wanglab/gogpt-training-data huggingface dataset:
Protein: Ubiquitin-NEDD8-like protein RUB1 [Cleaved into: Ubiquitin; NEDD8-like protein RUB1 (Ubiquitin-related protein 1) (AtRUB1)] (Q9SHE7)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Ubiquitin exists either covalently attached to another protein, or free (unanchored). When covalently bound, it is conjugated to target proteins via an isopeptide bond either as a monomer (monoubiquitin), a polymer linked via different Lys residues of the ubiquitin (polyubiquitin chains) or a linear polymer linked via the initiator Met of the ubiquitin (linear polyubiquitin chains). Polyubiquitin chains, when attached to a target protein, have different functions depending on the Lys residue of the ubiquitin that is linked: Lys-11-linked is involved in ERAD (endoplasmic reticulum-associated degradation) and in cell-cycle regulation; Lys-29-linked is involved in lysosomal degradation; Lys-33-linked is involved in kinase modification; Lys-48-linked is involved in protein degradation via the proteasome; Lys-63-linked is involved in endocytosis, and DNA-damage responses. Linear polymer chains formed via attachment by the initiator Met lead to cell signaling. Ubiquitin is usually conjugated to Lys residues of target proteins, however, in rare cases, conjugation to Cys or Ser residues has been observed. When polyubiquitin is free (unanchored-polyubiquitin), it also has distinct roles, such as in activation of protein kinases, and in signaling (By similarity).
Subcellular location: [Ubiquitin]: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
Interaction partners:
- Cullin-1
- NEDD8-specific protease 1
- RING-box protein 1a
- Cullin-2
- Cullin-3A
- COP9 signalosome complex subunit 8
- NEDD8-activating enzyme E1 catalytic subunit
- COP9 signalosome complex subunit 4
- NEDD8-activating enzyme E1 regulatory subunit AXR1
- SKP1-like protein 1A
Sequence:
MQIFVKTLTGKTITLEVESSDTIDNVKAKIQDKEGIPPDQQRLIFAGKQLEDGRTLADYNIQKESTLHLVLRLRGGTMIKVKTLTGKEIEIDIEPTDTIDRIKERVEEKEGIPPVQQRLIYAGKQLADDKTAKDYNIEGGSVLHLVLALRGGFGLL
Protein: Dynein axonemal assembly factor 11 (DNAAF11) (Leucine-rich repeat-containing 6-like protein) (Leucine-rich repeat-containing protein 6) (Protein tilB homolog) (Seahorse) (B3DH20)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Function: Plays a crucial role in regulating cilia motility in pronephric tubules, cloaca and neural tube. Required for establishing left-right asymmetry of the body plan; controls cell fate and convergent extension (CE) movements during gastrulation, respectively, via the Wnt and the planar cell polarity (PCP) signaling pathways. Required for the proper development of renal glomeruli and tubules.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:18539122}. Dynein axonemal particle {ECO:0000305|PubMed:18539122}. Cell projection, cilium {ECO:0000269|PubMed:18539122}. Note=Localized to cytoplasmic puncta in ciliated cells. In the semicircular canal, localized to kinocilia.
Interaction partners:
- Zinc finger MYND domain-containing protein 10
- Dynein axonemal assembly factor 3
- Sperm-associated antigen 1A
- Dynein axonemal assembly factor 19
- PIH1 domain containing 3
- Dynein, axonemal, heavy chain 5.
- Dynein axonemal assembly factor 4.
- TOG domain-containing protein.
- Coiled-coil domain-containing protein 40
- Dynein, axonemal, intermediate chain 1, paralog 1.
Sequence:
MVRISEDLIRRRAEHNNGEIFSLEELSLHQQDIQRIEHIHKWCRDLKILYLQNNLIPKIENVGRLKKLEYLNLALNNIEVIENLEGCESLQKLDLTVNFVGRLSSVETLKHNLHLKELYLVGNPCAEYQGYRQYVVATVPQLQSLDGKEISRAERIQALQELDAVRTRVLQQETKYLEEREKQKSNANEHPEINQSLSESQNGTQQYPESSSKTHTEAEDEEREFWEKPCPFTPESRLEAHRHLEEKRRANEKEKEKPKTKTPRTLITPDGRVLNVNEPKLDFSLFEDENNCLLLDLHVYRHMDSSLLDVDVQPMYVRVTVKGKVFQLVLPAEVKPDSSSAQRSQTTGHLLLILPLANEDVKPKKRTIRPTSVTSNQNNKKDTRAAPRRELLEVDPGLAGSLANIVPKGQESSHNPQRCGLEERPVSKDFVDDPEVPPLM
Protein: DNA 3'-5' helicase (EC 5.6.2.4) (Q9VSE6)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- DNA topoisomerase 3-alpha
- Exonuclease 1
- Protein MCM10 homolog
- DEAD-box ATP-dependent DNA helicase Fancm
- Flap endonuclease 1
- DNA repair protein Rad51 homolog
- DNA replication ATP-dependent helicase/nuclease
- Mlh1, isoform A
- Chromosome transmission fidelity protein 18 homolog
- CDC45L
Sequence:
MDDSVFKLKYQKYKLRVKVWEKDFKKKNGRVPSKYDIRDASQEIRDSYKMYYKLKTSFLEETLNDVLSEDGYDILEMSQASDFGVSMLDQDVSLNEGPQLPLDISALVGPQSSGNLEEIPQSVEGSFSNLIDLPNRQVLTNLVNRDENHVIRKFEAVEELPINQNAWGLNVSKKPPAPPQPVEASKSAPGHGKQPKAGASLKPSLSAKLFQSSRGFAKRNPRKPLSRCVSSSSSTTSLSSVPTDHHEELLDFETILIRKAQEYKEKQQAIANNPMLASEHSKESIKTLVDDGWLRRNTKENTLDEEVPFAEANNNSGTSKKTNFGLANLDLSKLKPTVKEEKVLQAKPDQMAIIQELQTDMNSSMNQKPDHLNHTPPASSQKSVAPKNKPPPSEQETDSDSDSVVAESEEEQEPQEYRQLSKRRKIVSTASGKVEVAAPVEIPNKVEPETETFAQENPDFSADEDQDATYVPENKKKDKAKRKQAAGKQKTTKPKAEPKPKTEKKAKVKAEKKPKAEKKPRNSKKAIAVEPAPDPEEDERQPLNPEDLKYVLALEAGDITSVPRINVQDLEEADATAQRYIRTFAAGPNPGLSEGSNIRVDEKRAAARKKLEERIAAGKLNENFVTINIQKKKFVRGKKSVNFSKYKKQQWRHKKRVAALSGPDMDMGGCDGGVLTCFQCGGVGHFAQQCKVKGDSLLPLSAQLEEDPSPFPTLAEAQEMASQGAVVAHSRNISRLPQAANAAILQGDELNESEEDDQESSGDEEVQQHPDPNWSSDEMDVDFEALDAAVEASLSQPVSQEKAASPIKTYVGHKIPEEFLKQAGLDTTASSSNRSQHGGVKPLYDLLPDGSVQDTTPEVLEALHMFGHTNFRKGQDRAIMRTLSGLSSLVTLSTGSGKSLCYQLPAYLYSRKVGAITLVISPLVSLMEDQVTGVPHFLRAHCLHTNQTAPQRMKIQQMIANGEIDILLVSPEAVVAGERATGFGAILRQLPPIAFACIDEAHCVSQWSHNFRPSYLMICKVLRKNLGVRTVLGLTATATLPTRVSIINHLGISDGERGIISDIPLPDNLVLSVSKDENRDAALLQLLNSERFEPCQSIIIYCTRRDECERIAGFIRTCVQDRREPTQDQTKKRKRVNWQAEPYHAGMPASRRRTVQKAFMSNELRIVVATIAFGMGINKPDIRAVIHYNMPRNFESYVQEIGRAGRDGLPSHCHLFLDAKGGDQSELRRHVYSNSIDRHVIRKLLQKIFVPCSCDKEASKRTALPIPLEGDGPRVHMCPGHEIGFSVEKTVEMLDIPAENISTLLCYMELDPRWCISVLSSAYVMAKVISYGGPKYLKHAAKECPPLAMAIALQIRDKTFKEDSNIIEFSVTDIAAGIGWNSGVVKYQLKDLEWVKVNGYPKRSPITVSFYDLGFRIKVPGDFTESEIDNALDTLYTRSVKQERTQLIQLQYVAHGLAAVAYSSCGQCCNADFPQDRGEQLKAIVRNYFANDYPQDLELEIEPSNVPDENIIDDVHALINMYPDNTFTGRNIARIFHGIMSPNYPAVIWGRCKFWRAHVKVDFNRILHLANMAIIKRRT
Protein: RE15215p (Q9VN08)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MGIGMLDSEESSSSALSAIALAVSATSDDNSNETTPCASVSRMAHQLQHTQRLSLGSTGDITLDSPAVEDSLSMSRQSAEKLQILAQAKRSSLGSEGSGNSNSPSKRLRNPLAAVTCNNQIDGTASLNFQPSTSRLAQVRQAKKPSTTNITTRIVAADSFFVFRTPAMSAHINSGINYFERLSDEILLDIFKWLPKKTLLRMATVCRRFNRCSRDETLWTRLDLGLRTIRPGALEQIVRRGVLVIRLAQTSIQEPAFAPYTEVFRTRLQYLDLSMASITRSSLLTLLSHCRQLKKISLENIELDDDICAEIAKNEALEAVNLTMASGLTSNSVRLMMESLTSLSSLNISWTDLSADAVTALVTHISPNLIRLNIAGCRRVLFDSHVATLQKRCPQLLELDLSDCNSLTPTVITAIMKFKMLEYLSVSRCYLIPATKFIELKSMPSLTYLDIFGMLSDTAMEVLEKQLPKMGINKFIHSSVSRPTVGTRRTSIWGLRTRD
Protein: Phosphatidylinositol N-acetylglucosaminyltransferase subunit GPI19 (GPI-GlcNAc transferase complex subunit GPI19) (GPI-GnT subunit GPI19) (EC 2.4.1.198) (Q04082)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Part of the complex catalyzing the transfer of N-acetylglucosamine from UDP-N-acetylglucosamine to phosphatidylinositol, the first step of GPI biosynthesis. Involved in cell wall biosynthesis.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
- Phosphatidylinositol N-acetylglucosaminyltransferase GPI2 subunit
- Phosphatidylinositol N-acetylglucosaminyltransferase subunit GPI15
- Phosphatidylinositol N-acetylglucosaminyltransferase GPI3 subunit
- Phosphatidylinositol N-acetylglucosaminyltransferase subunit GPI1
- N-acetylglucosaminyl-phosphatidylinositol de-N-acetylase
- Phosphatidylinositol N-acetylglucosaminyltransferase ERI1 subunit
- GPI mannosyltransferase 2
- GPI mannosyltransferase 3
- GPI mannosyltransferase 1
- GPI-anchor transamidase
Sequence:
MYTKEYYWFSQYMIITSTLVLTIIWSILPSSLGEAAPKQFINTLLDIFPQRRWIITLESIMLMGMLCTYIGLLMYNEDTLTPPLDSLSTVTDAGGQLVIEDDPDVFVKKWAFKETSGIYDLSLMDACQLLYLYDNDHTST
Protein: DEAD-box ATP-dependent DNA helicase Fancm (EC 5.6.2.4) (Fanconi anemia group M protein homolog) (Protein FACM homolog) (Q9VDA0)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Nucleus {ECO:0000250|UniProtKB:Q8IYD8}.
Interaction partners:
- E3 ubiquitin-protein ligase Fancl
- DNA topoisomerase 3-alpha
- Fanconi anemia group I protein homolog
- RecQ-like DNA helicase Blm
- Fanconi anemia group D2 protein homolog
- DNA topoisomerase 3-beta
- Crossover junction endonuclease MUS81
- ATP-dependent DNA helicase Q4
- Structural maintenance of chromosomes protein 5
- ATP-dependent DNA helicase Q5
Sequence:
MDVNWMDDDEDLVAALAMHEEQKSEDADGTRWEHCDEACDGFDMATGHNWIYPNNLPLRSYQQTIVQSALFKNTLVVLPTGLGKTFIAAVVMYNFYRWYPKGKIVFMAPTRPLVSQQIHASQKIMPFPSEDTVQLTGQLPRPKRAELWASKRVFFATPQVVHSDMLEADGECSFPFGSIKLIVVDEAHRAKGRYAYTQVADCLMARNRYFRMLALSATPGRTMEDVAAVCRNLYISNLQVRWDTSIDVQPYIHRRTIRTIVVSLKERIKEPRERLLQIIEPYLRQLMEAEIFKGNKGTVSRNSLLFEQKSFVERSAQGQRHPDHNIIMGNFAMCISMYHSLDLMERHGLRVFVNNFDADDDGREKFVLARDGNLRNLVEQVRQELGANPLDYTTHAMTNGEVPPLPSDLDFGHAKYEKLRQVLVQHFQANPDSRAIVFCEYRESVMLIHRLLLQHRPVLRPRCFVGQGSTVGASYALTQKQQLQIMTDFRSGTSNVLVATSIGEEGLDVGEVEMIVCFDICSTNPTRFIQRIGRTGRKKNGEVVMLVTEGREQQVLKDVLANKDQINKKLLNSSVVKLSLYEQNPRMVPSKFQPKCEEKHMEPVAEEKPKPKSAAKTKESRKRKQPVAQTGSLRKYFKESPPTESQQGILQGIKPYQMSEASQQLVKQQVLRRSVTLKNFFGESQASSTLTSSQEDVQRLRKLTRLLQSSKPFVSDSKDLMSHLQDDHLPRQIKLYLLKSNPEFLRETHLKMQVQSELNIADDRLNSRQRRTKNNYQLLLDICDGMDQMNELLQGDNSGAEISFRDELNPIYNQSPKKFDTICEQIFDGLNEHGLNSNNFELKQDLLEKLELRNLETTVNEQLGGIEASWSEEEWDQQEEDVKFESMYLSQQLNLPDANVVPHSSTPLRVKPLSKLMFKTLQGDIEEEYHSGMEASELGDNLGRLNSLMNASESKIKATERIAPIPVVDSTIETNHFPAVEESQRSTPISIADSSGESNHCAVNKNSEIYPMSIDETKVEVKSSLNLKMHAESIVEDLDIDLDDFLEPMDKELELASQTKGKSQENIVDHQMEKLEKNCEQKETAHNNDLDLTDEDLKEFLEPMVEEVELMSQKKANDFKDFLEPMPEELELMSQQKKNILLPSTETIKNSENKNSHEDGSRTVSPDIFGSDSMSPLKPQGKSLAAKLAAKAAAKVLPCPPPNSVGLNSPENRKRTNPSIQEKSPSIFDLYLNRMRGRGRLAKAAENLHRITSTNPTISVPKDEEDSPIARRPSKRKIVISSDEEEEQKPQIAETQVDCESDDYERILDTQMPDPRKTPTRPRHKRSKFNSFILDEAEKSGSDHEEEGETTIGTYLKDSMIVSSDDEDHNDTNTHAIYLRALKSPIQRPGAFKMPPPRVFRDESHIFSQPVEDDSSQYMQCSFIVDDESSTIERGHDVSECPLEKAERILKERRKQRRLGKVPSAPVNKRRRLQTISTSSDEDDVVLID
Protein: Fatty-acid-binding protein 2 (AtFAP2) (Chalcone-flavanone isomerase family protein 2) (Q84RK2)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Fatty-acid-binding protein. Associates with saturated fatty acid.
Subcellular location: Plastid, chloroplast stroma {ECO:0000269|PubMed:22622584}.
Interaction partners:
- Fatty-acid-binding protein 3, chloroplastic
- Probable chalcone--flavanone isomerase 3
- Peptidyl-prolyl cis-trans isomerase FKBP12
Sequence:
MSNMDPNSVLPKRSFLQHELFSQLHIPGSLAFEAFSCISKFTGALLCWFSHGNLQKEVSKHQWGLTCKSRDSLKHVFEHRNVSVFPFHYVSKDISPGFFGNISKSTIQHFVNEAERLHSCSLLSLAAAMIPSLNVMSANGLALPLGSNDVKLRENIEHRTCPENTEHRTCQVGCEEYSGLSFQKLDWTRQSVEPRTGIEFPMLLKENASRSNSEVLVATGSRTMKIIRIKSLKVYAFGFYVHPSSVCQKLGRKYASVPASKLDKCDDLYKDLLREDIVMSVRLVVNYNGLKINTVRDVFEKSLRARLVKANPKTDFNCLNDFGSFFRQDIPIPAGTIIDFRRTEDGQLITEIGGNLIGAVRSKDLCRAFFGMYIGDVPVSEQTKEEIGRKVVGIIKRC
Protein: Acyl-coenzyme A thioesterase 6 (Acyl-CoA thioesterase 6) (EC 3.1.2.-) (Q3I5F7)
Organism: Homo sapiens (Human)
Function: Catalyzes the hydrolysis of acyl-CoAs into free fatty acids and coenzyme A (CoASH), regulating their respective intracellular levels. Catalyzes the hydrolysis of phytanoyl-CoA and pristanoyl-CoA, two methyl-branched fatty acids derived from phytol, that enter the body via the diet.
Subcellular location: [Isoform 1]: Peroxisome {ECO:0000305|PubMed:16940157}. Note=Localization to the peroxisome is uncertain since the potential C-terminal peroxisome targeting signal found in the mouse ortholog is not perfectly conserved. {ECO:0000305|PubMed:16940157}.; SUBCELLULAR LOCATION: [Isoform 2]: Cytoplasm {ECO:0000305|PubMed:16940157}. Note=Recombinant N-terminally GFP-tagged protein localizes to the cytosol. {ECO:0000305|PubMed:16940157}.
Interaction partners:
Sequence:
MAATLILEPAGRCCWDEPLRIAVRGLAPEQPVTLRTSLRDEEGALFRAHARYRADARDELDLERAPALGGSFAGLQPMGLLWALEPEKALVRLVKRDVRTPFAVELEVLDGHDTEPGRLLCLAQNKRDFLRPGVRREPVRAGPVRAALFLPPDEGPFPGIIDLFGSSRGLCEYRASLLAGHGFAVLALAYFRFEDLPEDLNDVHLEYFEEAVDFMLQHPKVKGPSIALLGFSKGGDLCLSMASFLKGITATVLINACVANTVAPLHYKDMIIPKLVDDLGKVKITKSGFLTFMDTWSNPLEEHNHQSLVPLEKAQVPFLFIVGMDDQSWKSEFYAQIASERLQAHGKERPQIICYPETGHCIDPPYFPPSRASVHAVLGEAIFYGGEPKAHSKAQVDAWQQIQTFFHKHLNGKKSVKHSKI
Protein: C2H2 transcription factor (Swi5), putative (Q4WXZ7)
Organism: Aspergillus fumigatus (strain ATCC MYA-4609 / CBS 101355 / FGSC A1100 / Af293) (Neosartorya fumigata)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- Cyclin-dependent kinase 1
- protein-tyrosine-phosphatase
- G2/M-specific cyclin NimE
- non-specific serine/threonine protein kinase
Sequence:
MLANPHSNLHERYRQHRRQISTPNALEAAKVPTLPAQALQRINAHRRGQSLDQRPLHDGTVSITNATATQQHQILAGGEQHPQFSQSAHFPQHSSPMPVMPECPSLTSEDLQALSNSTSNANHPGMAYMNSSFFAMGNPSLGLRPMDNNLNLMQQQQQQNAHVSCVNSLEGQILDNGAWNFYQQGQLPTTLRSQVNNLSADGRRQSVQSDITPSQRPHTPKQANTHYFPITPATTPFKKPAELAQYSTDMQSTPTKETGRSAPASAQSVYMQRAKSLQGVAGSTFSNSKIEMPSPPNTASFEIDNFDAFSSQQGSSFEISESENLSQSHYASSSATSSFQSSPELAAMPSPEDNHEKAHKLPIFPAASNRPAHRKALSTSSSSTLTKPRLSPRVASIDSLNLDARVHASIKETGITIDEIASYISGPDPEDGKWVCLHPGCERRFGRKENIKSHVQTHLGDRQYKCDHCNKCFVRGHDLKRHAKIHTGDKPYECLCGNVFARHDALTRHRQRGMCIGGYKGIVRKTTKRGRPKKHRPELEERQDKAAKTRQRVAEKSSHDSSSGCVDSPNSPPSEILENMSLHGGSSPKENMPAFIQPNFSLPPSAFTFTPPASPRQSLGNQPSPAQSRRSLTPSSEDEMLPLSPSKRPLEKIVEEPSLPFTSSADPYTDIAASTAELSSPHTAPTLADSSHGSDLDIFISTDSSANFKHEFPDLSDPDMAAFPDYVNGSTFEPGMDLFSSKTFSAGTSMNEDFFSLQFQVDDMTKEFFMDC
Protein: Heterogeneous nuclear ribonucleoprotein A1 (hnRNP A1) (Helix-destabilizing protein) (Single-strand RNA-binding protein) (hnRNP core protein A1) [Cleaved into: Heterogeneous nuclear ribonucleoprotein A1, N-terminally processed] (P09651)
Organism: Homo sapiens (Human)
Function: Involved in the packaging of pre-mRNA into hnRNP particles, transport of poly(A) mRNA from the nucleus to the cytoplasm and modulation of splice site selection. Plays a role in the splicing of pyruvate kinase PKM by binding repressively to sequences flanking PKM exon 9, inhibiting exon 9 inclusion and resulting in exon 10 inclusion and production of the PKM M2 isoform. Binds to the IRES and thereby inhibits the translation of the apoptosis protease activating factor APAF1. May bind to specific miRNA hairpins.
Subcellular location: Nucleus {ECO:0000269|PubMed:17289661, ECO:0000269|PubMed:27694260}. Cytoplasm {ECO:0000269|PubMed:17289661}. Note=Localized in cytoplasmic mRNP granules containing untranslated mRNAs. Shuttles continuously between the nucleus and the cytoplasm along with mRNA. Component of ribonucleosomes (PubMed:17289661). {ECO:0000269|PubMed:17289661, ECO:0000269|PubMed:27694260}.; SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:17229681}. Note=(Microbial infection) In the course of viral infection, colocalizes with HCV NS5B at speckles in the cytoplasm in a HCV-replication dependent manner. {ECO:0000269|PubMed:17229681}.; SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:33360543}. Note=(Microbial infection) SARS coronavirus-2/SARS-CoV-2 ORF6 protein increases accumulation to the nucleus. {ECO:0000269|PubMed:33360543}.
Interaction partners:
- Heterogeneous nuclear ribonucleoproteins C1/C2
- Transportin-1
- Heterogeneous nuclear ribonucleoprotein H
- Heterogeneous nuclear ribonucleoproteins A2/B1
- Polypyrimidine tract-binding protein 1
- TAR DNA-binding protein 43
- Heterogeneous nuclear ribonucleoprotein K
- Heterogeneous nuclear ribonucleoprotein L
- Serine/arginine-rich splicing factor 1
- Heterogeneous nuclear ribonucleoprotein M
Sequence:
MSKSESPKEPEQLRKLFIGGLSFETTDESLRSHFEQWGTLTDCVVMRDPNTKRSRGFGFVTYATVEEVDAAMNARPHKVDGRVVEPKRAVSREDSQRPGAHLTVKKIFVGGIKEDTEEHHLRDYFEQYGKIEVIEIMTDRGSGKKRGFAFVTFDDHDSVDKIVIQKYHTVNGHNCEVRKALSKQEMASASSSQRGRSGSGNFGGGRGGGFGGNDNFGRGGNFSGRGGFGGSRGGGGYGGSGDGYNGFGNDGGYGGGGPGYSGGSRGYGSGGQGYGNQGSGYGGSGSYDSYNNGGGGGFGGGSGSNFGGGGSYNDFGNYNNQSSNFGPMKGGNFGGRSSGPYGGGGQYFAKPRNQGGYGGSSSSSSYGSGRRF
Protein: Presenilin (EC 3.4.23.-) (Q38F54)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Subcellular location: Endoplasmic reticulum membrane {ECO:0000256|RuleBase:RU361148}; Multi-pass membrane protein {ECO:0000256|RuleBase:RU361148}. Golgi apparatus membrane {ECO:0000256|RuleBase:RU361148}; Multi-pass membrane protein {ECO:0000256|RuleBase:RU361148}.
Interaction partners:
- Nicastrin
- Inhibitor of apoptosis-promoting Bax1
Sequence:
MRRSRVPADGVSHILGKRAVALLVPVLITLMLVTWSVLNLSSLIGERQNSLVIVEPYGNESSSLQVFEASVINALAVVALIVVFTFIMLALYKFGFEIVLYVWLGVSVGSILFITMWVFLDLVLTRFQIPYDFITMFLVLWNTGVVGLVSIFYYSHPTVAQVYLIAISVIVAWSATSLPAWTTWCLLVAVAIYDVVAVLCPYGPLRMLVEAADERNRPIPALVYDSDARIIVATSFPGEDAQMVEIAARARKQEGGRQRPRKRPPSPLDSLLGDTPFKLGLGDFIFYSLLCGIAASYSFIPWLMSVIAVLFGLVGTLLFLVLFKEKLTALPALPISIALGVITYFSSRYLVVPLDWFATLSVLAL
Protein: HTH-type transcriptional regulator TtgR (Toluene efflux pump ttgABC operon repressor) (Q9AIU0)
Organism: Pseudomonas putida (strain DOT-T1E)
Function: Represses expression from the ttgABC operon promoter and its own expression. Binds to a promoter region between the divergently transcribed ttgR and ttgABC genes/operons; in the presence of chloramphenicol or tetracycline this binding no longer occurs and ttgR and ttgABC are derepressed. This suggests that TtgR binds these antibiotics.
Interaction partners:
Sequence:
MVRRTKEEAQETRAQIIEAAERAFYKRGVARTTLADIAELAGVTRGAIYWHFNNKAELVQALLDSLHETHDHLARASESEDEVDPLGCMRKLLLQVFNELVLDARTRRINEILHHKCEFTDDMCEIRQQRQSAVLDCHKGITLALANAVRRGQLPGELDAERAAVAMFAYVDGLIRRWLLLPDSVDLLGDVEKWVDTGLDMLRLSPALRK
Protein: Outer spore wall protein 4 (Loss of heterozygosity protein 1) (P47055)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Involved in spore wall assembly. May be involved in maintaining genome integrity.
Subcellular location: Membrane {ECO:0000255}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Outer spore wall protein 7
- Outer spore wall assembly protein SHE10
- Uncharacterized protein YGL138C
- Chitin deacetylase 1
- Regulator of rDNA transcription protein 5
- Subtilase-type proteinase RRT12
- Outer spore wall protein 1
- Lipid droplet organization protein LDO16
- Ectonucleotide pyrophosphatase/phosphodiesterase 2
Sequence:
MRFQLFIYFYFTIVVIAGTNTIQQFSDAGDRLITSLRNLDNNGTYETLTAEKVPIIEGQIQNISAKYEQHTFILKGLEAVLNYKVKSLDNNERESLEIEYEKVEKALDAALNVSPFEYIKKFKEVSRGKVVNALENLSREQNRITINGGREDEKEKEAREKKKRLDRIKRILTVSLLELGLAQGVADLCAVAPFACLLGVTVGSIGFIFWLALIYNAIQ
Protein: Protein 60A (Protein glass bottom boat) (P27091)
Organism: Drosophila melanogaster (Fruit fly)
Function: Required for the growth of imaginal tissues and for patterning of the adult wing.
Subcellular location: Secreted {ECO:0000269|PubMed:1601181}.
Interaction partners:
- Dorsal-ventral patterning protein Sog
- receptor protein serine/threonine kinase
- Protein decapentaplegic
- receptor protein serine/threonine kinase
- receptor protein serine/threonine kinase
- Serine/threonine-protein kinase receptor
- Crossveinless 2
- receptor protein serine/threonine kinase
- Mothers against decapentaplegic homolog
- Mothers against decapentaplegic homolog
Sequence:
MSGLRNTSEAVAVLASLGLGMVLLMFVATTPPAVEATQSGIYIDNGKDQTIMHRVLSEDDKLDVSYEILEFLGIAERPTHLSSHQLSLRKSAPKFLLDVYHRITAEEGLSDQDEDDDYERGHRSRRSADLEEDEGEQQKNFITDLDKRAIDESDIIMTFLNKRHHNVDELRHEHGRRLWFDVSNVPNDNYLVMAELRIYQNANEGKWLTANREFTITVYAIGTGTLGQHTMEPLSSVNTTGDYVGWLELNVTEGLHEWLVKSKDNHGIYIGAHAVNRPDREVKLDDIGLIHRKVDDEFQPFMIGFFRGPELIKATAHSSHHRSKRSASHPRKRKKSVSPNNVPLLEPMESTRSCQMQTLYIDFKDLGWHDWIIAPEGYGAFYCSGECNFPLNAHMNATNHAIVQTLVHLLEPKKVPKPCCAPTRLGALPVLYHLNDENVNLKKYRNMIVKSCGCH
Protein: OXA1L mitochondrial inner membrane protein (J3KNA0)
Organism: Homo sapiens (Human)
Subcellular location: Membrane {ECO:0000256|RuleBase:RU003945}; Multi-pass membrane protein {ECO:0000256|RuleBase:RU003945}. Mitochondrion inner membrane {ECO:0000256|ARBA:ARBA00004448}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004448}.
Interaction partners:
Sequence:
MVTWLYRFLPTSNMAAKLRSLLPPDLRLQFWLHARLQKCFLSRGCGSYCAGAKASPLPGKMAMGLMCGRRELLRLLQSGRRVHSVAGPSQWLGKPLTTRLLFPAAPCCCRPHYLFLAASGPRSLSTSAISFAEVQVQAPPVVAATPSPTAVPEVASGETADVVQTAAEQSFAELGLGSYTPVGLIQNLLEFMHVDLGLPWWGAIAACTVFARCLIFPLIVTGQREAARIHNHLPEIQKFSSRIREAKLAGDHIEYYKASSEMALYQKKHGIKLYKPLILPVTQAPIFISFFIALREMANLPVPSLQTGGLWWFQDLTVSDPIYILPLAVTATMWAVLELGAETGVQSSDLQWMRNVIRMMPLITLPITMHFPTAVFMYWLSSNLFSLVQVSCLRIPAVRTVLKIPQRVVHDLDKLPPREGFLESFKKGWKNAEMTRQLREREQRMRNQLELAARGPLRQTFTHNPLLQPGKDNPPNIPSSSSKPKSKYPWHDTLG
Protein: Single-stranded DNA-binding protein, mitochondrial (P34496)
Organism: Caenorhabditis elegans
Function: Has a role in germline cell development and proliferation which affects the frequency of apoptosis. Required for mitochondrial DNA replication and transcription and fertility.
Subcellular location: Mitochondrion {ECO:0000250}. Mitochondrion matrix, mitochondrion nucleoid {ECO:0000250}.
Interaction partners:
- Small ribosomal subunit protein bS6m
- DNA-directed DNA polymerase
- Large ribosomal subunit protein bL21m
- Small ribosomal subunit protein uS10m
- Small ribosomal subunit protein uS10
- Eukaryotic translation initiation factor 4C
- Proliferating cell nuclear antigen
- Large ribosomal subunit protein uL4m
- DNA topoisomerase 3
- DNA topoisomerase
Sequence:
MLRSLSTISKSTVRCMSLTSKMAAEQPSKQEVDDLFAEKPQHHNPEQRRHAYSVNKVELVGGVALDPLYKTGRNGKPYLIFNIITNSYFKQQDGTTLDQTERHAVSVFGKQAEILSKTIKKGSRLMVQGRLHYSGGQKDEQGNRTQRNTYIIAQTVQPLARAARENPDQH
Protein: Zinc finger CCHC domain-containing protein 3 (Q8BPK2)
Organism: Mus musculus (Mouse)
Function: Nucleic acid-binding protein involved in innate immune response to DNA and RNA viruses. Binds DNA and RNA in the cytoplasm and acts by promoting recognition of viral nucleic acids by virus sensors, such as RIGI, IFIH1/MDA5 and CGAS. Acts as a co-sensor for recognition of double-stranded DNA (dsDNA) by cGAS in the cytoplasm, thereby playing a role in innate immune response to cytosolic dsDNA and DNA virus (By similarity). Binds dsDNA and probably acts by promoting sensing of dsDNA by CGAS, leading to enhance CGAS oligomerization and activation (By similarity). Promotes sensing of viral RNA by RIG-I-like receptors proteins RIGI and IFIH1/MDA5 via two mechanisms: binds double-stranded RNA (dsRNA), enhancing the binding of RIGI and IFIH1/MDA5 to dsRNA and promotes 'Lys-63'-linked ubiquitination and subsequent activation of RIGI and IFIH1/MDA5 (By similarity).
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:Q9NUD5}.
Interaction partners:
- Interferon-induced helicase C domain-containing protein 1
Sequence:
MATGGGAEEESQRGRPQLPLPARPVARVEEPEGVREKMGWAQVVKNLAEKKGDFREPRRRDETGSGASGGLGSPGGLATPNPGDFPPAARGDPKGRRRDPTGEASDAYRKKSASGAGDPSRRKKAEVTAAMATPARPGTTEDATERPLQDEPPAAGPGKGRFLVRICFQGDESACPTRDFVVGALILRSIGMDPDDIYAVIQIPGSREFDVSFRSAEKLALFLRVYEEKRELEDCWENFVVLGRSRSSLKTLFILFRNETVDVEDIVTWLKRHCDVLAVPVKVTDRFGIWTGEYKCEIELRQGEGGVRHLPGAFFLGAERGYSWYKGQPKTCFKCGSRTHMSGTCTQDRCFRCGEEGHLSPYCRKVIVCNLCGKRGHAFAQCPKAVHNSVTAQLTSVAGH
Protein: Transmembrane protein 150A (Transmembrane protein 150) (Q86TG1)
Organism: Homo sapiens (Human)
Function: Regulates localization of phosphatidylinositol 4-kinase (PI4K) to the plasma membrane, possibly by reducing the association of TTC7 (TTC7A or TTC7B) with the PI4K complex. Acts as a regulator of phosphatidylinositol 4-phosphate (PtdIns(4)P) synthesis. May also play a role in fasting-induced catabolism (By similarity).
Subcellular location: Cell membrane {ECO:0000269|PubMed:25608530}; Multi-pass membrane protein {ECO:0000269|PubMed:25608530}. Note=Localizes mainly at the plasma membrane; only a minor fraction localizes on intracellular structures (PubMed:25608530). {ECO:0000269|PubMed:25608530}.
Interaction partners:
- Tetratricopeptide repeat protein 7A
Sequence:
MTAWILLPVSLSAFSITGIWTVYAMAVMNHHVCPVENWSYNESCPPDPAEQGGPKTCCTLDDVPLISKCGSYPPESCLFSLIGNMGAFMVALICLLRYGQLLEQSRHSWVNTTALITGCTNAAGLLVVGNFQVDHARSLHYVGAGVAFPAGLLFVCLHCALSYQGATAPLDLAVAYLRSVLAVIAFITLVLSGVFFVHESSQLQHGAALCEWVCVIDILIFYGTFSYEFGAVSSDTLVAALQPTPGRACKSSGSSSTSTHLNCAPESIAMI
Protein: IST1 homolog (Charged multivesicular body protein 8) (H3BMU1)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MLGSGFKAERLRVNLRLVINRLKLLEKKKTELAQKARKEIADYLAAGKDERARIRVEHIIREDYLVEAMEILELYCDLLLARFGLIQSMKELDSGLAESVSTLIWAAPRLQSEVAELKIVADQLCAKYSKEYGKLCRTNQIGTVNDRLMHKLSVEAPPKILVERYLIEIAKNYNVPYEPDSVVMAEAPPGVETDLIDVGFTDDVKK
Protein: Tachykinin-like peptide-XV (P.nigriventer tachykinin peptides XV) (PnTkP-XV) (U29-ctenitoxin-Pn1o) (U29-CNTX-Pn1o) (P86297)
Organism: Phoneutria nigriventer (Brazilian armed spider) (Ctenus nigriventer)
Subcellular location: Secreted {ECO:0000269|PubMed:15573368}.
Interaction partners:
Sequence:
QKKDKKDRFPNGLV