wanglab/gogpt-training-data huggingface dataset:
Protein: Glycine receptor subunit beta (Glycine receptor 58 kDa subunit) (P48168)
Organism: Mus musculus (Mouse)
Function: Glycine receptors are ligand-gated chloride channels. GLRB does not form ligand-gated ion channels by itself, but is part of heteromeric ligand-gated chloride channels. Channel opening is triggered by extracellular glycine. Heteropentameric channels composed of GLRB and GLRA1 are activated by lower glycine levels than homopentameric GLRA1. Plays an important role in the down-regulation of neuronal excitability. Contributes to the generation of inhibitory postsynaptic currents.
Subcellular location: Postsynaptic cell membrane {ECO:0000269|PubMed:22592841}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P23415}. Synapse {ECO:0000269|PubMed:19723286, ECO:0000269|PubMed:22592841}. Cell projection, dendrite {ECO:0000269|PubMed:19723286}. Cell membrane {ECO:0000269|PubMed:12809985}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P23415}. Cytoplasm {ECO:0000250|UniProtKB:P48167}. Note=Retained in the cytoplasm upon heterologous expression by itself. Coexpression with GPHN promotes expression at the cell membrane. Coexpression with GLRA1, GLRA2 or GLRA3 promotes expression at the cell membrane. {ECO:0000250|UniProtKB:P20781}.
Interaction partners:
- Gephyrin
- Glycine receptor subunit alpha-3
- Glycine receptor subunit alpha-1
- Sodium- and chloride-dependent glycine transporter 2
- Glycine--tRNA ligase
- Glycine receptor subunit alpha-2
- Rho guanine nucleotide exchange factor 9
Sequence:
MKFSLAISFFILMSLLFEDACAKEKSSKKGKGKKKQYLCPSQQSPEDLARVPPNSTSNILNRLLVSYDPRIRPNFKGIPVDVVVNIFINSFGSIQETTMDYRVNIFLRQKWNDPRLKLPSDFRGSDALTVDPTMYKCLWKPDLFFANEKSANFHDVTQENILLFIFRDGDVLVSMRLSITLSCPLDLTLFPMDTQRCKMQLESFGYTTDDLRFIWQSGDPVQLEKIALPQFDIKKEDIEYGNCTKYYKGTGYYTCVEVIFTLRRQVGFYMMGVYAPTLLIVVLSWLSFWINPDASAARVPLGIFSVLSLASECTTLAAELPKVSYVKALDVWLIACLLFGFASLVEYAVVQVMLNNPKRVEAEKARIAKAEQADGKGGNAAKKNTVNGTGTPVHISTLQVGETRCKKVCTSKSDLRSNDFSIVGSLPRDFELSNYDCYGKPIEVNNGLGKPQAKNKKPPPAKPVIPTAAKRIDLYARALFPFCFLFFNVIYWSIYL
Protein: MFS gliotoxin efflux transporter gliA (Gliotoxin biosynthesis protein A) (E9R876)
Organism: Aspergillus fumigatus (strain ATCC MYA-4609 / CBS 101355 / FGSC A1100 / Af293) (Neosartorya fumigata)
Function: Efflux pump that provides the dual role of gliotoxin export and self-protection by allowing the fungus to evade the harmful effect of its own gliotoxin production. Moreover, it contributes also to the virulence through gliotoxin secretion.
Subcellular location: Cell membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
Sequence:
MSRPSIEESKQELSSSPNDSVMGKDPAPEEEMQYPSGFALSVIMAGLLAAIFLISLDTTIVSTAIPRITDEFHTVADIGWYGSAFFLTLASFQGTWGKIYRYFPLKLSFLAAVLLFEVGSLICAVAKNSVTLIVGRAIAGIGAAGISSGSYTILAFSVHPRRRAAMTGAIGASFAVAAVAGPLIGGAFTSHTTWRWCFWINLPIGGVSAGLIAIFFKAPPQARAKDVPYKEILLQMDPSGIVLLLGAILCFLLALQWGGSAKAWGNADVVGTLVGFGLLLIAFAINELWLQEKAMIPPRLFKGQTILFSSLFTFFFSGSFYLLLYYLPTYFQSVKGASASDSGVRTLPLVLGDGLFATLSGAVLGIIGYYMPLLTLGGVLTTVASGLLYTLDLDSGANAWIGYQAMAGIGIGLAIQVPMMASQAVVRVEDLSTVSAIVLFFQCMGGAIFVQAGQAAFTNKLVQEVQRHLPNISAARVTSTGATELQSEFHGHELQVILEAYVAGLKDAFIVAIVLAGIATLLSFGSGWRSVKSKKEEPKAQP
Protein: Uracil-DNA glycosylase (UDG) (EC 3.2.2.27) (Q388K2)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Subcellular location: Mitochondrion {ECO:0000256|HAMAP-Rule:MF_03166}. Nucleus {ECO:0000256|HAMAP-Rule:MF_03166}.
Interaction partners:
- Uncharacterized protein
- Proliferating cell nuclear antigen
- DNA-
- DNA-
- histidine--tRNA ligase
- DNA damage-binding protein 1
- Bifunctional dihydrofolate reductase-thymidylate synthase
- thioredoxin-dependent peroxiredoxin
- thioredoxin-dependent peroxiredoxin
Sequence:
MVQRTLFDFVSKKGDNATTEEVGSKTESGQPSASSRKRTAEDQVANGGASNLTRARVAKENNGALASLIVDPGWEAFLKPLTTSSNFERIEKFLEGELNAGKTILPPREMIFSAFNSTPLDMLKVVLLGQDPYHNVGQAHGLCFSVLPGVPPPPSLINMYKELATDIPGFVAPQHGYLQHWAEQGVLMLNATLTVEIHKANSHATCGWQTFTDDVIRLLSEKHKNPLVFLLWGGFAKRKISLIDRKRHVVIECAHPSPLSAAKWWGSRPFSKCNTALVEKKLSPIDWKLPVCLSKGK
Protein: Protein POF1B (Q8K4L4)
Organism: Mus musculus (Mouse)
Function: Plays a key role in the organization of epithelial monolayers by regulating the actin cytoskeleton. May be involved in ovary development (By similarity).
Subcellular location: Cell junction, tight junction {ECO:0000250}.
Interaction partners:
Sequence:
MMSSSYWSETSSSSCGTQQPTEVLQCQPQHYHYYHQPSQAQQPPEKNVVYERVRTYSGPMNKVVQALDPLGSREVLSPLKPASSYQSLVWSDHSQELYSPTLKISTCAPSTLHITQNAEQELHSPTVKVTTYPQTTIRRYIVQNPEQEPLSPFLRGSQFFPGNNVIYEKTIRKVEKLNTDQECCPQIQCHHHVIQQPQIIHSPHCQQSHSSHQIQCITENDSNIGHELCHGGPSQIHEQVIIQDDGPEKLDPKYFGELLADLSRKNTDLYHCLLEHLERIGGSKQDFESTDTSEDIESLIPKGLSEFTKQQIRYILQMRGMSDKSLRLVLSTFSNIREELGHLQNDLTSLENDKIRLEKDLAFKENQMKEYEELLASVRANNRQQQQGLQDSSAKCQSLEENNLSLRHTLSDLEYRLKELEYCKRNLEQENKNLRIQVSETCTGPTLQAKMDEIGNHYMEMVKNLRLDKDREISKLRSQLNQYQKDVSKREGSCSDFQFKLHELTSLLEEKDSLIKRQSEELSKLRQEIYSSHNQPSCGGRTTITTKKYRTQYPILGLLYDDYEYIPPGSDTQTIVIEKTEDKWTCP
Protein: D-xylose-proton symporter-like 2 (Q6AWX0)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}.
Interaction partners:
Sequence:
MALDPEQQQPISSVSREFGKSSGEISPEREPLIKENHVPENYSVVAAILPFLFPALGGLLYGYEIGATSCATISLQSPSLSGISWYNLSSVDVGLVTSGSLYGALFGSIVAFTIADVIGRRKELILAALLYLVGALVTALAPTYSVLIIGRVIYGVSVGLAMHAAPMYIAETAPSPIRGQLVSLKEFFIVLGMVGGYGIGSLTVNVHSGWRYMYATSVPLAVIMGIGMWWLPASPRWLLLRVIQGKGNVENQREAAIKSLCCLRGPAFVDSAAEQVNEILAELTFVGEDKEVTFGELFQGKCLKALIIGGGLVLFQQITGQPSVLYYAPSILQTAGFSAAGDATRVSILLGLLKLIMTGVAVVVIDRLGRRPLLLGGVGGMVVSLFLLGSYYLFFSASPVVAVVALLLYVGCYQLSFGPIGWLMISEIFPLKLRGRGLSLAVLVNFGANALVTFAFSPLKELLGAGILFCGFGVICVLSLVFIFFIVPETKGLTLEEIEAKCL
Protein: At5g54760 (Protein translation factor Sui1 homolog) (Translation initiation factor SUI1 family protein) (Q9FFV1)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- Eukaryotic translation initiation factor 4C
- Eukaryotic translation initiation factor 4C
- Eukaryotic translation initiation factor 3 subunit A
- Eukaryotic translation initiation factor 3 subunit E
- Eukaryotic translation initiation factor 3 subunit G
- Eukaryotic translation initiation factor 3 subunit C
- Eukaryotic translation initiation factor 3 subunit C
- Eukaryotic translation initiation factor 3 subunit G
- Eukaryotic translation initiation factor 3 subunit I
- Eukaryotic translation initiation factor 3 subunit I
Sequence:
MSELDSQVPTAFDPFADANVEDSGAGTKEYVHIRVQQRNGRKSLTTVQGLKKEYSYTKILKDLKKEFCCNGTVVQDSELGQVIQLQGDQRKNVSTFLVQAGLVKKDNIKIHGF
Protein: Blue copper protein 1b (MtBcp1b) (A0A072U307)
Organism: Medicago truncatula (Barrel medic) (Medicago tribuloides)
Subcellular location: Membrane {ECO:0000255}; Single-pass type I membrane protein {ECO:0000255}.
Interaction partners:
Sequence:
MASSRVVLILSISMVLLSSVAIAATDYIVGDDKGWTVDFDYTQWAQDKVFRVGDNLVFNYDPSRHNVFKVNGTLFQSCTFPPKNEALSTGKDIIQLKTEGRKWYVCGVADHCSARQMKLVITVLAEGAPAPSPPPSSDAHSVVSSLFGVVMAIMVAIAVIFA
Protein: Voltage-dependent N-type calcium channel subunit alpha-1B (CHCACHA1B) (Voltage-gated calcium channel subunit alpha Cav2.2) (O73706)
Organism: Gallus gallus (Chicken)
Function: The isoform alpha-1B gives rise to N-type calcium currents. N-type calcium channels belong to the 'high-voltage activated' (HVA) group. Calcium channels containing alpha-1B subunit may play a role in directed migration of immature neurons (By similarity). Mediates Ca(2+) release probability at hippocampal neuronal soma and synaptic terminals (By similarity).
Subcellular location: Membrane {ECO:0000250|UniProtKB:Q00975}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Voltage-dependent R-type calcium channel subunit alpha
- Voltage-dependent L-type calcium channel subunit beta-2
- VWFA domain-containing protein.
- SH3 domain-containing protein.
- Calcium voltage-gated channel auxiliary subunit alpha2delta 2.
- Calcium voltage-gated channel auxiliary subunit alpha2delta 3.
- Voltage-dependent L-type calcium channel subunit beta-3
- Calcium voltage-gated channel auxiliary subunit beta 1.
- VWFA domain-containing protein.
- Syntaxin 1A
Sequence:
LVTEIADTDNFINLSFLRLFRAARLIKLLRQGYTIRILLWTFVQSFKALPYVCLLIAMLFFIYAIIGMQVFGNIALNDETSINRHNNFRTFLQALMLLFRSATGEAWHEIMLSCLSNRACDPLSGLTKNECGSDFAYFYFVSFIFLCSFLMLNLFVAVI
Protein: Protocadherin 11 X-linked (Protocadherin 11 isoform 8) (Q2TJH7)
Organism: Mus musculus (Mouse)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004251}; Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004251}.
Interaction partners:
Sequence:
RCRQPPHLKASQKNKQNSEWVTPNPENRQMIMMKKKKKKKKKHPPKNLLLNFVTIEEAKPDDGENERNSVTLDLPIELEEQTMGKYNWGTTPTTFKPDSPDLARHYKSASPQPAFQIQPETPLNSKHHIIQELPLDNTFVGCDSISKCSSSSSDPYSVSECSYPVTTFKAPVSVHIRPTMKEVVRSHTPMKEATTVEIWTHPHPQRRSDGKKAGKSQRRVTFHLPEGSQESISDGGLGDHDAGSLPSTSHALPLGYPQEEYFDHAAPNNRTEGDGNSDPESTAEITVQPTVEEASDTCTQECLILGHSDSCWMPATLTNPSPSQIKTSAICHSPPRPRLSVRRYSPPVTQTVTICHSPPVTQAIALCHSPPPVQVTVPRHSPPPAQASAVSYSPTLVQAVVIHHSPPLPQAATHHRTQAQPPMGLQQGWVQGAGADGLYPIDQGVQGSTRAQFYTMAERFHPDDDSIKVIPLTTFTSGQQARSSRGDSPIIEEHPL
Protein: Probable cell division protein WhiA (Q9Z515)
Organism: Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145)
Function: Involved in cell division and chromosome segregation (By similarity). Involved in sporulation. May coordinate the cessation of aerial hyphae growth and subsequent chromosome segregation and/or septation. Required for expression of the ParB partioning protein during sporogenesis. Activates its own transcription and represses WhiB. Binds with low affinity to its own promoter and to the Parp2 sporulation-specific promoter. Also binds directly to the RNA polymerase sigma factor WhiG, leading to inhibition of WhiG-dependent transcription in a dose-dependent manner.
Interaction partners:
- RNA polymerase sigma factor WhiG
- Putative gluconeogenesis factor
- Cell division protein FtsZ
- Nucleotide-binding protein SCO1952
- Protein-export membrane protein SecG
- Phosphoenolpyruvate transferase
- UvrABC system protein C
- DNA-binding protein
- Transcriptional regulator WhiD
- Cell division protein CrgA
Sequence:
MTAAVKSEISQLPVTRTCCRKAEVSAVLRFAGGLHLVSGRIVIEAELDTGNAARRLKRDILEIFGHSSELIVMAPGGLRRGSRFVVRVVAGGDQLARQTGLVDGRGRPIRGLPPQVVSGATCDAEAAWRGAFLAHGSLTEPGRSSSLEVTCPGPEAALALVGAARRLSIPAKAREVRGVDRVVVRDGDAIGALLTRLGAHDSVLAWEERRLRREVRATANRLANFDDANLRRSARAAVAAGARVQRALEILADDVPEHLAAAGRLRMEHKQASLEELGALADPPLTKDAVAGRIRRLLAMADKRASDLGIAGTDANLGEEELADNLVG
Protein: BCL2-related protein A1 (G3V977)
Organism: Rattus norvegicus (Rat)
Subcellular location: Mitochondrion {ECO:0000256|ARBA:ARBA00004173}.
Interaction partners:
- BCL2-antagonist/killer 1, isoform CRA_b.
- Bcl-2-modifying factor
- BH3-interacting domain death agonist
- Bcl-2-like protein 11
- Phorbol-12-myristate-13-acetate-induced protein 1
- Bcl2-interacting killer, isoform CRA_a.
Sequence:
MTDCEFMYIHSLAENYLQYVLQVPAFESAPSKTSRVLQRVAFSVQKEVEKNLKPYLDDFHVESIDTARIIFNQVMEKEFEDGIINWGRIVTIFAFGGVLLKKLPQEQIALDVDTYKQVSSFVAEFIMNNTGEWIQQNGGWEDGFTKKFEPKSGWLTFLQMTGKIWEMLFLLKQHY
Protein: EGF-like domain-containing protein (H2L041)
Organism: Caenorhabditis elegans
Interaction partners:
Sequence:
MRLLFLVFILAEIMLQNEIMADHRTINQSFRGNFFRRRNYDGPRAYQIAPDLTCSYDNQCAGYPLAICHSVCQCVKGALNTGTTCIASSTAIQTSVACPAGQTYIREAGVCMTVQQPGEPCQYSQQCSALEPGAYCLKMRCECVYGMKKSSNGCTFVNNDCKERGHIFISEIGECREVFPPGGKGCSHNLQCSGAYPDATCFMQTCTCPPNLPVAADGTCGRSCPNNQVYSGVTGECLPEKQPGQDCIYSSQCQASFGGLVCDKNTCRCPNGLVFDGLKCSHGCPPHKRVIDKEICVEGCPSGIVEVAGRCVKQVSIGQPCVANAQCNFGSFCQSGTCQCPPGFYVQDEQCQAIESEPNESCQNNEKCTKGSVCYNGKCSCPRNHELINGHCQQNRAVPIGSACVRIGVTCDGGSVCVAGICVCPLGKTPRNGVCIEHVAARPGTSCQNEEECVDHSYCSPETNKCECMKASQMVIGGECRERLKAHPGYGCTMGEMCVGNSVCVNGKCACVDGKVEINKICIDQVSAKPGDTCGKGIICEGGSYCNTDSGKCACRRGENSINGICKGFTFVYPGDLCTDITSRCTGGSYCARGRCECPPRMSAIDKKCVHQQTAAPGEPCSEKVACSPFSVCENNVCKCVNNMMIRDKMCVQRRKVNIGNSCNNEDQCLGNSTCMDNNCQCGIGFVASMDVCVLRKTVTPGYLCNPEDICTGQSVCIKGVCQCQPDYKQMHNICVKKNIGIEGSPCSSRDDCGEGLMCGASGKCSCPEGLFSVNGKCRSYVQLGQTCTSDDRCAERNAQCQENYCTCRTGYTNINGQCAANIVTPAEPETLSQVKSGLLGHICTSNDHCKIAHSQCRRNVCQCIDGYRIFGSTQCIPRPGKPKERKTEKESKLVELGDKCDKLSLCSKGAICEKGVCSCPETFFESDGACVKNVAKIKVVVPPLSSCLGGEECSGNSECVHGICFCKEEFTLFEGKCQRLRIIEKLTVLESKKLIKPIKAHTTPTAASNTTPIPVKTTTTLQTTTATTLPENYVSSSTNRPLTPIIISMKLGSTSSPSPQITSNPEYKWRLSKPGHMCDNKTHCTNCSVCVNGFCRCPEGLVHYGDKCVSEIDATKCLASNQCPSGAQCVKGECRCKPGLGITRYGFCVPITFAEPGTSCAYGEHCQKDSHCEDGLCTCNEPLVLKENKCVVSPREQTRRRQPSRLLTECPRDGSCRLPSCFCTSTGKIPPNNFDTKQVPQMVMLSFDDPITDRIINTLKSLFSGSIRNPNGCAIKGTFFVSHQWNNYDQSLWLHSTNHEIGVNSITREDLSGRTQERWYKEQKGMRETLAEFSFIDRSHIIGTRAPELKIGGDAQYRMMSENNFTFDNSMLVSSPYWPQTLDHKLAWECDGNCPTQSHKAIWEIPIQNIQANDTRWYKTLTRAMKPFDSRDSVTKMLQRNFMNHYKTNRAPFILTLDTEFLTYLPDNGAVYALRDFLKFIVQKQDVFVVTGSQIIDYMRNPVDLNNIKSLRSWQCKPQMKDEANPCENPTTCSFSGRARGQFAHSFRMCGVCPKSYPWI
Protein: Brevinin-2Rc (P86024)
Organism: Pelophylax ridibundus (Marsh frog) (Rana ridibunda)
Function: Antimicrobial peptide.
Subcellular location: Secreted {ECO:0000305}.
Interaction partners:
Sequence:
GLMSTLKGAATNVAVTLLNKLQCKLTGTC
Protein: FRIGIDA-like protein 1 (AtFRIL1) (Protein SUPPRESSOR OF FRI 8) (Q9FFF1)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Required for FRI-mediated up-regulation of FLC transcripts, but not redundant with FRI and only partially redundant with FRL2. Required for the stabilization of the FRI-C complex.
Interaction partners:
- Protein SUPPRESSOR OF FRI 4
- Protein FRIGIDA-ESSENTIAL 1
- Protein FLC EXPRESSOR
- Protein FLX-like 4
- Inactive protein FRIGIDA
- Transmembrane protein
- Putative mitochondrial outer membrane protein porin 5
- ENHANCER OF AG-4 protein 2
- Transcription initiation factor TFIID subunit 14
- Protein VERNALIZATION INSENSITIVE 3
Sequence:
MTASETIATAINQIDEKKEKLKKAFDDLQAHRSLLSPSFSLSWSEIDSHFSSLQSSLASRFRLLHSTSPLEHDSYRIDASDAGKSSSSEEVSEQPVVEPELRALCEKIDGIGLIKYLIRIWDDETPLNQEVSAAIRYSPDTASMVLDAIEGSNYTPSSSGRSFDVRRVFVLLMEVLIEINANITVDTRNRAKKLAYHWKSKVGVKPFEALVFLHLVAAFELGSEFDTEELSDYVFMIAKYKQATLVCNKIGVDRKRVGKLIKTLLDSGKPILAVKFMYECGMTDEFEPIPVLKSYIKDCREAALRVCVEDNYSLKSQNEASDKEVSALKPLIKIIKDQNLESEFTQEKVEERVEELEKNKALRKRNTTNPPKQEPQQKGKKRTRDCKNGSQVPVPSQQLLSRPEALLMPEHSHHGLQLNPYGLMTSAFSGVVVNPLTGLFGSGATPQSLYYAQQTGYVLPPQYHPPYYSQ
Protein: Sticks and stones, isoform C (A0A0B4LEH1)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004479}; Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004479}.
Interaction partners:
Sequence:
MALQQQHQRHQQHQQHQQQQQQQQQQQHIKWQQHATKRRRCRQHWIKHLQLLRLLAVIVLASAPVPSHAQQQKFRTTPHDLQVLEGAEAMMRCEVANVAGAVQWTKDGFALGFSAVIPGFPRYSVLGDRKQGIYNLRISNASINDDADYQCQVGPARLNSAIRANAKLTVISPPASIEIKGYSHNSKVEVRENQDLQLKCIVANAKPAAQIVWYRGNVEYKPEKREDTVEESTAKRFTTTSSLKLKPGPDDDYTEYTCQARHKALSPDMPMRATVQLSVLYPPGPPYIEGYSAGETLRRGQTVELMCRSRGGNPPAQLIWYKNGSQIRMAYRTSGRLSENIYTFTAEAGDNKARFRCEASNVMSQNPLKAEVELSVLFAPTHVTVMGPTEARVGDIVPLTCTTAPSNPPAEIKWMVGGRQVRNATSKTIVSPEGGWTTTSNITAVVEPNKRSLVVICHGLNMQLTENVVSTHTINVLYPPAPPLISGYMEGQIIPAGSVQKLLCVSSGGNPLATLTWYKNDKRINSVIRAADKSVSAEITILANVSDNQAQYRCEASNSATEIPLFQSTTLSVHFAPETVKIRIEPEELRPGMEATIICDSSSSNPPAKLSWWKDGIPIEGINNTSKPGLWGGTVSTLEFRVNVTQEMNGQVYTCQSANEALQRSAHEAVSLDVLYRPKFVPPPSSTAVGVEGESLQVSLQTRANPTPVTYKWTKDGTTIPQDGDHRIFADGGSLNFTRLHRDDAGIYSCSASNSQGGATLNITVVVEYGTTIKSVSENIVVNPGEDAMLSCTVEGKPLTEEHVKWERVGYDMTVKTSTTFANGTSYLHIKDAKREDVGNFRCVADNRVDNPTNRDILLIVKFAPEIAKTPTLLRAASGTGERGRLPCRAQGSPKPQFIWRQDKKDLPINRTYKYEVEERKIDSLTYESTLIVDKVAPADYGAYECVARNELGEAVETVRLEITSQPDPPLSLNILNVTHDTVTLAWTPGFDGGLKASYRVRYRMADREQYKYIDGLPNSHKLTIGGLRMNTLYLFSVMSWNELGQSSYLPDLARAETKEAPPPSHPASSLGGGPPTTSQTPLGGTSGMLLVGVGAGIVVVLLNVFVIGCCLHKRNEKRLKRVAETTNQPAKTATIEMYAPSSYNDTVTGETLSSVSEKSESYSNEGSSQPEYIDEVRKKAASTYLVEGSDMPPPRYQKDGTLPVIYPNNVVNACTLPHPRHNNGSAAIHMTRDDQMLISKGVYIPSPSPAPPPDGSYYNMNSDRYLSYPPMEYPAALDFTAQPMPMAHLQPMTVTSLATNGGPTLIGNGSVAAVAGGSGTLRRGILRGVVGVPQPDVTHHTSTVGGSPMQMLHDLHPVNLSASTLTTSTTLNGSLPTATATLPRQPHGILKDPNRNKQQQQQQQQQQQQQQLQHQQQLLNASLVGVGVPVSAPLGSLQILNLPPASGGLGNNLLMTTNAFDPTTVGLSSFGAVSQAGGIPVAYTDADGHLV
Protein: Two component transcriptional regulatoryprotein (A0A0H3LF05)
Organism: Mycobacterium tuberculosis (strain ATCC 35801 / TMC 107 / Erdman)
Interaction partners:
Sequence:
MVKVFLVDDHEVVRRGLVDLLGADPELDVVGEAGSVAEAMARVPAARPDVAVLDVRLPDGNGIELCRDLLSRMPDLRCLILTSYTSDEAMLDAILAGASGYVVKDIKGMELARAVKDVGAGRSLLDNRAAAALMAKLRGAAEKQDPLSGLTDQERTLLGLLSEGLTNKQIADRMFLAEKTVKNYVSRLLAKLGMERRTQAAVFATELKRSRPPGDGP
Protein: Acetylcholine receptor subunit delta (P25110)
Organism: Rattus norvegicus (Rat)
Function: After binding acetylcholine, the AChR responds by an extensive change in conformation that affects all subunits and leads to opening of an ion-conducting channel across the plasma membrane.
Subcellular location: Postsynaptic cell membrane; Multi-pass membrane protein. Cell membrane; Multi-pass membrane protein.
Interaction partners:
- Acetylcholine receptor subunit alpha
- Acetylcholine receptor subunit beta
- Neuronal acetylcholine receptor subunit alpha-9
- Acetylcholine receptor subunit epsilon
- Neuronal acetylcholine receptor subunit alpha-4
- Neuronal acetylcholine receptor subunit beta-3
- Neuronal acetylcholine receptor subunit alpha-5
- Neuronal acetylcholine receptor subunit beta-4
- Neuronal acetylcholine receptor subunit beta-2
- Neuronal acetylcholine receptor subunit alpha-3
Sequence:
MAGPVPTLGLLAALVVCGSWGLNEEQRLIQHLFEEKGYNKELRPVARKEDIVDVALSLTLSNLISLKEVEETLTTNVWIDHAWIDSRLQWNANEFGNITVLRLPSDMVWLPEIVLENNNDGSFQISYACNVLVSDSGHVTWLPPAIFRSSCPISVTYFPFDWQNCSLKFSSLKYTAKEIRLSLKQEEEDNRSYPIEWIIIDPEGFTENGEWEIVHRAAKVNVDPSVPMDSTNHQDVTFYLIIRRKPLFYIINILVPCVLISFMINLVFYLPGDCGEKTSVAISVLLAQSVFLLLISKRLPATSMAIPLVGKFLLFGMVLVTMVVVICVIVLNIHFRTPSTHVLSEGVKKFFLETLPKLLHMSRPEEEDPGPRALIRRTSSLGYISKAEEYFSLKSRSDLMFEKQSERHGLARRLTTARKPPASSEQVQQELFNEMKPAVDGANFIVNHMRDQNSYNEEKDNWNQVARTVDRLCLFVVTPVMVVGTAWIFLQGVYNQPPPQPFPGDPFSYDEQDRRFI
Protein: DNA polymerase theta (Helicase domain only), putative (Q57YX8)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- DNA-directed DNA polymerase
Sequence:
MRKTVVRLKTFNPPQQLQGGNSSSVQLTRTNANIVTGNDNDKSRASSRAVTSVPERTLQSAAAPALQRVKRGREELPQNNSASGLSGVGAVIMPSSQFSEVGPWSQFMREGAADLTAHPHAVPTSTEGDAPPRDFCDGDEDDMPPVSQEELQREAEEDMRLSTDVILTPGTPNGNTCEPFSSVSAVPTCTLTVPSLNSEVSQISTGLDYGNVYGHVPFGTPVINDNVPSGTSASALPRPSVDDPDFFYDLPVSVKDFYATRRGIKKLYNWQHEVLMRDDIRAGGSLVYSLPTSGGKTLVAEISLLRCLINRGQSCLFVLPFVSLAEEKTDAMIPLGDVLGFTVDGHYSTRGRFPLPVSKAVFVCTIEKANSLVNHMLEENTIGRIGTIVVDELHMLGETSRGATLELLLTKLLCLRHKVQIIGMSATIPNLPDIARWLRASCYIGNYRPVPLRQYAVVGGEVLEDGREVCRSLVAAGHTSESSQLVFLTTEVKGASVLVFCASRQQTVSTARLIARSRKEEVDKEGGVRYNASSLALVADLRALDSEESSLLSQLVPYGVAFHHGGLVAEERTLIETAFRRRSIGVLCCTSTLAAGVNLPARRVIFKTPFVAVDFLTKSRYLQMCGRAGRAGLDEFGESFLFLSRKDRNRGCELMQQEVEACVSQLLEEKSTVERALLEFVAIGLIRSLSDARKWGENILFHHAPGPIDKGLNAGSVAVPEMLEGIIQSALSKLVERGLMQRLSRPAADASREDSDVLGDSDVTNAKNGDAKNNGTGDGDAILSSSPFGSCSVRSCFGVEDALIVRLELEKLQQSGLILADDLHMCYFVTPLRDPIDVDWSIYRDILSQLNETRQRIASMIGVDEFYVNQRAMGLGDAGGNGGGRAFATRRFYAALALADLLNEVPIGEVEQRYRCNRGQLQNLLRSASMFSSSITSFCRAMEWYSLEAVLASFVKRLGFGVKPDIIPLMEIKGVQPGRARALWRAGFKDPAAVAACTPAELLKRVKEANPPDSKVVKYFSIRSAVVVLREANAWVQQNIREKKGDLADLTLQSSTY
Protein: ESX-1 secretion system protein EccD1 (ESX conserved component D1) (Snm4 secretory protein) (Type VII secretion system protein EccD1) (T7SS protein EccD1) (P9WNQ7)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: Part of the ESX-1 specialized secretion system, which delivers several virulence factors to host cells during infection, including the key virulence factors EsxA (ESAT-6) and EsxB (CFP-10).
Subcellular location: Cell inner membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- ESX-1 secretion-associated protein EspI
- ESX-1 secretion system ATPase EccB1
- ESX-1 secretion system protein EccCa1
- 6 kDa early secretory antigenic target
- ESX-1 secretion system protein EccCb1
- ESX-1 secretion system protein EccE1
- ESX-1 secretion-associated protein EspK
- ESAT-6-like protein EsxB
- ESX-1 secretion-associated protein EspJ
- ESX-1 secretion-associated protein EspE
Sequence:
MSAPAVAAGPTAAGATAARPATTRVTILTGRRMTDLVLPAAVPMETYIDDTVAVLSEVLEDTPADVLGGFDFTAQGVWAFARPGSPPLKLDQSLDDAGVVDGSLLTLVSVSRTERYRPLVEDVIDAIAVLDESPEFDRTALNRFVGAAIPLLTAPVIGMAMRAWWETGRSLWWPLAIGILGIAVLVGSFVANRFYQSGHLAECLLVTTYLLIATAAALAVPLPRGVNSLGAPQVAGAATAVLFLTLMTRGGPRKRHELASFAVITAIAVIAAAAAFGYGYQDWVPAGGIAFGLFIVTNAAKLTVAVARIALPPIPVPGETVDNEELLDPVATPEATSEETPTWQAIIASVPASAVRLTERSKLAKQLLIGYVTSGTLILAAGAIAVVVRGHFFVHSLVVAGLITTVCGFRSRLYAERWCAWALLAATVAIPTGLTAKLIIWYPHYAWLLLSVYLTVALVALVVVGSMAHVRRVSPVVKRTLELIDGAMIAAIIPMLLWITGVYDTVRNIRF
Protein: mitogen-activated protein kinase kinase (EC 2.7.12.2) (Q7YTF7)
Organism: Plasmodium falciparum (isolate 3D7)
Interaction partners:
- Histone chaperone ASF1, putative
- Crossover junction endonuclease MUS81
- DNA helicase
Sequence:
MKDILSNYSNLIYLNKYVKEKDKYINDYRIIRTLNQGKFNKIILCEKDNKFYALKKYEKSLLEKKRDFTKSNNDKISIKSKYDDFKNELQIITDIKNEYCLTCEGIITNYDEVYIIYEYMENDSILKFDEYFFVLDKNYTCFIPIQVIKCIIKSVLNSFSYIHNEKNICHRDVKPSNILMDKNGRVKLSDFGESEYMVDKKIKGSRGTYEFMPPEFFSNESSYNGAKVDIWSLGICLYVMFYNVVPFSLKISLVELFNNIRTKNIEYPLDRNHFLYPLTNKKSTCSNNFLSNEDIDFLKLFLRKNPAERITSEDALKHEWLADTNIEDLREFSKELYKKRKKL
Protein: DnaJ homolog subfamily B member 3 (DnaJ protein homolog 3) (Heat shock protein J3) (HSJ-3) (MSJ-1) (O35723)
Organism: Mus musculus (Mouse)
Function: May operate as a co-chaperone of the male germ cell- and haploid stage-specific Hsp70 proteins.
Interaction partners:
- Heat shock 70 kDa protein 1A
- Heat shock 70 kDa protein 1B
- Heat shock-related 70 kDa protein 2
- Heat shock cognate 71 kDa protein
Sequence:
MVDYYEVLGVPRQASAEAIRKAYRKLALKWHPDKNPEHKEEAERRFKQVAQAYEVLSDVRKREVYDRCGEVGEVGGGGAAGSPFHDAFQYVFSFRDPAEVFREFFGGHDPFSFDFFGGDPLENFFGDRRSTRGSRSRGAVPFSTSFTEFPGFGGGFASLDTGFTSFGSPGNSGLSSFSMSCGGGAAGNYKSVSTSTEIINGKKITTKRIVENGQERVEVEEDGELKSLIINGREQLLRINTQ
Protein: Retinol dehydrogenase 13 (EC 1.1.1.300) (Short chain dehydrogenase/reductase family 7C member 3) (Q8NBN7)
Organism: Homo sapiens (Human)
Function: Retinol dehydrogenase with a clear preference for NADP. Oxidizes all-trans-retinol, but seems to reduce all-trans-retinal with much higher efficiency. Has no activity toward steroids.
Subcellular location: Mitochondrion inner membrane {ECO:0000269|PubMed:18039331}; Peripheral membrane protein {ECO:0000269|PubMed:18039331}. Note=Localized on the outer side of the inner mitochondrial membrane. {ECO:0000269|PubMed:18039331}.
Interaction partners:
- 3-ketodihydrosphingosine reductase
Sequence:
MSRYLLPLSALGTVAGAAVLLKDYVTGGACPSKATIPGKTVIVTGANTGIGKQTALELARRGGNIILACRDMEKCEAAAKDIRGETLNHHVNARHLDLASLKSIREFAAKIIEEEERVDILINNAGVMRCPHWTTEDGFEMQFGVNHLGHFLLTNLLLDKLKASAPSRIINLSSLAHVAGHIDFDDLNWQTRKYNTKAAYCQSKLAIVLFTKELSRRLQGSGVTVNALHPGVARTELGRHTGIHGSTFSSTTLGPIFWLLVKSPELAAQPSTYLAVAEELADVSGKYFDGLKQKAPAPEAEDEEVARRLWAESARLVGLEAPSVREQPLPR
Protein: CLIP domain-containing serine protease (EC 3.4.21.-) (A0A0B4KI65)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Secreted {ECO:0000256|RuleBase:RU366078}.
Interaction partners:
Sequence:
MKVIAAVLLCLLIIRTAHGQYVSCRNPNQRTGYCVNIPLCVPLNSVLAKSNPTDSEMRFIRESRCLVSDQSDLPFVCCTPDTDYNTTRARPNDEVIHSTLLPDRSICGGDIAYNQITKGNETVLTEFAWMVLLEYRPHDGQQLRTYCAGSLINNRYVVTAAHCVSAATRARKGDVVSVRLGEHNTSAVVDCLNGRCLPEPVQIAVEEIRIHESFGTRLFWNDIALIRLAREVAYSPSIRPVCLPSTVGLQNWQSGQAFTVAGWGRTLTSESSPVKMKLRVTYVEPGLCRRKYASIVVLGDSHLCAEGRSRGDSCDGDSGGPLMAFHEGVWVLGGIVSFGLNCGSRFWPAVYTNVLSYETWITQNIRP
Protein: Interferon regulatory factor 3 (D2SQZ9)
Organism: Salmo salar (Atlantic salmon)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MSQSKPLLIPWLREQINSGQYPGVTWTNQERTEFCIPWKHALRQDSCSDDVLIFKAWAEVSNGRVQGDPSIWKRNFRSALRAKGFKMLLDNKNDAANPNKLFQWPDEAPTGGSQHPEHDLYQDPSPLQESDGLPCLNDLYHAAEETVYTEGISTTFNQDILQKCLQGLNIEQTAGNQPFQCGTLDQGSPTEAIQGYELTVEQRQYPMEGAIGGHVLQGQQQYPVVMEDAVGGAVLPPQPVYPMDGPVGGAHEQQVVEQFTNELSRTMVGENFKTHFRVSVYYRGLKMLEQLVENEAGFRLVYRPELTQPLLDPDSGLNLVSLPSPPPVRDETQAKLTQDILALLGEGLEVGASGPIIYGLRKGGIKAFWSLDKFDKSRRPQAVSKFPEPLYQAKDFYGGLLKFMDSHRGECPPFSLFFCLGEKWPDPDNRPWEKKLVMVEVVLTALELLKSIAVEGGASSLQSVELQLSLQESLQEVMDLC