wanglab/gogpt-training-data huggingface dataset:
Protein: Pho81p (A0A1D8PRR1)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Interaction partners:
- Negative regulator of the PHO system
- Cyclin-dependent kinase 1
- Cyclin-dependent protein kinase-activating kinase
- Adenylate cyclase
- Serine/threonine-protein phosphatase SIT4
- Glycerophosphocholine phosphodiesterase GDE1
- Vacuolar transporter chaperone
- Acid phosphatase
- Phosphate transporter
- Vacuolar transporter chaperone complex subunit 4
Sequence:
MKFGKYLASRQLELPEYSGHFIDYKSLKKLIKQLAIPSTTATTTTSIDGEVTISNIQHTLKENKASFFFRVERELEKVNSFYLEKQANLAINLNLLLMKRDELFNKSNQYLKRHGSAGDDSSLSNADINFRNSISFLNLYQNFKKIHQDLLRLQQFIELNEIGFSKVVKKWDKRSKSHTKELFISTAVSVQPVFHKNEINELSDLVTQSLFDIESIMDGDYSSLSNYNASNSGVVSTTATTGTGNSSTPPAPNFNIPSVPGIGEDQAEEIFTRHSSIVSNQPNNNEIDELYTSFVNVATIKEPDLSLLARWVEKINNGGSKLPEQPFTPVVKYKISKIFLLSITNLKISDSFLELFLQFINYDVDFTFINDDFNNNKTILHQCCSIPTASSQSDPNNNNNSNNHHPHHVTINNGVKVINSTDLINHSRTFIVKYIVEKLQFPSVEEKTKLLVHKDFNGKTCLHYAAQMNRPDLLDLLLLSYPQSHIDELDNDSMSPLLLAIKHGHLNITKKLVRFGSNPFPTASKDTLQYLPINYACKFGDYKTLEYLLSNAKSQELIAKLINQQDVEGLLPLHVASRQGHYKLIKLLIQYGAQINKLDGFNKWTPIFYAAAEGHVKTTQELIKFGAKLNIIDEDGYNVLYYCVVEGHIDVINELLSYYQKAFSSSKLTSDSANSTNSTNSTSMSILGNDKDMDSGEEEEEGVSAITTTTTPTTATATADVDVSSLNENSSNNNNVDSIPDLQLPPPILPLRRYGHNFLEQKVLIELIFPSDQVFINLFNSTADLKPGRITITSNISDIVPRNILLPIKEDSYNNNSNSNNNCVFQTDVDSLCEFRIDFEIFPKFGTRLIAKTTALSFEHITGNSPEINTVSLPLFDLRLKNIGELKFSYQVIFPYSGTLLETSKFDTYWKSSTSFVKNRQTLKLNAAGGLSPNNFLSPGSVSTMPIPNNVNTINNTINNNNNINSSNGNGPAGGAGTNSTLIPSTQSIVTATSLSGEYLRIKVCLLSDGTPIVCPNWSISITDNIDLYLPNLTLKQLNSITNDLFDYPRIIHDLSRLTNKDIPLIKKLLQIIYLPLDLVLDILNIDINLNLEIVFPSIYELETLPFINNISNNLNQFIDNILSNVFNHIRSNKKRQRETLPTGNTPPNNNNNYRSIIFLSSNSLICKILNWKQPNFPVFLIMSGIAFNTKLNKFVKRSTNGLEIAPHVSQPHSQDNLLHSHSTSSSPSSASLELDDLTTRSIKEAVNFTINNNLIGLITSIHLLDLVPKLIPLIRSTGLILVASSDVINEDKDKQDDAILRKELDCYTKTEINGLRFDDVLSFKEDISM
Protein: GH05823p (Q86P89)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MNNLNANASAFLWQVPPPQQLTPQSVQQQTVQSVQSMQSVQHSQLLQSAVVSQPRKFGGNKSNYNYMQNHAIMGPGGGPMGGIGGNPNIYRKRHSINTYNAGLYQTNEPPLLGPGAAFPPFGAPEYHTTTPENWKGAAIHPTGLMKEPAGVVPGRNAPVAFTPQGQAQGAVMMVYGLDHDTSNTDKLFNLVCLYGNVARIKFLKTKEGTAMVQMGDAVAVERCVQHLNNIPVGTGGKIQIAFSKQNFLSEVINPFLLPDHSPSFKEYTGSKNNRFLSPAQASKNRIQPPSKILHFFNTPARLDRGPTDWNL
Protein: Plexin A, isoform B (Plexin A, isoform C) (Q0KIF1)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004251}; Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004251}.
Interaction partners:
Sequence:
MFNTKLTSVAATSTSGYTVVFVGTSDGFLKKVVIESSSIANEYASFAVDLGSEINRDMQFDNQNLYIYVMSKTKVSKVKVFDCSDYKTCGDCLGARDPYCGWCSLENKCSPRSNCQDDANDPLYWVSYKTGKCTTITSVVPHQLQRTTARTLELIIDHLPQLKENLICAFTTEDKALFTNATKKRNGVNCTTPRTDMLPQIEQGKHHFTAKLSVRTRNGPDLVSTDFTFFDCSTHSSCTRCVSSEFPCDWCVEAHRCTHDTAENCRNDILVTGVSRIGPSYRSGPGFCPTINATGDGSEVLVAGGTSKSIKVKVHIIGQFIVQTRFVCQFNIEGRVTSLNAQLLGDTIYCDSMEFQYTSRSPNLTATFAVIWGGSKPLDNPHNIHVVIYRCREMADSCGICLALSEKYNCGWCSSTNTCEVEEQCNKNKEGKTDWLNRSEICPNPEIHTFQPKTGPWEGGTNITIRGINLGKNYNDIYSGVRIAGINCMPFPQFYIDTKQIVCTVDSPGEQMYRNGKIVVQIGDYRGESKEDYEFVDPKILDFNPKFGPTSGGTEIHITGKHLNAGSRIQASINDHLPCKILSTDSSQAICRTSASPGIIEGRLKMSFDNGPREFNDYNFKYVLDPTVEHVSSGPSGQIKVPKGIPAGGIRISVTGTQFTSIQNPNIYVVYNGEMYASPCRVQSDTEMECASPVVDVDSHVIEAERPILLEYGFLMDNVLRVQNLSKVHNNHFELYPNPEYFIFEERVKYFKSEYLTINGRNLDRACKESDVEVKIGNGFCNITSLSRQQLTCRPPSEATATKSMNGPEVIVRIGTSLEYRIGILSYESSNIILDWGENVIFAVIATIVILLLIFVALLVAYKKKSSESSRVLRNMQEQMDILELRVAAECKEAFAELQTEMTDLTGDLTSGGIPFLDYRSYAMKILFPNHEDHIVLQWERPELLRKEKGLRIFGQLIMNKTFLLLFIRTLESNRYFSMRERVNVASLIMVTLQSKLEYCTDILKTLLGDLIEKCIEGKSHPKLLLRRTESVAEKMLSAWFTFLLYKFLKECAGEPLYMLFRAVKGQVDKGPVDACTHEARYSLSEEKLIRQSIDFRPMNVYASIIQQPIFCNNLDMLPSHTENVSVKVLDCDTIGQVKEKCLETIYRNIPSSQRPRKDDLDLEWRTGATGRVILYDEDVTSKTESEWKKLNTLQHYNVPDGAGLSLVPKQSSIYNFSILSDKNEKSHKYETLNISKYTSSSPTFSRAGSPLNNDMHENGLRYWHLVKHHDSDMQKEGERVNKLVSEIYLTRLLATKGTLQKFVDDLFETIFSTAHRGSALPLAIKYMFDFLDDQAQLHGITDPEVVHTWKSNSLPLRFWVNLIKNPNFVFDIHKSNIVDSCLSVVAQTFMDSCSTSDHRLGKDSPSSKLLYAKDIPEYRKWVDRYYRDIRDMSPISDQDMNAMLAEESRLHTTEFNTNCALHELYTYAVKYNEQLTVTLEEDEFSQKQRLAFKLEQVHNIMSSE
Protein: Starch-binding domain-containing protein 1 (Genethonin-1) (Glycophagy cargo receptor STBD1) (O95210)
Organism: Homo sapiens (Human)
Function: Acts as a cargo receptor for glycogen. Delivers its cargo to an autophagic pathway called glycophagy, resulting in the transport of glycogen to lysosomes.
Subcellular location: Preautophagosomal structure membrane {ECO:0000269|PubMed:20810658, ECO:0000305|PubMed:21893048}; Single-pass type III membrane protein {ECO:0000305|PubMed:9794794}. Endoplasmic reticulum membrane {ECO:0000269|PubMed:24837458}; Single-pass type III membrane protein {ECO:0000305|PubMed:9794794}. Cell membrane, sarcolemma, T-tubule {ECO:0000269|PubMed:9794794}. Note=Also detected near the junctional sarcoplasmic reticulum (PubMed:9794794). Concentrates at perinuclear structures (PubMed:21893048). {ECO:0000269|PubMed:21893048, ECO:0000269|PubMed:9794794}.
Interaction partners:
- GABA type A receptor associated protein like 1
- Glycogenin-1
- Laforin
- Protein phosphatase 1 regulatory subunit 3C
- Glycogen [starch] synthase, muscle
- Glycogen debranching enzyme
- 1,4-alpha-glucan-branching enzyme
- Glycogenin-2
- Protein phosphatase 1 regulatory subunit 3D
- Gamma-aminobutyric acid receptor-associated protein
Sequence:
MGAVWSALLVGGGLAGALFVWLLRGGPGDTGKDGDAEQEKDAPLGGAAIPGGHQSGSSGLSPGPSGQELVTKPEHLQESNGHLISKTKDLGKLQAASWRLQNPSREVCDNSREHVPSGQFPDTEAPATSETSNSRSYSEVSRNESLESPMGEWGFQKGQEISAKAATCFAEKLPSSNLLKNRAKEEMSLSDLNSQDRVDHEEWEMVPRHSSWGDVGVGGSLKAPVLNLNQGMDNGRSTLVEARGQQVHGKMERVAVMPAGSQQVSVRFQVHYVTSTDVQFIAVTGDHECLGRWNTYIPLHYNKDGFWSHSIFLPADTVVEWKFVLVENGGVTRWEECSNRFLETGHEDKVVHAWWGIH
Protein: PDZ and LIM domain protein 1 (C-terminal LIM domain protein 1) (Elfin) (LIM domain protein CLP-36) (O00151)
Organism: Homo sapiens (Human)
Function: Cytoskeletal protein that may act as an adapter that brings other proteins (like kinases) to the cytoskeleton. Involved in assembly, disassembly and directioning of stress fibers in fibroblasts. Required for the localization of ACTN1 and PALLD to stress fibers. Required for cell migration and in maintaining cell polarity of fibroblasts (By similarity).
Subcellular location: Cytoplasm {ECO:0000269|PubMed:10861853, ECO:0000269|PubMed:11110697}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:10861853, ECO:0000269|PubMed:11110697}. Cytoplasm, myofibril, sarcomere, Z line {ECO:0000269|PubMed:10861853}. Note=Associates with actin stress fibers. {ECO:0000269|PubMed:11110697}.
Interaction partners:
- Alpha-actinin-1
- Alpha-actinin-4
- Serine/threonine-protein kinase 35
- Alpha-actinin-2
- PDZ and LIM domain 5
- Estrogen receptor
- Vinculin
Sequence:
MTTQQIDLQGPGPWGFRLVGGKDFEQPLAISRVTPGSKAALANLCIGDVITAIDGENTSNMTHLEAQNRIKGCTDNLTLTVARSEHKVWSPLVTEEGKRHPYKMNLASEPQEVLHIGSAHNRSAMPFTASPASSTTARVITNQYNNPAGLYSSENISNFNNALESKTAASGVEANSRPLDHAQPPSSLVIDKESEVYKMLQEKQELNEPPKQSTSFLVLQEILESEEKGDPNKPSGFRSVKAPVTKVAASIGNAQKLPMCDKCGTGIVGVFVKLRDRHRHPECYVCTDCGTNLKQKGHFFVEDQIYCEKHARERVTPPEGYEVVTVFPK
Protein: Protein DETOXIFICATION 35 (AtDTX35) (Multidrug and toxic compound extrusion protein 35) (MATE protein 35) (Protein DETOXIFYING EFFLUX CARRIER 35) (Protein DTX5) (Protein FLOWER FLAVONOID TRANSPORTER) (Protein FFT) (F4JTB3)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Multidrug and toxin efflux transporter involved in flavonoid metabolism. Required for proper reproductive development.
Subcellular location: Vacuole membrane {ECO:0000269|PubMed:17151019}; Multi-pass membrane protein {ECO:0000269|PubMed:17151019}.
Interaction partners:
- Protein DETOXIFICATION 43
- Protein DETOXIFICATION 42
- Subtilisin-like protease SBT3.1
- Peptide transporter family protein
- Uncharacterized protein At5g19190
- At5g43870)
- Tagatose-6-phosphate ketose/aldose isomerase, putative
Sequence:
MDPTAPLLTHGGEVEEDYAPARSWTDVKRVLSTESAKLWMIAAPVGFNIICQYGVSSVTNIFVGHIGEVELSAVSISLSVIGTFSFGFLLGMGSALETLCGQAYGAGQVNMLGVYMQRSWIILFVSCFFLLPIYIFATPVLRLLGQAEEIAVPAGQFTLLTIPQLFSLAFNFPTSKFLQAQSKVVAIAWIGFVALSLHVIMLWLFIIEFGWGTNGAALAFNITNWGTAIAQIVYVIGWCNEGWTGLSWLAFKEIWAFVRLSIASAVMLCLEIWYMMSIIVLTGRLDNAVIAVDSLSICMNINGLEAMLFIGINAAISVRVSNELGLGRPRAAKYSVYVTVFQSLLIGLVFMVAIIIARDHFAIIFTSSKVLQRAVSKLAYLLGITMVLNSVQPVVSGVAVGGGWQGLVAYINLGCYYIFGLPFGYLLGYIANFGVMGLWSGMIAGTALQTLLLLIVLYKTNWNKEVEETMERMKKWGGSETTSKDILA
Protein: Neuroligin-1 (Q9XTG1)
Organism: Caenorhabditis elegans
Function: Probable neuronal cell surface protein thought to be involved in cell-cell-interactions by forming intercellular junctions through binding to beta-neurexins (By similarity). Plays a role in the clustering of the GABA(A) receptor unc-49 at postsynaptic sites in neuromuscular junctions (NMJs) via the interaction with madd-4 and neurexin nrx-1 and is thereby required for normal GABAergic synaptic transmission.
Subcellular location: Cell membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. Synapse {ECO:0000269|PubMed:26028574, ECO:0000269|PubMed:26028575}. Note=Localizes specifically to GABAergic synapses. {ECO:0000269|PubMed:26028574, ECO:0000269|PubMed:26028575}.
Interaction partners:
- Neurexin-3-beta
- Neuroligin-like protein glit-1
- Protein madd-4
- MoaB/Mog domain-containing protein
- Neuronal immunoglobulin domain-containing protein rig-3
- Moesin/ezrin/radixin homolog 1
- Protein lin-2
Sequence:
MERIYLLLLLFLPRIRSYDVRSVTTSWGMVRGEVVSPEGDDLPPVAQYLGIPYGVAPTGQYRFNMAISAAKWTHMPKDARKVSPVCIQTDMPELSETKAFKHTSAQRFDFNHRLLPHLKKQSEDCLYMNIYVPERLEISRDNYLPVMVIVHGEEYGWGTGNAFNGTTLAAYGHIIVVTLNYRLGVFGFLGRCESSSCSGNSGISDLVSALTMLNVILPSFGGDSKSVTLAGWGSGASLVSLLMASPLTQPGRRLFRRAILLDGSALSPWAISQNPQQYFMQLAEELACAPKNRTSSFNDNVDTIVRCMQVHSSENITKAVLKIDVPTFLSGFAPIVDGQLIPNKPQVSFSTQYGSLFREIDLLVGISSNPSHHMISNEDLKVGISKEKRMRIFRSLVRNLYDFHREEILASIINEYTDWENPRDHPKSIRNGVLNALSDVLYTAPLIETLRSHSADEVRKEANTFMFAFAHETRSWSQEQPNSGIRGSLSGDIVPYIFGYPLAQGDSEERLYSGFNTDDKGISKVMMHYVSNFVKSGDPSKPNPMSKNFPMGDVFHSTAWPQFDQPNREAYLEITDRPRVKNYYRNAQVGFWNNFIPQLHKNGKETEPVGEEHHLLSDHFRKDSYFGKTRHFSSYANLPFPPPPMPPSPPPELTTKPKPSESPTTLQTTTESEKAAAGSFTGKALGGVIFIGCGFLIMNVCLLIAVRREWGKKRRNEKKFQLQYQTYNSNHGGGAEQYNSLNSPEPLLSASHKNSTSMRPAGISPTCPRHGRAALALQNSRGNSLTAAQAPTLEEIQV
Protein: COP9 signalosome complex subunit 4 (SGN4) (Signalosome subunit 4) (JAB1-containing signalosome subunit 4) (O88544)
Organism: Mus musculus (Mouse)
Function: Component of the COP9 signalosome complex (CSN), a complex involved in various cellular and developmental processes (By similarity). The CSN complex is an essential regulator of the ubiquitin (Ubl) conjugation pathway by mediating the deneddylation of the cullin subunits of SCF-type E3 ligase complexes, leading to decrease the Ubl ligase activity of SCF-type complexes such as SCF, CSA or DDB2 (By similarity). Also involved in the deneddylation of non-cullin subunits such as STON2 (By similarity). The complex is also involved in phosphorylation of p53/TP53, c-jun/JUN, IkappaBalpha/NFKBIA, ITPK1, IRF8/ICSBP and SNAPIN, possibly via its association with CK2 and PKD kinases (By similarity). CSN-dependent phosphorylation of TP53 and JUN promotes and protects degradation by the Ubl system, respectively (By similarity).
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:Q9BT78}. Nucleus {ECO:0000250|UniProtKB:Q9BT78}. Cytoplasmic vesicle, secretory vesicle, synaptic vesicle {ECO:0000250|UniProtKB:Q9BT78}.
Interaction partners:
- COP9 signalosome complex subunit 8
- COP9 signalosome complex subunit 3
- COP9 signalosome complex subunit 1
- COP9 signalosome complex subunit 2
- COP9 signalosome complex subunit 6
- COP9 signalosome complex subunit 5
- COP9 signalosome complex subunit 7b
- COP9 signalosome complex subunit 7a
- E3 ubiquitin-protein ligase RBX1
- Ubiquitin-like protein NEDD8
Sequence:
MAAAVRQDLAQLMNSSGSHKDLAGKYRQILEKAIQLSGTEQLEALKAFVEAMVNENVSLVISRQLLTDFCTHLPNLPDSTAKEVYHFTLEKIQPRVISFEEQVASIRQHLASIYEKEEDWRNAAQVLVGIPLETGQKQYNVDYKLETYLKIARLYLEDDDPVQAEAYINRASLLQNESTNEQLQIHYKVCYARVLDYRRKFIEAAQRYNELSYKTIVHESERLEALKHALHCTILASAGQQRSRMLATLFKDERCQQLAAYGILEKMYLDRIIRGNQLQEFAAMLMPHQKATTADGSSILDRAVIEHNLLSASKLYNNITFEELGALLEIPAAKAEKIASQMITEGRMNGFIDQIDGIVHFETREALPTWDKQIQSLCFQVNNLLEKISQTAPEWTAQAMEAQMAQ
Protein: Aldo-keto reductase family 1 member C15 (EC 1.1.1.-) (EC 1.1.1.216) (RAKc) (D3ZF77)
Organism: Rattus norvegicus (Rat)
Function: Catalyzes the NADPH-dependent reduction of a variety of substrates including aromatic and aliphatic aldehydes, quinones, ketones, dicarbonyl compounds and 17-ketosteroids. Catalyzes the NADP(+)-dependent oxidation of aromatic, alicyclic and aliphatic alcohols, and 17beta-hydroxysteroids. To a lesser extent, can also catalyze the reduction of some aldoses and ketoses and the oxidation of some sugar alcohols. In the stomach, lung and colon tissues, mediates the reduction of farnesal and geranylgeranial into farnesol and geranylgeraniol respectively. By reducing 4-hydroxy-2-nonenal (HNE), produced during lipid peroxidation, into 1,4-dihydro-2-nonene (DHN), protects vascular endothelial cells from damage elicited by oxidized lipoproteins.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:17574202, ECO:0000269|PubMed:21187079}.
Interaction partners:
- 17-beta-hydroxysteroid dehydrogenase type 3
- Aromatase
- Steryl-sulfatase
- Steroid 17-alpha-hydroxylase/17,20 lyase
- 3 beta-hydroxysteroid dehydrogenase/Delta 5-->4-isomerase type 4
- Cytochrome P450 11B3, mitochondrial
- Carbonyl reductase
- NADPH-dependent 3-keto-steroid reductase Hsd3b5
- Carbonyl reductase 1])
- 3-oxo-5-alpha-steroid 4-dehydrogenase 1
Sequence:
MDLKHSRSVKLNDGNLMPVLGFGTFASKEIPKSKAAEATKVAIDVGFRHIDAAYFYQNEEEVGQALRDKMADGTVKREDLFYTTKIWITFLRPELVRQCLERSLKKLGLDYVDLCIIHIPIAMKPGEELLPKDANGKFIFDTVDIRDTWEALEKCKDAGLSKSIGVSNFNHKQLELILNKPRLKYKPTCNQVECHPYLNQSKLLEFCKSKDIVLVAYSALGSHRDSSWVSSDSPYLLEDPVLMTIAKKHNQTPGQVALRYQLQRGVVVLAKSFNEKRIKENFQVFDFELTPEDMKTIDSLNRNFRYSQMAFALDHPDYPFLEEY
Protein: Actin (Q95ZL1)
Organism: Caenorhabditis elegans
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
Interaction partners:
Sequence:
MVGMGQKDSYVGDEAQSKRGILTLKYPIEHGIVTNWDDMEKIWHHTFYNELRVAPEEHPVLLTEAPLNPKANREKMTQIMFETFNTPAMYVAIQAVLSLYASGRTTGVVLDSGDGVTHTVPIYEGYALPHAILRLDLAGRDLTDYLMKILTERGYSFTTTAEREIVRDIKEKLCYVALDFEQEMATAASSSSLEKSYELPDGQVITVGNERFRCPEALFQPSFLGMESAGIHETSYNSIMKCDIDIRKDLYANTVLSGGTTMYPGIADRMQKEITALAPSTMKIKIIAPPERKYSVWIGGSILASLSTFQQMWISKQEYDESGPSIVHRKCF
Protein: Serine/threonine-protein kinase TOUSLED (EC 2.7.11.1) (Q39238)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Required for correct initiation of floral organ primordia and for proper development of organ primordia. Phosphorylates in vitro ASF1B/SGA1, the C-terminal part of TKI1 and histone H3.
Subcellular location: Nucleus {ECO:0000269|PubMed:9038200}.
Interaction partners:
- Histone chaperone ASF1B
- Probable histone chaperone ASF1A
- TSL-kinase interacting protein 1
- Cell cycle checkpoint control protein family
- Checkpoint protein
- Histone H3-like 2
- Histone H3-like 4
- Histone H3-like 1
- Histone H3-like 3
- Histone H3.3
Sequence:
MSDDMVLHFSSNSSNQSDHSLPDKIAKLEARLTGKTPSSAKPPQQQQQQQQQVSLWSSASAAVKVVTSTPPGLSETSISDSDDENTGDFLIRANTKKRQKVQESNNFSVVDHVEPQEAAYDGRKNDAESKTGLDVSKKKQGRGRASSTGRGRGSKTNNDVTKSQFVVAPVSAASQLDASDQKDFRPDGQLRNGECSLQDEDLKSLRAKIAMLEEELRKSRQDSSEYHHLVRNLENEVKDLKDQEQQGKQKTTKVISDLLISVSKTERQEARTKVRNESLRLGSVGVLRTGTIIAETWEDGQMLKDLNAQLRQLLETKEAIERQRKLLKKRQNGDKNDGTDTESGAQEEDIIPDEVYKSRLTSIKREEEAVLRERERYTLEKGLLMREMKRIRDEDGSRFNHFPVLNSRYALLNLLGKGGFSEVYKAYDLVDHRYVACKLHGLNAQWSEEKKQSYIRHANRECEIHKSLVHHHIVRLWDKFHIDMHTFCTVLEYCSGKDLDAVLKATSNLPEKEARIIIVQIVQGLVYLNKKSQKIIHYDLKPGNVLFDEFGVAKVTDFGLSKIVEDNVGSQGMELTSQGAGTYWYLPPECFELNKTPMISSKVDVWSVGVLFYQMLFGKRPFGHDQSQERILREDTIIKAKKVEFPVTRPAISNEAKDLIRRCLTYNQEDRPDVLTMAQDPYLAYSKK
Protein: PAC-1 interacting and coiled-coil domain-containing protein 1 (H2KYP0)
Organism: Caenorhabditis elegans
Function: Linker protein which helps to recruit the Rho GTPase-activating protein, pac-1, to adherens junctions.
Subcellular location: Cell junction, adherens junction {ECO:0000269|PubMed:25938815}.
Interaction partners:
- GTPase-activating protein pac-1
- Juxtamembrane domain-associated catenin
- Alpha/beta hydrolase fold-3 domain-containing protein
Sequence:
MIITTPRRANMSSESGSSASTVHYAKPVLRHVPMPSSTTPSSIGSSSSSSSSYASSTKQTPPRSPVIRYPTVVVSKNSIATPSSSLTPQGTPSYAVPVSRNQMQYSASKLQYEHMRHRCKMLDDENQKLMRMQSDVVNDANRRVQMHVNEIRMLKEDNRKLAISNKELRDLSCFLDDDRQKTRKLAREWQKFGRYTSSLMKQEVDSYHQKMVSIEEKLCTKEREVDELRQLCMYLDEQRQSLMSNAAANVDCDNESEDLGCGSSEQSGGSEGHNDEEKHHEFNKCFNKHKESTLRRIMATSMCSEPSEEEERREVSKRERSRLLGYIQSLENRIKHLEMSQNHESFWNSSSNVGSDCDEKTIIERGWLGEEVMSNSEDCHLELKPVMTTSSTSSSHIFGNDKCPMFDSMTSNMTSSGCTTYASSGTDGDSVFVIGDEIDIGNLEVRTLSRIDEEATSASDTLKESARMPPKIAPPICSSLVLTNFDNMSEDCAPRLMRSASETCRPTTTLISSTQPAQRSVSVEKNNNNNVHTHN
Protein: Candida glabrata strain CBS138 chromosome E complete sequence (Q6FV31)
Organism: Candida glabrata (strain ATCC 2001 / BCRC 20586 / JCM 3761 / NBRC 0622 / NRRL Y-65 / CBS 138) (Yeast) (Nakaseomyces glabratus)
Interaction partners:
- Candida glabrata strain CBS138 chromosome F complete sequence
- Candida glabrata strain CBS138 chromosome M complete sequence
- RP41
- 40S ribosomal protein S7
- 40S ribosomal protein S4
- Small ribosomal subunit protein uS3
- Small ribosomal subunit protein eS1
- Small ribosomal subunit protein eS25
- 40S ribosomal protein S8
- Small ribosomal subunit protein uS14
Sequence:
MASDNSNTTVFVSGATGFIAQHVVRQLLDQNYKVIGSVRSAEKGDHLKNVIFKGGDFNYEIVKDISDPTAFDHVFEKHGKDIKVVLHTASPFHFNTTDIEKDLLIPAVNGTKGILESIKKYAAQTVERVVVTSSFAANTSTVDMFYAKDSSKTITEESWNQDTWESCQSDPIRGYCGSKKFAEKAAWDFYNANKDSVKFKLSIINPVYVFGPQNYVEPGKKILNTSSEVINSLVHLKKDDPLPEFAGGHIDVRDVAKAHILAFQKDELIEQRLMLHAGLFTTQTLLDIINEQFPELKGKIPAGKPGTGNPDDALTPVDNSKTKKLLGFEFIDLKKDLYDTISQILEAEKNSN
Protein: Potassium/chloride cotransporter 3 (Q09573)
Organism: Caenorhabditis elegans
Function: Probable potassium/chloride cotransporter that functions in the amphid sheath glial cells to regulate thermotaxis behavior. By maintaining chloride homeostasis, negatively regulates guanylate cyclase gcy-8 in the thermosensory AFD neurons and thereby controls the microvilli receptive ending morphology of the AFD neurons and thermotaxis. Modulates the temperature-evoked neuronal activity of the AFD neurons such as calcium responses to temperature gradients. Might also play a role in the chemotaxis behavior mediated by the sensory neurons AWA and AWC.
Subcellular location: Cell membrane {ECO:0000305|PubMed:27062922}; Multi-pass membrane protein {ECO:0000305}. Note=Localizes to the amphid sheath glia apical domain in which the AFD microvilli are embedded. {ECO:0000269|PubMed:27062922}.
Interaction partners:
- Receptor-type guanylate cyclase gcy-8
Sequence:
MSNARRRFSTVTQINTEGLQAMGKGGGRMETVGEDGIPADYKGNRKFTTSLGHLALYKEDEGIGTQASFISGYTTPGPKERATSEHVKANLGVMLGVYLPTIQHILGVTMFIRLFWVVGMSGVAWTMALLAICCLSTLLTSISLSAVATNGVVESGGAYFIISRNLGAEFGSAVGILFYLANTVAASMYIVGGVEVILMYLWPEMAIGGADALHDTEMFGSLYNNLRLYGTVFLLIQALIVAMGVKFVQLLAPVSLMCVILAIAACIGGGIEKQITMEGMKVCAIDNHLLQSSIVTHPIHKNQTSWFNETVDFCNLCDKSLYLESVFCANVNNDEASAEDDVFCTHYTSKKMTCQLAFPGFNMKTLNDNMWPEYMEKSEVVPGVRGKETAEVVQDESSTFFMLMAIYFPAVTGIFTGTNMSGDLRDPQRSIPVGTIAATLTTSAIYYILAILFGGSITRSVLRDKFGRSIGNTMVVAALSWPHPAVVTVGAFLSTFGAALQCLCSAPRLLQSIAKDDVIPILAPFARVTKNNEPFLGLVLTVIIAECGILLGAVDKIAEVLDFFFLMCYAFVNLIAVLHSVLKSPNWRPRFKYFHWTLSLLGAALCFFIMFASSVPLACIACTATAVIYKYVEWKGAKKEWGDGMRGLALTTAQYSLLKVEDKDPHPKNWRPQVLILLTSQWSKEMIDRRAVSMLNLGAQLKAGRGLAIACAFLKGSVDSQKDKNRARDVKTTLVKDMSSVRLRGFAKTMFYNNHQINGTISGLYQSIGIGGLRPNTILLNWPNEKNPDELVLFAEEIIHGAANDNCLIVTKGITDFPEYSERLTGFIDIWWIVQDGGILMLIAYLLRQHKVWKGCTLRIFAVSEQDSTKSEDMKAGLQKYIYMLRIDAELFIVDLLDMEVSDEVVEKAAEVERKQKEREEMRRSKSGYLNDGFMEDNGKPRQVMMRHSDSARSFSPQPGAHTSINLDETETSFTESLFDDFYRSGTPNEDLEGAMKLNIHKMNTSVRLNRVIRENSPDSQLILLNLPSPPRNRLAFNNSYMTYLDVLTEDLPRVLFIGGSGREVITIDS
Protein: Ubiquitin-ribosomal protein eS31 fusion protein [Cleaved into: Ubiquitin; Small ribosomal subunit protein eS31 (40S ribosomal protein S27a)] (P15357)
Organism: Drosophila melanogaster (Fruit fly)
Function: Ubiquitin exists either covalently attached to another protein, or free (unanchored). When covalently bound, it is conjugated to target proteins via an isopeptide bond either as a monomer (monoubiquitin), a polymer linked via different Lys residues of the ubiquitin (polyubiquitin chains) or a linear polymer linked via the initiator Met of the ubiquitin (linear polyubiquitin chains). Polyubiquitin chains, when attached to a target protein, have different functions depending on the Lys residue of the ubiquitin that is linked: Lys-48-linked is involved in protein degradation via the proteasome. Linear polymer chains formed via attachment by the initiator Met lead to cell signaling. Ubiquitin is usually conjugated to Lys residues of target proteins, however, in rare cases, conjugation to Cys or Ser residues has been observed. When polyubiquitin is free (unanchored-polyubiquitin), it also has distinct roles, such as in activation of protein kinases, and in signaling (By similarity).
Subcellular location: [Ubiquitin]: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.; SUBCELLULAR LOCATION: [Small ribosomal subunit protein eS31]: Nucleus, nucleolus {ECO:0000250|UniProtKB:P62979}.
Interaction partners:
- Large ribosomal subunit protein eL21
- Small ribosomal subunit protein uS17
- Large ribosomal subunit protein uL6
- Small ribosomal subunit protein eS10A
- Large ribosomal subunit protein uL13
- Large ribosomal subunit protein uL11
- 40S ribosomal protein S27
- Small ribosomal subunit protein uS14
- 60S ribosomal protein L27
- Large ribosomal subunit protein uL22
Sequence:
MQIFVKTLTGKTITLEVEPSDTIENVKAKIQDKEGIPPDQQRLIFAGKQLEDGRTLSDYNIQKESTLHLVLRLRGGAKKRKKKNYSTPKKIKHKRKKVKLAVLKYYKVDENGKIHRLRRECPGENCGAGVFMAAHEDRHYCGKCNLTFVFSKPEEK
Protein: Small toxic protein ShoB (C1P611)
Organism: Escherichia coli (strain K12)
Function: Toxic component of a type I toxin-antitoxin (TA) system. May be a toxic protein; overexpression causes cessation of growth and rapid membrane depolarization. Overexpression induces stress-response and a number of membrane protein genes.
Subcellular location: Membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}.
Interaction partners:
- Small toxic protein TisB
- Uncharacterized protein DinQ
- Small toxic polypeptide LdrD
- Toxic protein SymE
- Ribosome association toxin RatA
- Endodeoxyribonuclease toxin RalR
- Ferredoxin YfhL
Sequence:
MTDCRYLIKRVIKIIIAVLQLILLFL
Protein: leucine--tRNA ligase (EC 6.1.1.4) (Leucyl-tRNA synthetase) (A0A6I8PIT3)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MAERKGTAKVDFLKKIEKEIQQKWDTERVFEVNASNLEKQTSKGKYFVTFPYPYMNGRLHLGHTFSLSKCEFAVGYQRLKGKCCLFPFGLHCTGMPIKACADKLKREIELYGCPPDFPDEEEEEEETSVKTEDIIIKDKAKGKKSKAAAKAGSSKYQWGIMKSLGLSDEEIVKFSEAEHWLDYFPPLAIQDLKRMGLKVDWRRSFITTDVNPYYDSFVRWQFLTLRERNKIKFGKRYTIYSPKDGQPCMDHDRQTGEGVGPQEYTLLKLKVLEPYPSKLSGLKGKNIFLVAATLRPETMFGQTNCWVRPDMKYIGFETVNGDIFICTQKAARNMSYQGFTKDNGVVPVVKELMGEEILGASLSAPLTSYKVIYVLPMLTIKEDKGTGVVTSVPSDSPDDIAALRDLKKKQALRAKYGIRDDMVLPFEPVPVIEIPGFGNLSAVTICDELKIQSQNDREKLAEAKEKIYLKGFYEGIMLVDGFKGQKVQDGDALIYMEPEKQVMSRSSDECVVALCDQWYLDYGEENWKKQTSQCLKNLETFCEETRRNFEATLGWLQEHACSRTYGLGTHLPWDEQWLIESLSDSTIYMAFYTVAHLLQGGNLHGQAESPLGIRPQQMTKEVWDYVFFKEAPFPKTQIAKEKLDQLKQEFEFWYPVDLRVSGKDLVPNHLSYYLYNHVAMWPEQSDKWPTAVRANGHLLLNSEKMSKSTGNFLTLTQAIDKFSADGMRLALADAGDTVEDANFVEAMADAGILRLYTWVEWVKEMVANWDSLRSGPASTFNDRVFASELNAGIIKTDQNYEKMMFKEALKTGFFEFQAAKDKYRELAVEGMHRELVFRFIEVQTLLLAPFCPHLCEHIWTLLGKPDSIMNASWPVAGPVNEVLIHSSQYLMEVTHDLRLRLKNYMMPAKGKKTDKQPLQKPSHCTIYVAKNYPPWQHTTLSVLRKHFEANNGKLPDNKVIASELGSMPELKKYMKKVMPFVAMIKENLEKMGPRILDLQLEFDEKAVLMENIVYLTNSLELEHIEVKFASEAEDKIREDCCPGKPLNVFRIEPGVSVSLVNPQPSNGHFSTKIEIRQGDNCDSIIRRLMKMNRGIKDLSKVKLMRFDDPLLGPRRVPVLGKEYTEKTPISEHAVFNVDLMSKKIHLTENGIRVDIGDTIIYLVH