wanglab/gogpt-training-data huggingface dataset:
Protein: Auxin-responsive protein IAA6 (Indoleacetic acid-induced protein 6) (Q38824)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Aux/IAA proteins are short-lived transcriptional factors that function as repressors of early auxin response genes at low auxin concentrations. Repression is thought to result from the interaction with auxin response factors (ARFs), proteins that bind to the auxin-responsive promoter element (AuxRE). Formation of heterodimers with ARF proteins may alter their ability to modulate early auxin response genes expression.
Subcellular location: Nucleus {ECO:0000250}.
Interaction partners:
- Auxin response factor 5
- Protein TRANSPORT INHIBITOR RESPONSE 1
- Auxin response factor 7
- Auxin response factor 8
- Auxin response factor 1
- Protein AUXIN SIGNALING F-BOX 2
- Auxin-responsive protein IAA33
- Auxin-responsive protein IAA28
- Auxin response factor 6
- Auxin transporter protein 1
Sequence:
MAKEGLALEITELRLGLPGDNYSEISVCGSSKKKKRVLSDMMTSSALDTENENSVVSSVEDESLPVVKSQAVGWPPVCSYRRKKNNEEASKAIGYVKVSMDGVPYMRKIDLGSSNSYINLVTVLENLFGCLGIGVAKEGKKCEYIIIYEDKDRDWMLVGDVPWQMFKESCKRLRIVKRSDATGFGLQQD
Protein: Coiled-coil domain-containing protein 78 (hsCCDC78) (A2IDD5)
Organism: Homo sapiens (Human)
Function: Component of the deuterosome, a structure that promotes de novo centriole amplification in multiciliated cells that can generate more than 100 centrioles. Deuterosome-mediated centriole amplification occurs in terminally differentiated multiciliated cells (G1/0) and not in S phase. Essential for centriole amplification and is required for CEP152 localization to the deuterosome.
Subcellular location: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole. Cytoplasm, perinuclear region. Cell membrane, sarcolemma. Sarcoplasmic reticulum. Note=Localizes to centrioles and deuterosome. Found primarily in the perinuclear region as well as along the sarcolemmal membrane and in reticular pattern within the sarcoplasm.
Interaction partners:
- Deuterosome assembly protein 1
Sequence:
MEHAATTGPRPGPPSRRVENVVLRAKDWLPGAPGGTAVWATSLEAEVPPDLALNKEQQLQISKELVDIQITTHHLHEQHEAEIFQLKSEILRLESRVLELELRGDGTSQGCAVPVESDPRHPRAAAQELRHKAQVPGHSDDHRFQVQPKNTMNPENEQHRLGSGLQGEVKWALEHQEARQQALVTRVATLGRQLQGAREEARAAGQRLATQAVVLCSCQGQLRQAEAENARLQLQLKKLKDEYVLRLQHCAWQAVEHADGAGQAPATTALRTFLEATLEDIRAAHRSREQQLARAARSYHKRLVDLSRRHEELLVAYRAPGNPQAIFDIASLDLEPLPVPLVTDFSHREDQHGGPGALLSSPKKRPGGASQGGTSEPQGLDAASWAQIHQKLRDFSRSTQSWNGSGHSCWSGPRWLKSNFLSYRSTWTSTWAGTSTKS
Protein: TAP binding protein (Tapasin) (Q99JC6)
Organism: Rattus norvegicus (Rat)
Interaction partners:
- Protein disulfide-isomerase A3
- Calreticulin
- Calreticulin
- Calreticulin
- Beta-2-microglobulin
- Antigen peptide transporter 1
- Antigen peptide transporter 2
- Calnexin
- RT1 class I histocompatibility antigen, AA alpha chain
- RT1 class Ib, locus S3
Sequence:
MKLLPLLVVVALGLATVVVSAGPQTIECWFVEDAGGGGLSKKPATLLLRHGPRGPPPRPDLDPKLYFKVDDPAGMLLAAFRRYPAGAHAPHCEMSSYIPFPASAKWARGLSPQQNCSRALDGDWLMVSVSGTVFSLSSLLRPLPEPQREPVFITMATVVLTVLTRHPAPRIHLGKDAVLDLRFAYAPPALEDAPSVASGPPPFGLEWRRQHRGKGHLLLAAIPGLLEKMPPAREKAVAFAAWDDDNDPWGPWTGNGTLWLPAVSPSQEGVYLATVHLPYLQGQVSLELTVHKPPRVSLTPAPIVWAAPGEAPPELLCLVSHFYPEEGLEVEWELRGGPEGSSRKAEGKTWVSTVRHHSDGSVSQSGHLQLPPVTDKQHGVRYACRVRHPSLPSSGRSAEVTLEVAGFSGPSIEDGIGLFLSAFLLLGLFKALGWMAAYLTIPKILKEKASATSLTVPKDEKKSE
Protein: Coatomer subunit epsilon (Epsilon-coat protein) (Epsilon-COP) (O14579)
Organism: Homo sapiens (Human)
Function: The coatomer is a cytosolic protein complex that binds to dilysine motifs and reversibly associates with Golgi non-clathrin-coated vesicles, which further mediate biosynthetic protein transport from the ER, via the Golgi up to the trans Golgi network. The coatomer complex is required for budding from Golgi membranes, and is essential for the retrograde Golgi-to-ER transport of dilysine-tagged proteins. In mammals, the coatomer can only be recruited by membranes associated with ADP-ribosylation factors (ARFs), which are small GTP-binding proteins; the complex also influences the Golgi structural integrity, as well as the processing, activity, and endocytic recycling of LDL receptors (By similarity).
Subcellular location: Cytoplasm {ECO:0000250}. Golgi apparatus membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Cytoplasmic vesicle, COPI-coated vesicle membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Note=The coatomer is cytoplasmic or polymerized on the cytoplasmic side of the Golgi, as well as on the vesicles/buds originating from it. {ECO:0000250}.
Interaction partners:
- Coatomer subunit beta'
- Coatomer subunit alpha
- Coatomer subunit beta
- Coatomer subunit delta
- Coatomer subunit zeta-1
- Coatomer subunit gamma-1
- Coatomer subunit gamma-2
- Coatomer subunit zeta-2
- Protein SEC13 homolog
- N-terminal kinase-like protein
Sequence:
MAPPAPGPASGGSGEVDELFDVKNAFYIGSYQQCINEAQRVKLSSPERDVERDVFLYRAYLAQRKFGVVLDEIKPSSAPELQAVRMFADYLAHESRRDSIVAELDREMSRSVDVTNTTFLLMAASIYLHDQNPDAALRALHQGDSLECTAMTVQILLKLDRLDLARKELKRMQDLDEDATLTQLATAWVSLATGGEKLQDAYYIFQEMADKCSPTLLLLNGQAACHMAQGRWEAAEGLLQEALDKDSGYPETLVNLIVLSQHLGKPPEVTNRYLSQLKDAHRSHPFIKEYQAKENDFDRLVLQYAPSA
Protein: Lysine histidine transporter 1 (Q9FKS8)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Amino acid-proton symporter. Transporter with a broad specificity for histidine, lysine, glutamic acid, alanine, serine, proline and glycine. Involved in both apoplastic transport of amino acids in leaves and their uptake by roots.
Subcellular location: Cell membrane {ECO:0000269|PubMed:16816136}; Multi-pass membrane protein {ECO:0000269|PubMed:16816136}.
Interaction partners:
- Cationic amino acid transporter 6
- WAT1-related protein At2g39510
- WAT1-related protein At1g70260
- WAT1-related protein At1g25270
- WAT1-related protein At4g01430
- WAT1-related protein At1g09380
Sequence:
MVAQAPHDDHQDDEKLAAARQKEIEDWLPITSSRNAKWWYSAFHNVTAMVGAGVLGLPYAMSQLGWGPGIAVLVLSWVITLYTLWQMVEMHEMVPGKRFDRYHELGQHAFGEKLGLYIVVPQQLIVEIGVCIVYMVTGGKSLKKFHELVCDDCKPIKLTYFIMIFASVHFVLSHLPNFNSISGVSLAAAVMSLSYSTIAWASSASKGVQEDVQYGYKAKTTAGTVFNFFSGLGDVAFAYAGHNVVLEIQATIPSTPEKPSKGPMWRGVIVAYIVVALCYFPVALVGYYIFGNGVEDNILMSLKKPAWLIATANIFVVIHVIGSYQIYAMPVFDMMETLLVKKLNFRPTTTLRFFVRNFYVAATMFVGMTFPFFGGLLAFFGGFAFAPTTYFLPCVIWLAIYKPKKYSLSWWANWVCIVFGLFLMVLSPIGGLRTIVIQAKGYKFYS
Protein: Protoplast secreted protein 2 (Q12335)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Subcellular location: Secreted.
Interaction partners:
- Protein RFS1
- Flavoprotein-like protein YCP4
Sequence:
MPRVAIIIYTLYGHVAATAEAEKKGIEAAGGSADIYQVEETLSPEVVKALGGAPKPDYPIATQDTLTEYDAFLFGIPTRFGNFPAQWKAFWDRTGGLWAKGALHGKVAGCFVSTGTGGGNEATIMNSLSTLAHHGIIFVPLGYKNVFAELTNMDEVHGGSPWGAGTIAGSDGSRSPSALELQVHEIQGKTFYETVAKF
Protein: RING finger protein Z (Protein Z) (Zinc-binding protein) (P18541)
Organism: Lymphocytic choriomeningitis virus (strain Armstrong) (LCMV)
Function: Plays a crucial role in virion assembly and budding. Expressed late in the virus life cycle, it acts as an inhibitor of viral transcription and RNA synthesis by interacting with the viral polymerase L. Presumably recruits the NP encapsidated genome to cellular membranes at budding sites via direct interaction with NP. Plays critical roles in the final steps of viral release by interacting with host TSG101, a member of the vacuolar protein-sorting pathway and using other cellular host proteins involved in vesicle formation pathway. The budding of the virus progeny occurs after association of protein Z with the viral glycoprotein complex SSP-GP1-GP2 at the cell periphery, step that requires myristoylation of protein Z. Also selectively represses protein production by associating with host eIF4E.
Subcellular location: Virion {ECO:0000255|HAMAP-Rule:MF_04087}. Host cytoplasm, host perinuclear region {ECO:0000255|HAMAP-Rule:MF_04087}. Host cell membrane {ECO:0000255|HAMAP-Rule:MF_04087}; Lipid-anchor {ECO:0000255|HAMAP-Rule:MF_04087}; Cytoplasmic side {ECO:0000255|HAMAP-Rule:MF_04087}. Note=Mainly perinuclear. During budding, associates at the inner side of the plasma membrane of infected cells. {ECO:0000255|HAMAP-Rule:MF_04087}.
Interaction partners:
Sequence:
MGQGKSREEKGTNSTNRAEILPDTTYLGPLSCKSCWQKFDSLVRCHDHYLCRHCLNLLLSVSDRCPLCKYPLPTRLKISTAPSSPPPYEE
Protein: MAP kinase-activated protein kinase 3 (MAPK-activated protein kinase 3) (MAPKAP kinase 3) (MAPKAP-K3) (MAPKAPK-3) (MK-3) (EC 2.7.11.1) (Chromosome 3p kinase) (3pK) (Q16644)
Organism: Homo sapiens (Human)
Function: Stress-activated serine/threonine-protein kinase involved in cytokines production, endocytosis, cell migration, chromatin remodeling and transcriptional regulation. Following stress, it is phosphorylated and activated by MAP kinase p38-alpha/MAPK14, leading to phosphorylation of substrates. Phosphorylates serine in the peptide sequence, Hyd-X-R-X(2)-S, where Hyd is a large hydrophobic residue. MAPKAPK2 and MAPKAPK3, share the same function and substrate specificity, but MAPKAPK3 kinase activity and level in protein expression are lower compared to MAPKAPK2. Phosphorylates HSP27/HSPB1, KRT18, KRT20, RCSD1, RPS6KA3, TAB3 and TTP/ZFP36. Mediates phosphorylation of HSP27/HSPB1 in response to stress, leading to dissociate HSP27/HSPB1 from large small heat-shock protein (sHsps) oligomers and impair their chaperone activities and ability to protect against oxidative stress effectively. Involved in inflammatory response by regulating tumor necrosis factor (TNF) and IL6 production post-transcriptionally: acts by phosphorylating AU-rich elements (AREs)-binding proteins, such as TTP/ZFP36, leading to regulate the stability and translation of TNF and IL6 mRNAs. Phosphorylation of TTP/ZFP36, a major post-transcriptional regulator of TNF, promotes its binding to 14-3-3 proteins and reduces its ARE mRNA affinity leading to inhibition of dependent degradation of ARE-containing transcript. Involved in toll-like receptor signaling pathway (TLR) in dendritic cells: required for acute TLR-induced macropinocytosis by phosphorylating and activating RPS6KA3. Also acts as a modulator of Polycomb-mediated repression.
Subcellular location: Nucleus {ECO:0000269|PubMed:15302577, ECO:0000269|PubMed:26744326}. Cytoplasm {ECO:0000269|PubMed:15302577, ECO:0000269|PubMed:26744326}. Note=Predominantly located in the nucleus, when activated it translocates to the cytoplasm.
Interaction partners:
- Mitogen-activated protein kinase 14
- Mitogen-activated protein kinase 11
- Mitogen-activated protein kinase 13
- Heat shock protein beta-1
- MAP kinase-activated protein kinase 2
- Mitogen-activated protein kinase 12
- Cyclic AMP-dependent transcription factor ATF-4
- Putative serine/threonine-protein kinase PRKY
- Neuronal migration protein doublecortin
- CapZ-interacting protein
Sequence:
MDGETAEEQGGPVPPPVAPGGPGLGGAPGGRREPKKYAVTDDYQLSKQVLGLGVNGKVLECFHRRTGQKCALKLLYDSPKARQEVDHHWQASGGPHIVCILDVYENMHHGKRCLLIIMECMEGGELFSRIQERGDQAFTEREAAEIMRDIGTAIQFLHSHNIAHRDVKPENLLYTSKEKDAVLKLTDFGFAKETTQNALQTPCYTPYYVAPEVLGPEKYDKSCDMWSLGVIMYILLCGFPPFYSNTGQAISPGMKRRIRLGQYGFPNPEWSEVSEDAKQLIRLLLKTDPTERLTITQFMNHPWINQSMVVPQTPLHTARVLQEDKDHWDEVKEEMTSALATMRVDYDQVKIKDLKTSNNRLLNKRRKKQAGSSSASQGCNNQ
Protein: Phosphoglycerol transferase I (EC 2.7.8.20) (Phosphatidylglycerol--membrane-oligosaccharide glycerophosphotransferase) (P39401)
Organism: Escherichia coli (strain K12)
Function: Transfers a phosphoglycerol residue from phosphatidylglycerol to the membrane-bound nascent glucan backbones.
Subcellular location: Cell inner membrane {ECO:0000269|PubMed:15919996}; Multi-pass membrane protein {ECO:0000269|PubMed:15919996}.
Interaction partners:
- Glucans biosynthesis protein C
- Phosphoethanolamine transferase OpgE
- Uncharacterized protein YpfG
- Periplasmic chaperone Spy
Sequence:
MSELLSFALFLASVLIYAWKAGRNTWWFAATLTVLGLFVVLNITLFASDYFTGDGINDAVLYTLTNSLTGAGVSKYILPGIGIVLGLTAVFGALGWILRRRRHHPHHFGYSLLALLLALGSVDASPAFRQITELVKSQSRDGDPDFAAYYKEPSKTIPDPKLNLVYIYGESLERTYFDNEAFPDLTPELGALKNEGLDFSHTQQLPGTDYTIAGMVASQCGIPLFAPFEGNASASVSSFFPQNICLGDILKNSGYQNYFVQGANLRFAGKDVFLKSHGFDHLYGSEELKSVVADPHYRNDWGFYDDTVLDEAWKKFEELSRSGQRFSLFTLTVDTHHPDGFISRTCNRKKYDFDGKPNQSFSAVSCSQENIATFINKIKASPWFKDTVIVVSSDHLAMNNTAWKYLNKQDRNNLFFVIRGDKPQQETLAVKRNTMDNGATVLDILGGDNYLGLGRSSLSGQSMSEIFLNIKEKTLAWKPDIIRLWKFPKEMKEFTIDQQKNMIAFSGSHFRLPLLLRVSDKRVEPLPESEYSAPLRFQLADFAPRDNFVWVDRCYKMAQLWAPELALSTDWCVSQGQLGGQQIVQHVDKTTWQGKTAFKDTVIDMARYKGNVDTLKIVDNDIRYKADSFIFNVAGAPEEVKQFSGISRPESWGRWSNAQLGDEVKIEYKHPLPKKFDLVITAKAYGNNASRPIPVRVGNEEQTLVLGNEVTTTTLHFDNPTDADTLVIVPPEPVSTNEGNILGHSPRKLGIGMVEIKVVEREG
Protein: Zinc finger protein 703 (Zinc finger elbow-related proline domain protein 1) (Q9H7S9)
Organism: Homo sapiens (Human)
Function: Transcriptional corepressor which does not bind directly to DNA and may regulate transcription through recruitment of histone deacetylases to gene promoters. Regulates cell adhesion, migration and proliferation. May be required for segmental gene expression during hindbrain development.
Subcellular location: Nucleus {ECO:0000269|PubMed:21328542, ECO:0000269|PubMed:21337521}. Cytoplasm {ECO:0000250}.
Interaction partners:
- DDB1- and CUL4-associated factor 7
Sequence:
MSDSPAGSNPRTPESSGSGSGGGGKRPAVPAAVSLLPPADPLRQANRLPIRVLKMLSAHTGHLLHPEYLQPLSSTPVSPIELDAKKSPLALLAQTCSQIGKPDPPPSSKLNSVAAAANGLGAEKDPGRSAPGAASAAAALKQLGDSPAEDKSSFKPYSKGSGGGDSRKDSGSSSVSSTSSSSSSSPGDKAGFRVPSAACPPFPPHGAPVSASSSSSSPGGSRGGSPHHSDCKNGGGVGGGELDKKDQEPKPSPEPAAVSRGGGGEPGAHGGAESGASGRKSEPPSALVGAGHVAPVSPYKPGHSVFPLPPSSIGYHGSIVGAYAGYPSQFVPGLDPSKSGLVGGQLSGGLGLPPGKPPSSSPLTGASPPSFLQGLCRDPYCLGGYHGASHLGGSSCSTCSAHDPAGPSLKAGGYPLVYPGHPLQPAALSSSAAQAALPGHPLYTYGFMLQNEPLPHSCNWVAASGPCDKRFATSEELLSHLRTHTALPGAEKLLAAYPGASGLGSAAAAAAAAASCHLHLPPPAAPGSPGSLSLRNPHTLGLSRYHPYGKSHLSTAGGLAVPSLPTAGPYYSPYALYGQRLASASALGYQ
Protein: C2CD2 like (E9PK05)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
XEEQVELSTIEELIKDAIVSTQPAMMVNLRACSAPGGLVPSEKPPMMPQAQPAIPRPNRLFLRQLRASHLGNELEGTEELCCVAELDNPMQQKWTKPARAGSEVEWTEDLALDLGPQSRELTLKVLRSSSCGDTELLGQATLPVGSPSRPLSRRQLCPLTPGPGKALGPAATMAVELHYEEGSPRNLGTPTSSTPRPSITPTKKIELDRTIMPDGTIVTTVTTVQSRPRIDGKLDSPSRSPSKVEVTEKTTTVLSESSGPSNTSHSSSRDSHLSNGLDPVAETAIRQLTEPSGRVAKKTPTKRSTLIISGVSKVPIAQDELALSLGYAASLEASVQDDAGTSGGPSSPPSDPPAMSPGPLDALSSPTSVQEADETTRSDISERPSVDDIESETGSTGALETRSLKDHKASPLPLQ
Protein: Propionyl-CoA carboxylase beta chain, mitochondrial (PCCase subunit beta) (EC 6.4.1.3) (Propanoyl-CoA:carbon dioxide ligase subunit beta) (Q99MN9)
Organism: Mus musculus (Mouse)
Function: This is one of the 2 subunits of the biotin-dependent propionyl-CoA carboxylase (PCC), a mitochondrial enzyme involved in the catabolism of odd chain fatty acids, branched-chain amino acids isoleucine, threonine, methionine, and valine and other metabolites. Propionyl-CoA carboxylase catalyzes the carboxylation of propionyl-CoA/propanoyl-CoA to D-methylmalonyl-CoA/(S)-methylmalonyl-CoA (By similarity). Within the holoenzyme, the alpha subunit catalyzes the ATP-dependent carboxylation of the biotin carried by the biotin carboxyl carrier (BCC) domain, while the beta subunit then transfers the carboxyl group from carboxylated biotin to propionyl-CoA (By similarity). Propionyl-CoA carboxylase also significantly acts on butyryl-CoA/butanoyl-CoA, which is converted to ethylmalonyl-CoA/(2S)-ethylmalonyl-CoA (By similarity). Other alternative minor substrates include (2E)-butenoyl-CoA/crotonoyl-CoA (By similarity).
Subcellular location: Mitochondrion matrix {ECO:0000250|UniProtKB:P05166}.
Interaction partners:
- Propionyl-CoA carboxylase alpha chain, mitochondrial
- Methylcrotonoyl-CoA carboxylase subunit alpha, mitochondrial
- Methylmalonyl-CoA epimerase, mitochondrial
- Methylmalonate-semialdehyde/malonate-semialdehyde dehydrogenase [acylating], mitochondrial
- Lipoamide acyltransferase component of branched-chain alpha-keto acid dehydrogenase complex, mitochondrial
- 3-ketoacyl-CoA thiolase, mitochondrial
- Trifunctional enzyme subunit beta, mitochondrial
- 3-ketoacyl-CoA thiolase B, peroxisomal
- 3-ketoacyl-CoA thiolase A, peroxisomal
- Peroxisomal acyl-coenzyme A oxidase 1
Sequence:
MAAAIRIRAVAAGARLSVLNCGLGITTRGLCSQPVSVKERIDNKRHAALLGGGQRRIDAQHKRGKLTARERISLLLDPGSFMESDMFVEHRCADFGMAADKNKFPGDSVVTGRGRINGRLVYVFSQDFTVFGGSLSGAHAQKICKIMDQAITVGAPVIGLNDSGGARIQEGVESLAGYADIFLRNVTASGVIPQISLIMGPCAGGAVYSPALTDFTFMVKDTSYLFITGPEVVKSVTNEDVTQEQLGGAKTHTTVSGVAHRAFDNDVDALCNLREFFNFLPLSSQDPAPIRECHDPSDRLVPELDTVVPLESSKAYNMLDIIHAVIDEREFFEIMPSYAKNIVVGFARMNGRTVGIVGNQPNVASGCLDINSSVKGARFVRFCDAFNIPLITFVDVPGFLPGTAQEYGGIIRHGAKLLYAFAEATVPKITVITRKAYGGAYDVMSSKHLLGDTNYAWPTAEIAVMGAKGAVEIIFKGHQDVEAAQAEYVEKFANPFPAAVRGFVDDIIQPSSTRARICCDLEVLASKKVHRPWRKHANIPL
Protein: 14-3-3 domain-containing protein (Q388S1)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MQTTTAASHANISIPCITSLIRGDFTLLMQSLERNECSVSKTYILELALTLIRFDPHLREEECRAFVHAFDSLVRRLLGELRRFNEVESLLREDFHLLTELSERCHTLDQLWGRYSVGKEGEAKKTTDASESFAPSVTIEVPRPPFTTPSKRKNCQDTCSPTETCADSCSSCDVKLAPPVDLSVITNTGGQEETVGRLDDCSEVVRNCAPYSLRGKQLFPEDPLQSSGNEAVRRQQYVEEFLELLTGRLSRDDAAIIVQILGSKPTKCSGKTTGAKRQMSSVTHDEPVYSVSGKSSHAGSKGNIANSNGNISRLGSHVSLVDSLNLRRGGYSVEDNESMTRVDNGSFNAESSAPSSFSAGATPIRSMNKIALYLSVFADMLASGETCVARSLQSTLTRFGDGQHEDQAGDRSTSGNCFREGSNKGDSPMPSGLFPSQKAVNFLSVLFPSLRGYFRDFSWRADNVASDEGGANVVPSGLPHDCLSRKAGNTVRPNAFSAVGGGSNYAGIATLGDNANENEQTGGTGIAFSSGSSNGLYPGDIALFSLLRSLQKGGCIGPAVSADFTSGINDEGKEEEKTSVIDDSGRTTLQQYGDGDGSTIIYCVWVELQAVSKEVHSGVFAAQAMREQIQEEISLLCFRVVTIILELLIPAASSVDQRQVLFFRKWVCDIYRLLLEEELLGRFSALAGASSSAHFTEVVNPDSCAPSTLPPTTPQYRKKRASGKGTPVTITRRGSLTCVLVDDGNGTLQNDSGPPTLKEEIGGLLVPGTAYSRLACSLDKSSARAVEGGSSGTAATDGRLAFIQTPAAPSYPAAHFGHGHYYRRDDPAVVMAESLFDDAPTEPLPQCHFVITRLMAMLLRGAGSVKTSNPVPAPDRGSCSVNGSFAGVSPNEFQTNLPRKPTPSVKPLRQTTRKKITVQGHTQVAASKKVQTSLTGVENKSTLNQRPLNRVAYPVVSCTGDVKALYLSVLCEVELMLSPLDPIRAATVQNAVDFLVSVTQTPGEAFELLDAYLDDVGMEQIQLPQAQRGVIDYVADGGAGSHGYSPLGNEPPSSLGSVRRQRVATLETAASGGGRANAALRSCSVQQKRGGISAEKENSTSLLSMFPVIPTVIPSWNSPDESAQFMTILALLRHKHLTLQGAFGGRSSPPWLYPQGE
Protein: Ataxin 2 (V9GY86)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MSLKPQQQQQQQQQQQQQQQQQQQQQQQPPPAAANVRKPGGSGLLASPAAAPSPSSSSVSSSSATAPSSVVAATSGGGRPGLGRGRNSNKGLPQSTISFDGIYANMRMVHILTSVVGSKCEVQVKNGGIYEGVFKTYSPKCDLVLDAAHEKSTESSSGPKREEIMESILFKCSDFVVVQFKDMDSSYAKRDAFTDSAISAKVNGEHKEKDLEPWDAGELTANEELEALENDVSNGWDPNDMFRYNEENYGVVSTYDSSLSSYTVPLERDNSEEFLKREARANQLAEEIESSAQYKARVALENDDRSEEEKYTAVQRNSSEREGHSINTRENKYIPPGQRNREVISWGSGRQNSPRMGQPGSGSMPSRSTSHTSDFNPNSGSDQRVVNGGVPWPSPCPSPSSRPPSRYQSGPNSLPPRAATPTRPPSRPPSRPSRPPSHPSAHGSPAPVSTMPKRMSSEGPPRMSPKAQRHPRNHRVSAGRGSISSGLEFVSHNPPSEAATPPVARTSPSGGTWSSVVSGVPRLSPKTHRPRSPRQNSIGNTPSGPVLASPQAGIIPTEAVAMPIPAASPTPASPASNRAVTPSSEAKDSRLQDQRQNSPAGNKENIKPNETSPSFSKAENKGISPVVSEHRKQIDDLKKFKNDFRLQPSSTSESMDQLLNKNREGEKSRDLIKDKIEPSAKDSFIENSSSNCTSGSSKPNSPSISPSILSNTEHKRGPEVTSQGVQTSSPACKQEKDDKEEKKDAAEQVRKSTLNPNAKEFNPRSFSQPKPSTTPTSPRPQAQPSPSMVGHQQPTPVYTQPVCFAPNMMYPVPVSPGVQPLYPIPMTPMPVNQAKTYRAVPNMPQQRQDQHHQSAMMHPASAAGPPIAATPPAYSTQYVAYSPQQFPNQPLVQHVPHYQSQHPHVYSPVIQGNARMMAPPTHAQPGLVSSSATQYGAHEQTHAMYACPKLPYNKETSPSFYFAISTGSLAQQYAHPNATLHPHTPHPQPSATPTGQQQSQHGGSHPAPSPVQHHQHQAAQALHLASPQQQSAIYHAGLAPTPPSMTPASNTQSPQNSFPAAQQTVFTIHPSHVQPAYTNPPHMAHVPQAHVQSGMVPSHPTAHAPMMLMTTQPPGGPQAALAQSALQPIPVSTTAHFPYMTHPSVQAHHQQQL
Protein: ANKRD36 protein (A1A5B0)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MEDGKRERWPTLMERLCSDGFAFPQYPIKPYHLKRIHRAVLHGNLEKLKYLLLTYYDANKRDRKERTALHLACATGQPEMVHLLVSRRCELNLCDREDRTPLIKAVQLRQEACATLLLQNGANPNITDFFGRTALHYAVYNEDTSMIEKLLSHGTNIEECSKCEYQPLLFAVSRRKVKMVEFLLKKKANVNAIDYLGRSALIHAVTLGEKDIVILLLQHNIDVLSRDAFRKIAGDYAIEAKNRVIFDLIYEYERKRYEDLPINSNPVSSQKQPAWATERDSMSKIKKRKLIVMKKKSMVIQRFLVTFCK
Protein: B30.2/SPRY domain-containing protein (Q8BNK4)
Organism: Mus musculus (Mouse)
Interaction partners:
Sequence:
ELEEEDENLPIQEVSFDPEKAQCCIVENGQILTHGSGGKGYGLASTGVTSGCYQWKFYIVKENRGNEGTCVGVSRWPVHDFNHRTTSDMWLYRAYSGNLYHNGEQTLTLSSFTQGDFITCVLDMEARTISFGKNGEEPKLAFEDVDAAELYPCVMFYSSNPGEKVKICDMQMRGTPRDLLPGDPICSPVAAVLAEATIQLIRILHRTDRWTYCINKKMMERLHKIKICIKESGQKLKKSRSVQSREENEMREEKENKEEEKGKHNRHGLADLSEPQLRTLCIEVWPVLAVIGGVDAGLRVGGRCVHKQTGRHATLLGVVKEGSTSAKVQWDEAEITIRYDVLCYAFNREVFDGEMGNCPWTVSNNVL
Protein: Killing protein KilR (FtsZ inhibitor protein KilR) (P38393)
Organism: Escherichia coli (strain K12)
Function: Causes inhibition of cell division. At high levels of expression, can also abolish the rod shape of the cells. Division inhibition by KilR can be relieved by overexpression of the cell division protein FtsZ.
Interaction partners:
- Double-strand break reduction protein
- Endodeoxyribonuclease toxin RalR
- Protein RacC
- Uncharacterized protein YdaE
- Putative transcriptional regulator YdaS
- Division inhibition protein DicB
- Uncharacterized protein YdaF
- Uncharacterized protein YdaQ
- Uncharacterized protein YfdS
- Uncharacterized protein YdaG
Sequence:
MIAHHFGTDEIPRQCVTPGDYVLHEGRTYIASANNIKKRKLYIRNLTTKTFITDRMIKVFLGRDGLPVKAESW
Protein: Small ribosomal subunit protein mS39 (28S ribosomal protein S39, mitochondrial) (MRP-S39) (Pentatricopeptide repeat domain-containing protein 3, mitochondrial) (Transformation-related gene 15 protein) (TRG-15) (Q96EY7)
Organism: Homo sapiens (Human)
Function: Mitochondrial RNA-binding protein that has a role in mitochondrial translation.
Subcellular location: Mitochondrion {ECO:0000269|PubMed:19427859, ECO:0000269|PubMed:23908630}.
Interaction partners:
- Small ribosomal subunit protein mS35
- Small ribosomal subunit protein mS22
- Small ribosomal subunit protein mS31
- Small ribosomal subunit protein mS29
- Small ribosomal subunit protein uS2m
- Small ribosomal subunit protein uS5m
- Small ribosomal subunit protein mS27
- Small ribosomal subunit protein uS11m
- Small ribosomal subunit protein uS9m
- Small ribosomal subunit protein mS23
Sequence:
MAVVSAVRWLGLRSRLGQPLTGRRAGLCEQARSCRFYSGSATLSKVEGTDVTGIEEVVIPKKKTWDKVAVLQALASTVNRDTTAVPYVFQDDPYLMPASSLESRSFLLAKKSGENVAKFIINSYPKYFQKDIAEPHIPCLMPEYFEPQIKDISEAALKERIELRKVKASVDMFDQLLQAGTTVSLETTNSLLDLLCYYGDQEPSTDYHFQQTGQSEALEEENDETSRRKAGHQFGVTWRAKNNAERIFSLMPEKNEHSYCTMIRGMVKHRAYEQALNLYTELLNNRLHADVYTFNALIEATVCAINEKFEEKWSKILELLRHMVAQKVKPNLQTFNTILKCLRRFHVFARSPALQVLREMKAIGIEPSLATYHHIIRLFDQPGDPLKRSSFIIYDIMNELMGKRFSPKDPDDDKFFQSAMSICSSLRDLELAYQVHGLLKTGDNWKFIGPDQHRNFYYSKFFDLICLMEQIDVTLKWYEDLIPSAYFPHSQTMIHLLQALDVANRLEVIPKIWKDSKEYGHTFRSDLREEILMLMARDKHPPELQVAFADCAADIKSAYESQPIRQTAQDWPATSLNCIAILFLRAGRTQEAWKMLGLFRKHNKIPRSELLNELMDSAKVSNSPSQAIEVVELASAFSLPICEGLTQRVMSDFAINQEQKEALSNLTALTSDSDTDSSSDSDSDTSEGK
Protein: Frazzled (Q94537)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004479}; Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004479}.
Interaction partners:
Sequence:
MAITTNRSSRTLWNWLLSSCLIFQLIGSSLASQALSFTLEPQDAVVPEGHSVLLQCAGTASIGRGGKSKSNLPSSVSIRWRGPDGQDLVIVGDTFRTQLKNGSLYISSVEENRGLTGAYQCLLTAEGVGSILSRPALVAIVRQPDLNQDFLETYLLPGQTAYFRCMLGEANWQEGVKHSVQWLKDDLPLPLDKLRMVVLPNGALEIDEVGPSDRGSYQCNVTSGSSSRLSSKTNLNIKKPSDPGVENSVAPSFLVGPSPKTVREGDTVTLDCVANGVPKPQIKWLRNGMDLDFNDLDSRFSIVGTGSLQISSAEDIDSGNYQCRASNTVDSLDAQATVQVQEPPKFIKAPKDTTAHEKDEPELKCDIWGKPKPVIRWLKNGDLITPNDYMQLVDGHNLKILGLLNSDAGMFQCVGTNAAGSVHAAARLRVVPQGDSPEQDPSVPHPGGKPLDSGLQARLPSQPRDLVAQIVKSRFVTLSWVEPLQNAGDVVYYTVYYKMNNSEREQKMVTKSHDDQQVNIQSLLPGRTYQFRVEANTNFGSGASSAPLEVSTQPEVNIAGPPRNFEGYARSHKEIYVKWEEPTVTNGEILKYRVYYSENDSGADLYHDSTALEAVLTELRPHTDYVISVVPFNRNGMGDSSAEIRVKTFSSTPSEPPNNVTLEVTSSSSITVHWEPPAEEDRNGQITGYKIRYRKFKDAPQVKSTPANIRYFELSNLDRNAEYQVKIAAMTVNGSGPFTEWNRANTLENDLDETQVPGKPIWISIHPGANNIALHWGPPQHPEIKIRNYVLGWGRGIPDENTIELKETERYHILKNLESNMDYVVSLRARNVKGDGPPIYDNIKTRDEEPVDAPTPLEVPVGLRAITMSSSSIVVYWIDTMLNKNQHVTDNRHYTVSYGITGSNRYRYHNTTDLNCMINDLRPNTQYEFAVKVVKGRRESSWSMSVLNSTYQNVPVTPPREVTVRLDEMNPPTVIVQWIPPKHTLGQITGYNIYYTTDTTKRDRDWSVEAFAGEETMLMLPNLKPYTTYYFKVQARTTKGANNAPFSALVSYTTSAAVTMQEPDTIAKGIDNEKLLYIIIAATAVVLLVVLLGVLLLCRRKPQSSPEHTKKSYQKNNVGVPKPPDLWIHHDQMELKNIDKGLHTVTPVCSDGASSSGALTLPRSVVHSEYEVETPVPGHVTNSLDKRSYVPGYMTTSMNGTMERPQYPRTQYSHQNRSHMTMEAGLSQQSLTQPQSNSMAQTPEHPYGGYDANFCNAGNAAAGNGCVSTIESSKRGHPLKSFSVPGPPPTGGATPVTKHTPAVTIRPQNQSPYKKPSFSAATPNRLQGGGSVVHSTDEIQRLAPSTSTEELNQEMANLEGLMKDLSAITANEFEC