wanglab/gogpt-training-data huggingface dataset:
Protein: HIRA-interacting protein 5, putative (Q389M3)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- Paraflagellar rod component, putative
Sequence:
MVEEVTIGRDFVTVRRVDDDDTAAAVRQYAVRLGGNPTATPEETAERSAALQRKVMDAMEENCEQVKTLSGRNDPNESVDGGGENTEDNLGSQGGVALDSVDEAALRDLVRSTHWSELKLHVSALLTDHLYSGRAHIDADAPHPHPDTIPQDGDSEVVVVLKELISTTIRPQLQADGGDIRFVGLADSVMLVEMLGACRKCRSSKTTLRDMIERTTRHWVPEVQKVEEVERGGSHERQRQGKD
Protein: Ribonuclease 3 (EC 3.1.26.3) (Ribonuclease III) (RNase III) (Q02555)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: DsRNA-specific nuclease that cleaves eukaryotic pre-ribosomal RNA at the U3 snoRNP-dependent A0 site in the 5'-external transcribed spacer (ETS) and in the 3'-ETS. In vitro, cleaves synthetic 5'-ETS RNA A0 site in the absence of snoRNA or other factors. Has an essential growth function in addition to pre-rRNA processing.
Interaction partners:
- Small ribosomal subunit protein uS9m
- 5'-3' exoribonuclease 2
- Helicase SEN1
- Small ribosomal subunit protein bS6m
- Large ribosomal subunit protein bL27m
- Large ribosomal subunit protein bL17m
- Large ribosomal subunit protein bL19m
- Large ribosomal subunit protein bL33m
- Small ribosomal subunit protein bS16m
- Large ribosomal subunit protein bL32m
Sequence:
MGSKVAGKKKTQNDNKLDNENGSQQRENINTKTLLKGNLKISNYKYLEVIQLEHAVTKLVESYNKIIELSPNLVAYNEAVNNQDRVPVQILPSLSRYQLKLAAELKTLHDLKKDAILTEITDYENEFDTEQKQPILQEISKADMEKLEKLEQVKREKREKIDVNVYENLNEKEDEEEDEGEDSYDPTKAGDIVKATKWPPKLPEIQDLAIRARVFIHKSTIKDKVYLSGSEMINAHNERLEFLGDSILNSVMTLIIYNKFPDYSEGQLSTLRMNLVSNEQIKQWSIMYNFHEKLKTNFDLKDENSNFQNGKLKLYADVFEAYIGGLMEDDPRNNLPKIRKWLRKLAKPVIEEATRNQVALEKTDKLDMNAKRQLYSLIGYASLRLHYVTVKKPTAVDPNSIVECRVGDGTVLGTGVGRNIKIAGIRAAENALRDKKMLDFYAKQRAAIPRSESVLKDPSQKNKKRKFSDTS
Protein: PTS system glucitol/sorbitol-specific EIIA component (EIIA-Gut) (EIII-Gut) (Glucitol/sorbitol-specific phosphotransferase enzyme IIA component) (P05706)
Organism: Escherichia coli (strain K12)
Function: The phosphoenolpyruvate-dependent sugar phosphotransferase system (sugar PTS), a major carbohydrate active transport system, catalyzes the phosphorylation of incoming sugar substrates concomitantly with their translocation across the cell membrane. The enzyme II complex composed of SrlA, SrlB and SrlE is involved in glucitol/sorbitol transport. It can also use D-mannitol.
Subcellular location: Cytoplasm {ECO:0000305|PubMed:3553176}.
Interaction partners:
- PTS system glucitol/sorbitol-specific EIIB component
- PTS system glucitol/sorbitol-specific EIIC component
- Sorbitol-6-phosphate 2-dehydrogenase
- Glucitol operon activator protein
- Uncharacterized protein YggP
- Phosphocarrier protein HPr
- Glucitol operon repressor
- Arabinose 5-phosphate isomerase GutQ
- PTS system galactitol-specific EIIB component
- PTS system galactitol-specific EIIA component
Sequence:
MTVIYQTTITRIGASAIDALSDQMLITFREGAPADLEEYCFIHCHGELKGALHPGLQFSLGQHRYPVTAVGSVAEDNLRELGHVTLRFDGLNEAEFPGTVHVAGPVPDDIAPGSVLKFESVKE
Protein: Heat shock 70 kDa protein 6 (Heat shock 70 kDa protein B') (Q04967)
Organism: Sus scrofa (Pig)
Function: Molecular chaperone implicated in a wide variety of cellular processes, including protection of the proteome from stress, folding and transport of newly synthesized polypeptides, activation of proteolysis of misfolded proteins and the formation and dissociation of protein complexes. Plays a pivotal role in the protein quality control system, ensuring the correct folding of proteins, the re-folding of misfolded proteins and controlling the targeting of proteins for subsequent degradation. This is achieved through cycles of ATP binding, ATP hydrolysis and ADP release, mediated by co-chaperones. The affinity for polypeptides is regulated by its nucleotide bound state. In the ATP-bound form, it has a low affinity for substrate proteins. However, upon hydrolysis of the ATP to ADP, it undergoes a conformational change that increases its affinity for substrate proteins. It goes through repeated cycles of ATP hydrolysis and nucleotide exchange, which permits cycles of substrate binding and release.
Interaction partners:
- Heat shock protein HSP 90-alpha
- Toll-like receptor 2
- Heat shock protein beta-1
- Alpha-crystallin B chain
- Heat shock protein family A
- DnaJ heat shock protein family
- Stress-activated protein kinase JNK
- Stress-activated protein kinase JNK
- Heat shock 70 kDa protein 1-like
- DnaJ heat shock protein family
Sequence:
MSAAREVAIGIDLGTTYSCVGVFQHGRVEILANDQGNRTTPSYVAFTDTERLVGDAAKSQAALNPQNTVFDAKRLIGRKFADPTVQSDLKHWPFQVVSEGGKPKVRVSYRGEDKAFYPEEISSMVLSKMKETAEAYLGQPVRHAVITVPAYFNDSQRQATKDAGAIAGLNVLRIINEPTAAAIAYGLDRRGAGERNVLIFDLGGGTFDVSVLTIDAGVFEVKATAGDTHLGGEDFDNRLVNHFMEEFRRKHRKDLSRNKRALRRLRTACERAKRTLSSSTQATLEIDSLFEGVDFYTSITRARFEELCSDLFRSTLEPVEKALRDAKLDKAQIHDIVLVGGSTRIPKIQKLLQDFFNGRELNKSINPDEAVAYGAAVQAAVLMGDKCEKVQDLLLLDVAPLSLGLETAGGVMTTLIQRNATIPTKQTQTFTTYSDNQPGVLIQVYEGERAMTRDNNLLGRFELSGIPPAPRGVPQIEVTFDIDANGILSVTATDRSTGRANKITITNDKGRLSKEEVERMVREADEYKVEDEAQRDRVAAKNSLEAYVFHVKGSLHEESLRDKIPEEDRCKVQDKCQEVLTWLEHNQLAEKEEYEHQKRELEQICRPIFSRLYGAPGIPGGSSCGAQARQGAPSTGPVIEEVD
Protein: Cysteine-rich venom protein kaouthin-1 (Cysteine-rich venom protein 25) (CRVP-25k) (P84805)
Organism: Naja kaouthia (Monocled cobra) (Naja siamensis)
Function: Inhibits calcium-activated potassium channels (KCa), voltage-gated potassium channel (Kv), and the calcium release channel/ryanodine receptor (RyR).
Subcellular location: Secreted {ECO:0000269|PubMed:15670767}.
Interaction partners:
Sequence:
MIAFSLLCLAAVLRQSFGNVDFNSESTRRKKKQKEIVDLHNSLRRRVSPTASNMLKMEWYPEAASNAERWANTCSLNHSPDNLRVLEGIQCGESIYMSSNARTWTEIIHLWHDEYKNFVYGVGANPPGSVTGHYTQIVWYQTYRAGCAVSYCPSSAWSYFYVCQYCPSGNFQGKTATPYKLGPPCGDCPSACDNGLCTNPCTIYNKLTNCDSLLKQGSCQDDWIKSNCPASCFCRNKII
Protein: BTB/POZ domain-containing protein KCTD8 (Q6ZWB6)
Organism: Homo sapiens (Human)
Function: Auxiliary subunit of GABA-B receptors that determine the pharmacology and kinetics of the receptor response. Increases agonist potency and markedly alter the G-protein signaling of the receptors by accelerating onset and promoting desensitization (By similarity).
Subcellular location: Presynaptic cell membrane {ECO:0000250}. Postsynaptic cell membrane {ECO:0000250}.
Interaction partners:
Sequence:
MALKDTGSGGSTILPISEMVSSSSSPGASAAAAPGPCAPSPFPEVVELNVGGQVYVTKHSTLLSVPDSTLASMFSPSSPRGGARRRGELPRDSRARFFIDRDGFLFRYVLDYLRDKQLALPEHFPEKERLLREAEYFQLTDLVKLLSPKVTKQNSLNDEGCQSDLEDNVSQGSSDALLLRGAAAAVPSGPGAHGGGGGGGAQDKRSGFLTLGYRGSYTTVRDNQADAKFRRVARIMVCGRIALAKEVFGDTLNESRDPDRQPEKYTSRFYLKFTYLEQAFDRLSEAGFHMVACNSSGTAAFVNQYRDDKIWSSYTEYIFFRPPQKIVSPKQEHEDRKHDKVTDKGSESGTSCNELSTSSCDSHSEASTPQDNPSSAQQATAHQPNTLTLDRPSKKAPVQWIPPPDKRRNSELFQTLISKSRETNLSKKKVCEKLSVEEEMKKCIQDFKKIHIPDYFPERKRQWQSELLQKYGL
Protein: Tabersonine-19-hydroxy-O-acetyltransferase (EC 2.3.1.-) (A0A2K8FQU5)
Organism: Catharanthus roseus (Madagascar periwinkle) (Vinca rosea)
Function: Component of the monoterpenoid indole alkaloids (MIAs, e.g. echitovenine, tabersonine, lochnericine, 19-hydroxytabersonine and horhammericine) biosynthetic pathway; MIAs are used in cancer treatment and other medical applications. Acyltransferase catalyzing the conversion of horhammericine to 19-O-acetylhorhammericine, of 19-hydroxytabersonine to 19-O-acetyltabersonine and of minovincinine to echitovenine.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:29438577}. Nucleus {ECO:0000255|PROSITE-ProRule:PRU00768, ECO:0000269|PubMed:29438577}.
Interaction partners:
Sequence:
MASKMVEIVSKMFIKPSSPTPQSLRRYNLSSIDQTIDSEVTSLAFFYTYNPSHESSKIGDLLKNSLSKTLVSYYQFAGRLIENDYIDCNDEGVEFVEVRIHGRMNDILKRGKSFATDLVLPTRIIALHEDSLLIVQLSHFDCGGIAIGFGASHKVSDGVSNVMFMKDWASSTSLSTFHKPTPLLTADSIFPPEDNKLLSNKSIVSFQQCLGKRFVFSTEAIEKLKSKAIEYGIQKPSRVEVVTAFLCQCAANCDLPRKKPYAIISAVNLRPYLALPQNSIGNIFSFYFCINDEGMDNQFSALISKLRNGKQKLLENIISKEKLTYESQMQELTKCLDQLNISSLDTYFCSSWCRFPVYDIDFGWGKPILVSPFQPHVKDLILLMDSPEGDGIEALITMEEKKMAAFEKNEELRSFAYLDSPEPEALIIPEEDKSFE
Protein: Intracellular coagulation inhibitor 3 (Limulus intracellular coagulation inhibitor 3) (LICI-3) (Q94823)
Organism: Tachypleus tridentatus (Japanese horseshoe crab)
Function: Serine protease inhibitor that inhibits clotting factor G and to a lesser extent proclotting enzyme and clotting factor C.
Subcellular location: Secreted {ECO:0000250|UniProtKB:Q27086}. Note=Localizes in the large granules of hemocytes (By similarity). Secreted in hemolymph in response to external stimuli (By similarity). {ECO:0000250|UniProtKB:Q27086}.
Interaction partners:
Sequence:
MKTLIFTLSSLQLIFLPQLSLGNYLLDEILHLSDVDQQQLSAVTRITNASNYFGFDLYNTLKGSGNVLISPYSLSCAMAMVYLGSRGVTEREMHSVLNYGSFGLTRDDVRLGFQQAINTLTSNTIGYTLDTANALLIQRSFEVQEDFRQKIETDFGAEVREVDFQSQTTIVQQAINTWTAHKTQNNIQNILKEPPDSNTLLFFLNAVYFKGFWETTFDPKQSTIMKFYNNGSVSTDTVMMMMESRLPFGYVESLNCLALEMPYQGRNVTMLLLLPVSPNGLPELEQALSPASISLIYSTLRKRRVKVFIPKFKLEEEYEEVLKEGLSDMGMKSLFGFNANLNGITEDTGLYVTTVVHKTSIEVDEEGTVASAASGVGGGWRSATPRFMANHPFLFFIRHSETGAVLFMGRVSQL
Protein: Uncharacterized protein (Q57YK6)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MPPKRPPRARRTKESAKAVISPQEKPLTSSSSGEALGGSGNEVKRTNETPVARVARPLNSPSVRAVSEKAPSPTGFGPCHVIGVLLAVVLTCVWSIFPPWDATDAPPCHCFPAGGEVQQAIASRMFGVTGIHLRGAGHSAVEESLRGLSSCGKLYTLENQFDGVGSFMQRLQHDAKGTRCVVWLVKDLSVVKHVDNALKELLEDNTLRGNRILPDGARGLFIVLSNQSREEIKGLLPHRVVHQFRTINLPAKK
Protein: Icarus, isoform A (Icarus, isoform B) (Icarus, isoform C) (MIP12770p) (RE04081p) (Q9V428)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- LIM domain-containing protein
- Integrin linked kinase, isoform A
- GH23568p
- GH07711p
Sequence:
MSQSCIPVSAKMSKAKKVLDEARETHNPELDLADKGLSSFEELPGLFNMSNITRLTLSHNKISVISPGIANLLNLEILNLSNNQLTELPVSLSSMPKLRILNVSINRLINLPRGFGAFPVLEVLDLSYNNLNEQVLPGNFFGMETLRALYLGDNDFEYIPKEVGQLKNLQILGLRDNDLLELPREVGDLVRLRELHIQNNRLQVLPPEIAQLDLLSNKSVMKMEENPWVNPIAEQYLLGISHVIDYLKTETYKIIYNRHLQAGRSGPPPPKADKSKKASRIRA
Protein: Vomeronasal type-1 receptor 46 (Vomeronasal type-1 receptor A13) (Vomeronasal type-1 receptor B8) (Q9EQ45)
Organism: Mus musculus (Mouse)
Function: Putative pheromone receptor implicated in the regulation of social and reproductive behavior.
Subcellular location: Cell membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Olfactory receptor
Sequence:
MNKANIFCTDTNMKVILFSEVSVGISANSILFISHLCMFLGESRPKPIDLYIAFFSLTHLMLLVTMGLIAVDMFMPGGRWDSTTCTFLMYLHIVLRGPTLCATCLLNVLWTITLSPRNSCLTKFKHKSPHHISGAFLFLCVLYMSLSSELLSITASLNLTSENFLYVSQSCSILPMSYSIKSMFSTKMAIREAFLIGLMVLSSGYMVALLWSHKKQAQHLHSNSLSLKASPEQRATRTIMLLMSFFVVFYILDSVIFYSRMKFKDDSIFVCVQIIVSHSYVTVSPFVFICTEKHIIKFFWSLCGRIVNI
Protein: Secreted aspartic protease 9 (ACP 9) (Aspartate protease 9) (EC 3.4.23.24) (Candidapepsin-9) (Q59SU1)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Function: Secreted aspartic peptidases (SAPs) are a group of ten acidic hydrolases considered as key virulence factors. These enzymes supply the fungus with nutrient amino acids as well as are able to degrade the selected host's proteins involved in the immune defense. Involved in triggering host polymorphonuclear neutrophils chemotaxis toward germ tubes. Moreover, acts toward human hemoglobin though limited proteolysis to generate a variety of antimicrobial hemocidins, enabling to compete with the other microorganisms of the same physiological niche using the microbicidal peptides generated from the host protein. Required for cell surface integrity and cell separation during budding.
Subcellular location: Cell membrane {ECO:0000305}; Lipid-anchor, GPI-anchor {ECO:0000305}. Secreted, cell wall {ECO:0000269|PubMed:16269404, ECO:0000269|PubMed:21622905}.
Interaction partners:
- pH-response transcription factor pacC/RIM101
- Kexin
Sequence:
MRLNSVALLSLVATALAAKAPFKIDFEVRRGESKDDLSPEDDSNPRFVKRDGSLDMTLTNKQTFYMATLKIGSNEDENRVLVDTGSSDLWVMSHDLKCVSAPNSKRNERSFGHGTGVKLNERELMQKRKNLYQPSRTIETDEEKEASEKIHNKLFGFGSIYSTVYITEGPGAYSTFSPFVGTEGGSGGSGGSNTCTSYGSFNTENSDTFKKNNTNDFEIQYADDTSAIGIWGYDDVTISNVTVKDLSFAIANETSSDVGVLGIGLPGLEVTTQYGYTYQNLPLKLKADGIIAKSLYSLYLNTADAKAGSILFGAIDHAKYQGDLVTVKMMRTYSQISYPVRIQVPVSKIDVESSSGSTTNILSSTTGVVLDTGSTLSYVFSDTLQSLGKALNGQYSNSVGAYVVNCNLADSSRTVDIEFGGNKTIKVPISDLVLQASKSTCILGVMQQSSSSSYMLFGDNILRSAYIVYDLDDYEVSLAQVSYTNKESIEVIGASGITNSSGSGTTSSSGTSTSTSTRHSAGSIISKPVYGLLLSLLISCYVLV
Protein: Zinc finger protein basonuclin-2 (Q8BMQ3)
Organism: Mus musculus (Mouse)
Function: Probable transcription factor specific for skin keratinocytes. May play a role in the differentiation of spermatozoa and oocytes. May also play an important role in early urinary-tract development.
Subcellular location: Nucleus {ECO:0000269|PubMed:15081112}.
Interaction partners:
Sequence:
MARFVPSPPPNCLSYKSEGRLGEQDWQAHFKVPCCGVDPSQLESEEAEVDVRERDTQRDREPKRARDLTLRDSCTDNSMQFGTRTTAAEPGFMGTWQNADTNLLFRMSQQVPLACAGRVLGADFCPNLEEPDQRLEVQAIRCTLVNCTCECFQPGKINLRTCDQCKHGWVAHALDKLSTQHLYHPTQVEIVQSNVVFDISSLMLYGTQAVPVRLKILLDRLFSVLKQEEVLHILHGLGWTLRDYVRGYILQDAAGKVLDRWAIMSREEEIITLQQFLRFGETKSIVELMAIQEKEGQAVAVPSSKTDSDIRTFIESNNRTRSPSLLAHLENSNPSSIHHFENIPNSLAFLLPFQYINPVSAPLLGLPPNGLLLEQPGLRLREPSISTQNEYNESSESEVSPTPYKSDQTPNRNALTSITNVEPKTEPACVSPIQNSAPVSDLSKTEHPKSSFRIHRMRRMGSASRKGRVFCNACGKTFYDKGTLKIHYNAVHLKIKHRCTIEGCNMVFSSLRSRNRHSANPNPRLHMPMLRNNRDKDLIRATSGAATPVIASTKSNLTLTSPGRPPMGFTTPPLDPVLQNPLPSQLVFSGLKTVQPVPPFYRSLLTPGEMVSPPTSLPTSPIIPTSGTIEQHPPPPSEPIVPAVMMGTHEPSADLAPKKKPRKSSMPVKIEKEIIDTADEFDDEDDDPNDGGTVVNDMSHDNHCHSQDEMSPGMSVKDFSKHNRTRCISRTEIRRADSMTSEDQEPERDYENESESSEPKLGEESMEGDEHLHSEVSEKVLMNSERPDENHSEPSHQDVIKVKEEFTDPTYDMFYMSQYGLYNGGGASMAALHESFTSSLNYGSPQKFSPEGDLCSSPDPKICYVCKKSFKSSYSVKLHYRNVHLKEMHVCTVAGCNAAFPSRRSRDRHSANINLHRKLLTKELDDMSLDSSQPSLSKDLRDEFLMKIYGAQHPLGLDGREDASSPAGTEDSHLNGYGRGMAEDYMVLDLSTTSSLQSSSSVHSSRESDAGSDEGILLDDIDGASDSGESTHKAEAPTLPGSLGAEVSGSLMFSSLSGSNGGIMCNICHKMYSNKGTLRVHYKTVHLREMHKCKVPGCNMMFSSVRSRNRHSQNPNLHKNIPFTSID
Protein: Protein DELETION OF SUV3 SUPPRESSOR 1(I) (AtDSS1(I)) (Probable 26S proteasome complex subunit sem1-1) (Q9XIR8)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Subunit of the 26S proteasome which plays a role in ubiquitin-dependent proteolysis.
Interaction partners:
- Protein BREAST CANCER SUSCEPTIBILITY 2 homolog B
- Protein BREAST CANCER SUSCEPTIBILITY 2 homolog A
- 26S proteasome non-ATPase regulatory subunit 3 homolog B
- 26S proteasome non-ATPase regulatory subunit 3 homolog A
- 26S proteasome non-ATPase regulatory subunit 6 homolog
- 26S proteasome non-ATPase regulatory subunit 11 homolog
- SAC3 family protein C
- SAC3 family protein B
- 26S proteasome non-ATPase regulatory subunit 4 homolog
- SAC3 family protein A
Sequence:
MAAEPKAATAEVVKMDLFEDDDEFEEFEINEDWLEKEEVKEVSQQWEDDWDDDDVNDDFSRQLRKELENGTDKK
Protein: Regulator of G-protein signaling 6 (RGS6) (Q9Z2H2)
Organism: Mus musculus (Mouse)
Function: Regulates G protein-coupled receptor signaling cascades. Inhibits signal transduction by increasing the GTPase activity of G protein alpha subunits, thereby driving them into their inactive GDP-bound form. The RGS6/GNB5 dimer enhances GNAO1 GTPase activity.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:15897264}. Cytoplasm, cytosol {ECO:0000250|UniProtKB:P49758}. Membrane {ECO:0000250|UniProtKB:P49758}; Peripheral membrane protein {ECO:0000250|UniProtKB:P49758}. Nucleus {ECO:0000250|UniProtKB:P49758}. Cell membrane {ECO:0000269|PubMed:15897264}. Note=Interaction with GNB5 mediates translocation to the nucleus. {ECO:0000250|UniProtKB:P49758}.
Interaction partners:
- Guanine nucleotide-binding protein subunit beta-5
- Regulator of G-protein signaling 7-binding protein
- Guanine nucleotide-binding protein G
- T-complex protein 1 subunit epsilon
- Regulator of G-protein signaling 9-binding protein
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein subunit alpha-13
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein G
- Glutathione hydrolase 5 proenzyme
Sequence:
MAQGSGDQRAVGIADPEESSPNMIVYCKIEDIITKMQDDKTGGVPIRTVKSFLSKIPSVVTGTDIVQWLMKNLSIEDPVEAIHLGSLIAAQGYIFPISDHVLTMKDDGTFYRFQAPYFWPSNCWEPENTDYAIYLCKRTMQNKARLELADYEAENLARLQRAFARKWEFIFMQAEAQVKIDRKKDKTERKILDSQERAFWDVHRPVPGCVNTTEMDIRKCRRLKNPQKVKKSVYGVTDETQSQSPVHIPSQPIRKTTKDDIRKQITFLNAQIDRHCLKMSKVAESLIAYTEQYVEYDPFITPAEPSNPWISDDITLWDIEMSKEPSQQRVKRWGFSFDEILKDQVGRDQFLRFLESEFSSENLRFWLSVQDLKKQPLQDVAKRVEEIWQEFLAPGAPSAINLDSHSYEITSQNVKDGGRYTFEDAQEHIYKLMKSDSYARFLRSNAYQDLLLAKKKGKSLAGKRLTGLMQSS
Protein: Protein EXECUTER 1, chloroplastic (AtEX1) (Q93YW0)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Together with EX2, enables higher plants to perceive singlet oxygen as a stress signal in plastid that activates a genetically determined nuclear stress response program which triggers a programmed cell death (PCD). This transfer of singlet oxygen-induced stress-related signals from the plastid to the nucleus that triggers genetically controlled PCD pathway is unique to photosynthetic eukaryotes and operates under mild stress conditions, impeding photosystem II (PSII) without causing photooxidative damage of the plant.
Subcellular location: Plastid, chloroplast {ECO:0000269|PubMed:15539603, ECO:0000269|PubMed:17540731}.
Interaction partners:
- Pentatricopeptide repeat-containing protein GUN1, chloroplastic
- At1g32160/F3C3_6
- Alanine-tRNA ligase, putative
- At4g33110
- At1g63610
- AT3g29240/MXO21_9)
- Electron transporter, putative
- Pentatricopeptide repeat
- Thioredoxin domain-containing protein
- At5g52960
Sequence:
MPSLSTPPSQNLAFSPAASATSSRLTPSSKRSFYPHRLPDPTALCRCSSSSGSNSSSSSSSDDNPRWDSAIQDVLKSAIKRFDSVLSWYATLDNDDGEQGSENVEKIDDDWDWDRWKKHFDQVDDQDRLLSVLKSQLNRAIKREDYEDAARLKVAIAATATNDAVGKVMSTFYRALLEERYKDAVYLRDKAGAGLVGWWSGISEDVKDPFGLIVQITAEHGRYVARSYNPRQLSTSAAGAPLFEIFLTLDGKGNYKKQAVYLKWKEIFPDVPTMPSRTLTPGRFLTSPGRKEDTGNLAVESSEDEESDNSDDDSDLLEESSGFQSFLRDMIPGVKVKVMKVTAPGRVDKDFISKVIEQIADEEDEENDLDIEDIDVEDDTKAEIDEKNADIELESVTDEIIDNNGGREIAVKFVIGDIVDRLSGNQPLKESLRSPANLESVENSSFYLRLEKDLNVKESKGVEGTTLVDGKGSRQSRRRIENIMGDLAKSIEKEKKISVKMLKDVGELLSLTLSQAQNRQQLSGLTKFRRIDVTPSLDPLDGLYIGAHGLYTSEVIHLKRKFGQWKGGKESKKPTDIEFYEYVEAVKLTGDPYVPAGKVAFRAKIGRRYELPHKGLIPEEFGVIARYKGQGRLADPGFRNPRWVDGELVILDGKYVKGGPVVGFVYWAPEYHFVMFFNRLRLQA
Protein: TraB protein (Q3LAJ2)
Organism: Streptomyces venezuelae
Interaction partners:
Sequence:
MTEHLTEKNPAPADFDSIATVTFLRPTLPAPASVPEDNTWSDMPDDTDPAVVIPPMPTVAPAIGSDERTVVLETARVILDKTPAVEPVVRPGRFAGTVDLDDFDDAPLIPAWMYSAEGWAAWAGVFYRARRRDFRRWVRRQPTQHGHVRQFGRGTRRAHEWVVGFEGVRVQSAAHTAHVLTREARLAARHARFTPRILGSKKELAMKAADKATKAAEEAVLLHKKAKKDRNRVRNLRAGVVYGPPLTAIGTGYVMGGGLGLAAGLLSTFAGGAFVGRKPYDEEADWTSDWRSLGDGDRMTAPMLDASFRAAKVIGAEETLGVVQMPMLDTRGAWTAVLDLPPGVPAKKAIRATDELAAAFGVEEAQVSVAKRGRAGRIELYVARELPFTDKAAPGPLLALESAADFWGRISIGPDVRGIHQSISVVERSGLIGGEPGAGKSASGNTILLAAALDPRVILWLADGKGGGDLEPFEHLCERYEGDADPEAFNAMLDELLDVMKARYALLKKLGKRKVTEELANKYPELRQLLLWVDELMLYTTAEEFGKKITRKLRNLVSRGRAAGIITFCATQKPGSDVVDTSLRDLLSIRWALRCTTPEASDTILGKGAAASGYSAKTIQSEMRGAGLLWAEGTNPTMVRADYYDDDQVTALIERATEWRRKAGTLPNGPVPLVDQLRARGDDDALLLAAVLEVFAAQATEDDPVDWLPGQLLVDELKAAGHSVTAEKLGALVVRTDEEKAKRPWGEKKTRVTGYPLARVEAAATDRFGLTA
Protein: Uncharacterized protein (Q386Z5)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MKRGRSATSRSLRHNEDKKDFKLEDDSERKDTEESFVEEILTVEEKRTILLRFPCLDFFRNAHICETLCNSAQDASKGGTSGMETKFAPEALRFDADTLETPHPIVRLRTREFGELVFEGTWCQVSEINGGRESMSNRVVVHLCERSDEQSSGEVDKAVSGDNVGINRSNKSPLLSGSGSNSLSGSGVASLLKHSSVGVTADDARGQRRAQNALWFYNRIDVPCGTLVLARVK
Protein: RNA-binding (RRM/RBD/RNP motifs) family protein (F4JFN7)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- RNA binding
- Cleavage stimulating factor 64
Sequence:
MQSDNGKLFIGGISWDTNEERLKEYFSSFGEVIEAVILKDRTTGRARGFGFVVFADPAVAEIVITEKHNIDGRLVEAKKAVPRDDQNMVNRSNSSSIQGSPGGPGRTRKIFVGGLPSSVTESDFKTYFEQFGTTTDVVVMYDHNTQRPRGFGFITYDSEEAVEKVLLKTFHELNGKMVEVKRAVPKELSPGPSRSPLGAGYSYGVNRVNNLLNGYAQGFNPAAVGGYGLRMDGRFSPVGAGRSGFANYSSGYGMNVNFDQGLPTGFTGGTNYNGNVDYGRGMSPYYIGNTNRFGPAVGYEGGNGGGNSSFFSSVTRNLWGNNGGLNYNNNNTNSNSNTYMGGSSSGNNTLSGPFGNSGVNWGAPGGGNNAVSNENVKFGYGGNGESGFGLGTGGYAARNPGANKAAPSSSFSSASATNNTGYDTAGLAEFYGNGAVYSDPTWRSPTPETEGPAPFSYGIGGGVPSSDVSARSSSPGYVGSYSVNKRQPNRGEPSR
Protein: Cyclotide hyen-C (C0HLN7)
Organism: Pigea enneasperma (Spade flower) (Afrohybanthus enneaspermus)
Function: Probably participates in a plant defense mechanism (By similarity). Does not display any cytotoxic activity towards K562, HeLa, MCF-7, HUVEC or red blood cells. Does not bind to phospholipd membranes containing 1-palmitoyl 2-oleoyl phosphatidylcholine (POPC) or 1-palmitoyl-2-oleophosphatidylethanolamine (POPE).
Interaction partners:
Sequence:
GTHPCQETCVTSTRCSTQGCHCNWPICFKN
Protein: Eukaryotic translation elongation factor 1 epsilon 1 (H0YAL7)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
XGLSKGNKYSAQGERQIPVLQTNNGPSLTGLTTIAAHLVKQANKEYLLGSTAEEKAIVQQWLEYRVTQVDGHSSKNDIHTLLKDLNSYLEDKVYLTGYNFTLADILLYYGLHRFIANHDCFVYKKMRIVTGPHVCL
Protein: Gephyrin (Putative glycine receptor-tubulin linker protein) [Includes: Molybdopterin adenylyltransferase (MPT adenylyltransferase) (EC 2.7.7.75) (Domain G); Molybdopterin molybdenumtransferase (MPT Mo-transferase) (EC 2.10.1.1) (Domain E)] (Q03555)
Organism: Rattus norvegicus (Rat)
Function: Microtubule-associated protein involved in membrane protein-cytoskeleton interactions. It is thought to anchor the inhibitory glycine receptor (GLYR) to subsynaptic microtubules. Acts as a major instructive molecule at inhibitory synapses, where it also clusters GABA type A receptors (By similarity).
Subcellular location: Postsynaptic cell membrane {ECO:0000269|PubMed:16511563}; Lipid-anchor {ECO:0000305|PubMed:16511563}; Cytoplasmic side {ECO:0000269|PubMed:16511563}. Cell membrane {ECO:0000269|PubMed:12684523}; Lipid-anchor {ECO:0000305|PubMed:12684523}; Cytoplasmic side {ECO:0000305|PubMed:12684523}. Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q9NQX3}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:16511563}. Cell projection, dendrite {ECO:0000250|UniProtKB:Q9NQX3}. Postsynaptic density {ECO:0000250|UniProtKB:Q8BUV3}. Note=Cytoplasmic face of glycinergic postsynaptic membranes (PubMed:16511563). Forms clusters at synapses (By similarity). {ECO:0000250|UniProtKB:Q8BUV3, ECO:0000269|PubMed:16511563}.
Interaction partners:
- Molybdopterin synthase catalytic subunit
- Glycine receptor subunit alpha-1
- Glycine receptor subunit beta
- Neuroligin-2
- Glycine--tRNA ligase
- Molybdenum cofactor biosynthesis protein 1
- Vesicular inhibitory amino acid transporter
- Gamma-aminobutyric acid receptor-associated protein
- Disks large homolog 4
- Sulfite oxidase, mitochondrial
Sequence:
MATEGMILTNHDHQIRVGVLTVSDSCFRNLAEDRSGINLKDLVQDPSLLGGTISAYKIVPDEIEEIKETLIDWCDEKELNLILTTGGTGFAPRDVTPEKFPTFPFCGLQKGATKEVIEREAPGMALAMLMGSLNVTPLGMLSRPVCGIRGKTLIINLPGSKKGSQECFQFILPALPHAIDLLRDAIVKVKEVHDELEDLPSPPPPLSPPPTTSPHKQTEDKGVQCEEEEEEKKDSGVASTEDSSSSHITAAALAAKIPDSIISRGVQVLPRDTASLSTTPSESPRAQATSRLSTASCPTPKQIRRPDESKGVASRVGSLKVQSRCSSKENILRASHSAVDITKVARRHRMSPFPLTSMDKAFITVLEMTPVLGTEIINYRDGMGRVLAQDVYAKDNLPPFPASVKDGYAVRAADGPGDRFIIGESQAGEQPTQTVMPGQVMRVTTGAPIPCGADAVVQVEDTELIRESDDGTEELEVRILVQARPGQDIRPIGHDIKRGECVLAKGTHMGPSEIGLLATVGVTEVEVNKFPVVAVMSTGNELLNPEDDLLPGKIRDSNRSTLLATIQEHGYPTINLGIVGDNPDDLLNALNEGISRADVIITSGGVSMGEKDYLKQVLDIDLHAQIHFGRVFMKPGLPTTFATLDIDGVRKIIFALPGNPVSAVVTCNLFVVPALRKMQGILDPRPTIIKARLSCDVKLDPRPEYHRCILTWHHQEPLPWAQSTGNQMSSRLMSMRSANGLLMLPPKTEQYVELHKGEVVDVMVIGRL
Protein: ESX-1 secretion-associated protein EspC (P9WJD7)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: Required for ESX-1 function. Required for either stability or expression of EspA.
Subcellular location: Secreted {ECO:0000269|PubMed:19682254, ECO:0000269|PubMed:21427227}. Note=Secreted via the ESX-1 / type VII secretion system (T7SS). {ECO:0000269|PubMed:19682254, ECO:0000269|PubMed:21427227}.
Interaction partners:
- ESX-1 secretion-associated protein EspA
- ESX-1 secretion-associated protein EspD
- ESAT-6-like protein EsxB
- 6 kDa early secretory antigenic target
- ESX-1 secretion-associated protein EspB
- Uncharacterized protein
- Nucleoid-associated protein EspR
- ESX-1 secretion-associated protein EspE
- Transposase
Sequence:
MTENLTVQPERLGVLASHHDNAAVDASSGVEAAAGLGESVAITHGPYCSQFNDTLNVYLTAHNALGSSLHTAGVDLAKSLRIAAKIYSEADEAWRKAIDGLFT