wanglab/gogpt-training-data huggingface dataset:
Protein: Transcription factor tau 95 kDa subunit (TFIIIC 95 kDa subunit) (Transcription factor C subunit 1) (P32367)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: TFIIIC mediates tRNA and 5S RNA gene activation by binding to intragenic promoter elements. Upstream of the transcription start site, TFIIIC assembles the initiation complex TFIIIB-TFIIIC-tDNA, which is sufficient for RNA polymerase III recruitment and function. Part of the tauA domain of TFIIIC that binds boxA DNA promoter sites of tRNA and similar genes. Participates in the interconnection of tauA with tauB via its contacts with TFC3 and TFC6. Serves as a scaffold critical for tauA-DNA spatial configuration and tauB-DNA stability.
Subcellular location: Nucleus {ECO:0000269|PubMed:14562095}.
Interaction partners:
- Transcription factor tau 60 kDa subunit
- Transcription factor tau 55 kDa subunit
- Transcription factor tau 91 kDa subunit
- Transcription factor tau 138 kDa subunit
- Transcription factor tau 131 kDa subunit
- Transcription factor IIIB 70 kDa subunit
- Transcription factor TFIIIB component B''
- TATA-box-binding protein
- Transcription factor IIIA
- SAGA complex/transcription factor TFIID complex subunit TAF10
Sequence:
MPVEEPLATLSSIPDSSADQAPPLIADEFTLDLPRIPSLELPLNVSTKHSSIQKAIKMCGGIEKVKEAFKEHGPIESQHGLQLYLNDDTDSDGSKSYFNEHPVIGKRVPFRDESVILKVTMPKGTLSKNNNSVKDSIKSLKDSNKLRVTPVSIVDNTIKFREMSDFQIKLDNVPSAREFKSSFGSLEWNNFKSFVNSVPDNDSQPQENIGNLILDRSVKIPSTDFQLPPPPKLSMVGFPLLYKYKANPFAKKKKNGVTEVKGTYIKNYQLFVHDLSDKTVIPSQAHEQVLYDFEVAKKTKVYPGTKSDSKFYESLEECLKILRELFARRPIWVKRHLDGIVPKKIHHTMKIALALISYRFTMGPWRNTYIKFGIDPRSSVEYAQYQTEYFKIERKLLSSPIVKKNVPKPPPLVFESDTPGGIDSRFKFDGKRIPWYLMLQIDLLIGEPNIAEVFHNVEYLDKANELTGWFKELDLVKIRRIVKYELGCMVQGNYEYNKYKLKYFKTMLFVKESMVPENKNSEEGMGVNTNKDADGDINMDAGSQMSSNAIEEDKGIAAGDDFDDNGAITEEPDDAALENEEMDTDQNLKVPASIDDDVDDVDADEEEQESFDVKTASFQDIINKIAKLDPKTAETMKSELKGFVDEVDL
Protein: Multidrug transporter FLR2 (Drug:H(+) antiporter FLR2) (DHA FLR2) (Flucytosine exporter FLR2) (Q6FRT5)
Organism: Candida glabrata (strain ATCC 2001 / BCRC 20586 / JCM 3761 / NBRC 0622 / NRRL Y-65 / CBS 138) (Yeast) (Nakaseomyces glabratus)
Function: Multidrug transporter that confers resistance to 5-flucytosine (5-FC) and clotrimazole. Further confers azole drug resistance. Plays direct roles in extrusion of 5-flucytosine and clotrimazole.
Subcellular location: Cell membrane {ECO:0000269|PubMed:28066366}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
Sequence:
MYIGAFQDTLFVDMLEYFGWVTVGKEYLDIYRPNGVPVAPNAVAASISGKEEMKQDNQTSTDSMSTSTQQETDASNEDIERAMDTDNGLDKAMSGGQGVFGTEEDDSSTKDASKPEEADPFLVEFLGEDDPRKPWNWSFSKKTFVIVQLMVLTCINYMGSSIYTPGQEQIQHEFHVGHVVGTLNLSMYVLGYAIGPIIFSPLSEVSSIGRMPLYLWTFILFTILQVACALVRNIAGLVILRFITGILCSPVLATGGASVGDVCFPRYVPRFLGAWAVGAVAAPVMAPILGAAMVVAKDWRWIFWLMLFMCGATLLSIIFFFPETSHECILHRRAKRLRKLTGDDRYYTKKEKQEEALPVSVFIKNTLWRPIKMIALEPIILAFDVYIALCYGAFYLFFEAFPIVFAGIYHFTLVEVGLAFLGFCVGCVFAYTALIIFQEKVIRKKFLEGKFRPELFLILAMCLGWCLPFSLFFFGWTARIHWILPIIAELFFVLSVFNLFQATFSYLAVCYPEYVASVFAGNGLCRGAFAAAFPLFGKAMYDRLSTKKYPVAWGSTLIGFITVVLSLIPFVLYKYGPALRARSRFSPDS
Protein: Aspartate beta-hydroxylase (E5RG29)
Organism: Homo sapiens (Human)
Subcellular location: Sarcoplasmic reticulum membrane {ECO:0000256|ARBA:ARBA00004157}; Single-pass type II membrane protein {ECO:0000256|ARBA:ARBA00004157}.
Interaction partners:
Sequence:
MAEDKETKHGGHKNGRKGGLSGTSFFTWFMVIALLGVWTSVAVVWFDLVDYEEVLGKLGIYDADGDGDFDVDDAKVLLGLKERSTSEPAVPPEEAEPHTEPEEQVPVEAEPQNIEDEAKEQIQSLLHEMVHAEHETEHSYHVEETDSSEPVVEDERLHHDTDDVTYQVYEEQAVYEPLENEGIEITEVTAPPEDNPVE
Protein: Flotillin-1 (Reggie-2) (REG-2) (O13127)
Organism: Carassius auratus (Goldfish)
Function: May act as a scaffolding protein within caveolar membranes, functionally participating in formation of caveolae or caveolae-like vesicles.
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:O75955}; Peripheral membrane protein {ECO:0000250|UniProtKB:O75955}. Endosome {ECO:0000250|UniProtKB:O75955}. Membrane, caveola {ECO:0000250|UniProtKB:O08917}; Peripheral membrane protein {ECO:0000250|UniProtKB:O08917}. Melanosome {ECO:0000250|UniProtKB:O75955}. Membrane raft {ECO:0000250|UniProtKB:O75955}. Note=Identified by mass spectrometry in melanosome fractions from stage I to stage IV. Membrane-associated protein of caveola. {ECO:0000250|UniProtKB:O08917, ECO:0000250|UniProtKB:O75955}.
Interaction partners:
Sequence:
MFYTCGPNEAMVVSGFCRSPPVMISGGSVFVFPCVQQIQRISLNTLTLNVKSDKVYTRHGVPVSVTGIAQMKIQGQNKQMLAAKCQMFLGKSESDIAHIALETLEGHQRAIIAHLTVEEIYKDRKKFSEQVFKVASSDLFNMGISVVSYTLKDVHDDQDYLHSLGKARTAQVQKDARIGEAKNKRDAVIREANAIQEKVSAQYMNEIEMAKAQRDYELKKAVYDIEVCTKKAESEMAYQLQVAKTKQQIEEEKMQVMVVERSQQIMLQEQEIARKEKELEAQVMKPADAERYRLEKLAEAERLQLIMEAEAEAESIKMRGEAEAYAVEARGRAEAEQMAKKAEAFQTYKEGAMVDMLMEKLPLIAEEISKPLSATNKVTMVSSGGSEIGAAKLTGEVLDIMTKLPETIEKLTGVSISQVARTG
Protein: CaeNaCin (Caenorhabditis bacteriocin) (A4V4W3)
Organism: Caenorhabditis elegans
Interaction partners:
- CaeNaCin
- CaeNaCin
- UPF0057 membrane protein txt-9
- Neuropeptide-Like Protein
- CaeNaCin
Sequence:
MLRLIILLLVALLALSSAQYGYGYNYGYGAPMYPGYGGYGGGLLGLLIGKK
Protein: Nesprin-3 (KASH domain-containing protein 3) (KASH3) (Nuclear envelope spectrin repeat protein 3) (Q6ZMZ3)
Organism: Homo sapiens (Human)
Function: As a component of the LINC (LInker of Nucleoskeleton and Cytoskeleton) complex involved in the connection between the nuclear lamina and the cytoskeleton. The nucleocytoplasmic interactions established by the LINC complex play an important role in the transmission of mechanical forces across the nuclear envelope and in nuclear movement and positioning. Probable anchoring protein which tethers the nucleus to the cytoskeleton by binding PLEC which can associate with the intermediate filament system. Plays a role in the regulation of aortic epithelial cell morphology, and is required for flow-induced centrosome polarization and directional migration in aortic endothelial cells.
Subcellular location: Nucleus outer membrane {ECO:0000269|PubMed:21937718}; Single-pass type IV membrane protein {ECO:0000269|PubMed:21937718}. Nucleus envelope {ECO:0000269|PubMed:21937718}. Rough endoplasmic reticulum {ECO:0000250}.
Interaction partners:
- Plectin
- SUN domain-containing protein 2
- SUN domain-containing protein 1
- Nesprin-2
- Nesprin-4
- Nesprin-1
- SUN domain-containing protein 3
- Microtubule-actin cross-linking factor 1, isoforms 1/2/3/4/5
- Protein KASH5
- Torsin-1A
Sequence:
MTQQPQDDFDRSVEDAQAWMKAVQDQLQVNDNTQGPRAALEARLWETEKICQLEPEGRVRVDLVLRMAEALLACCPGDQKPGILARLKDIKAQWEETVTYMTHCHSRIEWVWLHWSEYLLARDEFYRWFQKMMVTLEPHIELQLGLKEKQWQLSHAQVLLHNVDNQAVLLDRLLEEAASLFNRIGDPSVDEDAQKRMKAEYDAVKAKAQKRVDLLEQVAREHEEYQAGVDEFQLWLKAVVEKVNGCLGRNCKLPITQRLSTLQDIAKDFPRGEESLETLEEQSAGVIRNTSPLGAEKITGELEEMRKVLEKLRALWEEEEERLRGLLRSRGAWEQQIKQLEAELSEFRMVLQRLAQEGLQPAAKAGTEDELVAHWRRYSATRAALASEEPRVDRLQAQLKELIVFPHNLKPLSDSVIATIQEYQSLKVKSARLRNAAAVELWQHFQRPLQDLQLWKALAQRLLEVTASLPDLPSLHTFLPQIEAALMESSRLKELLTMLQLKKDLLIGIFGQERATALLEQVAGSMRDRDLLHNSLLQRKSKLQSLLAQHKDFGAAFEPLQRKLLDLQVRVQAEKGLQRDLPGKQAQLSRLQGLQEEGLDLGAQMEAARPLVQENPNHQHKMDQLSSDFQALQRSLEDLVDRCRQSVQEHCTFSHQLLELRQWIVVTTQKLEAHRGEAGPGDAESQEAEFERLVAEFPEKEAQLSLVEAQGWLVMEKSSPEGAAVVQEELRELAESWRALRLLEESLLSLIRNWHLQRMEVDSGKKMVFTNNIPKSGFLINPMDPIPRHRRRANLLQEEEGSHEDFSQLLRNFGQWLQVENSKLVRIIAMRTSTAEDLRTRKSKLQELEARVPEGQHLFENLLRLGPARGTSDELEDLRYQWMLYKSKLKDSGHLLTQSSPGEPTGFQKTRRWRGLGSLFRRACCVALPLQLLLLLFLLLLFLLPIREEDRSCTLANNFARSFTLMLRYNGPPPT
Protein: Serine/threonine-protein phosphatase 2A activator (EC 5.2.1.8) (PP2A, subunit B', PR53 isoform) (Phosphotyrosyl phosphatase activator) (PTPA) (Serine/threonine-protein phosphatase 2A regulatory subunit 4) (Serine/threonine-protein phosphatase 2A regulatory subunit B') (Q15257)
Organism: Homo sapiens (Human)
Function: PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides. Acts as a regulatory subunit for serine/threonine-protein phosphatase 2A (PP2A) modulating its activity or substrate specificity, probably by inducing a conformational change in the catalytic subunit, a proposed direct target of the PPIase. Can reactivate inactive phosphatase PP2A-phosphatase methylesterase complexes (PP2A(i)) in presence of ATP and Mg(2+) (By similarity). Reversibly stimulates the variable phosphotyrosyl phosphatase activity of PP2A core heterodimer PP2A(D) in presence of ATP and Mg(2+) (in vitro). The phosphotyrosyl phosphatase activity is dependent of an ATPase activity of the PP2A(D):PPP2R4 complex. Is involved in apoptosis; the function appears to be independent from PP2A.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:17333320}. Nucleus {ECO:0000269|PubMed:17333320}.
Interaction partners:
- Serine/threonine-protein phosphatase 2A catalytic subunit alpha isoform
- Serine/threonine-protein phosphatase 2A 65 kDa regulatory subunit A alpha isoform
- Serine/threonine-protein phosphatase 4 catalytic subunit
- Serine/threonine-protein phosphatase 4 regulatory subunit 2
- Serine/threonine-protein phosphatase 4 regulatory subunit 3A
- Serine/threonine-protein phosphatase 2A 56 kDa regulatory subunit gamma isoform
- Serine/threonine-protein phosphatase 2A regulatory subunit B'' subunit alpha
- Serine/threonine-protein phosphatase 2A catalytic subunit beta isoform
- Serine/threonine-protein phosphatase 2A 65 kDa regulatory subunit A beta isoform
- Serine/threonine-protein phosphatase 4 regulatory subunit 1
Sequence:
MAEGERQPPPDSSEEAPPATQNFIIPKKEIHTVPDMGKWKRSQAYADYIGFILTLNEGVKGKKLTFEYRVSEMWNEVHEEKEQAAKQSVSCDECIPLPRAGHCAPSEAIEKLVALLNTLDRWIDETPPVDQPSRFGNKAYRTWYAKLDEEAENLVATVVPTHLAAAVPEVAVYLKESVGNSTRIDYGTGHEAAFAAFLCCLCKIGVLRVDDQIAIVFKVFNRYLEVMRKLQKTYRMEPAGSQGVWGLDDFQFLPFIWGSSQLIDHPYLEPRHFVDEKAVNENHKDYMFLECILFITEMKTGPFAEHSNQLWNISAVPSWSKVNQGLIRMYKAECLEKFPVIQHFKFGSLLPIHPVTSG
Protein: Protein kinase (Q5ANJ0)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Interaction partners:
- HORMA domain-containing protein
- Calmodulin
Sequence:
MTKTGKFTPWDETTGNKTTTANNTSYILSKKPLGDGSYSVVFECKNTSTGRHYAAKKYTKRLMYGFENMLKNEFKVLNRISLSHSHLLSLIDFFETEESFYLVTDLARGGDLWNKIAEEEKLNEQTTRTITRQLVESVEFLHKHQILHHDIKAENVFFQSKHQDTILLGDFGLAKILQPQEKLHEVAGTLSYMAPEMLDYKIGYDFPIDVWALGVCVYFMLCGYMPFDCDDDEETKDAIRSRKYLFEPSEYWVDVSSEAKDFILACLQVDPQKRLTASQLLQHSFLKINSTKPAITISSPLKRSFSNLSALQRDQIKNILQKVGGVSAPALSHSSSINEKLERGRFDSLNKDATLNGAICPSPECVSIFSSPANSTSVSRDGSGLNIFEESLKWDSSQKKALPLNTLRQGASFAL
Protein: BBG-LP15 (Q15K26)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MELLSSNTGTTTTTTTATHHLHQATTTKQLLVQDYLSYASPPTYSRLPPDGHEFPPNFSEPLIMHSHPLKVTTELSYEIQKGGKDESSAPPLPKTGPPATVPRKVYRQDLVINVEPAPSLTRDYQRSLSGGTPRKPSDWRKDEKSEKSVRDKIAMFSSNNELDAIPPAPATAPISSSFTRKPLNRSSENLLDSCSSS
Protein: Guanine deaminase (Guanase) (Guanine aminase) (EC 3.5.4.3) (Guanine aminohydrolase) (GAH) (Q9R111)
Organism: Mus musculus (Mouse)
Function: Catalyzes the hydrolytic deamination of guanine, producing xanthine and ammonia.
Interaction partners:
- Purine nucleoside phosphorylase
- Purine nucleoside phosphorylase
- Adenine phosphoribosyltransferase
- Xanthine dehydrogenase/oxidase
- Hypoxanthine-guanine phosphoribosyltransferase
- Disks large homolog 4
- Dihydropyrimidinase-related protein 1
- Adenylosuccinate lyase
- Stress-induced-phosphoprotein 1
- Adenosine deaminase
Sequence:
MCAARTPPLALVFRGTFVHSTWTCPMEVLRDHLLGVSDSGKIVFLEESSQQEKLAKEWCFKPCEIRELSHHEFFMPGLVDTHIHAPQYAFAGSNVDLPLLEWLNKYTFPTEQRFRSTDVAEEVYTRVVRRTLKNGTTTACYFGTIHTDSSLILAEITDKFGQRAFVGKVCMDLNDTVPEYKETTEESVKETERFVSEMLQKNYPRVKPIVTPRFTLSCTETLMSELGNIAKTHDLYIQSHISENREEIEAVKSLYPSYKNYTDVYDKNNLLTNKTVMAHGCYLSEEELNIFSERGASIAHCPNSNLSLSSGLLNVLEVLKHKVKIGLGTDVAGGYSYSMLDAIRRAVMVSNVLLINKVNEKNLTLKEVFRLATLGGSQALGLDSEIGNFEVGKEFDALLINPRASDSPIDLFYGDFVGDISEAVIQKFLYLGDDRNIEEVYVGGKQVVPFSSSV
Protein: Dynactin subunit 3 (D4A1B8)
Organism: Rattus norvegicus (Rat)
Interaction partners:
- Dynactin subunit 1
- Dynactin subunit 2
- Dynactin subunit 6
- Dynactin subunit 5
- Dynactin subunit 4
- Alpha-centractin
- Actin-related protein 10
- Beta-centractin
- Cytoplasmic dynein 1 intermediate chain 2
- Cytoplasmic dynein 1 heavy chain 1
Sequence:
RRRAQVDKGSKGRAVRSEQAQIRKVADGLVKVQVALGNIASKRERVKILYKKIEDLIKYLDPEYIDRIAIPEASKLQFILAEEQFILSQVALLEQVNTLVPMLDSASIKAVPEHAARLQRLAQIHIQQQDQCVEITEESKALLEEYNKTTMLLSKQFVQWDELLCQLEAAKQVKPAAE
Protein: Neuronal PAS domain protein 3 (F8VS42)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MIRIFPDFSVQVTAAAAGGAAAGVPAGAGMGRAGAAANGTPQNVQGITSYQQRLQALRKEKSRDAARSRRGKENFEFYELAKLLPLPAAITSQLDKASIIRLTISYLKMRDFANQGDPPWNLRMEGPPPNTSVKVIGAQRRRSPSALAIEVFEAHLGSHILQSLDGFVFALNQEGKFLYISETVSIYLGLSQVELTGSSVFDYVHPGDHVEMAEQLGMKLPPGRGLLSQGTAEDGASSASSSSQSETPEPVESTSPSLLTTDNTLERSFFIRMKSTLTKRGVHIKSSGYKVIHITGRLRLRVSLSHGRTVPSQIMGLVVVAHALPPPTINEVRIDCHMFVTRVNMDLNIIYCENRISDYMDLTPVDIVGKRCYHFIHAEDVEGIRHSHLDLLNKGQCVTKYYRWMQKNGGYIWIQSSATIAINAKNANEKNIIWVNYLLSNPEYKDTPMDIAQLPHLPEKTSESSETSDSESDSKDTSEDNENSKSDEKGNQSENSEDPEPDRKKSGNACDNDMNCNDDGHSSSNPDSRDSDDSFEHSDFENPKAGEDGFGALGAMQIKVERYVESESDLRLQNCESLTSDSAKDSDSAGEAGAQASSKHQKRKKRRKRQKGGSASRRRLSSASSPGGLDAGLVEPPRLLSSPNSASVLKIKTEISEPINFDNDSSIWNYPPNREISRNESPYSMTKPPSSEHFPSPQGGGGGGGGGGGLHVAIPDSVLTPPGADGAAARKTQFGASATAALAPVASDPLSPPLSASPRDKHPGNGGGGGGGGGGAGGGGPSASNSLLYTGDLEALQRLQAGNVVLPLVHRVTGTLAATSTAAQRVYTTGTIRYAPAEVTLAMQSNLLPNAHAVNFVDVNSPGFGLDPKTPMEMLYHHVHRLNMSGPFGGAVSAASLTQMPAGNVFTTAEGLFSTLPFPVYSNGIHAAQTLERKE
Protein: GPI inositol-deacylase (EC 3.1.-.-) (Post-GPI attachment to proteins factor 1) (Q3UUQ7)
Organism: Mus musculus (Mouse)
Function: Involved in inositol deacylation of GPI-anchored proteins. GPI inositol deacylation may important for efficient transport of GPI-anchored proteins from the endoplasmic reticulum to the Golgi (By similarity).
Subcellular location: Endoplasmic reticulum membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}.
Interaction partners:
- GPI-anchor transamidase component PIGT
- GPI-anchor transamidase component GPAA1
- GPI-anchor transamidase component PIGU
- GPI-anchor transamidase component PIGS
- Transmembrane emp24 domain-containing protein 10
- GPI-specific phospholipase A2-like PGAP3
- GPI-anchor transamidase
- Urokinase plasminogen activator surface receptor
- Acyltransferase PGAP2
- GPI alpha-1,4-mannosyltransferase I, catalytic subunit
Sequence:
MFLHSVNLWNLAFYVFMVFLATLGLWDVFFGFEENKCSMSYMFEYPEYQKIELPKKLTKRYPAYELYLYGEGSYAEEHKILPLTGIPVLFLPGNAGSYKQVRSIGSIALRKAEDIDFKYHFDFFSVNFNEELVALYGGSLQKQTKFVHECIKAILKLYKGQEFAPTSVAIIGHSMGGLVARALLTLKNFKQDLINLLVTQATPHVAPVMPLDRFITEFYMNVNNYWILNARHINLTTLSVAGGFRDYQVRSGLTFLPKLSHYTSALSVVSSAVPKTWVSTDHLSIVWCKQLQLTTIRAFFDLIDADTKQITQKPKKKLSVLNHHFIRHPAKQFEENPSIISDLTGTSMWVPVKVSRWSYVAYNESDKIYFAFPLANHRKIYTHAYCQSTMLDTNSWIFGCINSTSMCRQGVDLSWKAELLPTIKSLTLRLQDYPSLSHIVVYVPSVHGSKFVVDCEFFKKEARSMQLPVTHLFSFGLSSRKVTLNTNGLYYNIELLNFGQIYQAFKVNVVSKCTGSKEEITSIYKLHIPWSYEDSLTIAQVPSSTDISLKLHVAQPENDSHVALLKMYTSSDCQYEVTIKTSFPQILGQVVRFHGGALPAYVVSSILLAYGGQLYSLLSTGYCLEYSTILDKEAKPYKVDPFVIMIKFLLGYKWFKELWDAVLLPELDAIVLTSQSMCFPLVSLILFLFGTCTAYWSGLLSSTSVQLLSSLWLALKRPAELPKDIKVMSPDLPVLTVVFLIVSWTTCGALAILLSYLYYVFKVVHLQASLTTFKNNQPVNPKHSRRSEKKSNHHKDSAVQSLRLCANDAEDSLRMHSTVINLLTWVVLLSMPSLIYWLKNLRYYFKLSPDPCKPLAFLLIPAIAILGNTHTVSVKSSKLLKTVSQFPLPLAVGVIAFGSSHLYRVPCFVIIPLVFHALCNFM
Protein: Chlorophyll a-b binding protein, chloroplastic (F2Z293)
Organism: Spinacia oleracea (Spinach)
Subcellular location: Plastid, chloroplast thylakoid membrane {ECO:0000256|ARBA:ARBA00004334, ECO:0000256|RuleBase:RU363080}.
Interaction partners:
Sequence:
AQPKSGFSTDRPLWYPGAKAPEYLDGSLVGDYGFDPFGLGKPAEYLQYDYDGLDQNLAKNLAGDIIGTRTESADVKSTSLQPYSEVFGLQRFRECELIHGRWAMLATLGALTVEGLTGITWQDAGKVELIEGSSYLGQPLPFSMTTLIWIEVLVIGYIEFQRNAELDTEKRLYPGGTFDPLGLASDPEKKPILQLAEIKHARLAMVGFLGFAVQAAVTGKGPLNNWVTHLSDPLHTTILDRFL
Protein: Inner membrane protein RclC (Reactive chlorine resistance protein C) (P75685)
Organism: Escherichia coli (strain K12)
Function: Probably involved in reactive chlorine species (RCS) stress resistance.
Subcellular location: Cell inner membrane {ECO:0000269|PubMed:15919996}; Multi-pass membrane protein {ECO:0000269|PubMed:15919996}.
Interaction partners:
- Uncharacterized protein RclB
- Probable pyridine nucleotide-disulfide oxidoreductase RclA
- RCS-specific HTH-type transcriptional activator RclR
- H
Sequence:
MEKYLHLLSRGDKIGLTLIRLSIAIVFMWIGLLKFVPYEADSITPFVANSPLMSFFYEHPEDYKQYLTHEGEYKPEARAWQTANNTYGFSNGLGVVEVIIALLVLANPVNRWLGLLGGLMAFTTPLVTLSFLITTPEAWVPALGDAHHGFPYLSGAGRLVLKDTLMLAGAVMIMADSAREILKQRSNESSSTLKTEY
Protein: Ran-binding protein 6 (RanBP6) (Q8BIV3)
Organism: Mus musculus (Mouse)
Function: May function in nuclear protein import as nuclear transport receptor.
Subcellular location: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
Interaction partners:
- Importin subunit beta-1
- Ran-binding protein 17
- Importin-4
Sequence:
MAAAGSAGLPATVSEKQEFYQLLKNLINPSCMVRRQAEEVYENIPGLCKTTFLLDAVRNRRAGYEVRQMAAALLRRLLSSGFEEVYPNLPPEVQRDVKIELILAVKLETHASMRKKLCDIFAVLARNLIDESGTNHWPEGLKFLIDSIHSKNVVLWEVALHVFWHFPGIFGNQDRHDLDIIKRLLDQCIQDQEHPAIRTLSARAAATFVLANENNIALFKDFADLLPGILQAVNDSCYQDDDSVLESLVEIADTVPKYLGPYLEDTLQLSLKLCGDSRLSNLQRQLALEVIVTLSETATPMLKKHTNIIAQAVPHILAMMVDLQDDDDWVNADEMEEDDFDSNAVAAESALDRLACGLGGKVVLPMTKEHIMQMLQSPDWKCRHAGLMALSAIGEGCHQQMEPILDETVNSVLLFLQDPHPRVRAAACTTLGQMATDFAPSFQKKFHEIVITALLRTMENQGNQRVQSHAASALVIFIEDCPKSLLILYLENMVKSLHSILVIKLQELIRNGTKLALEQLVTTIASVADAIEESFIPYYDIFMPSLKHVVELAVQKELKLLRGKTIECISHVGLAVGKEKFMQDASNVMQLLLKTQSDLNNMEDDDPQTSYMVSAWARMCKILGKDFEQYLPLVIEPLIKTASAKPDVALLDTQDVENMSDDDGWQFVNLGDQQSFGIKTSGLEAKATACQMLVYYAKELREGFVEYTEQVVKMMVPLLKFYFHDNVRVAAAEAMPFLLECARIRGSEYLSQMWQFICDPLIKAIGTEPDTDVLSEIMNSFAKSIEVMGDGCLNDEHLEELGGILKAKLEGHFKNQELRQVKRQEENYDQQVEMSLQDEDECDVYILTKVSDILHSLFSTYKEKILPWFEQLLPLIVNLICSSRPWPDRQWGLCIFDDIIEHCSPTSFKYVEYFRWPMLLNMRDNNPEVRQAAAYGLGVMAQFGGDDYRSLCSEAVPLLVKVIKCANSKTKKNVIATENCISAIGKILKFKPNCVNVDEVLPHWLSWLPLHEDKEEAIQTLNFLCDLIESNHPVVIGPNNSNLPKIISIIAEGKINETISHEDPCAKRLANVVRQIQTSEELWLECTSQLDDEQQEALHELLSFA
Protein: Transcription and mRNA export factor SUS1 (Q6WNK7)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Involved in mRNA export coupled transcription activation by association with both the TREX-2 and the SAGA complexes. The transcription regulatory histone acetylation (HAT) complex SAGA is involved in RNA polymerase II-dependent regulation of approximately 10% of yeast genes. At the promoters, SAGA is required for recruitment of the basal transcription machinery. It influences RNA polymerase II transcriptional activity through different activities such as TBP interaction (SPT3, SPT8 and SPT20) and promoter selectivity, interaction with transcription activators (GCN5, ADA2, ADA3 and TRA1), and chromatin modification through histone acetylation (GCN5) and deubiquitination (UBP8). Within the SAGA complex, participates in a subcomplex with SGF11, SGF73 and UBP8 required for deubiquitination of H2B and for the maintenance of steady-state H3 methylation levels. The TREX-2 complex functions in docking export-competent ribonucleoprotein particles (mRNPs) to the nuclear entrance of the nuclear pore complex (nuclear basket), by association with components of the nuclear mRNA export machinery (MEX67-MTR2 and SUB2) in the nucleoplasm and the nucleoporin NUP1 at the nuclear basket. TREX-2 participates in mRNA export and accurate chromatin positioning in the nucleus by tethering genes to the nuclear periphery. SUS1 has also a role in mRNP biogenesis and maintenance of genome integrity through preventing RNA-mediated genome instability. Has a role in response to DNA damage induced by methyl methane sulfonate (MMS) and replication arrest induced by hydroxyurea. May also be involved in cytoplasmic mRNA decay by interaction with components of P-bodies.
Subcellular location: Nucleus, nucleoplasm {ECO:0000269|PubMed:16855026}. Cytoplasm, P-body {ECO:0000269|PubMed:20230609}. Note=The nucleoplasm localization requires the presence of UBP8 and SGF11 to bind part of SUS1 to the SAGA complex. {ECO:0000269|PubMed:16855026}.
Interaction partners:
- SAGA complex subunit SPT7
- SAGA complex subunit NGG1
- Histone acetyltransferase GCN5
- SAGA complex/NuA4 acetyltransferase complex subunit TRA1
- SAGA complex subunit ADA2
- Cell division control protein 31
- SAGA complex subunit SGF29
- SAGA complex subunit SGF73
- SAGA complex/transcription factor TFIID complex subunit TAF9
- Ubiquitin carboxyl-terminal hydrolase 8
Sequence:
MTMDTAQLKSQIQQYLVESGNYELISNELKARLLQEGWVDKVKDLTKSEMNINESTNFTQILSTVEPKALEMVSDSTRETVLKQIREFLEEIVDTQ
Protein: L-lactate dehydrogenase (EC 1.1.1.27) (Q7SI97)
Organism: Plasmodium berghei (strain Anka)
Interaction partners:
Sequence:
MAPKAKIVLVGSGMIGGVMATLIVQKNLGDVVMFDIVKNMPHGKALDTSHTNVMAYSNCKVSGSNTYDDLKDADVVIVTAGFTKAPGKSDKEWNRDDLLPLNNKIMIEIGGHIKNNCPNAFIIVVTNPVDVMVQLLHQHSGVPKNKIVGLGGVLDTSRLKYYISQKLNVCPRDVNAHIVGAHGNKMVLLKRYITVGGIPLQEFINNKKITDQELDAIFDRTINTALEIVNLHASPYVAPAAAIIEMAESYIRDLRKVLICSTLLEGQYGHKDIFAGTPLVIGGNGVEQVIELQLNADEKKKFDEAVAETSRMKALI
Protein: Matrix metalloproteinase-21 (MMP-21) (EC 3.4.24.-) (Q8K3F2)
Organism: Mus musculus (Mouse)
Function: Plays a specialized role in the generation of left-right asymmetry during embryogenesis. May act as a negative regulator of the NOTCH-signaling pathway. Cleaves alpha-1-antitrypsin (By similarity).
Subcellular location: Secreted {ECO:0000305}.
Interaction partners:
Sequence:
MLAASVLRLTLPLCWLVAPQPTQPERLFHSRDRSDLEPSPLSQAKPIADLHDAQSFLLKYGWSEIPSPKESAGVPVGFTLAQAVRRFQKANRLPASGELDSPTLAAMNKPRCGVPDTRLPPRAALPTPPALLTSLGLRPRARQKRFLQMLFPKPDGQQEDASDTGASRAFSKKTLTWRLVGDAYSSQLSGDEQRYIFRLAFRMWSEVTPLDFREDRTAPGTMVDIKLGFGRGRHLGCPRVFDGSGQEFAHAWRLGEIHFDDDEHFTPLSSDTGISLLKVAVHEIGHVLGLPHTYRVGSIMQPNYIPQEPAFELDWADRKAIQRLYGSCKGSFDTVFDWIRKERNQYGEVRVRFNTYFFRNSWYWLYENRNNRTRYGDPLQILTGWRGIPTQSIDAYVHVWSWGKDERYFFKGSQYWRYDSENDQAHTEDEQGRSYPKLISEGFPGIPSPLDTAFYDRRQQLIYFFKESLVFAFDVNRNQVLNSYPKKMSQVFPAIMPQNHPFRNLDSAYYSYAHNSIFFFKGNSYWKVVSDKDKQQNTRLPLNGLFPKKPVSEKWFDVCDVHTSTLNM
Protein: Protein PET18 (P25362)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Interaction partners:
- Hydroxymethylpyrimidine/phosphomethylpyrimidine kinase THI20
- Hydroxymethylpyrimidine/phosphomethylpyrimidine kinase THI21
- Protein MAK32
- Thiamine biosynthesis protein THI22
- N-alpha-acetyltransferase 35, NatC auxiliary subunit
- Cold tolerance protein 1
- Thiamine thiazole synthase
Sequence:
MSCTTDKLIQKYDALVRKTTEHKFAKELCAGTLKDRSLYIYLSQDLQFFETSLRLICKTTSLAPTTHALITLAKKIGFFSNDENSYFHDCLELLAPSLTKEERDNFDNKAIPGVDAYINFLDELRKDASITWPSLVTSLWVAEELYWRWARDTPRAPGLHWKYQKWIDLHDGEHFQTWCEFLKAEVDKFPVEEVESIFVKVSQFEFEFFESCYNA
Protein: non-specific serine/threonine protein kinase (EC 2.7.11.1) (E7ETM0)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MDLLGPSLEDLFNFCSRRFTMKTVLMLADQMISRIEYVHTKNFIHRDIKPDNFLMGIGRHCNKCLESPVGKRKRSMTVSTSQDPSFSGLNQLFLIDFGLAKKYRDNRTRQHIPYREDKNLTGTARYASINAHLGIEQSRRDDMESLGYVLMYFNRTSLPWQGLKAATKKQKYEKISEKKMSTPVEVLCKGFPAEFAMYLNYCRGLRFEEAPDYMYLRQLFRILFRTLNHQYDYTFDWTMLKQKAAQQAASSSGQGQQAQTPTGF
Protein: LIM/homeobox protein Lhx9 (LIM homeobox protein 9) (Q1LWV4)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Function: May be involved in gonadal development.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00108}.
Interaction partners:
Sequence:
MEVVGCKAKESSCTLRPAAMLFHGISGDHIQGIMEEMERRSKSESRLAKTVQMNGRETTMPSMSPEKPALCAGCGGKISDRYYLLAVDKQWHLRCLKCCECKLALESELTCFAKDGSIYCKEDYYRRFSVQRCARCHLGISASEMVMRARDSVYHLSCFTCTTCNKTLTTGDHFGMKDNLVYCRVHFETLIQGEYHPQLNYAELAAKGGGLALPYFNGTGTVQKGRPRKRKSPAMGIDIGSYSSGCNENDADHLDRDQQPYPPSQKTKRMRTSFKHHQLRTMKSYFAINHNPDAKDLKQLAQKTGLTKRVLQVWFQNARAKFRRNVLRQENGGVDKADGTSLPPPSSDSGALTPPSTATTLTDLTNPSITVVTSVTSSLDSHESGSPPQTTLTNLF
Protein: Fibroblast growth factor receptor ligand 1 (Teratocarcinoma-derived growth factor 1, member 3 L homeolog precursor) (Q91649)
Organism: Xenopus laevis (African clawed frog)
Interaction partners:
Sequence:
MQFLRFLAILIFSAKHFIKHCKGETCMGLNCNDPRLLEAIKSNTINQLLHDTINATHGKSPPKSTKTLPFLGITDSKKLNRKCCQNGGTCFLGTFCICPKQFTGRHCEHERRPASCSGVPHGDWIRQGCLLCRCVSGVLHCFKPESEDCDVVHEKNMRSGVPRMQLSLIIYCFLTANLFYHIVWHLNIGL