wanglab/gogpt-training-data huggingface dataset:
Protein: Small ribosomal subunit protein mS23 (37S ribosomal protein S25, mitochondrial) (P40496)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Component of the mitochondrial ribosome (mitoribosome), a dedicated translation machinery responsible for the synthesis of mitochondrial genome-encoded proteins, including at least some of the essential transmembrane subunits of the mitochondrial respiratory chain. The mitoribosomes are attached to the mitochondrial inner membrane and translation products are cotranslationally integrated into the membrane.
Subcellular location: Mitochondrion {ECO:0000269|PubMed:11278769, ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:16823961}. Note=Mitoribosomes are tethered to the mitochondrial inner membrane and spatially aligned with the membrane insertion machinery through two distinct membrane contact sites, formed by the 21S rRNA expansion segment 96-ES1 and the inner membrane protein MBA1. {ECO:0000269|PubMed:25609543}.
Interaction partners:
- Small ribosomal subunit protein mS43
- Small ribosomal subunit protein bS18m
- Small ribosomal subunit protein mS35
- Small ribosomal subunit protein mS26
- Small ribosomal subunit protein mS47
- Small ribosomal subunit protein uS17m
- Small ribosomal subunit protein mS37
- Small ribosomal subunit protein mS45
- Small ribosomal subunit protein uS5m
- Small ribosomal subunit protein bS1m
Sequence:
MKIQTNAVNVLQRTSAYLKSGLLKETPAWYNVVASIPPSTKFTREPRFKNPSNGHIIGKLVDVTEQPHANNKGLYKTRPNSSDKRVGVKRLYRPPKLTYVEDRLRSLFYKQHPWELSRPKILVENEIGDENYDWSHMLQIGRPLDGESVIQRTMYLIKTKQYGDMVEAYDHARYEFYALRMQEETEQQVALEEAEMFGSLFGVSAIEHGIQKEQEVLDVWEKKVVEETELMAARTSNPAGSWKDDTTLNTAQEEESTTSENLHF
Protein: Heat shock protein Hsp20 (D0KNS6)
Organism: Saccharolobus solfataricus (strain 98/2) (Sulfolobus solfataricus)
Interaction partners:
Sequence:
MMNVIMREIGKKLDELSREFYESVIPPIDMYEEGGELVVVADLAGFNKDKISVRLSAQNELIINAEREIQYIGTKYATQRPLKIHKVIRLPVKVKRDSQVTAKYENGVLTIRIPVEGSVSIRIE
Protein: Large Forked protein (Q24341)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cell projection, stereocilium {ECO:0000256|ARBA:ARBA00004645}.
Interaction partners:
Sequence:
MHHPGSVSGSERPNGGALALHYAAARGCLDCVQLLVAASVDICANTQMDNDVTPVYLAAQEGHLEVRKFLVLEAGGSLYVRARDGMAPIHAASQMGCLDCLKWMVQDQGVDPNLRDGDGATPLHFAASRGHLSVVRWLLNHGAKLSLDKYGKSPINDAAENQQVECLNVLVQHGTSVDYNGKSSSQRHKSQQQLHQQHQQQQQQQQQQHLSSSCNSNSNSSKQTSRSNTIKSKSSSTLSSDVEPFYLHPPALAGGSGGSEMGLGMGMGMGMGMSMGLGISRKNSDALYSQQSRSSSEKLYNGSSSLGGNPGGNSSSGGGGVGGGGGSGGALLPNDGLYVNPMRNVGMYNTPSPNGSISGESFFLHDPQDIIYNRVRDLFVDSDCSSSVKQHGKSHAHQLLQSKAGNAMTIQADVHSSSSGAGSGSDESVSISSSFNSPKQQQQLRSQSFNRHGSSSNISASGNIKNNNYKAHKGKPSNQNGGGDHDYEDIYLVREESRKQHQQQQQHQLQQQQQLQHQATQQQQQQQQQQQQLQHKYNVGRSRSRDSGSHSRSASASSTRSTDIVLQYSNHHLNNKRNMNNNSNMNNSSSNIAQSSSSNNNNNSLLIRNKSHSIIGLHSSKYESSLKDNYSAKNVNLKNQLLNGGIKSDTYESVCPPEDVVERTKQTHKNSMIRNNLADASSNNNTSGSINNISNIGNMNGGNQSSRNLKRVSSAPPMQNLAVVNGPPPPPLPPPLRAPVQQQRNNLSVDQPNSMTGNNGIYKKNVFGPNQGPTNANGTGGAAPPPVPAPNPVATEAVDSDSGLEVVEEPSLRPSELVRGNHNRTMSTISANKKAKLLNAGSTNGSSIAASSDDSQSRYGGSVHAANGSAANGHFYGYSEGNKNQGSNGNGNGNGNGGGGNYHSHPNQPHYATGQPHQYTPSLYGGGSSAEDHYELTQQQQQIYGETHLAGGQRTGGPNLVNKQLVLPFVPPSFPNKSQDGVTHLIKPSEYLKSISIDKVRAHPPPAPRIRRTTCRYRSPSSRHPHQHQHHPHPHPHPHHPHQLHGMGEQPPLPPPPPPLPHGMLPPQPPMGPPMGVAGGQDATMSGKSHKPKKPHGSAPNSQDTATRKQHQPLSAISIQDLNSVQLRRTDTQKVPKPYQMPARSLSMQCLTSSTETYLKSDLIAELKISKDIPGIKKMKVEQQMASRMDSEHYMEITKQFSGNNYVDQIYLQIPERDQAGNAIPDWKRQMMAKKAAERAKKDFEERMAQEAESRRLSQIPQWKRDLLARREETENKLKAAIYTPKVEENNRVADTWRLKNRAMSIDNININLAGMEQHYQQIQFQQKQQQLQLGNKENHVDPKGADQDQEHGVGIGSGVGNANSGVIGGQELIDPSEGSQGRAEEEEDNIIPWRAQLRKTNSRLSLI
Protein: t-SNARE protein aex-4 (Aboc, expulsion defective protein 4) (G5EEN8)
Organism: Caenorhabditis elegans
Function: t-SNARE protein which regulates the secretion of aex-5 from intestinal cells. Involved in the defecation motor program, which is a coordinated series of three muscle contractions that occurs every 45 seconds.
Subcellular location: Cell membrane {ECO:0000269|PubMed:18852466}.
Interaction partners:
- Putative syntaxin-3
- Alpha-soluble NSF attachment protein
- Putative syntaxin 6
- t-SNARE coiled-coil homology domain-containing protein
- C2 domain-containing protein aex-1
- Vesicle-trafficking protein SEC22b
- Putative syntaxin-4
- Endoprotease aex-5
- G-protein coupled receptor aex-2
- t-SNARE coiled-coil homology domain-containing protein
Sequence:
MARKTIDSIPEPIALPTEETVQKRIKLKMVDLDAEIAKLNVQSLDSSIQMIRDIDQMNVDAVQTTAALEDQDEQLDKIEANLSNVIDDLNVVSHNITAMEHYCGCGFFRILRAPFKYFRKRERDIIKEEVLEKMTSPKLRRKEESNMMMFTNSSKRRESTGDFMKRLTCDAIEDELERNLMQIDQGLESVKNLAVDMHVQLKLQEPKLNRIEELTETNDFVVEGVNDKVKKLLH
Protein: Uncharacterized protein (Q57XK2)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MVYPFSKQPDHFRERRSLLLPLSLVAGSLFFGVRLYKWWSEYRESMEDEQLFGETSASPLLSLDGGFPPKVQSQTLSAREGSGFECSSGVLTQEERGEALRLARMLLGETPISDSSSLGSGESSDSGVTDVSLNYQIAVELEREARDSLTEAVVQGEVARAAARGRPLTLADYSTVLPLVVEYLEVSMDREELRARRAAKRLVDQQNGGLRFSSGAGRHGPDDFFINDVDEISRRVAQMRSADISKACADLFSRSEEMDRLLRAPANNRWDDCMEMDWGGDDEADLMAYLDQDDSAGYANRAEARVGAQLQRDLRTFDDEEMYDDDAQEEESEDLDDELEKADFERMLLSKLYLLAESVGMEDAACECRAKRHKEGEALGFGGGEPRQPDTVDDLEEDHLQISDDADSDTWETEGDFEEEEVESSGG
Protein: Proton-coupled zinc antiporter SLC30A5 (Solute carrier family 30 member 5) (Zinc transporter 5) (ZnT-5) (Q6DG36)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Function: Together with SLC30A6 forms a functional proton-coupled zinc ion antiporter mediating zinc entry into the lumen of organelles along the secretory pathway. By contributing to zinc ion homeostasis within the early secretory pathway, regulates the activation and folding of enzymes like alkaline phosphatases and enzymes involved in phosphatidylinositol glycan anchor biosynthesis.
Subcellular location: Golgi apparatus, Golgi stack membrane {ECO:0000250|UniProtKB:Q8TAD4}; Multi-pass membrane protein {ECO:0000255}. Cytoplasmic vesicle, COPII-coated vesicle membrane {ECO:0000250|UniProtKB:Q8TAD4}; Multi-pass membrane protein {ECO:0000255}. Cytoplasmic vesicle, secretory vesicle membrane {ECO:0000250|UniProtKB:Q8TAD4}; Multi-pass membrane protein {ECO:0000255}. Golgi apparatus, trans-Golgi network membrane {ECO:0000250|UniProtKB:Q8TAD4}; Multi-pass membrane protein {ECO:0000255}. Note=Enriched in early compartments of the secretory pathway including COPII-coated vesicles and the Golgi cis cisterna. {ECO:0000250|UniProtKB:Q8TAD4}.
Interaction partners:
- Zinc transporter 6
- Zinc transporter Slc39a7
- Proton-coupled zinc antiporter SLC30A9, mitochondrial
- Zinc transporter ZIP13
- Zinc transporter ZIP9
- Zinc transporter ZIP10
- Zinc transporter ZIP1
- Solute carrier family 39 member 6.
- Solute carrier family 39 member 8.
- Solute carrier family 39
Sequence:
MDEKYSSNVISSGKLGRVEAPNARLTRYIVLLYFTKMLKAFGIFESYDILKVVHIVQFLFILKMGCAVILVFFQKPFSSGKMIPKRQWIKILKHAVISCIISLLGFFGLTLCGPLRSLLLFEHSDLVVISLLSVLFTSSGGGPSKTRGAAFFIIAVICLLLFDNDDLMAKMAEHPEGHHDSALTHALYTGIAFLGVADHKGGVVLLVLALCLKVAFNTASRKLSVEIGGAKRLYALSNLVSAVVLLPWVIVLSATTESKVESWSGLIFPFAMIIFSVMILDFYVESICMAKLETSRCARYGAIFLFLNGLLLANFWTHPLTGQIRAISTTGQQSSTEHVLSGGVLVSACFFIMADSILSAPSSKGQKGTLVGYSPEGTPLYNFMGDALQHTSQSLPRFIKDSLKQILEEYDSRQIFYFLCLNLAFTFVELFYGVWTNSLGLISDGFHMLFDCSALVLGLFAALMTRWKATRIYSYGYGRVEILSGFINGLFLMVIAFFVFVESVTRLVDPPNINTDMLTPVSVGGLIVNLVGICAFSHAHSHGASKGSCSGHDHGHSHHGHGHSSMEHSHGGHGHSHGGHGHSHGHGHSHSSGGMNANMRGVFLHVLADTLGSVGVIISTILIRQFGWLIADPICSLFISTLIFLSVIPLLKDACEVLLLRMPPQHEKELNFALEKIQKIEGVLSYRDPHFWRHSASVIAGTIHLQLMSDVVEQRVIQQVSAVLKDAGVNNLTIQLEKEAYFQHMSGLSSGFHEVLTMTQQMESMKYYKDGTCIM
Protein: Candida glabrata strain CBS138 chromosome J complete sequence (Q6FNS8)
Organism: Candida glabrata (strain ATCC 2001 / BCRC 20586 / JCM 3761 / NBRC 0622 / NRRL Y-65 / CBS 138) (Yeast) (Nakaseomyces glabratus)
Interaction partners:
- Ubiquitin fusion degradation protein 1
- Nuclear protein localization protein 4
- Candida glabrata strain CBS138 chromosome A complete sequence
- Candida glabrata strain CBS138 chromosome H complete sequence
- Protein OS-9 homolog
- ERAD-associated E3 ubiquitin-protein ligase component HRD3
- RING-type E3 ubiquitin transferase
- Derlin
- Ubiquitin thioesterase OTU
- Derlin
Sequence:
MGEEHKPLLDGSGAEPTVEDSTATAILRRKKKDNTLIVDDATNDDNSVIAINSNTMDKLELFRGDSVLVKGKKRKDTVLIVLIDDELEDGACRINRVVRNNLRVRLGDLVSIHPCPDIKYASRISVLPIADTIEGITGNLFDVYLKPYFVEAYRPVRKGDHFVVRGGMRAVEFKVVDVEPEEYAVVAQDTIIHWEGEPINREDEENNMNEVGYDDIGGCRKQMAQIREMVELPLRHPQLFKAIGIKPPRGVLMYGPPGTGKTLMARAVANETGAFFFLINGPEVMSKMAGESESNLRKAFEEAEKNAPAIIFIDEIDSIAPKRDKTNGEVERRVVSQLLTLMDGMKARSNVVVIAATNRPNSIDPALRRFGRFDREVDIGIPDATGRLEVLRIHTKNMKLADDVDLETLAAETHGYVGADIASLCSEAAMQQIREKMDLIDLEEDEIDAEVLDSLGVTMDNFRFALGNSNPSALRETVVESVNVTWDDVGGLDEIKEELKETVEYPVLHPDQYTKFGLAPSKGVLFYGPPGTGKTLLAKAVATEVSANFISVKGPELLSMWYGESESNIRDIFDKARAAAPTVVFLDELDSIAKARGGSLGDAGGASDRVVNQLLTEMDGMNAKKNVFVIGATNRPDQIDPAILRPGRLDQLIYVPLPDEPARLSILKAQLRKTPLEPGLDLTAIAKATQGFSGADLSYIVQRAAKYAIKDSIEAHRESLAAAEAEVKTEGGDVDMTSEDVKKEPVETVDPVPYITREHFAEAMKTAKRSVSDAELRRYEAYSQQMKASRGQFSNFNFGDSNQGTTETGNDGNSGANFGSAGDDDDDLYS
Protein: Ferroptosis suppressor protein 1 (FSP1) (EC 1.6.5.-) (Apoptosis-inducing factor homologous mitochondrion-associated inducer of death) (AMID) (p53-responsive gene 3 protein) (Q8BUE4)
Organism: Mus musculus (Mouse)
Function: A NAD(P)H-dependent oxidoreductase that acts as a key inhibitor of ferroptosis (By similarity). At the plasma membrane, catalyzes reduction of coenzyme Q/ubiquinone-10 to ubiquinol-10, a lipophilic radical-trapping antioxidant that prevents lipid oxidative damage and consequently ferroptosis (By similarity). Acts in parallel to GPX4 to suppress phospholipid peroxidation and ferroptosis (By similarity). This anti-ferroptotic function is independent of cellular glutathione levels (By similarity). Also acts as a potent radical-trapping antioxidant by mediating warfarin-resistant vitamin K reduction in the canonical vitamin K cycle: catalyzes NAD(P)H-dependent reduction of vitamin K (phylloquinone, menaquinone-4 and menadione) to hydroquinone forms. Hydroquinones act as potent radical-trapping antioxidants inhibitor of phospholipid peroxidation and ferroptosis. May play a role in mitochondrial stress signaling. Upon oxidative stress, associates with the lipid peroxidation end product 4-hydroxy-2-nonenal (HNE) forming a lipid adduct devoid of oxidoreductase activity, which then translocates from mitochondria into the nucleus triggering DNA damage and cell death.
Subcellular location: Lipid droplet {ECO:0000250|UniProtKB:Q9BRQ8}. Cell membrane {ECO:0000250|UniProtKB:Q9BRQ8}; Lipid-anchor {ECO:0000305}. Cytoplasm {ECO:0000269|PubMed:26689472}. Mitochondrion membrane {ECO:0000269|PubMed:26689472}. Nucleus {ECO:0000269|PubMed:26689472}.
Interaction partners:
- Phospholipid hydroperoxide glutathione peroxidase GPX4
Sequence:
MGSQVSVDTGAVHVVIVGGGFGGIAAASQLQALNVPFMLVDMKDSFHHNVAALRASVESGFAKKTFISYSATFKDNFRQGKVIGIDLKNRMVLLQGGEALPFSHLILATGSTGPFPGKFNEVSCQQAAIQAYEDMVKQIQRSQFIVVVGGGSAGVEMAAEIKTEYPEKEVTLIHSRVPLADKELLPCVRQEVKEILLRKGVQLLLSERVSNLEELPRNEYREYIKVETDKGTEVATNMVIVCNGIKINSSAYRSAFESRLASNGALKVNEFLQVEGYSNIYAIGDCADTKEPKMAYHAGLHANVAVANIVNSMKQRPLKAYKPGALTFLLSMGRNDGVGQISGFYVGRLMVRLAKSRDLLISTSWKTMRQSPP
Protein: Tubulin tyrosine ligase-like 4A, isoform K (Tubulin tyrosine ligase-like 4A, isoform M) (M9NCT3)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MSKFQKAGASRRDSREVDGTVIIGRRDNSEDRTWQGQKYEKHVLKEKLPSNDLKADYLDNGWGGDPGSEDDYRDIKDSYDPVVVIDNGLEQVGVHRRYCRMTENTVLDGSGDTLINNNNNELKIMRKSTDQPMPRLPMTPKRAKGGTVSTKKPMPTVHRVLLYSTQSPRLGRKQQFSTQRLSVKQQSSKVLGAGDERQTVLLLEPEHKQEDHRSAIDFDRNDDFDEDDDLDNLSNFDESDTASVLSDTEDGYRAHAFKLTHSVDRFSSPQSTPSFLSSQSSEDDLKNPDSLLVPSLFPYVPPYLSFSSNTKRGPRVPPDLHRVLKWRITNIMPKVVRLILANSGMRMLKKTNDWMGVWGKHLKSPCFKAIRSYQKINHLPGSFRIGRKDSCWKNLQRQMGKHSNKEFGFMPRTYIIPNDLGALRRHWPKYAQRNTKWIIKPPASARGAGIRVINRWGQIPKRRPLIVQKYIERPLLINGSKFDLRLYVLVTSVNPLRVFMYHNGLARFASVKYSAKTDTLNDRCMHLTNYSINKFSSNYSKNEDVNACHGHKWTIKSLWTYLANRGVRTDCLWEALRSLVLRTILAGENGINSMIRANVESKYSCFELFGFDVILDSDLVPWLLEVNISPSLHSELPLDAHVKAPLVQGVLNTALYNVPPKLSLDKQKELAAEFSFPPGTQMCYDKRLYINYLSREEKIKHNTFTRKSMEDRNEYVDAILNNLTPDDVRCLIIAEDELARCAPLERIFPTDQTHKYLKYNDTPRYYNRLLDAWESRYANNRTEGIALLRDYCQNKYHLQVPTPPAKKVRSLFINSAEAFHKTHLNES
Protein: Spermine oxidase (EC 1.5.3.16) (B8A458)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
- Spermidine synthase
- Spermine synthase.
- Amine oxidase.
- Amine oxidase.
- Aldehyde dehydrogenase
- Aldehyde dehydrogenase
- S-adenosylmethionine decarboxylase proenzyme
- E3 ubiquitin-protein ligase MARCHF2
Sequence:
MQSCEISSDSTDDPLSSALHGHRQPRIVVIGAGLAGLAATKTLLENGFTNVTVLEASDRIGGRVQSIQHGKTTLELGATWIHGANGNPVYHLAEDNGLLEHTTEEERSVGRISLYAKNGVAHYQTNNGKRIPKDLVEEFSDLYNEVYELTQEFFQNGKPVGAESQNSVGIFTRDVVRKKIMLDPYDSESIRKLKLSMLQQYLKVESCESSSPNMDEVSLSEFGEWTEIPGAHHVIPTGFIKVVEILAQDIPSCVLHLSKPVRRVHWNCSSQDAEEFGDQVDHNQDQRPSPSPVCVECEDGERLLADHVILTASLGVLKKAHKTLFSPGLPQDKAQAIQKLGISTTDKIFLEFAEPFWSPECNSIQFVWEDEAQLESQAYPEELWYRKICSFDVLYPPERYGHMLSGWICGEEALRMERCDDETVAEICTELLRQFTGNQNIPKPRRILRSSWGSNPYIRGSYSFTRVGSSGRDVEKLAEPLPYIKNTKAPPLQVLFAGEATHRKYYSTTHGALLSGQREANRLMELYQYSCAETTKPNI
Protein: Meiotic drive suppressor wtf23 (A0A482AU60)
Organism: Schizosaccharomyces kambucha (Fission yeast)
Function: Acts as a suppressor component of the dual wtf meiotic drive system, and can suppress but not confer meiotic drive by compatible poisons. Wtf meiotic drive systems promote unequal transmission of alleles from the parental zygote to progeny spores by encoding a poison and an antidote from the same locus; the poison is trans-acting and forms toxic aggregates in all spores within an ascus, wherease the antidote is spore-specific and targets aggregates for degradation by the vacuole (By similarity). Meiotic drive by wtf systems therefore lead to poisoning of all progeny that do not inherit the dual poison/antidote allele, or express a compatible antidote (By similarity).
Subcellular location: Spore membrane {ECO:0000250|UniProtKB:A0A218N034, ECO:0000255}; Multi-pass membrane protein {ECO:0000255}. Vacuole membrane {ECO:0000250|UniProtKB:A0A218N034, ECO:0000255}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
Sequence:
MKNNYTSLKSPIDEEDELKTGHEIDLEKGLLPEYDSEEEGALPPYSDHARVSNPPNTHRENHSSGTTDDSSPFLIKLLISFTPIVLLNALAVWYLKYKDAFFKNYGAAEWTLFGFWCLVCTLVLIILTYFYETWTKAVKVTVIFLAQCIKVTAVFLAQCVKGLFNIRREMMIIIWILWLIICCILFGCVKDGRLNFNKALICSTCTISAVLFLIVSSVCIPIWTLWRALSGMLQVLGIHGIIAVLVNGSMSLFGKHFGWRGYEIEGFVLFFTSNALFLYEMERPGVLKRMRNTTGNVIGYICGGIEDAFRRIKNAFRGANDNNNIPLGEMDVEGEV
Protein: At4g18070 (Suppressor) (Q8VZS7)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
Sequence:
MPSGAKKRKAAKKKQEEEQQQQGSSTLINLKSNNHDSRSQGDKESDDGVNERIEITDSSHDHDKSSSSSSSSSSSSSSSSSDDESREVKKIDDDKKTGDDVSEVITVSSVPIQPVPIAADAPFMGFTANAIVENTGLMDSAVPNDPESGELVEISHVDTIVSNEADDNSLPKATEIAAEVALAFDEIRQTSSGATDSDVKENEGKTSPLPESNGVPEGNIESNVVISHEEEAPILIPTHGIAKRTSWFSCCGLFDVVTGSSR
Protein: Cytochrome b5 (Q7T341)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Endoplasmic reticulum membrane {ECO:0000256|ARBA:ARBA00004131}; Single-pass membrane protein {ECO:0000256|ARBA:ARBA00004131}; Cytoplasmic side {ECO:0000256|ARBA:ARBA00004131}. Microsome membrane {ECO:0000256|ARBA:ARBA00037877}; Single-pass membrane protein {ECO:0000256|ARBA:ARBA00037877}; Cytoplasmic side {ECO:0000256|ARBA:ARBA00037877}.
Interaction partners:
Sequence:
MANNGTDGNGVKYYRLSEVEERNSFKSTWIIIHNKVYDVTKFLEEHPGGEEVLREQAGGDATESFEDVGHSTDAREMASSMLIGEVHPDDRDKIAKPPESLVTTVQETTSWWSNWLIPAVAAVIVTLMYRIYTAEEA
Protein: Elongator complex protein 1 (Q9N595)
Organism: Caenorhabditis elegans
Subcellular location: Cytoplasm {ECO:0000256|PIRNR:PIRNR017233}. Nucleus {ECO:0000256|PIRNR:PIRNR017233}.
Interaction partners:
- Elongator complex protein 3
- Elongator complex protein 2
- Elongator complex protein 4
- Elongator complex protein 5
- Cytoplasmic tRNA 2-thiolation protein 1
- Tetraspanin-17
- Adenylyltransferase and sulfurtransferase MOCS3
- DNA replication licensing factor mcm-5
- Protein KTI12 homolog
- NUC153 domain-containing protein
Sequence:
MKNLQIGSVKTFENPEIAGADDFAVHPILQTIAVSTKNELLLLENNLISSTIKWAEQRRELEVISLSFRTDGNQIVVILADGRALIVEDGEVMDLEIAELTDTTVSAAEWTADEQTLALADNQTLYLADSSLVPFAERPLIFSENERKSAPVNVGWGSESTQFRGSAGKLKPGEKIEKEKEQIEQHSRKTSVHWRWDGEIVAVSFYSSQNDTRNLTVFDRNGEILNNMNIRNIYLSHCFAHKPNANLLCSAIQENGSDDRIVIYERNGETRNSYVVKWPANQIEDRRIIEKIEWNSTGTILSMQTSLGKKHQLEFWHLSNYEFTRKCYWKFSESIIWKWSTVECQNIEVLLESGQFFSVHITPTASFSDVISQNVVVATDELRMYSLCRRVVPPPMCDYSIQCLSDIVAYTTSTHHVHVITSDWKIISFSQDTDGYKFNSDRASIDEVLHTEVTEGIICGFVYDEPSESYIIWNVSHGKHQISRVGANPEKIFEGENIGWIGVNPSNKHVEIASNDGKFIDLNTKEELFKIDKFESTEVHFIQNHHVIQVDNSMLFLDSERVSQDAISILTRGSDILLIDFDNKLRFIDAESGKTLEDVRNVEAGCELVACDSQSANVILQAARGNLETIQPRRYVMAHTRDLLDRKEYIASFKWMKKHRVDMSFAMKYKGDDLEDDIPIWLKTSNDSQFLEQLLISCTEVFEDAGSSLCMTVARYVRDLSDAEKTKMFPLLLTALLRSKPSKVNDCLKEVQEHVEKIADRKDVFTRNSLHHISFFVPAKELFNCALSTYDLKLAQQVAEASNYDPKEYLPVLNKLNRVMCTLERQYRINVVREAWIDAVSSLFLLDSSKERGSEETWWNDIEDIIQREKLYQDALTLVKPGDRRYKQCCELYAAELERKVHWREAALFYELSGNSEKTLKCWEMSRDVDGLAASARRLAVDAGKLKIHAIKMSTTLREARQPKELAKALKLAGSSSTQIVHVLCDAFEWLDASREVEVGKEEALKKAALSRNDQVLMDLERRKTEFENYKKRLAVVRENKLKRVEQFAAGEVDDLRDDISVISSISSRSGSSKVSMASTVRRRKQIEKKKSSLKEGGEYEDSALLNVLSENYRWLENIGNELSQLILVLITVGNFPESLKLRSAYDEFATKLQKSKAAIWPESLSVQHLPGPLHALFDPNQEPSPIPMPPIFRLEPELVAPTSSFASVFP
Protein: Probable G-protein coupled receptor 142 (Q7TQN9)
Organism: Mus musculus (Mouse)
Function: Orphan receptor.
Subcellular location: Cell membrane; Multi-pass membrane protein.
Interaction partners:
- Glucose-dependent insulinotropic receptor
- Free fatty acid receptor 1
Sequence:
MHLNSNPNSYICDAYQHADLLWSLSPHVLTKAVQPQVTLLPTVNGSNPRYDGVDGHWPESPERSPCVAGIIPVIYYSVLLSLGLPVALARLAARTRKPSYHYLLALTASDIVTQVIIVFVGFLLQGAVLARQVPQAVVRTANILEFAANHASVWIAVLFTVDRYNALCRPLRHRATSSPGRTHRAIAAVIGVTLLTGIPFYWWLDVWRDADPPSTMDKLLKWAHCLIVYFIPCNVFLVTNSAIILRLRKRGQRGLRPLVSKSTAILLGVTSLFALLWAPRIIVMLYHLYVAPVHRDWRVHLALDIANMLAMLNTEVNFGLYCFISKTFRATVRQVICDVHMACALKSQPKQTVVELMLKSVGTEL
Protein: Nucleolar transcription factor 1 (Upstream-binding factor 1) (UBF-1) (P25976)
Organism: Mus musculus (Mouse)
Function: Recognizes the ribosomal RNA gene promoter and activates transcription mediated by RNA polymerase I through cooperative interactions with the transcription factor SL1/TIF-IB complex. It binds specifically to the upstream control element.
Subcellular location: Nucleus, nucleolus {ECO:0000269|PubMed:20168301}.
Interaction partners:
- DNA-directed RNA polymerase I subunit RPA49
- DNA-directed RNA polymerase I subunit RPA2
- DNA polymerase iota
- RNA polymerase I-specific transcription initiation factor RRN3
- Stromelysin-1
- TATA-box-binding protein
- DNA-directed RNA polymerase I subunit RPA1
- NAD-dependent protein deacetylase sirtuin-7
- Transcriptional repressor CTCF
- rRNA 2'-O-methyltransferase fibrillarin
Sequence:
MNGEADCPTDLEMAAPKGQDRWSQEDMLTLLECMKNNLPSNDSSKFKTTESHMDWEKVAFKDFSGDMCKLKWVEISNEVRKFRTLTELILDAQEHVKNPYKGKKLKKHPDFPKKPLTPYFRFFMEKRAKYAKLHPEMSNLDLTKILSKKYKELPEKKKMKYIQDFQREKQEFERNLARFREDHPDLIQNAKKSDIPEKPKTPQQLWYTHEKKVYLKVRPDATTKEVKDSLGKQWSQLSDKKTLKWIHKALEQRKEYEEIMRDYIQKHPELNISEEGITKSTLTKAERQLKDKFDGRPTKPPPNSYSLYCAELMANMKDVPSTERMVLCSQQWKLLSQKEKDAYHKKCDQKKKDYEVELLRFLESLPEEEQQRVLGEEKMLNINKKQTTSPASKKPSQEGGKGGSEKPKRPVSAMFIFSEEKRRQLQEERPELSESELTRLLARMWNDLTEKKKAKYKAREAALKAQSERKPGGEREDRGKLPESPKRAEEIWQQSVIGDYLARFKNDRVKALKAMEMTWNNMEKKEKLMWIKKAAEDQKRYERELSEMRAPPAATNSSKKMKFQGEPKKPPMNGYQKFSQELLSNGELNHLPLKERMVEIGSRWQRISQSQKEHYKKLAEEQQRQYKVHLDLWVKSLSPQDRAAYKEYISNKRKNMTKLRGPNPKSSRTTLQSKSESEEDDDEEEEDDEEEEEEEEDDENGDSSEDGGDSSESSSEDESEDGDENDDDDDDEDDEDDDDEDEDNESEGSSSSSSSSGDSSDSGSN
Protein: (Lyso)-N-acylphosphatidylethanolamine lipase (EC 3.1.1.-) (Alpha/beta hydrolase domain-containing protein 4) (Abhydrolase domain-containing protein 4) (Alpha/beta-hydrolase 4) (Q8TB40)
Organism: Homo sapiens (Human)
Function: Lysophospholipase selective for N-acyl phosphatidylethanolamine (NAPE). Contributes to the biosynthesis of N-acyl ethanolamines, including the endocannabinoid anandamide by hydrolyzing the sn-1 and sn-2 acyl chains from N-acyl phosphatidylethanolamine (NAPE) generating glycerophospho-N-acyl ethanolamine (GP-NAE), an intermediate for N-acyl ethanolamine biosynthesis. Hydrolyzes substrates bearing saturated, monounsaturated, polyunsaturated N-acyl chains. Shows no significant activity towards other lysophospholipids, including lysophosphatidylcholine, lysophosphatidylethanolamine and lysophosphatidylserine.
Interaction partners:
- Glycerophosphodiester phosphodiesterase 1
- N-acyl-phosphatidylethanolamine-hydrolyzing phospholipase D
- Lysophosphatidylserine lipase ABHD12
- Monoglyceride lipase
- Monoacylglycerol lipase ABHD6
- Fatty-acid amide hydrolase 1
- Diacylglycerol lipase-alpha
Sequence:
MADDLEQQSQGWLSSWLPTWRPTSMSQLKNVEARILQCLQNKFLARYVSLPNQNKIWTVTVSPEQNDRTPLVMVHGFGGGVGLWILNMDSLSARRTLHTFDLLGFGRSSRPAFPRDPEGAEDEFVTSIETWRETMGIPSMILLGHSLGGFLATSYSIKYPDRVKHLILVDPWGFPLRPTNPSEIRAPPAWVKAVASVLGRSNPLAVLRVAGPWGPGLVQRFRPDFKRKFADFFEDDTISEYIYHCNAQNPSGETAFKAMMESFGWARRPMLERIHLIRKDVPITMIYGSDTWIDTSTGKKVKMQRPDSYVRDMEIKGASHHVYADQPHIFNAVVEEICDSVD
Protein: CAR1 transcription factor (CRTF) (CAR1-binding factor) (Q54YU6)
Organism: Dictyostelium discoideum (Social amoeba)
Function: Nuclear transcription factor with zinc-dependent sequence binding specificity. Required for carA-1 and carA-2 expression in early development. Also required throughout later developmental stages - where it has a cell-autonomous role that is distinct from its capacity to control carA-1 and carA-2 expression. Required for terminal spore differentiation but not essential for cell differentiation and cell sorting. May function to help insulate distinct pathways from simultaneous and universal activation by cAMP.
Subcellular location: Nucleus {ECO:0000269|PubMed:11493573, ECO:0000269|PubMed:9716534}.
Interaction partners:
- Myb domain-containing protein
Sequence:
MSSIEQLYSTTQFPSLSSCNTNINNTNNNNNINNINNNTNINTGNLLKNTFFKNNIIYNTNNNSINNNSNNNIINNNNNNLLNSNNQNSFQNQNNLNSIHNHNNNNNNNNSNNNNTSNSENLDSLKSALLSSNIFNGSSSSIAHQNLINLIISSQNNNNNNGNSNSNTPDQKSTMADILLNSSVPDYFEWCSDIINMPKDGNEKSNNSNGGNNNGNNNGNNNNNHNNNNNNNSNNNNNNNSDSVPSPQNNYQSPQSDNQSSMVPSFNFSNQNSANSSNNNNNNNGSSNNNNNVRSEPTTPNDESNNNSNNTNNNNNNNNNNNNNQQQQLSSNQNSSPLIYSVPSYYVPNYGVVLSAPMKGNSSSSILPPQAWPQNNNNNNGNSNSNNGNNNASGFSDFMFNGSNIDYNSIMNNNNNNNNNNNNNNNNNNNNNNNSNNNNNNSNNNNGNNGGMFNGGFVNNNNHNNNNNNNNNNGNLNFHNFLQFQNQLQNSNQQQQQQQLQQQQQLQQHQQQQQQLQQQQLQQQFNIGKPCNINQKKGRGANNNNNNMPIGNQASLVISHPSLKMEGHHHLQQQQQQQHHHQHQQHQQNGNGNNTQIVNSAFLDLSSPDSHNQMSPSSPICLPESPMGAQHWESGLDPSSLQKQNEINPPISVRSNVVFFEPYLAGEPGRHKACWNLLEPMHRNYYQPIQFKLPSFPDTSLPITQIDDKTGIFDSQRFLAFNNPQAMSKYESYRIYIHPSLGYSGNAKRFKQQPDVNEKALILDGNVYDGHLNPIYNCKICTEYYQTKSYFSANPHAKGKVLLVKNNILTRVKDGGFTLSLKPMCCSGHNSHIPLYFHFTLTNPLTNEVVLQSLINVNVKQWKKSVPNKSKKQRFE