wanglab/gogpt-training-data huggingface dataset:
Protein: Carboxypeptidase SOL1 (EC 3.4.17.-) (Protein SUPPRESSOR OF LLP1 1) (Q9M9H7)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Possesses in vitro carboxypeptidase activity against the C-terminal arginine and lysine residues. Involved in the maturation of CLE19. Removes the C-terminal arginine residue of CLE19 proprotein. The cleavage of the C-terminal arginine residue is necessary for CLE19 activity in vivo. Is not involved in generating active CLV3. Is not involved in CLE19 or CLV3 perception.
Subcellular location: Endosome membrane {ECO:0000269|PubMed:24118638}; Single-pass type I membrane protein {ECO:0000255}.
Interaction partners:
- WAT1-related protein At3g28050
- CLAVATA3/ESR
- Metalloendoproteinase 5-MMP
- Metalloendoproteinase 3-MMP
- Protease Do-like 10, mitochondrial
- Protease Do-like 9
- Aminopeptidase M1
- Protein Brevis radix-like 1
- Metalloendoproteinase 2-MMP
Sequence:
MSKLRFFQSLLISTVICFFLPSINARGGHSDHIHPGDGNYSFHGIVRHLFAQEEPTPSLELTRGYMTNDDLEKAMKDFTKRCSKISRLYSIGKSVNGFPLWVIEISDRPGEIEAEPAFKYIGNVHGDEPVGRELLLRLANWICDNYKKDPLAQMIVENVHLHIMPSLNPDGFSIRKRNNANNVDLNRDFPDQFFPFNDDLNLRQPETKAIMTWLRDIRFTASATLHGGALVANFPWDGTEDKRKYYYACPDDETFRFLARIYSKSHRNMSLSKEFEEGITNGASWYPIYGGMQDWNYIYGGCFELTLEISDNKWPKASELSTIWDYNRKSMLNLVASLVKTGVHGRIFSLDKGKPLPGLVVVKGINYTVKAHQTYADYHRLLVPGQKYEVTASSPGYKSKTTTVWLGENAVTADFILIPETSSRGNQLRSSCDCSCKSCGQPLLTQFFTETNNGITLTLFVVVVFLCFLLQRRVRFNLWKQRQSSRRSITV
Protein: Uncharacterized protein (Q57W11)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MLRRRVISPVIAVPVQWTSGLMRHQVHNTGSLGKISYTPPGNSVPHLPWFRGAQTTKPAASTPVPPSMLNVKPSIPPLSMPSSTELDGILSITMMEEEASRVGAGARIMPENVGVLQSTAAQCGPMRATATRRMPVLTGPTLDTRIGDIIKADESLAAEMLPDIVRLLIDPNAEGVENVSLTDFASMQPKRQLAALNGKRSWLEWLLESSHYKQVSRLSLESPHYDLRALRLAGITTLYQWAEQPNLVKVSSCTRSLLDAAVDKSVETYVDEVVKLVNTSNMLEDTLVLWAADIIGKFILDSLNIPANHAMLQSGGIGFDGASTGHICTLEHYHRLVKKVIASVRREYMMQRHMGAQDNEAMKASLDPQAEAEIREKAYATLSDAMLRVLETQAPNMPKELHPLRDYGFLALERLPGLLRQTASALQLQSIPVRYFVFHNTGEWGFSPSTAMSTQMFTHSDSTRFSGAHPGGNSMIVSGNAPSALDVAAPTLAGGVFLTGSTNYNVTLGEWCGSPQPSSSPELWQGNPVQNEYFSVLHRLKRHTIRVARTTLFDAIKGADRLGKGFSAAEALGLQQLFGAGKLVEERLLSVLSGYYMSSSASKQLHFVEAGHSCGKTSVLERLSKRMAESGRTAITVRYSGSTTPFAPGLDDHPLAFAPRFWFRVALASCPYLVRTEEIFTRAPQSVMWWANRNNWSWELYQKRIRIRGHCEGAPPPLHAILVDDIDRVLDCMEHHIPQLTYPGGLMNSMDTNSTLQLSAGEATMGVGVPQNPQYHSPQNVEKGAASDIKAAGIPSPAPSGVGHHAQHEQQFTQDMVETALSKVTVALGQLNMVFTGHHVSKVLLVHADAPVRRYFVPLASGIGLQQRLRVLPLVSVLHALHQRFRLGFSGLMYEVLKNCPGLLGYTLDVFWSGRAALMDLRGGAPRLMQWSGTHPLLRSYVPSELFADLPQRNYLLRNPPEARMRLVELLQRQLSSPTGYLTRDVDTTLQDERDGLIVPYNHTACQVHPFALFTIFSHQDPLESPRETPIVRAWGEVWAEYCAVVSPMGTTSVRKRDALRVLLHGALLLRAVAVSGVQIDLNLKIPPYGFPLLASPTRSKQRGSAIPTIMKATPETVRKAGSAYRAFFANTLLERFPFRPSVGLNGGCDVVFVDGTTLALYDLVTTTEALRNISYRFAEALLGVLHCIEKNILPQHRIQTVHYVSVVSVDQASSTNSGMGGVSNGGEGANSRVSVLTTDEMFTATPVPIVPYFLDLSAVFEDSVIDRLRVLQEILGIDKEFRTLNDILDELESVYHVHVHQDVVASQAELESLLSSTLMQLVPDATVLPPYRAEVLPPNALMVDILDDEHEGSRRPEMERVESGAAVPHDAPTGDDFVGGDPIQDSAELLEAMMNDAFSSSAQEYPATPAQDPSATTASMESVAVGNPISSSIPAVENTPHPAATASQEDALAWLHDIVTPAAASSQESDRSSATAPIAAYPSASTSRPAVITAPLPFNRKSNSSVTHSAMGNRATSTAREPAAELKKVQEEVKRGKVSGQKIEVVEVEEVEVEEQSDVEQATRDNKGRGRSRGRVSGSGSGSGTDGKGSSTKAVTGKRGRKPLQRSNVPEKKPKQQQANLKRTVQSVTPKRSSSSSSTTAASSRGRNKSRELAKPAKRTTSRASVAAASKTDKNAKKKQKKSALRMV
Protein: Actinin alpha 4 (Actinin, alpha 4, isoform CRA_a) (F5GXS2)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MVDYHAANQSYQYGPSSAGNGAGGGGSMGDYMAQEDDWDRDLLLDPAWEKQQRKTFTAWCNSHLRKAGTQIENIDEDFRDGLKLMLLLEVISGERLPKPERGKMRVHKINNVNKALDFIASKGVKLVSIGAEEIVDGNAKMTLGMIWTIILRFAIQDISVEETSAKEGLLLWCQRKTAPYKNVNVQNFHISWKDGLAFNALIHRHRPELIEYDKLRKDDPVTNLNNAFEVAEKYLDIPKMLDAEDIVGTLRPDEKAIMTYVSCFYHAFSGAQKAETAANRICKVLAVNQENEHLMEDYEKLASDLLEWIRRTIPWLEDRVPQKTIQEMQQKLEDFRDYRRVHKPPKVQEKCQLEINFNTLQTKLRLSNRPAFMPSEGKMVSDINNGWQHLEQAEKGYEEWLLNEIRRLERLDHLAEKFRQKASIHEAWTDGKEAMLKHRDYETATLSDIKALIRKHEAFESDLAAHQDRVEQIAAIAQELNELDYYDSHNVNTRCQKICDQWDALGSLTHSRREALEKTEKQLEAIDQLHLEYAKRAAPFNNWMESAMEDLQDMFIVHTIEEIEGLISAHDQFKSTLPDADREREAILAIHKEAQRIAESNHIKLSGSNPYTTVTPQIINSKWEKVQQLVPKRDHALLEEQSKQQSNEHLRRQFASQANVVGPWIQTKMEEIGRISIEMNGTLEDQLSHLKQYERSIVDYKPNLDLLEQQHQLIQEALIFDNKHTNYTMEHIRVGWEQLLTTIARTINEVENQILTRDAKGISQEQMQEFRASFNHFDKDHGGALGPEEFKACLISLGYDVENDRQGEAEFNRIMSLVDPNHSGLVTFQAFIDFMSRETTDTDTADQVIASFKVLAGDKNFITAEELRRELPPDQAEYCIARMAPYQGPDAVPGALDYKSFSTALYGESDL
Protein: Outer membrane beta-barrel protein (Outer membrane protein H1) (Q51486)
Organism: Pseudomonas aeruginosa
Interaction partners:
Sequence:
MKALKTLFIATALLGSAAGVQAADNFVGLTWGETSNNIQKSKSLNRNLNSPNLDKVIDNTGTWGIRAGQQFEQGRYYATYENISDTSSGNKLRQQNLLGSYDAFLPIGDNNTKLFGGATLGLVKLEQDGKGFKRDSDVGYAAGLQAGILQELSKNASIEGGYRYLRTNASTEMTPHGGNKLGSLDLHSSSQFYLGANYKF
Protein: Condensin-2 complex subunit H2 (Chromosome-associated protein H2) (AtCAP-H2) (Non-SMC condensin II complex subunit H2) (Protein HYPERSENSITIVE TO EXCESS BORON 2) (Hypersensitive to excess B 2) (Q9LUR0)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Regulatory subunit of the condensin-2 complex, a complex that seems to provide chromosomes with an additional level of organization and rigidity and in establishing mitotic chromosome architecture (By similarity). The condensin-2 complex plays a role in DNA damage repair or in protecting the genome from certain genotoxic stressors (e.g. boron excess, zeocin and aphidicolin).
Subcellular location: Nucleus, nucleolus {ECO:0000269|PubMed:15883832}. Chromosome {ECO:0000269|PubMed:15883832}. Note=Localized at mitotic chromosomes from pro-metaphase to telophase. During interphase, mainly found in nucleolus.
Interaction partners:
- ARM repeat superfamily protein
- Condensin-2 complex subunit CAP-D3
- Structural maintenance of chromosomes protein 2-1
- Structural maintenance of chromosomes protein 2-2
- Structural maintenance of chromosomes protein 4
- Structural maintenance of chromosomes protein
- Condensin complex subunit 2
- Structural maintenance of chromosomes protein 5
- Structural maintenance of chromosomes protein 6B
- Retinoblastoma-related protein 1
Sequence:
MTSHGGGEVRGERIHTVQPERDLVANWEVDLSEKLEEYLLKICSGEITGNEEDGQIPVNFAEAALLLQGSVQVYSKKVEYLYNLVLRTLEFLSKQRDQEQSKGTSNENEASSSRQVDEEENDLFWNVDDIPVDTKNRLDSSVGGDTCPSQFVKPPANLVVLEGDCLDTSGDGGELESYLLATTHLYRDFILLDPCDAVAVNEFLGDNYGGKGRNSAHRGSSVRKSFHSSVGRSGGSARKSSVGKNQGTNVHLSPICGNGPNDQNCDQGSQPPVFEDNDHGFDMDNEYGGAMDFSDTDADEDDPWKPLNPYEPGKLKVKPFKKVKILKKIGWSITKDHMTSMFPLARPNGPISSELIEIWKMHGCASKDEQASQDIPYYEKLREMLVNGGNQPCGANGNYNDNDKDNHDEANNGDFHDFGEHDGDDAEHPFMDEDVLNMNDGGAAEFHNYDGFENGESNCQESLEDLCRSHLDALLANIAKSEKQTDLAARVSTWKQKIEQNLEEQELHPPFDIQEYGDRIINKLTVEESGNVETFTDLMKDQEKHEVARAFSALLQLVNNGDVDLEKPGNSTNEPMCYTAVKPFSVRLLKVHNRKNEKRGIHLPQKRAKSPITKGKSHESPPPKKRNTCSVSSQTRKVSLKISKINGVGVRCTPNSKKRRKGRSDDVTEVTEVASIEKSLGKL
Protein: Interferon-induced GTP-binding protein Mx2 (Myxovirus resistance protein 2) (A0MWD1)
Organism: Bubalus bubalis (Domestic water buffalo)
Function: Interferon-induced dynamin-like GTPase with antiviral activity against vesicular stomatitis virus (VSV).
Subcellular location: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
Interaction partners:
Sequence:
MSLSFRPLKYKRHTQTSTPHHPKQDIYFHEQPPGPPLGQTMSPPQWQVEESNPGFLPNNFSQLNLDPQQPEANGGQQRSKGPENNLYRKYEEKVRPCIDLIDSLRALGVEQDLALPAIAVIGDQSSGKSSVLEALSGVALPRGSGIITRCPLVLKLTKRECEWTGKITYRNITQQLQNPSEVEWEIRRAQNIIAGNGRGISHELINLEVTSPDVPDLTLIDLPGITRVAVENQPQDIGLQIKALIIQRQETINLVVVPCNVDIATKKYTEALSMAQEVDPDGDRTIGILTKPDLVDKGTEKGVLKVMQNLTYHLKKGYMIVKCRGQQDITNKLSLAEATRKETMFFETHPYFRVLLDEGKATMPLLAERLTTELIWHINKSLPLLENQIKEKHQRATEELQQYGDDIPSDEGDKMFFLIEKIKVFNEDIGKLIEGEEIVMETESRLCNKIREEFTSWILILTTNIEKVKSILNEEVSKYEKKYRGKELLGFVNYKTFETVVKHYLGQLIDPALKMLQKAMEIVWQTFKDTAKKHFAEFCNLHQTVQNKIEDIKTKQMAEAANLIQLQFKMEKLVFCQDQIYGVVLNKVREDIFNSMGKASETPQSKQPFLNDQSSISSIVEIGVHLNAYFMETSKRLANQIPFIIQYFMLQENGDKVQKAMMQLLQDTQHYSWLLQEQSDTATKRKFLKEKIFRLTQAQQALYEFPHFKG
Protein: Calsequestrin (A0A0R4IKE0)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Sarcoplasmic reticulum lumen {ECO:0000256|ARBA:ARBA00004564}.
Interaction partners:
- Si:ch211-199i15.5.
- Ryanodine receptor 2b
- Ryanodine receptor 1a
- Ryanodine receptor 3.
- Triadin.
- Ryanodine receptor 1b
- Aspartyl/asparaginyl beta-hydroxylase isoform X3
- Uncharacterized protein.
- Calsequestrin
- Aspartate beta-hydroxylase
Sequence:
MKWNLVFLGLLLTFGQLSWGQKGMDIPEYDGKDRVHELNAKNYKSVMKKYDVMVVYYHEHVGSSKVAQKQFQIEELALELAAQVLADFDDEDIGIGLLDEKTDKAVAKKLGLDEADSIFIFIEDEVIEYDGELAADTLVEFIYDVIEDPVEIIGNVREMKGFNNIEEDIKLVGFFKSAKSDHYHEYEDAAEEFHPHIKFFATFNPKVALKLGLKLNEVDFYEPFMDKPVVIPGKPYSEKELVRFIEDNDRPTLRKMQPHNMYEIWEDALDGEHIIAFAEEGDPDGFEFLEIVKEVAEDNTENPDLSIIWIDPDDFPLLVHYWEKTFDIDLSSPQIGVVEVDDAESIWFDMDDDDMPTVDELEDWLEDVLENKIDPDDDDDDDDDDDDDDDDDDDDDDDDDDDDDDDDDDDDDDDDDDDDDDDDDDDDDDDDDDDDDDDDDDDDDDDDDDDDDDDDDDDDDDDDDDDDDDDDDDDDDDDDDDDDDDDDDDDDDDDDDDDDDDDDDDDDDDDDDDDDDDDDNDDDDDDDDDDDDDDDDDDDDDDDDDDDDDDDDD
Protein: Antitoxin VapB20 (P9WJ45)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: Antitoxin component of a type II toxin-antitoxin (TA) system. Upon expression in E.coli neutralizes the toxic effect of cognate toxin VapC20.
Interaction partners:
- 23S rRNA-specific endonuclease VapC20
Sequence:
MKRLQIYIDEDVDRALAVEARRRRTSKAALIREYVAEHLRQPGPDPVDAFVGSFVGEADLSASVDDVVYGKHE
Protein: SnoRNA-binding rRNA-processing protein (Q59Y40)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Subcellular location: Nucleus, nucleolus {ECO:0000256|ARBA:ARBA00004604}.
Interaction partners:
- SnoRNA-binding rRNA-processing protein
- U3 small nucleolar RNA-associated protein 10
- SnoRNA-binding rRNA-processing protein
- U three protein 7
- rRNA 2'-O-methyltransferase fibrillarin
- SnoRNA-binding rRNA-processing protein
- GTPase
- Utp4p
- Utp8p
- U3 small nucleolar ribonucleoprotein protein MPP10
Sequence:
MSSTKQDLPQARAPTLPSKTTPEQRYWRSYITPQLIKENHPITSIEFNPTTPNDFAIASATKIQVFSSKTRQVIKTFSRFKDVVYSGNYRYDGKLLVASDASGLVSIYDSYQPRNLLVSLTPSSHPTHVAKFHPTIGNQLITGSDDRMLRVYDISQTSNGPIIQFDNIDHEDYIRSVNFIPGDSNLIVTGCYDGNVRILDVRDPHRVVAKFDQENPVEDILAVSSNTLVSAGGPYVKIWDLNRMSQIHQLNNFNKSTTCLSNTHTNGLMVGSLDSTIKVFDYTSTNWQVQFGWKFGSGVLSCGVSPINQKHFVAGLTSGLISIRTKKTEPKVKQGIKNDVSGGYARMMKGRDYTGEEEDHIIESSKIITNKTNKSVNELMSSYKKYLGASGSIDDIKPNDLKQEISQCLKAKEICGMLELLGV
Protein: Somatolactin beta (Q330P5)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Secreted {ECO:0000256|ARBA:ARBA00004613, ECO:0000256|RuleBase:RU003618}.
Interaction partners:
Sequence:
MKKATALQVCVVVLVCLKKAVIGSPVECPDQEIGGTSCTISAEKLLDRAVQHAELIYRFSEEAKLLFDELLDLFGGMNQYIPGGAVCAPKTVPVPLSKSEIQQISDRWLLHSVLILVQFWIEPLVNLQKSLENYKSAPIGLLSRNQWIASKLSSLEEGLLVLIRQILGEGGLVLGPPEDVSDNTLSVDAFETVRRDYSVIYCFRKDAHKIQTFLKLLKCRQVDRENCSLF
Protein: Aryl hydrocarbon receptor nuclear translocator (ARNT protein) (Dioxin receptor, nuclear translocator) (Hypoxia-inducible factor 1-beta) (HIF-1-beta) (HIF1-beta) (P41739)
Organism: Rattus norvegicus (Rat)
Function: Required for activity of the AHR. Upon ligand binding, AHR translocates into the nucleus, where it heterodimerizes with ARNT and induces transcription by binding to xenobiotic response elements (XRE). Not required for the ligand-binding subunit to translocate from the cytosol to the nucleus after ligand binding. The complex initiates transcription of genes involved in the regulation of a variety of biological processes, including angiogenesis, hematopoiesis, drug and lipid metabolism, cell motility and immune modulation (By similarity). The heterodimer binds to core DNA sequence 5'-TACGTG-3' within the hypoxia response element (HRE) of target gene promoters and functions as a transcriptional regulator of the adaptive response to hypoxia (By similarity). The heterodimer ARNT:AHR binds to core DNA sequence 5'-TGCGTG-3' within the dioxin response element (DRE) of target gene promoters and activates their transcription (By similarity).
Subcellular location: Nucleus {ECO:0000250|UniProtKB:P27540}.
Interaction partners:
- Hypoxia-inducible factor 1-alpha
- Endothelial PAS domain-containing protein 1
- Hypoxia-inducible factor 3-alpha
- Aryl hydrocarbon receptor
- Histone lysine acetyltransferase CREBBP
- Neuronal PAS domain-containing protein 4
- Aryl hydrocarbon receptor nuclear translocator 2
- Aryl hydrocarbon receptor repressor
- SIM bHLH transcription factor 1
- Neuronal PAS domain-containing protein 1
Sequence:
MAATTANPEMTSDVPSLGPTIASGNPGPGIQGGGAVVQRAIKRRSGLDFDDEGEVNSKFLRCDDEQMCNDKERFARSDDEQSSADKERLARENHSEIERRRRNKMTAYITELSDMVPTCSALARKPDKLTILRMAVSHMKSLRGTGNTSTDGSYKPSFLTDQELKHLILEAADGFLFIVSCETGRVVYVSDSVTPVLNQPQSEWFGSTLYDQVHPDDVDKLREQLSTSENALTGRILDLKTGTVKKEGQQSSMRMCMGSRRSFICRMRCGTSSVDPVSMNRLSFLRNRCRNGLGSVKEGEPHFVVVHCTGYIKAWPPAGVSLPDDDPEAGQGSKFCLVAIGRLQVTSSPNCTDMSNICQPTEFISRHNIEGIFTFVDHRCVATVGYQPQELLGKNIVEFCHPEDQQLLRDSFQQVVKLKGQVLSVMFRFRAKNREWLWMRTSSFTFQNPYSDEMSIFICTNTNVKNSSQEPRPTLSNTIQRSQLGPTTNLSLEMGTGVLASRQQQQQQQQQQQQQQQQTELDMVPGRDGLASYSHSQVSVQPVATAGSEHSKPLEKSEGLFVQDRDPRFSEIYPNISADQSKGLSSSTVPATQQLFSQGSSFPPNPRPAENFRNSGLTPPVTIVQPSSSAGQILAQISRHSNLTQGSAPTWTSSTRPGFSAQLPTQATAKTRSSQFGVNNFQTSSSFSAMSLPGAPTASPSTAAYPTLPNRGSNFPPETGQTTGQFQTRTAEGVGVWPQWQGQQPHHRSSSNEQHVQPTSAQPSSQPEVFQEMLSMLGDQSNTYNNEEFPDLTMFPPFSE
Protein: Triacylglycerol lipase ptl2 (EC 3.1.1.3) (O14115)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Lipid particle-localized triacylglycerol (TAG) lipase. The lipid droplet/particle is a lipid storage compartment which serves as a depot of energy and building blocks for membrane lipid biosynthesis. Involved in the mobilization of the non-polar storage lipids triacylglycerols (TAGs) from lipid particles by hydrolysis of TAGs, releasing and supplying specific fatty acids to the appropriate metabolic pathways.
Subcellular location: Lipid droplet {ECO:0000250|UniProtKB:P36165}.
Interaction partners:
- Putative phospholipase A2
- Small COPII coat GTPase sar1
- Meiotic coiled-coil protein 4
- Acetyl-CoA carboxylase
Sequence:
MSIPEESEINKDYTVQEDLDEFAKYTCVYKKRHDEKIEYITAQHDWNPVYEAVVPRKSKPGKDEKREGFMYPILRWPLMFTAFLCLTFVAFLYLLDRLYINCYEYFIVWRGEARRLRKLLQEAKTYEEWKERARALDKYFGNDEWKLDPVYDYYDYTLVQAVYSSLVKHREQKDWNALKSVLDVCVRSNFGGIDSSMLYSRTYSGTKKLVEDYVNELKVCLETVIDQRLYTAQERSKMFEYFSHNYGRTALCLSGGASFAIYHTGVLRALLNQDLIPNVITGTSGGGLLAALVCTRTNEELKQLLVPELASKYQSDIGNWLDATKRYFRTGARFDEILWAKTCMYFTRGSLTFAEAYKRTGRILNISVIPSDVHSPPKLINYLTSPDTVIWSAVIASCAVPGILNPIPLMTRSQSHRLIPHNFGNRFKDGSLRTDIPLSELRTQFNVHFSIVSQTNPHVQVFFFSPRGTVGRPVSHRKGRGWRGGYVGSAIEQFLKYDMIKWLHVIRSLELLPRPLGTDWSSVFLQKFDGTITIWPKTKFQDFYYILSPPSVERLGYMIDAGQAATFPKLDFIAARMTIEKLIEKGRMMDKPSKLGRSIDGTIGTSMSRGDIEISQESASISPEDIDIVN
Protein: Cytochrome P450 3A (EC 1.14.14.-) (Q9PU44)
Organism: Gallus gallus (Chicken)
Subcellular location: Endoplasmic reticulum membrane {ECO:0000256|ARBA:ARBA00004406, ECO:0000256|RuleBase:RU368049}; Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004406}. Microsome membrane {ECO:0000256|ARBA:ARBA00004174, ECO:0000256|RuleBase:RU368049}; Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004174}.
Interaction partners:
Sequence:
MNFLPFFSIETWIILLIFVVLLIIYGTWPFGLFKKLGIPGPRPLPFFGTCLEYRKGFLDFDTECFQKYGKIWGIYDGRQPAVVVMDPQIIKTVLVKECYSTFTNRRRTDLAGVLRNAVSLAEDDQWKRLRTVLSPTFTSGKLKEMFPTMKYFGEMLVKNIQKRVEKNSSVPVKDFFGSYSMDVVTSTSFGVNIDSMNNPKSPFVREMQKLTKFDFFDPVFILSFVCPFLTPLMAKMNISFFPSDAVDFFMRSIDKIKKDRERETHTGRVDFLQMMIESQKSDSNGSSDAKHSYKALSDIEVLSQAFIFIFAGYEPTSNTLGYLAYQLALHPDVQQKVVNEIDTILPNKAPLTYEAIMQLEYLDMAVNETLRLYPLGGRLERTCKRDVEINGVTIPKGTIVIIPPYTLHRSPEYWPNPEEFRPERFSKENKDNIDPYTYLPFGAGPRNCIGMRFALLTLKVAITAVLQHFTFQVCKETQIPLKLQSLGLTTPEKPIVLKLVPRTNTAKA
Protein: RNA-binding protein Ro60 (60 kDa SS-A/Ro ribonucleoprotein) (60 kDa Ro protein) (60 kDa ribonucleoprotein Ro) (RoRNP) (TROVE domain family member 2) (O08848)
Organism: Mus musculus (Mouse)
Function: RNA-binding protein that binds to misfolded non-coding RNAs, pre-5S rRNA, and several small cytoplasmic RNA molecules known as Y RNAs (By similarity). May play roles in cilia formation and/or maintenance.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:P10155}. Note=Localized in cytoplasmic mRNP granules containing untranslated mRNAs. {ECO:0000250|UniProtKB:P10155}.
Interaction partners:
- E3 ubiquitin-protein ligase TRIM21
- Lupus La protein homolog
- Major centromere autoantigen B
Sequence:
MEGSANQLQPLSETQVVNSEGGCVWQVTDMNRLRRFLCFGSEGGTYYIKEQKLGLENAEALIRLIEDGRGCEVIQEIKSFSQEGRTAKQEPLLFALAVCSQCADINTKQAAFKAVPEVCRIPTHLFTFIQFKKDLKESMKCGMWGRALRKAVADWYNEKGGMAVALVVTKYKQRNGWSHKDLLRLSHLKPSSEGLAIVTKYITKGWKEVHEEYKEKALSVEAEKLLKYLEAVEKVKRTKDDLEVIHLIEEHQLVREHLLTNHLKSKEVWKALLQEMPLTALLRNLGKMTANSVLEPGNSEVSLICEKLSNEKLLKKARIHPFHVLIALETYRAGHGLRGKLKWIPDKDILQALDAAFYTTFKTVEPTGKRFLLAVDVSASMNQRALGSVLNASTVAAAMCMVVTRTEKESSVVAFACDMVPFPVTTDMTLQQVLTAMNKVPAGNTDCSLPMIWAQKTDTAADVFVVFTDNETFAGQVHPAVALREYRKKMDIPAKLIVCGMTSNGFTIADPDDRGMLDMCGFDTAALDVIRNFTLDVI
Protein: Sp3 transcription factor (A0A0G2K5M1)
Organism: Rattus norvegicus (Rat)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- Transcription factor Sp1
Sequence:
LPLFFANWIKLSQMIHHNIFVFFIQTGDLASAQLGGAPNRWEVLSATPTTIKDEAGNLVQIPGAATSSGQYVLPLQNLQNQQIFSVAPGSDSSNGTVSNVQYQVIPQIQSTDAQQVQIGFTGSSDNGGINQESSQIQIIPGSNQTLLASGTPPANIQNLIPQTGQVQVQGVAIGGSSFPGQTQVVANVPLGLPGNITFVPINSVDLDSLGLSGSSQTMTAGINADGHLINTGQAMDSSDNSERTGERVSPDVNETNADTDLFVPTSSSSQLPVTIDSTGILQQNTNSLTTTSGQVHSSDLQGNYIQSPVSEETQAQNIQVSTAQPVVQHLQLQDSQQPTSQAQIVQGITPQTIHGVQASGQNISQQALQNLQLQLNPGTFLIQAQTVTPSGQITWQTFQVQGVQNLQNLQIQNTAAQQITLTPVQTLTLGQVAAGGALTSTPVSLSTGQLPNLQTVTVNSIDSTGIQLHPGENADSPADIRIKEEEPDPEEWQLSGDSTLNTNDLTHLRVQVVDEEGDQQHQEGKRLRRVACTCPNCKEGGGRGTNLGKKKQHICHIPGCGKVYGKTSHLRAHLRWHSGERPFICNWMFCGKRFTRSDELQRHRRTHTGEKKFVCPECSKRFMRSDHLAKHIKTHQNKKVIHSSSTVLASVEAGRDDALITAGGTTLILANIQQGSVSGIGTVNASATSNQDILTNTEIPLQLVTVSGNETME
Protein: Swarming motility protein SwrC (O31501)
Organism: Bacillus subtilis (strain 168)
Function: Required for self-resistance to surfactin, an antimicrobial lipopeptide surfactant produced by B.subtilis. Also required for swarming motility.
Interaction partners:
- Putative efflux system protein YvrP
- Putative efflux system component YknX
- Sec translocon accessory complex subunit YrbF
Sequence:
MNHVINFVLKNKFAVWLMTIIVTAAGLYAGMNMKQESIPDVNMPYLTISTTYPGATPSQVADEVTKPVEQAVQNLDGVSVVTSTSYENASSVMIEYDYEKDMDKAKTEAAEALENVNLPDDAKDPEISRYSLNSFPILTLSVSSDKDNLQELTKQVEDSLVSKLEGIEGVASVQVSGQQVEEVEFSFKEDKLKEYGLDEDTVKQVIQGSDVTTPLGLYTFGNEEKSVVVSGDIETIKDLKNMRIPTASASSAGSSAASQAGAQSAQAAQSAQAAAQVQQSASTAVPTVKLSDIATIKDVKKAESVSRTNGKDSIGINIVKANDANTVEVADDVKAELKKFKEDHKGFNYSATLDMAEPITQSVDTMLSKAIFGAIFAIVIILLFLRDIKSTLISVVSIPLSLLIALLVLQQLDITLNIMTLGAMTVAIGRVVDDSIVVIENIYRRMRLKDEPLRGKALVREATKEMFKPIMSSTIVTIAVFLPLALVGGQIGELFIPFALTIVFALAASLVISITLVPMLAHSLFKKSLTGAPIKAKEHKPGRLANIYKKVLNWALSHKWITSIIAVLMLLGSLFLVPLIGASYLPSEEEKTMQLTYSPEPGETKKEAENEAEKAEKILLDRKHVDTVQYSLGSGSPLAGGDSNGALFYIKYESDTPDFDKEKDNVLKEIQKQSDRGEWKSQDFSSSGNNNELTYYVYGDSENDIKDTVKDIEKIMKDEKDLKNVNSGLSSTYDEYTFVADQEKLSKLGLTASQISQALMSQTSQEPLTTVKKDGKELDVNIKTEKDEYKSVKDLENKKITSATGQEVKIGDVAKVKEGSTSDTVSKRDGKVYADVTGEVTSDNVTAVSAAIQKKIDKLDHPDNVSIDTGGVSADIADSFTKLGLAMLAAIAIVYLVLVITFGGALAPFAILFSLPFTVIGALVGLYVSGETISLNAMIGMLMLIGIVVTNAIVLIDRVIHKEAEGLSTREALLEAGSTRLRPILMTAIATIGALIPLALGFEGGSQVISKGLGVTVIGGLISSTLLTLLIVPIVYEVLAKFRKKKPGTEEE
Protein: Inclusion membrane protein A (P0DPS5)
Organism: Chlamydia trachomatis
Function: Chlamydia replicate within a host intracellular vacuole, termed an inclusion. IncA is probably involved in the homotypic fusion of inclusions.
Subcellular location: Secreted {ECO:0000250|UniProtKB:A0A0H3MD02}. Host vacuole, host pathogen-containing vacuole, host pathogen-containing vacuole membrane {ECO:0000269|PubMed:9826388, ECO:0000305|PubMed:11402010}; Multi-pass membrane protein {ECO:0000255}. Note=Secreted, probably by a type III secretion system. Localized in the inclusion membrane (Probable) (PubMed:9826388). In the inclusion, the C-terminus faces the host cytosol (By similarity). {ECO:0000250|UniProtKB:A0A0H3MD02, ECO:0000269|PubMed:9826388, ECO:0000305|PubMed:11402010}.
Interaction partners:
Sequence:
MTTPTLIVTPPSPPAPSYSANRVPQPSLMDKIKKIAAIASLILIGTIGFLALLGHLVGFLIAPQITIVLLALFITSLAGNALYLQKTANLHLYQDLQREVGSLKEINFMLSVLQKEFLHLSKEFATTSKDLSAVSQDFYSCLQGFRDNYKGFESLLDEYKNSTEEMRKLFSQEIIADLKSSVASLREEIRFLTPLAEEVRRLAHNRESLTAAIEELKTIRDSLRDEIGQLSQLSRTLTSQIALQRKESSDLCSQIRETLSSPRKSASPSTKSS
Protein: C2H2-like zinc finger protein (F10A5.10) (Q9LR10)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- Nuclear pore complex protein NUP205
- Nuclear pore complex protein NUP88
- Nuclear pore complex protein NUP155
- Protein SEH1
- Nuclear pore complex protein NUP107
- Nuclear pore complex protein NUP54
- Nuclear pore complex protein NUP160
- 1-acyl-sn-glycerol-3-phosphate acyltransferase
- Nuclear pore complex protein NUP93B
- Nuclear pore complex protein NUP93A
Sequence:
MALLTFLPENAEAPQKHKPTSSKRKKRDNPTDQTQTQKHKPQKPKKAVPPKQPSSWDQIKNLLTCKQIEGSRVHDPSKNSQSGPSMTTNLSPSKLGSSCSSICSFRDVAHGNTRVVHRADHSPDVGNSATPNSETRLLTRKPGQHGSSSSRSLTSGSTRSNASGSYTSSSTTSFRAMQFRKLSGCYECHMIVDPSRYPISPRVCACSQCGEVFPKLESLELHQAVRHAVSELGPEDSGRNIVEIIFKSSWLKKDSPICQIERILKVHNTQRTIQRFEDCRDAVKARALQATRKDARCAADGNELLRFHCTTLTCSLGARGSSSLCSNLPVCGVCTVIRHGFQGKSGGGGANVANAGVRTTASSGRADDLLRCSDDARRVMLVCRVIAGRVKRVDLPAADASATAEKKSTVEDNSVVGVSSSGGTFDSVAVNAGVYSNLEELVVYNPRAILPCFVVIYKVLES
Protein: Putative myrosinase 3 (EC 3.2.1.147) (Beta-glucosidase 39) (AtBGLU39) (Sinigrinase 3) (Thioglucosidase 3) (Q3E8E5)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- Nitrilase 3
- Nitrilase 2
- Nitrilase 1
- Cytochrome P450 71A12
- Indoleacetaldoxime dehydratase
- Cytochrome P450 71A18
- Cytosolic sulfotransferase 16
- N-
Sequence:
MKFRALGLVLLLAVETCKAEEITCEETKPFTCNQTDRFNRKHFDDDFIFEGGKGRGLNVWDGFTHRYPEKGGPDLGNGDSTCGSYEHWQKDIDVMTELGVDGYRFSLAWSRIAPRESNQAGVKYYNDLIDGLLAKNITPFVTLFHWDLPQVLQDEYEGFLNHEIIDDFKDYANLCFKIFGDRVKKWITINQLYTVPTRGYAMGTDAPEPYIVAHNQLLAHAKVVHLYRKKYKPKQRGQIGVVMITRWFVPYDSTQANIDATERNKEFFLGWFMEPLTKGKYPDIMRKLVGRRLPKFNKKEAKLVKGSYDFLGINYYQTQYVYAIPANPPNRLTVLNDSLSAFSYENKDGPIGPWFNADSYYHPRGILNVLEHFKTKYGNPLVYITENGELLILSGCNVKGYFAWCLGDNYELWPSRSFHVSPFYLLHRKDKGAFPSFEA
Protein: Probable gamma-glutamyltranspeptidase GgtB (Gamma-glutamyltransferase) (Glutamyl transpeptidase) (P71750)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Interaction partners:
- Sulfite reductase [ferredoxin]
- Adenosine 5'-phosphosulfate reductase
- Ferrochelatase Che1
- Putative glutamate--cysteine ligase 2
- Probable 5-oxoprolinase OplA
- Glutathione hydrolase proenzyme
- Probable cytosol aminopeptidase
- Glutamate decarboxylase
- Aminopeptidase N
- Glutamate--cysteine ligase EgtA
Sequence:
MSVWLRAGALVAAVMLSLSGCGGFHAGAPSTAGPCEIVPNGTPAPKTPPATVPSSRNLATNPEIATGYRRDMTVVRTAHYAAATANPLATQVACRVLRDGGTAADAVVAAQAVLGLVEPQSSGIGGGGYLVYFDARTGSVQAYDGREVAPAAATENYLRWVSDVDRSAPRPNARASGRSIGVPGILRMLEMVHNEHGRTPWRDLFGPAVTLADGGFDISARMGAAISDAAPQLRDDPEARKYFLNPDGSPKPAGTRLTNPAYSKTLSAIASAGANAFYSGDIAHDIVAAASDTSNGRTPGLLTIEDLAGYLAKRRQPLCTTYRGREICGMPSSGGVAVAATLGILEHFPMSDYAPSKVDLNGGRPTVMGVHLIAEAERLAYADRDQYIADVDFVRLPGGSLTTLVDPGYLAARAALISPQHSMGSARPGDFGAPTAVAPPVPEHGTSHLSVVDSYGNAATLTTTVESSFGSYHLVDGFILNNQLSDFSAEPHATDGSPVANRVEPGKRPRSSMAPTLVFDHSSAGRGALYAVLGSPGGSMIIQFVVKTLVAMLDWGLNPQQAVSLVDFGAANSPHTNLGGENPEINTSDDGDHDPLVQGLRALGHRVNLAEQSSGLSAITRSEAGWAGGADPRREGAVMGDDA
Protein: trypsin (EC 3.4.21.4) (Q9VSV4)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Secreted, extracellular space {ECO:0000256|ARBA:ARBA00004239}.
Interaction partners:
Sequence:
MSSQNLFVLLVISFFPLYNCLGDSPRNAFSSLNRVKRLSDGDFDEDSIALSNYCVSLRSRSAEKFFGDNHFCSGVILAPMFVMTSAHCLINKRRVLISSRVLLIVAGTLNRLKYIPNRTFVTPVTHIWLPDSFTMRNKQDFGLLKVKNPFPRNNEHISIARLPVHPPLPGLKCKVMGWGRMYKGGPLASYMLYIDVQVIDSEACAKWLRVPSVEHVCAVDSDDLTAQQPCGGDWGAPMLHNGTVYGIVTILAGCGVSHLPSLYTNVHSNANWIHEKIISSAGSILLVPPLFRYLSIALIYVVTLFNFVMKYNGVM
Protein: Glutathione S transferase O3 (EC 1.8.5.1, EC 2.5.1.18) (Glutathione S-transferase omega class) (RE55344p) (Q9VSL2)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Glutathione peroxidase
- AT18092p
- glutathione-specific gamma-glutamylcyclotransferase
- Glutathione peroxidase
- glutathione-specific gamma-glutamylcyclotransferase
- 1-Cys peroxiredoxin
- Uncharacterized protein, isoform C
- RE13973p
- Gamma-glutamyl transpeptidase, isoform A
- RE21057p
Sequence:
MSSGKHLAKGSPKPVLPDDGVLRLYSMRFCPYAQRAHLVLNAKNVPYHSVYINLTEKPEWLVEVSPLLKVPALQLVAEKGEPSLIESLIIAEYLDDKYPENPLLPKDPLKRAQDKILLERFSSITSAFINILVQGTGLEDYWTALDIFEEELTKRGTPYFGGNKPGFVDYMIWPWFERLSVIELKLQKEYNFNESRFPKITKWIALLKADSVVQSFYATPEQHNEFWRTRKAGNANYDLLA