wanglab/gogpt-training-data huggingface dataset:
Protein: Glucosidase 2 subunit beta (A0A8I6ADW9)
Organism: Rattus norvegicus (Rat)
Interaction partners:
Sequence:
MLLLLLLLPLCWAVEVKRPRGVSLSNHHFYDESKPFTCLDGTATIPFDQVNDDYCDCKDGSDEPAACPNGSFHCTNTGYKPLYILSSRVNDGVCDCCDGTDEYNSGTVCENTCREKGRKEKESLQQLAEVTREGFRLKKILIEEWKTAREEKQSKLLELQAGKKSLEDQVETLRTAKEEAERPEKEAKDQHRKLWEEQQAAAKARREQELAASAFQELDDNMDGLVSLAELQTHPELDTDGDGGLSEEEAQALLSGDTQTDTTSFYDRVWAAIRDKYRSEVPPTDIPVPEVTEPKEEKLPVLPPMEEEEEEEEPEEEEEEEEEEVPGEQPKEVPPPQQPLRPPSPAEDEKMPPYDEETQAIIDAAQEARNKFEEVERSLKEMEESIRSLEQEISFDFGPSGEFAYLYSQCYELTTNEYVYRLCPFKLVSQKPKHGGSPTSLGTWGSWAGPDDDKFSAMKYEQGTGCWQGPNRSTTVRLLCGKETVVTSTTEPSRCEYLMELMTPAACPEPPPEVPTDGDHDEL
Protein: RNA-binding protein, putative (Q38D96)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MSLTAELFGAATPSSTSPSEKLKKKGTSKNSVVATSTVFEPTKKAAFDIFAVAPEVRKATRREKQRLRIEEGVSRKNGTWKGKGESATEDEIFRTVIVDNTTGGDEVGESKPDGRKKQLRHALHQNEEEDSRTVFVGNLVNDVKRRVLEKVFKTCGPIESVRIRAQALEGEKDLNGGEATVQPRGVGRAIRVLRGDVKKGEQYSAVAYVLFKDKSSIKEALDKNGVVVEGRHIVVTTLDPEGREYAPETSVFVGNVAYDSNEEALWNFFVEKGIRDVKRVRLVRDRESGMCKGFGYVEFQSKGSVAAAIALRGTLFMDREIRIVHVQKSKAVTASKATRREKRKLGTRGEVADSRSQGAEGNGKRMRTEGKTKVQGPVDDQPPWMGVVTNPRRKIPKDLRPLVEGKKSFSSPAPRAPVKRKMRNPEKGH
Protein: Iroquois-class homeodomain protein IRX-1 (Homeodomain protein IRXA1) (Iroquois homeobox protein 1) (P81068)
Organism: Mus musculus (Mouse)
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
- Iroquois-class homeodomain protein IRX-2
- Iroquois-class homeodomain protein IRX-6
Sequence:
MSFPQLGYPQYLSAAGPGAYGGERPGVLAAAAAAAAAASSGRPGTAELGAGAGAAAVTSVLGMYAAAGPYAGAPNYSAFLPYAADLSLFSQMGSQYELKDNPGVHPATFAAHTTPAYYPYGQFQYGDPGRPKNATRESTSTLKAWLNEHRKNPYPTKGEKIMLAIITKMTLTQVSTWFANARRRLKKENKVTWGARSKDQEDGALFGSDTEGDPEKAEDDEEIDLESIDIDQIDERDGDQSNEDEEDKAEAPRARVAPPASARDQSSPLSAAETLKSQDSPLGLVKEVSEPGSTRLLSPGAAAVGLQGAPHSKPKIWSLAETATSPDGAPKASPPPPSSHASAHGPPSGSPLQHPAFLPSHGLYTCHIGKFSNWTNGAFLAQGSLLNMRSFLGVSAPHAAPHGPHLTAPPPPQPPVQVATGVLHGEKASARSSPALPERDLVTRPDSPPQQLKSPFQPVRDNSLAPQEGTPRILAALPSA
Protein: Exocyst complex component 6B (Exocyst complex component Sec15B) (SEC15-like protein 2) (Q9Y2D4)
Organism: Homo sapiens (Human)
Function: Component of the exocyst complex involved in the docking of exocytic vesicles with fusion sites on the plasma membrane.
Interaction partners:
- Exocyst complex component 5
- Exocyst complex component 8
- Exocyst complex component 7
- Exocyst complex component 4
- Exocyst complex component 1
- Exocyst complex component 3
- Exocyst complex component 2
- Exocyst complex component 1-like
- Exocyst complex component 3-like protein
- Exocyst complex component 6
Sequence:
MERGKMAEAESLETAAEHERILREIESTDTACIGPTLRSVYDGEEHGRFMEKLETRIRNHDREIEKMCNFHYQGFVDSITELLKVRGEAQKLKNQVTDTNRKLQHEGKELVIAMEELKQCRLQQRNISATVDKLMLCLPVLEMYSKLRDQMKTKRHYPALKTLEHLEHTYLPQVSHYRFCKVMVDNIPKLREEIKDVSMSDLKDFLESIRKHSDKIGETAMKQAQQQRNLDNIVLQQPRIGSKRKSKKDAYIIFDTEIESTSPKSEQDSGILDVEDEEDDEEVPGAQDLVDFSPVYRCLHIYSVLGARETFENYYRKQRRKQARLVLQPPSNMHETLDGYRKYFNQIVGFFVVEDHILHTTQGLVNRAYIDELWEMALSKTIAALRTHSSYCSDPNLVLDLKNLIVLFADTLQVYGFPVNQLFDMLLEIRDQYSETLLKKWAGIFRNILDSDNYSPIPVTSEEMYKKVVGQFPFQDIELEKQPFPKKFPFSEFVPKVYNQIKEFIYACLKFSEDLHLSSTEVDDMIRKSTNLLLTRTLSNSLQNVIKRKNIGLTELVQIIINTTHLEKSCKYLEEFITNITNVLPETVHTTKLYGTTTFKDARHAAEEEIYTNLNQKIDQFLQLADYDWMTGDLGNKASDYLVDLIAFLRSTFAVFTHLPGKVAQTACMSACKHLATSLMQLLLEAEVRQLTLGALQQFNLDVRECEQFARSGPVPGFQEDTLQLAFIDLRQLLDLFIQWDWSTYLADYGQPNCKYLRVNPVTALTLLEKMKDTSRKNNMFAQFRKNERDKQKLIDTVAKQLRGLISSHHS
Protein: Cyclin-dependent kinase 1 (EC 2.7.11.22) (EC 2.7.11.23) (Cell division control protein 2 homolog) (Cell division protein kinase 1) (p34 protein kinase) (Q7T3L7)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000256|ARBA:ARBA00004300}. Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- Cyclin B1
- Cyclin-A1
- Cyclin B2
- M-phase inducer phosphatase
- Cyclin A2
- Cyclin B3
- Serine/threonine-protein kinase PLK
- Cell division cycle 20 homolog
- Wee1-like protein kinase
- Cyclin-H
Sequence:
MDDYLKIEKIGEGTYGVVYKGRNKTTGQVVAMKKIRLESEEEGVPSTAVREISLLKELQHPNVVRLLDVLMQESKLYLVFEFLSMDLKKYLDSIPSGEFMDPMLVKSYLYQILEGILFCHCRRVLHRDLKPQNLLIDNKGVIKLADFGLARAFGVPVRVYTHEVVTLWYRAPEVLLGASRYSTPVDLWSIGTIFAELATKKPLFHGDSEIDQLFRIFRTLGTPNNEVWPDVESLPDYKNTFPKWKSGNLANTVKNLDKNGIDLLMKMLIYDPPKRISARQAMTHPYFDDLDKSSLPASNLKI
Protein: Protovillin (100 kDa actin-binding protein) (P36418)
Organism: Dictyostelium discoideum (Social amoeba)
Function: Caps actin filaments but displays neither severing nor cross-linking nor nucleating activities. Protovillin seems to be a villin precursor with only archaic capping activity. It lacks essential changes in the sequence to allow bundling of actin filaments and consequently the appearance of microvilli.
Subcellular location: Cytoplasm, cytoskeleton.
Interaction partners:
- Actin domain-containing protein
Sequence:
MEPPLELPTQRKRVIPSKFGILKRNAEIEAEKNRENLQQSSCFSHINEIGKEIGLEIWKIIDDSTIQKVPKVNHSTFETNKSYLLLMGQFYDGNMNIKTYNIHFWIGELLINSQETINFCNDRIEELERIIKYNQKQFDSEQFYPEPILYREFQGKEGDIFMSYFKSYGGPRYVAPLKLTSASAAIATAAKQYKLFHLKGRRNIRVKQVDISSKSLNSGDVFVLDCEDFIYQWNGSESSRLEKGKGLDLTIRLRDEKSAKAKIIVMDENDTDKDHPEFWKRLGGCKDDVQKAEQGGDDFAYEKKSVEQIKLYQVENLNYEVHLHLIDPIGDVYSTTQLNAEFCYILDCETELYVWLGKASANDQRTVAMANAMDLLHEDNRPSWTPIIKMTQGSENTLFKDKFKKGSWGEYVNDNFEKKPITGKGVAAKAVQEKINVDALHNPEKYQLSKEERKSTIPTLHHVDDKHRGELKIWHVRNRNKFEISQSEFGLFYNQSCYLVLFTLFAADGSNNSILYYWQGRFSSSEDKGAAALLAKDVGKELHRSCIHVRTVQNKEPNHFLEHFQGRMVVFKGSRPNATTEVSLENLSSSLQGLYHVRGTEPINIHSIQVEKAISSLDSNDSFILVNFKNTISYIWVGKYSDEKEAALQISSNVFTGYNFQLIDEGDETSEFWESLETNSSLSLLKDYYTQLRTVEQEKKTRLFQCSNNSGVFKVFEIHDFSQDDLDSDDVMILDNQKQIFVWVGKESSDTEKLMANETALEYIMNAPTHRRDDPIFTIQDGFEPHEFTFNFHAWQVNKTQQDSYKSKLSAILGSNNSGPASPIMLPTSGVTLKPTTAATPKPITTPTVTTPKPITTPTVATLKTVTPAVTLKPTTVTTPSKVATTTNTSTPSPTTITTFYPLSVLKQKTNLPNDIDKSCLHLYLSDEEFLSTFKMTKEIFQKTPAWKTKQLRVDNGLF
Protein: Hexokinase-4 (HK4) (EC 2.7.1.1) (Glucokinase) (Hexokinase type IV) (HK IV) (Hexokinase-D) (P52792)
Organism: Mus musculus (Mouse)
Function: Catalyzes the phosphorylation of hexose, such as D-glucose, D-fructose and D-mannose, to hexose 6-phosphate (D-glucose 6-phosphate, D-fructose 6-phosphate and D-mannose 6-phosphate, respectively). Compared to other hexokinases, has a weak affinity for D-glucose, and is effective only when glucose is abundant (By similarity). Mainly expressed in pancreatic beta cells and the liver and constitutes a rate-limiting step in glucose metabolism in these tissues. Since insulin secretion parallels glucose metabolism and the low glucose affinity of GCK ensures that it can change its enzymatic activity within the physiological range of glucose concentrations, GCK acts as a glucose sensor in the pancreatic beta cell. In pancreas, plays an important role in modulating insulin secretion. In liver, helps to facilitate the uptake and conversion of glucose by acting as an insulin-sensitive determinant of hepatic glucose usage. Required to provide D-glucose 6-phosphate for the synthesis of glycogen. Mediates the initial step of glycolysis by catalyzing phosphorylation of D-glucose to D-glucose 6-phosphate (By similarity).
Subcellular location: Cytoplasm {ECO:0000269|PubMed:24187134}. Nucleus {ECO:0000269|PubMed:10713097}. Mitochondrion {ECO:0000250|UniProtKB:P17712}. Note=Under low glucose concentrations, GCK associates with GCKR and the inactive complex is recruited to the hepatocyte nucleus. {ECO:0000269|PubMed:10713097}.
Interaction partners:
- Glucokinase regulatory protein
- Glucose-6-phosphatase catalytic subunit 1
- Glucose-6-phosphatase 2
- Glucose-6-phosphatase 3
- GDH/6PGL endoplasmic bifunctional protein
- Glucose-6-phosphate isomerase
- Hexokinase-3
- Hexokinase-1
- Hexokinase HKDC1
- Phosphoglucomutase-1
Sequence:
MLDDRARMEATKKEKVEQILAEFQLQEEDLKKVMSRMQKEMDRGLKLETHQEASVKMLPTYVRSTPEGSEVGDFLSLDLGGTNFRVMLVKVGEGEAGQWSVKTKHQMYSIPEDAMTGTAEMLFDYISECISDFLDKHQMKHKKLPLGFTFSFPVRHEDIDKGILLNWTKGFKASGAEGNNIVGLLRDAIKRRGDFEMDVVAMVNDTVATMISCYYEDRQCEVGMIVGTGCNACYMEEMQNVELVEGDEGRMCVNTEWGAFGNSGELDEFLLEYDRMVDESSVNPGQQLYEKIIGGKYMGELVRLVLLKLVEENLLFHGEASEQLRTRGAFETRFVSQVESDSGDRRQILNILSTLGLRPSVADCDIVRRACESVSTRAAHMCSAGLAGVINRMRESRSEDVMRITVGVDGSVYKLHPSFKERFHASVRRLTPNCEITFIESEEGSGRGAALVSAVACKKACMLGQ
Protein: Response regulator receiver protein CpdR (Phospho-receiver protein CpdR) (Q2YIF7)
Organism: Brucella abortus (strain 2308)
Function: Component of a regulatory phosphorelay system that controls B.abortus cell growth, division, and intracellular survival inside mammalian host cells. This signaling pathway is composed of CckA, ChpT, CtrA and CpdR. CpdR is a response regulator substrate of ChpT. Unphosphorylated CpdR controls steady-state levels of CtrA in the B.abortus cell, likely via CtrA destabilization and activation of its proteolysis.
Subcellular location: Cytoplasm {ECO:0000305|PubMed:26124143}.
Interaction partners:
- histidine kinase
- Cell-division control histidine kinase PdhS
- histidine kinase
- Protein phosphotransferase ChpT
- histidine kinase
- PAS domain:GGDEF:PAS-associated C-terminal domain:PAC motif:EAL domain
- Polar-differentiation response regulator DivK
- Cell cycle response regulator CtrA
- histidine kinase
- ATP-dependent Clp protease ATP-binding subunit ClpX
Sequence:
MKRILLAEDDNDMRRFLVKALEKAGYHVTHFDNGASAYERLQEEPFSLLLTDIVMPEMDGIELARRATEIDPDLKIMFITGFAAVALNPDSDAPRDAKVLSKPFHLRDLVNEIEKMLIAA
Protein: AN1-type domain-containing protein (Q9XUW8)
Organism: Caenorhabditis elegans
Interaction partners:
- Uncharacterized protein F44E2.4
- Domain of unknown function DB domain-containing protein
- F-box domain-containing protein
- Probable inactive acireductone dioxygenase 2
- YitH/HolE acetyltransferase
- Ubiquitin-ribosomal protein eL40 fusion protein
Sequence:
MAEFPNLGKHCESTVCNRLDFLPIKCSGCGHFYCSEHFTFEAHNCPTGSRISVQVPICPICEKPVPTPKDVNVDQQVNEHIQNNCQTPKRAKVYSNACTVPKCKKKELVAMNCSKCRNNYCLSHRHERDHSCERKVGEMKINQKKSWTDSITSIARSRMNPCSAQARTEGDEALARSLQQEEYNRVAPPHQTRNSNSNCTVS
Protein: Disks large homolog 1 (MAGUK protein DLG-1) (SAP97-like protein DLG-1) (G5ECY0)
Organism: Caenorhabditis elegans
Function: Essential multidomain scaffolding protein required for normal development (Probable). Recruits channels, receptors and signaling molecules to discrete plasma membrane domains in polarized cells (By similarity). Required for proper embryonic elongation. Acts upstream of ajm-1 and becomes localized to apical junctions independently of ajm-1. With let-413, cooperatively regulates ajm-1 localization to apical junctions.
Subcellular location: Membrane {ECO:0000269|PubMed:11715019, ECO:0000269|PubMed:18411252}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q12959}. Apical cell membrane {ECO:0000269|PubMed:11493666, ECO:0000269|PubMed:11715019}. Cell junction, adherens junction {ECO:0000269|PubMed:11715019, ECO:0000269|PubMed:18411252, ECO:0000269|PubMed:19109941}. Lateral cell membrane {ECO:0000269|PubMed:18411252}. Cytoplasm {ECO:0000250|UniProtKB:Q12959}. Note=Localizes at the apical junctions (PubMed:11715019, PubMed:18411252). Localizes to the subapical membrane of epithelial cells (PubMed:11493666). Localization at adherens junctions requires PDZ domains, lateral distribution requires SH3 domain and is let-413 dependent (PubMed:18411252). {ECO:0000269|PubMed:11493666, ECO:0000269|PubMed:11715019, ECO:0000269|PubMed:18411252}.
Interaction partners:
- Apical junction molecule ajm-1
- LITAF domain-containing protein
- Protein Scribble homolog let-413
- Alpha-catenin-like protein hmp-1
- Tetratricopeptide repeat protein 28
- Protein lin-2
- Cadherin-related hmr-1
- NMDA-type ionotropic glutamate receptor NMR-2
- Potassium voltage-gated channel protein shk-1
- Kinesin motor domain-containing protein
Sequence:
MSHESSEKAHKAIENVEDYCQTLTRHGNEELRTNLERVITTFKSNLMHSLLDIHDLYEQTLLSERKSDAEKNMEVRRVIERLEGGPHSYNSRPAATTSTSNYNLSSTTPLISDLRDRGGFSYLNGGGLGNGLGNGLGNGLLSSPYNSSSTHYLHERQRQTSHDGTWRETTTRTVDTPSGLERRVVEHTGVIDDHGRKWELENIVLEKGHTGLGFSITGGMDQPTEDGDTSIYVTNIIEGGAALADGRMRKNDIITAVNNTNCENVKHEVAVNALKSSGNVVSLSLKRRKDEAFLPIGGNFGGSTSYLRSGVTPSVSAGNLQHAIHSPSAPIHPPPPPPVHHGSLSQLSVGQYRSTRPNTSVIDLVKGARGLGFSIAGGQGNEHVKGDTDIYVTKIIEEGAAELDGRLRVGDKILEVDHHSLINTTHENAVNVLKNTGNRVRLLIQQGTGAIFNDSASQQFMPTTPILRPSSVQDYNRSQMGSQSHLSYGGPLNTSYSSQAPIAIPLEPRPVQLVKGQNGLGFNIVGGEDNEPIYISFVLPGGVADLSGNVKTGDVLLEVNGVVLRNATHKEAAEALRNAGNPVYLTLQYRPQEYQIFESKIEKLRNDVIAQSRMGTLSRKSEYVRALFDYDPSRENSVAPHRSMGFNYGDILHIINSSDDEWWTARKVHENGEETAEGVIPSKKRVEKRERLRRKQVNFNSGSQSLGRNSSTTGLENRRGSRSQLSFSRKFPFVKSTDRLNDLNEESSNVAEEPVWSYQAVEQQAINYVRPVIILGALKDRINDELVNRDPSKFSSCVPHTSRPPREGEVNGRDYYFVNKHNMEEDVKNNLFIEAGQFQNNLYGTSIQSVRDVANQGRHCILDVSGNAIRRLQSNANIQPISIFIKPSSAQQILELDSQLATNRQDDRAMSGEEAQAQYSRCHRIEQTFGDLFTQEISNVHSANDVLSKVYSIISRESQTPIWVPRH
Protein: Neutrophil defensin 1 (Defensin, alpha 1) (HNP-1) (HP-1) (HP1) [Cleaved into: HP 1-56; Neutrophil defensin 2 (HNP-2) (HP-2) (HP2)] (P59665)
Organism: Homo sapiens (Human)
Function: Effector molecule of the innate immune system that acts via antibiotic-like properties against a broad array of infectious agents including bacteria, fungi, and viruses or by promoting the activation and maturation of some APCs. Interacts with the essential precursor of cell wall synthesis lipid II to inhibit bacterial cell wall synthesis. Inhibits adenovirus infection via inhibition of viral disassembly at the vertex region, thereby restricting the release of internal capsid protein pVI, which is required for endosomal membrane penetration during cell entry. In addition, interaction with adenovirus capsid leads to the redirection of viral particles to TLR4 thereby promoting a NLRP3-mediated inflammasome response and interleukin 1-beta (IL-1beta) release. Induces the production of proinflammatory cytokines including type I interferon (IFN) in plasmacytoid dendritic cells (pDCs) by triggering the degradation of NFKBIA and nuclear translocation of IRF1, both of which are required for activation of pDCs.
Subcellular location: Secreted.
Interaction partners:
- Neutrophil defensin 3
- Beta-defensin 1
- Defensin beta 4A
- Defensin alpha 4
- Beta-defensin 103
- GPI-linked NAD
- Beta-defensin 104
- T-cell surface glycoprotein CD4
Sequence:
MRTLAILAAILLVALQAQAEPLQARADEVAAAPEQIAADIPEVVVSLAWDESLAPKHPGSRKNMACYCRIPACIAGERRYGTCIYQGRLWAFCC
Protein: PIG-P domain-containing protein (Q5AUG0)
Organism: Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
- Phosphatidylinositol N-acetylglucosaminyltransferase GPI3 subunit
- N-acetylglucosaminylphosphatidylinositol deacetylase
- chitinase
- Phosphatidylinositol:UDP-GlcNAc transferase PIG-C
- N-acetylglucosaminyl transferase component Gpi1
- Dolichol phosphate-mannose biosynthesis regulatory protein
- CDP-diacylglycerol-inositol 3-phosphatidyltransferase PIS
Sequence:
MSLLREQKGEFYTQDETDASPVISHFEQKQPFPPLPPDELDAPRDADTQSNCFPGEDDQDLASSHPDGDVEDDVDFHSHYSLEDQSFSDASTDSNDEQSPEDGIAMHHPFRQSASSLHGPNAFAPPFYNRPPTPLPPSPSLTSLLRPPFSTNTSRPTTPDSSDVETPNDTEAAVAKSARRATTVPRASPKVPTYEYYGFVLYLASSLAFLIYILWSYLPSPFLHQLGIYYYPNRWWSLAFPSWLVMSIIYIYVALASYNTGYLTLPMNSVENIVDEVANVAVIDGKGRRRPGGAAKMRPGATSFQIMGPQNRKVNWREIWSEGTDAVLDIPVGGVCEVLYGPERDEKDDDCVESPDL
Protein: Hemoglobin alpha, adult chain 2 (A0A8I5ZYH2)
Organism: Rattus norvegicus (Rat)
Interaction partners:
Sequence:
MKLASGPIHSHSDRLRKQSWCSLQLTKPTSRTAGGRLVAMVVNMARRPYRGNIRTLFFKDSRIQTGPGTQWVAPKCAFPWPQLISPSHRMFAAFPTTKTYFSHIDVSPGSAQVKAHGKKVADALAKAADHVEDLPGALSTLSDLHAHKLRVDPVNFKFLSHCLLVTLACHHPGDFTPAMHASLDKFLASVSTVLTSKYR
Protein: Serine/threonine-protein kinase par-1 (EC 2.7.11.1) (Q9TW45)
Organism: Caenorhabditis elegans
Function: Required for cytoplasmic partitioning and asymmetric cell division in early embryogenesis. Phosphorylates and restricts the asymmetry effector mex-5 (and possibly also mex-6) to the anterior cytoplasm of the zygote. Regulates mes-1 expression during early embryogenesis. Critical role in postembryonic vulval morphogenesis. Involved in the establishment of neuronal polarity.
Subcellular location: Cytoplasm, cell cortex {ECO:0000269|PubMed:7758115}. Note=Colocalizes with germ granules (P granules). {ECO:0000269|PubMed:7758115}.
Interaction partners:
- Partitioning defective protein 3
- Zinc finger protein mex-5
- Partitioning defective protein 6
- Zinc finger protein mex-6
- RNA-binding protein pos-1
- RING-type domain-containing protein
Sequence:
MSSASVGKKPEHVNTPPGDNQQKSSKENQKSNKDKQSSNQPPGQIPHSTNSGTRKSSGSGLKTANLKHPARPSTESSTSSSHHRRPAQEMNGTSTATATGGGGTSGATTTASSGAPAASSGGSSARYSSSGRSHPTSGSSSSHARSTGQSGMSSRSAARRNDQDVHVGKYKLLKTIGKGNFAKVKLAKHVITGHEVAIKIIDKTALNPSSLQKLFREVKIMKQLDHPNIVKLYQVMETEQTLYLVLEYASGGEVFDYLVAHGRMKEKEARAKFRQIVSAVQYLHSKNIIHRDLKAENLLLDQDMNIKIADFGFSNTFSLGNKLDTFCGSPPYAAPELFSGKKYDGPEVDVWSLGVILYTLVSGSLPFDGQNLKELRERVLRGKYRIPFYMSTDCENLLKKFLVINPQRRSSLDNIMKDRWMNVGYEDDELKPFIEPPKDQIDEQRIEKLIQIFQLGFNKAAILESVEKEKFEDIHATYLLLGERKSDMDASEITMAQSLLSHSSINVSSSLGQHPAGVITREHVTSSSASGSSASPSRYSRSSATATGASITAGSALASAANAQKHQQSSAAPSSGSSSSRRSSQNDAAATAAGGTVVMSGTRHGGVQMRAQPTSRQATISLLQPPSYKPSSNTTQIAQIPPLFNRNSTATSSAAQPSTGITGTRKIADPKGRIPLNSTAVQGHRTATGAVAANNGGIPSHRDHAQQQQYMNQLTSSTMMSKLINKTPAAGGTAATSSSSSSSATSTAPLQKSGSQISHAPTEPVIREDDDENNSENQNGNVPLIGGVGPQTSPAVQVPTEDATSSSDKEQQQQKASSETPKESKPSMIHQSPSMPPSQMMTAMESLKLSESGQTGGPTVATGGPPQRATSQQMSRSATTNSANMGASSGGAAAAASATNQLSGAPSSTGASSQQYHPKAPSSSSSSSTNPPHQHQLTHNASFSVTPSSYQIPTSTAVNVTSTGMPTSSSSSAFPRNTRNRQTFHGKTEKDKGGDDSSDEIGETPGNVSIGATGPSANNAEATIWSKLSKLTRRDHNRESMTQPVSGRAGTIGASQGQQTAAALAAIREQSGPIAPGAGQVAPSLPIHEGDVKPRSLRFTWSMKTTSSLAPDDMMREIRKVLDANGCDYEQRERYMILCVHGDPNTDSLVQWEMEVCKLPRLSLNGVRFKRISGTSIGFKNIASKIAQELNL
Protein: Cip1p (A0A1D8PPI6)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Interaction partners:
- Oye32p
- Pre-mRNA-splicing factor CEF1
- Probable quinone oxidoreductase
Sequence:
MSKVSITIIGLNGFLGKPVLEAINSGIFDDKINFPIKAITRKEPETKNDKIEYVVSEINEESIKSTLSQKLSGTDVIIELIGPNPEAFANIEKLIDAIKPKLFIPSQFGTDIPKVDEYAPGFLGIKTQHSENVRKLGVKVVDIITSLFAVPGAFLYEWVGSTGINADDKTVKLIGDINQQFDISKLEDVGKAVLSIATNPNPRELPDTIRIGSDRITVKDVIDRYSKDHNVELKVVSEQSAEDAKKEFTESLKAGFDGEKFLWYLQVIAAQGLDKGLLSSKLDNELVNPGESLWKWGKY
Protein: Tetraspanin-12 (Tspan-12) (Transmembrane 4 superfamily member 12) (Q8BKT6)
Organism: Mus musculus (Mouse)
Function: Regulator of cell surface receptor signal transduction. Acts as a regulator of membrane proteinases such as ADAM10 and MMP14/MT1-MMP. Activates ADAM10-dependent cleavage activity of amyloid precursor protein (APP). Activates MMP14/MT1-MMP-dependent cleavage activity (By similarity). Plays a central role in retinal vascularization by regulating norrin (NDP) signal transduction. Acts in concert with norrin (NDP) to promote FZD4 multimerization and subsequent activation of FZD4, leading to promote accumulation of beta-catenin (CTNNB1) and stimulate LEF/TCF-mediated transcriptional programs. Suprisingly, it only activate the norrin (NDP)-dependent activation of FZD4, while it does not activate the Wnt-dependent activation of FZD4, suggesting the existence of a Wnt-independent signaling that also promote accumulation the beta-catenin (CTNNB1).
Subcellular location: Cell membrane {ECO:0000305|PubMed:19837033}; Multi-pass membrane protein {ECO:0000305|PubMed:19837033}.
Interaction partners:
- Frizzled-4
- Norrin
- Low-density lipoprotein receptor-related protein 5
- Zinc finger protein 408
- Adhesion G protein-coupled receptor A2
Sequence:
MAREDSVKCLRCLLYALNLLFWLMSISVLAVSAWMRDYLNNVLTLTAETRVEEAVILTYFPVVHPVMIAVCCFLIIVGMLGYCGTVKRNLLLLAWYFGTLLVIFCVELACGVWTYEQEVMVPVQWSDMVTLKARMTNYGLPRYRWLTHAWNYFQREFKCCGVVYFTDWLEMTEMDWPPDSCCVREFPGCSKQAHQEDLSDLYQEGCGKKMYSFLRGTKQLQVLRFLGISIGVTQILAMILTITLLWALYYDRREPGTDQMLSLKNDTSQHLSCHSVELLKPSLSRIFEHTSMANSFNTHFEMEEL
Protein: Transient receptor potential cation channel subfamily A member 1 homolog (Q18297)
Organism: Caenorhabditis elegans
Function: Receptor-activated non-selective cation channel involved in the nose-touch response and foraging behavior. Contributes to the neural responses of sensory neurons to touch, particularly after repeated mechanical stimulation. Has no apparent role in thermosensory or chemosensory behaviors.
Subcellular location: Cell membrane {ECO:0000269|PubMed:17450139}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
- Ion transport domain-containing protein
- Ion transport domain-containing protein
- Degenerin mec-10
- Transmembrane protein adipocyte-associated 1 homolog
- GTL-1
- Degenerin mec-4
- Ion transport domain-containing protein
- Acid-sensing ion channel 1
- Protein kinase C-like 2
- Amidase domain-containing protein
Sequence:
MSKKSLGLDVRLELEGLISNDDTIRSEKDGRQASIFRVAELDARTEADNLRSIIHQSAREGNVNALQEALLKAPLAVNAQDGDFMTPLHYAARYGNYDAVKLLLSKNALPNTKNREGDTPLHIASKYIYGYSDICSIIDEDQADSARKYNTATKKIINALVSENAEIDPVNKYQLTPLHYAAMKSNFSALHALIKLKADVDAEDDNKMTPLLLACVHGSQEIIQELIKANSNVTKRDQRLNTVFHIVALRGEPEYLEMMMDHDPVEAIKALNLFNNEKKTPLRMAVEGNHPETLKKILQMEKKNSCKWMDREKELIHFAAEKGFLEVLKALVEAGGNKNELNEVKAVPLHVAAQMNQLEVVSYLIEEEKDNIDVVDEQGLTPLMMAVTHDSKKCVEYLIAKKANLTITDKDERTPVFIGAKFNALSSVEYILDHLRKKNKETERSALKSPTRNTLRIVSEDVRRTMVNMVDRDQNTPMHIVASNGYLEMMQLLQKHGASITQVNEDEETALHRAAIGGQTGAVRQLLEWDIRLLLMKDEMGNSALHLAARSGHDATTKVLLDNGADKEAKNSYQKTPLQVAVDSGKLETCQRLVAKGAQIESSSDTKTVLHTAAFYGNESIVRYFIAEGVTIDRRDEEGKTAFDIACENDHKDVARAFLETDQWKNLMIPCDVIPLDKHRNPVNMKRRTPFRTLLTKFPELASFVMDNCIEKSKEETDSTQSVAYNFEFLDDTYMMRCVSDDGTGEQLIGCKSAYDEDFKLEKDAQSYASNYDRVYKYHPLKLMADAEKLHLLNHPLSKALLKYKWNRLGRPMYYFALFMYLVFIVSLTQYVRHTKAPYNVWNEESYYDSEYFDENETCPQINTTKPDVVWKIIIQTLAVCQILVECFQLFQRKFAYLVNWENWIDCFIYSTALITVYDFSECSATSGVRQNWQWILAALCIFFGWINLLFMIRKMPRFGIFVVMFVDIVKTFFRFFPVFVLFIIAFSSSFYVILQNRPEFSTIFMSPLKTTVMMIGEFEFTGIFHGDETTHAEKMFGPAHTAVACALFFFFCIIMTILLMNLLVGLAVDDIKGVQEKAELKRLAMQVDLVLQIEASLHFFIQRTKKYATCRYATFPYGKLHKTGFAGWWSNFRRRFGLSVSTDPEIDEMYEREAEFTSEMTQKLQNQAAKLKNIQENIDVMYEKQVRLEAIIAKLATGLNINIELEEKDN
Protein: Heat stress transcription factor 32 (I1MPZ9)
Organism: Glycine max (Soybean) (Glycine hispida)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MAPPPPVEHNGDSAATASASASAESQRSIPTPFLTKTYQLVDDQSIDDVISWNDDGSTFIVWNPTVFARDLLPKFFKHNNFSSFVRQLNTYGFRKVVPDRWEFSNDYFRRGEKRLLCEIQRRKISSPAPSPTAPTTVTVPMPLTAIPIISPSNSGEEQVISSNSSPLRAPAELLDENERLRKENVQLTKELAEMRSLCNNIYSLMSSYGNKNGNSNGSYQTDGGAGGAQGSRESGMTAVKPLDLMPVKRSSGEDAADTVPKEINLIPNPKLFGVAIGAKRAREGGGGSGSGRDCGGGGGGGEEDTLLRLHHVGSADVKSEPLDCQNHRENQETPWLSPCHRTNQRVCN