wanglab/gogpt-training-data huggingface dataset:
Protein: Leucine-rich glioma-inactivated protein 1 (Epitempin-1) (O95970)
Organism: Homo sapiens (Human)
Function: Regulates voltage-gated potassium channels assembled from KCNA1, KCNA4 and KCNAB1. It slows down channel inactivation by precluding channel closure mediated by the KCNAB1 subunit. Ligand for ADAM22 that positively regulates synaptic transmission mediated by AMPA-type glutamate receptors (By similarity). Plays a role in suppressing the production of MMP1/3 through the phosphatidylinositol 3-kinase/ERK pathway. May play a role in the control of neuroblastoma cell survival.
Subcellular location: Secreted {ECO:0000269|PubMed:16787412, ECO:0000269|PubMed:17067999, ECO:0000269|PubMed:17296837}. Synapse {ECO:0000250|UniProtKB:Q8K4Y5}. Cytoplasm {ECO:0000250|UniProtKB:Q9JIA1}.; SUBCELLULAR LOCATION: [Isoform 1]: Golgi apparatus {ECO:0000269|PubMed:17067999}. Secreted {ECO:0000269|PubMed:9879993}. Cytoplasm {ECO:0000250|UniProtKB:Q9JIA1}.; SUBCELLULAR LOCATION: [Isoform 2]: Endoplasmic reticulum {ECO:0000269|PubMed:17067999}. Cytoplasm {ECO:0000250|UniProtKB:Q9JIA1}.
Interaction partners:
- Disintegrin and metalloproteinase domain-containing protein 22
- Disintegrin and metalloproteinase domain-containing protein 23
- Contactin-associated protein-like 2
- Disintegrin and metalloproteinase domain-containing protein 28
- Potassium voltage-gated channel subfamily A member 1
- Disks large homolog 4
- Contactin-2
- Disintegrin and metalloproteinase domain-containing protein 11
- Voltage-dependent calcium channel gamma-2 subunit
- A-type potassium channel modulatory protein DPP6
Sequence:
MESERSKRMGNACIPLKRIAYFLCLLSALLLTEGKKPAKPKCPAVCTCTKDNALCENARSIPRTVPPDVISLSFVRSGFTEISEGSFLFTPSLQLLLFTSNSFDVISDDAFIGLPHLEYLFIENNNIKSISRHTFRGLKSLIHLSLANNNLQTLPKDIFKGLDSLTNVDLRGNSFNCDCKLKWLVEWLGHTNATVEDIYCEGPPEYKKRKINSLSSKDFDCIITEFAKSQDLPYQSLSIDTFSYLNDEYVVIAQPFTGKCIFLEWDHVEKTFRNYDNITGTSTVVCKPIVIETQLYVIVAQLFGGSHIYKRDSFANKFIKIQDIEILKIRKPNDIETFKIENNWYFVVADSSKAGFTTIYKWNGNGFYSHQSLHAWYRDTDVEYLEIVRTPQTLRTPHLILSSSSQRPVIYQWNKATQLFTNQTDIPNMEDVYAVKHFSVKGDVYICLTRFIGDSKVMKWGGSSFQDIQRMPSRGSMVFQPLQINNYQYAILGSDYSFTQVYNWDAEKAKFVKFQELNVQAPRSFTHVSINKRNFLFASSFKGNTQIYKHVIVDLSA
Protein: Uncharacterized protein YGR151C (P53287)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Subcellular location: Cytoplasm {ECO:0000269|PubMed:14562095}. Nucleus {ECO:0000269|PubMed:14562095}.
Interaction partners:
Sequence:
MKWKVLQLKTQEIKVNNLAKSSLHQPGSLVLRNRIRNNQTISNHQKVYITNLHKDKLKLNNLLRLMKSTNRHMPFRNLVLATGQELALLHNKRKRRKTLPLALFYSHLILL
Protein: Tudor domain-containing protein 1 (Q58EK5)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Function: Plays a central role during spermatogenesis by participating in the repression transposable elements and preventing their mobilization, which is essential for the germline integrity. Acts via the piRNA metabolic process, which mediates the repression of transposable elements during meiosis by forming complexes composed of piRNAs and Piwi proteins and governs the methylation and subsequent repression of transposons. Required for the localization of Piwi proteins to the meiotic nuage. Involved in the piRNA metabolic process by ensuring the entry of correct transcripts into the normal piRNA pool and limiting the entry of cellular transcripts into the piRNA pathway. May act by allowing the recruitment of piRNA biogenesis or loading factors that ensure the correct entry of transcripts and piRNAs into Piwi proteins (By similarity).
Subcellular location: Cytoplasm {ECO:0000250}. Note=Component of the meiotic nuage, also named P granule, a germ-cell-specific organelle required to repress transposon activity during meiosis. {ECO:0000250}.
Interaction partners:
- Piwi-like protein 2
- Piwi-like protein 1
- Tudor domain-containing 12.
- Ankyrin repeat, SAM and basic leucine zipper domain-containing 1.
- Mitochondrial cardiolipin hydrolase
- ATP-dependent RNA helicase TDRD9
- Serine/threonine kinase 31.
- peptidylprolyl isomerase
- Small RNA 2'-O-methyltransferase
- piRNA biogenesis protein EXD1
Sequence:
MNPAFAQPMMRPNLPLRRPATGPSSLSPRGPAPAIYEERLLASDVLDGPKIDTMRKDISQNCGDVLSSPQTAVSMMGQVVKLCNYCSHQGNLRCTRCKKTCYCSVACQTQDWIAHRHVCKPSIPEVTSEKPKESKAVPYANGLGGTQAKEISVDAQPKRIYRRDLHKKVVSKGSEIKGTVIDLRNPGMFSIHCQCEEMIESLKKITQQLQKTYCSSFAQEYKPEVGELCAVKFSLDQNWYRAEIQAVDVARKTAGVFYIDFGNEENVALDHIRPLSENIDAVPPFALQCCIAGVKPLTGSWTGECCIAVRQLIAGKSLTFTVLDIMNDGDLLAVDSLVSTLGKHVSTFLIDQSYAIKEDVPVKTQTEHSISSLLTASFENFKRFSGGKNENSEARPPEPLTQGVGDSFTAVVTHLQSPSEILCQKLENASIIQQLQMNLRVHCSNTAASDDFRPAPGTVCCSLFSEDNQWYRAKVLAYSSEDRVCVGYIDFGNSEEVELNRLRPISKELLALATQAIPCSLAGIKSLTDTWSDEAVLMLKHLVCNRFIRVEILGKKDGRALVSMIDESSDPQASVTELLVNMGFAAIESVETKKNEPDPATSTEIPLSQPVVEKLEWTGAELPFDGQKVELVISTLKSLDEFYCYNYSKTDEHTLTEMSFELMKHCESERAPFTPIVGEPCCALFTGDARWYRAMVLEVCGEGKARVCFVDYGNSCEVDAAHLKAITQSLLKLPFQAIRCWLAGVEPVEGQWKKEAMLRFQALCAGQPLSGKVLSITEKGYGMELESAGQTVASVLISEHLAKPYGQVRQPPQIQPAKPASQIEDLPSLKPIDQNPSVEEPLKVSSKGAATTPEDLPVSSGCFPLNWKTLELSCSGTFQPRVAAVISPSLFYIMNPGQVNVEGLKAVMTDVAKYCSKQPVPNQCHPLPGASCCAQFSGDKNWYRAVVLEVTTKHAHVIYSDYGNMETVPLSSILPITKELLQHPFQIVRCALTGKEHFPVVWPTEVLELFGIQLSGGVLASFQGFDGTSNLLTLTQQSGQSDRDINSIILGALQKGQIKPSSKLPANVNEEKKDVEQKQTQPISSNKAVEQTLSTNVEKPALDDQTLPLSVSLKHEEPENMSKTKTAEECTSTPDTVSSIESSHAAQSCCCQELKQKMDRIEELVLLLVKQVGSR
Protein: DNA-directed RNA polymerases I and III subunit RPAC2 (RNA polymerases I and III subunit AC2) (AC19) (DNA-directed RNA polymerases I and III 14 kDa polypeptide) (Q09177)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. Common core component of RNA polymerases I and III which synthesize ribosomal RNA precursors and small RNAs, such as 5S rRNA and tRNAs, respectively.
Subcellular location: Nucleus {ECO:0000250}.
Interaction partners:
- DNA-directed RNA polymerase I subunit RPA12
- DNA-directed RNA polymerase I subunit rpa43
- Probable DNA-directed RNA polymerase III subunit rpc6
- DNA-directed RNA polymerase III subunit rpc8
- DNA-directed RNA polymerases I, II, and III subunit RPABC5
- DNA-directed RNA polymerase I subunit rpa1
- DNA-directed RNA polymerases I, II, and III subunit RPABC2
- DNA-directed RNA polymerase III subunit rpc4
- DNA-directed RNA polymerases I, II, and III subunit RPABC3
- DNA-directed RNA polymerases I, II, and III subunit RPABC4
Sequence:
MAAMTDVTDPSSVAMESATEKIIILPGHSADLTSVTFQIQKEDHTLGNSLRYVIMKNPEVEFCGYSIPHPSEAKMNFRIQTAPSTTAVDVLRKGLDDLIDLCDAVTEKFTEQLPRDTSTTMEVDG
Protein: Fibroblast growth factor (FGF) (Q8AXC5)
Organism: Xenopus laevis (African clawed frog)
Interaction partners:
- Fibroblast growth factor receptor
- Fibroblast growth factor receptor
- Fibroblast growth factor receptor.
- Fibroblast growth factor receptor.
- Fibroblast growth factor receptor
- Fibroblast growth factor receptor
- Fibroblast growth factor receptor
- Fibroblast growth factor
- Hedgehog protein
- Fibroblast growth factor receptor-like 1
Sequence:
MNYITSILGYLLLHLFVICLQAQVTVQSPPNFTQHVREQSLVTDQLSRRLIRTYQLYSRTSGKHVQILANKKINAMAEDGDPHAKLIVETDTFGSRVRIKGAETGYYICMNKKGKLIGKTNGRGKDCVFSEIVLENNYTALQNVKYEGWFMAFTRRGRPRKGSKTRQHQREVHFMKRLPKGHHTTEPHKRFEFINYPFNRRSKRTRYSSSR
Protein: RNA helicase (EC 3.6.4.13) (J3QRQ7)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MSGYSSDRDRGRDRGFGAPRFGGSRAGPLSGKKFGNPGEKLVKKKWNLDELPKFEKNFYQEHPDLARRTAQEVETYRRSKEITVRGHNCPKPVLNFYEANFPANVMDVIARQNFTEPTAIQAQGWPVALSGLDMVGVAQTGSGKTLSYLLPAIVHINHQPFLERGDGPICLVLAPTRELAQQVQQVAAEYCRACRLKSTCIYGGAPKGPQIR
Protein: Chloride channel protein ClC-Kb (Chloride channel Kb) (x6clck) (xCIC-K) (Q9W701)
Organism: Xenopus laevis (African clawed frog)
Function: Voltage-gated chloride channel. Chloride channels have several functions including the regulation of cell volume, the stabilization of membrane potential, signal transduction and transepithelial transport.
Subcellular location: Cell membrane {ECO:0000269|PubMed:10359659}; Multi-pass membrane protein {ECO:0000255, ECO:0000269|PubMed:10359659}.
Interaction partners:
Sequence:
MSRVLVIEQREGEEKTLIQKHIFRPFPNTRRVVIDHLQRLKNFLFRIGDDWYFLFALGVIMALISFTMDFTVSKMLNAHRWLQQELGGNVLLRYLSWIVYPIALVAFSTGFAQSITPHSGGSGIPELKTILSGVILEEYLTIKNFGAKVVGLTCTLSAGSTMFLGKVGPFVHLSSMIAAYLGRMRTSVAGDYENKSKEHEMLVAAAAVGVSTVFGAPISGVLFSVEVMSSHFAIRNYWRGFFAATCGAFVFRLLAVFNSEQETITAVFKTSFKISFPFDLPEMFFFAILGVVCGLIGCAYLFCQRWLLGYVRRNSLTSKLLASDKPMYSALVALLISSITFPESLGQFLASRLTMKELLTSLFDNRTWWISLSQNSSLDRSPLVDPNNLWLEWANPQFTIFGTLAFFIIMKFWMFILATTLPMPAGYFMPVFVFGAAIGRLVGETVALLYPEGIAADGIVNPIIPGGYAWQGAPAYSGAVTHSVSTALLAFEATGQIAHILPVILCVLIANAFTQKLQPSFYDGTIIVKKLPYLPRIRSRDIDSYKVNTEEFMNPDIRVLPREAGFEDVLKVITASDDSEYPVVDNTESQVLVGTVKRPQLIHFLETHESHERAGPTEKENLSEGNLGEACSIEPVTFQLSTWTSLHQAHHLFELLHLQKAFVTKYGRIVGQVTRKEMKKAIEDLANPK
Protein: Mitochondrial ribosome-associated GTPase 1 (GTP-binding protein 7) (Mitochondrial GTPase 1) (Q8R2R6)
Organism: Mus musculus (Mouse)
Function: Plays a role in the regulation of the mitochondrial ribosome assembly and of translational activity (By similarity). Displays mitochondrial GTPase activity (By similarity).
Subcellular location: Mitochondrion inner membrane {ECO:0000250|UniProtKB:Q9BT17}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q9BT17}; Matrix side {ECO:0000250|UniProtKB:Q9BT17}.
Interaction partners:
- Mitochondrial assembly of ribosomal large subunit protein 1
- Large ribosomal subunit protein uL29m
- GTP-binding protein 8
- rRNA methyltransferase 3, mitochondrial
- Mitochondrial ribosome-associated GTPase 2
- Large ribosomal subunit protein uL3m
- Large ribosomal subunit protein uL11m
- Large ribosomal subunit protein bL21m
- Large ribosomal subunit protein uL24m
- Large ribosomal subunit protein mL43
Sequence:
MRLWPQAWGAVRGAWRECFPLQGHDVARWFPGHMAKGLKKMQSSLKSVDCVIEVHDARIPFSGRNPLFQELLGLKPHLLVLNKMDLADLTEQQKIVQRLEEKGLSNVLFTNCVKDENIKQIVPKVMELIRCSYRYHRAETPEYCIMVVGVPNVGKSSLINSLRRQHLRTGKAARVGGEPGITRAVTSRIQVCERPLVFLLDTPGVLAPRIESVETGLKLALCGTVLDHLVGEETMADYLLYTLNRHGLFGYVQHYALASACDQIEWVLKNVAIKLRKTRKVKVLTGTGNVNVIQPDYAMAARDFLRTFRSGLLGQVMLDRDIIPAC
Protein: ADAM metallopeptidase with thrombospondin type 1 motif A, isoform B (EC 3.4.24.-) (GH16393p) (Q8SXB0)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Secreted, extracellular space, extracellular matrix {ECO:0000256|ARBA:ARBA00004498}.
Interaction partners:
- Neurogenic locus Notch protein
Sequence:
MSMPDAGSLKSPAGGQEVECHRLLSDLPAFAYPSTTLRSTTSGHSTGTNSTTVCESPGARDRTSFACSSSCVSSACSATASDDDEDERALERCLRGTTDDLGESGLRYSLKGPPPELYSAKKDFISKGPLLGRQLEVKKRCEWWCHKYIQKMSTHWRQNACLYACCIAFLLGMLIMFHLGLRSAHKGQEELPQSTHPLANSPPATPATLHPRRLDNDTSTDHEPPDGLDDLDEEEHSAFVMPTKVYNYSLSEADLIYESKRNSDINSFLKESASAFAMTGTYRNMSNEIWDPHPQYNLNVFGRQLHLVLRQDASFVHNHSMTHIRILKEGEEHPGPETEAEAEQRHLGCFYSGYVEDDPHSMVSVSLCGGMTGYIKTSFGALLIQPVNRTSSDEVLHRVFRKSQRNARHAVSKFELGLDDFMSKLEQVQEEEQKSKSRKLNRKKRHYADVDNQVYTLEVLIAVDNSMKQFHGEDLQPYILILMSIVSSIFADASIGNSIRILLVRLISLPNINDQTHSSNEMLKHFCQFINQSGYERDTAMLITREPICGSVPGKICHMLGLAELGTVCSSSSCSIVQDTGLPTAFTMAHELGHILNMNHDDDDKCMPYVTRQNNNKVLHIMSSVMGIHMHPWSWSKCSRHFVSEFLEKTDKSCLETSVGAHIPYGTERLPGEIYSLDAQCQLSFGNDFGYCPTDEECKRLWCNRTSGNSNEQCASSNLPWADGTPCGSSGHWCQRGKCVSNKHGYGRQVNGGWGPWTPFTPCSLTCGGGVQESRRECNQPVPENGGKYCTGSRKKYRSCNTHQCPPGSMDPREQQCYAMNGRNMNIPGVNPDTKWVPKYEKDACKLFCRMDMKVTYFMLKSMVTDGTSCAVDSFDKCVNGICRPAGCDNELNSIAKLDKCGVCEGRNDTCHEVTGNLLVSNLLGLNDGNEPNKTLYYVTRIPKGASNIIITQRGYPDQNFIVLTDDRDNELLNGKFLKTYPLKFVYAGVTMQYTGSSSVVEQVNTTYSWKLSRDLIVQIISLDVSPSKRQDTVLLSYSYTIDKPPDYEAEVEIYRWEMQAPSNCDSLCEGRSHRLPACISTTQGVKVAPQFCDKSAMPKIDDRACNTDCRLNLTVTSISECSAACGELGTREKTYACVQTFTNMQRSNIVDMSYCKLKFDVAYHEECREGCWVLSEWSTCSKSCGTGSQQREAHCYLHNSRVSDDLCNPRTKPHLNTLIGICNTESCPTYTKSPNALAVSNWVIGEWGECNEWCEKTRSVSCSHPYGIGCGSRKPKDVRKCCHIKYTSDWTDCSVQCGEGVKRKKQSCTRVYKPDVPGTRKRRVYVDESYCISRKVHRPKLRTTTKSCRINCKWNASDWRRCPADCSEEYQTRDVRCESFQGDGVEDKHCDAKKRPSKRRICNNCVRRQSRVISQCNCEGVEKRRDFCFNSHKGRIACPTRARVERHSCTPPPHCRRRSAIGSSISSRPRGTGVSSSRSLNSIGGSRNRGTPRSCADLKEMHGYNKDGNYQLEVRSRMVHIYCHGMNSRTPQEYVNVDPQENYSIYYEYRTKQTNSCPPESRGHEYYNDQNSGRTHFRKLRLNITDLRIMDNDFKFADSRGLAQKLGSAGDCYNRIGQCPQGDFSINMKDTDFSIRPGTVWRMHGQYSVMKRISEFDTTTQMRRGFCGGYCGGCYIAPDSGLYLDVL
Protein: E3 ubiquitin-protein ligase ATL76 (EC 2.3.2.27) (RING-H2 finger protein ATL76) (RING-type E3 ubiquitin transferase ATL76) (Q6NML0)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: E3 ubiquitin-protein ligase able to catalyze polyubiquitination with ubiquitin-conjugating enzyme E2 UBC8 in vitro.
Subcellular location: Membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}.
Interaction partners:
- E3 ubiquitin-protein ligase RMA2
- E3 ubiquitin-protein ligase RMA1
- Bifunctional inhibitor/lipid-transfer protein/seed storage 2S albumin superfamily protein
Sequence:
MSANELPASAQSLQEQFLGSFVTRKLLLHDPFDHNSLRVFAVAPSPLITHENNLKGNVLMLLSVLICGIICCLGLHYIIRCAFRRSSRFMISEPISSLSTPRSSSNKGIKKKALRMFPVVSYSREMNLPGIGEECVICLSDFVSGEQLRLLPKCNHGFHVRCIDKWLQHHLTCPKCRHCLVETCQKILGDFSQADSMASTPTESVIVRIDPLEPEGRVNTFRESS
Protein: Glycine dehydrogenase (decarboxylating) (EC 1.4.4.2) (Glycine cleavage system P-protein) (Glycine decarboxylase) (Glycine dehydrogenase (aminomethyl-transferring)) (P33195)
Organism: Escherichia coli (strain K12)
Function: The glycine cleavage system catalyzes the degradation of glycine. The P protein binds the alpha-amino group of glycine through its pyridoxal phosphate cofactor; CO(2) is released and the remaining methylamine moiety is then transferred to the lipoamide cofactor of the H protein.
Interaction partners:
- Glycine cleavage system H protein
- Aminomethyltransferase
- Serine hydroxymethyltransferase
- Dihydrolipoyl dehydrogenase
- 2-amino-3-ketobutyrate coenzyme A ligase
- Low specificity L-threonine aldolase
- Phosphoribosylamine--glycine ligase
- Phosphoribosylformylglycinamidine synthase
- Fumarate hydratase class I, aerobic
- Fumarate hydratase class I, anaerobic
Sequence:
MTQTLSQLENSGAFIERHIGPDAAQQQEMLNAVGAQSLNALTGQIVPKDIQLATPPQVGAPATEYAALAELKAIASRNKRFTSYIGMGYTAVQLPPVILRNMLENPGWYTAYTPYQPEVSQGRLEALLNFQQVTLDLTGLDMASASLLDEATAAAEAMAMAKRVSKLKNANRFFVASDVHPQTLDVVRTRAETFGFEVIVDDAQKVLDHQDVFGVLLQQVGTTGEIHDYTALISELKSRKIVVSVAADIMALVLLTAPGKQGADIVFGSAQRFGVPMGYGGPHAAFFAAKDEYKRSMPGRIIGVSKDAAGNTALRMAMQTREQHIRREKANSNICTSQVLLANIASLYAVYHGPVGLKRIANRIHRLTDILAAGLQQKGLKLRHAHYFDTLCVEVADKAGVLTRAEAAEINLRSDILNAVGITLDETTTRENVMQLFNVLLGDNHGLDIDTLDKDVAHDSRSIQPAMLRDDEILTHPVFNRYHSETEMMRYMHSLERKDLALNQAMIPLGSCTMKLNAAAEMIPITWPEFAELHPFCPPEQAEGYQQMIAQLADWLVKLTGYDAVCMQPNSGAQGEYAGLLAIRHYHESRNEGHRDICLIPASAHGTNPASAHMAGMQVVVVACDKNGNIDLTDLRAKAEQAGDNLSCIMVTYPSTHGVYEETIREVCEVVHQFGGQVYLDGANMNAQVGITSPGFIGADVSHLNLHKTFCIPHGGGGPGMGPIGVKAHLAPFVPGHSVVQIEGMLTRQGAVSAAPFGSASILPISWMYIRMMGAEGLKKASQVAILNANYIASRLQDAFPVLYTGRDGRVAHECILDIRPLKEETGISELDIAKRLIDYGFHAPTMSFPVAGTLMVEPTESESKVELDRFIDAMLAIRAEIDQVKAGVWPLEDNPLVNAPHIQSELVAEWAHPYSREVAVFPAGVADKYWPTVKRLDDVYGDRNLFCSCVPISEYQ
Protein: Beta-1,4-galactosyltransferase 6 (Beta-1,4-GalTase 6) (Beta4Gal-T6) (b4Gal-T6) (EC 2.4.1.-) (Glucosylceramide beta-1,4-galactosyltransferase) (EC 2.4.1.274) (Lactosylceramide synthase) (LacCer synthase) (UDP-Gal:beta-GlcNAc beta-1,4-galactosyltransferase 6) (UDP-Gal:glucosylceramide beta-1,4-galactosyltransferase) (UDP-galactose:beta-N-acetylglucosamine beta-1,4-galactosyltransferase 6) (Q9UBX8)
Organism: Homo sapiens (Human)
Function: Catalyzes the synthesis of lactosylceramide (LacCer) via the transfer of galactose from UDP-galactose to glucosylceramide (GlcCer). LacCer is the starting point in the biosynthesis of all gangliosides (membrane-bound glycosphingolipids) which play pivotal roles in the CNS including neuronal maturation and axonal and myelin formation (By similarity).
Subcellular location: Golgi apparatus, Golgi stack membrane {ECO:0000250|UniProtKB:P15291}; Single-pass type II membrane protein. Note=Trans cisternae of Golgi stack. {ECO:0000250|UniProtKB:P15291}.
Interaction partners:
- Ceramide glucosyltransferase
- Lactosylceramide alpha-2,3-sialyltransferase
- Lactosylceramide 4-alpha-galactosyltransferase
- Lysosomal acid glucosylceramidase
- Non-lysosomal glucosylceramidase
- Beta-galactosidase
- Lactosylceramide 1,3-N-acetyl-beta-D-glucosaminyltransferase
- Beta-1,4 N-acetylgalactosaminyltransferase 1
- Alpha-1,3-galactosyltransferase 2
- Alpha-galactosidase A
Sequence:
MSVLRRMMRVSNRSLLAFIFFFSLSSSCLYFIYVAPGIANTYLFMVQARGIMLRENVKTIGHMIRLYTNKNSTLNGTDYPEGNNSSDYLVQTTTYLPENFTYSPYLPCPEKLPYMRGFLNVNVSEVSFDEIHQLFSKDLDIEPGGHWRPKDCKPRWKVAVLIPFRNRHEHLPIFFLHLIPMLQKQRLEFAFYVIEQTGTQPFNRAMLFNVGFKEAMKDSVWDCVIFHDVDHLPENDRNYYGCGEMPRHFAAKLDKYMYILPYKEFFGGVSGLTVEQFRKINGFPNAFWGWGGEDDDLWNRVHYAGYNVTRPEGDLGKYKSIPHHHRGEVQFLGRYKLLRYSKERQYIDGLNNLIYRPKILVDRLYTNISVNLMPELAPIEDY
Protein: (-)-beta-phellandrene synthase 4, chloroplastic (EC 4.2.3.52) (Terpene synthase TPS-Phel-4) (PsTPS-Phel-4) (F2XFA1)
Organism: Picea sitchensis (Sitka spruce) (Pinus sitchensis)
Function: Terpene synthase (TPS) involved in the biosynthesis of monoterpene natural products included in conifer oleoresin secretions and volatile emissions; these compounds contribute to biotic and abiotic stress defense against herbivores and pathogens. Catalyzes the conversion of (2E)-geranyl diphosphate (GPP) to (-)-beta-phellandrene.
Subcellular location: Plastid, chloroplast {ECO:0000255}.
Interaction partners:
Sequence:
MAIVSSVPLASKSCLHKSLISSIHKLKPFCRTIPTLGMSRPGKSVMPSMSMSSPVSDDGVQRRTGGYHSNLWNDDIIQFLSTPYGEPAYRERGERLIDEVKNMFNSISMEDVEFSPLNDLIQRLWIVDSVERLGIDRHFKNEIKSTLDYVYSYWTQKGIGCGIESVVPDLNSTALGLRTLRLHGYPVSAEVLKHFQNQNGQFACSPSETEGEMRSIVNLYRASLIAFPGEKVMEEAEIFSTKYLKEALQKIPVSSLSREIGDVLEQDWHTNLPRLEARNYIDVFGQDTKDTKLYMKTEKLLELAKLEFNIFQSLQKTELDSLLRWWKDSGFHHITFSRHLHVEYYTLASCIAFEPQHSRFRLGFAKACHVITILDDMYDVFGTIDELELFTAQIKRWDPSATDCLPKYMKRMYMILYDMVNEMSREAETAQGRDTLNYARQAWEDFIDSYMQEAKWIATGYLPTFDEYFENGKVSSGHRVAALQPILTMDIPFPHDILKEVDFPSKLNDLASAILRLRGDTRCYKADRARGEEASCISCYMKDNPGATEEDALSHINAVINDVIKGLNWELLNPNSSVPISSKKHVFDVSRALHYGYKYRDGYSVSNIETKSLVMRTLLESVPF
Protein: Homeobox protein DLX-2 (Homeobox protein TES-1) (P40764)
Organism: Mus musculus (Mouse)
Function: Acts as a transcriptional activator. Plays a role in terminal differentiation of interneurons, such as amacrine and bipolar cells in the developing retina. Likely to play a regulatory role in the development of the ventral forebrain. May play a role in craniofacial patterning and morphogenesis.
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
- Homeobox protein DLX-1
- Achaete-scute homolog 1
- Homeobox protein Meis2
- LIM/homeobox protein Lhx6
- Forkhead box protein G1
- T-box brain protein 1
- LIM/homeobox protein Lhx8
- Neurogenin-2
- Paired box protein Pax-6
- Glutamate decarboxylase 1
Sequence:
MTGVFDSLVADMHSTQITASSTYHQHQQPPSGAGAGPGGNSNSSSSNSSLHKPQESPTLPVSTATDSSYYTNQQHPAGGGGGGASPYAHMGSYQYHASGLNNVSYSAKSSYDLGYTAAYTSYAPYGTSSSPVNNEPDKEDLEPEIRIVNGKPKKVRKPRTIYSSFQLAALQRRFQKTQYLALPERAELAASLGLTQTQVKIWFQNRRSKFKKMWKSGEIPTEQHPGASASPPCASPPVSAPASWDFGAPQRMAGGGPGSGGGGAGSSGSSPSSAASAFLGNYPWYHQASGSASHLQATAPLLHPSQTPQAHHHHHHHHHAGGGAPVSAGTIF
Protein: Resuscitation-promoting factor RpfC (EC 3.-.-.-) (O07747)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: Factor that stimulates resuscitation of dormant cells. Has peptidoglycan (PG) hydrolytic activity. Active in the pM concentration range. Has little to no effect on actively-growing cells. PG fragments could either directly activate the resuscitation pathway of dormant bacteria or serve as a substrate for endogenous Rpf, resulting in low molecular weight products with resuscitation activity.
Interaction partners:
- Coenzyme Q-binding protein COQ10 START domain-containing protein
- Uncharacterized protein Rv1954A
- Secreted chorismate mutase
- Uncharacterized protein Rv1815
- Diacylglycerol acyltransferase/mycolyltransferase Ag85B
- Peptidoglycan endopeptidase RipA
Sequence:
MHPLPADHGRSRCNRHPISPLSLIGNASATSGDMSSMTRIAKPLIKSAMAAGLVTASMSLSTAVAHAGPSPNWDAVAQCESGGNWAANTGNGKYGGLQFKPATWAAFGGVGNPAAASREQQIAVANRVLAEQGLDAWPTCGAASGLPIALWSKPAQGIKQIINEIIWAGIQASIPR
Protein: Atypical kinase coq-8, mitochondrial (EC 2.7.-.-) (Q18486)
Organism: Caenorhabditis elegans
Function: Atypical kinase involved in the biosynthesis of coenzyme Q, also named ubiquinone, an essential lipid-soluble electron transporter for aerobic cellular respiration. Its substrate specificity is unclear: either acts as protein kinase that phosphorylates other proteins in the CoQ complex to stabilize their interactions or acts as a small molecule kinase that phosphorylates a prenyl lipid in the ubiquinone biosynthesis pathway.
Subcellular location: Mitochondrion {ECO:0000250|UniProtKB:Q8NI60}.
Interaction partners:
- Ubiquinone biosynthesis O-methyltransferase, mitochondrial
- 2-methoxy-6-polyprenyl-1,4-benzoquinol methylase, mitochondrial
- All trans-polyprenyl-diphosphate synthase PDSS1
- Ubiquinone biosynthesis protein coq-4, mitochondrial
- 4-hydroxybenzoate polyprenyltransferase, mitochondrial
- Ubiquinone biosynthesis monooxygenase COQ6, mitochondrial
- ABC1 atypical kinase-like domain-containing protein
- NADPH-dependent 3-demethoxyubiquinone 3-hydroxylase, mitochondrial
- ATP synthase subunit beta, mitochondrial
- ABC1 atypical kinase-like domain-containing protein
Sequence:
MAAKRPPASTLKWCQQEMGPICEGIGMVVRSQIGYDGRRIEKQIRRKALQTVVMGGQDVDPLKEPNKTNAPLLSPTLPSTNEALQRARVVAAGIETFAKLMSQGTYPGSAGFTVSETGERKYMKQTSPVQSNIVANLMATADKLSKGVISLAPFPLPTITKLGTWVIANPTAQLPIPPQLKSAIPAIGQIETLIQSILGVQGPVSSVSRAPRKLKLEGVTDQVVLEPETIHATVDVEPIDKTLTKEEAEFLIKAARSVDDDNAETAIFGTQKAKPKVYRPELPKNFEVNLEMGNVHTLTRSNESSVPATRIGRLATFGQLAFGLLGGATAEVTRRTFGIGKRLQEEGIPKNPFLSEANADRIVATLCRVRGAALKLGQMLSIQDSSTVPPALLQIFERVRQSADFMPIKQVHRQMKDAFGDDWREKFEHFDDKPFACASIGQVHKAVLKDGRNVAVKVQYPGVAEGIDSDIDNLVSVLSVGGIFPKGMFLDAFVGVARRELKQECDYEREARAMKKFRELIADWQDVYVPEVIDELSSSRVLTTELVYGKPVDACVEEPQVVRDYIAGKFIELCLKEIFLWRFMQTDPNWSNFFLGKHPKTGEPRLVLLDFGASRAYGKKFVDIYMNIIKSAYDGDKKKIIEYSREIGFLTGYETSVMEDAHVESVMIMGETLASNHPYNFANQDVTMRIQKLIPVMLEHRLTSPPEEIYSLHRKLSGCYLLAAKLKATVSCGGLFHEIHENYVFGEDGIDINID
Protein: 25-hydroxyvitamin D-1 alpha hydroxylase, mitochondrial (EC 1.14.15.18) (25-hydroxyvitamin D-1alpha-hydroxylase) (A0A097HUX0)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
Sequence:
MMMVLHQALKVTGRSALPLLRFAERWADVIRAPPTPQVKTLEQMPGPSPARFIRDLFMKRGFSRLHQLQLEGRQKYGPMWKASFGPILTVHVAEPELIQQVLRQEGQHPVRSELSSWKDYRALRGEGYGLLTAEGEEWQCVRSLLSKHMLRPQAVEAYDGALNAVVSDLLQKLKLRSQESSSRIVSDISAEFYRFGLEGISSVLFESRIGCLDAVVPVETERFIQSINTMFVMTLLTMAMPQWLHRLLPKPWDTFCRCWDVMFEFAKGHIDQRLQEEKQKLECGEQLEGRYLTYFLSQAGLPLTSVYSNVTELLLAGVDTISSTLSWSLYELSRHPDVQTALRDEVLSVMKDRSVPQASDVAAMPLLKAVVKEILRLYPVIPANARVINKDIEVGGYVIPKNTLITLCHYATSRDPQQFRDPDSFRPQRWGDRSDRSHPYATVPFGVGKRSCIGRRIAELEVYLALSRILMHFTMEPVRENDTVHPMTRTLLVPERQIDLRFTER
Protein: Alpha-tocopherol transfer protein (Alpha-TTP) (P41034)
Organism: Rattus norvegicus (Rat)
Function: Binds alpha-tocopherol, enhances its transfer between separate membranes, and stimulates its release from liver cells. Binds both phosphatidylinositol 3,4-bisphosphate and phosphatidylinositolphosphatidylinol 4,5-bisphosphate; the resulting conformation change is important for the release of the bound alpha-tocopherol (By similarity).
Subcellular location: Cytoplasm.
Interaction partners:
Sequence:
MAEMRPGPVVGKQLNEQPDHSPLVQPGLAELRRRAQEEGVPETPQPLTDAFLLRFLRARDFDLDLAWRLMKNYYKWRAECPELSADLHPRSILGLLKAGYHGVLRSRDPTGSRVLIYRISYWDPKVFTAYDVFRVSLITSELIVQEVETQRNGVKAIFDLEGWQISHAFQITPSVAKKIAAVVTDSFPLKVRGIHLINEPVIFHAVFSMIKPFLTEKIKGRIHLHGNNYKSSLLQHFPDILPLEYGGNESSMEDICQEWTNFIMKSEDYLSSISETIQ
Protein: F3H9.15 protein (Q9FZ93)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- At1g21010
- Basic-leucine zipper transcription factor K
- Uncharacterized protein At5g66580
- D-ribose-binding periplasmic protein
- HTH-type transcriptional regulator
- Uncharacterized protein At3g50800
- DUF4228 domain protein
- Uncharacterized protein At5g17350
- At5g67620
- Emb|CAB85509.1
Sequence:
MGHDNITKLGSLLVKLHKGPSSWLCLHPRPDRTSNGGRIKLVRSDGSLQVYDRPVVVSELTKDFPKHKICRSDLLYIGQKTPVLSETETLKLGLNYFLLPSDFFKNDLSFLTIATLKTPQNGGVLVKKTQQQPQPFLIQKGEKGERLRIRVSEEFVSELMMEGKKNRVNEEEEEEEGGGEGEGRVCTTVKLKKDYVQLVGLRRWKPKLETITETKAMKAATMEKTKKKRKRFTVMKKKSQSDSSSKRKLQSKSKSKTKKSIMRKID