator phoP1
Sequence:
MLRRLLPTLIALLLGFAGLAWGLGSLQRIFATERDDAQASLDSRREALEQYARASLAQSLRDRLEAARPALEAAALDPLAPATGLYLRERGTQLLPRLALHDTGEDTPAKGRYAGLRAGTERADEAEDPWAERLALIREVDRALSRGDRRASTVALMALLQHRAQYVLASTRDVPGFLVVLESLAERGDPVPQLMHALVRDGLADGRSGRLDGLQRLLLLRRARFTKEDFDFLRERIVALSTKAGVPVADFEARAAELASEPLPLPRTLPGPALVRAGWYLEPRGGNHVRGVAVDSGALLQSLTREMRERGLLEADGQVRLLADAEMLPLADLPLSVDTPEWARAQGALERRYRLKTGMVAACAVLALGIAALAFVAQHRKLRFLELKSDFVATVSHELRTPLASIRLLAETLEWRLAEGTDARDYPARIVREADGLGFLVENLLSFNRIDKGRWVPKLAPVRLDELVAQLRKDLEFWSKVPVELEADVGEFSLRADGQLLRLLLSNLARNACAYNTRSPVRLRIEALSDGRVRFSDNGVGIPQTQWERAFEEFVRLPGQGHDAPGSGLGLALCRRIMRVHGGTLRVAASSPEGTTFELRFPHTVTT
Protein: BOI-related E3 ubiquitin-protein ligase 1 (EC 2.3.2.27) (RING-type E3 ubiquitin transferase BRG1) (Q9FHE4)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: E3 ubiquitin-protein ligase involved in regulation of abiotic stress responses. Not involved in ubiquitination of MYB108/BOS1. Has no effect on the stability of the DELLA proteins.
Interaction partners:
- Purple acid phosphatase 22
- Probable disease resistance protein At1g12290
- ATP-dependent DNA helicase 2 subunit KU70
- Poly [ADP-ribose] polymerase 1
Sequence:
MAVEARHMNLFSSQYITNRECVKSQTNMNNGQQIAGGGFPVTIGDRNLQYIDPINSFNKSESELTAISKRQRDSTFDSDALIASQKRRAIAFSPASLIDAELVSQIQQQNSEIDRFVAQQTETLRIELEARQRTQTRMLASAVQNAILKKLKAKDEEIIRMGKLNWVLQERVKNLYVENQIWRDLAQTNEATANNLRSNLEQVLAQVDDLDAFRRPLVEEADDAESSCGSCDGGDVTAVVNGGCKRCGELTASVLVLPCRHLCLCTVCGSSALLRTCPVCDMVMTASVHVNMSS
Protein: Pyoverdine export membrane fusion protein PvdR (Q9I191)
Organism: Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Subcellular location: Periplasm {ECO:0000305|PubMed:19906986}.
Interaction partners:
- Pyoverdine export outer membrane protein OpmQ
- Pyoverdine export ATP-binding/permease protein PvdT
- Acyl-homoserine lactone acylase PvdQ
- Pyoverdine biosynthesis protein PvdE
- PvdN
- PvdL
- L-ornithine N
- L-2,4-diaminobutyrate:2-ketoglutarate 4-aminotransferase, PvdH
- PvdO
- PvdP
Sequence:
MRRTRSTRRALLVAVCLSPLIALAAWQAYPFRSNNFDTVSVSRGSIESSVSALGTLQPRRYVDVGAQASGQIRKLHVEAGDDVTEGQLLVEIDPSTQQAKVDAGRYSIEMLKAQLAEQRAQYTLARQQYQRQQRLAAGGATRTEDVQSAQAQMLATQARIEMYQAQIRQAQASLRSDEAELGYTRIYAPMSGTVVAVDAREGQTLNAQQQTPLILRIAKLSPMTVWAQVSEADIGRVKPGMPAYFTTLSGEGRRWTGKVRQILPVPPKPLDQSNQGGGSPTSGSGGQSGSGRVVLYTVLVDVDNGDHQLMAEMTAQVFFVAATAENILTAPVAAIHDDGKGGQVAWVVGSNGKPQSRQIRTGISDRLRVQVLAGLEEGDRLLMAAPDGSDS
Protein: Probable proteasome subunit beta type-7 (Q9USQ9)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Non-catalytic component of the proteasome, a multicatalytic proteinase complex which is characterized by its ability to cleave peptides with Arg, Phe, Tyr, Leu, and Glu adjacent to the leaving group at neutral or slightly basic pH. The proteasome has an ATP-dependent proteolytic activity (By similarity).
Subcellular location: Cytoplasm {ECO:0000255|PROSITE-ProRule:PRU00809, ECO:0000269|PubMed:16823372}. Nucleus {ECO:0000269|PubMed:16823372}.
Interaction partners:
- Probable proteasome subunit alpha type-1
- Probable proteasome subunit alpha type-6
- Probable proteasome subunit alpha type-7
- Probable proteasome subunit beta type-5
- Probable proteasome subunit alpha type-4
- Probable proteasome subunit beta type-6
- Probable proteasome subunit alpha type-2
- Probable proteasome subunit alpha type-5
- Probable proteasome subunit beta type-3
- Probable proteasome subunit alpha type-3
Sequence:
MSFLELTEVWGKPQKDIFFPSGSEVEESTDAPIQRTVQPIVTGSSVLALKFADGVMIAADNLASYGSLARFYDVERLTKVGDNTIVGAGGDISDYQQIQRLLEKLEIKEGNYGDGYALQPSYIHEYLSKVLYARRNKLDPYWNQLIVAGVDGENKEPYVAFADLRGTTYSAPAIATGFAMHLALPMLRKATDDDRWKTLSKESARATIDECMRVLFYRDARSLNKFSVATITPEGIEFQTDQSVSSKWAFAEKQYGYGTQTV
Protein: AP-5 complex subunit beta-1 (Adaptor-related protein complex 5 beta subunit) (Beta5) (Q2VPB7)
Organism: Homo sapiens (Human)
Function: As part of AP-5, a probable fifth adaptor protein complex it may be involved in endosomal transport.
Interaction partners:
- AP-5 complex subunit sigma-1
- AP-5 complex subunit zeta-1
- AP-5 complex subunit mu-1
- Spatacsin
- AP-4 complex subunit epsilon-1
- AP-4 complex subunit sigma-1
- AP-3 complex subunit sigma-2
- AP-4 complex subunit beta-1
- AP-4 complex subunit mu-1
- AP-1 complex subunit sigma-1A
Sequence:
MGPLSRDAWAQRLGAFRASPSAFMAGPEGEDLGRDLLSDLRSEKLSEQTKVSLLALSMEYPAQLWPDASAAEVAATSLLDTLVLLPPRPSALRRPLLLAATTALAAGGALGPTSGASCRLLPLLLGLAAGSDLGRGFVPASEQRPLQATACECLRELESCKPGLLGGSLGLLRGLLGQEGPVQPLSLLLALALRNTLVLQSRVGAGLGGLLTDKVSPTGGGPWDWTLVEEGDGRLQPQAPSWPAAEEGEGERSLTAREHSPEEARELRAAVIQLLDTSYLLTPVAQAQLLWLLGWALRGLQGQPPALFKPQLVRLLGTAQLTLLHAMLALKAAFGEALFTAQDEALLLRRLTLAAQHPALPPPTHLFYLHCVLSFPENWPLGPEGEEAAPLLLGPQLCRGLLPSLLHDPMALLARLHLLCLLCAEEEEEEKGQLPSPRHYLEELLAGLRQRAALDGGPRALATLCFQASYLVACCLAGQPTVLTPLIHGLAQLYQARPMLAPHFVDLLDQVDSELREPLKVVLRQVVVSRPGRDEALCWHLQMLAKVADGDAQSATLNFLQAAAAHCTNWDLQQGLLRVCRALLRAGVRGGLVDLLQVLARQLEDPDGRDHARLYYILLAHLAAPKLGVALGPSLAAPALASSLVAENQGFVAALMVQEAPALVRLSLGSHRVKGPLPVLKLQPEALEPIYSLELRFRVEGQLYAPLEAVHVPCLCPGRPARPLLLPLQPRCPAPARLDVHALYTTSTGLTCHAHLPPLFVNFADLFLPFPQPPEGAGLGFFEELWDSCLPEGAESRVWCPLGPQGLEGLVSRHLEPFVVVAQPPTSYCVAIHLPPDSKLLLRLEAALADGVPVALRTDDWAVLPLAGDYLRGLAAAV
Protein: Formin 1 (Q8I3F9)
Organism: Plasmodium falciparum (isolate 3D7)
Interaction partners:
- Micro-fibrillar-associated protein, putative
- Splicing factor 3B subunit 1, putative
- Pre-mRNA-splicing factor 38
- Splicing factor 3A subunit 1, putative
- Splicing factor 3A subunit 3, putative
- Splicing factor 3B subunit 4, putative
- Pre-mRNA-splicing factor CEF1, putative
- Pre-mRNA-processing protein 45, putative
- Pre-mRNA-processing-splicing factor 8, putative
- Pre-mRNA-splicing factor RBM22 homolog
Sequence:
MELNQTIKLATVNDIENDKNIDTLSLLTKMDLKSSNCKHVNCMKMKNINFEDSLRMNDEQIKVKEAVFILQNMENFNYSIGYSEIQNIRNDLRLFAVNSYHDKKYSDCLIQAIHSYMIAKKYYSKYFGYYLTGDMSTELILICKCFLLVQKIEEGKTYLQELKFLIDNTLLYTHRKGILDNKGLKKEVPSDNTKKNEDKNKNNDNNNNNNNNNTNSSGNNNYEEPVIMCGIQVLANILYIFADMLSLYKNNDEAENYFLKYLHINEKCYNDDSLNYSDALNDVCSFYIKIREYQKALTLCEKILNIRKLYFGDYNADKPSEIIADCYCNLGLLYRLTGNVVESLHKYIIAVDMRMRIHKTRHVIQIQDILFSFAIIMHQLNNFKMALQLYKEVYSFYKSYYGPNDMNTIMTLKLIEELQKDVMNKSGKSIKEQDSSCPIMPNYVKDKIDDTFINNKNEKYHHTNKTHNNNNNNDDDNNNMWWNTFNEKIKNISNNFNDVHPNLIEQIMNEKVTINTKNPYQNISDKKTFLTLQGKVTYNDLTYSSIDAYKHMQSNKQFQIIKNSFLNTSSINRIKSLYADSWRNTLIPSTYILPFLETKLVDKNLMKLSECKDFQNAILFKRKILPIVNIPLMERGYVQLQNDQPIMICNEDAKILLNEWYIKEPFVDSQGKVINKYESLDEQFDMFIPILDQNDDVMLGFYNTPLLVPNPAIHHCILLNDPSYFDKYNRINNIFPIDSLKFKDNLTDHNKSDITNSESYNSLNHSLSENTDSDSEHSTKKENAPLINNSRENVSSLQNFKKDTNTPKFSKKFNLKLNDPKKALKLSFSQSSSKQSSEIIKTKSSVISSTPNTSSKISDIRTQNITKTINQNDTPNIIQNHPSNGTLKSSSPDVSPNSSGTNITSKDNSLSKKITILKGKELTKNKSTNIAKDQDITLKIQNKTDNKTDNQTDNQTNNQTDNQTDNQTNNQTNNQTNNKIELSKVIEEKNLTLSDIMIGKKTNKDIKNKIPKKKIHVFKLNDNNTSRATSKFSREKYALKKFSKLNSSFKTSKDKLKLTTNENKSNEADTLEKTNRNLKFKEEPIVKSAMHPNIKMDLRNNMKKLEQYSFVNFKREIYDDDIPSNNYTNSTIFSHDDEKETVASFNEYNKGTQRKQKKSILSNRSSTVSSLSHVQNYDIIKKKIKINNKNINKNVNTNTSAHLNGTISDHITYSSSYLSKDDHKNHDTSELKYYKEDRNNIIGITEESIDNNNYDYHYDDEEDDDDINDDIVDIYKLFDSHSESSYSSVNNYTYRNEKEDNITSLSSQYTIDHVMNKKESKIYKNKYKIFSEIDNVEDDTLDEASYMETNDTYIQSHLKDTINNIKNVNKEDISFKFTYDENEFLNNDNVLSDNSFASNMINQKMLQNKKEENIIDININHDNLSDPSDFNESMSLKKGKYKQVNGNLYNNSSKHKLYDLHYDQNNIMLLNNNKIITNETKNIINNNNNIVEEMQLSENEEFFHEMMNVYDSEKYMDIVLCDNNDSTTKNTTNETSIMYDNKNEKDSHFKNNDNNITHNNNNNDNIFEKYEQPEILLENIFLSSNSIEELDSNLLNNKYKKNNSNNIYSIKALNKKTDHQSNIEYEDEANNSCISSNINCNTKETNIYHNKDDNNNVNVLRANHNKKNIENINNVLHINSEKYNTLNHSINTSNFSNPIDSNNHFNEANFDSPQYIDGITNNKNHSHTNNNKKEKKKKSNLSSSYKNTHISKLFTFLSKKRKNNNNNNTKRNATSLNNVYDEFLNNDISTKERKIYNNNNNNINHININHINSCDNICQLTKPLNDLLFDTKTFDGSNHFDHTIFDKHDNINIKKNKKTHLFITQSSHGMEKPKLLNMKGKTFTLKKLIGIKKNLGPKKQPPMQNKELTKNANMNQPEEPNDNSAKDDTPNENQNHEEIINNNQEENKQIELSNDKENQNQNQNENQNKRISLINNVQNNSEDITKKNISEKMQLKVIPKKSMNVVKHSTLDKMNEDSKNNNLLKRNNSALNKDVPYAKNINDKLSFNLLKDVKFCKIGYEKDDSMGTLPVVHLLNENKKVIAIVPWQIDLTSFALAKSSIDEEQIRKIGLMYREIDIPLEDRQKQIQVEKNLLLGEGLKELGLGRGGTPGVSSGMGVAVDSGSINLISGIDLNALKESYKIEKKIEVKEEKKESAPKKDTPKSKGAPKGGKGGKKGPPAFMKGPPKNVKGALAVGKTKFSKLTKAKDEGKTKRFFWEALFENDIPGTLFEDKKEFITKIAIEKENVEKSFAKAVSKKDNEKETKIKKPKVIQLLPDSKREYNMSIALSKFNNYTFKEIRDAIMELNPKILNIDNTEVLLQYVPTPEEFEIVKEYIHSNGDLNLVDKPEQYVAAIIGVPLLKQRLESHYYALSFKENYENTLNPLENILEACEAIKDSNKLFTILFTILNVGNTLNYGDAQRGNAFGFKLSTLSKLNDIRSSTKPVKTLLQYICEVIFEKSKETLSIIDELRCIEKSIKTDKQTIDAFLQKLKLGCNKIKTVLEQAKKTPTDPLCEALTEFYYSVEPKIVELENFYNQTFAAFKDIALYLGYKEKDINTIQVQDFFKELWTFIQAVEFNRKTINEALLKQLKKQEKELANEKQGTVLKKKQNFTITKKQDNEQKDKIEKKTFKIF
Protein: Ecdysteroid-phosphate phosphatase (EC 3.1.3.-) (Protein UBASH3A homolog) (Ubiquitin-associated and SH3 domain-containing protein) (Q9VCE9)
Organism: Drosophila melanogaster (Fruit fly)
Function: Steroid phosphatase that dephosphorylates ecdysteroids such as ecdysone 22-phosphate (E22P), 3-epi-ecdysone 22-phosphate (E22P) and 3-epi-ecdysone 2-phosphate (E2P). Likely catalyzes the conversion of inactive phosphorylated ecdysteroids into their active forms (By similarity). Shows high activity towards ecdysone 22-phosphate (E22P), but is also significantly active against 3-epi-ecdysone 22-phosphate (E22P) and 3-epi-ecdysone 2-phosphate (E2P). Also displays acid phosphatase activity towards 4-nitrophenyl phosphate (pNNP) in vitro. Has no activity towards 3-epi-ecdysone 3-phosphate (E3P).
Subcellular location: Cytoplasm, cytosol {ECO:0000269|PubMed:17348005}. Nucleus {ECO:0000269|PubMed:17348005}.
Interaction partners:
Sequence:
MATLPPRKSQTPTRICISKQHLTPLQTLLQMGFPRHRAEKALASTGNRGVQIASDWLLAHVNDGTLDECAPREYIIYACPTGPFLQQLEEFWAKSRQMCGWNGAHNYVPHITLVSFFKAPDECSLQLSKALKQVVDMTGALLDRPLKLEPYMSQNFMGFFVAEEDANYLKRLALQYVKEVSNSIISDTYEQLDAIVACFPWCGAVSSGTRCIPRSSRSISLEPHVKSLHLTLAYQFPQAQFNALKALVETLDASCASNWELRLYSRDPRLATKQVQKVVYPHNPHETDELELRIGDYIYLNTEVVDSSSDGWAEGISWLTGSTGHLPVNYTERTAESDAWTLHRVVQLSKSVASSLTSAEDLDIVDGRSISTEPDDRQNTAHPDIIEGSSFEESEQSVEKYLRQTLKPCLELPSVQLLNSHNLTHQHNPNTPTIEITTNMSSSSTSMSKQPVDEILVEPPAAQPPRPDDTLSVHSDHSLHPGSLDASHAKNRKIYIMRHGERVDFTFGTWIPYCFDEFGNYMRKDLNMPKTLPRRKNSPEGWQNDSPLTNVGVYQANLIGQALLEAQVQIDHVYCSPSYRCIQTCTSALEGLKLTGKQKIKLEPGLFEWMAWYPSGVPDWLTKNELTEAKFDVDLDYEPVQPASELTARLKESTEQFYERNHDVILQLLEQTTGNILVVAHATTLDTCSRQLTGGVPRSTNELRQVIHKIPYCSLATVEQVDGVWKLVEPECLPVTHSKNPRFEWNALSAT
Protein: Cyclin-dependent kinase inhibitor 2 (Inhibitor/interactor of CDK protein 2) (KIP-related protein 2) (Q9SCR2)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Binds and inhibits CYCD2-1/CDKA-1 complex kinase activity. Regulates cell division which is crucial for plant growth, development and morphogenesis. May regulate early lateral root initiation by blocking the G1/S phase transition. Controls the mitosis-to-endocycle transition and the onset of the endoreduplication cycle during leaf development through inhibition of mitotic CDKA-1 kinase complexes. Specifically targets CDKA-1.
Subcellular location: Nucleus, nucleoplasm {ECO:0000269|PubMed:17253089}. Note=Homogeneously distributed.
Interaction partners:
- Cyclin-dependent kinase A-1
- Cyclin-D2-1
- Cyclin-dependent kinase inhibitor 3
- Cyclin-dependent kinase inhibitor 5
- Cyclin-dependent kinase inhibitor 4
- Cyclin-D3-1
- Cyclin-dependent kinase B2-1
- Cyclin-dependent kinase B1-2
- Retinoblastoma-related protein 1
- F-box/LRR-repeat protein 17
Sequence:
MAAVRRRERDVVEENGVTTTTVKRRKMEEEVDLVESRIILSPCVQATNRGGIVARNSAGASETSVVIVRRRDSPPVEEQCQIEEEDSSVSCCSTSEEKSKRRIEFVDLEENNGDDRETETSWIYDDLNKSEESMNMDSSSVAVEDVESRRRLRKSLHETVKEAELEDFFQVAEKDLRNKLLECSMKYNFDFEKDEPLGGGRYEWVKLNP
Protein: Transcription factor (C8V7M0)
Organism: Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123, ECO:0000256|PIRNR:PIRNR002595}.
Interaction partners:
- Heat shock protein 90
- Puatative oxidoreductase
- Elongation factor 1-alpha
- Histidine-containing phosphotransfer protein
- TORC1 growth control complex subunit Kog1, putative
- Protein kinase domain-containing protein
- Hsp90 binding co-chaperone
- AAA+ ATPase domain-containing protein
- Histone deacetylase
- AAA family ATPase, putative
Sequence:
MLEDPSYAEIVRWGDDGDSFVVLECEKFTKTILPKHFKHSNFASFVRQLNKYDFHKVRQNNEENGQSPYGQNAWEFKHPEFRANSKESLDNIRRKAPAPRKQAQAHDDSVPTQQIDLLNQQIVAQQQQIQHISDRYAQMSVDHQLMLQEVLRVQKTVVNHENVIHQLVNYLVSIDARQKRDNKAGSFQAQVGASPSQVTPMDDGVSTPLQQASKLLSDMNAEVQFNLVPVESMGEPPKTGVVSTPTMETAPRRVAPQPAAAATNPALVYPKMNGEMEPVVYPVGATNGIDPMYGEHVNNVPYTVPPKQDMDDRRQFPENRKKSNHVDPGWMRSPRILLVEDDATCRQIGGKFLYSFSCEIDTALDGLEAVNKVQDGSKYDLILMDIIMPNLDGVSACHLIRQFDRTPIIAMTSNIRSDDIQLYFQHGMDDVLPKPFTRKSLLEMLEKHLVHLKTVPQGMEGHQATTPVTIAGQSSAAQSVTIKEDTSSPSQSPAAAMTAWQSPNQFQPMAAVPANLQQVQGQYVPANPATTAYAMDQNGMQYPAPPTCDRSHVGTSLN
Protein: Probable diguanylate cyclase DgcJ (DGC) (EC 2.7.7.65) (P76237)
Organism: Escherichia coli (strain K12)
Function: Catalyzes the synthesis of cyclic-di-GMP (c-di-GMP) via the condensation of 2 GTP molecules.
Subcellular location: Cell inner membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Probable cyclic di-GMP phosphodiesterase PdeI
- Cyclic di-GMP phosphodiesterase PdeL
- Cyclic di-GMP phosphodiesterase PdeR
- Probable cyclic di-GMP phosphodiesterase PdeK
- Probable cyclic di-GMP phosphodiesterase PdeN
- Probable cyclic di-GMP phosphodiesterase PdeA
- Oxygen sensor protein DosP
- Cyclic di-GMP phosphodiesterase PdeF
- Probable cyclic di-GMP phosphodiesterase PdeB
- Cyclic di-GMP phosphodiesterase PdeH
Sequence:
MKLHHRMLRHFIAASVIVLTSSFLIFELVASDRAMSAYLRYIVQKADSSFLYDKYQNQSIAAHVMRALAAEQSEVSPEQRRAICEAFESANNTHGLNLTAHKYPGLRGTLQTASTDCDTIVEAAALLPAFDQAVEGNRHQDDYGSGLGMAEEKFHYYLDLNDRYVYFYEPVNVEYFAMNNWSFLQSGSIGIDRKDIEKVFTGRTVLSSIYQDQRTKQNVMSLLTPVYVAGQLKGIVLLDINKNNLRNIFYTHDRPLLWRFLNVTLTDTDSGRDIIINQSEDNLFQYVSYVHDLPGGIRVSLSIDILYFITSSWKSVLFWILTALILLNMVRMHFRLYQNVSRENISDAMTGLYNRKILTPELEQRLQKLVQSGSSVMFIAIDMDKLKQINDTLGHQEGDLAITLLAQAIKQSIRKSDYAIRLGGDEFCIILVDSTPQIAAQLPERIEKRLQHIAPQKEIGFSSGIYAMKENDTLHDAYKASDERLYVNKQNKNSRS
Protein: 3-isopropylmalate dehydrogenase 3, chloroplastic (3-IPM-DH 3) (AtIMDH2) (AtIMDH3) (IMDH 3) (EC 1.1.1.85) (Beta-IPM dehydrogenase 3) (Isopropylmalate dehydrogenase 3) (AtIMD3) (Q9SA14)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Involved in leucine biosynthesis; catalyzes the oxidative decarboxylation step in leucine biosynthesis (primary metabolism). Catalyzes the oxidation of 3-carboxy-2-hydroxy-4-methylpentanoate (3-isopropylmalate, 3-IPM) to 3-carboxy-4-methyl-2-oxopentanoate. The product decarboxylates to 4-methyl-2 oxopentanoate.
Subcellular location: Plastid, chloroplast stroma {ECO:0000269|PubMed:19542295}.
Interaction partners:
- 3-isopropylmalate dehydratase small subunit 3
- 3-isopropylmalate dehydratase small subunit 2
- 3-isopropylmalate dehydratase large subunit, chloroplastic
- 3-isopropylmalate dehydratase small subunit 1
- Acetolactate synthase small subunit 1, chloroplastic
- Acetolactate synthase small subunit 2, chloroplastic
- Acetolactate synthase, chloroplastic
- Methylthioalkylmalate synthase 1, chloroplastic
- Methylthioalkylmalate synthase 3, chloroplastic
- Threonine dehydratase biosynthetic, chloroplastic
Sequence:
MAAFLQTNIRLEIIPGRYSSLTDHKFRAPYRIRCAAASPVKKRYNITLLPGDGIGPEVISVAKNVLQKAGFLQGLEFDFQEMPFGGAALDLVGVPLPEETSTAAKQSDAILLGAIGGYKWDKNEKHLRPEMGLLNIRRDLNVFANLRPATVLPQLVDASTLKKEVAQGVDMMIVRELTGGIYFGEPRGITINENGEEVGFNTEIYAAHEIDRIARVAFETARKRRGKLCSVDKANVLDASILWRKRVTALASEYPDVELSHMYVDNAAMQLVRDPKQFDTIVTNNIFGDILSDEASMITGSIGMLPSASLGESGPGLFEPIHGSAPDIAGQDKANPLATILSAAMLLKYGLGEEKAAKMIEDAVVDALNKGFRTGDIYSPGNKLVGCKEMGEEVLKSVDSKVPV