wanglab/gogpt-training-data huggingface dataset:
Protein: E3 ubiquitin-protein ligase ORTHRUS 1 (EC 2.3.2.27) (Protein VARIANT IN METHYLATION 3) (RING-type E3 ubiquitin transferase ORTHRUS 1) (Q9FKA7)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: E3 ubiquitin-protein ligase. Participates in CpG methylation-dependent transcriptional regulation and epigenetic transcriptional silencing. Mediates ubiquitination with the E2 ubiquitin-conjugating enzymes UBC11, UBC8 and UBC8 homologs (e.g. UBC10, UBC11, UBC28 and UBC29) but not with UBC27, UBC30, UBC32, UBC34 and UBC36. Promotes methylation-mediated gene silencing leading, for example, to early flowering. Can bind to CpG, CpNpG, and CpNpN DNA motifs, with a strong preference for methylated forms, and with highest affinity for CpG substrate.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00358, ECO:0000269|PubMed:18643997, ECO:0000269|PubMed:18704160}. Note=Broadly distributed in the nucleus and enriched in the heterochromatic chromocenters.
Interaction partners:
- DNA
- DNA
- DNA
- DNA
- Alpha/beta-Hydrolases superfamily protein
- At4g31150
- At1g62305
- Germin-like protein subfamily 1 member 19
- Probable inactive DNA
Sequence:
MAIETQLPCDGDGVCMRCQVNPPSEETLTCGTCVTPWHVPCLLPESLASSTGEWECPDCSGVVVPSAAPGTGNARPESSGSVLVAAIRAIQADETLTEAEKAKKRQKLMSGGGDDGVDEEEKKKLEIFCSICIQLPERPITTPCGHNFCLKCFEKWAVGQGKLTCMICRSKIPRHVAKNPRINLALVSAIRLANVTKCSVEATAAKVHHIIRNQDRPEKAFTTERAVKTGKANAASGKFFVTIPRDHFGPIPAENDVTRKQGVLVGESWEDRQECRQWGAHFPHIAGIAGQSAVGAQSVALSGGYDDDEDHGEWFLYTGSGGRDLSGNKRINKKQSSDQAFKNMNESLRLSCKMGYPVRVVRSWKEKRSAYAPAEGVRYDGVYRIEKCWSNVGVQGSFKVCRYLFVRCDNEPAPWTSDEHGDRPRPLPNVPELETAADLFVRKESPSWDFDEAEGRWKWMKSPPVSRMALDPEERKKNKRAKNTMKARLLKEFSCQICREVLSLPVTTPCAHNFCKACLEAKFAGITQLRERSNGGRKLRAKKNIMTCPCCTTDLSEFLQNPQVNREMMEIIENFKKSEEEADASISEEEEEESEPPTKKIKMDNNSVGGSGTSLSA
Protein: Potassium channel KAT1 (Q39128)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Highly selective inward-rectifying potassium channel. This voltage-gated channel could mediate long-term potassium influx into guard cells leading to stomatal opening. Assuming opened or closed conformations in response to the voltage difference across the membrane, the channel is activated by hyperpolarization. The channel activity is enhanced upon external acidification. Also permeable to ammonium ions. Blocked by tetraethylammonium and barium ions.
Subcellular location: Membrane; Multi-pass membrane protein.
Interaction partners:
- IQ domain-containing protein IQM1
- Guard cell S-type anion channel SLAC1
- Serine/threonine-protein kinase SRK2E
- SEC12-like protein
Sequence:
MSISWTRNFFERFCVEEYNIDTIKQSSFLSADLLPSLGARINQSTKLRKHIISPFNPRYRAWEMWLVLLVIYSAWICPFQFAFITYKKDAIFIIDNIVNGFFAIDIILTFFVAYLDSHSYLLVDSPKKIAIRYLSTWFAFDVCSTAPFQPLSLLFNYNGSELGFRILSMLRLWRLRRVSSLFARLEKDIRFNYFWIRCTKLISVTLFAIHCAGCFNYLIADRYPNPRKTWIGAVYPNFKEASLWNRYVTALYWSITTLTTTGYGDFHAENPREMLFDIFFMMFNLGLTAYLIGNMTNLVVHWTSRTRTFRDSVRAASEFASRNQLPHDIQDQMLSHICLKFKTEGLKQQETLNNLPKAIRSSIANYLFFPIVHNIYLFQGVSRNFLFQLVSDIDAEYFPPKEDIILQNEAPTDLYILVSGAVDFTVYVDGHDQFQGKAVIGETFGEVGVLYYRPQPFTVRTTELSQILRISRTSLMSAMHAHADDGRVIMNNLFMKLRGQQSIAIDDSNTSGHENRDFKSMGWEEWRDSRKDGYGLDVTNPTSDTALMDAIHKEDTEMVKKILKEQKIERAKVERSSSETAGRSYANDSSKKDPYCSSSNQIIKPCKREEKRVTIHMMSESKNGKLILLPSSIEELLRLASEKFGGCNFTKITNADNAEIDDLDVIWDGDHLYFSSN
Protein: Cyclin-D-binding Myb-like transcription factor 1 (hDMTF1) (Cyclin-D-interacting Myb-like protein 1) (hDMP1) (Q9Y222)
Organism: Homo sapiens (Human)
Function: Transcriptional activator which activates the CDKN2A/ARF locus in response to Ras-Raf signaling, thereby promoting p53/TP53-dependent growth arrest (By similarity). Binds to the consensus sequence 5'-CCCG[GT]ATGT-3' (By similarity). Isoform 1 may cooperate with MYB to activate transcription of the ANPEP gene. Isoform 2 may antagonize transcriptional activation by isoform 1.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00625, ECO:0000269|PubMed:17936562}.
Interaction partners:
- G1/S-specific cyclin-D2
- Cellular tumor antigen p53
- Aminopeptidase N
Sequence:
MSTVEEDSDTVTVETVNSVTLTQDTEGNLILHCPQNEADEIDSEDSIEPPHKRLCLSSEDDQSIDDSTPCISVVALPLSENDQSFEVTMTATTEVADDEVTEGTVTQIQILQNEQLDEISPLGNEEVSAVSQAWFTTKEDKDSLTNKGHKWKQGMWSKEEIDILMNNIERYLKARGIKDATEIIFEMSKDERKDFYRTIAWGLNRPLFAVYRRVLRMYDDRNHVGKYTPEEIEKLKELRIKHGNDWATIGAALGRSASSVKDRCRLMKDTCNTGKWTEEEEKRLAEVVHELTSTEPGDIVTQGVSWAAVAERVGTRSEKQCRSKWLNYLNWKQSGGTEWTKEDEINLILRIAELDVADENDINWDLLAEGWSSVRSPQWLRSKWWTIKRQIANHKDVSFPVLIKGLKQLHENQKNNPTLLENKSGSGVPNSNTNSSVQHVQIRVARLEDNTAISSSPMAALQIPVQITHVSSADSPATVDSETITLNSGTLQTFEILPSFHLQPTGTPGTYLLQTSSSQGLPLTLTASPTVTLTAAAPASPEQIIVHALSPEHLLNTSDNVTVQCHTPRVIIQTVATEDITSSISQAELTVDSDIQSSDFPEPPDALEADTFPDEIHHPKMTVEPSFNDAHVSKFSDQNSTELMNSVMVRTEEEISDTDLKQEESPSDLASAYVTEGLESPTIEEQVDQTIDDETILIVPSPHGFIQASDVIDTESVLPLTTLTDPILQHHQEESNIIGSSLGSPVSEDSKDVEDLVNCH
Protein: Probable ATP-dependent RNA helicase DDX20 (EC 3.6.1.15) (EC 3.6.4.13) (Component of gems 3) (DEAD box protein 20) (DEAD box protein DP 103) (Gemin-3) (Q9UHI6)
Organism: Homo sapiens (Human)
Function: The SMN complex catalyzes the assembly of small nuclear ribonucleoproteins (snRNPs), the building blocks of the spliceosome, and thereby plays an important role in the splicing of cellular pre-mRNAs. Most spliceosomal snRNPs contain a common set of Sm proteins SNRPB, SNRPD1, SNRPD2, SNRPD3, SNRPE, SNRPF and SNRPG that assemble in a heptameric protein ring on the Sm site of the small nuclear RNA to form the core snRNP (Sm core). In the cytosol, the Sm proteins SNRPD1, SNRPD2, SNRPE, SNRPF and SNRPG are trapped in an inactive 6S pICln-Sm complex by the chaperone CLNS1A that controls the assembly of the core snRNP. To assemble core snRNPs, the SMN complex accepts the trapped 5Sm proteins from CLNS1A forming an intermediate. Binding of snRNA inside 5Sm triggers eviction of the SMN complex, thereby allowing binding of SNRPD3 and SNRPB to complete assembly of the core snRNP. May also play a role in the metabolism of small nucleolar ribonucleoprotein (snoRNPs).
Subcellular location: Cytoplasm {ECO:0000269|PubMed:10601333, ECO:0000305|PubMed:12095920}. Nucleus, gem {ECO:0000269|PubMed:10601333, ECO:0000305|PubMed:10383418}. Note=Localized in subnuclear structures next to coiled bodies, called Gemini of Cajal bodies (Gems). {ECO:0000269|PubMed:10601333}.
Interaction partners:
- Protein argonaute-2
- Gem-associated protein 2
- Gem-associated protein 6
- Gem-associated protein 5
- Gem-associated protein 4
- Gem-associated protein 7
- Survival motor neuron protein
- Serine-threonine kinase receptor-associated protein
- Gem-associated protein 8
- Small nuclear ribonucleoprotein-associated proteins B and B'
Sequence:
MAAAFEASGALAAVATAMPAEHVAVQVPAPEPTPGPVRILRTAQDLSSPRTRTGDVLLAEPADFESLLLSRPVLEGLRAAGFERPSPVQLKAIPLGRCGLDLIVQAKSGTGKTCVFSTIALDSLVLENLSTQILILAPTREIAVQIHSVITAIGIKMEGLECHVFIGGTPLSQDKTRLKKCHIAVGSPGRIKQLIELDYLNPGSIRLFILDEADKLLEEGSFQEQINWIYSSLPASKQMLAVSATYPEFLANALTKYMRDPTFVRLNSSDPSLIGLKQYYKVVNSYPLAHKVFEEKTQHLQELFSRIPFNQALVFSNLHSRAQHLADILSSKGFPAECISGNMNQNQRLDAMAKLKHFHCRVLISTDLTSRGIDAEKVNLVVNLDVPLDWETYMHRIGRAGRFGTLGLTVTYCCRGEEENMMMRIAQKCNINLLPLPDPIPSGLMEECVDWDVEVKAAVHTYGIASVPNQPLKKQIQKIERTLQIQKAHGDHMASSRNNSVSGLSVKSKNNTKQKLPVKSHSECGIIEKATSPKELGCDRQSEEQMKNSVQTPVENSTNSQHQVKEALPVSLPQIPCLSSFKIHQPYTLTFAELVEDYEHYIKEGLEKPVEIIRHYTGPGDQTVNPQNGFVRNKVIEQRVPVLASSSQSGDSESDSDSYSSRTSSQSKGNKSYLEGSSDNQLKDSESTPVDDRISLEQPPNGSDTPNPEKYQESPGIQMKTRLKEGASQRAKQSRRNLPRRSSFRLQTEAQEDDWYDCHREIRLSFSDTYQDYEEYWRAYYRAWQEYYAAASHSYYWNAQRHPSWMAAYHMNTIYLQEMMHSNQ
Protein: Photoreceptor cilium actin regulator (Q6PAC4)
Organism: Mus musculus (Mouse)
Function: Plays an essential role for normal photoreceptor cell maintenance and vision.
Subcellular location: Cell projection, cilium, photoreceptor outer segment {ECO:0000269|PubMed:25616964}. Photoreceptor inner segment {ECO:0000269|PubMed:25616964}.
Interaction partners:
Sequence:
MGCTPSHNVIVNSVAKSGIQFFKKPKAILPGCQWGSPKCPIPLLVQSSTFCDSGGELHLGERLVEETVSSSKKLQAMAEGVRQLPKAMEGLIPESQTFQVNKPQGHRATDISFRTEGSHGTQEVDFSGKESKENTPQETSKGNRESVCHQPDSQDHCRQSATESKGRVDFPEPLVKAHQHAYAYLHTSLSRYEAIVRLVQQASQTWGLLRPMLNFLLLCFEEAGQLLSEISKDGDVLLQEVRGDLAWPLRKGEPWEQHPDLLQQLLQYTVSKLRALHGTVAALTGSFLEGSSSCLRSTAGHLEGKLSTKRGIDECLLRALGQLESLTSSHGDAGLLGPPLCSEDSGIGADNESVHSVEKLGKQASWDFAAELGEWKPGTAAQVEARPSGHAWQEGPYWTGSDRPQDCPLSSPRIAKVQPAVQDEARSASTSGAGAEAVTSGPSEAAESLPWDSLGAEIPVRTPLSRSSGLTDAPSLSEEEDCSPEEEDELSSTDLHPEPQKALPSRPRSSPDTRESLFQPYSKELRNPQAQEMILKMKEAISERIKFVPEPSRPQDWTEEEEGGTVVPPRPRSVSGSRGGPERQRRSQSEGCLKSHVEDPTLQELRRVQTDLSRRLEVFYALGATRQGQSRERCLPSRASVLWPPTNCRVSPSSAISKFKASLTQNFSILPNQDKSIFQKGSPCFDGEQPCQGKAEKLPNAIFCGKKSGRAPRDNERDIRACPTRPSVKTLIETFSPTESLRMPRNCRNLGSSPCLRKWGVPAMPPRFPIYRGLAPLYSKPQISPAAGWRPSAPFPSLPLAEVSESEDISGDVEEDLENLPPPPLEVLMDKSFAALECPECSQPAGSSLEETLLPGLQEASHPKRTWVSPRLKASMSPMDLLPSKGSGSSPRLHSTRSGSTRIVGDSRKLTLDLNSKQTASPSSEAKSRAQIQARAETIAGFSKQHQKAIPWHHTNPTPGQSRTLEPSLARFSRDPHSSEASRKGPERSLPRVRKASPQRAQWASQGDRRLQSLPSSHGPSQPGLPAVLSSPSPPLSPRTLSPPATRKTTSPPCQHPQSNPAPGSPPVRRTETNTPSSASCSSPSVSPSRGSKDSIHSEDSEATTAKASRNTCSIFYPAATSLFEAKSSSSTSHPQMLPEPGGLLRTPTGGWRGSSGQRLRADSQKRTVLNALNPLPFVRRTASDRQRQQGDQLQQSRSDWEFHSCQNSSSSSSSEENPKQELPPWNNSRVPELQGSSTKRASPLELCVLGHGLQPEARMNRGQDRPQPESQPQHKEIS
Protein: Septin ring organizing protein mid2 (Q9P7Y8)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Responsible for the proper stability and function of septins during cytokinesis. Required for the correct formation of the medial septin ring structure in mitosis and for the proper localization of endo-glucanases agn1 and eng1, which are needed for efficient cell separation. May act as a landmark for the localization of hydrolytic proteins to the medial region.
Subcellular location: Cytoplasm, cell cortex {ECO:0000269|PubMed:12654901}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:12668659}. Note=Localizes to the medial ring at the cell cortex of dividing cells (PubMed:12654901). Initially forms a single ring, which subsequently splits into two distinct rings as the septum forms, and disappears as cells separate (PubMed:12654901). Requires septins for proper localization (PubMed:12654901).
Interaction partners:
- GTP-binding protein rho4
- Glucan endo-1,3-alpha-glucosidase agn1
- Riboflavin synthase
- Primary septum glucan endo-1,3-beta-D-glucosidase
- Septin homolog spn4
- Septin homolog spn1
- Protein adg1
- Metallothionein expression activator
- Serine/threonine-rich protein adg2
- Probable secreted beta-glucosidase adg3
Sequence:
MLMTASQQDQHAKMYLADIHRALRIPSPIPSTDYECSDYASTIASISRESTMRNFNRSNISSTAPSFAESEDAEDGDSFPYDQTLSNSSSFDDHQSLLPFSTEVRRTPTYSVMNETDSSSTSVEDVNKENILSLNDSCLIKLSDDEASNKSSRSSTPRNSIKSNSSNQGHGDIPIPKKNPARSVCNSKLFNEDTLPAEFEEVSISPPVKLELPTHSHNSSDTSFTNSIVSSVSDMVGLGEGINSIASFGFSEDSSSFQDIKTPPRLSFADENRENCRTDIYRSDSIHEYEEPLTSSITSLDSPHVLDENAPIPLLPKVVSLPDPRFTNVLSAFDALTRTYLLRQNSKVVHATSQKQEMQTSRRVVNSCYMPESLSRNLSSSLQQTGGSGRLFVRLMEIRNLTIPLASGMTTRFTYTISGKHIQVPWNALHSTTKIENEYTFDESISSSIVCTLRAAYDPPKVRTRSTLGKVFSTNKRKSMTTDPVSEALHGFVSEDGTFGEVTINTDSVSRTALGRCQSMVLPIMNKWTVDPAAKDVKPLPRKVGELEIHVFFLPALPVSLKELPASIESAMYDLKLAEWDRTLLCDGYLCQQGGDCPYWRRRYFQLIGSKLVAFQQFSKVRRATIDLSEATHIVDDNHYSDEEELEGYLYFESGFRIIFSNGDYIDFYAETVGEKDEWMSTLRQHLGQCSMVHKNWTKSFLSLSF
Protein: ACP53C14B (Q6GUS1)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MSVIKSIFLLSILAVCLIPRETEAQATINESWGRLGKCTQVAIETLTSLADKIVPTVYELKQCSGYVTLEPANGKDRKITWYLKVSYEFFKKLVFDEPKCLHGLLNKLAATIKPFAEQISGLGCLDEEDYII
Protein: Ras guanyl-releasing protein 3 (Q19770)
Organism: Caenorhabditis elegans
Interaction partners:
- Ras-related protein Rap-1
- Ras protein let-60
- Sex muscle abnormal protein 5
- Myosin-3
Sequence:
MSSKVEEDQHQELLTEDQLVARCVECFDVDEEDEVEDIEFVDALFLSHQWLSDSLSLITHFVNFYQETRNVEQREAVCRAVSFWIEKFPMHFDAQPQVCAQVVRLKTIAEDINENIRNGLDVSALPSFAWLRAVSVRNPLAKQTAFSLSFVQASPSDISTSLSHIDYRVLSRISITELKQYVKDGHLRSCPMLERSISVFNNLSNWVQCMILNKTTPKERAEILVKFVHVAKHLRKINNFNTLMSVVGGITHSSVARLAKTYAVLSNDIKKELTQLTNLLSAQHNFCEYRKALGACNKKFRIPIIGVHLKDLVAINCSGANFEKTKCISSDKLVKLSKLLSNFLVFNQKGHNLPEMNMDLINTLKVSLDIRYNDDDIYELSLRREPKTFMNFEPSRGLVFAEWASGVTVAPDNATVSKHISAMVDAVFKHYDHDRDGFISQEEFQLIAGNFPFIDAFVNIDVDMDGQISKDELKTYFMAANKNTKDLRRGFKHNFHETTFLTPTTCNHCNKLLWGILRQGFKCKDCGLAVHSCCKSNAVAECRRKSSSNLTRAAEWFASPRGSMRSRIINTCKRSSRPRTVSAVVTSPTTEKPTCSTKLSPPKLKDIRPQSESTEYYNSGSTPDEEIGLVSLACEEVFEDDDLADISSASYRTA
Protein: GTP-binding protein 1 (P32235)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Interaction partners:
- RWD domain-containing protein C1393.09c
- mRNA export protein 33
- Spindle pole body-associated protein cut12
- eIF-2-alpha kinase activator gcn1
- Elongation factor 3
- mRNA export factor elf1
- Small ribosomal subunit protein uS3
- ATP-dependent RNA helicase dbp9
- Small ribosomal subunit protein uS5
- Small ribosomal subunit protein uS10
Sequence:
MGVLEKIQEIEAEMRRTQKNKATEYHLGLLKGKLAKLRAQLLEPTSKSGPKGEGFDVLKSGDARVAFIGFPSVGKSTLLSAITKTKSATASYEFTTLTAIPGVLEYDGAEIQMLDLPGIIEGASQGRGGRQAVSAARTADLILMVLDATKAADQREKIEYELEQVGIRLNRQPPNVTLTIKKNGGIKFNHTVPLTHMDYKMAYNILHEYRIHNADILIREDITVDDFIDLVMGNRRYINCLYCYSKIDAVSLEEVDRLARLPKSVVISCNMKLNLDFLKERIWEELNLYRIYTKRKGEMPDFSEALIVRKGSTIEQVCNRIHRTLAEQLKYALVWGTSAKHSPQVVGLNHRVEEGDVVTIVTK
Protein: Cholinesterase, putative (AFU_orthologue AFUA_7G01710) (Q5ARF0)
Organism: Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Interaction partners:
Sequence:
MHGLVAALLCGLAVAAPSCPAPAPSLGTLQTLKYNYLSAQNNGTSAVLVHDQLSNAAAQTRCAAIGESLYPFASAPAANRTELAHQFDYLVYAQDLRRDQDVWVAGADAGKGGKGGDCQAYSPSQREVVSVPCDRRLPALCTANVPPTRDIDRTVVPSSKVTVSTAGYTLTGYRDARSFRFLGIPFADPPVGELRLAPPREYSGPKRIDATRLGASCIQSVSGFGASRDISEDCLYLNVFTPIVPERPGIVRKPVAVYFYGGAFTSGTASIIDYDGGNFASRNDLVVVTVNYRLGALGWLATGNLTTGSYGTRDQILALRWVQANIAAFGGDPSHVTIFGQSAGGQSVVALLSSTAARGLFSGALIQSAPVDLPWYTRQVYSELVVPHVAQAVGCGNATTESESALLRCLRSLPATSFLDNSTAFEAATSAIATDVADSYLHVSQLLASIEPFMPMVDDSDSASGVIDNQFHRLVSENTLPNRVPTFFTTTPDEAALYVNRLVPELGSAQSGLNTLLGLAYPPPLASALINATAFPTDTKQPDSVRIEGASALTHSEWSCPLAHLLRVAVPGTFPTLYSAQITDGHAQSNGSTPDICKPNAIYNATCHSNDVLPAWGTLNSKTIDVLPYYGLADLKHSQFLNDIFGSFFRSYDPNPDLDMLRLRGSAYEHTLNVFGAGYKIDEYTPAEKTVPLLGRLPGRTANPGVTEQCDVFEAYGYTFENAVFTEA
Protein: Abnormal cell lineage protein 44 (Wnt protein) (Q27886)
Organism: Caenorhabditis elegans
Function: Ligand for members of the frizzled family of seven transmembrane receptors (By similarity). Affects male tail development, vulval precursor cell specification and egg laying. Involved in morphogenesis by influencing polarity of asymmetric cell divisions of the B, U, and F cells in the male, and the T cell in males and hermaphrodites. Controls spindle orientation in B-gamma cell division during male copulatory spicule development. Involved in specification of the P7.p lineage during vulval development. Has a role in providing polarity and default lin-17 localization in axon development and positioning of neuromuscular synapses in DA9 regions by negatively regulating synaptogenesis. Plays a role in motorneuron development by promoting the extension of the anterior neurite of ventral D-type GABAergic motorneurons along the anterior-posterior axis of the ventral nerve cord. Positively regulates cilium position and dendrite morphogenesis in postembryonic PQR gas-sensing neurons. This is likely through regulating the localization of grdn-1 to the distal dendrites of PQR sensory neurons.
Subcellular location: Secreted, extracellular space, extracellular matrix {ECO:0000250|UniProtKB:P24383}.
Interaction partners:
- Frizzled-4
- Protein mom-5
- Frizzled-2
- Inactive tyrosine-protein kinase RYK
- DiSHevelled related
- Segment polarity protein dishevelled homolog mig-5
- Protein wntless homolog
- Frizzled-4
- Tyrosine-protein kinase receptor cam-1
- Beta-catenin/armadillo-related protein 1
Sequence:
MRAAPFDFFFQSTALSTFFILCSLATNEIPTISGAPAGKIVQPPKPNILKQGCPSDLLHSRALRSIQLACRTHPATVISAFEGVQEGLQNCANRLRFQQWDCSEAGNIMHDPPLLRQGFRESSLIWALSSASAAWGVATACAQGWIDDCACNNQMGQNEYEFGGCTHGVQHGITASRKLLTKVGAVNTLLRKVEKHNLKAGRLAIKKTLISSCKCHGVSGSCQQKTCWKRTATLEHITDYLVEKYARAKLYTDDSVVKTTDLIYLEASPDVCKAKSVAGRVCAWRNETHTQGDCDRLCCGNGFSIRHEVVRVKCDCEFVWCCNLVCKDCIQHRWISTCNGTPPKSLIF
Protein: Phosphatidate cytidylyltransferase (EC 2.7.7.41) (CDP-DAG synthase) (CDP-DG synthase) (CDP-diacylglycerol synthase) (CDS) (CDP-diglyceride pyrophosphorylase) (CDP-diglyceride synthase) (CTP:phosphatidate cytidylyltransferase) (P0ABG1)
Organism: Escherichia coli (strain K12)
Subcellular location: Cell inner membrane; Multi-pass membrane protein.
Interaction partners:
- Ditrans,polycis-undecaprenyl-diphosphate synthase
- CDP-diacylglycerol--glycerol-3-phosphate 3-phosphatidyltransferase
- 1-acyl-sn-glycerol-3-phosphate acyltransferase
- CDP-diacylglycerol--serine O-phosphatidyltransferase PssA
- Diacylglycerol kinase
- 1-deoxy-D-xylulose 5-phosphate reductoisomerase
- Uncharacterized protein YnbB
- Regulator of sigma-E protease RseP
- CDP-diacylglycerol pyrophosphatase
- Phosphatidylserine decarboxylase proenzyme
Sequence:
MLKYRLISAFVLIPVVIAALFLLPPVGFAIVTLVVCMLAAWEWGQLSGFTTRSQRVWLAVLCGLLLALMLFLLPEYHRNIHQPLVEISLWASLGWWIVALLLVLFYPGSAAIWRNSKTLRLIFGVLTIVPFFWGMLALRAWHYDENHYSGAIWLLYVMILVWGADSGAYMFGKLFGKHKLAPKVSPGKTWQGFIGGLATAAVISWGYGMWANLDVAPVTLLICSIVAALASVLGDLTESMFKREAGIKDSGHLIPGHGGILDRIDSLTAAVPVFACLLLLVFRTL
Protein: Acyclic sesquiterpene synthase ((3R,6E)-nerolidol synthase) (EC 4.2.3.49) ((R)-linalool synthase) (EC 4.2.3.26) (Beta-farnesene synthase) (EC 4.2.3.47) (Ent-kaurene synthase 2.1) (ZmKS2.1) (EC 4.2.3.19) (Farnesyl diphosphatase) (EC 3.1.7.6) (Geraniol synthase) (EC 3.1.7.11) (Terpene synthase 1) (ZmTPS1) (Q84ZW8)
Organism: Zea mays (Maize)
Function: Involved in the formation of (E)-beta-farnesene and (3E)-4,8-dimethyl-1,3,7-nonatriene, key signal molecules in induced plant defense mediated by the attraction of enemies of herbivores. In the presence of geranyl diphosphate, catalyzes the formation of the acyclic monoterpens (3R)-linalool and geraniol. However, the in vitro rate of sesquiterpene formation is about four times higher than the rate of monoterpene formation. Mediates the conversion of ent-copalyl diphosphate into ent-kaurene, thus having probably a role in gibberellin biosynthesis.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:Q6Q3H2}. Plastid, chloroplast {ECO:0000269|PubMed:26620527}.
Interaction partners:
- Farnesyl pyrophosphate synthase
- Alpha-copaene synthase
- (E)-beta-farnesene synthase ((+)-germacrene D synthase) ((E)-alpha-bergamotene synthase) (Alpha-copaene synthase) (Alpha-muurolene synthase) (Beta-bisabolene synthase) (Beta-caryophyllene synthase) (Delta-cadinene synthase) (Sesquiphellandrene synthase) (Sesquisabinene A synthase) (Terpene synthase 10) (Zingiberene synthase)
- Dihydroflavonol-4-reductase
- Alkyl transferase
- Dehydrodolichyl diphosphate synthase 6
- Alkyl transferase
- Farnesyl diphosphate synthase2
- Farnesol kinase chloroplastic
- Alkyl transferase
Sequence:
MAMPVKLTPASLSLKAVCCRFSSGGHALRFGSSLPCWRRTPTQRSTSSSTTRPAAEVSSGKSKQHDQEASEATIRQQLQLVDVLENMGISRHFAAEIKCILDRTYRSWLQRHEEIMLDTMTCAMAFRILRLNGYNVSSDELYHVVEASGLHNSLGGYLNDTRTLLELHKASTVSISEDESILDSIGSRSRTLLREQLESGGALRKPSLFKEVEHALDGPFYTTLDRLHHRWNIENFNIIEQHMLETPYLSNQHTSRDILALSIRDFSSSQFTYQQELQHLESWVKECRLDQLQFARQKLAYFYLSAAGTMFSPELSDARTLWAKNGVLTTIVDDFFDVAGSKEELENLVMLVEMWDEHHKVEFYSEQVEIIFSSIYDSVNQLGEKASLVQDRSITKHLVEIWLDLLKSMMTEVEWRLSKYVPTEKEYMINASLTFGLGPIVLPALYFVGPKISESIVKDPEYDELFKLMSTCGRLLNDVQTFEREYNEGKLNSVSLLVLHGGSMSISDAKRKLQKPIDTCRRDLLSLVLREESVVPRPCKELFWKMCKVCYFFYSTTDGFSSQVERAKEVDAVINEPLKLQGSHTLVSDV
Protein: Regulator of G-protein signaling 17 (RGS17) (Q9UGC6)
Organism: Homo sapiens (Human)
Function: Regulates G protein-coupled receptor signaling cascades, including signaling via muscarinic acetylcholine receptor CHRM2 and dopamine receptor DRD2. Inhibits signal transduction by increasing the GTPase activity of G protein alpha subunits, thereby driving them into their inactive GDP-bound form. Binds selectively to GNAZ and GNAI2 subunits, accelerates their GTPase activity and regulates their signaling activities. Negatively regulates mu-opioid receptor-mediated activation of the G-proteins (By similarity).
Subcellular location: Membrane {ECO:0000250|UniProtKB:Q9QZB0}. Synapse, synaptosome {ECO:0000250|UniProtKB:Q9QZB0}. Nucleus {ECO:0000250|UniProtKB:Q9QZB0}. Cytoplasm {ECO:0000250|UniProtKB:Q9QZB0}.
Interaction partners:
- Guanine nucleotide-binding protein subunit beta-5
- Guanine nucleotide-binding protein G
- Succinate--CoA ligase [GDP-forming] subunit beta, mitochondrial
- Rho guanine nucleotide exchange factor 1
- Rho guanine nucleotide exchange factor 11
- Regulator of G-protein signaling protein-like
- Beta-adrenergic receptor kinase 1
- Guanine nucleotide-binding protein subunit alpha-13
- Regulator of G-protein signaling 7-binding protein
- Guanine nucleotide-binding protein G
Sequence:
MRKRQQSQNEGTPAVSQAPGNQRPNNTCCFCWCCCCSCSCLTVRNEERGENAGRPTHTTKMESIQVLEECQNPTAEEVLSWSQNFDKMMKAPAGRNLFREFLRTEYSEENLLFWLACEDLKKEQNKKVIEEKARMIYEDYISILSPKEVSLDSRVREVINRNLLDPNPHMYEDAQLQIYTLMHRDSFPRFLNSQIYKSFVESTAGSSSES
Protein: Platelet endothelial aggregation receptor 1 (hPEAR1) (Multiple epidermal growth factor-like domains protein 12) (Multiple EGF-like domains protein 12) (Q5VY43)
Organism: Homo sapiens (Human)
Function: When overexpressed, reduces the number of both early and late non-adherent myeloid progenitor cells.
Subcellular location: Cell membrane {ECO:0000269|PubMed:15851471}; Single-pass membrane protein {ECO:0000255}. Cell projection, lamellipodium {ECO:0000269|PubMed:36792666}. Note=Detected on the cell surface in resting platelets. {ECO:0000269|PubMed:15851471}.
Interaction partners:
- SHC-transforming protein 2
Sequence:
MSPPLCPLLLLAVGLRLAGTLNPSDPNTCSFWESFTTTTKESHSRPFSLLPSEPCERPWEGPHTCPQPTVVYRTVYRQVVKTDHRQRLQCCHGFYESRGFCVPLCAQECVHGRCVAPNQCQCVPGWRGDDCSSECAPGMWGPQCDKPCSCGNNSSCDPKSGVCSCPSGLQPPNCLQPCTPGYYGPACQFRCQCHGAPCDPQTGACFCPAERTGPSCDVSCSQGTSGFFCPSTHSCQNGGVFQTPQGSCSCPPGWMGTICSLPCPEGFHGPNCSQECRCHNGGLCDRFTGQCRCAPGYTGDRCREECPVGRFGQDCAETCDCAPDARCFPANGACLCEHGFTGDRCTDRLCPDGFYGLSCQAPCTCDREHSLSCHPMNGECSCLPGWAGLHCNESCPQDTHGPGCQEHCLCLHGGVCQATSGLCQCAPGYTGPHCASLCPPDTYGVNCSARCSCENAIACSPIDGECVCKEGWQRGNCSVPCPPGTWGFSCNASCQCAHEAVCSPQTGACTCTPGWHGAHCQLPCPKGQFGEGCASRCDCDHSDGCDPVHGRCQCQAGWMGARCHLSCPEGLWGVNCSNTCTCKNGGTCLPENGNCVCAPGFRGPSCQRSCQPGRYGKRCVPCKCANHSFCHPSNGTCYCLAGWTGPDCSQPCPPGHWGENCAQTCQCHHGGTCHPQDGSCICPLGWTGHHCLEGCPLGTFGANCSQPCQCGPGEKCHPETGACVCPPGHSGAPCRIGIQEPFTVMPTTPVAYNSLGAVIGIAVLGSLVVALVALFIGYRHWQKGKEHHHLAVAYSSGRLDGSEYVMPDVPPSYSHYYSNPSYHTLSQCSPNPPPPNKVPGPLFASLQNPERPGGAQGHDNHTTLPADWKHRREPPPGPLDRGSSRLDRSYSYSYSNGPGPFYNKGLISEEELGASVASLSSENPYATIRDLPSLPGGPRESSYMEMKGPPSGSPPRQPPQFWDSQRRRQPQPQRDSGTYEQPSPLIHDRDSVGSQPPLPPGLPPGHYDSPKNSHIPGHYDLPPVRHPPSPPLRRQDR
Protein: Pyruvate kinase (PK) (EC 2.7.1.40) (P78031)
Organism: Mycoplasma pneumoniae (strain ATCC 29342 / M129 / Subtype 1) (Mycoplasmoides pneumoniae)
Interaction partners:
- Large ribosomal subunit protein uL16
- Large ribosomal subunit protein uL10
- Large ribosomal subunit protein uL24
- Large ribosomal subunit protein uL5
- Large ribosomal subunit protein uL23
- Large ribosomal subunit protein uL2
- Large ribosomal subunit protein uL14
- Large ribosomal subunit protein uL3
- Large ribosomal subunit protein uL18
- Large ribosomal subunit protein uL6
Sequence:
MIHHLKRTKIIATCGPALTKKLWTLAMLDDPAYAAMKAEAYANIENIIKNGVTVIRLNFSHGNHEEQAVRIKIVRDVAKKLNLPVSIMLDTNGPEIRVFETAPEGLKILKDSEVVINTTTKEVAKNNQFSVSDASGTYNMVNDVKVGQKILVDDGKLSLVVKRIDTKNNQVICVAQNDHTIFTKKRLNLPNADYSIPFLSAKDLRDIDFGLTHQIDYIAASFVNTTENIKQLRDYLASKNAKHVKLIAKIESNHALNNIDGIIKASDGIMVARGDLGLEIPYYKVPYWQRYMIKACRFFNKRVITATQMLDSLEKNIQPTRAEVTDVYFAVDRGNDATMLSGETANGAFPLNAVYVMKMIDKQSETFFDYQYNLNYYMANSKARHSEFWKQVVLPLAQKTAPKRKLINSDFKYDFVVHATNNLNEIYALSNARLAAAVIILTNDPQVYTGHGVDYGIFPYLIDQKPQSLSKAEFKSLANVAIKHYQQHGEISQLKQCLGVFHNKIISL
Protein: AmpE protein (G3XD69)
Organism: Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Interaction partners:
- 1,6-anhydro-N-acetylmuramyl-L-alanine amidase AmpD
- DUF2066 domain-containing protein
- Mannuronan C5-epimerase
- Aminopeptidase
- Lipoprotein
Sequence:
MTFLVLLLALALEKFSGWRRRIQRDGAWLAWLSLVEDLPSVSRRSWLGLLLAVVLPLLPLALLLTLLQSLAYGWLSLPLHLLVVVYSLGRGDVMADLGPFRDAWRREEAQAAFHVAERDLGILGGSESELIGRVHGHLLWQGYQSFFAVIFWYALLGPVAALAYRLLALALEHARQPALREQAARVRHILDWLPVRALVLSFALVGNFLAVIRVLLHWLLAWDISAAALLGKAGRVASDVEAVELGAAGVASLDALWQLLVRAAVLWYAVFAFCALFL