wanglab/gogpt-training-data huggingface dataset:
Protein: Pikromycin polyketide synthase component PikAIV (Pikromycin PKS component PikAIV) (EC 2.3.1.239) (EC 2.3.1.240) (Narbonolide/10-deoxymethynolide synthase PikA4, module 6) (Narbonolide/10-deoxymethynolide synthase PikAIV) (Type I modular polyketide synthase PikAIV) (PKS) (Q9ZGI2)
Organism: Streptomyces venezuelae
Function: Involved in the biosynthesis of 12- and 14-membered ring macrolactone antibiotics such as methymycin and neomethymycin, and pikromycin and narbomycin, respectively. Component of the pikromycin PKS which catalyzes the biosynthesis of both precursors 10-deoxymethynolide (12-membered ring macrolactone) and narbonolide (14-membered ring macrolactone). Chain elongation through PikAI, PikAII and PikAIII followed by thioesterase catalyzed termination results in the production of 10-deoxymethynolide, while continued elongation through PikAIV, followed by thioesterase (TE) catalyzed cyclization results in the biosynthesis of the narbonolide. The thioesterase can use a series of diketide-N-acetylcysteamine (SNAC) thioesters, but has a strong preference for the 2-methyl-3-ketopentanoyl-SNAC over the stereoisomers of 2-methyl-3-hydroxyacyl-SNAC.
Interaction partners:
Sequence:
MTSSNEQLVDALRASLKENEELRKESRRRADRRQEPMAIVGMSCRFAGGIRSPEDLWDAVAAGKDLVSEVPEERGWDIDSLYDPVPGRKGTTYVRNAAFLDDAAGFDAAFFGISPREALAMDPQQRQLLEASWEVFERAGIDPASVRGTDVGVYVGCGYQDYAPDIRVAPEGTGGYVVTGNSSAVASGRIAYSLGLEGPAVTVDTACSSSLVALHLALKGLRNGDCSTALVGGVAVLATPGAFIEFSSQQAMAADGRTKGFASAADGLAWGEGVAVLLLERLSDARRKGHRVLAVVRGSAINQDGASNGLTAPHGPSQQHLIRQALADARLTSSDVDVVEGHGTGTRLGDPIEAQALLATYGQGRAPGQPLRLGTLKSNIGHTQAASGVAGVIKMVQALRHGVLPKTLHVDEPTDQVDWSAGSVELLTEAVDWPERPGRLRRAGVSAFGVGGTNAHVVLEEAPAVEESPAVEPPAGGGVVPWPVSAKTSAALDAQIGQLAAYAEDRTDVDPAVAARALVDSRTAMEHRAVAVGDSREALRDALRMPEGLVRGTVTDPGRVAFVFPGQGTQWAGMGAELLDSSPEFAAAMAECETALSPYVDWSLEAVVRQAPSAPTLDRVDVVQPVTFAVMVSLAKVWQHHGITPEAVIGHSQGEIAAAYVAGALTLDDAARVVTLRSKSIAAHLAGKGGMISLALSEEATRQRIENLHGLSIAAVNGPTATVVSGDPTQIQELAQACEADGIRARIIPVDYASHSAHVETIENELADVLAGLSPQTPQVPFFSTLEGTWITEPALDGGYWYRNLRHRVGFAPAVETLATDEGFTHFIEVSAHPVLTMTLPDKVTGLATLRREDGGQHRLTTSLAEAWANGLALDWASLLPATGALSPAVPDLPTYAFQHRSYWISPAGPGEAPAHTASGREAVAETGLAWGPGAEDLDEEGRRSAVLAMVMRQAASVLRCDSPEEVPVDRPLREIGFDSLTAVDFRNRVNRLTGLQLPPTVVFQHPTPVALAERISDELAERNWAVAEPSDHEQAEEEKAAAPAGARSGADTGAGAGMFRALFRQAVEDDRYGEFLDVLAEASAFRPQFASPEACSERLDPVLLAGGPTDRAEGRAVLVGCTGTAANGGPHEFLRLSTSFQEERDFLAVPLPGYGTGTGTGTALLPADLDTALDAQARAILRAAGDAPVVLLGHSGGALLAHELAFRLERAHGAPPAGIVLVDPYPPGHQEPIEVWSRQLGEGLFAGELEPMSDARLLAMGRYARFLAGPRPGRSSAPVLLVRASEPLGDWQEERGDWRAHWDLPHTVADVPGDHFTMMRDHAPAVAEAVLSWLDAIEGIEGAGK
Protein: Contactin-1 (Glycoprotein gp135) (Neural cell surface protein F3) (Q12860)
Organism: Homo sapiens (Human)
Function: Contactins mediate cell surface interactions during nervous system development. Involved in the formation of paranodal axo-glial junctions in myelinated peripheral nerves and in the signaling between axons and myelinating glial cells via its association with CNTNAP1. Participates in oligodendrocytes generation by acting as a ligand of NOTCH1. Its association with NOTCH1 promotes NOTCH1 activation through the released notch intracellular domain (NICD) and subsequent translocation to the nucleus. Interaction with TNR induces a repulsion of neurons and an inhibition of neurite outgrowth (By similarity).
Subcellular location: [Isoform 1]: Cell membrane; Lipid-anchor, GPI-anchor; Extracellular side.; SUBCELLULAR LOCATION: [Isoform 2]: Cell membrane; Lipid-anchor, GPI-anchor; Extracellular side.
Interaction partners:
- Contactin-associated protein 1
- Neurofascin
- Receptor-type tyrosine-protein phosphatase zeta
- Neuronal cell adhesion molecule
- Neural cell adhesion molecule L1
- Receptor-type tyrosine-protein phosphatase beta
- Neurogenic locus notch homolog protein 2
- Amyloid-beta precursor protein
- Neurogenic locus notch homolog protein 1
- E3 ubiquitin-protein ligase DTX1
Sequence:
MKMWLLVSHLVIISITTCLAEFTWYRRYGHGVSEEDKGFGPIFEEQPINTIYPEESLEGKVSLNCRARASPFPVYKWRMNNGDVDLTSDRYSMVGGNLVINNPDKQKDAGIYYCLASNNYGMVRSTEATLSFGYLDPFPPEERPEVRVKEGKGMVLLCDPPYHFPDDLSYRWLLNEFPVFITMDKRRFVSQTNGNLYIANVEASDKGNYSCFVSSPSITKSVFSKFIPLIPIPERTTKPYPADIVVQFKDVYALMGQNVTLECFALGNPVPDIRWRKVLEPMPSTAEISTSGAVLKIFNIQLEDEGIYECEAENIRGKDKHQARIYVQAFPEWVEHINDTEVDIGSDLYWPCVATGKPIPTIRWLKNGYAYHKGELRLYDVTFENAGMYQCIAENTYGAIYANAELKILALAPTFEMNPMKKKILAAKGGRVIIECKPKAAPKPKFSWSKGTEWLVNSSRILIWEDGSLEINNITRNDGGIYTCFAENNRGKANSTGTLVITDPTRIILAPINADITVGENATMQCAASFDPALDLTFVWSFNGYVIDFNKENIHYQRNFMLDSNGELLIRNAQLKHAGRYTCTAQTIVDNSSASADLVVRGPPGPPGGLRIEDIRATSVALTWSRGSDNHSPISKYTIQTKTILSDDWKDAKTDPPIIEGNMEAARAVDLIPWMEYEFRVVATNTLGRGEPSIPSNRIKTDGAAPNVAPSDVGGGGGRNRELTITWAPLSREYHYGNNFGYIVAFKPFDGEEWKKVTVTNPDTGRYVHKDETMSPSTAFQVKVKAFNNKGDGPYSLVAVINSAQDAPSEAPTEVGVKVLSSSEISVHWEHVLEKIVESYQIRYWAAHDKEEAANRVQVTSQEYSARLENLLPDTQYFIEVGACNSAGCGPPSDMIEAFTKKAPPSQPPRIISSVRSGSRYIITWDHVVALSNESTVTGYKVLYRPDGQHDGKLYSTHKHSIEVPIPRDGEYVVEVRAHSDGGDGVVSQVKISGAPTLSPSLLGLLLPAFGILVYLEF
Protein: Cobra venom factor (CVF) (CVFk) (Complement C3 homolog) [Cleaved into: Cobra venom factor alpha chain; Cobra venom factor gamma chain; Cobra venom factor beta chain] (Q91132)
Organism: Naja kaouthia (Monocled cobra) (Naja siamensis)
Function: Complement-activating protein in cobra venom. It is a structural and functional analog of complement component C3b, the activated form of C3. It binds factor B (CFB), which is subsequently cleaved by factor D (CFD) to form the bimolecular complex CVF/Bb. CVF/Bb is a C3/C5 convertase that cleaves both complement components C3 and C5. Structurally, it resembles the C3b degradation product C3c, which is not able to form a C3/C5 convertase. Unlike C3b/Bb, CVF/Bb is a stable complex and completely resistant to the actions of complement regulatory factors H (CFH) and I (CFI). Therefore, CVF continuously activates complement resulting in the depletion of complement activity.
Subcellular location: Secreted.
Interaction partners:
Sequence:
MERMALYLVAALLIGFPGSSHGALYTLITPAVLRTDTEEQILVEAHGDSTPKQLDIFVHDFPRKQKTLFQTRVDMNPAGGMLVTPTIEIPAKEVSTDSRQNQYVVVQVTGPQVRLEKVVLLSYQSSFLFIQTDKGIYTPGSPVLYRVFSMDHNTSKMNKTVIVEFQTPEGILVSSNSVDLNFFWPYNLPDLVSLGTWRIVAKYEHSPENYTAYFDVRKYVLPSFEVRLQPSEKFFYIDGNENFHVSITARYLYGEEVEGVAFVLFGVKIDDAKKSIPDSLTRIPIIDGDGKATLKRDTFRSRFPNLNELVGHTLYASVTVMTESGSDMVVTEQSGIHIVASPYQIHFTKTPKYFKPGMPYELTVYVTNPDGSPAAHVPVVSEAFHSMGTTLSDGTAKLILNIPLNAQSLPITVRTNHGDLPRERQATKSMTAIAYQTQGGSGNYLHVAITSTEIKPGDNLPVNFNVKGNANSLKQIKYFTYLILNKGKIFKVGRQPRRDGQNLVTMNLHITPDLIPSFRFVAYYQVGNNEIVADSVWVDVKDTCMGTLVVKGDNLIQMPGAAMKIKLEGDPGARVGLVAVDKAVYVLNDKYKISQAKIWDTIEKSDFGCTAGSGQNNLGVFEDAGLALTTSTNLNTKQRSAAKCPQPANRRRRSSVLLLDSNASKAAEFQDQDLRKCCEDVMHENPMGYTCEKRAKYIQEGDACKAAFLECCRYIKGVRDENQRESELFLARDDNEDGFIADSDIISRSDFPKSWLWLTKDLTEEPNSQGISSKTMSFYLRDSITTWVVLAVSFTPTKGICVAEPYEIRVMKVFFIDLQMPYSVVKNEQVEIRAILHNYVNEDIYVRVELLYNPAFCSASTKGQRYRQQFPIKALSSRAVPFVIVPLEQGLHDVEIKASVQEALWSDGVRKKLKVVPEGVQKSIVTIVKLDPRAKGVGGTQLEVIKARKLDDRVPDTEIETKIIIQGDPVAQIIENSIDGSKLNHLIITPSGCGEQNMIRMAAPVIATYYLDTTEQWETLGINRRTEAVNQIVTGYAQQMVYKKADHSYAAFTNRASSSWLTAYVVKVFAMAAKMVAGISHEIICGGVRWLILNRQQPDGAFKENAPVLSGTMQGGIQGAEEEVYLTAFILVALLESKTICNDYVNSLDSSIKKATNYLLKKYEKLQRPYTTALTAYALAAADQLNDDRVLMAASTGRDHWEEYNAHTHNIEGTSYALLALLKMKKFDQTGPIVRWLTDQNFYGETYGQTQATVMAFQALAEYEIQMPTHKDLNLDITIELPDREVPIRYRINYENALLARTVETKLNQDITVTASGDGKATMTILTFYNAQLQEKANVCNKFHLNVSVENIHLNAMGAKGALMLKICTRYLGEVDSTMTIIDISMLTGFLPDAEDLTRLSKGVDRYISRYEVDNNMAQKVAVIIYLNKVSHSEDECLHFKILKHFEVGFIQPGSVKVYSYYNLDEKCTKFYHPDKGTGLLNKICIGNVCRCAGETCSSLNHQERIDVPLQIEKACETNVDYVYKTKLLRIEEQDGNDIYVMDVLEVIKQGTDENPRAKTHQYISQRKCQEALNLKVNDDYLIWGSRSDLLPTKDKISYIITKNTWIERWPHEDECQEEEFQKLCDDFAQFSYTLTEFGCPT
Protein: Sugar ABC transporter substrate-binding protein (A0A0F6SRJ0)
Organism: [Brevibacterium] flavum
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
Interaction partners:
Sequence:
MGINRISQGSAPKLGVRSTRQRKAVIDVLEEIDNFASAKEIHHELSTREHNVGLTTVYRTLQSLADIGAVDVLTVTGGETLYRQCHDEGHHHHLVCTNCGRTVEIDGGPVETWAQEIATKNGFALSSHEAEIFGLCTDCKEEVT
Protein: A1 cistron-splicing factor AAR2 (P32357)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Component of the U5 snRNP complex that is required for spliceosome assembly and for pre-mRNA splicing. Involved in splicing pre-mRNA of the A1 cistron and other genes that are important for cell growth.
Subcellular location: Cytoplasm. Nucleus. Note=This protein lacks a nuclear localization signal, it may interact in the cytoplasm with a component of spliceosomes via the leucine-zipper and then be transported into the nucleus.
Interaction partners:
- Pre-mRNA-splicing factor 8
- Pre-mRNA-splicing factor SNU114
- Pre-mRNA-splicing helicase BRR2
- U1 small nuclear ribonucleoprotein A
- Protein LIN1
- Pre-mRNA-splicing ATP-dependent RNA helicase PRP28
- Small nuclear ribonucleoprotein-associated protein B
- Spliceosomal protein DIB1
- Small nuclear ribonucleoprotein Sm D1
- Small nuclear ribonucleoprotein F
Sequence:
MNTVPFTSAPIEVTIGIDQYSFNVKENQPFHGIKDIPIGHVHVIHFQHADNSSMRYGYWFDCRMGNFYIQYDPKDGLYKMMEERDGAKFENIVHNFKERQMMVSYPKIDEDDTWYNLTEFVQMDKIRKIVRKDENQFSYVDSSMTTVQENELLKSSLQKAGSKMEAKNEDDPAHSLNYTVINFKSREAIRPGHEMEDFLDKSYYLNTVMLQGIFKNSSNYFGELQFAFLNAMFFGNYGSSLQWHAMIELICSSATVPKHMLDKLDEILYYQIKTLPEQYSDILLNERVWNICLYSSFQKNSLHNTEKIMENKYPELLGKDNEDDALIYGISDEERDDEDDEHNPTIVGGLYYQRP
Protein: phenylalanine 4-monooxygenase (EC 1.14.16.1) (Q6WRI4)
Organism: Leishmania major
Interaction partners:
- 4a-hydroxytetrahydrobiopterin dehydratase
- Aspartate aminotransferase
- Transaminase A
- Dihydropteridine reductase
- Dihydropteridine reductase
- Tyrosine aminotransferase
Sequence:
MLLRSRLFLEAGMAAAAATLKAQYASPGSNIKGADKKTRCRTSLQVSLSTDKPGELCHLLSVFKPYSINISQVANRPRAYENKAPLRTIFLDVDAYIEDESMKKVMAELHAKFPNVVVTGSWVIPWYPTEPKDLDELDQSTLAAGEELQEDPENPHPGFHDEVYRARRREIVGLAKNYKTGDPIPIVNYTEEENRVWTVVYDHLTRLYPTHACQQYNYVFPLLLENGVLSRTKTPQLRDVSEFLNEATGFTVRPVTGLLTSRDFLNALAFRVFYSTQYIRHAAQPLYTPEPDMVHDIIGHLPLLSDPDFANFTQTIGLASLGASDELLDKLAKVYWYSVEFGLCSEGGRRKAYGAGILSSCGELEYALSDKPECVPWDPTMASKTPFPITKYQPLYFVAESFSDAQRKLEAWLSSQEKPLYTVYNSYSRRVQSYPKNTWNMLQEQMKRTNFTF
Protein: adenylate cyclase (EC 4.6.1.1) (A0A384P5Q5)
Organism: Homo sapiens (Human)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004651}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}. Cell projection, cilium {ECO:0000256|ARBA:ARBA00004138}.
Interaction partners:
Sequence:
MSGSKSVSPPGYAAQKTAAPAPRGGPEHRSAWGEADSRANGYPHAPGGSARGSTKKPGGAVTPQQQQRLASRWRSDDDDDPPLSGDDPLAGGFGFSFRSKSAWQERGGDDCGRGSRRQRRGAASGGSTRAPPAGGGGGSAAAAASAGGTEVRPRSVEVGLEERRGKGRAADELEAGAVEGGEGSGDGGSSADSGSGAGPGAVLSLGACCLALLQIFRSKKFPSDKLERLYQRYFFRLNQSSLTMLMAVLVLVCLVMLAFHAARPPLQLPYLAVLAAAVGVILIMAVLCNRAAFHQDHMGLACYALIAVVLAVQVVGLLLPQPRSASEGIWWTVFFIYTIYTLLPVRMRAAVLSGVLLSALHLAIALRTNAQDQFLLKQLVSNVLIFSCTNIVGVCTHYPAEVSQRQAFQETRECIQARLHSQRENQQQERLLLSVLPRHVAMEMKADINAKQEDMMFHKIYIQKHDNVSILFADIEGFTSLASQCTAQELVMTLNELFARFDKLAAENHCLRIKILGDCYYCVSGLPEARADHAHCCVEMGMDMIEAISLVREVTGVNVNMRVGIHSGRVHCGVLGLRKWQFDVWSNDVTLANHMEAGGKAGRIHITKATLNYLNGDYEVEPGCGGERNAYLKEHSIETFLILRCTQKRKEEKAMIAKMNRQRTNSIGHNPPHWGAERPFYNHLGGNQVSKEMKRMGFEDPKDKNAQESANPEDEVDEFLGRAIDARSIDRLRSEHVRKFLLTFREPDLEKKYSKQVDDRFGAYVACASLVFLFICFVQITIVPHSIFMLSFYLTCSLLLTLVVFVSVIYSCVKLFPSPLQTLSRKIVRSKMNSTLVGVFTITLVFLAAFVNMFTCNSRDLLGCLAQEHNISASQVNACHVAESAVNYSLGDEQGFCGSPWPNCNFPEYFTYSVLLSLLACSVFLQISCIGKLVLMLAIELIYVLIVEVPGVTLFDNADLLVTANAIDFFNNGTSQCPEHATKVALKVVTPIIISVFVLALYLHAQQVESTARLDFLWKLQATEEKEEMEELQAYNRRLLHNILPKDVAAHFLARERRNDELYYQSCECVAVMFASIANFSEFYVELEANNEGVECLRLLNEIIADFDEIISEDRFRQLEKIKTIGSTYMAASGLNDSTYDKVGKTHIKALADFAMKLMDQMKYINEHSFNNFQMKIGLNIGPVVAGVIGARKPQYDIWGNTVNVASRMDSTGVPDRIQVTTDMYQVLAANTYQLECRGVVKVKGKGEMMTYFLNGGPPLS
Protein: Protocadherin-8 (Arcadlin) (O95206)
Organism: Homo sapiens (Human)
Function: Calcium-dependent cell-adhesion protein (By similarity). May play a role in activity-induced synaptic reorganization underlying long term memory (By similarity). Could be involved in CDH2 internalization through TAOK2/p38 MAPK pathway. In hippocampal neurons, may play a role in the down-regulation of dendritic spines, maybe through its action on CDH2 endocytosis (By similarity).
Subcellular location: Cell membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}. Cell projection, dendrite {ECO:0000250}. Presynaptic cell membrane. Postsynaptic cell membrane. Note=Also expressed in neuronal cell bodies. Localized to excitatory, but not with inhibitory, synapses. {ECO:0000250}.
Interaction partners:
- Divergent protein kinase domain 2A
Sequence:
MSPVRRWGSPCLFPLQLFSLCWVLSVAQSKTVRYSTFEEDAPGTVIGTLAEDLHMKVSGDTSFRLMKQFNSSLLRVREGDGQLTVGDAGLDRERLCGQAPQCVLAFDVVSFSQEQFRLVHVEVEVRDVNDHAPRFPRAQIPVEVSEGAAVGTRIPLEVPVDEDVGANGLQTVRLAEPHSPFRVELQTRADGAQCADLVLLQELDRESQAAYSLELVAQDGGRPPRSATAALSVRVLDANDHSPAFPQGAVAEVELAEDAPVGSLLLDLDAADPDEGPNGDVVFAFGARTPPEARRLFRLDPRSGRLTLAGPVDYERQDTYELDVRAQDRGPGPRAATCKVIVRIRDVNDNAPDIAITPLAAPGAPATSPFAAAAAAAALGGADASSPAGAGTPEAGATSLVPEGAARESLVALVSTSDRDSGANGQVRCALYGHEHFRLQPAYAGSYLVVTAASLDRERIAEYNLTLVAEDRGAPPLRTVRPYTVRVGDENDNAPLFTRPVYEVSVRENNPPGAYLATVAARDRDLGRNGQVTYRLLEAEVGRAGGAVSTYVSVDPATGAIYALRSFDYETLRQLDVRIQASDGGSPQLSSSALVQVRVLDQNDHAPVLVHPAPANGSLEVAVPGRTAKDTVVARVQARDADEGANGELAFELQQQEPREAFAIGRRTGEILLTGDLSQEPPGRVFRALLVISDGGRPPLTTTATVSFVVTAGGGRGPAAPASAGSPERSRPPGSRLGVSGSVLQWDTPLIVIIVLAGSCTLLLAAIIAIATTCNRRKKEVRKGGALREERPGAAGGGASAPGSPEEAARGAGPRPNMFDVLTFPGTGKAPFGSPAADAPPPAVAAAEVPGSEGGSATGESACHFEGQQRLRGAHAEPYGASPGFGKEPAPPVAVWKGHSFNTISGREAEKFSGKDSGKGDSDFNDSDSDISGDALKKDLINHMQSGLWACTAECKILGHSDRCWSPSCSGPNAHPSPHPPAQMSTFCKSTSLPRDPLRRDNYYQAQLPKTVGLQSVYEKVLHRDYDRTVTLLSPPRPGRLPDLQEIGVPLYQSPPGRYLSPKKGANENV
Protein: Bromodomain and PHD finger containing, 1 (Peregrin) (Q803M2)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
Sequence:
MGLDFDVKTFCHNLRATKPPYECPVESCRKVYKSYSGIEYHLYHYDHENPPPPPQGTPQKKRKGRPPRGSSDGPDSSTGPGATSGQNTAPSSPAERSERSHSPVRETMTYAEAQRMVEMEIRGRVHRVSIFQNLDVVSEEDSGAEEPPGATGSTAAACNGGGESGGGDRMDTANGEKGAQKTGKHKSKEKKKDSGAHHHINTSGPAVKLPEVVFRELDQDRPDAPPRPMSYYRYIDKSAEELDEEVEYDIDEEDYIWLDIMNEKRRSDGVAPIPQEVFEYLMDRLEKESYFESHNKGDPSALIDEDAVCCICNDGECQNSNVILFCDMCNLAVHQECYGVPYIPEGQWLCRRCPQSPSRAVDCALCPNKGGAFKQTDDSRWAHVVCALWIPEVCFANTVFLEPIDSIEHIPPARWKLTCYICKQRGSGACIQCHKANCYTAFHVTCAQQAGLYMKMEPVRETGANGTSFSVRKTAYCDIHTPPGSARPLGGVGGVSADSSRSEAEPEEEEEPPAAEDDGKGWSSERAKRAKAKSRLKMKRARKILAERRAAAPVLSVPCIPPHKLSKITSNLTVQRKSQFMQRLHSYWTLKRQSRNGVPLLRRLQTHLQSQRNTEPLPVTRDGEEKHSVLKEQLKAWQRLRHDLERARLLVELIRKREKLKRETIKVQEMAMEMQLTPLLVLLRRTLEQLQERDTNNFFTEPVPLSEVPDYLDHIERPMDFHKMWKCVESHRYLSFEAFEGDFLQIVNNCLKYNAKDTVFYRAALRLREAGGVVLRQARRQAERIGFDYETGLHLHREPSPENTHTHQRDRERERVYIEGELLSESWRRLPVDEQLQILQSRYEEAASGKHSIGQQRRAKALKKEMTALRRKLAHPRDTLLLDTHSHTHILSKDGVCVV
Protein: Inorganic triphosphatase (PPPase) (EC 3.6.1.25) (ORFXE) (P30871)
Organism: Escherichia coli (strain K12)
Function: Involved in the hydrolysis of the beta-gamma-phosphoanhydride linkage of triphosphate-containing substrates (inorganic or nucleoside-linked). Catalyzes the hydrolysis of inorganic triphosphate (PPPi), which could be cytotoxic because of its high affinity for calcium ion, thereby interfering with calcium signaling. It also hydrolyzes slowly thiamine triphosphate (ThTP). YgiF is a specific PPPase, but it contributes only marginally to the total PPPase activity in E.coli, where the main enzyme responsible for hydrolysis of PPPi is inorganic pyrophosphatase (PPase).
Interaction partners:
- Bifunctional glutamine synthetase adenylyltransferase/adenylyl-removing enzyme
Sequence:
MAQEIELKFIVNHSAVEALRDHLNTLGGEHHDPVQLLNIYYETPDNWLRGHDMGLRIRGENGRYEMTMKVAGRVTGGLHQRPEYNVALSEPTLDLAQLPTEVWPNGELPADLASRVQPLFSTDFYREKWLVAVDGSQIEIALDQGEVKAGEFAEPICELELELLSGDTRAVLKLANQLVSQTGLRQGSLSKAARGYHLAQGNPAREIKPTTILHVAAKADVEQGLEAALELALAQWQYHEELWVRGNDAAKEQVLAAISLVRHTLMLFGGIVPRKASTHLRDLLTQCEATIASAVSAVTAVYSTETAMAKLALTEWLVSKAWQPFLDAKAQGKISDSFKRFADIHLSRHAAELKSVFCQPLGDRYRDQLPRLTRDIDSILLLAGYYDPVVAQAWLENWQGLHHAIATGQRIEIEHFRNEANNQEPFWLHSGKR
Protein: NADH dehydrogenase [ubiquinone] flavoprotein 3, mitochondrial (Complex I-9kD) (CI-9kD) (NADH-ubiquinone oxidoreductase 9 kDa subunit) (P25712)
Organism: Bos taurus (Bovine)
Function: Accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), that is believed not to be involved in catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone. May be the terminally assembled subunit of Complex I.
Subcellular location: Mitochondrion inner membrane {ECO:0000305|PubMed:18721790}; Peripheral membrane protein {ECO:0000305}; Matrix side {ECO:0000305}.
Interaction partners:
- NADH dehydrogenase iron-sulfur protein 4, mitochondrial
- NADH dehydrogenase 1 alpha subcomplex subunit 2
- NADH dehydrogenase 1 alpha subcomplex subunit 12
- NADH dehydrogenase 1 alpha subcomplex subunit 9, mitochondrial
- NADH dehydrogenase iron-sulfur protein 3, mitochondrial
- NADH dehydrogenase 1 alpha subcomplex subunit 7
- Acyl carrier protein, mitochondrial
- NADH-ubiquinone oxidoreductase 75 kDa subunit, mitochondrial
- NADH dehydrogenase flavoprotein 2, mitochondrial
- NADH dehydrogenase iron-sulfur protein 6, mitochondrial
Sequence:
MAASLLLRQGRAGALKTVLLEAGVFRGVAPAVSLSAESGKNEKGLPPNPKKQSPPKKPVSAAPTEPFDNTTYKNLQHHDYSTYTFLDLNLDLSKFRMPQPSSGRESPRH
Protein: [histone H3]-trimethyl-L-lysine(27) demethylase (EC 1.14.11.68) (A0A0G2K6D0)
Organism: Rattus norvegicus (Rat)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- 5'-AMP-activated protein kinase subunit gamma-1
- PAX-interacting protein 1
- Retinoblastoma-binding protein 5
- Set1/Ash2 histone methyltransferase complex subunit ASH2
- WD repeat-containing protein 5
- Protein dpy-30 homolog
- Nuclear receptor coactivator 6
- ATP synthase F
- ATP synthase F
- PAXIP1-associated glutamate-rich protein 1
Sequence:
MKSCGVSLATAAAAAAFGDEEKKMAAGKASGESEEASPSLTAEEREALGGLDSRLFGFVRFHEDGARMKALLGKAVRCYESLILKAEGKNAAFLYGLGLVYFHYNAFQWAIKAFQEVLYVDPSFCRAKEIHLRLGLMFKVNTDYESSLKHFQLALVDCNPCTLSNAEIQFHIAHLYETQRKYHSAKEAYEQLLQLENLSAQVKATVLQQLGWMHHTVDLLGDKATKESYAIQYLQKSLEADPNSGQSWYFLGRCYSSIGKVQDAFISYRQSIDKSEASADTWCSIGVLYQQQNQPMDALQAYICAVQLDHGHAAAWMDLGTLYESCNQPQDAIKCYLNATRSKNCSNTSGLAARIKYLQAQLCNLPQGSLQNKTKLLPSIEEAWSLPIPAELTSRQGAMNTAQQNTSDNWSGGNAVPHPPVQQQTHSWCLTPQKLQMRQTGVAQVRPTGIPNGPTADSSLPTNSASGQQPQLPLTRMPSVSQPGVQPACPRQALANGPFSAGHVPCSTSRTLGSTDTILIGNNHVTGSGSNGNVPYLQRNAPTLPHNRTNLTSSTEEPWKNQLSNSTQGLHKGQSSHLAGPNGERPLSSTGPSQHLQAAGSGIQNQNGHPTLPSNSVTQGAALNHLSSHTATSGGQQGITLTKESKPSGNTLTLPETNRQTGETPNSTASVEGLPNHVHQVMADAVCSPSHGDSKSPGLLSSDNPQLSALLMGKANNNVGPGTCDIVNNIHPTVHTKTDNSVASSPSSAISTATPSPKSTEQTTTNSVTSLNSPHSGLHTINGEGMEESQSPIKTDLLLVSHRPSPQIIPSVSVSIYPSSAEVLKACRNLGKNGLSNSSILLDKCPPPRPPSSPYPPLPKDKLNPPTPSIYYINNLVGCIFVLILLTSFIYLWLTYKDLGLFSTKTLVEANNEHMVEVRTQLLQPADENWDPTGTKKIWHCESNRSHTTIAKYAQYQASSFQESLREENEKRSHHKDHSDSESTSSDNSGKRRRGPFKTIKFGTNIDLSDDKKWKLQLHELTKLPAFVRVVSAGNLLSHVGHTILGMNTVQLYMKVPGSRTPGHQENNNFCSVNINIGPGDCEWFVVPEGYWGVLNDFCEKNNLNFLMGSWWPNLEDLYEANVPVYRFIQRPGDLVWINAGTVHWVQAIGWCNNIAWNVGPLTACQYKLAVERYEWNKLQSVKSIVPMVHLSWNMARNIKVSDPKLFEMVKYCLLRTLKQCQTLREALIAAGKEIIWHGRTKEEPAHYCSICEVEVFDLLFVTNESNSRKTYIVHCQDCAWKTSGNLENFVVLEQYKMEDLMQVYDQFTLVSEINM
Protein: Leukocyte elastase inhibitor C (Serine protease inhibitor EIC) (Serpin B1c) (Q5SV42)
Organism: Mus musculus (Mouse)
Function: Regulates the activity of the neutrophil proteases. Forms only a stable complex with CTSG/Cathepsin G (By similarity). During inflammation, limits the activity of inflammatory caspases CASP1 and CASP4 by suppressing their caspase-recruitment domain (CARD) oligomerization and enzymatic activation.
Subcellular location: Cytoplasm {ECO:0000250}.
Interaction partners:
- Albumin
- Thyroglobulin
- T-cell surface glycoprotein CD4
- Interleukin-4
- Granulocyte-macrophage colony-stimulating factor
- Interleukin-5
- Interferon gamma
- Interleukin-13
- H-2 class II histocompatibility antigen, A beta chain
- Toll-like receptor 4
Sequence:
MGQLSSANNLFALELFHTLNESNPTGNTIFSPVSISSALAMVYLGARGSTAAQLSKTLHFDSAEDIHSQFQSLTAEVSKRGASHTLKLANRLYGEKTYNFLPEYLASIQKTYSADLALVDFQHASEDARKEINQWVKGQTEEKIQELFAVGVVDSMTKLVLVNATYFKGMWQKKFMARDTTDAPFRLSKKVTKTVKMMYLKNNLPFGYIPDLKCKVLEMPYQGGELSMVILLPEDIEDETTGLEEIEKQLTLEKLQECENLQNIDVCVKLPKFKMEESYILNSNLGQLGVQDLFSSSKADLSGMSGSRDLFISKIVHKSYVEVNEEGTETDAAMPGTVVGCCLMPMEFTVDHPFLFFIRHNPTAHVLFLGRVCSP
Protein: non-specific serine/threonine protein kinase (EC 2.7.11.1) (Q8T9L5)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
Interaction partners:
- Protein Mo25
- STE20-related kinase adapter protein stlk
- LD22662p
- 5'-AMP-activated protein kinase subunit beta-1
- non-specific serine/threonine protein kinase
- Forkhead box protein O
- Gigas, isoform A
- Phosphatidylinositol 3,4,5-trisphosphate 3-phosphatase and dual-specificity protein phosphatase PTEN
- Axin
- Raptor, isoform B
Sequence:
MQCSSSRPVGGKAAGGAEAGGAGATGQMTVTTMEAQVKAAHHHHLHHPTGGGAQHKVEEEEPDPVEDEMTVLLANKNFHYDVASDLDDDAFVELKEDTAQADDAGAGVGFYNPDELLLDDQPHPQVTWLDDDEIETLDRVTLDMGNMFFNRVDSQDIIYQQKKKSIKMVGKYIMGDVLGEGSYGKVKEAMNSENLCRLAVKILTKRKLRRIPNGEQNVTREIALLKQLKHRHVVELVDVLYNEEKQKMYLVMEYCVGGLQEMIDYQPDKRMPLFQAHGYFKQLVDGLEYLHSCRVIHKDIKPGNLLLSLDQTLKISDFGVAEQLDLFAPDDTCTTGQGSPAFQPPEIANGHETFAGFKVDIWSSGVTLYNLATGQYPFEGDNIYRLLENIGRGQWEAPAWLYEMDADFANLILGMLQADPSKRLSLQEIRHDTWFRSAPVKTGPPIPIPPLKGDKYRNSTVIPYLEAYHYGTQEEDVYFTEHDVNQELARQAAAAASEIRAKQSAAALAACHTYEPPSTSAAAASNSLGNGSREEAPVKKKGSALKRRAKKLTSCISVRKLSHCRTS
Protein: Protein Wnt-3a (P27467)
Organism: Mus musculus (Mouse)
Function: Ligand for members of the frizzled family of seven transmembrane receptors (Probable). Functions in the canonical Wnt signaling pathway that results in activation of transcription factors of the TCF/LEF family. Required for normal embryonic mesoderm development and formation of caudal somites. Required for normal morphogenesis of the developing neural tube. Mediates self-renewal of the stem cells at the bottom on intestinal crypts (in vitro).
Subcellular location: Secreted, extracellular space, extracellular matrix {ECO:0000305}. Secreted {ECO:0000269|PubMed:17141155, ECO:0000269|PubMed:26902720}.
Interaction partners:
- Low-density lipoprotein receptor-related protein 6
- Low-density lipoprotein receptor-related protein 5
- Frizzled-1
- Frizzled-2
- Frizzled-8
- Wnt inhibitory factor 1
- Protein-serine O-palmitoleoyltransferase porcupine
- Glypican-3
- Tyrosine-protein kinase RYK
- Catenin beta-1
Sequence:
MAPLGYLLVLCSLKQALGSYPIWWSLAVGPQYSSLSTQPILCASIPGLVPKQLRFCRNYVEIMPSVAEGVKAGIQECQHQFRGRRWNCTTVSNSLAIFGPVLDKATRESAFVHAIASAGVAFAVTRSCAEGSAAICGCSSRLQGSPGEGWKWGGCSEDIEFGGMVSREFADARENRPDARSAMNRHNNEAGRQAIASHMHLKCKCHGLSGSCEVKTCWWSQPDFRTIGDFLKDKYDSASEMVVEKHRESRGWVETLRPRYTYFKVPTERDLVYYEASPNFCEPNPETGSFGTRDRTCNVSSHGIDGCDLLCCGRGHNARTERRREKCHCVFHWCCYVSCQECTRVYDVHTCK
Protein: Eukaryotic translation initiation factor 4E-2 (eIF-4E-2) (eIF4E-2) (eIF-4F 25 kDa subunit) (mRNA cap-binding protein) (Q21693)
Organism: Caenorhabditis elegans
Function: Recognizes and binds the 7-methylguanosine-containing mRNA cap during an early step in the initiation of protein synthesis and facilitates ribosome binding by inducing the unwinding of the mRNAs secondary structures. All 5 eIF4E proteins bind monomethyl cap structures. Only ife-1, ife-2 and ife-5 bind trimethyl cap structures which result from trans-splicing. Translation of trimethyl cap structure mRNAs may be regulated by intracellular redox state; disulfide bonds change the width and depth of the cap-binding cavity determining selectivity to mRNA caps. Probably by regulating mRNA translation in somatic cells, negatively regulates lifespan independently of daf-2/insulin and let-363/TOR pathways. Negatively regulates resistance to oxidative stress. May play a role in embryonic development.
Interaction partners:
- MIF4G domain-containing protein
- Cytoplasmic FMR1-interacting protein homolog
- Eukaryotic initiation factor 4A
- Translational repressor ifet-1
- Ribosomal protein S6 kinase beta
- Target of rapamycin homolog
- Eukaryotic translation initiation factor 2 subunit 2
- RNA helicase
- Prion-like-
- Eukaryotic translation initiation factor 5
Sequence:
MSEEPVAAPGTISHPVYKLKRNWTWWYLNDERNKSWEERLKNVKTFSSVGEFWALHDSIKPPSGLNPPSDYNVFRDGIEPMWEVPQNQNGGRWLITIEKGRTPEIMDTIWTEILMAMIGEQFSDDIESLCGIVCNVRGKGSKISVWTTNSADDGANLRIGGVLKQVLNNASMIHQRPLYDVLRYEDHESCQKKTSSGVKAKHAIYAVEPREEKAPVPVSTETPATPAT