wanglab/gogpt-training-data huggingface dataset:
Protein: Erythrocyte membrane protein 1, PfEMP1 (Q8IAK2)
Organism: Plasmodium falciparum (isolate 3D7)
Interaction partners:
Sequence:
MGSQGSKPVDTSDVKNESHNSARNVFENIAEIIYNRVKEDAEKRGKSLKGDYKRAKFHQPLLEAAKYVWYAPSNPCNFDFRFDTNAPDKGSYDRDPCHLRDTNRFSDKGDAICTNNKINCNNGGCGACAPYRRIQLCDYNLEYINEYNINSTHDLLGNLLVMAKREGDSIVNSHGHTGKGIYKSGICTSLARSFADIGDIIRGKDLFLGHNHKKKPLLDNLEKIFNRFQKIYEDINNLPIDDIREYWWALNRNDVWEALTCSAPYYADYFKKKSGNTYNFTTEGYCGRNEGAPPTNLDYVPQFLRWFDEWAEEFCRIKNIKIGNIKKSCTGESNNKHCSREGYDCNKTNLRLNEIFMDLECPRCADDCKSYETWVENKKKEFNKQKEKYKEEINESKPGVNSEHGKYNKAFYDKLRTIYRTNDKFFEILNKGQICENVDEKNKIDFNDLVKTFSRSEYCKSCPMLGVTCKGEQCNSLDDITCTNDKGGPNKVTDKNNNTFVIDILLNDNKKKVLSNDLNDYKECDLFKRLRRQNWNCKYKCNLHVCELNNFNNEIDDERVISIKVFIKRWLESFLKDYNKLKENLNPCINNENQLPCIKDCLENCDCVEKWIKKKGEEWKKIKERYLKDYKIEDNNSSNSLNKFLQQNQFHSDVVKAIKPFENLRAFEDSSGCTGTVPSGIEECKSNDVIKILLSKLKEKIELCKKNDVKKNKSNNCVTLLKPLNDEEDDEEQDDEPPAPKPLPTPNPCVNGGDDTSGAQITSVTEIAEGMHMGAQKQMLERSGDKSGKGTENGESVLKGDIKKAKFKNGASPSSLEDVCGITDQHTKDSRRRRRLRRLRLLVLRFRRRLRRGHRDYKGPCTGKDGHKKMFQVEKGWENGSKIGTENDVFLPPRREHFCTSNVEHLYRSASGLQGTTASHSLLGDVLLAANKEAGFIKERYKTQKTSEGFKDEATVCRAIKYSFADIADIIKGTDLWKANSGKKNTQDKLVKIFQKIKDNLPVNIKGKYNEDEKHLELRKDWWFANRDKVWEAMKCEQNGITCSGPTPLDDYIPQRLRWMTEWAEWYCKAQKEAYDKLKVCEKCMDNGKCTQGNGECAKCKTACENYKKFINTWQPQWKQMEQKYESLYKEAQENGNSSHKSTTEQDKYMVEFLSQLQKANNGDKTGDDKVYSTAAGYVHQEATMNCEKQTQFCKNKNGVKAANDAEDVNYTFKDTPNGYDVVCKCKDRPEQQIKKKEVEDACKIAQDIFKGKDENTTVGLCKKKDFGRTPYPDWKCEKNSKLVTGNGECMPPRRQKLCLYFLAHKIETPNLNTQEDLRKAFIKCAAAETFFSWYYFKKINDKLNKLDEKLKEGEIPPQFLRSMFYTFGDYKDICLDTDISLKTENGDITKAKSNIDRIIPKKSAKNPDEERKIWWDGIKEDVWEGMLCGLSHAVSNNDKATVQKTLTTKTIYDYDTVTFDGTTKLEDFSKRPQFLRWMTEWGEEFCKKRKEQLENLKDKCPDYTCSFDTKKQECENHCKVYEEWLKGWKDQYKKQSEKFTTDKEKPEYKDDPDVASSENAHKYLSKKLKQIFHNGSTTEKCDYTCMEYASRQPQTSACSQQQQQQNKSSTQNHFPEAFDYPPKEIGDRCTCPKLPEPKYCVDKTAYDIRKESGKKSDNSLKGNGNTYNNNCNNSMREEYANQNGETCKFNETFWSKKKPSIEECDINAKERFQIQKYWDCNGKTPDGKNTFCIPPRRKDMCLKQLEEINSADVNNSKKLLQKIQDVAKKEGDDIIKKLLPKYPCNEDVICKAMKYSFADLADIVRGIDKYKGPNGTNVLEKELKSVFETIYTKWKSENTNNKSKYTDVASFRSAWWDANRKDIWNAMTCNAPYDAKIYITKEGGYISPLTFTKNKCGHNDDPPDYDYIPQPFRWLSEWSETYCLAQKDLLETMKNCENCMKKNKNADCEQTQYGACRDCKRKCEEYKKFIEIWKKQFETQNKAYQEIYRNATTTNRDNNNIVDENTKNFVKKLQENCRTDRNESLDTADKYLENASVCRRFKFGNKDSRHLNYAFHTDPPSYEEHCKCAKDFDPLDECPVDNNECKKYGIGSCPKKNFHKKLEEWTNYVLNNKSNKNKSAIVPPRRRQLCLQNLTRNLSRLNKEKSFKEGILISAASEAKMLTEQYRENPAKALQAIKYSFADIGNIIKGDDIIGNVISVQLNKLINGNKKINTSTLWWEANKEKIWNAMMCYYTGDEKTATSCPSHGNIDKEDQFLLWFQEWGENFCARQKELYEHVQAECSHVICVNGTGNIDSKCTEACKNYSNFISETKNVYQSLKKQYNDNHNSIKVGGKEVHHYMKEKCKDKCECLSEKFNSDNNWEKPYDTFDDTVLKNKCQCKKPDSPILPVEPSVPAETEKEKKKDSPLKPHTEPKPAPPKKPEVPPPPPVQPPPANQPFNRDILEKTIPFGIALALGSIAFLFIKKKPKSPVDLIRVLDIHKGDYGMPTLKSKNRYIPYASDTYKGKTYIYMEGDSDSGHYYEDTTDITSSESEYEEMDINDIYVPDSPKYKTLIEVVLEPSKRDTPSSDAPMNKFTDDEWNQLKQDFISGILENEQKDLPKNNISGNTPMNTQPNTLYFNKPEEKPFITSIHDRDLYSGEEINYNINMSTNSMDDTSYVSNNVYSGIDLINDTLSGNQHIDIYDEVLKRKENELFGTNYKKNTSNNNVAKLTNSDPIMNQLDLLHKWLDRHRDMCEKWKSKEDILHKLNEQWNKDNDGGNVPIDNRSLNTDVWIEIDMDDPKGKKEFSNMDTILDDIEDDIYYDVNDDENPSVDNIPMDHNKVDVPKKVHVEMKILNNTSNGSLEPEFPISDVWNI
Protein: Receptor expression enhancing protein A, isoform P (A0A0B4JCV3)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MISSLFSRLIILFCGTLYPAYASYKAVRTKDVKEYVKWMMYWIVFAFFTCIETFTDIFISWLPFYYEVKVALVFWLLSPATKGSSTLYRKFVHPMLTRHEQEIDEYVNQAKERGYSAVLQLGSKGVNYATNVLMQTAIKGGGNLVQTIKRSYSLSDLSEPDMHRTQDELDDVMMSSMTSSAVVMRSTATGARLLRPRNQTPVGRSGSGTRHSTGMYFTEVDVTAKNAGDFNYNIRSQDDISSGYSSAEPVSGLSRTSSMTNASKARAKSKRNELLEEMRDEVYLDNQLYFQGVQRKSSVPEAEELKIVESSESIQSQELEKVLKEENIDAEDEAFFETLPLIEEHINEVVANYGRDEKLLPQERKHNSIEEEQFEDALFEEPQKCVSDEVDAKNIEEILTDRSQNQTPNGSAETTDSGTPSQNKPYVHPPIDPFLLVLSASASAPDPFMPERPRPMSPREMRETLEEIKHSFRAQLEAEPSVSASPSPSLRPKANHGKGRAPPPPLPPKKHSLSPQPDAISQTSTGSVERKSGQIHVC
Protein: Myosin XI-K (B0CN61)
Organism: Nicotiana benthamiana
Interaction partners:
Sequence:
MASVNIIVGSHVWVEDPKLAWSDGEVLKIHGPDVHVKTSNGKEVVANITKVFPKDTEAPPGGVDDMTKLSYLHEPGVLQNLATRYELNEIYTYTGNILIAVNPFQRLPHLYDTHMMEQYKGAAFGELSPHVFAVADVAYRAMINEGKSNSILVSGESGAGKTETTKMLMRYLAYLGGRSGVEGRTVEQQVLESNPVLEAFGNAKTVRNNNSSRFGKFVEIQFDKSGRISGAAIRTYLLERSRVCQISNPERNYHCFYLLCAAPAEEIEKYKLGNPKSFHYLNQSKCYALDGVNDAEEYLATRRAMDIVGISEEEQDAIFRVVAAILHPGNVEFAKGEEIDSSVIKDEQSRFHLNMTAELLKCDAKSLEDALITRVMVTPEEVITRTLDPEAALGSRDALAKTVYSRLFDWIVEKINISIGQDPNSKSIIGVLDIYGFESFKTNSFEQFCINFTNEKLQQHFNQHVFKMEQEEYEKEKINWSYIEFVDNQDVLDLIERKPGGIIALLDEACMFPKSTHETFAQKLYQTFTKNKRFIKPKLSRTSFTISHYAGEVTYQADLFLDKNKDYVVAEHQVLLTASMCPFVVGLFPPLPEESSKSSKFSSIGSRFKLQLQSLMETLSSTEPHYIRCVKPNNVLKPCIFENVNVIQQLRCGGVLEAIRISCAGYPTRRTFYEFLLRFGVLAPEVLAGSYDDKVACQMILDKMGLMGYQIGKTKVFLRAGQMAELDARRAEVLGNAAKIIQRQIRTYITRKEFVVLRHAAIQLQSCWRAMLSCKLYEQLRREAAALKIQKNFRCHVAHTAYTTLHSSAITLQTGMRAMVSRNEFRYRKHTKAAIKIQAHLRCHAAYSYYRSLQRAAIITQCGWRRRVAKKELRNLKMAARETGALKEAKDKLEKKVEELTWRLQFEKRLRTELEEAKAQEVAKLQEALHAMQKQVEEANAKVVQEREAARRAIEEAPPVIKETPVIIQDTEKINALSAEVENLKALLASEKKATEEARDSSRDAVARNSELANKLEDAERKVDQLQDSVQRLEEKLSNMESENQVLRQQALTMSPTGKTLSARPKTTIIQRTPENGNAINGESKPNSDMILAVASPKEPASEEKPQKSLNEKQQENQDLLIKCISQDLGFSGGKPIAACLIYKCLLHWRSFEVERTSVFDRIIQTIASAIEVPDNNDVLAYWLCNTSTLLMLLQQTLKASGAASLTPQRRRTSSASLFGRMSQGLRGSPQSAGLSVLNGRMLGRLDDLRHVEAKYPALLFKQQLTAFLEKIYGMIRDNLKKEISPLLGLCIQAPRTSRASLVKGRSQANAAAQQALFAHWQSIVKSLNNYLMMMKANYAPPFLVRKVFTQIFSFINVQLFNSLLLRRECCSFSNGEFVKAGLAELEQWCCYATEEYVGSAWDELKHIRQAVGFLVIHQKPKKTLHEITNELCPVLSIQQLYRISTMYWDDKYGTHTVSSDVISSMRVMMTEDSNNAVSSSFLLDDDSSIPFSVDDISKSIQQVDIADVEPPPLIRENSAFVFLHQRSS
Protein: Regulator of G-protein signaling 8 (RGS8) (P57771)
Organism: Homo sapiens (Human)
Function: Regulates G protein-coupled receptor signaling cascades, including signaling via muscarinic acetylcholine receptor CHRM2 and dopamine receptor DRD2 (By similarity). Inhibits signal transduction by increasing the GTPase activity of G protein alpha subunits, thereby driving them into their inactive GDP-bound form. Modulates the activity of potassium channels that are activated in response to DRD2 and CHRM2 signaling (By similarity).
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:P49804}; Peripheral membrane protein {ECO:0000250|UniProtKB:P49804}; Cytoplasmic side {ECO:0000250|UniProtKB:P49804}. Membrane {ECO:0000250|UniProtKB:P49804}; Peripheral membrane protein {ECO:0000250|UniProtKB:P49804}; Cytoplasmic side {ECO:0000250|UniProtKB:P49804}. Perikaryon {ECO:0000250|UniProtKB:P49804}. Cell projection, dendrite {ECO:0000250|UniProtKB:P49804}. Nucleus {ECO:0000250|UniProtKB:P49804}. Note=Detected in Purkinje cell soma and dendrites. Associated with Purkinje cell membranes. Not detected in Purkinje cell nuclei. Detected in the nucleus after heterologous expression. Recruited to the cell membrane in the presence of GNAO1. {ECO:0000250|UniProtKB:P49804}.
Interaction partners:
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein subunit beta-5
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein G
- Succinate--CoA ligase [GDP-forming] subunit beta, mitochondrial
- Regulator of G-protein signaling protein-like
- Rho guanine nucleotide exchange factor 1
- Rho guanine nucleotide exchange factor 11
- Regulator of G-protein signaling 7-binding protein
- Guanine nucleotide-binding protein subunit alpha-13
Sequence:
MAALLMPRRNKGMRTRLGCLSHKSDSCSDFTAILPDKPNRALKRLSTEEATRWADSFDVLLSHKYGVAAFRAFLKTEFSEENLEFWLACEEFKKTRSTAKLVSKAHRIFEEFVDVQAPREVNIDFQTREATRKNLQEPSLTCFDQAQGKVHSLMEKDSYPRFLRSKMYLDLLSQSQRRLS
Protein: U6 snRNA-associated Sm-like protein LSm5 (O42978)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Component of LSm protein complexes, which are involved in RNA processing and may function in a chaperone-like manner. LSm5 is required for processing of pre-tRNAs, pre-rRNAs and U3 snoRNA (By similarity).
Subcellular location: Nucleus {ECO:0000269|PubMed:16823372}.
Interaction partners:
- LSM1-LSM7 complex subunit lsm1
- LSM complex subunit lsm4
- LSM complex subunit lsm2
- LSM complex subunit lsm6
- LSM complex subunit lsm3
- LSM2-LSM8 complex subunit lsm8
- LSM complex subunit lsm7
- U4/U6 snRNA-associated-splicing factor prp24
- Small nuclear ribonucleoprotein Sm D2
- Small nuclear ribonucleoprotein E
Sequence:
MSMTILPLELIDKCIGSNLWVIMKSEREFAGTLVGFDDYVNIVLKDVTEYDTVTGVTEKHSEMLLNGNGMCMLIPGGKPE
Protein: Protocadherin 11 isoform 6 (Q2TJH6)
Organism: Mus musculus (Mouse)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004251}; Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004251}.
Interaction partners:
Sequence:
RCRQPPHLKASQKNKQNSEWVTPNPENRQMIMMKKKKKKKKKHPPKNLLLNFVTIEEAKPDDGENERNSVTLDLPIELEEQTMGKYNWGTTPTTFKPDSPDLARHYKSASPQPAFQIQPETPLNSKHHIIQELPLDNTFVGCDSISKCSSSSSDPYSVSECSYPVTTFKAPVSVHIRPTMKEVVRSHTPMKEATTVEIWTHPHPQSQRRVTFHLPEGSQESISDGGLGDHDAGSLPSTSHALPLGYPQEEYFDHAAPNNRTEGDGNSDPESTAEITVQPTVEEASDTCTQECLILGHSDSCWMPATLTNPSPSQIKTSAICHSPPRPRLSVRRYSPPVTQTVTICHSPPVTQAIALCHSPPPVQVTVPRHSPPPAQASAVSYSPTLVQAVVIHHSPPLPQAATHHRTQAQPPMGLQQGWVQGAGADGLYPIDQGVQGSTRAQFYTMAERFHPDDDSIKVIPLTTFTSGQQARSSRGDSPIIEEHPL
Protein: Inner centromere protein A (DdINCENP) (Q55GF9)
Organism: Dictyostelium discoideum (Social amoeba)
Function: Chromosomal passenger protein that seems to be required for chromosome segregation and the onset of cytokinesis during mitosis. Plays a key role in the abscission of daughter cells at the end of cytokinesis and in the establishment or maintenance of a bipolar spindle.
Subcellular location: Chromosome, centromere {ECO:0000269|PubMed:16339076}. Cytoplasm, cytoskeleton, spindle {ECO:0000269|PubMed:16339076}. Nucleus {ECO:0000269|PubMed:16339076}. Cleavage furrow {ECO:0000269|PubMed:16339076}. Note=During mitosis, found in the spindle midzone and poles. During cytokinesis, found in the cleavage furrow. During prometaphase, found concentrated adjacent to the condensed chromosome. During metaphase, found concentrated in the middle of the spindle surrounded by chromosomes. After the onset of anaphase, moved to the spindle midzone and spindle poles where it remains through late telophase. After initiation of the cleavage furrow, found increasingly concentrated at the furrow area, especially at the cortex area. By the abscission stage of cytokinesis, found highly concentrated in the thin cytoplasmic bridge connecting the two daughter cells.
Interaction partners:
- Aurora kinase
- Kinesin-related protein 12
- Cortexillin-1
Sequence:
MDSIKKNTINRINGLPINHNNLSKTSIISMDDDYNSNSSFYSTNNSILNSVTKNSNYLNNNNNNNNNNNNNNNISISNCNNNNTNNKINEQLKTFNNIFEEKGEFLKEEIDNKFNDIISLMNQSKNQLFLSLNDIDSLYDLSPLSTTSTITLENNNNNNNNLIKFKLFNNDSIKKYILPVSSKTIKFKQRQILIEQQEFNEKHNQQKHLLELQRQQVLSDQQNQFQEQHKQQLSLKQQELEAIQQDTNKVKQQLIETHDKLLIEKEKQFKQDLNSLELNLQNKFTNEYQSKEQEFNKKLEQQQQQLEKQFQQTKELLIVQETLTLKSKLTTEFQEQLKTHQDQINKQELLLKQQEYQLFLKQQEISSIQKQHQDDLSSLKSKLSSDQDQIKKQLLQQESDLLKKQQELLLKQQELDIQSKQLKEEQEKQQQQQEKQQEKQQQQQPVVVPVKPTTSTVVSATTATLIKAPIVSTTTVSTATVSKLVTNGIAKPTPLTTMKQTVTAVPTLMDNKTRLKKLVPTATTTTTKEENNKEYDKMMQELDTQPNNSNLKNLNEKKLETLKQQLTFDDSVSFSNGNDESSINLSKYLEETNKSVENTFDIMSNTLKRKNEPIQQPSSSSSQLSSSQQPSSSSSSSSSSIGLKKRLSDDKTTIVTSKPTNKVQPQSLNSNINNNVVPPSPVAAIANKLKKQQELEKLKLEEEERLRKKQEEQLAKREVEKEQERLEKKKKNDEKRKKVEENQQQRILEEEKKKKEAEDRELARKHKEDSDKKKREEEEDAKKRIQERFRETQEQERKREEFKKQQQEQELARIKKEKLQQEKLQQEKEKQEKQKQQQQQQEEEQQKKKTVQTILPTPQTPSRSANNNYDDAANTASATKAKYALSSILSMVFGATKSPHFKPSTSQDDQDDDDCEDYDGTDENSENEAKGEYQDDSDQEIEEQFENDSDESMASTESNGDIYFNKNKNSNNSNNNNDVNQSRKDKSIVFDSDSLNRNHNDSNNSSEEEEPERDPVFLTPLPKILSNMKNNNNNNTYSNSPVIKGLSPPSSVSDYSPSSESNDCFSPLTPTNNNKINNNKINNNNSNNNSFNNSNSYRGLSPAQIIESHTPKCINRSGESKTSPFLTIRNTPSPLKNSPIKFNMSSASSLSSFDSDNDSDYNDNDIDDGEILGNPNENFTTPLKNQENNNNNNSNNSNTQYPIITSPPSNEDGDENYYFEEEEIDYEYDKRVPDWAKNHNLDNSLKQQRFYDPDRIFSMIGPVYLYEIFPKQDLGGKIKDFSKVKRNLSSDWSRDCNTEKEDISYKKNMGFTNPIIVNKK
Protein: Cadherin domain-containing protein (Q6PD33)
Organism: Mus musculus (Mouse)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004370}.
Interaction partners:
Sequence:
MLQRSKRGWVWNQFFVIDEYNGHNPVLVGRLHSDIDAGDGNIKYILSGEGAGTIFVIDDKSGNIHATKTLDREERAQYTLMAQAVDRDTNKPLGPPSEFIDKDQDINDNPPEFLHEIYHTNVPERSNVGRNISYPSDSL
Protein: Synapsin-1 (Synapsin I) (P09951)
Organism: Rattus norvegicus (Rat)
Function: Neuronal phosphoprotein that coats synaptic vesicles, and binds to the cytoskeleton. Acts as a regulator of synaptic vesicles trafficking, involved in the control of neurotransmitter release at the pre-synaptic terminal. Also involved in the regulation of axon outgrowth and synaptogenesis (By similarity). The complex formed with NOS1 and CAPON proteins is necessary for specific nitric-oxide functions at a presynaptic level.
Subcellular location: Synapse {ECO:0000250|UniProtKB:O88935}. Golgi apparatus {ECO:0000250|UniProtKB:O88935}. Presynapse {ECO:0000269|PubMed:11685225}. Cytoplasmic vesicle, secretory vesicle, synaptic vesicle {ECO:0000269|PubMed:11685225}. Note=Dissociates from synaptic vesicles and redistributes into the axon during action potential firing, in a step that precedes fusion of vesicles with the plasma membrane. Reclusters to presynapses after the cessation of synaptic activity. {ECO:0000269|PubMed:11685225}.
Interaction partners:
- Synaptophysin
- Disks large homolog 4
- Vesicle-associated membrane protein 2
- Synaptotagmin-1
- Multifunctional fusion protein
- Neuromodulin
- Ras-related protein Rab-3A
- Calmodulin-1
- Syntaxin-1A
- Regulating synaptic membrane exocytosis protein 1
Sequence:
MNYLRRRLSDSNFMANLPNGYMTDLQRPQPPPPPPSAASPGATPGSAAASAERASTAAPVASPAAPSPGSSGGGGFFSSLSNAVKQTTAAAAATFSEQVGGGSGGAGRGGAAARVLLVIDEPHTDWAKYFKGKKIHGEIDIKVEQAEFSDLNLVAHANGGFSVDMEVLRNGVKVVRSLKPDFVLIRQHAFSMARNGDYRSLVIGLQYAGIPSVNSLHSVYNFCDKPWVFAQMVRLHKKLGTEEFPLIDQTFYPNHKEMLSSTTYPVVVKMGHAHSGMGKVKVDNQHDFQDIASVVALTKTYATAEPFIDAKYDVRVQKIGQNYKAYMRTSVSGNWKTNTGSAMLEQIAMSDRYKLWVDTCSEIFGGLDICAVEALHGKDGRDHIIEVVGSSMPLIGDHQDEDKQLIVELVVNKMTQALPRQRDASPGRGSHSQTPSPGALPLGRQTSQQPAGPPAQQRPPPQGGPPQPGPGPQRQGPPLQQRPPPQGQQHLSGLGPPAGSPLPQRLPSPTAAPQQSASQATPMTQGQGRQSRPVAGGPGAPPAARPPASPSPQRQAGPPQATRQASISGPAPPKVSGASPGGQQRQGPPQKPPGPAGPIRQASQAGPGPRTGPPTTQQPRPSGPGPAGRPTKPQLAQKPSQDVPPPIIAAAGGPPHPQLNKSQSLTNAFNLPEPAPPRPSLSQDEVKAETIRSLRKSFASLFSD
Protein: Polybia-MP-II (Polybia-MPII) (Venom protein 13a) (VP13a) (P84915)
Organism: Polybia paulista (Neotropical social wasp) (Swarm-founding polistine wasp)
Function: Antimicrobial peptide. Is active against both Gram-negative and -positive bacteria (Staphylococcus aureus (MIC=2 uM), Mycobacterium abscessus subsp. massiliense, S.aureus (EC(50)=1.83 uM), Escherichia coli (MIC=5 uM), Pseudomonas aeruginosa (MIC=38 uM), Bacillus cereus (MIC=5 uM), and the multidrug-resistant bacterium A.baumannii), and fungi (Candida albicans (EC(50)=12.9 uM, EC(90)=15.3 uM) and Cryptococcus neoformans (EC(50)=11 uM, EC(90)=22.7 uM)) (By similarity). Inhibits biofilm formation of A.baumannii and Staphylococcus spp. bacteria. Mycobacteria cell shape and cell wall integrity are not altered after exposure to the peptide (6.25 uM) (By similarity). Has low hemolytic activity (MIC=50 uM) (By similarity). Is also cytotoxic to mouse peritoneal macrophages (EC(50)=13.19 uM) (By similarity). Also causes moderate mast cell degranulation (ED(50)=80 uM) and exhibits chemotactic activity for polymorphonucleated leukocytes (PMNL). Shows antibacterial activity against multidrug-resistant A.baumannii adherence and biofilm formation on vascular stents, preventing its formation and treating mature biofilm. In vivo, shows antistaphylococcal activity (S.aureus) with a decline bacterial load after 6 days of topical treatment (By similarity).
Subcellular location: Secreted {ECO:0000269|PubMed:15150833, ECO:0000269|PubMed:19463874}. Target cell membrane {ECO:0000305|PubMed:19463874}. Note=Assumes an amphipathic alpha-helical conformation in a lipid environment. {ECO:0000305|PubMed:19463874}.
Interaction partners:
Sequence:
INWLKLGKMVIDAL
Protein: DNA topoisomerase 3 (EC 5.6.2.1) (DNA topoisomerase III) (P13099)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Releases the supercoiling and torsional tension of DNA introduced during the DNA replication and transcription by transiently cleaving and rejoining one strand of the DNA duplex. Introduces a single-strand break via transesterification at a target site in duplex DNA. The scissile phosphodiester is attacked by the catalytic tyrosine of the enzyme, resulting in the formation of a DNA-(5'-phosphotyrosyl)-enzyme intermediate and the expulsion of a 3'-OH DNA strand. The free DNA strand than undergoes passage around the unbroken strand thus removing DNA supercoils. Finally, in the religation step, the DNA 3'-OH attacks the covalent intermediate to expel the active-site tyrosine and restore the DNA phosphodiester backbone (By similarity). Essential for proper chromosome segregation in both meiosis and mitosis. Weakly relaxes negative supercoils and displays a distinct preference for binding single-stranded DNA. The TOP3-SGS1 protein complex may function as a eukaryotic reverse gyrase introducing positive supercoils into extrachromosomal ribosomal DNA rings.
Interaction partners:
- RecQ-mediated genome instability protein 1
- ATP-dependent helicase SGS1
- DNA topoisomerase 2
- Crossover junction endonuclease MUS81
- DNA replication ATP-dependent helicase/nuclease DNA2
- DNA topoisomerase 1
- ATP-dependent DNA helicase SRS2
- DNA repair protein RAD1
- Replication factor A protein 1
- ATP-dependent DNA helicase MPH1
Sequence:
MKVLCVAEKNSIAKAVSQILGGGRSTSRDSGYMYVKNYDFMFSGFPFARNGANCEVTMTSVAGHLTGIDFSHDSHGWGKCAIQELFDAPLNEIMNNNQKKIASNIKREARNADYLMIWTDCDREGEYIGWEIWQEAKRGNRLIQNDQVYRAVFSHLERQHILNAARNPSRLDMKSVHAVGTRIEIDLRAGVTFTRLLTETLRNKLRNQATMTKDGAKHRGGNKNDSQVVSYGTCQFPTLGFVVDRFERIRNFVPEEFWYIQLVVENKDNGGTTTFQWDRGHLFDRLSVLTFYETCIETAGNVAQVVDLKSKPTTKYRPLPLTTVELQKNCARYLRLNAKQSLDAAEKLYQKGFISYPRTETDTFPHAMDLKSLVEKQAQLDQLAAGGRTAWASYAASLLQPENTSNNNKFKFPRSGSHDDKAHPPIHPIVSLGPEANVSPVERRVYEYVARHFLACCSEDAKGQSMTLVLDWAVERFSASGLVVLERNFLDVYPWARWETTKQLPRLEMNALVDIAKAEMKAGTTAPPKPMTESELILLMDTNGIGTDATIAEHIDKIQVRNYVRSEKVGKETYLQPTTLGVSLVHGFEAIGLEDSFAKPFQRREMEQDLKKICEGHASKTDVVKDIVEKYRKYWHKTNACKNTLLQVYDRVKASM
Protein: ArfGAP with FG repeats 1 (B8ZZY2)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MAASAKRKQEEKHLKMLRDMTGLPHNRKCFDCDQRGPTYVNMTVGSFVCTSCSGSLRGLNPPHRVKSISMTTFTQQEIEFLQKHGNEVCKQIWLGLFDDRSSAIPDFRDPQKVKEFLQEKYEKKRWYVPPEQAKVVASVHASISGSSASSTSSTPEVKPLKSLLGDSAPTLHLNKGTPSQSPVVGRSQGQQQEKKQFDLLSDLGSDIFAAPAPQSTATANFANFAHFNSHAAQNSANADFANFDAFGQSSGSSNFGGFPTASHSPFQPQTTGGSAASVNANFAHFDNFPKSSSADFGTFNTSQSHQTASAVSKVSTNKAGLQTADKYAALANLDNIFSAGQVPSQSSASSDKYAALAELDSVFSSAATSSNAYTSTSNASSNVFGTVPVVASAQTQPASSSVPAPFGATPSTNPFVAAAGPSVASSTNPFQTNARGATAATFGTASMSMPTGFGTPAPYSLPTSFSGSFQQPAFPAQAAFPQQTAFSQQPNGAGFAAFGQTKPVVTPFGQVAAAGVSSNPFMTGAPTGQFPTGSSSTNPFL
Protein: ArfGAP with FG repeats 1 (C9J2I0)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MLCFKRRHKVCKQIWLGLFDDRSSAIPDFRDPQKVKEFLQEKYEKKRWYVPPEQAKVVASVHASISGSSASSTSSTPEVKPLKSLLGDSAPTLHLNKGTPSQSPVVGRSQGQQQEKKQFDLLSDLGSDIFAAPAPQSTATANFANFAHFNSHAAQNSANADFANFDAFGQSSGSSNFGGFPTASHSPFQPQTTGGSAASVNANFAHFDNFPKSSSADFGTFNTSQSHQTASAVSKVS
Protein: BTB/POZ domain-containing protein 6 (Lens BTB domain protein) (Q96KE9)
Organism: Homo sapiens (Human)
Function: Adapter protein for the cul3 E3 ubiquitin-protein ligase complex (By similarity). Involved in late neuronal development and muscle formation (By similarity).
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:Q2LE78}. Note=Found in punctated bodies in the cytoplasm. {ECO:0000250|UniProtKB:Q2LE78}.
Interaction partners:
- Cullin-3
Sequence:
MLLPLACLHGRVAQCLTSLLLLAEPLPRPRRGARARGAASTGAEAAPAAPPAKMAAELYAPASAAAADLANSNAGAAVGRKAGPRSPPSAPAPAPPPPAPAPPTLGNNHQESPGWRCCRPTLRERNALMFNNELMADVHFVVGPPGATRTVPAHKYVLAVGSSVFYAMFYGDLAEVKSEIHIPDVEPAAFLILLKYMYSDEIDLEADTVLATLYAAKKYIVPALAKACVNFLETSLEAKNACVLLSQSRLFEEPELTQRCWEVIDAQAEMALRSEGFCEIDRQTLEIIVTREALNTKEAVVFEAVLNWAEAECKRQGLPITPRNKRHVLGRALYLVRIPTMTLEEFANGAAQSDILTLEETHSIFLWYTATNKPRLDFPLTKRKGLAPQRCHRFQSSAYRSNQWRYRGRCDSIQFAVDRRVFIAGLGLYGSSSGKAEYSVKIELKRLGVVLAQNLTKFMSDGSSNTFPVWFEHPVQVEQDTFYTASAVLDGSELSYFGQEGMTEVQCGKVAFQFQCSSDSTNGTGVQGGQIPELIFYA
Protein: Probable RNA-binding protein 23 (CAPER beta) (CAPERbeta) (RNA-binding motif protein 23) (RNA-binding region-containing protein 4) (Splicing factor SF2) (Q86U06)
Organism: Homo sapiens (Human)
Function: RNA-binding protein that acts both as a transcription coactivator and pre-mRNA splicing factor. Regulates steroid hormone receptor-mediated transcription, independently of the pre-mRNA splicing factor activity.
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
- Cell division cycle 5-like protein
- RNA-binding protein 25
- Protein arginine N-methyltransferase 5
- SRSF protein kinase 2
Sequence:
MASDDFDIVIEAMLEAPYKKEEDEQQRKEVKKDYPSNTTSSTSNSGNETSGSSTIGETSKKKRSRSHNKSRDRKRSRSRDRDRYRRRNSRSRSPGRQCRHRSRSWDRRHGSESRSRDHRREDRVHYRSPPLATGYRYGHSKSPHFREKSPVREPVDNLSPEERDARTVFCMQLAARIRPRDLEDFFSAVGKVRDVRIISDRNSRRSKGIAYVEFCEIQSVPLAIGLTGQRLLGVPIIVQASQAEKNRLAAMANNLQKGNGGPMRLYVGSLHFNITEDMLRGIFEPFGKIDNIVLMKDSDTGRSKGYGFITFSDSECARRALEQLNGFELAGRPMRVGHVTERLDGGTDITFPDGDQELDLGSAGGRFQLMAKLAEGAGIQLPSTAAAAAAAAAQAAALQLNGAVPLGALNPAALTALSPALNLASQCFQLSSLFTPQTM
Protein: Small ribosomal subunit protein eS17A (40S ribosomal protein S17-A) (RP51A) (P02407)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Component of the ribosome, a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell. The small ribosomal subunit (SSU) binds messenger RNAs (mRNAs) and translates the encoded message by selecting cognate aminoacyl-transfer RNA (tRNA) molecules. The large subunit (LSU) contains the ribosomal catalytic site termed the peptidyl transferase center (PTC), which catalyzes the formation of peptide bonds, thereby polymerizing the amino acids delivered by tRNAs into a polypeptide chain. The nascent polypeptides leave the ribosome through a tunnel in the LSU and interact with protein factors that function in enzymatic processing, targeting, and the membrane insertion of nascent chains at the exit of the ribosomal tunnel.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:22096102}.
Interaction partners:
- Small ribosomal subunit protein eS1A
- Small ribosomal subunit protein eS4A
- Small ribosomal subunit protein uS11B
- Small ribosomal subunit protein eS27A
- Small ribosomal subunit protein uS14B
- Small ribosomal subunit protein eS10A
- Large ribosomal subunit protein uL18
- Small ribosomal subunit protein uS5
- Serine/threonine-protein kinase RIO2
- Small ribosomal subunit protein uS2A
Sequence:
MGRVRTKTVKRASKALIERYYPKLTLDFQTNKRLCDEIATIQSKRLRNKIAGYTTHLMKRIQKGPVRGISFKLQEEERERKDQYVPEVSALDLSRSNGVLNVDNQTSDLVKSLGLKLPLSVINVSAQRDRRYRKRV
Protein: Lysosomal enzyme receptor protein, isoform E (A0A0B4KH68)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Endomembrane system {ECO:0000256|ARBA:ARBA00004308}.
Interaction partners:
- Golgi-localized, gamma-adaptin ear containing, ARF binding protein
- GH05942p
- Sorting nexin 6, isoform B
- Vacuolar protein sorting-associated protein 52 homolog
Sequence:
MRCSLQKDCAAPTQENFRQQMRFPIVISLLLLLFCSGESVAADAANQLKFSTTECKLKEPIYGSTFDFSGLHSDLAHVVKSMNIGGDQFEFNICGNLSRTCNGESNVAACLKRQGKEYILGRQHELFYNNGNMFLKYKSGAKCDNGTADKPNYQLHVMFSCDYTLDAQPMHVTPYANEVCSFYISYRTPLACLSIPEGLQSNSCRVGDTKSNGTFDLMPLSDSNYHTSNRQGAFFVINVCKPVLYGENSMCPAGSSVCLFDSKATNPKERFINFGNVQTHPVVEKGQLLLRHESPTPCAKNSSANYTSVIYFSCDKFIRNAHPEFAGLGADSCTYQFNFATPLACNDLKPCTAFTSTNELLDLSSLSSKPARTLLKDGKNYTIAVCAHAGAPCQENGGACYEQNSTTISLGNSNSQLRFNQTGSLYLLYEDGAECSTATGMRRWSTKIEFVCANNATKDNGASTAGGSDSLKIIEDSNCQLLIQYQTPLACREPIRCKATTYVDHTNDGLGSSGDELIDLTPLISATDNYEARVELPASMEHLVPKTTKFFLNVCRPLVPKYQLGCAGGSAACMAKVTAAGAPEEERSMGFPLVSLTQRNRTFAELAYLKGDPCPTDNTSELSTHILFNCNMRAGRGQPVLRSVEDCAYRFEWETNVFCPPHECTFSADTCDLVHDELGRRFNFKSAPFTKDGKIEIDYNATKMSVNICGAHRKAMTDYSQALVNIFFTHESPNCGREGTMNVQIRLICSDQTESSSTISSDQQCNLLYVQRTPSICEFLSLGATQQNFESNGSTSSSTSSSSTSTTTSTTTQASPAGKPTKAATSTTTTTVGPDPAATPIGPTASVGTILGAILSVTFCVTCLGLLAFSPARRQRIRRLFRRSNSAVRYSRVQSNEEANLLLEPNGEFTESDDDMLL