wanglab/gogpt-training-data huggingface dataset:
Protein: C4-type zinc ribbon domain-containing protein (O25612)
Organism: Helicobacter pylori (strain ATCC 700392 / 26695) (Campylobacter pylori)
Interaction partners:
- GTP cyclohydrolase 1 type 2
- 3-deoxy-D-manno-octulosonic acid transferase
- Glycine--tRNA ligase alpha subunit
- Uncharacterized RNA pseudouridine synthase HP_0956
- Phosphatidylglycerol--prolipoprotein diacylglyceryl transferase
- Glycerol-3-phosphate dehydrogenase [NAD
- Oxygen-insensitive NADPH nitroreductase
- Secreted protein involved in flagellar motility
- RNA polymerase sigma-54 factor
Sequence:
MNTHLKQLIEISHLDKEIDSLEPLIREKRKDLDKALNDKEAKNKAILNLEEEKLALKLQVSKNEQTLQDTNTKIASIQKKMSEIKSERELRSLNIEEDIAKERSNQANREIENLQNEIKHKSEKQEDLKKEMLELEKLVQQLESLVENEVKNIKETQQIIFKKKEELVEKTEPKIYSFYERIRRWAKNTSIVTIKKQACGGCFIRLNDKIYTEVLTSGDMITCPYCGRILYAEGAYENSAQPPKESQEESQELV
Protein: GH04611p (Q95SS0)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MNAQRCRSVVPPVADPMCVEPLGVRNNTQLPPIPKILYFRRSRGHAVDLKIESSLLVYYFHVEVRSHIGRHFAARKLGPWQWQKVEKTMEENIGHSKHTYIFFHMRPGRWYEVRVAAVNAYGFRGYSEPSDPFPSTGNPKPPKSPNDSKIIGKQFDGRYMTLKLVWCPSKSNLPVEKYKITWSLYVNSAKASMITNSSYVKDTHQFEIKELLPNSSYYIQVQAISYLGSRRLKSEQWSMLFNTTLQPLEPITPLQCSGNGNRRRHHHTSSSMSSERATTSEPVALNEVSPTITNRTSAAATYEVGFRLNRKFGMIVQILGFQPHKEKVYELCPQETNCEQREFRAIRAKKDPLEFSKLKYNTTYVLRIPRSSPNSVLDDSRNVFTFTTPKCENFRKRFPKLQIKCSD
Protein: Transmembrane protein 106B (C9JZ87)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MGKSLSHLPLHSSKEDAYDGVTSENMRNGLVNSEVHNEDGRNGDVSQFPYVEFTGRDSVTCPTCQGTGRIPRGQENQLVALIPYSDQRLRPRRTKLYVMASVFVCLLLSG
Protein: Transcription factor Sp9 (Q6NW96)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Function: Transcription factor which plays a key role in limb development. Positively regulates FGF8 expression in the apical ectodermal ridge (AER) and contributes to limb outgrowth in embryos.
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
Sequence:
MATSILGEEPRFGTTPLAMLAATCNKIGNTSPLTTLPDSSAFSKGGFHPWKRSSSSCNLGSSLPGFTVATSRSTSGLTTTTGAGNSAFCLASTSPTSSAFSAEYSSLFSNTTSVSSQDSGQSAFISKVHSSADTLYPRVGMAHPYESWYKSGFHSTISGDVANGASTWWDVHTNPGSWLEVQNPAGTLQSSLHSGTPQAIHSQLSGYNPDFSSLTHSAFSSTGISPTASHLLSTSQHLLTQEGFKTVIPTYTDASATNAMISGASSGIGTSSRSSRRYSGRATCDCPNCQEAERLGPAGASLRRKGLHSCHIPGCGKVYGKTSHLKAHLRWHTGERPFVCNWLFCGKRFTRSDELQRHLRTHTGEKRFACPVCNKRFMRSDHLSKHIKTHTAGGGGKKGSDSDTDTSNLETPRSESPELILEGVNPRVTVKDQSPHHES
Protein: Ribosomal L1 domain-containing protein 1 (Q8BVY0)
Organism: Mus musculus (Mouse)
Function: Regulates cellular senescence through inhibition of PTEN translation. Acts as a pro-apoptotic regulator in response to DNA damage.
Subcellular location: Nucleus, nucleolus {ECO:0000250|UniProtKB:O76021}.
Interaction partners:
- MKI67 FHA domain-interacting nucleolar phosphoprotein
- ATP-dependent RNA helicase DDX18
- Ribosome biogenesis protein WDR12
- Pescadillo homolog
- Nucleolar complex protein 2 homolog
- Ribosome biogenesis protein NOP53
- Probable rRNA-processing protein EBP2
- mRNA turnover protein 4 homolog
- Ribosome production factor 2 homolog
- Ribosome biogenesis protein BRX1 homolog
Sequence:
MKGSASESPSASVAEATTTDVQVTPTALLQLDREQIRKAVEVISNRSKSKKNNNELLLSGSENLFLMVILWKIPEKELRVKVPLPHSILSESSDVCLFTKDEFDSPEQTEGFYKKLLKKHGVNTISQIIPFKTLKTEYKAYEAKLRLLGSFEVFITDARIRRHLPSHIGRHFYQRKKVPVSVNLLAKNLSKEINRCITGTVLNISKRGSCSTIRIGHTGMETEHIVDNILAVSEMLSEKLPEKWQSVKLLFLKTEKSVSLPIFSSFVTSQDENAVSLRSLRKQELKKRKRENAKLKKESKMLRKKSKKATSLLTQSGLASSAPAKSPGAQKKKTNKAHKKQKVTEECEEAIPQLVPIGETPDKENVKMQENITGKTPKSKSDPSTPKGKKRKALLATETPEASAPGTSGKKQKKDVQEFRKPEASSFSTPRKSGKKASNTPRDKKTKAAHSN
Protein: Uncharacterized protein (Q3V4A4)
Organism: Mus musculus (Mouse)
Interaction partners:
Sequence:
MSRLSPHAPCMGREKTQELAALEAEEGEGGPASYSAPQFLNYTRQPLYLALCCAMVLFAHVTCRYFCVVSMVCKMLPGRAHPPCSSLLPFGRKWVGRDVVTGSFCTVGLIK
Protein: Hydroxyacylglutathione hydrolase 1, mitochondrial (EC 3.1.2.6) (Glyoxalase II) (Glx II) (O24495)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Thiolesterase that catalyzes the hydrolysis of S-D-lactoyl-glutathione to form glutathione and D-lactic acid.
Subcellular location: Mitochondrion.
Interaction partners:
- Lactoylglutathione lyase GLX1
- Lactoylglutathione lyase
- Probable lactoylglutathione lyase, chloroplastic
- Protein DJ-1 homolog D
- DJ-1 protein homolog F
- DJ-1 protein homolog E
- D-lactate dehydrogenase [cytochrome], mitochondrial
- Monodehydroascorbate reductase 3
- Protein DJ-1 homolog B
- Protein DJ-1 homolog A
Sequence:
MPVISKASSTTTNSSIPSCSRIGGQLCVWPGLRQLCLRKSLLYGVMWLLSMPLKTLRGARKTLKITHFCSISNMPSSLKIELVPCSKDNYAYLLHDEDTGTVGVVDPSEAAPVIEALSRKNWNLTYILNTHHHDDHIGGNAELKERYGAKVIGSAVDKDRIPGIDILLKDSDKWMFAGHEVRILDTPGHTQGHISFYFPGSATIFTGDLIYSLSCGTLSEGTPEQMLSSLQKIVSLPDDTNIYCGRENTAGNLKFALSVEPKNETLQSYATRVAHLRSQGLPSIPTTVKVEKACNPFLRISSKDIRKSLSIPDSATEAEALRRIQRARDRF
Protein: AT14535p (Brivido-2, isoform A) (Q8T8Z2)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
Sequence:
MNLSSISRKDLTCFGVTTCVVMVCFVLVSIFSGFMHEPQRFKTMLVTIVLVFFFQYLILEPIRFFIQSIDYATWPQEDPPYRAEEGGPTMDHIGYLKIRLRSLRSELLISEGHTNEMLNQKYKHIAGDLLLYGSYFIALMLMVVLQEDHTNYYNTNNMQRLFWDNTSVTFGLSQVYFIYQVHSYMKITLVEAFYAQKTNGYEGWWAMEQWQKIGVVRLRQMRPVDCHIGLGKPEWDKKTYAPEWRLPYHRMHYTEKFWRIYDPFVPAEFEPSFLNGLLLNYDHYGYLLNYPEVAGYVVLMMSTKINCLKQIEYLRDYSWLDKNTSALFIDLTMYNADANLFTLITLRVENSPFGIQLPRVHVDSVSMLGNVETRSNSELLILFVYTVLVILFARGVFTKIWHHPAAAHEAWTMVDLAIYILNVFLTVLAIMRDIETDALLQIIETATKGQYLDFQRPLRLHQMLFIVKGFLVCITTLRLWKVLQFASVFQHFTQTLFSAWRAVASLGVIILVVLMAIGITLAVPNGNNAVVFSHMVQSVVTCMWYSMGFNGDIHPADFFHGGRILGILLYLALVFLLAIILMNVFASVIYDYFNETSRILKEHSNRSSITFLEFLHVEYADLFGDAFRCLRKTYESRGHTVAENVELELNRRELIKFKRDLIKSPQELKRALLTEEQRSADYRLRGEKLFKLMAILNLQVEILERMVLGDKDGKLPTPPASDSDPDDMPEMYRKRR
Protein: Phosphodiesterase (EC 3.1.4.-) (Q8WSK2)
Organism: Trypanosoma brucei brucei
Interaction partners:
Sequence:
MLEALRKCPTMFAVTSDGSSTMAKMDNSARQLALFVATTNGEFYQSNFGEEALETIKYQLGKDAGWGLFFDVLRNAFNGNCVSILARSEDTAHILCGKEDCSEKSALCFPIQKTEEDTSATILKCLVDANAVYANPKEEKNKVQKIMEELEKAKLQVRMLEEEVRVLCENNIWRRKQDTKNTLKIGKLRDNISRLSNQINPKAKEVSETSVGETSGPHAEDSYIPGRKLLRLVFEKKECKEYDVELLRLIKSRWPKTEGSKACNASNCLIDPYTESELPERLSRMSKKHKMVWGTLNGLDDWDYNVFELQAAIDGDDINCKNDQSGCGALFITMYALVVKYGFLRKFEINERIFLNWLSAVEGGYHANPYHNSMHAADVLHITHYLLSKGGLAELCKLNDRQVLAALFAAAIHDYNHPGINNNFSILTQTYNATLYNDRSVLENMHVASVFELMRNPALNILACFSEEHWRDFRNTVIDMVLATDMSLHEKYMTQFKRRLSEKRPFTEDCDQNLALAMALKLADISNCCRPLPLYLKWSERVSDEFYTQGDRERSLGMSCSPFMDRQTPMIAEGQTSFINYIFIPFLEVMAEFLPSMGFTLGLAAVCKSHRLVGNTGQGT
Protein: Type 3 secretion system stator protein (T3SS stator protein) (Low calcium response locus protein KC) (Yop proteins translocation protein L) (P69976)
Organism: Yersinia pestis
Function: Component of the type III secretion system (T3SS), also called injectisome, which is used to inject bacterial effector proteins into eukaryotic host cells (Probable). Acts as a regulator of the YscN/SctN ATPase activity (By similarity).
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:Q01253}.
Interaction partners:
Sequence:
MSQTCQTGYAYMQPFVQIIPSNLSLACGLRILRAEDYQSSLTTEELISAAKQDAEKILADAQEVYEQQKQLGWQAGMDEARTLQATLIHETQLQCQQFYRHVEQQMSEVVLLAVRKILNDYDQVAMTLQVVREALALVSNQKQVVVRVNPDQAGAIREQIAKVHKDFPEISYLEVTADARLDQGGCILETEVGIIDASIDGQIEALSRAISTTLGQMKVTE
Protein: 5-nitrosalicylic acid 1,2-dioxygenase (5NSA 1,2-dioxygenase) (EC 1.13.11.64) (5-nitroanthranilic acid degradation protein B) (D3WZ86)
Organism: Bradyrhizobium sp
Function: Dioxygenase that catalyzes the cleavage of the aromatic ring of 5-nitrosalicylate (5NSA) without prior removal of the nitro group in biodegradation of 5-nitroanthranilate.
Interaction partners:
Sequence:
MKWSNKDGYPWSKIIHAEKFFDKVIQNDTRPGKWEWADVVSGLRDLDKDPRMNSERRYVAIVNEDVGLGETKGIGITPGLFCGCQLIHPGEEVTSHRHNSVALYFIVEGTGELEVEGEVYSYKPFDIMTCPAWSYHAWRATGDKDTLMYVIHDMALLAYMRALFWEEPKGSENIRHMVKGSTHTWSNTKAPEVSKTQAAKELLKQGE
Protein: PTS system glucose-specific EIIA component (EIIA-Glc) (EIII-Glc) (Glucose-specific phosphotransferase enzyme IIA component) (Q44840)
Organism: Borreliella burgdorferi (strain ATCC 35210 / DSM 4680 / CIP 102532 / B31) (Borrelia burgdorferi)
Function: The phosphoenolpyruvate-dependent sugar phosphotransferase system (sugar PTS), a major carbohydrate active transport system, catalyzes the phosphorylation of incoming sugar substrates concomitantly with their translocation across the cell membrane. The enzyme II complex composed of PtsG and Crr is involved in glucose transport.
Subcellular location: Cytoplasm {ECO:0000305}.
Interaction partners:
- Pts system, maltose and glucose-specific iiabc component
- Phosphoenolpyruvate-protein phosphotransferase
- Pts system, iibc components
- Phosphocarrier protein HPr
- Phosphocarrier protein HPr
- Glycerol kinase
- Glucose-6-phosphate isomerase
- protein-N
- Putative phosphotransferase enzyme IIB component BB_0367
- Fructose-bisphosphate aldolase
Sequence:
MGFLDFFKKTATLDLIAPISGKVMSIDKVPDEAFAEKIVGDGIAILPTSNELLAPCDGKIGKIFKTNHAFSLETKEGVEIFVHFGINTLNLNGKGFTRVAEEGINVKQGEVIIRLDLEYLKEHSESVITPVVIANSDEVSSIEYSFGRLENDSEYILSSSTVLTEEIRHKISQTKPVIAGKDLVLRVKK
Protein: Probable membrane protein (O53962)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Interaction partners:
- Conserved protein
Sequence:
MFPRWPQQAHNHEVSRADTVSVPRAPTQAEVAAVLRIMTPLRKVIKPKVYGIENVPTERALLVGNHNTLGLVDAPLLAAELWERGRIVRSLGDHAHFKIPGWRDALTRTGVVEGTREITSELMRRGELVMVFPGGAREVNKRKNERYKLVWKNRLGFARLAIQHGYPIVPFASVGAEHGIDIVLDNESPLLAPVQFLAEKLLGTKDGPALVRGVGLTPVPRPERQYYWFGEPIDTTEFMGQQADDNAARRVRERAAAAIEHGIELMLAERAADPNRSLVGRLLRSDA
Protein: Cytochrome P450 family 2 subfamily C member 8 (A0A0D9SG51)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MAAKCCSTFFLGCEFSQFLPLFLLGIISSNGKRWKEIRRFSLTTLRNFGMGKRSIEDRVQEEAHCLVEELRKTKASPCDPTFILGCAPCNVICSVVFQKRFDYKDQNFLTLMKRFNENFRILNSPWIQVCNNFPLLIDCFPGTHNKVLKNVALTRSYIREKVKEHQASLDVNNPRDFIDCFLIKMEQEKDNQKSEFNIENLVGTVADLFVAGTETTSTTLRYGLLLLLKHPEVTAKVQEEIDHVIGRHRSPCMQDRSHMPYTDAVVHEIQRYSDLVPTGVPHAVTTDTKFRNYLIPKSFDNKIMLAA
Protein: Putative F-box protein At3g13830 (Q9LRW4)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
Sequence:
MTTTTTTTMSTLPMVLVDEILSRVPITSLRSLRSTCKRWEAQSKTNLVGGKATARKSSYLGFILIGNKICSMKLDLNGGDDFVDTSVNQISAFDDFEISQLFHCDGLLLCVSNKHYYSNTVMVCNMYLGETRLIEHCCLLEGFDNFGSYAFGYDSSKNRNHKIFRKKLVSGGYEIYSFKSDSWKDLNVDLGESTELCELGSVSLKGNAYFSVITKHEEEELWENNLLCFDFTTESFGKFLSLPFDNVTAEEEFGIMVLSCVRDEHLAVLYQLDTLGIWISTEIEPNKVSWREFLQVDLYTLDGFPDAFTAGRFIVDEEKQVVVVFNEATEIDLNHGNAFIFGRDGYFTSFNVGDTPPQDFTSYVPSLASLQIEKTGG
Protein: Lipoate--protein ligase 1 (EC 6.3.1.20) (Q8IEG9)
Organism: Plasmodium falciparum (isolate 3D7)
Function: Catalyzes both the ATP-dependent activation of exogenously supplied lipoate to lipoyl-AMP and the transfer of the activated lipoyl onto the lipoyl domains of lipoate-dependent enzymes. In the mitochondrion, functions as a redox switch between two lipoylation routes. Senses the oxidation state of lipoate and determines which downstream enzymes will be lipoylated. In low reducing conditions, uses lipoate in its oxidized ring form to lipoylate glycine cleavage system H-protein GCVH. In high reducing conditions and together with LipL2, uses reduced lipoate (dihydrolipoate) to lipoylate the E2 component of the branched chain alpha-ketoacid dehydrogenase complex BCKDH-E2/BCDH and the E2 component of the alpha-ketoglutarate dehydrogenase complex KDH. LipL1 is responsible for catalysing the activation of lipoate, forming lipoyl-AMP while LipL2 is required but is not capable of catalyzing this reaction.
Subcellular location: Mitochondrion {ECO:0000269|PubMed:15225307}.
Interaction partners:
- Lipoyl synthase, apicoplast
- Inactive lipoate--protein ligase 2
- Glycine cleavage system H protein
- Lipoate-protein ligase B
- 2-oxoisovalerate dehydrogenase subunit alpha
Sequence:
MKRIFRLVRRCHYSTEKRTNGPLVLVSNNQNIHFNLSLENFLLNNYNDLLKYLNINTIEKFNEPILFLWRNNRSIIIGKNQNIWSECNLKNIKEDGVLVARRFTGGGAVYHDLGNVCFTFLNNNINTSSNFLIILNTLKNHFNIEAKTQGRNDITVNDQKCSGSAFKKIKDVFLHHGTILINLEKNILNKYLTPDKIKYIKHGVSSVNARTINLSEINNNITCENLCIALIKEFTKFYEQNYKENINNIKNLENNINNSNFQNKEQININNTNENNLINNTNIIPNDITVHYIDQNNNITKNPEFLKYYNLLKDWDWCYGKTPKFQNHIWKQFTFGKLELFFNVSNGFIKDGNIFSDCLDINLIDHLKSIFNNDIKYSKEDISIFFKKLNVENKNYLDEVRSWILQEL
Protein: Sphingoid long chain base kinase 4 (LCB kinase 4) (EC 2.7.1.91) (Sphinganine kinase 4) (Q12246)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Catalyzes the phosphorylation of the sphingoid long chain bases dihydrosphingosine (DHS or sphinganine) and phytosphingosine (PHS) to form dihydrosphingosine 1-phosphate (DHS-1P) and phytosphingosine 1-phosphate (PHS-1P) respectively. Involved in the biosynthesis of sphingolipids and ceramides. Required with LCB3 for an effective incorporation of DHS into ceramides through a phosphorylation-dephosphorylation cycle. Involved in heat-induced transient cell cycle arrest. Accumulation of phosphorylated sphingoid long chain bases (LCBPs) stimulates calcium influx and activates calcineurin signaling. Involved in heat-stress resistance.
Subcellular location: Cell membrane {ECO:0000269|PubMed:12459470, ECO:0000269|PubMed:16141212}; Peripheral membrane protein {ECO:0000305}. Endoplasmic reticulum membrane {ECO:0000269|PubMed:12493772}; Peripheral membrane protein {ECO:0000305}. Late endosome membrane {ECO:0000269|PubMed:12459470}; Peripheral membrane protein {ECO:0000305}. Golgi apparatus membrane {ECO:0000269|PubMed:12459470}; Peripheral membrane protein {ECO:0000305}. Note=LCB4 is synthesized in the cytosol, palmitoylated at the Golgi apparatus by AKR1, and then transported to the plasma membrane (PM) via the late Sec pathway. Most of the LCB4 is delivered further to the cortical ER (cER), which is closely adjacent to the PM. In stationary phase, G1 cell cycle arrest causes ER-localized LCB4 to be transported to the Golgi apparatus via the early Sec pathway, and finally to the vacuole via the MVB pathway, where it is degraded. {ECO:0000269|PubMed:17686782}.
Interaction partners:
- Sphingosine-1-phosphate lyase
- Dihydrosphingosine 1-phosphate phosphatase LCB3
- Dihydrosphingosine 1-phosphate phosphatase YSR3
- Sphingolipid C4-hydroxylase SUR2
- Alkaline ceramidase YDC1
- Ceramide synthase LAG1
- Alkaline ceramidase YPC1
- Sphingoid long chain base kinase 5
- Ceramide synthase LAC1
- 3-ketodihydrosphingosine reductase TSC10
Sequence:
MVVQKKLRAILTDEGVLIKSQSHHMFNKHGQLRSGDSLSLLSCLSCLDDGTLSSDGGSFDEDDSLELLPLNTTIPFNRILNAKYVNVGQKGFNNGKISSNPFQTENLSSSSENDDVENHSLSNDKAPVSESQSFPKKDKWDTKTNTVKVSPDDSQDNSPSLGIKDNQQLIELTFAVPKGHDVIPQKLTLLIDHVSRKSRANTGEENISSGTVEEILEKSYENSKRNRSILVIINPHGGKGTAKNLFLTKARPILVESGCKIEIAYTKYARHAIDIAKDLDISKYDTIACASGDGIPYEVINGLYRRPDRVDAFNKLAVTQLPCGSGNAMSISCHWTNNPSYAALCLVKSIETRIDLMCCSQPSYMNEWPRLSFLSQTYGVIAESDINTEFIRWMGPVRFNLGVAFNIIQGKKYPCEVFVKYAAKSKKELKVHFLENKDKNKGCLTFEPNPSPNSSPDLLSKNNINNSTKDELSPNFLNEDNFKLKYPMTEPVPRDWEKMDSELTDNLTIFYTGKMPYIAKDTKFFPAALPADGTIDLVITDARIPVTRMTPILLSLDKGSHVLEPEVIHSKILAYKIIPKVESGLFSVDGEKFPLEPLQVEIMPMLCKTLLRNGRYIDTEFESM
Protein: Dye-decolorizing peroxidase (DyP) (EC 1.11.1.7) (I6Y4U9)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: Cargo of a type 1 encapsulin nanocompartment in situ; this cargo protects against oxidative stress at low pH. When expressed in the cytoplasm (absence of the encapsulin shell gene) it is almost as protective as the intact nanocompartment; its encapsulation has a modest yet significant effect on protection against oxidative stress at low pH. A heme-dependent peroxidase, it probably does not have deferrochelatase activity. Converts guaiacol and H2O2 to tetraguaiacol, also acts on 2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) (ABTS). Retains peroxidase activity when encapsulated but has a reduced set of substrates; acts on ABTS but not guaiacol.
Subcellular location: Encapsulin nanocompartment {ECO:0000269|PubMed:24855650}. Note=Consistently identified in encapsulin nanocompartments isolated in situ (PubMed:34751132). Located inside the nanocompartment in E.coli (Probable). {ECO:0000269|PubMed:34751132, ECO:0000305|PubMed:24855650}.
Interaction partners:
- Type 1 encapsulin shell protein
- Neutral ceramidase
- Sec-independent protein translocase protein TatB
- Probable M18 family aminopeptidase 2
- Sec-independent protein translocase protein TatC
- Conserved protein
Sequence:
MAVPAVSPQPILAPLTPAAIFLVATIGADGEATVHDALSKISGLVRAIGFRDPTKHLSVVVSIGSDAWDRLFAGPRPTELHPFVELTGPRHTAPATPGDLLFHIRAETMDVCFELAGRILKSMGDAVTVVDEVHGFRFFDNRDLLGFVDGTENPSGPIAIKATTIGDEDRNFAGSCYVHVQKYVHDMASWESLSVTEQERVIGRTKLDDIELDDNAKPANSHVALNVITDDDGTERKIVRHNMPFGEVGKGEYGTYFIGYSRTPTVTEQMLRNMFLGDPAGNTDRVLDFSTAVTGGLFFSPTIDFLDHPPPLPQAATPTLAAGSLSIGSLKGSPR
Protein: Histone deacetylase-like protein HDO2 (Q8T6T5)
Organism: Trypanosoma brucei
Interaction partners:
Sequence:
MVVEPPASIPPVAVIVSTDVDAPASLPALQHNKLIIDMVRHYGCTPFPRKEVGGEAAFCNDIFEWVDRNLPSVDVEDMTAFHDESYVRYLSLREVASGDDEHVLSFSGCSNIRGTPSKRFASRRCSAPLPPFVLFPQNGDKRFNLVGDSAPFSGMWRFTQAVVSGTLAATRLLAQPSRFAAIHWMGGKHNAKRASAGGSCLVNDVVLAVLELRKLLPANRNVVLAVDPDAHHGDGAQEAFLSDPRVVTLSLHAYGIGIFPGTGSLEEIGSGLGRGYTMNIPLPVGATDALVVPMAQRGIYSAFRRAGVELGAVVVVCGSNSLSGDPYGLLNLTIGGYQRILRTLLTEAASHSAKVLMLGGSCNVEVAAARLAGVLTRDVFSCATALRNGDTSYFSWSPDLSTEKGVEVPEDCEYFTMYGPSFLMHSLPLAVVDEVHHFPPDSVLFSRMRQIAAKGERNSQMRDRAARKTVIEDDEEEESESEEEDTDEEEETESEGDENTSSQEGTDEEVVIDEDEETNGEGDEDTSSQEGNDEEEDTDETVLTDHVREGFPCLKERICGSLSEGQ
Protein: ESX-1 secretion-associated protein EspE (P9WJD3)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Subcellular location: Cell inner membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000255}. Note=Localizes at or near the cell pole in (on average) 1 discrete spot upon overexpression in M.smegmatis (PubMed:22233444). {ECO:0000269|PubMed:22233444}.
Interaction partners:
- ESX-1 secretion-associated protein EspB
- ESX-1 secretion-associated protein EspG1
- ESX-1 secretion-associated protein EspI
- 6 kDa early secretory antigenic target
- ESX-1 secretion-associated protein EspH
- PPE family immunomodulator PPE68
- ESAT-6-like protein EsxB
- ESX-1 secretion system protein EccD1
- ESX-1 secretion-associated protein EspF
- FHA domain-containing protein
Sequence:
MASGSGLCKTTSNFIWGQLLLLGEGIPDPGDIFNTGSSLFKQISDKMGLAIPGTNWIGQAAEAYLNQNIAQQLRAQVMGDLDKLTGNMISNQAKYVSDTRDVLRAMKKMIDGVYKVCKGLEKIPLLGHLWSWELAIPMSGIAMAVVGGALLYLTIMTLMNATNLRGILGRLIEMLTTLPKFPGLPGLPSLPDIIDGLWPPKLPDIPIPGLPDIPGLPDFKWPPTPGSPLFPDLPSFPGFPGFPEFPAIPGFPALPGLPSIPNLFPGLPGLGDLLPGVGDLGKLPTWTELAALPDFLGGFAGLPSLGFGNLLSFASLPTVGQVTATMGQLQQLVAAGGGPSQLASMGSQQAQLISSQAQQGGQQHATLVSDKKEDEEGVAEAERAPIDAGTAASQRGQEGTVL
Protein: Serine/threonine-protein phosphatase 2A regulatory subunit B'' subunit delta (PP2A B''-PR59) (PP2A PR59) (Protein phosphatase 2A, 59 kDa regulatory subunit B) (Serine/threonine-protein phosphatase 2A regulatory subunit B'' subunit alpha) (Q9Z176)
Organism: Mus musculus (Mouse)
Function: The B regulatory subunit might modulate substrate selectivity and catalytic activity, and also might direct the localization of the catalytic enzyme to a particular subcellular compartment. Interacts with retinoblastoma-related protein p107 (in vivo). May target PP2A core dimer to p107 resulting in dephosphorylation of p107.
Interaction partners:
- Serine/threonine-protein phosphatase 2A 65 kDa regulatory subunit A alpha isoform
- Serine/threonine-protein phosphatase 2A catalytic subunit beta isoform
- Serine/threonine-protein phosphatase 2A catalytic subunit alpha isoform
- Serine/threonine-protein phosphatase 4 catalytic subunit
- Serine/threonine-protein phosphatase 2A 55 kDa regulatory subunit B alpha isoform
- Protein phosphatase 3 catalytic subunit alpha
- Ryanodine receptor 2
- Serine/threonine-protein phosphatase 2A 65 kDa regulatory subunit A beta isoform
- Serine/threonine-protein phosphatase 2B catalytic subunit gamma isoform
- Serine/threonine-protein phosphatase 2A 55 kDa regulatory subunit B beta isoform
Sequence:
MPERPPIRALRRDPDDPAVAQALASLARGSDLVFPSRFQKWLRDFRQVHAHRKEEPPPQSPPPGHTVPAFYFPCGRPPPRPQDTEDAIALVECAFEGLPRGRAGLGDMAVVAKACGCPLYWKAPLFYAAGGERTGSVSVHMFVAMWRKVLLTCHDDAARFVRLLGHPGCSGLIQEDFVPFLQDVVNSHPGLAFLRAAKDFHSRYITTVIQRIFYTVNRSWSGMISREELRRSSFLQAVSQLEVEPDINRMTSFFSYEHFYVIYCKFWELDLDRDLTIDRSDLARHGDGAISSRMIDRIFSGAVTRARLPRKVGKLSYADFVWFLLSEEDKTTPTSTEYWFRCMDLDGDGALSMFELEFFYEEQAQRMAARGVEPLPFHDLARQVLDLVAPRCPGRITLRDLKQCGLAGEFFDAFFNVDKYLAREQREQAGTPQDTDSDPAASAWDRYAAEEYDFLVAEEAMAEDDDDHDEGSDPIDLYGLADEDCDDLEPL
Protein: Glucan endo-1,3-beta-glucosidase 5 (EC 3.2.1.39) ((1->3)-beta-glucan endohydrolase 5) ((1->3)-beta-glucanase 5) (Beta-1,3-endoglucanase 5) (Beta-1,3-glucanase 5) (Q9M088)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Cell membrane; Lipid-anchor, GPI-anchor.
Interaction partners:
- At4g31150
- alpha-D-xyloside xylohydrolase
- Actin-related protein 4
Sequence:
MLFKGVFAVFFVITLLYASLLIEVEGIGVNWGSQARHPLPPATVVRLLRENGIQKVKLFEADSAILKALSRTGIQVMVGIPNDLLAPLAGSVAAAERWVSQNVSAHVSSNGVDIRYVAVGNEPFLKAFNGTFEGITLPALQNIQSAIIKAGLATQVKVTVPLNADVYQSASNLPSDGDFRPEIRDLMLNIVKFLSDNGAPFTINIYPFISLYNDPNFPVEFAFFDGTGTPINDNGRIYDNVLDANYDTLVWSLQKNGFGNLTIIVGEVGWPTDGDKNANLMYARRYNQGFMNRQKANKGTPMRPGAMDAYLFGLIDEDAKSIQPGNFERHWGIFYIDGQPKYQLSLGSGNGLIPAKDVHYLAKKWCILAPNANLQDPQLGPSVSYACDHADCTSLGYGSSCGNLNLAQNVSYAFNSYYQVSNQLDSACKFPGLSIVSTRDPSVGSCKFKIMIKSEDASEASAMMPITRSTAVLLLLSICLYIVL
Protein: KAT8 regulatory NSL complex subunit 1 (A0A1W2PPV8)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MAAMAPALTDAAAEAHHIRFKLAPPSSTLSPGSAENNGNANILIAANGTKRKAIAAEDPSLDFRNNPTKEDLGKLQPLVASYLCSDVTSVPSKESLKLQGVFSKQTVLKSHPLLSQSYELRAELLGRQPVLEFSLENLRTMNTSGQTALPQAPVNGLAKKLTKSSTHSDHDNSTSLNGGKRALTSSALHGGEMGGSESGDLKGGMTNCTLPHRSLDVEHTTLYSNNSTANKSSVNSMEQPALQGSSRLSPGTDSSSNLGGVKLEGKKSPLSSILFSALDSDTRITALLRRQADIESRARRLQKRLQVVQAKQVERHIQHQLGGFLEKTLSKLPNLESLRPRSQLMLTRKAEAALRKAASETTTSEGLSNFLKSNSISEELERFTASGIANLRCSEQAFDSDVTDSSSGGESDIEEEELTRADPEQRHVPLRRRSEWKWAADRAAIVSRWNWLQAHVSDLEYRIRQQTDIYKQIRANKGLIVLGEVPPPEHTTDLFLPLSSEVKTDHGTDKLIESVSQPLENHGAPIIGHISESLSTKSCGALRPVNGVINTLQPVLADHIPGDSSDAEEQLHKKQRLNLVSSSSDGTCVAARTRPVLSCKKRRLVRPNSIVPLSKKVHRNSTIRPGCDVNPSCALCGSGSINTMPPEIHYEAPLLERLSQLDSCVHPVLAFPDDVPTSLHFQSMLKSQWQNKPFDKIKPPKKLSLKHRAPMPGSLPDSARKDRHKLVSSFLTTAMLKHHTDMSSSSYLAATHHPPHSPLVRQLSTSSDSPAPASSSSQVTASTSQQPVRRRRGESSFDINNIVIPMSVAATTRVEKLQYKEILTPSWREVDLQSLKGSPDEENEEIEDLSDAAFAALHAKCEEMERARWLWTTSVPPQRRGSRSYRSSDGRTTPQLG
Protein: Centrosomal protein 112 (D4ABV2)
Organism: Rattus norvegicus (Rat)
Interaction partners:
Sequence:
MPAAARGGGTGKLDSSAPGLLDGPQGFETVRLWRRGVGGRVDRLLVVAPDRSMEMGSEEEKWEKLDAEFDHFVVDMKPFVLKLPHRSERQRCALWIRKLCEPSGTGAGLMGRKNRNLYAKLLLHMLRRGVLEGPFTHRPEPGTLKVLPSYMSIYFDEPNSAQSKDSSPEKLPDWVMGELEPGERRLSDSWQLSCGEENALLLSASDAHREQYTGKLRMRSHSVSPTDREDRQHITSKICEVHPKKSPISLDDSDIEVRLNSWNLGIENPRYLRQKPLPVSLMTPKVSLRNSSNLHDDHFLSRMHEKELDMKTKMMEAKFSEEKLKLQKKHDAEVQKILERKNNELEELKILYKKKQTETEETVRKLEKKVQILIRDCQVIRETKENQITELKKICEQSTESLNNDWEKKLHSAVAEMEKEKFELQKHHTETIQELLEDTNVRLSKMEGDYMVQTQSTNHMIKDLEGRVQQLMGEAENSNLQRQKLTQEKLELERCYQITCSELQELKTRQNLLHTEKEHLVNDYEQNVKLLKTKYDSDINILRQEHALSTSKTSVVIEELEQNIRQLKQQVQESELQRKQQVKDQEDKFHMEKNHLKYIYEEKVHELKSELDKEKEDAQRKIHKFEEALKEKEEQLGRVTEVQRLQAQQADAALEEFKRQVEVTSEKVYSDMKEQMEKVEADLSRSKSLREKQSKEFLWQLEDARQRYEQQIVELKLEHEQEKTHLLQQHNAEKDSLVRDHEREVENLENQLRAANMEHENQIQESKKRDAQVIADMEAQVHKLREELINVNSHRKQQLVELGLLREEEKQRAARDHETAVKKLKAESERVKMELKKTHAAETEMTLEKANSRLKQIEKEYTQKLAKSSQIIAELQTTISSLKEESSRQQLAAERRLQDVIQKFEDEKQQLIRDNDQAIKALQDELETRSNQVRSAEKKLQHKELEAQEQMMYIRQEYETKFKGLMPASLRQELEDTISSLKSQVNFLQKRASILQEELTTYQSRR