wanglab/gogpt-training-data huggingface dataset:
Protein: Aspartic proteinase yapsin-6 (EC 3.4.23.-) (P40583)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Cleaves proteins C-terminally to mono- and paired-basic residues (By similarity). Required for cell wall integrity.
Subcellular location: Cell membrane {ECO:0000305|PubMed:10383953}; Lipid-anchor, GPI-anchor {ECO:0000305|PubMed:10383953}.
Interaction partners:
Sequence:
MQLISILSLLSSLMCSLTVLGSSASSYVKFPVQKLADIINICTQDVSTVFKRNEVLNTTVINGIGVYVVKMEIGTPPQTLYLQLDTGSSDMIVNNADIAYCKSMSDGSDYASTDNYELTATFNGLPSTTISSEAYNTLCSYWGTFDASNSSTFENNATFFNNTYGDGTYYAGTYGTDVVSFENITLNDFTFGVSNDTIGNPSGILGISLPIAEFTDGIEYALALNRTPFIYDNFPMELKNQGKINKIAYSLFLNGPDAHFGSILFGAVDKSKYTGQLYTLPMLQAFNTLGSNPGMIITAQSVAILDSESGNKTVSDIQFPVMLDSGTTFSYLPTEIAEAIGKSFDGEYSSDDQGYIFDCSKVNDTLLSVDFGGFNISANISNFVTSAKDRCVLNVKQSESTYMLGDAFLVDAYVVYDLENYEISIAQASFNNQEEDIEVISDTVPGATPAPGYFSTWVYKPGSPIGTGDFINVSWTSYSEFSQYKSLLATAAQSDDASSFSSSGGSSESTTKKQNAGYKYRSSFSFSLLSFISYFLL
Protein: Tubulin polymerization-promoting protein (TPPP) (EC 3.6.5.-) (25 kDa brain-specific protein) (p25-alpha) (Q27957)
Organism: Bos taurus (Bovine)
Function: Regulator of microtubule dynamics that plays a key role in myelination by promoting elongation of the myelin sheath (By similarity). Acts as a microtubule nucleation factor in oligodendrocytes: specifically localizes to the postsynaptic Golgi apparatus region, also named Golgi outpost, and promotes microtubule nucleation, an important step for elongation of the myelin sheath (By similarity). Required for both uniform polarized growth of distal microtubules as well as directing the branching of proximal processes (By similarity). Shows magnesium-dependent GTPase activity; the role of the GTPase activity is unclear (By similarity). In addition to microtubule nucleation activity, also involved in microtubule bundling and stabilization of existing microtubules, thereby maintaining the integrity of the microtubule network. Regulates microtubule dynamics by promoting tubulin acetylation: acts by inhibiting the tubulin deacetylase activity of HDAC6 (By similarity). Also regulates cell migration: phosphorylation by ROCK1 inhibits interaction with HDAC6, resulting in decreased acetylation of tubulin and increased cell motility (By similarity). Plays a role in cell proliferation by regulating the G1/S-phase transition (By similarity). Involved in astral microtubule organization and mitotic spindle orientation during early stage of mitosis; this process is regulated by phosphorylation by LIMK2 (By similarity).
Subcellular location: Golgi outpost {ECO:0000250|UniProtKB:D3ZQL7}. Cytoplasm, cytoskeleton, microtubule organizing center {ECO:0000250|UniProtKB:D3ZQL7}. Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:O94811}. Nucleus {ECO:0000250|UniProtKB:O94811}. Cytoplasm, cytoskeleton, spindle {ECO:0000250|UniProtKB:O94811}. Note=Specifically localizes to the postsynaptic Golgi apparatus region, also named Golgi outpost, which shapes dendrite morphology by functioning as sites of acentrosomal microtubule nucleation (By similarity). Mainly localizes to the cytoskeleton. Also found in the nucleus; however, nuclear localization is unclear and requires additional evidences. Localizes to glial Lewy bodies in the brains of individuals with synucleinopathies. During mitosis, colocalizes with LIMK2 at the mitotic spindle (By similarity). {ECO:0000250|UniProtKB:D3ZQL7, ECO:0000250|UniProtKB:O94811}.
Interaction partners:
- Alpha-synuclein
Sequence:
MADSRPKPANKTPPKSPGEPAKDKAAKRLSLEAEGAGEGAAAAGAELSALEEAFRKFAVHGDARASGREMHGKNWSKLCRDCQVIDGRSVTVTDVDIVFSKIKGKSCRTITFEQFKEALEELAKKRFKDKSAEEAVREVHKLIEGKAPIISGVTKAISSPTVSRLTDTSKFTGSHKERFDPSGRGKGRAGRVDLVDESGYVPGYKHAGTYDQKVQGGK
Protein: Bromo domain-containing protein (Q382J7)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MSQNRQLLYPREEMVSLVRSLDRPQENGLFSQDVLLQYPELAESYTKVCPNRCDLATAADRAAKGAYGYDVQLTTLKEDIRLMVNNCILFNGAEGAYADAARTFEKFAMGKIDAYISQKVGGRRLSSFRVASVSVPEKHSTGKRGRDGESRERGPEAVDNDSSRRQPGRGNGIATSEDDSNRRSAELIKLVDSLNRREDDGAFAVDVAEAYPELKSAYEAMCPLKMNLIIMKERAQNGYYLGQQHRRRRTGDDPTLYMGSSIAESLTSLRDDVELMVRNCVNFNAGVVEWERRAASFHHFAHKKIDDFVLRIDPSLRGTRTGVEVYVQEAKKMQQSQLKQKIEGSERSNRGDVGAPENVAQSISPPSHTTATPMNPPRKATIPGTARIPTLSAHVNVVNTVTPIVQPTALQPVFNTPSTLRRRLISDHLHRETLHARLIHRLENDKSGTNGVPEIDRSGDAPQMYEPALSCRAVLDAFIISVRGFHKAQRESQDFVNPFMYAQQEENLYCDYVTLIKQQLERLFLHIVLYNREKAEMYDWAAAKAAQMAVADASLLPTAPAVSSHVSCCWLDEAHLCYLVRFLQHLPQLLGLACAEVDTAKSDGTGNAQLYLTTVEQGVVGKIAKITEELLSFIARYEEKITASRQNSESLKEQAEAPAL
Protein: NLR family CARD domain-containing protein 4 (CARD, LRR, and NACHT-containing protein) (CED-4-like protein Clan) (Caspase recruitment domain-containing protein 12) (Ice protease-activating factor) (Ipaf) (Q9NPP4)
Organism: Homo sapiens (Human)
Function: Key component of inflammasomes that indirectly senses specific proteins from pathogenic bacteria and fungi and responds by assembling an inflammasome complex that promotes caspase-1 activation, cytokine production and macrophage pyroptosis. The NLRC4 inflammasome is activated as part of the innate immune response to a range of intracellular bacteria (By similarity).
Subcellular location: Cytoplasm {ECO:0000269|PubMed:11390368}. Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q3UP24}. Inflammasome {ECO:0000269|PubMed:15107016, ECO:0000269|PubMed:33420028}.
Interaction partners:
- Interferon-inducible protein AIM2
- NACHT, LRR and PYD domains-containing protein 1
- NACHT, LRR and PYD domains-containing protein 6
- Apoptosis-associated speck-like protein containing a CARD
- Baculoviral IAP repeat-containing protein 1
- NACHT, LRR and PYD domains-containing protein 3
- Caspase-1
- Pyrin
- NACHT, LRR and PYD domains-containing protein 12
- NACHT, LRR and PYD domains-containing protein 7
Sequence:
MNFIKDNSRALIQRMGMTVIKQITDDLFVWNVLNREEVNIICCEKVEQDAARGIIHMILKKGSESCNLFLKSLKEWNYPLFQDLNGQSLFHQTSEGDLDDLAQDLKDLYHTPSFLNFYPLGEDIDIIFNLKSTFTEPVLWRKDQHHHRVEQLTLNGLLQALQSPCIIEGESGKGKSTLLQRIAMLWGSGKCKALTKFKFVFFLRLSRAQGGLFETLCDQLLDIPGTIRKQTFMAMLLKLRQRVLFLLDGYNEFKPQNCPEIEALIKENHRFKNMVIVTTTTECLRHIRQFGALTAEVGDMTEDSAQALIREVLIKELAEGLLLQIQKSRCLRNLMKTPLFVVITCAIQMGESEFHSHTQTTLFHTFYDLLIQKNKHKHKGVAASDFIRSLDHCGDLALEGVFSHKFDFELQDVSSVNEDVLLTTGLLCKYTAQRFKPKYKFFHKSFQEYTAGRRLSSLLTSHEPEEVTKGNGYLQKMVSISDITSTYSSLLRYTCGSSVEATRAVMKHLAAVYQHGCLLGLSIAKRPLWRQESLQSVKNTTEQEILKAININSFVECGIHLYQESTSKSALSQEFEAFFQGKSLYINSGNIPDYLFDFFEHLPNCASALDFIKLDFYGGAMASWEKAAEDTGGIHMEEAPETYIPSRAVSLFFNWKQEFRTLEVTLRDFSKLNKQDIRYLGKIFSSATSLRLQIKRCAGVAGSLSLVLSTCKNIYSLMVEASPLTIEDERHITSVTNLKTLSIHDLQNQRLPGGLTDSLGNLKNLTKLIMDNIKMNEEDAIKLAEGLKNLKKMCLFHLTHLSDIGEGMDYIVKSLSSEPCDLEEIQLVSCCLSANAVKILAQNLHNLVKLSILDLSENYLEKDGNEALHELIDRMNVLEQLTALMLPWGCDVQGSLSSLLKHLEEVPQLVKLGLKNWRLTDTEIRILGAFFGKNPLKNFQQLNLAGNRVSSDGWLAFMGVFENLKQLVFFDFSTKEFLPDPALVRKLSQVLSKLTFLQEARLVGWQFDDDDLSVITGAFKLVTA
Protein: RPW8-like protein 4 (AtHR4) (Q9SCS6)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Probable disease resistance (R) protein.
Subcellular location: Membrane {ECO:0000255}; Single-pass membrane protein {ECO:0000255}.
Interaction partners:
- Exocyst complex component SEC8
- Exocyst complex component SEC6
- Exocyst complex component SEC5A
- Exocyst complex component SEC5B
- Exocyst complex component SEC3A
- Exocyst complex component SEC3B
- Exocyst complex component EXO84A
- Exocyst complex component EXO84C
- Exocyst complex component EXO84B
- Serine rich endogenous peptide 7
Sequence:
MPIAELAVIKTVGGPLIAAALGVGAQVIYDGFRKGKDTSIINRLGRTMESISPVRDRIGKLSNVEGKPFREVHESLTRLLEDAKSIIEKYWKLRWSRHVCRKYRYIKKLESIELELVRVAREIQVHQWTDIKEMKAIQVHQWTDIKEMKAIQVDQWTDIKEMKAIQVDQWIDIKEMKAIQVDQWTDIKEMKAQISEKHNK
Protein: E3 ubiquitin-protein ligase RING2 (EC 2.3.2.27) (RING finger protein 1B) (RING1b) (RING finger protein 2) (RING-type E3 ubiquitin transferase RING2) (Q9CQJ4)
Organism: Mus musculus (Mouse)
Function: E3 ubiquitin-protein ligase that mediates monoubiquitination of 'Lys-119' of histone H2A (H2AK119Ub), thereby playing a central role in histone code and gene regulation. H2AK119Ub gives a specific tag for epigenetic transcriptional repression and participates in X chromosome inactivation of female mammals. May be involved in the initiation of both imprinted and random X inactivation. Essential component of a Polycomb group (PcG) multiprotein PRC1-like complex, a complex class required to maintain the transcriptionally repressive state of many genes, including Hox genes, throughout development. PcG PRC1 complex acts via chromatin remodeling and modification of histones, rendering chromatin heritably changed in its expressibility. E3 ubiquitin-protein ligase activity is enhanced by BMI1/PCGF4. Acts as the main E3 ubiquitin ligase on histone H2A of the PRC1 complex, while RING1 may rather act as a modulator of RNF2/RING2 activity. Plays a role in the transcriptional repression of genes that are required for pluripotency in embryonic stem cells, thereby contributing to differentiation of the ectodermal and endodermal germ layers. Association with the chromosomal DNA is cell-cycle dependent. In resting B- and T-lymphocytes, interaction with AURKB leads to block its activity, thereby maintaining transcription in resting lymphocytes. Also acts as a negative regulator of autophagy by mediating ubiquitination of AMBRA1, leading to its subsequent degradation.
Subcellular location: Nucleus {ECO:0000269|PubMed:12183370, ECO:0000269|PubMed:22325148, ECO:0000269|PubMed:24980959, ECO:0000269|PubMed:28900001}. Cytoplasm {ECO:0000269|PubMed:24980959}. Chromosome {ECO:0000269|PubMed:12183370, ECO:0000269|PubMed:22325148}. Note=Enriched on inactive X chromosome (Xi) in female trophoblast stem (TS) cells as well as differentiating embryonic stem (ES) cells (PubMed:12183370). The enrichment on Xi is transient during TS and ES cell differentiation. The association with Xi is mitotically stable in non-differentiated TS cells (PubMed:12183370). Co-localizes with SAMD7 in nuclear polycomb bodies (PubMed:28900001). {ECO:0000269|PubMed:12183370, ECO:0000269|PubMed:28900001}.
Interaction partners:
- Lysine-specific demethylase 2B
- Polycomb group RING finger protein 1
- Polycomb group RING finger protein 5
- Polycomb protein Suz12
- Chromobox protein homolog 7
- Polycomb group RING finger protein 2
- Polycomb group RING finger protein 6
- Chromobox protein homolog 2
- RING1 and YY1-binding protein
- Polycomb complex protein BMI-1
Sequence:
MSQAVQTNGTQPLSKTWELSLYELQRTPQEAITDGLEIVVSPRSLHSELMCPICLDMLKNTMTTKECLHRFCADCIITALRSGNKECPTCRKKLVSKRSLRPDPNFDALISKIYPSRDEYEAHQERVLARINKHNNQQALSHSIEEGLKIQAMNRLQRGKKQQIENGSGAEDNGDSSHCSNASTHSNQEAGPSNKRTKTSDDSGLELDNNNAAVAIDPVMDGASEIELVFRPHPTLMEKDDSAQTRYIKTSGNATVDHLSKYLAVRLALEELRSKGESNQMNLDTASEKQYTIYIATASGQFTVLNGSFSLELVSEKYWKVNKPMELYYAPTKEHK
Protein: Interferon gamma related precursor (Interferon gamma-related) (Interferon gamma_1) (Q5TLE6)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Secreted {ECO:0000256|ARBA:ARBA00004613}.
Interaction partners:
- Interferon gamma 1.
- Interferon gamma receptor 1-like.
- Interferon gamma receptor 1
- Interferon phi 3.
- Interferon phi 2
- Interferon gamma receptor 2.
- Interleukin 10 receptor, beta.
- Lymphotoxin-alpha
- Inteferon phi 4
- Solute carrier family 35 member E3
Sequence:
MDSCLKMVLLCGLLWIASLQTTSAYRFRRSRSENPILNTNIEKLKTHYNTLAKDWVGKSVFVSHLDQLNSKPTCTCQAVLLEGMLSIYEDIFQDMMNKSDNKEVRDDLKKVIHEVKNLKHKYNEEHKLWRELQDIHSVKAKNGTIQERALNDFLKVYYRASTEKRHLHMS
Protein: Sodium channel protein type 2 subunit alpha (Voltage-gated sodium channel subunit alpha Nav1.2) (B1AWN6)
Organism: Mus musculus (Mouse)
Function: Mediates the voltage-dependent sodium ion permeability of excitable membranes. Assuming opened or closed conformations in response to the voltage difference across the membrane, the protein forms a sodium-selective channel through which Na(+) ions may pass in accordance with their electrochemical gradient. Implicated in the regulation of hippocampal replay occurring within sharp wave ripples (SPW-R) important for memory.
Subcellular location: Cell membrane {ECO:0000269|PubMed:10827969}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Sodium channel regulatory subunit beta-1
- Sodium channel regulatory subunit beta-2
- Sodium channel protein type 3 subunit alpha
- Sodium channel protein type 9 subunit alpha
- Sodium channel protein type 1 subunit alpha
- Sodium channel regulatory subunit beta-3
- Potassium/sodium hyperpolarization-activated cyclic nucleotide-gated channel 4
- Sodium channel regulatory subunit beta-4
- Ankyrin-3
- Calcium homeostasis modulator protein 1
Sequence:
MAQSVLVPPGPDSFRFFTRESLAAIEQRIAEEKAKRPKQERKDEDDENGPKPNSDLEAGKSLPFIYGDIPPEMVSEPLEDLDPYYINKKTFIVLNKGKAISRFSATSALYILTPFNPIRKLAIKILVHSLFNVLIMCTILTNCVFMTMSNPPDWTKNVEYTFTGIYTFESLIKILARGFCLEDFTFLRDPWNWLDFTVITFAYVTEFVNLGNVSALRTFRVLRALKTISVIPGLKTIVGALIQSVKKLSDVMILTVFCLSVFALIGLQLFMGNLRNKCLQWPPDNSTFEINITSFFNNSLDWNGTAFNRTMNMFNWDEYIEDKSHFYFLEGQNDALLCGNSSDAGQCPEGYICVKAGRNPNYGYTSFDTFSWAFLSLFRLMTQDFWENLYQLTLRAAGKTYMIFFVLVIFLGSFYLINLILAVVAMAYEEQNQATLEEAEQKEAEFQQMLEQLKKQQEEAQAAAAAASAESRDFSGAGGIGVFSESSSVASKLSSKSEKELKNRRKKKKQKEQAGEEEKEDAVRKSASEDSIRKKGFRFSLEGSRLTYEKRFSSPHQSLLSIRGSLFSPRRNSRASLFSFKGRVKDIGSENDFADDEHSTFEDNDSRRDSLFVPHRHGERRPSNVSQASRASRGIPTLPMNGKMHSAVDCNGVVSLVGGPSALTSPVGQLLPEGTTTETEIRKRRSSSYHVSMDLLEDPTSRQRAMSMASILTNTMEELEESRQKCPPCWYKFANMCLIWDCCKPWLKVKHVVNLVVMDPFVDLAITICIVLNTLFMAMEHYPMTEQFSSVLSVGNLVFTGIFTAEMFLKIIAMDPYYYFQEGWNIFDGFIVSLSLMELGLANVEGLSVLRSFRLLRVFKLAKSWPTLNMLIKIIGNSVGALGNLTLVLAIIVFIFAVVGMQLFGKSYKECVCKISNDCELPRWHMHDFFHSFLIVFRVLCGEWIETMWDCMEVAGQTMCLTVFMMVMVIGNLVVLNLFLALLLSSFSSDNLAATDDDNEMNNLQIAVGRMQKGIDFVKRKIREFIQKAFVRKQKALDEIKPLEDLNNKKDSCISNHTTIEIGKDLNYLKDGNGTTSGIGSSVEKYVVDESDYMSFINNPSLTVTVPIAVGESDFENLNTEEFSSESDMEESKEKLNATSSSEGSTVDIGAPAEGEQPEAEPEESLEPEACFTEDCVRKFKCCQISIEEGKGKLWWNLRKTCYKIVEHNWFETFIVFMILLSSGALAFEDIYIEQRKTIKTMLEYADKVFTYIFILEMLLKWVAYGFQMYFTNAWCWLDFLIVDVSLVSLTANALGYSELGAIKSLRTLRALRPLRALSRFEGMRVVVNALLGAIPSIMNVLLVCLIFWLIFSIMGVNLFAGKFYHCINYTTGEMFDVSVVNNYSECQALIESNQTARWKNVKVNFDNVGLGYLSLLQVATFKGWMDIMYAAVDSRNVELQPKYEDNLYMYLYFVIFIIFGSFFTLNLFIGVIIDNFNQQKKKFGGQDIFMTEEQKKYYNAMKKLGSKKPQKPIPRPANKFQGMVFDFVTKQVFDISIMILICLNMVTMMVETDDQSQEMTNILYWINLVFIVLFTGECVLKLISLRHYYFTIGWNIFDFVVVILSIVGMFLAELIEKYFVSPTLFRVIRLARIGRILRLIKGAKGIRTLLFALMMSLPALFNIGLLLFLVMFIYAIFGMSNFAYVKREVGIDDMFNFETFGNSMICLFQITTSAGWDGLLAPILNSGPPDCDPEKDHPGSSVKGDCGNPSVGIFFFVSYIIISFLVVVNMYIAVILENFSVATEESAEPLSEDDFEMFYEVWEKFDPDATQFIEFCKLSDFAAALDPPLLIAKPNKVQLIAMDLPMVSGDRIHCLDILFAFTKRVLGESGEMDALRIQMEERFMASNPSKVSYEPITTTLKRKQEEVSAIVIQRAYRRYLLKQKVKKVSSIYKKDKGKEDEGTPIKEDIITDKLNENSTPEKTDVTPSTTSPPSYDSVTKPEKEKFEKDKSEKEDKGKDIRESKK
Protein: Membrane-associated guanylate kinase, WW and PDZ domain-containing protein 1 (BAI1-associated protein 1) (BAP-1) (Membrane-associated guanylate kinase inverted 1) (MAGI-1) (Q6RHR9)
Organism: Mus musculus (Mouse)
Function: May play a role as scaffolding protein at cell-cell junctions. May regulate acid-induced ASIC3 currents by modulating its expression at the cell surface.
Subcellular location: [Isoform 2]: Cytoplasm {ECO:0000305}. Cell membrane {ECO:0000305}; Peripheral membrane protein {ECO:0000305}. Cell junction, tight junction {ECO:0000250}. Note=Localizes to epithelial cells tight junctions. {ECO:0000250}.; SUBCELLULAR LOCATION: [Isoform 3]: Cytoplasm {ECO:0000305}. Cell membrane {ECO:0000305}; Peripheral membrane protein {ECO:0000305}.; SUBCELLULAR LOCATION: [Isoform 1]: Nucleus {ECO:0000305}.
Interaction partners:
- Synaptopodin
- Alpha-actinin-4
- Predicted gene, 49948
- Rap guanine nucleotide exchange factor 2
- Catenin beta-1
- Phosphatidylinositol 3,4,5-trisphosphate 3-phosphatase and dual-specificity protein phosphatase PTEN
- Cell division control protein 42 homolog
- Membrane-associated guanylate kinase, WW and PDZ domain-containing protein 3
- Rap guanine nucleotide exchange factor
- Partitioning defective 3 homolog
Sequence:
MSKVIQKKNHWTGRVHECTVKRGPQGELGVTVLGGAEHGEFPYVGAVAAAEAAGLPGGGEGPKLAEGELLLEVQGVRVSGLPRYDVLGVIDSCKEAVTFKAVRQGGRLNKDLRHFLNQRFQKGSPDHELQQTIRDNLYRHAVPCTTRSPREGEVPGVDYSFLTVKEFLDLEQSGTLLEVGTYEGNYYGTPKPPSQPVSGKVITTDALHSLQSGSKQSTPKRTKSYNDMQNAGIVHPENEEEEDVPEMNSSFTADSGDQDEHTLQEATLPPVNSSILAAPITDPSQKFPQYLPLSAEDNLGPLPENWEMAYTENGEVYFIDHNTKTTSWLDPRCLNKQQKPLEECEDDEGVHTEELDSELELPAGWEKIEDPVYGVYYVDHINRKTQYENPVLEAKRKKQLEQQQQQQQPQPPQPEEWTEDHASVVPPVAPSHPPSNPEPARETPLQGKPFFTRNPSELKGKFIHTKLRKSSRGFGFTVVGGDEPDEFLQIKSLVLDGPAALDGKMETGDVIVSVNDTCVLGHTHAQVVKIFQSIPIGASVDLELCRGYPLPFDPDDPNTSLVTSVAILDKEPIIVNGQETYDSPASHSSKTGKVSSMKDARPSSPADVASNSSHGYPNDTVSLASSIATQPELITVHIVKGPMGFGFTIADSPGGGGQRVKQIVDSPRCRGLKEGDLIVEVNKKNVQALTHNQVVDMLIECPKGSEVTLLVQRGGLPVPKKSPKSQPLERKDSQNSSQHSVSSHRSLHTASPSHGIQVLPEYLPADAPAPDQTDSSGQKKPDPFKIWAQSRSMYENRPMSPSPASGLSKGERDREINSTNFGECQIPDYQEQDIFLWRKETGFGFRILGGNEPGEPIYIGHIVPLGAADTDGRLRSGDELICVDGTPVIGKSHQLVVQLMQQAAKQGHVNLTVRRKVVFAVPKAENEVPSPASSHHSSNQPASLTEEKRTPQGSQNSLNTVSSGSGSTSGIGSGGGGGSGVVSAVLQPYDVEIRRGENEGFGFVIVSSVSRPEAGTTFGRIIEGSPADRCGKLKVGDRILAVNGCSITNKSHSDIVNLIKEAGNTVTLRIIPGDESSNATLLTNAEKIATITTTHAPSQQGTQETRTTTKPKQDSQFEFKGPQAAQEQDFYTVELERGAKGFGFSLRGGREYNMDLYVLRLAEDGPAERCGKMRIGDEILEINGETTKNMKHSRAIELIKNGGRRVRLFLRRGDGSVPEYDPSSDRNGPSTGAQGVPEVRPGPPDHRPHPALESSYPPELHKSSQHAEKRAHAKDPKGNREHSKQPNEHHTWNGTSRKQDSGACRPKDRPPDAWREAQPERTATNGSKRRSPEKRREGTRSADNTLERREKHEKRREISPERKRERSPTRRKDSSPSRRRRSLERLLDQRRSPERRRGGSPERRAKSTDRRRARSPERRRERSLDKRNRDDKVGHREREEAGLKLEAGRSPRNPPEQRRRPYKECSTDLSI
Protein: Tapas, isoform B (Q0E910)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
Interaction partners:
Sequence:
MEKQEVLEYVAKVVRALITSAKPPVTLRSIVADYMEIEGEPIPFRRLGYSNDQELLKDSNQFNFHQSGNQVFITAKYNANTEHIVRMVRQQKTSKSTSLSKPTPIAQKPKPIAQKHTHGNKYHYQQRNKQPNHQPDQEIGRAAKCENQAIAEHKQDLTGIITQELFESFNNIQGPFSENLQVFNKNPEYITRRKKELKKEDDLDRGQITKEVAREKQKEKETRDRAVTETIFVTIENKKAPVMNGHGPRHVKVANGQDKHNDGKPPLRAILGNSASQRQQDTSTVYHSPESSFKRPRHPRVMYPGHQRTTGVSVNHRLKVTPQSDAPTPAVAPITPPASPEYAQTTTAAKATYKEDIHGGQGETGNVVTNPKVKVPLKFDPSLDPVSTLNFYCAANDFEKPAYNIFNKLRNLHCSVQIAGDVYSSYPQEFTDKETAYQRTAQIAIQRIMHAQSHQKLSACTFSDVEFIDGLYKELLKHPHGILGHKLEDWYGSTFRQHLPSHWYDLIVKSNKIRVEHGIDPRIILFANDPGSSEPDRTSITTLPQMVLPWQSSEGGSHDWNMFISFCDSTKIVWARMIDQIANFEELTKHIGRQMESPHFRQKVSKPYAQEVYLVEMPDGWNRVRAISVDEETRSGRYHFIDFGDVAMFHSEDLFHCPPQFLALPAQAVCLSMYALDKFEDHPHALQVLTKELDGQTVVAHVLTTEKQFLELGGSAQGVVENGKRRACLVATLYDTSTAEDIHLNDLVAKRITKCTPAPSLSDEKKIGKTTPILVSHINDDGDLMVLLRNDDLKFVERSIAQTVADLGEQDRVSYSDLLHDRHIFVCDETVDGVKQWFRGRLVTRPLNPDEESFDVYYVDDGRQRKAHISNIYRLEANNRALATFPPQAIPVRLHDVPEIGGHMLHRLRGLIPWRTEALLKVVAMDGGKPLVNVFIREDPESMYMCVNIGLRLELEMASSIHPEKYDHTLLSSNVQLPRRGSFSSVFSNQSSSSDLVATTPPVTPEKKPSARSTGSTFSSLMLKDYEAIPAVGAYFEVRVALSVNPGHFAVQPYKYYNQLQTLMKNLQEHCQKTAAKGVQPSQLAIGEAYAAPDSEGVYHRVSIHKIYDEIIHVRFVDVGDDGVIACDQLKTLNPELRKLPKMALPAQLYGIQLTDVVWSKENCVRFRELSLGQKFIGIVRRMTKQKDGGRALCLELVDTSTPKDIKLHEILINEKHAQPAT
Protein: SUppressor of Tau pathology (H2KYJ0)
Organism: Caenorhabditis elegans
Interaction partners:
Sequence:
MSGASKKVSEEELQKQYADYRAQFEQWKENNKGSIGTEAYNSYVQQFEQWEKEVEARTSQQQKHRKAAAVDKEAEAAAAAYAQSQEAYMAHHLRGMEQTEMQKRAAAAAQLQQQQMMQNMMMQRPPQHQQPPPQDVMFGAVGRVAQGAPAAAPPPTQQPPPQLWGNNKPIYDARDPLFAKWGERAASAHCKPETEQQINPVACWLLLDALREKKMVLAPHSNTCPPPQIGGHQI
Protein: Rhomboid domain-containing protein 2 (Q6NTF9)
Organism: Homo sapiens (Human)
Subcellular location: Golgi apparatus, cis-Golgi network membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}.
Interaction partners:
Sequence:
MAASGPGCRSWCLCPEVPSATFFTALLSLLVSGPRLFLLQQPLAPSGLTLKSEALRNWQVYRLVTYIFVYENPISLLCGAIIIWRFAGNFERTVGTVRHCFFTVIFAIFSAIIFLSFEAVSSLSKLGEVEDARGFTPVAFAMLGVTTVRSRMRRALVFGMVVPSVLVPWLLLGASWLIPQTSFLSNVCGLSIGLAYGLTYCYSIDLSERVALKLDQTFPFSLMRRISVFKYVSGSSAERRAAQSRKLNPVPGSYPTQSCHPHLSPSHPVSQTQHASGQKLASWPSCTPGHMPTLPPYQPASGLCYVQNHFGPNPTSSSVYPASAGTSLGIQPPTPVNSPGTVYSGALGTPGAAGSKESSRVPMP
Protein: Lon protease homolog, mitochondrial (EC 3.4.21.53) (Lon protease-like protein) (LONP) (Mitochondrial ATP-dependent protease Lon) (Serine protease 15) (K7EJE8)
Organism: Homo sapiens (Human)
Subcellular location: Mitochondrion matrix {ECO:0000256|ARBA:ARBA00004305, ECO:0000256|HAMAP-Rule:MF_03120}.
Interaction partners:
Sequence:
MTIPDVFPHLPLIAITRNPVFPRFIKIIEVKNKKLVELLRRKVRLAQPYVGVFLKRDDSNESDVVESLDEIYHTGTFAQIHEMQDLGDKLRMIVMGHRRVHISRQLEVEPEEPEAENKHKPRRKSKRGKKEAEDELSARHPAELAMEPTPELPAEVLMVEALTAEIVKTIRDIIALNPLYRESVLQMMQAGQRVVDNPIYLSDMGAALTGAESHELQDVLEETNIPKRLYKALSLLKKEFELSKLQQRLGREVEEKIKQTHRKYLLQEQLKIIKKELGLEKDDKDAIEEKFRERLKELVVPKHVMDVVDEELSKLGLLDNHSSEFNVTRNYLDWLTSIPWGKYSNENLDLARAQAVLEEDHYGMEDVKKRILEFIAVSQLRGSTQGKILCFYGPPGVGKTSIARSIARALNREYFRFSVGGMTDVAEIKGHRRTYVGAMPGKIIQCLKKTKTENPLILIDEVDKIGRGYQGDPSSALLELLDPEQNANFLDHYLDVPVDLSKVLFICTANVTDTIPEPLRDRMEMINVSGYVAQEKLAIAERYLVPQARALCGLDESKAKLSSDVLTLLIKQYCRESGVRNLQKQVEKVLRKSAYKIVSGEAESVEVTPENLQDFVGKPVFTVERMYDVTPPGVVMGLAWTAMGGSTLFVETSLRRPQDKDAKGDKDGSLEVTGQLGEVMKESARIAYTFARAFLMQHAPANDYLVTSHIHLHVPEGATPKDGPSAGCTIVTALLSLAMGRPVRQNLAMTGEVSLTGKILPVGGIKEKTIAAKRAGVTCIVLPAENKKDFYDLAAFITEGLEVHFVEHYREIFDIAFPDEQAEALAVER
Protein: Germacrene A hydroxylase (EC 1.14.14.95) (Germacrene A oxidase) (BsGAO) (D5JBX1)
Organism: Barnadesia spinosa (Spiny barnadesia)
Function: Involved in the biosynthesis of germacrene-derived sesquiterpene lactones. Catalyzes three consecutive oxidations of germacrene A to produce germacrene A acid. Could also catalyze the three-step oxidation of non-natural substrate amorphadiene to artemisinic acid.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:D5JBW8}; Single-pass type II membrane protein {ECO:0000250|UniProtKB:D5JBW8}.
Interaction partners:
Sequence:
MELTLTTSLGLAVFVFILFKLLTGSKSTKNSLPEAWRLPIIGHMHHLVGTLPHRGVTDMARKYGSLMHLQLGEVSTIVVSSPRWAKEVLTTYDITFANRPETLTGEIVAYHNTDIVLSPYGEYWRQLRKLCTLELLSAKKVKSFQSLREEECWNLVKEVRSSGSGSPVDLSESIFKLIATILSRAAFGKGIKDQREFTEIVKEILRLTGGFDVADIFPSKKILHHLSGKRAKLTNIHNKLDSLINNIVSEHPGSRTSSSQESLLDVLLRLKDSAELPLTSDNVKAVILDMFGAGTDTSSATIEWAISELIRCPRAMEKVQTELRQALNGKERIQEEDIQELSYLKLVIKETLRLHPPLPLVMPRECREPCVLAGYEIPTKTKLIVNVFAINRDPEYWKDAETFMPERFENSPINIMGSEYEYLPFGAGRRMCPGAALGLANVELPLAHILYYFNWKLPNGARLDELDMSECFGATVQRKSELLLVPTAYKTANNSA
Protein: UDP-sulfoquinovose synthase (Q763T6)
Organism: Chlamydomonas reinhardtii (Chlamydomonas smithii)
Interaction partners:
- Uncharacterized protein
- UTP--glucose-1-phosphate uridylyltransferase
- UDP-glucose 6-dehydrogenase
- UDP-glucose 6-dehydrogenase
- UDP-glucose 6-dehydrogenase
- Protein BUNDLE SHEATH DEFECTIVE 2, chloroplastic
- UDP-glucose 4-epimerase
- Uncharacterized protein
- Galactokinase
- Uncharacterized protein
Sequence:
MQCSTMQQQKLAGRREAKAAAQKACAGVRVAGASARVPVSTVRQATSSVRAASRATSVKVQATATVEKATAPAGSLSSNGAGTRVMIIGGDGYCGWATALHLSARGYEVCIVDNLCRRQFDLQLGLDTLTPIATIHDRVRRWGEVSGKHISLQIGDICDWEFLSQAFTSFKPNHVVHFGEQRSAPYSMIDRQKAVFTQHNNVIGTINVLFAIKELQPDCHMVKLGTMGEYGTPNIDIEEGYITINHNGRTDTLPYPKQGNSFYHLSKIHDSTNMLFTCKAWKIAATDLNQGVVYGVRTDETMADPLLLNRYDYDGIFGTALNRFVVQAAVGHPLTVYGKGGQTRGFLDIRDTVRCIQLAIDNPAPKGEMRVYNQFTEQFSVNQLAEIVEREGKKLGLNVEVTKVPNPRVELEEHYYNAKCTKLRDLGLQPHLLADSMIDSLLEFAVTYKDRVRHELIKPAVDWRKTGVKVNTMGAAVAR
Protein: Bacteriorhodopsin (B0R5N9)
Organism: Halobacterium salinarum (strain ATCC 29341 / DSM 671 / R1)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004651}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}.
Interaction partners:
Sequence:
MLELLPTAVEGVSQAQITGRPEWIWLALGTALMGLGTLYFLVKGMGVSDPDAKKFYAITTLVPAIAFTMYLSMLLGYGLTMVPFGGEQNPIYWARYADWLFTTPLLLLDLALLVDADQGTILALVGADGIMIGTGLVGALTKVYSYRFVWWAISTAAMLYILYVLFFGFTSKAESMRPEVASTFKVLRNVTVVLWSAYPVVWLIGSEGAGIVPLNIETLLFMVLDVSAKVGFGLILLRSRAIFGEAEAPEPSAGDGAAATSD