wanglab/gogpt-training-data huggingface dataset:
Protein: Protein SDS23 (P53172)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Involved in DNA replication and cell separation during budding.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:14562095}. Nucleus {ECO:0000269|PubMed:14562095}.
Interaction partners:
- Cruciform DNA-recognizing protein 1
- SNF1 protein kinase subunit beta-2
- SNF1 protein kinase subunit beta-3
- Signal transduction protein MDG1
- SNF1 protein kinase subunit beta-1
- GMP synthase
- SIT4-associating protein SAP155
- Multifunctional tryptophan biosynthesis protein
- Protein SDS24
- Putative glutamine amidotransferase YLR126C
Sequence:
MPQNTRHTSIVEMLSTPPQLPNSTDLNSLSEQTDKNTEANKSDTESLHKSISKSSSSSSLSTLDNTEYSNNNGNSLSTLNSQNLLSVHRQEWQHTPLSNLVEQNKLIFIRGSISVEEAFNTLVKHQLTSLPVENFPGDMNCLTFDYNDLNAYLLLVLNRIKVSNDKITSDCQNGKSVPVGEIVKLTPKNPFYKLPETENLSTVIGILGSGVHRVAITNVEMTQIKGILSQRRLIKYLWENARSFPNLKPLLDSSLEELNIGVLNAARDKPTFKQSRVISIQGDEHLIMALHKMYVERISSIAVVDPQGNLIGNISVTDVKHVTRTSQYPLLHNTCRHFVSVILNLRGLETGKDSFPIFHVYPTSSLARTFAKLVATKSHRLWIVQPNDNQPTASSEKSSSPSPSTPPVTTLPSLASSYHSNTQSSRMANSPVLKSSDTSNNKINVNINLSGPSPSQPQSPSATMPPPQSPSNCPASPTPAHFEKEYRTGKLIGVVSLTDILSVLARKQTHHKEIDPQMARKQRGHIG
Protein: Homeobox protein SIX3 (Sine oculis homeobox homolog 3) (O73916)
Organism: Oryzias latipes (Japanese rice fish) (Japanese killifish)
Function: Transcriptional regulator which can act as both a transcriptional repressor and activator by binding a ATTA homeodomain core recognition sequence on these target genes. During forebrain development represses WNT1 expression allowing zona limitans intrathalamica formation and thereby ensuring proper anterio-posterior patterning of the diencephalon and formation of the rostral diencephalon. Acts as a direct upstream activator of SHH expression in the rostral diencephalon ventral midline and that in turn SHH maintains its expression. In addition, Six3 activity is required for the formation of the telencephalon. During postnatal stages of brain development is necessary for ependymal cell maturation by promoting the maturation of radial glia into ependymal cells through regulation of neuroblast proliferation and migration. Acts on the proliferation and differentiation of neural progenitor cells through activating transcription of CCND1 and CCND2. During early lens formation plays a role in lens induction and specification by activating directly PAX6 in the presumptive lens ectoderm. In turn PAX6 activates SIX3 resulting in activation of PDGFRA and CCND1 promoting cell proliferation. Also is required for the neuroretina development by directly suppressing WNT8B expression in the anterior neural plate territory. Its action during retina development and lens morphogenesis is AES and TLE4-dependent manner. Furthermore, during eye development regulates several genes expression. Before and during early lens development represses the CRYGF promoter by binding a SIX repressor element. Directly activates RHO transcription, or cooperates with CRX or NRL. Six3 functions also in the formation of the proximodistal axis of the optic cup, and promotes the formation of optic vesicles-like structures. During pituitary development, acts in parallel or alternatively with HESX1 to control cell proliferation through Wnt/beta-catenin pathway. Plays a role in eye development by suppressing WNT1 expression and in dorsal-ventral patterning by repressing BMP signaling pathway.
Subcellular location: Nucleus {ECO:0000250|UniProtKB:Q62233, ECO:0000255|PROSITE-ProRule:PRU00108}.
Interaction partners:
Sequence:
MVFRAPLDFISASRLLLPHFADAPPVLSRSRSPEHPPAGFLSLALPGLCFSATQIASVCETLEETGDIERLARFLWSLPVNTDGRDSISEHESVQRARAVVAFHTGCYRELYRILETHRFTRASHSKLQAMWLEAHYREAEKLRGRPLGPVDKYRVRKKFPLPRTIWDGEQKTHCFKERTRGLLREWYLQDPYPNPGKKRELAHATGLTPTQVGNWFKNRRQRDRAAAAKNRLQHHRICPDSACTLSGGDSSERADGDTFLSVTDSDSDLDV
Protein: MEC1-mediated checkpoint protein HUG1 (Q6Q5K6)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Involved in the MEC1-mediated checkpoint response to DNA damage and replication arrest.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:14562095}. Nucleus {ECO:0000305|PubMed:14562095}.
Interaction partners:
- Ribonucleoside-diphosphate reductase small chain 1
- Ribonucleoside-diphosphate reductase large chain 2
- Ribonucleoside-diphosphate reductase small chain 2
- Serine/threonine-protein kinase MEC1
- DNA damage response protein kinase DUN1
- Damage-regulated import facilitator 1
- Serine/threonine-protein kinase RAD53
- Ribonucleotide reductase inhibitor protein SML1
- Ribonucleoside-diphosphate reductase large chain 1
Sequence:
MTMDQGLNPKQFFLDDVVLQDTLCSMSNRVNKSVKTGYLFPKDHVPSANIIAVERRGGLSDIGKNTSN
Protein: Heat shock protein Hsp-12.2 (P34328)
Organism: Caenorhabditis elegans
Interaction partners:
- Heat-shock protein 12.1
- J domain-containing protein
Sequence:
MSAIEVTADAASTWDWPLQHNDGVVKVHNTKEKFEVGLDVQFFTPKEIEVKVSGQELLIHCRHETRSDNHGTVAREINRAYKLPDDVDVSTVKSHLATRGVLTITASKKA
Protein: Phosphatidylinositol 3-kinase catalytic subunit type 3 (PI3-kinase type 3) (PI3K type 3) (EC 2.7.1.137) (Phosphoinositide-3-kinase class 3) (Q9TXI7)
Organism: Caenorhabditis elegans
Function: Catalytic subunit of the PI3K complex that mediates formation of phosphatidylinositol 3-phosphate. Together with bec-1, mediates the production of phosphatidylinositol 3-phosphate on intracellular vesicles and thereby regulates membrane trafficking. Plays a role in endosome-to-Golgi retrograde transport of mig-14. Involved in clearance of apoptotic cell corpses by phagosomes. Phagosome maturation requires two sequential and non-overlapping pulses of phosphatidylinositol-3-phosphate (PI3P) on the vesicle surface which mediates recruitment of sortins snx-1 and lst-4 and small GTPases rab-5, rab-2 and rab-7, downstream of dynamin dyn-1. The first pulse is initiated by piki-1, then maintained by vps-34 which also produces the second pulse. Required for embryonic development. Together with bec-1, involved in L3/L4 larval molting stage probably by regulating cuticle shedding. Regulates the expansion of the nucleus outer membrane. Involved in the secretion and localization of lrp-1 at the apical surface of hyp7 syncytium. May regulate endocytosis in hypodermal cells. May play a role in the formation of gut granules (a lysosome-related organelle). Plays a role in germ stem cell proliferation during larval development.
Subcellular location: Nucleus outer membrane {ECO:0000269|PubMed:11927551}; Peripheral membrane protein {ECO:0000269|PubMed:11927551}. Cytoplasm {ECO:0000269|PubMed:11927551}. Cytoplasmic granule {ECO:0000269|PubMed:11927551}. Cell projection, phagocytic cup {ECO:0000269|PubMed:18425118}. Note=Colocalizes with rab-5 and dyn-1 at the phagocytic cup. {ECO:0000269|PubMed:18425118}.
Interaction partners:
- small monomeric GTPase
- non-specific serine/threonine protein kinase
- Beclin homolog
- MRG domain-containing protein
- Serine/threonine-protein kinase unc-51
- UV radiation resistance-associated gene protein-like
- Autophagy-related protein 5
- Autophagy-related protein 13 homolog
- Ubiquitin-like protein atg-12
- Ubiquitin-like modifier-activating enzyme ATG7
Sequence:
MIPGMRATPTESFSFVYSCDLQTNVQVKVAEFEGIFRDVLNPVRRLNQLFAEITVYCNNQQIGYPVCTSFHTPPDSSQLARQKLIQKWNEWLTLPIRYSDLSRDAFLHITIWEHEDDEIVNNSTFSRRLVAQSKLSMFSKRGILKSGVIDVQMNVSTTPDPFVKQPETWKYSDAWGDEIDLLFKQVTRQSRGLVEDVPWLDPFASRRIEMIRAKYKYSSPDRHVFLVLEMAAIRLGPTFYKVVYYEDETKNMRVSTSVNGGVGIVSACTRYCVADPELLLESLAEVKHSAMTRRIRDVEDERHRQVKPNKQAKDRLETIVNLPSSQVLTREQRDLVWKFRHYLRQFPKALNKYLRSVNWVHPQEVKTALALMNDWELIEAEDALELLSSAFTHPAVRAYSVSRLLEAASPEQVLLYLPQLVQALKYEQGQQLPEEGNPVPVVSEEEGKIPSVATTPTEELEGRDMTVVTKKEARKAASGDLATFLIDYALASPKVSNYLYWHLKTEIESTKESKEEHSKMYQNIQDRLMEALVKRPDTRAQVDSLHQQQIFVEDLIILMNEAKARGGRLNESKSAEFRTMLSRAKHMLDLKGVHLPLDPSFRLSSVIPDTASFFKSEMMPAKISFKVLQPNGKADRNIPEEYTVIFKTGDDLRQDQLIQQMVRLIDIILKKGQLDLKLTPYLVLSTGVGQGFVQCIKSKPLRAIQEQYKAHKMDCIREAMKELRPGDGPFGIEPNVIDNYVRSLAGYSVIMYILGLGDRHLDNLLLCENGKLFHVDFGFILGRDPKPMPPPMKLTSEMVQVMGGVKSKQFLEFVQHVDSAYRILRRHSNVLLNLFSLMLDAGIPDIAAEPDKAIFKIEQRLRLDLSDEAATKHIFTQIESSLNAKMAMISDIIHAYKQNLM
Protein: Phosphatidylserine synthase 1 (PSS-1) (PtdSer synthase 1) (EC 2.7.8.29) (Serine-exchange enzyme I) (P48651)
Organism: Homo sapiens (Human)
Function: Catalyzes a base-exchange reaction in which the polar head group of phosphatidylethanolamine (PE) or phosphatidylcholine (PC) is replaced by L-serine. Catalyzes mainly the conversion of phosphatidylcholine. Also converts, in vitro and to a lesser extent, phosphatidylethanolamine.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q99LH2}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q99LH2}. Note=Highly enriched in the mitochondria-associated membrane (MAM). {ECO:0000250|UniProtKB:Q99LH2}.
Interaction partners:
- Phosphatidylserine decarboxylase proenzyme, mitochondrial
- Phosphatidylethanolamine N-methyltransferase
- Choline/ethanolaminephosphotransferase 1
- Cholinephosphotransferase 1
- Phosphatidylserine synthase 2
- Membrane-bound glycerophospholipid O-acyltransferase 2
- Phospholipase D2
- Phospholipase D1
- Phospholipase A1 member A
- Phosphatidylcholine-sterol acyltransferase
Sequence:
MASCVGSRTLSKDDVNYKMHFRMINEQQVEDITIDFFYRPHTITLLSFTIVSLMYFAFTRDDSVPEDNIWRGILSVIFFFLIISVLAFPNGPFTRPHPALWRMVFGLSVLYFLFLVFLLFLNFEQVKSLMYWLDPNLRYATREADVMEYAVNCHVITWERIISHFDIFAFGHFWGWAMKALLIRSYGLCWTISITWELTELFFMHLLPNFAECWWDQVILDILLCNGGGIWLGMVVCRFLEMRTYHWASFKDIHTTTGKIKRAVLQFTPASWTYVRWFDPKSSFQRVAGVYLFMIIWQLTELNTFFLKHIFVFQASHPLSWGRILFIGGITAPTVRQYYAYLTDTQCKRVGTQCWVFGVIGFLEAIVCIKFGQDLFSKTQILYVVLWLLCVAFTTFLCLYGMIWYAEHYGHREKTYSECEDGTYSPEISWHHRKGTKGSEDSPPKHAGNNESHSSRRRNRHSKSKVTNGVGKK
Protein: Alcohol dehydrogenase, propanol-preferring (EC 1.1.1.1) (P39451)
Organism: Escherichia coli (strain K12)
Function: Preferred specificity is towards 1-propanol.
Interaction partners:
- Bifunctional aldehyde-alcohol dehydrogenase AdhE
- Probable alcohol dehydrogenase EutG
- Probable alcohol dehydrogenase
- Aldehyde reductase Ahr
- Aldehyde reductase YahK
- Aldehyde dehydrogenase B
- S-
- Lactaldehyde reductase
- NADPH-dependent aldehyde reductase YqhD
- Acetaldehyde dehydrogenase
Sequence:
MKAAVVTKDHHVDVTYKTLRSLKHGEALLKMECCGVCHTDLHVKNGDFGDKTGVILGHEGIGVVAEVGPGVTSLKPGDRASVAWFYEGCGHCEYCNSGNETLCRSVKNAGYSVDGGMAEECIVVADYAVKVPDGLDSAAASSITCAGVTTYKAVKLSKIRPGQWIAIYGLGGLGNLALQYAKNVFNAKVIAIDVNDEQLKLATEMGADLAINSHTEDAAKIVQEKTGGAHAAVVTAVAKAAFNSAVDAVRAGGRVVAVGLPPESMSLDIPRLVLDGIEVVGSLVGTRQDLTEAFQFAAEGKVVPKVALRPLADINTIFTEMEEGKIRGRMVIDFRH
Protein: Tubulin alpha chain (A9PL17)
Organism: Gossypium hirsutum (Upland cotton) (Gossypium mexicanum)
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000256|ARBA:ARBA00004245}.
Interaction partners:
- Uncharacterized protein LOC107899987
- Tubulin beta chain
- Tubulin beta chain
- Tubulin beta chain
- Tubulin beta chain
- Tubulin beta chain
- Tubulin beta chain
- Tubulin beta chain
- Tubulin beta chain
- Tubulin beta chain
Sequence:
MREIISVHIGQAGIQVGNSCWELYCLEHEIHPDGTMPSDTSMGVAHDAFNTFFSETGSGKHVPRAVFVDLEPTVIDEVRTGPYRQLFHPEQLISGKEDAANNFARGHYTIGKEIVDLCLDRVRKLADNCTGLQGFMVFNAVGGGTGSGLGSLLLERLSVDYGKKSKLGFTIYPSPQVSTAVVEPYNSVLSTHSLLEHTDVAVLLDNEAIYDICRRSLDIERPTYTNLNRLISQTISSLTTSLRFDGAINVDITEFQTNLVPYPRIHFMLSSYAPVISAEKAYHEQISVPEITNAVFEPSSMMAKCDPRHGKYMACCLMYRGDVVPKDVNAAVATIKTKRTVQFVDWCPTGFKCGINYQPPAVVPGGDLAKVQRAVCMISNNTAVAEVFARIDHKFDLMYSKRAFVHWYVGEGMEEGEFSEAREDLAALEKDYEEVGAEGGDDEEEGEEY
Protein: Uncharacterized protein, isoform D (M9PDQ9)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- RRM domain-containing protein
- LD05247p
- Uncharacterized protein, isoform A
- Uncharacterized protein, isoform B
- ZP domain-containing protein
- FI20203p1
Sequence:
MGEVPKIKNLPQVIEPHLPEGCTLDSYSTSYLTKPGDNYGSIMLSVQAKIRSADGGIRDLPLIAKLPPLTNDLYWQIFQPERTCITENAVYQYLSPELDKLQLESGILPAQIFDGFPRYYGSRVSLDNRATKVDRDAVLVQENVTTRGYRPGNRHRPYNLAETVLILHYLAQYHALPIALRLKKPQVYEEYVRPYFKKFDMNSNIDQAETEIMNKEILKDIKLVTSDERDVNRVKELLDIFQAFQASNDVDDGPFTTLVHGDLWINNMMLKYGMRGEEGTPLKVKIVDFQIAQYGSLVHDIIFVLFSSVDVNVLEDNFYNFLTIYYNAFIQTLRSVNVDTSNYTYELFLEEVQQTAHVQLPHAIFMMKVILADNSTIPKDYKDVDFSVLTKNTGAKTIVTKFEAILRLGKKFNIFY
Protein: Protein ROS1A (EC 3.2.2.-) (Protein REPRESSOR OF SILENCING 1 homolog a) (Protein ROS1 homolog) (OsROS1) (Protein THICK ALEURONE 2) (C7IW64)
Organism: Oryza sativa subsp. japonica (Rice)
Function: Bifunctional DNA glycosylase/lyase, which excises 5-methylcytosine (5-meC) and 5-hydroxymethylcytosine (5-hmeC), leaving an apyrimidinic (AP) site that is subsequently incised by the lyase activity (Probable). DNA demethylase that is indispensable in both male and female gametophyte development. Involved in the regulation of DNA methylation in the promoters of RISBZ1/BZIP58 and DOF3/RPBF, two transcription factors that functions synergistically to positively regulate genes that are key players in the development of aleurone layers. Active DNA demethylation carried out by ROS1A in rice endosperms may restrict the number of aleurone cell layers.
Subcellular location: Nucleus {ECO:0000250|UniProtKB:B8YIE8}.
Interaction partners:
Sequence:
MQDFGQWLPQSQTTADLYFSSIPIPSQFDTSIETQTRTSAVVSSEKESANSFVPHNGTGLVERISNDAGLTEVVGSSAGPTECIDLNKTPARKPKKKKHRPKVLKDDKPSKTPKSATPIPSTEKVEKPSGKRKYVRKKTSPGQPPAEQAASSHCRSELKSVKRSLDFGGEVLQESTQSGSQVPVAEICTGPKRQSIPSTIQRDSQSQLACHVVSSTSSIHTSASQMVNAHLFPPDNMPNGVLLDLNNSTSQLQNEHAKFVDSPARLFGSRIRQTSGKNSLLEIYAGMSDRNVPDLNSSISQTHSMSTDFAQYLLSSSQASVRETQMANQMLNGHRMPENPITPSHCIERAALKEHLNHVPHAKAAVMNGQMPHSYRLAQNPILPPNHIEGYQVMENLSELVTTNDYLTASPFSQTGAANRQHNIGDSMHIHALDPRRESNASSGSWISLGVNFNQQNNGWASAGAADAASSHAPYFSEPHKRMRTAYLNNYPNGVVGHFSTSSTDLSNNENENVASAINSNVFTLADAQRLIAREKSRASQRMISFRSSKNDMVNRSEMVHQHGRPAPHGSACRESIEVPDKQFGLMTEELTQLPSMPNNPQREKYIPQTGSCQLQSLEHDMVKGHNLAGELHKQVTSPQVVIQSNFCVTPPDVLGRRTSGEHLRTLIAPTHASTCKDTLKALSCQLESSRDIIRPPVNPIGPSSADVPRTDNHQVKVSEETVTAKLPEKRKVGRPRKELKPGEKPKPRGRPRKGKVVGGELASKDSHTNPLQNESTSCSYGPYAGEASVGRAVKANRVGENISGAMVSLLDSLDIVIQKIKVLDINKSEDPVTAEPHGALVPYNGEFGPIVPFEGKVKRKRSRAKVDLDPVTALMWKLLMGPDMSDCAEGMDKDKEKWLNEERKIFQGRVDSFIARMHLVQGDRRFSPWKGSVVDSVVGVFLTQNVSDHLSSSAFMALAAKFPVKPEASEKPANVMFHTISENGDCSGLFGNSVKLQGEILVQEASNTAASFITTEDKEGSNSVELLGSSFGDGVDGAAGVYSNIYENLPARLHATRRPVVQTGNAVEAEDGSLEGVVSSENSTISSQNSSDYLFHMSDHMFSSMLLNFTAEDIGSRNMPKATRTTYTELLRMQELKNKSNETIESSEYHGVPVSCSNNIQVLNGIQNIGSKHQPLHSSISYHQTGQVHLPDIVHASDLEQSVYTGLNRVLDSNVTQTSYYPSPHPGIACNNETQKADSLSNMLYGIDRSDKTTSLSEPTPRIDNCFQPLSSEKMSFAREQSSSENYLSRNEAEAAFVKQHGTSNVQGDNTVRTEQNGGENSQSGYSQQDDNVGFQTATTSNLYSSNLCQNQKANSEVLHGVSSNLIENSKDDKKTSPKVPVDGSKAKRPRVGAGKKKTYDWDMLRKEVLYSHGNKERSQNAKDSIDWETIRQAEVKEISDTIRERGMNNMLAERIKDFLNRLVRDHGSIDLEWLRYVDSDKAKDYLLSIRGLGLKSVECVRLLTLHHMAFPVDTNVGRICVRLGWVPLQPLPESLQLHLLEMYPMLENIQKYLWPRLCKLDQRTLYELHYQMITFGKVFCTKSKPNCNACPMRAECKHFASAFASARLALPGPEEKSLVTSGTPIAAETFHQTYISSRPVVSQLEWNSNTCHHGMNNRQPIIEEPASPEPEHETEEMKECAIEDSFVDDPEEIPTIKLNFEEFTQNLKSYMQANNIEIEDADMSKALVAITPEVASIPTPKLKNVSRLRTEHQVYELPDSHPLLEGFNQREPDDPCPYLLSIWTPGETAQSTDAPKSVCNSQENGELCASNTCFSCNSIREAQAQKVRGTLLIPCRTAMRGSFPLNGTYFQVNEVFADHDSSRNPIDVPRSWIWNLPRRTVYFGTSIPTIFKGLTTEEIQHCFWRGFVCVRGFDRTSRAPRPLYARLHFPASKITRNKKSAGSAPGRDDE
Protein: Beta-1,4-glucuronyltransferase 1 (EC 2.4.1.-) (I-beta-1,3-N-acetylglucosaminyltransferase) (iGnT) (N-acetyllactosaminide beta-1,3-N-acetylglucosaminyltransferase) (Poly-N-acetyllactosamine extension enzyme) (UDP-GlcNAc:betaGal beta-1,3-N-acetylglucosaminyltransferase 1) (O43505)
Organism: Homo sapiens (Human)
Function: Beta-1,4-glucuronyltransferase involved in O-mannosylation of alpha-dystroglycan (DAG1). Transfers a glucuronic acid (GlcA) residue onto a xylose (Xyl) acceptor to produce the glucuronyl-beta-1,4-xylose-beta disaccharide primer, which is further elongated by LARGE1, during synthesis of phosphorylated O-mannosyl glycan. Phosphorylated O-mannosyl glycan is a carbohydrate structure present in alpha-dystroglycan (DAG1), which is required for binding laminin G-like domain-containing extracellular proteins with high affinity. Required for axon guidance; via its function in O-mannosylation of alpha-dystroglycan (DAG1) (By similarity).
Subcellular location: Golgi apparatus membrane {ECO:0000269|PubMed:19587235, ECO:0000269|PubMed:23359570, ECO:0000269|PubMed:25279699}; Single-pass type II membrane protein {ECO:0000269|PubMed:23359570}. Note=Localizes near the trans-Golgi apparatus. {ECO:0000269|PubMed:25279699}.
Interaction partners:
- Ribitol-5-phosphate xylosyltransferase 1
- Xylosyl- and glucuronyltransferase LARGE2
- Xylosyl- and glucuronyltransferase LARGE1
- Protein O-mannose kinase
- Protein O-linked-mannose beta-1,4-N-acetylglucosaminyltransferase 2
- Protein O-mannosyl-transferase 1
- UDP-GalNAc:beta-1,3-N-acetylgalactosaminyltransferase 2
- Ribitol-5-phosphate transferase FKTN
- Ribitol 5-phosphate transferase FKRP
- Protein O-mannosyl-transferase 2
Sequence:
MQMSYAIRCAFYQLLLAALMLVAMLQLLYLSLLSGLHGQEEQDQYFEFFPPSPRSVDQVKAQLRTALASGGVLDASGDYRVYRGLLKTTMDPNDVILATHASVDNLLHLSGLLERWEGPLSVSVFAATKEEAQLATVLAYALSSHCPDMRARVAMHLVCPSRYEAAVPDPREPGEFALLRSCQEVFDKLARVAQPGINYALGTNVSYPNNLLRNLAREGANYALVIDVDMVPSEGLWRGLREMLDQSNQWGGTALVVPAFEIRRARRMPMNKNELVQLYQVGEVRPFYYGLCTPCQAPTNYSRWVNLPEESLLRPAYVVPWQDPWEPFYVAGGKVPTFDERFRQYGFNRISQACELHVAGFDFEVLNEGFLVHKGFKEALKFHPQKEAENQHNKILYRQFKQELKAKYPNSPRRC
Protein: Beta-transducin repeat containing isoform 3 (A0A0S2Z507)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MDPAEAVLQEKALKFMSRFVAQAGVKWRDLGSLQTPPLASSDSRGLQCSMPRSLWLGCSSLADSMPSLRCLYNPGTGALTAFQNSSEREDCNNGEPPRKIIPEKNSLRQTYNSCARLCLNQETVCLASTAMKTENCVAKTKLANGTSSMIVPKQRKLSASYEKEKELCVKYFEQWSESDQVEFVEHLISQMCHYQHGHINSYLKPMLQRDFITALPARGLDHIAENILSYLDAKSLCAAELVCKEWYRVTSDGMLWKKLIERMVRTDSLWRGLAERRGWGQYLFKNKPPDGNAPPNSFYRALYPKIIQDIETIESNWRCGRHSLQRIHCRSETSKGVYCLQYDDQKIVSGLRDNTIKIWDKNTLECKRILTGHTGSVLCLQYDERVIITGSSDSTVRVWDVNTGEMLNTLIHHCEAVLHLRFNNGMMVTCSKDRSIAVWDMASPTDITLRRVLVGHRAAVNVVDFDDKYIVSASGDRTIKVWNTSTCEFVRTLNGHKRGIACLQYRDRLVVSGSSDNTIRLWDIECGACLRVLEGHEELVRCIRFDNKRIVSGAYDGKIKVWDLVAALDPRAPAGTLCLRTLVEHSGRVFRLQFDEFQIVSSSHDDTILIWDFLNDPAAQAEPPRSPSRTYTYISR
Protein: 4-substituted benzoates-glutamate ligase GH3.12 (EC 6.3.2.-) (Auxin-responsive GH3-like protein 12) (AtGH3-12) (Protein GH3-LIKE DEFENSE GENE 1) (Protein GRETCHEN HAGEN 3.12) (Protein HOPW1-1-INTERACTING 3) (Protein avrPPHB SUSCEPTIBLE 3) (Q9LYU4)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Catalyzes the conjugation of specific amino acids (e.g. Glu and possibly His, Lys, and Met) to their preferred acyl substrates (e.g. 4-substituted benzoates), in a magnesium ion- and ATP-dependent manner. Can use 4-substituted benzoates such as 4-aminobenzoate (pABA), 4-fluorobenzoate and 4-hydroxybenzoate (4-HBA), and, to a lesser extent, benzoate, vanillate and trans-cinnamate, but not 2-substituted benzoates and salicylic acid (SA), as conjugating acyl substrates. Involved in both basal and induced resistance in a SA-dependent manner. Confers resistance to virulent and avirulent pathogens (at least bacteria and oomycetes), and promotes SA glucosides accumulation. Required for the establishment of hyper-sensitive response (HR) upon incompatible interaction and subsequent systemic acquired resistance (SAR).
Interaction partners:
- Protein ENHANCED PSEUDOMONAS SUSCEPTIBILITY 1
- Isochorismate synthase 1, chloroplastic
- Calmodulin-binding protein 60 G
- Probable flavin-containing monooxygenase 1
- Protein SAR DEFICIENT 1
- Lipase-like PAD4
- Protein EDS1
- Probable WRKY transcription factor 46
- Aminotransferase ALD1, chloroplastic
- Regulatory protein NPR1
Sequence:
MKPIFDINETFEKQLKDLTSNVKSIQDNLLEEIITPNTKTEYLQRFLIDRFDKELFKKNVPIVSYEDIKPYLDRVVNGESSDVISARTITGFLLSSGTSGGAQKMMPWNNKYLDNLTFIYDLRMQVITKHVKGVEEGKGMMFLFTKQESMTPSGLPARVATSSYFKSDYFKNRPSNWYYSYTSPDEVILCPNNTESLYCHLLCGLVQRDEVVRTGSIFASVMVRAIEVLKNSWEELCSNIRSGHLSNWVTDLGCQNSVSLVLGGPRPELADTIEEICNQNSWKGIVKRLWPNTKYIETVVTGSMGQYVPMLNYYCNDLPLVSTTYGSSETTFGINLDPLCKPEDVSYTFMPNMSYFEFIPMDGGDKNDVVDLEDVKLGCTYEPVVTNFAGLYRMRVGDIVLVTGFYNNAPQFKFVRRENVVLSIDSDKTNEEDLFKAVSQAKLVLESSGLDLKDFTSYADTSTFPGHYVVYLEVDTKEGEEKETAQFELDEEALSTCCLVMEESLDNVYKRCRFKDGSIGPLEIRVVRQGTFDSLMDFFISQGASTGQYKTPRCIKSGKALQVLETCVVAKFFSI
Protein: Protein GrpE (HSP-70 cofactor) (P9WMT5)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins, in association with DnaK and GrpE. It is the nucleotide exchange factor for DnaK and may function as a thermosensor. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, DnaK and GrpE are required for fully efficient folding.
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01151}.
Interaction partners:
- Chaperone protein DnaK
- Chaperone protein DnaJ 1
- Chaperone protein ClpB
- Probable heat shock protein transcriptional repressor HspR
- Chaperonin GroEL 2
- Co-chaperonin GroES
- Chaperonin GroEL 1
- Chaperone protein DnaJ 2
- Heat-inducible transcription repressor HrcA
- Hypothetical alanine and valine rich protein
Sequence:
MTDGNQKPDGNSGEQVTVTDKRRIDPETGEVRHVPPGDMPGGTAAADAAHTEDKVAELTADLQRVQADFANYRKRALRDQQAAADRAKASVVSQLLGVLDDLERARKHGDLESGPLKSVADKLDSALTGLGLVAFGAEGEDFDPVLHEAVQHEGDGGQGSKPVIGTVMRQGYQLGEQVLRHALVGVVDTVVVDAAELESVDDGTAVADTAENDQADQGNSADTSGEQAESEPSGS
Protein: RNA uridylyltransferase (EC 2.7.7.52) (Q4GZ86)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- RNA-editing ligase 2, mitochondrial
Sequence:
MNVAKREFIRGMMAHYRASLPPPEHSVVIHELQKRVLDIGMLAVNKAHVELFGSHVSGFCTPHSDADISLTYRNFSPWLQGMERVDEQNNKRMTRFGKEASAMGMEDVRYIRARIPVVQFTDGVTGIHCDVSIGNIGGVENSKILCAIRQVFPDFYGAYIHLVKAWGKAREVIAPERSTFNSFTVTTMALMVLQELGLLPVFSKPTGEFGELTVADAEMLLQEFKLPPIYDSLHDDDEKLGEAVFFCLQRFAEYYAKYDFSAGTVSLIHPRRHRTVYERVVRRHLELLGSRKRLEWEKHIAEHKEDGPLDENDFSASMQNETTQRPSNSPYVVEDFVNYVNCGRRVQASRVRHIQQEFNRLREMLIDKESELKFDEVFRESDTVPRFQGFEGVGTRDHRVKTFRPQ
Protein: Sporozoite surface antigen MB2 (Q8I3U2)
Organism: Plasmodium falciparum (isolate 3D7)
Interaction partners:
- Small ribosomal subunit protein eS30
- 40S ribosomal protein S3
- 40S ribosomal protein S11
- 60S ribosomal protein L6, putative
- 40S ribosomal protein S19
- 40S ribosomal protein S5, putative
- 60S ribosomal protein L5, putative
- 40S ribosomal protein S11, putative
- 60S ribosomal protein L23
- 60S ribosomal protein L11a, putative
Sequence:
MFLIWRLYKTLFLILYIIILQEYVCHSSNHIKSVNRCFIPFISEYIYKQKNRKNNISYDSSNSHYNDKIIPCGNYNKQLKYKINFCRNLYFNNKNEYNRICSRNKLNFHNIQTDNTIYKPKKKYYEVGKVREKIKMYTLFKDDKINTLKCNEEESVTSETINKHDSSVKVKGRRKKNITSNENIMNPNNKSVSSINTNLSDSSNNKNDNSLNSKKNDNTLNSKKNDNTLNSKKNDNTLNSKNNNNSLNSKNNNNSLNSKKSNNSYNDKHIDHIIPEGKNKINNNIDVKHNINNKLNEINEEPYEDTHNKEENSSNKNDNDEKRKEENNNITRRYIKNDQMSYNNINTNSNEYDKNASTLDETYIGKTFEGYVYSVNKNAACIKLKNINKYGLLFKNKANLGDDIEDMNDFFEKDQPVHVKILGINTKKNIFYLGNIIKYNENIKLSKGEYSKGLITKVCDSYCFIKVLKNGSTGYLHKSKLFCMNDKEKKNNDNQNYDNPNNDNPNYDNQNYDNQNYNNPNYDHPNYDNQNYDNQNYNNPNNDYSTSQLYNSDNLQMDFIYKLQFTKIFNIWDIIDVEILGTPQNDYKSNYILTIPRGSKTFKKILNYLNVLKENEDINNIQYKGDYIYSIDNNKNDNIIDSDINNHHINNKKKKKNLYDIQNNMNHSPFNKFHTEDEYLFNDHVQENVHTFYEKNKKYKITYDKENNHKMNKSYYLKKNKELPFNNKFKKIIKNIYDLPNTISLSMLSKTIKIPLASIKKYFIIHENKEYNSSYKINSEQIKRICQHFKIDCNVEQRDDNVVTKVNGTTKDCQEKVFKNVTQDRLKEGEQERVIKVEAKIKNDEMVMQEQKDTKEEKHMDVQFIEEKDINVQHINVQDMDVQDMDVQDINVQDMDVQNINVQDINIQDMDVQNINNSITLNKSTSCQTDESRDAPGGDQNESLDEKDSMEKSKEKKKKKGKSRKKNKDTNLTLKSDSIQKSKTTLDDKKRNVVVTFIGHINHGKTSLFDYICKTNEQKKEYGLITQNIRAFKATVRNNFTFTLVDTPGHEAFMPMRSRGVKISDLSILVISGDEGIQEQTVECIKLIKEFNIKIIIAITKVDIPNVDVDRIINDLLYHDITTELNGGEIQVVECSIYKEESIDKLLDAIYLESEFLNLQTNPDKKHEQAQGVVLDSYIDKNGIVSINLLQNGVLNINDHFYTGSSYGKVKILKDHLNKNIKSAYPSDPIKIIGYNKNSVPVAGDKFYVVENEALAKEIAEHNKNKMLTMEINNFTYDQTNMNRYKDFIISRENKIGGSSGILGENNLKNDIDGNMTRDDNMTRDDNMTSDDNMTRDGNRTNNDNITSDDNMSNDYDKIKETKMYTNNKSFQKDDFLKIHLNNTNENVINMDPSTHIGKNEIKTIYSNYIIKCDKQGSIEVLKNCMLKLQKEDSICKIKNKIIYADIGNVTSSDIKYATSFNATIIAFGVKLSNDIKGSKNSKGSKNHNNYPIIYSNVLYELIENVEKEMEKKLSKKPMGELKGTAQILKVFNISKLGKVAGCIVKKGTISINSNIRILRNDKVIYMGKIISIKIVKEEKTQVTEADECGIGFDNFLDFEPNDIIEAYEN