wanglab/gogpt-training-data huggingface dataset:
Protein: Phosphotransferase (EC 2.7.1.-) (Q9W330)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Glucose-6-phosphate isomerase
- ATP-dependent 6-phosphofructokinase
- Phosphoglucomutase 1
- Fructose-1,6-bisphosphatase isozyme 2
- Probable glucosamine 6-phosphate N-acetyltransferase
- mannose-6-phosphate isomerase
- Glucosamine-6-phosphate deaminase
- FI19814p1
- Phosphoglucomutase 2b
- Phosphoglucomutase 2a
Sequence:
MDRELNGAMKSVSINSAQLNGHNNGGGLDETDRVGVAQGAALSATEKITTTTAAATKSATATTNATTATATTTNLTTHSPQQIALLSAAEKSKMVHELCQQLLLTDEQVQELCYRILHELRRGLAKDTHPKANVKCFVTYVQDLPNGNERGKFLALDLGGTNFRVLLIHLQENNDFQMESRIYAIPQHIMIGSGTQLFDHIAECLSNFMAEHNVYKERLPLGFTFSFPLRQLGLTKGLLETWTKGFNCAGVVNEDVVQLLKDAIARRGDVQIDVCAILNDTTGTLMSCAWKNHNCKIGLIVGTGANACYMERVEEAELFAAEDPRKKHVLINTEWGAFGDNGALDFVRTEFDRDIDVHSINPGKQTFEKMISGMYMGELVRLVLVKMTQAGILFNGQDSEVLNTRGLFFTKYVSEIEADEPGNFTNCRLVLEELGLTNATDGDCANVRYICECVSKRAAHLVSAGIATLINKMDEPTVTVGVDGSVYRFHPKFHNLMVEKISQLIKPGITFDLMLSEDGSGRGAALVAAVACREDILNGKK
Protein: GRF1-interacting factor 2 (AtGIF2) (Transcription coactivator GIF2) (Q9MAL9)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Transcription coactivator that plays a role in the regulation of cell expansion in leaf and cotyledons tissues (By similarity). Component of a network formed by miR396, the GRFs and their interacting factors (GIFs) acting in the regulation of meristem function, at least partially through the control of cell proliferation (By similarity). GIFs are involved in the positive regulation of cell proliferation of lateral organs in a functionally redundant manner.
Interaction partners:
- Growth-regulating factor 1
- Growth-regulating factor 4
- Growth-regulating factor 5
- Cytochrome P450 78A5
- Growth-regulating factor 2
Sequence:
MQQQQSPQMFPMVPSIPPANNITTEQIQKYLDENKKLIMAIMENQNLGKLAECAQYQALLQKNLMYLAAIADAQPPPPTPGPSPSTAVAAQMATPHSGMQPPSYFMQHPQASPAGIFAPRGPLQFGSPLQFQDPQQQQQIHQQAMQGHMGIRPMGMTNNGMQHAMQQPETGLGGNVGLRGGKQDGADGQGKDDGK
Protein: POU domain, class 5, transcription factor 1 (POU domain protein 2) (Q90270)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Function: Involved in early development of embryos, especially in the process of gastrulation. May play an important role in establishing and specifying rhombomeric segments. Seems to be required to maintain the cells in a highly undifferentiated state. In contrast to POU2, T-POU2 lacks DNA-binding activity because of its incomplete pou domain structure. Overexpression of POU2 does not have any effect on development, whereas overexpression of t-POU2 causes developmental retardation or arrest before gastrulation.
Subcellular location: Nucleus.
Interaction partners:
- Kruppel-like factor 4.
- Transcription factor Sox-2
- Biklf
- Nanog
- Protein lin-28 homolog A
- Transcriptional regulator Myc-A
- Spalt-like transcription factor 4.
- SRY-box containing gene 17
- Catenin beta-1
- Estrogen-related receptor beta.
Sequence:
MTERAQSPTAADCRPYEVNRAMYPQAAGLDGLGGASLQFAHGMLQDPSLIFNKAHFNGITPATAQTFFPFSGDFKTNDLQGGDFTQPKHWYPFAAPEFTGQVAGATAATQPANISPPIGETREQIKMPSEVKTEKDVEEYGNEENKPPSQYHLTAGTSSIPTGVNYYTPWNPNFWPGLSQITAQANISQAPPTPSASSPSLSPSPPGNGFGSPGFFSGGTAQNIPSAQAQSAPRSSGSSSGGCSNSEEEETLTTEDLEQFAKELKHKRITLGFTQADVGLALGNLYGKMFSQTTICRFEALQLSFKNMCKLKPLLQRWLNEAENSENPQDMYKIERVFVDTRKRKRRTSLEGTVRSALESYFVKCPKPNTLEITHISDDLGLERDVVRVWFCNRRQKGKRLALPFDDECVEAQYYEQSPPPPPHMGGTVLPGQGYPGPAHPGGAPALYMPSLHRPDVFKNGFHPGLVGHLNS
Protein: Ripening-related protein-like; hydrolase-like (Q9LTI1)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
Sequence:
MIFRTTRFAVSGEMEFVNSSPPRYECLLFDLDDTLYPLSSGLSDACSNNIIEYMVEKLGIDEDGVVELNQILYKKYGTSMAGLKAVGYEFDNDEYHRYVHGRLPYENLKPDPVLRSLLLGLPLRKLVFSNGDEVHVMKALTRLGIEDCFERIISFETLNPDINEAELSCVTGHLPENPVICKPTEIAFEKAFDIAQLNPHKTLFFDDSTRNIQTGKAVGLHTVLVGKSEKIDGSDYALESIHNMKEAFPELWSESIINNKETERIDYASQISIETSVQA
Protein: Troponin C, slow skeletal and cardiac muscles (Q4PP99)
Organism: Rattus norvegicus (Rat)
Interaction partners:
- Troponin I, cardiac muscle
- Troponin T, cardiac muscle
- Troponin I, slow skeletal muscle
- Troponin I, fast skeletal muscle
- Troponin T, slow skeletal muscle
- Troponin T, fast skeletal muscle
- Troponin C, skeletal muscle
- Myosin regulatory light chain 2, ventricular/cardiac muscle isoform
- Tropomyosin alpha-1 chain
- Myosin-6
Sequence:
MDDIYKAAVEQLTEEQKNEFKAAFDIFVLGAEDGCISTKELGKVMRMLGQNPTPEELQEMIDEVDEDGSGTVDFDEFLVMMVRCMKDDSKGKSEEELSDLFRMFDKNADGYIDLDELKMMLQATGETITEDDIEELMKDGDKNNDGRIDYDEFLEFMKGVE
Protein: Protein phosphatase PHLPP-like protein (EC 3.1.3.16) (PH domain leucine-rich repeat protein phosphatase) (dPHLPP) (Q9VJ07)
Organism: Drosophila melanogaster (Fruit fly)
Function: Protein phosphatase that specifically mediates dephosphorylation of 'Ser-586' of Akt1, a protein that regulates the balance between cell survival and apoptosis through a cascade that primarily alters the function of transcription factors that regulate pro- and antiapoptotic genes. Dephosphorylation of 'Ser-586' of Akt1 triggers apoptosis and suppression of tumor growth.
Interaction partners:
- Adenylyl cyclase-associated protein
- RAC serine/threonine-protein kinase
- CG9617 protein
- Ubiquitin carboxyl-terminal hydrolase 12/46 homolog
- cAMP-dependent protein kinase type II regulatory subunit
- cAMP-dependent protein kinase type I regulatory subunit
Sequence:
MLKATRKQADPYKSKLKVSASHSGPHPLPVEVTAAEEEQAATFGQTSPQKLSLKGSQLGGSILIGNYNYLTQLEVCENEMEVLDLSSLAQLETLKCSRNKLMELIINGTNLQTLVADHNYLHNISTTNTHPVPLKLQRIDISHNNFSELPNWVGACASLTAINASHNRLNNVAVLLRNYRITELVSLDLAYNDLKQLDQFPEGFSSIRSLQLQSNELPSLPDNFFAVTHARLETLNVSCNKLSTLPRYEQNNHAALVNLSLAGNHLNDSIFEPLHNAAKLRVLHLAYNRIGVLPAACVRNWPELEILVLSGNMLQQLPEEVATLGQLRVLRCCNNLLLCTPQLAKLAMLKVLDLSHNHLDRVNLLALVPSRNLKYLDLSGNLQLQVDEQQFKVCQSQSQRHWSLVDVSGNNRAALPTTKIRQVSAQRNQNKTSGPWTMGFAETPGSGDCRKLSVYQLRAANYGGSDEALYGMFEALEGRGRAAQEMSHLVPDLMKQEQMVKDSAVRDYMKFTLLAAQQQCGSVRSAALFHLTRTRAPSKVRPLKSKRYVLRMASTGGLDAYLIRRTSQLRLTKPDVIQKDQIHSMPDPHVLELILSNDDEYLVVGNAQLWSVMDIDRAAREIRKEENSLLAAKRLVDIAQSFAAAESLSVIVVRFRHLGTDVDHLIRELKQSVRKKPQPVSLPLSSGSVCKRTCCDRSNACRHRAIEQEPLAGRSSPSGQSDRDLLAKDKDDEFVLAHARVLQEEQQLEMLDETESVSESVLSEEQFKCWEYMLEQNTQLLFDKELNTISKSFTKQRTVPNAIMAATVLPERNDFTSNLMRTVTNKFISTSTPQLPQPITTSVPLGSYHQVKQAPPGHFGSALSFQQAHSYGYNLFDAKPRPKFHGGTVKRSAGPNSAYFGSLQRLMPYNFEYDFAVTQERERNILDEEEHDDDDFNEHESRMRKYWGVATTEL
Protein: Lipid phosphate phosphatase 1 (EC 3.6.1.75) (Lysophosphatidate phosphatase) (EC 3.1.3.106) (Phosphatidate phosphatase) (EC 3.1.3.4) (Q04396)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Catalyzes the dephosphorylation of diacylglycerol diphosphate (DGPP) to phosphatidate (PA) and the subsequent dephosphorylation of PA to diacylglycerol (DAG). Together with DPP1, regulates intracellular DGPP and PA levels which are phospholipid molecules believed to play a signaling role in stress response. Can also use lysophosphatidic acid (LPA) as a substrate. Substrate preference is PA > DGPP > LPA.
Subcellular location: Golgi apparatus membrane {ECO:0000269|PubMed:14562095}; Multi-pass membrane protein {ECO:0000269|PubMed:14562095}.
Interaction partners:
- Phosphatidic acid phosphohydrolase 1
- Transmembrane 9 superfamily member 3
- Diacylglycerol O-acyltransferase 1
- Phospholipid:diacylglycerol acyltransferase
- CTP-dependent diacylglycerol kinase 1
- Lysophospholipid acyltransferase
- Triacylglycerol lipase 3
- Cholinephosphotransferase 1
- Phospholipase D1
- 1-acyl-sn-glycerol-3-phosphate acyltransferase
Sequence:
MISVMADEKHKEYFKLYYFQYMIIGLCTILFLYSEISLVPRGQNIEFSLDDPSISKRYVPNELVGPLECLILSVGLSNMVVFWTCMFDKDLLKKNRVKRLRERPDGISNDFHFMHTSILCLMLIISINAALTGALKLIIGNLRPDFVDRCIPDLQKMSDSDSLVFGLDICKQTNKWILYEGLKSTPSGHSSFIVSTMGFTYLWQRVFTTRNTRSCIWCPLLALVVMVSRVIDHRHHWYDVVSGAVLAFLVIYCCWKWTFTNLAKRDILPSPVSV
Protein: Gastrulation brain homeo box 2 (Gastrulation brain homeobox 2) (Homeobox protein GBX-2) (Transcription factor Gbx2) (Q8QGU1)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123, ECO:0000256|PROSITE-ProRule:PRU00108, ECO:0000256|RuleBase:RU000682}.
Interaction partners:
- Fibroblast growth factor 8
- Protein Wnt-1
- Paired box protein Pax-2a
- Odd-paired-like)
- Homeobox protein OTX2
Sequence:
MSAAFSTPFMMMQRPVGSTTAFSIDSLIGGPPQPSPGHFVYTGYPMFMPYRSVVLPPPPPPPPPTLPQSALPTTHPHHPIPGLPSSFCSSLAQGMALTSTLMATLPGGFSSSPSQQHQDAARKLGSQSIHAMFDKSQDIRLDGEDGKTFATKDSTSIPSFHDSQSVHTSTVRGHSKDDSKEDDCHRKDESFSMDSDLDYSSDDNGPGNAMCQKEDGDGSGGLDDGVHGGNGAGNTTSTGKNRRRRTAFTSEQLLELEKEFHCKKYLSLTERSQIAHALKLSEVQVKIWFQNRRAKWKRVKAGNVNSKTGEPSRNPKIVVPIPVHVSRFAIRSQHQQLEQARP
Protein: Cytochrome P450 monooxygenase pkfB (EC 1.-.-.-) (Aspernidine A biosynthesis cluster protein pkfB) (C8VI81)
Organism: Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Function: Cytochrome P450 monooxygenase; part of the gene cluster that mediates the biosynthesis of aspernidine A, a prenylated isoindolinone. The starting point of the biosynthesis of aspernidin A is the production of orsellinaldehyde by the non-reducing polyketide synthase pkfA. Hydroxylation, methylation of one of the phenol groups, and prenylation, presumably catalyzed by the prenyltransferase pkfE, would be needed to yield aspernidine D (Probable). Subsequently, the cytochrome P450 monooxygenase pkfB is responsible for hydroxylation of aspernidine D to yield aspernidine E. The dehydrogenase pkfF may be responsible for further oxidation of aspernidine E to form a dialdehyde intermediate which is further transformed in a series of steps, some of which are enzyme-mediated, to generate aspernidine A (Probable). The possibility that additional enzymes outside of the cluster are involved in aspernidine A biosynthesis cannot be excluded (Probable).
Subcellular location: Membrane {ECO:0000255}; Single-pass membrane protein {ECO:0000255}.
Interaction partners:
Sequence:
MDHPHPSTFSLGLSQILVCLALLYAAIHILSVYRRLCHISGPFWARISNLPRVWWVNTSRAHEIHQQLHEKYGDVVRFGPNMVSLRNPTWIPTVYPTRMGVKKSDFYRTLAPYTPSGALPAVFSSRDEEVHRGLRGPIASLYSMSKVLPLEVFVDRTIDVLVRQLDGRFAGAGETFDLASWLQFFAFDVMGTLTFSKRYGFLEKGMDVHGMLDTIWRFLKGAAPFTQIPWVDEIWNKNVLATKLKGATGVSILGIVGKFVSQRQEESKAGKIDGTADRDMLSLFMEIQKNNQLPPWYVTAWTFSNITAGSDSAAVVMRTVFYNLLSHPSTLQKLRSELLSAGPLTQPYPSWKDVCNLPYLDACILEALRLHPPFCLPFERIVPQGGMVLGDTYFPEGTVVGMSPWVVNRHKPTFGEDSDVWNPERWMVSKELKSKREAAVLTFGAGRRVCLGRHIAILELKKIVPALVLRYDFELIDPERFTTENFWFFRQRGMDVRVKKRMQAEAGI
Protein: non-specific serine/threonine protein kinase (EC 2.7.11.1) (Q6IS31)
Organism: Mus musculus (Mouse)
Subcellular location: Cytoplasm, cytosol {ECO:0000256|ARBA:ARBA00004514}. Mitochondrion inner membrane {ECO:0000256|ARBA:ARBA00004434}; Single-pass membrane protein {ECO:0000256|ARBA:ARBA00004434}. Mitochondrion outer membrane {ECO:0000256|ARBA:ARBA00004572}; Single-pass membrane protein {ECO:0000256|ARBA:ARBA00004572}.
Interaction partners:
Sequence:
APVTAPPWRCDRHWAEAWGRGELPGRVVSPGAQPRPVGLPLPDRYRFFRQSVAGLAARIQRQFMVRARGGAGPCGRAVFLAFGLGLGLIEEKQAEGRRAASACQEIQAIFTQKTKRVSDPLDTRCWQGFRLEDYLIGQAIGKGCNAAVYEATMPTLPQHLEKAKHLGLIGKGPDVVLKGADGEQAPGTPTFPFAIKMMWNISAGSSSEAILSKMSQELVPASRVALDGEYGAVTYRRSRDGPKQLAPHPNIIRVFRAFTSSVPLLPGALADYPDMLPPHYYPEGLGHGRTLFLVMKNYPCTLRQYLEEQTPSSRLATMMTLQLLEGVDHLVQQGIAHRDLKSDNILVEWDSDGCPWLVISDFGCCLADQHVGLRLPFNSSSVERGGNGSLMAPEVSTAHSGPSAVIDYSKADTWAVGAIAYEIFGLANPFYGQGSAHLESRSYQEAQLPEMPKSVPPEARRLVRSLLQREASKRPSARLAANVLHLSLWGEHLLALKNLKLDKMIAWLLQQSAATLLADRLREKSCVETKLQMLFLANLECEALCQAALLLSSWRAAP
Protein: Tubulin beta-2 chain (Beta-2-tubulin) (P52275)
Organism: Caenorhabditis elegans
Function: Tubulin is the major constituent of microtubules, a cylinder consisting of laterally associated linear protofilaments composed of alpha- and beta-tubulin heterodimers. Microtubules grow by the addition of GTP-tubulin dimers to the microtubule end, where a stabilizing cap forms. Below the cap, tubulin dimers are in GDP-bound state, owing to GTPase activity of alpha-tubulin.
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:Q13509}.
Interaction partners:
- Tubulin alpha-2 chain
- Tubulin alpha chain
- Tubulin alpha-3 chain
- Tubulin alpha chain
- Tubulin alpha chain
- Dynein heavy chain, cytoplasmic
- Protein unc-119
- Serine/threonine-protein kinase zyg-8
- Tubulin alpha chain
- Tubulin alpha chain
Sequence:
MREIVHVQAGQCGNQIGSKFWEVISDEHGIQPDGTFKGETDLQLERIDVYYNEANNGKYVPRAVLVDLEPGTMDSVRSGPFGQLFRPDNFVFGQSGAGNNWAKGHYTEGAELVDNVLDVIRKEAEGCDCLQGFQLTHSLGGGTGSGMGTLLISKIREEYPDRIMSSFSVVPSPKVSDTVVEPYNATLSVHQLVENTDETYCIDNEALYDICYRTLKLTNPTYGDLNHLVSLTMSGVTTCLRFPGQLNADLRKLAVNMVPFPRLHFFMPGFAPLSAKGTQAYRALTVAELTQQMFDAKNMMAACDPRHGRYLTVAAMFRGRMSMREVDEQMLNVQNKNSSYFVEWIPNNVKTAVCDIPPRGLKMAATFVGNSTAIQELFKRISEQFTAMFRRKAFLHWYTGEGMDEMEFTEAESNMNDLISEYQQYQEATAEDDVDGYAEGEAGETYESEQ
Protein: Protein canopy homolog 4 (Protein associated with Tlr4) (Q8BQ47)
Organism: Mus musculus (Mouse)
Function: Plays a role in the regulation of the cell surface expression of TLR4.
Subcellular location: Secreted {ECO:0000305}.
Interaction partners:
- Protein canopy homolog 2
Sequence:
MCGLRFIMGPVRLEILLFILAAYGAWAEATKEEEDDTERLPSKCEVCKLLSMELQEALSRTGRSREVLELGQVLDTGKRKRHVPYSLSETRLEEALENLCERILDYNVHAERKGSLRYAKGQSQTMATLKGLVQKGVKVDLGIPLELWDEPSVEVTFLKKQCETMLEEFEDVVGDWYFHHQEQPLQHFLCERHVLPASETACLREAWTGKEKISDGQEEADDEEEEEEEEITKTSGNPKHDPEDL
Protein: Fibulin-7 (FIBL-7) (Protein TM14) (Q501P1)
Organism: Mus musculus (Mouse)
Function: An adhesion molecule that interacts with extracellular matrix molecules in developing teeth and may play important roles in differentiation and maintenance of odontoblasts as well as in dentin formation.
Subcellular location: Secreted, extracellular space, extracellular matrix.
Interaction partners:
Sequence:
MGPGSQRALFLLLLLLASPGARAFQSCLNKQQLLTTIRQLQQLLKGQETRFTEGIRNMKSRLAALQNTVNKMTPDAPPVSCPALEAPPDGKKFGSKYLVDHEVYFTCNPGFQLVGPSSVVCLANGSWTGEQPRCRDISECSSQPCHNGGTCVEGINHYRCICPPGKTGNRCQHQTQAAAPDGGEAGDPAFSRAPRCAQVEREQHCSCEAGFHLSSTTGGHSVCQDVNECEIYGQKGRPRLCMHACVNTPGSYRCTCPSGYRILADGKSCEDVDECAGPQHMCPRGTTCINTGGGFQCVNPECPEGSGNISYVKTSPFQCERNPCPMDSRPCRHLPKTISFHYLSLPSKLKTPITLFRMATASIPGHPGPNSLRFGIVGGNSRGHFVMQRSDRQTGELILTQTLEGPQTLEVDVDMSEYLERSFQANHVSKVTIFVSRYDF
Protein: Fanconi anemia group D2 protein homolog (Protein FACD2) (Q80V62)
Organism: Mus musculus (Mouse)
Function: Required for maintenance of chromosomal stability. Promotes accurate and efficient pairing of homologs during meiosis. Involved in the repair of DNA double-strand breaks, both by homologous recombination and single-strand annealing. May participate in S phase and G2 phase checkpoint activation upon DNA damage. Plays a role in preventing breakage and loss of missegregating chromatin at the end of cell division, particularly after replication stress (By similarity). Promotes BRCA2/FANCD1 loading onto damaged chromatin. May also be involved in B-cell immunoglobulin isotype switching.
Subcellular location: Nucleus {ECO:0000250}. Note=Concentrates in nuclear foci during S phase and upon genotoxic stress. {ECO:0000250}.
Interaction partners:
- E3 ubiquitin-protein ligase FANCL
- Breast cancer type 2 susceptibility protein homolog
- Fanconi anemia group A protein homolog
- Fanconi anemia group G protein homolog
- Fanconi anemia group I protein homolog
- Breast cancer type 1 susceptibility protein homolog
- Fanconi anemia group C protein homolog
- Fanconi anemia, complementation group E
- Fanconi-associated nuclease 1
- Fanconi anemia group F protein
Sequence:
MISKRRRLDSEDKENLTEDASKTMPLSKLAKKSHNSHEVEENGSVFVKLLKASGLTLKTGENQNQLGVDQVIFQRKLFQALRKHPAYPKVIEEFVNGLESYTEDSESLRNCLLSCERLQDEEASMGTFYSKSLIKLLLGIDILQPAIIKMLFEKVPQFLFESENRDGINMARLIINQLKWLDRIVDGKDLTAQMMQLISVAPVNLQHDFITSLPEILGDSQHANVGKELGELLVQNTSLTVPILDVFSSLRLDPNFLSKIRQLVMGKLSSVRLEDFPVIVKFLLHSVTDTTSLEVIAELRENLNVQQFILPSRIQASQSKLKSKGLASSSGNQENSDKDCIVLVFDVIKSAIRYEKTISEAWFKAIERIESAAEHKALDVVMLLIIYSTSTQTKKGVEKLLRNKIQSDCIQEQLLDSAFSTHYLVLKDICPSILLLAQTLFHSQDQRIILFGSLLYKYAFKFFDTYCQQEVVGALVTHVCSGTEAEVDTALDVLLELIVLNASAMRLNAAFVKGILDYLENMSPQQIRKIFCILSTLAFSQQPGTSNHIQDDMHLVIRKQLSSTVFKYKLIGIIGAVTMAGIMAEDRSVPSNSSQRSANVSSEQRTQVTSLLQLVHSCTEHSPWASSLYYDEFANLIQERKLAPKTLEWVGQTIFNDFQDAFVVDFCAAPEGDFPFPVKALYGLEEYSTQDGIVINLLPLFYQECAKDASRATSQESSQRSMSSLCLASHFRLLRLCVARQHDGNLDEIDGLLDCPLFLPDLEPGEKLESMSAKDRSLMCSLTFLTFNWFREVVNAFCQQTSPEMKGKVLSRLKDLVELQGILEKYLAVIPDYVPPFASVDLDTLDMMPRSSSAVAAKNRNKGKTGGKKQKADSNKASCSDTLLTEDTSECDMAPSGRSHVDKESTGKEGKTFVSLQNYRAFFRELDIEVFSILHSGLVTKFILDTEMHTEATEVVQLGPAELLFLLEDLSQKLENMLTAPFAKRICCFKNKGRQNIGFSHLHQRSVQDIVHCVVQLLTPMCNHLENIHNFFQCLGAEHLSADDKARATAQEQHTMACCYQKLLQVLHALFAWKGFTHQSKHRLLHSALEVLSNRLKQMEQDQPLEELVSQSFSYLQNFHHSVPSFQCGLYLLRLLMALLEKSAVPNQKKEKLASLAKQLLCRAWPHGEKEKNPTFNDHLHDVLYIYLEHTDNVLKAIEEITGVGVPELVSAPKDAASSTFPTLTRHTFVIFFRVMMAELEKTVKGLQAGTAADSQQVHEEKLLYWNMAVRDFSILLNLMKVFDSYPVLHVCLKYGRRFVEAFLKQCMPLLDFSFRKHREDVLSLLQTLQLNTRLLHHLCGHSKIRQDTRLTKHVPLLKKSLELLVCRVKAMLVLNNCREAFWLGTLKNRDLQGEEIISQDPSSSESNAEDSEDGVTSHVSRNRATEDGEDEASDEQKDQDSDESDDSSS
Protein: Exocyst complex component SEC10 (Q06245)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
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 SEC5
- Exocyst complex component SEC6
- Exocyst complex component SEC15
- Exocyst complex component SEC8
- Exocyst complex component SEC3
- Exocyst complex component EXO84
- Exocyst complex component EXO70
- Ras-related protein SEC4
- Protein transport protein SEC9
- Protein transport protein SEC1
Sequence:
MNSLYELDPKWKKLLKTDNFLGGLTVNEFVQELSKDHRNDVLIDANTKNLPTNEKDQDAIREAIWKQLDPKPYIRTFESTLKELKNLNEETLNKRQYFSEQVATQEVIHSENVIKLSKDLHTTLLTFDKLDDRLTNVTQVVSPLGDKLETAIKKKQNYIQSVELIRRYNDFYSMGKSDIVEQLRLSKNWKLNLKSVKLMKNLLILSSKLETSSIPKTINTKLVIEKYSEMMENELLENFNSAYRENNFTKLNEIAIILNNFNGGVNVIQSFINQHDYFIDTKQIDLENEFENVFIKNVKFKEQLIDFENHSVIIETSMQNLINDVETVIKNESKIVKRVFEEKATHVIQLFIQRVFAQKIEPRFEVLLRNSLSISNLAYVRILHGLFTLFGKFTKSLIDYFQLLEIDDSNQILSTTLEQCFADLFSHYLYDRSKYFGIEKRSLEAILVDMTSKFTVNYDKEINKRVLLDKYKEKLSTNVDAFMHSPRGNTHSRQDSTSRSKLSQFNSFLKTHLDKDHLSLNRTNTLSDSFNNSSSSTQYDVANNSSSLVNSSFTASDIDNSPNSPANYSLNDVDSMLKCVVESTARVMELIPNKAHLYILEILKIMFLGIVDSYMEIALEVAYWKICKVDINKTAGVVNLNFLKFISMSTEILDLLSISIKSIFLPLLNNSPEIKAQIIEMTNSQIQKMEILINIILQETITVISTKFSAILCKQKKKDFVPKSQELLDQDTLPAIEIVNILNLIFEQSSKFLKGKNLQTFLTLIGEELYGLLLSHYSHFQVNSIGGVVVTKDIIGYQTAIEDWGVASLIDKFATLRELANLFTVQPELLESLTKEGHLADIGRDIIQSYISNREDFNHDNFINSVKLNFR
Protein: Intraflagellar transport protein-like protein (Q57WF2)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- C2H2-type domain-containing protein
- Intraflagellar transport protein 22
- IFT80/172/WDR35 TPR domain-containing protein
- Intraflagellar transport protein IFT88, putative
- Intraflagellar transport complex B protein 46 C terminal
- Uncharacterized protein
- Intraflagellar transport protein component, putative
- Intraflagellar transport protein 57/55
- Intraflagellar transport protein 80
- Intraflagellar transport
Sequence:
MQGGFGRTNFNQTSGLRPGSQMRPGSQMRPGSQMRGARVAGMGESLQQAVSVSAQAPVTLEGMRAATRSGNAGPGRQVGDRSYYIGLLRPKITELTTEIERLNEQEELIVKGGSVLTQLQQRNKALTDEAAKLKGTLADINLALEKSTTQDPSSVKDQATKLNQVNGEKRKQVDQLFLNAKEMEALTKKNTQTLEEEMQNLDRRILAENQDFGLYKATRDEAFNVSDAVLSHQHQIRMLTAKQELLMTKLSTDPDKKRAAEVLRGILSKRQLKEELTKQCALSVEEERQLLIKQVKTARGDIEVLERQVNETRDALSESKNRCASLDEELKSYSGDNIKAFQELQEKDRELQSFMDSFPAKLKEEMDKITEVQRNIATLLERISQALELKKQMPQEGSPNALQALESEVDAKRNQIEHDTMTHQRLERELMDRKVELEKVENLDTKIKAELQAHALKMEEQSQEMIKYGDMDGLRRNVDARRTELLNERTFLIKLRDSSKQQLNVLSGTVDTLRKQLNEDTSYRSMSTLEGRLRQLRQSSFTLEEFVRLKGRESYFVGLKTECLRLVDEINILLKETEQARGTSVGGGAVLMVGDR
Protein: Organic cation/carnitine transporter 6 (AtOCT6) (Q9SA36)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: High affinity carnitine transporter involved in the active cellular uptake of carnitine. Also transports organic cations (By similarity).
Subcellular location: Vacuole membrane {ECO:0000269|PubMed:18710496}; Multi-pass membrane protein {ECO:0000269|PubMed:18710496}.
Interaction partners:
- Membrane lipoprotein
- At4g01860
- Putative ALA-interacting subunit 4
- E3 ubiquitin-protein ligase listerin
- Wall-associated receptor kinase-like 8
- F3O9.7 protein
- Endoglucanase 7
- Metal tolerance protein 10
- Pentatricopeptide repeat-containing protein At1g71460
- Trimethylguanosine synthase
Sequence:
MADPISEPLLSHLTDDSGVNEKTRLEALTFDKIVEQSLSDFGFWQFFQISLVGLALLFDAQQIFITVYTDAYPTWHCLNHTICDPSASDICKLPRSAWEWDGGSQGKSVISEFGLECSSSLLRGMPSSAFYIGAIVGGFFLALIPDDSLGRKKLVLFSTFAMSITSISVIFSTNVWIYTFLKFIIGFSRSQTWSYALVLISERVSTRWRPRATMIPFTLFVLGFMSLSGIAFLAQDSSWRYLYLYTSVPAVFYCIFLYLFALESPRWLHMQGKDKEAIDVLTKMSPKEKAYLESVVSKLPLKQENFEQAPTYSIKDFFFRKWAFRRILVVMIIMFGLGISYYGVPLAARDIDVNIYLSETLNALVELPTFVITPILLERFNRRSSVLVNTLLGGASGVLCFVLSILGKTEIAFAFELGTFFCARIGFNLMAVFMVEMFPTCVRSSATMMFRQALVVGGACCPLIASIGRYIPSVSFAIFGIAMSGLGMFVLILPETKGLSLCDSMEEQEKRDQAVNTSHVC
Protein: Innexin-19 (Neuronal symmetry protein 5) (Protein opu-19) (O61715)
Organism: Caenorhabditis elegans
Function: Structural component of the gap junctions that specifically coordinates left-right asymmetry in the developing nervous system. Acts by forming gap junction network linking embryonic neurons and providing electrical coupling between cells, leading to promote or inhibit AWC signaling. Required for the left and right AWC olfactory neurons to establish asymmetric patterns of gene expression during embryogenesis. Acts autonomously.
Subcellular location: Cell membrane {ECO:0000269|PubMed:17512411}; Multi-pass membrane protein {ECO:0000255|PROSITE-ProRule:PRU00351, ECO:0000269|PubMed:17512411}. Cell junction, gap junction {ECO:0000269|PubMed:17512411}. Note=Specifically present at the transient gap junctions formed between the cell bodies of embryonic neurons. Excluded from axons and dendrites.
Interaction partners:
- Clc-like protein
- Serpentine receptor class r-10
- G-protein coupled receptors family 1 profile domain-containing protein
- Transcription factor nsy-7
- G_PROTEIN_RECEP_F1_2 domain-containing protein
Sequence:
MWRTPASTGPLRQDRQMFFHATLARSFINALSVRGDDDAVDRLNYYYTPLILAVCCLVISAKQYGGTPIECWVNPHSRESMEEYIESYCWIQNTYWIPMYENVPDDHTAREEKQIGYYQWVPFILIAEALMFSLPCIFWRLCSFQSGLNIQTLINAACDGQALLDASDRQKAVEAITTNFVDNLDLQSPNGRIRARGWIARIKFSRFLSGQCLSILHSFTKLLYSMNVVAQFLILNACLKSSDFLFFGFQVLNDIWAGRPWTETGHFPRVTLCDFEVRYLANLNRYTVQCALLINIINEKVFAFLWCWYMILAIITTCSFIYWIANSFIHSEKVDYVMKFIQIAESSEFKKLQKFEKDATVERLYTVIAFAPHLLDTFVSDFLKSDGVLMLRMISNHAGDMIVVQLVRNLWQEFRERNWREFEEHEEMKDVEMRRIHGGERIVISNPGQTKSFL
Protein: Phosphoglycerate mutase (EC 5.4.2.11) (G8BE40)
Organism: Candida parapsilosis (strain CDC 317 / ATCC MYA-4646) (Yeast) (Monilia parapsilosis)
Interaction partners:
- Fructose-bisphosphate aldolase
- Phosphoglycerate kinase
- Glucose-6-phosphate isomerase
- Triosephosphate isomerase
- phosphopyruvate hydratase
- phosphopyruvate hydratase
- Pyruvate kinase
- Transaldolase
- Glucose-6-phosphate 1-dehydrogenase
- Transketolase
Sequence:
MPKLVLIRHGQSDWNEKNLFTGWVDVKLSETGRKEAKRAGELIKEAGIKGDVLHTSLLSRAIQTADIALEEADQLWLPVKRSWRLNERHYGDLQGKDKAETLEQYGKEKFQTWRRSFDVPPPPISADNKYSQVGERRYADLDPSVVPHTESLKLVIDRLIPYWQDEIAADLLDGKVVIVAAHGNSLRALVKHLDNISDEEIAGLNIPTGIPLVYELDEKLKPTKPAYYLDPEAAAAGAAAVAAQGTKK
Protein: Alpha-amylase inhibitor BMAI-1 (Alpha-amylase flour inhibitor) (allergen Hor v 1) (P16968)
Organism: Hordeum vulgare (Barley)
Function: Could be involved in insect defense mechanisms. Inhibits insect-type alpha-amylase.
Subcellular location: Secreted.
Interaction partners:
Sequence:
PTSVAVDQGSMVSNSPGEWCWPGMGYPVYPFPRCRALVKSQCAGGQVVESIQKDCCRQIAAIGDEWCICGALGSMRGSMYKELGVALADDKATVAEVFPGCRTEVMDRAVASLPAVCNQYIPNTNGTDGVCYWLSYYQPPRQMSSR