wanglab/gogpt-training-data huggingface dataset:
Protein: Aquaporin PIP1-6 (Plasma membrane intrinsic protein 1-6) (ZmPIP1-6) (ZmPIP1;6) (Q9ATN0)
Organism: Zea mays (Maize)
Function: Aquaporins facilitate the transport of water and small neutral solutes across cell membranes.
Subcellular location: Cell membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}.
Interaction partners:
- Expansin
Sequence:
MAGGTLQDRSEEEDVRVGVDRFPERQPIGTAADDLGRDYSEPPAAPLFEASELSSWSFYRAGIAEFVATFLFLYVTVLTVMGVSKSPSKCGTVGIQGIAWAFGGMIFALVYCTAGVSGGHINPAVTFGLLLARKLSLTRAVYYVVMQCLGAVCGAGVVKAFGSALYESAGGGANAVSPGYTKGDGLGAEVVGTFVLVYTVFSATDAKRTARDSHVPALAPLPIGFAVFLVHLATIPITGTGINPARSLGAAIIYDNPHGWHGHWIFWVGPFAGAALAAVYHQVVLRAIPFKSSAHY
Protein: Trehalose monomycolate exporter MmpL3 (TMM exporter MmpL3) (MmpL3 transporter) (Mycobacterial membrane protein large 3) (A0QP27)
Organism: Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155) (Mycobacterium smegmatis)
Function: Transports trehalose monomycolate (TMM) to the cell wall. Flips TMM across the inner membrane. Membrane potential is not required for this function. Transports probably phosphatidylethanolamine (PE) as well. Binds specifically both TMM and PE, but not trehalose dimycolate (TDM). Binds also diacylglycerol (DAG) and other phospholipids, including phosphatidylglycerol (PG), phosphatidylinositol (PI), and cardiolipin (CDL). Contributes to membrane potential, cell wall composition, antibiotic susceptibility and fitness.
Subcellular location: Cell inner membrane {ECO:0000269|PubMed:28698380, ECO:0000269|PubMed:30682372, ECO:0000269|PubMed:31113875}; Multi-pass membrane protein {ECO:0000255, ECO:0000305|PubMed:30682372, ECO:0000305|PubMed:31113875}. Cell septum {ECO:0000269|PubMed:31239378}. Cell tip {ECO:0000269|PubMed:31239378}. Note=Colocalizes with TtfA to the cell poles and septa. Trehalose monomycolate (TMM) synthesis is not required for localization to the poles or septa. {ECO:0000269|PubMed:31239378}.
Interaction partners:
Sequence:
MFAWWGRTVYQFRYIVIGVMVALCLGGGVYGISLGNHVTQSGFYDEGSQSVAASLIGDEVYGRDRTSHVVAILTPPDDKKVTDKAWQKKVTEELDQVVKDHEDQIVGWVGWLKAPDTTDPTVSAMKTQDLRHTFISIPLQGDDDDEILKNYQVVEPELQQVNGGDIRLAGLNPLASELTGTIGEDQKRAEVAAIPLVAVVLFFVFGTVIAAALPAIIGGLAIAGALGIMRLVAEFTPVHFFAQPVVTLIGLGIAIDYGLFIVSRFREEIAEGYDTEAAVRRTVMTSGRTVVFSAVIIVASSVPLLLFPQGFLKSITYAIIASVMLAAILSITVLAAALAILGPRVDALGVTTLLKIPFLANWQFSRRIIDWFAEKTQKTKTREEVERGFWGRLVNVVMKRPIAFAAPILVVMVLLIIPLGQLSLGGISEKYLPPDNAVRQSQEQFDKLFPGFRTEPLTLVMKREDGEPITDAQIADMRAKALTVSGFTDPDNDPEKMWKERPANDSGSKDPSVRVIQNGLENRNDAAKKIDELRALQPPHGIEVFVGGTPALEQDSIHSLFDKLPLMALILIVTTTVLMFLAFGSVVLPIKAALMSALTLGSTMGILTWMFVDGHGSGLMNYTPQPLMAPMIGLIIAVIWGLSTDYEVFLVSRMVEARERGMSTAEAIRIGTATTGRLITGAALILAVVAGAFVFSDLVMMKYLAFGLLIALLLDATIIRMFLVPAVMKLLGDDCWWAPRWMKRVQEKLGLGETELPDERKRPTVRESETDQRALVGVGAPPPPPRPHDPTHPAPEPVRPMPPMRSNAPSAAGTARISTPPQPPQPPQAPAQQAGDEPATTRFAMARNAVRNAVNSAVHGGAGSAAAPTERAPRPGGPAQPPAPPQREEREIESWLGALRGPAPAKNVPQPPAQPQRPSTDTTRAMPPQGRPPAGPADRGNENAPTTAFSAQRPPNGGAPADATTAIPTPPQREQEPSTEKLNTREDAPEDPETKRRGGGMSAQDLLRREGRL
Protein: DNA replication regulator DPB11 (P47027)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Has a role in the initiation of DNA replication. Required at S-phase checkpoint. Required for the association of PSF1 with origins. Also required for the proper activation of RAD53 in response to DNA damage and replication blocks. Multicopy suppressor of DPB2 mutation. Overexpression restores the growth defect conferred by POL2 mutation.
Subcellular location: Nucleus {ECO:0000269|PubMed:12730134}.
Interaction partners:
- DNA replication licensing factor MCM3
- DNA replication regulator SLD3
- Minichromosome maintenance protein 5
- DNA replication complex GINS protein SLD5
- DNA damage checkpoint protein 1
- DNA replication regulator SLD2
- Cell division control protein 45
- DNA repair protein RAD9
- Regulator of Ty1 transposition protein 107
- DNA replication complex GINS protein PSF3
Sequence:
MKPFQGITFCPTAINNEILAKKISKKIIKLGGIFSKDLTRQVNVLVVGSTTNTNKFKFAVKHRFDIIFIDIQAIDDIYQLWLSGENILPDSNTATMTGSTYEMLKILYRRFSFKYLHNFNIFIGRITDTNITSIDSLVRSIKKLGCSSYNYQNFVIKDTSSHNDDDDQGQNGQISIFVTDTLLGARVNAAIEQNIPIVHFKWILDCQKRSALLPYDPYYLLPNIKDLPYDSIGSNSCDCWDKINTTFPTNIDAQSSLQRQQSSSTLTPSLPKTSSLLNKFKPKGEKIWDKAMSLQQHSKTNFSVLGQSPLSINNKQEDLSDNSTLIFKNCAFIIHHIFPGNHRSILTKIVVQNGGKIETSYLSGIYDHSYYIIPSNKALDSFNDLPEIIDDNDGIVTEFFIERCLYYQKLLHPIDLWSKPFLSTIEFQVSSSSKLLHHEFSSSPFLNVTITGFSGVELLHLTKVLNLLKPMGINYVEYLNKSTDILLINLAALPSIPKTHPLWSNEFSDLFTQFCINNNNDDPGDNNRKDFQNNSILRNSMKRKIEYIKKFHSIPVVTPAFIFKLLSAASGENNEIFLNNIKWCIICPRGHKDDFKCKIKKPYYTSISSEKKYQNNDPKIDKTILLKRNNSSLSEHSMKDTKNELLQKIRETDSGRKKRSVSSSIMDVSSERQMPDTKRIKLESLPKNFVPKQIKRTTSWGTIMSENVPTEQPTAISNPEEIPRTEEVSHTQVTYGSIQDKKRTASLEKPMRRQTRNQTKELDS
Protein: Pendrin (Sodium-independent chloride/iodide transporter) (Solute carrier family 26 member 4) (Q9R154)
Organism: Rattus norvegicus (Rat)
Function: Sodium-independent transporter of chloride and iodide. Mediates electroneutral chloride-bicarbonate and chloride-formate exchange with 1:1 stoichiometry. Mediates electroneutral iodide-chloride and iodide-bicarbonate exchange (By similarity).
Subcellular location: Cell membrane {ECO:0000269|PubMed:26791486}; Multi-pass membrane protein {ECO:0000255}. Apical cell membrane {ECO:0000269|PubMed:11208611, ECO:0000269|PubMed:11274445}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Sodium/iodide cotransporter
- Forkhead box I1
- Gap junction beta-2 protein
- Cystic fibrosis transmembrane conductance regulator
- Epithelial sodium channel subunit gamma
- ATP-sensitive inward rectifier potassium channel 10
- Iodotyrosine deiodinase 1
- Solute carrier family 12 member 1-chloride cotransporter 1)
- Thyroid peroxidase
- Band 3 anion transport protein
Sequence:
MAARDRRSEPPQLAEYSCSYAVSRPVYSELAFQQQRERRLPERRTLRDSLARSCSCSRKRAFGALKALLPILDWLPKYRVKEWLLSDIISGVSTGLVGTLQGMAYALLAAVPVQYGLYSAFFPILTYFVFGTSRHISVGPFPVVSLMVGSVVLSMAPDDHFLVPSGNGSTLNTTTLDTGTRDAARVLLASTLTLLVGIIQLVFGGLQIGFIVRYLADPLVGGFTTAAAFQVLVSQLKIVLNVSTKNYNGVLSIIYTLIEIFQNIGDTNIADFIAGLLTIIVCMAVKELNDRFKHKIPVPIPIEVIVTIIATAISYGANLEANYNAGIVKSIPSGFLPPVLPSVGLFSDMLAASFSIAVVAYAIAVSVGKVYATKHDYIIDGNQEFIAFGISNVFSGFFSCFVATTALSRTAVQESTGGKTQVAGLISAVIVMVAIVALGKLLEPLQKSVLAAVVIANLKGMFMQVCDVPRLWKQNKTDAVIWVFTCIMSIILGLDLGLLAGLLFGLLTVVLRVQFPSWNGLGSVPSTDIYKSITHYKNLEEPEGVKILRFSSPIFYGNVDGFKKCVKSTVGFDAIRVYNKRLKALRRIQKLIKKGQLRATKNGIISDVGSSNNAFEPDEDVEEPEELDIPTKEIEIQVDWNSELPVKVNVPKVPIHSLVLDCGAVSFLDVVGVRSLRMIVKEFQRIDVNVYFALLQDDVLEKMEQCGFFDDNIRKDRFFLTVHDAILYLQNQAKSREGQDSLLETITLIQDCKDPLELMEAEINEEELDVQDEAMRRLAS
Protein: Mitogen-activated protein kinase kinase kinase 8 (Q5T857)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MEYMSTGSDNKEEIDLLIKHLNVSDVIDIMENLYASEEPAVYEPSLMTMCQDSNQNDERSKSLLLSGQEVPWLSSVRYGTVEDLLAFANHISNTAKHFYGQRPQESGILLNMVITPQNGRYQIDSDVLLIPWKLTYRNIGSDFIPRGAFGKVYLAQDIKTKKRMACKLIPVDQFKPSDVEIQACFRHENIAELYGAVLWGETVHLFMEAGEGGSVLEKLESCGPMREFEIIWVTKHVLKGLDFLHSKKVIHHDIK
Protein: Uncharacterized protein, isoform A (Q9VJ24)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MRGLQTNRHSSFHHLLLLFLVLLRSDRCFGIVCYHCDSIALPECSQTLGEVGVLPYKECATELTCAMSIVDSITYRGCGAETPIIGATYSKTCSTNLCNAGVYPPGRLKCHHCAGQECVAAPASKPKPCRYHLEEDQCYTDVISSSDAYRGCTSEQNHTLSTSAQLCEINGCNEEQGAWTQVCATCDSAIGRGCKIDLFQVNTGRCNVSLYEECQQDVLLGEQEDKYCFSFRRLSRVVRGCSTKIPTDLEPYVEQLEKCNTSDHCNAGCITQQKCFTCNSVDQELCRTNITAIANSTCSSAEASSCFSCEYSNWSIQRGCGAPPENPQITKCYECDEGAGCNSKDFTRCYQCSTDQAGAGCANWESPGEIYIEECDEPAAPCVVVSFNNATTARGCQKSDFSCASANVASCRLCEGSFCNKGSFPEERLWCHQCRGVQDCEEISRGQTAMPCPARANEPEDQELACLEYFDINSKEIVRGCRSNPELYYECLLRSNHFDSCRTCHSQACNNSPGRELRASYELEAKALSLLQGKSSAISIKFSNAGYGVWLIFSVIYIVTC
Protein: Casein kinase 1 alpha 1 (H0Y9X2)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
XQHIPYREDKNLTGTARYASINAHLGIEQSRRDDMESLGYVLMYFNRTSLPWQGLKAATKKQKYEKISEKKMSTPVEVLCKGFPAEFAMYLNYCRGLRFEEAPDYMYLRQLFRILFRTLNHQYDYTFDWTMLKQKAAQQAASSSGQGQQAQTPTGKQTDKTKSNMKG
Protein: Toll-like receptor 9 (M0RAA8)
Organism: Rattus norvegicus (Rat)
Subcellular location: Cytoplasmic vesicle, phagosome {ECO:0000256|ARBA:ARBA00004262}. Endoplasmic reticulum membrane {ECO:0000256|ARBA:ARBA00004115}; Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004115}. Endosome {ECO:0000256|ARBA:ARBA00004177}. Lysosome {ECO:0000256|ARBA:ARBA00004371}.
Interaction partners:
- Myeloid differentiation primary response protein MyD88
- High mobility group protein B1
- High mobility group protein B1
- Toll/interleukin-1 receptor domain-containing adapter protein
- Toll-like receptor 7
- TIR domain-containing adapter molecule 2
- Toll-like receptor 4
- Toll-like receptor 2
- Interleukin-1 beta
- Protein unc-93 homolog B1
Sequence:
MVLCRRTLHPLSLLVQAAMLAEALALGTLPAFLPCELKPHGLVDCNWLFLKSVPHFSAAEPRSNITSLSLIANRIHHLHNLDFVHLPNVRQLNLKWNCPPPGLSPLHFSCRMTIEPKTFLAMRMLEELNLSYNGITTVPRLPSSLTNLSLSHTNILVLDASSLAGLHSLRVLFMDGNCYYKNPCNGAVNVTPDAFLGLSNLTHLSLKYNNLTEVPRQLPSSLEYLLLSYNLIVKLGPEDLANLTSLRVLDVGGNCRRCDHAPDLCTECRQKSLDLHPQTFRHLSHLEGLVLKDSSLHSLNSKWFQGLVNLSVLDLSENFLYESINKTSAFQNLTRLRKLDLSFNYCKKVSFARLHLASSFKSLVSLQELNMNGIFFRLLNKNTLRWLAGLPKLHTLHLQMNFINQAQLSVFSTFRALRFVDLSNNRISGPPTLSRVAPEKADEAEKGVPWPASLTPALPSTPVSKNFMVRCKNLRFTMDLSRNNLVTIKPEMFVNLSHLQCLSLSHNCIAQAVNGSQFLPLTNLKVLDLSYNKLDLYHSKSFSELPQLQALDLSYNSQPFSMQGIGHNFSFLANLSRLQNLSLAHNDIHSRVSSRLYSTSVEYLDFSGNGVGRMWDEEDLYLYFFQDLRSLIHLDLSQNKLHILRPQNLNYLPKSLTKLSFRDNHLSFFNWSSLAFLPNLRDLDLAGNLLKALTNGTLPNGTLLQKLDVSSNSIVFVVPAFFALAVELKEVNLSHNILKTVDRSWFGPIVMNLTVLDVSSNPLHCACGAPFVDLLLEVQTKVPGLANGVKCGSPRQLQGRSIFAQDLRLCLDDVLSRDCFGLSLLAVAVGTVLPLLQHLCGWDVWYCFHLCLAWLPLLTRGRRSAQALPYDAFVVFDKAQSAVADWVYNELRVRLEERRGRRALRLCLEDRDWLPGQTLFENLWASIYGSRKTLFVLAHTDKVSGLLRTSFLLAQQRLLEDRKDVVVLVILRPDAHRSRYVRLRQRLCRQSVLFWPHQPNGQGSFWAQLSTALTRDNHHFYNRNFCRGPTAE
Protein: Importin subunit beta-3 (Karyopherin subunit beta-3) (Karyopherin-121) (Protein secretion enhancer 1) (P32337)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Functions in nuclear protein import as nuclear transport receptor. Serves as receptor for classical and arginine/glycine-rich nuclear localization signals (cNLS and rg-NLS) in cargo substrates. Its predominant cargo substrate seems to be ribosomal proteins and ribosome biogenesis trans- and cis-acting factors. Required for nuclear transport of YAP1, NOP1 and SOF1. Mediates the nuclear import of histones H3 and H4. Mediates docking of the importin/substrate complex to the nuclear pore complex (NPC) through binding to repeat-containing nucleoporins. The complex is subsequently translocated through the pore by an energy requiring, Ran-dependent mechanism. At the nucleoplasmic side of the NPC, GTP-Ran binding leads to release of the cargo. The importin is re-exported from the nucleus to the cytoplasm where GTP hydrolysis releases Ran from importin. The directionality of nuclear import is thought to be conferred by an asymmetric distribution of the GTP- and GDP-bound forms of Ran between the cytoplasm and nucleus.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:9238021}. Nucleus {ECO:0000269|PubMed:9238021}.
Interaction partners:
- Nucleoporin NUP53
- GTP-binding nuclear protein GSP1/CNR1
- Ubiquitin-like-specific protease 1
- RNA annealing protein YRA1
- Phosphate system positive regulatory protein PHO4
- Importin subunit beta-1
- Importin subunit alpha
- Nucleoporin ASM4
- Protein STE12
- Importin subunit beta-2
Sequence:
MSALPEEVNRTLLQIVQAFASPDNQIRSVAEKALSEEWITENNIEYLLTFLAEQAAFSQDTTVAALSAVLFRKLALKAPPSSKLMIMSKNITHIRKEVLAQIRSSLLKGFLSERADSIRHKLSDAIAECVQDDLPAWPELLQALIESLKSGNPNFRESSFRILTTVPYLITAVDINSILPIFQSGFTDASDNVKIAAVTAFVGYFKQLPKSEWSKLGILLPSLLNSLPRFLDDGKDDALASVFESLIELVELAPKLFKDMFDQIIQFTDMVIKNKDLEPPARTTALELLTVFSENAPQMCKSNQNYGQTLVMVTLIMMTEVSIDDDDAAEWIESDDTDDEEEVTYDHARQALDRVALKLGGEYLAAPLFQYLQQMITSTEWRERFAAMMALSSAAEGCADVLIGEIPKILDMVIPLINDPHPRVQYGCCNVLGQISTDFSPFIQRTAHDRILPALISKLTSECTSRVQTHAAAALVNFSEFASKDILEPYLDSLLTNLLVLLQSNKLYVQEQALTTIAFIAEAAKNKFIKYYDTLMPLLLNVLKVNNKDNSVLKGKCMECATLIGFAVGKEKFHEHSQELISILVALQNSDIDEDDALRSYLEQSWSRICRILGDDFVPLLPIVIPPLLITAKATQDVGLIEEEEAANFQQYPDWDVVQVQGKHIAIHTSVLDDKVSAMELLQSYATLLRGQFAVYVKEVMEEIALPSLDFYLHDGVRAAGATLIPILLSCLLAATGTQNEELVLLWHKASSKLIGGLMSEPMPEITQVYHNSLVNGIKVMGDNCLSEDQLAAFTKGVSANLTDTYERMQDRHGDGDEYNENIDEEEDFTDEDLLDEINKSIAAVLKTTNGHYLKNLENIWPMINTFLLDNEPILVIFALVVIGDLIQYGGEQTASMKNAFIPKVTECLISPDARIRQAASYIIGVCAQYAPSTYADVCIPTLDTLVQIVDFPGSKLEENRSSTENASAAIAKILYAYNSNIPNVDTYTANWFKTLPTITDKEAASFNYQFLSQLIENNSPIVCAQSNISAVVDSVIQALNERSLTEREGQTVISSVKKLLGFLPSSDAMAIFNRYPADIMEKVHKWFA
Protein: Dynein light chain roadblock (Q381D2)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000256|ARBA:ARBA00004245, ECO:0000256|PIRNR:PIRNR009998}.
Interaction partners:
- Cytoplasmic dynein 2 light intermediate chain 1
- Dynein light chain, putative
- Dynein light chain, putative
- Dynein light chain
- Dynein light chain
- Dynein light chain
- Dynein light chain
- Dynein light chain
- Dynein light chain
- Uncharacterized protein
Sequence:
MTSERVESVLELITYTKGVAGAVVCNRNGEPIRDSFQDLDRNRAVAYSNMAADLARDAALLFSADESLDAVRVRSLNNEIIIKCHEEFLLVVIQELTK
Protein: Geranylfarnesyl diphosphate synthase, chloroplastic (LcGFDPS) (EC 2.5.1.81) (A0A0U3BRC5)
Organism: Leucosceptrum canum (Hairy white-wand) (Clerodendron leucosceptrum)
Function: Involved in the biosynthesis of leucosceptrane sesterterpenoids natural products, which are playing defensive roles toward herbivorus insects (e.g. Spodoptera exigua). Catalyzes the condensation of isopentenyl pyrophosphate (IDP) with the allylic pyrophosphates to yield geranylfarnesyl diphosphate (GFDP), the C(25) prenyl diphosphate precursor to all sesterterpenoids. Geranylgeranyl diphosphate (GGPP) is the preferred substrate, however dimethylallyl diphosphate (DMADP), farnesyl diphosphate (FDP) and geranyl diphosphate (GDP) can also be used as allylic substrate.
Subcellular location: Plastid, chloroplast {ECO:0000269|PubMed:26941091}.
Interaction partners:
Sequence:
MSHCTIFLYKYFPGKPRYQHCSFLHPLNHKLKSLFLPITGSRFLSNSTFSVSDSAHSHQAKPHVRNAQFDFKAYMLEKITAVNQALDAALPVREPVKIHEAMRYSLLLGGKRICPIVCLAACHLVGGDESTAMPSAAALEMIHAMSLMHDDLPCMDNDDLRRGRPSNHVVFGEGATVLAGYALIARAFEHIATATQGVGPGKILRVIGELAQLIGAEGVVGGQVVDLRCGGEGQMAIGLEQLEYIHLHKTAASVEASAVAGAVLGGASEEEIERLRKYSRSAGLLFQVVDDILDVTKSSEELGKTAGKDLAAGKTTYPKLLGMEKSREMAEKLKREAQEQLLGFDPIKAAPLIALVDFIAYRDK
Protein: Leucine-rich repeat protein (LRRP) (Q38CF8)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MESPVEMYRSHCQAVGVAMNSALLRGLPETTEKLRNMKVMHFGRNFLGDRGILPLLPVIKQAKSLHTLDLRNNGIGNEGVKALCRQLRDHPSLRVLELGGNPFTYLAARQLTYLCEYNDRITFIGVDDTLMTEPLRQSIVHRMQATMKRRENRRQRKQASPNVIDNEENTTEEVTATGDTEYIDDAAVAMGVFVSEDPLATPLQPVEVVTEACVQLISPPANTPSVKSEKVAEMTGDEMISGPSPSSSSVTPPSTGAAASSTSDSRETTQANEDEVGEPAEVFSDEEQNKVAAVEETDETSDVSVHSAGEELSGSMVDDDVQSESSVTRSDATEPQEDSIVEDED
Protein: Flagellar transcriptional regulator FlhC (P0ABY9)
Organism: Escherichia coli O157:H7
Function: Functions in complex with FlhD as a master transcriptional regulator that regulates transcription of several flagellar and non-flagellar operons by binding to their promoter region. Activates expression of class 2 flagellar genes, including fliA, which is a flagellum-specific sigma factor that turns on the class 3 genes. Also regulates genes whose products function in a variety of physiological pathways.
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01891}.
Interaction partners:
- Flagellar transcriptional regulator FlhD
- Flagellar transcriptional regulator FlhD
- RNA polymerase sigma factor FliA
- Motility protein B
- RNA polymerase sigma factor FliA
- Flagellar motor protein MotA
- Flagellar motor protein MotA
- Motility protein B
- Flagellar protein FliL
- Flagella basal body P-ring formation protein FlgA
Sequence:
MSEKSIVQEARDIQLAMELITLGARLQMLESETQLSRGRLIKLYKELRGSPPPKGMLPFSTDWFMTWEQNVHASMFCNAWQFLLKTGLCNGVDAVIKAYRLYLEQCPQAEEGPLLALTRAWTLVRFVESGLLQLSSCNCCGGNFITHAHQPVGSFACSLCQPPSRAVKRRKLSQNPADIIPQLLDEQRVQAV
Protein: Myomesin 1 (Q80UL1)
Organism: Rattus norvegicus (Rat)
Interaction partners:
Sequence:
NTDTSVVVSWEESKDAKELVGYYIESSVVGSGQWEPCNNNPVKGSRFTCHGLTTGQSYIFRVRAVNAAGLSEYSQDSEAIEVKAAIAVPSPPYDITCLESFRDSMVLGWKQPDKTGGAEITGYY
Protein: Disease resistance protein SUMM2 (Disease resistance protein At1g12280) (Protein SUPPRESSOR OF MKK1 MKK2 2) (P60838)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Disease resistance protein that mediates defense responses against the bacterial pathogen Pseudomonas syringae pv tomato strain DC3000, and the virulent oomycete Hyaloperonospora arabidopsidis isolate Noco2. Becomes active when the MEKK1-MKK1-MKK2-MPK4 kinase cascade is disrupted by the microbial effector hopAI1. Does not seem to be required for the activation of MPK4 by flg22, or flg22-induced up-regulation of PAD3. Functions downstream of MEKK2/SUMM1 in immune responses, including cell death and defense responses.
Interaction partners:
- Mitogen-activated protein kinase kinase 1
- Mitogen-activated protein kinase 4
- Mitogen-activated protein kinase kinase kinase 9
- Calmodulin-binding receptor-like cytoplasmic kinase 3
- Mitogen-activated protein kinase kinase kinase 1
- Mitogen-activated protein kinase kinase 2
- Mitogen-activated protein kinase 3
- Mitogen-activated protein kinase 6
- Mitogen-activated protein kinase kinase 5
- RPM1-interacting protein 4
Sequence:
MGACLTLSFSCDEVVNQISQGLCINVGYICELSKNVVAMKKDMEVLKKKRDDVKRRVDIEEFTRRRERLSQVQGWLTNVSTVENKFNELLTTNDAELQRLCLFGFCSKNVKMSYLYGKRVVLMLKEIESLSSQGDFDTVTLATPIARIEEMPIQPTIVGQETMLERVWTRLTEDGDEIVGLYGMGGVGKTTLLTRINNKFSEKCSGFGVVIWVVVSKSPDIHRIQGDIGKRLDLGGEEWDNVNENQRALDIYNVLGKQKFVLLLDDIWEKVNLEVLGVPYPSRQNGCKVVFTTRSRDVCGRMRVDDPMEVSCLEPNEAWELFQMKVGENTLKGHPDIPELARKVAGKCCGLPLALNVIGETMACKRMVQEWRNAIDVLSSYAAEFPGMEQILPILKYSYDNLNKEQVKPCFLYCSLFPEDYRMEKERLIDYWICEGFIDENESRERALSQGYEIIGILVRACLLLEEAINKEQVKMHDVVREMALWIASDLGEHKERCIVQVGVGLREVPKVKNWSSVRRMSLMENEIEILSGSPECLELTTLFLQKNDSLLHISDEFFRCIPMLVVLDLSGNSSLRKLPNQISKLVSLRYLDLSWTYIKRLPVGLQELKKLRYLRLDYMKRLKSISGISNISSLRKLQLLQSKMSLDMSLVEELQLLEHLEVLNISIKSSLVVEKLLNAPRLVKCLQILVLRGVQEESSGVLTLPDMDNLNKVIIRKCGMCEIKIERKTLSLSSNRSPKTQFLHNLSTVHISSCDGLKDLTWLLFAPNLTSLEVLDSELVEGIINQEKAMTMSGIIPFQKLESLRLHNLAMLRSIYWQPLSFPCLKTIHITKCPELRKLPLDSEIAIRDEELVIKYQEEEWLERVEWDNEATRLRFLPFFKFFGPEWQVSYVR
Protein: FMR1-interacting protein NUFIP1 (Nuclear FMR1-interacting protein 1) (Nuclear FMRP-interacting protein 1) (Q9UHK0)
Organism: Homo sapiens (Human)
Function: Binds RNA.
Subcellular location: Nucleus {ECO:0000269|PubMed:10556305}. Note=Distributed in the nucleus in a dot-like pattern.
Interaction partners:
- Zinc finger HIT domain-containing protein 3
- Box C/D snoRNA protein 1
- Nucleolar protein 58
- Fragile X messenger ribonucleoprotein 1
- NHP2-like protein 1
- RNA-binding protein FXR1
- PIH1 domain-containing protein 1
- FMR1-interacting protein NUFIP2
- RNA-binding protein FXR2
- Nucleolar protein 56
Sequence:
MAEPTSDFETPIGWHASPELTPTLGPLSDTAPPRDSWMFWAMLPPPPPPLTSSLPAAGSKPSSESQPPMEAQSLPGAPPPFDAQILPGAQPPFDAQSPLDSQPQPSGQPWNFHASTSWYWRQSSDRFPRHQKSFNPAVKNSYYPRKYDAKFTDFSLPPSRKQKKKKRKEPVFHFFCDTCDRGFKNQEKYDKHMSEHTKCPELDCSFTAHEKIVQFHWRNMHAPGMKKIKLDTPEEIARWREERRKNYPTLANIERKKKLKLEKEKRGAVLTTTQYGKMKGMSRHSQMAKIRSPGKNHKWKNDNSRQRAVTGSGSHLCDLKLEGPPEANADPLGVLINSDSESDKEEKPQHSVIPKEVTPALCSLMSSYGSLSGSESEPEETPIKTEADVLAENQVLDSSAPKSPSQDVKATVRNFSEAKSENRKKSFEKTNPKRKKDYHNYQTLFEPRTHHPYLLEMLLAPDIRHERNVILQCVRYIIKKDFFGLDTNSAKSKDV
Protein: Stachyose synthase (EC 2.4.1.67) (Galactinol--raffinose galactosyltransferase) (Q93XK2)
Organism: Pisum sativum (Garden pea) (Lathyrus oleraceus)
Function: Catalyzes stachyose synthesis by transfer of a galactosyl moiety from galactinol to raffinose. Also catalyzes verbascose synthesis by galactosyl transfer from galactinol to stachyose or from one stachyose molecule to another. Oligosaccharides of the raffinose family play a protective role in maturation drying of seeds. They may act as cryoprotectants in frost-hardy plants.
Subcellular location: Cytoplasm {ECO:0000305}.
Interaction partners:
Sequence:
MAPPLNSTTSNLIKTESIFDLSERKFKVKGFPLFHDVPENVSFRSFSSICKPSESNAPPSLLQKVLAYSHKGGFFGFSHETPSDRLMNSIGSFNGKDFLSIFRFKTWWSTQWIGKSGSDLQMETQWILIEVPETKSYVVIIPIIEKCFRSALFPGFNDHVKIIAESGSTKVKESTFNSIAYVHFSENPYDLMKEAYSAIRVHLNSFRLLEEKTIPNLVDKFGWCTWDAFYLTVNPIGIFHGLDDFSKGGVEPRFVIIDDGWQSISFDGYDPNEDAKNLVLGGEQMSGRLHRFDECYKFRKYESGLLLGPNSPPYDPNNFTDLILKGIEHEKLRKKREEAISSKSSDLAEIESKIKKVVKEIDDLFGGEQFSSGEKSEMKSEYGLKAFTKDLRTKFKGLDDVYVWHALCGAWGGVRPETTHLDTKIVPCKLSPGLDGTMEDLAVVEISKASLGLVHPSQANELYDSMHSYLAESGITGVKVDVIHSLEYVCDEYGGRVDLAKVYYEGLTKSIVKNFNGNGMIASMQHCNDFFFLGTKQISMGRVGDDFWFQDPNGDPMGSFWLQGVHMIHCSYNSLWMGQMIQPDWDMFQSDHVCAKFHAGSRAICGGPIYVSDNVGSHDFDLIKKLVFPDGTIPKCIYFPLPTRDCLFKNPLFDHTTVLKIWNFNKYGGVIGAFNCQGAGWDPIMQKFRGFPECYKPIPGTVHVTEVEWDQKEETSHLGKAEEYVVYLNQAEELSLMTLKSEPIQFTIQPSTFELYSFVPVTKLCGGIKFAPIGLTNMFNSGGTVIDLEYVGNGAKIKVKGGGSFLAYSSESPKKFQLNGCEVDFEWLGDGKLCVNVPWIEEACGVSDMEIFF
Protein: Abscisic acid receptor PYL5 (PYR1-like protein 11) (OsPYL11) (PYR1-like protein 5) (OsPYL5) (Regulatory components of ABA receptor 5) (Q6I5C3)
Organism: Oryza sativa subsp. japonica (Rice)
Function: Intracellular abscisic acid (ABA) receptor that functions as a positive regulator of ABA signaling pathway. Together with ABI5, PP2C30 and SAPK2, is part of an ABA signaling unit that modulates seed germination and early seedling growth. Acts as positive regulator of abiotic stress-responsive gene expression. Inhibits the protein phosphatases PP2C06 and PP2C09 when activated by ABA.
Subcellular location: Nucleus {ECO:0000269|PubMed:22071266, ECO:0000269|PubMed:26362328, ECO:0000269|PubMed:28000033}. Cytoplasm, cytosol {ECO:0000269|PubMed:26362328}.
Interaction partners:
- Probable protein phosphatase 2C 30
- Probable protein phosphatase 2C 6
- Probable protein phosphatase 2C 8
- Probable protein phosphatase 2C 68
- Probable protein phosphatase 2C 49
- Protein phosphatase 2C 53
- Protein phosphatase 2C 50
- Protein phosphatase 2C 51
- Probable protein phosphatase 2C 37
- protein-serine/threonine phosphatase
Sequence:
MVGLVGGGGWRVGDDAAGGGGGGAVAAGAAAAAEAEHMRRLHSHAPGEHQCSSALVKHIKAPVHLVWSLVRSFDQPQRYKPFVSRCVVRGGDLEIGSVREVNVKTGLPATTSTERLELLDDDEHILSVKFVGGDHRLRNYSSIVTVHPESIDGRPGTLVIESFVVDVPDGNTKDETCYFVEAVIKCNLTSLAEVSERLAVQSPTSPLEQ
Protein: SD06722p (Q95SU9)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MSMLFDLVWQLLHWFSCGCAQQKNKNKNSVLFIIYASVHATFVSVSSSVIPRTEISLYTMIIQSEQFTQCMCCVCVCSQIYYLYIYIYISIVICTLKGSNNDQTQLSCIIRRMFESNLCFNKILYQTIVLISK
Protein: Poly(rC)-binding protein 4 (Alpha-CP4) (P57723)
Organism: Homo sapiens (Human)
Function: Single-stranded nucleic acid binding protein that binds preferentially to oligo dC.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:14612387}.
Interaction partners:
- Cellular tumor antigen p53
- Cyclin-dependent kinase inhibitor 1
Sequence:
MSGSDGGLEEEPELSITLTLRMLMHGKEVGSIIGKKGETVKRIREQSSARITISEGSCPERITTITGSTAAVFHAVSMIAFKLDEDLCAAPANGGNVSRPPVTLRLVIPASQCGSLIGKAGTKIKEIRETTGAQVQVAGDLLPNSTERAVTVSGVPDAIILCVRQICAVILESPPKGATIPYHPSLSLGTVLLSANQGFSVQGQYGAVTPAEVTKLQQLSSHAVPFATPSVVPGLDPGTQTSSQEFLVPNDLIGCVIGRQGSKISEIRQMSGAHIKIGNQAEGAGERHVTITGSPVSIALAQYLITACLETAKSTSGGTPSSAPADLPAPFSPPLTALPTAPPGLLGTPYAISLSNFIGLKPMPFLALPPASPGPPPGLAAYTAKMAAANGSKKAERQKFSPY
Protein: NADPH-dependent codeinone reductase 1-2 (PsCor1.2) (EC 1.1.1.247) (Q9SQ69)
Organism: Papaver somniferum (Opium poppy)
Function: Reduces codeinone to codeine in the penultimate step in morphine biosynthesis. Can use morphinone, hydrocodone and hydromorphone as substrate during reductive reaction with NADPH as cofactor, and morphine and dihydrocodeine as substrate during oxidative reaction with NADP as cofactor.
Subcellular location: Cytoplasm, cytosol {ECO:0000269|PubMed:11079569}. Note=Present in the cytosolic part of laticifer cells that secrete latex (PubMed:11079569). Localized to the parietal region of the sieve element cytoplasm (PubMed:14508000). {ECO:0000269|PubMed:11079569, ECO:0000269|PubMed:14508000}.
Interaction partners:
Sequence:
MESNGVPMITLSSGIRMPALGMGTVETMEKGTEREKLAFLNAIEVGYRHFDTAAAYQSEECLGEAIAEALQLGLIKSRDELFITSKLWCADAHADLVLPALQNSLRNLKLEYLDLYLIHHPVSLKPGKLVNEIPKDHILPMDYKSVWAAMEECQTLGFTRAIGVSNFSCKKLQELMATAKIPPVVNQVEMSPTLHQKNLREYCKANNIMITAHSVLGAIGAPWGSNAVMDSKVLHQIAVARGKSVAQVSMRWVYQQGASLVVKSFNEARMKENLKIFDSELTAEDMEKISEIPQSRTSSADFLLSPTGPFKTEEEFWDEKD