wanglab/gogpt-training-data huggingface dataset:
Protein: Transmembrane protein 108 (Retrolinkin) (Q6UXF1)
Organism: Homo sapiens (Human)
Function: Transmembrane protein required for proper cognitive functions. Involved in the development of dentate gyrus (DG) neuron circuitry, is necessary for AMPA receptors surface expression and proper excitatory postsynaptic currents of DG granule neurons. Regulates the organization and stability of the microtubule network of sensory neurons to allow axonal transport. Through the interaction with DST, mediates the docking of the dynein/dynactin motor complex to vesicle cargos for retrograde axonal transport. In hippocampal neurons, required for BDNF-dependent dendrite outgrowth. Cooperates with SH3GL2 and recruits the WAVE1 complex to facilitate actin-dependent BDNF:NTRK2 early endocytic trafficking and mediate signaling from early endosomes.
Subcellular location: Membrane {ECO:0000250|UniProtKB:Q8BHE4}; Multi-pass membrane protein {ECO:0000255}. Postsynaptic density {ECO:0000250|UniProtKB:Q8BHE4}. Endosome membrane {ECO:0000250|UniProtKB:Q8BHE4}. Cell projection, axon {ECO:0000250|UniProtKB:Q8BHE4}. Cell projection, dendrite {ECO:0000250|UniProtKB:Q8BHE4}. Early endosome {ECO:0000250|UniProtKB:Q8BHE4}.
Interaction partners:
- Endophilin-A1
Sequence:
MKRSLQALYCQLLSFLLILALTEALAFAIQEPSPRESLQVLPSGTPPGTMVTAPHSSTRHTSVVMLTPNPDGPPSQAAAPMATPTPRAEGHPPTHTISTIAATVTAPHSESSLSTGPAPAAMATTSSKPEGRPRGQAAPTILLTKPPGATSRPTTAPPRTTTRRPPRPPGSSRKGAGNSSRPVPPAPGGHSRSKEGQRGRNPSSTPLGQKRPLGKIFQIYKGNFTGSVEPEPSTLTPRTPLWGYSSSPQPQTVAATTVPSNTSWAPTTTSLGPAKDKPGLRRAAQGGGSTFTSQGGTPDATAASGAPVSPQAAPVPSQRPHHGDPQDGPSHSDSWLTVTPGTSRPLSTSSGVFTAATGPTPAAFDTSVSAPSQGIPQGASTTPQAPTHPSRVSESTISGAKEETVATLTMTDRVPSPLSTVVSTATGNFLNRLVPAGTWKPGTAGNISHVAEGDKPQHRATICLSKMDIAWVILAISVPISSCSVLLTVCCMKRKKKTANPENNLSYWNNTITMDYFNRHAVELPREIQSLETSEDQLSEPRSPANGDYRDTGMVLVNPFCQETLFVGNDQVSEI
Protein: Initiation-specific alpha-1,6-mannosyltransferase (EC 2.4.1.232) (Q9UTR6)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Mannosyltransferase involved in outer chain elongation of asparagine-linked oligosaccharides of the type Man(9)GlcNAc(2). May otherwise add the first alpha-1,6-mannose to the Man(8)GlcNAc(2) core oligosaccharide from the ER. Represents the first enzymatic event required for synthesis of outer chain mannose linkages on yeast secretory proteins.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P31755}; Single-pass type II membrane protein {ECO:0000250|UniProtKB:P31755}. Golgi apparatus membrane {ECO:0000250|UniProtKB:P31755}; Single-pass type II membrane protein {ECO:0000250|UniProtKB:P31755}. Note=Is recycled between the trans-Golgi network and a late compartment of the endoplasmic reticulum. {ECO:0000250|UniProtKB:P31755}.
Interaction partners:
- Mannan polymerase complex subunit mnn9
- Dol-P-Man:Man
- Mannan polymerase II complex anp1 subunit
- Alpha-1,2-galactosyltransferase
- Inositol phosphoceramide mannosyltransferase 2
- Dolichol-phosphate mannosyltransferase
- Dolichol-phosphate mannosyltransferase subunit 3
- Dolichol phosphate-mannose biosynthesis regulatory protein
Sequence:
MLRLRLRSIVIGAAIAGSILLLFNHGSIEGMEDLTEISMLEDYTPEAANKDYVGQQEEEELLYDQPSYIEEEEDPDLEAYLSDLEREELEHSLEELDEENNYKLHLRYSFSQLQDFDEENEAVHMIVPKDTYEFEVPYHADIPKLIWQTSKDPFDREVMKYTRFWRINHPSYSHAVLDDEQSKALVISSFGDSSVSKISQAYAMMPLPVLKADFFRYLVLLAKGGIYSDIDTAPLKHINNWIPREYRKRNIRLIVGIEADPDRPDWNDYYARRVQFCQWTIAAAPGHPILWELVRRITDETWKLHDSKKLSKNGESVMEWTGPGIWTDAIMDYLNWQYGPFSVENITNLEEPYLVGDVLILPITAFSPGVGHMGSKSPNDPMAYVQHFFAGSWKDD
Protein: FI02019p (Uncharacterized protein, isoform A) (Uncharacterized protein, isoform B) (Uncharacterized protein, isoform C (EC 1.-.-.-, EC 1.1.-.-)) (Q9VY08)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- alkaline phosphatase
Sequence:
MVLNLLFITTVIKSTFGVVTTGLWLIPLMLAAITYYRYDAVDPESRPLDQLNLYPEYDFIVVGSGSAGAVVANRLSEVRKWKVLLIEAGPDENEISDVPSLAAYLQLSKLDWAYKTEPSTKACLGMQNNRCNWPRGRVLGGSSVLNYMLYVRGNRHDYDHWASLGNPGWDYDNVLRYFKKSEDNRNPYLANNKYHGRGGLLTVQESPWHSPLVAAFVEAGTQLGYDNRDINGAKQAGFMIAQGTIRRGSRCSTAKAFLRPIRMRKNFHLSMNSHVTRVIIEPGTMRAQAVEFVKHGKVYRIAARREVIISAGAINTPQLMMLSGLGPRKHLEKHGIRVLQDLPVGENMQDHVGMGGLTFLVDKPVAIVQDRFNPTAVTFQYVLRERGPMTTLGGVEGLAFVHTPYSNRSLDWPDIQFHMAPASINSDNGARVKKVLGLKESVYQEVYHPIANKDSWTIMPLLLRPRSRGSVKLRSANPFHYPLINANYFDDPLDAKTLVEGAKIALRVAEAQVFKQFGSRLWRKPLPNCKQHKFLSDAYLECHVRTISMTIYHPCGTAKMGPAWDPEAVVDPRLRVYGVRGLRVIDASIMPTISSGNTNAPVIMIAEKGADLIKEDWLTNPEYKVKRQANRLRDPDPASSNIQGIITLPNNITQGDSSNISDRSNMESNFSNSSHINNINFNSNSNSSNIESSSNFTLNYANS
Protein: FI14740p (Ravus) (Q9VFX8)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Nucleus {ECO:0000256|PROSITE-ProRule:PRU00371}.
Interaction partners:
Sequence:
MSNLQLTQEKLDALRSEYRPRRPCALLKYPRPKTKPEYQAIYPWLLPDETDPHFVFCAVCECRLSCKRSDLGKHEGSIKHSENAQRKSLPAKANNSSFNGSSSGAMKWEDTEDEEGLLQYGTDPQDDETEDEEEGELDETEGDCEDDEKRTQELEAQNDLETEPVIKQQRRTSETDSQNSGMLDYLPLHVTINEGPQSLPTTVSAYPTSSATATVAPPCRITIKKVPVHSTPLSGMCQAQEINSKATITPIHTTPSYAARPLQSYQLQPLSPITPPRDSLELFFDSICATVKNLPPKLATEGKIRVMQLIGELELRALCEQEALSEVAGLPDLAGNSRSGAAEASGSGQQNATVASTTK
Protein: Ovotransferrin (Allergen Gal d III) (Conalbumin) (Serum transferrin) (allergen Gal d 3) (P02789)
Organism: Gallus gallus (Chicken)
Function: Transferrins are iron binding transport proteins which can bind two Fe(3+) ions in association with the binding of an anion, usually bicarbonate. Responsible for the transport of iron from sites of absorption and heme degradation to those of storage and utilization. There are two forms of hen transferrin, ovotransferrin, found in the ovoducts and, serum transferrin, secreted by the liver. Serum transferrin may also have a role in stimulating cell proliferation and is regulated by iron levels. Ovotransferrin has a bacteriostatic function and, is not controlled by iron levels.
Subcellular location: Secreted.
Interaction partners:
- Ovalbumin
- Ovomucoid
- Transferrin receptor protein 1
- Ovomucoid
- Lysozyme C
- Ovoinhibitor
- Albumin
- Alpha-1-acid glycoprotein
- Ovocalyxin-32
- Ovostatin
Sequence:
MKLILCTVLSLGIAAVCFAAPPKSVIRWCTISSPEEKKCNNLRDLTQQERISLTCVQKATYLDCIKAIANNEADAISLDGGQAFEAGLAPYKLKPIAAEVYEHTEGSTTSYYAVAVVKKGTEFTVNDLQGKTSCHTGLGRSAGWNIPIGTLLHRGAIEWEGIESGSVEQAVAKFFSASCVPGATIEQKLCRQCKGDPKTKCARNAPYSGYSGAFHCLKDGKGDVAFVKHTTVNENAPDQKDEYELLCLDGSRQPVDNYKTCNWARVAAHAVVARDDNKVEDIWSFLSKAQSDFGVDTKSDFHLFGPPGKKDPVLKDLLFKDSAIMLKRVPSLMDSQLYLGFEYYSAIQSMRKDQLTPSPRENRIQWCAVGKDEKSKCDRWSVVSNGDVECTVVDETKDCIIKIMKGEADAVALDGGLVYTAGVCGLVPVMAERYDDESQCSKTDERPASYFAVAVARKDSNVNWNNLKGKKSCHTAVGRTAGWVIPMGLIHNRTGTCNFDEYFSEGCAPGSPPNSRLCQLCQGSGGIPPEKCVASSHEKYFGYTGALRCLVEKGDVAFIQHSTVEENTGGKNKADWAKNLQMDDFELLCTDGRRANVMDYRECNLAEVPTHAVVVRPEKANKIRDLLERQEKRFGVNGSEKSKFMMFESQNKDLLFKDLTKCLFKVREGTTYKEFLGDKFYTVISSLKTCNPSDILQMCSFLEGK
Protein: Tubulin tyrosine ligase like 5 (G3V4R8)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MNYMLATRLFQDRGNPRRSLLTGRTRMTADGAPELKIESLNSKAKLHAALYERKLLSLEVRKRRRRSSRLRAMRPKYPVITQPAEMNVKTETESEEEEEVALDNEDEEQEASQEESAGFLRENQAKYTPSLTALVENTPKENSMKVREWNNKGGHCCKLETQELEPKFNLMQILQDNGNLSKMQARIAFSAYLQHVQIRLMKDSGGQTFSASWAAKEDEQMELVVRFLKRASNNLQHSLRMVLPSRRLALLERRRILAHQLGDFIIVYNKETEQMAEKKSKKKVEEEEEDGVNMENFQEFIRQASEAELEEVLTFYTQKNKSASVFLGTHSKISKNNNNYSDSGAKGDHPETIMEEVKIKPPKQQQTTEIHSDKLSRFTTSAEKEAKLVYSNSSSGPTATLQKIPNTHLSSVTTSDLSPGPCHHSSLSQIPSAIPSMPHQPTILLNTVSASASPCLHPGAQNIPSPTGLPRCRSGSHTIGPFSSFQSAAHIYSQKLSRPSSAKAGSCYLNKHHSGIAKTQKEGEDASLYSKRYNQSMVTAELQRLAEKQAARQYSPSSHINLLTQQVTNLNLATGIINRSSASAPPTLRPIISPSGPTWSTQSDPQAPENHSSSPGSRSLQTGGFAWEGEVENNVYSQATGVVPQHKYHPTAGSYQLQFALQQLEQQKLQSRQLLDQSRARHQAIFGSQTLPNSNLWTMNNGAGCRISSATASGQKPTTLPQKVVPPPSSCASLVPKPPPNHEQVLRRATSQKASNTRFRSSFQNYLWYFFQAVS
Protein: Large ribosomal subunit protein mL67 (Cross-linked transcription component 1) (Mitochondrial homologous recombination protein 1) (Q06630)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Component of the mitochondrial ribosome (mitoribosome), a dedicated translation machinery responsible for the synthesis of mitochondrial genome-encoded proteins, including at least some of the essential transmembrane subunits of the mitochondrial respiratory chain. The mitoribosomes are attached to the mitochondrial inner membrane and translation products are cotranslationally integrated into the membrane. mL67/MHR1 also has extraribosomal functions, being involved in regulation of mitochondrial DNA recombination, maintenance and repair, and generation of homoplasmic cells. mL67/MHR1 also acts as transcription factor involved in regulation of RNA polymerase II-dependent transcription.
Subcellular location: Nucleus {ECO:0000269|PubMed:12034822}. Mitochondrion {ECO:0000269|PubMed:12034822, ECO:0000269|PubMed:12198175, ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:14576278}. Note=Mitoribosomes are tethered to the mitochondrial inner membrane and spatially aligned with the membrane insertion machinery through two distinct membrane contact sites, formed by the 21S rRNA expansion segment 96-ES1 and the inner membrane protein MBA1. {ECO:0000269|PubMed:25609543}.
Interaction partners:
- Large ribosomal subunit protein mL43
- Large ribosomal subunit protein mL49
- Large ribosomal subunit protein uL3m
- Large ribosomal subunit protein bL19m
- Large ribosomal subunit protein uL16m
- Large ribosomal subunit protein mL57
- Large ribosomal subunit protein uL29m
- Large ribosomal subunit protein mL58
- Large ribosomal subunit protein uL15m
- Large ribosomal subunit protein mL40
Sequence:
MKVNHSISRFRPASWFEKTKIIPPQVYIFRNLEYGQVLYSQFPNFSQTQVDKLFVRPNWSNRKPSLRRDIWKCMCVVNLQNYKQSVHLYQNLCRLRYLRDVAQRKESDKLRKKDSNGHVWYSGQYRPTYCQEAVADLRESLLKVFENATPAEKQTVPAKKPSIYWEDPWRMGDKDKHWNYDVFNALGLEHKLIQRVGNIAREESVILKELAKLESHPTEQTEVSSQ
Protein: Astrocytic phosphoprotein PEA-15 (15 kDa phosphoprotein enriched in astrocytes) (Q62048)
Organism: Mus musculus (Mouse)
Function: Blocks Ras-mediated inhibition of integrin activation and modulates the ERK MAP kinase cascade. Inhibits RPS6KA3 activities by retaining it in the cytoplasm. Inhibits both TNFRSF6- and TNFRSF1A-mediated CASP8 activity and apoptosis. Regulates glucose transport by controlling both the content of SLC2A1 glucose transporters on the plasma membrane and the insulin-dependent trafficking of SLC2A4 from the cell interior to the surface (By similarity).
Subcellular location: Cytoplasm {ECO:0000269|PubMed:10926929}. Note=Associated with microtubules.
Interaction partners:
- Mitogen-activated protein kinase 1
- Mitogen-activated protein kinase 3
- FAS-associated death domain protein
Sequence:
MAEYGTLLQDLTNNITLEDLEQLKSACKEDIPSEKSEEITTGSAWFSFLESHNKLDKDNLSYIEHIFEISRRPDLLTMVVDYRTRVLKISEEEELDTKLTRIPSAKKYKDIIRQPSEEEIIKLAPPPKKA
Protein: FANCD2 (Q9U2H4)
Organism: Caenorhabditis elegans
Interaction partners:
- FANCI helical domain-containing protein
- Fanconi-associated nuclease 1 homolog
- Breast cancer type 1 susceptibility protein homolog
- DNA repair protein RAD51 homolog
- DNA repair endonuclease XPF
- Large ribosomal subunit protein uL1
- FANCM homolog
- Centromere protein X
- Crossover junction endonuclease MUS81
- RAD51-like protein 1
Sequence:
MSDEEFDILDDENSHVAASQHVEDDDPDDRHNSGNRRNFSMAMTQKLFGNLDGAGAENHVSYAENAYVTPRNRFEEILKEENVRIVNDQDEGMMDMEMGSYEKCVVFGNNLNSEDLCRNLEKRMENDRGETFAEFLLACGSDQDMLALFLSPAKSLFGLQDTIFRAFLQIKATQTKAFDFLLQKLNILAKRQDERDLLLAQTCVAHMRHLSRLFEPQAVFNTIFEFQWRFWSPNVRNDLIAALPEIFTDISLQQSTAVRLHKECSETQGVPGLPSFQLQIIETLRLLRMDPGTARKIRMDLCNLCMDLDPACLPSLVAFSLGSLLVFQGKADDEEAHFHEMLRQLARLLKIDGLKKKTSKPSSDSLIVEVFGHFLKFFRLNDKRAWKHITTWISKSKKPVVATKPEEDMDSEETPSPPEEESATWLTTFEAFLYFSLLSNTESCPPTFVAAVNSKILNIPAAFTTKFLRIIDLVISCKKFATCHLPALIHVARHCFWSSDGNVRQMGVSMWKQLFVGMEKRDREKVFTELMKHFSQSETECEAVLDVFFKVIKSTNSSVIQEFSTQIQKCIELIHKLSIPNIKRLFQVMLMMPSKSTEKEATRFEIDEIISRFLLSVSDREKFLGLLALLMKIQVEMGKKHSENQEHLVREGISRCEEAVKSSSALRGAFYEHMRIVLQQHKRTEEIRFLSDWSTDLLKRFKNDFFELPPNPESNTDPDSQSTWNLKLNSARLLEIAPMFELIKEIQVLKMRWREEDQDSLTSSYDISVIKNLSFAFEAVLPKDENLPLNRQEKLAQLFFNVQWTRTVLNGFLSQSSVDFLSSDDVSTLSIKNFYVMMDAEKKLAASLVDLATWNVPNLNFGRSGKRDVIVISSEKTKSKKGRKRKSDETTVIGGDGQTNSADVTVNDDDREENLEAEVVKEAPSVLLQLKSHYIPLKLRPIVHLMKLANKKRSALKYLCDELQSVIDTLIKQKKKTPPMLLAARRAAAPTTPNSSKFYHGDSVTIWFCVKKAVEQVWGIVELVFGVFAEQSDASQELKSRVQKDMDDLGEKSLNLIHSILSGELYGGEEKLSPAERVERKSVLIRIIEKKMLSSEHLSNDSEKARVEIGKFLAKSAEFSPTPAVAVAILDVFEDLKLDEDDDAETRKIMAKYALAYLKKDWSKVDELWSKGTRYTCAVRDILHHYIRLRKEKDQLLAIQWILTNKVVQLVPEDDKRKSCVFSQQSDDDLLEKEDRKATFYCISKTTFGVIFKTLFGNLNSRCLKYDMSASAAKNGGVDIEDTLESWETASSCFLILCLLLRINKIRTTAVLTSAIKEGKQFLITVSKKSSFIFLMDNITKGTNFDTICRRVEKILSAVQQGNRVLQSIGTFAKTNKCVLLLKKFPELRAESENCLRVIHSAMVKNECLNAFTVGLVKSRSIDGDIIMDQRASEIDSDSE
Protein: Axoneme-associated protein mst101(2) (Q08696)
Organism: Drosophila hydei (Fruit fly)
Function: Possible structural role in the sperm tail.
Subcellular location: Cytoplasm.
Interaction partners:
Sequence:
MSLCRCSSICLRRPILRSFNFLNKYIDQSQHSGGLSSFQRLSFSNTGKNESTDDSNQIRCDADKTAADKKKQKQKEEEQAKIREYKRECLKVQKRVLAEEIRCSGEKDRILIQGMMKCLTDGMKKACTKIAKAKLIADKELAVQCAALSKKDKVKALLKKCEREKSKEKECNQNSPAEGDKDRTKKGKTKGKSGGGNKKRSTKENRAKKGKKLVKNRFTQKLEHCIKSEWADVCECRQNFTEDERKRLAASYKCMGTKIKSICRKRVIAEMCEAAGYVKSSEPKKKGKKKKNDEKKEKELEREILKEQAEEEAKIRGVVKEVKKKCKEKALKKKCKDLGRKMKEEAEKKKCAALAKKQKEEDEKKACKELAKKKKEADEKKKCEEAANKEKKAAEKKKCEKAAKERKEAAEKKKCEEAAKKEKEAAERKKCEELAKNIKKAAEKKKCKEAAKKEKEAAERKKCEELAKKIKKAAEKKKCEETAKKGKEVAERKKCEELAKKIKKAEIKKKCKKLAKKEKETAEKKKCEKAAKKRKEAAEKKKCEKAAKKRKEAAEKKKCEKSAKKRKEAAEKKKCEKAAKERKEAAEKKKCEEAAKKEKEVAERKKCEELAKKIKKAAEKKKCKEAAKKEKEAAEREKCGELAKKIKKAAEKKKCKKLAKKEKETAEKKKCEKAAKKRKEAAEKKKCAEAAKKEKEAAEKKKCEEAAKKEKEAAERKKCEELAKKIKKAAEKKKCKKLAKKKKAGEKNKLKKGNKKGKKALKEKKKCRELAKKKAAEKKKCKEAAKKEKEAAEKKKCEKTAKKRKEEAEKKKCEKTAKKRKEAAEKKKCEKAAKKRKEEAEKKKCEKTAKKRKETAEKKKCEKAAKKRKQAAEKKKCEKAAKKRKEAAEKKKCAEAAKKEKELAEKKKCEEAAKKEKEVAERKKCEELAKKIKKAAEKKKCKKLAKKEKKAGEKNKLKKKAGKGKKKCKKLGKKSKRAAEKKKCAEAAKKEKEAATKKKCEERAKKQKEAAEKKQCEERAKKLKEAAEQKQCEERAKKLKEAAEKKQCEERAKKLKEAAEQKQCEERAKKLKEAAEKKQCEERAKKEKEAAEKKQCEERAKKLKEAAEKKQCEERAKKEKEAAEKKRCEEAAKREKEAAEKKKCAEAAKKEKEATEKQKCAEAAKKEKEAAEKKKCAEAAKREKEAAQKKKCADLAKKEQEPAEMKKCEEAAKKEKEAAEKQKCAKAAKKEKEAAEKKKCAEAAKKEQEAAEKKKCAEAAKKEKEAEKKRKCEKAEKAAALKRQCAKLVIRAKEAALRKKCAIIAKKAKMAAEKKECEKLAKKAKEAIEWKKCAKLAKKKREAEKKKCAKLAKKEKEAAEKKKRCKDLAKNKKKGHKKKGRNENRKKRTDC
Protein: MutS2 (F4IVK9)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
Sequence:
MATTVYGQASLPQMHSLFSKVRPFLSHSPSFTAPFTRRRSFPFSALPTTKAIDAALMKEKWLDSLSLTSQDEDTTPENAESSCIIGIDPDLSGALALLKFDHLGSSSFAQNQTYYQSWLCFEHLVLMLRNYLSLQGSYVICEKNRECEGFCESFMLLCLVQFEVYDTPHIPVLVGKRVRKRLDAKSIVQLIQSLDVPSGSRVYIEQSNPFPKDGKQGWYSGGFGYGLWIGTLVASGFCVIPVSASLWKRHFQLASGSCTKDDSRRVAAELFPSLSSQLKRKKDHGRAEALLIAAYGEALKTEKLLIQPKELLSQVNYLENQLVEVK
Protein: FOS like 2, AP-1 transcription factor subunit (C9JCN8)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MPGSGSAFIPTINAITTSQDLQWMVQPTVITSMSNPYPRSHPYSPLPGLASVPGHMALPRPGVIKTIGTTVGRRRRDEQLSPEEEEKRRIRRERNKLAAAKCRNRRRELTEKLQAETEELEEEKSGLQKEIAELQKEKEKLEFMLVAHGPVCKISPEERRSPPAPGLQPMRSGGGSVGAVVVKQEPLEEDSPSSSSAGLDKA
Protein: Arginine ADP-riboxanase OspC3 (EC 4.3.99.-) (A0A0H2US87)
Organism: Shigella flexneri
Function: ADP-riboxanase effector that inhibits host cell pyroptosis. Acts by mediating arginine ADP-riboxanation of host CASP4/CASP11, blocking CASP4/CASP11 autoprocessing. This prevents CASP4 activation and ability to recognize and cleave GSDMD, thereby inhibiting LPS-induced pyroptosis. ADP-riboxanation takes place in two steps: OspC3 first catalyzes ADP-ribosylation of target Arg, and then initiates a deamination to remove one N-omega group. Independently of its ADP-riboxanase activity, acts as an inhibitor of calcium signaling by inhibiting host calmodulin, preventing activation of the JAK-STAT signaling pathway in response to interferon-beta. Mechanistically, acts by binding to the apo form of calmodulin, preventing calcium-binding and ability to activate host CaMK2 (CAMKII), which is required to stimulate the JAK-STAT signaling pathway in response to interferon-beta.
Subcellular location: Secreted {ECO:0000269|PubMed:23684308}. Host cytoplasm {ECO:0000305|PubMed:34409271}. Note=Secreted via the type III secretion system (T3SS). {ECO:0000269|PubMed:23684308}.
Interaction partners:
Sequence:
MKIPEAVNHINVQNNIDLVDGKINPNKDTKALQKNISCVTNSSSSGISEKHLDHCADTVKSFLRKSIAAQSYSKMFSQGTSFKSLNLSIEAPSGARSSFRSLEHLDKVSRHYLSEIIQKTHPLSSDERHLLSIIINSDFNFRHQSNANLSNNTLNIKSFDKIKSENIQTYKNTFSEDIEEIANHDFVFFGVEISNHQETLPLNKTHHTVDFGANAYIIDHDSPYGYMTLTDHFDNAIPPVFYHEHQSFFLDNFKEVVDEVSRYVHGNQGKTDVPIFNTKDMRLGIGLHLIDFIRKSKDQRFREFCYNKNIDPVSLDRIINFVFQLEYHIPRMLSTDNFKKIKLRDISLEDAIKASNYEEINNKVTDKKMAHQALAYSLGNKKADIALYLLSKFNFTKQDVAEMEKMKNNRYCNLYDVEYLLSKDGANYKVLEYFINNGLVDVNKKFQKVNSGDTMLDNAMKSKDSKMIDFLLKNGAILGKRFEI
Protein: Ubiquitin thioesterase otulin (EC 3.4.19.12) (Deubiquitinating enzyme otulin) (OTU domain-containing deubiquitinase with linear linkage specificity) (Ubiquitin thioesterase Gumby) (Q96BN8)
Organism: Homo sapiens (Human)
Function: Deubiquitinase that specifically removes linear ('Met-1'-linked) polyubiquitin chains to substrates and acts as a regulator of angiogenesis and innate immune response. Required during angiogenesis, craniofacial and neuronal development by regulating the canonical Wnt signaling together with the LUBAC complex. Acts as a negative regulator of NF-kappa-B by regulating the activity of the LUBAC complex. OTULIN function is mainly restricted to homeostasis of the LUBAC complex: acts by removing 'Met-1'-linked autoubiquitination of the LUBAC complex, thereby preventing inactivation of the LUBAC complex. Acts as a key negative regulator of inflammation by restricting spontaneous inflammation and maintaining immune homeostasis. In myeloid cell, required to prevent unwarranted secretion of cytokines leading to inflammation and autoimmunity by restricting linear polyubiquitin formation. Plays a role in innate immune response by restricting linear polyubiquitin formation on LUBAC complex in response to NOD2 stimulation, probably to limit NOD2-dependent pro-inflammatory signaling.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:23746843}.
Interaction partners:
- E3 ubiquitin-protein ligase RNF31
- Polyubiquitin-C
- Sorting nexin-27
- Sharpin
- Polyubiquitin-B
- RanBP-type and C3HC4-type zinc finger-containing protein 1
- Ubiquitin-ribosomal protein eL40 fusion protein
- Ubiquitin-ribosomal protein eS31 fusion protein
- Tumor necrosis factor
- OTU domain-containing protein 7B
Sequence:
MSRGTMPQPEAWPGASCAETPAREAAATARDGGKAAASGQPRPEMQCPAEHEEDMYRAADEIEKEKELLIHERGASEPRLSVAPEMDIMDYCKKEWRGNTQKATCMKMGYEEVSQKFTSIRRVRGDNYCALRATLFQAMSQAVGLPPWLQDPELMLLPEKLISKYNWIKQWKLGLKFDGKNEDLVDKIKESLTLLRKKWAGLAEMRTAEARQIACDELFTNEAEEYSLYEAVKFLMLNRAIELYNDKEKGKEVPFFSVLLFARDTSNDPGQLLRNHLNQVGHTGGLEQVEMFLLAYAVRHTIQVYRLSKYNTEEFITVYPTDPPKDWPVVTLIAEDDRHYNIPVRVCEETSL
Protein: Neutrophil cytosolic factor 4 (A0A494BZS1)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MRIPALNAYMKSLLSLPVWVLMDEDVRIFFYQSPYDSEQVPQALRRLRPRTRKVKSVSPQGNSVDRMAAPRAEALFDFTGNSKLELNFKAGDVIFLLSRINKDWLEGTVRGATGIFPLSFVKILKDFPEEDDPTNWLRCYYYEDTISTIKDIAVEEDLSSTPLLKDLLELTRREFQREDIALNYRDAEGDLVRLLSDEDVALMVRQARGLPSQKRLFPWKLHITQKDNYRVYNTMP
Protein: Lipoxygenase domain-containing protein (Q54W35)
Organism: Dictyostelium discoideum (Social amoeba)
Interaction partners:
- Lipoxygenase domain-containing protein
- Probable microsomal glutathione S-transferase
Sequence:
MANFLIYDGASTYNPFDYEYPINKINNNPKTFKFPPKHSVCLPQKDHFIVERQLALETKQYTYNFEHNVRVAGFDTPVVGLPPCFKYMAPTYELPKCEQLMNPSFAAHGFSLLFSDFQAKINNYLTNKKSEYFGSVSEYLKMIMLPNPPKLIENQTIESLNKFEWLNDKEFGRQRLQGLNAGQLIRLTNEKVQELDLFNKLKFEKMLPTFNMILSSEVNSNFQKMLDNGNLYMVDYSIFDDVNYYESAKKRGRYISSPIALFYINENDEKLYPLCIKILQNDELSPVFTPASNPPESWIFAKLWFQSADGQHMEFFTHLYECHLLGEVFTIATHRQLSTSHPIYQLLHPHFDLLLDINHRARGNLLSSFGPIESLLGGGSIAALHLIVKYHKNFIWRDNTFLNRLKKNNTLNDNKNRKYYFKEDGIEIYKNLFGFVQDVLSKFYTSKEDIERDFELHSWVDEITSEHGGTIKGLIEGEKLVELTQVVELVTDIIFRVTVEHSIGNHGQWDMFGFTPNVPGALYMDPHKIIEGIPTTFEMIINSLPPKKETQDQIAITHLLANTDTGLPTFISTIYEFEKDQSAPNFKDICSSYRSKMEHLSTIIENRNKNVNMPYSYMDPSKICGSIYI
Protein: Endo-1,4-beta-xylanase F1 (Xylanase F1) (EC 3.2.1.8) (1,4-beta-D-xylan xylanohydrolase F1) (O94163)
Organism: Aspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold)
Function: Endo-1,4-beta-xylanase involved in the hydrolysis of xylan, a major structural heterogeneous polysaccharide found in plant biomass representing the second most abundant polysaccharide in the biosphere, after cellulose.
Subcellular location: Secreted {ECO:0000269|PubMed:10586505}.
Interaction partners:
- Endo-1,4-beta-xylanase A
- Probable endo-1,4-beta-xylanase B
- Probable alpha-L-arabinofuranosidase axhA
- Exo-1,4-beta-xylosidase xlnD
- Xylanolytic transcriptional activator xlnR
- Probable exo-1,4-beta-xylosidase bxlB
Sequence:
MVHLKALASGTLFASLASSAVISRQAAASINDAFVAHGKKYFGTCSDQALLQNSQNEAIVRADFGQLTPENSMKWDALEPSQGSFSFAGADFLADYAKTNNKLVRGHTLVWHSQLPSWVQGITDKDTLTEVIKNHITTIMQRYKGQIYAWDVVNEIFDEDGTLRDSVFSQVLGEDFVRIAFETAREADPNAKLYINDYNLDSADYAKTKGMVSYVKKWLDAGVPIDGIGSQSHYSANGFPVSGAKGALTALASTGVSEVAVTELDIEGASSESYLEVVNACLDVSSCVGITVWGVSDKDSWRSSTSPLLFDSNYQAKDAYNAIIDAL
Protein: Regulator of nonsense transcripts 2 (Up-frameshift suppressor 2 homolog) (hUpf2) (Q9HAU5)
Organism: Homo sapiens (Human)
Function: Involved in nonsense-mediated decay (NMD) of mRNAs containing premature stop codons by associating with the nuclear exon junction complex (EJC). Recruited by UPF3B associated with the EJC core at the cytoplasmic side of the nuclear envelope and the subsequent formation of an UPF1-UPF2-UPF3 surveillance complex (including UPF1 bound to release factors at the stalled ribosome) is believed to activate NMD. In cooperation with UPF3B stimulates both ATPase and RNA helicase activities of UPF1. Binds spliced mRNA.
Subcellular location: Cytoplasm, perinuclear region {ECO:0000269|PubMed:11073994, ECO:0000269|PubMed:11113196, ECO:0000269|PubMed:11163187}. Cytoplasm {ECO:0000250|UniProtKB:A2AT37}.
Interaction partners:
- Regulator of nonsense transcripts 3A
- RNA-binding protein 8A
- RNA-binding protein with serine-rich domain 1
- Regulator of nonsense transcripts 3B
- Regulator of nonsense transcripts 1
- Serine/threonine-protein kinase SMG1
- Serine/arginine repetitive matrix protein 1
- Protein CASC3
- Eukaryotic initiation factor 4A-III
- Nonsense-mediated mRNA decay factor SMG8
Sequence:
MPAERKKPASMEEKDSLPNNKEKDCSERRTVSSKERPKDDIKLTAKKEVSKAPEDKKKRLEDDKRKKEDKERKKKDEEKVKAEEESKKKEEEEKKKHQEEERKKQEEQAKRQQEEEAAAQMKEKEESIQLHQEAWERHHLRKELRSKNQNAPDSRPEENFFSRLDSSLKKNTAFVKKLKTITEQQRDSLSHDFNGLNLSKYIAEAVASIVEAKLKISDVNCAVHLCSLFHQRYADFAPSLLQVWKKHFEARKEEKTPNITKLRTDLRFIAELTIVGIFTDKEGLSLIYEQLKNIINADRESHTHVSVVISFCRHCGDDIAGLVPRKVKSAAEKFNLSFPPSEIISPEKQQPFQNLLKEYFTSLTKHLKRDHRELQNTERQNRRILHSKGELSEDRHKQYEEFAMSYQKLLANSQSLADLLDENMPDLPQDKPTPEEHGPGIDIFTPGKPGEYDLEGGIWEDEDARNFYENLIDLKAFVPAILFKDNEKSCQNKESNKDDTKEAKESKENKEVSSPDDLELELENLEINDDTLELEGGDEAEDLTKKLLDEQEQEDEEASTGSHLKLIVDAFLQQLPNCVNRDLIDKAAMDFCMNMNTKANRKKLVRALFIVPRQRLDLLPFYARLVATLHPCMSDVAEDLCSMLRGDFRFHVRKKDQINIETKNKTVRFIGELTKFKMFTKNDTLHCLKMLLSDFSHHHIEMACTLLETCGRFLFRSPESHLRTSVLLEQMMRKKQAMHLDARYVTMVENAYYYCNPPPAEKTVKKKRPPLQEYVRKLLYKDLSKVTTEKVLRQMRKLPWQDQEVKDYVICCMINIWNVKYNSIHCVANLLAGLVLYQEDVGIHVVDGVLEDIRLGMEVNQPKFNQRRISSAKFLGELYNYRMVESAVIFRTLYSFTSFGVNPDGSPSSLDPPEHLFRIRLVCTILDTCGQYFDRGSSKRKLDCFLVYFQRYVWWKKSLEVWTKDHPFPIDIDYMISDTLELLRPKIKLCNSLEESIRQVQDLEREFLIKLGLVNDKDSKDSMTEGENLEEDEEEEEGGAETEEQSGNESEVNEPEEEEGSDNDDDEGEEEEEENTDYLTDSNKENETDEENTEVMIKGGGLKHVPCVEDEDFIQALDKMMLENLQQRSGESVKVHQLDVAIPLHLKSQLRKGPPLGGGEGEAESADTMPFVMLTRKGNKQQFKILNVPMSSQLAANHWNQQQAEQEERMRMKKLTLDINERQEQEDYQEMLQSLAQRPAPANTNRERRPRYQHPKGAPNADLIFKTGGRRR