wanglab/gogpt-training-data huggingface dataset:
Protein: Granulocyte colony-stimulating factor (G-CSF) (Pluripoietin) (Filgrastim) (Lenograstim) (P09919)
Organism: Homo sapiens (Human)
Function: Granulocyte/macrophage colony-stimulating factors are cytokines that act in hematopoiesis by controlling the production, differentiation, and function of 2 related white cell populations of the blood, the granulocytes and the monocytes-macrophages. This CSF induces granulocytes.
Subcellular location: Secreted.
Interaction partners:
- Granulocyte-macrophage colony-stimulating factor
- Granulocyte colony-stimulating factor receptor
- Interleukin-1 beta
- Eotaxin
- Interleukin-1 alpha
- Erythropoietin
- Interferon gamma
- Tyrosine-protein kinase JAK2
- Interleukin-6
- Thrombopoietin
Sequence:
MAGPATQSPMKLMALQLLLWHSALWTVQEATPLGPASSLPQSFLLKCLEQVRKIQGDGAALQEKLVSECATYKLCHPEELVLLGHSLGIPWAPLSSCPSQALQLAGCLSQLHSGLFLYQGLLQALEGISPELGPTLDTLQLDVADFATTIWQQMEELGMAPALQPTQGAMPAFASAFQRRAGGVLVASHLQSFLEVSYRVLRHLAQP
Protein: Lysine-specific demethylase 4D (EC 1.14.11.66) (JmjC domain-containing histone demethylation protein 3D) (Jumonji domain-containing protein 2D) ([histone H3]-trimethyl-L-lysine(9) demethylase 4D) (Q6B0I6)
Organism: Homo sapiens (Human)
Function: Histone demethylase that specifically demethylates 'Lys-9' of histone H3, thereby playing a central role in histone code. Does not demethylate histone H3 'Lys-4', H3 'Lys-27', H3 'Lys-36' nor H4 'Lys-20'. Demethylates both di- and trimethylated H3 'Lys-9' residue, while it has no activity on monomethylated residues. Demethylation of Lys residue generates formaldehyde and succinate.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00537, ECO:0000269|PubMed:35145029}.
Interaction partners:
- Probable JmjC domain-containing histone demethylation protein 2C
- Histone-lysine N-methyltransferase SUV39H1
- Histone H3.2
- Histone H3.1
Sequence:
METMKSKANCAQNPNCNIMIFHPTKEEFNDFDKYIAYMESQGAHRAGLAKIIPPKEWKARETYDNISEILIATPLQQVASGRAGVFTQYHKKKKAMTVGEYRHLANSKKYQTPPHQNFEDLERKYWKNRIYNSPIYGADISGSLFDENTKQWNLGHLGTIQDLLEKECGVVIEGVNTPYLYFGMWKTTFAWHTEDMDLYSINYLHLGEPKTWYVVPPEHGQRLERLARELFPGSSRGCGAFLRHKVALISPTVLKENGIPFNRITQEAGEFMVTFPYGYHAGFNHGFNCAEAINFATPRWIDYGKMASQCSCGEARVTFSMDAFVRILQPERYDLWKRGQDRAVVDHMEPRVPASQELSTQKEVQLPRRAALGLRQLPSHWARHSPWPMAARSGTRCHTLVCSSLPRRSAVSGTATQPRAAAVHSSKKPSSTPSSTPGPSAQIIHPSNGRRGRGRPPQKLRAQELTLQTPAKRPLLAGTTCTASGPEPEPLPEDGALMDKPVPLSPGLQHPVKASGCSWAPVP
Protein: OTU domain-containing protein 6A (EC 3.4.19.12) (DUBA-2) (Q7L8S5)
Organism: Homo sapiens (Human)
Function: Deubiquitinating enzyme that hydrolyzes 'Lys-27'-, 'Lys-29'- and 'Lys-33'-linked polyubiquitin chains. Also able to hydrolyze 'Lys-11'-linked ubiquitin chains.
Interaction partners:
- Zinc finger-containing ubiquitin peptidase 1
- Ubiquitin thioesterase OTU1
Sequence:
MDDPKSEQQRILRRHQRERQELQAQIRSLKNSVPKTDKTKRKQLLQDVARMEAEMAQKHRQELEKFQDDSSIESVVEDLAKMNLENRPPRSSKAHRKRERMESEERERQESIFQAEMSEHLAGFKREEEEKLAAILGARGLEMKAIPADGHCMYRAIQDQLVFSVSVEMLRCRTASYMKKHVDEFLPFFSNPETSDSFGYDDFMIYCDNIVRTTAWGGQLELRALSHVLKTPIEVIQADSPTLIIGEEYVKKPIILVYLRYAYSLGEHYNSVTPLEAGAAGGVLPRLL
Protein: BEM1-interacting protein 1 (Growth inhibitory protein 7) (P38041)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Binds to the BEM1 protein.
Subcellular location: Bud {ECO:0000269|PubMed:12097146}. Bud neck {ECO:0000269|PubMed:12097146}. Note=Localizes to the periphery of buds during much of the budding cycle and to necks late in the cell cycle. {ECO:0000269|PubMed:12097146}.
Interaction partners:
- Bud emergence protein 1
- BEM1-interacting protein 2
- Cell division control protein 24
- 26S proteasome regulatory subunit RPN10
- Cell division control protein 42
- GTP-binding protein RHO3
- Protein ZDS2
- GTP-binding protein RHO4
- Large ribosomal subunit protein uL23
- Uncharacterized protein YMR124W
Sequence:
MSLEGNTLGKGAKSFPLYIAVNQYSKRMEDELNMKPGDKIKVITDDGEYNDGWYYGRNLRTKEEGLYPAVFTKRIAIEKPENLHKSPTQESGNSGVKYGNLNDSASNIGKVSSHQQENRYTSLKSTMSDIDKALEELRSGSVEQEVSKSPTRVPEVSTPQLQDEQTLIQEKTRNEENTTHDSLFSSTADLNLSSESLKNISKSNISTKSLEPSSESVRQLDLKMAKSWSPEEVTDYFSLVGFDQSTCNKFKEHQVSGKILLELELEHLKELEINSFGIRFQIFKEIRNIKSAIDSSSNKLDADYSTFAFENQAAQLMPAATVNRDEIQQQISSKCNKLSSESSDRKSSSVTTELQRPSSVVVNPNFKLHDPAEQILDMTEVPNLFADKDIFESPGRAPKPPSYPSPVQPPQSPSFNNRYTNNNARFPPQTTYPPKNKNPTVYSNGLIPNSSTSSDNSTGKFKFPAMNGHDSNSRKTTLTSATIPSINTVNTDESLPAISNISSNATSHHPNRNSVVYNNHKRTESGSSFVDLFNRISMLSPVKSSFDEEETKQPSKASRAVFDSARRKSSYGHSRDASLSEMKKHRRNSSILSFFSSKSQSNPTSPTKQTFTIDPAKMTSHSRSQSNSYSHARSQSYSHSRKHSLVTSPLKTSLSPINSKSNIALAHSETPTSSNNKEAVSQPSEGKHKHKHKHKSKHKHKNSSSKDGSSEEKSKKKLFSSTKESFVGSKEFKRSPSELTQKSTKSILPRSNAKKQQTSAFTEGIRSITAKESMQTADCSGWMSKKGTGAMGTWKQRFFTLHGTRLSYFTNTNDEKERGLIDITAHRVLPASDDDRLISLYAASLGKGKYCFKLVPPQPGSKKGLTFTEPRVHYFAVENKSEMKAWLSAIIKATIDIDTSVPVISSYATPTIPLSKAQTLLEEARLQTQLRDAEEEEGRDQFGWDDTQNKRNSNYPIEQDQFETSDYLESSAFEYPGGRL
Protein: Riboflavin transporter RibJ (Riboflavin/flavin transporter) (Q4D3E8)
Organism: Trypanosoma cruzi (strain CL Brener)
Function: Transporter involved in riboflavin (vitamin B2) uptake. Also transports FMN and FAD.
Subcellular location: Cell membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
Sequence:
MLPCFTRKPVDHPLGFLVALSGLLMQLMSYGIDNSYSIFSDDMHKDPSLGYPSVTTISLGNSVSLGLSPAFGVLCGFLVDRVPPRLMMAVSTLMLFAGLWLSSTFAHNVTAVTFSYCLLASISSACMLSPGAAATSSWFNRYQGLAMGINFSGGGVGSAIIPSLAGKWVVAYGWRKTFRLMSAFCAIGVVATLLSARRAPPKKEEAGPSEYDEGQERQEQGEEEQAHTDEENRNNNNSNGETTPARRGLHTHKLNPWELFLTMFSRAFLGNFFCWLIFSWAFYSLIYVAVPYVSSMGKAGTVYADISPIPTDIASTLFTFYGVFQIVGSILVGWLATGTTNEFAYVLCATIGGIFCAFLGFCRSYVAFALLLCVIGFCMAGMFAVMPALIAERLYGPNLGFYMGAVFLAGVVGGFSAPPIQAELQQRHYGNYTYVCVFMSACMTLAAAVCYITMWRDKRVRIVSAAAEAKLA
Protein: Cytochrome P450 monooxygenase ausG (EC 1.-.-.-) (Austinoid biosynthesis clusters protein G) (Q5AR32)
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 B that mediates the biosynthesis of austinol and dehydroaustinol, two fungal meroterpenoids. The first step of the pathway is the synthesis of 3,5-dimethylorsellinic acid by the polyketide synthase ausA. 3,5-dimethylorsellinic acid is then prenylated by the polyprenyl transferase ausN. Further epoxidation by the FAD-dependent monooxygenase ausM and cyclization by the probable terpene cyclase ausL lead to the formation of protoaustinoid A. Protoaustinoid A is then oxidized to spiro-lactone preaustinoid A3 by the combined action of the FAD-binding monooxygenases ausB and ausC, and the dioxygenase ausE. Acid-catalyzed keto-rearrangement and ring contraction of the tetraketide portion of preaustinoid A3 by ausJ lead to the formation of preaustinoid A4. The aldo-keto reductase ausK, with the help of ausH, is involved in the next step by transforming preaustinoid A4 into isoaustinone which is in turn hydroxylated by the P450 monooxygenase ausI to form austinolide. Finally, the cytochrome P450 monooxygenase ausG modifies austinolide to austinol. Austinol can be further modified to dehydroaustinol which forms a diffusible complex with diorcinol that initiates conidiation. Due to genetic rearrangements of the clusters and the subsequent loss of some enzymes, the end products of the Emericella nidulans austinoid biosynthesis clusters are austinol and dehydroaustinol, even if additional enzymes, such as the O-acetyltransferase ausQ and the cytochrome P450 monooxygenase ausR are still functional.
Subcellular location: Membrane {ECO:0000255}; Single-pass membrane protein {ECO:0000255}.
Interaction partners:
- Multifunctional dioxygenase ausE
- Terpene cyclase ausL
- FAD-dependent monooxygenase ausM
- Austinoid biosynthesis clusters protein J
- Austinoid biosynthesis clusters protein H
- Aldo-keto reductase ausK
Sequence:
MAMGNPELRTHFFRSSHEPGIPNSLRFPNGFLVTCGLPWLLLLFSVTIILFHPLRKKSDLPLINPGKGRIGILRGYRSRKTFTTELPRLVADGLSKASAFRIAAPDGVNIVLAPSYAHEIAEHPDLNPGPIAGDEFNSHINGFEVFAQLGTSDVISESVRTRLTRQLTKLTPLLTSETPLLLQSQWKDAPDWVEVSPHETALFILSRLSSLVFVGDDLGRNPDWIRILTSYNTEAFAAAEELNLWPQILRPLIARLKPSCRQLRRYIRDARALLVPVLEQRRHAQSQGDRREYNDAIEWLDETSRSTGQPYDPILSQMLLAIGSFHTSSDLLGQVLLDLCMRPDWKVLVRELRKEIISSLQGEGWDKIALNNLKLMDSVLKESQRLKPASTVTMGRYASREITLSDGTIIPKGSTVFIANVAMRDSNIYPDPDDFVPDRFTTRREKGDSSAYLVSASPEHLGFGLGRHACPGRFFAANELKIVLSHMLMKYDIKLPDNGAVAPSKSGIFLATNPDARICVRRRKEEIVI
Protein: AT2g04793 (Expressed protein) (Q94JV8)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
Sequence:
MLKMLSILRRNLQNLRKSPRVADESALPSTTVNGDHGGGNGSNGGIMKFPLSIMSCFSVPRVSRADGVWVSGDYGRVSEVNHLMVCDGMRYALLM
Protein: Tyrosine--tRNA ligase (EC 6.1.1.1) (Tyrosyl-tRNA synthetase) (TyrRS) (P0AGJ9)
Organism: Escherichia coli (strain K12)
Function: Catalyzes the attachment of L-tyrosine to tRNA(Tyr) in a two-step reaction: tyrosine is first activated by ATP to form Tyr-AMP and then transferred to the acceptor end of tRNA(Tyr). Can also mischarge tRNA(Tyr) with D-tyrosine, leading to the formation of D-tyrosyl-tRNA(Tyr), which can be hydrolyzed by the D-aminoacyl-tRNA deacylase. In vitro, can also use the non-natural amino acid azatyrosine.
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_02006, ECO:0000305}.
Interaction partners:
- Proline--tRNA ligase
- Asparagine--tRNA ligase
- Tryptophan--tRNA ligase
- Methionine--tRNA ligase
- Glutamine--tRNA ligase
- Arginine--tRNA ligase
- Isoleucine--tRNA ligase
- Valine--tRNA ligase
- Leucine--tRNA ligase
- Histidine--tRNA ligase
Sequence:
MASSNLIKQLQERGLVAQVTDEEALAERLAQGPIALYCGFDPTADSLHLGHLVPLLCLKRFQQAGHKPVALVGGATGLIGDPSFKAAERKLNTEETVQEWVDKIRKQVAPFLDFDCGENSAIAANNYDWFGNMNVLTFLRDIGKHFSVNQMINKEAVKQRLNREDQGISFTEFSYNLLQGYDFACLNKQYGVVLQIGGSDQWGNITSGIDLTRRLHQNQVFGLTVPLITKADGTKFGKTEGGAVWLDPKKTSPYKFYQFWINTADADVYRFLKFFTFMSIEEINALEEEDKNSGKAPRAQYVLAEQVTRLVHGEEGLQAAKRITECLFSGSLSALSEADFEQLAQDGVPMVEMEKGADLMQALVDSELQPSRGQARKTIASNAITINGEKQSDPEYFFKEEDRLFGRFTLLRRGKKNYCLICWK
Protein: At5g61220 (LYR family of Fe/S cluster biogenesis protein) (Q8L9E3)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- Frataxin, mitochondrial
- Photosystem II reaction center protein J
- Photosystem II reaction center protein L
- Photosystem II reaction center protein K
- Photosystem II reaction center protein H
- Cytochrome b559 subunit beta
- Cytochrome b559 subunit alpha
- Photosystem II reaction center protein I
- Photosystem II D2 protein
- Photosystem II reaction center protein T
Sequence:
MVSSSEVLSLCRALLRAGRQFPDYNIREYSKRRTLDGFRMNKNLTDPSKVTEAYAEAKKQLFVAERVLKVYLAYPPKTKNIMEVKLQ
Protein: Amelotin (Q3HS82)
Organism: Rattus norvegicus (Rat)
Function: Is a promoter of calcium phosphate mineralization, playing a critical role in the formation of the compact, mineralized, aprismatic enamel surface layer during the maturation stage of amelogenesis.
Subcellular location: Secreted {ECO:0000250|UniProtKB:Q9D3J8}.
Interaction partners:
- Odontogenic ameloblast-associated protein
- Enamelin
- Ameloblastin
- Secretory calcium-binding phosphoprotein proline-glutamine-rich protein 1
- Amelogenin, X isoform
- Kallikrein-4
- FAM20A, golgi associated secretory pathway pseudokinase
- Dentin matrix acidic phosphoprotein 1
- acid phosphatase
- Matrix metallopeptidase 20
Sequence:
MKTVVLLLCLLGSAQSLPRQLSPALGAPATKPTPGQVTPLTQQQPNQVFPSISLIPLTQLLTLGSDLPLFNPATMPHGTQTLPFTLGPLNGQQQLQPQMLPIIVAQLGAQGALLSSEELPLASQIFTGLLIHPLFPGAIQPSGQTGAKPDVQNGALPTRQAGASPANQATTPGHTTPAVTDDDDYEMSTPAGLQRATHTTEGTTMDPPNRTK
Protein: Deletion Meq (Q80IW4)
Organism: Gallid alphaherpesvirus 2
Interaction partners:
Sequence:
MSQEPEPGAMPYSPADDPSPLDLSLGSTSRRKKRKSHDIPNSPSKHPFPDGLSEEEKQKLERRRKRNRDASRRRRRAQTDYVDKLHEACEELQRANEHRGSRTGFLVFGPDLYSVSLGYSVYGLVVSR
Protein: Probable iron export permease protein FetB (P77307)
Organism: Escherichia coli (strain K12)
Function: Part of the ABC transporter complex FetAB, which is probably involved in iron export and enhances resistance to H(2)O(2)-mediated oxidative stress. Probably responsible for the translocation of the substrate across the membrane.
Subcellular location: Cell inner membrane {ECO:0000269|PubMed:24038693}; Multi-pass membrane protein {ECO:0000269|PubMed:24038693}.
Interaction partners:
- Probable iron export ATP-binding protein FetA
- Inner membrane protein YbbJ
Sequence:
MNSHNITNESLALALMLVVVAILISHKEKLALEKDILWSVGRAIIQLIIVGYVLKYIFSVDDASLTLLMVLFICFNAAWNAQKRSKYIAKAFISSFIAITVGAGITLAVLILSGSIEFIPMQVIPIAGMIAGNAMVAVGLCYNNLGQRVISEQQQIQEKLSLGATPKQASAILIRDSIRAALIPTVDSAKTVGLVSLPGMMSGLIFAGIDPVKAIKYQIMVTFMLLSTASLSTIIACYLTYRKFYNSRHQLVVTQLKKK
Protein: Putative uncharacterized protein KIRREL3-AS3 (KIRREL3 antisense RNA 1) (KIRREL3 antisense gene protein 1) (Proline-rich protein 10) (Q8N7Y1)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MEKRGESLDLGVRCKRGEERDRRPCWKPSRPGAARGGRGLWTVGGGGSPTETAESQQLGKPPEFWVSAHPGWLQVSCAHRASRWDASRWHPLQRFFARRGVRRPNPSVPSPLPKPPVPSAGSCEPLAPPPTSASGASRSWVTQTLAEAGAYRGCRPAPGSAAGWPRSDRRARLPRKASKPCSPALPSLAACCPQGFLRSGTKRVMCKVLGPGAGVRGTAVECSEQAGVWAHCRPQLTATFS
Protein: protein-tyrosine-phosphatase (EC 3.1.3.48) (G5EDC5)
Organism: Caenorhabditis elegans
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004479}; Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004479}.
Interaction partners:
Sequence:
MQSSSILIYLLTVVGCSIAFLDNTLPLYLFKNLDTKETSTVQTGLVTDKVRRVPPYFSYKLERQYVVGVGGNINLTCVAVGYPMPRVFWKKTDLMVLDDPSTAPIGKNVLTLTHVESTENFTCVAVSALGNIEATTTVIAKELPPPPVNIVVSSVTSESVVITWKPPKYNEAINKYVVNYRLKSENKDDAALFAKDSRAEDESDSERYSEGRSSRGKTMETLENSLVIDGLVAFQTYEFTVRSAGPVGVGLESLPVEAQTKPSKPATAPVSPQARSLNRDSILVKWGPCEQPNGLITGYKVYYTNDLVTTPIREWKQHDAKSDEFMTTINGLEPDSRYFVRVIAQNSEGDSPLSTLVTVATRQGIPGQPPMLTVKALDSRRMQLTWDKPLYSSPVVGYTVRYNTSDGEKELTLTSPHEKHVVTGLHPDKYYYFRVAAYSDRGQGEFTEPMISKTIASIPLSSPTIVSAAATSSKSVEIRWKGPEQKKLNGVLTAYRINYFRLEDSKTANLESVEYDEDMDDSSSFLDRMSVVVPSDATSYVLSDLLPYSSYEITVAASTMDGYGPESSIRVVKTLEDVPSAPRNFNAELTSATSVKLTWDAPAAANGALLGYYVYLDRMVNGEPVVEKGSKKRIVMIRDSSKRYFELDSLDPNTEYSFRLNAFNRNGDGEFSERKSIITQGIPPEAPEIVSVSLDRDEPPVVARIEWKMPKMKPNETPIEKYNLWLRAQGYPDSYVKAKTVDGTDLSTTISGLWMGVVYDVLLAAENREGRSQNATETIATPVGSPDGEPIDVQYEVMKGKIVVSWRPPSEEKRNGNITSYKAILSAMDATADRYEQPVPAPSTSSTFEVNVRRAYLFKVAAATMKGIGPYSPVLTINPDPAALVGPPTNVRVEATSNSTAVVQWDFESQKADSFVVKYMHEPGNRMDTEKWKQLPVVSIDKENPKRFAVVSDLNAHKPYAFCVLAVKNNRQGPCSDPPTVLESVTPTYMVQNLRVLWKTSNSVQLTWEYNGPRNVGFYVNHTGRKDYVNHELQEKTMSTPGFGQDVDEKHREYLWTNLRPHMMYTIHVGVRTLPPGARKYWPQEVVTITDPTGPPFVDVPKLVDSSGTQPGQQMIRLTPATEEYGPISHYWIILVPANYSTEDVVNLDPIELEKATAEKRAQLARSLSVSPSKKLKRKASEVGDDSQSASYHPKEKRARRATVPGAYVTARLSADRVKQQYRNNQPFIVGDSQLYDGFTNYPLEHNLHYRLMMRAFAKNDVRTKDSFEQRAPMSEKLSRMYSDSVLTEPFTIKSALRGASQKSSPWVGACIAFLVLFSIVGMLICWWLRCNKKSAGRHPRHGSITKVALTGNIMNGGGGIPGETSKLLSTSNEYGRQIMNPYEQMNGNHHMESSMDLYPLPTSHSRSNGYAPVPVAIPSLPNNGNNMTTVSHPAVPIAELANHIERLRMNNNAGFQSEFESIETGQHFTWEHSSADMNKHKNRYANVAAYDHSRVVLSNVEGYPGMDYINANYVDGYDKPRSYIATQGPLPETFSDFWRMVWEEQSVTIVMLTNLEERSRVKCDQYWPSRGTATYGDIEVTLLESVHLAHYTMRTMRLKMVGEPEVREIKHLQYTAWPDHGVPDHPTPFLIFLKRVKTLNPNDAGPIISHCSAGIGRTGAFIVIDCMLERLRYDNTVDIYGCVTALRAQRSYMVQTEEQYIFIHDAVLDAVNSGSTEVPASRLHQHLHILSQPSADQLSGIDMEFRHLTTLKWTSNRCTVANLPVNRPKNRMLSAVPYDSNRVIMRLLPGADGSDYINASWIDGYKERGAYIATQAPTNETAADFWRAIWEHNSPIIAMLVRTNERGQEQCSDYWPLETGVQVGMLVVEPMAEYDMKHYHLREFRISDINTREVRTVRQFHFMEWPDVGKPHTADHFLDFVTQVHNTYAQFGCTGPITVHCCSGAGRTAVFIALSIILDRMRAEHVVDVFTTVKLLRTERQNMIQEPEQYHFLYLAAYEYLAAYDNFS
Protein: Zinc finger protein mex-5 (Q9XUB2)
Organism: Caenorhabditis elegans
Function: Functions with mex-6 to affect embryonic viability, establish soma germline asymmetry in embryos and establish plk-1, pie-1, mex-1, and pos-1 asymmetry in embryos. Also affects formation of intestinal cells. Binds to mRNA in vitro, and inhibits pgl-3-mediated P-granule formation, probably by competing with pgl-3 for binding to mRNA.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:18199581, ECO:0000269|PubMed:18842813}.
Interaction partners:
- RNA-binding protein pos-1
- PUM-HD domain-containing protein
- LDL receptor repeat-containing protein egg-1
- Chondroitin proteoglycan 1
- CCCH-type zinc finger protein oma-2
- CCCH-type zinc finger protein oma-1
- Pumilio domain-containing protein 5
- Chitin-binding domain protein cbd-1
- Inactive protein-tyrosine phosphatase egg-5
- K Homology domain-containing protein
Sequence:
MKAASNSVSSAGGSVSPTTTQPPLPPGQSSHPQIYDQQMQYYFAAAMPNQPMATYAAQNGSSQQYAPAAPYYQDANGQYVQVPANGSMAPQQHMMVSGQPYLYMAQPQQGAQQVMQSGQPQLIYYQQSMAPQAAPMYFHPMQAAPMLPEQMGVMPHTQPAIPPQQQPRQVGVEISSTRTAPLTSSTPLPTSLEYETVQRDNRNRNIQFRYHRVMEHDELPIDEISKITLDNHNDDTMSAEKENHFHEHRGEKFGRRGFPIPETDSQQPPNYKTRLCMMHASGIKPCDMGARCKFAHGLKELRATDAPARYPNNKYKTKLCKNFARGGTGFCPYGLRCEFVHPTDKEFQNIPPYQRMSHDDQDYDQDVIPEDYVVARHQPRFMRTGGRATTPTKVMLKHRNVAGSMMCLSNAGRDLQAGGDYNQPESNEDDLPPHLRRNRRENPPMNKRRTSLSTKWTSEENLGLRGHY
Protein: FERRY endosomal RAB5 effector complex subunit 3 (D4A770)
Organism: Rattus norvegicus (Rat)
Function: Plays a role in mast cell degranulation.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:25122211}. Early endosome {ECO:0000250|UniProtKB:Q9NQ89}.
Interaction partners:
- Structure-specific endonuclease subunit SLX1
- Exocyst complex component 8
Sequence:
MKKNRERFSSKEREFVYKFQIGSERLELRVPLRFPVDENASHLHGRLMLLHSLPCFIENDLKEALARFIEEESLRDHDSDAEACLEAVKSGEVDLHQLASTWAKAYAETTLEHARPEEPNWDEDFADVYHDLIHSPASETLLNLEHNYFVSISELIGERDVELKKLRERQGIEMEKVMQELGKSLTDQDVNSLAAQHFESQQDLENKWSNELKQSTAIQKQEYQEWVIKLHQDLKNPNNSSLSEEIKVQPSQFRESADAAGRIYEEQRKLEESFTIHLGAQLKTMHNLRLLRADMLDFCKHKRTQGSGVKLHRLQTALSLYSTSLCGLVLLVDNRINSYSGIKRDFATVCQECTDFHFPRIEEQLEVVQQVALYARTQRRSKCKEARDSGNQNGGSDEKSKNAERNYLNILPGEFYITRHSNLSEIHVAFHLCVDDNVKSGNITARDPAIMGLRNILKVCCTHDITTISIPLLLVHDMSEEMTIPWCLRRAELVFKCVKGFMMEMASWDGGISRTVQFLVPQSISEEMFYQLSNMLPQIFRVSSTLTLTSKH
Protein: B-type flagellin (P72151)
Organism: Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Function: Flagellin is the subunit protein which polymerizes to form the filaments of bacterial flagella.
Subcellular location: Secreted. Bacterial flagellum.
Interaction partners:
- B-type flagellar hook-associated protein 2
- Flagellar secretion chaperone FliSB
- Flagellar hook-associated protein 1
- Flagellar hook-associated protein type 3 FlgL
- Flagellar hook protein FlgE
- Flagellar motor switch protein FliG
- Flagellar basal body rod protein FlgB
- Flagellar M-ring protein
- Flagellar motor switch protein FliM
- Basal-body rod modification protein FlgD
Sequence:
MALTVNTNIASLNTQRNLNASSNDLNTSLQRLTTGYRINSAKDDAAGLQISNRLSNQISGLNVATRNANDGISLAQTAEGALQQSTNILQRIRDLALQSANGSNSDADRAALQKEVAAQQAELTRISDTTTFGGRKLLDGSFGTTSFQVGSNAYETIDISLQNASASAIGSYQVGSNGAGTVASVAGTATASGIASGTVNLVGGGQVKNIAIAAGDSAKAIAEKMDGAIPNLSARARTVFTADVSGVTGGSLNFDVTVGSNTVSLAGVTSTQDLADQLNSNSSKLGITASINDKGVLTITSATGENVKFGAQTGTATAGQVAVKVQGSDGKFEAAAKNVVAAGTAATTTIVTGYVQLNSPTAYSVSGTGTQASQVFGNASAAQKSSVASVDISTADGAQNAIAVVDNALAAIDAQRADLGAVQNRFKNTIDNLTNISENATNARSRIKDTDFAAETAALSKNQVLQQAGTAILAQANQLPQAVLSLLR
Protein: AP2/ERF family protein (Aptella 2-like transcription factor) (A2WVZ6)
Organism: Oryza sativa subsp. indica (Rice)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MAPRAATVEKVAVAPPTGLGLGVGGGVGAGGPHYRGVRKRPWGRYAAEIRDPAKKSRVWLGTYDTAEEAARAYDAAAREFRGAKAKTNFPFASQSMVGCGGSPSSNSTVDTGGGGVQTPMRAMPLPPTLDLDLFHRAAAVTAVAGTGVRFPFRGYPVARPATHPYFFYEQAAAAAAAEAGYRMMKLAPPVTVAAVAQSDSDSSSVVDLAPSPPAVTANKAAAFDLDLNRPPPVEN
Protein: Auxin-responsive protein IAA27 (Auxin-induced protein 27) (Indoleacetic acid-induced protein 27) (Phytochrome-associated protein 2) (Q9ZSY8)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Aux/IAA proteins are short-lived transcriptional factors that function as repressors of early auxin response genes at low auxin concentrations. Repression is thought to result from the interaction with auxin response factors (ARFs), proteins that bind to the auxin-responsive promoter element (AuxRE). Formation of heterodimers with ARF proteins may alter their ability to modulate early auxin response genes expression.
Subcellular location: Nucleus {ECO:0000250}.
Interaction partners:
- Auxin response factor 7
- Auxin response factor 9
- Auxin response factor 5
- Protein TRANSPORT INHIBITOR RESPONSE 1
- Auxin response factor 18
- Auxin response factor 22
- Auxin response factor 8
- Auxin transporter protein 1
- Auxin-responsive protein IAA31
- Auxin-responsive protein IAA6
Sequence:
MSVSVAAEHDYIGLSEFPTMEATTMSDKTKTRDNNNGLNFKATELRLGLPGSESPERVDSRFLALNKSSCPVSGAKRVFSDAINDSNKWVFSPGSTTATGDVGSGSGPRTSVVKDGKSTTFTKPAVPVKEKKSSATAPASKAQVVGWPPIRSFRKNSMASSQSQKPGNNSETEEAEAKSGPEQPCLYVKVSMEGAPYLRKIDLKTYKSYLELSSALEKMFSCFTIGQFGSHGGCGRDGLNESRLTDLLRGSEYVVTYEDKDSDWMLVGDVPWEMFICSCKKLRIMKSSEAIGLAPRVMEKCRSRN
Protein: Galactocerebrosidase (EC 3.2.1.46) (Galactosylceramidase) (Q7ZUD5)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
Sequence:
MYIGNQCCVVLSIFLYISGCLGENYDIDDSLGLGQTFDGIGGLSGGGATSRLLVNYEEPYRSQILDYLFKPKFGASLQILKVEIGGDAQTTDGTEPSHMHYEDDENYFRGYEWWLMVEAKKRNPNITLIGLPWAFPGWVGNGKNWPYDFPDITASYVVAWIHGAKKYHDLDIDYIGIWNEKSFNVKYIKLLRYLLDKRGLEKVKIIASDDLWEPITSAVFADKELYDAIEVLGVHYPGTKTVPRALKTGKKLWSSEDYSTFNDNVGGGCWARILNQNYVNGKMTATISWNLVASYYENLPFGRDGIMTANEPWSGNYVVESPVWTTAHTTQFTEPGWTYLQTVGHFTHGGSYVALTDQRGNLSIITETMTHDHSVCIRPPLRPYNVTVQNVTFNLKGTFAFISQLDVWHSKFDFKTDKTVLFQKLDPVKVIGGSFSIELDVDEIYTFTTITNGQRGTYPDPPPSAPFPKSYRDDFNVSGNFSEAPNFADQTGVFEYFTNLTDPGPHVFTLRQVVTQRPITWAADADQTISVIGDYGWHDIMVSCDVYMEAVQTGGVFIAARVDRGGGVIRSTRGVFFWVYADGTYKITNDLRGLAVLAKGSAGTRARTWYTLTLRVQGNYASADLNGYSLWKNAVLLNPLHGWVAIGTSSFQLAQFDNFVIEAE
Protein: Monothiol glutaredoxin-S2 (AtGrxS2) (Protein ROXY 10) (Q8L8Z8)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: May only reduce GSH-thiol disulfides, but not protein disulfides.
Subcellular location: Cytoplasm {ECO:0000250}.
Interaction partners:
- Peroxiredoxin-2D
- Protein disulfide-isomerase 5-1
- Glutaredoxin-C3
Sequence:
MDMITKMVMERPVVIYSKSSCCMSHTIKTLLCDFGANPAVYELDEISRGREIEQALLRLGCSPAVPGVFIGGELVGGANEVMSLHLNGSLIPMLKRAGALWV
Protein: SET domain protein, putative (EC 2.1.1.43) (Q8I352)
Organism: Plasmodium falciparum (isolate 3D7)
Interaction partners:
Sequence:
MSKIRKKLLENKKEIGFCSCVIKVKEKKEIEENKDINGNKAKVWLEHFNDIISEDIKNMMNNKNRLKLHKSLNLINNLQLYNNRVGGKNINVLLNNPFGFDLNKIVNEKIKEKENQNNNNNFDDDKVNNSTELSRNNTKVSYDDYIWNNEMKRYMSLKESQSVYQFNGTNSKRNKTCFDVSNSNHHNRSMNDKMKILKSENLYINNNDDNNRYNISLRNVDVHNNLSISKKKEESTIFNNNNNIDDDEHTKKKETYLKISSNKKNNNKITYDFNHINQRNNYNYHGLYINEKEKKDRLNNEIFNESYDIKYKTIQQNYNNILIIQDKNNKKAKIVANKKVEVGQILFIEHELLETAILFDDLWETFNMLNEDQKKQIDYIIHLKYYKNEYDNVTNINNNEPVIKEDGYLKEKKNIPHRNDNNTNNDHHNKNNMTNQNAMVFKEFTNSNNNNNNNNIYKESINNFRNDRFIDKLIQFEKFTDILKNSFISSSNKSKIKLFKHASFLNHSCFPNASYCFIDDKNICLLAMRTINMYDEITISLINELYTSIQYRNEKLNKIKNITCSCNRCLQIIDEERNILCAACKYSYVSKKINQNYMPTIMYQQKNFKQKDDKNENDMENQSHNNNLLKYNTLNGEEKNSINTTNYKNKEIFDENNLYKYSNTTNYNETHINEYEYNNISKNNLGKNNIVSEKIQGNITYPSDIAYTNLLNDSEDSKIHNADNINKSQNLLFGMKYKEISQNKLDHEKRLDEIYVEHHLPRNNKSLHNICNNNTFCLANENVYDFNKSKTELIIKNNIKKRTNKKDNIEDPNMFNSENVLLSSTSLYNNKYNNDKNNRNNKYNNIKNYGCNNNNMGIEQTRCLTNNNINLNVLCNSHLPFSIKLKNNFLHILNVKNAEDEKIGYCKFVNNEEWICAICNNSISKYVMPLKSEYYFIIQYNAIKEKINTNNFELSILISNIEETLSYIISILGEKHWLYASFNYIIADICFSLYTMNSLNENYISTCFNAFYNFFYFIQIQCPQAIHTDLVPLVLKFFIICIYTGNYNTIYNLATSGFLELIKQKYGSWDVSYICLQRAFKMCYEHMHNRKIMDRTTILTLADMANNNILNMVH
Protein: Cytochrome c-type biogenesis CcmH-like mitochondrial protein (AtCCMH) (Q9XI46)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Plays a central role in mitochondrial cytochrome c maturation. Probable component of a heme lyase complex involved in the reduction of apocytochrome c. Forms a complex with CCMF proteins (CCMFC, CCMFN1 and CCMFN2) that performs the assembly of heme with c-type apocytochromes in mitochondria.
Subcellular location: Mitochondrion inner membrane {ECO:0000269|PubMed:16236729}; Single-pass membrane protein {ECO:0000255}.
Interaction partners:
- Cytochrome c biogenesis CcmF N-terminal-like mitochondrial protein 2
- Cytochrome c-type biogenesis protein CcmE homolog, mitochondrial
- Cytochrome c biogenesis CcmF N-terminal-like mitochondrial protein 1
- Cytochrome c biogenesis FN2.
- Cytochrome c biogenesis FN1
- Cytochrome c-type biogenesis ccda-like chloroplastic protein
- Surfeit locus protein 1-like
- Surfeit locus protein 1
- Cytochrome c biogenesis FC.
- Cytochrome c biogenesis CcmF C-terminal-like mitochondrial protein
Sequence:
MEKTDEERKKAQMLDARARNISHNVRCTECGSQSIEDSQADIAILLRQLIRNEIGAGKTDKEIYSKLEDEFGETVLYAPKFDLQTAALWLTPVIIAGGTAAGIVYQKHRLRKNVDIMALNLIRGVPLTPKERVTILDVLIPPSPPPQGVVSRLRRWLNR