wanglab/gogpt-training-data huggingface dataset:
Protein: Mitochondrial thiamine pyrophosphate carrier 1 (Q5AL11)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Subcellular location: Mitochondrion inner membrane {ECO:0000256|ARBA:ARBA00004448}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004448}.
Interaction partners:
Sequence:
MSSLSSELKAKEIFNQFATEGANEEKIITLPDFINVLSPFTTDIPKQAFSLLYLIADAEKKGFVTEDNWLKFVNTLTSPDGEYKLLYQFLSGQQNTNSKITYSQCIDILNKINSSIDPSYQQKLIKLNWIYFPRFFEPNGSIEFNDFVTLISYLPVTKLIGNFEITASKSKTVNGEELVRLLSTNLNHKLSNKLKINLHNVTDFFGKQQDYTLSNLLFIYDALSKVDLINEVIVNTPPTTKDKDDILINKTDLYNHLNDPLLKSANFKPVSRLELDLLFYLINKKTDEDIPRRELVSFLNPNFNNNLNTLAPIFEHSQSKHSTIDGGDNFSLWPLYDSLYSFFLGSIAGCIGATAVYPIDLVKTRMQAQKHNALYDNSLDCFKKILRNEGFKGLYSGLGAQLVGVAPEKAIKLTVNDLVRGIGSNEDGSITMKWEILAGSTAGGCQVIFTNPLEIVKIRLQMQGNTKNLSKPGEIPHKHLNASQIIRQLGLRGLYKGASACLLRDVPFSAIYFPTYANLKKHMFGFDPNDKTKHQKLSTWQLLVAGALAGAPAAFFTTPADVIKTRLQVAGKKNEAKYKGILDCGASILKQEGLSAFFKGSLARVFRSSPQFGFTLASYELLQNLFPLHPPLTRESSFKGISGYPGVYNLTNDQVYNSQEKNERLILMNKSELSPSPSSSSSSLDTVNDTLVKLPAEYIYKSQDAVKLLLDIDYKFGNFNYDSYVNYIKKK
Protein: Tegument protein UL24 (F5H9N4)
Organism: Human cytomegalovirus (strain Merlin) (HHV-5) (Human herpesvirus 5)
Subcellular location: Virion tegument {ECO:0000250}.
Interaction partners:
Sequence:
MEETRAGRYIVRAGSGGQTEDTASGAESVLATLAAVRTRRRSVVCDGPPGSPTDSARHMSDLASLALTAEFGLGCLEAYVRINAGQVLPVVWPPGWNLVLQEIETDEDFKPEDVKAWSHYLCCQTRLAFVGRFVNEGVLSPDQQKKTAVCLISDEGYVFCYVREDTAVYYLARNLMEFARVGLRAVETLHCMRYLTSSLVKRYFRPLLRAWSLGLDTMARFIIRHHGQFMPLTYPPGTELRLCNLRCFENSVEGGHLLRNIKTAFGMRVLGLGTVSLKGENAPFPHLRWPVDLIPIVVAYTGAVYACDVRDDRYIRVGDNLNTFMCLGLNLLFENRRFSGHNGIYDRVPDCPKGRQHR
Protein: Ribosome biogenesis protein WDR12 homolog (Q9VKQ3)
Organism: Drosophila melanogaster (Fruit fly)
Function: Required for maturation of ribosomal RNAs and formation of the large ribosomal subunit.
Subcellular location: Nucleus, nucleolus {ECO:0000255|HAMAP-Rule:MF_03029}. Nucleus, nucleoplasm {ECO:0000255|HAMAP-Rule:MF_03029}.
Interaction partners:
- Pescadillo homolog
- Ribosome biogenesis protein BOP1 homolog
- Probable ATP-dependent RNA helicase pitchoune
- LD47540p
- 60S ribosome subunit biogenesis protein NIP7 homolog
- RRM domain-containing protein
- Ribosomal L1 domain-containing protein CG13096
- Protein MAK16 homolog
- Ribosome biogenesis protein BRX1 homolog
- Nucleolar complex protein 2
Sequence:
MDVDNGEGQVQVHLKTKQEHYAVPDVPYAIDGTVTTVELNTFVNALLRQKDGSSDTDFDFLVFDEYLRGRLCDHLREKAISFEDAIEIEYVERFPAPEPQDCLLHDDWVSAVKARGKWILSGCYDNTLNLWTNKGKHILTISGHTAPIKAVDWISLDEETGRFVSTSQDQTAMLWQWNVGSNSVECVSVCKGHERGVDSVSVSPDGLRFATGSWDTMLKVWSAELDDAVEGSSKRMKESGVRTPKITLQGHRESVSAVQWMDATTLLTGSWDHTLKVWDLSLEGIKTEISTNKSIFDASYSKLNRLILTASADKNLRLYDPRTNQGSVVRNTYLGHNAWVQTVMWSTTEEFLFVSGAYDNQNKLWDCRSPKAPLYDLLGHGEKVLDIDWSNPKYIVSGGVDNTVRVFKSRKALAEEAETK
Protein: Kotanin synthase (EC 2.3.1.-) (Kotanin biosynthesis cluster protein S) (Non-reducing polyketide synthase ktnS) (A2QK66)
Organism: Aspergillus niger (strain ATCC MYA-4892 / CBS 513.88 / FGSC A1513)
Function: Non-reducing polyketide synthase; part of the gene cluster that mediates the biosynthesis of the bicoumarin kotanin. The non-reducing polyketide synthase ktnS first catalyzes the formation of the pentaketidic 4,7-dihydroxy-5-methylcoumarin from acetyl coenzyme A and 4 malonyl coenzyme A molecules. Further O-methylation by ktnB leads to the formation of 7-demethylsiderin. Then, an oxidative phenol coupling catalyzed by the cytochrome P450 monooxygenase ktnC forms the 8,8'-dimer P-orlandin via dimerization the monomeric precursor, 7-demethylsiderin. P-orlandin is subsequently O-methylated in a stepwise fashion to demethylkotanin and kotanin.
Interaction partners:
Sequence:
MLADMCVGVYKAAMNYEIRPHEFSFNTQESLFTGLGLGFLAATAVVASPSLLDLPITAAEVVRIAMRAGILLYQKSQDLEQLSLDSSLESWTTVVRGLDESIVRGELEKFNKSMETPPSSRIYISVVEPDGSVFISGPPSGLREFFNKSGKVQSAPRAPLPVYGGPCHAAHLYDRTHTEWVVSKVNPEIASRRLSGHPLVLSMGDGQPLAGENARDLFESATYVLLTSIIRWDSVLAAVKKLPHWKQDTKLQLETFRPSSPAVHGLISAVQSEYPDCTVSVDDLGDWIIDNSLEPPTIPIDSRIAVVGMSCRLPGGSDDLQRFWELLEDGRDVHQKVPGNRYDVESHTDMTGRRLNTSHTPFGCFIDSPGLFDASFFDMSPREAGQTDPTHRLALLTAYEALEYSGYVPNRTRSTTRDRVGTVYGQCSDDYREANAGQNIDMYFIPGNYRAFAPGRISYFFKFSGPSFNCDTACSASLAAVQIACSALIRGEADMVVAGGLNILTGSDSFAGLSRGFFLSKTGNCKVFDDGADGYCRADGIGSIVLKRLSDAQQDNDNILGVILGTATNHSSHAISITHPHAPTQEHLYRSVLSQAGIGPHDVDLVEMHGTGTQAGDAAEIESVTRVFSPPVPRRSHPLYISSVKANLGHGEAAAGITALMKALLIFQHNAIPRHVGIKTALNSKFPDLERLNVHIPKETIPWPYRSNRKRYVMINNFSAAGGNTSLLLEEPPVRPDPQGPPQTRFVVALSAKSTTSLRRNLESLITWLEGNRSARLASLAYTTTARRMHHKHRIAVHGASVAEIIQALHQRGSRAELGLLVSKPPSVAFIFSGQGSFYAGVGSQLFKEYPPYREQLQRLDEICQQNGFGSILPAITDTDADVSQLSALVTQLTTVCVQIALCRLWRTLGVKPAVVIGASLGEYAALYAAGALSASDAIFLVGQRTLLMQKLCTANSYGMLAVQGSVDDIRRCVQDRTYEVACINAPRSITICASIKDIVDIQQSLVSQGYRSVKLNVPFAFHSSQMDPILDRYEEIAKAVSFRSLQIPLISSTLADAAVQSRSLVASLFLRENTRAPARFAEAVAKAQDMGLVNSHTVWVEIGVHSTYSGAVRATVADLQAIVPSLRSDETNWHTLAVSMCTLQETGVPLDWNEWYRPFEPEVRLLDLPSYRWDLKNHWIQYNGDWLLVKDKRPRTDQISAATPSLRTALVHQIMEESFRPDGGEIVVQSDVMDKEFFAVASGHKMSGRPLVSVFSYPDIAFTLARYMYSRLKPESPLPAMDFGQVRVLQGLLPRKDRSKPQWVRMRMRADPQCAALQLSISGLSDESSRHVEEKLASGVVRCGDRQSWQDEWADYAHLLTTRIVTLQQMAENGQASRVSRDLVYTLFKNIVDYADHYRGIQSAVLHGLEAVADVILAPSNDSRWTAPPHHIDPITHVGGLVLNAGHATDHHNTIYVMEGWKSMRFAEELVAGELYRSYVKMNPARDGSGFFVGDVYVMREDHIVGKVRGMTLRPLPRILMNRFFDPPDDGDGLATQHIQPHDLPQVQHQPSPTTDSGPDDDPKDPNTGPLTPEVDLPVAPSVEKANTKLVRGALALLAAETGVEPDGLTDETEVSALGIDSLLSLVLVEKFATELQVNIQSSFFLESPTIRELKEYLTASW
Protein: Neuronal acetylcholine receptor subunit alpha-5 (P26152)
Organism: Gallus gallus (Chicken)
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: Synaptic cell membrane {ECO:0000250|UniProtKB:P32297}; Multi-pass membrane protein {ECO:0000255}. Cell membrane {ECO:0000250|UniProtKB:P32297}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Neuronal acetylcholine receptor subunit beta-2
- Neuronal acetylcholine receptor subunit alpha-3
- Neuronal acetylcholine receptor subunit beta-4
- Neuronal acetylcholine receptor subunit alpha-2
- Acetylcholine receptor subunit alpha
Sequence:
MPLRARSRKPGAGPAARAPQAGVSEPSFVAKSEDRLFKHLFEDYQRWVRPVEHLNDTIKIKFGLAISQLVDVDEKNQLMTTNVWLKQEWIHVKLRWNPEDYAGITSIRVPSDSIWIPDIVLYDNADGRFEGTSTKTVVKYDGTIAWTPPVNYKSSCTIDVTFFPFDLQNCSMKFGSWTYDGSQVDIILEDYEVDKRDFFDNGEWEIVTATGSKGNRTDGCCWYPFVTYSFIIRRLPLFYTLFLIIPCIGLSFLTVLVFYLPSNEAEKISLCTSVLVSLTVFLLVIEEIIPSSSKVIPLIGEYLVFTMIFVTLSIVITVFAINIHHRSSSTHNAMAPWVRKIFLHKLPKLLCMRSHVDRYFAQKEEKGNMSGSESSRNTLEAALDSIRYITRHVMKENEVREVVEDWKFIAQVLDRMFLWAFLLVSIIGSLVLFIPVIHKWASIIVPVHIGSTNT
Protein: Aldose 1-epimerase (EC 5.1.3.3) (Q9VRU1)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- UDP-glucose 4-epimerase
- Beta galactosidase, isoform A
- Beta-galactosidase
- Alpha-galactosidase
- FI19814p1
- LD24362p
- GH11113p
Sequence:
MVNVTEDVFANGAVNPFTKSKDTIKRFTLTNGAGMSVQLITRGATITSIKTPDASGQIDDVTLGFDDLAGYQSERNPYFGATIGRVCNRIANGSFYLDGKLVQVSKNRDNKFQLHGGFVGFDKAHWEVVEVRVDGVTLSHTNPDGHEGYPGKVTATASFTLSEDNCLHVQMSALADKTTPVNLTNHSYFNLAGHKSGANGLYEHTIEINAYGITETDQSSIPTGRITPVEGTGFDLRVSSNLGERLKALQPARGYDDNFCVTFSPPQPLAKVARATHPPSGRWLEVVSNQPGVQFYTSNFMPDVERGESPIPGKDGAAYAKHCAFCLETQKFPDSVNHSNFPSTILRPGESYQHEVIYKFGVSH
Protein: dTDP-glucose 4,6-dehydratase (EC 4.2.1.46) (P9WN65)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: Catalyzes the dehydration of dTDP-D-glucose to form dTDP-6-deoxy-D-xylo-4-hexulose via a three-step process involving oxidation, dehydration and reduction (By similarity). Involved in the biosynthesis of the dTDP-L-rhamnose which is a component of the critical linker, D-N-acetylglucosamine-L-rhamnose disaccharide, which connects the galactan region of arabinogalactan to peptidoglycan via a phosphodiester linkage.
Interaction partners:
- dTDP-4-dehydrorhamnose 3,5-epimerase
- Glucose-1-phosphate thymidylyltransferase
- dTDP-4-dehydrorhamnose reductase
- Possible dTDP-glucose 4,6-dehydratase
- N-acetylglucosaminyl-diphospho-decaprenol L-rhamnosyltransferase
- UDP-galactopyranose mutase
- Decaprenyl-phosphate N-acetylglucosaminephosphotransferase
- Possible dTDP-glucose 4,6-dehydratase
- Probable UDP-glucose 4-epimerase GalE3
- UDP-glucose 6-dehydrogenase
Sequence:
MRLLVTGGAGFIGTNFVHSAVREHPDDAVTVLDALTYAGRRESLADVEDAIRLVQGDITDAELVSQLVAESDAVVHFAAESHVDNALDNPEPFLHTNVIGTFTILEAVRRHGVRLHHISTDEVYGDLELDDRARFTESTPYNPSSPYSATKAGADMLVRAWVRSYGVRATISNCSNNYGPYQHVEKFIPRQITNVLTGRRPKLYGAGANVRDWIHVDDHNSAVRRILDRGRIGRTYLISSEGERDNLTVLRTLLRLMDRDPDDFDHVTDRVGHDLRYAIDPSTLYDELCWAPKHTDFEEGLRTTIDWYRDNESWWRPLKDATEARYQERGQ
Protein: Uncharacterized protein (Q4GY98)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MRSREVYSGSQPIEEYHSPSSPSISSSGDPCREPISPLGDRTLIMALDGMLHASRKDGGFEGVLRYDDLRQLLARLGLTWETDRIDDCWYDIVRGHAAPVADDMSWVRHCVCEHLYGECAGISTTELLSEQQTLSPRDEFCNLAELNAISAWRTPAKEKRDRTQAVAPSKFTLRAKTVVKGGAGLEGTSPKREAQPQRQRSPPRSATSPQLLFDEAVCGRGISPRQGICFTSPTMSSMRRGRATAVMSRHRSGLSTDSFPRRRSPSPSSHGDVFHRLTEDAHSRRNRQLAVAAAAVEAQSAAQTGGTVSTSPARSRRPSPGGRGMWERPTKSYQAKFSGEPPPFDPLESQPATPPVTRHKPPGPSSFVPTGYVEAVARLRKYASSRPHYQDFMSSLRSEPVTSHVVDDTPILRLPVRGGARQFSGKVVDVRLATPTRSRSNDVLRDVPYDDPSRVIYQNMLRGRRCA
Protein: Caspase-2 (CASP-2) (EC 3.4.22.55) (Neural precursor cell expressed developmentally down-regulated protein 2) (NEDD-2) (Protease ICH-1) [Cleaved into: Caspase-2 subunit p18; Caspase-2 subunit p13; Caspase-2 subunit p12] (P29594)
Organism: Mus musculus (Mouse)
Function: Involved in the activation cascade of caspases responsible for apoptosis execution. Might function by either activating some proteins required for cell death or inactivating proteins necessary for cell survival. Associates with PIDD1 and CRADD to form the PIDDosome, a complex that activates CASP2 and triggers apoptosis in response to genotoxic stress (By similarity).
Interaction partners:
- Death domain-containing protein CRADD
- p53-induced death domain-containing protein 1
- BH3-interacting domain death agonist
- Apoptotic protease-activating factor 1
- Caspase-9
- Caspase-8
- Caspase-3
- Caspase-7
- Caspase-1
- Cytochrome c, somatic
Sequence:
MAAPSGRSQSSLHRKGLMAADRRSRILAVCGMHPDHQETLKKNRVVLAKQLLLSELLEHLLEKDIITLEMRELIQAKGGSFSQNVELLNLLPKRGPQAFDAFCEALRETRQGHLEDLLLTTLSDIQHVLPPLSCDYDTSLPFSVCESCPPHKQLRLSTDATEHSLDNGDGPPCLLVKPCTPEFYQAHYQLAYRLQSQPRGLALVLSNVHFTGEKDLEFRSGGDVDHTTLVTLFKLLGYNVHVLHDQTAQEMQEKLQNFAQLPAHRVTDSCVVALLSHGVEGGIYGVDGKLLQLQEVFRLFDNANCPSLQNKPKMFFIQACRGDETDRGVDQQDGKNHTQSPGCEESDAGKEELMKMRLPTRSDMICGYACLKGNAAMRNTKRGSWYIEALTQVFSERACDMHVADMLVKVNALIKEREGYAPGTEFHRCKEMSEYCSTLCQQLYLFPGYPPT
Protein: RE12054p (Q8MS42)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MSENTYQIETRRRSRSKTPFLRSSCDHENCEHAGEEGHVHHLKRKSAAPNVQTIIEEHIVESSISKKTRAKAFAQLTSDYSSDDMTPDAKRKQNSITATVTSILTKRSGGATSTPRNRSQLETTQNTLNSAQEKLNQSNGNLSSGNVSDYLAYIEYRDAGEYWNKTPKTDYTYSELSPHRRQLAPGIVAMPNMSRKSLENHNDRVNYMVQQNPAQEEFIRRRYQSKYTQQVNYDSADELDATFGQQKQSWWLIRLIQLVVSSITTVWSRVTNLSATETTAYQNYHAKRQQSQQVGLWWKIVQTIGGGLASLLRYLYVFIGSVLSLDTWLLRSSDAENKSKKRFLIFLLILLPLLLLSGLFYYIHPNETFPPKSLSEYTFTLPELPKIDVKDYLNQGAVRIATLSGRRACGPRSRLGRRLRFVLENHRSERGQQGSSVISGR
Protein: DNA-directed RNA polymerase III subunit RPC7 (RNA polymerase III subunit C7) (DNA-directed RNA polymerase III 31 kDa polypeptide) (C31) (P17890)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. Specific peripheric component of RNA polymerase III which synthesizes small RNAs, such as 5S rRNA and tRNAs. C31 is involved in the formation of the initiation complex.
Subcellular location: Nucleus.
Interaction partners:
- DNA-directed RNA polymerase III subunit RPC3
- DNA-directed RNA polymerase III subunit RPC4
- DNA-directed RNA polymerase III subunit RPC2
- DNA-directed RNA polymerase III subunit RPC1
- DNA-directed RNA polymerase III subunit RPC10
- DNA-directed RNA polymerase III subunit RPC5
- DNA-directed RNA polymerase III subunit RPC9
- DNA-directed RNA polymerases I and III subunit RPAC2
- DNA-directed RNA polymerases I, II, and III subunit RPABC2
- DNA-directed RNA polymerase III subunit RPC8
Sequence:
MSSYRGGSRGGGSNYMSNLPFGLGYGDVGKNHITEFPSIPLPINGPITNKERSLAVKYINFGKTVKDGPFYTGSMSLIIDQQENSKSGKRKPNIILDEDDTNDGIERYSDKYLKKRKIGISIDDHPYNLNLFPNELYNVMGINKKKLLAISKFNNADDVFTGTGLQDENIGLSMLAKLKELAEDVDDASTGDGAAKGSKTGEGEDDDLADDDFEEDEDEEDDDDYNAEKYFNNGDDDDYGDEEDPNEEAAF
Protein: Envelope small membrane protein (E protein) (sM protein) (Q89894)
Organism: Avian infectious bronchitis virus (strain Beaudette) (IBV)
Function: Plays a central role in virus morphogenesis and assembly. Acts as a viroporin and self-assembles in host membranes forming pentameric protein-lipid pores that allow ion transport. Also plays a role in the induction of apoptosis.
Subcellular location: Host Golgi apparatus membrane {ECO:0000255|HAMAP-Rule:MF_04206}; Single-pass type III membrane protein {ECO:0000255|HAMAP-Rule:MF_04206}. Note=The cytoplasmic tail functions as a Golgi complex-targeting signal. {ECO:0000255|HAMAP-Rule:MF_04206}.
Interaction partners:
Sequence:
MNLLNKSLEENGSFLTALYIIVGFLALYLLGRALQAFVQAADACCLFWYTWVVIPGAKGTAFVYKYTYGRKLNNPELEAVIVNEFPKNGWNNKNPANFQDAQRDKLYS
Protein: E3 ubiquitin-protein ligase ipaH7.8 (EC 2.3.2.27) (Invasion plasmid antigen 7.8) (P18014)
Organism: Shigella flexneri
Function: E3 ubiquitin ligase effector protein that interferes with host's innate immunity. Functions to alter host cell physiology and promote bacterial survival in host tissues. Catalyzes ubiquitination of host gasdermins GSDMB and GSDMD, promoting their degradation by the proteasome, thereby preventing cell death. In contrast, activates host cell pyroptosis in mouse cells: catalyzes ubiquitination of mouse Nlrp1b allele 1 protein, releasing the cleaved C-terminal part of Nlrp1b, which polymerizes and forms the Nlrp1b inflammasome followed by host cell pyroptosis.
Subcellular location: Secreted {ECO:0000250|UniProtKB:D0ZVG2}. Host cytoplasm {ECO:0000250|UniProtKB:D0ZVG2}. Note=Secreted via Mxi-Spa type III secretion system (T3SS), and delivered into the host cytoplasm. {ECO:0000250|UniProtKB:D0ZVG2}.
Interaction partners:
Sequence:
MFSVNNTHSSVSCSPSINSNSTSNEHYLRILTEWEKNSSPGEERGIAFNRLSQCFQNQEAVLNLSDLNLTSLPELPKHISALIVENNKLTSLPKLPAFLKELNADNNRLSVIPELPESLTTLSVRSNQLENLPVLPNHLTSLFVENNRLYNLPALPEKLKFLHVYYNRLTTLPDLPDKLEILCAQRNNLVTFPQFSDRNNIRQKEYYFHFNQITTLPESFSQLDSSYRINISGNPLSTRVLQSLQRLTSSPDYHGPQIYFSMSDGQQNTLHRPLADAVTAWFPENKQSDVSQIWHAFEHEEHANTFSAFLDRLSDTVSARNTSGFREQVAAWLEKLSASAELRQQSFAVAADATESCEDRVALTWNNLRKTLLVHQASEGLFDNDTGALLSLGREMFRLEILEDIARDKVRTLHFVDEIEVYLAFQTMLAEKLQLSTAVKEMRFYGVSGVTANDLRTAEAMVRSREENEFTDWFSLWGPWHAVLKRTEADRWAQAEEQKYEMLENEYSQRVADRLKASGLSGDADAEREAGAQVMRETEQQIYRQLTDEVLALRLSENGSRLHHS
Protein: Adenylate cyclase-activating polypeptide 1a (pituitary) receptor type I (Pituitary adenylate cyclase-activating polypeptide type I receptor) (E7FF76)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004651}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}.
Interaction partners:
- Adcyap1a protein
- Adcyap1b protein
- VIP peptides
- Vasoactive intestinal peptide b.
- Adenylate cyclase-activating polypeptide 1a
- Somatoliberin
- Corticotropin-releasing hormone a.
- Corticotropin-releasing hormone b.
- Glucagon b
Sequence:
MASTVRKCQHLFLALILLPMIYCMHPDCVIQLEKEKCIERMFLDDPNSEPELVCRWMWDNLTCWQPARLGQVVWMPCPELFEVMNDENNEFGKVSRNCTEYGWSEMVPHYVDVCPFNENGTNPDMYYVSVKALYTVGYSTSLVSLTTAMVILCKFRKLHCTRNFIHMNLFVSFILRAISVFIKDGILYAEEDSNHCFIHTVECKAVMVFFHYCVLSNYFWLFIEGLYLFTLLVETFFPEKRYFYWYTIIGWGTPTICVTIWAVLRAHFDNIGCWDINDNATIWWVIKGPVLASIMINFILFIGIIIILVQKLQSPDIGGNESSIYLRLARSTLLLIPLFGIHYTVFAFTPEDVSKRERLVFELGLGSFQGFVVAVLYCFLNGEVQSEIKRKWRSWTVNRYFAVDMKHRHPSLASSGVNGGTQLSILSKSSSQIRMSSLQAETPAT
Protein: Delta-type opioid receptor (D-OR-1) (DOR-1) (Opioid receptor A) (P33533)
Organism: Rattus norvegicus (Rat)
Function: G-protein coupled receptor that functions as receptor for endogenous enkephalins and for a subset of other opioids. Ligand binding causes a conformation change that triggers signaling via guanine nucleotide-binding proteins (G proteins) and modulates the activity of down-stream effectors, such as adenylate cyclase. Signaling leads to the inhibition of adenylate cyclase activity. Inhibits neurotransmitter release by reducing calcium ion currents and increasing potassium ion conductance. Plays a role in the perception of pain and in opiate-mediated analgesia. Plays a role in developing analgesic tolerance to morphine.
Subcellular location: Cell membrane {ECO:0000269|PubMed:7519274, ECO:0000269|PubMed:8394245}; Multi-pass membrane protein {ECO:0000269|PubMed:7519274, ECO:0000269|PubMed:8394245}.
Interaction partners:
- Proenkephalin-A
- Pro-opiomelanocortin
- Proenkephalin-B
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein G
- Kininogen-1
Sequence:
MEPVPSARAELQFSLLANVSDTFPSAFPSASANASGSPGARSASSLALAIAITALYSAVCAVGLLGNVLVMFGIVRYTKLKTATNIYIFNLALADALATSTLPFQSAKYLMETWPFGELLCKAVLSIDYYNMFTSIFTLTMMSVDRYIAVCHPVKALDFRTPAKAKLINICIWVLASGVGVPIMVMAVTQPRDGAVVCTLQFPSPSWYWDTVTKICVFLFAFVVPILIITVCYGLMLLRLRSVRLLSGSKEKDRSLRRITRMVLVVVGAFVVCWAPIHIFVIVWTLVDINRRDPLVVAALHLCIALGYANSSLNPVLYAFLDENFKRCFRQLCRAPCGGQEPGSLRRPRQATARERVTACTPSDGPGGGAAA
Protein: GH09250p (Q95TE7)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MLGVDEEFDVKRLEELAESLLADITADLETGAGASSPAAAQDAGNAERLPGPMVGPAAERLESDGHRANGLNVEQEQETEHKVSLNVQMLKINGNPQHTTAAPASRTATITATAAASQLQATPDTVYGTYDAKTNSITIVMDGDAVPVNEAVEEIYCDGVSAGDDSTDVIMKCPPPATSPSQVYLNVMNAVDNSDDEESFDPIDRFLRPRVKAISPLAKSPALSLHSATSDHGYESILGSPTSVALTLPADEDDFPWESNFDELFPSLI
Protein: ECXA (Q8GAV4)
Organism: Escherichia coli
Interaction partners:
Sequence:
MKYNVTMLIVFISFIPATTQAERTPNEEKKVIGYADHNGQLYNITSIYGPVINYTVPDENITINTINSTGERTQLTINYSDYVREAFNEWAPSGIRVQQVSSSGAEARVVSFSTTNYADNSLGSTIFDPSGNSRTRIDIGSFNRIVMNNFEKLKSRGAIPANMSPEEYIKLKLRITIKHEIGHILGLLHNNEGGSYFPHGVGLEVARCRLLNQAPSIMLNGSNYDYIDRLSHYLERPVTETDIGPSRNDIEGVRVMRRGGSGNSFTNRFSCLGLGLAFSRSGGDL
Protein: Forkhead box protein D2 (Forkhead-related protein FKHL17) (Forkhead-related transcription factor 9) (FREAC-9) (O60548)
Organism: Homo sapiens (Human)
Function: Probable transcription factor involved in embryogenesis and somatogenesis.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00089}.
Interaction partners:
Sequence:
MTLGSCCCEIMSSESSPAALSEADADIDVVGGGSGGGELPARSGPRAPRDVLPHGHEPPAEEAEADLAEDEEESGGCSDGEPRALASRGAAAAAGSPGPGAAAARGAAGPGPGPPSGGAATRSPLVKPPYSYIALITMAILQSPKKRLTLSEICEFISGRFPYYREKFPAWQNSIRHNLSLNDCFVKIPREPGNPGKGNYWTLDPESADMFDNGSFLRRRKRFKRQPLPPPHPHPHPHPELLLRGGAAAAGDPGAFLPGFAAYGAYGYGYGLALPAYGAPPPGPAPHPHPHPHAFAFAAAAAAAPCQLSVPPGRAAAPPPGPPTASVFAGAGSAPAPAPASGSGPGPGPAGLPAFLGAELGCAKAFYAASLSPPAAGTAAGLPTALLRQGLKTDAGGGAGGGGAGAGQRPSFSIDHIMGHGGGGAAPPGAGEGSPGPPFAAAAGPGGQAQVLAMLTAPALAPVAGHIRLSHPGDALLSSGSRFASKVAGLSGCHF
Protein: Probable 2' cyclic ADP-D-ribose synthase TcpB (2'cADPR synthase TcpB) (EC 3.2.2.-) (Brucella TIR-containing protein 1) (Btp1) (NAD(+) hydrolase TcpB) (EC 3.2.2.6) (TIR domain-containing protein in Brucella) (TcpB) (C0RGW8)
Organism: Brucella melitensis biotype 2 (strain ATCC 23457)
Function: Virulence factor that interferes with host Toll-like receptor 2 (TLR2) and TLR4 signaling, resulting in the reduction of dendritic cell maturation, inhibition of pro-inflammatory cytokine secretion and impaired NF-kappa-B activation in macrophages. Acts as a NAD(+) hydrolase (NADase) by catalyzing cleavage of NAD(+) into ADP-D-ribose (ADPR) and nicotinamide. In addition to ADPR, also generates a cyclization variant of cyclic ADPR (cADPR), termed v-cADPR, for which the cyclizing bond is unknown.
Subcellular location: Secreted {ECO:0000250|UniProtKB:Q8YF53}. Host cell membrane {ECO:0000250|UniProtKB:Q8YF53}. Note=Translocated into the host cell via the type IV secretion system (T4SS). {ECO:0000305}.
Interaction partners:
Sequence:
MSSYSSNIDRLQREIARLKADDSREMSKEKQAQSKAHKAQQAISSAKSLSTQKSKMSELERATRDGAAIGKKRADIAKKIADKAKQLSSYQAKQFKADEQAVKKVAQEQKRLSDERTKHEAFIKQSLSSMRTTASATMEAEEEYDFFISHASEDKEAFVQDLVAALRDLGAKIFYDAYTLKVGDSLRRKIDQGLANSKFGIVVLSEHFFSKQWPARELDGLTAMEIGGQTRILPIWHKVSYDEVRRFSPSLADKVALNTSLKSVEEIAKELHSLI
Protein: DNA replication licensing factor MCM3 (EC 3.6.4.12) (J3KQ69)
Organism: Homo sapiens (Human)
Subcellular location: Chromosome {ECO:0000256|ARBA:ARBA00004286}. Nucleus {ECO:0000256|ARBA:ARBA00004123, ECO:0000256|RuleBase:RU368061}.
Interaction partners:
Sequence:
MWSCGRLREITWTSWTTRLLNNAFEELVAFQRALKDFVASIDATYAKQYEEFYVGLEGSFGSKHVSPRTLTSCFLSCVVCVEGIVTKCSLVRPKVVRSVHYCPATKKTIERRYSDLTTLVAFPSSSVYPTKDEENNPLETEYGLSVYKDHQTITIQEMPEKAPAGQLPRSVDVILDDDLVDKAKPGDRVQVVGTYRCLPGKKGGYTSGTFRTVLIACNVKQMSKDAQPSFSAEDIAKIKKFSKTRSKDIFDQLAKSLAPSIHGHDYVKKAILCLLLGGVERDLENGSHIRGDINILLIGDPSVAKSQLLRYVLCTAPRAIPTTGRGSSGVGLTAAVTTDQETGERRLEAGAMVLADRGVVCIDEFDKMSDMDRTAIHEVMEQGRVTIAKAGIHARLNARCSVLAAANPVYGRYDQYKTPMENIGLQDSLLSRFDLLFIMLDQMDPEQDREISDHVLRMHRYRAPGEQDGDAMPLGSAVDILATDDPNFSQEDQQDTQIYEKHDNLLHGTKKKKEKMVSAAFMKKYIHVAKIIKPVLTQESATYIAEEYSRLRSQDSMSSDTARTSPVTARTLETLIRLATAHAKARMSKTVDLQDAEEAVELVQYAYFKKVLEKEKKRKKRSEDESETEDEEEKSQEDQEQKRKRRKTRQPDAKDGDSYDPYDFSDTEEEMPQVHTPKTADSQETKESQKVELSESRLKAFKVALLDVFREAHAQSIGMNRLTESINRDSEEPFSSVEIQAALSKMQDDNQVMVSEGIIFLI
Protein: SWI/SNF complex subunit SWI3A homolog (OsSWI3A) (Transcription regulatory protein SWI3A homolog) (Q0JCC3)
Organism: Oryza sativa subsp. japonica (Rice)
Function: Component of a multiprotein complex equivalent of the SWI/SNF complex, an ATP-dependent chromatin-remodeling complex, which is required for the positive and negative regulation of gene expression of a large number of genes. It changes chromatin structure by altering DNA-histone contacts within a nucleosome, leading eventually to a change in nucleosome position, thus facilitating or repressing binding of gene-specific transcription factors.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00624, ECO:0000269|PubMed:32808364}.
Interaction partners:
- Os02g0723700 protein
- Actin-related protein 4
- Os04g0382100 protein
- Os07g0609766 protein.
- Expressed protein
- Os06g0255200 protein
- Os01g0884500 protein.
- Histone H4
- Histone H4
- ARID transcription factor
Sequence:
MSPPVAGAASSGDGPPGRPPRELYTIPASSGWFQWDEIHETERRALPEFFGGAGGSGFGTASRNPRIYREYRDYIISRYREDTSRRLTFTEVRKALVGDVTLLRKLFAFLDSSGLINFSASPSRPEAQQQQRQTEAEAVVEAPVGLQVTPRPPPSYFAEEKGGGGNENGFRLPPLTSYSDVFGEWAPGMAPICGLCGMECRDGNAQILKDGFKVCSKCYANNDNKGEANIHPGDKKERIDNHSSSAWTDAETLLLLEGVLKHGDDWDLIAQHVRTKNKSECIARLIQLPFGEHMLGTVNGKLDNRLHKIQTTDGKVNKSTVKESSSQPTETVDDMQIDGNEDGADKSVEEHPTKHRRLFSSIDITVSLMEQLAHLTTSTSPDVVAAAADAAIKALGNENPQARRAFQLSEKEYQTRAFSSNHARQSDDVGGGDRDVEMHGHPDKKQGKMFISTTYQVRAAVATSIGVAAARAKMLADQEEREMELLMASIIETQLKKIQYKIKHFEELELIMDQEYATLQQMKSSLVDEWQKVLKRAFETGVPISRDEVLIKLFQNKPNL
Protein: Kynureninase (EC 3.7.1.3) (L-kynurenine hydrolase) (Q9CXF0)
Organism: Mus musculus (Mouse)
Function: Catalyzes the cleavage of L-kynurenine (L-Kyn) and L-3-hydroxykynurenine (L-3OHKyn) into anthranilic acid (AA) and 3-hydroxyanthranilic acid (3-OHAA), respectively. Has a preference for the L-3-hydroxy form. Also has cysteine-conjugate-beta-lyase activity.
Subcellular location: Cytoplasm, cytosol {ECO:0000255|HAMAP-Rule:MF_03017}.
Interaction partners:
- Kynurenine 3-monooxygenase
- Tryptophan 2,3-dioxygenase
- 3-hydroxyanthranilate 3,4-dioxygenase
- Indoleamine 2,3-dioxygenase 1
- Indoleamine 2,3-dioxygenase 2
- Kynurenine/alpha-aminoadipate aminotransferase, mitochondrial
- Kynurenine formamidase
- Kynurenine--oxoglutarate transaminase 1
- Kynurenine--oxoglutarate transaminase 3
- Nicotinate-nucleotide pyrophosphorylase [carboxylating]
Sequence:
MEPSPLELPVDAVRRIAAELNCDPTDERVALRLDEEDKLSHFRNCFYIPKMRDLPSIDLSLVSEDDDAIYFLGNSLGLQPKMVRTYLEEELDKWAKMGAYGHDVGKRPWIVGDESIVSLMKDIVGAHEKEIALMNALTINLHLLLLSFFKPTPKRHKILLEAKAFPSDHYAIESQIQLHGLDVEKSMRMVKPREGEETLRMEDILEVIEEEGDSIAVILFSGLHFYTGQLFNIPAITKAGHAKGCFVGFDLAHAVGNVELRLHDWGVDFACWCSYKYLNSGAGGLAGAFVHEKHAHTVKPALVGWFGHDLSTRFNMDNKLQLIPGANGFRISNPPILLVCSLHASLEVFQQATMTALRRKSILLTGYLEYMLKHYHSKDNTENKGPIVNIITPSRAEERGCQLTLTFSIPKKSVFKELEKRGVVCDKREPDGIRVAPVPLYNSFHDVYKFIRLLTSILDSSERS