wanglab/gogpt-training-data huggingface dataset:
Protein: Lupeol synthase (EC 5.4.99.41) (Q2XPU7)
Organism: Ricinus communis (Castor bean)
Function: Oxidosqualene cyclase involved in the biosynthesis of the cuticular lupeol of glaucous individuals, but not of the glossy phenotype.
Interaction partners:
Sequence:
MWRIKIAEGGNNPYIYSTNNFQGRQIWVFDPNAGTPEEQAEVEEARQNFWKNRFQVKPNSDLLWQLQFLREKNFKQKIPKVKVEDGEEITSEIAAAALRRSVHLFSALQASDGHWCAENGGLLFFLPPLVFAVYITGHLNTVFSPEHRKEILRYIYCHQNEDGGWGIHIEGHSTMFCTVLNYICMRILGEARDGGIENACERGRKWILDHGGATGISSWGKTWLSILGVYEWDGTNPMPPEFWAFPSSFPLHPAKMFCYCRITYMPMSYLYGKRFVGPITPLILQIREEIYNEPYNKIKWNSVRHLCAKEDNYFPHPTIQKLLWDALYTFSEPLFSRWPFNKLREKALKITMDHIHYEDHNSRYITIGCVEKPLCMLACWIEDPHGEAFKKHLARIADYIWVGEDGIKMQSFGSQTWDTSLALQALIASDLSHEIGPTLKQGHVFTKNSQATENPSGDFRKMFRHISKGAWTFSDKDQGWQVSDCTAESLKCCLLFSMMPPEIVGEKMEPEKVYDSVNVILSLQSQNGGFTAWEPARAGSWMEWLNPVEFMEDLVVEHEYVECTSSAIQALVLFKKLYPRHRNKEIENCIINAAQFIENIQEPDGSWYGNWGICFSYGTWFALKGLAAAGRTYENCSAIRKGVDFLLKSQRDDGGWAESYLSCPKKVYVPFEGNRSNLVQTAWAMMGLIYGGQAKRDPMPLHRAAKLLINSQTDLGDFPQQELTGAFMRNCMLHYALFRNTFPIWALAEYRRHVLFPSAGFGFGFTNNL
Protein: Alcohol dehydrogenase class-3 (EC 1.1.1.1) (Alcohol dehydrogenase class-III) (Glutathione-dependent formaldehyde dehydrogenase) (FALDH) (FDH) (GSH-FDH) (EC 1.1.1.-) (Octanol dehydrogenase) (EC 1.1.1.73) (S-(hydroxymethyl)glutathione dehydrogenase) (EC 1.1.1.284) (P46415)
Organism: Drosophila melanogaster (Fruit fly)
Function: Class-III ADH is remarkably ineffective in oxidizing ethanol, but it readily catalyzes the oxidation of long-chain primary alcohols and the oxidation of S-(hydroxymethyl) glutathione.
Interaction partners:
- S-formylglutathione hydrolase
- Probable hydroxyacid-oxoacid transhydrogenase, mitochondrial
- Alcohol dehydrogenase
- Aldehyde dehydrogenase type III, isoform Q
- aldehyde dehydrogenase
- aldehyde dehydrogenase
- Uncharacterized protein, isoform B
- Dehydrogenase/reductase 4
- LD24679p
- monoamine oxidase
Sequence:
MSATEGKVITCKAAVAWEAKKPLVIEDIEVAPPKAHEVRIKITATGVCHTDAFTLSGADPEGLFPVVLGHEGAGIVESVGEGVTNFKAGDHVIALYIPQCNECKFCKSGKTNLCQKIRLTQGAGVMPEGTSRLSCKGQQLFHFMGTSTFAEYTVVADISLTKINEKAPLEKVCLLGCGISTGYGAALNTAKVEAGSTCAVWGLGAVGLAVGLGCKKAGAGKIYGIDINPDKFELAKKFGFTDFVNPKDVADKGSIQNYLIDLTDGGFDYTFECIGNVNTMRSALEATHKGWGTSVVIGVAGAGQEISTRPFQLVVGRVWKGSAFGGWRSVSDVPKLVEDYLKKDLLVDEFITHELPLSQINEAFDLMHKGESIRSIIKY
Protein: Spermatogenesis- and oogenesis-specific basic helix-loop-helix-containing protein 1 (Q6IUP1)
Organism: Mus musculus (Mouse)
Function: Transcription regulator of both male and female germline differentiation. Suppresses genes involved in spermatogonial stem cells maintenance, and induces genes important for spermatogonial differentiation. Coordinates oocyte differentiation without affecting meiosis I.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16690745, ECO:0000269|PubMed:28504655}. Nucleus {ECO:0000255|PROSITE-ProRule:PRU00981, ECO:0000269|PubMed:16690745, ECO:0000269|PubMed:28504655}.
Interaction partners:
- Stimulated by retinoic acid gene 8 protein
- Homeobox protein NOBOX
- Factor in the germline alpha
- Spermatogenesis- and oogenesis-specific basic helix-loop-helix-containing protein 2
- LIM/homeobox protein Lhx8
- Zinc finger and BTB domain containing 16
- Nanos homolog 2
- GDNF family receptor alpha-1
Sequence:
MASGGHERANEDYRVSGITGCSKTPQPETQDSLQTSSQSSALCTAPVAAANLGPSLRRNVVSERERRRRISLSCEHLRALLPQFDGRREDMASVLEMSVYFLQLAHSMDPSWEQLSVPQPPQEMWHMWQGDVLQVTLANQIADSKPDSGIAKPSAVSRVQDPPCFGMLDTDQSQATERESELLERPSSCPGHRQSALSFSEPESSSLGPGLPPWIPHSWQPATPEASDIVPGGSHQVASLAGDPESSGMLAEEANLVLASVPDARYTTGAGSDVVDGAPFLMTTNPDWWLGSVEGRGGPALARSSPVDGAEPSFIGDPELCSQELQAGPGELWGLDFGSPGLALKDEADSIFPDFFP
Protein: Mitochondrial inner membrane m-AAA protease component AFG3L2 (EC 3.4.24.-) (EC 3.6.-.-) (AFG3-like protein 2) (Q8JZQ2)
Organism: Mus musculus (Mouse)
Function: ATP-dependent protease which is essential for axonal and neuron development. In neurons, mediates degradation of SMDT1/EMRE before its assembly with the uniporter complex, limiting the availability of SMDT1/EMRE for MCU assembly and promoting efficient assembly of gatekeeper subunits with MCU (By similarity). Required for the maturation of paraplegin (SPG7) after its cleavage by mitochondrial-processing peptidase (MPP), converting it into a proteolytically active mature form. Required for the maturation of PINK1 into its 52kDa mature form after its cleavage by mitochondrial-processing peptidase (MPP) (By similarity). Involved in the regulation of OMA1-dependent processing of OPA1 (By similarity).
Subcellular location: Mitochondrion inner membrane {ECO:0000269|PubMed:19656850, ECO:0000269|PubMed:24856930}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Mitochondrial inner membrane m-AAA protease component paraplegin
- Mitochondrial inner membrane m-AAA protease component AFG3L1
- ATP-dependent clpX-like chaperone, mitochondrial
- Prohibitin 1
- Lon protease homolog, mitochondrial
- Prohibitin-2
- NADH dehydrogenase 1 alpha subcomplex subunit 13
- ATP-dependent Clp protease proteolytic subunit, mitochondrial
- Metalloendopeptidase OMA1, mitochondrial
- Mitochondrial-processing peptidase subunit alpha
Sequence:
MAHRCLLLWSRGGCRRGLPPLLVPRGCLGPDRRPCLRTLYQYATVQTASSRRSLLRDVIAAYQRFCSRPPKGFEKYFPNGKNGKKASEPKEAVGEKKEPQPSGPQPSGGAGGGGGKRRGKKEDSHWWSRFQKGDFPWDDKDFRMYFLWTALFWGGVMIYFVFKSSGREITWKDFVNNYLSKGVVDRLEVVNKRFVRVTFTPGKTPVDGQYVWFNIGSVDTFERNLETLQQELGIEGENRVPVVYIAESDGSFLLSMLPTVLIIAFLLYTIRRGPAGIGRTGRGMGGLFSVGETTAKVLKDEIDVKFKDVAGCEEAKLEIMEFVNFLKNPKQYQDLGAKIPKGAILTGPPGTGKTLLAKATAGEANVPFITVSGSEFLEMFVGVGPARVRDLFALARKNAPCILFIDEIDAVGRKRGRGNFGGQSEQENTLNQLLVEMDGFNTTTNVVILAGTNRPDILDPALLRPGRFDRQIFIGPPDIKGRASIFKVHLRPLKLDSALEKDKLARKLASLTPGFSGADVANVCNEAALIAARHLSDAINEKHFEQAIERVIGGLEKKTQVLQPEEKKTVAYHEAGHAVAGWYLEHADPLLKVSIIPRGKGLGYAQYLPKEQYLYTKEQLLDRMCMTLGGRVSEEIFFGRITTGAQDDLRKVTQSAYAQIVQFGMNEKVGQISFDLPRQGDMVLEKPYSEATARMIDDEVRILISDAYRRTVALLTEKKADVEKVALLLLEKEVLDKNDMVQLLGPRPFTEKSTYEEFVEGTGSLDEDTSLPEGLQDWNKEREKEEKKEKEKEEPLNEKVVS
Protein: Thrombospondin type-1 domain-containing protein 7A [Cleaved into: Thrombospondin type-1 domain-containing protein 7A, soluble form] (Q9UPZ6)
Organism: Homo sapiens (Human)
Function: Plays a role in actin cytoskeleton rearrangement.
Subcellular location: [Thrombospondin type-1 domain-containing protein 7A]: Cell membrane {ECO:0000269|PubMed:22194972, ECO:0000269|PubMed:25394321, ECO:0000269|PubMed:27214550}; Single-pass type I membrane protein {ECO:0000269|PubMed:22194972}. Cell projection {ECO:0000250|UniProtKB:Q69ZU6}. Note=Detected on podocyte foot processes. {ECO:0000250|UniProtKB:Q69ZU6}.; SUBCELLULAR LOCATION: [Thrombospondin type-1 domain-containing protein 7A, soluble form]: Secreted {ECO:0000269|PubMed:22194972}. Note=Proteolytic cleavage in the extracellular region generates a 210 kDa soluble form. {ECO:0000269|PubMed:22194972}.
Interaction partners:
- Secretory phospholipase A2 receptor
- Protein kinase C-binding protein NELL1
- Exostosin-1
- Semaphorin-3B
Sequence:
MGLQARRWASGSRGAAGPRRGVLQLLPLPLPLPLLLLLLLRPGAGRAAAQGEAEAPTLYLWKTGPWGRCMGDECGPGGIQTRAVWCAHVEGWTTLHTNCKQAERPNNQQNCFKVCDWHKELYDWRLGPWNQCQPVISKSLEKPLECIKGEEGIQVREIACIQKDKDIPAEDIICEYFEPKPLLEQACLIPCQQDCIVSEFSAWSECSKTCGSGLQHRTRHVVAPPQFGGSGCPNLTEFQVCQSSPCEAEELRYSLHVGPWSTCSMPHSRQVRQARRRGKNKEREKDRSKGVKDPEARELIKKKRNRNRQNRQENKYWDIQIGYQTREVMCINKTGKAADLSFCQQEKLPMTFQSCVITKECQVSEWSEWSPCSKTCHDMVSPAGTRVRTRTIRQFPIGSEKECPEFEEKEPCLSQGDGVVPCATYGWRTTEWTECRVDPLLSQQDKRRGNQTALCGGGIQTREVYCVQANENLLSQLSTHKNKEASKPMDLKLCTGPIPNTTQLCHIPCPTECEVSPWSAWGPCTYENCNDQQGKKGFKLRKRRITNEPTGGSGVTGNCPHLLEAIPCEEPACYDWKAVRLGNCEPDNGKECGPGTQVQEVVCINSDGEEVDRQLCRDAIFPIPVACDAPCPKDCVLSTWSTWSSCSHTCSGKTTEGKQIRARSILAYAGEEGGIRCPNSSALQEVRSCNEHPCTVYHWQTGPWGQCIEDTSVSSFNTTTTWNGEASCSVGMQTRKVICVRVNVGQVGPKKCPESLRPETVRPCLLPCKKDCIVTPYSDWTSCPSSCKEGDSSIRKQSRHRVIIQLPANGGRDCTDPLYEEKACEAPQACQSYRWKTHKWRRCQLVPWSVQQDSPGAQEGCGPGRQARAITCRKQDGGQAGIHECLQYAGPVPALTQACQIPCQDDCQLTSWSKFSSCNGDCGAVRTRKRTLVGKSKKKEKCKNSHLYPLIETQYCPCDKYNAQPVGNWSDCILPEGKVEVLLGMKVQGDIKECGQGYRYQAMACYDQNGRLVETSRCNSHGYIEEACIIPCPSDCKLSEWSNWSRCSKSCGSGVKVRSKWLREKPYNGGRPCPKLDHVNQAQVYEVVPCHSDCNQYLWVTEPWSICKVTFVNMRENCGEGVQTRKVRCMQNTADGPSEHVEDYLCDPEEMPLGSRVCKLPCPEDCVISEWGPWTQCVLPCNQSSFRQRSADPIRQPADEGRSCPNAVEKEPCNLNKNCYHYDYNVTDWSTCQLSEKAVCGNGIKTRMLDCVRSDGKSVDLKYCEALGLEKNWQMNTSCMVECPVNCQLSDWSPWSECSQTCGLTGKMIRRRTVTQPFQGDGRPCPSLMDQSKPCPVKPCYRWQYGQWSPCQVQEAQCGEGTRTRNISCVVSDGSADDFSKVVDEEFCADIELIIDGNKNMVLEESCSQPCPGDCYLKDWSSWSLCQLTCVNGEDLGFGGIQVRSRPVIIQELENQHLCPEQMLETKSCYDGQCYEYKWMASAWKGSSRTVWCQRSDGINVTGGCLVMSQPDADRSCNPPCSQPHSYCSETKTCHCEEGYTEVMSSNSTLEQCTLIPVVVLPTMEDKRGDVKTSRAVHPTQPSSNPAGRGRTWFLQPFGPDGRLKTWVYGVAAGAFVLLIFIVSMIYLACKKPKKPQRRQNNRLKPLTLAYDGDADM
Protein: Alpha-galactosidase C (EC 3.2.1.22) (Melibiase C) (Q5AU92)
Organism: Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Function: Hydrolyzes a variety of simple alpha-D-galactoside as well as more complex molecules such as oligosaccharides and polysaccharides. Active on paranitrophenyl-alpha-galactoside, raffinose, locust bean gum and gum guar.
Subcellular location: Secreted {ECO:0000250}.
Interaction partners:
- Alpha-galactosidase D
- Probable alpha-galactosidase B
- alpha-galactosidase
- Probable alpha-galactosidase G
- beta-galactosidase
- Beta-hexosaminidase
- Zn
- Lactase
- Beta-galactosidase
- Glycosyl hydrolases family 32 superfamily
Sequence:
MFRSTATVAAATAMGLLTATGHGSLAIAQGTTGSNAVVVDGTNFALNGASMSYVFHANSTTGDLVSDHFGATISGAIPAPKEPAVNGWVGMPGRIRREFPDQGRGDFRIPAVRIRQTAGYTVSDLQYQGHEVVDGKPALPGLPATFGEAGDVTTLVVHLYDNYSAVAADLSYSVFPEFDAVVRSVNVTNKGKGNITIENLASLSVDFPLEDLDLVSLRGDWAREANRERRRVEYGIQGFGSSTGYSSHLHNPFFALVHPSTTESQGEAWGFNLVYTGSFSAQVEKGSQGLTRALIGFNPDQLSWNLGPGETLTSPECVSVYSKDGIGGMSRKFHRLYRKHLIRSKFATSDRPPLLNSWEGVYFDFNQSSIETLAEQSAALGIRLFVMDDGWFGDKYPRTSDNAGLGDWTPNPDRFPNGLEPVVEEITNLTVNDTSAEKLRFGIWVEPEMVNPNSSLYREHPDWALHAGAYARTERRNQLVLNLALPEVQEYIIDFMTDLLNSADISYIKWDNNRGIHEAPSPSTDHEYMLGVYRVFDTLTARFPDVLWEGCASGGGRFDAGVLHYFPQIWTSDNTDGVDRVTIQFGTSLAYPPSAMGAHLSAVPNHQTGRTVPLEFRAHVAMMGGSFGLELDPATLQDDPDVPELIQMAEKVNPLVLNGDLYRLRLPEESQWPAALFVAEDGSQAVLFYFQLSPNVNHAAPWVRLQGLDPEASYTVDGDKTYTGATLMNLGLQYTFDTEYGSKVVFLERQ
Protein: Kinesin, putative (Q382E5)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
Interaction partners:
Sequence:
MGSSVTVCCLVEVSICRVGSFRSGFNMSKKHQGAENIRVVIRCRNLLGFETERGDKALVRLDLATNQVIVQHPIGDADVFAFDAVYNNTYTQRDLFLQEVQPLVEAVLQGYNATVFAYGQSGSGKTHTMTGKLNDQEMWGMMPQVVNHLFNEIKKLTSATRTYKVKVSYIELYNGKSRDLLSAKQGNLEIKQNMAKNFYVKGAEMPEVTNFGEALRWFNAGTDRRQTASTDLNDNSSRSHSLFTLQVEQFDFEQDPSAPIVLTSKINLVDLAGSEKLSKTNATGETAKEGCNINLSLSALATVIDTIVKGGKHIPYRGSPLTMLLKDSLGGNAKTVMFANIGPSDKNISETISTLRFALRAKEIENKPIKNLDPKDARIQDLLDQIADLKSRMGDVDLNKEDQLKQRIEELEIENADLRGGSDKNNLELEENCRNLQAQLEKVNEALVEKQKEVAKEVDARAMVEWNLQNETSHVQDLRSVAINFIRRVCSESQLKDIRAKMPQDGSYNVKDETWDVKEIRFCLDEFTAMYESMRTSSYTREDLEQYAQKAAVSLQEQAQRQLHEAVRSRDELARQRQEDSAKRAAESELLSQLKVEVNSLKDENAKLRDKIERDQERIKAKVAKSKEEYKTVAEQLERTKSVVTEKERDIERLKKMLEESGSSTPGNTQSAWATSEERANLLRMLEEEKNARKDLESCVRETNVSLRRYGVCISQSKAPATSEGESAAENAEAFILQAASEEPIDGDLYSQFQQQIRVMQRLTQLRHQQQKKLGDMVKKYELLKTGKVTSNHVAPPGAAAQGGGVDETTAQQIKELLRKKDDEIERITQEKEKTCDKIVKKLNKSEMKIRELETALEEERAQFTEERQVLDSENQELQKFNQQLSVEVEMLRAQLNVVKEEMSSLERAKAAELERWKEEEEDYNTRINEMRSSMSAYDELQKSYDRLQQQLQHAEAALKEKTDNLENNRQIIKWSNSLLSAEKEKVEQMEMMMKRQEEEMRRHEEQLRSEMVDEINKQVVANNRRLQDQAAQFQDIISQEQEKQKSIVKKVKAARKDAQKAAQRYDEMILENESLLSKLEELKVNSMRIFLEKQEAQRELDALRPSRVAATRRL
Protein: Conserved protein (CPSA-related protein) (P96872)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Interaction partners:
- TIGR03089 family protein
- dTDP-4-dehydrorhamnose reductase
- N-acetylglucosaminyl-diphospho-decaprenol L-rhamnosyltransferase
- Mannose-1-phosphate guanylyltransferase
- SteA-like C-terminal domain-containing protein
- Manganese-exporting P-type ATPase
Sequence:
MMSAQRVVRTVRTARAISTALAVAIVLGTGVAWSSVRSFEDGIFHMSAPSLGHGGDDGAIDILLVGLDSRTDAHGNPLSAEELATLHAGDEEATNTDTIILIRVPNNGKSATAISIPRDSYVAAPGLGKTKINGVYGQTRETKRAGLVQAGASPTEAAAAGTEAGREALIKTVADLTGVTVDHYAEIGLLGFALIADALGGVDVCLKEPVYEPLSGADFPAGRQKLNGPQALSFVRQRHDLPRGDLDRVVRQQAVMAALAHRVISGQTLSSPATLKRLEQAVQRSVVLSSGWDIMDFVRQLQKLAGGNVAFATIPVLDGAGWSDDGMQSVVRVDPRQVQDWVVGLLHEQDQGKTDELAYTPAKTTANVVNDTDINGLAAAVSKVLSSKGFTTGSVGNNDGDHVPGSQVRAAKADDLGAQQVAKELGGLPVVADASIAPGSVRVVLANDYSGPGSGLGGSDPNGVVSPARAFNLGSADDTTPPPSPILTAGSDAPECIN
Protein: Cytosolic 10-formyltetrahydrofolate dehydrogenase (10-FTHFDH) (FDH) (EC 1.5.1.6) (Aldehyde dehydrogenase family 1 member L1) (O75891)
Organism: Homo sapiens (Human)
Function: Cytosolic 10-formyltetrahydrofolate dehydrogenase that catalyzes the NADP(+)-dependent conversion of 10-formyltetrahydrofolate to tetrahydrofolate and carbon dioxide. May also have an NADP(+)-dependent aldehyde dehydrogenase activity towards formaldehyde, acetaldehyde, propionaldehyde, and benzaldehyde (By similarity).
Subcellular location: Cytoplasm, cytosol {ECO:0000305|PubMed:19933275}.
Interaction partners:
- Trifunctional purine biosynthetic protein adenosine-3
- C-1-tetrahydrofolate synthase, cytoplasmic
- Serine hydroxymethyltransferase, cytosolic
- Serine hydroxymethyltransferase, mitochondrial
- Bifunctional methylenetetrahydrofolate dehydrogenase/cyclohydrolase
- Bifunctional methylenetetrahydrofolate dehydrogenase/cyclohydrolase 2, mitochondrial
- Mitochondrial 10-formyltetrahydrofolate dehydrogenase
- Methionine synthase
- Dihydrofolate reductase
- Formimidoyltransferase-cyclodeaminase
Sequence:
MKIAVIGQSLFGQEVYCHLRKEGHEVVGVFTVPDKDGKADPLGLEAEKDGVPVFKYSRWRAKGQALPDVVAKYQALGAELNVLPFCSQFIPMEIISAPRHGSIIYHPSLLPRHRGASAINWTLIHGDKKGGFSIFWADDGLDTGDLLLQKECEVLPDDTVSTLYNRFLFPEGIKGMVQAVRLIAEGKAPRLPQPEEGATYEGIQKKETAKINWDQPAEAIHNWIRGNDKVPGAWTEACEQKLTFFNSTLNTSGLVPEGDALPIPGAHRPGVVTKAGLILFGNDDKMLLVKNIQLEDGKMILASNFFKGAASSVLELTEAELVTAEAVRSVWQRILPKVLEVEDSTDFFKSGAASVDVVRLVEEVKELCDGLELENEDVYMASTFGDFIQLLVRKLRGDDEEGECSIDYVEMAVNKRTVRMPHQLFIGGEFVDAEGAKTSETINPTDGSVICQVSLAQVTDVDKAVAAAKDAFENGRWGKISARDRGRLMYRLADLMEQHQEELATIEALDAGAVYTLALKTHVGMSIQTFRYFAGWCDKIQGSTIPINQARPNRNLTLTRKEPVGVCGIIIPWNYPLMMLSWKTAACLAAGNTVVIKPAQVTPLTALKFAELTLKAGIPKGVVNVLPGSGSLVGQRLSDHPDVRKIGFTGSTEVGKHIMKSCAISNVKKVSLELGGKSPLIIFADCDLNKAVQMGMSSVFFNKGENCIAAGRLFVEDSIHDEFVRRVVEEVRKMKVGNPLDRDTDHGPQNHHAHLVKLMEYCQHGVKEGATLVCGGNQVPRPGFFFEPTVFTDVEDHMFIAKEESFGPVMIISRFADGDLDAVLSRANATEFGLASGVFTRDINKALYVSDKLQAGTVFVNTYNKTDVAAPFGGFKQSGFGKDLGEAALNEYLRVKTVTFEY
Protein: Alpha-conotoxin-like ts14a (P86362)
Organism: Conus tessulatus (Tessellate cone)
Function: Alpha-conotoxins act on postsynaptic membranes, they bind to the nicotinic acetylcholine receptors (nAChR) and thus inhibit them.
Subcellular location: Secreted {ECO:0000269|PubMed:20691232}.
Interaction partners:
Sequence:
DGCPPHPVPGMHPCMCTNTC
Protein: F-box protein SKIP5 (SKP1-interacting partner 5) (Q94FT2)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- Putative F-box protein At3g25750
- F-box protein At3g54460
- At3g29270
- non-specific serine/threonine protein kinase
- Glutamate receptor 3.7
- F-box protein SKIP1
- Elongation factor Ts, mitochondrial
- Probable protein phosphatase 2C 51
Sequence:
MELHEISKLDNKKHPERIVESKMKKRMKPYSLTSLNNLDDGCLMHILSFLSPIPDRYNTALVCHRWRYLACHPRLWLRVDRFVKDLSQPGVFLNIESAVSAARPGDTILIVAGGNYRVSNIQIKKPLCLVGGGEIPDETTLVCARGSDSALELLSTCKLANLTVKAELGCCLLHRSGRLTIDGCVLQCETNPLDHLSCPIVSTAGDEDIENILSHVEVKETVTGKIKANSVTVLQTRIEGGAKAVSTRGDLVLQRVRVMYSKAYLYFWFDVDYE
Protein: Poly(3-hydroxyalkanoate) depolymerase (Q6YNP7)
Organism: Rhodospirillum rubrum
Interaction partners:
Sequence:
MRAFCRFVGAALLLVGLAGPAWADSLPKLAIDADHVTVSGISSGAYMANQFHVAHSARVDGAGLVAGGLYGCAVSTVVNDKVMATASRALAHCMRQSAFLESADRFVGIARQLERAGAIDALAGLRGDRVYLFTGEADTVVGAKVVRTAAEALGTLGVTTTLVSSLQGTPGAGAKAGHAFLTPDRGNAACSAEKSPFFNACRYDQAEAILKVLYGPSLAPPAPVLSGRLSRFDQSAYVRGGNAIKASLWDEGLVYVPADCAAGAACRLHIAFHGCKQSDQVLGSAEKFWDLAGYNGWADTNHIVVLYPQARAIGATEGFPLTAINPEGCWNWWGYGLDGKFLGREGLQISAVNAMINALAGR
Protein: Bifunctional dihydrocamalexate synthase/camalexin synthase (EC 1.14.19.52) (Cytochrome P450 71B15) (Dihydrocamalexate:NADP(+) oxidoreductase (decarboxylating)) (Protein PHYTOALEXIN DEFICIENT 3) (Q9LW27)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Multifunctional enzyme involved in the biosynthesis of the indole-derived phytoalexin camalexin. Catalyzes two reactions, the formation of dihydrocamalexate from indole-3-acetonitrile-cysteine conjugate and the oxidative decarboxylation of dihydrocamalexate which is the final step in camalexin biosynthesis. Required for the resistance to the fungal pathogens A.brassicicola, B.cinerea, B.elliptica, B.tulipae, L.maculans and Colletotrichum higginsianum. Seems not to be required for resistance to P.syringae, P.porri, and not involved in age-related resistance.
Subcellular location: Membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}.
Interaction partners:
- Probable WRKY transcription factor 33
- Protein MKS1
- Transcription factor MYB51
- Defensin-like protein 16
- Mitogen-activated protein kinase 3
- Mitogen-activated protein kinase 4
- Mitogen-activated protein kinase 6
- Lipase-like PAD4
- Regulatory protein NPR1
- Isochorismate synthase 1, chloroplastic
Sequence:
MSVFLCFLVLLPLILIFLNVLKPSKYKLPPGPKKLPIIGNLHQRRTLHPRNRRNLAEMYGPVALLQYGFVPVVAISSKEAAEEVLKINDLECCSRPEAAGMRATFYNFKDIGMAPFGDEWSLMRKLSVVELFSVKKLQSFKYIIEEENNLCVKKLSEFATRQSPVNLERAIFTLVGNIVCRIGYGINLYECDFFEADRVVDLVLKAEAVIRETVFSDFFPGRIGRFIDCISGQNRRLKNNFSVVDTFFQNVLNEHLKPGRESSTIVDLMIDMKKKQENDGDALKFTTDHLKGMISDIFVAGIGGVAGITLWGMTELIRNPRVMKKVQDEIRTTLGDKKERIKEEDLNQLHYFKLVVKETLRLHPTTPLLLPRQTMSHIKIQGYDVPAKTQILVNVYAMGRDPKLWENADEFNPDRFLDSSVDFKGKNYEFIPFGSGRRICPGMTMGTILVEMALLNLLYFFDWGLAKQEEAKEIINGEENFLAFFQVLHH
Protein: Zinc finger MYM-type protein 3 (DXHXS6673E protein) (Zinc finger protein 261) (Q9JLM4)
Organism: Mus musculus (Mouse)
Function: Plays a role in the regulation of cell morphology and cytoskeletal organization.
Subcellular location: Nucleus {ECO:0000269|PubMed:10662551}.
Interaction partners:
- Genetic suppressor element 1
Sequence:
MDPSDFPSPFDPLTLPEKPLAGDLPVDMEFGEDLLESQTAPSRGWAPPGPSPSSGALDLLDTPSGLEKDPGGVLDGATELLGLGGLLYKAPSPPEVDHGPEGTLAWDSGEQTLEPGPGCQTPEVMPPDPGAGASPPSPEGLLEPLAPDSPIILESPHIEEEIPPLATRRRGSPGQEEEHTQGQPQSPNAPPSPSVGETLGDGINSSQSKPGVCTPTAHPSLPGDGLTGKEIEKPPERVQKRSERVRRAEPPKPEVVDSTESIPVSDEDSDAMVDDPNDEDFVPFRPRRSPRMSLRSSMAQRAGRSSMGTKMSCAHCRTPLQKGQTAYQRKGLPQLFCSSSCLTTYSKKPLGRKTCTFCKKEIWNTKDSVVVQTGPGGSFHEFCTSVCLSLYEAQQQRPIPQSGDPADATRCSICQKTGEVLHEVSNGSVVHRLCSDSCFSKFRANKGLKTNCCDQCGAYIYARPGGLGPELLFHDGQQKRFCNTTCLGAYKKKNTRVYPCVWCKTLCKNFEMLSHVDRNGKTSLFCSLCCTTSYKVKQAGLTGPPRPCSFCRRSLSDPCYYNKVDRTVYQFCSPSCWTKFQHTSPEGGIHLSCHYCHSLFSGKPEVLEWQDQVFQFCCRDCCEDFKRLRGVVSQCEHCRQEKLLHEKLRFSGVEKSFCSEGCVLLYKQDFTKKLGLCCITCTYCSQTCQRGVTEQLDGSTWDFCSEDCKTKYLLWYCKAARCHACKRQGKLLETIHWRGQIRHFCNQQCLLRFYSQQNQPNLDTQSGPESLLNSQSSESKPQTPSQTKVENNHTVRTPDENGNLGKTPVKRATPSVPTPPPPPPPATPRKNKAAMCKPLMQNRGVSCKAEMKSKGSQTEEWKPQVIVLPIPVPIFVPVPMHLYCQKVPVPFSMPIPVPVPMFLPTTLESTEKIVETIEELKVKIPSNPLEADILAMAEMIAEAEELDKASSDLCDLVSNQSAEGLLEDCDLFGTARDDVLAMAVKMANVLDEPGQDLEADFPKNPLDINPSVDFLFDCGLVGPEDVSTEQDLPRAMRKGQKRLMLSESCSRDSLSSQPSCTGLNYSYGVNAWKCWVQSKYANGETSKGDELRFGPKPMRIKEDILACSAAELNYGLAQFVREITRPNGERYEPDSIYYLCLGIQQYLLENNRMVNIFTDLYYLTFVQELNKSLSTWQPTLLPNNTVFSRVEEEHLWECKQLGVYSPFVLLNTLMFFNTKFFGLQTAEEHMQLSFTNVVRQSRKCTTPRGTTKVVSIRYYAPVRQRKGRDTGPGKRKREDETILEQRENRMNPLRCPVKFYEFYLSKCPESLRTRNDVFYLQPERSCIAESPLWYSVIPMDRSMLESMLNRILAVREIYEELGRPGEEDLD
Protein: Epididymis secretory sperm binding protein (A0A384P5D7)
Organism: Homo sapiens (Human)
Subcellular location: Mitochondrion inner membrane {ECO:0000256|ARBA:ARBA00004434}; Single-pass membrane protein {ECO:0000256|ARBA:ARBA00004434}.
Interaction partners:
Sequence:
MALSRVCWARSAVWGSAVTPGHFVTRRLQLGRSGLAWGAPRSSKLHLSPKADVKNLMSYVVTKTKAINGKYHRFLGRHFPRFYVLYTIFMKGLQMLWADAKKARRIKTNMWKHNIKFHQLPYREMEHLRQFRQDVTKCLFLGIISIPPFANYLVFLLMYLFPRQLLIRHFWTPKQQTDFLDIYHAFRKQSHPEIISYLEKVIPLISDAGLRWRLTDLCTKIQRGTHPAIHDILALRECFSNHPLGMNQLQALHVKALSRAMLLTSYLPPPLLRHRLKTHTTVIHQLDKALAKLGIGQLTAQEVKSACYLRGLNSTHIGEDRCRTWLGEWLQISCSLKEAELSLLLHNVVLLSTNYLGTRR
Protein: KAT8 regulatory NSL complex subunit 1 (NSL complex protein NSL1) (Non-specific lethal 1 homolog) (Q80TG1)
Organism: Mus musculus (Mouse)
Function: As part of the NSL complex it is involved in acetylation of nucleosomal histone H4 on several lysine residues and therefore may be involved in the regulation of transcription.
Subcellular location: Nucleus {ECO:0000250|UniProtKB:Q7Z3B3}. Chromosome, centromere, kinetochore {ECO:0000250|UniProtKB:Q7Z3B3}. Mitochondrion {ECO:0000269|PubMed:37813994}.
Interaction partners:
- PHD finger protein 20
- KAT8 regulatory NSL complex subunit 2
- KAT8 regulatory NSL complex subunit 3
- WD repeat-containing protein 5
- Microspherule protein 1
- Histone acetyltransferase KAT8
- Host cell factor 1
- UDP-N-acetylglucosamine--peptide N-acetylglucosaminyltransferase 110 kDa subunit
- Male-specific lethal 1 homolog
- Histone-lysine N-methyltransferase 2A
Sequence:
MAAMAPALTDAAAEAHHIRFKLAPPSSTLSPGSAENNGNANILISANGTKRKAIAAEDPSLDFRNNPTKEDLGKLQPLVASYLCSDVTSVPAKESLKLQGVFSKQTVLKSHPLLSQSYELRAELLGRQPVLEFSLENLRTMNTSGQTALPQAPVNGLAKKLTKSSTHSDHDNSSSLNGGKRSLTSSSLQGGEVGGPDSGNLKGGMTNCTLPHRSLDIQHTTLYSNNSTANKSSVNSMDQPALQGSSRLSPSTDSSSNLTNVKLEVKKSPLSSILFSALDSDTRITALLRRQADIEIRARRLQKRLQVVQAKQVERHLQHQLGGFLETTLSKLPNLESLRSRSQLMLTRKAEAALRKAASESATSEGLSNFLKSDSISEELERFTASGIANLRCSEQAFDSDVTDSSSGGESDIEEEELTRADPEQCHVPLKRRSEWRWAADRAAIVSRWNWLQAHVSDLEYRIRQQTDIYKQIRANKGLIVLGEAPFPDHTTDLLSLSSEVKTDHGRDKLIESVSQPSENHGILVSNITESLSTKSCGAPRPVNGVVNSLQPVLADQVPGDSSDAEEQLHKKQRLNLVSSSDGTCVAARTRPVLTCKKRRLVRPSSIVPLSKKVHRNVRSGCDVNPSCALCGSGSVNTMPPEIHYEAPLLERLSQLDSCVHPVLAFPDDVPTSLHFQSMLKSQWQNKPFDKIKPTKKFSLKHRATMPCSLSDPVRKDRHKLVNSFLTTAMLKHHTDMSSPSYLTATHHPPHSPLVRQLSTSSDTSTPTSSGSQVAASTSQPVRRRRGESSFDINNIVIPMSVAATTRVEKLQYKEILTPSWREVDVQSLKGSPDEENEEIEDLSDAAFAALHAKCEEMERARWLWTTSVPPQRRGSRSYRSSDGRTTPQLGSANPSTPQPASPDVSSSHSLSEFSHGQSPRSPISPELHSAPLTPVARDSLRHLASEDTRCSTPELGLDEQSVQPWERRTFPLAYSPQAECEEQLDAQDTAARCTRRTSGSKTGREAEVAPTSPPVVPLKSRHLAATVTAQRPAHR
Protein: Heterogeneous nuclear ribonucleoprotein 87F (HRP36.1 protein) (Protein P11) (P48810)
Organism: Drosophila melanogaster (Fruit fly)
Function: This protein is a component of ribonucleosomes. Could be needed to organize a concentration gradient of a dorsalizing morphogen (Dm) originating in the germinal vesicle.
Subcellular location: Nucleus {ECO:0000269|PubMed:1717937}. Cytoplasm {ECO:0000269|PubMed:1717937}. Note=Nuclear and/or cytoplasmic.
Interaction partners:
- Heterogeneous nuclear ribonucleoprotein K, isoform C
- Heterogeneous nuclear ribonucleoprotein A1
- Zinc finger protein on ecdysone puffs
- Serine-arginine protein 55
- AT27789p
- RNA-binding protein squid
- LD31543p
- FI21236p1
- LD32469p
- Protein no-on-transient A
Sequence:
MAEQNDSNGNYDDGEEITEPEQLRKLFIGGLDYRTTDDGLKAHFEKWGNIVDVVVMKDPKTKRSRGFGFITYSQSYMIDNAQNARPHKIDGRTVEPKRAVPRQEIDSPNAGATVKKLFVGGLRDDHDEECLREYFKDFGQIVSVNIVSDKDTGKKRGFAFIEFDDYDPVDKIILQKTHSIKNKTLDVKKAIAKQDMDRQGGGGGRGGPRAGGRGGQGDRGQGGGGWGGQNRQNGGGNWGGAGGGGGFGNSGGNFGGGQGGGSGGWNQQGGSGGGPWNNQGGGNGGWNGGGGGGYGGGNSNGSWGGNGGGGGGGGGFGNEYQQSYGGGPQRNSNFGNNRPAPYSQGGGGGGFNKGNQGGGQGFAGNNYNTGGGGQGGNMGGGNRRY