wanglab/gogpt-training-data huggingface dataset:
Protein: F-box/FBD/LRR-repeat protein At5g18770 (Q93ZK9)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- DNA glycosylase superfamily protein
Sequence:
MVNLMRKFAKSIGRPGTEFWRGEDMISALPDHLLCHILIFLSTDESVLTSVLSSRWRNLWKWVPRLDLNTSDFPYPNDVTCAAFIDKFLNLYNESYLREFKLRIDQANFRSNVSLYEPCLGVVIKKPNVRHFQVESDLLEHWCTSEIRLTLSACQALVCLKLHLVWLNDFESLSLPCLKIMYLEDVVFPSDAAAETLISCSPVLEDLKLSLHRDDVVVVLRVYSQSLKSFTLKRAVPVYAINGAHTVLVDTPRLVYMSLIDYQFKSFKIISMSDYVKVDLDVDFELMRDELSERNIVYDLLNNFSGVRNMTISWTTLKFIHRFHDMNPLPKFRDLTRLRATMSSDASLEVLRIVLESCPKLKHFHFTLELVNDFPEAVITGFSRVLPRCLVFSLESVEMESPITEKATELKLVRYFLENSATLKKLVLLLNHESTGEKHEPGVLKQLIESPRRSSLCQFEVLAVPPNPEPWWIYVKPQRFL
Protein: Acetyl-CoA acetyltransferase 1 (H0YEL7)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
XKLGSIAIQGAIEKAGIPKEEVKEAYMGNVLQGGEGQAPTRQAVLGAGLPISTPCTTINKVCASGMKAIMMASQSLMCGHQDVMVAGGMESMSNVPYVMNRGSTPYGGVKLEDLIVKDGLTDVYNKIHMVNVIFSG
Protein: Paxillin (Q66H76)
Organism: Rattus norvegicus (Rat)
Function: Cytoskeletal protein involved in actin-membrane attachment at sites of cell adhesion to the extracellular matrix (focal adhesion).
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:P49023}. Cell junction, focal adhesion {ECO:0000250|UniProtKB:P49023}. Cytoplasm, cell cortex {ECO:0000250|UniProtKB:Q8VI36}. Note=Colocalizes with integrins at the cell periphery. Colocalizes with PXN to membrane ruffles and the leading edge of migrating cells (By similarity). {ECO:0000250|UniProtKB:P49023}.
Interaction partners:
- Talin 1
- Protein-tyrosine kinase 2-beta
- Breast cancer anti-estrogen resistance protein 1
- Vinculin
- Proto-oncogene tyrosine-protein kinase Src
- Focal adhesion kinase 1
- Scaffold protein ILK
- Alpha-parvin
- Adapter molecule crk
- Talin 2
Sequence:
MDDLDALLADLESTTSHISKRPVFLSEEPPYSYPTGNHTYQEIAVPPPVPPPPSSEALNGTVLDPLDQWQPSGSRYAHQQPPSPSPIYSSSTKNSSASNPQDSVGSLCSRAGEEEHVYSFPNKQKSAEPSPTVMSSSLGSNLSELDRLLLELNAVQRSPSGFSAGMVSVQASREPLGSWGTEGRAIILSPFFQDEAESSPPLPGALSPLYGVPESNNLLGGKAGPLMKEKPKRNGGRGLEDVRPSVESLLDELENSVPSPVPAITVNQGEMSSPQRVTSSQQQTRISASSATRELDELMASLSDFKFMAQGKTGSSSPPGGLSKPGSQLDSMLGSLQSDLNKLGVATVAKGVCGACKKPIAGQVVTAMGKTWHPEHFVCTHCQEEIGSRNFFERDGQPYCEKDYHSLFSPRCYYCNGPILDKVVTALDRTWHPEHFFCAQCGAFFGPEGFHEKDGKAYCRKDYFDMFAPKCGGCARAILENYISALNTLWHPECFVCRECFTPFVNGSFFEHDGQPYCEVHYHERRGSLCSGCQKPITGRCITAMAKKFHPEHFVCAFCLKQLNKGTFKEQNDKPYCQSCFLKLFC
Protein: L-dopachrome isomerase (EC 5.3.2.1) (EC 5.3.3.12) (L-dopachrome tautomerase) (Phenylpyruvate tautomerase) (Q8I5C5)
Organism: Plasmodium falciparum (isolate 3D7)
Subcellular location: Secreted {ECO:0000256|ARBA:ARBA00004613}.
Interaction partners:
Sequence:
MPCCEVITNVNLPDDNVQSTLSQIENAISDVMGKPLGYIMSNYDYQKNLRFGGSNEAYCFVRITSIGGINRSNNSALADQITKLLVSNLNVKSRRIYVEFRDCSAQNFAFSGSLFG
Protein: Homeobox protein SIX3 (Sine oculis homeobox homolog 3) (Q62233)
Organism: Mus musculus (Mouse)
Function: Transcriptional regulator which can act as both a transcriptional repressor and activator by binding a ATTA homeodomain core recognition sequence on these target genes. During forebrain development represses WNT1 expression allowing zona limitans intrathalamica formation and thereby ensuring proper anterio-posterior patterning of the diencephalon and formation of the rostral diencephalon. Acts as a direct upstream activator of SHH expression in the rostral diencephalon ventral midline and that in turn SHH maintains its expression. In addition, Six3 activity is required for the formation of the telencephalon. During postnatal stages of brain development is necessary for ependymal cell maturation by promoting the maturation of radial glia into ependymal cells through regulation of neuroblast proliferation and migration. Acts on the proliferation and differentiation of neural progenitor cells through activating transcription of CCND1 AND CCND2. During early lens formation plays a role in lens induction and specification by activating directly PAX6 in the presumptive lens ectoderm. In turn PAX6 activates SIX3 resulting in activation of PDGFRA and CCND1 promoting cell proliferation. Also is required for the neuroretina development by directly suppressing WNT8B expression in the anterior neural plate territory. Its action during retina development and lens morphogenesis is TLE5 and TLE4-dependent manner. Furthermore, during eye development regulates several genes expression. Before and during early lens development represses the CRYGF promoter by binding a SIX repressor element. Directly activates RHO transcription, or cooperates with CRX or NRL. Six3 functions also in the formation of the proximodistal axis of the optic cup, and promotes the formation of optic vesicles-like structures. During pituitary development, acts in parallel or alternatively with HESX1 to control cell proliferation through Wnt/beta-catenin pathway. Plays a role in eye development by suppressing WNT1 expression and in dorsal-ventral patterning by repressing BMP signaling pathway (By similarity).
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00108, ECO:0000269|PubMed:12050133}.
Interaction partners:
- Paired box protein Pax-6
- Visual system homeobox 2
- Homeobox protein OTX2
- Zinc finger protein ZIC 2
- LIM/homeobox protein Lhx2
- Protein phosphatase EYA1
- Sonic hedgehog protein
- Ventral anterior homeobox 1
Sequence:
MVFRSPLDLYSSHFLLPNFADSHHCSLLLASSGGGSGASGGGGGAGGGGGGNRAGGGGAGGAGGGSGGGGSRAPPEELSMFQLPTLNFSPEQVASVCETLEETGDIERLGRFLWSLPVAPGACEAINKHESILRARAVVAFHTGNFRDLYHILENHKFTKESHGKLQAMWLEAHYQEAEKLRGRPLGPVDKYRVRKKFPLPRTIWDGEQKTHCFKERTRSLLREWYLQDPYPNPSKKRELAQATGLTPTQVGNWFKNRRQRDRAAAAKNRLQHQAIGPSGMRSLAEPGCPTHGSAESPSTAASPTTSVSSLTERADTGTSILSVTSSDSECDV
Protein: Protein SUR7 (P54003)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Involved in sporulation and affects the sphingolipid composition of the plasma membrane. Probably involved in endocytosis.
Subcellular location: Cell membrane {ECO:0000269|PubMed:11784867, ECO:0000269|PubMed:12469340, ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:15536122, ECO:0000269|PubMed:16496001}; Multi-pass membrane protein {ECO:0000269|PubMed:11784867, ECO:0000269|PubMed:12469340, ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:15536122, ECO:0000269|PubMed:16496001}. Note=Localizes at eisosomes, structures which colocalize with sites of protein and lipid endocytosis.
Interaction partners:
- Sphingolipid long chain base-responsive protein PIL1
- Arginine permease CAN1
- Non-classical export protein 2
- Sphingolipid long chain base-responsive protein LSP1
- Non-classical export protein 2 homolog 1
- Uracil permease
- Reduced viability upon starvation protein 167
- Plasma membrane ATPase 1
- Tryptophan permease
Sequence:
MVKVWNIVLRLVVLLFLAGNTLLLILMIISGATDHYPVNRFYWVQGNTTGIPNAGDETRWTFWGACLQDKDGSDTCTSNLAPAYPISPVDNFNTHINVPHQFISKRDAFYYLTRFSFCFFWIALAFVGVSFILYVLTWCSKMLSEMVLILMSFGFVFNTAAVVLQTAASAMAKNAFHDDHRSAQLGASMMGMAWASVFLCIVEFILLVFWSVRARLASTYSIDNSRYRTSSRWNPFHREKEQATDPILTATGPEDMQQSASIVGPSSNANPVTATAATENQPKGINFFTIRKSHERPDDVSV
Protein: histone acetyltransferase (EC 2.3.1.48) (A0A8I6G641)
Organism: Rattus norvegicus (Rat)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
Interaction partners:
Sequence:
MLLSDYPIQVNQIPPQPPVQAKNQQSQPSGQSPQGMRSMNNMSASPMGVNGGVGVQTPNLLSDSMLHSTINSQNPMMNENASVASLGPLPTAAQPSSTGIRKQWHEDITQDLRNHLVHKLVQAIFPTPDPAALKDRRMENLVAYARKVEGDMYESANNRAEYYHLLAEKIYKIQKELEEKRRTRLQKQNMLPSAPGMVPVPMNTAPNMGQQPTGMTTNGPLPDPSMIRGSVPNQMMPRMTPQPGLNQFGQMNIPQPPIGPRQPSPLQHHGQLAQSGSLNPPMGYGPRMQQTSGQNQFLSQTQFPSQGMNVTNMPLAPSSSQAPVSQAQMSSSSCPVNSPIMPPGSQGSHIHCPTLPQQAHQNSPSPVPSRTPTPHHTPPSIGTQQPAATAIPAPVPTPPAMPPGAQPQSLRPPSRQTPTPPTHLPPQVQPSLPVPPADQSQPQPRSQQSTAASVPTPTAPLLPPQPPTPLSQPAVSVEGQVSNPPSTSSTEVNSQTIPEKQPSQEVKMEVKMDVDQPEPADAQPDDTKEAKAEDGKVEPTETEERGPELKTEVKEEEDQPSTSAAQSSPAPGQSKKKIFKPEELRQALMPTLEALYRQDPESLPFRQPVDPQLLGIPDYFDIVKSPMDLSTIKRKLDTGQYQEPWQYIDDIWLMFNNAWLYNRKTSRVYKYCSKLSEVFEQEIDPVMQSLGYCCGRKLEFSPQTLCCYGKQLCTIPRDATYYSYQNRYHFCEKCFNEIQGESVSLGDDPSQPQTTINKEQFSKRKNDTLDPELFVECTECGRKMHQICVLHHEVIWPSGFVCDGCLKKTARTRKENKFSAKRLPSTRLGTFLENRVNDFLRRQNHPESGEVTVRVVHASDKTVEVKPGMKARFVDSGEMAESFPYRTKALFAFEEIDGVDLCFFGMHVQEYGSDCPPPNQRRVYISYLDSVHFFRPKCLRTAVYHEILIGYLEYVKKLGYTTGHIWACPPSEGDDYIFHCHPPDQKIPKPKRLQEWYKKMLDKAVSERIVHDYKDILKQATEDRLTSAKELPYFEGDFWPNVLEESIKELEQEEEERKREENTSNESTDVTKGDSKNAKKKNNKKTSKNKSSLSRGNKKKPGVPNVSNDLSQKLYATMEKHKEVFFVIRLIACPAPNSLPPIVDPDPLIPCDLMDGRDAFLTLARDKHLEFSSLRRAQWSTMCMLVELHTQSQDRFVYTCNECKHHVETRWHCTVCEDYDLCITCYNTKNHDHKMEKLGLGLDDESNNQQAAATQSPGDSRRLSIQRCIQSLVHACQCRNANCSLPSCQKMKRVVQHTKGCKRKTNGGCPICKQLIALCCYHAKHCQENKCPVPFCLNIKQKLRQQQLQHRLQQAQMLRRRMASMQRTGVAGQQQGLPSPTPATPTTPTGQQPATPQTPQPQPTSQPQPTPPNNMTPYLPRTQTAGPVSQGKAAGQVTPPTPPQTAQPPLPGPPPAAVEMAMQIQRAAETQRQMAHVQIFQRPIQHQMAPMAPMGMNPPPMARGPGGHLDPGMGPAGMQQQPPWAQGGMPQPQQMQSGMPRPAMMSVAQHGQPLNMAPQPGLGQVGVSPLKPGTVSQQALQNLLRTLRSPSSPLQQQQVLSILHANPQLLAAFIKQRAAKYANSNPQPLPGQPGMPQGQPGLQPPTMPGQQGVHSNPALQNMNPMQAGVQRAGLPQQQPQQQLQPPMGGMSPQAQQMNMNHNTMPSQFRDILRRQMMQQQGAGPGIGPGMANHNQFQQPQGIGYPPQQQQQQQQQRMQHHMQQMQQGNMGQMGQLPQALGAEAGASLQAYQQRLLQQQMGSPAQPNPMSPQQHMLPNQAQSPHLQGQQIPNSLSNQVRSPQPVPSPRPQSQPPHSSPSPRMQPQPSPHHVSPQTSSPHPGLVAAQAANPMEQGHFASPDQNSMLSQLASNPGMANLHGASATDLGLSADSADLSSNLSQSTLDIH
Protein: RNA-directed RNA polymerase (EC 2.7.7.48) (G5EBQ3)
Organism: Caenorhabditis elegans
Interaction partners:
- Helicase ATP-binding domain-containing protein
- Tudor domain-containing protein
- NFX1-type zinc finger-containing protein 1 homolog
- Piwi-like protein ergo-1
- Argonaute protein wago-1
- Piwi domain-containing protein
- Argonaute protein hrde-1
- Argonaute protein wago-4
- MUTator
- DRBM domain-containing protein
Sequence:
MGDEGYRGWIKLEIPCSLPERQMGPIVKCHVAKLEPALNEYNIKVLTKGQVQVVEEQDCEPFYETNYEVATSRFSHDLIAAIQTYLKDLSTDHLMPFQRGNLVLHSSDFWSSELTCHLVDIPLAAVFFGNIQGGTFINHWEVSFWDDVRRRKSARTRNTEPTQADKIGMNQIKVEFEFDKIDFMTVHFKHFENDFEVADKDAKRTKQTVTMYYQITVRRTSIRRIIVDPVVQDCNGSDRIRVHFELNCPVLIRRAYRTAKQESENRHSVPHYRRYLVINRGRSANQYPTAKAITDSPVFTIEFDQSVGLNEIYRLLSRLRIRTGVSIEFADIPSIDCLIWRENPYNRWTFLNNQHLSPTHFSAPIYRDFITTAFPKKHEVCGSREVDTNRERKFAITYLLECLISRGAVVKDQILLDEGIWHRFLEVILHYYTKDDKLCEAGLEDLVHMIDGRKRIGSLIKCFDRICQTRQRNSLVNGLTTEEMREGYQRVRKIIFTPTRVIYVAPETLMGNRVLRRYDHDGTRVLRITFRDDDNQKMRTNKTSTMLEKTVNQYLKNGITVAGRNFGYLGSSNSQMRDNGAYFMEKYSSSQCREYERIYQIKPPITFNPKIQAARKNLGRFETIDNIPKMMARLGQCFTQSRLSGVNLERCTYMTTYDLTGGKNLKGDEYTFSDGVGMMSYRFAQMVSEVMDFGKGVPSCFQFRFRGMKGVISIEPLLDNLRQWSISYNISKPSDDSSWSLNCMFRPSQIKFISKRHPRDQVEIVKYSSPVPVALNKPFINILDQVSEMQSLECHRRVTNRIEELLDRQMLSFAQQMVDETFCRNRLKELPRRVDIDYLRTTWGFTLSSEPFFRSLIKASIKFSITRQLRKEQIPIPCDLGRSMLGVVDETGRLQYGQIFVQYTKNLALKLPPKNAARQVLTGTVLLTKNPCIVAGDVRIFEAVDIPELHHMCDVVVFPQHGPRPHPDEMAGSDLDGDEYSIIWDQQLLLDKNEDPYDFTSEKQKASFKEDEIDDLMREFYVKYLKLDSVGQISNSHLHNSDQYGLNARVCMDLAKKNCQAVDFTKSGQPPDELERKWRKDEETGEMIPPERAERVPDYHMGNDHTPMYVSPRLCGKLFREFKAIDDVLKISEERDEQVEISIDETIKIDGYTEYMASAKNDLARYNAQLRSMMENYGIKTEGEVFSGCIVDMRNRISDKDQDDMSFFNTNQMIETKLTNLFKKYREIFFEEFEGGWEGNTEAFSRYGRDSNILQRQCRAPTVQMMKKAVAWYRACYEEARITRENKKLSFAWLAYDVIAKVKQDKSLTSDEVKMGGANPLYTMLDDHRSQYLVDNSRKFEAFRQFSTPKTSGEQVKRAHRIIKMYTETYPGLDAVLFMLDEWARISNLFENQSLREYHLSLLFILFATRQFSSVDGNAAKFFNKVDEKSYKQSKTIGDFEPSLYIEEKGKSQMMVKFLEFLASRKFRKMANLSFCALDFSSIFMRGEWQIFHLAALKTYYNVLFNLRFEELPVSTDPTTTVRSIIRENEPFVIELPANCDRSLVHRKLVEHTGVKEIFMRNMEKSVRSSDDVQKINMRLLVSTRGTLESMYKLRQLVAVKVPIKTYVTGQDVSTQMARLCYEKIVRGHINI
Protein: Sensor protein VanS (VanS) (VanSA) (EC 2.7.13.3) (Vancomycin histidine protein kinase) (Vancomycin resistance protein VanS) (Q06240)
Organism: Enterococcus faecium (Streptococcus faecium)
Function: Member of the two-component regulatory system VanS/VanR. Activates the transcription of vanH, vanA and vanX in response to vancomycin which results in vancomycin resistance. VanS activates VanR by phosphorylation.
Subcellular location: Membrane {ECO:0000255}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
Sequence:
MVIKLKNKKNDYSKLERKLYMYIVAIVVVAIVFVLYIRSMIRGKLGDWILSILENKYDLNHLDAMKLYQYSIRNNIDIFIYVAIVISILILCRVMLSKFAKYFDEINTGIDVLIQNEDKQIELSAEMDVMEQKLNTLKRTLEKREQDAKLAEQRKNDVVMYLAHDIKTPLTSIIGYLSLLDEAPDMPVDQKAKYVHITLDKAYRLEQLIDEFFEITRYNLQTITLTKTHIDLYYMLVQMTDEFYPQLSAHGKQAVIHAPEDLTVSGDPDKLARVFNNILKNAAAYSEDNSIIDITAGLSGDVVSIEFKNTGSIPKDKLAAIFEKFYRLDNARSSDTGGAGLGLAIAKEIIVQHGGQIYAESNDNYTTFRVELPAMPDLVDKRRS
Protein: Acetylglutamate kinase, chloroplastic (EC 2.7.2.8) (N-acetyl-L-glutamate 5-phosphotransferase) (NAG kinase) (AtNAGK) (Q9SCL7)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Involved in the arginine biosynthetic pathway via the intermediate compound ornithine.
Subcellular location: Plastid, chloroplast stroma {ECO:0000269|PubMed:16377628}.
Interaction partners:
- Arginine biosynthesis bifunctional protein ArgJ
- Nitrogen regulatory protein P-II homolog
- Probable N-acetyl-gamma-glutamyl-phosphate reductase, chloroplastic
- Argininosuccinate lyase, chloroplastic
- Acetylornithine aminotransferase, chloroplastic/mitochondrial
- Argininosuccinate synthase, chloroplastic
- Ornithine transcarbamylase, chloroplastic
- Ornithine aminotransferase, mitochondrial
- Probable amino-acid acetyltransferase NAGS1, chloroplastic
- Probable amino-acid acetyltransferase NAGS2, chloroplastic
Sequence:
MATVTSNASPKSFSFTVSNPFKTLIPNKSPSLCYPTRNKNHHRLGFSIKATVSTPPSIATGNAPSPDYRVEILSESLPFIQKFRGKTIVVKYGGAAMTSPELKSSVVSDLVLLACVGLRPILVHGGGPDINRYLKQLNIPAEFRDGLRVTDATTMEIVSMVLVGKVNKNLVSLINAAGATAVGLSGHDGRLLTARPVPNSAQLGFVGEVARVDPSVLRPLVDYGYIPVIASVAADDSGQAYNINADTVAGELAAALGAEKLILLTDVAGILENKEDPSSLIKEIDIKGVKKMIEDGKVAGGMIPKVKCCIRSLAQGVKTASIIDGRRQHSLLHEIMSDEGAGTMITG
Protein: Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit SWP1 (Oligosaccharyl transferase subunit SWP1) (Oligosaccharyl transferase subunit delta) (Q02795)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Subunit of the oligosaccharyl transferase (OST) complex that catalyzes the initial transfer of a defined glycan (Glc(3)Man(9)GlcNAc(2) in eukaryotes) from the lipid carrier dolichol-pyrophosphate to an asparagine residue within an Asn-X-Ser/Thr consensus motif in nascent polypeptide chains, the first step in protein N-glycosylation. N-glycosylation occurs cotranslationally and the complex associates with the Sec61 complex at the channel-forming translocon complex that mediates protein translocation across the endoplasmic reticulum (ER). All subunits are required for a maximal enzyme activity.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:8181570}; Multi-pass membrane protein {ECO:0000269|PubMed:29301962}.
Interaction partners:
- Protein transport protein SEC61
- Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit 1
- Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit WBP1
- Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit 3
- Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit OST2
- Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit STT3
- Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit OST4
- Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit OST5
- Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit OST6
- Protein transport protein SSS1
Sequence:
MQFFKTLAALVSCISFVLAYVAQDVHVSFPSTAGKSRVMIGKVEPRIGIDETVPTTITVEDPNEVIQVNFAIESTNKPFQNTLLIGLPNKNLEMAFEPEIKDNGKLSMYKYRIDLAKLDAALLQEASRSPEPIKATLILASSTAKPKENLFREILQLNLNFDVDHSDSSLVDKFGIKPEIHHIFHAEPKRVAKPIAVIFVLIIFITILSLIVTWLNSCAAAFNNIPTGVTAVYFLGFIATIVGFEVIFARYYLGTSIFETLFSSLYLGAPGLLTSTKFLRSFGQTI
Protein: Protein rough sheath 2 (Protein PHANTASTICA) (ZmPHAN) (Q9S7B2)
Organism: Zea mays (Maize)
Function: Transcription factor required for normal cell differentiation. Interacts directly with asymmetric leaves 2 (AS2) to repress the knox homeobox genes.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00625, ECO:0000269|PubMed:12750468}. Note=Localized in discrete subnuclear bodies.
Interaction partners:
- Homeotic protein knotted-1
Sequence:
MKERQRWRPEEDAVLRAYVRQYGPREWHLVSQRMNVALDRDAKSCLERWKNYLRPGIKKGSLTEEEQRLVIRLQAKHGNKWKKIAAEVPGRTAKRLGKWWEVFKEKQQRELRDSRRPPPEPSPDERGRYEWLLENFAEKLVGERPQQAAAAPSPLLMAAPVLPPWLSSNAGPAAAAAAAVAHPPPRPPSPSVTLSLASAAVAPGPPAPAPWMPDRAAADAAPYGFPSPSQHGGAAPPGMAVVDGQALAELAECCRELEEGRRAWAAHRREAAWRLKRVEQQLEMEREMRRREVWEEFEAKMRTMRLEQAAAAERVERDHREKVAELRRDAQVKEEKMAEQWAAKHARVAKFVEQMGGCSRSWSSATDMNC
Protein: Anoctamin 1 (E9PP68)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MRVNEKYSTLPAEDRSVHIINICAIEDIGYLPSEGTLLNSLSVDPDAECKYGLYFRDGRRKVDYILVYHHKRPSGNRTLVRRVQHSDTPSGARSVKQDHPLPGKGASLDAGSGEPPMDYHEDDKRFRREEYEGNLLEAGLELERDEDMYHINETRGLLKKINSVLQKITDPIQPKVAEHRPQTMKRLSYPFSREKQHLFDLSDKDSFFDSKTRSTIVYEILKRTTCTKAKYSMGITSLLANGVYAAAYPLH
Protein: 2-dehydro-3-deoxy-phosphogluconate/2-dehydro-3-deoxy-6-phosphogalactonate aldolase (EC 4.1.2.55) (Q4JC35)
Organism: Sulfolobus acidocaldarius (strain ATCC 33909 / DSM 639 / JCM 8929 / NBRC 15157 / NCIMB 11770)
Function: Involved in the degradation of glucose and galactose via the Entner-Doudoroff pathway. Catalyzes the reversible cleavage of 2-keto-3-deoxy-6-phosphogluconate (KDPG) and 2-keto-3-deoxygluconate (KDG) forming pyruvate and glyceraldehyde 3-phosphate or glyceraldehyde, respectively. It is also able to catalyze the reversible cleavage of 2-keto-3-deoxy-6-phosphogalactonate (KDPGal) and 2-keto-3-deoxygalactonate (KDGal).
Interaction partners:
- 2-keto-3-deoxygluconate kinase
- Glyceraldehyde-3-phosphate dehydrogenase
- gluconate dehydratase
- Glyceraldehyde dehydrogenase medium chain
- Glyceraldehyde dehydrogenase large chain
- Glyceraldehyde dehydrogenase small chain
- Glyceraldehyde-3-phosphate dehydrogenase
- Phosphoglucomutase/phosphomannomutase
- Triosephosphate isomerase
- Pyruvate kinase
Sequence:
MEIISPIITPFDKQGKVNVDALKTHAKNLLEKGIDAIFVNGTTGLGPALSKDEKRQNLNALYDVTHKLIFQVGSLNLNDVMELVKFSNEMDILGVSSHSPYYFPRLPEKFLAKYYEEIARISSHSLYIYNYPAATGYDIPPSILKSLPVKGIKDTNQDLAHSLEYKLNLPGVKVYNGSNTLIYYSLLSLDGVVASFTNFIPEVIVKQRDLIKQGKLDDALRLQELINRLADILRKYGSISAIYVLVNEFQGYDVGYPRPPIFPLTDEEALSLKREIEPLKRKIQELVH
Protein: Eukaryotic aspartyl protease family protein (F15K9.17 protein) (Q9ZVS4)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- Defensin-like protein 112
- Defensin-like protein 159
- Subtilisin-like protease SBT4.15
- R3H domain protein
- Defensin-like protein 286
- Defensin-like protein 151
- Pre-mRNA-splicing factor 18
- Cysteine proteinases superfamily protein
- N-terminal acetyltransferase B complex catalytic subunit NAA20
Sequence:
MAPSPIIFSVLLLFIFSLSSSAQTPFRPKALLLPVTKDQSTLQYTTVINQRTPLVPASVVFDLGGRELWVDCDKGYVSSTYQSPRCNSAVCSRAGSTSCGTCFSPPRPGCSNNTCGGIPDNTVTGTATSGEFALDVVSIQSTNGSNPGRVVKIPNLIFDCGATFLLKGLAKGTVGMAGMGRHNIGLPSQFAAAFSFHRKFAVCLTSGKGVAFFGNGPYVFLPGIQISSLQTTPLLINPVSTASAFSQGEKSSEYFIGVTAIQIVEKTVPINPTLLKINASTGIGGTKISSVNPYTVLESSIYNAFTSEFVKQAAARSIKRVASVKPFGACFSTKNVGVTRLGYAVPEIELVLHSKDVVWRIFGANSMVSVSDDVICLGFVDGGVNARTSVVIGGFQLEDNLIEFDLASNKFGFSSTLLGRQTNCANFNFTSTA
Protein: Alpha-1,4 glucan phosphorylase L-2 isozyme, chloroplastic/amyloplastic (EC 2.4.1.1) (Starch phosphorylase L-2) (P53535)
Organism: Solanum tuberosum (Potato)
Function: Phosphorylase is an important allosteric enzyme in carbohydrate metabolism. Enzymes from different sources differ in their regulatory mechanisms and in their natural substrates. However, all known phosphorylases share catalytic and structural properties.
Subcellular location: Plastid, chloroplast. Plastid, amyloplast.
Interaction partners:
- 1,4-alpha-glucan-branching enzyme
- Isoamylase isoform 3
- Isoamylase isoform 1
- Starch branching enzyme
- Isoamylase isoform 2
- Phosphoglucomutase, cytoplasmic
- Phosphoglucomutase, chloroplastic
- UTP--glucose-1-phosphate uridylyltransferase
- ADP-sugar diphosphatase
- Ectonucleotide pyrophosphatase/phosphodiesterase
Sequence:
MATFAVSGLNSISSISSFNNNFRSKNSNILLSRRRILLFSFRRRRRSFSVSSVASDQKQKTKDSSSDEGFTLDVFQPDSTSVLSSIKYHAEFTPSFSPEKFELPKAYYATAESVRDTLIINWNATYEFYEKMNVKQAYYLSMEFLQGRALLNAIGNLGLTGPYADALTKLGYSLEDVARQEPDAALGNGGLGRLASCFLDSMATLNYPAWGYGLRYQYGLFKQLITKDGQEEVAENWLEMGNPWEIVRNDISYPVKFYGKVIEGADGRKEWAGGEDITAVAYDVPIPGYKTKTTINLRLWTTKLAAEAFDLYAFNNGDHAKAYEAQKKAEKICYVLYPGDESLEGKTLRLKQQYTLCSASLQDIIARFEKRSGNAVNWDQFPEKVAVQMNDTHPTLCIPELLRILMDVKGLSWKQAWEITQRTVAYTNHTVLPEALEKWSFTLLGELLPRHVEIIAMIDEELLHTILAEYGTEDLDLLQEKLNQMRILDNVEIPSSVLELLIKAEESAADVEKAADEEQEEEGKDDSKDEETEAVKAETTNEEEETEVKKVEVEDSQAKIKRIFGPHPNKPQVVHMANLCVVSGHAVNGVAEIHSEIVKDEVFNEFYKLWPEKFQNKTNGVTPRRWLSFCNPELSEIITKWTGSDDWLVNTEKLAELRKFADNEELQSEWRKAKGNNKMKIVSLIKEKTGYVVSPDAMFDVQIKRIHEYKRQLLNIFGIVYRYKKMKEMSPEERKEKFVPRVCIFGGKAFATYVQAKRIVKFITDVGETVNHDPEIGDLLKVVFVPDYNVSVAEVLIPGSELSQHISTAGMEASGTSNMKFSMNGCLLIGTLDGANVEIREEVGEDNFFLFGAQAHEIAGLRKERAEGKFVPDPRFEEVKAFIRTGVFGTYNYEELMGSLEGNEGYGRADYFLVGKDFPDYIECQDKVDEAYRDQKKWTKMSILNTAGSFKFSSDRTIHQYARDIWRIEPVELP
Protein: Heterogeneous nuclear ribonucleoprotein K, isoform B (A1ZBW3)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MLKYFEERDEDFDVRLLIHQSLAGCVIGKGGQKIKEIRDRIGCRFLKVFSNVAPQSTDRVVQTVGKQSQVIEAVREVITLTRDTPIKGAIHNYDPMNFDRVYADEYGGYGTGSGSTRPSQRGNNRNGGGAGGVAGGAAGGNGGGFNAGGARGNAGGRGGADRFGGAAGGAVAGAGMGQRDNPFINPWANGGGGDVDGFGNNAGGAGGFAGNSFGGGAGGPFGGGSFGNNGFGGGPSDFGGNSGNFGQAQGTNSLPSLGSFSQNQGGTSSLPSLGSFGQNPGGPGGLGNGLSGGANGGVGTLGGANGAGGFNAVGGANGGPNGSPNAATNVPQGHDPNNSTQVTIPKELAGAIIGKGGGRIRRIRNESSAYITIDEPLPNSNDRIITISGTPKQIQMAQYLLQQSVHENGRRNI
Protein: Ribosomal protein L1p/L10e family (Q38AE4)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- RNA-binding protein, putative
- Nucleolar protein, putative
- Bms1-type G domain-containing protein
- Nucleolar RNA binding protein, putative
- KRR1 small subunit processome component
- Uncharacterized protein
- NLE domain-containing protein
- rRNA processing protein, putative
- Bystin, putative
- Nrap protein domain-containing protein
Sequence:
METPRSREALEKLCEFLLREAGHSEVSDTLEDLFATAPQKAFRKVDVEVAFLVSPVAHRVPLYYIVPHEIHQGSICIVTPPPQRRYKDEVLKLSEDGDAIFQRVKRVIDSNKLSVKFTHPVTVRALAKSFDNFFVYGVKKYPPQLTGEFCGHQRHPIWVPRRSPFAERIREAAKTVVVPRRGHNSVTCCIGHTGLSIEKLDENLRSFLTQLTNDPQGVTHENILRIRVMGMDYKNRCAGLPIFCHTFQIPRTLPEGEEEGRQTKKRKKE
Protein: NAD+ synthase, putative (EC 6.3.5.1) (Q381U8)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- Cytidyltransferase-like domain-containing protein
- ATP-NAD kinase-like protein
- NAD-dependent protein deacylase SIR2rp3
- NAD-dependent protein deacetylase SIR2rp1
- nicotinate phosphoribosyltransferase
Sequence:
MPKEPILHAELREWLEEYRRHRAFNPIAWIEEKCTKLNEYMRNNKLRGCVTNVSGGVDSAVVLSLCSRAQRMEGSPIVRNVGICQPICSSAWALERGRENIRAAGAEEVVVDQTDIHRQLSLSVEAAVGIDGKDFARGQLRSYMRAPVGYYVAQLCSQSGTPTIVMGTGNMDEDGYLGYFCKAGDGVVDVQLISDLHKSEVFKVARELGVPENTLQAAPSADLWDGQTDEEELGFPYDFVELYTGYFLKLNNGEREMKKKSLSAEARHQFEAYMKSCEETHCRNAHKLNGIVNL
Protein: T-box protein 37 (Q9U2C9)
Organism: Caenorhabditis elegans
Function: Transcription factor (By similarity). Required for mesodermal induction, acting redundantly with transcription factor tbx-38. Together with tbx-38, acts by inducing cell fates in the AB lineage, thereby playing a role in development of the anterior pharynx.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00201}.
Interaction partners:
- C2H2-type domain-containing protein
- Homeobox protein ceh-51
- GATA-type domain-containing protein
- Helix-loop-helix protein 14
- Defective pharyngeal development protein 4
Sequence:
MYSCTSPSGIEVSLNKPEIWEKFYPKTEMIVTRKRGRVIFPHLDYNVKGLDPDSLYSIYIHLERVDGIKYKFDAGEWKEAGKGDPILPIQYKEHPRGKRTGTEWMSEPVSFAHLKITNDPENKDQKLILAQSLHKYIPVLHIKQLDPYKGTFQMDFHGVEFRLEATQFIVVTAYQNEELTKLKVHHNKFASGFRSNGKRRLSSESENSENSPPKRSASAISSLTPPAISPPMDYTQQNPYFFNQNFFSTPQSHQPQFAAHSANAQNYNNFGAQNGAQFDWNVYYQRQWYWQQQMMMSGGIGQPQMLNNGFPNL
Protein: Platelet-activating factor acetylhydrolase homolog 2 (EC 3.1.1.47) (Q22943)
Organism: Caenorhabditis elegans
Interaction partners:
- Lissencephaly-1 homolog
- phospholipase A2
- Intracellular phospholipase A2
- Phospholipase A2
- Phospholipase A2
- 1-alkyl-2-acetylglycerophosphocholine esterase
Sequence:
MGSYISSPQVLTRQVSGQFQVGCKDLMIDGTVLGDRGLFMRLYFPTDSQAADISSYPLWLPKPQYAHGLGEYLGQSSQKMNVITSTVVGEKREDCIENAQMSTKCDKWPIVVFSHGLGGSRTFYSTYCTSLASHGYVVAAVEHKDHSACWTYQLTEKNGELVEQPIKIKLIEKNEKNEFKIRNQQVGKRVTECVKALNVLEQLNLGTVPEKVLIGNDYNWAQFKNKLVMSSASVIGHSFGGATSLASSAYTTDFQKAIVFDGWMYPLDSTQQEQAKQPTLFLNVGDWQWNENLDVMKKIISHNDGNLALTLNGAVHQCFSDFPFIFPSWLAKKFGVQGRTEPSLCMQAAIELSLAFLENGKDGAQKLKDEKFSSFISNEIYGREKYKL