wanglab/gogpt-training-data huggingface dataset:
Protein: Alpha-2A adrenergic receptor (Alpha-2 adrenergic receptor subtype C10) (Alpha-2A adrenoreceptor) (Alpha-2A adrenoceptor) (Alpha-2AAR) (P08913)
Organism: Homo sapiens (Human)
Function: Alpha-2 adrenergic receptors mediate the catecholamine-induced inhibition of adenylate cyclase through the action of G proteins. The rank order of potency for agonists of this receptor is oxymetazoline > clonidine > epinephrine > norepinephrine > phenylephrine > dopamine > p-synephrine > p-tyramine > serotonin = p-octopamine. For antagonists, the rank order is yohimbine > phentolamine = mianserine > chlorpromazine = spiperone = prazosin > propanolol > alprenolol = pindolol.
Subcellular location: Cell membrane {ECO:0000269|PubMed:23105096}; Multi-pass membrane protein {ECO:0000269|PubMed:23105096}.
Interaction partners:
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein subunit alpha-12
- Guanine nucleotide-binding protein subunit alpha-13
- Guanine nucleotide-binding protein subunit alpha-11
- Sodium-dependent dopamine transporter
- Sodium-dependent noradrenaline transporter
- Guanine nucleotide-binding protein G
Sequence:
MFRQEQPLAEGSFAPMGSLQPDAGNASWNGTEAPGGGARATPYSLQVTLTLVCLAGLLMLLTVFGNVLVIIAVFTSRALKAPQNLFLVSLASADILVATLVIPFSLANEVMGYWYFGKAWCEIYLALDVLFCTSSIVHLCAISLDRYWSITQAIEYNLKRTPRRIKAIIITVWVISAVISFPPLISIEKKGGGGGPQPAEPRCEINDQKWYVISSCIGSFFAPCLIMILVYVRIYQIAKRRTRVPPSRRGPDAVAAPPGGTERRPNGLGPERSAGPGGAEAEPLPTQLNGAPGEPAPAGPRDTDALDLEESSSSDHAERPPGPRRPERGPRGKGKARASQVKPGDSLPRRGPGATGIGTPAAGPGEERVGAAKASRWRGRQNREKRFTFVLAVVIGVFVVCWFPFFFTYTLTAVGCSVPRTLFKFFFWFGYCNSSLNPVIYTIFNHDFRRAFKKILCRGDRKRIV
Protein: StAR related lipid transfer domain containing 10 (F5H1Z6)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MEKLAASTEPQGPRPVLGRESVQVPDDQDFRSFRSECEAEVGWNLTYSRAGVSVWVQAVEMDRTLHKIKCRMECCDVPAETLYDVLHDIEYRKKWDSNVIETFDIARLTVNADVGYYSWRCPKPLKNRDVITLRSWLPMGADYIIMNYSVKHPKYPPRKDLVRAVSIQTGYLIQSTGPKSCVITYLAQVDPKGSLPKWVVNKSSQFLAPKAMKKMYKACLKYPEWKQKHLPHFKPWLHPEQSPLPSLALSEL
Protein: Probable G-protein coupled receptor 156 (GABAB-related G-protein coupled receptor) (Q6PCP7)
Organism: Mus musculus (Mouse)
Function: Orphan receptor.
Subcellular location: Cell membrane; Multi-pass membrane protein. Postsynaptic cell membrane; Multi-pass membrane protein.
Interaction partners:
- Gamma-aminobutyric acid type B receptor subunit 1
- Gamma-aminobutyric acid type B receptor subunit 2
Sequence:
MEPEINCSEFCDSFPGQELDRRPLHDLCKTTITESQHSSTAASPLSPALLGIMWTFLSCGLLLVLFFLAFTIRCRKNRIVKMSSPNLNVVTLLGSCLTYISAYLFGIQDALEGSSVEALIQTRLSLLCIGTSLVFGPILGKSWRLYKVFTQRVPDKRVIIKDLQLLGLVAALVVADVILLVTWVLTDPIQCLQMLGVSMKVTGRDVSCSLTNTHFCASRYSDVWIALVLGCKGLLLLYGAYLAGLTNHVSSPPVNQSLTIMVGVNLLLLTAGLLFVVTRYLHSWPNLVFGLTSGGIFVCTTTVNCCVFIPQLKQWKAFEGENQTMRHMAKYFSTPSKSFHSQFDEDPSCHLRDEKSCMERLLTEKNAVIESLQEQVSNAKEKLVKLMSAECTYDSPEWAVPDAASARGLALPGPSECPAVSENESGAAARDSLHVPAACQHVQGPGASRRDTSPSPAQQDNMPLKQYCDHLDTGCNQKPKAEQSEGPERGDQEPMAPSQRLMADGVACEPHKPRQSPEGLPKKLPGVSSVVREKLQEVLQELDLGSEAPLSPLPCPQQLWKSTTSRSPQKLSPSKLGFSPYVVRRRRAAQRARSHIPGSVGLNVGHQANSTVSSSQSGLIVQNRDSPRLDHHNARSKVPRSSSVKPSPLSEPRRKQGTLEGSKQCETEPQEAGGACNVAFPCQSSASVQAQSPAAPCLPSSPALPRQRQPRPRLSPGCPSLSSGCYNLDSESSSSDEFFCRCHRPYCEICFQSSLDSNDSDTSDSDLEQASGLASWEKLWARSKPVVNFKDDLKPTLV
Protein: Histidinol-phosphate aminotransferase (EC 2.6.1.9) (Imidazole acetol-phosphate transaminase) (Q72DA0)
Organism: Nitratidesulfovibrio vulgaris (strain ATCC 29579 / DSM 644 / CCUG 34227 / NCIMB 8303 / VKM B-1760 / Hildenborough) (Desulfovibrio vulgaris)
Interaction partners:
- Imidazoleglycerol-phosphate dehydratase
- Histidinol dehydrogenase
- Imidazole glycerol phosphate synthase subunit HisH
- Prephenate dehydrogenase
- Imidazole glycerol phosphate synthase subunit HisF
- ATP phosphoribosyltransferase
- Bifunctional chorismate mutase/prephenate dehydratase
- Aminotransferase
- Phosphoribosyl-AMP cyclohydrolase
- 1-
Sequence:
MTAPSMSRPDDVRPEVLDFKPYVPGLSIDEIRDRFGLADVVKLASNENPLGTSPVVQRTLKTKADLAFRYAQSGNPRLTRAIAAHHGVAPERVVAGNGSDEIIDLLIRVRATPGKHNIVAFRPCFSIYELQAKFCGLEFRQADLRPDFTFDWDAFLAATDENTAIAFVTTPDNPSGWCPPVSELEHVARTLPPSCLFVIDEAYMDFCGDEAAHSLLSRLDAFPNIAVLRTFSKSFGLAGLRLGYGILPERLADYLHRVRLPFSVNILAEEAGLAALEDTVFRSETLRVTAEGRAYIAEGLTALGCEVMPSWANFIMFRPPTDATDLFEALLRRGIIIRPLKSYGLPQHLRVSVGNADENRRFIEACKEILPHA
Protein: Zinc finger MYM-type containing 3 (A6NC58)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MDPSDFPSPFDPLTLPEKPLAGDLPVDMEFGEDLLESQTAPTRGWAPPGPSPSSGALDLLDTPAGLEKDPGVLDGATELLGLGGLLYKAPSPPEVDHGPEGTLAWDAGDQTLEPGPGGQTPEVVPPDPGAGANSCSPEGLLEPLAPDSPITLQSPHIEEEETTSIATARRGSPGQEEELPQGQPQSPNAPPSPSVGETLGDGINSSQTKPGGSSPPAHPSLPGDGLTAKASEKPPERVQKRSERVRRAEPPKPEVVDSTESRRSGTPRTRLWRRLVLEAPSMSSAHPSVSPCMRPSSSARSPSLGIPPTLLAAAYARRLERSCTRSAMAAWYTGSAAILASPNSGPTRD
Protein: Heptaprenylglyceryl phosphate synthase (HepGP synthase) (EC 2.5.1.n9) (Glycerol-1-phosphate heptaprenyltransferase) (Q8Y6C8)
Organism: Listeria monocytogenes serovar 1/2a (strain ATCC BAA-679 / EGD-e)
Function: Prenyltransferase that catalyzes in vivo the transfer of the heptaprenyl moiety of heptaprenyl pyrophosphate (HepPP; 35 carbon atoms) to the C3 hydroxyl of sn-glycerol-1-phosphate (G1P), producing heptaprenylglyceryl phosphate (HepGP). This reaction is an ether-bond-formation step in the biosynthesis of archaea-type G1P-based membrane lipids found in Bacillales. To a much lesser extent, is also able to use geranylgeranyl diphosphate (GGPP; C20) as the prenyl donor.
Interaction partners:
- ATP-dependent DNA helicase
- Lmo1920 protein
- Lmo2480 protein
Sequence:
MKHLFKLDPAKNLPTNDVTKLIHSGTDGFIIGGTDNVQIEAVQNLYELLVETDLPIFLEISNESMILPEADHFLIPVVLNTENSKWTHGLHKELIKEMGEFIPWKRVTSEGYVILNKDAKVAHLTEAKTDLTDEDIVAYARLAENIFHLPIFYVEYSGMYGDPEVVRKASAALSNTKFWYGGGIRSKEQAAEMAKYADTIIVGNIIYEDLEKALETATIFRKKTV
Protein: RE17884p (Transcription factor AP-2) (O96378)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MHILHRTNDHQFEDQKFMMERLSGHGSLGLSSGSAAYTTHSGGHTGRSGPATGHSGHSSTHGSAATMHHQSLQSDFQPPYFPPPFHHSTQSPPQQQNHGALEYLGTDPYGQPLSSLHHAPLHHYNQLAGLRSTQDQLGIHRTHREAELQGHVTQLSHGFPYTDRRSDYGSAISAGAAHGTRLGHEHESLALHQALQNAVDDVQAPALDDNVAFMSDLPLIKSMKSGKEAGNIGSGSPSEVFCAVPGRLSLLSSTSKYKVTIAEVQRRLSPPECLNASLLGGVLRRAKSKNGGRLLREKLEKIGLNLPAGRRKAANVTLLTSLVEGEATHLAKDFHFVCETEFPARQLAEYIVRHQTEPQDSYRRKELILHSQQITKELMQILSQDRTTHFGTRSQHLLEPSMQRHLTHFSLITHGFGSPAIMAVLHAFQTFLNESLNYLEKLYPSNGGGMVSSSLDKSKIDNEKK
Protein: Dexamethasone-induced protein (Protein MYLE) (O95424)
Organism: Homo sapiens (Human)
Interaction partners:
- Protein CLEC16A
Sequence:
MLGARVAAHLDALGPLVPYVPPPLLPSMFYVGLFFVNVLILYYAFLMEYIVLNVGLVFLPEDMDQALVDLGVLSDPGSGLYDADSELDVFDAYLE
Protein: Stromelysin-2 (SL-2) (EC 3.4.24.22) (Matrix metalloproteinase-10) (MMP-10) (Transin-2) (P09238)
Organism: Homo sapiens (Human)
Function: Can degrade fibronectin, gelatins of type I, III, IV, and V; weakly collagens III, IV, and V. Activates procollagenase.
Subcellular location: Secreted, extracellular space, extracellular matrix {ECO:0000305}.
Interaction partners:
- Metalloproteinase inhibitor 1
- Metalloproteinase inhibitor 2
- Stromelysin-1
- U1 small nuclear ribonucleoprotein A
- Matrilysin
- Fibronectin
- Histone deacetylase 7
- Interstitial collagenase
- Stromelysin-3
- 72 kDa type IV collagenase
Sequence:
MMHLAFLVLLCLPVCSAYPLSGAAKEEDSNKDLAQQYLEKYYNLEKDVKQFRRKDSNLIVKKIQGMQKFLGLEVTGKLDTDTLEVMRKPRCGVPDVGHFSSFPGMPKWRKTHLTYRIVNYTPDLPRDAVDSAIEKALKVWEEVTPLTFSRLYEGEADIMISFAVKEHGDFYSFDGPGHSLAHAYPPGPGLYGDIHFDDDEKWTEDASGTNLFLVAAHELGHSLGLFHSANTEALMYPLYNSFTELAQFRLSQDDVNGIQSLYGPPPASTEEPLVPTKSVPSGSEMPAKCDPALSFDAISTLRGEYLFFKDRYFWRRSHWNPEPEFHLISAFWPSLPSYLDAAYEVNSRDTVFIFKGNEFWAIRGNEVQAGYPRGIHTLGFPPTIRKIDAAVSDKEKKKTYFFAADKYWRFDENSQSMEQGFPRLIADDFPGVEPKVDAVLQAFGFFYFFSGSSQFEFDPNARMVTHILKSNSWLHC
Protein: Keratin, type II cytoskeletal 5 (58 kDa cytokeratin) (Cytokeratin-5) (CK-5) (Keratin-5) (K5) (Type-II keratin Kb5) (P13647)
Organism: Homo sapiens (Human)
Function: Required for the formation of keratin intermediate filaments in the basal epidermis and maintenance of the skin barrier in response to mechanical stress (By similarity). Regulates the recruitment of Langerhans cells to the epidermis, potentially by modulation of the abundance of macrophage chemotactic cytokines, macrophage inflammatory cytokines and CTNND1 localization in keratinocytes (By similarity).
Subcellular location: Cytoplasm {ECO:0000269|PubMed:20128788}.
Interaction partners:
- Keratin, type I cytoskeletal 14
- Keratin, type II cytoskeletal 1
- Keratin, type II cytoskeletal 6A
- Epidermal growth factor receptor
- Keratin, type II cytoskeletal 2 epidermal
- Keratin, type I cytoskeletal 17
- Keratin, type I cytoskeletal 16
- Keratin, type II cytoskeletal 6B
- Tumor protein 63
- Plakophilin-1
Sequence:
MSRQSSVSFRSGGSRSFSTASAITPSVSRTSFTSVSRSGGGGGGGFGRVSLAGACGVGGYGSRSLYNLGGSKRISISTSGGSFRNRFGAGAGGGYGFGGGAGSGFGFGGGAGGGFGLGGGAGFGGGFGGPGFPVCPPGGIQEVTVNQSLLTPLNLQIDPSIQRVRTEEREQIKTLNNKFASFIDKVRFLEQQNKVLDTKWTLLQEQGTKTVRQNLEPLFEQYINNLRRQLDSIVGERGRLDSELRNMQDLVEDFKNKYEDEINKRTTAENEFVMLKKDVDAAYMNKVELEAKVDALMDEINFMKMFFDAELSQMQTHVSDTSVVLSMDNNRNLDLDSIIAEVKAQYEEIANRSRTEAESWYQTKYEELQQTAGRHGDDLRNTKHEISEMNRMIQRLRAEIDNVKKQCANLQNAIADAEQRGELALKDARNKLAELEEALQKAKQDMARLLREYQELMNTKLALDVEIATYRKLLEGEECRLSGEGVGPVNISVVTSSVSSGYGSGSGYGGGLGGGLGGGLGGGLAGGSSGSYYSSSSGGVGLGGGLSVGGSGFSASSGRGLGVGFGSGGGSSSSVKFVSTTSSSRKSFKS
Protein: Large ribosomal subunit protein uL24 (50S ribosomal protein L24) (P9WHB7)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: One of two assembly initiator proteins, it binds directly to the 5'-end of the 23S rRNA, where it nucleates assembly of the 50S subunit.
Interaction partners:
- Uncharacterized protein Rv0500B
- Large ribosomal subunit protein bL33B
- Large ribosomal subunit protein bL25
- Large ribosomal subunit protein uL10
- Large ribosomal subunit protein bL31
- Large ribosomal subunit protein bL27
- Large ribosomal subunit protein uL18
- Large ribosomal subunit protein bL17
- Large ribosomal subunit protein uL4
- Large ribosomal subunit protein uL13
Sequence:
MKVHKGDTVLVISGKDKGAKGKVLQAYPDRNRVLVEGVNRIKKHTAISTTQRGARSGGIVTQEAPIHVSNVMVVDSDGKPTRIGYRVDEETGKRVRISKRNGKDI
Protein: Mitochondrial import receptor subunit TOM20 homolog (Mitochondrial 20 kDa outer membrane protein) (Outer mitochondrial membrane receptor TOM20) (Translocase of outer mitochondrial membrane protein 20) (Q19766)
Organism: Caenorhabditis elegans
Function: Central component of the receptor complex responsible for the recognition and translocation of cytosolically synthesized mitochondrial preproteins (By similarity). Together with tomm-22 functions as the transit peptide receptor at the surface of the mitochondrion outer membrane and facilitates the movement of preproteins into the translocation pore.
Subcellular location: Mitochondrion outer membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}.
Interaction partners:
- Mitochondrial import receptor subunit TOM40 homolog
- Mitochondrial import receptor subunit tomm-70
- Mitochondrial import receptor subunit TOM22 homolog
- Probable voltage-dependent anion-selective channel
- Mitochondrial import receptor subunit TOM7 homolog
- Metaxin-1 homolog
- Mitochondrial Rho GTPase 1
- SAM50-like protein gop-3
- Serine/threonine-protein kinase pink-1, mitochondrial
- Mitochondrial import inner membrane translocase subunit TIM23
Sequence:
MSDTILGFNKSNVVLAAGIAGAAFLGYCIYFDHKRINAPDYKDKIRQKRRAQAGAGGMAPRRPAAAGNDAAPDVTDPSQMQRFFLQEVQLGEELMAAGNVDEGAVHIANAVMLCGESQQLLSIFQQTLSEDQFRAVVQQLPSTRERLAEMFGAKADEAENEPPMVQYLGDGPPPAQIQELIDDTDDLE
Protein: Spineless, isoform A (Q9VEV9)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MSQLGTVYATKRRRRNGKSLKPPPKDGVTKSNPSKRHRERLNAELDLLASLLPFEQNILSKLDRLSILRLSVSYLRTKSYFQVVMHKDKEDNGVLPHIHAHDGYRTRELGAFEHGLLDGDMFLQALNGFLMILTCEGEVFFATHSIESYLGFHQSDIVHQSVYELVHSEDREELQRQLLWNSFLPADMSSMQLAETLAPDKALYLERSFTVRFRCLLDNTSGFLRLDIRGRIKVLHGQNRKTEEPPLALFAYCTPFGPPSLLEIPHKENMFKSKHKLDFSLVSMDQRGKHILGYADAELVNMGGYDLVHYDDLAYVASAHQELLKTGASGMIAYRYQKKDGEWQWLQTSSRLVYKNSKPDFVICTHRQLMDEEGHDLLGKRTMDFKVSYLDTGLASTYFSEADQLVVPPSTSPTAHALPPPVTPTRPNRRYKTQLRDFLSTCRSKRKLQQQNQPQTQQTSPLGGQVGSPAPAVAVEYLPDPAAAVAAAYSNLNPMYTTSPYASAADNLYMGSSMPANAFYPVSENLFHQYRLQGAVGGYYTDYPHSGAPASAYVANGFLSYDGYAIASKADEKWQETGKYYSGYSSGYGSPTSTPQVRKQIPLKTPKSSPQVMEVISCSSDGPSPVGGATPNGVGSVTPKVELAGTTAAAAAGQDPYERQTVLMWGTTHSSGVPLNSHGGRTGAGNPASPQRSTPLGNGLGYASANNNNNDLEPATAAKWNGTKELPGKSGSASTPESYQMQHDDSGLYSASSHTTSPQQQQQQQLQQSQRGVGSNVSAPSSSLTSTGTDQQAVHPSSCHQQQQQQQQQHHHAHPHPHSHHHHHHHHHHETAHQHSSEVWTPASYTQYSQYFTYHHPHPHPHHPSAGGGGHVPAQSHHLHHGHR
Protein: Nicotinate-nucleotide pyrophosphorylase [carboxylating] (EC 2.4.2.19) (Quinolinate phosphoribosyltransferase [decarboxylating]) (QAPRTase) (P30011)
Organism: Escherichia coli (strain K12)
Function: Involved in the catabolism of quinolinic acid (QA).
Interaction partners:
- L-aspartate oxidase
- Quinolinate synthase
- Nicotinate phosphoribosyltransferase
- Nicotinate-nucleotide adenylyltransferase
- Trifunctional NAD biosynthesis/regulator protein NadR
- Nicotinamide-nucleotide amidohydrolase PncC
- Fumarate reductase flavoprotein subunit
- 5'/3'-nucleotidase SurE
- Nucleoside triphosphate pyrophosphohydrolase
- NAD-capped RNA hydrolase NudC
Sequence:
MPPRRYNPDTRRDELLERINLDIPGAVAQALREDLGGTVDANNDITAKLLPENSRSHATVITRENGVFCGKRWVEEVFIQLAGDDVTIIWHVDDGDVINANQSLFELEGPSRVLLTGERTALNFVQTLSGVASKVRHYVELLEGTNTQLLDTRKTLPGLRSALKYAVLCGGGANHRLGLSDAFLIKENHIIASGSVRQAVEKASWLHPDAPVEVEVENLEELDEALKAGADIIMLDNFETEQMREAVKRTNGKALLEVSGNVTDKTLREFAETGVDFISVGALTKHVQALDLSMRFR
Protein: Pyruvate dehydrogenase E1 component subunit alpha, mitochondrial (EC 1.2.4.1) (Pyruvate dehydrogenase complex component E1 alpha) (PDHE1-A) (P16387)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: The pyruvate dehydrogenase complex catalyzes the overall conversion of pyruvate to acetyl-CoA and CO(2).
Subcellular location: Mitochondrion matrix.
Interaction partners:
- Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex, mitochondrial
- Dihydrolipoyl dehydrogenase, mitochondrial
- Pyruvate dehydrogenase E1 component subunit beta, mitochondrial
- Pyruvate dehydrogenase complex protein X component, mitochondrial
- Pyruvate kinase 1
- Pyruvate decarboxylase isozyme 1
- Glucose-6-phosphate isomerase
- NAD-dependent malic enzyme, mitochondrial
- Pyruvate carboxylase 2
- Pyruvate kinase 2
Sequence:
MLAASFKRQPSQLVRGLGAVLRTPTRIGHVRTMATLKTTDKKAPEDIEGSDTVQIELPESSFESYMLEPPDLSYETSKATLLQMYKDMVIIRRMEMACDALYKAKKIRGFCHLSVGQEAIAVGIENAITKLDSIITSYRCHGFTFMRGASVKAVLAELMGRRAGVSYGKGGSMHLYAPGFYGGNGIVGAQVPLGAGLAFAHQYKNEDACSFTLYGDGASNQGQVFESFNMAKLWNLPVVFCCENNKYGMGTAASRSSAMTEYFKRGQYIPGLKVNGMDILAVYQASKFAKDWCLSGKGPLVLEYETYRYGGHSMSDPGTTYRTRDEIQHMRSKNDPIAGLKMHLIDLGIATEAEVKAYDKSARKYVDEQVELADAAPPPEAKLSILFEDVYVKGTETPTLRGRIPEDTWDFKKQGFASRD
Protein: Heat shock protein 22 (P02515)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Heat shock protein 68
- Major heat shock 70 kDa protein Aa
- Heat shock protein 83
- Major heat shock 70 kDa protein Ba
- Major heat shock 70 kDa protein Bbb
- MAP kinase-activated protein kinase 2
- Heat shock factor protein
- IP07647p
- Heat shock 70 kDa protein cognate 2
Sequence:
MRSLPMFWRMAEEMARMPRLSSPFHAFFHEPPVWSVALPRNWQQIARWQEQEFAPPATVNKDGYKLTLDVKDYSELKVKVLDESVVLVEGKSEQQEAEQGGYSSRHFLRRFVLPEGYEADKVTSTLSSDGVLTISVPNPPGVQETLKEREVTIEQTGEPAKKSAEEPNDKAASQ
Protein: RNA polymerase I-specific transcription initiation factor rrn5 (O14013)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Component of the UAF (upstream activation factor) complex which interacts with the upstream element of the RNA polymerase I promoter and forms a stable preinitiation complex. UAF seems to stimulate basal transcription to a fully activated level.
Subcellular location: Nucleus, nucleolus {ECO:0000269|PubMed:10759889, ECO:0000269|PubMed:16823372, ECO:0000269|PubMed:17538026}.
Interaction partners:
- RNA polymerase I-specific transcription initiation factor rrn10
- RNA polymerase I-specific transcription initiation factor rrn11
- RNA polymerase I-specific transcription initiation factor RRN9 homolog
- RNA polymerase I-specific transcription initiation factor rrn7
- Upstream activation factor subunit spp27
- TATA-box-binding protein
- RNA polymerase I-specific transcription initiation factor rrn3
- Uncharacterized protein C3B8.11
Sequence:
MSSSINGLNESEGSTPLSTASIIGSSEQLYMTHDERYLDVLQQYEVETENKRDFDLEEEQWGVLSGSCVDGTYWSAEEKELFFQAVARNGKRDLDLIAYSIPSKSAVQIERYINALENELRWLRNHVDASVRSQCLLKYEDIPIAMEMSQNWIDWEEKIAERLLEGSNISGVETSHYNAQSVKNKTSNEDLFDTNEMRKISERFYHFDRQAPFPSNPLSAGATEFLLQIIKSKLKELIGTSIFLAESRFRKLEANNAFHRKPIIKNRDVVLSGKFLRFHRFNIPGFWKYLPTRQKMNVYKRNKRLKFQNYIHIMESDERQSKLKLGRVRARKTKNNENTMFFDSKEHSTDESDGNLGEHDVKRKVDSVPADETSINGFKKSVNQAEYPDNAQMFMDESVAEESLVEIDDSVEAYDMIQSKNYESFVWKYVLHLTDEMSTEDALFETIPLSNLLAQKRMKDKLKGSDVFTTLKITSKSLHNIDEHSDSDDEVQPICYYYKDPVVSHAPGAAEVVSELESGYVGLISYDLSNLPNSTEDPERKLAKPVSSWELSLPLK
Protein: Gene 0.4 protein (Gene product 0.4) (Gp0.4) (P03776)
Organism: Escherichia phage T7 (Bacteriophage T7)
Function: Plays a role in the inhibition of host cell division. Interacts with and inhibits the major host cytoskeletal protein in bacterial division FtsZ to confer growth advantage to the phage.
Interaction partners:
Sequence:
MSTTNVQYGLTAQTVLFYSDMVRCGFNWSLAMAQLKELYENNKAIALESAE
Protein: Protein phosphatase 1 regulatory subunit 3C (T1SFR8)
Organism: Clarias batrachus (Walking catfish) (Silurus batrachus)
Function: Acts as a glycogen-targeting subunit for PP1 and regulates its activity. Activates glycogen synthase, reduces glycogen phosphorylase activity and limits glycogen breakdown.
Interaction partners:
Sequence:
MPVDMAVQLYITSSPPLHHRFLSSYKDYRVRNLISVNCKPLRPCINTKNTHNTSLNPPCSVWKAPEPKAKKKVVFADSKGMSLTAVRVFSPCENKKSDSQVQFQLPKLEVALKPVQSRILAFRQPATEYMEFRKRLMKNSVCLESCTLQGHTLTGTIKVRNVSFEKSVQVRITFDSWENHRDIECTFLNDVCGCRDTDTFSFIIEIPACVLPQDSVEFCVSYTCGGKTHWDNNNGKNYALVTTHDEKKDKTKETDLLDPFRNQQKRNRFTADWNSLMIGIRGPTW
Protein: Iron ABC transporter substrate-binding protein (Q5FA17)
Organism: Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090)
Subcellular location: Cell envelope {ECO:0000256|ARBA:ARBA00004196}.
Interaction partners:
- Fe3+ dicitrate ABC transporter permease
- Fe
Sequence:
MKTSIRYALLAAALTAATPALADITVYNGQHKEAAQAVADAFTRATGIKVKLNSAKGDQLAGQIKEEGSRSPADVFYSEQIPALATLSAANLLEPLPASTINETRGKGVPVAAKKDWVALSGRSRVVVYDTRKLSEKDLEKSVLNYATPKWKNRIGYVPTSGAFLEQIVAIVKLKGEAAALKWLKGLKEYGKPYAKNSVALQAVENGEIDAALINNYYWHAFAREKGVQNVHTRLNFVRHRDPGALVTYSGAAVLKSSQNKDEAKKFVAFLAGKEGQRALTAVRAEYPLNPHVVSTFNLEPIAKLEAPQVSATTVSEKEHATRLLEQAGMK
Protein: Putative tyrosine-protein phosphatase TPTE (EC 3.1.3.48) (Cancer/testis antigen 44) (CT44) (Transmembrane phosphatase with tensin homology) (Tumor antigen BJ-HCC-5) (P56180)
Organism: Homo sapiens (Human)
Function: Could be involved in signal transduction.
Subcellular location: Membrane; Multi-pass membrane protein.
Interaction partners:
- DNA-dependent metalloprotease SPRTN
- Serine/threonine-protein kinase Nek3
- Melanoma-associated antigen 3
- Cancer/testis antigen 1
Sequence:
MNESPDPTDLAGVIIELGPNDSPQTSEFKGATEEAPAKESPHTSEFKGAARVSPISESVLARLSKFEVEDAENVASYDSKIKKIVHSIVSSFAFGLFGVFLVLLDVTLILADLIFTDSKLYIPLEYRSISLAIALFFLMDVLLRVFVERRQQYFSDLFNILDTAIIVILLLVDVVYIFFDIKLLRNIPRWTHLLRLLRLIILLRIFHLFHQKRQLEKLIRRRVSENKRRYTRDGFDLDLTYVTERIIAMSFPSSGRQSFYRNPIKEVVRFLDKKHRNHYRVYNLCSERAYDPKHFHNRVVRIMIDDHNVPTLHQMVVFTKEVNEWMAQDLENIVAIHCKGGTDRTGTMVCAFLIASEICSTAKESLYYFGERRTDKTHSEKFQGVKTPSQKRYVAYFAQVKHLYNWNLPPRRILFIKHFIIYSIPRYVRDLKIQIEMEKKVVFSTISLGKCSVLDNITTDKILIDVFDGLPLYDDVKVQFFYSNLPTYYDNCSFYFWLHTSFIENNRLYLPKNELDNLHKQKARRIYPSDFAVEILFGEKMTSSDVVAGSD
Protein: Transmembrane protein 204 (Claudin-like protein 24) (Q7TQI0)
Organism: Mus musculus (Mouse)
Function: Can influence paracellular permeability. Appears to be involved in cell-cell interactions through adherens (By similarity).
Subcellular location: Cell junction, adherens junction. Cell membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Note=Co-localizes with the beta-catenin adherins. {ECO:0000250}.
Interaction partners:
- Vascular endothelial growth factor receptor 2
- Vascular endothelial growth factor receptor 3
Sequence:
MTLQKLVATAVLVALVSLILNNAAAFTPNWVYQTLEDGRKRSVGLWKSCWLVDRGKGVTSPGTRTGQVDTHDCEVLGWGSESAGFQESRGTVKLQFDMMRACNLVATAALVVGQITFILGLTGLPLMSPESQCWEEAMAAAFQLASFVLVIGLVTFYRIGPYTNLSWSCYLNIGACLLATLAAAMLIWNILHRREDCMAPRVIVISRSLTARFRRGLDNDYVESPC
Protein: Protein disulfide-isomerase (EC 5.3.4.1) (Q4WH99)
Organism: Aspergillus fumigatus (strain ATCC MYA-4609 / CBS 101355 / FGSC A1100 / Af293) (Neosartorya fumigata)
Subcellular location: Endoplasmic reticulum lumen {ECO:0000256|ARBA:ARBA00004319}.
Interaction partners:
- Oxidoreductin
- Calnexin homolog
- Endoplasmic reticulum chaperone BiP
- Oxidoreductase, 2OG-Fe
- Peptidyl-prolyl cis-trans isomerase B
- Hsp70 family chaperone Lhs1/Orp150, putative
- Tryptophan synthase
- tryptophan synthase
- Protein transport protein Sec61 alpha subunit, putative
- alpha-1,2-Mannosidase
Sequence:
MRSFAPLVLSLLGASAVASADATADTTSDVVSLTKDSFKDFMKEHDLVLAEFYAPWCGHCKALAPKYEEAATELKGKNIPLVKVDCTEEEDLCKENGVEGYPTLKIFRGPDSSKPYQGARQADSIVSYMIKQSLPAVSTVTEENLEEIKTMDKIVVIGYFASDDKAANDVFTSFAESQRDNYLFAATSDSAIAKAEGVKQPSIVLYKDFDEKKAVYDGAIEQEAILSWVKTASTPLVGEIGPETYSSYITAGIPLAYIFAETKEERDQYAEDFKPVAEKHKGAINIATIDAKMFGAHAGNLNLDPQTFPAFAIQDPEKNAKYPYDQSREFNAKEIGKFIQDVLDGKVEPSIKSEPIPETQEGPVTVVVAHSYQDIVINNDKDVLLEFYAPWCGHCKALAPKYEELAALYAGDFKDKVTIAKIDATANDVPDSITGFPTIKLYPAGAKDSPVEYSGSRTVEDLANFIKENGKYKVDALVAASEKVEEGPDVTASPSATSTEAEAPAATGDEKGDHDEL
Protein: Sister chromatid cohesion protein (Q385C7)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- DNA polymerase eta
- Structural maintenance of chromosomes protein
- Structural maintenance of chromosomes protein
- SCD domain-containing protein
- Double-strand-break repair protein rad21 homolog, putative
- EF-hand domain-containing protein
- Structural maintenance of chromosomes protein
- N-acetyltransferase ESCO acetyl-transferase domain-containing protein
- Uncharacterized protein
- Sister chromatid cohesion protein
Sequence:
MSLGKVLRSKRSSGHAAAQLAAAKEKKPRLEEEDASILSGSLLQEKADAQLLQWLFKCHRFLRNVQPPFSLDKTFLEELLSPRYLNSSIAGVQQITGCLLSDLVRLHNSPADKMAETQLPFRRTRADDVLTCLVAPFVEVVRDGKPLKTCENIIERASVSRVFVHVIPSCKLPLDERLTYLFASVLHASGTPAPGASTSSTSSAITTTTASEMAKILNDVLLTTTAITREQLSPLLKVIVTASPALLRCAAANRARGGSGVETICPRANKEPSSRQSLGAIIAARVLLGQVDVIPPAISDFVTDMVKEGVSMLLSAKGTGNDKDASSQGLRDISRAMEFLVALTELHVDLVCQLVPSLEPYLQHLHDEVRLFLLRGFFTALGAHEAAIRVYRSTFNVLLERFEDTAHPLRIEMLELSVEAVRSELARLGTTENLLISGEIVQHVEQRLVDVNAQVRRAAVIAYGRIVAAAPSLVKGERLQETLAPLIADKNFRVRQVAVEHLCIIYRRESYPWIPEAVLECPSWEGGVMLLETLFETMLPPPKVARETAPQGGAALAQSQLQGLQRKRRNIPIFDFEKETSHEPTYANCLAVLCGDMSPECFDRLLVFAGKKARVRLSVLRLFQLREEGRNIDLRSAEGQEVANKAHRILKFLVGISHSQHGEWNALFLAKDDRVSRAFINCCSEGVTRCATERERLIRGLEGRVDKHVLKFVQDSLSKQMMLPTEVEDVEELLARLGDICRLGRESKPPKPCATLQGKVNGLLRALLFCCRSTPAFLPACVGPLVELLEKACAGVTACATPSNVLLTLFCITDWARYVSQYGEKESKQAIFPGGGDTATVVRNCGLVKTLCTLCERPGGPLLNDVAPVMQGKVCKQAARCLIAIARIRGLEQFCKVGELANTLAHHIRHSAAEINNGAVCLLKALSVFIKDPCAQRSVKGGSLVPAVTNYLLVAARDKSSDSETPHMKAKCLELPSMSLASAVVDAAAKCLSALSTYVPSEGDGSISTNEVLDTLLSAYKLVGEFDSQSIRACLRRRSINQQLLKLIVHPSSTIERALAVAVVLSAESETAVRRAIQHKVFRHVTNGRCDMRYVACLILTAISEETKSDYQQLRDVLCKVGNHLRSRQTQSGATLSSREALSCFPEYSIPFLVLFMAHHTFYESESDSHFIAYQRVWHLLFDELFRQNAQCASFVMELFSRIKQTDDKLDNHGSKKARLICDLGIRVMQECMGKKQINVEALRRYPGSIQLPGFFVKSEAGSEALNTVYLGSHVLIPSHVPFRVPTASPAATSPEEHRDATVSPALTVGEGDNEANEK