wanglab/gogpt-training-data huggingface dataset:
Protein: Cell division inhibitor SidA (SOS-induced inhibitor of cell division A) (B8GWS7)
Organism: Caulobacter vibrioides (strain NA1000 / CB15N) (Caulobacter crescentus)
Function: Inhibits cell division by binding directly to FtsW to prevent the final constriction of the FtsZ ring.
Subcellular location: Cell inner membrane {ECO:0000269|PubMed:21685367}; Single-pass membrane protein {ECO:0000269|PubMed:21685367}.
Interaction partners:
Sequence:
MIRVARESFALVSVIGFVWMMCTVANLVA
Protein: Carbohydrate sulfotransferase 13 (EC 2.8.2.5) (Chondroitin 4-O-sulfotransferase 3) (Chondroitin 4-sulfotransferase 3) (C4ST-3) (C4ST3) (Q8NET6)
Organism: Homo sapiens (Human)
Function: Catalyzes the transfer of sulfate to position 4 of the N-acetylgalactosamine (GalNAc) residue of chondroitin. Chondroitin sulfate constitutes the predominant proteoglycan present in cartilage and is distributed on the surfaces of many cells and extracellular matrices. Transfers sulfate to the C4 hydroxyl of beta1,4-linked GalNAc that is substituted with a beta-linked glucuronic acid at the C-3 hydroxyl. No activity toward dermatan.
Subcellular location: Golgi apparatus membrane {ECO:0000250}; Single-pass type II membrane protein {ECO:0000250}.
Interaction partners:
- Carbohydrate sulfotransferase 12
- Carbohydrate sulfotransferase 11
- Carbohydrate sulfotransferase 7
- Carbohydrate sulfotransferase 15
- Carbohydrate sulfotransferase 3
Sequence:
MGRRCCRRRVLAAACLGAALLLLCAAPRSLRPAFGNRALGSSWLGGEKRSPLQKLYDLDQDPRSTLAKVHRQRRDLLNSACSRHSRRQRLLQPEDLRHVLVDDAHGLLYCYVPKVACTNWKRVLLALSGQARGDPRAISAQEAHAPGRLPSLADFSPAEINRRLRAYLAFLFVREPFERLASAYRNKLARPYSAAFQRRYGARIVQRLRPRALPDARARGHDVRFAEFLAYLLDPRTRREEPFNEHWERAHALCHPCRLRYDVVGKFETLAEDAAFVLGLAGASDLSFPGPPRPRGAAASRDLAARLFRDISPFYQRRLFDLYKMDFLLFNYSAPSYLRLL
Protein: Anion-transporting ATPase-like domain-containing protein (O69648)
Organism: Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh)
Interaction partners:
Sequence:
MSVTPKTLDMGAILADTSNRVVVCCGAGGVGKTTTAAALALRAAEYGRTVVVLTIDPAKRLAQALGINDLGNTPQRVPLAPEVPGELHAMMLDMRRTFDEMVMQYSGPERAQSILDNQFYQTVATSLAGTQEYMAMEKLGQLLSQDRWDLIVVDTPPSRNALDFLDAPKRLGSFMDSRLWRLLLAPGRGIGRLITGVMGLAMKALSTVLGSQMLADAAAFVQSLDATFGGFREKADRTYALLKRRGTQFVVVSAAEPDALREASFFVDRLSQESMPLAGLVFNRTHPMLCALPIERAIDAAETLDAETTDSDATSLAAAVLRIHAERGQTAKREIRLLSRFTGANPTVPVVGVPSLPFDVSDLEALRALADQLTTVGNDAGRAAGR
Protein: Arginine-glutamic acid dipeptide repeat protein (At2g47820) (Q8GZA1)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- Solute carrier family 35 protein
- UDP-N-acetylglucosamine/UDP-glucose/GDP-mannose transporter
- UDP-N-acetylglucosamine transporter UGNT1
- UDP-galactose/UDP-glucose transporter 7
- ADP-ribosylation factor
- Kinetochore protein NDC80 homolog
- OVARIAN TUMOR DOMAIN-containing deubiquitinating enzyme 11
- OVARIAN TUMOR DOMAIN-containing deubiquitinating enzyme 10
- OVARIAN TUMOR DOMAIN-containing deubiquitinating enzyme 4
- OVARIAN TUMOR DOMAIN-containing deubiquitinating enzyme 9
Sequence:
MEPIHSDDMEEAFVDESSMLLNSPYLNGIHGDPDVLPRVGDQYQADLPVLLTESDRLKLITCFHSEPPLQKLLTFGLPIPLMWTRSEKFRGFREADIDKASPPVDDQSLQNAACMKPRSIVLALPCQKNAKFKFDWLDKTLYPFPGTLGQPWEDAEQERFLLGLYCLGKNLVLVQRFVGSKHMGDMLSYYYGSFYRSTEYRRWVDGRKSRSRRSVQGQKLLSGWRQQELLSRISSHVSEECKITLLKVSKAFREDKIALEDYVFTLKNTVGIDMLTQVIGIGKGKRDLTNCALEPTKLNHGASGNSQVRIRNDLPIADIVKFLTGEYRMSKTRSSDLFWEAVWPRLLARGWHSEQPKDGPKNSLVFLVPEANKFSRRKMSKGNHYFDSLTDVLNKVALDPTLLELDEDLERKGSKEEVIKNDPPTNLEEFDDSSPNSKKKKKYLQPRSKTRKIQEVMLFTIIDTSETNSIEGCTLKELRSLPVGTGSSIANSSSYLSESEDNMSEESENKAETTAKSMASRVCGGGSISSGKSSSVNMDNATSPSTISLNERQQKNRKGGRPRNPKLLPVCTKRSSLADCTLREAGCFGETQSRKKKPLKKGKHMRPNPLKADLNVVLTREERINEDKTLKLSSTSSFARDSSCRRNIDREISPERSESREDFDLNVSQISLEREADGTDTVMADVVQNSESSCAEQSSVQVDVEKQCKPQELQVTADLLPERRQSTRTRPLTTKALEAFAFGYLGNSNKERKASEESRTKSNKKRKASEESRTKSTKRIHRHLPVSSKFRNGTVEDGSNTDETE
Protein: Mitogen-activated protein kinase HOG1 (MAP kinase HOG1) (EC 2.7.11.24) (Q6FIU2)
Organism: Candida glabrata (strain ATCC 2001 / BCRC 20586 / JCM 3761 / NBRC 0622 / NRRL Y-65 / CBS 138) (Yeast) (Nakaseomyces glabratus)
Function: Mitogen-activated protein kinase involved in a signal transduction pathway that is activated by changes in the osmolarity of the extracellular environment. Controls osmotic regulation of transcription of target genes (By similarity).
Subcellular location: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
Interaction partners:
- Candida glabrata strain CBS138 chromosome J complete sequence
- Transcription factor
- mitogen-activated protein kinase kinase
- Candida glabrata strain CBS138 chromosome C complete sequence
- protein-tyrosine-phosphatase
- High-osmolarity-induced transcription protein 1
- Candida glabrata strain CBS138 chromosome L complete sequence
- Candida glabrata strain CBS138 chromosome F complete sequence
- Candida glabrata strain CBS138 chromosome M complete sequence
- High osmolarity signaling protein SHO1
Sequence:
MATNEEFIRTQIFGTVFEITNRYSDLNPVGMGAFGLVCSATDTLTNQQVAIKKIMKPFATAVLAKRTYRELKLLKHLRHENLICLQDIFLSPLEDIYFVTELQGTDLHRLLQTRPLEKQFVQYFHYQILRGLKYVHSAGVVHRDLKPSNILINENCDLKICDFGLARIQDPQMTGYVSTRYYRAPEIMLTWQKYDVEVDIWSAGCIFAEMIEGKPLFPGKDHVHQFSIITDLLGSPPSDVIDTICSENTLKFVTSLPHRDPIPFSERFKTVEPDAVDLLEKMLVFDPKKRITAADALAHPYLAPYHDPTDEPVAEAKFDWHFNDADLPVDTWRVMMYSEILDFHKIGGTDGQIDTSATFDDQVAAATVAAAQAQAHALAQAQMSQNMIDPNQLLNEDGTPVSGSIAENSSNSATTNLNGAAAGMNSASDTINEYANQAVHFANEFQQ
Protein: RAS protein activator like 2 (E9PW37)
Organism: Mus musculus (Mouse)
Interaction partners:
- GTPase HRas
- GTPase KRas
- GTPase NRas
- Ras-related protein M-Ras
- Ras-related protein R-Ras2
- Ras-related protein R-Ras
- Ras GTPase-activating protein 3
Sequence:
MELSPSSGGAAEALSWPEMFTGLESDSPLPPEDLDAVVPVSGAVAGGMLDRILLESVCQQQSWVRVFDVKGPPTHRLSCGQSPYTETTSWERKYCILTDSQLVLLNKEKEMPVEGQDQQTDSTKGRCLRRTVSVPSEGQFPEYPQEGTTKLEVPAERSPRRRSISGTSTSEKPNSMDTANTSPFKVPGFFSKRLKGSIKRTKSQSKLDRNTSFRLPSLRNADDRSRGLPKLKESRSHESLLSPCSAVECLDLGRGEPVSVKPLHSSILGQDFCFEVTYLSGSKCFSCSSASERDKWMENLRRTVQPNKDNCRRAENVLRLWIIEAKDLAPKKKYFCELCLDDTLFARTTSKTKADNIFWGEHFEFYSLPPLHSITVHIYKDVEKKKKKDKNNYVGLVNIPTASVTGRQFVEKWYPVSTPTPNKGKTGGPSIRIKSRFQTITILPMEQYKEFAEFITSNYTMLCSVLEPVISVRNKEELACALVHILQSTGRAKDFLTDLVMSEVDRCGEHDVLIFRENTIATKSIEEYLKLVGQQYLHDALGEFIKALYESDENCEVDPSKCSSSELMDHQSNLKMCCELAFCKIINSYCVFPRELKEVFASWKQQCLNRGKQDISERLISASLFLRFLCPAIMSPSLFNLMQEYPDDRTSRTLTLIAKVIQNLANFAKFGNKEEYMAFMNDFLEHEWGGMKRFLLEISNPDTISNTPGFDGYIDLGRELSVLHSLLWEVVSQLDKGENSFLQATVAKLGPLPRVLADITKSLTNPTPIQQQLRRFAEHSSSPNVSGSLSSGLQRICEDPTDSDLHKLKSPSQDNTDSYFRGKTLLLVQQASSQSMTYSEKDEKENSLPNGRSISLMDLQDTHAAQAEHASVMLDVPMRLAGSQLSITQVASIKQLRETQSTPQSAPQVRRPLHPALNQPGSLQPLSFQNPVYHLNNPVPAMPKASADSSLENLSTASSRSQSNSEDFKLSGPSNSSMEDFTKRSSHSEDFSRRHTVPDRHIPLALPRQNSTGQSQIRKLDHSGLGARAKAPPSLPHSASLRSTGSMSVASAALMAEPVQNGSRSRQQSSSSRESPVPKVRAIQRQQTQQVQSPVDSATMSPVERTAAWVLNNGQYEEDVEETEQNQDEAKHAEKYEQEITKLKERLRVSSRRLEEYERRLLVQEQQMQKLLLEYKARLEDSEERLRRQQEEKDSQMKSIISRLMAVEEELKKDHAEMQAVIDAKQKIIDAQEKRIVSLDSANTRLMSALTQVKERYSMQVRNGISPTNPTKLSITENGEFKNSSC
Protein: Mannose/glucose-specific lectin (PpeL) (C0HLR9)
Organism: Parkia pendula (Inga pendula)
Function: D-mannose/D-glucose-binding lectin that also binds derivatives N-acetyl-D-glucosamine and alpha-methyl-D-mannopyranoside (Ref.1). Does not bind D-galactose, L-Rhamnose, D-fructose, lactose or glycoproteins fetiun and mucin (Ref.1). Shows agglutinating activity towards human and rabbit erythrocytes (Ref.1). Also displays antimicrobial activity against L.infantum (Ref.1).
Interaction partners:
Sequence:
QLKGMISVGPWGGQGGDHWSFKANHAITEILIHVKDNIKSISFKDASGDISGTFGGKDPRENEKGDEKKIGIHWPTEYLKSISGSYGDYNGLLVIRSLSFITNLTTYGSFGSTSGGESFSIPIADSVVVGFHGRGGYYLDALGVFVKPVPHGTISFGPWGGPAGDDAFNFKVGSWIKDIIIYSNGAIQSIAFKDGNGHCYGKFGGKDPNDIGVEKKVEIDGNLEHLTSISGTYGNYKGFEVVTSLSFITNVTKHGPFGTASGTSFSIPIEGSLVTGFHGKGGYYLDSIGIYVKPRDVEGSISIGPWGGSGGDPWSYTANEGINQIIIYAGSDIKSLAFKDTSGFDSATFGGVNPKDTGEKNTVSINWPSEYLTSISGTYGQYKFKDVFTTITSLSFTTNLATYGPFGKASGTSFSVPINNNTVLGFHGRAGDYLDAIGIFVKPDTAV
Protein: Mitoregulin (Micropeptide in mitochondria) (Micropeptide regulator of beta-oxidation) (Small integral membrane protein 37) (lncRNA-encoded micropeptide) (Q8BT35)
Organism: Mus musculus (Mouse)
Function: Positively regulates mitochondrial complex assembly and/or stability. Increases mitochondrial membrane potential while decreasing mitochondrial reactive oxygen species (By similarity). Increases mitochondrial respiration rate. Increased mitochondrial respiratory activity promotes myogenic differentiation which facilitates muscle growth and regeneration. Increases mitochondrial calcium retention capacity. Plays a role in maintenance of cellular lipid composition through its interaction with cytochrome b5 reductase CYB5R3 which is required for mitochondrial respiratory complex I activity. Interacts with the mitochondrial trifunctional enzyme complex (MTE) and enhances fatty acid beta-oxidation. Not required for MTE formation or stability. Modulates triglyceride clearance in adipocytes through its role in regulating fatty acid beta-oxidation and lipolysis.
Subcellular location: Mitochondrion inner membrane {ECO:0000269|PubMed:29949755, ECO:0000269|PubMed:29949756, ECO:0000269|PubMed:30796188, ECO:0000269|PubMed:31296841, ECO:0000269|PubMed:32393776}; Single-pass membrane protein {ECO:0000305}. Note=Preferentially binds to cardiolipin relative to other common cell membrane lipids. {ECO:0000269|PubMed:29949756}.
Interaction partners:
- Ncbp2 antisense 2
Sequence:
MADVSERTLQVSVLVAFASGVVLGWQANRLRRRYLDWRKRRLQDKLATTQKKLDLA
Protein: Sin3A, isoform H (A0A0B4LF82)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123, ECO:0000256|PROSITE-ProRule:PRU00810}.
Interaction partners:
Sequence:
MMKRTRVDEVQFGTRPVPQTSGGVGVGVVGVTGGGPTSGGGGTATVGVNTTGVTIGTVVPSAHNATISGIGSIHHRILTPQHGGAQTIAYLPSTTPTATNLKTTTSIVDSTTAGGPVGAGAQVAVGVGSAAGGGGVVVSTGSTGTQTLQYTTSYSVASIQAGGTLKANTADGANTVQIHVTGGGAANNPASAQTVSSSSQTGTIRQRTISGTQTVATAVGNLATISQQQPVQQSPLGKAQTPPSSVVANSIPVGGTTPPQGQSGNATPRLKVEDALSYLDQVKYQYADQPQIYNNFLDIMKEFKSHCIDTPGVIERVSTLFKGHTELIYGFNMFLPPGYKIEIHSDALGCSVPVVSMPSPPGAPTSTGTVHMLTGNSSMSGAGHIAIKTTNAATLTPAAGAGAAAAAAAVAQIQSAGAVNLMTHGGASLTQTTIHALQQATPPQSQSPGGGHVHVSVTNSTAANAVVPGQPGISVSAHNVPQNYSRDRERATITPTGQVAGAAANVNASASIVVGGPPTPNSLSELSPHGGAGGGPGAGAAQHNLHHIQQAHQSILLGETGQQNQPVEFNHAITYVNKIKNRFQNQPAKYKKFLEILHDYQREQKVMKEGSLNQGKMLTEQEVYTQVAKLFGQDEDLLREFGQFLPDATNHQSGQYMSKSASVHNDHGKRPTATLSGGAHITMSSASPAPSGSPLHLGATTLPQIDKSAHAAAIGNLSAVNTSVSIKTYNNNQQQQNHVIGSGLNATRNDILFEKDYHAGLQQQAHQRGAGVGGHHHLAGTAAGANIGRPGVGASVMVSYDKEHRNNHHVQKYVGHAPNQNLTHGHNAKKSPSYGIPSVIGSMPHISDNSLDRSSPGISYATPPLPSGPHGQHNSGSATRRPGDDSLVGHYASGAPPAKRPKPYCRDVSFSEASSKCTISDAAFFDKVRKALRSPEVYDNFLRCLTLFNQEIVSKTELLGLVSPFLMKFPDLLRWFTDFLGPPSGQPAGGLIDGMPLAATQRQGGGSSNSSHDRGTSHQSAAEYVQDVDLSSCKRLGASYCALPQSTVPKKCSGRTALCREVLNDKWVSFPTWASEDSTFVTSRKTQFEETIYRNIHRTEDERFELDLVIEVNSATIRVLENLQKKMSRMSTEELSKFHLDDHLGGTSQTIHQRAIHRIYGDKSGEIITGMKKNPFVAVPIVLKRLKVKEEEWREAQKTFNKQWREQNEKYYLKSLDHQAINFKPNDMKALRSKSLFNEIETLYDERHDQEDDAMEPFGPHLVLPYKDKTILDDAANLLIHHVKRQTGIQKQEKQKIKQIIRQFVPDLFFAPRQPLSDDERDDDDNTKMDVDSPLGRTESSTRNAKSTPSESASPARSNASTSSVTPAGIKKETDDSKATTGSFAPASSATASSATPVDDATPSTSSAAAAASAASSSTVSGTEGKPKDDPLSSHKEEGAGSTSSGVATSPRQAQDTAGAGVDVEIKLEHPADFSNPKLLPPHAHGQREDESYTLFFANNNWYLFLRLHAILCDRLHVMYERARLLAIEEERCRVNRRESTATALRLKPKPEIQVEDYYPTFLDMLKNVLDGNMDSNTFEDTMREMFGIYAYISFTLDKVVSNAVRQLQYCVTERAALDCVELFATEQRRGCTGGFCRDAHKTFDREMSYQRKAESILNEENCFKVYIYKIDCRVTIELLDSEPEEVDKPAALKAQKFSKYVERLANPALGGGGNTGRSDSALGNDSVVDGSDIKTEADEDTAELRYREGGIGGAGKARFLVRNKRRSKLLEEQVRQLFEHRRNRIEQHGTAASLEPISVDSAISSNSTTGGGGSGTNNNNNNNNNNNSWGGKRLERLGAPQVGLAEQYAFNDRDEISTNISNGRCFVTSKNLKLLKYDAVRRAKKSHCRVTQAKYAHFQTYVNKWLQQHVSEQQQQNCVDWLLGKTADQINASGWGSASKTKTVQQKDTSKTPYRIYNRYRVVQSAVSGGLMSATAPTPDGSVPAVNSAPSGSVSTVNNVQGSAAVSSTSHSMCNSSILSADSTTNTNASAQQQQHCNSAAAATTPNAEALQQVRPMES
Protein: Mediator of RNA polymerase II transcription subunit 4 (Mediator complex subunit 4) (Q12343)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Component of the Mediator complex, a coactivator involved in the regulated transcription of nearly all RNA polymerase II-dependent genes. Mediator functions as a bridge to convey information from gene-specific regulatory proteins to the basal RNA polymerase II transcription machinery. The Mediator complex, having a compact conformation in its free form, is recruited to promoters by direct interactions with regulatory proteins and serves for the assembly of a functional preinitiation complex with RNA polymerase II and the general transcription factors. The Mediator complex unfolds to an extended conformation and partially surrounds RNA polymerase II, specifically interacting with the unphosphorylated form of the C-terminal domain (CTD) of RNA polymerase II. The Mediator complex dissociates from the RNA polymerase II holoenzyme and stays at the promoter when transcriptional elongation begins.
Subcellular location: Nucleus {ECO:0000269|PubMed:14562095}.
Interaction partners:
- Mediator of RNA polymerase II transcription subunit 31
- Mediator of RNA polymerase II transcription subunit 14
- Mediator of RNA polymerase II transcription subunit 7
- Mediator of RNA polymerase II transcription subunit 10
- Mediator of RNA polymerase II transcription subunit 19
- Mediator of RNA polymerase II transcription subunit 9
- Mediator of RNA polymerase II transcription subunit 21
- Mediator of RNA polymerase II transcription subunit 17
- Mediator of RNA polymerase II transcription subunit 6
- Mediator of RNA polymerase II transcription subunit 18
Sequence:
MSVQDTKAVEFSMGHIRSSSVSLVAEATSNTNSEDKLSKVQLYEDLCRYEDTLSKLVESVDRFKPNLDIAKDLIRTDEALFENVKLLAEYDNIYRNLQKIDKDSEELDSKTRKILEILNECHDELKALPMLEQVEFEKNTILQQRSKINSTELLDYATKLSKFTKIPPTFDKGAVGPNNFIWPAEDALRRGMLAMASLHSKELTRIPGEEVEETEVPTVPPSQSEEQKGQMAKKEGTPKTDSFIFDGTAKEVGDEADNTKDKEKEENNDDALDLDLDLFDPDDF
Protein: Neuraminidase (EC 3.2.1.18) (Q0A456)
Organism: Influenza A virus (strain A/Turkey/Wisconsin/1/1966 H9N2)
Function: Catalyzes the removal of terminal sialic acid residues from viral and cellular glycoconjugates. Cleaves off the terminal sialic acids on the glycosylated HA during virus budding to facilitate virus release. Additionally helps virus spread through the circulation by further removing sialic acids from the cell surface. These cleavages prevent self-aggregation and ensure the efficient spread of the progeny virus from cell to cell. Otherwise, infection would be limited to one round of replication. Described as a receptor-destroying enzyme because it cleaves a terminal sialic acid from the cellular receptors. May facilitate viral invasion of the upper airways by cleaving the sialic acid moieties on the mucin of the airway epithelial cells. Likely to plays a role in the budding process through its association with lipid rafts during intracellular transport. May additionally display a raft-association independent effect on budding. Plays a role in the determination of host range restriction on replication and virulence. Sialidase activity in late endosome/lysosome traffic seems to enhance virus replication.
Subcellular location: Virion membrane {ECO:0000255|HAMAP-Rule:MF_04071}. Host apical cell membrane {ECO:0000255|HAMAP-Rule:MF_04071}; Single-pass type II membrane protein {ECO:0000255|HAMAP-Rule:MF_04071}. Note=Preferentially accumulates at the apical plasma membrane in infected polarized epithelial cells, which is the virus assembly site. Uses lipid rafts for cell surface transport and apical sorting. In the virion, forms a mushroom-shaped spike on the surface of the membrane. {ECO:0000255|HAMAP-Rule:MF_04071}.
Interaction partners:
Sequence:
MNPNQKIITIGSVSLTIATVCFLMQIAILATTVTLHFKQNECNPPANNQVVPCEPIIIERNITEIVYLNNITIEKEVCPEVAEYRNWSKPQCQITGFAPFSKDNSVRLSAGGDIWVTREPYVSCDPGKCYQFALGQGTTLDNKHSNGTIHDRIPHRTLLMNELGVPFHLGTKQVCIAWSSSSCHDGKAWLHVCVTGDDRNATASFIYDGMLVDSIGSWSQNILRTQESECVCINGTCTVVMTDGSASGNADTRVLFIREGKIIHISPLSGSAQHIEECSCYPRYPDVRCVCRDNWKGSNRPVIDIKMADYSINSGYVCSGLVGDTPRSDDSSSNSNCRDPNNERGNPGVKGWAFDNGDDVWMGRTISKDSRSGYETFRVIGGWTTPNSKSQVNRQVIVDSNNWSGYSGIFSVEGKSCINRCFYVELIRGRPQETRVWWTSNSIVVFCGTSGTYGTGSWPDGANINFMPI
Protein: ShKT domain-containing protein (Q22714)
Organism: Caenorhabditis elegans
Interaction partners:
- CUB-like domain-containing protein
- CUB-like domain-containing protein
- Mitogen-activated protein kinase pmk-1
- CUB-like domain-containing protein
- CUB-like domain-containing protein
- C-type lectin domain-containing protein
- Transcription factor atf-7
- CUB-like domain-containing protein
- CUB-like domain-containing protein
- CUB domain-containing protein
Sequence:
MRYLIGFVIVLVAYTASESCVDSRPSCPSLKNYCNEADVRSGCRKTCGVCVTDTPFVCEDKLGLCPNYVRQCHDENIAEQCPKTCQICGTTAQPMQKSA
Protein: Demilune cell-specific protein (Q60601)
Organism: Mus musculus (Mouse)
Interaction partners:
Sequence:
MFQLEAMLPLLILAFLGTPTVLTQDYHGPEVGKHSCTSAPEGKNITSIRVFLQGRSIVGIQFNYNNEDGQVYGSTAGKVMVARLNNEESIIAAEGTYSPSALTQIIFTTNQPRQLMVGYYVGSSEYSKIASLTIPAMCSRELVSLGGQVA
Protein: Dopamine receptor 1 (D-DOP1) (DmDop1) (dDA1) (Dopamine 1-like receptor 1) (P41596)
Organism: Drosophila melanogaster (Fruit fly)
Function: Receptor for dopamine. The activity of this receptor is mediated by G proteins which activate adenylyl cyclase. Might be involved in the processing of visual information and/or visual learning. Important for Pavlovian conditioning: required in the mushroom body as a receptor conveying unconditional stimuli information, has a role in memory formation for aversive and appetitive learning. Sleep-deprivation-induced impairments in learning can be partially explained through alterations in dopamine signaling, Dop1R1 expression levels are reduced; sleep may have a role in restoring dopamine homeostasis.
Subcellular location: Cell membrane; Multi-pass membrane protein.
Interaction partners:
- Dopamine D2-like receptor
- G protein alpha s subunit subunit alpha)
- Dopamine receptor 2
- Transient receptor potential cation channel subfamily A member 1
- Guanine nucleotide-binding protein subunit beta-1
- G protein beta subunit 5
- Dopamine/Ecdysteroid receptor, isoform A
Sequence:
MYTPHPFGFLIILVPMTNAMRAIAAIAAGVGSVAATVATSTTSSISSSTTIINTSSATTIGGNHTSGSTGFSTNSTLLDADHLPLQLTTAKVDLDIEIDIQLLTNGYDGTTLTSFYNESSWTNASEMDTIVGEEPEPLSLVSIVVVGIFLSVLIFLSVAGNILVCLAIYTERSLRRIGNLFLASLAIADLFVASLVMTFAGVNDLLGYWIFGAQFCDTWVAFDVMCSTASILNLCAISMDRYIHIKDPLRYGRWVTRRVAVITIAAIWLLAAFVSFVPISLGIHRPDQPLIFEDNGKKYPTCALDLTPTYAVVSSCISFYFPCVVMIGIYCRLYCYAQKHVKSIKAVTRPGEVAEKQRYKSIRRPKNQPKKFKVRNLHTHSSPYHVSDHKAAVTVGVIMGVFLICWVPFFCVNITAAFCKTCIGGQTFKILTWLGYSNSAFNPIIYSIFNKEFRDAFKRILTMRNPWCCAQDVGNIHPRNSDRFITDYAAKNVVVMNSGRSSAELEQVSAI
Protein: Protein ABHD8 (EC 3.-.-.-) (Alpha/beta hydrolase domain-containing protein 8) (Abhydrolase domain-containing protein 8) (Q96I13)
Organism: Homo sapiens (Human)
Interaction partners:
- Ankyrin repeat and LEM domain-containing protein 1
Sequence:
MLTGVTDGIFCCLLGTPPNAVGPLESVESSDGYTFVEVKPGRVLRVKHAGPAPAAAPPPPSSASSDAAQGDLSGLVRCQRRITVYRNGRLLVENLGRAPRADLLHGQNGSGEPPAALEVELADPAGSDGRLAPGSAGSGSGSGSGGRRRRARRPKRTIHIDCEKRITSCKGAQADVVLFFIHGVGGSLAIWKEQLDFFVRLGYEVVAPDLAGHGASSAPQVAAAYTFYALAEDMRAIFKRYAKKRNVLIGHSYGVSFCTFLAHEYPDLVHKVIMINGGGPTALEPSFCSIFNMPTCVLHCLSPCLAWSFLKAGFARQGAKEKQLLKEGNAFNVSSFVLRAMMSGQYWPEGDEVYHAELTVPVLLVHGMHDKFVPVEEDQRMAEILLLAFLKLIDEGSHMVMLECPETVNTLLHEFLLWEPEPSPKALPEPLPAPPEDKK
Protein: Disintegrin and metalloproteinase domain-containing protein 33 (ADAM 33) (EC 3.4.24.-) (Q9BZ11)
Organism: Homo sapiens (Human)
Subcellular location: Membrane; Single-pass type I membrane protein.
Interaction partners:
- PHD finger protein 11
- Inactive dipeptidyl peptidase 10
Sequence:
MGWRPRRARGTPLLLLLLLLLLWPVPGAGVLQGHIPGQPVTPHWVLDGQPWRTVSLEEPVSKPDMGLVALEAEGQELLLELEKNHRLLAPGYIETHYGPDGQPVVLAPNHTDHCHYQGRVRGFPDSWVVLCTCSGMSGLITLSRNASYYLRPWPPRGSKDFSTHEIFRMEQLLTWKGTCGHRDPGNKAGMTSLPGGPQSRGRREARRTRKYLELYIVADHTLFLTRHRNLNHTKQRLLEVANYVDQLLRTLDIQVALTGLEVWTERDRSRVTQDANATLWAFLQWRRGLWAQRPHDSAQLLTGRAFQGATVGLAPVEGMCRAESSGGVSTDHSELPIGAAATMAHEIGHSLGLSHDPDGCCVEAAAESGGCVMAAATGHPFPRVFSACSRRQLRAFFRKGGGACLSNAPDPGLPVPPALCGNGFVEAGEECDCGPGQECRDLCCFAHNCSLRPGAQCAHGDCCVRCLLKPAGALCRQAMGDCDLPEFCTGTSSHCPPDVYLLDGSPCARGSGYCWDGACPTLEQQCQQLWGPGSHPAPEACFQVVNSAGDAHGNCGQDSEGHFLPCAGRDALCGKLQCQGGKPSLLAPHMVPVDSTVHLDGQEVTCRGALALPSAQLDLLGLGLVEPGTQCGPRMVCQSRRCRKNAFQELQRCLTACHSHGVCNSNHNCHCAPGWAPPFCDKPGFGGSMDSGPVQAENHDTFLLAMLLSVLLPLLPGAGLAWCCYRLPGAHLQRCSWGCRRDPACSGPKDGPHRDHPLGGVHPMELGPTATGQPWPLDPENSHEPSSHPEKPLPAVSPDPQADQVQMPRSCLW
Protein: Lutropin-choriogonadotropic hormone receptor (LH/CG-R) (Luteinizing hormone receptor) (LSH-R) (cLH-R) (Q90674)
Organism: Gallus gallus (Chicken)
Function: Receptor for lutropin-choriogonadotropic hormone. The activity of this receptor is mediated by G proteins which activate adenylate cyclase.
Subcellular location: Cell membrane {ECO:0000269|PubMed:9545511}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
- Glycoprotein hormones alpha chain
- Steroidogenic acute regulatory protein, mitochondrial
- Steroid 17-alpha-hydroxylase/17,20 lyase
- Follitropin subunit beta
- Cholesterol side-chain cleavage enzyme, mitochondrial
- Aromatase
- Hydroxysteroid 17-beta dehydrogenase 3
Sequence:
MLPALLPLLLPALLPGAGGGRCPQRCACTQPALRCPTPPPGARPAPARASFTHLPVKVIPSHAFEGLRDAFIIEISQSDSLERIEASAFDSLPALSEILILNTKNLLHIEDGAFRNLPRLKYLSICNTGIIEFPDLTQIFSSEAHFILELCDNLRMTTIPQNAFQGMSNESLTLKLYKNGFEDIHSHAFNGTKLNQLILKDNKNLRRIHNDALRGATGPDVLDISSTALESLPSYGLEAIQVLNAMSSYSLKRLPPLDKFSSLLEAVLTYPSHCCAFQNLRTEKQNSLLSIFDNFSKQCESTMRKPASEVFYRDASSNTSLWPAEKHMYPLETGEEAFPYSYSTVFYEDEMTGFDFEYDFCQPKILTCTPEPDAFNPCEDILGYSFLRVLIWFINILALAGNFIVLLVLITSHYKLTVPRFLMCNLSFADFCMGLYLLLIASVDAQTSGQYYNHAIDWQTGSGCSTAGFFTVFASELSVYTLTVITIERWHTITYAMQLDRKLRLRHAVPIMLGGWVFSILIAVLPLLGVSSYMKVSICLPMDIETGLSQAYILLILMLNVIAFLVICACYIKIYVAVQNPELVAANKDTKIAKRMAILIFTDFTCMAPISFFAISAAIKVPLITVTNSKILLVLFYPVNSCANPFLYAIFTKAFQRDFFLLMSKLGCCKSRAELYRVNYFSAYTPNCKNGSSAPGPSKASQALLLLSASEKLCKTRRSTKKSQPECQ
Protein: Flavone 3'-O-methyltransferase 1 (AtOMT1) (EC 2.1.1.42) (Acetylserotonin O-methyltransferase OMT1) (EC 2.1.1.4) (Caffeate O-methyltransferase 1) (AtCOMT) (EC 2.1.1.68) (Quercetin 3'-O-methyltransferase 1) (EC 2.1.1.-) (Serotonin O-methyltransferase) (EC 2.1.1.-) (Q9FK25)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Methylates OH residues of flavonoid compounds. Converts quercetin into isorhamnetin. Dihydroquercetin is not a substrate. Catalyzes the methylation of monolignols, the lignin precursors. Does not contribute to the phenylpropanoid pattern of the pollen tryphine, but is probably confined to isorhamnetin glycoside biosynthesis. Involved in melatonin biosynthesis. Can function as acetylserotonin O-methyltransferase. Catalyzes the transfer of a methyl group onto N-acetylserotonin, producing melatonin (N-acetyl-5-methoxytryptamine).
Subcellular location: Cytoplasm {ECO:0000269|PubMed:25250906, ECO:0000269|PubMed:32354877}. Nucleus {ECO:0000269|PubMed:32354877}.
Interaction partners:
- Cinnamoyl-CoA reductase 1
- Cytochrome P450 84A1
- Cinnamoyl-CoA reductase 2
- 4-coumarate--CoA ligase 1
- Caffeoylshikimate esterase
- Cinnamyl alcohol dehydrogenase 5
- Alpha/beta-Hydrolases superfamily protein
- 4-coumarate--CoA ligase 2
- Alpha/beta-Hydrolases superfamily protein
- 4-coumarate--CoA ligase 4
Sequence:
MGSTAETQLTPVQVTDDEAALFAMQLASASVLPMALKSALELDLLEIMAKNGSPMSPTEIASKLPTKNPEAPVMLDRILRLLTSYSVLTCSNRKLSGDGVERIYGLGPVCKYLTKNEDGVSIAALCLMNQDKVLMESWYHLKDAILDGGIPFNKAYGMSAFEYHGTDPRFNKVFNNGMSNHSTITMKKILETYKGFEGLTSLVDVGGGIGATLKMIVSKYPNLKGINFDLPHVIEDAPSHPGIEHVGGDMFVSVPKGDAIFMKWICHDWSDEHCVKFLKNCYESLPEDGKVILAECILPETPDSSLSTKQVVHVDCIMLAHNPGGKERTEKEFEALAKASGFKGIKVVCDAFGVNLIELLKKL