wanglab/gogpt-training-data huggingface dataset:
Protein: PE-PGRS family protein PE_PGRS33 (P9WIF5)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: Induces TNF-alpha release through human Toll-like receptor 2 (TLR2) signaling pathway, leading to macrophage apoptosis. The signaling pathway involves TLR2-dependent activation of the mitogen-activated protein kinase kinase kinase 5 (ASK1), which activates the p38 and JNK MAPKs, leading to enhanced expression of TNF-alpha and tumor necrosis factor receptor superfamily member 1A (TNFRI) genes. Signals are amplified through classical caspase 8-dependent mitochondrial release of cytochrome c, leading to the activation of caspases 9 and 3. Mediates Ca(2+)-dependent up-regulation of the anti-inflammatory cytokine IL-10. Mediates entry into macrophages in a TLR2-dependent mechanism and activates the TLR2-dependent pro-adhesive pathway.
Subcellular location: Secreted, cell wall {ECO:0000269|PubMed:15101979, ECO:0000269|PubMed:18028308, ECO:0000269|PubMed:22110736, ECO:0000269|PubMed:27483162}. Cell surface {ECO:0000269|PubMed:15101979, ECO:0000269|PubMed:18028308, ECO:0000269|PubMed:18957600, ECO:0000269|PubMed:22110736, ECO:0000269|PubMed:27483162}. Cell outer membrane {ECO:0000269|PubMed:18028308}. Note=Exported to the cell surface via the ESX-5 / type VII secretion system (T7SS) (PubMed:22110736). Localizes mostly at the cell poles (PubMed:15101979). Colocalizes to mitochondria in transfected eukaryotic cells (PubMed:17223373, PubMed:21081760). {ECO:0000269|PubMed:15101979, ECO:0000269|PubMed:17223373, ECO:0000269|PubMed:21081760, ECO:0000269|PubMed:22110736}.
Interaction partners:
Sequence:
MSFVVTIPEALAAVATDLAGIGSTIGTANAAAAVPTTTVLAAAADEVSAAMAALFSGHAQAYQALSAQAALFHEQFVRALTAGAGSYAAAEAASAAPLEGVLDVINAPALALLGRPLIGNGANGAPGTGANGGDGGILIGNGGAGGSGAAGMPGGNGGAAGLFGNGGAGGAGGNVASGTAGFGGAGGAGGLLYGAGGAGGAGGRAGGGVGGIGGAGGAGGNGGLLFGAGGAGGVGGLAADAGDGGAGGDGGLFFGVGGAGGAGGTGTNVTGGAGGAGGNGGLLFGAGGVGGVGGDGVAFLGTAPGGPGGAGGAGGLFGVGGAGGAGGIGLVGNGGAGGSGGSALLWGDGGAGGAGGVGSTTGGAGGAGGNAGLLVGAGGAGGAGALGGGATGVGGAGGNGGTAGLLFGAGGAGGFGFGGAGGAGGLGGKAGLIGDGGDGGAGGNGTGAKGGDGGAGGGAILVGNGGNGGNAGSGTPNGSAGTGGAGGLLGKNGMNGLP
Protein: Protein transport protein SEC31 (O96221)
Organism: Plasmodium falciparum (isolate 3D7)
Subcellular location: Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00004240}.
Interaction partners:
- Protein transport protein SEC13
- Protein transport protein SEC23
- Protein transport protein Sec24A
- Small GTP-binding protein sar1
- Protein transport protein Sec24B, putative
- Trafficking protein particle complex subunit
- Protein transport protein SEC22
- Coatomer alpha subunit, putative
Sequence:
MALKSINISGNFEWCPFEEYKNYLLCFNSHNLLYSNNNSLNNYIYLLDINLNSEIRNLEIVNKYNFEDALKYDNDVIKGGNKKNNKNNKNNHNNNSVNEYVTCFEWMNSNNFVDINNNEELSKGIIVGGLTNGDIVLLNAKNLFETNRNYDNFILSKTNIHDNGINCLEYNRHKNNLIATGGNDGQLFITDIENLYSPTSYDPYLDKNNLQKITCLNWNKKVSHILATSSNNGNTVIWDLKIKKSAVSFRDPHSRTKTSSLSWLSNQPTQVLISYDDDKNPCLQLWDLRNSNYPIKEIIGHSKGINNICFSPIDTNLLLSSGKDVTKCWYLDNNNFDIFNEINNSANNIYSKWSPYIPDLFASSTNMDTIQINSINNGNKMTSKYIPTFYKKEAGICIGFGGKICTFDNSTNNMSNVNNMNNVNNMNNINSFNNDNSCDGEYDSNKGKNKSTQKKFLIKYHIYPTDMELISEADNFEKYITSGNYKEFCESKINKCDDDHEKLTWQILQLLCTSQRGDIVKYLGHDINNIVDKIMQTIGKQPGFIFKTLIDEKENNNNNNNNNSTNQMYQNDVLLHNDPNLMNNYLLKDNMNPNIMLNNNNNNINNRTGTNVMYSNGQNLLGDTNHNEENFNGNFDIDPEKFFRELGEKTENEKIKQNEEDISGNDEHLLNSSIKGKENKTKNKKSGLGTDDNNDNGDHNKNEGSNINGEHVSEHILNEKNNTNNWNLGIEAIIKECVLIGNIETAVELCLHKNRMADALLLSSFGGEQLWHKTKTIYIKKQNDNFLKNINYVLDDKLENLINNVDLNSWEEALSILCTYAINNPNFNSLCEMLAKRLQNEKFDIRAASICYLCACNFSETVEIWNNMPSKKTSLLNVLQDIVEKMTILKMIIKYENFNSIMNQKISQYAELLANSGRLKAAMTFLCLIQHDQSIESLILRDRIYNSANHVLCQQIKPPISPFQIVDIKPSPNVYQNNMYNNNNNNNNININSSSNNNNNNNNNKVLSSMHHPMQQFNQCNVNKMYTSTSNIINNNTMNSNFKSVIPPPLPMNTQMNNSTSSIQPPPSVPPTKFHTQIINNTMNSRSSIATTTKNYPTSNLNSVIPTSMNNMNTNISHGNNVTPPYMSQTNVAVPNMNNNNNNNNTMNPTYPSLPKFPNYNLNSQVQQNSIIPEKQLTSPMFSSNSYGNINKTHTTNNAVPPPPNVTSSVVTPPMPSNQLNNTRSSFADIQNVVSPPRNKNQSISSTANLNYQHDNQFNKRECMEQPVYPMTNQSSMFSMNNTMQKKNVPGGFQDNTSQMNYGMQPTGSPPPSSLSTTSPIAGALTVTPGMPVPWPIPTTTQQLGSTTQSTANENKKIQTATKEQNGVLMNRNHIENIKKTISNLLNIYTSQESVKKKADDVSSKVYELFEKLDCGAFNEQINDSLLNLVNCINANDFKTTNKIIVDLSRNLWDGSNKAWIMGVKHIIPKC
Protein: Xyloglucan endotransglucosylase protein 7 (XET protein 7) (EC 2.4.1.207) (DkXTH7) (Xyloglucan endotransglucosylase/hydrolase protein 7) (XTH protein 7) (A0A067XR63)
Organism: Diospyros kaki (Kaki persimmon) (Diospyros chinensis)
Function: Catalyzes xyloglucan endotransglycosylation (XET). Cleaves and religates xyloglucan polymers. Does not catalyze xyloglucan endohydrolysis (XEH). Probably involved in cell wall assembly and synthesis in fast growing tissues and in the maintenance of firmness in mature fruits.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:27242828}. Note=Dispersed throughout the cell. {ECO:0000269|PubMed:27242828}.
Interaction partners:
Sequence:
MNAEGGNLHREFEITWGDGRARIHNNGGLLTLSLDRASGSGFRSKNEYLFGRIEIQIKLVAGNSAGTVATYYLSSEGPTHDEIDFEFLGNSSGEPYTLHTNVFSQGKGNREQQFFLWFDPTMDFHTYTILWNPQRIIFYVDETPIREFKNLERHGIPFPRSQAMRVYSSMWNADDWATRGGLVKTDWTKAPFTASYRSYKADACVWSGEASSCGSQDSNPSDKWWMTEELNATRMKRLRWVQKKYMVYNYCVDKMRFPEGLAPECNIS
Protein: MOB kinase activator-like 1 homolog B (Mps one binder kinase activator-like 1 homolog B) (Q54CR8)
Organism: Dictyostelium discoideum (Social amoeba)
Interaction partners:
Sequence:
MFKIFNSDKNKTFKPKKGFSKGTKRHDLHKHAKATLGSGNLRLAVSLPEREDLNEWLAVNTVDFFNQINLLYGSITEFCTPKTCEVMSAGPKYEYLWADGESVKKPIKVSAPEYVEFLMTWVQGILDDENIFPSRVDVQFPKNFQSIVKNIFKRLFRVYGHIYYSHFTKIVSLGEEAHLNTCFKHFYFFIVEFNLVDKKEMLPLQDLIDNLTKSST
Protein: MADS-box transcription factor FBP9 (Q9ATF1)
Organism: Petunia hybrida (Petunia)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MGRGRVELKRIENKINRQVTFAKRRNGLLKKAYELSVLCDAEVALIIFSSRGKLYEFCSTSSMMKTLEKYQQCSYASLDPMQSANDTQNNYHEYLRLKARVELLQRSQRNLLGEDLGSLNSKELEQLEHQLDSSLKQIRSKKTQHMLDQLADLQQKEQMLAEANKQLRRKLEESAARIPLRLSWDNGGQPMQHNRLPPQTEGFFQPLGLNSSSPQFGYSPMGANEVNNAVSTAQNMNGFIPGWML
Protein: Voltage-dependent calcium channel gamma-3 subunit (Neuronal voltage-gated calcium channel gamma-3 subunit) (Transmembrane AMPAR regulatory protein gamma-3) (TARP gamma-3) (Q8VHX0)
Organism: Rattus norvegicus (Rat)
Function: Regulates the trafficking to the somatodendritic compartment and gating properties of AMPA-selective glutamate receptors (AMPARs). Promotes their targeting to the cell membrane and synapses and modulates their gating properties by slowing their rates of activation, deactivation and desensitization. Does not show subunit-specific AMPA receptor regulation and regulates all AMPAR subunits. Thought to stabilize the calcium channel in an inactivated (closed) state.
Subcellular location: Membrane {ECO:0000255}; Multi-pass membrane protein {ECO:0000255}. Note=Displays a somatodendritic localization and is excluded from axons in neurons. {ECO:0000250|UniProtKB:Q9JJV5}.
Interaction partners:
- Glutamate receptor 4
- Glutamate receptor ionotropic, kainate 4
- Protein cornichon homolog 3
- Protein cornichon homolog 2
- Glutamate receptor 1
- Voltage-dependent calcium channel gamma-5 subunit
- Voltage-dependent calcium channel gamma-7 subunit
- Glutamate receptor ionotropic, NMDA 3A
- Glutamate receptor ionotropic, NMDA 2B
- Glutamate receptor ionotropic, NMDA 1
Sequence:
MRMCDRGIQMLITTVGAFAAFSLMTIAVGTDYWLYSRGVCRTKSTSDNETSRKNEEVMTHSGLWRTCCLEGAFRGVCKKIDHFPEDADYEQDTAEYLLRAVRASSVFPILSVTLLFFGGLCVAASEFHRSRHSVILSAGIFFVSAGLSNIIGIIVYISANAGDPGQRDSKKSYSYGWSFYFGAFSFIIAEIVGVVAVHIYIEKHQQLRARSHSELLKKSTFARLPPYRYRFRRRSSSRSTEPRSRDLSPISKGFHTIPSTDISMFTLSRDPSKLTMGTLLNSDRDHAFLQFHNSTPKEFKESLHNNPANRRTTPV
Protein: Nucleolar complex-associated protein 2 (AtNOC2) (Q9ZPV5)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Together with SWA2, probably involved in pre-ribosome export from the nucleus to the cytoplasm.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00768}. Nucleus, nucleolus {ECO:0000269|PubMed:30338215}. Nucleus, nucleoplasm {ECO:0000269|PubMed:30338215}. Note=Also observed in nucleoplasmic bodies. {ECO:0000269|PubMed:30338215}.
Interaction partners:
- Nucleolar complex-associated protein 3
- Protein SLOW WALKER 2
- Pescadillo homolog
- Ribosome biogenesis protein BOP1 homolog
- Probable rRNA-processing protein EBP2 homolog
- 60S ribosome subunit biogenesis protein NIP7 homolog
- At4g01560
- Ribosome assembly factor mrt4
- Ribosome production factor 2 homolog
- rRNA biogenesis protein RRP5
Sequence:
MGAKDDKKRVKKLKSKKLEAEEELNNVQEIDAHDIVMEQKSDKKRGKKVKSKKAEAEEHEEELKRLQEKDPDFFQYMKEHDAELLKFDATEIEDDADVEPDTDLEDTEKEGDDEATKMEIAKKVHVQKTITASMVDAWSKSIEDEAKLGGVRSILRAYRTACHYGDDTGDDQSTKFSVMSSEVFNKIMIYVLSEMDGILRKLLRFPEDTRGTKETILELTNTRPWKNYNHLVKSYLGNSLHVLNQMTDTEMITFTLRRLKHSSVFLAAFPSLLRKYIKVALHFWGTGSGALPVVSLLFLRDLCIRLGSDCVDDCFKGMYKAYVLNCQFVNADKLKHISFLGNCFIELLGTDISAAYQHAFVFIRQLAMILREALNTKTKEAFRKVYQWKFIHCLELWTGAVCAYSSQSELRPVAYPLAQIITGVARLVPTARYTPLRLRCVRMLNRLAAATGTFIPVSMLLVDMLEMKELNRPPTGGVGKGVDLRTLLKVSKPAVKTRAFQEACVYTVVEELVEHLSQWSCSVAFFELSFIPTIRLRSFCKSTKAERFRKEMKQLISQIEANSEFVNKKRALIKFLPNDLAAESFLEDEKKAGKTPLLQYAEIIRQRAQQRNESLVESDVIVGENSAVFGKNAPSSDDEDDEDRMEKGAAAFNSSWLPGSDSKEKEPEEEKTKKKKRKRGGKSKTEKKQDEQGLGEDDVVEDFVLSSDEEEEDLFDIGGDKDEDDAVDEIADPETKTSKKTKGTYKTWHKAYKKTKKKKARVAS
Protein: BTB/POZ domain and ankyrin repeat-containing protein NOOT2 (Protein NODULE ROOT 2) (MtNOOT2) (A0A072VIM5)
Organism: Medicago truncatula (Barrel medic) (Medicago tribuloides)
Function: Involved in the regulation of indeterminate nodule identity in association with NOOT1.
Subcellular location: Nucleus {ECO:0000250|UniProtKB:G3LSH3}. Cytoplasm {ECO:0000250|UniProtKB:G3LSH3}. Cell membrane {ECO:0000250|UniProtKB:G3LSH3}; Peripheral membrane protein {ECO:0000250|UniProtKB:G3LSH3}; Cytoplasmic side {ECO:0000250|UniProtKB:G3LSH3}.
Interaction partners:
- Leucine zipper transcription factor
- BZIP family transcription factor
Sequence:
MSLEETLRSLSLDYLNLLINGQAFSDVTFQVEGRLVHAHRCILAARSLFFRKFFCGPDPPSGLDPIGGGSSRQPTVRPGVIPVNSVGYEVFLLLLQFLYSGQVSIVPQKHEPRPNCGERGCWHTHCTSAVDLALDTLAAARYFGVEQLALLTQKQLVSMVEKASIDDVMKVLIASRKQEMPQLWTTCSHLVAKSGLPPEILAKHLSIDVVAKIEELRLKSSLARRSLMPLHHHHHHHHHHDFGDLEDQKIRRMRRALDSSDVELVKLMVMGEGLNLDEALALHYAVENCSREVVKALLELGAADVNYPAGPAGKTSLHVAAEMVSPEMVAVLLDHHADPTVRTVDGVTPLDILRTLTSDFLFKGAVPGLNHIEPNKLRLCLELVQSAALVLSREENNASNNNNNNNNASSSAAPVYPPMSEDHSSSSSGNNNNNNNSIGNLNLDSRLVYLNLGATQMGGDDDNRHNNSHREAMNRQGGHGCDPSMYHHSHDF
Protein: Tiggy-winkle hedgehog protein (TWHH) (EC 3.1.-.-) (Sonic hedgehog protein B) (SHHB) [Cleaved into: Tiggy-winkle hedgehog protein N-product (Shh N-terminal processed signaling domains) (ShhNp) (Sonic hedgehog protein N-product) (ShhN)] (Q90419)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Function: The C-terminal part of the tiggy-winkle hedgehog protein precursor displays an autoproteolysis and a cholesterol transferase activity (By similarity). Both activities result in the cleavage of the full-length protein into two parts (N-product and C-product) followed by the covalent attachment of a cholesterol moiety to the C-terminal of the newly generated N-product (By similarity). Both activities occur in the reticulum endoplasmic (By similarity). Once cleaved, the C-product is degraded in the endoplasmic reticulum (By similarity).
Subcellular location: [Tiggy-winkle hedgehog protein N-product]: Cell membrane {ECO:0000250|UniProtKB:Q62226}; Lipid-anchor {ECO:0000250|UniProtKB:Q62226}. Note=The dual-lipidated tiggy-winkle hedgehog protein N-product (TWHHN) is firmly tethered to the cell membrane where it forms multimers (By similarity). Further solubilization and release from the cell surface seem to be achieved through different mechanisms, including the interaction with DISP1 and SCUBE2, movement by lipoprotein particles, transport by cellular extensions called cytonemes or by the proteolytic removal of both terminal lipidated peptides. {ECO:0000250|UniProtKB:Q62226}.; SUBCELLULAR LOCATION: [Tiggy-winkle hedgehog protein]: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q15465}. Golgi apparatus membrane {ECO:0000250|UniProtKB:Q15465}. Note=Co-localizes with HHAT in the ER and Golgi membrane. {ECO:0000250|UniProtKB:Q15465}.
Interaction partners:
- Protein patched homolog 1
- Protein patched homolog 1
- Protein smoothened
- Hedgehog-interacting protein.
- BOC cell adhesion-associated, oncogene-regulated.
- Cell adhesion molecule-related/down-regulated by oncogenes
- GLI family zinc finger 2a.
- GLI family zinc finger 1
- GLI family zinc finger 3.
- Neurogenic locus notch homolog protein 1
Sequence:
MDVRLHLKQFALLCFISLLLTPCGLACGPGRGYGKRRHPKKLTPLAYKQFIPNVAEKTLGASGKYEGKITRNSERFKELIPNYNPDIIFKDEENTNADRLMTKRCKDKLNSLAISVMNHWPGVKLRVTEGWDEDGHHLEESLHYEGRAVDITTSDRDKSKYGMLSRLAVEAGFDWVYYESKAHIHCSVKAENSVAAKSGGCFPGSGTVTLGDGTRKPIKDLKVGDRVLAADEKGNVLISDFIMFIDHDPTTRRQFIVIETSEPFTKLTLTAAHLVFVGNSSAASGITATFASNVKPGDTVLVWEDTCESLKSVTVKRIYTEEHEGSFAPVTAHGTIIVDQVLASCYAVIENHKWAHWAFAPVRLCHKLMTWLFPARESNVNFQEDGIHWYSNMLFHIGSWLLDRDSFHPLGILHLS
Protein: Guanine nucleotide-binding protein alpha-15 subunit (P91907)
Organism: Caenorhabditis elegans
Function: Guanine nucleotide-binding proteins (G proteins) are involved as modulators or transducers in various transmembrane signaling systems.
Interaction partners:
- Guanine nucleotide-binding protein subunit alpha
- Guanine nucleotide-binding protein subunit beta-1
- Guanine nucleotide-binding protein subunit beta-2
- Guanine nucleotide-binding protein subunit gamma
- G protein gamma domain-containing protein
- G Protein, Alpha subunit
Sequence:
MGSTCSTPESKEQKRINSVIDKQIRKDEDDEIGNQKLLLLGTGECGKSTILKQINILHSSGFSKADLKNVAGTVYSNIIQGVATLLKAKDHFYYELSTPELDADAQHILSLADSSKDAMPFIPLTFNAIKRLWHDPVVQKTFERRAEFQMMDTLVYFMNELDRINNADYIPTVDDMLRIRIPTMGVVQQTIEIKGTKFRIYDVGGQRSERRKWIHLFDNVNATIFISAINEFNQKLNEDGQTNRMKESIKLFETICNSRWFVQAAMILFLNKRDLFEQKLKTTSINVLFSTYQGSNDYAECVAYIQMRFERLNKYSDIKKIYTHVTCATDTNQIQLVIDSVVDMVIGRNLRGTGME
Protein: histidine kinase (EC 2.7.13.3) (Q9HWI4)
Organism: Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Interaction partners:
- BfiR
- histidine kinase
- histidine kinase
- histidine kinase
- MifR
- histidine kinase
- histidine kinase
- histidine kinase
- BfmR
- histidine kinase
Sequence:
MSPLPASPALNSLLRLLREGAPLVERVGALRRLLLEHPGTRQAWYLAWQPQAQTYTPVPPSPALPPGAGEPNRASDLALRERLVRDGRLALDELRRSASWLGARLRRAGVEHGMAFALDLQAGDEGLLLVASDTPQSAALDWLGLLLAPLLAAARGVTRAAPFLAADPQPALLLDGEAQAVELNQAFLALLGERPREAWRAYLPANHGQLVRASLGQARALGEVEAECDGRILLWQFIPDSAEARVLARCRDATASLRGEREAARASRLYRLITENTTDLISRHTLDGIFLDASPASWTLLGYWPEELRGRPAQALFHPQDRGQVALRAREALEQDGYLTITYRIRHRDGRYRWFETASRAIRETYTGAVVEVVSVSRDVTRRVEAEENRRRLAEVVEANTDLVLFVEHGGRVTYLNPSARAALGIADGQEAPALERLLAGDTPARLAEEGWRQARDGGVWSREGRLQPQDGRPSLPVSLVLLAHRGRGEERYYSLVARDMTERELREAQQRRHQDELAHTARLVTLGELASGIAHEINQPLAAVMNYASTSQRYLAVLGSQPEAAGRVAEGLARIGEHAGHAAEVIKRLRAFLRKGQRRLQALDLNQVAREAIGLCAWEAGHWQVAVEEAMTDNPPPLYADRVLLEQVFLNLLRNAIEANREAHPGSPSRVVIGSRVEPGGLLCLWVRDQGPGVPADQLEHIFTPFHTSKPEGLGLGLSMSRSIVEGFGGTLEAELPADGGLLMNCRLPLAAGATGG
Protein: Multidrug resistance-associated protein 5 (ATP-binding cassette sub-family C member mrp-5) (G5EE72)
Organism: Caenorhabditis elegans
Function: Heme transporter required for the export of intestinal heme to different tissues and subcellular compartments. Also, required for the export of vitamin B12 from the intestine of the mother to the embryo to support embryonic development.
Subcellular location: Basolateral cell membrane {ECO:0000269|PubMed:24836561}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Heme transporter hrg-1
- Heme transporter hrg-4
- Mitochondrial cytochrome c oxidase subunit VIa
- GST_C_6 domain-containing protein
- VWFA domain-containing protein
- ABC transporter domain-containing protein
- CC domain-containing protein
- Mitochondrial scaffolding protein 1
Sequence:
MPSDSEEVCLQQSGTGVYENVVYSKETSDRAKRYAGDTNRKTIGRYSAAVQNLIPLRTTERNKNNGGSRIDDAGLFSFVTYSWVFPYLYQAVRGKLDRNQVWGCSFYDSCGLNMARLEVLWEDEKKANAKSPSLFKVIYRFISTRLWFSCAVFFFCLIFGFIGPTCFIRRLIAFAENPERDEQSRIVYSYGIALVAAISVVEFARVLSYGATWAVSYRTGIRVRGAVLALLYKNVLNSKDLCGKTESDVINIFANDGQRLFDAVTFAPLVLVGPLVLVGGIGYLLMVIGRWSLLGILVFFVFDVIQFGLGKSMVACRNLAIVKTEKRISMMAEIIKYIRIVKMNGWEQIFSAKIDQFRKEEKVQIRKSGYAQSLAIACGPVVPVVAAILTFVGVVLAGNDLLASDAFSAITVYFVMLFGIRMIPYGSRYLAEAVVAMRRIQEYLLLEQYAPYPVTNAEDVVLDCQGATYTYQPKAAKAPVDETKEPTENEVIVVETPVFTCSFDKLSIKRGEHIAVIGAVGCGKSAILKAISGHMFTTDDALSVDRSQTVYVPQKAWIFNGTVQDNILFGDKMNSERYYKAVNGCQLTEDLTTLSVGDRTEVGERGATLSGGQKARVALARAVFQTKNLYLFDDIFASLDKKVANKIHEEIIQKLLKKKALMMVTNNMELLHHFDRVLFVEGGNIVADGNHDILYEKNDAYKTFVDACETYQATSGATSPCGDGPAQPAPLDAEILRNSSEDLKGDADKLISDEEDMGNSTIAWRIYKQYIHAAGGWPIWTCLVIGFIVNVVSNIFSTYWLSRWLKKGHDETTTITNGTEFLEMKTSLADSPVTGFYAAVYLVALVVLTISGLFKACVFVKVSLTAATRLHDRMFQAVIHGATSFFDSTPTGRILNRFSKDMDEIDVKLPFTAEVFLQNMITCLGFLVVITSVFPYFLLFAIPLFVVFVVFVSCFRAGIRNLKRSEHISRSPLYDHVSASLEGITTIHTFQQSNRFLEVLKKHLDCNSGAIFMFQSAMRWLAVWLDLLVVVMTAIVALLTVMLTGTVSPADAGMAIAFAVQMSGIFQFAVRTQTELEAKMTSVERVSYYADNIPEDGEWNTRQGLDIESSWPANGQINFSEVNLRYRKSHPLALNDITFEIKGGEKVGIIGRTGSGKSSLANLIFRLYPVTNGTIYIDGVDIRTVGLVKLRRGISAIAQDPSLFSGTVRFNLDPSLEYSDSMIWEALEKCHLKTLVQSLDKKLEADVSHGGNNFSVGERQLFCLARALLMKSRIVILDEATASVDAGTDKLIQEVIKTVFADATVIIIAHRLDNVRNMDRIMHLKNGKLINFTTPQEMFKDDWSVYKLEDKDDDQHSAVVVGENSEHSMEKSSQGSSQESDDIVKVENEQKDSSDDVVHIESGDDDVKADSSEVKETSSDTDIEVVQ
Protein: Cyclin-dependent kinase inhibitor 1B (Cyclin-dependent kinase inhibitor p27) (p27Kip1) (Q6I9V6)
Organism: Homo sapiens (Human)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}. Endosome {ECO:0000256|ARBA:ARBA00004177}. Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MSNVRVSNGSPSLERMDARQAEHPKPSACRNLFGPVDHEELTRDLEKHCRDMEEASQRKWNFDFQNHKPLEGKYEWQEVEKGSLPEFYYRPPRPPKGACKVPAQESQDVSGSRPAAPLIGAPANSEDTHLVDPKTDPSDSQTGLAEQCAGIRKRPATDDSSTQNKRANRTEENVSDGSPNAGSVEQTPKKPGLRRRQT
Protein: Exported virulence protein (Q7D2D9)
Organism: Agrobacterium fabrum (strain C58 / ATCC 33970) (Agrobacterium tumefaciens (strain C58))
Interaction partners:
Sequence:
MEPSQRSLSDESEASRTEVHSTSTNRDMPPELLAKVATYIPTQDPVETARNLGSLERTGRAGREAVTSDPVGKYHARMKRIGASAKTVFDTVIPGNQLPEWETNRPSPTARTRAVGPILKFQSEAGKSRFVTNILNLPESAQCDAILSVIKHLNDLGEANKTRLIERSIEILRLEPPLTWNMGQKCPAVDVLVQGEKYLNADQLARIQQERSSRPRLSPLFGRAIADFEVQKTMDANPRRYRDAAGPEVRAVDTVIETIERYSASLARGGPNAVGLLTTNESFEKNINEVYNRTRAELDASSRDRSRSGLSR
Protein: Replication factor C subunit 3 (SD11293p) (Q9VKW3)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- Replication factor C subunit 2
- Replication factor C subunit 2
- Replication factor C subunit 3
- Replication factor C subunit 1
- Rad17
- Enhanced level of genomic instability 1
- Chromosome transmission fidelity protein 18 homolog
- Proliferating cell nuclear antigen
- DNA repair protein Rad1
- Cell cycle checkpoint control protein Rad9
Sequence:
MSETSGPAVRMPWVEKYRPSGLDDLISHEEIISTITRFISRKQLPHLLFYGPPGTGKTSTILACARQLYSPQQFKSMVLELNASDDRGIGIVRGQILNFASTRTIFCDTFKLIILDEADAMTNDAQNALRRIIEKYTDNVRFCVICNYLSKIIPALQSRCTRFRFAPLSQDQMMPRLEKIIEAEAVQITEDGKRALLTLAKGDMRKVLNVLQSTVMAFDTVNEDNVYMCVGYPLRQDIEQILKALLSGSSLEDSFKTVESAKYARGLALEDIITELHLFVMRLELPMSVMNKLIVKLAQIEERLAKGCTEVAQTAALVAAFFICRDMVSMEK
Protein: DNA damage-inducible protein 1 (EC 3.4.23.-) (v-SNARE-master 1) (P40087)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Aspartic protease. Appears to act as negative regulator of constitutive exocytosis. May act at the level of secretory vesicle docking and fusion as a competitive inhibitor of SNARE assembly. Acts as a linker between the 19S proteasome and polyubiquitinated proteins like the HO endonuclease and UFO1 via UBA domain interactions with ubiquitin for their subsequent degradation. Required for S-phase checkpoint control.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:10330187}. Cell membrane {ECO:0000269|PubMed:10330187}; Peripheral membrane protein {ECO:0000269|PubMed:10330187}; Cytoplasmic side {ECO:0000269|PubMed:10330187}.
Interaction partners:
- Mitotic check point protein BUB2
- Polyubiquitin
- UV excision repair protein RAD23
- Ubiquitin-ribosomal protein eL40A fusion protein
- 26S proteasome regulatory subunit RPN1
- Ubiquitin domain-containing protein DSK2
- 26S proteasome regulatory subunit RPN10
- Ubiquitin-ribosomal protein eS31 fusion protein
- Ubiquitin carboxyl-terminal hydrolase RPN11
- Ubiquitin ligase complex F-box protein UFO1
Sequence:
MDLTISNELTGEIYGPIEVSEDMALTDLIALLQADCGFDKTKHDLYYNMDILDSNRTQSLKELGLKTDDLLLIRGKISNSIQTDAATLSDEAFIEQFRQELLNNQMLRSQLILQIPGLNDLVNDPLLFRERLGPLILQRRYGGYNTAMNPFGIPQDEYTRLMANPDDPDNKKRIAELLDQQAIDEQLRNAIEYTPEMFTQVPMLYINIEINNYPVKAFVDTGAQTTIMSTRLAKKTGLSRMIDKRFIGEARGVGTGKIIGRIHQAQVKIETQYIPCSFTVLDTDIDVLIGLDMLKRHLACVDLKENVLRIAEVETSFLSEAEIPKSFQEGLPAPTSVTTSSDKPLTPTKTSSTLPPQPGAVPALAPRTGMGPTPTGRSTAGATTATGRTFPEQTIKQLMDLGFPRDAVVKALKQTNGNAEFAASLLFQ
Protein: Replicase polyprotein [Cleaved into: Protein 1A (CrPV-1A); Protein 2A; Protein 2B; Protein 2C; Protein 3A; Protein 3B; 3C-like protease (EC 3.4.22.-); RNA-directed RNA polymerase 3D-POL (EC 2.7.7.48)] (Q9IJX4)
Organism: Cricket paralysis virus (isolate Teleogryllus commodus/Australia/CrPVVIC/1968) (CrPV)
Function: Protein 1A functions as a suppressor of RNA-mediated gene silencing, an antiviral defense mechanism of insect cells. Inhibits siRNA function, but does not interfere with miRNA pathway. Does not bind to dsRNA or siRNA.
Subcellular location: Host cytoplasm, host perinuclear region {ECO:0000269|PubMed:28003491}.
Interaction partners:
Sequence:
MSFQQTNNNATNNINSLEELAAQELIAAQFEGNLDGFFCTFYVQSKPQLLDLESECYCMDDFDCGCDRIKREEELRKLIFLTSDVYGYNFEEWKGLVWKFVQNYCPEHRYGSTFGNGLLIVSPRFFMDHLDWFQQWKLVSSNDECRAFLRKRTQLLMSGDVESNPGPVQSRPVYACDNDPRAIRLEKALQRRDEKISTLIKKLRQEIKNNRIYTQGFFDDLKGAKGEVGQLNGNLTRICDFLENSLPTLTAQIQTTVLTTTDKYVNLKEDLLKVAILLVLVRLLMVWKKYRAALIVIILFVMHFYGFDKQILDIVLDLKDKILQTTTQAGTETLEEVVYHPWFDTCGKLIFAVLAFFAIKKIPGKQDWDNYISRLDRIPKAIEGSKKIVDYCSEYFNLSVDEVKKVVLGKELKGTQGLYDEIHVWAKEIRHYLDLDERNKITLDTETAAKVEDLYKRGLKYSEEKIPDRDIARFITTMLFPAKSLYEQVLLSPVKGGGPKMRPITVWLTGESGIGKTQMIYPLCIDILREMGIVKPDAYKHQAYARQVETEYWDGYNGQKIVIYDDAFQLKDDKTKPNPEIFEVIRTCNTFPQHLHMAALQDKNMYSQAEVLLYTTNQFQVQLESITFPDAFYNRMKTHAYRVQIKQEKSIWVRNARGEEYNALDVTKLNKDEAIDLSVYEFQKMRFDDESATKWIDDGEPISYDEFARTICKAWKEEKEKTFHQLQWLEAYASRTVAQGGSETSEYYDVWDETYFSNLLSQGFMAGKSLIEMEAEFASDAETFNAYIEYKKNIPKETKWSKWMTILDEQISALSTKIRELKNKAYKFISEHPYLTALGFIGVMISAFAMYSFFERTLTDDTITSEVGSSGDNKTQKISKRVVEVGGSGDVKTTKPAKTAVEVGSSGDSKTMKNKITKVEVGSSGDSKTQKQRNTKVEVGKELEKEAETQGCSDPAAHALVLDVLQKNTYCLYYERMVKGEMKRYRLATATFLRGWVCMMPYHFIETLYARKVAPSTNIYFSQPNCDDVIVVPVSHFIAPNAERVELTTACTRIHYKDETPRDCVLVNLHRRMCHPHRDILKHFVKKSDQGNLRGVFQGTLATFHQSANELCRAYQWLQAIRPLDQEITIYHEDTDMFDYESESYTQRDCYEYNAPTQTGNCGSIVGLYNKRMERKLIGMHIPGNVSECHGYACPLTQEAIMDGLNRLEKLDPVNNITVQCCFEPPSDIKDTMSGETPEGKFCAIGKSNIKVGQAVKTTLLKSCIYGMLSKPITKPAHLTRTRLPNGEIVDPLMKGLKKCGVDTAVLDAEIVESAALDVKQVVLTQYNSMLDVNKYRRFLTYEEATQGTGDDDFMKGIARQTSPGYRYFQMPRKLPGKQDWMGSGEQYDFTSQRAQELRRDVEELIDNCAKGIIKDVVFVDTLKDERRPIEKVDAGKTRVFSAGPQHFVVAFRKYFLPFAAYLMNNRIDNEIAVGTNVYSTDWERIAKRLKKHGNKVIAGDFGNFDGSLVAQFFGQSCGKSFYPWFKTFNDVNTEDGKRNLMICIGLWTHIVHSVHSYGDNVYMWTHSQPSGNPFTVIINCLYNSMIMRIVWILLARKLAPEMQSMKKFRENVSMISYGDDNCLNISDRVVEWFNQITISEQMKEIKHEYTDEGKTGDMVKFPSLSEIHFLKKRFVFSHQLQRTVAPLQKDVIYEMLNWTRNTIDPNEILMMNINTAFREIVYHGKSEYQKLRSGIEDLAMKGILPQQPQILTFKAYLWDATMLADEVYDF
Protein: MIP27703p (Zinc-finger protein at 72D, isoform E) (F0JAG2)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MANNNYAGFNYGGTQYNTGQVSYPAVTNATYANAAAYQNAAVAAGQGGYGGAAGAGAGATSGPGAGGYGGYGDYRSAMQYDATKTFYQQSPASYNASGSTASVSKTHYSAPPVKNQVKGKMDKSNGGPKPPSSAPPAGNNYSGYDTALYNAASMYVAQQHQGNPNQKPNGGANNWYQRKMGATIPGATAIRGMRPKAPPRPQQLHYCEVCKISCAGPQTYREHLEGQKHKKREASLKMSASANSATQNRGNNYHCELCDVTCTGTDAYAAHVRGAKHQKVVKLHQKLGKPIPSEEPKKMGKINFVPAAAGGAGVAKTEGGANESDAAGDLDDNLDDSLGENTDNIKPVGGEYIEEVKDEEGKILSFNCKLCDCKFNDPNAKEMHMKGRRHRLQYKRKVQPDLVVDFKPTPRQRRLAEARANRAMMSSHRGGDDHDGGYWEEQRNRQYNEEYDYNNWMSRSFGGAQRFGRMGNGPPPHFGMMPGGNVRRPESTDDRHAIARHAEIYPKEEELQTIQRIVSHTERALKLVSDALAEQPSDAGAANKKDKAEKPSEKDGRDNQIFSFQKDADNGGNVVRILKGVMRVGYLAKGLLLHGDNAVELVVLCAEKPTSGLLQRVANVLPDKLKEVAGK