wanglab/gogpt-training-data huggingface dataset:
Protein: Pleiotropic drug resistance protein 1 (PaPDR1) (ABC transporter G family PDR1) (Strigolactone transporter) (H6WS93)
Organism: Petunia axillaris (Large white petunia) (Nicotiana axillaris)
Function: Cellular strigolactone (SL) transporter required for the exudation of SL from the root to the soil. The presence of SL in the vicinity of the roots is required for development of symbiotic interactions with arbuscular mycorrhizal fungi (AMF). Transports SL in the above ground tissues and is required for the control of shoot branching. SL regulates plant shoot architecture by inhibiting the outgrowth of axillary buds. Involved in the regulation of shootward and outward directional strigolactone transport in roots. Due to its polar localization in root cells, mediates directional shootward strigolactone transport, as well as localized outward directional transport for exudation to the soil.
Subcellular location: Cell membrane {ECO:0000269|PubMed:22398443, ECO:0000269|PubMed:25683808, ECO:0000269|PubMed:27040840}; Multi-pass membrane protein {ECO:0000255}. Note=Localizes to the plasma membrane (PubMed:22398443, PubMed:25683808, PubMed:27040840). Exhibits asymmetric localization in different root tissues (PubMed:25683808). In root tips, localizes at the apical membrane of hypodermal cells (PubMed:25683808). In the hypodermal passage cells localizes in the outer-lateral membrane (PubMed:25683808). {ECO:0000269|PubMed:22398443, ECO:0000269|PubMed:25683808, ECO:0000269|PubMed:27040840}.
Interaction partners:
Sequence:
MEGGEELFRVSSARLSSSNVWRNSAMDVFSRSSREADDEEALKWAALEKLPTYLRIRRGILTEEEGQSREVDITKLDLVERRNLLERLIKITDEDNEKFLLKLKERIDRVGLDLPTIEVRFEHLSVDAEARVGSRALPTVFNFTVNILEDFLNYLHILPNRKQPLPILHDVSGIIKPGRMTLLLGPPSSGKTTLLLALAGKLDKDLKVSGRVTYNGHDMNEFVAQRSSAYISQYDLHIGEMTVRETLAFSARCQGVGAKYEILAELSRREKEANIKPDPDVDIFMKAAWNEGQEANVVTDYTLKILGLEICADTIVGDEMIPGISGGQRKRLTTGEMMVGPARALFMDEISTGLDSSTTYQIVNSIRQSIHILQGTAVISLLQPAPETYDLFDDIILLSDGQIVYQGPRENVLEFFEYMGFICPERKGVADFLQEVTSRKDQEQYWARREESYKFITVREFSEAFQAFHIGRKLGDELAVPFDKSKSHPAALTTKRYGVSKKELLKACTAREYLLMKRNSFVYIFKMIQLTLMASITMTLFLRTEMHRNTTIDGAVFLGALFYALIMIMFNGFSELALSIMKLPSFYKHRDLLFFPPWAYALPTWILKIPITLVEVAIWVCMTYYVIGFEADVGRFFKQLLLLICVNQMASGLFRLMGALGRNIIVANTFGSFVLLTVLVMGGFVLSRDDVKKWWIWGYWISPMMYAQNAIAVNEFLGKSWAHVPPNSTSTETLGVSFLKSRGIFPDARWYWIGAGALIGYVFLFNFLFAVALAYLNPFGKPQAVLSEETVAERNASKRGEVIELSSLGKSSSEKGNDVRRSASSRSMSSRVGSITAADLSKRRGMILPFEPLSITFDDIRYAVDMPQEMKAQGFTEDRLELLRGVSGAFRPGVLTALMGVSGAGKTTLMDVLAGRKTGGYIDGTISISGYPKQQETFARIAGYCEQTDIHSPHVTVYESLQFSAWLRLPREVDTATRKMFIEEVMELIELIPLRDALVGLPGVNGLSTEQRKRLTVAVELVANPSIIFMDEPTSGLDARAAAIVMRTVRNTVDTGRTVVCTIHQPSIDIFDAFDELLLLKRGGEEIYVGPLGRQSSHLIKYFEGIDGVPKIKDGYNPATWMLEITSVAQEGALGNDFTELYKNSELYRRNKALIKELSVPASCSKDLYFPTKYSQSFFTQCMACFWKQHWSYWRNPPYTAVRIMFTFFIALMFGTIFWDLGSRRERQQDLLNAIGSMYIAVLFLGVQNATTVQPVIAIERTVFYRERAAGMYSAMPYAFGQVMIELPYLFLQTIIYGVIVYAMIGFEWTVAKFFWYLFFMYFTLLYFTLYGMMTVAVTPNHSIAAIISSAFYAVWNLFCGFIVPKTRMPVWWRWYYYICPISWTLYGLIASQFGDIQDRLDTNETVEQFIENFFDFKHDFVGYVALILVGISVLFLFIFAFSIKTFNFQKR
Protein: Prostaglandin E synthase 2 (EC 5.3.99.3) (GATE-binding factor 1) (GBF-1) (Microsomal prostaglandin E synthase 2) (mPGES-2) [Cleaved into: Prostaglandin E synthase 2 truncated form] (Q8BWM0)
Organism: Mus musculus (Mouse)
Function: Isomerase that catalyzes the conversion of PGH2 into the more stable prostaglandin E2 (PGE2) (in vitro). The biological function and the GSH-dependent property of PTGES2 is still under debate (By similarity). In vivo, PTGES2 could form a complex with GSH and heme and would not participate in PGE2 synthesis but would catalyze the degradation of prostaglandin E2 H2 (PGH2) to 12(S)-hydroxy-5(Z),8(E),10(E)-heptadecatrienoic acid (HHT) and malondialdehyde (MDA) (By similarity). May also have transactivation activity toward IFN-gamma (IFNG), possibly via an interaction with CEBPB; however, the relevance of transcription activation activity remains unclear.
Subcellular location: Golgi apparatus membrane {ECO:0000250|UniProtKB:Q9H7Z7}; Single-pass membrane protein {ECO:0000250|UniProtKB:Q9H7Z7}. Nucleus {ECO:0000269|PubMed:12050152}. Note=According to PubMed:12050152, some fraction may be nuclear. {ECO:0000269|PubMed:12050152}.; SUBCELLULAR LOCATION: [Prostaglandin E synthase 2 truncated form]: Cytoplasm {ECO:0000250|UniProtKB:Q9H7Z7}. Note=Synthesized as a Golgi membrane-bound protein, which is further cleaved into the predominant soluble truncated form. {ECO:0000250|UniProtKB:Q9H7Z7}.
Interaction partners:
- Prostaglandin E synthase 3
- Prostaglandin E synthase
- Prostaglandin G/H synthase 1
- Prostaglandin G/H synthase 2
- Prostacyclin synthase
- Thromboxane-A synthase
- Prostaglandin-H2 D-isomerase
- Hematopoietic prostaglandin D synthase
- Carbonyl reductase 1])
- Prostamide/prostaglandin F synthase
Sequence:
MAQAARLSWVLVSSRCALTEGLLTRPWQPLSAQSRAGFTRVAAGSRGAAVRKGSPRLLGAAALALGGALGLYHTVRWHQRSQDLRAERSAAQLPLSNSLQLTLYQYKTCPFCSKVRAFLDFHSLPYQVVEVNPVRRTEIKFSSYRKVPILVAQEGDSLQQLNDSSVIISALKTYLVSGQPLEEVITYYPPMKAMNDQGKEVTEFCNKYWLMLDEKEAQQMYGGKEARTEEMKWRQWADDWLVHLISPNVYRTPAEALASFDYIVREGKFGAVEAAMAKYVGAAAMYLISKRLKSRHHLQDDVRVDLYEAANKWVTAVGKDRPFMGGQKPNLADLAVYGVLRVMEGLEAFDDLMRHSHIQPWYLRMERAIEEAPSVHHVNPSCKD
Protein: Aminodeoxychorismate/anthranilate synthase component 2 (ADC synthase) (ADCS) (EC 2.6.1.85) (EC 4.1.3.27) (4-amino-4-deoxychorismate synthase component 2) (Aminodeoxychorismate synthase, glutamine amidotransferase component) (P28819)
Organism: Bacillus subtilis (strain 168)
Function: Part of a heterodimeric complex that catalyzes the two-step biosynthesis of 4-amino-4-deoxychorismate (ADC), a precursor of p-aminobenzoate (PABA) and tetrahydrofolate. In the first step, a glutamine amidotransferase (PabA) generates ammonia as a substrate that, along with chorismate, is used in the second step, catalyzed by aminodeoxychorismate synthase (PabB) to produce ADC. PabA converts glutamine into glutamate only in the presence of stoichiometric amounts of PabB. Also involved in the biosynthesis of anthranilate (By similarity). Complements a glutamine amidotransferase-negative mutant.
Interaction partners:
- Aminodeoxychorismate synthase component 1
- Anthranilate synthase component 1
- Anthranilate phosphoribosyltransferase
- Aminodeoxychorismate lyase
- Tryptophan synthase alpha chain
- Tryptophan synthase beta chain
- N-
- Dihydropteroate synthase
- Protein AroA
- Uncharacterized HTH-type transcriptional regulator YazB
Sequence:
MILMIDNYDSFTYNLVQYLGELGEELVVKRNDSITIDEIEELSPDFLMISPGPCSPDEAGISLEAIKHFAGKIPIFGVCLGHQSIAQVFGGDVVRAERLMHGKTSDIEHDGKTIFEGLKNPLVATRYHSLIVKPETLPSCFTVTAQTKEGEIMAIRHNDLPIEGVQFHPESIMTSFGKEMLRNFIETYRKEVIA
Protein: FAD-linked oxidoreductase patO (EC 1.-.-.-) (Patulin biosynthesis cluster protein O) (A0A075TR33)
Organism: Penicillium expansum (Blue mold rot fungus)
Function: FAD-linked oxidoreductase; part of the gene cluster that mediates the biosynthesis of patulin, an acetate-derived tetraketide mycotoxin produced by several fungal species that shows antimicrobial properties against several bacteria. PatO acts with patJ in the vacuole to convert gentisyl alcohol to isoepoxydon. The pathway begins with the synthesis of 6-methylsalicylic acid by the polyketide synthase (PKS) patK via condensation of acetate and malonate units. The 6-methylsalicylic acid decarboxylase patG then catalyzes the decarboxylation of 6-methylsalicylic acid to yield m-cresol (also known as 3-methylphenol). These first reactions occur in the cytosol. The intermediate m-cresol is then transported into the endoplasmic reticulum where the cytochrome P450 monooxygenase patH converts it to m-hydroxybenzyl alcohol, which is further converted to gentisyl alcohol by the cytochrome P450 monooxygenase patI. The oxidoreductases patJ and patO further convert gentisyl alcohol to isoepoxydon in the vacuole. PatN catalyzes then the transformation of isoepoxydon into phyllostine. The cluster protein patF is responsible for the conversion from phyllostine to neopatulin whereas the alcohol dehydrogenase patD converts neopatulin to E-ascladiol. The steps between isoepoxydon and E-ascladiol occur in the cytosol, and E-ascladiol is probably secreted to the extracellular space by one of the cluster-specific transporters patC or patM. Finally, the secreted patulin synthase patE catalyzes the conversion of E-ascladiol to patulin (Probable).
Subcellular location: Vacuole lumen {ECO:0000269|PubMed:30680886}.
Interaction partners:
Sequence:
MRLHQSPPRLLVCILSVLQVSAGLSSNCRCMPGDSCWPSLNDWARFNTSIGGRLVDTQPLGQPCHDPFYTASECNELKQQWTHPELHDASSSSIMSAAVANETCDAFTPRSKPCTLGAMVRYAVNASSPDDFVQTIRFSQERNIRLVIRNTGHDYAGKSTGAGALSIWTHSLKEIDFLNYTSAHYTGPAVRMTAGIQGTDINPAAHKKGLVIVGGECATVGPVGGFTQGGGHSALSSRFGLAADQVLEWEVVDGMGRLLTASPTQNPDLYWALSGGGGGTFGVVYAVTVKTFPDFAVTGVVLQFENIDPSSNRFFEAVGHYHRHLPTYTSAGGMAIAQITNSSFLLTPLTLPAYTAAATKKLLGPFLQDLHQLNISYTLNVTESASYFQHYMKLIEPNPTQLVQNAQYGGRLLPLDLIERNNSQLTDAVQKLTADGVTFVGIGLNVSSSVTGDIWNSVLPGWRTAAMTVILTTSWPLGANLTKMKILADKMTTKWVPILTALSPESGCYMSEADPQQPDWKQTFYGRNYDSLYAIKTKYDPLQTFYATTAVGSEDWQVEAGGRLCQATRKN
Protein: Diencephalon/mesencephalon homeobox protein 1-A (Paired homeobox protein 1) (Q8JI10)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Function: Required for eye and tectum development. May act as a transcriptional repressor.
Subcellular location: Nucleus {ECO:0000250|UniProtKB:O35137, ECO:0000255|PROSITE-ProRule:PRU00108, ECO:0000255|PROSITE-ProRule:PRU00138}.
Interaction partners:
Sequence:
MQHYGVNGYSLHAMNSLSAMYNLHQQAAQQAQHAPDYRPSVHALTLAERLAGCTFQDIILEARYGSQHRKQRRSRTAFTAQQLEALEKTFQKTHYPDVVMRERLAMCTNLPEARVQVWFKNRRAKFRKKQRSLQKEQLQKQKDVSTDGALAASDKDEAPSTLNLENQPPSSTSSSSSMEAEAAPHALGSELSVELNVTSAEQSGSESATEDNATDKEEEIKQHREDLKVEKEPAPGNLSPLCKRLSPKPDSPLGSPAISSSSSGVTGGISQSHSYSSSPLSLFRLQEQFRQHMAATNNLVHYPSFDMATPSSIPYLGMNVNMPAPLGSLPCQSYYQSLSHHAQQVWNSPLLQASGGLPSHNSKTTSIENLRLRAKQHAASLGLDTLPN
Protein: Ribonuclease H (RNase H) (EC 3.1.26.4) (P13319)
Organism: Enterobacteria phage T4 (Bacteriophage T4)
Function: Plays essential roles in DNA replication by removing the RNA primers from lagging strand fragments. Exhibits 5'to 3' exonuclease activity on either RNA/DNA or DNA/DNA duplexes and endonuclease activity on either flap or fork DNA structures.
Interaction partners:
Sequence:
MDLEMMLDEDYKEGICLIDFSQIALSTALVNFPDKEKINLSMVRHLILNSIKFNVKKAKTLGYTKIVLCIDNAKSGYWRRDFAYYYKKNRGKAREESTWDWEGYFESSHKVIDELKAYMPYIVMDIDKYEADDHIAVLVKKFSLEGHKILIISSDGDFTQLHKYPNVKQWSPMHKKWVKIKSGSAEIDCMTKILKGDKKDNVASVKVRSDFWFTRVEGERTPSMKTSIVEAIANDREQAKVLLTESEYNRYKENLVLIDFDYIPDNIASNIVNYYNSYKLPPRGKIYSYFVKAGLSKLTNSINEF
Protein: Glycosyl hydrolase family protein 43 (Q9M2X0)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- Assimilatory sulfite reductase
- Ferredoxin--nitrite reductase, chloroplastic
- Anamorsin homolog
- Beta-galactosidase 17
Sequence:
MRVMKNKHNKKATFLRCSPFGLVSTVVGCVFMIHLTMLYSRSYSVDLDLSPQLLIHHPIVRELERVEEENIHMPPPRKRSPRAIKRKPKTPTTLVEEFLDENSQIRHLFFPDMKSAFGPTKEDTNDTSHYYFPGRIWTDTEGNPIQAHGGGILFDDISKVYYWYGEYKDGPTYLSHKKGAARVDIIGVGCYSSKDLWTWKNEGVVLAAEETDETHDLHKSNVLERPKVIYNSDTGKYVMWMHIDDANYTKASVGVAISDNPTGPFDYLYSRSPHGFDSRDMTVYKDDDNVAYLIYSSEDNSVLHIGPLTENYLDVKPVMKRIMVGQHREAPAIFKHQNTYYMITSGCTGWAPNEALAHAAESIMGPWETLGNPCVGGNSIFRSTTFFAQSTFVIPLPGVPGVFIFMADRWNPADLRDSRYLWLPLIVGGPADRPLEYSFGFPMWSRVSVYWHRQWRLPSAREKKIA
Protein: Sin3A-associated protein 130, isoform F (M9PI47)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MSAPSEGGAGGGPVGGGSTATAPSAHPAVAAKITHVKSDGGGGISIAGTPILSGGTIKVASANQVQQTSLGGTPIALNAGQATTAASIRAIGAGGQSTQVRVVMPMIKQLENVTATGRTQITAIPAAPARSGANASITVTRPVTQATYLPRASVTATQMGGVGVGVGQRLVTPLRATSSATVTPTAPTVLSSTGGFVRGATASVSRSGVALTSQPSSAVISSSNSGAWMQSQGQVQLIRTIHQPRQRIITTSAGVSNASVVTTTPVQAPTALSVSAGQPLATQQATGPGGGPQAYVATVLPQRQHQATLVYSSNVSAPNASQNPGQQFNPRFAVATPTGGVTTTTPGGTTVTPRQVRPIPLGKSFPTAKLNTTSISIRAPSIPQLNTSVTASPTAVSVSGGATVAPGRGPGAGGTALTATNLPTTRIIQLQQPATGTTQQIIGSGARLAGNVMLQPFLMSTTAAAKMGIRPPVTMTAKVQPSLTITQLNPIGKLSAGGGSGGQTMGPQGVASIQAVPVPNVSASVVNSSSVTGATSAAGGATVLPLTISGRGAGVGPGGNILTGTLTPIKNASGITLGKMMMAPASSAPGADGSSTSGATVTGFQRTWNPVVASQSQLMKIDEKGSAATIYYESMPASASTGVLSLTTTTVTQSTQAQAQLVSSAGGSLSVSSLPFASHATAGAGSGGGGSQATFTVLPSGAGGTATRTIGHQQLIIPAGPNSAPPQHMVIPLHTSVKVTTGAGNPQQATASGALVSSFMRKRDAEGSPIRAAKNLGPTLLSMASNNSGQNMPPAPGTTFNIQPVSVTVPQSVGSGLTVEALAKKERERVTHGVASSAASVPATVGPVNSTRNSRADSPASSDGSTTVSANSSPGVDQQLQDRIGDQPATGGAGGRDNSTHFNPINENLGHSSLGARSGSSAFVDVQAPTPQQQQPQQVPHLVGSTQMQQGTRMNGTGNSSSSSYDCSSRKKPRRSTNDSQHSTQSQASLSLPPPSSEPTPPAGASYMQKHNNGGLLVTAATPGVAPNSAPGDANHRNSTPAVAGNKENANPVDFVIRRPRNCALLNTYKPTHKLANNHFHRYTDVKPREERRATVIDLANQPNVQGKINGWKIYHLRSQMEDLNESEVFSLGRLETMLQDLEKDKEKHSEIERVTELLKGNIQRSKIITDGINEAQNQLMKIFEHKPHVSNIITRCASKRNFKKREKI
Protein: Nuclear egress protein 1 (P89454)
Organism: Human herpesvirus 2 (strain HG52) (HHV-2) (Human herpes simplex virus 2)
Function: Plays an essential role in virion nuclear egress, the first step of virion release from infected cell. Within the host nucleus, NEC1 interacts with the newly formed capsid through the vertexes and directs it to the inner nuclear membrane by associating with NEC2. Induces the budding of the capsid at the inner nuclear membrane as well as its envelopment into the perinuclear space. There, the NEC1/NEC2 complex promotes the fusion of the enveloped capsid with the outer nuclear membrane and the subsequent release of the viral capsid into the cytoplasm where it will reach the secondary budding sites in the host Golgi or trans-Golgi network.
Subcellular location: Host nucleus inner membrane {ECO:0000255|HAMAP-Rule:MF_04023, ECO:0000269|PubMed:10550666, ECO:0000269|PubMed:11369887}. Note=Remains attached to the nucleus inner membrane through interaction with NEC2. {ECO:0000255|HAMAP-Rule:MF_04023}.
Interaction partners:
Sequence:
MYDIAPRRSGSRPGPGRDKTRRRSRFSAAGNPGVERRASRKSLPSHARRLELCLHERRRYRGFFAALAQTPSEEIAIVRSLSVPLVKTTPVSLPFSLDQTVADNCLTLSGMGYYLGIGGCCPACSAGDGRLATVSREALILAFVQQINTIFEHRTFLASLVVLADRHSTPLQDLLADTLGQPELFFVHTILRGGGACDPRFLFYPDPTYGGHMLYVIFPGTSAHLHYRLIDRMLTACPGYRFAAHVWQSTFVLVVRRNAEKPADAEIPTVSAADIYCKMRDISFDGGLMLEYQRLYATFDEFPPP
Protein: Transcription factor WRKY1 (Q6R8H1)
Organism: Gossypium arboreum (Tree cotton) (Gossypium nanking)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MEPAWVDTTLDLNINPCFRTNKAMKREFEGDVAESAPVKYESGVLVEELNRVSAENKKLTEMLTVLCEQYYSLQHQFMELVNKNPEIETTAAATTSSSKKRKAEWEDYGANMIGFSGNTETSSSDDGSPKTPKDCIKPKVSRVQVRTNPSDNSLIVRDGYQWRKYGQKVTRDNPCPRAYFKCSFAPSCPVKKKVQRSAEDPSILVATYEGEHNHHEHHRSPPAEISLNSNNNTPSSNTGSGPVSSAPTKALASTVTLELLQPAGLGGDETERAALQIDAPAIQQILVHQMAASLSRDPNFTAALAAAISGRAV
Protein: At5g22020 (Calcium-dependent phosphotriesterase superfamily protein) (Putative strictosidine synthase-like) (Q9C586)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Vacuole {ECO:0000256|ARBA:ARBA00004116}.
Interaction partners:
Sequence:
MALFLSPKTITLLFFSLSLALYCSIDPFHHCAISDFPNFVSHEVISPRPDEVPWERDSQNSLQKSKILFFNQIQGPESVAFDSLGRGPYTGVADGRVLFWDGEKWIDFAYTSSNRSEICDPKPSALSYLRNEHICGRPLGLRFDKRTGDLYIADAYMGLLKVGPEGGLATPLVTEAEGVPLGFTNDLDIADDGTVYFTDSSISYQRRNFLQLVFSGDNTGRVLKYDPVAKKAVVLVSNLQFPNGVSISRDGSFFVFCEGDIGSLRRYWLKGEKAGTTDVFAYLPGHPDNVRTNQKGEFWVALHCRRNYYSYLMARYPKLRMFILRLPITARTHYSFQIGLRPHGLVVKYSPEGKLMHVLEDSEGKVVRSVSEVEEKDGKLWMGSVLMNFVAVYDL
Protein: N(6)-L-threonylcarbamoyladenine synthase (EC 2.3.1.234) (E7EVL7)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MLILTKTAGVFFKPSKRKVYEFLRSFNFHPGTLFLHKIVLGIETSCDDTAAAVVDETGNVLGEAIHSQTEVHLKTGGIVPPAAQQLHRENIQRIVQEALSASGVSPSDLSAIATTIKPGLALSLGVGLSFSLQLVGQLKKPFIPIHHMEAHALTIRLTNKVEFPFLVLLISGGHCLLALVQGVSDFLLLGKSLDIAPGDMLDKVARRLSLIKHPECSTMSGG
Protein: LD24646p (Pachytene checkpoint 2, isoform A) (Pachytene checkpoint 2, isoform B) (Q8SX76)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Mitotic spindle assembly checkpoint protein MAD2A
- DNA polymerase zeta subunit 2
- Cytochrome c1, heme protein, mitochondrial
- Exonuclease 1
- Cytochrome c1, heme protein, mitochondrial
- DNA replication licensing factor Mcm7
- DNA repair protein RAD51 homolog 3
- Origin recognition complex subunit 1
- DNA repair protein Rad51 homolog
- CDC45L
Sequence:
MSFLSNSDTVHVEVCLRGNDLRSNAIRNNVETALKAYFQTARKLPRNVSFLPDLTAEQTEHVHSVLLERDNGGVQPLKVAETKFRFHFYATRPEEGQLGLFSGEEGSDGIDSIVAASHALLPAAQFVGLWENLIYETGLKEKLLKFALSALMFSEHRVDTNVIACNRLILLHGPPGTGKTSLCKALAQKLSIRTQGSYAYTHLVEINSHSLFSKWFSESGKLVAQLFNKIAELVSDPNNLVCVLIDEVESLAYARSAMSSNEPRDAMRVVNAVLTQLDSLKTCPNVLILATSNLAQSIDLAFVDRADIRLFIGYPGISAIREIYKGMLAELMSAGVLQREVLESEDAEEGLLTQLAERSVGLSGRTLRKLPLLAHAQYTSSTLFELDQKISLSDFLDAMLEALEQHLGEQRLLKLESMEQL
Protein: MAGE family member A11 (Melanoma antigen family A, 11, isoform CRA_a) (G5E962)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MSKVSTMFSEDDFQSTERAPYGPQLQWSQDLPRVQVFREQANLEDRSPRRTQRITGGEQVLWGPITQIFPTVRPADLTRVIMPLEQRSQHCKPEEGLQAQEEDLGLVGAQALQAEEQEAAFFSSTLNVGTLEELPAAESPSPPQSPQEESFSPTAMDAIFGSLSDEGSGSQEKEGPSTSPDLIDPESFSQDILHDKIIDLVHLLLRKYRVKGLITKAEMLGSVIKNYEDYFPEIFREASVCMQLLFGIDVKEVDPTSHSYVLVTSLNLSYDGIQCNEQSMPKSGLLIIVLGVIFMEGNCIPEEVMWEVLSIMGVYAGREHFLFGEPKRLLTQNWVQEKYLVYRQVPGTDPACYEFLWGPRAHAETSKMKVLEYIANANGRDPTSYPSLYEDALREEGEGV
Protein: Mediator of RNA polymerase II transcription subunit 20 (Hyper-recombination suppressor protein 2) (Mediator complex subunit 20) (Suppressor of RNA polymerase B 2) (P34162)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Component of the Mediator complex, a coactivator involved in the regulated transcription of nearly all RNA polymerase II-dependent genes. Mediator functions as a bridge to convey information from gene-specific regulatory proteins to the basal RNA polymerase II transcription machinery. The Mediator complex, having a compact conformation in its free form, is recruited to promoters by direct interactions with regulatory proteins and serves for the assembly of a functional preinitiation complex with RNA polymerase II and the general transcription factors. The Mediator complex unfolds to an extended conformation and partially surrounds RNA polymerase II, specifically interacting with the unphosphorylated form of the C-terminal domain (CTD) of RNA polymerase II. The Mediator complex dissociates from the RNA polymerase II holoenzyme and stays at the promoter when transcriptional elongation begins.
Subcellular location: Nucleus {ECO:0000269|PubMed:14562095}.
Interaction partners:
- Mediator of RNA polymerase II transcription subunit 10
- Mediator of RNA polymerase II transcription subunit 31
- Mediator of RNA polymerase II transcription subunit 11
- Mediator of RNA polymerase II transcription subunit 6
- Mediator of RNA polymerase II transcription subunit 8
- Mediator of RNA polymerase II transcription subunit 7
- Mediator of RNA polymerase II transcription subunit 18
- Mediator of RNA polymerase II transcription subunit 22
- Mediator of RNA polymerase II transcription subunit 14
- Mediator of RNA polymerase II transcription subunit 17
Sequence:
MGKSAVIFVERATPATLTELKDALSNSILSVRDPWSIDFRTYRCSIKNLPADVSKLMYSITFHHHGRQTVLIKDNSAMVTTAAAADIPPALVFNGSSTGVPESIDTILSSKLSNIWMQRQLIKGDAGETLILDGLTVRLVNLFSSTGFKGLLIELQADEAGEFETKIAGIEGHLAEIRAKEYKTSSDSLGPDTSNEICDLAYQYVRALEL
Protein: Cysteine and histidine-rich domain-containing protein RAR1 (CHORD domain-containing protein RAR1) (OsRAR1) (Protein REQUIRED FOR MLA12 RESISTANCE 1) (Q6EPW7)
Organism: Oryza sativa subsp. japonica (Rice)
Function: Involved in basal disease resistance to virulent strain of bacterial blight (X.oryzae) and compatible race of rice blast fungus (M.grisea). May act as positive regulator of basal defense. Associates with HSP90 and is essential for the pathogen-associated molecular pattern (PAMP)-triggered immune responses specifically enhanced by RAC1.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:18257679}. Nucleus {ECO:0000269|PubMed:18257679}.
Interaction partners:
- Protein SGT1 homolog
- Heat shock protein 81-2
- Protein SGT1 homolog
- Endoplasmin homolog
- Os04g0107900 protein
- Heat shock protein 81-1
- Hsp90 protein, expressed
- Os09g0474300 protein
- Os08g0487800 protein
- Heat shock protein 81-3
Sequence:
MSTEAETTSAAAPAPAPAPASAPARCQRIGCDATFTDDNNPDGSCQYHPSGPMFHDGMKQWSCCKQKSHDFSLFLAIPGCKTGKHTTEKPITKAVPTKPSKAVPVQTSKQSVGADTCSRCRQGFFCSDHGSQPKAQIPTATSDTNMVPVEKPAVPPPKKKIDLNEPRVCKNKGCGKTYKEKDNHDEACDYHPGPAVFRDRIRGWKCCDIHVKEFDEFMEIPPCTKGWHNADAA
Protein: Calcium uptake protein 1, mitochondrial (Atopy-related autoantigen CALC) (ara CALC) (Calcium-binding atopy-related autoantigen 1) (allergen Hom s 4) (Q9BPX6)
Organism: Homo sapiens (Human)
Function: Key regulator of mitochondrial calcium uniporter (MCU) that senses calcium level via its EF-hand domains. MICU1 and MICU2 form a disulfide-linked heterodimer that stimulates and inhibits MCU activity, depending on the concentration of calcium. MICU1 acts both as an activator or inhibitor of mitochondrial calcium uptake. Acts as a gatekeeper of MCU at low concentration of calcium, preventing channel opening. Enhances MCU opening at high calcium concentration, allowing a rapid response of mitochondria to calcium signals generated in the cytoplasm. Regulates glucose-dependent insulin secretion in pancreatic beta-cells by regulating mitochondrial calcium uptake. Induces T-helper 1-mediated autoreactivity, which is accompanied by the release of IFNG.
Subcellular location: Mitochondrion intermembrane space {ECO:0000269|PubMed:23747253, ECO:0000269|PubMed:24560927, ECO:0000269|PubMed:26387864}. Mitochondrion inner membrane {ECO:0000269|PubMed:23747253, ECO:0000269|PubMed:24231807, ECO:0000269|PubMed:26387864, ECO:0000269|PubMed:27099988, ECO:0000269|PubMed:28615291}. Note=Recruited to the mitochondrial inner membrane by EMRE/SMDT1 (PubMed:30454562). Also localizes to mitochondrial cristae junctions (PubMed:31427612). {ECO:0000269|PubMed:30454562, ECO:0000269|PubMed:31427612}.; SUBCELLULAR LOCATION: [Isoform 6]: Mitochondrion intermembrane space {ECO:0000250|UniProtKB:Q8VCX5}. Mitochondrion inner membrane {ECO:0000250|UniProtKB:Q8VCX5}.
Interaction partners:
- Calcium uniporter protein, mitochondrial
- Calcium uniporter regulatory subunit MCUb, mitochondrial
- Essential MCU regulator, mitochondrial
- Calcium uptake protein 2, mitochondrial
- Mitochondrial calcium uniporter regulator 1
- Calcium uptake protein 3, mitochondrial
- Mitochondrial adenyl nucleotide antiporter SLC25A23
- Mitochondrial intermembrane space import and assembly protein 40
- Mitochondrial proton/calcium exchanger protein/H
- Prohibitin-2
Sequence:
MFRLNSLSALAELAVGSRWYHGGSQPIQIRRRLMMVAFLGASAVTASTGLLWKRAHAESPPCVDNLKSDIGDKGKNKDEGDVCNHEKKTADLAPHPEEKKKKRSGFRDRKVMEYENRIRAYSTPDKIFRYFATLKVISEPGEAEVFMTPEDFVRSITPNEKQPEHLGLDQYIIKRFDGKKISQEREKFADEGSIFYTLGECGLISFSDYIFLTTVLSTPQRNFEIAFKMFDLNGDGEVDMEEFEQVQSIIRSQTSMGMRHRDRPTTGNTLKSGLCSALTTYFFGADLKGKLTIKNFLEFQRKLQHDVLKLEFERHDPVDGRITERQFGGMLLAYSGVQSKKLTAMQRQLKKHFKEGKGLTFQEVENFFTFLKNINDVDTALSFYHMAGASLDKVTMQQVARTVAKVELSDHVCDVVFALFDCDGNGELSNKEFVSIMKQRLMRGLEKPKDMGFTRLMQAMWKCAQETAWDFALPKQ
Protein: Olfactory receptor 10G7 (Olfactory receptor OR11-283) (Q8NGN6)
Organism: Homo sapiens (Human)
Function: Odorant receptor.
Subcellular location: Cell membrane; Multi-pass membrane protein.
Interaction partners:
- Olfactory receptor 10G9
- Olfactory receptor 10G4
- Guanine nucleotide-binding protein G
Sequence:
MSNATLLTAFILTGLPHAPGLDAPLFGIFLVVYVLTVLGNLLILLVIRVDSHLHTPMYYFLTNLSFIDMWFSTVTVPKMLMTLVSPSGRTISFHSCVAQLYFFHFLGSTECFLYTVMSYDRYLAISYPLRYTNMMTGRSCALLATGTWLSGSLHSAVQTILTFHLPYCGPNQIQHYFCDAPPILKLACADTSANEMVIFVNIGLVASGCFVLIVLSYVSIVCSILRIRTSEGRHRAFQTCASHCIVVLCFFGPGLFIYLRPGSRDALHGVVAVFYTTLTPLFNPVVYTLRNKEVKKALLKLKNGSVFAQGE