wanglab/gogpt-training-data huggingface dataset:
Protein: CgeB family protein (Q72C19)
Organism: Nitratidesulfovibrio vulgaris (strain ATCC 29579 / DSM 644 / CCUG 34227 / NCIMB 8303 / VKM B-1760 / Hildenborough) (Desulfovibrio vulgaris)
Interaction partners:
- Heptosyltransferase family protein
- Heptosyltransferase family protein
- Uncharacterized protein
- TPR domain protein
- Heptosyltransferase family protein
- TPR domain protein
- Flagellar hook-associated protein FlgL, putative
- Glycosyl transferase, group 1 family protein
Sequence:
MVSQAILAKVETFEPDLVLCLAQAPMSRQALRRLRRDGVATAMWFVEDFRVFTYWRAFAPFYDFFAVIQREPLLDELAAIGVENAIYLPLAALPAFHRPMELSPVERHRYGADVAFLGAGYPNRRVAFRRLTHLDFRIWGTEWDGDAVLARHVQMNGGRVSPEDAVKIYNATRINLNLHSSVQAQTLVTGGDFVNPRTFELAAIGAFQLVDRRGLMDELFTDDELATFGDMDELVALIERFLADPDERAAFAARGQARVLRDHTYQQRMTTLLDFIAARRPGWPPRRQDAGFPADMPEGLRAELGGLLQRLGLPHDAAFGDVIARLRQQTGELDALETSLLFLDEWRKQYAAKG
Protein: Cyclic nucleotide-gated channel alpha-4 (CNG channel alpha-4) (CNGa4) (Olfactory cyclic nucleotide-gated channel subunit 2) (OCNC2) (Q64359)
Organism: Rattus norvegicus (Rat)
Function: Second messenger, cAMP, causes the opening of cation-selective cyclic nucleotide-gated (CNG) channels and depolarization of the neuron (olfactory sensory neurons, OSNs). CNGA4 is the modulatory subunit of this channel which is known to play a central role in the transduction of odorant signals and subsequent adaptation. By accelerating the calcium-mediated negative feedback in olfactory signaling it allows rapid adaptation to odor stimulation and extends its range of odor detection (By similarity).
Subcellular location: Cell projection, cilium membrane {ECO:0000305|PubMed:10377344}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Cyclic nucleotide-gated channel alpha-2
- Cyclic nucleotide-gated channel subunit beta 1.
- Calmodulin-1
- Calmodulin-like protein 4
- Calmodulin-like protein 3
- Cyclic nucleotide-gated channel alpha-1
- Cyclic nucleotide gated channel subunit beta 3
- PEX5-related protein
- Receptor
- Adenylate cyclase type 3
Sequence:
MSQDGKVKTTESTPPAPTKARKWLPVLDPSGDYYYWWLNTMVFPIMYNLIIVVCRACFPDLQHSYLVAWFVLDYTSDLLYLLDIGVRFHTGFLEQGILVVDKGMIASRYVRTWSFLLDLASLVPTDAAYVQLGPHIPTLRLNRFLRVPRLFEAFDRTETRTAYPNAFRIAKLMLYIFVVIHWNSCLYFALSRYLGFGRDAWVYPDPAQPGFERLRRQYLYSFYFSTLILTTVGDTPLPDREEEYLFMVGDFLLAVMGFATIMGSMSSVIYNMNTADAAFYPDHALVKKYMKLQHVNKRLERRVIDWYQHLQINKKMTNEVAILQHLPERLRAEVAVSVHLSTLSRVQIFQNCEASLLEELVLKLQPQTYSPGEYVCRKGDIGREMYIIREGQLAVVADDGVTQYAVLGAGLYFGEISIINIKGNMSGNRRTANIKSLGYSDLFCLSKEDLREVLSEYPQAQAVMEEKGREILLKMNKLDVNAEAAEIALQEATESRLKGLDQQLDDLQTKFARLLAELESSALKIAYRIERLEWQTREWPMPEDMGEADDEAEPGEGTSKDGEGKAGQAGPSGIE
Protein: Protein E6 (P06462)
Organism: Human papillomavirus type 6b
Function: Plays a major role in the induction and maintenance of cellular transformation. E6 associates with host UBE3A/E6-AP ubiquitin-protein ligase and modulates its activity. Sequesters tumor suppressor TP53 in the host cytoplasm and modulates its activity by interacting with host EP300 that results in the reduction of TP53 acetylation and activation. In turn, apoptosis induced by DNA damage is inhibited. E6 protects also host keratinocytes from apoptosis by mediating the degradation of host BAK1. May also inhibit host immune response.
Subcellular location: Host cytoplasm {ECO:0000255|HAMAP-Rule:MF_04006}. Host nucleus {ECO:0000255|HAMAP-Rule:MF_04006}.
Interaction partners:
Sequence:
MESANASTSATTIDQLCKTFNLSMHTLQINCVFCKNALTTAEIYSYAYKHLKVLFRGGYPYAACACCLEFHGKINQYRHFDYAGYATTVEEETKQDILDVLIRCYLCHKPLCEVEKVKHILTKARFIKLNCTWKGRCLHCWTTCMEDMLP
Protein: Alpha/beta-Hydrolases superfamily protein (F4K2Y3)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- Stromal processing peptidase, chloroplastic
- Prolyl endopeptidase
- Subtilisin-like protease SBT1.4
- Serine carboxypeptidase-like 26
- Insulin-degrading enzyme-like 1, peroxisomal
- Prolyl carboxypeptidase like protein
- Proteasome subunit alpha type-5-B
- Serine carboxypeptidase-like 34
- Probable cytosolic oligopeptidase A
- Serine carboxypeptidase-like 42
Sequence:
MALLLLTSLNHLVSFSLTRLPSSSAHNLFLSRSFSSSIRRFNRFSLKPLRSFASMSSSSPDAAQTPLTTAPYGSWKSPITADIVSGASKRLGGTAVDSHGRLVLLESRPNESGRGVLVLQGETSIDITPKDFAVRTLTQEYGGGAFQISSDDTLVFSNYKDQRLYKQDITDKDSSPKPITPDYGTPAVTYADGVFDSRFNRYVTVREDGRQDRSNPITTIVEVNLSGETLEEPKVLVSGNDFYAFPRLDPKCERLAWIEWSHPNMPWDKAELWVGYISEGGNIDKRVCVAGCDPKYVESPTEPKWSSRGELFFVTDRKNGCWNIHKWIESTNEVVSVYPLDGEFAKPLWIFGTNSYEIIECSEEKNLIACSYRQKGKSYLGIVDDSQGSCSLLDIPLTDFDSITLGNQCLYVEGASAVLPPSVARVTLDQHKTKALSSEIVWSSSPDVLKYKAYFSVPELIEFPTEVPGQNAYAYFYPPTNPLYNASMEEKPPLLVKSHGGPTAESRGSLNLNIQYWTSRGWAFVDVNYGGSTGYGREYRERLLRQWGIVDVDDCCGCAKYLVSSGKADVKRLCISGGSAGGYTTLASLAFRDVFKAGASLYGVADLKMLKEEGHKFESRYIDNLVGDEKDFYERSPINFVDKFSCPIILFQGLEDKVVTPDQSRKIYEALKKKGLPVALVEYEGEQHGFRKAENIKYTLEQQMVFFARVVGGFKVADDITPLKIDNFDT
Protein: cDNA FLJ36438 fis, clone THYMU2012113, highly similar to Artemis protein (B3KSJ7)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MDKVVEILKPLCRSSQSTEPKYKPLGKLKRARTVHRDSEEEDDYLFDDPLPIPLRHKVPYPETFHPEVFSMTAVSEKQPEKLRQTPGCCRAECMQSSRFTNFVDCEESNSESEEEVGIPASLQGDLGSVLHLQKADGDVPQWEVFFKRNDEITDESLENFPSSTVAGGSQSPKLFSDSDGESTHISSQNSSQSTHITEQGSQGWDSQSDTVLLSSQERNSGDITSLDKADYRPTIKENIPASLMEQNVICPKDTYSDLKSRDKDVTIVPSTGEPTTLSSETHIPEEKSLLNLSTNADSQSSSDFEVPSTPEAELPKREHLQYLYEKLATGESIAVKKRKCSLLDT
Protein: Biotin-dependent acetyl-/propionyl-coenzyme A carboxylase beta6 subunit (Acetyl-CoA carboxylase) (ACC) (EC 2.1.3.15) (Propionyl-CoA carboxylase) (PCC) (EC 2.1.3.-) (P9WQH5)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: Component of a biotin-dependent acyl-CoA carboxylase complex. This subunit transfers the CO2 from carboxybiotin to the CoA ester substrate. When associated with the alpha3 subunit AccA3, is involved in the carboxylation of acetyl-CoA and propionyl-CoA, with a preference for acetyl-CoA.
Interaction partners:
- Malonyl CoA-acyl carrier protein transacylase
- Biotin-dependent acyl-coenzyme A carboxylase alpha3 subunit
- 3-oxoacyl-[acyl-carrier-protein] synthase 1
- 3-oxoacyl-[acyl-carrier-protein] synthase 2
- Biotin-dependent 3-methylcrotonyl-coenzyme A carboxylase alpha1 subunit
- Biotin-dependent 3-methylcrotonyl-coenzyme A carboxylase alpha1 subunit
- Probable fatty acid synthase Fas
- Biotinylated protein TB7.3
- Conserved protein
- Meromycolate extension acyl carrier protein
Sequence:
MTIMAPEAVGESLDPRDPLLRLSNFFDDGSVELLHERDRSGVLAAAGTVNGVRTIAFCTDGTVMGGAMGVEGCTHIVNAYDTAIEDQSPIVGIWHSGGARLAEGVRALHAVGQVFEAMIRASGYIPQISVVVGFAAGGAAYGPALTDVVVMAPESRVFVTGPDVVRSVTGEDVDMASLGGPETHHKKSGVCHIVADDELDAYDRGRRLVGLFCQQGHFDRSKAEAGDTDIHALLPESSRRAYDVRPIVTAILDADTPFDEFQANWAPSMVVGLGRLSGRTVGVLANNPLRLGGCLNSESAEKAARFVRLCDAFGIPLVVVVDVPGYLPGVDQEWGGVVRRGAKLLHAFGECTVPRVTLVTRKTYGGAYIAMNSRSLNATKVFAWPDAEVAVMGAKAAVGILHKKKLAAAPEHEREALHDQLAAEHERIAGGVDSALDIGVVDEKIDPAHTRSKLTEALAQAPARRGRHKNIPL
Protein: Large ribosomal subunit protein eL19z (60S ribosomal protein L19-2) (Q9LUQ6)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- Large ribosomal subunit protein uL24y
- Large ribosomal subunit protein eL42z/eL42y
- Large ribosomal subunit protein uL22z
- Large ribosomal subunit protein uL18y
- Large ribosomal subunit protein eL29y
- Large ribosomal subunit protein eL8y
- At1g43860
- Small ribosomal subunit protein uS14z/uS14y/uS14x
- Large ribosomal subunit protein uL6x
- Large ribosomal subunit protein uL4z
Sequence:
MVSLKIQKRLAASVMKCGKGKVWLDPNESGDISMANSRQNIRKLVKDGFIIRKPTKIHSRSRARALNEAKRKGRHSGYGKRKGTREARLPTKILWMRRMRVLRRFLSKYRESKKIDRHMYHDMYMKVKGNVFKNKRVLMESIHKMKAEKAREKTLADQFEAKRIKNKASRERKFARREERLAQGPGGGETTTPAGAPQQPEVTKKKSKK
Protein: U4/U6.U5 tri-snRNP-associated protein snu66 (O94538)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Required for efficient splicing of pre-mRNA.
Subcellular location: Nucleus {ECO:0000269|PubMed:15620657, ECO:0000269|PubMed:16823372}.
Interaction partners:
- Uncharacterized protein C1782.03
- Pre-mRNA-splicing factor prp1
- Pre-mRNA-splicing factor cwf10
- 13 kDa ribonucleoprotein-associated protein
- U4/U6.U5 small nuclear ribonucleoprotein component snu23
- Pre-mRNA-splicing factor brr2
- Pre-mRNA-processing factor 31
- U4/U5/U6 small nuclear ribonucleoprotein prp3
- Uncharacterized WD repeat-containing protein C227.12
- Pre-mRNA-splicing factor spp42
Sequence:
MSGNSGASESISIEETNRIRISLGLKPLDISEEKPQKELSDASVKSSYVDQEQQAYENWKKQEQEEINRKKEEELKSKFEKLRQKNERRRRTQGKTLAETLAEEDDQIDANDTRAWILKMRNSSLNKNGNGLNFEAKNDAPRRSTLHSQNAGPNVNSSLEGMKIAHGFQDLNKNDGLVLTLKDADILDEDNHDLLENVEMVQRKTKNERKEDNPYKPYEDENDFLQQSEADQPSEDTFTTIGPQNSLTVNSTIEKHKSDNKKTFGTLVSFVEPTITGSEQSDYRQIKIKKSKKKKSKSDRRKRLVELDAENENENDPSDFVLPNGQSNSDLSVEQDSAIFKEQKKMKIQKRMRELETQSFADDDDLQQSIAMQRRLAQKRAKILKPEDVAEQLQNAEEVTDMTDSDTASGLIFDDTRAFVNSIKETENREALGSINEQAFEDSKDLNDTNSITGSSPTEESNALVEDTSVDISATLEEANTQQENAEDEPLVSDNVGAVLSLLRNKGVIKVSDEAKEKIQKEEEYNKWFARKQQARVELEEQRRKKKEQDRLSGKFEKMTQKEREQYAKKENERWDKKIAEIELEQFHDYKPQVDIKYVDEFGVELGPKEAYKYLLSHQFHGKGSGKAKTEKRLRRIVEKEREERKPIF
Protein: Laminin subunit alpha-4 (Laminin-14 subunit alpha) (Laminin-8 subunit alpha) (Laminin-9 subunit alpha) (P97927)
Organism: Mus musculus (Mouse)
Function: Binding to cells via a high affinity receptor, laminin is thought to mediate the attachment, migration and organization of cells into tissues during embryonic development by interacting with other extracellular matrix components.
Subcellular location: Secreted, extracellular space, extracellular matrix, basement membrane. Secreted {ECO:0000250|UniProtKB:Q16363}. Note=Major basement membrane component.
Interaction partners:
- Laminin subunit beta-1
- Laminin subunit gamma-1
- Laminin subunit gamma-3
- CD44 antigen
- Integrin beta-1
- Laminin subunit beta-2
- Integrin alpha-7
- Multiple epidermal growth factor-like domains protein 11
- Laminin subunit gamma-2
- Integrin alpha-6
Sequence:
MGWSTAWCSVLALWLLWCAVCSNAASGDGNAFPFDIEGSAVVGRQDPSETSDSGVTLGRLPPAAERCDAGFFRTLSGECAPCDCNGNSHECLDGSGFCLHCQRNTTGEHCEKCLDGYIGDSIRGTPRFCQPCPCPLPHLANFAESCYRKNGAVRCICKENYVGPNCERCAPGYYGNPLLIGSTCKKCDCSGNSDPNLIFEDCDEITGQCRNCLRNTTGFKCERCAPGYYGDARTAKNCAVCNCGGGPCDSVTGECLEEGFEVPTGCDKCVWDLTDDLRLAALSIEESKSGLLSVSSGAAAHRHVTDMNSTIHLLRTRLSERENQYTLRKIQINNSENTLRSLLPDVEGLHEKGSQASRKGMLVEKESMDTIDQATHLVEQAHNMRDKIQEINSKMLYYGENQELGPEEIAEKLVLAQKMLEEIRSRQPFLTHRELVDEEADEAQELLSQAENWQRLHNDTRSLFPVVLEQLDDYNAKLSDLQESINQALDHVRDAEDMNRAITFKQRDHEKQHERVKEQMEVVGASLSMSADSLTIPQLTLEELDEIIKNASGIYAEIDGAKNELQGKLSNLSNLSHDLVQEATDHAYNLQQEADELSRNLHSSDMNGLVQKALDASNVYENIANYVSEANETAELALNITDRIYDAVSGIDTQIIYHKDESDNLLNQARELQAKADSSNDEAVADTSRRVGGALWRKGALRDRLNDAVKQLQAAERGDAHQRLGQSKLFIEEANKTTAAVQQVTTPMANNLSNWSQNLQTFDSSAYNTAVDSARDAVRNLTEVVPQLLDQLRTVEQKRPASNISASIQRIRELIAQTRSVASKIQVSMMFDGQSAVEVHPKVSVDDLKAFTSISLYMKPPPKPAEPTGAWVADQFVLYLGSKNAKKEYMGLAIKNDNLVYVYNLGMKDVEILLDSKPVSSWPAYFSIVKIERVGKHGKVFLTVPSLSSTAEEKFIKKGEFAGDDSLLDLTPEDTVFYVGGVPANFKLPASLNLPSYSGCLELATLNNDVISLYNFKHIYNMDPSKSVPCARDKLAFTQSRAASYFFDGSSYAVVRDITRRGKFGQVTRFDIEIRTPADNGLVLLMVNGSMFFSLEMRNGYLHVFYDFGFSNGPVHLEDTLKKAQINDAKYHEISIIYHNDKKMILVVDRRHVKSTDNEKKKIPFTDIYIGGAPQEVLQSRTLRAHLPLDINFRGCMKGFQFQKKDFNLLEQTETLGVGYGCPEDSLISRRAYFNGQSFIASIQKISFFDGFEGGFNFRTLQPNGLLFYYTSGSDVFSISLDNGTVVMDVKGIKVMSTDKQYHDGLPHFVVTSISDTRYELVVDKSRLRGKNPTKGKAEQTQTTEKKFYFGGSPISPQYANFTGCISNAYFTRLDRDVEVEDFQRYSEKVHTSLYECPIESSPLFLLHKKGKNSSKPKTNKQGEKSKDAPSWDPIGLKFLEQKAPRDSHCHLSSSPRAIEHAYQYGGTANSRQEFEHEQGDFGEKSQFAIRLKTRSSHGMIFYVSDQEENDFMTLFLAHGRLVFMFNVGHKKLKIRSQEKYNDGLWHDVIFIREKSSGRLVIDGLRVLEERLPPSGAAWKIKGPIYLGGVAPGRAVKNVQITSVYSFSGCLGNLQLNGASITSASQTFSVTPCFEGPMETGTYFSTEGGYVVLDESFNIGLKFEIAFEVRPRSSSGTLVHGHSVNGEYLNVHMRNGQVIVKVNNGVRDFSTSVTPKQNLCDGRWHRITVIRDSNVVQLDVDSEVNHVVGPLNPKPVDHREPVFVGGVPESLLTPRLAPSKPFTGCIRHFVIDSRPVSFSKAALVSGAVSINSCPTA
Protein: Methyl-CpG binding domain protein 3 (F7EY92)
Organism: Rattus norvegicus (Rat)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- Chromodomain-helicase-DNA-binding protein 4
- Histone-binding protein RBBP7
- Metastasis-associated gene family, member 2
- Histone deacetylase 1
- RB-binding protein 4, chromatin-remodeling factor.
- Histone deacetylase 2
- GATA zinc finger domain containing 2A
- DNA helicase
- Metastasis-associated protein MTA1
- Metastasis-associated protein MTA3
Sequence:
MERKSPSGKKFRSKPQLARYLGGSMDLSTFDFRTGKMLMNKMNKSRQRVRYDSSNQVKALAKHLPGPSNPSWTPVGAARCRVFSPQGKPDLNTALPVRQTASIFKQPVTKITNHPSNKVKSDPQKAVDQPRQLFWEKKLSGLSAFDIAEELVRTMDLPKGLQGVGPGCTDETLLSAIASALHTSTLPITGQLSAAVEKNPGVWLNTAQPLCKAFMVTDDDIRKQEELVQQVRKRLEEALMADMLAHVEELARDGEAPLDKACAEEEEEEEEEEEEEPEPERV
Protein: Serine/threonine-protein kinase receptor (EC 2.7.11.30) (A0A8I5ZXN2)
Organism: Rattus norvegicus (Rat)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004479, ECO:0000256|RuleBase:RU361271}; Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004479, ECO:0000256|RuleBase:RU361271}.
Interaction partners:
Sequence:
MKSSKYMSSFCIFVTSYFNLVTYCLFHRNPEGCPNPHSLFFTEKFVDNMLLRSSGKLNVGTKKEDGESTAPTARPKVLRCKCHHHCPEDSVNNICSTDGYCFTMIEEDDSGTPVVTSGCLGLEGSDFQCRDTPIPHQRRSIECCTERNECNKDLHPTLPPLKDRDFVDGPIHHKALLISVTVCSLLLVLIILFCYFRYKRQEARPRYSIGLEQDETYIPPGESLRDLIEQSQSSGSGSGLPLLVQRTIAKQIQMVKQIGKGRYGEVWMGKWRGEKVAVKVFFTTEEASWFRETEIYQTVLMRHENILGFIAADIKGTGSWTQLYLITDYHENGSLYDYLKSTTLDAKSMLKLAYSSVSGLCHLHTEIFSTQGKPAIAHRDLKSKNILVKKNGTCCIADLGLAVKFISDTNEVDIPPNTRVGTKRYMPPEVLDESLNRTHFQSYIMADMYSFGLILWEIARRCVSGGIVEEYQLPYHDLVPSDPSYEDMREIVCMKKLRPSFPNRWSSDECLRQMGKLMTECWAHNPASRLTALRVKKTLAKMSESQDIKL
Protein: 5-phosphohydroxy-L-lysine phospho-lyase (EC 4.2.3.134) (Alanine--glyoxylate aminotransferase 2-like 2) (Q8R1K4)
Organism: Mus musculus (Mouse)
Function: Catalyzes the pyridoxal-phosphate-dependent breakdown of 5-phosphohydroxy-L-lysine, converting it to ammonia, inorganic phosphate and 2-aminoadipate semialdehyde.
Subcellular location: Mitochondrion {ECO:0000250|UniProtKB:Q8IUZ5}.
Interaction partners:
- Hydroxylysine kinase
- Alpha-aminoadipic semialdehyde dehydrogenase
- Alpha-aminoadipic semialdehyde synthase, mitochondrial
Sequence:
MAADTRAKAVTLDLRRRLLSSSCRLFFPEDPVKIIRGQGQYLYDEQGREYLDCINNVAHVGHCHPTVVQAAHEQNLVLNTNSRYLHDNIVDYAQRLSETLPEQLSVFYFLNSGSEANDLALRLARQYTGHQDVVVLDHAYHGHLSSLIDISPYKFRNLGGQKEWVHVAPLPDTYRGPYREDHPNPAEAYANEVKHVISSAQQKGRKIAAFFAESLPSVSGQIIPPAGYFSQVAEHIHRAGGLFVADEIQVGFGRIGKHFWAFQLEGEDFVPDIVTMGKSIGNGHPVACMATTQAVSRAFEATGVEYFNTFGGNPVSCAVGLAVLDVLKTEQLQAHATNVGSFLLEHLTQQKAKHPIIGDVRGTGLFIGVDLIKDETLRTPATEEAEYLVSRLKENYILLSIDGPGKNILKFKPPMCFNVDNAQHVVAKLDDILTDMEEKVRSCETLRIKHPPEDTHPTQILLTRQQD
Protein: CRP-like protein Clp (Catabolite activation-like protein) (CAP-like) (P22260)
Organism: Xanthomonas campestris pv. campestris (strain ATCC 33913 / DSM 3586 / NCPPB 528 / LMG 568 / P 25)
Function: Global transcriptional regulator that regulates virulence factors production by activating or repressing the expression of a large set of genes in diffusible signal factor (DSF) pathway. It includes, among others, genes involved in extracellular polysaccharide (EPS) synthesis, flagellum synthesis, protein and fatty acid metabolism, multidrug resistance, iron uptake or genes encoding extracellular enzymes, membrane components and a few transcription factors. Regulation can be direct or indirect, via regulation of other transcriptional regulators. Not involved in DSF-mediated biofilm dispersal.
Subcellular location: Cytoplasm {ECO:0000305}.
Interaction partners:
- Response regulator
- RNA polymerase sigma factor RpoD
- DNA-directed RNA polymerase subunit alpha
- DNA-directed RNA polymerase subunit beta
- DNA-directed RNA polymerase subunit beta'
- DNA-directed RNA polymerase subunit omega
- Sensory/regulatory protein RpfC
- RpfF protein
Sequence:
MSLGNTTVVTTTVRNATPSLTLDAGTIERFLAHSHRRRYPTRTDVFRPGDPAGTLYYVISGSVSIIAEEDDDRELVLGYFGSGEFVGEMGLFIESDTREVILRTRTQCELAEISYERLQQLFQTSLSPDAPRILYAIGVQLSKRLLDTTRKASRLAFLDVTDRIVRTLHDLSKEPEAMSHPQGTQLRVSRQELARLVGCSREMAGRVLKKLQADGLLHARGKTVVLYGTR
Protein: Fructose-bisphosphate aldolase (Glfba) (glFBPA) (EC 4.1.2.13) (Fructose-1,6-bisphosphate aldolase) (A8B2U2)
Organism: Giardia intestinalis (strain ATCC 50803 / WB clone C6) (Giardia lamblia)
Interaction partners:
- Ribosomal protein S11
- Phosphoglycerate kinase
- Triosephosphate isomerase
- phosphopyruvate hydratase
- Glucose-6-phosphate isomerase
- Glyceraldehyde-3-phosphate dehydrogenase
- Glyceraldehyde-3-phosphate dehydrogenase
- Transketolase
- Pyrophosphate--fructose 6-phosphate 1-phosphotransferase
- Glucokinase
Sequence:
MPLCTLRQMLGEARKHKYGVGAFNVNNMEQIQGIMKAVVQLKSPVILQCSRGALKYSDMIYLKKLCEAALEKHPDIPICIHLDHGDTLESVKMAIDLGFSSVMIDASHHPFDENVRITKEVVAYAHARGVSVEAELGTLGGIEEDVQNTVQLTEPQDAKKFVELTGVDALAVAIGTSHGAYKFKSESDIRLAIDRVKTISDLTGIPLVMHGSSSVPKDVKDMINKYGGKMPDAVGVPIESIVHAIGEGVCKINVDSDSRMAMTGAIRKVFVEHPEKFDPRDYLGPGRDAITEMLIPKIKAFGSAGHAGDYKVVSLEEAKAWYK
Protein: Tripartite motif-containing protein 12A (Q99PQ1)
Organism: Mus musculus (Mouse)
Subcellular location: Cytoplasm {ECO:0000269|PubMed:11331580}.
Interaction partners:
Sequence:
MASQFMKNLKEEVTCPVCLNLMVKPVSADCGHTFCQGCITLYFESIKCDKKVFICPVCRISYQFSNLRPNRNVANIVERLKMFKPSPEEEQKVFNCARHGKKLQLFCRKDMMAICWLCERSQEHRGHKTALIEEVAQEYKEQLQVVLQRLMADKKKFENWKDDLQKDRTYWENQIQKDVQNVRSEFKRMRDIMDSEEKKELQKLRQEKEDILNNLAESESEHAQQSKLLEDFISDVEHQLQCSDIEILQVRLQDVPGSESQKAWKPLPFLSAAVVFLVMTVSSS
Protein: Translocase of inner mitochondrial membrane 44 (M0QXM9)
Organism: Homo sapiens (Human)
Subcellular location: Mitochondrion inner membrane {ECO:0000256|ARBA:ARBA00004273}.
Interaction partners:
Sequence:
LFSKTEMSEVLTEILRVDPAFDKDRFLKQCENDIIPNVLEAMISGELDILKDWCYEALAMGKMMEQGPVLIITFQAQLVMVVRNPKGEVVEGDPDKVLRMLYVWALCRDQDELNPYAAWRLLDISASSTEQIL
Protein: small monomeric GTPase (EC 3.6.5.2) (Q9VD29)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00004240}. Golgi apparatus, Golgi stack membrane {ECO:0000256|ARBA:ARBA00037843}; Peripheral membrane protein {ECO:0000256|ARBA:ARBA00037843}.
Interaction partners:
- FI09914p
- Protein transport protein SEC23
- Protein transport protein Sec31A
- Protein SEC13 homolog
- Secretory 24AB, isoform A
- Secretory 16, isoform I
- Secretory 24CD, isoform C
- Transport and Golgi organization protein 1
- BET1 homolog
- GEO07453p1
Sequence:
MFIWDWFTGVLGYLGLWKKSGKLLFLGLDNAGKTTLLHMLKDDKLAQHVPTLHPTSEELSIGNMRFTTFDLGGHTQARRVWKDYFPAVDAIVFLIDAWDRGRFQESKNELDSLLTDEALSNCPVLILGNKIDKPGAASEDELRNVFGLYQLTTGKGKVARADLPGRPLELFMCSVLKRQGYGEGFRWLAQYID
Protein: Transmembrane protein 17 (Q8K0U3)
Organism: Mus musculus (Mouse)
Function: Transmembrane component of the tectonic-like complex, a complex localized at the transition zone of primary cilia and acting as a barrier that prevents diffusion of transmembrane proteins between the cilia and plasma membranes. Required for ciliogenesis and sonic hedgehog/SHH signaling.
Subcellular location: Cell projection, cilium membrane {ECO:0000269|PubMed:22179047}; Multi-pass membrane protein {ECO:0000269|PubMed:22179047}. Note=Localizes to the transition zone of primary cilia.
Interaction partners:
- Transmembrane protein 231
- B9 domain-containing protein 1
- Coiled-coil and C2 domain-containing protein 2A
- B9 domain-containing protein 2
- Transmembrane protein 216
- Tectonic-1
- Meckelin
- Tectonic-2
- Centrosomal protein of 290 kDa
- Jouberin
Sequence:
MELPDPVRQRLSNLSLTVFGDSSRTGPESSDAADNEMVSSLALQMSLYFNSYFFPLWWVSCIVMLHLKYSILPDYYKFIVVTVVILITLIEAIRLYLGCMGNLQEKVPELAGFWLLSLLLQLPLILFLLLNDGLRNLPLEKAIHIIFTIFLTFQVISAFLTLKKMVNQLAARFHLQDFDQLSSSSAAVRRVRQCTEEL
Protein: Lymphocyte cytosolic protein 1 (A0A8I6AGS0)
Organism: Rattus norvegicus (Rat)
Interaction partners:
Sequence:
MARGSVSDEEMMELREAFAKVDTDGNGYISCNELNDLFKAACLPLPGYRVREITENLMATGDLDQDGKISFDEFIKVFHGLKSTEVAKTFRKAINKKEGICAIGGTSEQSSVGTQHSYSEEEKYAFVNWINKALENDPDCRHVIPMNPNTDDLFNAVGDGIVLCKMVNLSVPDTIDERTINKKKLTPFTIQENLNLALNSASAIGCHVVNIGAEDLKEGKPYLVLGLLWQVIKIGLFADIELSRNEALIALLREGESLEDLMKLSPEELLLRWANYHLENAGCTKITNFSTDIKDSKAYYHLLEQVAPRGDEEGIPAVVIDMSGLREKDDIQRAECMLQQFVTATDVVRGNPKLNLAFIANLFNKYPALHKPENQDIDWGALEGETREERTFRNWMNSLGVNPGVNHLYSDLSDALVIFQLYEKIKVPVDWNRVNRPPYPKLGGNMKKLENCNYAVDLGKNQAKFSLVGIAGQDLNEGNRTLTLALVWQLMRRYTLNILEDIGGGQKVNDDIIVNWVNTTLKEAQKSSSITSFKDPKISTSLPVLDLIDAIQPGSINYDLLKTENLDDEEKLNNAKYAISMARKIGARVYALPEDLVEVNPKMVMTVFACLMGKGMKRV
Protein: Ribonuclease VapC31 (RNase VapC31) (EC 3.1.-.-) (Toxin VapC31) (P9WF75)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: Toxic component of a type II toxin-antitoxin (TA) system. An RNase (By similarity). Upon expression in M.smegmatis inhibits colony formation. Its toxic effect is neutralized by coexpression with cognate antitoxin VapB31 (By similarity).
Interaction partners:
- Antitoxin VapB31
- Ribonuclease VapC4
- Ribonuclease VapC25
- Ribonuclease VapC48
- Ribonuclease VapC10
Sequence:
MFLLDANVLLAAHRGDHPNHRTVRPWFDRLLAADDPFTVPNLVWASFLRLATNRRIFEIPSPRAEAFAFVEAVTAQPHHLPTNPGPRHLMLLRKLCDEADASGDLIPDAVLAAIAVGHHCAVVSLDRDFARFASVRHIRPPL
Protein: Neurofilament heavy polypeptide (NF-H) (200 kDa neurofilament protein) (Neurofilament triplet H protein) (P16884)
Organism: Rattus norvegicus (Rat)
Function: Neurofilaments usually contain three intermediate filament proteins: NEFL, NEFM, and NEFH which are involved in the maintenance of neuronal caliber. NEFH has an important function in mature axons that is not subserved by the two smaller NEF proteins. May additionally cooperate with the neuronal intermediate filament proteins PRPH and INA to form neuronal filamentous networks (By similarity).
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:P19246}. Cell projection, axon {ECO:0000250|UniProtKB:P19246}.
Interaction partners:
- Kinesin heavy chain isoform 5C
- Mitogen-activated protein kinase 14
- Mitogen-activated protein kinase 13
- Mitogen-activated protein kinase 12
- mitogen-activated protein kinase
- Kinesin heavy chain isoform 5A
- Kinesin-1 heavy chain
- Kinesin light chain 1
- Kinesin light chain
- Kinesin light chain 3
Sequence:
MMSFGSADALLGAPFAPLHGGGSLHYALSRKAGAGGTRSAAGSSSGFHSWARTSVSSVSASPSRFRGAASSTDSLDTLSNGPEGCVAAVAARSEKEQLQALNDRFAGYIDKVRQLEAHNRTLEGEAAALRQQKGRAAMGELYEREVREMRGAVLRLGAARGHVRLEQEHLLEDIAHVRQRLDEEARQREEAEAAARALARFAQEAEAARVELQKKAQALQEECGYLRRHHQEEVGELLGQIQGCGAAQAQAQAEARDALKCDVTSALREIRAQLEGHTVQSTLQSEEWFRVRLDRLSEAAKVNTDAMRSAQEEITEYRRQLQARTTELEALKSTKESLERQRSELEDRHQVDMASYQDAIQQLDNELRNTKWEMAAQLREYQDLLNVKMALDIEIAAYRKLLEGEECRIGFGPSPFSLTEGLPKIPSMSTHIKVKSEEKIKVVEKSEKETVIVEEQTEEIQVTEEVTEEEDKEAQGEEEEEAEEGGEEAATTSPPAEEAASPEKETKSPVKEEAKSPAEAKSPAEAKSPAEAKSPAEVKSPAEVKSPAEAKSPAEAKSPAEVKSPAEVKSPAEAKSPAEAKSPAEVKSPATVKSPGEAKSPAEAKSPAEVKSPVEAKSPAEAKSPASVKSPGEAKSPAEAKSPAEVKSPATVKSPVEAKSPAEVKSPVTVKSPAEAKSPVEVKSPASVKSPSEAKSPAGAKSPAEAKSPVVAKSPAEAKSPAEAKPPAEAKSPAEAKSPAEAKSPAEAKSPAEAKSPVEVKSPEKAKSPVKEGAKSLAEAKSPEKAKSPVKEEIKPPAEVKSPEKAKSPMKEEAKSPEKAKTLDVKSPEAKTPAKEEAKRPADIRSPEQVKSPAKEEAKSPEKEETRTEKVAPKKEEVKSPVEEVKAKEPPKKVEEEKTPATPKTEVKESKKDEAPKEAQKPKAEEKEPLTEKPKDSPGEAKKEEAKEKKAAAPEEETPAKLGVKEEAKPKEKAEDAKAKEPSKPSEKEKPKKEEVPAAPEKKDTKEEKTTESKKPEEKPKMEAKAKEEDKGLPQEPSKPKTEKAEKSSSTDQKDSQPSEKAPEDKAAKGDK
Protein: Adenylate kinase isoenzyme 5 (AK 5) (EC 2.7.4.3) (EC 2.7.4.6) (ATP-AMP transphosphorylase 5) (Q9Y6K8)
Organism: Homo sapiens (Human)
Function: Nucleoside monophosphate (NMP) kinase that catalyzes the reversible transfer of the terminal phosphate group between nucleoside triphosphates and monophosphates. Active on AMP and dAMP with ATP as a donor. When GTP is used as phosphate donor, the enzyme phosphorylates AMP, CMP, and to a small extent dCMP. Also displays broad nucleoside diphosphate kinase activity.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:19647735}.
Interaction partners:
- Adenine phosphoribosyltransferase
- Adenylosuccinate lyase
- Adenosine kinase
- Deoxycytidine kinase
- Pyruvate kinase PKM
- Ectonucleoside triphosphate diphosphohydrolase 2
- Thiamine pyrophosphokinase 1
- Pyruvate kinase PKLR
- Cancer-related nucleoside-triphosphatase
- Ectonucleotide pyrophosphatase/phosphodiesterase family member 1
Sequence:
MNTNDAKEYLARREIPQLFESLLNGLMCSKPEDPVEYLESCLQKVKELGGCDKVKWDTFVSQEKKTLPPLNGGQSRRSFLRNVMPENSNFPYRRYDRLPPIHQFSIESDTDLSETAELIEEYEVFDPTRPRPKIILVIGGPGSGKGTQSLKIAERYGFQYISVGELLRKKIHSTSSNRKWSLIAKIITTGELAPQETTITEIKQKLMQIPDEEGIVIDGFPRDVAQALSFEDQICTPDLVVFLACANQRLKERLLKRAEQQGRPDDNVKATQRRLMNFKQNAAPLVKYFQEKGLIMTFDADRDEDEVFYDISMAVDNKLFPNKEAAAGSSDLDPSMILDTGEIIDTGSDYEDQGDDQLNVFGEDTMGGFMEDLRKCKIIFIIGGPGSGKGTQCEKLVEKYGFTHLSTGELLREELASESERSKLIRDIMERGDLVPSGIVLELLKEAMVASLGDTRGFLIDGYPREVKQGEEFGRRIGDPQLVICMDCSADTMTNRLLQRSRSSLPVDDTTKTIAKRLEAYYRASIPVIAYYETKTQLHKINAEGTPEDVFLQLCTAIDSIF