wanglab/gogpt-training-data huggingface dataset:
Protein: Spastin (EC 5.6.1.1) (A0A126GV13)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Membrane {ECO:0000256|HAMAP-Rule:MF_03021}; Peripheral membrane protein {ECO:0000256|HAMAP-Rule:MF_03021}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000256|HAMAP-Rule:MF_03021}. Cytoplasm, cytoskeleton {ECO:0000256|HAMAP-Rule:MF_03021}. Chromosome {ECO:0000256|HAMAP-Rule:MF_03021}. Lipid droplet {ECO:0000256|HAMAP-Rule:MF_03021}. Note=Forms an intramembrane hairpin-like structure in the membrane. Colocalizes with cellular microtubule arrays. Localizes to chromosomes from prometaphase/metaphase to anaphase, and this requires microtubules. Localizes to discrete punctate cytoplasmic foci which may correspond to secretory vesicles. {ECO:0000256|HAMAP-Rule:MF_03021}.
Interaction partners:
Sequence:
MAANRPGGGYSPGPGDPLLAKQKHHHRRAFEYISKALKIDEENEGHKELAIELYRKGIKELEDGIAVDCWSGRGDVWDRAQRLHDKMQTNLSMARDRLHFLASGRKLTIGSKRPVNLAVANKSQTLPRNLGSKTSVGAVQRQPAKTAATPPAVRRQFSSGRNTPPQRSRTPINNNGPSGSGASTPVVSVKGVEQKLVQLILDEIVEGGAKVEWTDIAGQDVAKQALQEMVILPSVRPELFTGLRAPAKGLLLFGPPGNGKTLLARAVATECSATFLNISAASLTSKYVGDGEKLVRALFAVARHMQPSIIFIDEVDSLLSERSSSEHEASRRLKTEFLVEFDGLPGNPDGDRIVVLAATNRPQELDEAALRRFTKRVYVSLPDEQTRELLLNRLLQKQGSPLDTEALRRLAKITDGYSGSDLTALAKDAALEPIRELNVEQVKCLDISAMRAITEQDFHSSLKRIRRSVAPQSLNSYEKWSQDYGDITI
Protein: Transcription factor S (Transcription elongation factor IIS/RNA polymerase subunit homolog) (TFIIS/RPSU homolog) (Q56254)
Organism: Thermococcus celer
Function: Induces RNA cleavage activity in the RNA polymerase. In its presence, the cleavage activity of the RNA polymerase truncates the RNA back to position +15 in a stepwise manner by releasing mainly dinucleotides from the 3'-end of the nascent RNA. The truncated RNAs are able to continue elongation. Involved in transcriptional proofreading and fidelity. Misincorporation of nucleotides during elongation of transcription leads to arrested elongation complexes which are rescued by TFS-promoted removal of a dinucleotide from the 3'-end. TFS is able to induce a cleavage resynthesis cycle in stalled elongation complexes (resulting from the next missing nucleotide or a reduced incorporation rate of a wrong nucleotide) preventing misincorporation and enabling proofreading in a post-incorporation manner. Pausing of elongation complexes is the main determinant of TFS-induced RNA cleavage.
Interaction partners:
Sequence:
MKFCPKCGNLMLPDRKRKVWVCRSCGYEEPFDEEKDREKTVIKQEVKHKPDEGIVVIEQDLKTLPTTKITCPKCGNDTAYWWEMQTRAGDEPSTIFYKCTKCGHTWRSYE
Protein: NADP-reducing hydrogenase subunit HndB (EC 1.12.1.3) (Hydrogen dehydrogenase (NADP(+))) (Q46506)
Organism: Solidesulfovibrio fructosivorans (Desulfovibrio fructosivorans)
Function: Catalyzes the reduction of NADP in the presence of molecular H2 to yield NADPH.
Interaction partners:
Sequence:
MSTIRSFEDLKAKRQEILDRKAARNGKTIINVSLATCSIAAGGKVAMEAMQDEVAKNGLTGVEFMQSSCMTYCYAEPTVEITLPGKDPVVFGGVDENRARELVTEYVMKGEPVEGIIPVNYERVVL
Protein: Hemoglobin subunit alpha (Alpha-globin) (Hemoglobin alpha chain) (P83623)
Organism: Pseudaphritis urvillii (Congolli) (Freshwater flathead)
Function: Involved in oxygen transport from gills to the various peripheral tissues.
Interaction partners:
Sequence:
SLTDKDKATVKALWGKISKSADAVGADAVGRMIVVYPQTKTYFSHWPDLAPNSPHVKTHGKTVMTGIALAVSKIDDLTNGLLELSEEHAYKMRVDPANFKILSHCMLVVIATMFPKEFTPEAHVCLDKFLCAVSLALSERYR
Protein: Sensor protein kinase PilS (EC 2.7.13.3) (P33639)
Organism: Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Function: Member of the two-component regulatory system PilS/PilR that regulates the expression of multiple genes including the type IV pilus (T4P) major subunit PilA. Thereby, plays a major role in the regulation of multiple motility pathways. Functions as a membrane-associated protein kinase that phosphorylates PilR in response to environmental signals leading to activation of specific gene promoters including the pilin gene.
Subcellular location: Cell inner membrane {ECO:0000269|PubMed:27162347, ECO:0000269|PubMed:8550520}; Multi-pass membrane protein {ECO:0000305}. Note=Localizes at both poles of P.aeruginosa. Also accumulates at the septum of dividing cells, so when the daughter cells separate, PilS is already in place at both poles. {ECO:0000269|PubMed:10760172}.
Interaction partners:
- Response regulator protein PilR
- RNA polymerase sigma-54 factor
- Protein PilG
- Protein PilH
- Type IV pilus inner membrane component PilM
- Type 4 fimbrial biogenesis protein PilZ
- Type IV pilus inner membrane component PilO
- Type IV pilus inner membrane component PilN
- Fimbrial assembly protein PilQ
- Type IV pilus inner membrane component PilP
Sequence:
MRAERLRLSEEQGQRILRLYHLYRLTIGLVLVLLISSELEDQVLKLVHPELFHVGSWCYLVFNILVALFLPPSRQLLPIFILALTDVLMLCGLFYAGGGVPSGIGSLLVVAVAIANILLRGRIGLVIAAAASLGLLYLTFFLSLSSPDATNHYVQAGGLGTLCFAAALVIQALVRRQEQTETLAEERAETVANLEELNALILQRMRTGILVVDSRQAILLANQAALGLLRQDDVQGASLGRHSPMLMHCMKQWRLNPSLRPPTLKVVPDGPTVQPSFISLNREDDQHVLIFLEDISQIAQQAQQMKLAGLGRLTAGIAHEIRNPLGAISHAAQLLQESEELDAPDRRLTQIIQDQSKRMNLVIENVLQLSRRRQAEPQQLDLKEWLQRFVDEYPGRLRNDSQLHLQLGAGDIQTRMDPHQLNQVLSNLVQNGLRYSAQAHGRGQVWLSLARDPESDLPVLEVIDDGPGVPADKLNNLFEPFFTTESKGTGLGLYLSRELCESNQARIDYRNREEGGGCFRITFAHPRKLS
Protein: Carbon monoxide dehydrogenase (CODH) (EC 1.2.7.4) (P31896)
Organism: Rhodospirillum rubrum
Function: Allows growth in a CO-dependent manner in the dark. CODH oxidizes carbon monoxide coupled, via CooF, to the reduction of a hydrogen cation by a hydrogenase (possibly CooH).
Subcellular location: Cytoplasm. Cell inner membrane; Peripheral membrane protein; Cytoplasmic side. Note=Loosely attached to the inner membrane, probably via CooF. {ECO:0000250}.
Interaction partners:
Sequence:
MTHHDCAHCSSDACATEMLNLAEANSIETAWHRYEKQQPQCGFGSAGLCCRICLKGPCRIDPFGEGPKYGVCGADRDTIVARHLVRMIAAGTAAHSEHGRHIALAMQHISQGELHDYSIRDEAKLYAIAKTLGVATEGRGLLAIVGDLAAITLGDFQNQDYDKPCAWLAASLTPRRVKRLGDLGLLPHNIDASVAQTMSRTHVGCDADPTNLILGGLRVAMADLDGSMLATELSDALFGTPQPVVSAANLGVMKRGAVNIAVNGHNPMLSDIICDVAADLRDEAIAAGAAEGINIIGICCTGHEVMMRHGVPLATNYLSQELPILTGALEAMVVDVQCIMPSLPRIAECFHTQIITTDKHNKISGATHVPFDEHKAVETAKTIIRMAIAAFGRRDPNRVAIPAFKQKSIVGFSAEAVVAALAKVNADDPLKPLVDNVVNGNIQGIVLFVGCNTTKVQQDSAYVDLAKSLAKRNVLVLATGCAAGAFAKAGLMTSEATTQYAGEGLKGVLSAIGTAAGLGGPLPLVMHMGSCVDNSRAVALATALANKLGVDLSDLPLVASAPECMSEKALAIGSWAVTIGLPTHVGSVPPVIGSQIVTKLVTETAKDLVGGYFIVDTDPKSAGDKLYAAIQERRAGLGL
Protein: LD36620p (Vermiform, isoform G) (Q8IQU1)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MARWWPILSVVCLCLAVAHGQDKLEGVDVEEVCADRPADEYFRLETDGDCREVYRCTKSGLKEIQCPSGLAFDVIKQTCDWKAKVTNCDEKEKPRKAKPILKTDEPICPEGKLSCGDGECLDKELFCNGKSDCKDESDENACSVDEDPNRAPECDPTQCALPDCFCSADGTRIPGGIEPQQVPQMITITFNGAVNVDNIDLYEDIFNGQRQNPNGCSIKGTFFVSHKYTNYSAVQDLHRRGHEISVFSLTHKDDPNYWTGGSYDDWLAEMAGSRLIVERFANITDGSIIGMRAPYLRVGGNKQFEMMADQFFVYDASITASLGRVPIWPYTLYFRMPHKCNGNAHNCPSRSHPVWEMVMNELDRRDDPTFDESLPGCHMVDSCSNVASGDQFARLLRHNFNRHYNSNRAPLGLHFHASWLKSKKEYRDELIKFIEEMLGRNDVFFVTNLQVIQWMQNPTELNSLRDFQEWKEKCDVKGQPYCSLPNACPLTTRELPGETLRLFTCMECPNNYPWILDPTGDGFSV
Protein: Peptidyl-prolyl cis-trans isomerase, microsomal (PPIase) (EC 5.2.1.8) (Cyclophilin) (Rotamase) (Q10724)
Organism: Zea mays (Maize)
Function: PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides.
Subcellular location: Microsome {ECO:0000269|PubMed:8645184}. Endoplasmic reticulum {ECO:0000269|PubMed:8645184}.
Interaction partners:
- UPF0235 protein
- Peptidyl-prolyl cis-trans isomerase
- Nuclear pore complex protein NUP107
- Nuclear pore complex protein NUP88
- Seh1-like protein
- Zinc finger CCCH domain-containing protein 4
- Ribosomal protein S2
- Ribosomal protein S2
- Elongation factor 1-alpha
- Elongation factor 1-alpha
Sequence:
KKDLTEVTHKVYFDVEIDGKPAGRIVMGLF
Protein: Cytochrome c oxidase assembly protein COX18, mitochondrial (Q8VC74)
Organism: Mus musculus (Mouse)
Function: Mitochondrial membrane insertase required for the translocation of the C-terminus of cytochrome c oxidase subunit II (MT-CO2/COX2) across the mitochondrial inner membrane. Plays a role in MT-CO2/COX2 maturation following the COX20-mediated stabilization of newly synthesized MT-CO2/COX2 protein and before the action of the metallochaperones SCO1/2. Essential for the assembly and stability of the mitochondrial respiratory chain complex IV (also known as cytochrome c oxidase).
Subcellular location: Mitochondrion inner membrane {ECO:0000250|UniProtKB:Q8N8Q8}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Cytochrome c oxidase subunit 2
- Large ribosomal subunit protein mL45
- Cytochrome c oxidase assembly protein COX16 homolog
- Cytochrome c oxidase assembly protein COX11
- Large ribosomal subunit protein mL62
- Ribonuclease H1
- Cytochrome c oxidase assembly factor 6 homolog
Sequence:
MLCRSCAGWLRSLPTLRLPAPGSPPAWSSARLPALPVWAAASVSAASPGGWYEALAASAPVRTAEEVLLGAQEATGLPWWSNIILSTVALRGAVTLPLAAYQHYILAKVENLQPEIKDIAKRLNQEVAVCARQFGWSKRVARLTYLKNMRRLISELYVRDNCHPFKATVLVWVQLPMWVFISVALRNLSTGATHSDGISVQEQLAAGGTLWFPDLTAVDSTWILPVSVGVVNLLIVEIFALQKIGTSRFQMYVTNFVRAVSVLMIPVAATVPSALVLYWLCSSLMGLAQNLLLRSPGFRQLCRIPPSKSDSETPYRDLSAAFCAKFLSRKR
Protein: Myosin binding subunit, isoform M (M9NFF6)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MSSLDARNNSAMMKRAEQLKRWEESDTNRAAPTPRHEHGRRIKFSSGCVFLAACLSGDKDEVVQLLDQGADINTANVDGLTALHQACIDDNLDMVEFLVERGADINRQDNEGWTPLHATASCGFVSIARYLVENGADVAAVNSDGDLALDLAIDVQHMAMIDYMEKMVQELNINVDEARKAEELAMLNDAKKWLRSDAAEVDRPHPKTGATALHVAAAKGYTKVLGLLLAGRGNVDRQDNDGWTPLHAASHWGQRETAEMLVESLADMDIRNYAGQSCIDVADRKIVKFLEELRANKRNKRRPSSQIRISDAMENHVEKTPTKLVRVEVRTDATKDAENVKPNQQIHAVEHPVEEEAPWRRKLPRTPSDSPTNNLPDRELGTNSSETANDVILRRTQSFENDQKFYQKYNELRARIKANSCPILPANANANAAAANKSNNNNNLSSNNYHNNNNNNNKSDLLLGYAAGTTTTTSTPTTTTTTTSSTFNNTHSNTNNTSTTQQQPAAAAAASAANQLYSVQRSASLKDNSMYYRKPTVTIATSTAATAINSPSTTVQTPPIRSQVTAKIAEKSNNGSSSTASVSDAESSKPPPKQSASNMIKNFFKSFVPPVRDEESETQRKAHAKRVRETRRSTQGVTLDEIKSAEELVKKKNMGMANNNNNNNISTTTTNTISNSGNETSSASSTSAPTPSILGSNEQQDELQPPPPPTTPPPAVIPTTTTATDETEIEEVVSSPPAGQSQNDTTASFTLSAPVRRSLSTEGEADANSDPEGDQDQTVVSASYTIMPRRERLPESSENVESIRSPQKTEPVAKSSSEDKSEEPPHARPTDLPLIPAPAAPSTEAIKSSSAATTPAALESPVRLRDKRGLSGSQESETKSDTASPVSSHPDFNARDSLLSLYARRTTDSSAGGGGVGGGAGVGAGGASGAATSSSTSAAERRPSWRLKFDAGSKFKLEDITSGGTYPPNNSTIIPSAPAVMAAANLSTTTGVQRRISSGPIALNASNQSLNSVGRPVSAPSEGTNNSAYVTPSARKFETNATSTGATTAATTTSNSTSNSVSATSANHTTATAPNATSNHDDKDNDKENDNRTQTVIQRRRKPKRRSTGVVHIDMDELDPERQNESSNNDNEEKEKESGSERTSRSRLGSTASTATTSESKSSSSNDKTENGDGIDYKALWEAEKLENDKLRQMLKQKDDEAVQTRATLERFANAQLDAYKSDNHRLKEENAALIRVISKLSK
Protein: Proteasome activator protein PA26 (Q9U8G2)
Organism: Trypanosoma brucei
Interaction partners:
Sequence:
MPPKRAALIQNLRDSYTETSSFAVIEEWAAGTLQEIEGIAKAAAEAHGTIRNSTYGRAQAEKSPEQLLGVLQRYQDLCHNVYCQAETIRTVIAIRIPEHKEEDNLGVAVQHAVLKIIDELEIKTLGSGEKSGSGGAPTPIGMYALREYLSARSTVEDKLLGSVDAESGKTKGGSQSPSLLLELRQIDADFMLKVELATTHLSTMVRAVINAYLLNWKKLIQPRTGSDHMVS
Protein: Actin-57B (EC 3.6.4.-) (P53501)
Organism: Drosophila melanogaster (Fruit fly)
Function: Actins are highly conserved proteins that are involved in various types of cell motility and are ubiquitously expressed in all eukaryotic cells.
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000269|PubMed:9344535}. Note=Associated with spectrosomes during female cystocyte proliferation and differentiation, but dissociates, or becomes undetectable, upon fusome maturation (PubMed:9344535). Component of the inner rim of ring canals connecting the cytoplasm of nurse cells and oocyte during oogenesis (PubMed:9344535). {ECO:0000269|PubMed:9344535}.
Interaction partners:
- Adenylyl cyclase-associated protein
- Actin, larval muscle
- Actin, indirect flight muscle
- Actin-42A
- Glutaredoxin domain-containing cysteine-rich protein CG12206
- Glutaredoxin domain-containing cysteine-rich protein CG31559
- Myosin light chain alkali
- Myosin heavy chain, muscle
- Muscle-specific protein 20
- Tropomyosin-2
Sequence:
MCDDEVAALVVDNGSGMCKAGFAGDDAPRAVFPSIVGRPRHQGVMVGMGQKDSYVGDEAQSKRGILTLKYPIEHGIITNWDDMEKIWHHTFYNELRVAPEEHPVLLTEAPLNPKANREKMTQIMFETFNSPAMYVAIQAVLSLYASGRTTGIVLDSGDGVSHTVPIYEGYALPHAILRLDLAGRDLTDYLMKILTERGYSFTTTAEREIVRDIKEKLCYVALDFEQEMATAAASTSLEKSYELPDGQVITIGNERFRCPESLFQPSFLGMESCGIHETVYNSIMKCDVDIRKDLYANIVMSGGTTMYPGIADRMQKEITSLAPSTIKIKIIAPPERKYSVWIGGSILASLSTFQQMWISKEEYDESGPGIVHRKCF
Protein: Manganese transporter SMF2 (P38778)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: High-affinity manganese transporter involved in mobilizing manganese from vesicular stores iin conditions of low manganese ion concentrations.
Subcellular location: Vacuole lumen {ECO:0000269|PubMed:11027260}. Vesicle {ECO:0000305}. Cell membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000255}. Note=In the presence of excess manganese, targeted to the vacuolar lumen, where it is degraded (PubMed:11027260). Under metal starvation conditions, localization is restricted to intracellular punctate bodies (PubMed:11027260). {ECO:0000269|PubMed:11027260}.
Interaction partners:
- Mitochondrial carrier protein MTM1
- Superoxide dismutase, mitochondrial
- Metal homeostatis protein BSD2
- Small nuclear ribonucleoprotein F
- Calcium-transporting ATPase 1
- Protein CCC1
- Inorganic phosphate transporter PHO84
- Low-affinity Fe
Sequence:
MTSQEYEPIQWSDESQTNNDSVNDAYADVNTTHESRRRTTLQPNSTSQSMIGTLRKYARFIGPGLMVSVSYMDPGNYSTAVAAGSAHRYKLLFSVLVSNFMAAFWQYLCARLGAVTGLDLAQNCKKHLPFGLNITLYILAEMAIIATDLAEVVGTAISLNILFHIPLALGVILTVVDVLIVLLAYKPNGSMKGIRIFEAFVSLLVVLTVVCFTVELFYAKLGPAKEIFSGFLPSKAVFEGDGLYLSLAILGATVMPHSLYLGSGVVQPRLREYDIKNGHYLPDANDMDNNHDNYRPSYEAISETLHFTITELLISLFTVALFVNCAILIVSGATLYGSTQNAEEADLFSIYNLLCSTLSKGAGTVFVLALLFSGQSAGIVCTLSGQMVSEGFLNWTVSPALRRSATRAVAITPCLILVLVAGRSGLSGALNASQVVLSLLLPFVSAPLLYFTSSKKIMRVQLNRTKELSRTTDKKPVADRTEDDETIELEEMGIGSSSQERSLVSPAPEYKDMSNGMIVTVLAIIVWLIISGLNFYMLLGFTTGKEVHL
Protein: Nuclear transcription factor Y subunit gamma (CAAT box DNA-binding protein subunit C) (CCAAT-binding transcription factor subunit C) (CBF-C) (Nuclear transcription factor Y subunit C) (NF-YC) (Q62725)
Organism: Rattus norvegicus (Rat)
Function: Component of the sequence-specific heterotrimeric transcription factor (NF-Y) which specifically recognizes a 5'-CCAAT-3' box motif found in the promoters of its target genes. NF-Y can function as both an activator and a repressor, depending on its interacting cofactors.
Subcellular location: Nucleus.
Interaction partners:
- Nuclear transcription factor Y subunit alpha
- Nuclear transcription factor Y subunit beta
- CCAAT/enhancer-binding protein zeta
- MHC class II transactivator
- Cyclic AMP-dependent transcription factor ATF-2
- DNA polymerase epsilon 3, accessory subunit, pseudogene 2
- Inhibitor of growth protein.
Sequence:
MSTEGGFGSTSSSDAQQSLQSFWPRVMEEIRNLTVKDFRVQELPLARIKKIMKLDEDVKMISAEAPVLFAKAAQIFITELTLRAWIHTEDNKRRTLQRNDIAMAITKFDQFDFLIDIVPRDELKPPKRQEEVRQSVTPAEPVQYYFTLAQQPTAVQVQGQQQGQQTTSSTTTIQPGQIIIAQPQQGQTTPVTMQVGEGQQVQIVQAQPQGQAQQAQSGTGQTMQVMQQIITNTGEIQQIPVQLNAGQLQYIRLAQPVSGTQVVQGQIQTLATNAQQITQTEVQQGQQQFSQFTDGQQLYQIQQVTMPAGQDLAQPMFIQSANQPSDGQTPQVTGD
Protein: Shutoff protein (100 kDa protein) (p100K) (100K-chaperone protein) (L4-100K) (Shutoff protein 100K) (P24933)
Organism: Human adenovirus C serotype 5 (HAdV-5) (Human adenovirus 5)
Function: Protein that inhibits host translation while promoting late viral translation by ribosome shunting. Blocks host cap-dependent translation by binding to eIF4G, displacing MKNK1 from cap initiation complexes and preventing EIF4E phosphorylation. Binds to the tripartite leader sequence of viral late mRNAs and recruits host eIF4G, PABPC1/poly-A binding protein and 40S ribosomes subunits on viral mRNAs, allowing ribosome shunting and efficient translation of late viral mRNAs even though conventional translation via ribosome scanning from the cap has been shut off in the host cell. During assembly, acts as a chaperone protein that helps hexon proteins assembly into trimers.
Subcellular location: Host cytoplasm {ECO:0000255|HAMAP-Rule:MF_04060, ECO:0000269|PubMed:14633984}.
Interaction partners:
Sequence:
MESVEKKDSLTAPSEFATTASTDAANAPTTFPVEAPPLEEEEVIIEQDPGFVSEDDEDRSVPTEDKKQDQDNAEANEEQVGRGDERHGDYLDVGDDVLLKHLQRQCAIICDALQERSDVPLAIADVSLAYERHLFSPRVPPKRQENGTCEPNPRLNFYPVFAVPEVLATYHIFFQNCKIPLSCRANRSRADKQLALRQGAVIPDIASLNEVPKIFEGLGRDEKRAANALQQENSENESHSGVLVELEGDNARLAVLKRSIEVTHFAYPALNLPPKVMSTVMSELIVRRAQPLERDANLQEQTEEGLPAVGDEQLARWLQTREPADLEERRKLMMAAVLVTVELECMQRFFADPEMQRKLEETLHYTFRQGYVRQACKISNVELCNLVSYLGILHENRLGQNVLHSTLKGEARRDYVRDCVYLFLCYTWQTAMGVWQQCLEECNLKELQKLLKQNLKDLWTAFNERSVAAHLADIIFPERLLKTLQQGLPDFTSQSMLQNFRNFILERSGILPATCCALPSDFVPIKYRECPPPLWGHCYLLQLANYLAYHSDIMEDVSGDGLLECHCRCNLCTPHRSLVCNSQLLNESQIIGTFELQGPSPDEKSAAPGLKLTPGLWTSAYLRKFVPEDYHAHEIRFYEDQSRPPNAELTACVITQGHILGQLQAINKARQEFLLRKGRGVYLDPQSGEELNPIPPPPQPYQQQPRALASQDGTQKEAAAAAATHGRGGILGQSGRGGFGRGGGGHDGRLGEPRRGSFRGRRGVRRNTVTLGRIPLAGAPEIGNRFQHGYNLRSSGAAGTARSPTQP
Protein: Proline-rich protein 20E (P86478)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MEEPRPSKRLRSMAPNQASGGPPPEPGCCVADPEGSVEADGPAQPAQPAKPIAYVKPFRRQPPARPESPPPAERGRRRGGSRRPGRGRGRRAGPRGDAGQRQGAEGLMAPDVHIQLDHHGEPGHQGEPEITETAAFSLSETGPPPGTVQEGPGPDVAQPELGFQEPPAAPGPQAVDWQPVLTLYPCIGFRALGDSAVLQVIQTPQGTYVQGVPVFLTDIAY
Protein: Conserved oligomeric Golgi complex subunit 1 (COG complex subunit 1) (Component of oligomeric Golgi complex 1) (Q9FFF3)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Required for normal Golgi function.
Subcellular location: Golgi apparatus membrane {ECO:0000250|UniProtKB:Q8WTW3}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q8WTW3}; Cytoplasmic side {ECO:0000250|UniProtKB:Q8WTW3}.
Interaction partners:
- Conserved oligomeric Golgi complex subunit 2
- Conserved oligomeric Golgi complex subunit 8
- Conserved oligomeric Golgi complex subunit 6
- Conserved oligomeric Golgi complex subunit 3
- Conserved oligomeric Golgi complex subunit 7
- Conserved oligomeric Golgi complex subunit 4
- Conserved oligomeric Golgi complex subunit 5
- Proline-rich family protein
- Vacuolar protein sorting-associated protein 51 homolog
- Syntaxin-31
Sequence:
MRMSSASAGEYRPSAVSLSSNGGGQRDAESLFRTKPMSEIRIVESATRKNIEDKKEELRQLVGTRYRDLIDSADSIVHMKSLCESISANISSIHGNIRSLSSSSVAETPKLASLNPVRVNVYGIACRVKYLVDTPENIWGCLDESMFLEAAGRYMRAQHVQQRLIKLEGCGGGVAEVDQSKLLANFPLLEHQWQIVESFKAQISQRSHERLLDPGLGLGAYVDALTAVAVVDELDPEQVLELFLDSRKTWILQKLNACTGEDAGEVVLVFCDVLSVIQVTVGQVGELFLQALTDMPLFYKTILSTPPASQLFGGIPNPEEEVELWKSFRDKLESVMLILDKNDVSKSCLTWLRECGGQIVGKVSGKHLIEAIVTGAELGSAEKLIRETMDSKDVLRGSLDWLKSVFGSEVELPWNRIRELVLGDDLNLWDEIFEKAFVERMKSIIDSKFENLTKAVNVADSVHAYSEITGEKINFQAYLNRPSTGGGVWFIEPNSKKVGLISGNKSSPEESDFQSCLTAYFGPEVSQMRDAVDRRCHSVLEDLLSFFESEKAGPRLKDLAPYVQNKCYDSVSALLADVDKELEFLCAAVKKENKDSEAIPPAIIIEKSLFMGRLLFALLNHSKHVPLILGSPRLWCRETMTAVSDKLSSLLRQPRFSSNTPATADSPGKQLHTDLRKQTSLAVAALLGAEEKTSPKFEELNRTMRDLCIKAHTLWIKWLSDELSAILLRDLRSDDGLSATTPLRGWEETIVKQEQDESQSELKISLPSLPSLYMISFLCRASEEIHRIGGHVLDRSILQKFASSLLEKITIIYEDFLSAREASEPQISEKGVLQILLDLRFAADVLSGGDTSTNVETPKSTINRSAYRRRQDQQKTKLVNRGRIDGVTSQLTQKLDPIDWLTYEPYLWENEKQSYLRHAVLFGFFVQLNRMYTDTAQKLSINIESNIMPCSTVPRFKYLPISAPALSSRSTNKVSIPVTSNDASARNSWKAFTNGEQSQTSDLEENSNFGVAFKSFMQESTLKLGSILTDGQVGIFKDRSAAAMSTFGDILPAQAAGLLSSFTNTRSE
Protein: Squamous cell carcinoma antigen recognized by T-cells 3 (SART-3) (B3DJT0)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Function: U6 snRNP-binding protein that functions as a recycling factor of the splicing machinery. Promotes the initial reassembly of U4 and U6 snRNPs following their ejection from the spliceosome during its maturation. May also function as a substrate targeting factor for deubiquitinases and mediate the deubiquitination of components of the spliceosome and histones (By similarity).
Subcellular location: Nucleus, nucleoplasm {ECO:0000250|UniProtKB:Q15020}. Nucleus, Cajal body {ECO:0000250|UniProtKB:Q15020}. Nucleus speckle {ECO:0000250|UniProtKB:Q15020}. Cytoplasm {ECO:0000250|UniProtKB:Q15020}.
Interaction partners:
- U6 snRNA-associated Sm-like protein LSm8
- U6 snRNA-associated Sm-like protein LSm7
- U6 snRNA-associated Sm-like protein LSm5
- U6 snRNA-associated Sm-like protein LSm6
- U6 snRNA-associated Sm-like protein LSm4
- PRP3 pre-mRNA-processing factor 3 homolog
- U6 snRNA-associated Sm-like protein LSm2
- U4/U6 small nuclear ribonucleoprotein Prp4
- Actin maturation protease
- U6 snRNA-associated Sm-like protein LSm3
Sequence:
MAATGNEEQTLLPDIEEEAEGMEREMESEDDEEEGMGVEHSEEEDEEDTSEDERENEAEIQRLEEQLSINAFDYNCHVDLIKLLRQEGKLHRLRKARQKMSELFPLTEEIWLDWLKDEIRITEDESDREKVYELFERAIKDYVCPEIWLEYVQYSIGGMGAQGGIERVRSIFERALTAVGLHMTKGASIWEAYREFEIVILSTVQPPPGTVPSQEQQELLSAQLERIHTLFRRQLAVPLMDMEGTYAEYSDWADDGVPETVTHQYRRALQQMEKGKPYEEALLVSEPPKLAEYQSYIDFEIKEGDPARVQIIFERALAENCLVPDLWIKYTTYLDRQLKIKDLVLSAHERAVRNCPWTMGLWKSYLLALERHGADHQTVKDVFEKALNAGFIQATDYVEIWQSYLDYLRRRVDFSKEWSRELDELRAAFSRSLEYLKQDVEERFSESGDLSCTLMQIWARIEALHCKNMQKARELWDSIMTKGNAKYANMWLEYYNLERSYGDAAHCRKALHRAVQCTSDYPEHVCDVLLNFERVEGSLEDWDAAVQKTETKLNRVCEQRARVAEKEALHARQEEEKAEQRRKVKADKKAQKKGQKANRTGDKRKAEDDDEEEWGEEAELPSKRLRGEDDFDSTVTEELMETESGLFGRRAPPARKTEPPGFRKNQQGAPEPQRQPHDMPKEQRKDENCVFVSNLTFNMEDPEGKLRTLFQGCGTIQQVRPVFTAKGTFRGYCYVQFEDRLAVPEALKMDRQEVDGRPMYVSPCVDKNKNPDFKVFKYKTSMEKHKIFISGLPYSATKETLEDLCKEHGTIRAIRIVTNRSGKSKGLAYVEFEDEAQASQAVLKMDGTMLENFTLSVAISNPPGRRMKDEAAPSRFLGAAMPRQLQGARGKGRTQISLLPRSLYRQSTPDAKAENGTISAPHATVTDGETSLDTQTKSLSNEDFARMLLKK
Protein: NF-kappa-B inhibitor-like protein 1 (Inhibitor of kappa B-like protein) (I-kappa-B-like protein) (IkappaBL) (Nuclear factor of kappa light polypeptide gene enhancer in B-cells inhibitor-like 1) (Q9UBC1)
Organism: Homo sapiens (Human)
Function: Involved in the regulation of innate immune response. Acts as negative regulator of Toll-like receptor and interferon-regulatory factor (IRF) signaling pathways. Contributes to the negative regulation of transcriptional activation of NF-kappa-B target genes in response to endogenous proinflammatory stimuli.
Subcellular location: Nucleus {ECO:0000269|PubMed:20829348}. Note=Nuclear localization with a speckled expression pattern in some cells. Colocalizes with CACTIN in the nucleus.
Interaction partners:
- V-type proton ATPase subunit G 2
- Lymphotoxin-alpha
- Putative RNA-binding protein Luc7-like 1
- Leukocyte-specific transcript 1 protein
Sequence:
MSNPSPQVPEEEASTSVCRPKSSMASTSRRQRRERRFRRYLSAGRLVRAQALLQRHPGLDVDAGQPPPLHRACARHDAPALCLLLRLGADPAHQDRHGDTALHAAARQGPDAYTDFFLPLLSRCPSAMGIKNKDGETPGQILGWGPPWDSAEEEEEDDASKEREWRQKLQGELEDEWQEVMGRFEGDASHETQEPESFSAWSDRLAREHAQKCQQQQREAEGSRRPPRAEGSSQSWRQQEEEQRLFRERARAKEEELRESRARRAQEALGDREPKPTRAGPREEHPRGAGRGSLWRFGDVPWPCPGGGDPEAMAAALVARGPPLEEQGALRRYLRVQQVRWHPDRFLQRFRSQIETWELGRVMGAVTALSQALNRHAEALK
Protein: ADAM metallopeptidase domain 22 (A0A8I5Y6E8)
Organism: Rattus norvegicus (Rat)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004479}; Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004479}.
Interaction partners:
Sequence:
MQAVAAAFFWLLCVLGTYPLARCGRAGDASLRELERGDGNRFLERQSTVPLRLIYRLGGEDETQHEQLNTRVRGDPGGRQPTHVDKASFRVDAFGTSFILDVLLNHELLSSGYVERHIEHGGKVVENKGGEHCYYQGQIRGNPASFVALSTCHGLHGMFYDGNHTYLIEPEENEMSQESQFHSVYKSRLLEFPLDDLPSEFQRINITAPQFTLKPRLKRRKRQLLRFPRNVEEETKYIELMIVNDHLMFKKHRLSVVYTNTYAKSVVNMADVIYKDQLKTRIVLVAMETWAADNKFAISENPLVTLREFMKYRRDFIKEKADAVHLFSGSQFESSRSGAAYIGGICSLLRGGGVNEFGKTDLMAVTLAQSLAHNIGIISDKRKLASGECKCEDTWSGCIMGDTGYYLPKKFTQCNIEEYHDFLNSGGGACLFNKPSKLLDPPECGNGFIETGEECDCGTPAECALEGAECCKKCTLTQDSQCSDGLCCKKCKFQPLGTVCREAVNDCDIREICSGNSSQCAPNVHKMDGYSCDGTQGICFGGRCKTRDRQCKYIWGQKVTASDRYCYEKLNIEGTEKGNCGKDKDTWTQCNKRDVLCGFLLCTNIGNIPRLGELDGEITSTLVVQQGRTLNCSGGHVKLEEDVDLGYVEDGTPCGPQMMCLEHRCLPMASFNFSTCLSNKAGTVCSGNGVCSNELKCVCNRHWTGADCGTHFPHNDDAKTGITLSGNGVAGTNIIIGIIAGTILVLALILGITAWGYKNYREQRQLPQGDYVKKPGDGDSFYSDFPPGGSADSASSSKKRSAFLSHFQISTCSITHYSISQNISLFCSRSNGLSHSWSERIPDTKHISDICENGRPRSNSWQGNVGGNKKKIRGKRFRPRSNSTEREPQAPEPGHSLAQTSPGISPGGSDSPQTGSLDHRTLSPAKSPSSSTGSIASSRKYPYPMPPLPDEEKTVNRQSARLWETSI