wanglab/gogpt-training-data huggingface dataset:
Protein: PH domain leucine-rich repeat-containing protein phosphatase 2 (EC 3.1.3.16) (PH domain leucine-rich repeat-containing protein phosphatase-like) (PHLPP-like) (Q6ZVD8)
Organism: Homo sapiens (Human)
Function: Protein phosphatase involved in regulation of Akt and PKC signaling. Mediates dephosphorylation in the C-terminal domain hydrophobic motif of members of the AGC Ser/Thr protein kinase family; specifically acts on 'Ser-473' of AKT1, 'Ser-660' of PRKCB isoform beta-II and 'Ser-657' of PRKCA. Akt regulates the balance between cell survival and apoptosis through a cascade that primarily alters the function of transcription factors that regulate pro- and antiapoptotic genes. Dephosphorylation of 'Ser-473' of Akt triggers apoptosis and decreases cell proliferation. Also controls the phosphorylation of AKT3. Dephosphorylates STK4 on 'Thr-387' leading to STK4 activation and apoptosis. Dephosphorylates RPS6KB1 and is involved in regulation of cap-dependent translation. Inhibits cancer cell proliferation and may act as a tumor suppressor. Dephosphorylation of PRKCA and PRKCB leads to their destabilization and degradation. Dephosphorylates RAF1 inhibiting its kinase activity.
Subcellular location: Cytoplasm. Membrane; Peripheral membrane protein. Nucleus. Note=In colorectal cancer tissue, expression is concentrated in the cytoplasm and nucleus.
Interaction partners:
- RAC-gamma serine/threonine-protein kinase
- RAC-alpha serine/threonine-protein kinase
- PH domain leucine-rich repeat-containing protein phosphatase 1
- RAC-beta serine/threonine-protein kinase
- Ubiquitin carboxyl-terminal hydrolase 46
- Ubiquitin carboxyl-terminal hydrolase 12
- WD repeat-containing protein 20
- WD repeat-containing protein 48
- Na
- Phosphatidylinositol 3,4,5-trisphosphate 3-phosphatase and dual-specificity protein phosphatase PTEN
Sequence:
MKRNGSRNCLNRRSRFGSRERDWLREDVKRGCVYLYGADTTTATTTTTTSSSSSSSSSSSDLHLVLCTVETPASEICAGEGRESLYLQLHGDLVRRLEPTERPLQIVYDYLSRLGFDDPVRIQEEATNPDLGCMIRFYGEKPCHMDRLDRILLSGIYNVRKGKTQLHKWAERLVVLCGTCLIVSSVKDCQTGKMHILPLVGGKIEEVKRRQYSLAFSSAGAQAQTYHVSFETLAEYQRWQRQASKVVSQRISTVDLSCYSLEEVPEHLFYSQDITYLNLRHNFMQLERPGGLDTLYKFSQLKGLNLSHNKLGLFPILLCEISTLTELNLSCNGFHDLPSQIGNLLNLQTLCLDGNFLTTLPEELGNLQQLSSLGISFNNFSQIPEVYEKLTMLDRVVMAGNCLEVLNLGVLNRMNHIKHVDLRMNHLKTMVIENLEGNKHITHVDLRDNRLTDLDLSSLCSLEQLHCGRNQLRELTLSGFSLRTLYASSNRLTAVNVYPVPSLLTFLDLSRNLLECVPDWACEAKKIEVLDVSYNLLTEVPVRILSSLSLRKLMLGHNHVQNLPTLVEHIPLEVLDLQHNALTRLPDTLFSKALNLRYLNASANSLESLPSACTGEESLSMLQLLYLTNNLLTDQCIPVLVGHLHLRILHLANNQLQTFPASKLNKLEQLEELNLSGNKLKTIPTTIANCKRLHTLVAHSNNISIFPEILQLPQIQFVDLSCNDLTEILIPEALPATLQDLDLTGNTNLVLEHKTLDIFSHITTLKIDQKPLPTTDSTVTSTFWSHGLAEMAGQRNKLCVSALAMDSFAEGVGAVYGMFDGDRNEELPRLLQCTMADVLLEEVQQSTNDTVFMANTFLVSHRKLGMAGQKLGSSALLCYIRPDTADPASSFSLTVANVGTCQAVLCRGGKPVPLSKVFSLEQDPEEAQRVKDQKAIITEDNKVNGVTCCTRMLGCTYLYPWILPKPHISSTPLTIQDELLILGNKALWEHLSYTEAVNAVRHVQDPLAAAKKLCTLAQSYGCQDNVGAMVVYLNIGEEGCTCEMNGLTLPGPVGFASTTTIKDAPKPATPSSSSGIASEFSSEMSTSEVSSEVGSTASDEHNAGGLDTALLPRPERRCSLHPTPTSGLFQRQPSSATFSSNQSDNGLDSDDDQPVEGVITNGSKVEVEVDIHCCRGRDLENSPPLIESSPTLCSEEHARGSCFGIRRQNSVNSGMLLPMSKDRMELQKSPSTSCLYGKKLSNGSIVPLEDSLNLIEVATEVPKRKTGYFAAPTQMEPEDQFVVPHDLEEEVKEQMKQHQDSRLEPEPHEEDRTEPPEEFDTAL
Protein: non-specific serine/threonine protein kinase (EC 2.7.11.1) (Q86NK8)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
Interaction partners:
Sequence:
MQRRERQASGGGPQTTTAGPSAGNVANATTALAGGKSSSNNMYSTRQSVSTTTGVLMVGPNFRVGKKIGCGNFGELRLGKNLYNNEHVAIKMEPMKSKAPQLHLEYRFYKLLGSHADNAPDGIPRIYHLGTCGGRYNAMVLELLGLSLEDLFNICARKFSLKTVLMIAKQLLHRIEYVHSRHLIYRDVKPENFLIGRTSTKREKIIHIIDFGLAKEYIDLDTNRHIPYREHKSLTGTARYMSINTHMGREQSRRDDLEALGHMFMYFLRGSLPWQGLKADTLKERYQKIGDTKRATPIEVLCDGHPEEFATYLRYVRRLDFFETPDYDFLRRLFQDLFDRKGYTDEGEFDWTGKTMSTPVGSLQTGHEVIISPNKDRHNVTAKTNAKGGVAAWPDVPKPGATLGNLTPADRHGSVQVVSSTNGELNPDDPTAGHSNTPITQQPEVEVVDETNGSLYSRCCCFFKRKKKKSTRQK
Protein: Smad protein daf-3 (Abnormal dauer formation protein 3) (Q95QI7)
Organism: Caenorhabditis elegans
Function: Transcriptional regulator and common SMAD (co-SMAD), required to regulate entry into a developmentally arrested larval state known as dauer, in response to harsh environmental conditions. Probable component of transcriptional regulatory complex with SMAD protein daf-5. Acts antagonistically to SMAD signaling downstream of TGF-beta-like daf-7 signaling. Binds to the 5'-GTCTG-3' motif found in regulatory regions and may modulate the expression of genes involved in TGF-beta-like daf-7 and Notch lag-2 signaling. May regulate gene expression outside the dauer pathway.
Subcellular location: Cytoplasm {ECO:0000255|RuleBase:RU361195, ECO:0000269|PubMed:9334330}. Nucleus {ECO:0000255|RuleBase:RU361195, ECO:0000269|PubMed:9334330}. Chromosome {ECO:0000269|PubMed:9334330}. Note=Localization observed during mitosis. {ECO:0000269|PubMed:9334330}.
Interaction partners:
Sequence:
MGDHHNLTGLPGTSIPPQFNYSQPGTSTGGPLYGGKPSHGLEDIPDVEEYERNLLGAGAGFNLLNVGNMANEFKPIITLDTKPPRDANKSLAFNGGLKLITPKTEVPDEHTPMMSPVNTTTKILQRSGIKMEIPPYLDPDSQDDDPEDGVNYPDPDLFDTKNTNMTEYDLDVLKLGKPAVDEARKKIEVPDASAPPNKIVEYLMYYRTLKESELIQLNAYRTKRNRLSLNLVKNNIDREFDQKACESLVKKLKDKKNDLQNLIDVVLSKGTKYTGCITIPRTLDGRLQVHGRKGFPHVVYGKLWRFNEMTKNETRHVDHCKHAFEMKSDMVCVNPYHYEIVIGTMIVGQRDHDNRDMPPPHQRYHTPGRQDPVDDMSRFIPPASIRPPPMNMHTRPQPMPQQLPSVGATFAHPLPHQAPHNPGVSHPYSIAPQTHYPLNMNPIPQMPQMPQMPPPLHQGYGMNGPSCSSENNNPFHQNHHYNDISHPNHYSYDCGPNLYGFPTPYPDFHHPFNQQPHQPPQLSQNHTSQQGSHQPGHQGQVPNDPPISRPVLQPSTVTLDVFRRYCRQTFGNRFFEGESEQSGAIIRSSNKFIEEFDSPICGVTVVRPRMTDGEVLENIMPEDAPYHDICKFILRLTSESVTFSGEGPEVSDLNEKWGTIVYYEKNLQIGEKKCSRGNFHVDGGFICSENRYSLGLEPNPIREPVAFKVRKAIVDGIRFSYKKDGSVWLQNRMKYPVFVTSGYLDEQSGGLKKDKVHKVYGCASIKTFGFNVSKQIIRDALLSKQMATMYLQGKLTPMNYIYEKKTQEELRREATRTTDSLAKYCCVRVSFCKGFGEAYPERPSIHDCPVWIELKINIAYDFMDSICQYITNCFEPLGMEDFAKLGINVSDD
Protein: Solanesyl diphosphate synthase 2, chloroplastic (AtSPS2) (EC 2.5.1.85) (All-trans-nonaprenyl-diphosphate synthase 2 (geranylgeranyl-diphosphate specific)) (Q76FS5)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Involved in providing solanesyl diphosphate for plastoquinone-9 (PQ-9) formation in plastids (Probable). Catalyzes the elongation of the prenyl side chain of PQ-9 in plastids. Contributes to the biosynthesis of plastochromanol-8 (PC-8) in plastids. Does not contribute to the synthesis of tocopherol or ubiquinone. PQ-9 and PC-8 are lipophilic antioxidants that act as protectant against photooxidative stress under high light stress conditions. Prefers geranylgeranyl diphosphate to farnesyl diphosphate as substrate. No activity with geranyl diphosphate or dimethylallyl diphosphate as substrate.
Subcellular location: Plastid, chloroplast {ECO:0000269|PubMed:15653808, ECO:0000269|PubMed:15784989, ECO:0000269|PubMed:23913686, ECO:0000269|PubMed:26432861}.
Interaction partners:
- Geranylgeranyl diphosphate reductase, chloroplastic
- Solanesyl diphosphate synthase 1, chloroplastic
- Phytoene synthase 1, chloroplastic
- Homogentisate solanesyltransferase, chloroplastic
- Fibrillin-5, chloroplastic
- 2-carboxy-1,4-naphthoquinone phytyltransferase, chloroplastic
- 4-hydroxybenzoate polyprenyltransferase, mitochondrial
- Homogentisate phytyltransferase 1, chloroplastic
- Ent-copalyl diphosphate synthase, chloroplastic
- Farnesyl pyrophosphate synthase 1, mitochondrial
Sequence:
MMMSCRNIDLGTSVLDHSCSSSSTSRRFLFGNSSKTVCMIGGRSCVGNLVFLRRDLATCRAVPAKSKENSLVNGIGQDQTVMLNLRQESRKPISLETLFEVVADDLQRLNDNLLSIVGAENPVLISAAEQIFSAGGKRMRPGLVFLVSRATAELAGLKELTVEHRRLGEIIEMIHTASLIHDDVLDESDMRRGRETVHELFGTRVAVLAGDFMFAQASWYLANLENLEVIKLISQVIKDFASGEIKQASSLFDCDVKLDDYMLKSYYKTASLVAASTKGAAIFSKVESKVAEQMYQFGKNLGLSFQVVDDILDFTQSTEQLGKPAANDLAKGNITAPVIFALENEPRLREIIESEFCEPGSLEEAIEIVRNRGGIKKAQELAKEKAELALKNLNCLPRSGFRSALEDMVMFNLERID
Protein: Neuropeptide-Like Protein (O01970)
Organism: Caenorhabditis elegans
Interaction partners:
- G-protein coupled receptors family 1 profile domain-containing protein
- G-protein coupled receptors family 1 profile domain-containing protein
- Neuropeptide-Like Protein
- Neuropeptide-Like Protein
- Neuropeptide-Like Protein
- FMRFamide-like neuropeptides 1
- Neuropeptide-like peptide 11
- Neuropeptide-Like Protein
- FMRFamide-like neuropeptide 18
- FMRFamide-like neuropeptides 14
Sequence:
MLRHHSCALLMLILVFVEVFATQSPTFDRQDRDYRPLQFGKRDGYRPLQFGKRDYRPLQFGKRSSGSSGPVVLEPIWEWQ
Protein: AT27450p (Q8MZ81)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MKKVSKSIKREGSPSDEEYTLEEDPIEFELEKMERGSSNGESEEEGQRDQKQADSIIDDMVEQNDKEQEAAGEQDVERENDLRKMYELSLLPPAAIAAQIQQMEKEIYELSQWEARELIRSKHLRIFGNCRRRANK
Protein: S-adenosylmethionine carrier 1, chloroplastic/mitochondrial (S-adenosylmethionine transporter 1) (AtSAMT1) (Q94AG6)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Transporter involved in exchange reactions through membranes. Has a low uniporter activity. Specifically mediates the transport of S-adenosylmethionine (SAM) and its closest analogs. Probably involved in the uptake of SAM in exchange for S-adenosylhomocysteine (SAHC), which is produced from SAM in the mitochondrial matrix and plastidial stroma by methyltransferase activities.
Subcellular location: Mitochondrion membrane; Multi-pass membrane protein. Plastid, chloroplast membrane; Multi-pass membrane protein. Note=Detected in chloroplast envelope, but not in thylakoid membranes or in chloroplast stroma (PubMed:17098813). According to another report, localization is restricted to the mitochondria (PubMed:16950860). {ECO:0000269|PubMed:16950860, ECO:0000269|PubMed:17098813}.
Interaction partners:
- AT5g24690/MXC17_8)
- Plastidal glycolate/glycerate translocator 1, chloroplastic
- Pentatricopeptide repeat-containing protein At3g22150
- Dicarboxylate transporter 1, chloroplastic
- ADP,ATP carrier protein 2, chloroplastic
Sequence:
MAPLTLSVDVKSSSATSHDVSKRVMQSSQLKINKGFFASVNTQEDKPFDFFRTLFEGFIAGGTAGVVVETALYPIDTIKTRLQAARGGGKIVLKGLYSGLAGNIAGVLPASALFVGVYEPTKQKLLKTFPDHLSAVAHLTAGAIGGLAASLIRVPTEVVKQRMQTGQFTSAPSAVRMIASKEGFRGLYAGYRSFLLRDLPFDAIQFCIYEQLCLGYKKAARRELSDPENALIGAFAGALTGAVTTPLDVIKTRLMVQGSAKQYQGIVDCVQTIVREEGAPALLKGIGPRVLWIGIGGSIFFGVLESTKRTLAQRRPNTVKETKEE
Protein: LexA repressor (EC 3.4.21.88) (Q6MHM9)
Organism: Bdellovibrio bacteriovorus (strain ATCC 15356 / DSM 50701 / NCIMB 9529 / HD100)
Interaction partners:
- Protein RecA
- RecA protein
- DNA polymerase IV
- DNA repair protein RecN
- DNA polymerase I
- DNA polymerase Y family protein
- UvrABC system protein B
- Holliday junction branch migration complex subunit RuvA
- Error-prone DNA polymerase
- DNA replication and repair protein RecF
Sequence:
MTMKTPLPPLTPKEKSVLEFIEAHILSSGVSPSYQEIKDHFGLASFNSVQNYLKQLTNKGYISNPQNLKRAIQVLHSASAVQDQLQSKTVSTKTGSPRTQLLQARDEILSLPLLGKVAAGQPIEAIKHDEFVDVPPSMVRNPSKSFALKVQGDSMIEDGIFDEDIILIQKQNSANNGDIIVATVDNEATVKRFYLRPRPETGDADKMVELRPSNSTMKSMWYTPDEVEIRGIVVGLIRKF
Protein: Hypoxanthine-guanine phosphoribosyltransferase (HGPRT) (HGPRTase) (EC 2.4.2.8) (P27605)
Organism: Rattus norvegicus (Rat)
Function: Converts guanine to guanosine monophosphate, and hypoxanthine to inosine monophosphate. Transfers the 5-phosphoribosyl group from 5-phosphoribosylpyrophosphate onto the purine. Plays a central role in the generation of purine nucleotides through the purine salvage pathway (By similarity).
Subcellular location: Cytoplasm.
Interaction partners:
- Adenine phosphoribosyltransferase
- Purine nucleoside phosphorylase
- AMP deaminase 2
- AMP deaminase 1
- AMP deaminase 3
- Guanine deaminase
- Adenylosuccinate synthetase isozyme 2
- Inosine-5'-monophosphate dehydrogenase 1
- Adenylosuccinate synthetase isozyme 1
- Bifunctional purine biosynthesis protein ATIC
Sequence:
MSTLSPSVVISDDEPGYDLDLFCIPNHYAEDLEKVFIPHGLIMDRTERLARDVMKEMGGHHIVALCVLKGGYKFFADLLDYIKALNRNSDRSIPMTVDFIRLKSYCNDQSTGDIKVIGGDDLSTLTGKNVLIVEDIIDTGKTMQTLLSLVKQYSPKMVKVASLLVKRTSRSVGYRPDFVGFEIPDKFVVGYALDYNEHFRDLNHVCVISESGKAKYKA
Protein: Tyrosine-protein kinase (EC 2.7.10.2) (A0A8I5ZU24)
Organism: Rattus norvegicus (Rat)
Interaction partners:
Sequence:
MQYLNIKEDCNAMAFCAKMRSFKKTEVKQVAPEPGVEVTFYLLDREPLRLGSGEYTAEELCIRAAQECSISPLCHNLFALYDESTKLWYAPNHIITVDDKMSLRLHYRMRFYFTNWHGTNDNEQSVWRHSPKKQKNGYEKKKVPEATPLLDASSLEYLFAQGQYDLIKCLAPIRDPKTEQDGHDIENECLGMAVLAISHYAMMKKMQLPELPKDISYKRYIPETLNKSIRQRNLLTRMRINNVFKDFLKEFNNKTICDSSVSTHDLKVKYLATLETLTKHYGAEIFETSMLLISSENELSRCHSNDSGNVLYEVMVTGNLGIQWRQKPNVLPVEKEKNKLKRKKLDYNKHKKEDDRNKLREEWNSFSYFPEITHIVIKESVVSINKQDNKNMELKLSSHEEALSFVSLVDGYFRLTADAHHYLCTDVAPPLIVHNIQNGCHGPICTEYAINKLRQEGSEEGMYVLRWSCTDFDNILMTVSCFEKSEVLGNQKQFKNFQIEVQKGRYSLHGSVDHFPSLRDLMNHLKKQILRTDNISFVLKRCCQPKPREISNLLVATKKAQEWQPVYSMSQLSFDRILKKDIIQGEHLGRGTRTHIYSGTLLDYKDDEGIAEEKKIKVILKVLDPSHRDISLAFFEAASMMRQVSHKHIVYLYGVCVRDVENIMVEEFVEGGPLDLFMHRKSDALTTPWKFKVAKQLASALSYLEDKDLVHGNVCTKNLLLAREGIDSDIGPFIKLSDPGIPVSVLTRQECIERIPWIAPECVEDSKNLSVAADKWSFGTTLWEICYNGEIPLKDKTLIEKERFYESRCRPVTPSCKELADLMTRCMNYDPNQRPFFRAIMRDINKLEEQNPDIVSEKQPITEVDPTHFEKRFLKRIRDLGEGHFGKVELCRYDPEGDNTGEQVAVKSLKPESGGNHIADLKKEIEILRNLYHENIVKYKGICMEDGGNGIKLIMEFLPSGSLKEYLPKNKNKINLKQQLKYAIQICKGMDYLGSRQYVHRDLAARNVLVESEHQVKIGDFGLTKAIETDKEYYTVKDDRDSPVFWYAPECLIQCKFYIASDVWSFGVTLHELLTYCDSDFSPMALFLKMIGPTHGQMTVTRLVNTLKEGKRLSCPPNCPDEVAVSPSWEGNFLSNVFIA
Protein: Protection of telomeres protein 1b (AtPOT1b) (Protection of telomeres protein 2) (AtPot2) (Q6NKX5)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Negatively regulates telomerase activity and participates in chromosome end protection. Binds RNA non-specifically. Associates with a regulatory Pol III-dependent lncRNA, which represses telomerase activity in response to DNA damage. Binds single-stranded telomeric DNA with weak affinity.
Subcellular location: Nucleus {ECO:0000250}. Chromosome, telomere {ECO:0000250}.
Interaction partners:
- Telomerase reverse transcriptase
- CST complex subunit CTC1
- Telomere repeat-binding factor 1
- CST complex subunit TEN1
- D-tagatose-1,6-bisphosphate aldolase subunit
- Telomere repeat-binding factor 3
- CST complex subunit STN1
- H/ACA ribonucleoprotein complex subunit 3-like protein
- H/ACA ribonucleoprotein complex subunit 4
- Putative H/ACA ribonucleoprotein complex subunit 1-like protein 1
Sequence:
MEEERRDDYKFLRIQDAFKALHLHVNLIGVIVELGFSNGSDCSCTLKIVDPWYSGSGLPVKFVARTIRDLPRVESIGDIILLSRVKIVLINRKITALCNETTSSSFALFNGKHSVDSIPYQSSPKFLMREQDKNFLSNLREWMITYKFEDGSCCFTSLKDIKEGECSNLSCQIVHISKVYKDRWYLFVWDGTEMPPCNILVKSERLPLCVEPEMLPTYMLRKFPTFGSVLRIIVDRVSEKQAIHCLQPGQHVKLLNLFFQVNMGLWNATFTPSTKMQYTMSREMEAFSPQRMCGEKFSPRWNPIARCISRSHSEITGVAHDDAPFVSLMDILTYHNVTAKFRCVVRFIQVYPRDVRKLRDINGNIKLVAILEDATARIHASLYADEGEKFFGCDESDEEALVKKLNRLLGGEEMEKVPRNPPWVQCCLFSFYKHKMDQWESRRFRIFDTWINAS
Protein: Glutamate receptor ionotropic, kainate 3 (GluK3) (Glutamate receptor 7) (GluR-7) (GluR7) (P42264)
Organism: Rattus norvegicus (Rat)
Function: Receptor for glutamate that functions as ligand-gated ion channel in the central nervous system and plays an important role in excitatory synaptic transmission. L-glutamate acts as an excitatory neurotransmitter at many synapses in the central nervous system. The postsynaptic actions of Glu are mediated by a variety of receptors that are named according to their selective agonists. This receptor binds domoate > kainate >> L-glutamate = quisqualate >> AMPA = NMDA.
Subcellular location: Cell membrane {ECO:0000305|PubMed:10023812}; Multi-pass membrane protein {ECO:0000255}. Postsynaptic cell membrane {ECO:0000305|PubMed:10023812}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Glutamate receptor ionotropic, kainate 4
- Glutamate receptor ionotropic, kainate 1
- Glutamate receptor ionotropic, kainate 2
- Glutamate receptor ionotropic, kainate 5
- Glutamate receptor 1
- Lysine--tRNA ligase
- Glutamate receptor ionotropic, NMDA 2A
- Glutamate receptor ionotropic, NMDA 2B
- Glutamate receptor ionotropic, NMDA 3B
- Disks large homolog 4
Sequence:
MTAPWRRLRSLVWEYWAGFLVCAFWIPDSRGMPHVIRIGGIFEYADGPNAQVMNAEEHAFRFSANIINRNRTLLPNTTLTYDIQRIHFHDSFEATKKACDQLALGVVAIFGPSQGSCTNAVQSICNALEVPHIQLRWKHHPLDNKDTFYVNLYPDYASLSHAILDLVQSLKWRSATVVYDDSTGLIRLQELIMAPSRYNIRLKIRQLPIDSDDSRPLLKEMKRGREFRIIFDCSHTMAAQILKQAMAMGMMTEYYHFIFTTLDLYALDLEPYRYSGVNLTGFRILNVDNAHVSAIVEKWSMERLQAAPRAESGLLDGVMMTDAALLYDAVHIVSVCYQRASQMTVNSLQCHRHKPWRFGGRFMNFIKEAQWEGLTGRIVFNKTSGLRTDFDLDIISLKEDGLEKVGVWSPADGLNITEVAKGRGPNVTDSLTNRSLIVTTLLEEPFVMFRKSDRTLYGNDRFEGYCIDLLKELAHILGFSYEIRLVEDGKYGAQDDKGQWNGMVKELIDHKADLAVAPLTITHVREKAIDFSKPFMTLGVSILYRKPNGTNPSVFSFLNPLSPDIWMYVLLAYLGVSCVLFVIARFSPYEWYDAHPCNPGSEVVENNFTLLNSFWFGMGSLMQQGSELMPKALSTRIIGGIWWFFTLIIISSYTANLAAFLTVERMESPIDSADDLAKQTKIEYGAVKDGATMTFFKKSKISTFEKMWAFMSSKPSALVKNNEEGIQRTLTADYALLMESTTIEYITQRNCNLTQIGGLIDSKGYGIGTPMGSPYRDKITIAILQLQEEDKLHIMKEKWWRGSGCPEEENKEASALGIQKIGGIFIVLAAGLVLSVLVAVGEFIYKLRKTAEREQRSFCSTVADEIRFSLTCQRRLKHKPQPPMMVKTDAVINMHTFNDRRLPGKDSMSCSTSLAPVFP
Protein: RING-type E3 ubiquitin transferase (EC 2.3.2.27) (Q7K4D1)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Ubiquitin-ribosomal protein eS31 fusion protein
- Mitogen-activated protein kinase kinase kinase 7
- UDP-glucuronic acid decarboxylase 1
Sequence:
MDEHTLNDLLECSVCLERLDTTSKVLPCQHTFCRKCLQDIVASQHKLRCPECRILVSCKIDELPPNVLLMRILEGMKQNAAAGKGEEKGEETETQPERAKPQPPAESVAPPDNQLLQLQSHQQSHQPARHKQRRFLLPHAYALFDFASGEATDLKFKKGDLILIKHRIDNNWFVGQANGQEGTFPINYVKVSVPLPMPQCIAMYDFKMGPNDEEGCLEFKKSTVIQVMRRVDHNWAEGRIGQTIGIFPIAFVELNAAAKKLLDSGLHTHPFCHPPKQQGQRALPPVPVIDPTVVTESSSGSSNSTPGSSNSSSTSSSNNCSPNHQISLPNTPQHVVASGSASVRFRDKGAKEKRHSLNALLGGGAPLSLLQTNRHSAEILSLPHELSRLEVSSSTALKPTSAPQTSRVLKTTVQQQMQPNLPWGYLALFPYKPRQTDELELKKGCVYIVTERCVDGWFKGKNWLDITGVFPGNYLTPLRARDQQQLMHQWKYVPQNADAQMAQVQQHPVAPDVRLNNMLSMQPPDLPPRQQQATATTTSCSVWSKPVEALFSRKSEPKPETATASTTSSSSSGAVGLMRRLTHMKTRSKSPGASLQQVPKEAISTNVEFTTNPSAKLHPVHVRSGSCPSQLQHSQPLNETPAAKTAAQQQQFLPKQLPSASTNSVSYGSQRVKGSKERPHLICARQSLDAATFRSMYNNAASPPPPTTSVAPAVYAGGQQQVIPGGGAQSQLHANMIIAPSHRKSHSLDASHVLSPSSNMITEAAIKASATTKSPYCTRESRFRCIVPYPPNSDIELELHLGDIIYVQRKQKNGWYKGTHARTHKTGLFPASFVEPDC
Protein: Nuclear migration protein nudC (Nuclear distribution protein C homolog) (Q9VVA6)
Organism: Drosophila melanogaster (Fruit fly)
Function: Chaperone protein with functions in nuclear localization and cytoplasmic mRNA trafficking. In postmitotic neurons, acts with nudE downstream of dar1 to ensure correct positioning of the nuclei in primary dendrites and as a consequence, is required for determining multipolar neuron morphology. Stabilizes PCID2 in the cytoplasm and thereby is required for promoting cytoplasmic mRNA trafficking.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:33602059}.
Interaction partners:
- Serine/threonine-protein kinase polo
- Nuclear distribution protein nudE homolog
- Lissencephaly-1 homolog
- T-complex protein 1 subunit eta
Sequence:
MAAEEGKFDNILLAVAEKHHGGVPEFLGTLASFLRRKTDFFTGAKQTEWEKLLLDVFNKESKLAVTENYEKIKAREASQRLKAEKERAERKARKQEIDDNKICDITDEEAAAIIKEEETKKRQQLLDSAGGEPSASNRDGISKPIEKVDDESDKSELGKLMPNAGNGCTLENYTWTQTLEEVELKIPFNLTFGLRARDLVISIGKKSLKVGIKGQTPIIDGELCGEVKTEESVWVLQDSKTVMITLDKINKMNWWSRLVTTDPEISTRKINPESSKLSDLDGETRSMVEKMMYDQRQKELGLPTSEDRKKQDILEKFKQQHPEMDFSKCKFN
Protein: Transforming growth factor beta activator LRRC33 (Leucine-rich repeat-containing protein 33) (Negative regulator of reactive oxygen species) (Q86YC3)
Organism: Homo sapiens (Human)
Function: Key regulator of transforming growth factor beta-1 (TGFB1) specifically required for microglia function in the nervous system (By similarity). Required for activation of latent TGF-beta-1 in macrophages and microglia: associates specifically via disulfide bonds with the Latency-associated peptide (LAP), which is the regulatory chain of TGFB1, and regulates integrin-dependent activation of TGF-beta-1 (By similarity). TGF-beta-1 activation mediated by LRRC33/NRROS is highly localized: there is little spreading of TGF-beta-1 activated from one microglial cell to neighboring microglia, suggesting the existence of localized and selective activation of TGF-beta-1 by LRRC33/NRROS (By similarity). Indirectly plays a role in Toll-like receptor (TLR) signaling: ability to inhibit TLR-mediated NF-kappa-B activation and cytokine production is probably a consequence of its role in TGF-beta-1 signaling.
Subcellular location: Cell membrane {ECO:0000269|PubMed:23545260, ECO:0000269|PubMed:29909984}; Single-pass type I membrane protein {ECO:0000255}. Endoplasmic reticulum membrane {ECO:0000269|PubMed:32197075}; Single-pass type I membrane protein {ECO:0000255}.
Interaction partners:
- Transforming growth factor beta-1 proprotein
Sequence:
MELLPLWLCLGFHFLTVGWRNRSGTATAASQGVCKLVGGAADCRGQSLASVPSSLPPHARMLTLDANPLKTLWNHSLQPYPLLESLSLHSCHLERISRGAFQEQGHLRSLVLGDNCLSENYEETAAALHALPGLRRLDLSGNALTEDMAALMLQNLSSLRSVSLAGNTIMRLDDSVFEGLERLRELDLQRNYIFEIEGGAFDGLAELRHLNLAFNNLPCIVDFGLTRLRVLNVSYNVLEWFLATGGEAAFELETLDLSHNQLLFFPLLPQYSKLRTLLLRDNNMGFYRDLYNTSSPREMVAQFLLVDGNVTNITTVSLWEEFSSSDLADLRFLDMSQNQFQYLPDGFLRKMPSLSHLNLHQNCLMTLHIREHEPPGALTELDLSHNQLSELHLAPGLASCLGSLRLFNLSSNQLLGVPPGLFANARNITTLDMSHNQISLCPLPAASDRVGPPSCVDFRNMASLRSLSLEGCGLGALPDCPFQGTSLTYLDLSSNWGVLNGSLAPLQDVAPMLQVLSLRNMGLHSSFMALDFSGFGNLRDLDLSGNCLTTFPRFGGSLALETLDLRRNSLTALPQKAVSEQLSRGLRTIYLSQNPYDCCGVDGWGALQHGQTVADWAMVTCNLSSKIIRVTELPGGVPRDCKWERLDLGLLYLVLILPSCLTLLVACTVIVLTFKKPLLQVIKSRCHWSSVY
Protein: 5-taurinomethyluridine-[tRNA] synthase subunit GTPB3, mitochondrial (EC 3.6.1.-) (GTP-binding protein 3) (Mitochondrial GTP-binding protein 1) (tRNA modification GTPase GTPBP3, mitochondrial) (Q969Y2)
Organism: Homo sapiens (Human)
Function: GTPase involved in the 5-carboxymethylaminomethyl modification (mnm(5)s(2)U34) of the wobble uridine base in mitochondrial tRNAs.
Subcellular location: Mitochondrion {ECO:0000269|PubMed:12370316, ECO:0000269|PubMed:33619562}.; SUBCELLULAR LOCATION: [Isoform 4]: Cytoplasm {ECO:0000269|PubMed:33619562}.
Interaction partners:
- 5-taurinomethyluridine-[tRNA] synthase subunit MTO1, mitochondrial
- Mitochondrial tRNA-specific 2-thiouridylase 1
- Large ribosomal subunit protein uL11m
- GTP-binding protein 8
- Mitochondrial ribosome-associated GTPase 1
- Endoplasmic reticulum-Golgi intermediate compartment protein 2
- Endoplasmic reticulum-Golgi intermediate compartment protein 1
- Large ribosomal subunit protein bL21m
- Endoplasmic reticulum-Golgi intermediate compartment protein 3
- rRNA methyltransferase 3, mitochondrial
Sequence:
MWRGLWTLAAQAARGPRRLCTRRSSGAPAPGSGATIFALSSGQGRCGIAVIRTSGPASGHALRILTAPRDLPLARHASLRLLSDPRSGEPLDRALVLWFPGPQSFTGEDCVEFHVHGGPAVVSGVLQALGSVPGLRPAEAGEFTRRAFANGKLNLTEVEGLADLIHAETEAQRRQALRQLDGELGHLCRGWAETLTKALAHVEAYIDFGEDDNLEEGVLEQADIEVRALQVALGAHLRDARRGQRLRSGVHVVVTGPPNAGKSSLVNLLSRKPVSIVSPEPGTTRDVLETPVDLAGFPVLLSDTAGLREGVGPVEQEGVRRARERLEQADLILAMLDASDLASPSSCNFLATVVASVGAQSPSDSSQRLLLVLNKSDLLSPEGPGPGPDLPPHLLLSCLTGEGLDGLLEALRKELAAVCGDPSTDPPLLTRARHQHHLQGCLDALGHYKQSKDLALAAEALRVARGHLTRLTGGGGTEEILDIIFQDFCVGK