wanglab/gogpt-training-data huggingface dataset:
Protein: Lid2 complex component jmj3 (Lid2C component jmj3) (O94691)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
- Lid2 complex component lid2
- Lid2 complex component snt2
- Set1 complex component ash2
- Set1 complex component sdc1
- JmjC domain-containing protein 1
- JmjC domain-containing protein 4
Sequence:
MQQNVKEKHAGKSDTSVSSLECEIDYHIEGSDGIPVVEPKISEFVDMESFIRRVERLGKKYGAIKVVRPSSVLNPWNEDTMKPSDVKMDLWLERMVRRKGEYFEIQSDIDHGSAGPKKPTDMNVDDRFPSNAGSSNDFENNVAKAIAYYWRSLTHDSLWYGYTNRPSIPFYFIPSISAAQKDRVHLRSNTLINTWPNVGHLFAGKWKTTLPWRVESPELHAVQVHLGGSSLQWYVIPSAHSESFKKLAGKLAQDEHWRCSDFLLHQNILFPPSTLVQNGIVTYSTVLKQDELLITFPGTHHSAFCLGDAVLRRFVFRSPRSASNYEFSNLRRLMVSESLYSSKSLWPHSHKPQRACSQKFLDEFYLHDLPESNIHDSGNFHPIHSSVDNNSFSQRDFDSPNSINPPSPLMSNHESASTEHFNSTTTTEKELSSLHVGEERKNRSLPLSLIWNSKAREEYIKKQKEENGDNIEFSHFDPLYTRPSSHPLHPPPILGLPVPAQFARGELFLGRILEDRVSEHMLLLECEKSDVVEVPYECILTSSSAAGRRESSYYNPALKAPNIVYDDGVPINWNEYSELPSLDRFVLPKLLPGKPIEFTPPISVEPTSIKTIAAEESSEPTSSVDVAPTPVEDVNVNLESISNTNESVVDLSDPLVSKNGFEDVERSSVADLEEDVLETRSSIFETSDIDDRLTVIDRSQSVVPSESEFSIAGANLTRRNAVDFSVSLDTYELYVSDEVENVDDFSLFPSLE
Protein: DNA-directed RNA polymerase II subunit RPB11 (RNA polymerase II subunit B11) (DNA-directed RNA polymerase II 13.3 kDa polypeptide) (DNA-directed RNA polymerase II subunit J) (Q9VJE4)
Organism: Drosophila melanogaster (Fruit fly)
Function: DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. Component of RNA polymerase II which synthesizes mRNA precursors and many functional non-coding RNAs. Pol II is the central component of the basal RNA polymerase II transcription machinery. It is composed of mobile elements that move relative to each other. RPB11 is part of the core element with the central large cleft (By similarity).
Subcellular location: Nucleus {ECO:0000250}.
Interaction partners:
- DNA-directed RNA polymerase II subunit RPB7
- DNA-directed RNA polymerase II subunit RPB9
- DNA-directed RNA polymerase II subunit RPB3
- DNA-directed RNA polymerases I, II, and III subunit RPABC3
- DNA-directed RNA polymerases I, II, and III subunit RPABC1
- DNA-directed RNA polymerases I, II, and III subunit RPABC5
- DNA-directed RNA polymerases I, II, and III subunit RPABC2
- DNA-directed RNA polymerases I, II, and III subunit RPABC4
- DNA-directed RNA polymerase II subunit RPB2
- DNA-directed RNA polymerase II subunit RPB1
Sequence:
MNAPPTFESFLLYEGEKKIIKELDTKVTNAAIFTINKEDHTLGNMIRNQLLKDPNVLFAGYKVPHPLEHKFVIRIQTTADYSPQEAFMNAITDLLAELSLFEERFKDAIKEKKEGGD
Protein: Ly49 inhibitory receptor 2 (A0A0G2K3K6)
Organism: Rattus norvegicus (Rat)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004606}; Single-pass type II membrane protein {ECO:0000256|ARBA:ARBA00004606}.
Interaction partners:
Sequence:
MSKQDVPCSTVRFKKSSGLRYQVRPEDTQRPREAGCRVPWQLTVIAIGIILSLRLVAVAILVTNIFQYSNEKHELQKTQNRQHNCSTMEKDINLKEETLRNMSVESVHYNALLDLINREQNRWYKKTKTVLASPQHTGGCDEMHWFCYGIKCYYFTMDIRIWHECKQTCQNYSLSFLKIDDKDELKFLQDHIIRDNYWIGSSYNNKKKEWSWIDNSPFNLDFVARNSLRKTGYCMYFSMAGLHDDDCGKRYLCICEKGMDKIPAPLCSVKETSHSAV
Protein: Low-density lipoprotein receptor-related protein 8 (LRP-8) (Apolipoprotein E receptor 2) (Q924X6)
Organism: Mus musculus (Mouse)
Function: Cell surface receptor for Reelin (RELN) and apolipoprotein E (apoE)-containing ligands. LRP8 participates in transmitting the extracellular Reelin signal to intracellular signaling processes, by binding to DAB1 on its cytoplasmic tail. Reelin acts via both the VLDL receptor (VLDLR) and LRP8 to regulate DAB1 tyrosine phosphorylation and microtubule function in neurons. LRP8 has higher affinity for Reelin than VLDLR. LRP8 is thus a key component of the Reelin pathway which governs neuronal layering of the forebrain during embryonic brain development. Binds the endoplasmic reticulum resident receptor-associated protein (RAP). Binds dimers of beta 2-glycoprotein I and may be involved in the suppression of platelet aggregation in the vasculature. Highly expressed in the initial segment of the epididymis, where it affects the functional expression of clusterin and phospholipid hydroperoxide glutathione peroxidase (PHGPx), two proteins required for sperm maturation. May also function as an endocytic receptor. Not required for endocytic uptake of SEPP1 in the kidney which is mediated by LRP2. Together with its ligand, apolipoprotein E (apoE), may indirectly play a role in the suppression of the innate immune response by controlling the survival of myeloid-derived suppressor cells.
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:Q14114}; Single-pass type I membrane protein {ECO:0000255}. Secreted {ECO:0000269|PubMed:12426372, ECO:0000269|PubMed:12871934}. Note=Isoforms that contain the exon coding for a furin-type cleavage site are proteolytically processed, leading to a secreted receptor fragment. {ECO:0000269|PubMed:12426372, ECO:0000269|PubMed:12871934}.
Interaction partners:
- Reelin
- Apolipoprotein E
- Disabled homolog 1
- Very low-density lipoprotein receptor
- Spondin-1
- Clusterin
- Beta-2-glycoprotein 1
- C-Jun-amino-terminal kinase-interacting protein 2
- C-Jun-amino-terminal kinase-interacting protein 1
- Thrombospondin-1
Sequence:
MGRPELGALRPLALLLLLLLQLQHLSAADPLPGGQGPVKECEEDQFRCRNERCIPLVWRCDEDNDCSDNSDEDDCPKRTCADSDFTCDNGHCIPERWKCDGEEECPDGSDESKATCSSEECPAEKLSCGPTSHKCVPASWRCDGEKDCEGGADEAGCPTLCAPHEFQCSNRSCLASVFVCDGDDDCGDGSDERGCSDPACPPREFRCGGGGTCIPERWVCDRQFDCEDRSDEAAELCGRAGQGTTATPAACAPTAQFTCRSGECIHLGWRCDGDRDCKDKSDEADCSPGPCRENEFQCGDGTCVLAIKRCNQERDCPDGSDEAGCLQESTCEGPRRFQCKSGECVDGGKVCDDQRDCRDWSDEPQKVCGLNECLHNNGGCSHICTDLKIGFECTCPAGFQLLDQKTCGDIDECQDPDACSQICVNYKGYFKCECHPGYEMDTLTKNCKAVAGKSPSLIFTNRHEVRRIDLVKRDYSRLIPMLKNVVALDVEVATNRIYWCDLSYRKIYSAHMDKASIPDEQVVLIDEQLHSPEGLAVDWVHKHIYWTDSGNKTISVATTDGRRRCTLFSRELSEPRAIAVDPLRGFMYWSDWGFQAKIEKAGLNGADRQTLVSDNIEWPNGITLDLLSQRLYWVDSKLHQLSSIDFNGGNRKMLIFSTDFLSHPFGVAVFEDKVFWTDLENEAIFSANRLNGLEIAILAENLNNPHDIVIFHELKQPKAADACDLSAQPNGGCEYLCLPAPQISSHSPKYTCACPDTMWLGPDMKRCYRAPQSTSTTTLASAMTRTVPATTRAPGTTIHDPTYQNHSTETPSQTAAAPHSVNVPRAPSTSPSTPSPATSNHSQHYGNEGSQMGSTVTAAVIGVIVPIVVIALLCMSGYLIWRNWKRKNTKSMNFDNPVYRKTTEEEEEDELHIGRTAQIGHVYPAAISNYDRPLWAEPCLGETRDLEDPAPALKELFVLPGEPRSQLHQLPKNPLSELPVVKCKRVALSLEDDGLP
Protein: Ubiquitin carboxyl-terminal hydrolase, putative (EC 3.1.2.15) (Q382V7)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- Small ribosomal subunit protein uS5
- Ribosomal protein L11, putative
- Large ribosomal subunit protein uL3m
- Large ribosomal subunit protein bL21m
- Polyubiquitin, putative
- KOW domain-containing protein
- 40S ribosomal protein S18, putative
Sequence:
MLSSSSPVLVSEQTCDKVDYGMELMPGKRLNTPVETPVIICPLYNLGNTCYFNAGVQLLVNCPQFVYCLRDSLFRHPEHHRYAERVSRSCGKAALELFEAFTQLVNDMEFTQLEPDCAISPLRALECLSAVHPLFEGREQQDCPEMVNAVIANVAEVGRQEIELDNLLKSFEGDYLCLEKAMGCRRGDTSFVPMRCTRQRMEFDEISLQSGSLYGSDQMNRNGAASANHEQNENGSENNHFTTSAQTHNAPQFPVFPGSWWNFNTMRINQFVNRENRLLQLQEDSKNGKLPQSTFRPPKIFYNSVTDGFTGQILSEIRCHTCQRSSRIVESFSSLTIGIPSPRQRLQYAKKHPEVQRVKQDGTPQNLARSLYWRSVFSWFYAATRWIVGLFTGFSRRGNCPVTLQECLDIHFEPVELKGSNMYHCSTCNAKREATKQETLLTMPEYLLLHMKRFEQGKCFNTKKTDEVIFPMSWDVGAAQSTDVLRLRNYLDSNVLAFNYPLSTFHGTTSAGDSTPMENSTSVTTPLTATNDHQKFAAASSSPLQSMQTRENPDIEAPIDTYTLEAVVNHHGTIARGHYTTFARKKTASKDVWVYLNDEELSTTTADSVANSEEYLLLYKKQSLFPRSEAFEKLRTKARELLAKPLSSRMGLDAAGVDKSSRNPNSNTNLSISGGGDGCHDVVYISRPWLQRMTFMEEPGPILNRLSYRAATQETGESSSAHGTQSSPKQNLGEPTSAKGPPYEKSLPVEWFYVSLLQQEYDAFYDMYGGNQAVTQSEYNLMMSEQDALV
Protein: Glutamate synthase [NADH] (EC 1.4.1.14) (Glutamine-oxoglutarate aminotransferase) (GOGAT) (Q9C102)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Forms L-glutamate from L-glutamine and 2-oxoglutarate. Represents an alternative pathway to L-glutamate dehydrogenase for the biosynthesis of L-glutamate. Participates with glutamine synthetase in ammonia assimilation processes. The enzyme is specific for NADH, L-glutamine and 2-oxoglutarate.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16823372}.
Interaction partners:
- NADP-specific glutamate dehydrogenase
- Probable NADPH:adrenodoxin oxidoreductase, mitochondrial
- Glutamine synthetase
- Probable NAD-specific glutamate dehydrogenase
- Putative glycine dehydrogenase
- Probable isocitrate dehydrogenase, mitochondrial
- Carbamoyl phosphate synthase arginine-specific large chain, mitochondrial
- Multifunctional protein ura1
- Carbamoyl phosphate synthase arginine-specific small chain
- Probable glutamine--fructose-6-phosphate aminotransferase
Sequence:
MAVLSSVQPINHNSALVEARDEQVNTTACSDDLLNAPPYEYDTEGNPSWAGALPKAQALYDPAYEKDSCGVGFTCHIKGQVSHKIVTDARLLLCNMTHRGATGADTRDGDGAGVMTGMPYTFMQKEFGQIGCTLPKSGEYAIGNVFFSPEADVCREAMTAFTQVAEKLGLAILAWRSVPCDNSILGPAALSREPTILQPCVVLKAAYDGEAEFDTDLFERQLYVLRKQSSHLIGKEKWFYICSLHRETIVYKGQLAPVQVYNYFLDLNNAEYVSHFALVHSRFSTNTFPSWDRAQPMRLAAHNGEINTLRGNKNWMHAREGLMKSSRFGEEFASLLPIIERGGSDSAAFDNVIELLCASGVVSLPEAVMLLIPEAWQNDKNISDEKAAFYEWAACQMEPWDGPALFTFADGRYCGANLDRNGLRPCRFYLTSDDMMICASEVGTVGIEPDRIVQKGRLYPGRMLLVDTKEGRIVDDKELKHNIASRYDFRSWLDQELIDMNSIVDSLIESTSVDLTPIVDDVPLADDKTMLAFGYTLEQINMIMAPMANGGKETLGSMGNDAAIACLSDQPRLLYDYFRQLFAQVTNPPIDPIREAIVMSLQCYIGPSGNLLEINQSQCRRLRMPTPILTVEEFNALKNVDRIYPDWKVASIDITFFKSEGVAGYAAAIERICSEADTAVNEGYKAIVLSDRNVNSERVPLASIAACGAVHHYLVQNKLRSRVALVCESGDAREVHHMCTLLGYGADAVCPYLAMEALTKLVRQNAMKPGITEETAIKNFKHAINGGILKVMSKMGISTLQSYKGAQIFEALGIDNEVINKCFLGTASRIRGVTFEHIALDAFALHERGYPTDQSIRSLQIPDMGDFYYRDGGEQHVNHPKAIASLQDAVRNKNEAAYAEFSRTHYEQTRRCTLRGMLDFDFDSSQAIPIEQVEPWTEIVRRFCTGAMSYGSISMESHSSLAIAMNRLGGKSNTGEGGEDPARSQRLANGDTMRSAIKQIASGRFGVTSWYLSDADELQIKMAQGAKPGEGGELPGNKVSESIAKTRHSTAGVGLISPPPHHDIYSIEDLKQLIYDMKSANPRARVSVKLVSEVGVGIVASGVAKAKADHILVSGHDGGTGASRWTGIKYAGLPWELGVAETHQTLVLNDLRGRVVIQTDGQIRTGRDVAIACLLGAEEWGFATTPLIALGCIMMRKCHLNTCPVGIATQDPELRKKFEGQPEHVVNFFYYVAEELRGIMAKLGFRTINEMVGRSDKLKVAEPINNKSKLLDLTPLLTPAFTLRPGAATYNVRKQDHRLYTRLDNKLIDEAEVTLEEGIPSVVECEIINTDRTLGATLSNKISKRYGEEGLPTDSIRVNVFGSAGQSFGAFLAPGVTLQLEGDCNDYVGKGLSGGRLIIYPPRVSPFKPEENMIIGNVCLYGATSGHAFISGVAAERFAVRNSGAIAVVEGVGDHGCEYMTGGRVVILGSTGRNFAAGMSGGIAYVYDMQMDFAGKINTEMVDISSVTDAAEIAFLRGLIQDHRHYTGSQVADRILSDFPRHLSRFVKVLPREYKAVLEREAAKKEEAKRLQYPKAFMPGNPIRQQIEETNAQIADVEDTLGATVKKSAPLDKLRGFMKYQRRSEHYRNPLKRTNDWKELSVRLREDELRVQTARCMDCGTPFCQSDYGCPISNKIFTWNDLVFKQQWKEALTQLLLTNNFPEFTGRVCPAPCEGACTLGIIESPVGIKSVERAIIDKAWEEGWIVPRPPAERTGRRVAIIGSGPAGLAAADQLNRAGHHVVIYERADRPGGLLQYGIPNMKLDKKVVERRIQLMIDEGIEVLTNVEVGKNGDVSLDELHKVYDAVVLASGSTVPRDLPIPNRDSKGIHFAMEFLHKNTKSLLDSELKDGNYISAKGKDVIVIGGGDTGNDCLGTSVRHGAKSVRNLELLPIPPRERAFDNPWPQYPRVFRVDYGHAEVQAHYGQDFREYSILTKSFEKDEDGNVKGINTVRIEWTKNSKGRWIMKEIRNSEEFFPADLVILALGFLGPEEQATAGMNVDRDARSNISTPTKSYETSVPGIYAAGDCRRGQSLVVWGIQEGRQCAREIDLKFQGKTFLPGDGGLVKRTVNC
Protein: Palmitoyltransferase ZDHHC17 (EC 2.3.1.225) (Acyltransferase ZDHHC17) (EC 2.3.1.-) (DHHC domain-containing cysteine-rich protein 17) (DHHC17) (Huntingtin yeast partner H) (Huntingtin-interacting protein 14) (HIP-14) (Huntingtin-interacting protein 3) (HIP-3) (Huntingtin-interacting protein H) (Putative MAPK-activating protein PM11) (Putative NF-kappa-B-activating protein 205) (Zinc finger DHHC domain-containing protein 17) (Q8IUH5)
Organism: Homo sapiens (Human)
Function: Palmitoyltransferase that catalyzes the addition of palmitate onto various protein substrates and is involved in a variety of cellular processes. Has no stringent fatty acid selectivity and in addition to palmitate can also transfer onto target proteins myristate from tetradecanoyl-CoA and stearate from octadecanoyl-CoA (By similarity). Palmitoyltransferase specific for a subset of neuronal proteins, including SNAP25, DLG4/PSD95, GAD2, SYT1 and HTT. Also palmitoylates neuronal protein GPM6A as well as SPRED1 and SPRED3. Could also play a role in axonogenesis through the regulation of NTRK1 and the downstream ERK1/ERK2 signaling cascade (By similarity). May be involved in the sorting or targeting of critical proteins involved in the initiating events of endocytosis at the plasma membrane. May play a role in Mg(2+) transport. Could also palmitoylate DNAJC5 and regulate its localization to the Golgi membrane (By similarity). Palmitoylates CASP6, thereby preventing its dimerization and subsequent activation.
Subcellular location: Golgi apparatus membrane {ECO:0000269|PubMed:15603740, ECO:0000269|PubMed:18794299}; Multi-pass membrane protein {ECO:0000255}. Cytoplasmic vesicle membrane {ECO:0000269|PubMed:18794299}; Multi-pass membrane protein {ECO:0000255}. Presynaptic cell membrane {ECO:0000269|PubMed:18032660}; Multi-pass membrane protein {ECO:0000255}. Note=Low extracellular Mg(2+) induces increase in Golgi and in post-Golgi membrane vesicles. {ECO:0000269|PubMed:18794299}.
Interaction partners:
- Huntingtin
- Synaptosomal-associated protein 25
- DnaJ homolog subfamily C member 5
- Paralemmin-1
- Synaptosomal-associated protein 23
Sequence:
MQREEGFNTKMADGPDEYDTEAGCVPLLHPEEIKPQSHYNHGYGEPLGRKTHIDDYSTWDIVKATQYGIYERCRELVEAGYDVRQPDKENVTLLHWAAINNRIDLVKYYISKGAIVDQLGGDLNSTPLHWATRQGHLSMVVQLMKYGADPSLIDGEGCSCIHLAAQFGHTSIVAYLIAKGQDVDMMDQNGMTPLMWAAYRTHSVDPTRLLLTFNVSVNLGDKYHKNTALHWAVLAGNTTVISLLLEAGANVDAQNIKGESALDLAKQRKNVWMINHLQEARQAKGYDNPSFLRKLKADKEFRQKVMLGTPFLVIWLVGFIADLNIDSWLIKGLMYGGVWATVQFLSKSFFDHSMHSALPLGIYLATKFWMYVTWFFWFWNDLNFLFIHLPFLANSVALFYNFGKSWKSDPGIIKATEEQKKKTIVELAETGSLDLSIFCSTCLIRKPVRSKHCGVCNRCIAKFDHHCPWVGNCVGAGNHRYFMGYLFFLLFMICWMIYGCISYWGLHCETTYTKDGFWTYITQIATCSPWMFWMFLNSVFHFMWVAVLLMCQMYQISCLGITTNERMNARRYKHFKVTTTSIESPFNHGCVRNIIDFFEFRCCGLFRPVIVDWTRQYTIEYDQISGSGYQLV
Protein: Cox19-like CHCH family protein (F4JPC0)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
Sequence:
MNSDGLYGPLKILFFFESSPPRSWVIRLTGNIFVSLRNPSLGFIPSMEKQSTQPICGQEALQLLNCVAESPFDQEKCVRFLQSLRECVLSKKVKKFSIPSQDHDSEGAASATKRPS
Protein: Polyketide synthase PltB (Q4KCY9)
Organism: Pseudomonas fluorescens (strain ATCC BAA-477 / NRRL B-23932 / Pf-5)
Interaction partners:
- AMP-binding enzyme
- NADH-quinone oxidoreductase subunit C/D
- Non-ribosomal peptide synthetase PvdL
- L-cysteine--[L-cysteinyl-carrier protein] ligase
- Non-ribosomal peptide synthetase PvdJ
- Non-ribosomal peptide synthetase OfaB
- Non-ribosomal peptide synthetase PvdD
- Non-ribosomal peptide synthetase OfaC
- Non-ribosomal peptide synthetase OfaA
- L-cysteine--[L-cysteinyl-carrier protein] ligase
Sequence:
MDARAPMDFEPIAIIGSGCRFAKGASTPEAFWELLRAGTDFVGPVPAERWDTAAIYDESAAETGTTYSKVGAFLEHIDRFDAHYFGISASEAKEMDPQQRLLLEVACESVARAGLTREQLKGSRTAVYVGMLGMDYLALHSREAGIEQINPYYAAGKEFSFAAGRIAYHLGVHGPAMTVTTACSSSLVAMHLACRALQAGEADMALAGGVNLMLAPDLTIYMSQIRAISPSGRCRVFDAAADGIVRGEGCGVTVLKRLADALRDGDPIQAVIRGSAINQDGASAGQTVPNANAQAAVISQALKVAGLSVDDIDYVEAHGTGTPLGDPIELSSLDSAFQGRERPLWVGSVKANMGHLDAAAGMASVIKTMMVLKHAEVPAQLHLAQLNPLVDWKRSRLAVPTAIESLPDRPRLAGISGFGLSGTNVHMILEDASVYRQAQPQQERSAQGRPWVLPVSARSAQAVVEQARAYAVHLPQQDDGQLQAFVASAIHRRDHFPYRSAVVGANAGQLKSQLEQLPAPTLACTTDEEDRRGPVLVFTGQGAQWVGMGRDLLEREPAFLAMIRRCDQALAQWASWSVEAELRSDASGSRLHLTEFAQPCIFAIQVAISECLRQWGVIPAAVVGHSMGEVAAAYCAGALDLESAVRVIHHRAQAMKDTLGQGRMLVVGLPAPTLQSRLANNPQLELSVVNSRNSCVVSGSPQAVQALDQQLRDEGIFTYLMPAEYAFHSCQMDECLTQIRAGLEDLPVVAAHTPWISTSAMPEEPILADADYWARNARGIVRFDRAIEQLIEQGHRLFVEIGPHTVLAASINQALADKGTQGLVCGALHKQGDAALELASIVARLYEWGAGPDWQAFQPREAALELPAYPWQQERFWFAPAPRPQPAGLVSQLRAQVLVYDAQGNLCAQANDVALSVPQLAQVAVPAPAKVSAAAQPVGDVRAQIGALLTQIIGVACADPDPDRGFFELGLSSISLVEFKRMLERQFALKLSATVGFDYPTINRLGQYLEGLLSREPASTPVTVDAGATDAAGSVAVVAMACRFPQADSPEALWKLMLEQTDTVGPVPPSRLAGAKPEETFPRFASLIQRPEGFDEAFFRISPKEARSMDPQQRLLLMVAWEALERAGIPQEKLLEQRVGVFVGANSHDYETRVLGSAQGVDAHYGTGSSFSAICGRLSHFLGVRGPSLTVDTACSSSLTAIHLACNSLRAAECDIAIVGGVNVIASASIFQSMGQAGALAPDGISKAFDDSADGYGRGEGCGVVILKRQAQAERERDPIVATILGSAVNHDGACAGLTVPNGPAQEALISEALANAGVHPGQVSYVEAHGTGTVLGDPIELNALHNAYRQASPDSPPLTVASVKANIGHLEAAAGIASLIKACLVVEHGRIAPQAHLQRANTRVDWAAMNLKLAHQAMDWPGRPESRVAGVSAFGFTGTNVHVLLKGYTAPATAPLPPATAPVALCLSAATPAALAELAQRYVSFLGATEHCPQTICYNALMRRTAFKERLVVHGQDCRELAQALQAWLAGSPIANDRKPAAGEPWATLAEAFGRGAQSPGPERLPDGCQAIGLPTYPWQLNDYWIDAGQPATAVQPARAASGHPCLQGLVRPAGQLWYWSGALAPQAGHYDPLGEQGYRVKTHLLLDAVLQAVRETPRGVQQIRDLQIAQLRLRGEQHLTSHLSIHLTQAPDACFELALQGAGDERRQVCMSGTLVDCAAQLQEETLCGVSMLDEPSPPAPDVGLCPWSGCAATGGQRALYRFAHSLTAAERQTQLLASVVELFEGAHAAALVGFSGLQVWADLPAQVWIVLAGHDADKPDSLQVVDARGCQLALFEGPQFGHPGSWYLPDLQTAPLDLPMIARQWQDYPMPGEGARQREGYWMVLAWSTAEVQPLAAAFAAEQRPVEVIELHAGQQPLARKLSSALRGAVADPSCLGVIVAGVEAQEADGLGISLVASAALVQAFAGAIASVGTPAKPVWFALHASDAASPAMAAVQATWQGAAHIFALEHPAWWGGLVTLQGSDRRSYASLCRLLHGQPGHDHFAISGARVEVQYLVEDQADPLQRLEPPALNGTVVLHAVPGSDLETVLTALGQRGVQRVLLLCEAPGQLHMPERMPEAMAISSLSDLSRENLADTFATLRAQDRIAGFIHLDLDWRTVALKEPEFVVRMQEGVRPLEVLQQVHQLIDDPEAFFLILGSVSSLLGGAGFARSAIADAYALWVHAQRRRQGLNCQLLHLTQSEQELEQDAAARTAMQGSGLQPLQRSQIVQAIARVLGGQGQCGLLNVDWQQLKGLYLSVLPWPLLEHLGAADSAADQRLAELIGLPPLQQRRAMQALVCEVVGQVFGVADGLELDVRKGFFDMGMSSVMSLDLRSRLGRALSIDLPSTFGFEYTSIEQVTDYLMGQLLAPETREPVAAPEPVSPASRHQDLHELSRAELIGALEDELRDIANY
Protein: Protein rpi-1 (Q69Z08)
Organism: Caenorhabditis elegans
Subcellular location: Cell projection, cilium membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000255}. Cell projection, cilium {ECO:0000269|PubMed:27930654}. Cytoplasm, cytoskeleton, cilium axoneme {ECO:0000269|PubMed:27930654}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:27930654}. Note=Localizes to the base of the cilium. Localizes to ciliary and cytoplasmic microtubules. {ECO:0000269|PubMed:27930654}.
Interaction partners:
- Protein maph-9
- Protein fam-161
- Doublecortin domain-containing protein
- Cilia- and flagella-associated protein 36
- Protein KATNIP homolog
- F59G1.4
Sequence:
MPTPSTKKKVKKVAEDPLSSSGVSSLSGISSYNIRKISIYKNGDRYHRGVKFVINPRVIKDMEPLLNQVNDRIELSHGAKKLYTTDGKIVNSIKELEDGKIYVAASAQFIPMRYGEFAEKVWKPPSRKHSPIMSSDRIKTARTRSQDPSKRRQPQNSGSSAPTGSGVQRSRSVRTLAEDRKSRRDANPARPNVNGASNAPKKFDGARPKAPPARQTIPKPKKILTTSTTNKKPPTPKRKVSKKVLGAAAAAGVTVVGAAAIGAVAAAKRSTPKPIPTAVSDVSTASSIPIPNVTGAAEILEFPEEEKKIDMATIHRTPTPPVVASRPATAKAPGTPANRSATALEAKSVSQQPTPESSEEEEDEGNGDEDDDEEVEDDEEDAGSDEAEEEPSDEEEEDEETEEEEEEEEEEEEDDDESRVETPASRKSSSAVSFSGSTEEDHKKGDEAKK
Protein: At5g44730 (Dreg-2 like protein) (Haloacid dehalogenase-like hydrolase (HAD) superfamily protein) (O48587)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- AT4g27450/F27G19_50
- Two-on-two hemoglobin-3
- 5-amino-6-
- Plant cysteine oxidase 2
- Small ribosomal subunit protein uS4y
- Large ribosomal subunit protein eL21x/eL21w
- Large ribosomal subunit protein uL5z
- Deoxyhypusine synthase
- Large ribosomal subunit protein eL28z
- Large ribosomal subunit protein eL28y
Sequence:
MAVSLLSKLRCITVDVTGTLIAYKGELGDYYCMAAKAIGLPCPDYKRVHEGFKLAYTDMAQKYPCFGFHAKMPNIVWWKTCVRDSFVKAGYEYDEETFEKIFRRIYSTFGSAAPYSVFQDSQPFLRWARRKGLIVGLVSNAEYRYQEVILPSFGLSKAEWDFGVFSGIEGIEKPDPRIFTLALERAGNNIAPEEVLHIGDSMRKDYVPAKSIGMHALLVDRFKTEAAKDWIEAGAIVLPDLVAVQQLLESDKLKC
Protein: Ubiquitin-like protein atg12 (Autophagy-related protein 12) (APG12-like) (Q86CR6)
Organism: Dictyostelium discoideum (Social amoeba)
Function: Ubiquitin-like protein involved in autophagy vesicles formation. Required for atg8 association to the vesicle membranes. Conjugated to atg5 through a ubiquitin-like conjugating system involving also atg7 as an E1-like activating enzyme is essential for its function (By similarity).
Subcellular location: Cytoplasm {ECO:0000250}.
Interaction partners:
- Autophagy protein 5
- Ubiquitin-like modifier-activating enzyme atg7
- Autophagy-related protein 3
- Protein tipD
- Ubiquitin-like-conjugating enzyme ATG10
- Autophagy-related protein 18
- Autophagy-related protein 8
- Serine/threonine-protein kinase atg1
- Probable serine/threonine-protein kinase vps15
- Autophagy-related protein 9
Sequence:
MEEEEKNNNEVASPTEQNTESTTEQQPQLPVKITSESKIIVYFKNAGGAQPLKQKKFKIQANVSFQNVIDKLRGQLKLKSNESLFLFINQVFQPSPDEILGELYKCFSHNDQLIINYSLQMAWG
Protein: Glutathione peroxidase 1 (GPx-1) (GSHPx-1) (EC 1.11.1.9) (Cellular glutathione peroxidase) (Phospholipid-hydroperoxide glutathione peroxidase GPX1) (EC 1.11.1.12) (Selenium-dependent glutathione peroxidase 1) (P11352)
Organism: Mus musculus (Mouse)
Function: Protects the hemoglobin in erythrocytes from oxidative breakdown. In platelets, plays a crucial role of glutathione peroxidase in the arachidonic acid metabolism.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:10754271, ECO:0000269|PubMed:9126277}. Mitochondrion {ECO:0000269|PubMed:10754271, ECO:0000269|PubMed:9126277}.
Interaction partners:
- Glutathione reductase, mitochondrial
- Peroxisome proliferator-activated receptor gamma coactivator 1-alpha
- Glutathione synthetase
- Polyunsaturated fatty acid lipoxygenase ALOX15
- Polyunsaturated fatty acid 5-lipoxygenase
- Thioredoxin
- Superoxide dismutase
- Polyunsaturated fatty acid lipoxygenase ALOX8
- Peroxiredoxin-2
- Glutathione-specific gamma-glutamylcyclotransferase 1
Sequence:
MCAARLSAAAQSTVYAFSARPLTGGEPVSLGSLRGKVLLIENVASLUGTTIRDYTEMNDLQKRLGPRGLVVLGFPCNQFGHQENGKNEEILNSLKYVRPGGGFEPNFTLFEKCEVNGEKAHPLFTFLRNALPTPSDDPTALMTDPKYIIWSPVCRNDIAWNFEKFLVGPDGVPVRRYSRRFRTIDIEPDIETLLSQQSGNS
Protein: Trk system potassium uptake protein TrkA (K(+)-uptake protein TrkA) (P9WFZ3)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: Part of a potassium transport system.
Interaction partners:
- Trk system potassium uptake protein TrkA
- Probable conserved integral membrane alanine and valine and leucine rich protein
- Conserved protein
Sequence:
MKVAVAGAGAVGRSVTRELVENGHDITLIERNPDHLDAAAIPEAHWRLGDACELSLLESIHLEEFDVVVAATGDDKVNVVLSLLAKTEFAVPRVVARVNDPRNEWLFNDAWGVDVAVSTPRMLASLIEEAVTIGDLVRLMEFRTGQANLVEITLPDNTPWGGKPVRKLQLPRDAALVTILRGPRVIVPEADEPLEGGDELLFVAVTEAEEELSRLLLPSM
Protein: Ferredoxin (P83525)
Organism: Scopolia japonica (Japanese belladonna)
Function: Ferredoxins are iron-sulfur proteins that transfer electrons in a wide variety of metabolic reactions.
Subcellular location: Plastid, chloroplast {ECO:0000269|PubMed:12392097}.
Interaction partners:
Sequence:
ATYKVKLVTPDGPVEFDCPDDVYILDQAEEEGHELPYSCRAGSCSSCAGKVSAGTVDQSDGNFLDDDQMADGFVLTCVAYPQSDVIIETHKEEELTG
Protein: Small ribosomal subunit protein uS8x (40S ribosomal protein S15a-4) (Q9LX88)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- Small ribosomal subunit protein eS6y
- Small ribosomal subunit protein uS14z/uS14y/uS14x
- Small ribosomal subunit protein eS7x
- Large ribosomal subunit protein uL15x
- Large ribosomal subunit protein uL16x
- Small ribosomal subunit protein uS9y
- Small ribosomal subunit protein uS9x
- Small ribosomal subunit protein eS30z/eS30y/eS30x
- Small ribosomal subunit protein eS7y
- Small ribosomal subunit protein uS17z
Sequence:
MVRISVLNDGLKSMYNAEKRGKRQVMIRPSSKVIIKFLIVMQKHGYIGEFEYVDDHRSGKIVVELNGRLNKCGVISPRFDVGVKEIEGWTARLLPSRQFGFIVLTTSAGIMDHEEARRKNVGGKVLGFFY
Protein: Myoblast determination protein 1 homolog (MYOD1 homolog) (P16075)
Organism: Gallus gallus (Chicken)
Function: Acts as a transcriptional activator that promotes transcription of muscle-specific target genes and plays a role in muscle differentiation. Induces fibroblasts to differentiate into myoblasts. Interacts with and is inhibited by the twist protein. This interaction probably involves the basic domains of both proteins (By similarity).
Subcellular location: Nucleus.
Interaction partners:
- PAX7 protein
- Paired box 3
- Myocyte enhancer factor 2D
- Growth/differentiation factor 8
- DNA-binding protein inhibitor ID-4
- Mothers against decapentaplegic homolog 3
- Myosin-1B
- E1A binding protein p300.
- Transcription factor 12
- Myocyte enhancer factor 2C.
Sequence:
MDLLGPMEMTEGSLCSFTAADDFYDDPCFNTSDMHFFEDLDPRLVHVGGLLKPEEHPHTRAPPREPTEEEHVRAPSGHHQAGRCLLWACKACKRKTTNADRRKAATMRERRRLSKVNEAFETLKRCTSTNPNQRLPKVEILRNAIRYIESLQALLREQEDAYYPVLEHYSGESDASSPRSNCSDGMMEYSGPPCSSRRRNSYDSSYYTESPNDPKHGKSSVVSSLDCLSSIVERISTDNSTCPILPPAEAVAEGSPCSPQEGGNLSDSGAQIPSPTNCTPLPQESSSSSSSNPIYQVL
Protein: PDGF- and VEGF-related factor 3, isoform E (Q9VM40)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MQLNTLRLALIFLSFVRLEAQANVQNNGWQKVLPDDFRRERDKSSTRTRRNPQEELRLRHEQHHLRLQQHQMAWELDLQRQLQQHLQEQQSEQSEQQSRPVRHHQHKSHTKELAKKPIRRAPSFGDDKAKMVQKRRLHYNEYDNEDLELHTIETGDQGTFTPRQWQQIEIAHRRQKEQHQLQLLAQRQQQRQLLTTTTATATAMAMATTSKATEPNDAKSEDNDDVENIYARNYVAAKVGQKKEDQLGTPEAVIKARRLHAQKQKSERALAHAHMNQVLKEATCRIPQKRCQLVQQDPSKIYTPHCTILHRCSEDSGCCPSRSQICAAKSTHNVELHFFVKSSKHRSVIEKRTFVNHTECHCIERSTYNEETAMAHYGQSVVRATILSCTCPKSFEKILQDDGQCRCDCSSGNYDCDWLKRGNEHFAMNDRKCIQQGRCKPPTCEFGLYMDKHGRCPKQHEQPSYNAMS