wanglab/gogpt-training-data huggingface dataset:
Protein: PRKCA-binding protein (Protein interacting with C kinase 1) (Protein kinase C-alpha-binding protein) (Q80VC8)
Organism: Mus musculus (Mouse)
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000256|ARBA:ARBA00004245}. Cytoplasm, perinuclear region {ECO:0000256|ARBA:ARBA00004556}. Membrane {ECO:0000256|ARBA:ARBA00004635}; Lipid-anchor {ECO:0000256|ARBA:ARBA00004635}. Membrane {ECO:0000256|ARBA:ARBA00004170}; Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004170}. Postsynaptic density {ECO:0000256|ARBA:ARBA00034105}. Synapse, synaptosome {ECO:0000256|ARBA:ARBA00034102}.
Interaction partners:
Sequence:
MFADLDYDIEEDKLGIPTVPGKVTLQKDAQNLIGISIGGGAQYCPCLYIVQVFDNTPAALDGTVAAGDEITGVNGKSIKGKTKVEVAKMIQEVKGEVTIHYNKLQADPKQGMSLDIVLKKVKHRLVENMSSGTADALGLSRAILCNDGLVKRLEELERTAELYKGMTEHTKNLLRAFYELSQTHRAFGDVFSVIGVREPQPAASEAFVKFADAHRSIEKFGIRLLKTIKPMLTDLNTYLNKAIPDTRLTIKKYLDVKFEYLSYCLKVKEMDDEEYSCIALGEPLYRVSTGNYEYRLILRCRQEARARFSQMRKDVLEKMELLDQKHVQDIVFQLQRFVSTMSKYYNDCYAVLRDADVFPIEVDLAHTTLAYGPNQGSFTDGEEEDEEEEDGAAREVSKDACGATGPTDKGGSWCDS
Protein: Large ribosomal subunit protein mL38 (39S ribosomal protein L38, mitochondrial) (Q9VY48)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Mitochondrion {ECO:0000256|ARBA:ARBA00004173}.
Interaction partners:
- Large ribosomal subunit protein mL40
- Large ribosomal subunit protein uL30m
- Large ribosomal subunit protein mL52
- Large ribosomal subunit protein uL3m
- Large ribosomal subunit protein bL19m
- Large ribosomal subunit protein uL4m
- GH05406p
- LD24471p
- Large ribosomal subunit protein uL10m
- Large ribosomal subunit protein uL18m
Sequence:
MSFSNLLMKSGLTVAVRDAQAAVLMTATRQGHTIRGKPPGVARSLEQRIREENVEDPEVVARINIGFPQLKESRSAQLKKRLEHLKSQRSDKQLEQLARSNKLIIDLDKVQRTYVKTTGQHDLRLVADHYGIFEHLFGSAYFVPRVPLNISYQLDGDSLAPVYNGNVIKPTEAAKAPQIDFDGLVDPITGQAAGQDTYWTLVASNPDAHYTNGTAECLHWFIANIPNGKVSEGQVLAEYLPPFPPRGVGYQRMVFVLYKQQARLDLGSYQLAAADYGNLEKRTFSTLDFYRQHQEQLTPAGLAFYQTNWDESLTQFYHDVLKIKEPVYEYDFPKPYLTDQKFFPLKQPFNLYMDKHRDQKQVNKEYLERKLAKTHPFEGPKKPLRYPNAHPIRDVPSWLRTEIRKERLGTGRVQDY
Protein: FLYWCH transcription factor 1 (Q9XWR1)
Organism: Caenorhabditis elegans
Function: Probable transcription factor. Binds to the DNA sequence motif 5'-[AG]GGCGCCG-3' in the promoters of target genes, including micro-RNA genes, in order to repress expression, and acting redundantly with flh-2.
Interaction partners:
- Alpha-soluble NSF attachment protein
- RRM domain-containing protein
- HMG box domain-containing protein
- UBR-type domain-containing protein
- Nuclear hormone receptor family member nhr-111
- BTB and MATH domain-containing protein 42
- FLYWCH transcription factor 3
- REPS homolog
- Syntaxin-1A homolog
Sequence:
MYSPESMNSNISSPSPPSSSSLNAPSLADAPEVRSDDGEAETSEPSTSVTAVPMEIVSQASTSAPVNQLLASGIDMSSVIKNNAVLQALLASASAGGFGDNAGLTMSKLLTAALANGSTAVAKRDAGSPRTDIPKKTRLKVFSNGFFMTFDKLSSCQKKYFWRCEYKNTCKARMHTDIVTEKILTFIHEHNHSAPIDEEVRLYGLDPTNIERNRVYIVGNVADPNQRRKIRKQVADREAAAKRLVQQQEEEQQKQQSASSIVAARAAYAQAMQNGSIPTSSGVASFLQSTSATAPMTSHSMLLAQMPFLNNIKTEMSNMVKNEQFTPERYTQHMSPNLPLQTATIAPLIIPTENYDSPSYRQPAIKRKATDLTNEEHDLRRDPMFQPTFELARKLRKLWKGEPNRYPRTTTTPTHHFEFFLSKNDGTDEHLYVPMRINLRDEAHLKEALQDFCGQQCIGMLLFGISPKISVMFNQPMLNNWDNNQFFLLDISNPSRWRLMYVDDQAV
Protein: Spore wall structural constituent isp3 (Meiotic expression up-regulated protein 4) (Sexual differentiation process protein isp3) (P40899)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Forms fibrillar structures on the spore surface that contribute to spore wall integrity.
Subcellular location: Spore coat {ECO:0000269|PubMed:24623719, ECO:0000269|PubMed:33375328}. Cytoplasm {ECO:0000269|PubMed:24623719}.
Interaction partners:
- Ras modification protein erf4
- Zinc-type alcohol dehydrogenase-like protein C16A3.02c
- Zinc metalloprotease mde10
- Putative pyridoxal kinase C6F6.11c
- Palmitoyltransferase erf2
- Uncharacterized protein P19A11.02c
- Sexual differentiation process protein isp4
- Meiotic coiled-coil protein 4
Sequence:
MGLGNLCSYKQDDSLDILQKKVLIDAFNKVTIDGKPNVQHQQPTYWYPPPPPRHHKEHKKSHHHWEYSSDDDSSDDEESCEKKKPKCCEKKKPKCCESEQNNGCGRRNQLARRLAFLGSFGDGDCDGCNEAFTVTGPITYFRTCPDPLTGITPAVAAAAATPAAAATPATPAAAATPAAPAA
Protein: Vesicle-fusing ATPase (EC 3.6.4.6) (B7Z5J7)
Organism: Homo sapiens (Human)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496, ECO:0000256|RuleBase:RU367045}.
Interaction partners:
Sequence:
MQAARCPTDELSLTNCAVVNEKDFQSGQHVIVRTSPNHRYTFTLKTHPSVVPGSIAFSLPQRKWAGLSIGQEIEVSLYTFDKAKQCIGTMTIEIDFLQKKSIDSNPYDTDKMAAEFIQQFNNQALSVGQQLVFSFNEKLFGLLVKDIEAMDPSILKGEPATGKRQKIEVGLVVGNSQVAFEKAENSSLNLIGKAKTKENRQSIINPDWNFEKMGIGGLDKEFSDIFRRAFASRVFPPEIVEQMGCKHVKGILLYGPPGCGKTLLARQIGKMLNAREPKVVNGPEILNKYVGESEANIRKLFADAEEEQRRLGANSGLHIIIFDEIDAICKQRGSMAGSTGVHDTVVNQLLSKIDGVEQLNNILVIGMTNRPDLIDEALLRPGRLEVKMEIGLPDEKGRLQILHIHTARMRGHQLLSADVDIKELAVETKNFSGAELEGLVRAAQSTAMNRHIKASTKVEVDMEKAESLQVTRGDFLASLENDIKPAFGTNQEDYASYIMNGIIKWGDPVTRVLDDGELLVQQTKNSDRTPLVSVLLEGPPHSGKTALAAKIAEESNFPFIKICSPDKMIGFSETAKCQAMKKIFDDAYKSQLSCVVVDDIERLLDYVPIGPRFSNLVLQALLVLLKKAPPQGRKLLIIGTTSRKDVLQEMEMLNAFSTTIHVPNIATGEQLLEALELLGNFKDKERTTIAQQVKGKKVWIGIKKLLMLIEMSLQMDPEYRVRKFLALLREEGASPLDFD
Protein: Serine/threonine-protein phosphatase (EC 3.1.3.16) (Q6FKJ3)
Organism: Candida glabrata (strain ATCC 2001 / BCRC 20586 / JCM 3761 / NBRC 0622 / NRRL Y-65 / CBS 138) (Yeast) (Nakaseomyces glabratus)
Interaction partners:
- Calcineurin subunit B
- FK506-binding protein 1
- Candida glabrata strain CBS138 chromosome E complete sequence
- Calmodulin
- Candida glabrata strain CBS138 chromosome G complete sequence
- Calcium-binding protein NCS-1
- Candida glabrata strain CBS138 chromosome M complete sequence
- Candida glabrata strain CBS138 chromosome F complete sequence
- Coatomer subunit epsilon
- Protein phosphatase PP2A regulatory subunit B
Sequence:
MPDKTDAELNTEKINAALKVIESKKHEGDTAQSAVPDLTVYTMEDGTQVNTKERVMKSVTPINGHIPSDEEVFDRKTGLPNHQFLRDHFKGEGRITEDQALKILSMATECMKKEPNLLTVPAPVTVCGDIHGQYFDLLKLFEIGGDPETTPYLFLGDYVDRGSFSFECLIYLYALKLNYNAHFWMLRGNHECMHLTSYFTFKNECLHKYSLKIYEACCESFNALPLAALMNEQYFCVHGGISPDLKTPEDVNKINRFREIPSRGLMCDLVWADPIEKYDEVADDLTQGKFVINQVRGCSFAFTYQASCEFLQRSGLLSIIRAHEAQDAGYRMYKNTKTLGFPSLLTLFSAPNYLDTYNNKAAILKYENNVMNIRQFNMSPHPYWLPDFMDVFTWSLPFVGEKVTEMLVAILNICTEDELEEDTPYIAGEVGKIDSTHSATTSTTSPQASATVSADAIASATSEGHQHTSSILDDEHRRKTLRNKILAIAKVSRMYSVLREESDKVQYLKSMNSGILPRGALAHGSQGLNETLSTFERARKQDLINEKLPPSLDEVKKKKQEYYHSILRQAQSDHR
Protein: LisH domain-containing protein C1711.05 (Q9P785)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Subcellular location: Nucleus, nucleolus {ECO:0000269|PubMed:16823372}.
Interaction partners:
- Nucleolar protein 56
- Nucleolar protein 58
- H/ACA ribonucleoprotein complex subunit cbf5
- rRNA 2'-O-methyltransferase fibrillarin
- Uncharacterized RNA-binding protein C126.11c
- Putative splicing factor C222.18
- 25S rRNA
- GTPase grn1
- Probable DNA-directed RNA polymerase I subunit RPA2
- DNA-directed RNA polymerase I subunit rpa1
Sequence:
MGEISMKSKVCPLIYHFLQENGYVKTAQTFLKETGDKDLAKGKVKKNLLDLLSQKEFLPYLTTEDVGKHKKTKESLEKSNDDSQKISKKGAPPEKAHSSSEASGSGSSSDESDSSSSESESSSEDNDSSSSSSDSESESSSEDSDSSSSSSDSESESSSEGSDSSSSSSSSESESSSEDNDSSSSSSDSESESSSEDSDSSSSSSDSESESSSEGSDSSSSSSSSESESSSEDNDSSSSSSDSESESSSEDSDSSSSSSDSESESSSKDSDSSSNSSDSEDDSSSDSSDSESESSSEDSDSTSSSSDSDSSSSSEDGNSNTDTTTSGEVSAQSSTNSTSSEESTSVKDEDSSKIHDKSLKRKHEDDESSTSTKSSRTTKTPFTRVGDPSQWDFASPALRDNSFNFEDDYGTLANRDLIVTRGKGFRQEKNKKKRGSYRGGRINTEVRSFKF
Protein: Ectoine dioxygenase (EC 1.14.11.55) (Ectoine hydroxylase) (A4VFY4)
Organism: Stutzerimonas stutzeri (strain A1501) (Pseudomonas stutzeri)
Function: Involved in the biosynthesis of 5-hydroxyectoine, called compatible solute, which helps organisms to survive extreme osmotic stress by acting as a highly soluble organic osmolyte. Catalyzes the 2-oxoglutarate-dependent selective hydroxylation of L-ectoine to yield (4S,5S)-5-hydroxyectoine.
Interaction partners:
Sequence:
MQADLYPSRQEDQPSWQERLDPVVYRSDLENAPIAAELVERFERDGYLVIPNLFSADEVALFRAELERMRQDPAVAGSGKTIKEPDSGAIRSVFAIHKDNELFARVAADERTAGIARFILGGDLYVHQSRMNFKPGFTGKEFYWHSDFETWHIEDGMPRMRCLSCSILLTDNEPHNGPLMLMPGSHKHYVRCVGATPENHYEKSLRKQEIGIPDQNSLSELASRFGIDCATGPAGSVVFFDCNTMHGSNGNITPSARSNLFYVYNHVDNAVQAPFCEQKPRPAFVAERENFKPLDIRPQQYL
Protein: Thiosulfate dehydrogenase (EC 1.8.2.2) (Tetrathionate synthase) (Q4FQB7)
Organism: Psychrobacter arcticus (strain DSM 17307 / VKM B-2377 / 273-4)
Function: Catalyzes the oxidation of 2 molecules of thiosulfate to tetrathionate.
Subcellular location: Periplasm {ECO:0000250}.
Interaction partners:
- Putative cytochrome c, class I
Sequence:
MKIIPYRKRSVLIATIFAISAVGITGCSDNTETKAVERVEEAAALARVKDLEARAEALKSNMPAANDMTATAGGTDTASGKPTIKMPDESTIPDDEFGAAVRRGLQISNHTYKELPNNVGNQLNCTSCHLGNGSEAYAAPWNNTPSVYPNYSKRTGRINTIQERINGCFERSLNGKALDLNSDDMNAMVSYMSWLSQDMPFGVSPEGSGFVKVDKTLEPNTDNGKKLFAEKCSVCHGATGEGQYNDDGTYVYPAIAGDKSFNDGAGMARTYTAASFIKGKMPFGQGGSLSDQEAVDIASYFTHLPRPIKANKDKDWPNGDAPKDVRR
Protein: Activator of spomin::LUC2 (Activator of sporamin LUC 2) (MJM20.3 protein) (Q9LDL9)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123, ECO:0000256|PROSITE-ProRule:PRU00357}.
Interaction partners:
- CCT motif family protein
- Protein CHLOROPLAST IMPORT APPARATUS 2
- Transcription factor bHLH149
- Alpha/beta-Hydrolases superfamily protein
- Serine/threonine-protein kinase WNK
- At3g49760
Sequence:
MASSLPQFYADFTTFSCETSSQFHGSSSCPDVDSSLSSYLDDCYGSFNTSSNPESIFVPQVFGISDVSVPEYNNYYQKMSVNNATHYFHGGDHQEYYGFSPEIKPLFRPATGEQSWGNSEGGIQAEPNTKVGRYSVEERKDRIMRYLKKKNQRNFNKTIKYVCRKTLADRRVRVRGRFARNNDTCEEQPHMSKNHNNHSEKEEDMFSGSDDYLIQMEHDDGWLHEAMSNLIPFPCEFDAPGDAHHPTNWSF
Protein: Androgen-induced gene 1 protein (AIG-1) (Fatty acid esters of hydroxy fatty acids hydrolase AIG1) (FAHFA hydrolase AIG1) (EC 3.1.-.-) (Q9NVV5)
Organism: Homo sapiens (Human)
Function: Hydrolyzes bioactive fatty-acid esters of hydroxy-fatty acids (FAHFAs), but not other major classes of lipids. Show a preference for FAHFAs with branching distal from the carboxylate head group of the lipids.
Subcellular location: Cell membrane {ECO:0000269|PubMed:27018888}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
Sequence:
MALVPCQVLRMAILLSYCSILCNYKAIEMPSHQTYGGSWKFLTFIDLVIQAVFFGICVLTDLSSLLTRGSGNQEQERQLKKLISLRDWMLAVLAFPVGVFVVAVFWIIYAYDREMIYPKLLDNFIPGWLNHGMHTTVLPFILIEMRTSHHQYPSRSSGLTAICTFSVGYILWVCWVHHVTGMWVYPFLEHIGPGARIIFFGSTTILMNFLYLLGEVLNNYIWDTQKSMEEEKEKPKLE
Protein: AAA-ATPase At3g28510 (EC 3.6.1.-) (Q9LH84)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Membrane {ECO:0000255}; Single-pass membrane protein {ECO:0000255}.
Interaction partners:
- Protein DJ-1 homolog A
- O-fucosyltransferase 4
- Photosynthetic NDH subunit of subcomplex B 4, chloroplastic
- Aspartyl protease AED1
- E3 ubiquitin-protein ligase
- NAD
- E3 ubiquitin-protein ligase RING1
Sequence:
MLETGAIWGITGTTVTSFMFFWAIYKQYVPAHFRAYVERYFHKMIGWISYYVDIKFTEYTDEGLKRSQAYDSIRNYLASKSTALAKRLKANETKNSKSLVFSMDDHEEIEDEFEGVKVKWYSNVKVIQPQSNYGQRSSEERRHFTLSFHRRHRGMIIETYLDHVLREGKAIGLMNRERKLYTNNSSQEWYPWRSGKWSNVPFHHPATFETLAMDPEKKEGIKKDLIKFSKGKDYYKKVGKPWKRGYLLFGPPGTGKSTMIAAIANFLDYDVYDLELTTVKDNSELKKLLLDTTSKSIIVIEDIDCSLDLTGQRKKKKEEDEEEDGEEKKEGEKKPKVDDKQSKVTLSGLLNSIDGLWSACSGEKIIVFTTNFVDKLDPALIRRGRMDNHIEMSYCKFEAFKVLAKNYLEIETHDLYGEIERKLEETDMSPADVAETLMPKSDEEDADICIKRLVKTLEEEKEKARKLAEEEEKKKAEKEAKKMKKAEEAEEKKKKTEEDEKKEKVKAKEENGNVSQQNGNSIDLNKKSDS
Protein: RE37361p (Q8IGS5)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
VEILKSSRSAVFEMWRHRILQQASRRGISKQVREDGGARREPSGFLPGAADVVVIGGGSAGCHTLYHLARRGVKAVLLERAQLTAGTTWHTAGLLWRLRPNDVDIQLLANSRRMLQQLEEETELDPGWIQNGGIFIAHNETRLDEYRRLATVGSALGIENQVLSPEDTQKLFPLLDPSAFVGALYSPGDGVMDPAMLCAALKKAATNLGAQVIENCGVDDLLLEQTARGKKVVGVSTPFGDIKAEKVVNATGVWGRDLVARHGTHLPLVPMKRAYIVSESIPGVRGLPNIRDHDYSTYFRIQGDAICMGGYEPNPILLEPVPKDFHFGLYELDWSVFETHVEGAQELCPSYAKYGVKSTVCGPESFTPDHKPLMGPDPNLDGLYHNCGFNSAGMMFGGGCGEQTALWVIQGQPDLPMFGFDLRRFTQEQGKAIQWIREKSHESYVKNYSMVFKYDQPLAGRDFQKDPLHDEMMKAGAVMEEKQGWERPGFFLPTGSKKAVVQPYDWYGSYVHQRHKDSEYERVLDGDLHYSRFSEYHDLIGSEALACRNNAVVFNMSYFAKLLLDGPQAQEAADWLFSANTNRDPSKTVYTCALNDAGGVEADVTISRLAPGSGEVYNPKINGQGFYIVAGGASAFYTYSVLLAEIRRKGFNASLKDLTAELGVISIQGPNSRKILQPLIDCDLSDEHVAPNSTRLAKFGDVGLRLLRVSFVGELGYELHVPKKDCAAVYRSLMKAGAGEDLRNAGYRSLYSLSSEKGYHLWSFDLRPDDTPLEAGLGFTCRKTGADYRGKAAIENQRAEGLKKRLVYLTLRDQVPIWGLEGVYRNGEPVGILRRAEYAYTLGKSLGQTYVSRPDGKIIDADYIRNGEYEVDILGKKYRADCHLRSPFDPTGQRVLGNYASESKSNK
Protein: Uncharacterized FAD-binding protein C17H9.12c (O13809)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Subcellular location: Mitochondrion outer membrane {ECO:0000269|PubMed:16823372}; Single-pass membrane protein {ECO:0000269|PubMed:16823372}.
Interaction partners:
- Dihydroorotate dehydrogenase
- Probable NADPH:adrenodoxin oxidoreductase, mitochondrial
- NADH-cytochrome b5 reductase 1
- Probable cytochrome b5 1
- Probable cytochrome b5 2
- Protein transport protein got1
- Orotate phosphoribosyltransferase
- Orotidine 5'-phosphate decarboxylase
- Putative holocytochrome-c synthase
- Putative holocytochrome-c1 synthase
Sequence:
MSSSTYRKLPKILAAGLAIGCAGGYYAYKNSNKPPGLNPEIYAPFTVNKITELTSDASLFSLVPQSPSEHLTTLEPIAKVTIRDPSMQVQRPYTPLYLDANELKFFIRKYEEGPVSSYIHSKKEGDTIELRGPFKTTKLDCTKYPRIVAIVAGTGIAPIYQLAQSVKSPVDIVYCSRPGQPPLLKEELEKECPNVRVKSVQNRLVNIHDILDWDNVTVPLKDTLCIVCGSQKFVSTIAGPKADYGARQGEVKGLLSNNPFGKVWKL
Protein: Splicing factor, arginine/serine-rich 19 (CTD-binding SR-like protein rA1) (SR-related and CTD-associated factor 1) (Q63624)
Organism: Rattus norvegicus (Rat)
Function: May function in pre-mRNA splicing.
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
- Ets2 repressor factor
- Proline rich 12
- Protein PRRC2A
Sequence:
MEEEDESRGKTEESGEDRGDGPPDRDPALSPSAFILRAIQQAVGSSLQGDLPNDKDGSRCCGLQWRRCCRSPRSEPRSQESGGADMATVLDTAADSFLVELVSILDPPDTWVPSHLDLQPGESEDVLELVAEVRIGDRDPMPLPVPSLLPRLRAWRTGKTVSPQSHASRPACSRHLLTLGTGDGGPAPPPAPSSASSSPSPSPSSSSPSPPPPPPPPPPPALPAPRFDIYDPFHPTDEAYSPPPAPEQKYDPFEPTGSNPSSSAGTPSPEEEEEEEEEEEEEGLSQSISRISETLAGIYDDNSLSQDFPGDDSPHREPPPPQTLGAPGTPPQADSTRAEGAPRRRVFVVGPEAEACLEGKVSVEVVTTAGGPALPLPPLPPTDPEIEEGEIVQPEEEPRVAVSLFRAARPRQPPASVATLASVAAPAAPPASAPRAPEGDDFLSLHADSDGEGALQVDLGEPPAPPAADARWGGLDLRRKILTQRRERYRQRSASPGPPPARKKARRERQRSGDPAPPDSPTWEAKKHRSRERKLGSHSTARRRSRSRSRRRSRSRSADRRRGSHRSRSREKRRRRRRSASPPPAASSSSSSRRERHRGKRREGGKKKKKRSRSRAEKRSGDLEKLPAPVPPSGSDRDSRRRGAVPPSIQDLTDHDLFAIKRTITVGRPDKTEPRAPSPAPAVSPKREVLYDSEGLSADERGAKGDKDRRRSGAASSSSSSREKASRRKALDGDRGRDRDRSSKKTRPPKDSAPGSGALPKAPPSSGSSSSSSSCSSRKVKLQSKVAVLIREGVSSTTPAKDSSSSGLGSIGVKFSRDRESRSPFLKPDERAPAEGVKVAPGSTKPKKTKAKAKAGAKKAKGTKGKTKPSKTRKKVRSGGSSTASGGPGSLKKSKADSCSQAASAKGTEETSWSGEERTTKAPSTPPPKVAPPPPALTPDSQTVDSSCKTPEVSFLPEEASEDTGVRVGAEEEEEEEEEEEEEEEQQPATTTATSTAAAAPSTAPSAGSTAGDSGAEDGPAARASQLPTLPPPMPWNLPAGVDCTTSGVLALTALLFKMEEANLASRAKAQELIQATNQILSHRKPPSTLGVTPAPVPTSLGLPPGPSSYLLPGSLPIGGCGSTPPTPTGLVPASDKREGSSSSEGRGDTDKYLKKLHTQERAVEEVKLAIKPYYQKKDITKEEYKDILRKAVHKICHSKSGEINPVKVSNLVRAYVQRYRYFRKHGRKPGDPPGPPRPPKEPGPPDKGGPGLPLPPL
Protein: Isopentenyl-diphosphate Delta-isomerase (IPP isomerase) (EC 5.3.3.2) (IPP:DMAPP isomerase) (Isopentenyl pyrophosphate isomerase) (Q46822)
Organism: Escherichia coli (strain K12)
Function: Catalyzes the 1,3-allylic rearrangement of the homoallylic substrate isopentenyl (IPP) to its highly electrophilic allylic isomer, dimethylallyl diphosphate (DMAPP).
Subcellular location: Cytoplasm.
Interaction partners:
- Farnesyl diphosphate synthase
- 4-hydroxy-3-methylbut-2-enyl diphosphate reductase
- 1-deoxy-D-xylulose-5-phosphate synthase
- 2-C-methyl-D-erythritol 2,4-cyclodiphosphate synthase
- 4-diphosphocytidyl-2-C-methyl-D-erythritol kinase
- 1-deoxy-D-xylulose 5-phosphate reductoisomerase
- 2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase
- 4-hydroxy-3-methylbut-2-en-1-yl diphosphate synthase
- Acetyl-CoA acetyltransferase
- Probable acetyl-CoA acetyltransferase
Sequence:
MQTEHVILLNAQGVPTGTLEKYAAHTADTRLHLAFSSWLFNAKGQLLVTRRALSKKAWPGVWTNSVCGHPQLGESNEDAVIRRCRYELGVEITPPESIYPDFRYRATDPSGIVENEVCPVFAARTTSALQINDDEVMDYQWCDLADVLHGIDATPWAFSPWMVMQATNREARKRLSAFTQLK
Protein: Protein kinase, putative (Q387Y1)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MLLDFVLKYVRGTHPADSEDASKEGSPSAASAYGGKDRKHHPPAEGHRSPPDENVSGNEQGRGIMTLLPKVPSAESVRDKPFYSNGSGHGERRELDGHEKESSVDGKHRQHRSHVLPSMDMDRAPSQFSASGSRQLEGPHGVNCAQVTEQSLEVHDPNDGVDRCHDRSGTGTAHDNNRLAADQIGCTATVAEELRAHRSTTPIKIVNAAAQNVEDDIDDDNEVVGNALVKPMTPQSYSSLMFNSDFRKLNYKEDDIKRRIAVGEGRSLLILQNRGVSCDALSAIPALERHVSDARSCPARSVQSSECAGGVLTSSPRKEEPQRERNFHSEKRPPTADTDGQTICTCGLTVGSSPTEQFSCPGGAAEDSFNRKTCKIHGTNLGCRAHSSELISEWVSECIPPEPVELINVNAGRPRVNVLKKGVINCCVAVRKSLDDAKMMLNNKYVIYFRWCLGVGSSSKVFLCYNLHEKAFYAMKVYNRGRLRRKGFGANCALNNVRREIDIMKKLRHPNILSLVEVIDDPFSRKIYLVLELAEKGAVMTLEGDGTVVPSVSGAALPEEEVARAIRSVVEALIYVHDLGIVHRDVKPQNILLDAEECVKLSDFGVSIMVDGCTSPVPREGTVAFLPPEMLASSEVRVALSDAASHKDTSIGSTNSHQVCSRMNDELPVKTLPEGEREEIGSLQTTDTSVRTQNDNASVSVGSECKQVASTGVASLSGSNNPGCEVSPSDCAGLPACDPTGTPVADFFKADVFALGVTTFVLLMGRLPWLARSSRSQMKAINAQPDPFEEPLRKAYGCPSGEGLKGPTLCNRSLHGSEPPESSAIFLEGTTERTASQQMFSSSSCGRFLASNDADTLDHHVSRSSTKPDCTDWCNSGMSRVSREDEVGAQLLASSPTQCAIGGEWKDSKLLQSSEVGGSPRAHEEADGAQRSPYGHTNTSMRVCCGCRSSSNTATVPTTSFGSLSEAGKAPVSRENKPEFSAVSCFSQPNAAGEATPFRRTHSPSKFPLGRRSTSVFVSNNSSLHSWRIQEGHQPHAGDAVLNEDLEGSLTSDANFPLSAGREFTFPLCQHCATCNNTNNGPYTESGVGDTMSGEQTSGSKMEVPERRGLPETDTHKCISADAIEFVRSCLRINPMERSTMKELYEMPWLQKGR
Protein: Tubulin glycylase 3B (dmTTLL3B) (EC 6.3.2.-) (Q9VM92)
Organism: Drosophila melanogaster (Fruit fly)
Function: Essential glycylase which modifies both tubulin and non-tubulin proteins, generating side chains of glycine on the gamma-carboxyl groups of specific glutamate residues of target proteins. Monoglycylates alpha-tubulin by adding a single glycine chain to generate monoglycine side chains, but is not involved in elongation step to generate polyglycine side chains on alpha-tubulin. Has the ability to both mono- and polyglycylate non-tubulin proteins such as up (Troponin T). Required for early steps of spermatogenesis.
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000269|PubMed:19524510}. Nucleus {ECO:0000269|PubMed:19524510}.
Interaction partners:
Sequence:
MTTQNTTPAGFTGNRNRYYNPVSKIQSLIHNLDAELVQLCKQCSVQKPLTSLNNSTSLGSHFSNFGALGGGSGSKTMGGSSSMGSNNFSPDSIGNLLARVRASTPLPRTVTSSPTAPEAQKRQMRNVYRTRVIDAYRNRRIFTVYGNYHTVRRALMRRGWLEKLPASRHAKLQSMSEDALLEHARRGNDYEAVVISKMINHFPAFFIWQGKGQRDLCAEVRPFRNRVRRSQFLDFSTKVGLVGCAEQERWYREDGVCGMSYPRFYRLGGNNLEERMAFIEDYQQTQARSLLLYVREHQPAELISENGTIFSTTLDFALGKVKKMVRHAEHYSLDDARIKPPTPAEIVENQTFMVQSTDVLKSNAKFKVSEKVMAEYARLAGLYLDQIESLRPDYRWDGSRNLWILKPGYQSRGIGIVIRSSLDDILQWTSNNQNKKYIVQKYIERPLLIYRTKFDIRQYMLLTITDTKVSIWTYRDCYLRFSSQEFTMDDLRESIHLTNNSVQKRYKNKTNRDSRLPKNNMWSLDQFKNYLRIMGAPDGSWSKTYNGFKQNLVAVVMASLDETELLQNAFELYGCDFMLDEHYNPILIEINSTPDLSPSTEITARICPMVLKDCIRVVVDLPKNPTAATGLFELAFEVNYSINKGADGKPLELNGKQMTLFENMPRMRNSPRTRLLRKILNNVKTSTTKKVEKVVEAPAKNVKNPTAKITKKKKLSASAGSSTAASAQPSTQNLTTKLILNPATRENLALQYTAPK
Protein: ATPase, F0/V0 complex, subunit C protein (B3H4N3)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
Sequence:
MSGVVALGHASSWGAALVRISPYTFSAIGIAISIGVSVLGAAWGIYITGSSLIGAAIEAPRITSKNLISVIFCEAVAIYGVIVAIILQTKLESVPSSKMYDAESLRAGYAIFASGIIVGFANLVCGSVSTLFSFLTVLVFGFHCQICNRGPHFSCRLCVGIIGSSCALSDAQNSTLFVKILVIEIFGSALGLFGVIVGIIMSAQATWPTK
Protein: Popeye domain-containing protein 1 (Popeye protein 1) (Q8NE79)
Organism: Homo sapiens (Human)
Function: Cell adhesion molecule involved in the establishment and/or maintenance of cell integrity. Involved in the formation and regulation of the tight junction (TJ) paracellular permeability barrier in epithelial cells. Plays a role in VAMP3-mediated vesicular transport and recycling of different receptor molecules through its interaction with VAMP3. Plays a role in the regulation of cell shape and movement by modulating the Rho-family GTPase activity through its interaction with ARHGEF25/GEFT. Induces primordial adhesive contact and aggregation of epithelial cells in a Ca(2+)-independent manner. Also involved in striated muscle regeneration and repair and in the regulation of cell spreading (By similarity). Important for the maintenance of cardiac function. Plays a regulatory function in heart rate dynamics mediated, at least in part, through cAMP-binding and, probably, by increasing cell surface expression of the potassium channel KCNK2 and enhancing current density. Is also a caveolae-associated protein important for the preservation of caveolae structural and functional integrity as well as for heart protection against ischemia injury.
Subcellular location: Lateral cell membrane {ECO:0000269|PubMed:16188940}. Cell junction, tight junction {ECO:0000269|PubMed:16188940}. Membrane {ECO:0000269|PubMed:26642364}; Multi-pass membrane protein {ECO:0000305}. Cell membrane, sarcolemma {ECO:0000269|PubMed:26642364}. Membrane, caveola {ECO:0000250|UniProtKB:Q9ES83}. Note=Colocalizes with VAMP3 at the cell-cell contact in cardiac and skeletal muscle (By similarity). Its movement from the cytoplasm to membrane is an early event occurring concurrently with cell-cell contact. Colocalizes in epithelial cells with OCLN and TJP1 in an apical-lateral position within the z axis. Detected at cell-cell contact but never observed at the free surface of epithelial cells. {ECO:0000250|UniProtKB:Q9ES83}.
Interaction partners:
- Tight junction protein 1
- Rho guanine nucleotide exchange factor 25
- Potassium channel subfamily K member 2
- Serine/threonine-protein phosphatase 2A 56 kDa regulatory subunit alpha isoform
Sequence:
MNYTESSPLRESTAIGFTPELESIIPVPSNKTTCENWREIHHLVFHVANICFAVGLVIPTTLHLHMIFLRGMLTLGCTLYIVWATLYRCALDIMIWNSVFLGVNILHLSYLLYKKRPVKIEKELSGMYRRLFEPLRVPPDLFRRLTGQFCMIQTLKKGQTYAAEDKTSVDDRLSILLKGKMKVSYRGHFLHNIYPCAFIDSPEFRSTQMHKGEKFQVTIIADDNCRFLCWSRERLTYFLESEPFLYEIFRYLIGKDITNKLYSLNDPTLNDKKAKKLEHQLSLCTQISMLEMRNSIASSSDSDDGLHQFLRGTSSMSSLHVSSPHQRASAKMKPIEEGAEDDDDVFEPASPNTLKVHQLP
Protein: C-type lectin 37Db (Q59DY5)
Organism: Drosophila melanogaster (Fruit fly)
Function: Galactose-specific lectin that displays calcium-dependent activity. Binds to the surface of hemocytes and enhances hemocyte encapsulation and melanization. This is likely by interacting with carbohydrates on the surface of the hemocytes. Also displays agglutination activity against the Gram-negative bacterium E.coli.
Subcellular location: Secreted {ECO:0000269|PubMed:16475980}.
Interaction partners:
Sequence:
MMVKLLLLFLVCWSALPLESSPLGNRYNLEIGEKQYYISLAKTNWFEASNHCRQNGGFLLNLESREELELLSPHLHPAYSYWLSINDLGERGVYVSEATGLEAPFLNWSAGEPDNSSGYDRCVELWLSTTSFQMNDLPCYSSVAFICQLN
Protein: ADAM metallopeptidase with thrombospondin type 1 motif 3 (G3X9D2)
Organism: Mus musculus (Mouse)
Subcellular location: Secreted, extracellular space, extracellular matrix {ECO:0000256|ARBA:ARBA00004498}.
Interaction partners:
Sequence:
MVFLSLWLIAASLVEVRTSADGQAGTDEMVQIDLPTKRYREYELVTPVSTNLKGHYLSHILSANHKKRSPRDVSSNSEHLFFNVTAFGRDFHLRLKPNTHFIAPGAVVEWHETAPRPGNTTDPRNSHLHGSASEGSWRSEPLQTSCAYVGDIMDIPGTSVAISNCDGLAGMIKSDDEEYFIEPLERGKQMDEENGRIHVVYKRSAVEQPPRDVSEDVYHRESDLEGLDDLGTVYSNIGQQLNKTMRRRRHTGENDYNIEVLLGVDDSVVRFHGKEHVQNYLLTLMNIVNEIYHDESLGVHINVVLVRMIMLGYAKSISLIERGNPSRSLENVCRWACQQQKTDPNHAEHHDHAIFLTRQDFGPAGMQGYAPVTGMCHPVRSCTLNHEDGFSSAFVVAHETGHVLGMEHDGQGNRCGDETAMGSVMAPLVQAAFHRYHWSRCSGQELKRYIHSYDCLLDDPFEHDWPKLPELPGINYSMDEQCRFDFGVGYKMCTAFRTFDPCKQLWCSHPDNPYFCKTKKGPPLDGTECAAGKWCYKGHCMWKNANQQKQDGNWGSWTKFGSCSRTCGTGVRFRTRQCNNPTPINGGQDCPGVNFEYQLCNTEECQKHFEDFRAQQCQQRNSHFDYQNTKHHWLPHEHPDSKKRCHLYCQSKETGDVAYMKQLVHDGTRCSYKDPYSICVRGECVKVGCDREIGSNKVEDKCGVCGGDNSHCRTVKGTFTRTPRKLGYLKMFDIPPGARHVLIQEDEASPHVLAIKNQATGHYILNGKGEEAKSRTFIDLGVEWDYNIEDDIETLHTDGPLHDPVIVLIIPQENDTRSSLTYKYIIHEDSVPTINSNNVIQEELDTFEWALKSWSQCSEPCGGGFQYTKYGCRRKSDSKMVHRSFCEVNKKPKPIRRMCNIQECTHPVWAADEWEHCSRSCGSSGNQLRTVRCLQPLQDGTNRSVHSKYCLGDRPESRRPCNRVPCPAQWKTGSWNECSVTCGEGTEVRQVLCRTGDHCDGEKPESVRPCQLPPCNDEPCLGDKSIFCQMEVLARYCSIPGYNKLCCESCSKRSGTLPPPYLQEAAEIHSDAIFGPSDLPRSLVMPTPFLPSSSGTRAEKKSLSSFSSMANPNADAAFRASSRASADFPRKRAHQAGRKTLESVPSSSSIKTDHLRPASPVAAAPSPAISDSIGASPQTRTPKKDDAKSVSRRHPTRSTASER