wanglab/gogpt-training-data huggingface dataset:
Protein: Ras-like protein 2 (EC 3.6.5.2) (P04388)
Organism: Drosophila melanogaster (Fruit fly)
Function: May be involved in endocytic processes and/or other transport pathways mediated by vesicle trafficking. May interact functionally with ROP protein. Ras proteins bind GDP/GTP and possess intrinsic GTPase activity.
Subcellular location: Cell membrane {ECO:0000305}; Lipid-anchor {ECO:0000305}; Cytoplasmic side {ECO:0000305}.
Interaction partners:
- Ras-like protein 1
- Inosine-5'-monophosphate dehydrogenase
- Raf homolog serine/threonine-protein kinase Raf
- non-specific serine/threonine protein kinase
- Neurofibromin 1, isoform B
- cAMP-dependent protein kinase catalytic subunit 1
- cAMP-dependent protein kinase catalytic subunit 2
Sequence:
MQMQTYKLVVVGGGGVGKSAITIQFIQSYFVTDYDPTIEDSYTKQCNIDDVPAKLDILDTAGQEEFSAMREQYMRSGEGFLLVFALNDHSSFDEIPKFQRQILRVKDRDEFPMLMVGNKCDLKHQQQVSLEEAQNTSRNLMIPYIECSAKLRVNVDQAFHELVRIVRKFQIAERPFIEQDYKKKGKRKCCLM
Protein: Cathepsin L-like cysteine proteinase (Q6E7B6)
Organism: Brugia malayi (Filarial nematode worm)
Interaction partners:
Sequence:
MRHYLLSPLKAFLFLSFLQISILSCSSLIYQQFKALSHSKLRALYSKHYDDYVKFVTEYKQGVKDNRPEPHRLLAYAKNVEEIQKHNELYKQGKSSFMLGLTVMSDMAEEDMQDEFPVIKFNDTDDSHIPQNLTHLVKAVNWVTNKYVTAVRNLKIDRRFCPGASSASAVADVVEALAKSQTKKLRKLSIQELLDCSGSGCRSYGDFDKYSIYLMEKRGLVCENNYPYVRAEKTCLVKGQRHGKVSNMLHARQGHQTLFKALLSKGPVATRVLVTPNFINYKEGIFRHNCQPNAYSHTVLAVGFTDTYVLIKNSWGTDWGEKGYMRISINPKENCNLYLESLAAM
Protein: Septin-2A (Septin-A) (XlSeptA) (Q9DE33)
Organism: Xenopus laevis (African clawed frog)
Function: Filament-forming cytoskeletal GTPase. Required for normal organization of the actin cytoskeleton. Plays a role in the biogenesis of polarized columnar-shaped epithelium. Required for the progression through mitosis through regulation of chromosome congression. During anaphase, may be required for chromosome segregation and spindle elongation (By similarity). Probably plays a role in ciliogenesis and collective cell movements including convergent extension during gastrulation. In cilia, required for the integrity of the diffusion barrier at the base of the primary cilium that prevents diffusion of transmembrane proteins between the cilia and plasma membranes. Controls cell shape and not polarization of cells during convergent extension.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:20671153}. Cytoplasm, cytoskeleton {ECO:0000250}. Cytoplasm, cytoskeleton, spindle {ECO:0000250}. Cleavage furrow {ECO:0000250}. Midbody {ECO:0000250}. Cell projection, cilium membrane {ECO:0000250}. Note=Localizes at the base of the cilia near the morphological distinction between the cilia and plasma membranes (By similarity). Cytoplasm, cell cortex. {ECO:0000250}.
Interaction partners:
Sequence:
MSKQQAQFTNPETPGYVGFANLPNQVHRKSVRKGFEFTLMVVGESGLGKSTLINSLFLTDLYPERVVPGAADKIERTVDIEASTVEIEERGVKLRLTVVDTPGYGDAMNCVDCFKPIISYVDNQFERYLHDESGLNRRHIVDNRVHCCFYFISPFGHGLKPLDVEFMKALHNKVNIVPVIAKADTLTLRERERLKRRVLDEIEEHGIKIYQLPDAESDEDEDFKEQTRLLKASIPFTVVGSNQLIEAKGKKVRGRLYPWGVVEVENTEHNDFLKLRTMLITHMQDLQEVTQDLHYENFRSERLKKGVTSSKVEHVEVTKDQILQEKEAELRRMQEMITRMQAQMQIQGQSGDAQHL
Protein: Beta-secretase 1 (EC 3.4.23.46) (Beta-site amyloid precursor protein cleaving enzyme 1) (Memapsin-2) (Membrane-associated aspartic protease 2) (Q6NZT7)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004251}; Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004251}. Cell projection, axon {ECO:0000256|ARBA:ARBA00004489}. Cell projection, dendrite {ECO:0000256|ARBA:ARBA00004279}. Cell surface {ECO:0000256|ARBA:ARBA00004241}. Cytoplasmic vesicle membrane {ECO:0000256|ARBA:ARBA00004156}. Early endosome {ECO:0000256|ARBA:ARBA00004412}. Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00004240}. Golgi apparatus, trans-Golgi network {ECO:0000256|ARBA:ARBA00004601}. Late endosome {ECO:0000256|ARBA:ARBA00004603}. Lysosome {ECO:0000256|ARBA:ARBA00004371}. Membrane raft {ECO:0000256|ARBA:ARBA00004285}. Recycling endosome {ECO:0000256|ARBA:ARBA00004172}.
Interaction partners:
Sequence:
MRAARLLLLCGVAVCVARLCASSGPALLRVPLRQGPLTPHSTPAAHRSPHGPRARSRRAASGISFINMIDNLRGKSGQGYYIEMAVGSPAQRLNILVDTGSSNFAVGAAAHPFLHRYYHRSLSSSYRDLGRGVYVPYTQGRWEGELGTDVVSVPCGPNVSLRANIAAITQSDRFFINGSNWEGILGLAYAEIARPDETLEPFFDSLLRQSTVADVFSLQLCGAGYNHNYSTGSSSTVGGSMIIGGVDPSLYVGELWYTPIRREWYYEVIIVRIEVNGQDLNMDCKEYNYDKSIVDSGTTNLRLPRKVFQAAVKAIEAASSTEQFPSGFWLGEQLVCWQAGTTPWHIFPVISLYLMSENRNQSFRISILPQQYLRPVEDVASAQEDCYKFAVSQSSTGTVMGAVIMEGFYVVFERQHKRIGFAVSTCHVHDEFRTAAVEGPFHGLDLEDCGYNVPQTDESTLMTIAYIMAGICALFMLPLCVMVCQWRFTCCLQPADGSDDISLLK
Protein: Polycystin-2 (Polycystic kidney disease 2 protein homolog) (H2LRU7)
Organism: Oryzias latipes (Japanese rice fish) (Japanese killifish)
Function: Component of a heteromeric calcium-permeable ion channel formed by PKD1 and PKD2 that is activated by interaction between PKD1 and a Wnt family member, such as WNT3A and WNT9B. Can also form a functional, homotetrameric ion channel (By similarity). Functions as non-selective, voltage-gated cation channel. Required for normal oscillation of Ca(2+) levels within cilia; these oscillations of the intraciliary Ca(2+) levels can trigger cytoplasmic Ca(2+) signaling cascades (By similarity). May contribute to the release of Ca(2+) stores from the endoplasmic reticulum (By similarity). Plays a role in fluid-flow mechanosensation: forms a complex with pkd1l1 in cilia to facilitate flow detection in left/right patterning. Required for normal specification of the body left-right axis during embryogenesis.
Subcellular location: Cell projection, cilium membrane {ECO:0000269|PubMed:21307098}; Multi-pass membrane protein {ECO:0000269|PubMed:21307098}. Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q13563}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q13563}. Cell membrane {ECO:0000250|UniProtKB:Q13563}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q13563}. Basolateral cell membrane {ECO:0000250|UniProtKB:Q13563}. Cytoplasmic vesicle membrane {ECO:0000250|UniProtKB:Q13563}.
Interaction partners:
- Polycystic kidney disease 1a
- Polycystic kidney disease 1 like 2a
- Exocyst complex component 5
Sequence:
MSATRVRPQSQAGTDKPPRTLDSSEGIEMENIQHQDPGLGGVAGSPSPPSRQAWSRDNPVFEPEEEIMQADWPQASPGRRSAFTASGGSSCSSGHGGYTRAGSSTQIPRGGLYPTQTLNGQQQDRHEHPGCMKRIFQNIRILWGTELMEDGDSNRERYLWNVLRELLTYIAFLITICILTYGMISTNMYYYTKAMSQLFLDAPLSSENPKTFRSLSTMEDFWKYTQGPFLGGMYWEVWYNNQSLPGNQSFIYYENILLGVPRLRQVRVHNETCSIHEDLRDEVQGCYGVYTPSNEDNSPFGPQNGTAWVHTTESKMNASTHWGQVSKYGGGGYYQDLSRTREESGLQLQFLKDHLWLDRGTRAIFLDFSVYNGNVNLVCIARLLVEFPATGGVLTSWQFQTLRLIKYVSSWDYFVGVCEVAFCLFVLYYVVEEVLEIHIHRLHYFKNLWNCLDVLIVTLSVVAIIMSITRAAMGGDLLKGLENYTSHTSFDSLANLQVQFNNMAAVIVFFCWVKLFKFINFNKTMSQLSTTMSRCAKDLVGFAIMFFIIFLAYAQLAYLVFGTQVNDFSTFQGSVFTQFRIILGDFDFFEIKEANPVLGPIYFITFVLFIFFILMNMFLAIINDTYSEVKADMAQHRSEMEMTDFIKKGCTKALVKLRLKKTTVDDISDSLRQAGGKLNYDELLQDLKEKGHTEAEIQAIFAKYDQDGDLELTEHDHQQMRDDLEKEREDLDLERNSLTRPSSGRSFPRTQDDSEEDDDEDSGHSSRRRGSSSGGVSYEEFQVLVRRVDRMEHSIGSIVSKIDAVIVKLEGMERAKLKRRDVLVRLLDGVMEDERLGRDADTHREQMERLVKEELERWETDDVASQVSHPQPATPIGPRPRPPSSLSTDGLDTSANGGTHV
Protein: Tehao (Q58SL5)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
FCLGLSPQCTCAAEGNVVRFHCPDEYAMLLEVSEPGASLYMSYYASTELQWLPRFNISSLVXIXFDAXIFWXEXXLSDLLKTLGVQTVKTIIFRDRTLETVVTRDVLNSGNGYMETSQPENITTWHFGSVPGLKKFKFFSHVPELQESIFHGFDTLRDLHLSVNVTTLPGNMLSTVNGTLKTLTIESPGIVSFGNPLLRELQQLRNLSLALIHPFHERDKQLQPHFFGSMTNLEEVRLASATSSVNRSMFKGTNKLQLIKMNGNDDLMELPGEIFLDQVNLKTLDLSCNAIVTLHEDVFKGLGNLTLLDLSKNRLTNLS
Protein: Prospero homeobox 1a (Prospero homeobox protein 1a isoform X2) (F1QAE1)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- Lymphatic vessel endothelial hyaluronic receptor 1b
- Vascular endothelial growth factor C
- Vascular endothelial growth factor receptor 3
- Hematopoietically-expressed homeobox protein hhex
- SRY-box transcription factor 18
- Collagen and calcium-binding EGF domain-containing protein 1
- Actinodin1
- COUP transcription factor 2
- Lymphatic vessel endothelial hyaluronic acid receptor 1a precursor
- Fli-1 protein
Sequence:
MPDHDSTSLLSRQTKRRRVDIGVKRTVGQASVVFTRAKATFLSAMNPHGSEQDVECSVVQHADGEKSNVLRKLLKRANSYEDAVMPFPGATIISQLLKNNLTKNGGSEPNFQGSGLSSTGSEMQQEDACSNSSRGSPQECLSPFSRPSMTQFEMERLTDEHLRAKRARVENIIRGMSHSPSVTLRAGDNDREGAAQPPSPRENYRENKRKQKLPQQQQQSFQQLVSARKEQKHEERRQLKLQLEDMQKQLRQLQEKFYQIYDSTDSENDEDGNLSEDSMRSDGMDNRAHDSVPDRSDNEMSDLDPGHFLDRARALIREQSMMEGDKPKRDGSRGKSQGPTSMHAEGKQLAETLKQELNTAMSQVVDTVVKVFAKPPRPVPQVFPPLHMESPDRFAVNGENPNFHTANQRLQCFGDVIIPNPLDTFASMQVPNSNDQTEALPLVVRKNSSDQTGSLSTPGGHHHHPSLHPPPLSSTMGFSPPSFRHPFPLPLMGYPFQSPLGAPTGPYPGKDRSSPESLDLSRETTSLRTKMSSNHLSHHRSISPTHPGNEGLSLSLIKSECGDLQDMSDISPYSGSTIQEGLSPNHLKKAKLMFFYTRYPSSNMLKMFFSDVKFNRCITSQLIKWFSNFREFYYIQMEKFARQAINDGVTGSEELSVSRDCELFRALNMHYNKANDFEVPERFLEVAQITLREFFNAIVAGKDVDPSWKKAIYKVICKLDSEVPEIFKSPNCLQELLHE
Protein: Matrix metallopeptidase 14b (membrane-inserted) (Matrix metalloproteinase-14b isoform X1) (B0R0I1)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004479}; Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004479}.
Interaction partners:
- Matrix metalloproteinase 2.
- Matrix metallopeptidase 14a
- Tissue inhibitor of metalloproteinase 2.
- Matrix metallopeptidase 13b.
- Heparan sulfate proteoglycan 2.
- Decorin
Sequence:
MIWSGFTRLLLLIFVCAHRSSSKQDMKPEAWLQQYGYLPPGDLRTHTARSPQSVPSAIAAMQRFYGLTVTGNLDANTLEAMKRPRCGVPDKFGSELKSNLRKKRYAIQGLKWDKNEITFCIQNYTPKVGEYETFEAIRKAFKVWESVTPLRFREISYSDIRDKVVDFADIMLFFADGFHGDASPFDGEGGFLAHAYFPGNGIGGDTHFDAAEPWTIGNKDLLGNDVFLVAVHELGHALGMEHSNDPSAIMAPFYQWMETDHFVLPDDDRKGIQKLYGPGSGGHPRTPVTPETPHHTPYPTPYRPGGPSYGPNICEGHFDTIGIFRGEMFVFKGKWFWRVRNNQVMENYPMPIGHFWRGLPTDINAAYEREDGKFVFFKGDRHWVFTESNLEPGYPKVLGELGSGVPKDKLDAALLYTPTGYTYFFRGNKYYRYNEDTHSVDPDYPKPISKWQGVPDNIKAAFMSRDQGYTYFYKANKYWKFNNQLLKVEPGYPKSALKDWMGCPNEDSNTGGGGSDRDRERERERERERERERERAREREREQDRTNEVDKTEEEGKKEETEVLIIEVEDAPSSRGGAAAVVVPLMLLVCVIFTLGALLFFRRYGTPRRLLYCQRSLLDKV
Protein: At1g21440 (Phosphoenolpyruvate carboxylase family protein) (Q501F7)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- 3-isopropylmalate dehydratase small subunit 3
- 3-isopropylmalate dehydrogenase 3, chloroplastic
- Malate synthase
- Molybdenum cofactor sulfurase family protein
- Amino-terminal region of chorein
- Aspartate aminotransferase, cytoplasmic isozyme 2
- Reactive Intermediate Deaminase A, chloroplastic
- 3-isopropylmalate dehydratase small subunit 1
- Peptide methionine sulfoxide reductase A2
- GDSL esterase/lipase At3g14220
Sequence:
MSMLMAAKSTSLFSSNPTISAKIGQNPRGVRSVYPTVRMQSRVHRLIEEQGAVLIPGVYDALSAAIVQQTGFSAALISGYALSAVTLGKPDFGLITPPEMAATARSVCAAAPKIPIIADADTGGGNALNVQRTVKDLIAAGAAGCFLEDQAWPKRCGHMRGKEVIPAEEHAAKIASARDAIGDADFFLIARTDARALSAKTGLSDAIDRANLYMEAGADASFVEAPRDDDELKEIGRRTKGYRLCNMLEGGRTPLHTPDELKEMGFHLIAHPLTSLYASTRALVDVLKILKEKGTTKDHLEKMITFEEFNRLVNLDSWYELETKYSNLRNALGETK
Protein: Uncharacterized protein At4g37920 (Q84WN0)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- NAD
- NADH dehydrogenase iron-sulfur protein 7, mitochondrial
- NADH dehydrogenase subunit 7
- NAD
- NADH dehydrogenase subunit 9
- NADH dehydrogenase iron-sulfur protein 2
- NAD
- NADH dehydrogenase iron-sulfur protein 3
- NADH dehydrogenase iron-sulfur protein 8-B, mitochondrial
- NADH dehydrogenase iron-sulfur protein 8-A, mitochondrial
Sequence:
MANLLETSIFFSSADKLLSFPPKNSQTHHLPFSAFINGGRKIRKSSTITFATDTVTYNGTTSAEVKSSVEDPMEVEVAEGYTMAQFCDKIIDLFLNEKPKVKQWKTYLVLRDEWNKYSVNFYKRCRIRADTETDPILKQKLVSLESKVKKIDKEMEKHNDLLKEIQENPTDINAIAAKRRRDFTGEFFRYVTLLSETLDGLEDRDAVARLATRCLSAVSAYDNTLESVETLDTAQAKFEDILNSPSVDSACEKIRSLAKAKELDSSLILLINSAYAAAKESQTVTNEAKDIMYHLYKATKSSLRSITPKEIKLLKYLLNITDPEERFSALATAFSPGDDHEAKDPKALYTTPKELHKWIKIMLDAYHLNKEETDIKEAKQMSQPIVIQRLFILKDTIEDEYLDKKTIVADETPKKEEEDTTIEDFLN
Protein: ABC transporter patM (Patulin biosynthesis cluster protein M) (B6RAL1)
Organism: Penicillium expansum (Blue mold rot fungus)
Function: ABC transporter; part of the gene cluster that mediates the biosynthesis of patulin, an acetate-derived tetraketide mycotoxin produced by several fungal species that shows antimicrobial properties against several bacteria (Probable). May be involved in the secretion of E-ascladiol to be converted to patulin by the secreted patulin synthase patE (Probable).
Subcellular location: Vacuole membrane {ECO:0000269|PubMed:30680886}; Multi-pass membrane protein {ECO:0000269|PubMed:30680886}. Cell membrane {ECO:0000269|PubMed:30680886}; Multi-pass membrane protein {ECO:0000269|PubMed:30680886}.
Interaction partners:
- CDR ABC transporter
Sequence:
MVDNYHSSLDVAKTPIQSDADAQKSEAETEGPSSKSSQIAAGESIADSVRNFLELRQGGIPDDTGVVFDKISAVGSGTGSQDAPTVTSAAQSAFGLLSPLQNRQRKQYSRPILSGFSGTINPGEMLLVLGKPGSGCTTFLKTLSGLWDEYKEIQGELTLGGHPLLDVMKQRPQDILFCAESDDHFPTLTVAETLRFATRARCGPQVSAREIDTMVTQLAKLVGLGNVLNTKVGDAKIRGVSGGERRRVSLAEALATCARLICLDNPTHGLDSSTAVEFMEMMREWTTQSRCVAAMSVYQASDAIVSYFDKVLIINSGRQIYYGPVRDAKAYFEDLGFECLSTTTVADFLNVMSADPDVRRAQENRENQVPRTAEEFERAFSASPIYQEMQKSVQVAKERFQTNPSPLVKTSAFALPIWHQIWYCAGRQFRIVTSDYSLWAVELATIVVQSLVLGTLFRNQQRTTSSLFIFASALFYSVLVPALQSMAEFGNGFAQRPLILKQKRYQISRPIAYALGLVTTDVVWKVAAICYNIPLYFLTGFQRTAGNFFTWFLIIYLEHLALSMFFRSVAIFSPNMHRAVLPVGIFFNMYVLYTGLYVPAPQMQVWLGWLRYLNPLYYAFESVMVNEFRDLSYQCSASDPVPSGLGYNDMAHQVCAVVGSEPGDRLLSGASYIHAQYGFKTSHLWRNVGINAALFVFFALCSGIGMEMLKTPAGQLATVFYKSSPGVTHRRDKIDSETGQDQGNESSEMSAGQSNDALRLQEHQGPDKSHNLAWTNLCLDIKTKEGDQRLLNNLSGSVKSGQLKALMGVSGAGKTTLLNALAGRSTIGNLTGTLALNGQVLPTFFRSRMGYVQQQDIHLPTQTVREALQMTARLRRPESISVADKNAYVEKVIEWLSMEHIADALVGVPGAGLNLEQRKKVSIGVEMASKPEILFLDEPTSGLDGQSAMLIARLLRRLADSGQAILCTIHQPAAELIDQFDKLYLLSRGGNLVYDGSLGTRCHEAIQYFQPRSRPCGPEENPAEYFLAVIGAGSRNDAHMDWASLWNDSEQGKEREKAEESLVPAAEQAPQLEQQSLYSVPFHVQLWVVVQRTWLYYWREPDYVNSKLWMSVGNSLLNSLTHLQSPNTERGAYNRVFSAFMSLIVGPPLGLQVQPRFVTLRDIFVHRERESLTYHWLAFVLSAFIVELPFTFLSSLVYWLLWYFPVGYFNAPSRAGYSFLMYELFGVFATSLAQLCASLMPNIEAAFAANGFFFMFCNTFAGTLSPKPVTPSGWRWFYNISPLFYLGEGVTVDVLQDLPIRCEESEVSIFYAVNGTTCGQYAQDFLKTATGYLLNPASTTECQYCRYRDGQSYFQQYGYEFAHRHRNIGVFICFIAFNFTMVLVMTYLTKTRRH
Protein: Alpha-globin transcription factor CP2 (Q9ERA0)
Organism: Mus musculus (Mouse)
Function: Binds a variety of cellular promoters including fibrinogen, alpha-globin promoters. Activation of the alpha-globin promoter in erythroid cells is via synergistic interaction with UBP1 (By similarity). Functions as part of the SSP (stage selector protein) complex. Facilitates the interaction of the gamma-globin genes with enhancer elements contained in the locus control region in fetal erythroid cells. Interacts by binding to the stage selector element (SSE) in the proximal gamma-globin promoter (By similarity).
Subcellular location: Nucleus {ECO:0000250}.
Interaction partners:
- Amyloid beta precursor protein binding family B member 1
- Gamma-aminobutyric acid receptor subunit beta-3
- Carboxypeptidase Z
- Peroxiredoxin-6
- Transcription factor CP2-like protein 1
Sequence:
MAWALKLPLADEVIESGLVQDFDASLSGIGQELGAGAYSMSDVLALPIFKQEESSLPPDNENEILPFQYVLCAATSPAVKLHDETLTYLNQGQSYEIRMLDNRKLGELPELNGKLVKSIFRVVFHDRRLQYTEHQQLEGWRWNRPGDRILDIDIPMSVGVIDPRANPTQLNTVEFLWDPSKRTSVFIQVHCISTEFTMRKHGGEKGVPFRVQIDTFKENGNGEYTEHLHSASCQIKVFKPKGADRKQKIDREKMEKRTPHEKEKYQPSYETTILTECSPWPEITYVNNSPSPGFNSSHSSFSLGEGNGSPNHQPEPPPPVTDNLLPTTTPQEAQQWLHRNRFSTFTRLFTNFSGADLLKLTRDDVIQICGPADGIRLFNALKGRMVRPRLTIYVCQESLQLREQQPQPQPQPQKQEDGDSNGTFFVYHAIYLEELTAVELTEKIAQLFSISPHQISQIYKQGPTGIHVVISDEMVQNFQEEACFILDTMEAETSDSYHVILK
Protein: Sulfated surface-like glycoprotein (T3P18.8) (Q9SXE5)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
Sequence:
MANGWVKSLQCKSKAFDDVYNPIKNPNPNPSPSPKHLMSSYSCRKSTQSLKDVIETKKPKPKPKKPNPKPDKRETDPVLSPSTRIRSTGVRDRDPFLPTLTELSEGHQSRNVVEIIFQTSWGPKPFSGRVEMIFKVQNGSKTLTRFEEYREAVKARSVGKAREENARSVADGNETMRFYCLGPSYGGGGSAWGILGGKGGGASIYTFAGSSTANEKAGGGKGRKAMLVCRVIAGRVTKQNELKYDSDLRSRFDSVSGDDGELLVFDTRAVLPCFLIIYRL
Protein: Casein kinase II subunit beta (CK II beta) (Q8IIW5)
Organism: Plasmodium falciparum (isolate 3D7)
Interaction partners:
- non-specific serine/threonine protein kinase
- Casein kinase II subunit beta
- RNA-binding protein, putative
- Nrap protein domain-containing protein
- FACT complex subunit
- ATP-dependent RNA helicase
- U3 small nucleolar ribonucleoprotein protein IMP3, putative
- KRR1 small subunit processome component
- U3 small nucleolar ribonucleoprotein protein IMP4, putative
- rRNA biogenesis protein RRP36
Sequence:
MENSDSNKDLQDSKSDKSTSWVKWFNNRALSNFLVEVDNEYITDSFNLYGLKTEIPNFNHLLSIIAGDAPEDDDDSKNSFSKDCICLYSLIHARFITTPKGLSLMKDKYIKGDFGTCPRVSCAQHNVLPIGLFDQMKIAKVHVYCPLCQEIYKIHEDEKVYLDGSFFGTSFPHILLQTYPYYATLKTPPYCSSKIFGFNVYHNFTRTEYKLAKGEFGIITRENFLKKNPKYFKKLRKEELQISET
Protein: Microtubule-associated protein (A0A0B4LIT4)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000256|ARBA:ARBA00004245, ECO:0000256|RuleBase:RU000686}.
Interaction partners:
Sequence:
MADVLEKSSLLDAVPPLGDPHPPLPHQQLQQEAAAAAAANAAPPAPPQQQQPPPHQLQQQQPQQQQLQQKPANARANQDQKEGDNDSGVDESTQEKDRNGPNSPSSPVKTPTSTSSKPDKSGTSRPPSATPSNKSAPKSRSASKNRLLLKTPEPEPVKKVPMNKVQVGHAPSPNLKAVRSKIGSLDNATYKPGGGHVKIESKKIDIKAAPRIEAKNDKYMPKGGEKKIVTTKLQWNAKSKIGSLENAAHKPGGGDKKIETLKMDFKDKAKPKVGSTANVKHQPGGGDIKDNNPKDIQTQKLEIKAQSKVGSLDNVKHKPGGGEKKIFDDKDYLKNVEHSVALTTPPTQSPLPSMTASGADENLNQQS
Protein: Protein FAM47E (Q6ZV65)
Organism: Homo sapiens (Human)
Function: Promotes histone methylation by localizing the arginine methyltransferase PRMT5 to chromatin.
Subcellular location: Nucleus {ECO:0000269|PubMed:33376131}. Chromosome {ECO:0000269|PubMed:33376131}. Cytoplasm {ECO:0000269|PubMed:33376131}. Note=Localizes to promoter regions of PRMT5 target genes. {ECO:0000269|PubMed:33376131}.
Interaction partners:
Sequence:
MADRRRRLRPGTLAPVREGVNCRSRCFTKHKNGLKFPTSLHSRQLVFPRKGLDDFRKGCPPCTGLVTQVPVEGFLPQIYHRAPQLAPKKRQIKLLKEADVLSKLSPAQQARKAFLEDVEAHLTPHPLALYLNLEEAMPIELLSKVLEVLDPDRKLEDTWAYCQDTRKGMKEPTKLLKKHSTQVYLGPSKKTSVSNAGQWLYEEKPHKMDLLHENGPRPGLHENGISDIDEEFILKQFDIDYETKPSHDALHTMKLNQVPLELKRSVGLSKLQETEFFQKLGYERKLQKPQNPYKPKWVKMRYGAWYLNPKLWKKQRVDEPLVDPEVSHKAQEENFKKELQEQEELLADLHGTVAFKDFILSRGYRTPRFLENMYIGKECKRACNKTPIKRTQA
Protein: Uncharacterized protein C18B11.03c (Q09710)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Subcellular location: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
Sequence:
MDTYMEEREAGRLEIYSVKRNVLNMFSIVIVSATYSISLDSTVLYPAVYHAIVNQPMLGARIHNCHSKIPIVKKLKTIDLDKVVKYADDQKVDSFCNNALQNFKLCYDDETLPLWMVYVLNDKSELVFIYDHSLFDGGSGPLFHKYVLEGLQMSKTNFSSSTVPVSELPLPKNLEKLIDVHPSWFCLMKALWTNSGLPFSKGFRSPSYKGHAPVRPFSSHTIFFSISNAVVKNIKQLSKNIDASFTSIFYSVFMLSIYYAIAKNGKVNLDMLIDVNARRFLPVAKQTMGNYVFSYVHHLNGFQPSQRQEDYKHTMVDLATEFSHRLKAALSNPREMSQQIGLLSYIDIEDYLLKSCEKTRGNTAEISNLGYFSFPADSSVKIKNMAFAQPCSSLSAPFVLNVITVADGPCSFSLSIFDDGNTEQTHELAIKIRDKFLSILEKVSMNS
Protein: PH domain-containing protein (Q86JG3)
Organism: Dictyostelium discoideum (Social amoeba)
Interaction partners:
Sequence:
MSTLEQYLKVIGLKSYKDLMIDNGYDDPELISELTEDDLVAINVKRGHAKRAFLKAKELAGKQNESSAKSPDVSSSTTTASTSSSSSSSTSAPVEEKKRTTTISIGKKGEDNDDDDEEEEKASYSGPILQSKVLNEGFIQKKGNEGFFGSKMFQKRYFKIYEEGRLAYFKNQNDVSPIGVIEMKGALACEDMEGKPQGFKLSMKTSARVYWLVAMTNDQKQKWVSVIKQQITPPAVPKPIDPNEIRPYLQNTEEPPQCASTRFDASNSWDAIEKQIIEGQIRLHIHSNGDLFVEETRSIEVGEEGLVWIEDLPKSIDDRTVHFQSFTEPTAFVSEQTYHNDAKTPERMLSKLIGKEIQVSVPRDDHFDEPLLLKGQLIYNANDSTYALQDKETNTIHFLKTDEAISYNLLDTTTIDPIFRNSSLEWNINGKEPKHLSKISYNSKDLFKWNATYVSVLNPRETEMEIRGWFTIENESGKTFNNSNVILVREPEEKKKDEEKTDESALPIGLPKLGGFGLKLPKIGGFGGDSETPVPEKRIYRYEVPHKTTLRDGESKQICFVSTKLPVKSFDFITFATPNYQKYAMIGKDQGANAASSVNSSVTFTWNLPYSIPAGQMKLQRQLKDKFGSDIVNTFDIAHYNPTDIISLPLQPLGKVSSTRTQTGFNFDLNGLFIVETYEIRVNNGREEPIKITVEESLYRSTFWEITSSSHKFTPHPTHSRKIHWQLSIPPLDGEVIKYSVFYSGLNLPASMTAKKDEKTN
Protein: Cytochrome P450 monooxygenase patI (EC 1.-.-.-) (Patulin biosynthesis cluster protein I) (m-hydroxybenzyl alcohol hydroxylase) (A0A075TMP8)
Organism: Penicillium expansum (Blue mold rot fungus)
Function: Cytochrome P450 monooxygenase; part of the gene cluster that mediates the biosynthesis of patulin, an acetate-derived tetraketide mycotoxin produced by several fungal species that shows antimicrobial properties against several bacteria. PatI catalyzes the conversion of m-hydroxybenzyl alcohol into gentisyl alcohol. The pathway begins with the synthesis of 6-methylsalicylic acid by the polyketide synthase (PKS) patK via condensation of acetate and malonate units. The 6-methylsalicylic acid decarboxylase patG then catalyzes the decarboxylation of 6-methylsalicylic acid to yield m-cresol (also known as 3-methylphenol). These first reactions occur in the cytosol. The intermediate m-cresol is then transported into the endoplasmic reticulum where the cytochrome P450 monooxygenase patH converts it to m-hydroxybenzyl alcohol, which is further converted to gentisyl alcohol by the cytochrome P450 monooxygenase patI. The oxidoreductases patJ and patO further convert gentisyl alcohol to isoepoxydon in the vacuole. PatN catalyzes then the transformation of isoepoxydon into phyllostine. The cluster protein patF is responsible for the conversion from phyllostine to neopatulin whereas the alcohol dehydrogenase patD converts neopatulin to E-ascladiol. The steps between isoepoxydon and E-ascladiol occur in the cytosol, and E-ascladiol is probably secreted to the extracellular space by one of the cluster-specific transporters patC or patM. Finally, the secreted patulin synthase patE catalyzes the conversion of E-ascladiol to patulin (Probable).
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:30680886}; Single-pass membrane protein {ECO:0000269|PubMed:30680886}.
Interaction partners:
Sequence:
MDILQLAPTHLLAILLSSTSALFLITYLLRAGHRPSDLPNGPPTVPLFGNELQVPKSDAHFQFSRWAKEYGGFFTLKRYNNTTIVISDQKLIKTLLDKKSNIYSHRPASLVSHLITQSDHLLVMQYGERWRMLRKTIHQYFMEPRCERDHWKVQEAEAKQMLHDYLTMPEDHMLHPKRYSNSITNSLVFGIRTKTVHDEYMKKLFYLMDKWSLVQELGATPPVDSFALLRYVPQWMLGNWRNRAVEVGDLMQSLYQTVLDQVKERRQRGIQRDSFMDRVLDTLKQTPLSENELRFLGGVLMEGGSDTSSSLILTIIQAMTKYPEVQAKAHAQIDSIIGHNRSPAWSDWSKLPYINMIIKESHRWRPVSPLGVPHAVAEDDHIDGKLIPQGSSIVLNVWGMHHDSDRWQEPEHFQPERFADFPALASGYAGSERRDHLGYGAGRRICPGIHLAERNLIIGIAKLLWAFEFLEPLGSDSDISAHSGASKGFLHCPKDYGCVIRLRSPEKRETIMREFAEAQEVFARFD
Protein: THO complex subunit 3 (Tho3) (Q8VE80)
Organism: Mus musculus (Mouse)
Function: Required for efficient export of polyadenylated RNA and spliced mRNA. Acts as component of the THO subcomplex of the TREX complex which is thought to couple mRNA transcription, processing and nuclear export, and which specifically associates with spliced mRNA and not with unspliced pre-mRNA. TREX is recruited to spliced mRNAs by a transcription-independent mechanism, binds to mRNA upstream of the exon-junction complex (EJC) and is recruited in a splicing- and cap-dependent manner to a region near the 5' end of the mRNA where it functions in mRNA export to the cytoplasm via the TAP/NFX1 pathway (By similarity).
Subcellular location: Nucleus {ECO:0000305}. Nucleus speckle {ECO:0000305}.
Interaction partners:
- THO complex subunit 2
- THO complex subunit 7 homolog
- THO complex subunit 6 homolog
- THO complex subunit 5 homolog
- THO complex subunit 1
- Spliceosome RNA helicase Ddx39b
- THO complex subunit 4
- Aly/REF export factor 2
- THO complex subunit 2
- SAP domain-containing ribonucleoprotein
Sequence:
MAAPAAVLGPSALGQSGPGSMAPWCSVSSGPSRYVLGMQELFRGHSKTREFPAHSAKVHSVAWSCDGRRLASGSFDKTASVFLLEKDRLVKENNYRGHGDSVDQLCWHPSNPDLFVTASGDKTIRIWDVRTTKCIATVNTKGENINICWSPDGQTIAVGNKDDVVTFIDAKTHRSKAEEQFKFEVNEISWNNDNNMFFLTNGNGCINILSYPELKPVQSINAHPSNCICIKFDPMGKYFATGSADALVSLWDVDELVCVRCFSRLDWPVRTLSFSHDGKMLASASEDHFIDIAEVETGDKLWEVQCESPTFTVAWHPKRPLLAFACDDKDGKYDSSREAGTVKLFGLPNDS