wanglab/gogpt-training-data huggingface dataset:
Protein: Zinc finger protein zfp-1 (Protein AF-10 homolog) (P34447)
Organism: Caenorhabditis elegans
Function: Recruits the histone methyltransferase dot-1.1 to chromatin to methylate 'Lys-79' of histone H3 and activate transcription. Recognizes and binds histone H3 methylated at 'Lys-4' (H3K4me) at the promoters of target genes. During stress, the zfp-1-dot-1.1 complex also plays a role in the deubiquitination of histone H2B sites, which negatively modulates the RNA polymerase II-induced transcription of highly expressed genes. In response to stress, binds to the pdk-1 promoter to negatively regulate pdk-1 expression, which negatively modulates daf-16/FOXO-mediated gene expression. Thus, most likely via this mechanism, in response to stress, it confers a protective role against neuronal necrosis. Plays a role in Insulin/IGF-1-like signaling (IIS)- and diet restriction-mediated lifespan extension by controlling daf-16/FOXO and pha-4/FOXA recruitment to target promoters. May negatively regulate the expression of genes required for vulval development. May play a role in axon guidance in D-type motor neurons. May suppress sensitivity to RNAi.
Subcellular location: Nucleus {ECO:0000269|PubMed:23263989, ECO:0000305|PubMed:21980302, ECO:0000305|PubMed:23806335}. Chromosome {ECO:0000269|PubMed:23263989, ECO:0000305|PubMed:23806335}. Note=Localizes to all six condensed chromosomes (PubMed:23263989). zfp-1 and dot-1.1 colocalize to promoters of highly expressed genes (PubMed:23806335). {ECO:0000269|PubMed:23263989, ECO:0000269|PubMed:23806335}.
Interaction partners:
- Histone-lysine N-methyltransferase, H3 lysine-79 specific
- YEATS domain-containing protein
- DRBM domain-containing protein
Sequence:
MKEMVGGCCVCADENGWTDNPLIYCDGENCEVAVHQGCYGIQEVPEGEWFCAKCTKASAMMPGSINEATFCCQLCPFDYGALKKTDRNGWAHVICALYIPEVRFGNVHSMEPVILNDVPTDKFNKLCYICNEERPNDAKKGACMSCNKSTCKRSFHVTCAQRKGLLCEEGAISRNVKYCGYCENHLKKAINDPAIKVIPACPPVQRLSKEQDKKKTVLLTSLPLPPPAPRLHMLADPLPIKSNKVNNVLGLGSAINAVSLEERPASGSTVNSGIFVPPPTAFSPPLTTSSRSSVAQDPSPPLTINKNSLSSSGPLIPSTAHLSATTASATPIMANGSTLPPSSETTVGTHCLQQLQIQSAAAAAITQNQIGPSELNGYPAASQLSSFMHEIPARNTTSVASLLPPGAAEYHLNGSGDEEKTVKAVLTAPLTKAKRIRDSKNDMMDKTHKRPRANARPPAVLGSMSSGSSGGTVGKSPSMQRLQNLVAPIVSETVTDFQRDRVADRTAAERRAAAAQSQPSTSTNGGPNVTIPAVVEVHTNSTNSTNHQNNGLTQNAPASTSMQAGTSSNDGVISQNGTSSTSQSNRLNLPSFMEQLLERQWDQGSSLLMANAHFDVAQLLSCLFQLKSENFRLEENLSGLRKRRDHLFALNSRLAEVNTLDVSKRQRSDGLLLQQQIAHHLDPTSIVPKAEVHKQEPLSAPTSVPLPANHSSSLFEDIKAPKATYSRKTPSNIPLTVPLSTAATALTTTTAASSGAPVNSNIQNHRATPSTAGAPMAATPIMTAVTSANELAALSPERAQALLNMYRMPLDANVAAQLSMITNFPGQVNPSLFSRLLAVNMMNGGLQPNGQPLSALPPPTSATPNGK
Protein: Defensin-A (DefA) (GmDefA) (Q8WTD4)
Organism: Glossina morsitans morsitans (Savannah tsetse fly)
Function: Antibacterial peptide mostly active against Gram-positive and Gram negative bacteria.
Subcellular location: Secreted {ECO:0000255|PROSITE-ProRule:PRU00710, ECO:0000269|PubMed:11592981, ECO:0000269|PubMed:11886771}.
Interaction partners:
Sequence:
MKFYLVLAFLTLCAVAVTALPAGDETRIDLETLEEDLRLVDGAQVTGELKRDKRVTCNIGEWVCVAHCNSKSKKSGYCSRGVCYCTN
Protein: Structural maintenance of chromosomes protein 3 (SMC protein 3) (SMC-3) (Chromosome segregation protein SMC-3) (Cohesin complex subunit SMC-3) (Protein TITAN7) (Q56YN8)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Central component of cohesin, a complex required for chromosome cohesion during the cell cycle. The cohesin complex may form a large proteinaceous ring within which sister chromatids can be trapped. At anaphase, the complex is cleaved and dissociates from chromatin, allowing sister chromatids to segregate. Cohesion is coupled to DNA replication and is involved in DNA repair. The cohesin complex also plays an important role in spindle pole assembly during mitosis and in chromosomes movement (By similarity). Essential protein plant viability. Required for chromosome segregation (e.g. sister chromatid alignment) and cell division during embryogenesis.
Subcellular location: Nucleus {ECO:0000269|PubMed:15972315}. Cytoplasm {ECO:0000269|PubMed:15972315}. Nucleus matrix {ECO:0000269|PubMed:15972315}. Chromosome {ECO:0000269|PubMed:15972315}. Cytoplasm, cytoskeleton, spindle {ECO:0000269|PubMed:15972315}. Chromosome, centromere {ECO:0000250}. Note=Primarily associated with the nuclear matrix during interphase and with chromatin from prophase through anaphase in both somatic and meiotic cells. During mitosis and meiosis the protein also colocalized with the spindle from metaphase to telophase.
Interaction partners:
- Protein CHROMOSOME TRANSMISSION FIDELITY 7
- Structural maintenance of chromosomes protein 1
- Sister chromatid cohesion protein SCC2
- Sister chromatid cohesion 1 protein 1
- Sister chromatid cohesion 1 protein 2
- Sister chromatid cohesion 1 protein 3
- Sister chromatid cohesion 1 protein 4
- Sister-chromatid cohesion protein 3
- Protein GRAVITROPIC IN THE LIGHT 1
- Wings apart-like protein 1
Sequence:
MFIKQVIIEGFKSYKEQVATEEFSNKVNCVVGANGSGKSNFFHAIRFVLSDIYQNLRSEDRHALLHEGAGHQVVSAFVEIVFDNSDNRFPVDKEEIRLRRTVGLKKDDYFLDGKHITKGEVMNLLESAGFSRANPYYVVQQGKIASLTLMKDIERLDLLKEIGGTRVYEERRRESLRIMQETGNKRKQIIEVVHYLDERLRELDEEKEELRKYQQLDKQRKSLEYTIYDKELHDAREKLEQVEVARTKASEESTKMYDRVEKAQDDSKSLDESLKELTKELQTLYKEKETVEAQQTKALKKKTKLELDVKDFQDRITGNIQSKNDALEQLNTVEREMQDSLRELEAIKPLYESQVDKENQTSKRINELEKTLSILYQKQGRATQFSNKAARDKWLRKEIEDLKRVLDSNTVQEQKLQDEILRLNTDLTERDEHIKKHEVEIGELESRISKSHELFNTKKRERDEEQRKRKEKWGEESQLSSEIDKLKTELERAKKNLDHATPGDVRRGLNSIRRICADYRINGVFGPLVELVDCDEKFFTAVEVTAGNSLFNVVVENDDISTKIIRHLNSLKGGRVTFLPLNRIKAPRVNYPKDSDAIPLLKKLKFDSKFEPALGQVFGRTVVCRDLNVATRVAKNDDLDCITMEGDQVSRKGGMTGGFYDHRRSKLRFMNIIMQNTKSINEKEKELEDVRRQLQVIDQQITQLVTEQQRLEADWTLCKLQVEQLKQEIANANKQKHAIHKAIEYKEKLLGDIRTRIDQVRSSMSMKEAEMGTELVDHLTPEEREQLSKLNPEIKDLKEKKFAYQADRIERETRKAELEANIATNLKRRITELQATIASIDDDSLPSSAGTKEQELDDAKLSVNEAAKELKSVCDSIDEKTKQIKKIKDEKAKLKTLEDDCKGTLQDLDKKLEELFSLRNTLLAKQDEYTKKIRGLGPLSSDAFDTYKRKNIKELQKMLHRCSEQLQQFSHVNKKALDQYVNFTEQREELQNRQAELDAGDEKIKELITVLDQRKDESIERTFKGVAHHFRDVFSELVQDGYGNLIIMKKKDLDNDDEDDDDDDGGREAVTEGRVEKYIGVKVKVSFTGQGETQLMKQLSGGQKTVVALALIFAIQRCDPAPFYLFDEIDAALDPQYRTAVGNLIRRLADDYGTQFITTTFRPELVRVADKIYGVFHKNRVSIVNVISKDQALDFIEKDQSHDT
Protein: Transgelin-2 (Epididymis tissue protein Li 7e) (SM22-alpha homolog) (P37802)
Organism: Homo sapiens (Human)
Interaction partners:
- WD repeat-containing protein 90
- Actin, cytoplasmic 1
- Peptidyl-prolyl cis-trans isomerase A
- Cofilin-1
- Profilin-1
Sequence:
MANRGPAYGLSREVQQKIEKQYDADLEQILIQWITTQCRKDVGRPQPGRENFQNWLKDGTVLCELINALYPEGQAPVKKIQASTMAFKQMEQISQFLQAAERYGINTTDIFQTVDLWEGKNMACVQRTLMNLGGLAVARDDGLFSGDPNWFPKKSKENPRNFSDNQLQEGKNVIGLQMGTNRGASQAGMTGYGMPRQIL
Protein: 3-isopropylmalate dehydratase small subunit 3 (EC 4.2.1.33) (2-(omega-methylthio)alkylmalate dehydratase small subunit 3) (EC 4.2.1.170) (AtLEUD2) (Isopropylmalate isomerase 1) (Isopropylmalate isomerase small subunit 3) (IPMI SSU3) (Methylthioalkylmalate isomerase small subunit) (MAM-IS) (Q9LYT7)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Catalyzes the isomerization between 2-isopropylmalate and 3-isopropylmalate, via the formation of 2-isopropylmaleate (Probable). Functions redundantly with LEUD1 in the methionine chain elongation pathway of aliphatic glucosinolate formation.
Subcellular location: Plastid, chloroplast stroma {ECO:0000269|PubMed:20663849}. Plastid {ECO:0000269|PubMed:32612621}.
Interaction partners:
- 3-isopropylmalate dehydrogenase 3, chloroplastic
- 3-isopropylmalate dehydrogenase 1, chloroplastic
- 3-isopropylmalate dehydratase large subunit, chloroplastic
- 3-isopropylmalate dehydrogenase 2, chloroplastic
- 2-isopropylmalate synthase 2, chloroplastic
- 2-isopropylmalate synthase 1, chloroplastic
- Methylthioalkylmalate synthase 1, chloroplastic
- Methylthioalkylmalate synthase 3, chloroplastic
- Methionine aminotransferase BCAT4
- 3-isopropylmalate dehydratase small subunit 2
Sequence:
MATSQQFLNPTLFKSLASSNKNSCTLCPSPFLQLKSASTIFNYKPLTSSSATIITRVAASSSDSGESITRETFHGLCFVLKDNIDTDQIIPAEYGTLIPSIPEDREKLGSFALNGLPKFYNERFVVPGEMKSKYSVIIGGDNFGCGSSREHAPVCLGAAGAKAVVAESYARIFFRNCVATGEIFPLESEVRICDECKTGDVVTIEHKEDGSSLLINHTTRKEYKLKPLGDAGPVIDAGGIFAYARKAGMIPSA
Protein: Ribosomal protein S13p/S18e (AFU_orthologue AFUA_6G13550) (Q5B1Y9)
Organism: Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Interaction partners:
- 60S ribosomal protein L23
- 40S ribosomal protein S24
- 60S ribosomal protein L29
- GBLP_NEUCR Guanine nucleotide-binding protein beta subunit-like proteinGbeta like protein
- 60S ribosomal protein L35Ae
- RNA polymerase I specific transcription initiation factor Rrn7, putative
- 60S ribosomal protein L12
- Uncharacterized protein
- Ribosomal protein L26
- 40S ribosomal protein S6
Sequence:
MSLVSGEKTNFQYILRLLNTNVDGKEKIMYALTQVKGVGRRYSNLVCKKADVDLNKRAGELTTEELERIVTILQNPTQYKIPTWFLNRQRDIVDGKDYQVLSNGLDSKYREDLERLKKIRSHRGLRHYWGLRVRGQHTKTTGRRGRTVGVSKKKG
Protein: LIM domain-containing protein E (DdLim) (O60952)
Organism: Dictyostelium discoideum (Social amoeba)
Function: Associates with the actin cytoskeleton and may regulate actin polymerization in lamellipodia, through a rac1-dependent signaling pathway. May play a role in cell motility. Involved in cytokinesis by regulating the microtubule system and linking it to the cortical actin network.
Subcellular location: Cytoplasm. Cytoplasm, cell cortex. Nucleus. Cell projection, lamellipodium. Cell projection, filopodium. Cytoplasm, cytoskeleton. Note=Weakly expressed in cytoplasm. Found in actin-rich protrusions, and lamellipodia and filopodia during motility.
Interaction partners:
- Elongation factor 1-beta
Sequence:
MSASVKCGACAKTAYPLESVVANNNSYHKGCFKCSTCNSTLNVKTFKSFEGKLYCPVHTPKVSATAVTDSVALKNALNAPKKVAEGLGNAHRGLDEKPNIGLDSMATANALNAPKKVVEGLGNVQKGIGGKPTYAVFGADGQPTGEQQEQQQYTEEQYEQPQEEQQYQEEQQQYQEEEQQYQEEEQQYQEEEQQYEEEQ
Protein: RNA-binding KH domain-containing protein RCF3 (Protein ENHANCED STRESS RESPONSE 1) (Protein HIGH OSMOTIC STRESS GENE EXPRESSION 5) (Protein REGULATOR OF CBF GENE EXPRESSION 3) (Protein SHINY 1) (Q8W4B1)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Acts as negative regulator of osmotic stress-induced gene expression. Involved in the regulation of thermotolerance responses under heat stress. Functions as an upstream regulator of heat stress transcription factor (HSF) genes. Negatively regulates HSFA1A, HSFA1B and HSFA1D, but positively controls the expression of HSFA1E, HSFA3, HSFA9, HSFB3, and DREB2C. Forms a complex with CPL1 that modulates co-transcriptional processes such as mRNA capping and polyadenylation, and functions to repress stress-inducible gene expression. Regulates pre-mRNA processing under salt stress. Involved in primary miRNA processing and pri-miRNA biogenesis. Binds both intronless and intron-containing pri-miRNAs. Acts as a regulator of biotic stress response gene expression and basal JA-mediated responses involved in defense. Acts as negative regulator of resistance to the fungal pathogen Fusarium oxysporum.
Subcellular location: Nucleus {ECO:0000269|PubMed:23087326, ECO:0000269|PubMed:23874224, ECO:0000269|PubMed:24146632, ECO:0000269|PubMed:24303021}. Nucleus speckle {ECO:0000269|PubMed:24146632}. Note=Localizes predominantly in nuclear speckles. {ECO:0000269|PubMed:24146632}.
Interaction partners:
- RNA polymerase II C-terminal domain phosphatase-like 1
- RNA polymerase II C-terminal domain phosphatase-like 2
- KH domain-containing protein
- Double-stranded RNA-binding protein 1
- Serine/arginine-rich splicing factor RS40
- Serine/arginine-rich splicing factor RS41
- KH domain-containing protein
- Nuclear cap-binding protein subunit 2
- G patch domain-containing protein TGH
- Protein MOS2
Sequence:
MERSRSKRNYHYDQDYDGDSMPRSKPRYNNNYHFGGGGGGNNRYRGGGGGGGGNGRPSKSHPETMATTTYRILCHDAKAGGVIGKSGTIIKSIRQHTGAWINVHELVPGDAERIIEISDNRRRDPDGRMPSFSPAQEALFSVHDRILESEAQFGYGGPPPEEEEDYGGVRPGGGRVVTRLVVSRMHVGCLLGKGGKIIEQMRIETKTHIRILPRESNLPRCVSLSEEIVQIVGELNAVKNALAIVSSRLRESQHRDRSNFQGRSHSPERSFAAAGDDYMPQLRRQSSDRFPRGNFRNNNFSSRQSNYAEEAPAVPVGENVYSEELVFQILCPADKIVRVVGESQGIIDLLQNEIGVDVRVSDPVAGSDEQIITISSEEAPDDPFFPAQEALLHIQTQIIDLIPDKDNLITTRLLVPSRDSICLEGKAGSVSEISRLTGTSVQILAREEIPRCASINDVVIQITGEIRAAREALVELTLLLRSHMFKELSQKETPPASTSTTGPLEGVAGVMEVASSNNTIQSREGPTSSNLNLQQVSTILPQFKEGFGSVAKAGESEHREEVPVTTSRMAVPLVTRSTLEVVLPEAVVPKLVTKSRNKLAQISEWSGASVTIVEDRPEETQNIIRISGTPEQAERAQSLLQGFILSIQEDGP
Protein: Putative 6-pyruvoyl tetrahydrobiopterin synthase (PTP synthase) (PTPS) (EC 4.2.3.12) (O02058)
Organism: Caenorhabditis elegans
Function: Involved in the biosynthesis of tetrahydrobiopterin, an essential cofactor of aromatic amino acid hydroxylases. Catalyzes the transformation of 7,8-dihydroneopterin triphosphate into 6-pyruvoyl tetrahydropterin (By similarity).
Interaction partners:
- GTP cyclohydrolase 1
- Cysteine--tRNA ligase, cytoplasmic
- Tyrosine-protein phosphatase 4
- 3-oxo-5-alpha-steroid 4-dehydrogenase
- 3-oxo-5-alpha-steroid 4-dehydrogenase
- cGMP-dependent protein kinase
- cGMP-dependent protein kinase egl-4
- Putative pterin-4-alpha-carbinolamine dehydratase
- Phenylalanine-4-hydroxylase
Sequence:
MFRMPIVTMERVDSFSAAHRLHSEKLSDAENKETFGKCNNSNGHGHNYVWKVKLRGEVDPTSGMVYDLAKLKKEMSLVLDTVDHRNLDKDVEFFKTTVSTSENVAIYMFEKLKSVMSNPSVLYKVTIEETPKNIFTYKGC
Protein: Nucleoporin 155 (Q54F20)
Organism: Dictyostelium discoideum (Social amoeba)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- Nuclear pore protein
- Nuclear pore protein
- Uncharacterized protein
- Nuclear pore complex protein nup54
- Nucleoporin 133
- Nuclear pore complex protein
- Nuclear pore complex protein nup85
- Protein SEC13 homolog
- Nuclear pore complex protein nup43
- Uncharacterized protein
Sequence:
MRQSQLYPNLGYNNQNGQFNYLPSPEQQSIYRNNIQTPTSGISNNLFPLQSQQRIIQPQYHYQTPLINNNIINNNNNINNNNIVYQQDQQTQPQAQPQQQPQQTQTQSPSQQEKEQEQQQQELKEQQQKQQQQQEQEQQELMRQKKTNSLLSITPFNKEEDLKKIFLNSIESIDSSIDKVATIPDPTLKVLYKRDPGFNYFDGGSYFWSTLVIEKHIELPQEITNGYLSTSTKSLLGLFPEIGRAWISIDQTLYLWDYRDSGELISHNLSQIITNCALIQPKKNTFKDAVKKVMVVCTHVEIFLFALCYSNETKFEILSTLSIPSDNIFITDIVGTKEGRIFLSGQDGNIYEIEYSKDNLFWFSNEKIKKINLTQTFFNSFINLSKKKEIIQLIYDEDRYLLYSLSKDSTINVYSLGKIGDKFEHLKTIYPINDIDSLFNNNINNNNNNNNYYSQQYQYQQQQQNQQYQQSQYGQQQQQQQPNQYGQQQQQQQPLQQQQQQQQQQQQNFSRKNMVIMSIHISPKETEFNFIAILSSGERLYYTLNRLAYIRSPPNNVDNNGNSNIHYTYYSNGVFFTASEVSDQEDRLVGTTLFGNDIIKSHYETSKSGFSNQISQDTLSEKSNLFSIRGRVSVIKEDIVNDGKPTVYYKELSNEHMNTPRRFLCLNSLGLHFISKLRYVDLLQNILSSNNPQDIDNFFDAFGKIIASSLCISLYCSSPHSSILLHDQVYSGISIPKTTTTRIADLAMTFLRRKSGKPQYYQPVVIQQMFGDMGAPVNKTELMYSNAYNGLLAYLARVLYPLWNQSVVTSAGCSYWSIVQLQLFQSHLSNLLSFLDISQLIPKGQEIPIIKIATNKTSSTTTTTTTANNSSSNEIYGEDEAIKNEKRSLIGLKNIIVKSIQILNLFLILSQYNFKQLFDSSSIELDIKRKIDLLKFRDILNSDILGKNLPLPTISSLTTSTTTTTTTTTTSTTSSSSSSTSPLTTSTSNSTLTLLIDSLMKTLNSHNINIDQVSNQLETECPIFFKKENRELYKVKEKLNMVLRDGSTYFTDSLVKDSALILDSISPNYNLSEIVDLFIAIKAFNYVTPLCLQYAQDLDPRGITLIPSNNPSDEFKLKLSQKKSTFQEIIKLLNFIQSDNNNNNNNSGGGGGDNNNYNNTFEIIDIIIQQVLVCQDRLAHEMIYSWILNNGMTSKFFEINTPFITEFLFANDIDLCWKVLAKHQELLKAVHVLFQIAERSTTLDEKILAYTNCTMILSEQKDEDAYIQAKNQITFANIQKQIVLQLENYLNNPNESNNRNNSSNNNGGQPFDINQIKESISNLNKTIFDITTLFTDYARKYYLHEQMLYLCHIGNHSDQNFIQILWKIIIDKEIPPPSSNLSLDDNAENDDGLKISVGGVIESLVSKISNIGYDFYPNEITFPVEFIINYGERAIFNFSRNKSEAEKKEISPNWLTSSLHDHVKIDYWILVDYYNNTIEKGSWKEEDESLIYITSVYFYLVESLINTIQTATERRLFSSKQILQSLENRESTFKSIFNRQRSSLNQETIKKLEQLLIKFEKIISISKSFKDFRGY
Protein: p300/CBP-associated factor (Q568Z2)
Organism: Rattus norvegicus (Rat)
Interaction partners:
- Histone lysine acetyltransferase CREBBP
- histone acetyltransferase
- Transcriptional adapter 3
- Nuclear receptor coactivator
- Transcriptional adapter 2-alpha
- Nuclear receptor coactivator 2
- SAGA-associated factor 29
- Recombining binding protein suppressor of hairless
- Transcription initiation factor TFIID subunit 10
- Transcription initiation factor TFIID subunit 9B
Sequence:
MEPVKRTEAPGYYEVIRFPMDLKTMSERLRNRYYVSKKLFMADLQRVFTNCKEYNPPESEYYKCASVLEKFFFSKIKEAGLMDK
Protein: HPr kinase/phosphorylase (HPrK/P) (EC 2.7.11.-) (EC 2.7.4.-) (HPr kinase/phosphatase) (HPr(Ser) kinase/phosphorylase) (O34483)
Organism: Bacillus subtilis (strain 168)
Function: Catalyzes the ATP- as well as the pyrophosphate-dependent phosphorylation of 'Ser-45' in HPr, a phosphocarrier protein of the phosphoenolpyruvate-dependent sugar phosphotransferase system (PTS). HprK/P also catalyzes the pyrophosphate-producing, inorganic phosphate-dependent dephosphorylation (phosphorolysis) of seryl-phosphorylated HPr (P-Ser-HPr). The two antagonistic activities of HprK/P are regulated by several intracellular metabolites, which change their concentration in response to the absence or presence of rapidly metabolisable carbon sources (glucose, fructose, etc.) in the growth medium. Also phosphorylates/dephosphorylates the HPr-like catabolite repression protein crh on 'Ser-46'. Therefore, by controlling the phosphorylation state of HPr and crh, HPrK/P is a sensor enzyme that plays a major role in the regulation of carbon metabolism and sugar transport: it mediates carbon catabolite repression (CCR), and regulates PTS-catalyzed carbohydrate uptake and inducer exclusion.
Interaction partners:
- HPr-like protein Crh
- Phosphocarrier protein HPr
- DNA-binding transcriptional repressor ScoC
- Pyrophosphatase PpaX
- Phosphatidylglycerol--prolipoprotein diacylglyceryl transferase
- Phosphoenolpyruvate-protein phosphotransferase
- Catabolite control protein A
- Fructose-1,6-bisphosphatase class 3
- Uncharacterized membrane protein YvoD
- Serine/threonine-protein kinase PrkC
Sequence:
MAKVRTKDVMEQFNLELISGEEGINRPITMSDLSRPGIEIAGYFTYYPRERVQLLGKTELSFFEQLPEEEKKQRMDSLCTDVTPAIILSRDMPIPQELIDASEKNGVPVLRSPLKTTRLSSRLTNFLESRLAPTTAIHGVLVDIYGVGVLITGKSGVGKSETALELVKRGHRLVADDCVEIRQEDQDTLVGNAPELIEHLLEIRGLGIINVMTLFGAGAVRSNKRITIVMNLELWEQGKQYDRLGLEEETMKIIDTEITKLTIPVRPGRNLAVIIEVAAMNFRLKRMGLNAAEQFTNKLADVIEDGEQEE
Protein: Similar to cain (Q8CGG3)
Organism: Mus musculus (Mouse)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MIRIAALNASSTIEDDHEGSFKSHKIQTKEAQEAEAFALYHKALDLQKHDRFEESAKAYHELLEARLLREAVSSGDEKEGLKHPGLILKYSTYKNLAQLAAQREDLETAMEFYLEAVMLDSTDVNLWYKIGHVALRLIRLPLARHAFEEGLRCNPDHWPCLDNLITVLYTLSDYTTCLYFICKALEKDCRYSKGLVLKEKIFEEQPCLRKDSLRMFLKCDMSIHDVSVSAAETQAIVDEALGLRKKRQALIVREKEPDLKLVQPIPFFTWKCLGESLLAMYSHLTTCEPPRPSLGKRIDLSDYQDPSQLLASSVVVTPVSVVQPSPICTNPTVAVAEPVLSYTSVTAASFPLHSPSLLDTGTPMGDVSGGDKSKKGVKRKKTVEESGETAKRRSARVRNTKCKKKKKKK
Protein: RAF proto-oncogene serine/threonine-protein kinase (EC 2.7.11.1) (Proto-oncogene c-RAF) (Raf-1) (A0A0S2Z559)
Organism: Homo sapiens (Human)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004236}.
Interaction partners:
Sequence:
MEHIQGAWKTISNGFGFKDAVFDGSSCISPTIVQQFGYQRRASDDGKLTDPSKTSNTIRVFLPNKQRTVVNVRNGMSLHDCLMKALKVRGLQPECCAVFRLLHEHKGKKARLDWNTDAASLIGEELQVDFLDHVPLTTHNFARKTFLKLAFCDICQKFLLNGFRCQTCGYKFHEHCSTKVPTMCVDWSNIRQLLLFPNSTIGDSGVPALPSLTMRRMRESVSRMPVSSQHRYSTPHAFTFNTSSPSSEGSLSQRQRSTSTPNVHMVSTTLPVDSRMIENNNLSASPRAWSRRFCLRGRDAIRSHSESASPSALSSSPNNLSPTGWSQPKTPVPAQRERAPVSGTQEKNKIRPRGQRDSSYYWEIEASEVMLSTRIGSGSFGTVYKGKWHGDVAVKILKVVDPTPEQFQAFRNEVAVLRKTRHVNILLFMGYMTKDNLAIVTQWCEGSSLYKHLHVQETKFQMFQLIDIARQTAQGMDYLHAKNIIHRDMKSNNIFLHEGLTVKIGDFGLATVKSRWSGSQQVEQPTGSVLWMAPEVIRMQDNNPFSFQSDVYSYGIVLYELMTGELPYSHINNRDQIIFMVGRGYASPDLSKLYKNCPKAMKRLVADCVKKVKEERPLFPQILSSIELLQHSLPKINRSASEPSLHRAAHTEDINACTLTTSPRLPVF
Protein: CREB regulated transcription coactivator 1 (M0QX46)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MLQLQKSQYLQLGPSRGQYYGGSLPNVNQIGSGTMDLPFQTPFQSSGLDTSRTTRHHGLVDRVYRERGRLGSPHRRPLSVDKHGRQADSCPYGTMYLSPPADTSWRRTNSDSALHQSTMTPTQPESFSSGSQDVHQKRVLLLTVPGMEETTSEADKNLSKQAWDTKKTGSRPKSCEVPGINIFPSADQENTTALIPATHNTGGSLPDLTNIHFPSPLPTPLDPEEPTFPALSSSSSTGNLAANLTHLGIGGAGQGMSTPGSSPQHRPAGVSPLSLSTEARRQQASPTLSPLSPITQAVAMDALSLEQQLPYAFFTQAGSQQPPPQPQPPPPPPPASQQPPPPPPPQAPVRLPPGGPLLPSASLTRGPQPPPLAVTVPSSLPQSPPENPGQPSMGIDIASAPALQQYRTSAGSPANQSPTSPVSNQGFSPGSSPQHTSTLGSVFGDAYYEQQMAARQANALSHQLEQFNMMENAISSSSLYSPGSTLNYSQAAMMGLTGSHGSLPDSQQLGYASHSGIPNIILTVTGESPPSLSKELTSSLAGVGDVSFDSDSQFPLDELKIDPLTLDGLHMLNDPDMVLADPATEDTFRMDRL
Protein: WD repeat-containing protein 47 (Neuronal enriched MAP-interacting protein) (Nemitin) (O94967)
Organism: Homo sapiens (Human)
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000250}. Note=Localization along microtubules is mediated by MAP1S. {ECO:0000250}.
Interaction partners:
- Calmodulin-regulated spectrin-associated protein 3
- Calmodulin-regulated spectrin-associated protein 2
Sequence:
MTAEETVNVKEVEIIKLILDFLNSKKLHISMLALEKESGVINGLFSDDMLFLRQLILDGQWDEVLQFIQPLECMEKFDKKRFRYIILKQKFLEALCVNNAMSAEDEPQHLEFTMQEAVQCLHALEEYCPSKDDYSKLCLLLTLPRLTNHAEFKDWNPSTARVHCFEEACVMVAEFIPADRKLSEAGFKASNNRLFQLVMKGLLYECCVEFCQSKATGEEITESEVLLGIDLLCGNGCDDLDLSLLSWLQNLPSSVFSCAFEQKMLNIHVDKLLKPTKAAYADLLTPLISKLSPYPSSPMRRPQSADAYMTRSLNPALDGLTCGLTSHDKRISDLGNKTSPMSHSFANFHYPGVQNLSRSLMLENTECHSIYEESPERDTPVDAQRPIGSEILGQSSVSEKEPANGAQNPGPAKQEKNELRDSTEQFQEYYRQRLRYQQHLEQKEQQRQIYQQMLLEGGVNQEDGPDQQQNLTEQFLNRSIQKLGELNIGMDGLGNEVSALNQQCNGSKGNGSNGSSVTSFTTPPQDSSQRLTHDASNIHTSTPRNPGSTNHIPFLEESPCGSQISSEHSVIKPPLGDSPGSLSRSKGEEDDKSKKQFVCINILEDTQAVRAVAFHPAGGLYAVGSNSKTLRVCAYPDVIDPSAHETPKQPVVRFKRNKHHKGSIYCVAWSPCGQLLATGSNDKYVKVLPFNAETCNATGPDLEFSMHDGTIRDLAFMEGPESGGAILISAGAGDCNIYTTDCQRGQGLHALSGHTGHILALYTWSGWMIASGSQDKTVRFWDLRVPSCVRVVGTTFHGTGSAVASVAVDPSGRLLATGQEDSSCMLYDIRGGRMVQSYHPHSSDVRSVRFSPGAHYLLTGSYDMKIKVTDLQGDLTKQLPIMVVGEHKDKVIQCRWHTQDLSFLSSSADRTVTLWTYNG
Protein: Cas4p (A0A1D8PJ86)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Interaction partners:
- Serine/threonine-protein kinase CBK1
- Hym1p
- Sog2p
- CBK1 kinase activator protein MOB2
- non-specific serine/threonine protein kinase
Sequence:
MIEIPDLDELSLHNYSASNNVTPEENHSEDESQQPPPQQQQQQFTLQPQHSIHSPSIEENGYLQHQQNQLHQYMQQQQHNTLTPEPPTISDFTKDQLPPSATSFQNSTIGSDILGETIALYNSSANSSNIHKSQPQLPQESSDHLTQKETSTVSASSHPMLDQAPQMIDARLERIEHEVDNFNERENNYQHPQMQPYSQDTESGLSLGTEDSQNISSQKVDYVQTKNSSLEFDAPIGLVYMPDNLDEHKTSFKLQQPPIVTDYRDTTTTTPDLASESNDQLGQLETPLMAGFDFNLGTNTSSANQLSSPMSSFPLHNRVEPSPQLPPPMSSASLQKLTLRNGEEFGSIRRDLATDSKTSAEYTLHIIFTQFVRHAERKLNLCLDYPLNEEPPILDLIAEGVDTEFDKIISALGYIARRKPKPVIDSVMFWRKSKSEVASMAATEVEKAVGVAQTNLLRISKTSSATATTTTSPISPSNPGIAKNSNTASTAKRSLSLMRKKSFSRIAHRRNVSSSAAIQSSQNVPESESVFMKQKQFYDDQISQAKETAVHADRKSLASIYILCRVLIEIVKQTPLSVMGSDLSSKLEEIVYTQLKTTDPISTSQSLVRAANWNLFAELLGFMSRERFVSVNDRFIADLEKVPQQIRHEDEPKLYLLINGMKYLKLTIYPLEEFEESAEFIQSLAKFFDKTTNETVLYAYCEVFSQLFLPLANVMTAEANYPSWVEGVEKVYYKAFKLWRQSLGSTSSPTSLALPTSNTSGVSSNNGWSHSLILMASALSVSRKELFSEVWVNVINENSFKLKPKVEAEDKTTYIMSITRLIWVYLNRLPDTLNNTIKRLDAIFELLFFHNNATSKKHQWISPDLFLIGSLIELIRIVGYNHLNYVLEQVLIRLLNMSFNGTSLENAFPEKLIIVIKSYLAILKDYEIGDKPSFPADFPNEQKKKVNEFLFISKNSTNSAAHEEICRTLVLLLKILDSQYGSGFNNESNSLFSLGSSKSQSSFGFHFNYDPTPQTTKEVHIQLFATVIEAIPWGIVGASGDNSQNLIPFKQVVDILIRGAIHPDSRISMASIKSLKYLASKKNPTSLMTIYAKLAFHFSDKTGPTYDTQYLYSDQFTKLLKLYTELLDCWLISFQDLLEKKKADQSIGVLAGNDKSNNRDALNNLYKINRKNADLSDSHPTRLNPSDEFEWKTIITAIEDIEGNGLFFLCSQNPKTRYYGIKVLKLVEQFDQAVYNVTDSATDTSSGTKQHSRSSSKFAADVGTRLIHILEDLDFVELIQPYRKELSVPERTRLTKLKNKKNILIRLAESDYGIDSAIWLRLYPKVLEIFFDRCPMPVAMCRNLVCVCLVQMHEFVLEFSDSYKSYTSSLFSKSATNVPPEVLVNQWKLYLIFACSTLTATNDQKISFPNQPTHGRKKSLQMFIQHQKITSAKSVFKMVLPLLKSSQPMVKESVIVGLSHININILKSFLENIPLAVEEWNTNIKTRNPQDDAFRIEVVHILTNLTEKFGSHELIYTDDSIVANLVAIVKNVKNFLSEPAIQTNFECQRLRRYFCGFLENVYTGLEAKSDLEKWLPFEARVACFNYLKEWCGYGDSSAVTEERYNAIISRIKTEKAGPSALAILEIERKKLQLASLKCMAILCSGQIKKKIEIPGNLAVVSFDIPGLMNWIQALLESNVEKIKEIGHCASRNVIEKNFEFQDIISAVVQRCYVSQTSLESYFCLFVEIFMEKNTFEIVSDELLCLASVLTANESFQVRKSAIALLKYFEKKSLGSESLERYTEAICSKSSVVYKKVLFDLSNDVQNIKPESLYNRISYLTQNINLIFPAAREAILSLLVPMVSKVTLNYETPLPEKDSTTDIHEKAFDSSSLMVLSNLFEITVNFGSSMSNQVEVLWISLSNNVQNIDKIVEFLLQSSLESKNPSFVEQSRQIIDYLAFARSDPAYIIDKLINNLQPRMMVPPQLGNKSTAPISKDYPYVCDIKRIIQTNEKDVIFSLGQLSMVFLVDIVTLKNDLMIEKLPLLLHVSLSLMDHYLPIVQEQAGTFLVHLIHALVRDDPKAQETISSLRENDHIKHLWVYDDLNNDKKGARTPKNMDLLIRSAIKMFAAVAPNIQDDWSRVSLHWATTCAVRHIACRSFQVFRSLLSFLDQSMLKDMLHRLSNTISDETVDIQGFAMQILMTLNAITAELDSEKLIDFPQLFWSSVACLSTIHEQEFIEVLSTLNKFISKIDLDAADTVACLTKTFPQKWEGKFEGLQQVILVGLRSSTSWEPTLKFLDKLIVHKDSLIIGMGDSRVLTALLANMPRFLHHLSEENVTPEIENTAMALSQLAEDSGKSSLAKLLVSFAKRRFRSKSDFLDQSISCIKNAFFPEYQAQTLVLLLGLLFNKMPWVKTETLGLLQSIFPLVDLQRDEFIGVGADLISPLLRLLLTDYAEWALQVLDEAEIIPGSQSDKDILRMSLGSTSMKKEYENTATLFGIPDESGWSIPMPAITAATTRNNVHAVFSTCTLDNIVDENVEQEEDGIDIQFHSEDYYGTASDQTQFVDSVSVSVDEREASLSNVWAALDDFDSFFTKESEQAGSIPVVANRAMRRSHAHPRHHVHSASVDTKYSNSSDTLMPMESAPNVYDKKASVILNRSLARTTSNTSFRANLADSIGSTQIATNSNHSNKRSYIPFRSSRHGNKARAEVFSTPKIPLSAGFDANDLDQTPSSIQSTAISSPTISVARNDGDHELASNANENVTRFEGILGTKKKSKKGIRQNSPNESTTNISPDLTANNSFRNSHVSSIASPKGAAAVISSPIQVVGSNTAVTPNSGKEKKRISQKFR