wanglab/gogpt-training-data huggingface dataset:
Protein: Laccase-C1 (EC 1.10.3.2) (Benzenediol:oxygen oxidoreductase C1) (Diphenol oxidase C1) (Lac C1) (Urishiol oxidase C1) (P86328)
Organism: Cerrena unicolor (Canker rot fungus) (Daedalea unicolor)
Function: Lignin degradation and detoxification of lignin-derived products (Probable). Oxidation of a broad range of substrates including mono-, di- and polyphenols, aromatic amines and methoxy-substituted phenols accompanied by reduction of oxygen to water.
Subcellular location: Secreted {ECO:0000269|PubMed:20175123}.
Interaction partners:
Sequence:
AIGPVADIDIDVVSLGMVDQSLLREMHEVSNVALQAMKGSDEYDFNANLRLVLWNQPDFMWLR
Protein: Protein S100-A13 (S100 calcium-binding protein A13) (P97352)
Organism: Mus musculus (Mouse)
Function: Plays a role in the export of proteins that lack a signal peptide and are secreted by an alternative pathway. Binds two calcium ions per subunit. Binds one copper ion. Binding of one copper ion does not interfere with calcium binding. Required for the copper-dependent stress-induced export of IL1A and FGF1. The calcium-free protein binds to lipid vesicles containing phosphatidylserine, but not to vesicles containing phosphatidylcholine.
Subcellular location: Cytoplasm. Secreted. Note=Secretion is mediated by exposure to stress and requires copper ions.
Interaction partners:
- Synaptotagmin-1
- Fibroblast growth factor 1
- Interleukin-1 alpha
- Advanced glycosylation end product-specific receptor
- Protein S100-A6
- Sphingosine kinase 1
Sequence:
MAAETLTELEAAIETVVSTFFTFAGREGRKGSLNINEFKELATQQLPHLLKDVGSLDEKMKTLDVNQDSELRFSEYWRLIGELAKEVRKEKALGIRKK
Protein: OriC-binding nucleoid-associated protein (H-NS/StpA-binding protein 2) (Transcription modulator YdgT) (P64467)
Organism: Escherichia coli (strain K12)
Function: Modifies the set of genes regulated by H-NS; Hha and Cnu (YdgT) increase the number of genes bound by H-NS/StpA and may also modulate the oligomerization of the H-NS/StpA-complex on DNA. The complex formed with H-NS binds to the specific 26-bp cnb site in the origin of replication oriC. Can complement, at least partially, the absence of the Hha protein in hha mutants.
Interaction partners:
- DNA-binding protein H-NS
- DNA-binding protein StpA
- Inner membrane protein YdgK
Sequence:
MTVQDYLLKFRKISSLESLEKLYDHLNYTLTDDQELINMYRAADHRRAELVSGGRLFDLGQVPKSVWHYVQ
Protein: Uncharacterized protein C11D3.16c (Q10095)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Interaction partners:
Sequence:
MTTLKVDEDLECALMEQFIEALHQRCTDIPRTQLCVLAISFNRFILHKSPDIFTYIQYYQQKLNSYGFPLPPVVLKSLQMPLTSPEPDADERFRDGDTEFDTAGVTASSCFPVDVKSPSVRAFGNVTFQSD
Protein: Guanine nucleotide-binding protein alpha-3 subunit (G alpha-3) (Q54KV6)
Organism: Dictyostelium discoideum (Social amoeba)
Function: Guanine nucleotide-binding proteins (G proteins) are involved as modulators or transducers in various transmembrane signaling systems. G alpha-3 plays a role in development. G alpha-3 mutants fail to aggregate.
Interaction partners:
- Latrophilin receptor-like protein A
- Guanine nucleotide-binding protein subunit beta
Sequence:
MDFNPVPPPRETLRAYLSKKGHVVKNWKLRLFVLKPGSSYMEYFVDETKEQQHLPQGRVPLYGTRVMEYVYNSNNNPREFCLSVETENKNWIISTGSKAQQLEWIEAIKHAIESAVETDEIKLQKHKSIEKQLQLDGKNKNKIPVLKLLLLGTGESGKSTVVKQMKILHHKGFSKEEEEFYRNLIYINLLDGMALLIHVIKENNIEIPQETLSAIKNYSSWYRVYIEKRNKNGIRNNPIGSMIPISILNNNKDNNNSNSSSLKNNSGGSSSSELDKKMTHLSLDGSTCINSNSASPNGPSSSTTTSTINTHNRSNSDGSSNNIFNVQDFGIPPIITNYISTIWSDPVVQSEVMLQAQKYHINESTQYYLNEIKRIGKPTYQPVNLDILKSRATTNGVVETDFNVNGEVIFRIVDVAGQRGERKKWINFFDDVTAIVFVAAINEYDQKLVEDNCTNRLHESLNLFDSICNDSTFPKTSIILFLNKIDLFREKLKRTSINICFPDYNGDQSYEKSSNYIKNNFLSKKKGGNGINSQNFIYFHFTCATDTKSFETVFNSVRDIIISKTLEFYC
Protein: Tripeptidyl-peptidase 2 (TPP-2) (EC 3.4.14.10) (Tripeptidyl aminopeptidase) (Tripeptidyl-peptidase II) (TPP-II) (P29144)
Organism: Homo sapiens (Human)
Function: Cytosolic tripeptidyl-peptidase that releases N-terminal tripeptides from polypeptides and is a component of the proteolytic cascade acting downstream of the 26S proteasome in the ubiquitin-proteasome pathway. It plays an important role in intracellular amino acid homeostasis. Stimulates adipogenesis (By similarity).
Subcellular location: Cytoplasm {ECO:0000269|PubMed:19747897}. Nucleus {ECO:0000269|PubMed:19747897}. Note=Translocates to the nucleus in response to gamma-irradiation.
Interaction partners:
- Endoplasmic reticulum aminopeptidase 2
- Endoplasmic reticulum aminopeptidase 1
- DNA polymerase beta
Sequence:
MATAATEEPFPFHGLLPKKETGAASFLCRYPEYDGRGVLIAVLDTGVDPGAPGMQVTTDGKPKIVDIIDTTGSGDVNTATEVEPKDGEIVGLSGRVLKIPASWTNPSGKYHIGIKNGYDFYPKALKERIQKERKEKIWDPVHRVALAEACRKQEEFDVANNGSSQANKLIKEELQSQVELLNSFEKKYSDPGPVYDCLVWHDGEVWRACIDSNEDGDLSKSTVLRNYKEAQEYGSFGTAEMLNYSVNIYDDGNLLSIVTSGGAHGTHVASIAAGHFPEEPERNGVAPGAQILSIKIGDTRLSTMETGTGLIRAMIEVINHKCDLVNYSYGEATHWPNSGRICEVINEAVWKHNIIYVSSAGNNGPCLSTVGCPGGTTSSVIGVGAYVSPDMMVAEYSLREKLPANQYTWSSRGPSADGALGVSISAPGGAIASVPNWTLRGTQLMNGTSMSSPNACGGIALILSGLKANNIDYTVHSVRRALENTAVKADNIEVFAQGHGIIQVDKAYDYLVQNTSFANKLGFTVTVGNNRGIYLRDPVQVAAPSDHGVGIEPVFPENTENSEKISLQLHLALTSNSSWVQCPSHLELMNQCRHINIRVDPRGLREGLHYTEVCGYDIASPNAGPLFRVPITAVIAAKVNESSHYDLAFTDVHFKPGQIRRHFIEVPEGATWAEVTVCSCSSEVSAKFVLHAVQLVKQRAYRSHEFYKFCSLPEKGTLTEAFPVLGGKAIEFCIARWWASLSDVNIDYTISFHGIVCTAPQLNIHASEGINRFDVQSSLKYEDLAPCITLKNWVQTLRPVSAKTKPLGSRDVLPNNRQLYEMVLTYNFHQPKSGEVTPSCPLLCELLYESEFDSQLWIIFDQNKRQMGSGDAYPHQYSLKLEKGDYTIRLQIRHEQISDLERLKDLPFIVSHRLSNTLSLDIHENHSFALLGKKKSSNLTLPPKYNQPFFVTSLPDDKIPKGAGPGCYLAGSLTLSKTELGKKADVIPVHYYLIPPPTKTKNGSKDKEKDSEKEKDLKEEFTEALRDLKIQWMTKLDSSDIYNELKETYPNYLPLYVARLHQLDAEKERMKRLNEIVDAANAVISHIDQTALAVYIAMKTDPRPDAATIKNDMDKQKSTLVDALCRKGCALADHLLHTQAQDGAISTDAEGKEEEGESPLDSLAETFWETTKWTDLFDNKVLTFAYKHALVNKMYGRGLKFATKLVEEKPTKENWKNCIQLMKLLGWTHCASFTENWLPIMYPPDYCVF
Protein: Cysteine-rich secretory protein 4 (G5E862)
Organism: Mus musculus (Mouse)
Interaction partners:
Sequence:
MDVGMAVKFILLLFVAAFVPVVTIRPLKLDRALYNKLITESQTEPQEEIVNTHNAFRRKVSPPARNMLKVSWSSAAAENARILARYCDKSDSDSLERRLPNTFCGENMLMEHYPSSWSKVIEIWFNESKYFKYGEWPSTDDDIETDHYTQMVWASTYLVGCDVAACRRQKAATYLYVCHYCHEGNHQDTLNMPYKEGSPCDDCPNNCEDGLCTNPCIYYDEYNNCDTQVKLYGCSHPAVQPFCKASCLCTTEIK
Protein: ToMV susceptible protein tm-1(GCR26) (Disease susceptible protein tm-1) (Protein p80(GCR26)) (A7M6E8)
Organism: Solanum lycopersicum (Tomato) (Lycopersicon esculentum)
Function: Inhibitor of viral RNA replication which confers resistance to some tobamoviruses including tobacco mild green mosaic virus (TMGMV) and pepper mild mottle virus (PMMoV), but not to tomato mosaic virus (ToMV strains L, ToMV0 and ToMV1-2) and tobacco mosaic virus (TMV). Prevents tobamoviruses RNA replication by affecting the association of tobamoviruses replication proteins (large and small subunits) with host membrane-associated proteins (e.g. TOM1, TOM2A and ARL8), thus inhibiting the replication complex formation on the membranes and avoiding viral negative-strand RNA synthesis.
Interaction partners:
- ToMV susceptible protein tm-2
- ToMV resistance protein Tm-2
- Agamous-like MADS-box protein AGL9 homolog
- ToMV resistance protein Tm-2
- X intrinsic protein
Sequence:
MATAQSNSPRVFCIGTADTKFDELRFLSEHVRSSLNSFSNKSSFKVGVTVVDVSTSRKETNSCADFDFVPSKDVLSCYARGEGTVGRFPDIRGQAIAIMNKALETFLSKANGEQNLAGVIGLGGSGGTSLLSSAFRSLPIGIPKVIISTVASGQTESYIGTSDLVLFPSVVDICGINNVSKVVLSNAGAAFAGMVIGRLESSKEHSITNGKFTVGVTMFGVTTPCVNAVKERLVKEGYETLVFHATGVGGRAMEDLVRGGFIQGVLDITTTEVADYVVGGVMACDSSRFDAILEKKIPLVLSVGALDMVNFGPKTTIPPEFQQRKIHQHNEQVSLMHTTVGENKKFAAFIAEKLNKASSSVCVCLPEKGVSALDAPGKDFYDPEATSCLTHELQMLLENNERCQVKVYPYHINDVEFANALVDSFLEMSPKSGHVECQTAESKSIQGIQNVNAVLEKYPSCNGKNFSRLNDFPNAKPETLQKRIVILQKLKDQISKGKPIIGAGAGTGISAKFEEAGGVDLIVLYNSGRFRMAGRGSLAGLLPFADANAIVLEMANEVLPVVKEVAVLAGVCATDPFRRMDNFLKQLESVGFCGVQNFPTVGLFDGNFRQNLEETGMGYGLEVEMIATAHRMGLLTTPYAFCPDEAVAMAEAGADIIVAHMGLTTSGSIGAKTAVSLEESVTCVQAIADATHRINPDAIVLCHGGPISSPEEAAYVLKRTTGVHGFYGASSMERLPVEQAITATVQQYKSISME
Protein: 40S ribosomal protein S6 (F2Z5Q6)
Organism: Sus scrofa (Pig)
Interaction partners:
- Ubiquitin-like protein FUBI
- 40S ribosomal protein S30
- Ubiquitin-like protein FUBI
- Ribosomal protein S6 kinase
- Ribosomal protein S6 kinase beta-2
- Small ribosomal subunit protein uS7
- 40S ribosomal protein S4
- Large ribosomal subunit protein uL18
- 40S ribosomal protein S8
- Small ribosomal subunit protein uS9
Sequence:
MKLNISFPATGCQKLIEVDDERKLRTFYEKRMATEVAADALGEEWKGYVVRISGGNDKQGFPMKQGVLTHGRVRLLLSKGHSCYRPRRTGERKRKSVRGCIVDANLSVLNLVIVKKGEKDIPGLTDTTVPRRLGPKRASRIRKLFNLSKEDDVRQYVVRKPLNKEGKKPRTKAPKIQRLVTPRVLQHKRRRIALKKQRTKKNKEEAAEYAKLLAKRMKEAKEKRQEQIAKRRRLSSLRASTSKSESSQK
Protein: Protein Tex24 (Testis-expressed protein 24) (Testis-specific factor 1) (Q5DP50)
Organism: Mus musculus (Mouse)
Function: Nuclear factor which might have a role in spermatogenesis.
Subcellular location: Nucleus {ECO:0000269|PubMed:16343427}.
Interaction partners:
- Predicted gene 4884
- Uncharacterized protein C2orf78 homolog
- Predicted gene 8020.
- Olfactory receptor
- MAS-related GPR, member A9
- Olfactory receptor
- Late cornified envelope 1C
- Zfp617 protein
- GSARP1
Sequence:
MGSQSLNSTFLKVRRLSLISSNERLLGQTSGLATGSRLVTQEVDDLRVIPGSRPDLDDHQPQCSLAELPSTAHGKRKPGHLPRLRSSAVKGHAPDPNPSLSIVSKRIFKGESVIKGPEDRQTFVGPSGLPKISPKATAGEAQGKKRTMELLNKARKQEEKVSNLLDIRQLPKQEVFINNTHPCKKHLKQQPMSLEEWRRGHLGGDNTGLISQEPFRCCKRLGKKAQCQLLEVTSLEAEASLEVLKRRRRMQAMEMSKKPQDRGLGQEKAVFLSREKVKPSSHDMHLSTAERSFKPKSMPKAEDWDLSVQGTPVVLTVRDHSNVSQAQKHLGCAEIFHSRDGRCTLLKRGGA
Protein: Serine acetyltransferase 4 (AtSAT-4) (AtSERAT3;2) (EC 2.3.1.30) (Q8W2B8)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Cytoplasm {ECO:0000269|PubMed:15579666}.
Interaction partners:
- S-sulfo-L-cysteine synthase
- Phosphoserine phosphatase, chloroplastic
- Bifunctional aspartokinase/homoserine dehydrogenase 2, chloroplastic
- Bifunctional aspartokinase/homoserine dehydrogenase 1, chloroplastic
- Serine racemase
- Cysteine synthase 1
- Homoserine kinase
- Threonine dehydratase biosynthetic, chloroplastic
- Serine--glyoxylate aminotransferase
- Putative inactive cysteine synthase 2
Sequence:
MACINGENRDFSSSSSLSSLPMIVSRNFSARDDGETGDEFPFERIFPVYARGTLNPVADPVLLDFTNSSYDPIWDSIREEAKLEAEEEPVLSSFLYASILSHDCLEQALSFVLANRLQNPTLLATQLMDIFCNVMVHDRGIQSSIRLDVQAFKDRDPACLSYSSAILHLKGYLALQAYRVAHKLWKQGRKLLALALQSRVSEVFGIDIHPAARIGKGILLDHGTGVVIGETAVIGDRVSILHGVTLGGTGKETGDRHPNIGDGALLGACVTILGNIKIGAGAMVAAGSLVLKDVPSHSMVAGNPAKLIGFVDEQDPSMTMEHDATREFFQNVAVAYRETIPNGSSVSGSCRERRH
Protein: Inner membrane protein YnbA (P76090)
Organism: Escherichia coli (strain K12)
Subcellular location: Cell inner membrane; Multi-pass membrane protein.
Interaction partners:
- Uncharacterized protein YnbC
- Uncharacterized protein YnbB
- Uncharacterized protein YnbD
- Inner membrane protein YnjF
- Inner membrane protein YnjI
- Inner membrane protein YidH
- Inner membrane protein YgiZ
- Uncharacterized protein YecT
Sequence:
MTLYQIKPLFQSLLRPTMFWLYKHHVTANHITLAALALSLLTGLLLMLAAQPILFLLLPIVLFIRMALNALDGMLARECNQQTRLGAILNETGDVISDIALYLPFLFLPESNASLVILMLFCTILTEFCGLLAQTINGVRSYAGPFGKSDRALIFGLWGLAVAIYPQWMQWNNLLWSIASILLLWTAINRCRSVLLMSAEI
Protein: Alpha-taxilin (P40222)
Organism: Homo sapiens (Human)
Function: May be involved in intracellular vesicle traffic and potentially in calcium-dependent exocytosis in neuroendocrine cells.
Interaction partners:
- Syntaxin-3
- Syntaxin-4
- Syntaxin-1A
- Gamma-taxilin
- Tumor susceptibility gene 101 protein
- Beta-taxilin
- Serine/threonine-protein kinase TBK1
Sequence:
MKNQDKKNGAAKQSNPKSSPGQPEAGPEGAQERPSQAAPAVEAEGPGSSQAPRKPEGAQARTAQSGALRDVSEELSRQLEDILSTYCVDNNQGGPGEDGAQGEPAEPEDAEKSRTYVARNGEPEPTPVVNGEKEPSKGDPNTEEIRQSDEVGDRDHRRPQEKKKAKGLGKEITLLMQTLNTLSTPEEKLAALCKKYAELLEEHRNSQKQMKLLQKKQSQLVQEKDHLRGEHSKAVLARSKLESLCRELQRHNRSLKEEGVQRAREEEEKRKEVTSHFQVTLNDIQLQMEQHNERNSKLRQENMELAERLKKLIEQYELREEHIDKVFKHKDLQQQLVDAKLQQAQEMLKEAEERHQREKDFLLKEAVESQRMCELMKQQETHLKQQLALYTEKFEEFQNTLSKSSEVFTTFKQEMEKMTKKIKKLEKETTMYRSRWESSNKALLEMAEEKTVRDKELEGLQVKIQRLEKLCRALQTERNDLNKRVQDLSAGGQGSLTDSGPERRPEGPGAQAPSSPRVTEAPCYPGAPSTEASGQTGPQEPTSARA
Protein: Lectin-like protein At3g16530 (Q9LK72)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Secreted, extracellular space, apoplast {ECO:0000269|PubMed:18324730}.
Interaction partners:
- PLC-like phosphodiesterases superfamily protein
- RING-type E3 ubiquitin transferase
- Endochitinase At2g43580
- Endochitinase At2g43590
- AR781
Sequence:
MQIHKLCFLVLFLANAAFAVKFNFDSFDGSNLLFLGDAELGPSSDGVSRSGALSMTRDENPFSHGQGLYINQIPFKPSNTSSPFSFETSFTFSITPRTKPNSGQGFAFIITPEADNSGASDGGYLGILNKTNDGKPENHILAIEFDTFQNKEFLDISGNHVGVNINSMTSLVAEKAGYWVQTRVGKRKVWSFKDVNLSSGERFKAWVEFRNKDSTITVTLAPENVKKPKRALIEAPRVLNEVLLQNMYAGFAGSMGRAVERHDIWSWSFENAAKNN
Protein: DNA polymerase alpha-associated DNA helicase A (EC 3.6.4.12) (O94247)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: DNA polymerase alpha-associated DNA helicase which may be involved in DNA replication.
Subcellular location: Cytoplasm. Nucleus.
Interaction partners:
- F-box DNA helicase protein 1
- Endonuclease III homolog lyase)
- Suppressor of kinetochore protein 1
Sequence:
MSSSNEQICLDEDWIQKFGDREIEFVDEAQKSEVDETEKSIKRFPLSVLQRKGLALINLRIGVVKTGFGGKTIIDFEKDPAFSNGEELPANSFSPGDVVSIRQDFQSSKKKRPNETDISVEGVVTRVHERHISVALKSEEDIPSSVTRLSVVKLVNRVTYERMRHTMLEFKRSIPEYRNSLFYTLIGRKKADVSIDQKLIGDIKYFNKELNASQKKAVKFSIAVKELSLIHGPPGTGKTHTLVEIIQQLVLRNKRILVCGASNLAVDNIVDRLSSSGIPMVRLGHPARLLPSILDHSLDVLSRTGDNGDVIRGISEDIDVCLSKITKTKNGRERREIYKNIRELRKDYRKYEAKTVANIVSASKVVFCTLHGAGSRQLKGQRFDAVIIDEASQALEPQCWIPLLGMNKVILAGDHMQLSPNVQSKRPYISMFERLVKSQGDLVKCFLNIQYRMHELISKFPSDTFYDSKLVPAEEVKKRLLMDLENVEETELTDSPIYFYDTLGNYQEDDRSEDMQNFYQDSKSNHWEAQIVSYHISGLLEAGLEAKDIAVVTPYNAQVALIRQLLKEKGIEVEMGSVDKVQGREKEAIIFSLVRSNDVREVGFLAEKRRLNVAITRPKRHLCVIGDSNTVKWASEFFHQWVDFLEENAIVMDIDATMFE
Protein: Nematode resistance protein-like HSPRO1 (AKINbetagamma-interacting protein 1) (Ortholog of sugar beet HS1 PRO-1 protein 1) (Protein Hs1pro-1) (Q9LY61)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Positive regulator of basal resistance.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:17028154}.
Interaction partners:
- Non-canonical heme oxygenase HOZ, chloroplastic
- Protein transport protein SEC24 A
- Serine/threonine-protein kinase Nek5
- Profilin-1
- Profilin-3
- Serine/threonine-protein kinase Nek6
- Protein NSP-INTERACTING KINASE 3
Sequence:
MADLDLQRKMVSPKLHVTIPEPCKLSSVSSPISSSSSAACSAYELYLRLPELRNLWSSLYFPHWISEPVLKPALQALEITFRLILTVASDTRPYINRREWIRRLDSLTTSQIKIVAAICGDEDNYEENVSAAPVSNGWSSLSLLSEIATCRTSESVGQKILSTIENEMRWCKYTLGLGEPNLAGKPYLQYDAVCLPEELHSLKNNPYADHIENQENQMLYTSHQILESWIYVSVNLLYRIESRIEEGKFEKASSDVYLLERIWKLLSEIEDLHILMDPEDFLKVKKQLQIKSTFPNDAFCFRSKGLVEMAKMSKELRQKVPAVLEVEVDPTGGPRLQEAAMKLYSRKTEYEKIHLLQGMQAVESAAKRFFFGYQKLVAAMIGNAEANANRTVANHESYDSLTQVFMEPPYYPSLDAAKTFLGEFWSQL
Protein: V-type proton ATPase subunit a (Q8IML3)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
Sequence:
MGSLFRSEEMALCQLFLQSEAAYACVSELGELGLVQFRDLNPDVNAFQRKFVNEVRRCDEMERKLRYLEKEIKKDGIPMLDTGESPEAPQPREMIDLEATFEKLENELREVNQNAEALKRNFLELTELKHILRKTQVFFDEQEGGVNQTTESMTRALITDEARTAGASMGPVQLGFVAGVILRERLPAFERMLWRACRGNVFLRQAMIETPLEDPTNGDQVHKSVFIIFFQGDQLKTRVKKICEGFRATLYPCPEAPADRREMAMGVMTRIEDLNTVLGQTQDHRHRVLVAAAKNLKNWFVKVRKIKAIYHTLNLFNLDVTQKCLIAECWVPLLDIETIQLALRRGTERSGSSVPPILNRMQTFENPPTYNRTNKFTKAFQALIDAYGVASYREMNPAPYTIITFPFLFAVMFGDLGHGAIMALFGLWMIRKEKGLAAQKTDNEIWNIFFGGRYIIFLMGVFSMYTGLIYNDIFSKSLNIFGSHWHLSYNKSTVMENKFLQLSPKGDYEGAPYPFGMDPIWQVAGANKIIFHNAYKMKISIIFGVIHMIFGVVMSWHNHTYFRNRISLLYEFIPQLVFLLLLFFYMVLLMFIKWIKFAATNDKPYSEACAPSILITFIDMVLFNTPKPPPENCETYMFMGQHFIQVLFVLVAVGCIPVMLLAKPLLIMQARKQANVQPIAGATSDAEAGGVSNSGSHGGGGGHEEEEELSEIFIHQSIHTIEYVLGSVSHTASYLRLWALSLAHAQLAEVLWTMVLSIGLKQEGPVGGIVLTCVFAFWAILTVGILVLMEGLSAFLHTLRLHWVEFQSKFYKGQGYAFQPFSFDAIIENGAAAAEE
Protein: Acetylcholine receptor subunit epsilon (P09660)
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 delta
- Neuronal acetylcholine receptor subunit beta-3
- Acetylcholine receptor subunit beta
- Neuronal acetylcholine receptor subunit alpha-9
- Neuronal acetylcholine receptor subunit alpha-4
- 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:
MTMALLGTLLLLALFGRSQGKNEELSLYHHLFDNYDPECRPVRRPEDTVTITLKVTLTNLISLNEKEETLTTSVWIGIEWQDYRLNFSKDDFAGVEILRVPSEHVWLPEIVLENNIDGQFGVAYDCNVLVYEGGSVSWLPPAIYRSTCAVEVTYFPFDWQNCSLIFRSQTYNAEEVELIFAVDDDGNAINKIDIDTAAFTENGEWAIDYCPGMIRHYEGGSTEDPGETDVIYTLIIRRKPLFYVINIIVPCVLISGLVLLAYFLPAQAGGQKCTVSINVLLAQTVFLFLIAQKIPETSLSVPLLGRYLIFVMVVATLIVMNCVIVLNVSLRTPTTHATSPRLRQILLELLPRLLGLSPPPEDPGAASPARRASSVGILLRAEELILKKPRSELVFEGQRHRHGTWTAAALCQNLGAAAPEVRCCVDAVNFVAESTRDQEATGEELSDWVRMGKALDNVCFWAALVLFSVGSTLIFLGGYFNQVPDLPYPPCIQP
Protein: Cytosolic acyl coenzyme A thioester hydrolase (EC 3.1.2.2) (Acyl-CoA thioesterase 7) (Brain acyl-CoA hydrolase) (BACH) (CTE-IIa) (CTE-II) (Long chain acyl-CoA thioester hydrolase) (Q91V12)
Organism: Mus musculus (Mouse)
Function: Catalyzes the hydrolysis of acyl-CoAs into free fatty acids and coenzyme A (CoASH), regulating their respective intracellular levels (Probable). Preferentially hydrolyzes palmitoyl-CoA, but has a broad specificity acting on other fatty acyl-CoAs with chain-lengths of C8-C18 (Probable). May play an important physiological function in brain (Probable).
Subcellular location: [Isoform A]: Cytoplasm, cytosol {ECO:0000305|PubMed:15288813}.; SUBCELLULAR LOCATION: [Isoform D]: Cytoplasm, cytosol {ECO:0000305|PubMed:15288813}.
Interaction partners:
- Acyl-coenzyme A thioesterase 1
- Peroxisomal succinyl-coenzyme A thioesterase
- Acyl-coenzyme A thioesterase 2, mitochondrial
- Acyl-coenzyme A thioesterase 5
- Acyl-coenzyme A thioesterase 3
- Acyl-coenzyme A thioesterase THEM5
- Acyl-coenzyme A thioesterase THEM4
- Very-long-chain enoyl-CoA reductase
- Acyl-coenzyme A thioesterase 13
Sequence:
MKLLVGTLRLWEVGRQVAFSSLTPGQECSGLRKTFWAAMRAVRTRADHQKLGHCVTMGRIMRPDDANVAGNVHGGTILKMIEEAGAIISTRHCNSQNGERCVAALARVERTDFLSPMCIGEVAHVSAEITYTSKHSVEVQVHVMSENILTGTKKLTNKATLWYVPLSLKNVDKVLEVPPIVYLRQEQEEEGRKRYEAQKLERMETKWRNGDIVQPVLNPEPNTVSYSQSSLIHLVGPSDCTLHGFVHGGVTMKLMDEVAGIVAARHCKTNIVTASVDAINFHDKIRKGCVITISGRMTFTSNKSMEIEVLVDADPVVDNSQKRYRAASAFFTYVSLNQEGKPMPVPQLVPETEDEKKRFEEGKGRYLQMKAKRQGHTEPQP
Protein: Flavoprotein-like protein YCP4 (P25349)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Subcellular location: Cytoplasm {ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:19064668}. Membrane raft {ECO:0000269|PubMed:19064668}. Mitochondrion {ECO:0000269|PubMed:14576278}.
Interaction partners:
- Protoplast secreted protein 2
- Protein RFS1
Sequence:
MVKIAIITYSTYGHIDVLAQAVKKGVEAAGGKADIYRVEETLPDEVLTKMNAPQKPEDIPVATEKTLLEYDAFLFGVPTRFGNLPAQWSAFWDKTGGLWAKGSLNGKAAGIFVSTSSYGGGQESTVKACLSYLAHHGIIFLPLGYKNSFAELASIEEVHGGSPWGAGTLAGPDGSRTASPLELRIAEIQGKTFYETAKKLFPAKEAKPSTEKKTTTSDAAKRQTKPAAATTAEKKEDKGLLSCCTVM
Protein: Coiled-coil domain-containing protein 141 (Coiled-coil protein associated with myosin II and DISC1) (Q6ZP82)
Organism: Homo sapiens (Human)
Function: Plays a critical role in radial migration and centrosomal function.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:E9Q8Q6}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250|UniProtKB:E9Q8Q6}. Note=Co-localized with DISC1 at/around the centrosome. Localizes to the centrosome, at least in part, in a DISC1-dependent manner. Accumulates and oscillates at the dilation in cortical neurons during migration. CAMDI protein level is stabilized at the G1 phase and destabilized at the G2 /M phase. {ECO:0000250|UniProtKB:E9Q8Q6}.
Interaction partners:
- Disrupted in schizophrenia 1 protein
- Titin
Sequence:
MSSQGSPSVALSTTTVSSVAVQAGDSKIVIAVIKCGKWVQLQLAESQPNLLEIGSSQDETKKLLHDHELLLAKLKALEDRVWELLQEADKTAEENKDQSQVYDAMAETLGEAWAALVSMLERRTELLRLTSEFFENALEFAIKIDQAEDFLQNTHEFESAESLKSLLQLHEHHTKELLERSLALLNKSQQLTDFIEKFKCEGPNVNPELTQGAHSSCLKVDRLLELLQDRRRQLDKYLKQQWQELSQVLQICQWDQQENQVTCWFQKTIRNLQEQSLGSSLSDNEDRIHKQEELIIKAKEWNSAVEKLKSEALRILLSKDYVEKEHLQLSHQKLSQLQEEFGQLMVERNTWLKKANEFFNSANKAFDVLGRVEAYLKLLKSEGLSLAVLAVRHEELHRKIKDCTTDALQKGQTLISQVDSCSSQVSGIHEMMGCIKRRVDHLTEQCSAHKEYALKKQQLTASVEGYLRKVEMSIQKISPVLSNAMDVGSTRSESEKILNKYLELDIQAKETSHELEAAAKTMMEKNEFVSDEMVSLSSKARWLAEELNLFGQSIDYRSQVLQTYVAFLKSSEEVEMQFQSLKEFYETEIPQKEQDDAKAKHCSDSAEKQWQLFLKKSFITQDLGLEFLNLINMAKENEILDVKNEVYLMKNTMENQKAEREELSLLRLAWQLKATESKPGKQQWAAFKEQLKKTSHNLKLLQEALMPVSALDLGGSLQFILDLRQKWNDMKPQFQQLNDEVQYIMKESEELTGRGAPVKEKSQQLKDLIHFHQKQKERIQDYEDILYKVVQFHQVKEELGRLIKSRELEFVEQPKELGDAHDVQIHLRCSQEKQARVDHLHRLALSLGVDIISSVQRPHCSNVSAKNLQQQLELLEEDSMKWRAKAEEYGRTLSRSVEYCAMRDEINELKDSFKDIKKKFNNLKFNYTKKNEKSRNLKALKYQIQQVDMYAEKMQALKRKMEKVSNKTSDSFLNYPSDKVNVLLEVMKDLQKHVDDFDKVVTDYKKNLDLTEHFQEVIEECHFWYEDASATVVRVGKYSTECKTKEAVKILHQQFNKFIAPSVPQQEERIQEATDLAQHLYGLEEGQKYIEKIVTKHKEVLESVTELCESLTELEEKLKQGDVLKMNPNLEDFHYDYIDLLKEPAKNKQTIFNEERNKGQVQVADLLGINGTGEERLPQDLKVSTDKEGGVQDLLLPEDMLSGEEYECVSPDDISLPPLPGSPESPLAPSDMEVEEPVSSSLSLHISSYGVQAGTSSPGDAQESVLPPPVAFADACNDKRETFSSHFERPYLQFKAEPPLTSRGFVEKSTALHRISAEHPESMMSEVHERALQQHPQAQGGLLETREKMHADNNFTKTQDRLHASSDAFSGLRFQSGTSRGYQRQMVPREEIKSTSAKSSVVSLADQAPNFSRLLSNVTVMEGSPVTLEVEVTGFPEPTLTWYKKGQKLSADGHLQVLHKETRHSVFIPKVCKADAGLYVARAQNSSGALSSNVILHVTGNCRLPITRVNWITLCVVYVSVSLMYWLLTQ
Protein: Pyruvate dehydrogenase E1 component subunit beta-1, mitochondrial (PDHE1-B) (EC 1.2.4.1) (Protein MACCI-BOU) (Q38799)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: The pyruvate dehydrogenase complex catalyzes the overall conversion of pyruvate to acetyl-CoA and CO(2). It contains multiple copies of three enzymatic components: pyruvate dehydrogenase (E1), dihydrolipoamide acetyltransferase (E2) and lipoamide dehydrogenase (E3).
Subcellular location: Mitochondrion matrix {ECO:0000269|PubMed:14671022, ECO:0000305|PubMed:25732537}.
Interaction partners:
- Pyruvate dehydrogenase E1 component subunit alpha-3, chloroplastic
- Pyruvate dehydrogenase E1 component subunit alpha-1, mitochondrial
- Pyruvate dehydrogenase E1 component subunit alpha-2, mitochondrial
- Dihydrolipoyllysine-residue acetyltransferase component 1 of pyruvate dehydrogenase complex, mitochondrial
- 2-oxoisovalerate dehydrogenase subunit alpha 1, mitochondrial
- 2-oxoisovalerate dehydrogenase subunit alpha 2, mitochondrial
- Dihydrolipoyllysine-residue acetyltransferase component 3 of pyruvate dehydrogenase complex, mitochondrial
- Dihydrolipoyllysine-residue acetyltransferase component 2 of pyruvate dehydrogenase complex, mitochondrial
- Dihydrolipoyl dehydrogenase 1, mitochondrial
- Dihydrolipoyllysine-residue acetyltransferase component 5 of pyruvate dehydrogenase complex, chloroplastic
Sequence:
MLGILRQRAIDGASTLRRTRFALVSARSYAAGAKEMTVRDALNSAIDEEMSADPKVFVMGEEVGQYQGAYKITKGLLEKYGPERVYDTPITEAGFTGIGVGAAYAGLKPVVEFMTFNFSMQAIDHIINSAAKSNYMSAGQINVPIVFRGPNGAAAGVGAQHSQCYAAWYASVPGLKVLAPYSAEDARGLLKAAIRDPDPVVFLENELLYGESFPISEEALDSSFCLPIGKAKIEREGKDVTIVTFSKMVGFALKAAEKLAEEGISAEVINLRSIRPLDRATINASVRKTSRLVTVEEGFPQHGVCAEICASVVEESFSYLDAPVERIAGADVPMPYAANLERLALPQIEDIVRASKRACYRSK