wanglab/gogpt-training-data huggingface dataset:
Protein: DNA ligase (EC 6.5.1.1) (F1QJL4)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- DNA repair protein XRCC1
- DNA helicase
- DNA polymerase beta
- X-ray repair cross-complementing protein 5
- Bifunctional polynucleotide phosphatase/kinase
- Proliferating cell nuclear antigen
- Poly [ADP-ribose] polymerase.
- Flap endonuclease 1
- Double-strand break repair protein
- Tyrosyl-DNA phosphodiesterase 1
Sequence:
MPSLWLGRALRTLSRSSLTKISWEPLFRATLKHQYLQCSRTLIFTRGSESSPSGVFFCAPHTPAFTLISSSYFHISWPVRRSEQADMAEQRYCVEYAKRGTAGCKKCKDKIMKGLVRIGKIVPNPFSESAGEMKEWYHVKCIFEKLERARATTKKIEDITELEGWEELQDEDKDLINKHVSELAAKVNSTPKKKVQAKLNTSGQLSSPPADPTVNAPRKFSGFTATKAGSSSSSPGPSPAKPAQGSVLSAQMCDPTHKDNLLREFRKLCALVAEKSGYNAKTEIVRDFLTKGSGGDKFRGDLYLTVKLLLPGVVKNVYNLNDKQIVKLFSRILNCNQDDMVQDLEQGDVSETVRMFFEESKSFPPSAKSLLTIQEVDASLSRLSQLTKEDDQQAELQSIAKKCTGNDLKCYIRLVKHDLKINSGAKHILDAVDPNAYDAFKASRNLGDVIDRVLRNQQDASNGTGPRKILSIEASLMTPVQPMLAEACKSIEYAMKKCPNGMYSEIKYDGERVQVHKNGNHFSYFSRSLKPVLPHKVAHFKDFIPQAFAGGHSMILDAEVLLIDTKTSKPLPFGTLGVHKKAAFQDAQVGLFVFDCIYFNGVSLMDKPLCERRKFLHDNMVEVPNRILFSEMKHVTRAPDLAEMITRVIREGLEGLVLKDIKGLYEPGKRHWLKVKKDYLNEGAMADTADLVVLGAFYGKGSNGGIMSSFLMGCYDPESRKWCTVTKCSGGFDDAMLDRLQKDLDVIKIGKDPSKIPGWLKIVKNYYPDFIIRDPQKAPVWEITGAEFSKSEMHTADGISIRFPRCTRMRDDKDWKTATNLQQLKELYRISKENCDFEVTAGPSKANQNDKSSSGGESGGSSPSASRGASTANKPKNGHTPKAKAAKTESSAPAVKRKLPAEKQDVKKIKTESVHSNGQSKLKSVPTTDPKQEKTLLDIFTGVKLYLPESVKDFEKLRRYFLAYDGDLVPEYDSALATHTLGQPEDGSSAQKVTSNWIWECIRKRRVVPPC
Protein: Putative glyoxylase CFP32 (27 kDa antigen Cfp30B) (P9WIR3)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: May function as a glyoxylase involved in the methylglyoxal detoxification pathway. Induces maturation of dendritic cells in a TLR2-dependent manner, causing increased expression of cell-surface molecules (CD80, CD86, MHC class I and II) and pro-inflammatory cytokines (TNF-alpha, IL-6, IL-1 beta and IL-12p70). Acts via both the NF-kappa-B and MAPK signaling pathways. Induces Th1-polarized immune responses.
Subcellular location: Secreted {ECO:0000269|PubMed:14638775}.
Interaction partners:
- Uncharacterized protein Rv1510
- Uncharacterized oxidoreductase Rv2298
- Probable FEIII-dicitrate-binding periplasmic lipoprotein FecB
- Probable transcriptional regulatory protein
Sequence:
MPKRSEYRQGTPNWVDLQTTDQSAAKKFYTSLFGWGYDDNPVPGGGGVYSMATLNGEAVAAIAPMPPGAPEGMPPIWNTYIAVDDVDAVVDKVVPGGGQVMMPAFDIGDAGRMSFITDPTGAAVGLWQANRHIGATLVNETGTLIWNELLTDKPDLALAFYEAVVGLTHSSMEIAAGQNYRVLKAGDAEVGGCMEPPMPGVPNHWHVYFAVDDADATAAKAAAAGGQVIAEPADIPSVGRFAVLSDPQGAIFSVLKPAPQQ
Protein: Ptr22p (Q59ST2)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141, ECO:0000256|RuleBase:RU003755}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141, ECO:0000256|RuleBase:RU003755}.
Interaction partners:
- Oligopeptide transporter
Sequence:
MSTEEKHSQTDVINSSTQGSHSVEKSSRDDEYAGDNLGSDIQIDDEGREPTDHEMETLRHVSESIPISCWLVAIVELAERFSYYGLSAPFQNYMQFTPEHSPKGMLGLKQQGATALSYFFQFWCYVTPILGGWISDTYWGKYKTIFVFCVIYIVGIFLLFITSVPSITSKSTATGGYIAAIIIIGLGTGGVKSNVSPLIADQIPKKKPYIKVTKKGERVIVDPNITVQNVFMFFYLMINIGSLSVIATTQMEAHIGFWSSYLLTFCFFFIAIAALIVGRNKYVKVPVGDKIVNKTFKCVWVGIINGFNFDAAKPSVKPEKSYPWDDHFVDEVKRTISACKVFVWYPIYWVQYNGMMNMFVSSAAGMSRDIPNDFLTVFDSVAIIVFIPIFERFLYPFVRHFTPFKPITKIFWGFMFGSGAMVYAAVLQHYIYKAGPCYDHPLDCPNGNHINIGLQTPAYVLIAISEILASITGLEYAYTKAPVQMKSLVMAMFLLTNAVGAAIGIALSSVSVDPKMVWTYSGLAVSCFIAGCLFLTLFKHYNKKEDEWNNLEYEANIEEAALMPVSSLTPSRKSIA
Protein: Interferon beta (IFN-beta) (P70499)
Organism: Rattus norvegicus (Rat)
Function: Type I interferon cytokine that plays a key role in the innate immune response to infection, developing tumors and other inflammatory stimuli. Signals via binding to high-affinity (IFNAR2) and low-affinity (IFNAR1) heterodimeric receptor, activating the canonical Jak-STAT signaling pathway resulting in transcriptional activation or repression of interferon-regulated genes that encode the effectors of the interferon response, such as antiviral proteins, regulators of cell proliferation and differentiation, and immunoregulatory proteins (By similarity). Signals mostly via binding to a IFNAR1-IFNAR2 heterodimeric receptor, but can also function with IFNAR1 alone and independently of Jak-STAT pathways. Elicits a wide variety of responses, including antiviral and antibacterial activities, and can regulate the development of B-cells, myelopoiesis and lipopolysaccharide (LPS)-inducible production of tumor necrosis factor. Plays a role in neuronal homeostasis by regulating dopamine turnover and protecting dopaminergic neurons: acts by promoting neuronal autophagy and alpha-synuclein clearance, thereby preventing dopaminergic neuron loss. IFNB1 is more potent than interferon-alpha (IFN-alpha) in inducing the apoptotic and antiproliferative pathways required for control of tumor cell growth (By similarity).
Subcellular location: Secreted {ECO:0000250|UniProtKB:P01574}.
Interaction partners:
- Interferon alpha/beta receptor 1
- Toll-like receptor 4
- Interferon regulatory factor 3
- Interferon regulatory factor 7.
- Interferon alpha/beta receptor 2
- Toll-like receptor 3
- Tyrosine-protein kinase
- Transcription factor p65
- Interferon gamma receptor 1
- Nuclear factor NF-kappa-B p105 subunit
Sequence:
MANRWTLHIAFLLCFSTTALSIDYKQLQFRQSTSIRTCQKLLRQLNGRLNLSYRTDFKIPMEVMHPSQMEKSYTAFAIQVMLQNVFLVFRSNFSSTGWNETIVESLLDELHQQTELLEIILKEKQEERLTWVTSTTTLGLKSYYWRVQRYLKDKKYNSYAWMVVRAEVFRNFSIILRLNRNFQN
Protein: Keratin, type I cytoskeletal 39 (Cytokeratin-39) (CK-39) (Keratin-39) (K39) (Type I hair keratin Ka35) (Q6A163)
Organism: Homo sapiens (Human)
Function: May play a role in late hair differentiation.
Interaction partners:
Sequence:
MDTKGCTTTNSPSTPCQNCSRITNVSTISSNNGCHPGGLTVNNCQPAGHVLRIPWDQGCQPTPRFCRKPIYLMNNFNARFSLDDCSWYGEGINSNEKETMQILNERLANYLQKVRMLERENAELESKIQEESNKELPVLCPDYLSYYTTIEELQQKILCTKAENSRLVSQIDNTKLTADDLRAKYEAEVSLRQLVESDANGLKQILNVLTLGKADLEAQVQSLKEELLCLKNNHKEEINSLQCQLGERLDIEVTAAPSADLNQVLQEMRCQYEPIMETNRKDVEQWFNTQIEELNQQVVTSSQQQQCCQKEIIELRRSVNTLEVELQAQHRMRDSQECILTETEARYTALLTQIQSLIDNLEAQLAEIRCALERQNQEYEILLDVKSRLECEITTYRSLLESSDGKRPCYPRATKCEPSPWTSCKSGAIESTAPACTSSSPCSLKEHCSACGPLSRILVKICTITKEIKDGKVISSYEHVQPCFIIRPAKV
Protein: Jacalin-related lectin 40 (Q9LKR6)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- S-adenosyl-L-methionine-dependent methyltransferases superfamily protein
- Berberine bridge enzyme-like 28
- Ulp1 protease family protein
- Vicilin-like seed storage protein At4g36700
- Expressed protein
Sequence:
MAQKLEAIGRGLQWDDSSDHDNVTKILVRGGREGIQYVKFDYVKSGQPQTGLIHGLSGRGGFTQTFEIDQKDEHLVSVEGYYDVTKGVIQALKFKTNKKTSEMIGYDDTGIKLSLEVKGKKIIGFHGYAETNLNSLGAYFTTTGPIGLNPQVGHIKLAYQGGGGGIPWDHGPNHNGVKRVSFIFDENEIRQWRVDYDDGGVIRQYEPINGYDMFEVKEYPTEYIISVECTYDDVIPRSGRRMIRSIMFKTSKGRVSPIFGYPAARKFVLENNGGALIGFHGRVGAGIDALGAYFSSFIPSPPPPSPEKLQPEGGEAVGDPWDDGIFNGVREIHLEDGEGIALKFVYDKDVQVTELKVHGEPSGIGFNEFKLDYPSEYITTVEGFWDKTSGNERGVITRLRFTTNKQTFRPVGLESTTSFSLGKEGYKIVGFHGNSSTDKLHQLGVYVVPITRE
Protein: CREB-regulated transcription coactivator 2 (Transducer of regulated cAMP response element-binding protein 2) (TORC-2) (Transducer of CREB protein 2) (Q3U182)
Organism: Mus musculus (Mouse)
Function: Transcriptional coactivator for CREB1 which activates transcription through both consensus and variant cAMP response element (CRE) sites. Acts as a coactivator, in the SIK/TORC signaling pathway, being active when dephosphorylated. Acts independently of CREB1 'Ser-133' phosphorylation. Enhances the interaction of CREB1 with TAF4. Regulates gluconeogenesis as a component of the LKB1/AMPK/TORC2 signaling pathway. Regulates the expression of specific genes such as the steroidogenic gene, StAR. Potent coactivator of PPARGC1A and inducer of mitochondrial biogenesis in muscle cells (By similarity).
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16148943, ECO:0000269|PubMed:16308421, ECO:0000269|PubMed:17805301, ECO:0000269|PubMed:29211348}. Nucleus {ECO:0000269|PubMed:16148943, ECO:0000269|PubMed:16308421, ECO:0000269|PubMed:17805301, ECO:0000269|PubMed:29211348}. Note=Translocated from the nucleus to the cytoplasm on interaction of the phosphorylated form with 14-3-3 protein (By similarity). In response to cAMP levels and glucagon, relocated to the nucleus (PubMed:16148943). {ECO:0000250|UniProtKB:Q53ET0, ECO:0000269|PubMed:16148943}.
Interaction partners:
- Cyclic AMP-responsive element-binding protein 1
- Histone lysine acetyltransferase CREBBP
- Serine/threonine-protein kinase SIK2
- Serine/threonine-protein kinase SIK1
- CREB-regulated transcription coactivator 3
- Cyclic AMP-responsive element-binding protein 3-like protein 3
- RAC-alpha serine/threonine-protein kinase
- Protein phosphatase 3 catalytic subunit alpha
- 5'-AMP-activated protein kinase catalytic subunit alpha-1
- 5'-AMP-activated protein kinase catalytic subunit alpha-2
Sequence:
MATSGANGPGSATASASNPRKFSEKIALQKQRQAEETAAFEEVMMDIGSTRLQAQKLRLAYTRSSHYGGSLPNVNQIGCGLAEFQSPLHSPLDSSRSTRHHGLVERVQRDARRMVSPLRRYPRHIDSSPYSPAYLSPPPESGWRRMMPWGNLPAEKGQLFRLPSALNRTSSDSALHTSVMNPNPQDTYPGPTPPSVLPSRRGGGFLDGEMDAKVPAIEENVVDDKHLLKPWDAKKLSSSSSRPRSCEVPGINIFPSPDQPANVPVLPPAMNTGGSLPDLTNLHFPPPLPTPLDPEETVYPSLSGGNSTTNLTHTMTHLGISGGLGLGPSYDVPGLHSPLSHPSLQSSLSNPNLQASLSSPQPQLQGSHSHPSLPASSLAHHALPTTSLGHPSLSAPALSSSSSSSSTSSPVLSAPPYPASTPGASPRHRRVPLSPLSLPAGPADARRSQQQLPKQFSPTMSPTLSSITQGVPLDTSKLPTDQRLPPYPYSPPSLVIPTHPPTPKSLQQLPSQACLVQPSGGQPPGRQPHYGALYPPGSSGHGQQPYHRPINDFSLGNLEQFNMESPSTSLVLDPPAFSEGPGFLGSEGSMSGPQDPHVLNHQNLTHCSRHGSGPNIILTGDSSPGFSKEIAAALAGVPGFEVSASGLELGLGLEDELRMEPLGLEGLTMLSDPCALLPDPAVEDSFRSDRLQ
Protein: Interleukin-18-binding protein (IL-18BP) (Tadekinig-alfa) (O95998)
Organism: Homo sapiens (Human)
Function: Isoform A binds to IL-18 and inhibits its activity. Functions as an inhibitor of the early TH1 cytokine response.
Subcellular location: Secreted {ECO:0000269|PubMed:31213488}.
Interaction partners:
- Interleukin-18
- Interleukin-37
- Interleukin-18 receptor 1
- Interleukin-18 receptor accessory protein
- Interferon gamma
Sequence:
MTMRHNWTPDLSPLWVLLLCAHVVTLLVRATPVSQTTTAATASVRSTKDPCPSQPPVFPAAKQCPALEVTWPEVEVPLNGTLSLSCVACSRFPNFSILYWLGNGSFIEHLPGRLWEGSTSRERGSTGTQLCKALVLEQLTPALHSTNFSCVLVDPEQVVQRHVVLAQLWAGLRATLPPTQEALPSSHSSPQQQG
Protein: Large ribosomal subunit protein P1z (60S acidic ribosomal protein P1-2) (O23095)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Plays an important role in the elongation step of protein synthesis.
Interaction partners:
- Large ribosomal subunit protein eL42z/eL42y
- Large ribosomal subunit protein P2w
- Large ribosomal subunit protein eL24z
- Large ribosomal subunit protein eL30x
- Large ribosomal subunit protein eL38z/eL38y
- Large ribosomal subunit protein eL21x/eL21w
- Large ribosomal subunit protein uL10x
- Large ribosomal subunit protein uL10y
- Large ribosomal subunit protein uL18y
- Large ribosomal subunit protein eL24y
Sequence:
MSTVGELACSYAVMILEDEGIAITSDKIATLVKAAGVEIESYWPMLFAKMAEKRNVTDLIMNVGAGGGGGGAPVSAAAPAAAGGAAAAAPAKEEKKDEPAEESDGDLGFGLFD
Protein: T-complex protein 1 subunit theta (CCT-theta) (Q7K3J0)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
Interaction partners:
- T-complex protein 1 subunit alpha
- T-complex protein 1 subunit delta
- T-complex protein 1 subunit eta
- T-complex protein 1 subunit epsilon
- T-complex protein 1 subunit beta
- Chaperonin containing TCP1 subunit 6
- T-complex protein 1 subunit gamma
- Uncharacterized protein
- Hsc70Cb, isoform G
- Phosducin-like protein 2
Sequence:
MALSVPKAPGVSQMLKDGARMYSGLEEAVFRNISACKEFAQTMRSAYGPNGMNKMIINHIEKQFVTSDAGTIMRELDVEHPAAKLIVMASQMQDAEVGDGTNFVVVLAGALLESAEELLRLGITTAEISDGYEKALEKALEILPNLVSHKIEDYRNVEKVKEVLRTSIMSKQYGQEDFLNDLVSKACVSILPDEGTFNVDNIRICKILGSGLTKSEVVRGMVFKRFVEGDVTYAEKAKIVIFSCPVDIIQTETKGTVLIKSADELLSFSSGEESLLESQIKAIADAGVKVVVAGGKVGDMALHFLNKYGLMAVRLNSKFDLRRLSRSVNATVLPRITTPSQEELGYCDKVCIEELGDTTIVAFRNEGKDSRIATVVIRGATDNFMDDIERALDDAINNFKCLTRDGRYLPGAGATEIELATQLSAYADTLPGLDQYAVRKFANALEVFPKALAENSGINGTEIVNQLYLAHNNEAGKTIGFDIEAEKASTIDTTKAKLFDLYQSKFWGLKYAVGAAATILKVDQIIMAKRAGGPKVRQAAGSDDES
Protein: Phospholipid-transporting ATPase (EC 7.6.2.1) (E9PEJ6)
Organism: Homo sapiens (Human)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141, ECO:0000256|RuleBase:RU362033}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141, ECO:0000256|RuleBase:RU362033}.
Interaction partners:
Sequence:
MDCSLVRTLVHRYCAGEENWVDSRTIYVGHREPPPGAEAYIPQRYPDNRIVSSKYTFWNFIPKNLFEQFRRVANFYFLIIFLVQLIIDTPTSPVTSGLPLFFVITVTAIKQGYEDWLRHKADNAMNQCPVHFIQHGKLVRKQSRKLRVGDIVMVKEDETFPCDLIFLSSNRGDGTCHVTTASLDGESSHKTHYAVQDTKGFHTEEDIGGLHATIECEQPQPDLYKFVGRINVYSDLNDPVVRPLGSENLLLRGATLKNTEKIFGVAIYTGMETKMALNYQSKSQKRSAVEKSMNAFLIVYLCILISKALINTVLKYMWQSEPFRDEPWYNQKTESERQRNLFLKAFTDFLAFMVLFNYIIPVSMYVTVEMQKFLGSYFITWDEDMFDEETGEGPLVNTSDLNEELGQVEYIFTDKTGTLTENNMEFKECCIEGHVYVPHVICNGQVLPESSGIDMIDSSPSVNGREREELFFRALCLCHTVQVKDDDSVDGPRKSPDGGKSCVYISSSPDEVALVEGVQRLGFTYLRLKDNYMEILNRENHIERFELLEILSFDSVRRRMSVIVKSATGEIYLFCKGADSSIFPRVIEGKVDQIRARVERNAVEGLRTLCVAYKRLIQEEYEGICKLLQAAKVALQDREKKLAEAYEQIEKDLTLLGATAVEDRLQEKAADTIEALQKAGIKVWVLTGDKMETAAATCYACKLFRRNTQLLELTTKRIEEQSLHDVLFELSKTVLRHSGSLTRDNLSGLSADMQDYGLIIDGAALSLIMKPREDGSSGNYRELFLEICRSCSAVLCCRMAPLQKAQIVKLIKFSKEHPITLAIGDGANDVSMILEAHVGIGVIGKEGRQAARNSDYAIPKFKHLKKMLLVHGHFYYIRISELVQYFFYKNVCFIFPQFLYQFFCGFSQQTLYDTAYLTLYNISFTSLPILLYSLMEQHVGIDVLKRDPTLYRDVAKNALLRWRVFIYWTLLGLFDALVFFFGAYFVFENTTVTSNGQIFGNWTFGTLVFTVMVFTVTLKLALDTHYWTWINHFVIWGSLLFYVVFSLLWGGVIWPFLNYQRMYYVFIQMLSSGPAWLAIVLLVTISLLPDVLKKVLCRQLWPTATERVQNGCAQPRDRDSEFTPLASLQSPGYQSTCPSAAWYSSHSQQVTLAAWKEKVSTEPPPILGGSHHHCSSIPSHSCPRSRVGMLV
Protein: Cta1p (Q5A4P1)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Interaction partners:
- Vta1p
- Vacuolar protein sorting-associated protein 4
- Vacuolar-sorting protein SNF7
- ESCRT-III subunit protein
- Vacuolar protein-sorting-associated protein 46
- Ist1p
- ESCRT-III subunit protein
- 3,4-dihydroxy-2-butanone 4-phosphate synthase
- ESCRT-III subunit protein
- Uncharacterized protein
Sequence:
MNRLFGTKSTAPKPSLNDAIKGIDERVGSLDVKLSKINSELSTYQQKISRMRDGPGKSALKQKAIKLLRQRKQIEAQKDQLENQSWNMTQASMTTDNLQNTMVTINAMKTANKSLKQTYGKINIDELEDLQDEMLDLIDKSNELQEALSTSYDVPDDISESELDAELEALGEEIDFENEMAESGIGAPSYLNDTEPTAADKLPTFIDEQPEEAQKIAN
Protein: Ubiquitin-conjugating enzyme E2 U (EC 2.3.2.23) (E2 ubiquitin-conjugating enzyme U) (Ubiquitin carrier protein U) (Ubiquitin-protein ligase U) (Q5VVX9)
Organism: Homo sapiens (Human)
Function: Catalyzes the covalent attachment of ubiquitin to other proteins.
Interaction partners:
- E3 ubiquitin-protein ligase BRE1A
- E3 ubiquitin-protein ligase BRE1B
- Ubiquitin conjugating enzyme E2 V1
- Ubiquitin-conjugating enzyme E2 variant 2
- Ubiquitin-ribosomal protein eS31 fusion protein
- Ubiquitin-like modifier-activating enzyme 1
- Ubiquitin-like modifier-activating enzyme 7
- Ubiquitin-like modifier-activating enzyme 6
- Ubiquitin-ribosomal protein eL40 fusion protein
Sequence:
MHGRAYLLLHRDFCDLKENNYKGITAKPVSEDMMEWEVEIEGLQNSVWQGLVFQLTIHFTSEYNYAPPVVKFITIPFHPNVDPHTGQPCIDFLDNPEKWNTNYTLSSILLALQVMLSNPVLENPVNLEAARILVKDESLYRTILRLFNRPLQMKDDSQELPKDPRKCIRPIKTTSFSDYYQTWSRIATSKATEYYRTPLLKVPNFIGQYYKWKKMDLQHQKEWNLKYSVIKCWLARKRMPHEVTHSMEEIKLCPTLIPTTDEIFLESPTAINSITDIYETEEEGWKSDTSLYENDTDEPREEEVEDLISWTNTLNTNTSED
Protein: Necdin homolog (Mouse) (Q5PPL0)
Organism: Rattus norvegicus (Rat)
Interaction partners:
Sequence:
MSEQSKDLSDPNFAAEDPDTEMQVSDAVPVGVPPPAPLAANLSGPSCAPEGPMAAPQASPPPAERFEEVDPKILQQAAEEGRAHQPQSPARPIPAPPAPAQLVQKAHELMWYVLVKDQKRMVLWLPDMVKEVMGSYKKWCRSILRRTSVILARVFGLHLRLTNLHTMEFALVKALSPEELDRVALNNRMPMTGLLLMILSLIYVKGRGAREGAVWNVLRILGLRPWKKHSTFGDVRKIITEEFVQQNYLKYQRVPHIEPPEYEFFWGPRANREITKMQIMEFLARVFKKDPQAWPSRYREALEQARALREANLVAQAPRSSVSED
Protein: T-cell acute lymphocytic leukemia protein 2 homolog (TAL-2) (Q62282)
Organism: Mus musculus (Mouse)
Interaction partners:
- Rhombotin-1
- Rhombotin-2
Sequence:
MTRKIFTNTRERWRQQSVNNAFAKLRKLIPTHPPDKKLSKNETLRLAMRYINFLVKVLGEQSLHQTGVAAQGNILGLFPPKTRLPDEDDRTLLNDYRVPSPGPSHGAP
Protein: Zinc finger protein 19 (Zinc finger protein KOX12) (P17023)
Organism: Homo sapiens (Human)
Function: May be involved in transcriptional regulation.
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
- NADPH oxidase 4
- Transcription intermediary factor 1-beta
Sequence:
MAAMPLKAQYQEMVTFEDVAVHFTKTEWTGLSPAQRALYRSVMLENFGNLTALGYPVPKPALISLLERGDMAWGLEAQDDPPAERTKNVCKDVETNIDSESTLIQGISEERDGMMSHGQLKSVPQRTDFPETRNVEKHQDIPTVKNIQGKVPRIPCARKPFICEECGKSFSYFSYYARHQRIHTGEKPFECSECGKAFNGNSSLIRHQRIHTGERPYQCEECGRAFNDNANLIRHQRIHSGDRPYYCTECGNSFTSSSEFVIHQRIHTGEKPYECNECGKAFVGNSPLLRHQKIHTGEKPYECNECGKSFGRTSHLSQHQRIHTGEKPYSCKVCGQAFNFHTKLTRHQRIHSEEKPFDCVDCGKAFSAQEQLKRHLRIHTQESSYVCDECGKALTSKRNLHQHQRIHTGEKPYECSKYEKAFGTSSQLGHLEHVYSGEKPVLDICRFGLPEFFTPFYW
Protein: Catabolic NAD-specific glutamate dehydrogenase RocG (NAD-GDH) (EC 1.4.1.2) (Glutamate dehydrogenase) (GlutDH) (Trigger enzyme RocG) (P39633)
Organism: Bacillus subtilis (strain 168)
Function: Devoted to catabolic function of glutamate (and other amino acids of the glutamate family) utilization as sole nitrogen source. It is not involved in anabolic function of glutamate biosynthesis since B.subtilis possesses only one route of glutamate biosynthesis from ammonia, catalyzed by glutamate synthase. Wild-type cells are unable to utilize glutamate or glutamine as a sole carbon source; thus RocG does not function physiologically to synthesize glutamate, but it is involved in the utilization of arginine, and proline as carbon or nitrogen source. The catabolic RocG is essential for controlling gltAB expression via an inhibitory interactions with the transcriptional regulator GltC in response to the availability of sugars.
Interaction partners:
- 1-pyrroline-5-carboxylate dehydrogenase
- Glutamate synthase large chain
- Glutamine synthetase
- Glutamate synthase small chain
- Transcriptional dual regulator GltC
- Protein RocB
- Aspartate aminotransferase
- Isocitrate dehydrogenase
- 2-oxoglutaramate amidase
- Arginine biosynthesis bifunctional protein ArgJ
Sequence:
MSAKQVSKDEEKEALNLFLSTQTIIKEALRKLGYPGDMYELMKEPQRMLTVRIPVKMDNGSVKVFTGYRSQHNDAVGPTKGGVRFHPEVNEEEVKALSIWMTLKCGIANLPYGGGKGGIICDPRTMSFGELERLSRGYVRAISQIVGPTKDIPAPDVYTNSQIMAWMMDEYSRLREFDSPGFITGKPLVLGGSQGRETATAQGVTICIEEAVKKKGIKLQNARIIIQGFGNAGSFLAKFMHDAGAKVIGISDANGGLYNPDGLDIPYLLDKRDSFGMVTNLFTDVITNEELLEKDCDILVPAAISNQITAKNAHNIQASIVVEAANGPTTIDATKILNERGVLLVPDILASAGGVTVSYFEWVQNNQGYYWSEEEVAEKLRSVMVSSFETIYQTAATHKVDMRLAAYMTGIRKSAEASRFRGWV
Protein: Dynein heavy chain, cytosolic (Q38DW3)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- Uncharacterized protein
- Flagellar attachment zone protein 1 conserved domain-containing protein
Sequence:
MSRRGGKDKESLLEVSQGLSGTATPRGSDRRAARGIVSPRVPGRHRADDKKEYTSVYVETVDEKTHIAEGSIVAFQFVSKGKWMWAIGTVVSDGATADGVGSSPAVTDPGLVSLLCWKVVWNSKDDVPEREERVVETAQERRERISRELYVHDVMRRENIVEGIRKDIRNISRESWKELMRLKEAPKAVLRAVRAVFELLCIELVASSESDEWDQMKRFMASSAFTDLLSDPNAVRMDDALADALNEKYLSDRLFDFTVVSANNRLAGLLQKWVTSEVYLYKARASLRMIDDQLSDTMGAQGSKFSASLRSGNSSTRVRPFSGRDGEDSVKMTVRSFSESGEISFVRTDEKVVVLQMSIFCKLIPLTGPLKSREMILKRDSIAQIRSAASKQLRGTPRGSNVATRVAGDRHVTESYVSTAPTGLTHIFCNQSIERLRLVARELGSLFDLHQMFTAERWKIMHRDTTSLRDRPNNISSKSADSERKLSRAMKRINELEGHLREKEDELRDVWGKTEEETKSLKKHVRSRSDEDSERRVNRGCGLNFRILCLLQDEEVNRMRLGTIEIQERFMLQLRETRSSNDMALNELKAEYVKETIALQREVSNLEGCQQRALSILRECLSRTQEGPLKHQQYVEKEDLHSCLLDVEQAMMELGASRLPSTHLFSERSDECTEHRTSRITTRRDAHAQTHALERLKNVVDDVGDNDVILIKDRLVEAMYDRELIQELLTREQQKCRELEKKEETLLLDLEQVTNQRTELDEEVQVLQAEVEALTKALKRATDGNKDADVHGARRPNSKKSGMDFMDGDDEQQTTEVAETFNSANTVQDQWLINLLEEEGVDHSGGVFTALCTYIEQLKANRATLEADRDMHASEARMLEMCLKTAADALEDALLHDERWRPRTTSSQHTTFHSKKFPGDDWGLVAANTPEALVNAIVHDVAAACHLPEDYVLDVDYRDDGVELHVTFDLRHDPSITTEEIARRLEECNFYEMEKIYANRHERKSGIDELRRDLQAKVEEINALRGTLRRLQTGTSGYSYSSR
Protein: ADP-ribosylhydrolase ARH3 (EC 3.2.1.143) (ADP-ribose glycohydrolase ARH3) (ADP-ribosylhydrolase 3) (O-acetyl-ADP-ribose deacetylase ARH3) (Poly(ADP-ribose) glycohydrolase ARH3) ([Protein ADP-ribosylarginine] hydrolase-like protein 2) ([Protein ADP-ribosylserine] hydrolase) (G3H9W3)
Organism: Cricetulus griseus (Chinese hamster) (Cricetulus barabensis griseus)
Interaction partners:
Sequence:
MARALVQSLLAKEAFDEVDMAHRFAQEYKKDPDRGYGAGVITVFKKLLSPKCRDVYEPARAQFNGKGSYGNGGAMRVAGIPLAYSSVKDVQKFARLSAQLTHASSLGYNGAILQALAVHLALQGVSSSEHFLKQLVGHMEELEGDAQSILDAKELGMEERPYSSRLKKVAELLDQEVVSREEVVSELGNGIAAFESVPTAIYCFLRCMEPDPEIPSTFNSLQRTLIYSISLGGDTDTIATMAGAIAGAYYGMEQVPESWQQSCEGYEETDVLAQSLHRVFQKSV
Protein: Uncharacterized protein YcbX (P75863)
Organism: Escherichia coli (strain K12)
Interaction partners:
- Sulfite reductase flavoprotein alpha-component
- Protein YiiM
- NADH oxidoreductase HCR
- 1,2-phenylacetyl-CoA epoxidase, subunit E
- NADH-quinone oxidoreductase subunit C/D
- NAD
- GTP 3',8-cyclase
- Molybdopterin synthase catalytic subunit
- Cyclic pyranopterin monophosphate synthase
Sequence:
MATLIRLFIHPVKSMRGIGLTHALADVSGLAFDRIFMITEPDGTFITARQFPQMVRFTPSPVHDGLHLTAPDGSSAYVRFADFATQDAPTEVWGTHFTARIAPDAINKWLSGFFSREVQLRWVGPQMTRRVKRHNTVPLSFADGYPYLLANEASLRDLQQRCPASVKMEQFRPNLVVSGASAWEEDRWKVIRIGDVVFDVVKPCSRCIFTTVSPEKGQKHPAGEPLKTLQSFRTAQDNGDVDFGQNLIARNSGVIRVGDEVEILATAPAKIYGAAAADDTANITQQPDANVDIDWQGQAFRGNNQQVLLEQLENQGIRIPYSCRAGICGSCRVQLLEGEVTPLKKSAMGDDGTILCCSCVPKTALKLAR
Protein: Large ribosomal subunit protein uL29c (50S ribosomal protein L29, chloroplastic) (CL29) (Q9FJP3)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Plastid, chloroplast {ECO:0000250}.
Interaction partners:
- Large ribosomal subunit protein uL13c
- Small ribosomal subunit protein uS9c
- Large ribosomal subunit protein bL17c
- Large ribosomal subunit protein uL24c
- Large ribosomal subunit protein bL27c
- Large ribosomal subunit protein bL9c
- Large ribosomal subunit protein uL23z
- Large ribosomal subunit protein eL21z/eL21y
- Large ribosomal subunit protein uL23y
- Large ribosomal subunit protein uL6c
Sequence:
MLSLSIATPGTAAIFRRGTASATSTSSSFHGVRIQHQVSARVPAAATISSSSPKPSVVMMSKREAELKEIRSKTTEQLQEEVVDLKGELFMLRLQKSARNEFKSSDFRRMKKQVARMLTVKREREIKEGIKKRLSRKLDRQWKKSIVPRPPPSLKKLQEEEAAEEAAEAAKSA
Protein: F10K1.14 protein (Mitogen-activated protein kinase kinase kinase 13) (Q9LMK8)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- Protein kinase ATN1-like protein
- RAF-like serine/threonine-protein kinase 20
Sequence:
MEKQSIRNTCSSSLMLSSPSSFWVRGACIGRGCFGAVSTAISKTNGEVFAVKSVDLATSLPTQSESLENEISVFRSLKPHPYIVKFLGDGVSKEGTTTFRNLYLEYLPNGDVASHRAGGKIEDETLLQRYTACLVSALRHVHSQGFVHCDVKARNILVSQSSMVKLADFGSAFRIHTPRALITPRGSPLWMAPEVIRREYQGPESDVWSLGCTIIEMFTGKPAWEDHGIDSLSRISFSDELPVFPSKLSEIGRDFLEKCLKRDPNQRWSCDQLLQHPFLSQCHNSSPTESSPRCVLDWVNSGFDLEEEEEEVGRSEFEDAAKAIICNLATTGGVIWESDGWVEVRCHASEEEGTTMEYSGSTRVESEYNTSSDPNDDVAGDSAIIDVSMSQNLPPGNGGSAAALPYEFVVVLHLLMEIMVYTTCIFREIVLTMYLLYQYNQSNKLETLSFNHSLKFCLFAHVIRIGQNYLLRGEMRSSVLITSHCLILITLVYSQIVVF
Protein: Adapter protein MecA 1 (P37958)
Organism: Bacillus subtilis (strain 168)
Function: Enables the recognition and targeting of unfolded and aggregated proteins to the ClpC protease or to other proteins involved in proteolysis. Acts negatively in the development of competence by binding ComK and recruiting it to the ClpCP protease. When overexpressed, inhibits sporulation. Also involved in Spx degradation by ClpC.
Interaction partners:
- Negative regulator of genetic competence ClpC/MecB
- Competence protein S
- Competence transcription factor
- ATP-dependent Clp protease proteolytic subunit
- ATP-dependent Clp protease ATP-binding subunit ClpX
- ClpXP adapter protein SpxH
- Protein-arginine kinase
- Global transcriptional regulator Spx
- Competence protein CoiA
- Transition state regulatory protein AbrB
Sequence:
MEIERINEHTVKFYMSYGDIEDRGFDREEIWYNRERSEELFWEVMDEVHEEEEFAVEGPLWIQVQALDKGLEIIVTKAQLSKDGQKLELPIPEDKKQEPASEDLDALLDDFQKEEQAVNQEEKEQKLQFVLRFGDFEDVISLSKLNVNGSKTTLYSFENRYYLYVDFCNMTDEEVENQLSILLEYATESSISIHRLEEYGKLIISEHALETIKKHFAS