wanglab/gogpt-training-data huggingface dataset:
Protein: 15-cis-phytoene synthase (PSase) (EC 2.5.1.32) (P37269)
Organism: Synechococcus elongatus (strain ATCC 33912 / PCC 7942 / FACHB-805) (Anacystis nidulans R2)
Function: Involved in the biosynthesis of carotenoids. Catalyzes the condensation of two molecules of geranylgeranyl diphosphate (GGPP) to give prephytoene diphosphate (PPPP) and the subsequent rearrangement of the cyclopropylcarbinyl intermediate to yield 15-cis-phytoene.
Interaction partners:
- 15-cis-phytoene desaturase
- Carotene isomerase
- Probable zeta-carotene desaturase
- prolycopene isomerase
- Phytoene dehydrogenase-like
- dimethylallyltranstransferase
- Beta-carotene hydroxylase
- Trans-hexaprenyltranstransferase
- Methyltransferase type 11 domain-containing protein
- Geranylgeranyl reductase
Sequence:
MLQMIPARPSRALASLSEAYEECRQITARYAKTFYLGTLLMPEAKRQAIWAIYVWCRRTDELVDGPQAAQTNFATLDAWERRLERLFAGEPEDDCDVALVDTLARYPLDIQPFRDMIEGQRMDLLQNRYSTFEDLYTYCYRVAGTVGLMSQPVMGIESTNSRAPWDPTTPPDPTQEALALGIANQLTNILRDVGEDARRGRIYLPQEELAQFNYSEQDLFNGVIDDRWRAFMQFQLDRARDYFEQAERGIRQLSHDARWPVWASLMLYREILDVIEQNNYDVFRKRAYVPTWRKLCSLPVAMLRATVL
Protein: Integrin subunit alpha V (F1LZX9)
Organism: Rattus norvegicus (Rat)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004479, ECO:0000256|RuleBase:RU003762}; Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004479, ECO:0000256|RuleBase:RU003762}.
Interaction partners:
Sequence:
MADPGRLLLRPRPGGLLLLLLGLLLPFAGSFNLDVESPAEYAGPEGSYFGFAVDFFVPSTSSMFLLVGAPKANTTQPGIIEGGQVLKCDCSSSRRCQPIEFDSTGNRDYAKDDPLEFKSHQWFGASVRSKQDKILACAPLYHWRTEMKQEREPVGTCFLQDGTKTVEYAPCRSKNIDADGQGFCQGGFSIDFTKADRVLLGGPGSFYWQGQLISDQVAEIISKYDPNVYSIKYNNQLATRTAQAIFDDSYLGYSVAVGDFNGDGIEDFVSGVPRAARTLGMVYIYDGKNMSSLHNFTGEQMAAYFGFSVAATDINGDDYADVFIGAPLFMDRGSDGKLQEVGQVSVSLQRASGDFQTTKLNGFEVFARFGSAIAPLGDLDQDGFNDIAIAAPYGGEDKKGLVYIFNGRSTGLNSVPSQILQGQWAAQSMPPSFGYSMKGATDVDRNGYPDLVVGAFGVDRAVLYRARPVVTVNAGLEVYPSILNQDNKICPLPGTALKVSCFNVRFCLKADGKGTLPRKLNFQVELLLDKLKQKGAIRRALFLHNRSPGHSKDMTVFRGGQTQCEELVAYLRDESEFRDKLTPITIFMEYRLDQRTAADATGLQPILNQFTPANVSRQAHILLDCGEDNVCKPKLEVSVDSDQKKIYIGDDNPLTLTVKAQNQGEGAYEAELIVSIPPQADFIGVVRNNEALARLSCAFKTENQTRQVVCDLGNPMKAGTQLLAGLRFSVHQQSEMDTSVKFDLKIQSSNSFDNVSPVVSYKVDLAVLAAVEIRGVSSPDHIFLPIPNWEYKETPETEEDVGPVVQHIYELRNNGPSSFSKAILNLQWPYKYNNNTLLYILHYDIDGPMNCTADTEINPLRIKTPEKNDTAAEQGGRNHLITKRDLSLSEGDVHTLGCGTAQCLQITCQVGRLDRGKSAILYVKSLLWTETFMNKENQNHSYSLKSSASFNIIEFPYKNLPIEDLFNSTLVTTNITWGIQPAPMPVPVWVIILAVLAGLLLLAVLVFVMYRMGFFKRVRPPQEEQEREQLQPHENGEGNSET
Protein: Transcription factor (A0A1D8PDR2)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- Amino acid starvation-responsive transcription factor
- non-specific serine/threonine protein kinase
Sequence:
MELTVDNTNTTSNIDDLSVATPTSLMTSTTTSPSMSTSTSSHSNTLDIDPATFKSTLPPRKRAKTQEEKEQRKIERILRNRRAAHASREKKRKHVEYLENYVLKLETNLMKLNNNYNQAFELLTKDNQELLLSKLEVLDDVSDLKEQIHSNMSGTRRSHNKKSNDEDIEEEDEDEHQEEGHVEKQEIKKEEPVSKKRKLNTKTKSKTKTKSSNKTMTSTPPSSVSSLSPDVTNFSGTNTTMSSPIQIKKEFNIDNIFIKKEFSQSPLQPTHQPEQQEQQHEIYLKSESKDAFWNYPSPLSFHDSPLQIDIDTSSSSSTSPSSSSSLISSSGPTNHSIADLAEPIESFQLDFDDFFSILGDDVEVHKV
Protein: Inositol-3-phosphate synthase isozyme 1 (AtIPS1) (MIP synthase 1) (EC 5.5.1.4) (Myo-inositol 1-phosphate synthase 1) (AtMIPS 1) (MI-1-P synthase 1) (P42801)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Key enzyme in myo-inositol biosynthesis pathway that catalyzes the conversion of glucose 6-phosphate to 1-myo-inositol 1-phosphate in a NAD-dependent manner. Catalyzes the majority of myo-inositol synthesis required for plant growth and development. Acts as a repressor of programmed cell death and protects plant cells against cell death under high light intensity or long days. Controls its own transcription by inhibiting ATXR6 activity. Reduces the deposition of inhibitory histone marks on its own promoter.
Subcellular location: Cytoplasm, cytosol {ECO:0000269|PubMed:18603618, ECO:0000269|PubMed:19812700, ECO:0000269|PubMed:20215587}. Nucleus {ECO:0000269|PubMed:19812700}.
Interaction partners:
- Inositol-phosphate phosphatase
- Phosphatase IMPL1, chloroplastic
- Bifunctional phosphatase IMPL2, chloroplastic
- Probable ubiquitin-conjugating enzyme E2 24
- Inositol-3-phosphate synthase isozyme 2
- Inositol 3-kinase
- Phosphate transporter PHO1
- Probable inositol 3-phosphate synthase isozyme 3
- Protein PHOSPHATE STARVATION RESPONSE 1
- Sulfoquinovosyl transferase SQD2
Sequence:
MFIESFKVESPNVKYTENEIHSVYDYETTEVVHEKTVNGTYQWIVKPKTVKYDFKTDIRVPKLGVMLVGLGGNNGSTLTAGVIANKEGISWATKDKVQQANYFGSLTQASSIRVGSFNGEEIYAPFKSLLPMVNPDDVVFGGWDISDMNLADAMARARVLDIDLQKQLRPYMENIVPLPGIFDPDFIAANQGSRANHVIKGTKKEQVDHIIKDMREFKEKNKVDKVVVLWTANTERYSNVVVGMNDTMENLMESVDRDEAEISPSTLYAIACVLEGIPFINGSPQNTFVPGLIDMAIRNNVLIGGDDFKSGQTKMKSVLVDFLVGAGIKPTSIVSYNHLGNNDGMNLSAPQTFRSKEISKSNVVDDMVASNGILFEPGEHPDHVVVIKYVPYVADSKRAMDEYTSEIFMGGKNTIVMHNTCEDSLLAAPIILDLVLLAELSTRIQFKSEGEGKFHSFHPVATILSYLTKAPLVPPGTPVINALSKQRAMLENIMRACVGLAPENNMIMEFK
Protein: Putative uncharacterized hydrolase C7D4.05 (EC 3.-.-.-) (O14262)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus {ECO:0000269|PubMed:16823372}.
Interaction partners:
- Uncharacterized membrane protein C977.17
- Uncharacterized protein C186.04c
Sequence:
MIPSKNIQKIKLVTFDAFGTILHLSKPVPIVYSEVAQKYGVHATIDEIEHNSNKAFKDFSEKHKNHGKKSGLNPHDWWIKVIEHSFPTPVPAEMAEELWSYFSKKTGYTIHPLLIDFLKRNKEERKYIIGIISNTDERIRTVLEDYGIDHLIDIYAFSYDVGFEKPSREIFDYAMEKAVKLLGQEIQPEECMHLGDDLIKDVSAARNIQWNAEYCDIKTNFLKYFEQK
Protein: BAR domain-containing protein (C7FZZ5)
Organism: Dictyostelium discoideum (Social amoeba)
Interaction partners:
- RCR-type E3 ubiquitin transferase
- PH domain-containing protein
- Pleckstrin domain-containing protein
Sequence:
MFKKGLDVLSKTKNAAVSSMTELETESDEVQNAKVALKNMKWSIKLLIQLAKNYFATSDKQVQQGTAFSVILQRFSEKISHTNYIINQTLPLSDSLREVGEGIKNSSTYFQQYTQIFCDKFATNIEALYVGHVKKVATLEKQQEESRIKYNNALNYLKSTQKSGHTGTKLAEKTTEYENAKAYYEQISLNLISATNDMVNYVQREVAVQMKQFVAEQQLMVQECIKMWVIAENKLFNSQSPVNTTSTTSPNTYGDYNNNANTVNLSKLSLDKEEQPPQPYQPPQQHSPPQQTFHQSPPTDFSSQHQQYSFDQSSPQETYQPPQQQQPEGQKSPNPFDDKNPFDN
Protein: THAP domain-containing protein 8 (Q8NA92)
Organism: Homo sapiens (Human)
Interaction partners:
- THAP domain-containing protein 10
Sequence:
MPKYCRAPNCSNTAGRLGADNRPVSFYKFPLKDGPRLQAWLQHMGCEHWVPSCHQHLCSEHFTPSCFQWRWGVRYLRPDAVPSIFSRGPPAKSQRRTRSTQKPVSPPPPLQKNTPLPQSPAIPVSGPVRLVVLGPTSGSPKTVATMLLTPLAPAPTPERSQPEVPAQQAQTGLGPVLGALQRRVRRLQRCQERHQAQLQALERLAQQLHGESLLARARRGLQRLTTAQTLGPEESQTFTIICGGPDIAMVLAQDPAPATVDAKPELLDTRIPSA
Protein: Prefoldin subunit 1 (Gene involved in microtubule biogenesis 6) (Q94AF7)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Binds specifically to cytosolic chaperonin (c-CPN) and transfers target proteins to it. Binds to nascent polypeptide chain and promotes folding in an environment in which there are many competing pathways for nonnative proteins. Together with other chaperonins, contribute to the regulation of gene expression by modulating the spliceosome function on pre-mRNA splicing post-transcriptionally by acting as a co-chaperone of Hsp90 to control levels of LSM8 (By similarity). Required for microtubules (MTs) organization and dynamicity (By similarity). Involved in the process leading to microtubules dissociation in response to gibberellic acid (GA) probably due to the DELLA proteins-mediated translocation of the prefoldin co-chaperone complex from the cytoplasm to the nucleus (By similarity).
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:P57742}. Nucleus {ECO:0000250|UniProtKB:P57742}. Note=In the presence of gibberellic acid (GA) and at room temperature, the prefoldin complex stays in the cytoplasm and is functional (By similarity). But in the absence of GA or in response to cold, the prefoldin complex is localized to the nucleus in the presence of DELLA proteins, which severely compromises alpha/beta-tubulin heterodimer availability, thus affecting microtubules (MTs) organization (By similarity). This changing subcellular localization follows a daily rhythm coordinated oscillation (By similarity). {ECO:0000250|UniProtKB:P57742}.
Interaction partners:
- Prefoldin subunit 4
- Prefoldin subunit 6
- Prefoldin subunit 2
- Prefoldin subunit 3
- Prefoldin subunit 5
- T-complex protein 1 subunit delta
- T-complex protein 1 subunit beta
- T-complex protein 1 subunit eta
- T-complex protein 1 subunit gamma
- T-complex protein 1 subunit alpha
Sequence:
MADEATRAAFMEIQASMIELTGKLKQVQNQMRNKEGDRKRAFLTLEELRPLPEETNTYKSIGRTFVLEPKTVLEGEQEQKLKDSEAAVASLQTSKEYLEKQVAEVENNLRELLQQEPGIAQQIMSMSM
Protein: Autophagy-related protein 8 (Autophagy-related ubiquitin-like modifier ATG8) (Q51MW4)
Organism: Pyricularia oryzae (strain 70-15 / ATCC MYA-4617 / FGSC 8958) (Rice blast fungus) (Magnaporthe oryzae)
Function: Ubiquitin-like modifier involved in autophagosomes formation. With ATG4, mediates the delivery of the autophagosomes to the vacuole via the microtubule cytoskeleton. Required for selective autophagic degradation of the nucleus (nucleophagy) as well as for mitophagy which contributes to regulate mitochondrial quantity and quality by eliminating the mitochondria to a basal level to fulfill cellular energy requirements and preventing excess ROS production. Participates also in membrane fusion events that take place in the early secretory pathway. Also involved in endoplasmic reticulum-specific autophagic process and is essential for the survival of cells subjected to severe ER stress. The ATG8-PE conjugate mediates tethering between adjacent membranes and stimulates membrane hemifusion, leading to expansion of the autophagosomal membrane during autophagy.
Subcellular location: Cytoplasmic vesicle, autophagosome membrane {ECO:0000250|UniProtKB:P38182}; Lipid-anchor {ECO:0000250|UniProtKB:P38182}. Vacuole membrane {ECO:0000250|UniProtKB:P38182}; Lipid-anchor {ECO:0000250|UniProtKB:P38182}.
Interaction partners:
- Cysteine protease ATG4
- Autophagy-related protein 3
- Ubiquitin-like modifier-activating enzyme ATG7
- Serine/threonine-protein kinase ATG1
- triacylglycerol lipase
- Ubiquitin-like protein ATG12
- Autophagy-related protein 18
- Autophagy protein 5
- Beclin-1
- Autophagy-related protein 9
Sequence:
MRSKFKDEHPFEKRKAEAERIRQKYTDRIPVICEKVEKSDIATIDKKKYLVPADLTVGQFVYVIRKRIKLSPEKAIFIFVQDTLPPTAALMSSIYELHKDEDGFLYITYSGENTFGDLFEEVE
Protein: Utrophin (A0A1W2P8G5)
Organism: Mus musculus (Mouse)
Interaction partners:
Sequence:
MAKYGDLEARPDDGQNEFSDIIKSRSDEHNDVQKKTFTKWINARFSKSGKPPISDMFSDLKDGRKLLDLLEGLTGTSLPKERGSTRVHALNNVNRVLQVLHQNNVDLVNIGGTDIVDGNPKLTLGLLWSIILHWQVKDVMKDIMSDLQQTNSEKILLSWVRQTTRPYSQVNVLNFTTSWTDGLAFNAVLHRHKPDLFSWDRVVKMSPIERLEHAFSKAHTYLGIEKLLDPEDVAVHLPDKKSIIMYLTSLFEVLPQQVTIDAIREVETLPRKYKKECEEEEIHIQSAVLAEEGQSPRAETPSTVTEVDMDLDSYQIALEEVLTWLLSAEDTFQEQDDISDDVEEVKEQFATHETFMMELTAHQSSVGSVLQAGNQLMTQGTLSEEEEFEIQEQMTLLNARWEALRVESMERQSRLHDALMELQKKQLQQLSSWLALTEERIQKMESLPLGDDLPSLQKLLQEHKSLQNDLEAEQVKVNSLTHMVVIVDENSGESATALLEDQLQKLGERWTAVCRWTEERWNRLQEISILWQELLEEQCLLEAWLTEKEEALNKVQTSNFKDQKELSVSVRRLAILKEDMEMKRQTLDQLSEIGQDVGQLLSNPKASKKMNSDSEELTQRWDSLVQRLEDSSNQVTQAVAKLGMSQIPQKDLLETVHVREQGMVKKPKQELPPPPPPKKRQIHVDVEAKKKFDAISTELLNWILKSKTAIQNTEMKEYKKSQETSGMKKK
Protein: E3 ubiquitin-protein ligase CBL (EC 2.3.2.27) (Q9VSK2)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Epidermal growth factor receptor
- Growth factor receptor-bound protein 2
- Protein sprouty
- Adapter molecule Crk
- CIN85 and CD2AP related, isoform J
- Protein vav
- E3 ubiquitin-protein ligase Nedd-4
- GH01161p
- E3 ubiquitin-protein ligase NRDP1
- E3 ubiquitin-protein ligase Smurf1
Sequence:
MATRGSGTRVQSQPKIFPSLLSKLHGAISEACVSQRLSTDKKTLEKTWKLMDKVVKLCQQPKMNLKNSPPFILDILPDTYQRLRLIYSKNEDQMHLLHANEHFNVFINNLMRKCKQAIKLFKEGKEKMFDENSHYRRNLTKLSLVFSHMLSELKAIFPNGVFAGDQFRITKADAADFWKSNFGNSTLVPWKIFRQELNKVHPIISGLEAMALKTTIDLTCNDFISNFEFDVFTRLFQPWVTLLRNWQILAVTHPGYVAFLTYDEVKARLQRYILKAGSYVFRLSCTRLGQWAIGYVTAEGEILQTIPQNKSLCQALLDGHREGFYLYPDGQAYNPDLSSAVQSPTEDHITVTQEQYELYCEMGSTFQLCKICAENDKDIRIEPCGHLLCTPCLTSWQVDSEGQGCPFCRAEIKGTEQIVVDAFDPRKQHNRNVTNGRQQQQEEDDTEDIGDFNIATSSLHALSTSSTVAAEKHSPHTSPRLGRRSTTPSLMAVQNDLYAGGTPTLSLPSSSCSSIAAASTSSSSSLASVATVAASTSSSQHQQPQPSAPPASAVLSNGGGGGGGGGASSSQKNTNRMSAPLIGSCVANSTYGQKLPQNCSHSSTSSSSDNASSSSSYAILQNLHDTGTPATAAAVVAPPLPPRKSSPGVETPSKATAPPPPSSSKSIDNIQCSLDNVPPQTTAPPIPPHVSPSVDTLAEDLMRQQLIATSTTSPVLSLLDEDIVEVGPAETISGVIDTRPLEARGVTLCRQDSASSHYTQLCTTSSGGSAAALANGKKANSAKQSQATTTTSAAAAAATAGNGSNPGQQSQPLLYANVTINQKDCGTVPYENINLEYIARLMNAGYSKENAITALGISRNNIEMAGDILREFVSKNSA
Protein: Si:dkey-235h8.3 (A4JYQ1)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
Sequence:
MNFIALLLTSTCFFSCISAKYHYNQDKDKELKYLLEPLVFAEVSARRGHAAILPCVMRFKPSHYRVKWTKLEPSSRGVENIVLITNGHADKQYGSVGPRAALQRAHDLDVSLRLSDLELEDDGSYRCELINGIEDESVIITLRIEGVVFPYQSQKGRYRFTFFDAKEACAEQDATLATYKQLYRAWTEGLDWCNAGWLSDGTVSYPVLHPRPACGGDLLSGIRSYGPRHKTRENYDAFCFTSTSKGSVFFIEGQLNFAEAERACRRDGAGLAKTGQIYSSWRFQQLDRCDGGWLEDGSVRFPIINPREHCGGIAEPGVRSFGFPSKSMRLYGAYCYR
Protein: Outer kinetochore KNL1 complex subunit sos7 (Kinetochore protein Sos7) (Suppressor of spc7 protein) (U3H042)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Acts as a component of the NMS (Ndc80-MIND-Spc7) super complex which has a role in kinetochore function during late meiotic prophase and throughout the mitotic cell cycle. Essential for chromosome segregation and bipolar sister chromatid association. Required for kinetochore targeting of MIND, but not Ndc80 complex components.
Subcellular location: Nucleus {ECO:0000269|PubMed:22711988}. Chromosome, centromere, kinetochore {ECO:0000269|PubMed:22711988}.
Interaction partners:
- mRNA export factor elf1
- Elongation factor 3
- Outer kinetochore KNL1 complex subunit spc7
- Small ribosomal subunit protein eS21
- Small ribosomal subunit protein uS15
- Large ribosomal subunit protein uL24
- Large ribosomal subunit protein eL14
- Large ribosomal subunit protein eL31
- Large ribosomal subunit protein eL29
- Small ribosomal subunit protein uS10
Sequence:
MDQNKSTQATGNGKKTEEINELLESFIKEGPKLLWGSTNLKYEDQISRSSEHELQQYRELFTRLKFSYIEQGTKERYLRAILDDPPMLVEAEDNEKLETTNSSLKGRLKSEKREVDLLTEELKTTSRELSSNYESVMEECKNTKSTLSKLESLESELLKLQQDSSTKTPILPEVEAAIHDLESELNITNESIETIDGKIDNDEKYFIQLTKNLSLLEKEYKIASERSNQIKAAIHTRTPDADAKKQVQNWYTSMLEIYDQLLQK
Protein: Transcriptional regulator CmeR (Q0PBE2)
Organism: Campylobacter jejuni subsp. jejuni serotype O:2 (strain ATCC 700819 / NCTC 11168)
Interaction partners:
- Periplasmic fusion protein CmeA
- Outer membrane channel protein CmeC
- Inner membrane efflux transporter CmeB
- Ferredoxin domain-containing integral membrane protein
- DNA gyrase subunit A
Sequence:
MNSNRTPSQKVLARQEKIKAVALELFLTKGYQETSLSDIIKLSGGSYSNIYDGFKSKEGLFFEILDDICKKHFHLIYSKTQEIENGTLKEILTSFGLAFIEIFNQPEAVAFGKIIYSQVYDKDRHLANWIENNQQNFSYNILMGFFKQQNNSYMKKNAEKLAVLFCTMLKEPYHHLNVLINAPLKNKKEQKEHVEFVVNVFLNGINSSKA
Protein: ER membrane protein complex subunit 7 (A1ZA83)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004167}; Single-pass membrane protein {ECO:0000256|ARBA:ARBA00004167}.
Interaction partners:
- ER membrane protein complex subunit 4
- ER membrane protein complex subunit 3
- ER membrane protein complex subunit 10
- ER membrane protein complex subunit 1
- ER membrane protein complex subunit 6
- Membrane magnesium transporter
- ER membrane protein complex subunit 2
- ER membrane protein complex subunit 2
- ER membrane protein complex subunit 8/9 homolog
- Actin-related protein 2/3 complex subunit 4
Sequence:
MCLKLFVFTALLALVSCEVIIGQDELVDEVSGLYTIEGRVSPPDSIFSPTQGGGRSAPVNKNTPKWHTEITLSINDGEFKGFVREDGQFMISGVPSGSYILDVHHPDVFYEPVRVEINPKGKFRARKVNFVQPAQIMQVAYPLRVKPLMPFKYFQTREQWKITDFLFSPMVLMMVLPLLLMLVLPKMINDPETKKEIDNLQFPKMGNDMPEISEMLTSLLTGKQPEPKEKKPAPAVRQAKKRKDQ
Protein: SD07795p (Q960C3)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MDVDSPLGRTESSTRNAKSTPSESASPARSNASTSSVTPAGIKKETDDSKATTGSFAPASSATASSATPVDDATPSTSSAAAAASAASSSTVSGTEGKPKDDPLSSHKEEGAGSTSSGVATSPRQAQDTAGAGVDVEIKLEHPADFSNPKLLPPHAHGQREDESYTLFFANNNWYLFLRLHAILCDRLHVMYERARLLAIEEERCRVNRRESTATALRLKPKPEIQVEDYYPTFLDMLKNVLDGNMDSNTFEDTMREMFGIYAYISFTLDKVVSNAVRQLQYCVTERAALDCVELFATEQRRGCTGGFCRDAHKTFDREMSYQRKAESILNEENCFKVYIYKIDCRVTIELLDSEPEEVDKPAALKAQKFSKYVERLANPALGGGGNTGRSDSALGNDSVVDGSDIKTEADEDTAELRYREGGIGGAGKARFLVRNKRRSKLLEEQVRQLFEHRRNRIKQHGTAASLEPISVDSAISSNSTTGGGGSGTNNNNNNNNNNNSWGGKRLERLGAPQVGLAEQYAFNDRDEISTNISNGRCFVTSKNLKLLKYDAVRRAKKSHCRVTQAKYAHFQTYVNKWLQQHVSEQQQQNCVDWLLGKTADQINASGWGSASKTKTVQQKDTSKTPYRIYNRYRVVQSAVSGGLMSATAPTPDGSVPAVNSAPSGSVSTVNNVQGSAAVSSTSHSMCNSSILSADSTTNTNASAQQQQHCNSAAAATTPNAEALQQVRPMES
Protein: Mitochondrial Rho GTPase (EC 3.6.5.-) (A0A8I6AVD9)
Organism: Rattus norvegicus (Rat)
Subcellular location: Mitochondrion outer membrane {ECO:0000256|ARBA:ARBA00004200, ECO:0000256|PIRNR:PIRNR037488}; Single-pass type IV membrane protein {ECO:0000256|ARBA:ARBA00004200, ECO:0000256|PIRNR:PIRNR037488}.
Interaction partners:
Sequence:
MRAGRVRPLRASDMKKDVRILLVGEPRVGKTSLIMSLVSEEFPEEVPPRAEEITIPADVTPERVPTHIVDYSEAEQSDEQLHQEISQANVICIVYAVNNKHSIDKVTSRWIPLINERTDKDSRLPLILVGNKSDLVEYSSMETILPIMNQYTEIETCVECSAKNLKNISELFYYAQKAVLHPTGPLYCPEEKEMKPACIKALTRIFKISDQDNDGTLNDAELNFFQRICFNTPLAPQALEDVKNVVRKHLSDGVADSGLTLRGFLFLHTLFIQRGRHETTWTVLRRFGYDDDLDLTPEYLFPLLKIPPDCTTELNHHAYLFLQSTFDKHDLDRDCALSPDELKDLFQVFPYIPWGPDVNNTVCTNESGWITYQGFLSQWTLTTYLDVQRCLEYLGYLGYSILTEQESQASAITVTRDKKIDLQKKQTQRNVFRCNVIGVKGCGKTGVLQSLLGRNLMRQKKIRDDHKSYYAINTVYVYGQEKYLLLHDISESEFLTEAEIVCDVVCLVYDVTNPKSFEYCARIFKQHFMDSRIPCLIVAAKSDLHEVKQEHSVSPTDFCRKHKMPPPQAFTCNTADAPSKDIFVKLTTMAMYPEDHYRGSLSRDMGSTDRIENLRKIWVFLKTAFHARLRCMCTCNRCTFCICQNLLNSDLLQSVKNKVFTAVLNRHVTQADLKSSTFWLRASFGATVFAVVGFAMYRALLKQR
Protein: Taste receptor type 2 member 1 (T2R1) (Taste receptor family B member 7) (TRB7) (Q9NYW7)
Organism: Homo sapiens (Human)
Function: Receptor that may play a role in the perception of bitterness and is gustducin-linked. May play a role in sensing the chemical composition of the gastrointestinal content. The activity of this receptor may stimulate alpha gustducin, mediate PLC-beta-2 activation and lead to the gating of TRPM5.
Subcellular location: Membrane; Multi-pass membrane protein.
Interaction partners:
- Guanine nucleotide-binding protein G
- Semaphorin-5A
- Taste receptor type 1 member 2
- Taste receptor type 1 member 1
- Cadherin-9
- Taste receptor type 1 member 3
- Cadherin-10
- Taste receptor type 2 member 20
- Taste receptor type 2 member 39
- Extracellular calcium-sensing receptor
Sequence:
MLESHLIIYFLLAVIQFLLGIFTNGIIVVVNGIDLIKHRKMAPLDLLLSCLAVSRIFLQLFIFYVNVIVIFFIEFIMCSANCAILLFINELELWLATWLGVFYCAKVASVRHPLFIWLKMRISKLVPWMILGSLLYVSMICVFHSKYAGFMVPYFLRKFFSQNATIQKEDTLAIQIFSFVAEFSVPLLIFLFAVLLLIFSLGRHTRQMRNTVAGSRVPGRGAPISALLSILSFLILYFSHCMIKVFLSSLKFHIRRFIFLFFILVIGIYPSGHSLILILGNPKLKQNAKKFLLHSKCCQ
Protein: tRNA 2-thiolation protein NcsA (N-type ATP pyrophosphatase superfamily protein) (tRNA adenylyltransferase NcsA) (EC 2.7.7.-) (D4GSH6)
Organism: Haloferax volcanii (strain ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM B-1768 / DS2) (Halobacterium volcanii)
Function: Required for thiolation of mcm(5)S(2)U at the wobble uridine position of tRNA specific for lysine (tRNA(Lys)). Probably acts by catalyzing adenylation of tRNA, an intermediate required for 2-thiolation. May also act as a sulfurtransferase that transfers sulfur from thiocarboxylated SAMP2 onto the uridine of tRNA at wobble position. Required for cell growth at elevated temperatures.
Interaction partners:
- Small archaeal modifier protein 2
- Homolog to elongator complex protein ELP3.
- SAMP-activating enzyme E1
- Probable tRNA pseudouridine synthase D
- Probable tRNA sulfurtransferase
- Probable ribosomal RNA small subunit methyltransferase A
Sequence:
MECDKCGRDAVMHAAYSGAHLCDDHFCASVEKRVRRRIREDNMLPRDASPENPQTWVIGLSGGKDSVVLTHILDDTFGRDPRIELVALTIHEGIEGYRDKSVDACVELAEDLDIHHELVTYEDEFGVQMDDVVEKDPENMAACAYCGVFRRDLLERFADELGADKLLTGHNLDDEAQTALMNFFEGDLKQVAKHFDASIGDFEKRRDAGEFIPRAKPLRDVPEKEVALYAHLKDLPAHITECPHSSEAYRGEIQQLLLKLEENHPGTRHSIMAGYEELAELTAREYRGEGRVDLNDCERCGSKTAGDVCRKCRLIESIEAV
Protein: Peptide-N(4)-(N-acetyl-beta-glucosaminyl)asparagine amidase (EC 3.5.1.52) (Peptide:N-glycanase) (PNGase) (Q9TW67)
Organism: Caenorhabditis elegans
Function: Specifically deglycosylates the denatured form of N-linked glycoproteins in the cytoplasm and assists their proteasome-mediated degradation. Cleaves the beta-aspartyl-glucosamine (GlcNAc) of the glycan and the amide side chain of Asn, converting Asn to Asp. Prefers proteins containing high-mannose over those bearing complex type oligosaccharides. Can recognize misfolded proteins in the endoplasmic reticulum that are exported to the cytosol to be destroyed and deglycosylate them, while it has no activity toward native proteins. Deglycosylation is a prerequisite for subsequent proteasome-mediated degradation of some, but not all, misfolded glycoproteins. Also displays oxidoreductase (thioredoxin) activity. Involved in regulating the expression of proteasomal subunits such as rpt-3 in order to confer resistance to proteasomal dysfunction.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:17522090}. Endoplasmic reticulum {ECO:0000269|PubMed:17522090}. Note=ER localization inferred from partial colocalization with an ER marker, membrane protein PIG-X.
Interaction partners:
- UV excision repair protein RAD23
- Ubiquitin-like domain-containing protein
- Derlin-1
- E3 ubiquitin-protein ligase hrd-like protein 1
- Probable 26S proteasome regulatory subunit 4
- Transitional endoplasmic reticulum ATPase homolog 2
- UBX domain-containing protein 1
- Ubiquilin
- Thioredoxin domain-containing protein
- Ubiquitin conjugation factor E4 ufd-2
Sequence:
MPVTEVGSLPELNNILERSDANRLIIIDFFANWCGPCRMISPIFEQFSAEYGNATFLKVNCDVARDIVQRYNISAMPTFIFLKNRQQVDMVRGANQQAIAEKIRQHYSPTPANPNAASDSEKRFLEQFVKCSNVPRSYQDEVFKALARSVMPEELVGRAMTEGPRDEKAILKDLLHWFKTQFFTWFDRPTCPKCTLKCSTDGLQGTPTREEQKEGGASRVEVYICDGCNTEMRFPRYNNPAKLLQTRTGRCGEWANCFGLLLAALNLESRFIYDTTDHVWNEVYLLAEQRWCHVDPCENTMDRPLLYTRGWGKTLGYCIGYGSDHVVDVTWRYIWDSKKLVTQRNEVRQPVFENFLSKLNSRQAEGQTEPRKRELAVRRVCELMEMMAQEAKNHKIGWEKIGDDLGGRITGSEEWRRERGELGESGPKLLAEPIKLAPPTGPAQNYLEFNYDVITDTYSQPPEIGFSAQAFELENVQRVEETDWNMTYLCRKRGDAPGNISWHFDLKSLKKSIEKIEIRMAGIQKFEKGKAMAIACLGDSCMRLPIDCSALTIEDPKNAEILKITATLSGGEGAIGFQQAQIFRTELKRGGGARTESFSVKIWMKN
Protein: E3 ubiquitin-protein ligase (EC 2.3.2.26) (F6P346)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
- Mediator of RNA polymerase II transcription subunit 25
- Polyubiquitin-C
- Polyubiquitin-B
- Ubiquitin-ribosomal protein eS31 fusion protein
Sequence:
MAAASVSQSASIQAIEKSQLTLKVLSAKPQSPKLPNRHSRLSSFVEVTADGLSSETKKTGKRSGHLELQWNEDLTLNVTPQSRLDLKVWSCHTLRKELLGSATIDLLDTLRTHDGKMENVQLSLVLQTENKGSVVAGGELNVCLDGLVVDLGSLPNGSAASDKIHSSRSSLHRAHSEETPSTSSPRGRSLGQSSRGSCGDSPAEIQGAALTNGDVNGALAETTSRHNSKTTVNNLSSAGKGETAANGLESAHLTCPAPSSPSLSSNPPDGTVPPPAAEPPASTEQSDTTSDTQNTDALPAGWEQRILPHGRVYYVDHNTKTTTWERPLPPGWEKRVDQRGRFYYVDHNTRTTTWQRPTAESVRNYEQWQSQRSQLQGAMQQFNQRYLYQPSGAVVENDPLGALPPGWEKRQDNGRVYYVNHNTRTTQWEDPRTQGMIQEPPLPPGWEMKYTAEGVRYFVDHNSRTTTFKDPRPGFESGSRQGGSPGAYDRSFRWKYHQFRFLCHSNALPSHVKISVSRQTLFEDSFQQIMNMKPYDLRRRLYIIMRGEEGLDYGGIAREWFFLLSHEVLNPMYCLFEYAGKNNYCLQINPASSINPDHLTYFRFIGRFIAMALYHGKFIDTGFTLPFYKRMLNKKPTLKDLESIDPEFYNSIMWVKENDLEECGVELYFAQDMEILGKVTTHQLKDDGENELVTQDNKEEYIGLLTDWRFTRGVEEQTKAFLDGFNEVVPLEWLRYFDEKELELMLCGMQEIDLNDWQKNTIYRHYTKNSKQIHWFWQVVKEMDNEKRIRLLQFVTGTCRLPVGGFAELIGSNGPQKFCIDKVGKETWLPRSHTCFNRLDLPPYKNLEQLREKLLFAIEETEGFGQE