wanglab/gogpt-training-data huggingface dataset:
Protein: Guanylate-binding protein 4 (EC 3.6.5.-) (GTP-binding protein 4) (GBP-4) (Guanine nucleotide-binding protein 4) (Q96PP9)
Organism: Homo sapiens (Human)
Function: Binds GTP, GDP and GMP. Hydrolyzes GTP very efficiently; GDP rather than GMP is the major reaction product. Plays a role in erythroid differentiation (By similarity).
Subcellular location: Golgi apparatus membrane {ECO:0000269|PubMed:21151871}. Cytoplasm {ECO:0000269|PubMed:17266443}. Nucleus {ECO:0000269|PubMed:17266443}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:21151871}. Note=Heterodimers with GBP1, GBP2 and GBP5 localize in the compartment of the prenylated GBPs: with GBP1 in a vesicle-like compartment, with GBP2, around the nucleus and with GBP5, at the Golgi apparatus. {ECO:0000269|PubMed:21151871}.
Interaction partners:
- Guanylate-binding protein 1
- Guanylate-binding protein 5
- Signal transducer and activator of transcription 1-alpha/beta
- Guanylate-binding protein 2
- C-X-C motif chemokine 10
- Epithelial-stromal interaction protein 1
- Protein mono-ADP-ribosyltransferase PARP14
- Interferon regulatory factor 1
- Interferon-induced protein with tetratricopeptide repeats 3
- Interferon-induced protein with tetratricopeptide repeats 2
Sequence:
MGERTLHAAVPTPGYPESESIMMAPICLVENQEEQLTVNSKALEILDKISQPVVVVAIVGLYRTGKSYLMNRLAGKRNGFPLGSTVQSETKGIWMWCVPHLSKPNHTLVLLDTEGLGDVEKSNPKNDSWIFALAVLLSSSFVYNSVSTINHQALEQLHYVTELAELIRAKSCPRPDEAEDSSEFASFFPDFIWTVRDFTLELKLDGNPITEDEYLENALKLIPGKNPKIQNSNMPRECIRHFFRKRKCFVFDRPTNDKQYLNHMDEVPEENLERHFLMQSDNFCSYIFTHAKTKTLREGIIVTGKRLGTLVVTYVDAINSGAVPCLENAVTALAQLENPAAVQRAADHYSQQMAQQLRLPTDTLQELLDVHAACEREAIAVFMEHSFKDENHEFQKKLVDTIEKKKGDFVLQNEEASAKYCQAELKRLSEHLTESILRGIFSVPGGHNLYLEEKKQVEWDYKLVPRKGVKANEVLQNFLQSQVVVEESILQSDKALTAGEKAIAAERAMKEAAEKEQELLREKQKEQQQMMEAQERSFQEYMAQMEKKLEEERENLLREHERLLKHKLKVQEEMLKEEFQKKSEQLNKEINQLKEKIESTKNEQLRLLKILDMASNIMIVTLPGASKLLGVGTKYLGSRI
Protein: Elongation factor 1-alpha (Q95VF2)
Organism: Leishmania donovani
Interaction partners:
Sequence:
MGKDKVHMNLVVVGHVDAGKSTATGHLIYKCGGIDKRTIEKFEKEAAEIGKASFKYAWVLDKLKAERERGITIDIALWKFESPKSVFTIIDAPGHRDFIKNMITGTSQADAAILMIDSTHGGFEAGISKDGQTREHALLAFTLGVKQMVVCCNKMDDKTVTYAQSRYDEISKEVGAYLKRVGYNPEKVRFIPISGWQGDNMIERSDNMPWYKGPTLLDALDMLEPPVRPVDKPLRLPLQDVYKIGGIGTVPVGRVETGIMKPGDVVTFAPANVTTEVKSIEMHHEQLAEAQPGDNVGFNVKNVSVKDIRRGNVCGNSKNDPPKEAADFTAQVIVLNHPGQISNGYAPVLDCHTSHIACRFAEIESKIDRRSGKELEKNPKAIKSGDAAIVKMVPQKPMCVEVFNDYAPLGRFAVRDMRQTVAVGIIKGVNKKEGSGGKVTKAAAKAAKK
Protein: Ribosomal protein L37 (C0H4L5)
Organism: Plasmodium falciparum (isolate 3D7)
Interaction partners:
- 40S ribosomal protein S26
- 40S ribosomal protein S16, putative
- 60S ribosomal protein L34
- Small ribosomal subunit protein uS5
- 60S ribosomal protein L38
- 60S ribosomal protein L19
- Large ribosomal subunit protein eL43
- 40S ribosomal protein S15A, putative
- 40S ribosomal protein S29, putative
- 60S ribosomal protein L39
Sequence:
MGKAGKGTGSFGKRNGKTHFLCLRCGKRSYHLQKKKCASCGYPSAKKRRFNWSVKAKRRNTTGTGRCRYIKTLRRKLKNKFTEGSTPKPKQR
Protein: Phosphatidylinositol 3-kinase 1 (PI3-kinase) (PI3K) (PtdIns-3-kinase) (EC 2.7.1.137) (P54673)
Organism: Dictyostelium discoideum (Social amoeba)
Interaction partners:
- Phosphatidylinositol 3,4,5-trisphosphate 3-phosphatase and dual-specificity protein phosphatase PTEN
- Phosphatidylinositol 3-kinase
- Phosphatidylinositol 3-kinase 3
- Inositol 5-phosphatase 4
- Phosphatidylinositol 3-kinase 2
- Phosphatidylinositol 3-kinase
- Phosphatase and tensin homolog
- LIM-domain containing phosphatase
- Probable phosphatidylinositol phosphate kinase DDB_G0267588
- PIPK domain-containing protein
Sequence:
MNSIESSSNDSNEINKNSNKNNTHLNSNYNNIYKNNSTSSNNNNNHNNIEIIGIDNNKNNNKNNNDNNNNNNNIDKKRKDSKNKQNQEINQEMSENKKIYNSNDSNCSSGSSSGGHVNNGHHILIEENERLEHENQEIQEIYKQKGMEFQKKDLRFGYDVNSNNNNNNGGGSSSGSSSGGSDESASNQPIIRTRNREGSILNLKKQGLVKEISQRFQTPDTASYTRPNANNISIKDKISILKKEQERRKQDSEVQQREKVIVLSADSSNIQIYHPSVLIEKMNSKLDTEEKPATTTTTTTTTSTSISTSTPTTTTTTTTNTSTTNDITIKPKTSPTKNNEERSQSPITTPKQPVEEIVKKVSTPKSNNTSKKTSSDTTPTGKTTKKDKKDKKDKSRDSGNLVIVNNTNNTSSNNNNNNNNNNNNETIIKRRGRVLVTPSSDLKKNIQIYFTIPINPPVNKTNKPNQLLSNTSQQFLKTLISNEIPIDCKINDINDTDAFSDLSASASSSSFITKSSQSLLNVQSLRVKAIKTSFNILFLMPNQSKKILQVKGSDTIENLKERIISDYLFNNNSNNNNNNCKYGADSYLILDFNDNPMERSLVLNKSDYILDKRAQGLIPKLKVIEKSTILDSDPSDELSPSEYEIIRKLIPGTDTWRGEEVEYFRRVTSRLRYEALPLIKGSIQSTLLVRLSPLPIPIVGNKILISIFLPITQVTKTLDLELNETADQFTNRLFTKNYSKHLPNVNSNDFILKVVGSSDFIHGPHDIRTFESIRNHIIQGTKPQLTLIQRPKPELDPQPFKPRFDYPPELIIDHSCSNAINCNNNNTNSTNNNNINFDNWDQITHISIREIKKPFRVKVMGSTRIPLSCIKDIDSSSVIVSISLYHGIECFSKAFTQPIIPPPFAFLAETLSVDWCEWLVFTNIDYSNLPVDARLSISVYSANETVDDVEEIKNLDEATKKLTPIGWINVMITDFKYQLRQGMVELSLWPSDFSNPLGTCSNNPSSSQSVGLTLEFEEFNLPVLFPRKTKFSTSVSVIEQPPTNINSNEMREFFEQITALDPLSDLKQEKYNQLWTLRHYSILFPQVLPRLMLSVPWTQATAVDEAISLLDRWPKLKPYESLELLDAKHANRKVREFAVTCLEDLSEDELLDILLQLVQVLKYEPFHDSKLSRFLLRKAILNRNIGHSFFWYLKSDLHDSNLSERFGILLESYLYACGAHRIELLKQMEVINNLTEVAKKIKPLKDQDRREFMIKEFESLEWPKRFHLTLNPRFESNGLIINKSKYMDSKKLPLRLSFTNTDMNADPIEVIFKAGDDLRQDMLTLQMIRLMDKLWQKEGLDLKLSPYGCISTGDMIGMIEVVLNSETTAKIQKSEGGGAASAFKLDPLANWILQHNKSDMEYQKAVDTFILSCAGYCVATYVLGIGDRHNDNLMVTKGGRLFHIDFGHFLGNYKKKFGFKRERAPFVFTPDFCYVMGGKESFKFSQFVNYCCTAYNIVRKNAKLFMNLFAMMVSTGIPELQSMEDLNYLKESFSIELSDEKAREKFVALIHESLATKTTQLNNFFHHLAHA
Protein: Probable fatty-acid-CoA ligase FadD2 (Fatty-acid-CoA synthetase) (Fatty-acid-CoA synthase) (P95227)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Interaction partners:
- Phthioceranic/hydroxyphthioceranic acid synthase
- Mycoketide-CoA synthase
- Mycocerosic acid synthase-like polyketide synthase
- Probable multifunctional mycocerosic acid synthase membrane-associated Mas
- Phenolphthiocerol/phthiocerol polyketide synthase subunit C
Sequence:
MPNLTDLPGQAVSKLQKSIGQYVARGTAELHYLRKIIESGAIGLEPPLNYAALAADIRKWGEVGMLPSHNARRAPNRAAVIDEEGTLTFSELDEAAHAVANGLLAKGVRAGDGVAILARNHRWFVIANYGAARVGARIILLNSEFSGPQIKEVSDREGAKVIIYDDEYTKAVSLAQPPLGKLRALGVNPDDDKPSGSSDETLAELIAHSSTAPAPKASRRASIIILTSGTTGTPKGANRNTPPTLAPIGGILSHVPFKAGEVTLLPSPMFHALGYMHAALAMFLGSTLVLRRRFKPALVLEDIEKHKATSMVVVPVMLSRILDQLEKTEPKPDLSSLKIVFVSGSQLGAELATRALGDLGPVIYNMYGSTEVAFATIAGPKDLQFNPSTVGPVVKGVTVKILDENGNEVPQGAVGRIFVGNAFPFEGYTGGGGKQIIDGLLSSGDVGYFDERGLLYVSGRDDEMIVSGGENVFPAEVEDLISGHPDVVEAAAIGVDDKEFGARLRAFVVKKPGADLDEDTIKQYVRDHLARYKVPREVIFLDELPRNPTGKVLKRELRKL
Protein: Probable isoprenylcysteine alpha-carbonyl methylesterase ICMEL1 (EC 3.1.1.n2) (Isoprenylcysteine methylesterase-like protein 1) (Q8VYP9)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Catalyzes the demethylation of isoprenylcysteine methylesters (By similarity). May be involved in the regulation of ABA signaling (By similarity).
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:20868530}. Golgi apparatus membrane {ECO:0000269|PubMed:20868530}; Multi-pass membrane protein {ECO:0000269|PubMed:20868530}.
Interaction partners:
- Protein-S-isoprenylcysteine O-methyltransferase A
- Protein-S-isoprenylcysteine O-methyltransferase B
- CAAX prenyl protease 2
- CAAX prenyl protease 1 homolog
- Isoprenylcysteine alpha-carbonyl methylesterase ICME
- Probable isoprenylcysteine alpha-carbonyl methylesterase ICMEL2
- Succinate dehydrogenase flavoprotein subunit 2, mitochondrial
- Succinate dehydrogenase flavoprotein subunit 1, mitochondrial
- Succinate dehydrogenase iron-sulfur subunit 1, mitochondrial
- Succinate dehydrogenase subunit 3-1
Sequence:
MPSQILQISHHLPPKSSPSTEMMFKSLIYDDPSTTLLSRFGDDHHTISSTVKPLLSRSSSYNGTAMKTSSSSSAGGFTGWYQNRRRRSNSDNCLSAFSDDTNGTADGGNNSGDRQTTIGQEVGHAAAETFLLTRLCLKLLSYLGVGYRWITRFMALGCYAFLLMPGFIQVGYYYFFSPYVRRSIVYGDQPRNRLDLYLPKNSTGPKPVVAFVTGGAWIIGYKAWGSLLGQQLSERDIIVACIDYRNFPQGSISDMVKDASSGISFVCNHIAEYGGDPDRIYLMGQSAGAHIAACTIVEQVIKESGEGDSVSWSSSQINAYFGLSGGYNLLNLVDHFHSRGLYRSIFLSIMEGEESLRQFSPELVVQNPNLKHIIARLPPFILFHGTDDYSIPSDASKSFAETLQRLGAKAKVILYEGKTHTDLFLQDPMRGGIDEMFEDIVTVVLGDDQEAIGKSVDRRRLVPEFMLKLAHWVSPF
Protein: T-box containing transcription factor (Q8JFF9)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123, ECO:0000256|PROSITE-ProRule:PRU00201}.
Interaction partners:
Sequence:
MAEKRRSPCTMSLKAHAFSVEALIGTEKKRKLEEEDSENCFEEINEVPRMTESPQPSTGRTCPSTRSCEIDCTSDESPEPEDVLLDSPQPASQGAQVLVQSATSSGEEMRVDLQGSDLWKRFHEIGTEMIITKAGRRMFPAMRVKIAGLDPHQQYYIAMDIVPVDNKRYRYVYHSSKWMVAGNADSPVPPRVYIHPDSPASGETWMRQVISFDKLKLTNNELDDQGHIILHSMHKYQPRVHVIRKECGEELSPVKAVPTGDGVKAFSFTETVFTTVTAYQNQQITRLKIDRNPFAKGFRDSGRNRMGLEALVESYAFWRPSLRTLTFEDILGITKQGAAGSHGVVGSSAHLLSSSSCPSPTFHLGSGAGPVCDYSTCSRTSHPLHRYGPSLSADSYSRLTSPTADAFSTSRSSTYVSGTESEAFSCTQTGLPIQIHSMPSTTSQLQYLMPGHAHNAFSTNQSTQGSYNGFRLHNPYGLYGYNFSTSPRLATSPEKAAATQTSFLGSSPSGTLTDRQVLSTMDGLHMLSSSQQNLFDSRTLGLTSSSSQVTAHMA
Protein: SD09259p (Q9VAJ9)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
- FI01031p
Sequence:
MSATSVQEAPKKAVATNAIKFLFGGLSGMGATMVVQPLDLVKTRMQISGAGSGKKEYRSSLHCIQTIVSKEGPLALYQGIGAALLRQATYTTGRLGMYTYLNDLFREKFQRSPGITDSMAMGTIAGACGAFIGTPAEVALVRMTSDGRLPVAERRNYTNVANALARITREEGLTALWRGSLPTVGRAMVVNMTQLASYSQFKTYFRHGPLQMEEGIKLHFCASMLSGLLTTITSMPLDIAKTRIQNMKMVDGKPEYRGTADVLLRVARQEGVFALWKGFTPYYCRLGPHTVLTFIILEQLNQGYNKYVLGSNKSTGL
Protein: DNA packaging terminase subunit 1 (F8RFH0)
Organism: Human herpesvirus 1 (HHV-1) (Human herpes simplex virus 1)
Interaction partners:
Sequence:
MFGQQLASDVQQYLERLEKQRQLKVGADEASAGLTMGGDALRVPFLDFATATPKRHQTVVPGVGTLHDCCEHSPLFSAVARRLLFNSLVPAQLKGRDFGGDHTAKLEFLAPELVRAVARLRFKECAPADVVPQRNAYYSVLNTFQALHRSEAFRQLVHFVRDFAQLLKTSFRASSLTETTGPPKKRAKVDVATHGRTYGTLELFQKMILMHATYFLAAVLLGDHAEQVNTFLRLVFEIPLFSDAAVRHFRQRATVFLVPRRHGKTWFLVPLIALSLASFRGIKIGYTAHIRKATEPVFEEIDACLRGWFGSARVDHVKGETISFSFPDGSRSTIVFASSHNTNGIRGQDFNLLFVDEANFIRPDAVQTIMGFLNQANCKIIFVSSTNTGKASTSFLYNLRGAADELLNVVTYICDDHMPRVVTHTNATACSCYILNKPVFITMDGAVRRTADLFLADSFMQEIIGGQARETGDDRPVLTKSAGERFLLYRPSTTTNSGLMAPDLYVYVDPAFTANTRASGTGVAVVGRYRDDYIIFALEHFFLRALTGSAPADIARCVVHSLTQVLALHPGAFRGVRVAVEGNSSQDSAVAIATHVHTEMHRLLASEGADAGSGPELLFYHCEPPGSAVLYPFFLLNKQKTPAFEHFIKKFNSGGVMASQEIVSATVRLQTDPVEYLLEQLNNLTETVSPNTDVRTYSGKRNGASDDLMVAVIMAIYLAAQAGTPHTFAPITRVS
Protein: Calcium channel, voltage-dependent, T type, alpha 1G subunit (Q5SUF9)
Organism: Mus musculus (Mouse)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
Sequence:
MDEEEDGAGAEESGQPRSFTQLNDLSGAGGRQGPGSTEKDPGSADSEAEGLPYPALAPVVFFYLSQDSRPRSWCLRTVCNPWFERVSMLVILLNCVTLGMFRPCEDIACDSQRCRILQAFDDFIFAFFAVEMVVKMVALGIFGKKCYLGDTWNRLDFFIVIAGMLEYSLDLQNVSFSAVRTVRVLRPLRAINRVPSMRILVTLLLDTLPMLGNVLLLCFFVFFIFGIVGVQLWAGLLRNRCFLPENFSLPLSVDLEPYYQTENEDESPFICSQPRENGMRSCRSVPTLRGEGGGGPPCGLDYEAYNSSSNTTCVNWNQYYTNCSAGEHNPFKGAINFDNIGYAWIAIFQVITLEGWVDIMYFVMDAHSFYNFIYFILLIIVGSFFMINLCLVVIATQFSETKQRESQLMREQRVRFLSNASTLASFSEPGSCYEELLKYLVYILRKAARRLAQVSRAVGVRAGLLSSPVARGGQEPQPSGSCSRSHRRLSVHHLVHHHHHHHHHYHLGNGTLRVPRASPEIQDRDANGSRWLMLPPPSTPTPSGGPPRGAESVHSFYHADCHLEPVRCQAPPPRSPSEASGRTVGSGKVYPTVHTSPPPEMLKDKALVEVAPSPGPPTLTSFNIPPGPFSSMHKLLETQSTGACHSSCKISSPCSKADSGACGPDSCPYCARTGAGEPESADHEMPDSDSEAVYEFTQDAQHSDLRDPHRRRRPSLGPDAEPSSVLAFWRLICDTFRKIVDSKYFGRGIMIAILVNTLSMGIEYHEQPEELTNALEISNIVFTSLFALEMLLKLLVYGPFGYIKNPYNIFDGVIVVISVWEIVGQQGGGLSVLRTFRLMRVLKLVRFLPALQRQLVVLMKTMDNVATFCMLLMLFIFIFSILGMHLFGCKFASERDGDTLPDRKNFDSLLWAIVTVFQILTQEDWNKVLYNGMASTSSWAALYFIALMTFGNYVLFNLLVAILVEGFQAEGDATKSESEPDFFSPSVDGDGDRKKRLALVALGEHSELRKSLLPPLIIHTAATPMSLPKSSSTGVGEALGSGSRRTSSSGSAEPGTAHHEMKSPPSARSSPHSPWSAASSWTSRRSSRNSLGRAPSLKRRSPSGERRSLLSGEGQESQDEEESSEEDRASPAGSDHRHRGSLEREAKSSFDLPDTLQVPGLHRTASGRSSASEHQDCNGKSASGRLARTLRADDPPLDGDDGDDEGNLSKGERLRAWVRARLPACCRERDSWSAYIFPPQSRFRLLCHRIITHKMFDHVVLVIIFLNCITIAMERPKIDPHSAERIFLTLSNYIFTAVFLAEMTVKVVALGWCFGEQAYLRSSWNVLDGLLVLISVIDILVSMVSDSGTKILGMLRVLRLLRTLRPLRVISRAQGLKLVVETLMSSLKPIGNIVVICCAFFIIFGILGVQLFKGKFFVCQGEDTRNITNKSDCAEASYRWVRHKYNFDNLGQALMSLFVLASKDGWVDIMYDGLDAVGVDQQPIMNHNPWMLLYFISFLLIVAFFVLNMFVGVVVENFHKCRQHQEEEEARRREEKRLKRLEKKRRNLMLDDVIASGSSASAASEAQCKPYYSDYSRFRLLVHHLCTSHYLDLFITGVIGLNVVTMAMEHYQQPQILDEALKICNYIFTVIFVLESVFKLVAFGFRRFFQDRWNQLDLAIVLLSIMGITLEEIEVNASLPINPTIIRIMRVLRIARVLKLLKMAVGMRALLDTVMQALPQVGNLGLLFMLLFFIFAALGVELFGDLECDETHPCEGLGRHATFRNFGMAFLTLFRVSTGDNWNGIMKDTLRDCDQESTCYNTVISPIYFVSFVLTAQFVLVNVVIAVLMKHLEESNKEAKEEAELEAELELEMKTLSPQPHSPLGSPFLWPGVEGVNSPDSPKPGAPHTTAHIGAASSGFSLEHPTMVPHTEEGPVPLGPDLLTVRKSGVSRTHSLPNDSYMCRNGSTAERSLGHRGWGLPKAQSGSILSVHSQPADTSCILQLPKDAHYLLQPHGAPTWGAIPKLPPPGRSPLAQRPLRRQAAIRTDSLDVQGLGSREDLLSEVSGPSCPLTRSSSFWGGSSIQVQQRSGSQSKVSKHIRLPAPCPGLEPSWAKDPQETRSSLELDTELSWISGDLLPSSQEEPLSPRDLKKCYSVEAQSCRRRPGSWLDEQRRHSIAVSCLDSGSQPRLCPSPSSLGGQPLGGPGSRPKKKLSPPSISIDPPESQGPRPPCSPGVCLRRRAPASDSKDPSASSPLDSTAASPSPKKDALSLSGLSSDPTDLDP
Protein: Heme chaperone HemW (Q9CGF7)
Organism: Lactococcus lactis subsp. lactis (strain IL1403) (Streptococcus lactis)
Function: Could serve in the delivery of heme to a membrane-localized target protein (Probable). Binds one molecule of heme per monomer, possibly covalently; heme and Fe-S cluster binding are independent. Incubation with the reductant sodium dithionite increases binding. Does not have coproporphyrinogen III dehydrogenase activity in vitro, does not complement an E.coli hemN deletion in vivo. Binds 1 Fe-S cluster, it is probably [4Fe-4S]. The cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine; only dimeric protein has the cluster (Probable).
Subcellular location: Cytoplasm {ECO:0000269|PubMed:22142238}. Cell membrane {ECO:0000305|PubMed:22142238}. Note=A minor, heme-containing fraction is associated with the cell membrane. {ECO:0000305|PubMed:22142238}.
Interaction partners:
Sequence:
MLQKPNSAYFHIPFCSHICYYCDFAKVLMTGQPIDAYIESLIEEFQSFEIEKLRTIYIGGGTPSVLSAQQLERLLTAIAEQLDLEVLEEFTVEANPGDLSDEVIKVLADSAVNRISLGVQTFNNALLKKIGRTHTEVQVYDSVERLKKAGFENITIDLIYALPGQTMEMVKSDVEKFLELKLPHVALYSLILEDHTVFMNRQRRGLLRLPSEDKNADMYEYIMDILAKNGYNHYEVSNFGLPGFESKHNITYWDNEEYYGIGAGASGYLAGIRYKNLGPVHHYLKAAPTEKRINEEVLSKKSQIEEEMFLGLRKKSGVLVEKFENKFKCSFEKLYGEQITELINQKLLYNDRQRIHMTDKGFELGNNVFEKFLLDDINF
Protein: Proteasome subunit beta (O17311)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cytoplasm {ECO:0000256|RuleBase:RU004203}. Nucleus {ECO:0000256|RuleBase:RU004203}.
Interaction partners:
Sequence:
MDLDNARELPRAGFNFDNCKRNATLLNRGFKPPITTKTGTTIVGIIYKDGVILGADTRATEGPIVSDKNCAKIHYLAKNIYCCGAGTAADTEMTTDLISSQLELHRLQTDREVRVVAANTMLKQMLFRYQGHISAALVLGGVDKTGPHIYSIHPHGSSDKLPYATMGSGSLAAMTVFESRWKPDLSEEEGKKLVRDADPTGVFNDLGSGSNIDLCVIRKGSVEYLRNYELANKKGKRQLDYRFKTGTSTVLHTNIKDLLVTERVQAVPMEIS
Protein: Cyclic di-GMP phosphodiesterase PA4108 (EC 3.1.4.-) (Q9HWS0)
Organism: Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Function: Phosphodiesterase (PDE) that catalyzes the hydrolysis of cyclic diguanylate (c-di-GMP) to GMP. Hydrolyzes c-di-GMP to GMP in a two-step reaction, via the linear intermediate 5'-phosphoguanylyl(3'->5')guanosine (pGpG). In vitro, can use pGpG as an alternative substrate and hydrolyze it into GMP. Acts in regulation of motility, synthesis of virulence determinants and biofilm architecture.
Interaction partners:
- Cyclic di-GMP phosphodiesterase PA2567
- Diguanylate cyclase
- EAL domain-containing protein
- diguanylate cyclase
- cyclic-guanylate-specific phosphodiesterase
- GGDEF domain-containing protein
- Probable transcriptional regulator
- Diguanylate cyclase
- Probable chemotaxis transducer
Sequence:
MLKRIPVTQLRLGMFVQSLCGSWLDHPFWKRGGFLLDSQADLQRLRESAVKEVWIDASKGLDLPEEAAVSAAAVLPVTMPAGPSPARVALEEEIRHAALLCSRAKAAVVSMFRDARMGQAIDTAHASDLVDEISASVLRHPNALLSLVRLKTSDEYTYMHSVAVCALMIALARQLELPDPLVREAGLAGLLHDIGKMAVPDPILNKPGKLTDPEFGLVRRHPQNGARMLLDCRQVSALVVDVCLHHHERIDGTGYPFGLAQEQISLLARMGAVCDVYDAITSDRPYKKGWNAAEAIRRMAEWNGHFDPQVFRAFVKAVGIYPVGALVRLESGRLGVVLEQHGRSLLTPRVKVFFSARSKVPIPQQVVDLGRAGQTDRIVGFEPAEAWNFRNLDEMWTGLAKSTGSYFDAGTGNP
Protein: Centrosomal protein kizuna (Polo-like kinase 1 substrate 1) (Q3UXL4)
Organism: Mus musculus (Mouse)
Function: Centrosomal protein required for establishing a robust mitotic centrosome architecture that can endure the forces that converge on the centrosomes during spindle formation. Required for stabilizing the expanded pericentriolar material around the centriole.
Subcellular location: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250|UniProtKB:Q2M2Z5}. Cytoplasm, cytoskeleton, cilium basal body {ECO:0000250|UniProtKB:Q2M2Z5}. Note=Localizes to centrosomes throughout the cell cycle. After centrosome duplication, it usually remains associated only with the mother centrosome, containing the older mature centriole and particles surrounding it. During prophase, additional particles accumulate around both separating centrosomes. Does not accumulate at the microtubule minus ends, but instead localizes to the centrosomes and centrosome- surrounding area in a microtubule-independent and dependent manner, respectively. {ECO:0000250|UniProtKB:Q2M2Z5}.
Interaction partners:
- V-set and immunoglobulin domain-containing protein 10-like
Sequence:
MPRGRGGGGGGLRQASATSAPLASPSYYERVGQLQQALRDSEKKRLDLEDKLYEYNKSDKCRAKLKCAKLKKYLKEVCESERRAQVRNQGYLKKFECVQTYVEHLTTNTEKLQKLKTEYEAEVKRMRLLSKDSLGMSDEDGAKDAVQAGINSGTAMSRGLYQPATIFMGRQMSAISSIEDFSTELKSNQPTKNFSISDPHSHQQTAQSSCVTDSCVVQTNGDTQCLNKSDKIHGKTSLQTGEKAPVTSYVLSAEEQTHCLEIGSSTQHSKSNLSEGRKSAELHSSLQERLSPENSITDLKCDSSSRSEGSDREILTQEHIEVREERAGPLVPMMAASEHCTSAKKWAGEKHSAWEASSDDLDHGDSKSQKAVLKHEEEQEEGSSCSSSDLTVSVSEDDLILESLAALSNPGAKMAGKDGMQALRAAHTEPRQDSLFTEYVLQTQSFPDSKREPSPDSPRQPEKVPDCHLLKTRGQCMKEHDNSLKEEATTLLKKVLTEECDHRSAIHSNESSCSMPSILNDNNGIKEAKPALRLNSVLTREQEVSSGCGDESKEESIAAAPGTGHREADLVPSELFQFSLGAAMKETKAYQLLKKSTLQDNSNQAEERFESQFSGLDIGGSMFTTKTAHKIASEASFSSSEGSPLSRHESKRDPVTTIKSNAFWGESDDSNSEIEAALRPRDHDMPDDFDDFYDT
Protein: Putative Tubby-like protein 4 (AtTLP4) (O80699)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- Tubby-like protein 8
- Germin-like protein subfamily 1 member 1
- Germin-like protein subfamily 2 member 1
- Germin-like protein subfamily T member 1
- Glutathione S-transferase U4
Sequence:
MPPELLRDVLMRIERSEDTWPSRKNVVSCVGVCKNWRQIFKEIVNVPEVSSKFTFPISLKQPGPGGSLVQCYVKRNRSNQTFYLYLGGEAKIFCQSEPSEPNKSIWKLSLKPGGTATTQTELDNFVSFRSPSGQKEGVLVLKSKVPRLEEQSWCLDFNGWRDIVSSGKKFQLVALLRTNLRMKTTFSSLRKSETCTNSSYEAEWIPLVRTSVFAVIARVCRDKKHTPSYELKLALYFAKNSAILKKFVLRGYTREEDLLALPVAN
Protein: Glutathione S-transferase YfcF (EC 2.5.1.18) (P77544)
Organism: Escherichia coli (strain K12)
Function: Exhibits glutathione (GSH) S-transferase activity toward 1-chloro-2,4-dinitrobenzene (CDNB); however this activity is as low as 1% of that of GstA. Also displays a GSH-dependent peroxidase activity toward cumene hydroperoxide. Is involved in defense against oxidative stress, probably via its peroxidase activity.
Interaction partners:
- Thioredoxin/glutathione peroxidase BtuE
- Glutathione S-transferase GstA
- Glutathione S-transferase GstB
- Glutathione synthetase
- Glutathione reductase
- Glutathione-specific gamma-glutamylcyclotransferase
- Glutathione hydrolase proenzyme
- Bifunctional glutathionylspermidine synthetase/amidase
- Disulfide-bond oxidoreductase YfcG
- Maltose/maltodextrin-binding periplasmic protein
Sequence:
MSKPAITLWSDAHFFSPYVLSAWVALQEKGLSFHIKTIDLDSGEHLQPTWQGYGQTRRVPLLQIDDFELSESSAIAEYLEDRFAPPTWERIYPLDLENRARARQIQAWLRSDLMPIREERPTDVVFAGAKKAPLTAEGKASAEKLFAMAEHLLVLGQPNLFGEWCIADTDLALMINRLVLHGDEVPERLVDYATFQWQRASVQRFIALSAKQSG
Protein: Set1 complex component spp1 (Set1C component spp1) (COMPASS component spp1) (Complex proteins associated with set1 protein spp1) (O74508)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: The Set1 complex specifically methylates 'Lys-4' of histone H3.
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
- Histone-lysine N-methyltransferase, H3 lysine-4 specific
- Set1 complex component swd1
- Set1 complex component ash2
- Set1 complex component swd3
- Set1 complex component sdc1
- Set1 complex component swd2
- Set1 complex component shg1
- Uncharacterized WD repeat-containing protein C824.04
- Histone H3.1/H3.2
- Histone H4
Sequence:
MELTQENTEENEKTHVESIVKFEDSNRGTITDFHIETANNEEEKDANVILNKSVKMEVEEVNGHVDSSSTETDIEMQVIQQPTIPKKPPVSAHRRGPRKHRGNANSQLNLSTADHQRPLYCICQKPDDGSWMLGCDGCEDWFHGTCVNIPESYNDLTVQYFCPKCTEEGKGITTWKRKCRLRECSNPTRPNSNYCSDKHGVDFFREKVKLSTVEPSAIKNLVLFAKKREEFQNLGTVGPTLPSQVPPEVVYNFEIEEANRLNAEIVQLNKEKEVASNKKIFLQLIKDSSRRAVLAYKEREGIKKDLCGFDSRLLFNQQQMNELWEKVSNGAPLSLDMSIDPSPESTCFTEKRRCAKHTSWQVIFTEDFELQESNILQKLNMKQTAKDVMLEHQKQRCLPGIQYDGYARFCHEQLSPEKMANLLK
Protein: HTH-type transcriptional repressor BdcR (P39334)
Organism: Escherichia coli (strain K12)
Function: Negatively regulates expression of bdcA.
Interaction partners:
- Cyclic-di-GMP-binding biofilm dispersal mediator protein
- RutC family protein YjgH
- 2,3-dihydroxyphenylpropionate/2,3-dihydroxicinnamic acid 1,2-dioxygenase
- 3-
- Galactofuranose transporter ATP-binding protein YtfR
Sequence:
MVTKKQSRVPGRPRRFAPEQAISAAKVLFHQKGFDAVSVAEVTDYLGINPPSLYAAFGSKAGLFSRVLNEYVGTEAIPLADILRDDRPVGECLVEVLKEAARRYSQNGGCAGCMVLEGIHSHDPQARDIAVQYYHAAETTIYDYIARRHPQRAQCVTDFMSTVMSGLSAKAREGHSIEQLCATAAMAGEAIKTILEE
Protein: ADP-ribosylation factor 2 (Q8BSL7)
Organism: Mus musculus (Mouse)
Function: GTP-binding protein that functions as an allosteric activator of the cholera toxin catalytic subunit, an ADP-ribosyltransferase. Involved in protein trafficking; may modulate vesicle budding and uncoating within the Golgi apparatus.
Subcellular location: Golgi apparatus.
Interaction partners:
- Cytohesin-2
- Cytohesin-3
- Cytohesin-1
- Cytohesin-4
- Phospholipase D1
- Phospholipase D2
- Nck-associated protein 1-like
- Nck-associated protein 1
- Protein BRICK1
- Cytoplasmic FMR1-interacting protein 1
Sequence:
MGNVFEKLFKSLFGKKEMRILMVGLDAAGKTTILYKLKLGEIVTTIPTIGFNVETVEYKNISFTVWDVGGQDKIRPLWRHYFQNTQGLIFVVDSNDRERVNEAREELTRMLAEDELRDAVLLVFVNKQDLPNAMNAAEITDKLGLHSLRQRNWYIQATCATSGDGLYEGLDWLSNQLKNQK