wanglab/gogpt-training-data huggingface dataset:
Protein: Coilin (p80-coilin) (Q5SU73)
Organism: Mus musculus (Mouse)
Function: Component of nuclear coiled bodies, also known as Cajal bodies or CBs, which are involved in the modification and assembly of nucleoplasmic snRNPs.
Subcellular location: Nucleus {ECO:0000269|PubMed:10806077}. Nucleus, Cajal body {ECO:0000250|UniProtKB:P38432}.
Interaction partners:
- rRNA 2'-O-methyltransferase fibrillarin
- Nucleolar and coiled-body phosphoprotein 1
- Survival motor neuron protein
- Telomerase Cajal body protein 1
- Ataxin-1
- Gem-associated protein 2
- Spliceosome associated factor 3, U4/U6 recycling protein
- X-ray repair cross-complementing protein 6
Sequence:
MAASETVRLRLQFDYPPPATPHCTVFWLLVDLNRCRVVTDLISLIRQRFGFSSGALLGLYLEGGLLPPAESARLVRDNDSLRVKLEDQGLPENLIVSNGGDSSFPCRKAKKRAFKLMEDEETDQGYKSLKKHCKRQEDSGQNEKASDLETKLLPDETGRTKSKKKSKVTGSPAEEDEEETKKKSSKRKEKCEPKKQTRASKSSKQQTPKEGASQNCSFPRASPRSLGKARRRSSTGLKGSSGHLSESESCPESVSDGHCSVMMQEVTFSEKLSAELLKDAPATKTAAANRQASKPGFTFSSGKGKASRTSSSSSDSSSESEDQFLVSKNMLEGASAGFLKPTGLFAGQGGSGPGLSLETPGIMGWKSSDSNRGRQAPGPPSTPVPTSLGRGWGRGEDLLFGKGLRGRGVRGRGRGRGQAVSCVFNRSSESQKQRQLNDILTNSSVVIQNPVEPPKKDYSLLPLLAAAPQVGEKIAFKLLELTSDYSPDVSDYKEGKILSHDPETQQVDIEVLSSLPALKEPGKFDLVYHNENGTEVVEYAVTQEKRITVLWRELIDPRLIIDSSGSISST
Protein: Glycine receptor subunit alpha-2 (F1R8P4)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Function: Glycine receptors are ligand-gated chloride channels. Channel opening is triggered by extracellular glycine. Channel opening is also triggered by taurine and beta-alanine. Plays a role in synaptic plasticity. Contributes to the generation of inhibitory postsynaptic currents, and is involved in the down-regulation of neuronal excitability. Plays a role in cellular responses to ethanol.
Subcellular location: Postsynaptic cell membrane {ECO:0000250|UniProtKB:Q7TNC8}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P23415}. Synapse {ECO:0000250|UniProtKB:Q7TNC8}. Cell membrane {ECO:0000250|UniProtKB:P23416}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P23415}. Cell projection {ECO:0000250|UniProtKB:Q7TNC8}.
Interaction partners:
- G protein-coupled receptor, class C, group 5, member Bb
- Gephyrin
- Gephyrin
- Transmembrane protein 130.
- Glutamate receptor, ionotropic, kainate 1b.
- Glycine receptor subunit beta
Sequence:
MTRPSVKLLTTLLACLMEMLNFRVSSGKDPDLLSSSSSSMSPSDFLDKLMGRTSGYDARIRPNFKGPPVNVTCNIFINSFGSVTETTMDYRVNIFLRQKWNDPRLAYSEYPDSSLDLDPSMLDSIWKPDLFFANEKGANFHDVTTDNKLLRIFKDGTVLYSIRLTLILSCPMDLKNFPMDVQTCTMQLESFGYTMNDLIFEWLDKGPVQVADGLTLPQFLIRDEKDLGYCTKHYNTGKFTCIEVKFHLERQMGYYLIQMYIPSLLIVILSWVSFWINMDAAPARVALGITTVLTMTTQSSGSRASLPKVSYVKAIDIWMAVCLLFVFAALLEYAGVNFVSRQQKEFLRLKRRQRRTQKEEDLQDGRLHFSSYNTTTCVKDGAVVKNTQVNQIQQPSILKNTETNRKKFVDRAKRIDTISRAAFPLAFLIFNVFYWITYKIIRHESARKD
Protein: B-box zinc finger protein 18 (Protein DOUBLE B-BOX 1A) (Protein SALT TOLERANCE HOMOLOG 4) (Q9SJU5)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Acts as negative regulator of seedling photomorphogenesis. Acts as a negative regulator of blue light-mediated inhibition of hypocotyl elongation through increase of bioactive gibberellin levels. Acts as a repressor of thermotolerance by modulating expression of a set of heat shock-responsive genes.
Subcellular location: Nucleus {ECO:0000269|PubMed:20872270}.
Interaction partners:
- B-box zinc finger protein 32
- Zinc finger protein CONSTANS-LIKE 7
- B-box zinc finger family protein
- E3 ubiquitin-protein ligase COP1
- Zinc finger protein CONSTANS-LIKE 6
- B-box domain protein 31
- Transcription factor HY5
- Putative E3 ubiquitin-protein ligase XBAT31
- B-box type zinc finger family protein
- Two-component response regulator-like APRR5
Sequence:
MRILCDACESAAAIVFCAADEAALCCSCDEKVHKCNKLASRHLRVGLADPSNAPSCDICENAPAFFYCEIDGSSLCLQCDMVVHVGGKRTHRRFLLLRQRIEFPGDKPNHADQLGLRCQKASSGRGQESNGNGDHDHNMIDLNSNPQRVHEPGSHNQEEGIDVNNANNHEHE
Protein: Chromosome partition protein Smc (P9WGF3)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: Required for chromosome condensation and partitioning.
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01894}.
Interaction partners:
- Segregation and condensation protein A
- Possible segregation and condensation protein ScpB
- Acylphosphatase
- Uncharacterized protein Rv2923c
- Signal recognition particle receptor FtsY
- Formamidopyrimidine-DNA glycosylase 1
- Ribonuclease 3
Sequence:
MYLKSLTLKGFKSFAAPTTLRFEPGITAVVGPNGSGKSNVVDALAWVMGEQGAKTLRGGKMEDVIFAGTSSRAPLGRAEVTVSIDNSDNALPIEYTEVSITRRMFRDGASEYEINGSSCRLMDVQELLSDSGIGREMHVIVGQGKLEEILQSRPEDRRAFIEEAAGVLKHRKRKEKALRKLDTMAANLARLTDLTTELRRQLKPLGRQAEAAQRAAAIQADLRDARLRLAADDLVSRRAEREAVFQAEAAMRREHDEAAARLAVASEELAAHESAVAELSTRAESIQHTWFGLSALAERVDATVRIASERAHHLDIEPVAVSDTDPRKPEELEAEAQQVAVAEQQLLAELDAARARLDAARAELADRERRAAEADRAHLAAVREEADRREGLARLAGQVETMRARVESIDESVARLSERIEDAAMRAQQTRAEFETVQGRIGELDQGEVGLDEHHERTVAALRLADERVAELQSAERAAERQVASLRARIDALAVGLQRKDGAAWLAHNRSGAGLFGSIAQLVKVRSGYEAALAAALGPAADALAVDGLTAAGSAVSALKQADGGRAVLVLSDWPAPQAPQSASGEMLPSGAQWALDLVESPPQLVGAMIAMLSGVAVVNDLTEAMGLVEIRPELRAVTVDGDLVGAGWVSGGSDRKLSTLEVTSEIDKARSELAAAEALAAQLNAALAGALTEQSARQDAAEQALAALNESDTAISAMYEQLGRLGQEARAAEEEWNRLLQQRTEQEAVRTQTLDDVIQLETQLRKAQETQRVQVAQPIDRQAISAAADRARGVEVEARLAVRTAEERANAVRGRADSLRRAAAAEREARVRAQQARAARLHAAAVAAAVADCGRLLAGRLHRAVDGASQLRDASAAQRQQRLAAMAAVRDEVNTLSARVGELTDSLHRDELANAQAALRIEQLEQMVLEQFGMAPADLITEYGPHVALPPTELEMAEFEQARERGEQVIAPAPMPFDRVTQERRAKRAERALAELGRVNPLALEEFAALEERYNFLSTQLEDVKAARKDLLGVVADVDARILQVFNDAFVDVEREFRGVFTALFPGGEGRLRLTEPDDMLTTGIEVEARPPGKKITRLSLLSGGEKALTAVAMLVAIFRARPSPFYIMDEVEAALDDVNLRRLLSLFEQLREQSQIIIITHQKPTMEVADALYGVTMQNDGITAVISQRMRGQQVDQLVTNSS
Protein: Contig An14c0130, genomic contig (A2R3C4)
Organism: Aspergillus niger (strain ATCC MYA-4892 / CBS 513.88 / FGSC A1513)
Interaction partners:
Sequence:
MSTSILNIQRDLILNTIRYAAGNEWKVLVVDETSRKLIDNAVSEDDILNLNVTNVEQIEHRRSPNPTMDALYILSPLPHIVDCIMADFERKRYRKAWLVWTSFLDPEQRARLDRSQLARDQIANVQIMNADYFPRESRLITFRDPWSFPVLFHPGCNHLIRAHLEGLAQKIVSLCASLGEYPVIRYYRPRAPTHEASVLCSHLARFIQNELDQFAQFQRDFPPPSPRPRGVLLIVDRSMDLIAPLLHEFTYQSMVHDLLPISDGDKVTYKTVINEGSHNEELKDMEINEEDNVWVEYRHMHMKDVLGKLGEDFAKFRAANPQFAEDNNKANVNTIKDMLAGLTEFQKGRDAYTLHLNMAQECMSYFQKHKLLEVSSVEQCFATGMDENYKKAKNLASQLVQLLDDDAIKQPERLRLLLLYIIYRGGILAGDIRKLLAHAQLAPQDGEIVANLDLLGARVEKPLKDDKPPVQPLFTRKPPSGPIDEEESLSRYDLNLKLILEELVRGTLDPSVFPFTRPHTDTDTPGQQEGLSQASLRSAKPTWARTRSTGEQPKQRIIVFMAGGATYGEARTCYEISQTCGKDVFLATSHMLSPGLFLRQVGDLSVDRRRLDIPAERPKPTAPAHLFEREAPPAPAQPVKKPVPVNLKPMAPTSALATMSLGTNGKAANGAAPPEKEKDKKEKKEKKEKKHRFFR
Protein: G antigen 1 (A0A158RFV5)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MSWRGRSTYYWPRPRRYVQPPEMIGPMRPEQFSDEVEPATPEEGEPATQRQDPAAAQEGEDEGASAGQGPKPEADSQEQGHPQTGCECEDGPDGQEMDPPNPEEVKTPEEEMRSHYVAQTGILWLLMNNCFLNLSPRKP
Protein: PH domain-containing protein YHR131C (P38835)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Subcellular location: Cytoplasm {ECO:0000269|PubMed:14562095}.
Interaction partners:
- RNA polymerase II degradation factor 1
- E3 ubiquitin-protein ligase RSP5
- Mitotic spindle-associated protein SHE1
- Uncharacterized protein YKR045C
Sequence:
MALPIEGKLSMANNRIERLKSPSSSSTCSMDEVLITSSNNSSSICLETMRQLPREGVSGQINIIKETAASSSSHAALFIKQDLYEHIDPLPAYPPSYDLVNPNKEVRFPIFGDTAPCPKSSLPPLYAPAVYELTLISLKLERLSPYEISSNRSWRNFIIEINSTQLNFYHIDESLTKHIRNYSSGETKSEKEDRIHSDLVHRSDQSQHLHHRLFTLPTRSASEFKKADQERISYRVKRDRSRYLTDEALYKSFTLQNARFGIPTDYTKKSFVLRMSCESEQFLLRFSHIDDMIDWSMYLSIGISVSLDLEVREYPDYRIVPRRRRRRRRRRRRRRHTHRSESSMGSFSQRFIRSNSRPDLIQRYSTGSSTNNNTTIRERSNTFTAGLLDHYCTGLSKTPTEALISSAASGESSDNSTLGSTRSLSGCSASRSIASRSLKFKIKNFFRPKNSSRTEKLHRLRSNSSNLNSVIETEEDDEHHESSGGDHPEPGVPVNTTIKVERPMHRNRAISMPQRQSLRRAISEEVVPIKFPNSTVGESVHSPSPIEHLSVDGCEIMLQSQNAVMKEELRSVASNLVANERDEASIRPKPQSSSIYLSGLAPNGESATDLSQSSRSLCLTNRDAEINDDESATETDEDENDGETDEYAGDDTNDDTDDSNIGYAYGSESDYSCLIEERIRNRRRASSTLSCFSNIPYGTDDIKWKPAIKEISRRRYLRDSLKCIKPFLDSNDCLGKVIYIPVSGPTFETSNKIHFSNRQSLQKQKNHFLKGFIVGPTALIELNCKNKNAIVGTTKDAEDHGEDDGDGDDGEDDDDDDDDDDDDDDDEDDDDDDDDDDDDDDDDDDGQITA
Protein: ATP-dependent RNA helicase DHX58 (EC 3.6.4.13) (ATP-dependent helicase LGP2) (Protein D11Lgp2) (RIG-I-like receptor 3) (RLR-3) (RIG-I-like receptor Lgp2) (RLR) (Q99J87)
Organism: Mus musculus (Mouse)
Function: Acts as a regulator of RIGI and IFIH1/MDA5 mediated antiviral signaling. Cannot initiate antiviral signaling as it lacks the CARD domain required for activating MAVS/IPS1-dependent signaling events. Can have both negative and positive regulatory functions related to RIGI and IFIH1/MDA5 signaling and this role in regulating signaling may be complex and could probably depend on characteristics of the infecting virus or target cells, or both. Its inhibitory action on RIG-I signaling may involve the following mechanisms: competition with RIGI for binding to the viral RNA, binding to RIGI and inhibiting its dimerization and interaction with MAVS/IPS1, competing with IKBKE in its binding to MAVS/IPS1 thereby inhibiting activation of interferon regulatory factor 3 (IRF3). Its positive regulatory role may involve unwinding or stripping nucleoproteins of viral RNA thereby facilitating their recognition by RIGI and IFIH1/MDA5. Involved in the innate immune response to various RNA viruses and some DNA viruses such as poxviruses, and also to the bacterial pathogen Listeria monocytogenes. Can bind both ssRNA and dsRNA, with a higher affinity for dsRNA. Shows a preference to 5'-triphosphorylated RNA, although it can recognize RNA lacking a 5'-triphosphate.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:11735219}.
Interaction partners:
- Mitochondrial antiviral-signaling protein
- Interferon-induced helicase C domain-containing protein 1
- Antiviral innate immune response receptor RIG-I
- Interferon regulatory factor 7
- DExD/H box helicase 60
- Ubl carboxyl-terminal hydrolase 18
- Interferon-induced, double-stranded RNA-activated protein kinase
- S-adenosylmethionine-dependent nucleotide dehydratase RSAD2
- Interferon regulatory factor 3
- 2'-5'-oligoadenylate synthase 2
Sequence:
MELRPYQWEVILPALEGKNIIIWLPTGAGKTRAAAFVAKRHLETVDRGKVVVLVNRVHLVSQHAEEFRRMLDKHWTVTTLSGDMGSRAGFGLMARSHDLLICTAELLQLALNSSEEDEHVELREFSLIVVDECHHTHKDTVYNTILSRYLEQKLKKAEPLPQVLGLTASPGTGGATKLQGAIDHILQLCANLDTCHIMSPKNCYSQLLMHNPKPCKQYDLCQRRAQDPFGDLIKKLMNQIHQQLEMPDLKQQFGTQMYEQQVVQLCKDAAEAGLQEQRVYALHLRRYNDALFIHDTVRARDALDMLQDFYDRERTTKTQMVRAESWLLKLFDDHKNVLGQLAARGPENPKLEMLERILLKQFGSPGHTRGIIFTRTRQTASSLLLWLRQQPCLQTVGIKPQMLIGAGNTSQSTHMTQKDQQEVIQEFRDGILSLLVATSVAEEGLDIAQCNVVVRYGLLTNEISMVQARGRARAGQSVYSFLATEGSREMKRELTNEALEVLMEKAVAAVQKMDPDEFKAKIRDLQQASLVKRAARAAHREIQQGQFLPEHVQLLCINCMVAVGYGSDLRKVEGTHHVNVNPNFSVYYTTSQNPVVINKVFKDWRPGGTIRCSNCGEVWGFQMIYKSVTLPVLKIGSILLETPRGKIQAKKWSRVPFSIPVFDILQDCTQSLSELSLD
Protein: Endonuclease-1 (EC 3.1.21.1) (Endonuclease I) (Endo I) (P25736)
Organism: Escherichia coli (strain K12)
Function: Has double-strand break activity.
Subcellular location: Periplasm {ECO:0000269|PubMed:4955462}.
Interaction partners:
- Crossover junction endodeoxyribonuclease RuvC
- Ribosomal RNA small subunit methyltransferase E
Sequence:
MYRYLSIAAVVLSAAFSGPALAEGINSFSQAKAAAVKVHADAPGTFYCGCKINWQGKKGVVDLQSCGYQVRKNENRASRVEWEHVVPAWQFGHQRQCWQDGGRKNCAKDPVYRKMESDMHNLQPSVGEVNGDRGNFMYSQWNGGEGQYGQCAMKVDFKEKAAEPPARARGAIARTYFYMRDQYNLTLSRQQTQLFNAWNKMYPVTDWECERDERIAKVQGNHNPYVQRACQARKS
Protein: Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnH (RPnTP synthase subunit PhnH) (EC 2.7.8.37) (P16686)
Organism: Escherichia coli (strain K12)
Function: Together with PhnG, PhnI and PhnL is required for the transfer of the ribose triphosphate moiety from ATP to methyl phosphonate.
Interaction partners:
- Putative phosphonates utilization ATP-binding protein PhnK
- Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL
- Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnG
- Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnI
- Alpha-D-ribose 1-methylphosphonate 5-triphosphate diphosphatase
- Alpha-D-ribose 1-methylphosphonate 5-phosphate C-P lyase
- Ribose 1,5-bisphosphate phosphokinase PhnN
- Probable transcriptional regulator PhnF
- Phosphonates import ATP-binding protein PhnC
- Phosphonates-binding periplasmic protein
Sequence:
MTLETAFMLPVQDAQHSFRRLLKAMSEPGVIVALHQLKRGWQPLNIATTSVLLTLADNDTPVWLSTPLNNDIVNQSLRFHTNAPLVSQPEQATFAVTDEAISSEQLNALSTGTAVAPEAGATLILQVASLSGGRMLRLTGAGIAEERMIAPQLPECILHELTERPHPFPLGIDLILTCGERLLAIPRTTHVEVC
Protein: Homeobox protein Hox-D13 (Homeobox protein Hox-4I) (P35453)
Organism: Homo sapiens (Human)
Function: Sequence-specific transcription factor that binds gene promoters and activates their transcription. Part of a developmental regulatory system that provides cells with specific positional identities on the anterior-posterior axis (By similarity).
Subcellular location: Nucleus {ECO:0000305|PubMed:24789103}.
Interaction partners:
- Sonic hedgehog protein
- Protein Spindly
- Nuclear pore complex protein Nup98-Nup96
- Homeobox protein Hox-D10
- Homeobox protein Hox-D11
- Programmed cell death 1 ligand 1
- Homeobox protein Hox-D9
- Programmed cell death 1 ligand 2
Sequence:
MSRAGSWDMDGLRADGGGAGGAPASSSSSSVAAAAASGQCRGFLSAPVFAGTHSGRAAAAAAAAAAAAAAASGFAYPGTSERTGSSSSSSSSAVVAARPEAPPAKECPAPTPAAAAAAPPSAPALGYGYHFGNGYYSCRMSHGVGLQQNALKSSPHASLGGFPVEKYMDVSGLASSSVPANEVPARAKEVSFYQGYTSPYQHVPGYIDMVSTFGSGEPRHEAYISMEGYQSWTLANGWNSQVYCTKDQPQGSHFWKSSFPGDVALNQPDMCVYRRGRKKRVPYTKLQLKELENEYAINKFINKDKRRRISAATNLSERQVTIWFQNRRVKDKKIVSKLKDTVS
Protein: Proline-rich protein 19 (A6NJB7)
Organism: Homo sapiens (Human)
Function: Promotes meiotic crossing over formation through its interaction with CNTD1 by participating in the crossover differentiation step of crossover-specific recombination intermediates.
Subcellular location: Nucleus {ECO:0000250|UniProtKB:B2RW88}. Chromosome {ECO:0000250|UniProtKB:B2RW88}. Note=Co-localized at crossover sites with CNTD1. Localizes on synapsed chromosome only in mid/late pachytene spermatocytes. {ECO:0000250|UniProtKB:B2RW88}.
Interaction partners:
- Ankyrin repeat family A protein 2
- Transmembrane protein 145
Sequence:
MDTQGPVSQPFQQPEKPGRVRRRKTRRERNKALVGSRRPLAHHDPPVAIRDPPVVPTASKLVVITQGRLSREHRGLFNHEVKSLDVARLLSSGTLVPGSPTLPAKPSPSPGRAQEPAPRSRDKENQVPGGSGPGPPSSPELSGVGQLLAELQCQLSLPQAFPRRNLIQDARDAIVHTLQACHGCVPDLALVLRGCQPPLPGAKPGVSERKMTPFWINSPDQVPEQERQRKQQGTKEFTFPMPYTSSMPTAHRGSLAPPRGPWPPYFPSLSSPSGTAWGPPTAFDLLKSIWLVATPPPPRPWGVGLPQPLPQPSSPLLPRTSVLDWSPSPPSPLPSLSWVVAQSSPEAWSFPPMRLY
Protein: Polyamine-transporting ATPase 13A3 (ATPase family homolog up-regulated in senescence cells 1) (Putrescine transporting ATPase) (EC 7.6.2.16) (Q9H7F0)
Organism: Homo sapiens (Human)
Function: ATP-driven pump involved in endocytosis-dependent polyamine transport. Uses ATP as an energy source to transfer polyamine precursor putrescine from the endosomal compartment to the cytosol.
Subcellular location: Recycling endosome membrane {ECO:0000269|PubMed:29505581}; Multi-pass membrane protein {ECO:0000255}. Early endosome membrane {ECO:0000269|PubMed:29505581}; Multi-pass membrane protein {ECO:0000255}. Late endosome membrane {ECO:0000269|PubMed:29505581}; Multi-pass membrane protein {ECO:0000255}. Note=Mainly targeted to the recycling endosomes and to a lesser extent to the early and late endosomes. {ECO:0000269|PubMed:29505581}.
Interaction partners:
- Copper-transporting ATPase 2
- Copper-transporting ATPase 1
Sequence:
MDREERKTINQGQEDEMEIYGYNLSRWKLAIVSLGVICSGGFLLLLLYWMPEWRVKATCVRAAIKDCEVVLLRTTDEFKMWFCAKIRVLSLETYPVSSPKSMSNKLSNGHAVCLIENPTEENRHRISKYSQTESQQIRYFTHHSVKYFWNDTIHNFDFLKGLDEGVSCTSIYEKHSAGLTKGMHAYRKLLYGVNEIAVKVPSVFKLLIKEVLNPFYIFQLFSVILWSTDEYYYYALAIVVMSIVSIVSSLYSIRKQYVMLHDMVATHSTVRVSVCRVNEEIEEIFSTDLVPGDVMVIPLNGTIMPCDAVLINGTCIVNESMLTGESVPVTKTNLPNPSVDVKGIGDELYNPETHKRHTLFCGTTVIQTRFYTGELVKAIVVRTGFSTSKGQLVRSILYPKPTDFKLYRDAYLFLLCLVAVAGIGFIYTIINSILNEVQVGVIIIESLDIITITVPPALPAAMTAGIVYAQRRLKKIGIFCISPQRINICGQLNLVCFDKTGTLTEDGLDLWGIQRVENARFLSPEENVCNEMLVKSQFVACMATCHSLTKIEGVLSGDPLDLKMFEAIGWILEEATEEETALHNRIMPTVVRPPKQLLPESTPAGNQEMELFELPATYEIGIVRQFPFSSALQRMSVVARVLGDRKMDAYMKGAPEAIAGLCKPETVPVDFQNVLEDFTKQGFRVIALAHRKLESKLTWHKVQNISRDAIENNMDFMGLIIMQNKLKQETPAVLEDLHKANIRTVMVTGDSMLTAVSVARDCGMILPQDKVIIAEALPPKDGKVAKINWHYADSLTQCSHPSAIDPEAIPVKLVHDSLEDLQMTRYHFAMNGKSFSVILEHFQDLVPKLMLHGTVFARMAPDQKTQLIEALQNVDYFVGMCGDGANDCGALKRAHGGISLSELEASVASPFTSKTPSISCVPNLIREGRAALITSFCVFKFMALYSIIQYFSVTLLYSILSNLGDFQFLFIDLAIILVVVFTMSLNPAWKELVAQRPPSGLISGALLFSVLSQIIICIGFQSLGFFWVKQQPWYEVWHPKSDACNTTGSGFWNSSHVDNETELDEHNIQNYENTTVFFISSFQYLIVAIAFSKGKPFRQPCYKNYFFVFSVIFLYIFILFIMLYPVASVDQVLQIVCVPYQWRVTMLIIVLVNAFVSITVEESVDRWGKCCLPWALGCRKKTPKAKYMYLAQELLVDPEWPPKPQTTTEAKALVKENGSCQIITIT
Protein: Nischarin (C9J715)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MATARTFGPEREAEPAKEARVVGSELVDTYTVYIIQVTDGSHEWTVKHRYSDFHDLHEKLVAERKIDKNLLPPKKIIGKNSRSLVEKREKDLEVYLQKLLAAFPGVTPRVLAHFLHFHFYEINGITAALAEELFEKGEQLLGAGEVFAIGPLQLYAVTEQLQQGKPTCASGDAKTDLGHILDFTCRLKYLKVSGTEGPFGTSNIQEQLLPFDLSIFKSLHQVEISHCDAKHIRGLVASKPTLATLSVRFSATSMKEVLVPEASEFDEWEPEGTTLEGPVTAVIPTWQALTTLDLSHNSVSEIDESVKLIPKIEFLDLSHNGLLVVDNLQHLYNLVHLDLSYNKLSSLEGLHTKLGNIKTLNLAGNLLESLSGLHKLYSLVNLDLRDNRIEQMEEVRSIGSLPCLEHVSLLNNPLSIIPDYRTKVLAQFGERASEVCLDDTVTTEKELDTVEVLKAIQKAKEVKSKLSNPEKKGGEDSRLSAAPCIRPSSSPPTVAPASASLPQPILSNQGNRVCILLLVEPHSPAWAPWLGWGWGRGASTCFQQGQTQGGQCLLQAGPRGGTHGRGAWPDASCCLLGEDSQLL
Protein: Uncharacterized membrane protein YGR026W (P53217)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Subcellular location: Cell membrane {ECO:0000269|PubMed:14562095}; Multi-pass membrane protein {ECO:0000269|PubMed:14562095}.
Interaction partners:
- Uncharacterized peptidase YFR006W
- Probable transcriptional regulatory protein HAH1
Sequence:
MAKTIKVIRKKDPKKKNLSDPLAKQKLVWKIGHVLTLVFGLLFSITYFYHVLIFFKYRSWKWLFLRVNKNYSFIQSKRWYMKLLSWSPQVMYRLSLIGVFMSESVTMQQNWVGLNPTWNDLLSSENFHTLLIACLWFFGGGKSFYKILPYMILSYLHLTKMNYELNANKEEKIPLTPKDRKMLHLLAYSELLVILALTLDTILFKTGTSGFMLVIYVGIYWLRLNFSPYAQVAVLELLVKFEKYVPKKYRDKWQVIKNFIYMKMKEHEKRTEEVARYA
Protein: ATP-sensitive inward rectifier potassium channel 12 (Potassium inwardly rectifying channel subfamily J member 12a) (A0A0R4ICH9)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141, ECO:0000256|RuleBase:RU003822}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141, ECO:0000256|RuleBase:RU003822}.
Interaction partners:
Sequence:
MSVGRIGRYSIVSTEEDGLRLTTMHGGGMNGYGNGKIHTRRKSRNRFVKKNGQCNVQFTNMDEKSQRYMADIFTTCVDIRWRYMLIVFTLVFVISWLAFGLAFWVIALLHGDLDNPAGDDNFTPCVLQVNGFIAAFLFSIETQTTIGYGFRCVTEECPLAVFLVVFQSIVGSIIDCFMIGAIMAKMARPKKRAQTLLFSHNAVIAMRDGKLCLMWRVGNLRKSHIVEAHVRAQLIKPRVTTEGEYIPLDQLDINVGFDKGLDRIFLVSPITILHQIDHESPLFGISKQDLETADFEIVVILEGMVEATAMTAQARSSYLASEILWGHRFEPVLFEEKNQYKVDYSHFHKTYEVPSTPRCSAKDMMENKYLVVPTANSFCYENELAILSHEEEDDSPERIKPERAMSLSPERTPRHDFDRLQTPRCTEQRSYRRESEI
Protein: Pumilio homolog 14 (APUM-14) (AtPUM14) (Q4PSD1)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Sequence-specific RNA-binding protein that regulates translation and mRNA stability by binding the 3'-UTR of target mRNAs.
Subcellular location: Cytoplasm. Nucleus.
Interaction partners:
- Pumilio homolog 24
- Pumilio homolog 26
- Pumilio homolog 23
- Putative pumilio homolog 22
- Putative pumilio homolog 25
Sequence:
MDKNFRVNTNDERNIWLSTAVNENLTMASSSSQPQPISSPFHQPENQVNRVNPGSHYYDLETLESSFGGLSFNDSSVGQNGDSIHLPRRTNQVFTGSSSGGAGDDNGYLLPPMGSHHHRELEELQRHNYLNQLRMSYQNDYAHQSYWYNTDGDGNGMLNNGFLNDVPSSSRDRVSDYYTNRFGYEGYNYWRGNEGFDYNQCQASFSAFAKDKEMSERLGMSIFQGTKETVDAIYNGLIGDICELMVDPYGSDVVQLLMRRCSSEQIVQLVDIVTQQMFQFVNICIDSLGTNAIQVLLTCINERAKDQIPRIVDVVRTVALQLSKSNHAIFVILACFRLFPLHCRLLLELIVQNCHQIAIDQHGCCLLQLCFNKDRVPNLEIRQRLIMEAIANALRLCLNCYGNYVVQYIVELNNRYLIDALVRQLIGNYAHLARNKYGSHAVQKLLKLRWIDSRVIVIDLLREIDTLLLDPFGNYVIQTAWFVSKDDVRRMLRYHIERNIPMMRCNKFGNKVLEKLNI
Protein: Rho guanine nucleotide exchange factor 9 (Collybistin) (Rac/Cdc42 guanine nucleotide exchange factor 9) (F1Q628)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}. Postsynaptic density {ECO:0000256|ARBA:ARBA00034105}.
Interaction partners:
- Formin-like protein 3
- Cell division control protein 42 homolog
Sequence:
MLISGGSVVSAEAVWDHVTMAERELAFKAGDVIKVLDASNKDWWWGQIDDEEGWFPASFVRLWVNQENIATESAEGASEVQNGHTDPSNGCLCIGQPLQNRDQMRANVINEIMSTERHYIKHLKDICEGYLRQCRKRIDMFNDDQLKVIFGNIEDIYRFQMGFVRDLEKQYNIEEPHLSEIGPCFLEHQDGFWIYSEYCNNHLDACMELSKLMKDGRYQHFFEACRLLQQMIDIAIDGFLLTPVQKICKYPLQLAELLKYTAQEHSDYRYVAAALAVMRNVTQQINERKRRLENIDKIAQWQASVLDWEGDDILDRSSELIYTGEMSWIYQPYGRSQQRVFFLFDHQLVLCKKDLIRRDILYYKGRIDMDRYAVRDAIDGRDDDFNVSVKNAFKLHNRDSDEIHIFLAKKPEEKIRWLRAFHEERKMVQEDEKIGFEISEYQKKQAAMTVRKVTKQKGVSQSRCVSPSDPSSHGPFVLSDDMQQSDLVEFHVSKSGQSPFWQNFNKFTSKNGKK
Protein: Large ribosomal subunit protein uL1 (50S ribosomal protein L1) (P9WHC7)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: Binds directly to 23S rRNA. The L1 stalk is quite mobile in the ribosome, and is involved in E site tRNA release.
Interaction partners:
- Large ribosomal subunit protein uL13
- Large ribosomal subunit protein uL4
- Large ribosomal subunit protein uL15
- Large ribosomal subunit protein uL5
- Large ribosomal subunit protein uL11
- Large ribosomal subunit protein uL16
- Large ribosomal subunit protein uL30
- Large ribosomal subunit protein bL17
- Large ribosomal subunit protein uL6
- Large ribosomal subunit protein uL10
Sequence:
MSKTSKAYRAAAAKVDRTNLYTPLQAAKLAKETSSTKQDATVEVAIRLGVDPRKADQMVRGTVNLPHGTGKTARVAVFAVGEKADAAVAAGADVVGSDDLIERIQGGWLEFDAAIATPDQMAKVGRIARVLGPRGLMPNPKTGTVTADVAKAVADIKGGKINFRVDKQANLHFVIGKASFDEKLLAENYGAAIDEVLRLKPSSSKGRYLKKITVSTTTGPGIPVDPSITRNFAGE
Protein: Peptidyl-prolyl cis-trans isomerase FKBP3 (PPIase FKBP3) (EC 5.2.1.8) (25 kDa FK506-binding protein) (25 kDa FKBP) (FKBP-25) (FK506-binding protein 3) (FKBP-3) (Immunophilin FKBP25) (Rapamycin-selective 25 kDa immunophilin) (Rotamase) (Q62446)
Organism: Mus musculus (Mouse)
Function: FK506- and rapamycin-binding proteins (FKBPs) constitute a family of receptors for the two immunosuppressants which inhibit T-cell proliferation by arresting two distinct cytoplasmic signal transmission pathways. PPIases accelerate the folding of proteins (By similarity).
Subcellular location: Nucleus {ECO:0000250}.
Interaction partners:
- Serine/threonine-protein kinase mTOR
- Calcineurin subunit B type 1
Sequence:
MAAAVPQRAWTVEQLRSEQLPKKDIIKFLQDHGSDSFLAEHKLLGNIKNVAKTANKDHLVNAYNHLFESKRFKGTETISKVSEQVKNVKLSDDKPKDSKSEETLDEGPPKYTKSILKKGDKTNFPKKGDVVHCWYTGTLPDGTVFDTNIQTSSKKKKNAKPLSFKVGVGKVIRGWDEALLTMSKGEKARLEIEPEWAYGKKGQPDAKIPPNTKLIFEVELVDID
Protein: Glycolate oxidase subunit GlcD (EC 1.1.99.14) (Glycolate dehydrogenase subunit GlcD) (P0AEP9)
Organism: Escherichia coli (strain K12)
Function: Component of a complex that catalyzes the oxidation of glycolate to glyoxylate. Is required for E.coli to grow on glycolate as a sole source of carbon. Is also able to oxidize D-lactate ((R)-lactate) with a similar rate. Does not link directly to O(2), and 2,6-dichloroindophenol (DCIP) and phenazine methosulfate (PMS) can act as artificial electron acceptors in vitro, but the physiological molecule that functions as primary electron acceptor during glycolate oxidation is unknown.
Subcellular location: Cell inner membrane {ECO:0000269|PubMed:2689218}. Note=Glycolate oxidoreductase activity was shown to be firmly associated with the cytoplasmic membranes. {ECO:0000269|PubMed:2689218}.
Interaction partners:
- Glycolate oxidase subunit GlcE
- Glycolate oxidase iron-sulfur subunit
- Malate synthase G
- Protein GlcG
- Glyoxylate/hydroxypyruvate reductase B
- Lactaldehyde dehydrogenase
- Glyoxylate/hydroxypyruvate reductase A
- Phosphoglycolate phosphatase
- Anaerobic glycerol-3-phosphate dehydrogenase subunit C
- Isocitrate lyase
Sequence:
MSILYEERLDGALPDVDRTSVLMALREHVPGLEILHTDEEIIPYECDGLSAYRTRPLLVVLPKQMEQVTAILAVCHRLRVPVVTRGAGTGLSGGALPLEKGVLLVMARFKEILDINPVGRRARVQPGVRNLAISQAVAPHNLYYAPDPSSQIACSIGGNVAENAGGVHCLKYGLTVHNLLKIEVQTLDGEALTLGSDALDSPGFDLLALFTGSEGMLGVTTEVTVKLLPKPPVARVLLASFDSVEKAGLAVGDIIANGIIPGGLEMMDNLSIRAAEDFIHAGYPVDAEAILLCELDGVESDVQEDCERVNDILLKAGATDVRLAQDEAERVRFWAGRKNAFPAVGRISPDYYCMDGTIPRRALPGVLEGIARLSQQYDLRVANVFHAGDGNMHPLILFDANEPGEFARAEELGGKILELCVEVGGSISGEHGIGREKINQMCAQFNSDEITTFHAVKAAFDPDGLLNPGKNIPTLHRCAEFGAMHVHHGHLPFPELERF