wanglab/gogpt-training-data huggingface dataset:
Protein: Alpha/beta-syntrophin-like protein SYN1 (Q9GT69)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}. Membrane {ECO:0000256|ARBA:ARBA00004170}; Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004170}.
Interaction partners:
Sequence:
GEELRDATHDEAVRALKRSGRVVDLEVKFLREVTPYFRKASIISEVGWELQRAFLCPLGPGVPTSPPAPKTTPRADTRYIPLQLTHLARNLKYIDPENRCFELHSPDGVHSCILRAADSAEALVWFNALHSAMGTSTQRALAEANRALTNLIGELKHIGWLSKRMSGGGSSGSAGGGAASGGSGTSNSVVAGELPSGRSSSESSDESDKWLPIFVAVTEREFRIYESAPWSVEAWSRPLEIYALATTRLAGAGNNSSLNGQQTTVFCVRCGTARGVLVYWLRSETHRDMAAWARSLVQGSHQAVNYQREFSFRCLFQGRQCQLVVHINRGFFLYDCGGFAPTTPTVATAKTQLWQFAFDKLKGSADDGARMLYLDFGEDGEIELDMECCPKPVVFVVHNCLSAKVHNIA
Protein: Heparin-binding fibroblast growth factor receptor 2 (Q63241)
Organism: Rattus norvegicus (Rat)
Interaction partners:
Sequence:
CTDNISVQMGLTSTWRYGRGPGIGTVTMVSWGRFICLVLVTMATLSLARPSFSLVEDTTLEPEGAPYWTNTEKMEKRLHAVPAANTVKFRCPAGGNPTPTMRWLKNGKEFKQEHRIGGYKVRNQHWSLIMESVVPSDKGNYTCVVENEYGSINHTYHLDVVERSPHRPILQAGLPANASTVVGGDVEFVCKVYSDAQPHIQWIKHVEKNGSKYGPDGLPYLKVLKAAGVNTTDKEIEVLYIRNVTFEDAGEYTCLAGNSIGISFHSAWLTVLPAPVREKEITASPDYLEIAIYSIGVFLIACMVVTVIFCRMKTTTKKPDFSSQPAVHKL
Protein: DNA helicase assembly protein (Gene product 59) (Gp59) (Helicase loader) (Helicase loading protein) (P13342)
Organism: Enterobacteria phage T4 (Bacteriophage T4)
Function: DNA helicase loader protein that participates in viral DNA replication, recombination, and repair. At the fork, required for loading of the replicative helicase onto DNA protected by the ssDNA-binding protein. Coordinates simultaneous synthesis of leading- and lagging-strands.
Interaction partners:
Sequence:
MIKLRMPAGGERYIDGKSVYKLYLMIKQHMNGKYDVIKYNWCMRVSDAAYQKRRDKYFFQKLSEKYKLKELALIFISNLVANQDAWIGDISDADALVFYREYIGRLKQIKFKFEEDIRNIYYFSKKVEVSAFKEIFEYNPKVQSSYIFKLLQSNIISFETFILLDSFLNIIDKHDEQTDNLVWNNYSIKLKAYRKILNIDSQKAKNVFIETVKSCKY
Protein: DNA polymerase sliding clamp 1 (Proliferating cell nuclear antigen homolog 1) (PCNA 1) (Q5JF32)
Organism: Thermococcus kodakarensis (strain ATCC BAA-918 / JCM 12380 / KOD1) (Pyrococcus kodakaraensis (strain KOD1))
Function: Sliding clamp subunit that acts as a moving platform for DNA processing. Responsible for tethering the catalytic subunit of DNA polymerase and other proteins to DNA during high-speed replication.
Interaction partners:
- Flap endonuclease 1
- Replication factor C small subunit
- PCNA-inhibitor
- DNA polymerase
- DNA polymerase II small subunit
- DNA ligase
- DNA polymerase II large subunit
- Replication factor C large subunit
- DNA primase small subunit PriS
- DNA primase large subunit PriL
Sequence:
MPFEVVFDGAKEFADLIATASNLIDEAAFKFTEEGISMRAMDPSRVVLIDLNLPESIFSKYEVEEPETIGINMDQFKKILKRGKAKDTLILRKGDENFLEITFEGTAKRTFRLPLIDVEELELELPELPFTAKVVLLGEVLKEGIKDASLVSDAIKFIAKENEFTMKAEGETNEVEIRLTLEDEGLLDLEVEEETKSAYGIRYLSDMVKGIGKADEVILRFGNEMPLQMEYMIRDEGRLTFLLAPRVEE
Protein: Isoamylase 2, chloroplastic (OsISA2) (EC 3.2.1.68) (Q6AU80)
Organism: Oryza sativa subsp. japonica (Rice)
Function: Starch-debranching enzyme involved in amylopectin biosynthesis in endosperm. Functions by removing excess branches or improper branches that interfere with the formation of double helices of the cluster chains of amylopectin and crystallization of starch. Works together with ISA1 as heterooligomer. The heterooligomer ISA1 and ISA2 possesses higher affinity than the ISA1 homooligomer for various branched polyglucans in vitro, but no marked differences exist in chain preferences for debranching of amylopectin and phytoglycogen between these forms.
Subcellular location: Plastid, chloroplast {ECO:0000255}.
Interaction partners:
- Isoamylase 1, chloroplastic
- Alpha-1,4 glucan phosphorylase
- Alpha-1,4 glucan phosphorylase
- 4-alpha-glucanotransferase DPE2
- 1,4-alpha-glucan-branching enzyme, chloroplastic/amyloplastic
- ornithine carbamoyltransferase
- Soluble starch synthase 3a, chloroplastic/amyloplastic
- 4-alpha-glucanotransferase DPE1, chloroplastic/amyloplastic
- Os04g0409200 protein
- 1,4-alpha-glucan branching enzyme
Sequence:
MASLPAPPTPLGSCPRGRGGGRVVARPRRAGLACAARSCYRFRTDDDGVVDVAVSGEDGDGGGGGYAVSVEVPGTRGREGGLVLRASGSGEGVPLAPAAGGASLAAELSFDPTRAPFYLSFLLTDASGAEIRTHRKTSFRVPVGVGPGSPAPLGMSISGDGAVNFAVYSKNANAVSLYLYAAAVGGGGGDEPALEIDLDPYIHRTGNVWHVSLASVDGYVSYAFCCGGIRRPLLDPYAKVIGDFVSSNSVYDEGVTAPSMRCFASLAIAPSYNWGRDRHPRLPLEKLVVYRANVALFTKDRSSGLPDDAAGTFTGLSAKVEHFRSLGVNAILLEPVFPFHQVKGPYFPYHFFSPMNLYSSKGLSVSAIKSMKDMVRVMHRNGIEVLLEVVFTHTAEGESECQTISMRGIDNSSYYIANGIAGCKASILNCNHPVTQKLILDSLRHWVLDFHVDGFCFINAPFLVRGPGGEYLSRPPLLEAITFDPVLSMTKIIADPWSPLDISNVQFPFPHWKRWAEVNTRFSIDVRKFLKREALISDLATRLCGSGDLFSTRGPAFSFNHVSRNSGLSLVDLVSFSNDDLLSESSWNCGEEGPSENSAVLQTRLRQIRNFLFILFVSLGVPVLNMGDECGHSAAGSVSYKDRGPLNWRGMKTTFVKEVTGFISFLTALRSRRGDIFQRREFLKLENIHWYGSDLCEPGWDDPTSNFLCMHINAEVDEMAADSVRGDLYICFNANEESVSAALPALAEGSVWLRLVDTSLAFPGFFATESNPKVQQVPGLSSYHVEAHTCVLFESKSALA
Protein: Deoxyguanosine kinase (A0A0G2K478)
Organism: Rattus norvegicus (Rat)
Interaction partners:
Sequence:
MAAGRFLLRRLRASFRSQPRNALVDAPRARGMHDGGGPRRLCIEGNIAVGKSTFVKLLTKTHPEWQVATEPIATWQNVQAAGTQKDSTSRRLGNLLDMMYQEPARWSYTFQTLSFMSRLKVQLEPTPGRLLQADTSVRVFERSVYSDRASSMVPSRQARGPLSQGLGQLSSSYPSGQLHCAALARQDQLFCSHGLEDSSPNYCRYIFAKNLFENGSLSDVEWHIYQDWHSFLLQEFEDRLLLHGFIYLQASPQVCMERLCQRGREEEKGIELAYLKQLHGQHEDWFINKTTKLHFEALRHVPVLVLNISEDFSENAAKQEELMGQVNTFMRNL
Protein: Sulfotransferase 1 family member D1 (ST1D1) (EC 2.8.2.-) (Amine N-sulfotransferase) (SULT-N) (Dopamine sulfotransferase Sult1d1) (Tyrosine-ester sulfotransferase) (Q3UZZ6)
Organism: Mus musculus (Mouse)
Function: Sulfotransferase with broad substrate specificity that utilizes 3'-phospho-5'-adenylyl sulfate (PAPS) as sulfonate donor to catalyze the sulfate conjugation of catecholamines, such as dopamine, prostaglandins, leukotriene E4, drugs and xenobiotic compounds. Has sulfotransferase activity towards p-nitrophenol, 2-naphthylamine and minoxidil (in vitro). Sulfonation increases the water solubility of most compounds, and therefore their renal excretion, but it can also result in bioactivation to form active metabolites.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:19966186}.
Interaction partners:
Sequence:
MDNKLDVFRRELVDVEGIPLFWSIAEHWSQVESFEARPDDILISTYPKSGTTWVSEILDLIYNNGDAEKCKRDAIYKRVPFMELIIPGITNGVEMLNNMPSPRIVKTHLPVQLLPSSFWKNDCKIIYVARNAKDVVVSYYYFYQMAKIHPEPGTWEEFLEKFMAGQVSFGPWYDHVKSWWEKRKEYRILYLFYEDMKENPKCEIQKILKFLEKDIPEEILNKILYHSSFSVMKENPSANYTTMMKEEMDHSVSPFMRKGISGDWKNQFTVAQYEKFEEDYVKKMEDSTLKFRSEI
Protein: Tumor necrosis factor receptor superfamily member 5 (B-cell surface antigen CD40) (Bp50) (CD40L receptor) (CDw40) (CD antigen CD40) (P25942)
Organism: Homo sapiens (Human)
Function: Receptor for TNFSF5/CD40LG. Transduces TRAF6- and MAP3K8-mediated signals that activate ERK in macrophages and B cells, leading to induction of immunoglobulin secretion (By similarity).
Subcellular location: [Isoform I]: Cell membrane; Single-pass type I membrane protein.; SUBCELLULAR LOCATION: [Isoform II]: Secreted.
Interaction partners:
- T-lymphocyte activation antigen CD80
- TNF receptor-associated factor 3
- TNF receptor-associated factor 6
- CD40 ligand
- T-cell-specific surface glycoprotein CD28
- TNF receptor-associated factor 2
- TNF receptor-associated factor 5
- Proto-oncogene c-Rel
- Tumor necrosis factor
- Heat shock 70 kDa protein 4
Sequence:
MVRLPLQCVLWGCLLTAVHPEPPTACREKQYLINSQCCSLCQPGQKLVSDCTEFTETECLPCGESEFLDTWNRETHCHQHKYCDPNLGLRVQQKGTSETDTICTCEEGWHCTSEACESCVLHRSCSPGFGVKQIATGVSDTICEPCPVGFFSNVSSAFEKCHPWTSCETKDLVVQQAGTNKTDVVCGPQDRLRALVVIPIIFGILFAILLVLVFIKKVAKKPTNKAPHPKQEPQEINFPDDLPGSNTAAPVQETLHGCQPVTQEDGKESRISVQERQ
Protein: Acylamidase (EC 3.5.1.13) (EC 3.5.1.14) (EC 3.5.1.4) (K9NBS6)
Organism: Rhodococcus erythropolis (Arthrobacter picolinophilus)
Function: Amidase with broad substrate specificity, catalyzing the hydrolysis of a wide range of N-substituted amides, and, to a lesser extent, the hydrolysis of non-substituted amides. Acid para-nitroanilides (4'-nitroacetanilide, Gly-pNA, Ala-pNA, Leu-pNA) are the best substrates for this enzyme. N-substituted acrylamides (isopropyl acrylamide, N,N-dimethyl-aminopropyl acrylamide, and methylene-bis-acrylamide), N-acetyl derivatives of glycine, alanine and leucine, and aliphatic amides (acetamide, acrylamide, isobutyramide, n-butyramide, and valeramide) can also be used as substrates but with less efficiency.
Interaction partners:
- Aspartyl/glutamyl-tRNA
- Aspartyl/glutamyl-tRNA
- Amidase
- glutamyl-tRNA amidotransferase
- LuxR family transcriptional regulator
Sequence:
MTEQNLHWLSATEMAASVASNNLSPNEIAEAMIQRVDAVNPSINAIVQFDREQVTRDAAELSRQQEAGEKLGPLHGVPFTIKDLTAVDGLPTTFGMKPMADNIATGNAVVVDRLRGAGGLFLGKTNTPESGYYGGTDNHLYGPTHNPWKLGNSAGGSSGGASAAVAAGLGPLAEGSDGAGSVRIPSALCGVVGLKPTTGVIPQTILAGRFYNWAYHGPITRTVADNALMLDIMAGPDNADPLSIERAETSYVEASKGDVKGLRVAWSPNLGLGHVDPEVLAVCLDALAAFEELGAQITEATPQWGNPSESMWSGIWVPGFASEYDLLDWENQRGEVDDYLIEIMHEAERLTGVDVGRADAFRGDMWDTWTTFMNDYDVLVSPTLASATFPLRQFAPSWLEGASLREQLLDWLFTYPYNMLNNPAITVPAGFTADGRPVGLQIAARHRRDALVLRTAANFEAVRPWADKKPADSLVVA
Protein: APOL4 protein (Apolipoprotein L, 4, isoform CRA_c) (Apolipoprotein L4) (Q9BRG6)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MGSWVQLITSVGTSGLFLGVRVREEGAGMRCSKTIQAGQWLDSSKGPLGPSPPPVPTAGYSSSFCVHYVNLLPGVLVLSVTSQYPHLSMALCQLAAHDWPRLSCVCV
Protein: SD10334p (Q960B1)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cytoplasm, perinuclear region {ECO:0000256|ARBA:ARBA00004556}.
Interaction partners:
Sequence:
MTNTINSEEVSDAGSYKDKGNEAFKASRWEEAVEHYGKAIKAGSKHKELAVFYKNRAAAYLKLGKYENAVEDCTESLKAAPGDPKALFRRAQAYEALEKFEEAYKDATALFKADPGNKTVQPMLQRLHVVVEERSARNAKTSTKVKQMMDLTFDLATPIDKRRAAANNLVVLAKEQTGAELLYKDHCIAKVASLTKVEKDQDIYVNMVHLVAALCENSVERTKGVLTELGVPWFMRVLDQKHENCVSTAQFCLQTILNALSGLKNKPDSKPDKELCTRNNREIDTLLTCLVYSITDRTISGAARDGVIELITRNVHYTALEWAERLVEIRGLCRLLDVCSELEDYKYESAMDITGSSSTIASVCLARIYENMYYDEAKARFTDQIDEYIKDKLLAPDMESKVRVTVAITALLNGPLDVGNQVVAREGILQMILAMATTDDELQQRVACECLIAASSKKDKAKALCEQGVDILKRLYHSKNDGIRVRALVGLCKLGSYGGQDAAIRPFGDGAALKLAEACRRFLIKPGKDKDIRRWAADGLAYLTLDAECKEKLIEDKASIHALMDLARGGNQSCLYGVVTTFVNLCNAYEKQEMLPEMIELAKFAKQHIPEEHELDDVDFINKRITVLANEGITTALCALAKTESHNSQELIARVLNAVCGLKELRGKVVQEGGVKALLRMALEGTEKGKRHATQALARIGITINPEVSFSGQRSLDVIRPLLNLLQQDCTALENFESLMALTNLASMNESVRQRIIKEQGVSKIEYYLMEDHLYLTRAAAQCLCNLVMSEDVIKMFEGNNDRVKFLALLCEDEDEETATACAGALAIITSVSVKCCEKILAIASWLDILHTLIANPSPAVQHRGIVIILNMINAGEEIAKKLFETDIMELLSGLGQLPDDTRAKAREVATQCLAAAERYRIIERSDNAEIPDVFAENSKISEIIDD
Protein: Elastin-like, isoform A (Elastin-like, isoform C) (GH13458p) (Q8SY52)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Zinc finger protein Noc
- Zinc finger protein Elbow
Sequence:
MLSRRVIAFAALALIQIASGQASQFSRDESQEDQKTEFNLASTLTGGITSSRHRQRANLNSQLYPGLGQLGSGYAGATGSIDDAHGHEQGGSGVRVASTNSVVFPGNQSPNPALTITGGHQIPAYPPPGFPGQQAPVPYPAAGGSSGGSSSSGGYQSAGAVSPPGYPVAGAVPAQYPVGVPPQQPVGAGAPGYFPGTGAYPGYPYPGVYLPQYPAYPQPAQFPAYGVLPGAVAQPGVPGVAGVPGAPGVAGVPGAAGQAPATSGMNYHRYPAHNPADPSHWDHHFSMNTEYKEDGVHKGPFGVLNNHNAFGYGSGYGGGYNGAFNSPAY
Protein: DSki protein long isoform (A0PDV1)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MISTVLKKYQTSATKSLQGPGHALTTAGVLDIVTNGRSESPGLNGKCQASPPVVALIKKEILSSPEPQDLHHHECSTRGTPPQIYSPATPPRELSQPILSVADAGCGELYETKLEGKTIGCFSVGGEMRLCLPQFLNNVLNDFSLEQINRIFDELGIYCSQCTHGQLVEFKAAKILPSDVKASGLITRTDAERLCAALLHRSDRNSYVPIESLAKGALSFHVYHKCFGKCEGICTPDMYSYQKPTCIKCLECDGWFSSQKFVGHVHRKFENHTCHWGFDSRNWHDYPHVALDVENRVKYQIILDQLKEVELKEMHKAQRELEHKKRKAEMLMDDGMLGSGPVLGLAGHPHGLVGALAPPPPPPMKQPQMDIPSGKKQLQQLKGATVAASALEYQYQVMYAHCVQKEREREREHLPHSHPLPRQHRAVLVATTPYPHLPQYPTPPTLNSSSAFRPWGPDTTKAFLHAYGATLSSLPYACQEPPELQNPERVVRSTDKRYAERTYQPNVALAPRKSILSKERDKDRERMEREVMERQRLREKETDHQVVHIKQERSQTPTPPTASPPDGVVLPLDVVEPPHPSSSGSNSPLPAHLPAAPATAPPNAGGAPPTPTNLRNMRSPEEFSAGGSNEITSSTSPHHQQSSHHQVVQPTAGAPPPSQHIIATVNQHAKLLPSSSSLPNGNGSSSLAATNNEPSRIRINKNLMSQQPLVAVSGMTPHHHQHHPTHMHHFSHGYYKSQASSPTQSSSAGLNLSTHSSNVVSSPHHATQPKTHHSSVGSGNHGLQNGKPHLGSEFELSTDTDDTDSLNGEPDSSAMLPPWEQAVESLRETRPKDRERVLLILQRLLQENDQYRYNNIQLSELLHKQDAHIADLTEQLQRYRRQFEEQVCKVDLRKMPFKHQTRLENVVEAGRGEAEEDEELEEDEMEDRANNNNQQELSPLIKAPANGLRRSVTPPNCCASEGGDCEKPDEPESKRIKLQVGEKAEDKQVENEESPSNGTESHDLEKLEKKK
Protein: Osteoclast-stimulating factor 1 (Q92882)
Organism: Homo sapiens (Human)
Function: Induces bone resorption, acting probably through a signaling cascade which results in the secretion of factor(s) enhancing osteoclast formation and activity.
Subcellular location: Cytoplasm {ECO:0000305}.
Interaction partners:
- Unconventional myosin-Ie
Sequence:
MSKPPPKPVKPGQVKVFRALYTFEPRTPDELYFEEGDIIYITDMSDTNWWKGTSKGRTGLIPSNYVAEQAESIDNPLHEAAKRGNLSWLRECLDNRVGVNGLDKAGSTALYWACHGGHKDIVEMLFTQPNIELNQQNKLGDTALHAAAWKGYADIVQLLLAKGARTDLRNIEKKLAFDMATNAACASLLKKKQGTDAVRTLSNAEDYLDDEDSD
Protein: Non-specific phospholipase C1 (EC 3.1.-.-) (Q8L7Y9)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Secreted {ECO:0000305}.
Interaction partners:
- CDP-diacylglycerol--inositol 3-phosphatidyltransferase 1
- Phospholipase D beta 1
- Phospholipase D delta
- Lecithin-cholesterol acyltransferase-like 4
- Phospholipase D alpha 1
- Phospholipase A
- Choline/ethanolaminephosphotransferase 1
- Phospholipase D alpha 4
- Phospholipase D gamma 1
- Phosphatase IMPL1, chloroplastic
Sequence:
MAFRRVLTTVILFCYLLISSQSIEFKNSQKPHKIQGPIKTIVVVVMENRSFDHILGWLKSTRPEIDGLTGKESNPLNVSDPNSKKIFVSDDAVFVDMDPGHSFQAIREQIFGSNDTSGDPKMNGFAQQSESMEPGMAKNVMSGFKPEVLPVYTELANEFGVFDRWFASVPTSTQPNRFYVHSATSHGCSSNVKKDLVKGFPQKTIFDSLDENGLSFGIYYQNIPATFFFKSLRRLKHLVKFHSYALKFKLDAKLGKLPNYSVVEQRYFDIDLFPANDDHPSHDVAAGQRFVKEVYETLRSSPQWKEMALLITYDEHGGFYDHVPTPVKGVPNPDGIIGPDPFYFGFDRLGVRVPTFLISPWIEKGTVIHEPEGPTPHSQFEHSSIPATVKKLFNLKSHFLTKRDAWAGTFEKYFRIRDSPRQDCPEKLPEVKLSLRPWGAKEDSKLSEFQVELIQLASQLVGDHLLNSYPDIGKNMTVSEGNKYAEDAVQKFLEAGMAALEAGADENTIVTMRPSLTTRTSPSEGTNKYIGSY
Protein: Neurogenic differentiation factor 1 (NeuroD) (NeuroD1) (Class A basic helix-loop-helix protein 3) (bHLHa3) (Q13562)
Organism: Homo sapiens (Human)
Function: Acts as a transcriptional activator: mediates transcriptional activation by binding to E box-containing promoter consensus core sequences 5'-CANNTG-3'. Associates with the p300/CBP transcription coactivator complex to stimulate transcription of the secretin gene as well as the gene encoding the cyclin-dependent kinase inhibitor CDKN1A. Contributes to the regulation of several cell differentiation pathways, like those that promote the formation of early retinal ganglion cells, inner ear sensory neurons, granule cells forming either the cerebellum or the dentate gyrus cell layer of the hippocampus, endocrine islet cells of the pancreas and enteroendocrine cells of the small intestine. Together with PAX6 or SIX3, is required for the regulation of amacrine cell fate specification. Also required for dendrite morphogenesis and maintenance in the cerebellar cortex. Associates with chromatin to enhancer regulatory elements in genes encoding key transcriptional regulators of neurogenesis (By similarity).
Subcellular location: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000255|PROSITE-ProRule:PRU00981, ECO:0000269|PubMed:14752053}. Note=In pancreatic islet cells, shuttles to the nucleus in response to glucose stimulation (By similarity). Colocalizes with NR0B2 in the nucleus. {ECO:0000250}.
Interaction partners:
- Transcription factor 12
- Transcription factor E2-alpha
- Insulinoma-associated protein 1
- Paired box protein Pax-4
- Transcription factor 4
- Hexokinase-4
- Neurogenin-3
- Insulin
- Forkhead box protein N4
- Solute carrier family 2, facilitated glucose transporter member 2
Sequence:
MTKSYSESGLMGEPQPQGPPSWTDECLSSQDEEHEADKKEDDLETMNAEEDSLRNGGEEEDEDEDLEEEEEEEEEDDDQKPKRRGPKKKKMTKARLERFKLRRMKANARERNRMHGLNAALDNLRKVVPCYSKTQKLSKIETLRLAKNYIWALSEILRSGKSPDLVSFVQTLCKGLSQPTTNLVAGCLQLNPRTFLPEQNQDMPPHLPTASASFPVHPYSYQSPGLPSPPYGTMDSSHVFHVKPPPHAYSAALEPFFESPLTDCTSPSFDGPLSPPLSINGNFSFKHEPSAEFEKNYAFTMHYPAATLAGAQSHGSIFSGTAAPRCEIPIDNIMSFDSHSHHERVMSAQLNAIFHD
Protein: TNFAIP3-interacting protein 1 (A20-binding inhibitor of NF-kappa-B activation 1) (ABIN-1) (HIV-1 Nef-interacting protein) (Nef-associated factor 1) (Naf1) (Nip40-1) (Virion-associated nuclear shuttling protein) (VAN) (hVAN) (Q15025)
Organism: Homo sapiens (Human)
Function: Inhibits NF-kappa-B activation and TNF-induced NF-kappa-B-dependent gene expression by regulating TAX1BP1 and A20/TNFAIP3-mediated deubiquitination of IKBKG; proposed to link A20/TNFAIP3 to ubiquitinated IKBKG. Involved in regulation of EGF-induced ERK1/ERK2 signaling pathway; blocks MAPK3/MAPK1 nuclear translocation and MAPK1-dependent transcription. Increases cell surface CD4(T4) antigen expression. Involved in the anti-inflammatory response of macrophages and positively regulates TLR-induced activation of CEBPB. Involved in the prevention of autoimmunity; this function implicates binding to polyubiquitin. Involved in leukocyte integrin activation during inflammation; this function is mediated by association with SELPLG and dependent on phosphorylation by SRC-family kinases. Interacts with HIV-1 matrix protein and is packaged into virions and overexpression can inhibit viral replication. May regulate matrix nuclear localization, both nuclear import of PIC (Preintegration complex) and export of GAG polyprotein and viral genomic RNA during virion production. In case of infection, promotes association of IKBKG with Shigella flexneri E3 ubiquitin-protein ligase ipah9.8 p which in turn promotes polyubiquitination of IKBKG leading to its proteasome-dependent degradation and thus is perturbing NF-kappa-B activation during bacterial infection.
Subcellular location: Cytoplasm. Nucleus. Note=Shuttles between the nucleus and cytoplasm in a CRM1-dependent manner.
Interaction partners:
- Tumor necrosis factor alpha-induced protein 3
- Tumor necrosis factor
- Tumor necrosis factor receptor superfamily member 1A
- Polyubiquitin-C
- NF-kappa-B essential modulator
- Nuclear factor NF-kappa-B p105 subunit
- Optineurin
- Polyubiquitin-B
- Tax1-binding protein 1
- TNFAIP3-interacting protein 2
Sequence:
MEGRGPYRIYDPGGSVPSGEASAAFERLVKENSRLKEKMQGIKMLGELLEESQMEATRLRQKAEELVKDNELLPPPSPSLGSFDPLAELTGKDSNVTASPTAPACPSDKPAPVQKPPSSGTSSEFEVVTPEEQNSPESSSHANAMALGPLPREDGNLMLHLQRLETTLSVCAEEPDHGQLFTHLGRMALEFNRLASKVHKNEQRTSILQTLCEQLRKENEALKAKLDKGLEQRDQAAERLREENLELKKLLMSNGNKEGASGRPGSPKMEGTGKKAVAGQQQASVTAGKVPEVVALGAAEKKVKMLEQQRSELLEVNKQWDQHFRSMKQQYEQKITELRQKLADLQKQVTDLEAEREQKQRDFDRKLLLAKSKIEMEETDKEQLTAEAKELRQKVKYLQDQLSPLTRQREYQEKEIQRLNKALEEALSIQTPPSSPPTAFGSPEGAGALLRKQELVTQNELLKQQVKIFEEDFQRERSDRERMNEEKEELKKQVEKLQAQVTLSNAQLKAFKDEEKAREALRQQKRKAKASGERYHVEPHPEHLCGAYPYAYPPMPAMVPHHGFEDWSQIRYPPPPMAMEHPPPLPNSRLFHLPEYTWRLPCGGVRNPNQSSQVMDPPTARPTEPESPKNDREGPQ
Protein: Protein PEAK3 (Q6ZS72)
Organism: Homo sapiens (Human)
Function: Probable catalytically inactive kinase (Probable). Interacts with CRK-II and antagonizes CRK-II-signaling. Prevents the formation of CRK-II-dependent membrane ruffling and lamellipodia-like extensions.
Interaction partners:
Sequence:
MSSPEPPTEPPEPDNPTWSTQPTYSNLGQIRAHLLPSKACRLRTPGSLSTNPEPLPPPLPKKILTRTQSLPTRRTLHPSSIQVQPPRRPFLGSHSVDKSQAAVGPACLPAELTFGPADAPLGLSLRDLHSPEAVHTALAARQLQGLRTIYARLRARLMGGHPGPCHPGHSFRLLDSSPCAESGDALYYRVVRAHEDAWHILVAKVPKPGADVPHPWGLELQASLSPHFNLQGLCGLVPEGTLPGAPWRGAVALAAEVPERTVAQWLAEACTQPPEEFVWAVALLLLQLSAALKFLEAWGAALVELRPENLLLVAPRGCATTGPPRLLLTDFGRVCLQPPGPPGSPGPHAPQLGSLLRALLSLAAPSTTPLAAGLELLAAQLTRLRPSASRTRGALQALLWGPGPELRGRGAPLGPWLRALGPWLRVRRGLLVLRLAERAAGGEAPSLEDWLCCEYLAEATESSMGQALALLWD
Protein: Protein DWARF AND LOW-TILLERING (GRAS family protein 32) (OsGRAS-32) (Protein SMALL ORGAN SIZE 2) (Q9LWU9)
Organism: Oryza sativa subsp. japonica (Rice)
Function: Probable transcription factor that acts as positivie regulator of brassinosteroid (BR) signaling. Functions downstream of BRI1 and GSK2 to modulate BR responses. Acts as a direct target of GSK2 kinase to mediate BR responses. Involved in feedback inhibition of BR biosynthetic genes. Repressed by BZR1. Cooperatively functions in a transactivating complex with SMOS1 to enhance the transcription of the SMOS1 target PHI-1, and regulate plant organ size. Interaction between SMOS1 and DLT is a crosstalk point for auxin and brassinosteroid signaling.
Subcellular location: Nucleus {ECO:0000269|PubMed:22685166}.
Interaction partners:
- AP2-like ethylene-responsive transcription factor SMOS1
Sequence:
MLAGCSFSSSRHQMSTAQRFDILPCGFSKRGSRGDGAAPRVAGDARSGATTCSFRTHPAPPVTQSVSWGAKPEPGGNGNGAHRAVKRAHDEDAVEEYGPIVRAKRTRMGGDGDEVWFHQSIAGTMQATAAGEGEEAEEEKVFLVPSAAAFPHGMAAAGPSLAAAKKEEYSKSPSDSSSSSGTDGGSSAMMPPPQPPEFDARNGVPAPGQAEREALELVRALTACADSLSAGNHEAANYYLARLGEMASPAGPTPMHRVAAYFTEALALRVVRMWPHMFDIGPPRELTDDAFGGGDDDAMALRILNAITPIPRFLHFTLNERLLREFEGHERVHVIDFDIKQGLQWPGLLQSLAARAVPPAHVRITGVGESRQELQETGARLARVAAALGLAFEFHAVVDRLEDVRLWMLHVKRGECVAVNCVLAMHRLLRDDAALTDFLGLARSTGATILLLGEHEGGGLNSGRWEARFARALRYYAAAFDAVDAAGLPEASPARAKAEEMFAREIRNAVAFEGPERFERHESFAGWRRRMEDGGGFKNAGIGEREAMQGRMIARMFGPDKYTVQAHGGGGSGGGEALTLRWLDQPLYTVTAWTPAGDGAGGSTVSASTTASHSQQS
Protein: SD05887p (Q8T8Q5)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MFANLKNKLIEEVKASPSKFQQFANAAQAAVSSSSSTTPNSETNTSNNENFFSITEEDTPQNSPYRIQKLPATSASALRGRSTQSLNGATSRTRKLSNSSMASDVSFRLPTYEAPAVYHLQSDLDETSSEFDDSASTARLDVITKDQLYDAYKKSLDRYHKYRCRYTDLAKKYKELERDSSKARSVLVETQDKALRRISELREQCTLEQQAKAHLEEALRVEMDDMSCKMQAYQTKLQLLGENPENITAALERSGQQLESEQLIDLEESIGKSPLSTNGSSGVSDLQRLLKERDEQLKSVTEKYEAVRKQEEENVLLLAQTKQAIHTELELKDTEVRKLQEKLKQLESQRESHNNEVKEQFKKLQATKQEVDAKLMATEHLLNTLKESYAIKEQQVVTLEAQLEAIRVENEQKVKDLQKQNEDRNTQASDSSEQLKKLQAAVQDAESQLLSKDQLLESLRSEQAAKEQQLKHLKEQLGKLKQENENYLDKLRESKKSSDSQTNEAQDQQKKLQAAKDEAESKLLATEELLHSLRNDYKAQEEKVALLEDKLKTLSKENDVNVEKLHHINEQREAQSTDSQQKINELRAAKDEAEAKLLSTEHSLNALQAALSAKEEQAASLEQSLNALKTESEHSLQDLRLHNDQLLEIVQRHQQNDWEAQLARAREELAAIQSQRELHALELEKSLEMERESVAALNSEKASQEEQHRLKLEQLQREIQILQDQHANSESETVAALKGQLEALSQDLATSQASLLAKEKELKASGNKLNKIKKQHEQHQAKSSEQSVRLEALQSQLADRLSHSRQVESEKEELQARVTGILEEIGTMQAQMQQVQDSHSELEREKRKLESRIESLQQEQVDSSAQDERTSAKLEEIQSENTKLAERNCLLEEQANHLESQLQAKQDEIGKIQAKLQQVLDEHSKLQNAQELMDHDHRTLQDKCDAYEKDKLLTKHTLDCLQSASEELHRVKANLDRELKEQDQQLSELRERQREQEQQLKDQAERCAKLKAQNSESETQLQATISNLREQLDAYKQTEQGIQEKLQATNSSYTTQIATLEARWSAANSDVERLHEANDALQLEMEQLKIKHGQEREEVKESIAQKNRQVVELQEAMATRDRQLQEKIEASEKLAKFDEILIENEYLNKHTKQLEAELAESAELKEKLKSLQCELYVLQEKAEQHAVQMAEKETQSATATAEVSELKKAIEEQAVELTRQKEHASFVTEQSDAVQKDLLQAQQQLHDKQIELAMSRDEQALLQAEADGLRQEMICLKEHLSPSTDSDSLRSLNERLQRELEDLKHKSAGAESNMQQEIEELQANNQQMAERINELETLRAGIQAQQLLASMAPKNVQEAAAAGEKAELESKLKEIMNEVQDVTNRNLFLEQKCENFLILEQSNERLKLQNAKLSRQLDETLVSMQHSEAVPANTEFEYLRNIMFQYLTGNTNNETLVKVISAVLKFSPQQAQVALEKEHQRRSLLNKLI
Protein: Candida glabrata strain CBS138 chromosome M complete sequence (Q6FK20)
Organism: Candida glabrata (strain ATCC 2001 / BCRC 20586 / JCM 3761 / NBRC 0622 / NRRL Y-65 / CBS 138) (Yeast) (Nakaseomyces glabratus)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004609}; Lipid-anchor, GPI-anchor {ECO:0000256|ARBA:ARBA00004609}.
Interaction partners:
Sequence:
MKVTSLVYAAMATSVLGQNSTSDDVPSGCSLGSSATATAQSDLDKYSGCETIVGNLTITGALGSAALAGVKKIDGSLRIYNATSLGSFAADSVKEITGALNMQDLTILTTASFGALEEVDTINLITLPAISTFNTNLQSANNIVVSDTSLESVEGFGSLKEVNVLNINNNRYLNSFKSSLESVSGALQFASNADETAVSFDNLIWANNITLRDVQNASFAKLESVNASLGFINNTISTLNLTHLSKVGQSLSVVSNDDLTQLSFLNLTSVGGGLVVANNTNLKTIDGLKNVQTVGGAIDITGNFTTLDLSSLKSVRGGATFNTVSGNFSCSPLKSLQSKGAIQGDSFVCKNGATSTSISMSSRSRSSSASSSASATVTARSNDTASTSSTKTKKSKGAAAQEVFPAGSFFGAVAAVAVALL
Protein: Superoxide dismutase [Mn] (EC 1.15.1.1) (P53652)
Organism: Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Function: Destroys superoxide anion radicals which are normally produced within the cells and which are toxic to biological systems (Probable). Partially complements double sodA-sodB deletions in E.coli.
Interaction partners:
- Fumarate hydratase class II 2
- Tetratricopeptide repeat protein
- ZIP family metal transporter
- Catalase HPII
- FagA protein
- Catalase
- Alkyl hydroperoxide reductase C
- Redox-sensitive transcriptional activator SoxR
- Alkyl hydroperoxide reductase subunit F
- Aconitate hydratase A
Sequence:
MPHALPPLPYAYDALEPHIDALTMEIHHSKHHQTYVNNLNAALEGTPYAEQPVESLLRQLAGLPEKLRTPVVNNGGGHANHSLFWTVMSPQGGGRPDGDLGRAIDEQLGGFEAFKDAFTKAALTRFGSGWAWLSVTPQGSLLVESSGNQDSPLMNGNTPILGLDVWEHAYYLKYQNRRPEYIGAFYNVIDWREVARRYAQALA