wanglab/gogpt-training-data huggingface dataset:
Protein: Microtubule-associated protein 1S (MAP-1S) [Cleaved into: MAP1S heavy chain; MAP1S light chain] (P0C5W1)
Organism: Rattus norvegicus (Rat)
Function: Microtubule-associated protein that mediates aggregation of mitochondria resulting in cell death and genomic destruction (MAGD). Plays a role in anchoring the microtubule organizing center to the centrosomes. Binds to DNA. Plays a role in apoptosis. Involved in the formation of microtubule bundles (By similarity).
Subcellular location: Nucleus {ECO:0000250}. Cytoplasm, cytosol {ECO:0000250}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:17658481}. Cytoplasm, cytoskeleton, spindle {ECO:0000269|PubMed:17658481}. Note=Detected in perinuclear punctate network corresponding to mitochondrial aggregates and in the nucleus in cells exhibiting apoptosis. Associated specifically with microtubules stabilized by paclitaxel and colocalizes with RASSF1. In interphase cells, shows a diffuse cytoplasmic staining with partial localization to the microtubules. During the different stages of mitosis detected at the spindle microtubules (By similarity). Detected in filopodia-like protrusions and synapses. {ECO:0000250}.
Interaction partners:
- Microtubule-associated protein 1 light chain 3 alpha
- Sequestosome-1
- Beclin-1
- Microtubule-associated protein 1 light chain 3 beta
- Ubiquitin-like protein ATG12
- Autophagy protein 5
- Ubiquitin-like modifier-activating enzyme ATG7
- Microtubule-associated protein 1 light chain 3 beta
- Ras association domain-containing protein 1
- Ubiquitin-like-conjugating enzyme ATG3
Sequence:
MAAVMAAPEPAEAPSSLLLLVVGGECGCPGLLAYVLEELERGVRSWEDVDPDVCSLDEQLKAFVSRHSATFSSIVKGQRSLHHRGETLETLVLLNPSDKSLCDELRNLLMDPAPHKLLVLAGPCLEETGELLLQTGGFSAHHFLQVLGDKEVQDALASAPAAPALTVSCPTFGDWALLGPAPGLRLRLNPPARLPSSEGLRAFLEYVAESLEPPSPFELLEPPATGGFLRLARPCCYVFPGGLGDAAFFAVNGFTVLVNGGSNPKSSFWKLVRHLDRVDAVLVTHAGADSLPGLNSLLRRKLAEREAAAGPQGQHEERLRRLLSPALGVVFLNAREAGSRLRGGEDEAVCARSLLRSLGIVPLPLQRGPQPSCPTVLFEKLGVGRLELFVLHPPPGDPAAPACALLVWQPAAPGDKVVRVLFPGRTPPARLLDGLQRLQHLPCLRRPVVTTQDLEVPSRANSQDSLASRDSTRKEPVRGTVGATSRSAVRREPALATRDQKKDTKPGPTRSTVRDVRRSGPGVVTTKPRVSQNGPRAPVPAAPPAAPAPEFPGEAENIVESERPPAPSPTLSPAQSPPPTAPGNSPERLSLSPLRPEPAPDASPSATTPTLTTPSLPAELGSPHSTEVDESLSVSFEQVLPAGDAGLSLPLRLARRSTSPHDVDLCLVSPCEFSHRKPPPPASPGSSDSSARSQERPPETPPTSVSESLPTLSDSDPVPVADSDDDAGSESAARDPLPTPRVPPPLPDAPGICMVDPEALPPRARQPLSTANSSRGRKAPARPSSASAAPRAATVAAKTKGPVGDRSRPLSARSEPADKPGRVPLTRKPSVPKTVPKMASATRNSSGPSSRPAPLAAGSPVYLDLAYLPGGGAGHLDQNFFLRVRALCYVISGQGQRQEEGLRGVLDALLAGKRQWDLDLQVTLIPTFDSAVMHRWYEETHEQHQALGIRVLGSGSLVSMQDEAFPACKVEF
Protein: Serine hydroxymethyltransferase 1 (SHM1) (SHMT 1) (Serine methylase 1) (EC 2.1.2.1) (P9WGI9)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: Catalyzes the reversible interconversion of serine and glycine with tetrahydrofolate (THF) serving as the one-carbon carrier. This reaction serves as the major source of one-carbon groups required for the biosynthesis of purines, thymidylate, methionine, and other important biomolecules. Also exhibits THF-independent aldolase activity toward beta-hydroxyamino acids, producing glycine and aldehydes, via a retro-aldol mechanism. Thus, is able to catalyze the cleavage of L-allo-threonine.
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00051, ECO:0000305|PubMed:12913008}.
Interaction partners:
- Probable glycine dehydrogenase
- Aminomethyltransferase
- Bifunctional purine biosynthesis protein PurH
- Bifunctional protein FolD
- Phosphoribosylglycinamide formyltransferase
- L-serine dehydratase
- Glycine cleavage system H protein
- Phosphoserine phosphatase SerB2
- L-threonine dehydratase biosynthetic IlvA
- Formyltetrahydrofolate deformylase
Sequence:
MTAAPDARTTAVMSAPLAEVDPDIAELLAKELGRQRDTLEMIASENFVPRAVLQAQGSVLTNKYAEGLPGRRYYGGCEHVDVVENLARDRAKALFGAEFANVQPHSGAQANAAVLHALMSPGERLLGLDLANGGHLTHGMRLNFSGKLYENGFYGVDPATHLIDMDAVRATALEFRPKVIIAGWSAYPRVLDFAAFRSIADEVGAKLLVDMAHFAGLVAAGLHPSPVPHADVVSTTVHKTLGGGRSGLIVGKQQYAKAINSAVFPGQQGGPLMHVIAGKAVALKIAATPEFADRQRRTLSGARIIADRLMAPDVAKAGVSVVSGGTDVHLVLVDLRDSPLDGQAAEDLLHEVGITVNRNAVPNDPRPPMVTSGLRIGTPALATRGFGDTEFTEVADIIATALATGSSVDVSALKDRATRLARAFPLYDGLEEWSLVGR
Protein: Uncharacterized protein (Q9VIV8)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Chorion protein S19
- IP19005p
- Chorion protein S36
- Femcoat
- Chorion protein S16
- RE05851p
- Chorion protein c at 7F
- IP19013p
- Uncharacterized protein
- GEO10373p1
Sequence:
MKVLITFFFLGACLCGIQADESIADLLKDNAKGVQAANVLLTRIAQVSEQTQVGLAEQKEALKALTLVEKLLAKLTVVLEVGSHNLVATLENLSRQGEEYGNRTESELLELVRLQEGTKEILNVLEAKLDAYQRHVLHSSRNIDNSIDGLAKLITRTVLPQLNGLKCTFDSLETSQINVEVELKNLAGVKELSENSNFKLNVLEHQLKQLNRTQEQRLDILIDAVKHLQPHSSWKVEAVLRELIISQKRIELGLEECSRQQPYPQYGHHDESYLPTYGAEVPEPQHAHPKPKQVDLEQVWSIKEEPKHGEHSGNHKATAYAQSPEPKKNYQSSSAVSWRQTVPWEYGSPYQSAPVHHHQPWNPAPAHVPTSVTKPKPCPKKEHPTPASYVPLPHDQPESYKLPVDYSPKPNHEQPHKPHHEPQSYNEEIYKPQPIQPGESFRIWYGDSSLPQGY
Protein: Oxidized low density lipoprotein receptor 1 (F5GZH1)
Organism: Homo sapiens (Human)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004401}; Single-pass type II membrane protein {ECO:0000256|ARBA:ARBA00004401}.
Interaction partners:
Sequence:
MTFDDLKIQTVKDQPDEKSNGKKAKGLQFLYSPWWCLAAATLGVLCLGLVVTIMVLGMQLSQVSDLLTQEQANLTHQKKKLEGQISARQQAEEASQESENELKEMIETLARKLNEKSKEQMELHHQNLNLQETLKRVANCSAVYAENCILAAFSICQKKANLRAQ
Protein: PRRG2 protein (Q8TAS3)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MSLGPEVFLGPPEAQSFLSSHTRIPRANHWDLELLTPGNLERECLEERCSWEEAREYFEDNTLTERFWESYIYNGKGGRGRVDVASLAVGLTCGILLIVLAGLGAFWYLRWRQHRGQQPCPQEAGLISPLSPLNPLGPPTPLPPPPPPPPGLPTYEQALAASGVHDAPPPPYTSLRRPH
Protein: ubiquitinyl hydrolase 1 (EC 3.4.19.12) (Q57X20)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- Polyubiquitin, putative
Sequence:
MLDLDSWVDEFHAGNEQKAVNQDTCNAAAGSSPSPLSVDVITLAYRLRTPCCVRHTLPSDCPVGCVASPWCLAGLSTLSTNNTTLQDFVADLLGDDTSLASSHQPQLQRGEHGPNDGDSPADTSSVDVYKYPIRRGIRDLGNTCYLNAVLQMLFHIPAVRDEVLRASASFPVAAHNSAKKITPLLASGLGELFAEMAYSRDERGVDAERFATFLSIDKGIQQDAQEFFVLLINWLQREVGDAVRHVFEGTILHDRECSKCGRSCKRAEPFSFLSLPVRQSIEESLEELLRVHEVQGFKCEECGAVTSAFSRLHIRTLPDVLVVHFNRFSFSLQEKRREKITRSVSFPIEWDLTPYKDRWRQVQKQTASNNSGVADSVVEARSNAAQLYRLVGVVNHHGEAAVCGHYTYHGKMDGHGGWYQFDNAVVTRLQRFHGTRASSKEAYMLVYERHAHPTNNPLTSAEEDVERAGSLDTTIILPPHLQNHIERLNHEVEKVRQARQLQRSVVMNFLKQWKDVADDIFYRSARRKGHPIAVMEECEDLTQYVAFPTRWMKLFGRCFIPSYIDTNRYCSFERGMKRHRRNSSKSAVELSNELPAAGSDSKEVEDNAPLVAAEMVLDTTKGAMPGDCVLIKSIYKSTLTDYLEDVRCPHGKLAPWGQYKLLSGASARRLNSFLNSVPSLLTSLTTVGEFTPFKGWKLSEYICEECVKRMSKEVQRIKTSWNEDMEIQTAVTPTSKFAEREDADELVYVSVEAVEHWEQMLKVTEKYRYIVKQQGFTGLVVAMKARSEDVDTEVIPLPSPSKLLCEHQLLSSVAAVREVPASVWHLLKKRILQLFYGDSVSVKHTLTPSVKAHMEMLLPYLPVSRTGKCLECIQNKMRMMMERHSAKMEKLNEGKRFSTLVEASRVMALPSVEVRIRHPNTLVWKRDIKRSYRRCYRTWEREQEDKITAVEARIKSLKEVGGQREKKQRTLPTPPVRCDRKQSQEPSDSQQVCEVTCENSQSIPDVMEVPSPLQSACDELAALRAATPPDVSAVYGCIPTWWVARWYKWYTNDADTGVGPPPCVDYSAFFCQHGGTVLPPSSLNPTDAHWSKTFTLGPIIRAWKSWLKDPSALDVVEESGSVHFPPIVLVPLKEMIAVLERYGGEGQLLPEVTDSKDLVTRLNNGRVVLFVERRGERMLDPPTCEICSTAVLDGVTELSRGFIDGSLRLRLHLRRSKRQHYDANDVLSGVSYNMTVGKLKVEISQRVLEYHGYILPVNDMKLLLGRKPLGPNRICKENTCANSDGNAPDGAASPSVASDDRNEESTTGALSTVDVDTCTLFECGLRDGDEVTVDASNTPLEKVLVNDSLCIRVPGAPTSSSETPTAEDVAAFGATRLYGVLDNVQNGRERKAPGQKACAVCTYLNVREAERCEMCEAAL
Protein: EamA domain-containing protein (Q381N1)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MSKQSRKEGTVGGRQYLLYSLLAGTFGALSAVVGKLAFAHDNSGSATSLSGVVSFFFALVGIDARSNSLAAALVLGLRAVSLAANGYCTAQMWRWYVRALSCGPTPVCQVVNTGANFGVSAILGFFVFHEVVTITWLAGALLVVVGLMLVVSDTDVSHE
Protein: Floral homeotic protein APETALA 2 (P47927)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Probable transcriptional activator that promotes early floral meristem identity. Is required subsequently for the transition of an inflorescence meristem into a floral meristem. Plays a central role in the specification of floral identity, particularly for the normal development of sepals and petals in the wild-type flower, by spatially controlling the expression domains of multiple floral organ identity genes. Acts as A class cadastral protein by repressing the C class floral homeotic gene AGAMOUS in association with other repressors like LEUNIG and SEUSS. Directly represses AGAMOUS by recruiting the transcriptional corepressor TOPLESS and the histone deacetylase HDA19. It is also required during seed development.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00366}.
Interaction partners:
- Basic leucine zipper 8
- Histone deacetylase 19
- Floral homeotic protein APETALA 3
- B3 domain-containing transcription factor ABI3
- Auxin transporter protein 1
- Protein LEAFY
- Ethylene-responsive transcription factor 2
- Protein TOPLESS
- Dehydration-responsive element-binding protein 1B
- MADS-box protein SOC1
Sequence:
MWDLNDAPHQTQREEESEEFCYSSPSKRVGSFSNSSSSAVVIEDGSDDDELNRVRPNNPLVTHQFFPEMDSNGGGVASGFPRAHWFGVKFCQSDLATGSSAGKATNVAAAVVEPAQPLKKSRRGPRSRSSQYRGVTFYRRTGRWESHIWDCGKQVYLGGFDTAHAAARAYDRAAIKFRGVEADINFNIDDYDDDLKQMTNLTKEEFVHVLRRQSTGFPRGSSKYRGVTLHKCGRWEARMGQFLGKKYVYLGLFDTEVEAARAYDKAAIKCNGKDAVTNFDPSIYDEELNAESSGNPTTPQDHNLDLSLGNSANSKHKSQDMRLRMNQQQQDSLHSNEVLGLGQTGMLNHTPNSNHQFPGSSNIGSGGGFSLFPAAENHRFDGRASTNQVLTNAAASSGFSPHHHNQIFNSTSTPHQNWLQTNGFQPPLMRPS
Protein: Polyketide synthase-like Pks10 (EC 2.3.1.-) (Chalcone synthase-like protein) (CHS-like) (Polyketide synthase type III Pks10) (P9WPF5)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: Could catalyze the elongation of hydroxybenzoyl-CoA as well as elongation of the aliphatic precursor involved in the synthesis of phthiocerol dimycocerosate (DIM).
Interaction partners:
- Conserved hypothetical membrane protein
- Probable polyketide synthase Pks17
- Possible oxidoreductase
- Phenolphthiocerol/phthiocerol polyketide synthase subunit C
- Phenolphthiocerol/phthiocerol polyketide synthase subunit B
- Mycolipanoate synthase
- Probable polyketide synthase Pks7
- Phenolphthiocerol/phthiocerol polyketide synthase subunit A
- Methyl-branched alkylpyrone synthesis polyketide synthase-like Pks11
- DNA-directed RNA polymerase subunit beta
Sequence:
MSVIAGVFGALPPYRYSQRELTDSFVSIPDFEGYEDIVRQLHASAKVNSRHLVLPLEKYPKLTDFGEANKIFIEKAVDLGVQALAGALDESGLRPEDLDVLITATVTGLAVPSLDARIAGRLGLRADVRRVPLFGLGCVAGAAGVARLHDYLRGAPDGVAALVSVELCSLTYPGYKPTLPGLVGSALFADGAAAVVAAGVKRAQDIGADGPDILDSRSHLYPDSLRTMGYDVGSAGFELVLSRDLAAVVEQYLGNDVTTFLASHGLSTTDVGAWVTHPGGPKIINAITETLDLSPQALELTWRSLGEIGNLSSASVLHVLRDTIAKPPPSGSPGLMIAMGPGFCSELVLLRWH
Protein: Inhibitor of g-type lysozyme (P76002)
Organism: Escherichia coli (strain K12)
Function: Inhibits activity of g-type lysozyme, which confers increased lysozyme tolerance to the bacterium.
Subcellular location: Periplasm {ECO:0000269|PubMed:20734102}.
Interaction partners:
- Metal-binding protein ZinT
- Membrane-bound lysozyme inhibitor of C-type lysozyme
- Uncharacterized protein YcgJ
Sequence:
MKIKSIRKAVLLLALLTSTSFAAGKNVNVEFRKGHSSAQYSGEIKGYDYDTYTFYAKKGQKVHVSISNEGADTYLFGPGIDDSVDLSRYSPELDSHGQYSLPASGKYELRVLQTRNDARKNKTKKYNVDIQIK
Protein: RNA helicase (EC 3.6.4.13) (Q57Z07)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- CCHC-type domain-containing protein
- Nucleolar GTP-binding protein 1
- Pescadillo homolog
- RNA-binding protein
Sequence:
MSSRAEEGTHRHEGHVTKTKRSREEMTGNEETDQEPNNGSAAVGRPFSEFNLSSGMVKALEAQGIVSLFPVQALTFEAIMRGEDVLVQARTGSGKTLAFGIPIVEKLNKKEGPLARGRGPAAVIFCPTRELAIQVRDVLAGVSGDLVVAALYGGVAYSTQERVLFSGVDIVVATPGRAKDFLEKGTLHFERVKMVCLDEADHMLDIGFKEDIELLLQRVAEQNGSTPDEPKHQTLLFSATVPDWVHTCSFISKNKKFIDMVGQGAMRAANTIRFYRRKCGFAEVSSMLADLVKVYSGRHGRTLIFTNTKKDCHDLSINNTKLDSQCLHGDMQQEQRESTMKSFRDNKFSVLIATDVAARGLDLPMVDLVIQCAPPTDIDAFIHRAGRTGRAGRKGVCVLLHQPKDEYVVERIERHAKIKFEVLPAPTREEILKAVARDAAEDMARVERSATNLFMDQAAELLKDADPTEILASAIAVMSGYTSSITKRGLISGARGSATVQMLGQRSLPTHVFCSILRNNLGDELFMRCRDITLLQDAPGCVFDVPEDVVDRILNTPVQGMELSVIETLPPIIARELNSGSRGNRGGGGGGGGYRGGPRGGGYNQYNRNGGGGGGGGGRSWGSGYRSTQRRY
Protein: Tyrosine-protein kinase (EC 2.7.10.2) (S5RRC4)
Organism: Salmo salar (Atlantic salmon)
Interaction partners:
- Signal transducer and activator of transcription
- Signal transducer and activator of transcription
- Signal transducer and activator of transcription
- Signal transducer and activator of transcription
- Signal transducer and activator of transcription
- Signal transducer and activator of transcription
- Tyrosine-protein kinase
- Tyrosine-protein kinase
- Tyrosine-protein kinase
- Signal transducer and activator of transcription
Sequence:
MMSRSGRFKSTRTGSSTGQCEPPQGPGVHVYLFWTKGGERYLTHTEGKVTAEELSISAAQTVGITPLCHVLFSLYDPESHCWYSPNHFFNSEEQTRLTLHYRMRFYFRNWHGLSEKEPSVVRYAPRSGTEHGGSPLLEMTSLEYLFCQAKFDFVNDVTPMEDAQGKEELSRFKNESLGMAVLHLSHQALRSGCTLQEVAKSVSFLRCIPRSFAKHIARDNFLTKIRIRRVFADFVRTFQEHTVDVGRLGSQEVMYKYLSTLEHLAPRFGTETFLAAHLELRTDGGDGSGSYLNTSRAHGASDPENVGPQVMHEVMVSGTKGIQWRKMTVQKPQANSYFGNDYLGNRKSVKQSPLQQEPTSSDTWTSFCDFPEISHITITGANVSIIKQDNFSMEVQMNSSLEALSFVSLLDGYFRLTADAHHYLCHEVAPPRVVLSATNGLHGPMNDDFVLQRLRKEAVEEGAFLVRWSVLDYHRIILAVLNKSQNGQAAIHKQFRILHSGSVFALEGWDREFSSVKELTDSLKAFVLKSGTDNFTVKKCCLPRPAELSNLLVMRQGVDQCVQPDSVALCLTQLKFHQIKDKEITQEQHLGRGTRTNIYSGRLLVWGGAEEDEEDKWNNNLTDRKEIRVVLKILDQSHKDIALAFFETASLMSQVSHSHLVFVHGVSVKGSENIMVEEFVEFGPLDVFLRRERALVTPQWKFTVAKQLASALSYLETKQLVHGNVCGKNILVARRGLEEGTFPFVKLSDPGIALNVLSREERVERIPWIAPECVPSSAPFGRAADQWSFGATLLEICNNGDLPMSGSTLTEKERFYETRSRLTEPSSQELASFISMCLTYEPRERPSFRTVLRELTELQLKNPDISPLESLPDADPNVFLKRYLKKIRDLGEGHFGKVMLYVYDPANDGTGDYVAVKALKHEGGSHLHEGWMKEIEILKSLYHSNIVKYKGCCSELGGQTVQLIMEFLPLGSLREYLVKHRLGVAHSLLFAQQICQGMDYLHSKRYIHRDLAARNVLVENEHLVKIGDFGLTKYIPEGDVYYRVREDGDSPVYWYAIECLKESKFSFSSDIWSFGVTLYEVLTHGDHRQSPPVKFTQMMGNVHGQMTVMVLVKLLEKHNRLPCPRDCPSEVHMLMQHCWDFDPARRPSFKSLIESIGAIRKTYERQPNMRLAQISQ
Protein: Nucleolar transcription factor 1 (Autoantigen NOR-90) (Upstream-binding factor 1) (UBF-1) (P17480)
Organism: Homo sapiens (Human)
Function: Recognizes the ribosomal RNA gene promoter and activates transcription mediated by RNA polymerase I through cooperative interactions with the transcription factor SL1/TIF-IB complex. It binds specifically to the upstream control element.
Subcellular location: Nucleus, nucleolus {ECO:0000250|UniProtKB:P25976}.
Interaction partners:
- RNA polymerase I-specific transcription initiation factor RRN3
- NAD-dependent protein deacetylase sirtuin-7
- DNA-directed RNA polymerase I subunit RPA49
- TATA box-binding protein-associated factor RNA polymerase I subunit A
- DNA polymerase iota
- DNA-directed RNA polymerase I subunit RPA1
- Chromodomain-helicase-DNA-binding protein 4
- TATA-box-binding protein
- DNA-directed RNA polymerase I subunit RPA34
- rRNA 2'-O-methyltransferase fibrillarin
Sequence:
MNGEADCPTDLEMAAPKGQDRWSQEDMLTLLECMKNNLPSNDSSKFKTTESHMDWEKVAFKDFSGDMCKLKWVEISNEVRKFRTLTELILDAQEHVKNPYKGKKLKKHPDFPKKPLTPYFRFFMEKRAKYAKLHPEMSNLDLTKILSKKYKELPEKKKMKYIQDFQREKQEFERNLARFREDHPDLIQNAKKSDIPEKPKTPQQLWYTHEKKVYLKVRPDATTKEVKDSLGKQWSQLSDKKRLKWIHKALEQRKEYEEIMRDYIQKHPELNISEEGITKSTLTKAERQLKDKFDGRPTKPPPNSYSLYCAELMANMKDVPSTERMVLCSQQWKLLSQKEKDAYHKKCDQKKKDYEVELLRFLESLPEEEQQRVLGEEKMLNINKKQATSPASKKPAQEGGKGGSEKPKRPVSAMFIFSEEKRRQLQEERPELSESELTRLLARMWNDLSEKKKAKYKAREAALKAQSERKPGGEREERGKLPESPKRAEEIWQQSVIGDYLARFKNDRVKALKAMEMTWNNMEKKEKLMWIKKAAEDQKRYERELSEMRAPPAATNSSKKMKFQGEPKKPPMNGYQKFSQELLSNGELNHLPLKERMVEIGSRWQRISQSQKEHYKKLAEEQQKQYKVHLDLWVKSLSPQDRAAYKEYISNKRKSMTKLRGPNPKSSRTTLQSKSESEEDDEEDEDDEDEDEEEEDDENGDSSEDGGDSSESSSEDESEDGDENEEDDEDEDDDEDDDEDEDNESEGSSSSSSSSGDSSDSDSN
Protein: Catabolite control protein A (A8AWB2)
Organism: Streptococcus gordonii (strain Challis / ATCC 35105 / BCRC 15272 / CH1 / DL1 / V288)
Interaction partners:
- Phosphocarrier protein HPr
Sequence:
MNTDDTVTIYDVAREAGVSMATVSRVVNGNKNVKENTRKKVLEVIDRLDYRPNAVARGLASKKTTTVGVVIPSITNSYFSTLAKGIDDIAEMYKYNIVLANSDEDDDKEVSVVNTLFSKQVDGIIFMGYHLTEKIRSEFSRSRTPVVLAGTIDVEHQLPSVNIDYKQATIDAITFLAKRNKKIAFVCGPLVDDINGKVRLSGYKTALKSKKLSYSEGLVFESKYGYDDGYNLAERVIASKATAAFVTGDELAAGLLNGLADCGVKIPEDFEIITSDDSQISRYTRPNLSTISQPLYDLGAISMRMLTKIMHKEELEEREVVLSHGIYERNSTRK
Protein: Embryonic polarity protein dorsal (P15330)
Organism: Drosophila melanogaster (Fruit fly)
Function: Embryonic developmental protein. The lateral or ventral identity of a cell depends upon the concentration of this protein in its nucleus during the blastoderm stage. A morphogenetic protein that specifically binds to the kappa B-related consensus sequence 5'-GRGAAAANCC-3', located in the enhancer region of zygotic genes such as Zen, Twist, Snail and Decapentaplegic. Mediates an immune response in larvae. Part of a signaling pathway involving NF-kappa-B and Toll-related receptors, that functions in the apoptosis of unfit cells during cell competition. May be part of a NF-kappa-B and Tollo signaling cascade that regulates development of the peripheral nervous system.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:14638854, ECO:0000269|PubMed:17032737, ECO:0000269|PubMed:2598266}. Nucleus {ECO:0000269|PubMed:14638854, ECO:0000269|PubMed:17032737, ECO:0000269|PubMed:2598266}. Note=In ventral regions it is first cytoplasmic, then the protein is relocalized in the nucleus (PubMed:2598266). Its nuclear localization is essential to its function as a morphogen (PubMed:2598266). In dorsal regions it remains cytoplasmic (PubMed:2598266). Tamo negatively regulates nuclear import of dl (PubMed:12653959). Emb is responsible for export of dl from the nucleus (PubMed:14638854). Nuclear localization is enhanced upon microbial infection (PubMed:17032737). {ECO:0000269|PubMed:12653959, ECO:0000269|PubMed:14638854, ECO:0000269|PubMed:17032737, ECO:0000269|PubMed:2598266}.; SUBCELLULAR LOCATION: [Isoform A]: Nucleus {ECO:0000305}.
Interaction partners:
- NF-kappa-B inhibitor cactus
- Dorsal-related immunity factor Dif
- Nuclear factor NF-kappa-B p110 subunit
- Daisho1
- Cecropin-B
- Drosomycin-like 3
- Dro6 protein
- Dro1 protein
- Cecropin-C
- Dro2 protein
Sequence:
MFPNQNNGAAPGQGPAVDGQQSLNYNGLPAQQQQQLAQSTKNVRKKPYVKITEQPAGKALRFRYECEGRSAGSIPGVNSTPENKTYPTIEIVGYKGRAVVVVSCVTKDTPYRPHPHNLVGKEGCKKGVCTLEINSETMRAVFSNLGIQCVKKKDIEAALKAREEIRVDPFKTGFSHRFQPSSIDLNSVRLCFQVFMESEQKGRFTSPLPPVVSEPIFDKKAMSDLVICRLCSCSATVFGNTQIILLCEKVAKEDISVRFFEEKNGQSVWEAFGDFQHTDVHKQTAITFKTPRYHTLDITEPAKVFIQLRRPSDGVTSEALPFEYVPMDSGKHTFWNLHRHLKRKPDEDLFQQILRLDAKREVQPPTIEVIDLDTPKIDVQREIPSEMEFNHEESQQSEPALEQEQSVQQEQYTQEQSLQQEQYTQEQSLQQEQYLQQLEQQQSFQLEEPMQQDQELPAQQSFDQAIDHLPDHTSDHIPEDMEAADAHAEAEAHRLRSEQEKEIDTIIDEKVRELEQLDLGQQLEPRPLTANDKITEWMKSSEIEQQVHEPSPTAEADVLDSALEISKADKTLDELLETVAELDEIYTDFKVQRDTYKNTIQNELAGLQGRAPLQVEDSFDDAATYTSLQIAFKNPVLIPMDDIMPPTPPMSQCAPEDAHQHYDPVEVNSQARKPETPMRPVPPVPPAILTIQYPPEEDKLPPLPPKRIRKQDSNAENRSIEANTVQTKPSTGESPLNKRLPPAPKNPNFNTLPRQKKPGFFSKLFSRRKSKPDLAQGQENSSILDSKANSREPSIGHFNMQDPMRASLRSSKSAAPFISNPAPAKSSPVKAKKPGSKLTKPVGRSVSSVSGKRPAYLNADVVHIPLKGDSVNSLPQQQRTEGYSQSSTISVGAGLDRRTASALQLADIPISEGGMELVAIADRQSLHNLVSSIEGHFNVQLDPNLDLTEAEHFALYTSIPPLAAASEFDETSAYYAPVDAGEILTPDEVAKRLAAANGI
Protein: AP-3 complex subunit delta (Delta adaptin subunit of AP-3) (Delta-adaptin) (Garnet protein) (P54362)
Organism: Drosophila melanogaster (Fruit fly)
Function: Part of the AP-3 complex, an adapter-related complex which is not clathrin-associated. The complex is associated with the Golgi region as well as more peripheral structures. It facilitates the budding of vesicles from the Golgi membrane and may be directly involved in trafficking to lysosomes (By similarity).
Subcellular location: Cytoplasmic vesicle, clathrin-coated vesicle membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Golgi apparatus {ECO:0000250}. Note=Component of the coat surrounding the cytoplasmic face of coated vesicles located at the Golgi complex. {ECO:0000250}.
Interaction partners:
- Carmine, isoform A
- Adaptor protein complex AP-3 small chain sigma3
- AP-3 complex subunit beta
- AP complex subunit beta
- Adaptor protein complex 2, mu subunit, isoform A
- AP complex subunit sigma
- Adaptor protein complex 1, mu subunit
- AP complex subunit sigma
- AP-2 complex subunit alpha
- Vacuolar protein sorting-associated protein 41 homolog
Sequence:
MALKKVKGNFFERMFDKNLTDLVRGIRNNKDNEAKYISTCIEEIKQELRQDNISVKCNAVAKLTYIQMLGYDISWAGFNIIEVMSSSRFTCKRIGYLAASQCFHPDSELLMLTTNMIRKDLNSQNQYDAGVALSGLSCFISPDLSRDLANDIMTLMSSTKPYLRMKAVLMMYKVFLRYPEALRPAFPKLKEKLEDPDPGVQSAAVNVICELARKNPKNYLPLAPIFFKLMTTSTNNWMLIKIIKLFGALTPLEPRLGKKLIEPLTNLIHSTSAMSLLYECINTVIAVLISISSGMPNHSASIQLCVQKLRILIEDSDQNLKYLGLLAMSKILKTHPKSVQAHKDLILACLDDKDESIRLRALDLLYGMVSKKNLMEIVKRLLGHMERAEGSAYRDELLYKVIEICAQSSYLYVTNFEWYLTVLVELIQLEAGSRHGRLIAEQLLDVAIRVPVVRQFAVNEMTNLLDTFTVSAQSNSMYEVLYAAAWIVGEFAGELEDAEKTLNILLRPRLLPGHIQGVYVQNVIKLFARLATTCLELQDLPGLVTLCDHVLDKLQHFNGSSDIEVQERANSACMLIEMLRNQLSTSTDAMAMDTTTEGGIPPLAIEIVQEMTLLFTGELIPVAPKAQRKVPLPDGLDLDEWINAPPPEDAASSSSSEHDKDELFVSATQAGTGADGGEKRRQSLELTPEQLERQRMARLIEQSNNPHYLKSTPTASGASNADQYDNIDDIPITELPLDMEGVAALRVGITKRSDKYLQEQQAAQGSKDGKKKHKKGKKSKKAKNKVAYNSSSESEGEPKPLHIVNTTLDMPEGVSMSDSEDKDGKYDPNDPHRALDIELDITEFEAPAVRSASKKSAADKENLKTPADLAGGGNAAKKDRKKDKDKDKERKVKREHRESKRERKEAAVQPVIDLIDADTPTPSPSHISATSNNNNTSTVLPDAPKHHKKKKNKEKTTDEAPDALATATGSSIIDVGGEEASEVASKVHKKKHKKEKSQRKEKKKASESASVSAIVSIGDYEQPLGISTPSKEIL
Protein: Dipeptidyl peptidase 8 (DP8) (EC 3.4.14.5) (Dipeptidyl peptidase IV-related protein 1) (DPRP-1) (Dipeptidyl peptidase VIII) (DPP VIII) (Prolyl dipeptidase DPP8) (Q6V1X1)
Organism: Homo sapiens (Human)
Function: Dipeptidyl peptidase that cleaves off N-terminal dipeptides from proteins having a Pro or Ala residue at position 2. Acts as a key inhibitor of caspase-1-dependent monocyte and macrophage pyroptosis in resting cells by preventing activation of NLRP1 and CARD8. Sequesters the cleaved C-terminal part of NLRP1 and CARD8, which respectively constitute the active part of the NLRP1 and CARD8 inflammasomes, in a ternary complex, thereby preventing their oligomerization and activation. The dipeptidyl peptidase activity is required to suppress NLRP1 and CARD8; however, neither NLRP1 nor CARD8 are bona fide substrates of DPP8, suggesting the existence of substrate(s) required for NLRP1 and CARD8 inhibition (By similarity).
Subcellular location: Cytoplasm {ECO:0000269|PubMed:11012666, ECO:0000269|PubMed:12534281, ECO:0000269|PubMed:12662155}.
Interaction partners:
- Prolyl endopeptidase
- Small ubiquitin-related modifier 1
- Dipeptidyl peptidase 2
- Transcription factor Dp family member 3
- Activator of apoptosis harakiri
Sequence:
MWKRSEQMKIKSGKCNMAAAMETEQLGVEIFETADCEENIESQDRPKLEPFYVERYSWSQLKKLLADTRKYHGYMMAKAPHDFMFVKRNDPDGPHSDRIYYLAMSGENRENTLFYSEIPKTINRAAVLMLSWKPLLDLFQATLDYGMYSREEELLRERKRIGTVGIASYDYHQGSGTFLFQAGSGIYHVKDGGPQGFTQQPLRPNLVETSCPNIRMDPKLCPADPDWIAFIHSNDIWISNIVTREERRLTYVHNELANMEEDARSAGVATFVLQEEFDRYSGYWWCPKAETTPSGGKILRILYEENDESEVEIIHVTSPMLETRRADSFRYPKTGTANPKVTFKMSEIMIDAEGRIIDVIDKELIQPFEILFEGVEYIARAGWTPEGKYAWSILLDRSQTRLQIVLISPELFIPVEDDVMERQRLIESVPDSVTPLIIYEETTDIWINIHDIFHVFPQSHEEEIEFIFASECKTGFRHLYKITSILKESKYKRSSGGLPAPSDFKCPIKEEIAITSGEWEVLGRHGSNIQVDEVRRLVYFEGTKDSPLEHHLYVVSYVNPGEVTRLTDRGYSHSCCISQHCDFFISKYSNQKNPHCVSLYKLSSPEDDPTCKTKEFWATILDSAGPLPDYTPPEIFSFESTTGFTLYGMLYKPHDLQPGKKYPTVLFIYGGPQVQLVNNRFKGVKYFRLNTLASLGYVVVVIDNRGSCHRGLKFEGAFKYKMGQIEIDDQVEGLQYLASRYDFIDLDRVGIHGWSYGGYLSLMALMQRSDIFRVAIAGAPVTLWIFYDTGYTERYMGHPDQNEQGYYLGSVAMQAEKFPSEPNRLLLLHGFLDENVHFAHTSILLSFLVRAGKPYDLQIYPQERHSIRVPESGEHYELHLLHYLQENLGSRIAALKVI
Protein: Eukaryotic translation initiation factor 1A (eIF-1A) (Eukaryotic translation initiation factor 4C) (eIF-4C) (P38912)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Seems to be required for maximal rate of protein biosynthesis. Enhances ribosome dissociation into subunits and stabilizes the binding of the initiator Met-tRNA(I) to 40 S ribosomal subunits.
Interaction partners:
- Eukaryotic translation initiation factor 2 subunit gamma
- Eukaryotic translation initiation factor 5
- Eukaryotic translation initiation factor 3 subunit A
- Eukaryotic translation initiation factor 3 subunit C
- Small ribosomal subunit protein uS5
- Small ribosomal subunit protein uS3
- Eukaryotic translation initiation factor 5B
- Eukaryotic translation initiation factor 2 subunit beta
- Small ribosomal subunit protein uS10
- Eukaryotic translation initiation factor eIF-1
Sequence:
MGKKNTKGGKKGRRGKNDSDGPKRELIYKEEGQEYAQITKMLGNGRVEASCFDGNKRMAHIRGKLRKKVWMGQGDIILVSLRDFQDDQCDVVHKYNLDEARTLKNQGELPENAKINETDNFGFESDEDVNFEFGNADEDDEEGEDEELDIDDI