wanglab/gogpt-training-data huggingface dataset:
Protein: Rho GTPase activating protein 21 (A0A087WW76)
Organism: Homo sapiens (Human)
Subcellular location: Cell junction {ECO:0000256|ARBA:ARBA00004282}. Cytoplasm, cytoskeleton {ECO:0000256|ARBA:ARBA00004245}. Cytoplasmic vesicle membrane {ECO:0000256|ARBA:ARBA00004284}; Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004284}. Golgi apparatus membrane {ECO:0000256|ARBA:ARBA00004395}; Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004395}.
Interaction partners:
Sequence:
MATRRTGLSEGDGDKLKACEVSKNKDGKEQSETVSLSEDETFSWPGPKTVTLKRTSQGFGFTLRHFIVYPPESAIQFSYKDEENGNRGGKQRNRLEPMDTIFVKQVKEGGPAFEAGLCTGDRIIKVNGESVIGKTYSQVIALIQNSDTTLELSVMPKDEDILQVAYSQDAYLKGNEAYSGNARNIPEPPPICYPWLPSAPSAMAQPVEISPPDSSLSKQQTSTPVLTQPGRAYRMEIQVPPSPTDVAKSNTAVCVCNESVRTVIVPSEKVVDLLSNRNNHTGPSHRTEEVRYGVSEQTSLKTVSRTTSPPLSIPTTHLIHQPAGSRSLEPSGILLKSGNYSGHSDGISSSRSQAVEAPSVSVNHYSPNSHQHIDWKNYKTYKEYIDNRRLHIGCRTIQERLDSLRAASQSTTDYNQVVPNRTTLQGRRRSTSHDRVPQSVQIRQRSVSQERLEDSVLMKYCPRSASQGALTSPSVSFSNHRTRSWDYIEGQDETLENVNSGTPIPDSNGEKKQTYKWSGFTEQDDRRGICERPRQQEIHKSFRGSNFTVAPSVVNSDNRRMSGRGVGSVSQFSSIPSIMRKTFEKKPTATGTFGVRLDDCPPAHTNRYIPLIVDICCKLVEERGLEYTGIYRVPGNNAAISSMQEELNKGMADIDIQDDKWRDLNVISSLLKSFFRKLPEPLFTNDKYADFIEANRKEDPLDRLKTLKRLIHDLPEHHYETLKFLSAHLKTVAENSEKNKMEPRNLAIVFGPTLVRTSEDNMTHMVTHMPDQYKIVETLIQHHDWFFTEEGAEEPLTTVQEESTVDSQPVPNIDHLLTNIGRTGVSPGDVSDSATSDSTKSKGSWGSGKDQYSRELLVSSIFAAASRKRKKPKEKAQPSSSEDELDNVFFKKENVEQCHNDTKEESKKESETLGRKQKIIIAKENSTRKDPSTTKDEKISLGKESTPSEEPSPPHNSKHNKSPTLSCRFAILKESPRSLLAQKSSHLEETGSDSGTLLSTSSQASLARFSMKKSTSPETKHSEFLANVSTITSDYSTTSSATYLTSLDSSRLSPEVQSVAESKGDEADDERSELISEGRPVETDSESEFPVFPTALTSERLFRGKLQEVTKSSRRNSEGSELSCTEGSLTSSLDSRRQLFSSHKLIECDTLSRKKSARFKSDSGSLGDAKNEKEAPSLTKVFDVMKKGKSTGSLLTPTRGESEKQEPTWKTKIADRLKLRPRAPADDMFGVGNHKVNAETAKRKSIRRRHTLGGHRDATEISVLNFWKVHEQSGERESELSAVNRLKPKCSAQDLSISDWLARERLRTSTSDLSRGEIGDPQTENPSTREIATTDTPLSLHCNTGSSSSTLASTNRPLLSIPPQSPDQINGESFQNVSKNASSAANAQPHKLSETPGSKAEFHPCL
Protein: Protein STAY-GREEN 1, chloroplastic (LeSGR1) (SlSGR1) (Protein GREEN FLESH) (Q4JFW8)
Organism: Solanum lycopersicum (Tomato) (Lycopersicon esculentum)
Function: Required to trigger chlorophyll degradation during leaf senescence and fruit ripening. Binds directly PSY1 to regulate the accumulation of lycopene and beta-carotene in the maturing fruits.
Subcellular location: Plastid, chloroplast {ECO:0000255}.
Interaction partners:
- Rieske domain-containing protein
- Rieske domain-containing protein
- 7-hydroxymethyl chlorophyll a reductase
- Staygreen protein domain-containing protein
- Divinyl chlorophyllide a 8-vinyl-reductase, chloroplastic
- Chlorophyll synthase, chloroplastic
- Staygreen protein domain-containing protein
- NADPH-protochlorophyllide oxidoreductase
- NADPH-protochlorophyllide oxidoreductase
- Chlorophyllase
Sequence:
MGTLTTSLVVPSKLNNEQQSSIFIHKTRRKCKKNQSIVPVARLFGPAIFEASKLKVLFLGVDEEKHPGKLPRTYTLTHSDITSKLTLAISQTINNSQLQGWYNRLQRDEVVAEWKKVKGKMSLHVHCHISGGHFMLDLFARLRNYIFCKELPVVLKAFVHGDENLLRNYPELQEALVWVYFHSNIQEFNKVECWGPLRDATSPSSSSGGVGGVKSTSFTSNSNKKWELPKPCEEACACCFPPVSVMPWLSSNLDGVGEENGTIQQGLQEQQS
Protein: Phospholipid scramblase (Q9VT88)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Putative lipoyltransferase 2, mitochondrial
Sequence:
MKSNVNQGGYAPPGFGSGFQPNAPPAEGFGYPPPTGGHNAPYPPAPGHPQPPPPTNYGFMPGPQPAGYAPVPQMPPYGEAPPYGAGQPPYMGGPGGQPPYAGGPGGQPPYVGGPGGQPHYGGGAPPPQAFGGYPPGPAGPGGPPNAFGGYPPGQPQQPIVTQPGMGPGMGPGMAPQGGPAGDWMSIPTGIPNCPRGLEYLTTIDQLLVKQKVELLEAFTGFETNNKFTIKNALGQKVYFAAEDNDCCTRNCCGPARPFDMRVFDNFQQEVIHMHRPLACSSCLFPCCLQSIEVSAPPGNVIGTIEQEWSICSPSFRILNHVGDTVMRIEGPFCTFSLCGDVEFNVVSLTGEKIGKISKQWSGLAREIFTDADFFGINFPLDLDVRMKAVLLGATFLIDAMFFEKAGNQETDRPGML
Protein: Large ribosomal subunit protein uL16 (60S ribosomal protein L10) (Q5AIB8)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (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:0000305|PubMed:35613268}.
Interaction partners:
- Small ribosomal subunit protein eS1
- 60S acidic ribosomal protein P0
- Large ribosomal subunit protein eL15
- Large ribosomal subunit protein eL19
- Small ribosomal subunit protein eS10
- Large ribosomal subunit protein uL22
- Small ribosomal subunit protein eS26
- Large ribosomal subunit protein uL5
- Large ribosomal subunit protein eL27
- Large ribosomal subunit protein uL4
Sequence:
MARRPARCYRYCKNKPYPKSRYNRAVPDAKIRIYDLGRKKATVDEFPLCIHLVSNELEQLSSEALEAARICANKYITKVSGRDSFHLRVRVHPFHVLRINKMLSCAGADRLQQGMRGAWGKPHGLAARVSIGQIIMSARTKDSNKDVVIEGLRRARYKFPGQQKIIISKKWGFTPLNRDEYIAKKTNGEVIDDGAYVKFLSRKGNLEANLQQFPNYQYSA
Protein: DNA primase large subunit (DNA primase 2) (O74761)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Regulatory subunit of the DNA primase complex and component of the DNA polymerase alpha complex (also known as the alpha DNA polymerase-primase complex - primosome/replisome) which play an essential role in the initiation of DNA synthesis (By similarity). During the S phase of the cell cycle, the DNA polymerase alpha complex (composed of a catalytic subunit pol1, an accessory subunit spb70/pol12 and two primase subunits, the catalytic subunit spp1/pri1 and the regulatory subunit spp2/pri2) is recruited to DNA at the replicative forks (By similarity). The primase subunit of the polymerase alpha complex initiates DNA synthesis by oligomerising short RNA primers on both leading and lagging strands (By similarity).
Subcellular location: Nucleus {ECO:0000269|PubMed:10759889}. Chromosome {ECO:0000269|PubMed:15314153}. Note=Present on chromatin fraction at 40 min after release from G2 arrest and from G1 to S phase. {ECO:0000269|PubMed:15314153}.
Interaction partners:
- DNA primase small subunit
- DNA polymerase alpha catalytic subunit
- DNA polymerase alpha subunit B
- DNA polymerase epsilon catalytic subunit A
- DNA polymerase delta catalytic subunit
- DNA polymerase epsilon subunit B
- Cell division control protein 45 homolog
- Uncharacterized RNA-binding protein C126.11c
- DNA replication licensing factor mcm2
- DNA polymerase zeta catalytic subunit
Sequence:
MFRTTKSRVVEKNQNFSSASFESLSYPTRLNFYKKPPVSEISIEEFETWAIDRLVVLGEIESAMLRNKTKNELNGIIKKILDKRLPMSSNMARTVKGNSLDEERRKDHYSHFILRLAFSRSDELRIRFLRAESTLFRFRFVNEETRERQAFIDSLDFQWESVSQEEKDVFYEKLQASSQRNIENESFFKVPFFKVPDLVERRAVFVHKGYAYVPFSEQVSLVVEEFEENLKKALESTAKSLPRLDEDDRLLPILNHLSKGFVAPESSIVAPKSGAITAGQVDSFVSHFPLCAKHLHEVLKRDKHLRHFGRLQYGLFLKDIGLSVDEALVFWRKSFTNVTEDKFNKEYRYNIRHTYGLEGNRKNYKGYNCQQILTGPQLGPGDAHGCPYRTYSVNNLVSALASMGIAPDSAGCREVVEAVKARHYHIACTRVFELTHPNVGSLEESIHHPLQYFQLSLES
Protein: F-box protein PP2-B7 (Protein PHLOEM PROTEIN 2-LIKE B7) (AtPP2-B7) (Q9ZVQ9)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
Sequence:
MTKTRCMHVHFRKILQRVKKTLRLSASDQQSQGVTEPLSLGDLPEECISLIISFTSPRDACVFALVSKTFESAVQSDIVWEKFIPPEYESLLSRSQHFSSKKELFFALCDESVLINVSKKDLWIEKATGKRCMMLSASALNLSTHHTWKWITNPVSAWLETVPELLTTRWFEIRCRTNTRFLSPRTRYSVYIVFLKADICYGFAYVAMEAVVRMVGHELSESCRRYVCFHEAMEWQFLTRKNLVNPERREDGWMEIEIGEFFNEGAFRNNDEIEMSVSETTQRNTKRGLIIQGIEIRPTKKPGNEMP
Protein: L-Ala-D/L-Glu epimerase (AE epimerase) (AEE) (EC 5.1.1.20) (Q9WXM1)
Organism: Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8)
Function: Catalyzes the epimerization of L-Ala-D-Glu to L-Ala-L-Glu and has probably a role in the metabolism of the murein peptide, of which L-Ala-D-Glu is a component. Is also able to catalyze the reverse reaction and the epimerization of a broad range of other dipeptides; is most efficient with L-Ala-D/L-Phe, L-Ala-D/L-Tyr, and L-Ala-D/L-His.
Interaction partners:
- Hypothetical protein
- DNA helicase, putative
Sequence:
MSRIVNVKLSLKRYEYEKPFHITGSVSSESRNVEVEIVLESGVKGYGEASPSFRVNGERVEALLAIENAVREMITGIDVRNYARIFEITDRLFGFPSLKAAVQFATLDALSQELGTQVCYLLGGKRDEIETDKTVGIDTVENRVKEAKKIFEEGFRVIKIKVGENLKEDIEAVEEIAKVTRGAKYIVDANMGYTQKEAVEFARAVYQKGIDIAVYEQPVRREDIEGLKFVRFHSPFPVAADESARTKFDVMRLVKEEAVDYVNIKLMKSGISDALAIVEIAESSGLKLMIGCMGESSLGINQSVHFALGTGAFEFHDLDSHLMLKEEVFRGKFIQDGPRMRVKDQ
Protein: Mediator of RNA polymerase II transcription subunit 27 (Cofactor required for Sp1 transcriptional activation subunit 8) (CRSP complex subunit 8) (Mediator complex subunit 27) (P37 TRAP/SMCC/PC2 subunit) (Transcriptional coactivator CRSP34) (Q6P2C8)
Organism: Homo sapiens (Human)
Function: Component of the Mediator complex, a coactivator involved in the regulated transcription of nearly all RNA polymerase II-dependent genes. Mediator functions as a bridge to convey information from gene-specific regulatory proteins to the basal RNA polymerase II transcription machinery. Mediator is recruited to promoters by direct interactions with regulatory proteins and serves as a scaffold for the assembly of a functional preinitiation complex with RNA polymerase II and the general transcription factors.
Subcellular location: Nucleus {ECO:0000269|PubMed:10882111, ECO:0000269|PubMed:9989412}.
Interaction partners:
- Mediator of RNA polymerase II transcription subunit 12
- Mediator of RNA polymerase II transcription subunit 30
- Mediator of RNA polymerase II transcription subunit 19
- Mediator of RNA polymerase II transcription subunit 11
- Mediator of RNA polymerase II transcription subunit 1
- Mediator of RNA polymerase II transcription subunit 15
- Mediator of RNA polymerase II transcription subunit 14
- Mediator of RNA polymerase II transcription subunit 24
- Mediator of RNA polymerase II transcription subunit 10
- Mediator of RNA polymerase II transcription subunit 20
Sequence:
MADVINVSVNLEAFSQAISAIQALRSSVSRVFDCLKDGMRNKETLEGREKAFIAHFQDNLHSVNRDLNELERLSNLVGKPSENHPLHNSGLLSLDPVQDKTPLYSQLLQAYKWSNKLQYHAGLASGLLNQQSLKRSANQMGVSAKRRPKAQPTTLVLPPQYVDDVISRIDRMFPEMSIHLSRPNGTSAMLLVTLGKVLKVIVVMRSLFIDRTIVKGYNENVYTEDGKLDIWSKSNYQVFQKVTDHATTALLHYQLPQMPDVVVRSFMTWLRSYIKLFQAPCQRCGKFLQDGLPPTWRDFRTLEAFHDTCRQ
Protein: dCTP deaminase (EC 3.5.4.13) (Deoxycytidine triphosphate deaminase) (P28248)
Organism: Escherichia coli (strain K12)
Function: Catalyzes the deamination of dCTP to dUTP.
Interaction partners:
- Deoxyuridine 5'-triphosphate nucleotidohydrolase
- Thymidylate synthase
- Nucleoside diphosphate kinase
- Nucleoside triphosphate pyrophosphohydrolase
- CTP synthase
- Uridine kinase
- Anaerobic ribonucleoside-triphosphate reductase
- tRNA-dihydrouridine
- Ribonucleoside-diphosphate reductase 1 subunit alpha
- Protein AsmA
Sequence:
MRLCDRDIEAWLDEGRLSINPRPPVERINGATVDVRLGNKFRTFRGHTAAFIDLSGPKDEVSAALDRVMSDEIVLDEGEAFYLHPGELALAVTLESVTLPADLVGWLDGRSSLARLGLMVHVTAHRIDPGWSGCIVLEFYNSGKLPLALRPGMLIGALSFEPLSGPAVRPYNRREDAKYRNQQGAVASRIDKD
Protein: Matrix Gla protein (MGP) (P08494)
Organism: Rattus norvegicus (Rat)
Function: Associates with the organic matrix of bone and cartilage. Thought to act as an inhibitor of bone formation.
Subcellular location: Secreted.
Interaction partners:
- Alpha-2-HS-glycoprotein
- Bone morphogenetic protein 2
- Vitamin K-dependent gamma-carboxylase
- Osteopontin
- Osteocalcin
- Vitamin K-dependent protein S
- Prothrombin
- Unique cartilage matrix-associated protein
- Bone morphogenetic protein 4
- SPARC
Sequence:
MKSLLPLAILAALAVAALCYESHESMESYEVSPFTTRRNANTFISPQQRWHAKAQERVRELNKPAQEINREACDDYKLCERYALIYGYNAAYNRYFRQRRGAK
Protein: Purple acid phosphatase (EC 3.1.3.2) (Zinc(II) purple acid phosphatase) (Q09131)
Organism: Glycine max (Soybean) (Glycine hispida)
Subcellular location: Secreted {ECO:0000269|PubMed:16668896}.
Interaction partners:
- Uncharacterized protein
- Uncharacterized protein
- carotenoid 9,10-dioxygenase
- Serine/threonine-protein phosphatase
- Small ribosomal subunit protein RACK1
Sequence:
MGVVEGLLALALVLSACVMCNGGSSSPFIRKVEKTVDMPLDSDVFAVPPGYNAPQQVHITQGDLVGKAVIVSWVTVDEPGSSEVHYWSENSDKKKIAEGKLVTYRFFNYSSGFIHHTTIRNLEYKTKYYYEVGLGNTTRQFWFVTPPEIGPDVPYTFGLIGDLGQSFDSNKTLSHYELNPRKGQTVLFVGDLSYADNYPNHDNIRWDSWGRFTERSVAYQPWIWTAGNHENHFAPEIGETVPFKPYTHRYHVPYKASQSTSPFWYSIKRASAHIIVLASYSAYGKYTPQYKWLEKELPKVNRTETPWLIVLMHSPWYNSYNYHYMEGETMRVMYEPWFVQYKVDVVFAGHVHAYERSERVSNVAYNIVNGLCAPVNDKSAPVYITIGDGGTLEGLATNMTEPQPKYSAFREASFGHAIFDITNRTHAHYSWHRNQDGVAVEADSLWSFNRYWHPVDDSTAHVSH
Protein: Glucosidase II subunit alpha (Q5A4X3)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Subcellular location: Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00004240}.
Interaction partners:
- Uncharacterized protein
- Mannosyl-oligosaccharide glucosidase
- alpha-1,2-Mannosidase
- Calnexin
- Kre5p
- Beta-mannosyltransferase 4
Sequence:
MKLFLTIIFIIASVNAVKEYLFKSCSQSGFCNRNRHYATEVSNCENFQSPYSIDSIKVDNDTITGVVFKHLPQLDHPIQFPFEISILEGNFRFKLTEKENLVAKNVNPVRYNETEKWAFKQGVTKSSDFDVSLRDNEARVIYGDHEVLIQYHPIMFVFKYAGKEQLRINDKQFLNIEHRRTRDENDNNMLPQESDFNMFSDSFQDSKFDTLPLGPESIGLDFTLLGFSNLYGIPEHADSLLLRDTSSGEPYRLYNVDIFEYEPNSRLPMYGSIPLVVAAKPDVSIGIFWLNSADTYVDIHKSKSSTVHWMSENGILDFIVIIEKSPAMVNSQYGKVTGNTQLPPLFSLGYHQCRWNYNDEKDVLDVHAKFDEYEIPYDTIWLDIEYTDEKKYFTWHKENFATPEKMLRELDRTGRNLVAIIDPHIKTGYDVSDEIIKKGLTMKDSNNNTYYGHCWPGESVWIDTLNPNSQSFWDKKHKQFMTPAPNIHLWNDMNEPSVFNGPETSAPKDNLHFGQWEHRSIHNVFGLSYHETTFNSLLNRSPEKRPFILTRSYFAGSQRTAAMWTGDNMSKWEYLKISIPMVLTSNVVGMPFAGADVGGFFGNPSSELLTRWYQAGIWYPFFRAHAHIDSRRREPWLAGEPYTQYIRDAIRLRYALLPLFYTSFYEASKTGTPVIKPVFYENTHNADSYAIDDEFFIGNSGLLVKPVTDEGAKEIEFYLPDDKVYYDFTNGVLQGVYKGGKKPVQLSDIPMLLKGGSIIPMKTRYRRSSKLMKSDPYTLVIALDEEGSASGKLYVDDGETFAQGTEVAFTVDNNIINAKKIGPTASIPIEKIIIASKDQTTTLNNPKLDINSDWSLPFSFDSHRKIEHDEL
Protein: Fructose-1,6-bisphosphatase 2 class 2 (FBPase 2 class 2) (EC 3.1.3.11) (D-fructose-1,6-bisphosphate 1-phosphohydrolase 2 class 2) (P21437)
Organism: Escherichia coli (strain K12)
Function: Catalyzes the hydrolysis of fructose 1,6-bisphosphate to fructose 6-phosphate. Also displays a low activity toward glucose 1,6-bisphosphate, and no activity against ribulose 1,5-bisphosphate, fructose 2,6-bisphosphate, or fructose 1-phosphate.
Interaction partners:
- Transketolase 1
- Fructose-1,6-bisphosphatase class 1
- Transketolase 2
- Fructose-bisphosphate aldolase class 2
- Transaldolase A
- Fructose-bisphosphate aldolase class 1
- Transaldolase B
- ATP-dependent 6-phosphofructokinase isozyme 1
- Glucose-6-phosphate isomerase
- 1-phosphofructokinase
Sequence:
MMSLAWPLFRVTEQAALAAWPQTGCGDKNKIDGLAVTAMRQALNDVAFRGRVVIGEGEIDHAPMLWIGEEVGKGDGPEVDIAVDPIEGTRMVAMGQSNALAVMAFAPRDSLLHAPDMYMKKLVVNRLAAGAIDLSLPLTDNLRNVAKALGKPLDKLRMVTLDKPRLSAAIEEATQLGVKVFALPDGDVAASVLTCWQDNPYDVMYTIGGAPEGVISACAVKALGGDMQAELIDFCQAKGDYTENRQIAEQERKRCKAMGVDVNRVYSLDELVRGNDILFSATGVTGGELVNGIQQTANGVRTQTLLIGGADQTCNIIDSLH
Protein: Mas-related G-protein coupled receptor member G (Q7TN39)
Organism: Rattus norvegicus (Rat)
Function: Orphan receptor. May regulate nociceptor function and/or development, including the sensation or modulation of pain.
Subcellular location: Cell membrane; Multi-pass membrane protein.
Interaction partners:
Sequence:
MLSIFNIWGTFNRVLFFLSLTVSLAGLAGNTLLLWHLGLRIKKGPFNTYLLHLAAADFLFLSCQVGFSIAKIASGYEDTLYFPVTFLWFAVGLWLLAAFIVDCCLSYMFPSFCGPNCRPRYTSFVLCLVIWALTMLAVLLPANACGLLYNRMSLLVCLKYHWVSVVWLGVLASTACGASMFLLVFGNCCSSQPPSKFCKLAQCSGILLFFCRLPLVFYWCLRPVIKFLLPFFFPLATLLACIDSSAKPLLYYLKGRQLRKEPLQVALNRALGEESQSSSGGISLPMSRV
Protein: Gamma-glutamylputrescine oxidoreductase (Gamma-Glu-Put oxidase) (Gamma-glutamylputrescine oxidase) (EC 1.4.3.-) (P37906)
Organism: Escherichia coli (strain K12)
Function: Involved in the breakdown of putrescine via the oxidation of L-glutamylputrescine.
Interaction partners:
- Gamma-glutamylputrescine synthetase PuuA
- NADP/NAD-dependent aldehyde dehydrogenase PuuC
- 4-aminobutyrate aminotransferase PuuE
- Gamma-glutamyl-gamma-aminobutyrate hydrolase PuuD
- HTH-type transcriptional regulator PuuR
- Putrescine importer PuuP
- 4-aminobutyrate aminotransferase GabT
- Agmatinase
Sequence:
MTEHTSSYYAASANKYAPFDTLNESITCDVCVVGGGYTGLSSALHLAEAGFDVVVLEASRIGFGASGRNGGQLVNSYSRDIDVIEKSYGMDTARMLGSMMFEGGEIIRERIKRYQIDCDYRPGGLFVAMNDKQLATLEEQKENWERYGNKQLELLDANAIRREVASDRYTGALLDHSGGHIHPLNLAIGEADAIRLNGGRVYELSAVTQIQHTTPAVVRTAKGQVTAKYVIVAGNAYLGDKVEPELAKRSMPCGTQVITTERLSEDLARSLIPKNYCVEDCNYLLDYYRLTADNRLLYGGGVVYGARDPDDVERLVVPKLLKTFPQLKGVKIDYRWTGNFLLTLSRMPQFGRLDTNIYYMQGYSGHGVTCTHLAGRLIAELLRGDAERFDAFANLPHYPFPGGRTLRVPFTAMGAAYYSLRDRLGV
Protein: Chimerin 2 (Q965N4)
Organism: Caenorhabditis elegans
Interaction partners:
- Cell division control protein 42 homolog
- Protein kinase C-like 3
- Rho-GAP domain-containing protein
- Ras-like GTP-binding protein rhoA
Sequence:
MEDDGPPGSSGASKGYWKQNLYLLQEKAPKPNAVLCRKPLQQRPRHFGAEFHGLIDRNEAEKMLLEAGEGSYLVRESNRSRDACTLCMIFDAKVMNYKLYYDGQFYVGEKRFDTMDLLVADGLISMFVDLHAADYIKRMADEAIYEDSPYSRYTNAAATTSDIVRRPVTRAHNFTSYTFKAPHYCDYCRNFLWGLVHQGMRCEDCGFAAHKKCSEKTLHDCVPDSKYVKRMFGVDITTLCMAHGADLPPIVPLCIGEVESRGLDVEGIYRVSGSYDHMEKLKQQFDSNQYVDLATVCDIHTVCGLLKLYFRLLPQQLIPFSVHKQLLVAYQETNQRSTHERERQIRKVMMELSDANIITLGAVLAHLKKVADHSAKNKMTVENLATIFSPTLFCSGSIPAMPNHQLLHFLINNPRVVPKHH
Protein: Moonshiner (Q9VYQ0)
Organism: Drosophila melanogaster (Fruit fly)
Function: Part of a rhi-dependent transcription machinery that enables the generation of piRNA precursors from heterochromatin while maintaining the suppression of transposon-encoded promoters and enhancers. Moonshiner/CG12721 recruits transcriptional machinery to heterochromatin to initiate the bidirectional transcription of piRNA clusters. Functions by forming a complex with transcription initiation factors TfIIA-S and Trf2, and interacting with del which is part of the RDC (rhi, del and cuff) complex that binds to repressive H3K9me3 marks in the chromatin. This mechanism allows transcription to occur in piRNA clusters despite the lack of proper promoter elements and in the presence of the repressive H3K9me3 mark.
Subcellular location: Nucleus {ECO:0000269|PubMed:28847004}. Note=Expressed in nuclear foci. {ECO:0000269|PubMed:28847004}.
Interaction partners:
- Transcription initiation factor IIA subunit 1
- Chromo domain-containing protein rhino
- Protein deadlock
- Transcription initiation factor IIA subunit 2
- TATA box-binding protein-like 1
- Bootlegger
- Transcription initiation factor IIA subunit 2-2
Sequence:
MAKILPTDGIWIPESCSFPEDVMIDMMEGLFRDVPNLTHKEYLALADLQSRWMAKLANRQPESNPLPPKPKKRKKIAPKKQDQPVEEKGSEVDIYDVDDNEMVNNRIYIPRLRSAWRARYFNIMMRAFVIKRGLLNKHINWQILDKIMAAPDAEGQAELQAFVDKVVAGQEM
Protein: LD37574p (Ypsilon schachtel, isoform A) (Q95RE4)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- ATP-dependent RNA helicase me31b
- Trailer hitch, isoform H
- Eukaryotic translation initiation factor 4E1
- FI20148p1
- Protein cup
- Polyadenylate-binding protein
- Purine-rich binding protein-alpha, isoform B
- Maternal protein exuperantia
- Fragile X messenger ribonucleoprotein 1 homolog
- Protein CASC3
Sequence:
MADAAESKPLAAEQQQAQQQPEQQQNPPNPQEQDHEQEPLDELQGQQGQPAPPTKEVIATKVTGTVKWFNVKSGYGFINRNDTREDVFVHQSAIARNNPKKAVRSVGDGEVVEFDVVIGEKGNEAANVTGPSGEPVRGSQFAADKRRNFRPWMKKNRRKDGEVEGEDAESSAQQQQQQAAPIVDGQPQQQVQSGPRQPRQNFRRGPPGGPPGGPRGGPRGPPGGAPGGPRRYNNYYLRQPRRGLGGGDGSAEPGVHDQNPEGLQRGEGQGPRRGGGPPGGPQRRFFRRNFNNGPPPPRRDGGEYIQGQGPPRPQQPRPRRQRKPNGPGGGSEQQPEKNGAQELQNTTTESTA
Protein: Radical S-adenosyl methionine domain-containing protein 1, mitochondrial (Putative heme chaperone) (Q9HA92)
Organism: Homo sapiens (Human)
Function: May be a heme chaperone, appears to bind heme. Homologous bacterial proteins do not have oxygen-independent coproporphyrinogen-III oxidase activity (Probable). Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine (By similarity).
Subcellular location: Mitochondrion {ECO:0000305}.
Interaction partners:
- Ubiquitin-like protein FUBI
- Large ribosomal subunit protein uL23
- Small ribosomal subunit protein uS13
- Large ribosomal subunit protein uL29
- Large ribosomal subunit protein uL14
- Large ribosomal subunit protein uL5
- Large ribosomal subunit protein eL14
- Small ribosomal subunit protein uS17
- Small ribosomal subunit protein uS19
- Small ribosomal subunit protein eS24
Sequence:
MALPGARARGWAAAARAAQRRRRVENAGGSPSPEPAGRRAALYVHWPYCEKRCSYCNFNKYIPRRLEEAAMQKCLVTEAQTLLRLSGVQRVESVFFGGGTPSLASPHTVAAVLEAVAQAAHLPADLEVTLEANPTSAPGSRLAEFGAAGVNRLSIGLQSLDDTELRLLGRTHSACDALRTLAEARRLFPGRVSVDLMLGLPAQQVGPWLGQLQELLHHCDDHLSLYQLSLERGTALFAQVQRGALPAPDPELAAEMYQRGRAVLREAGFHQYEVSNFARNGALSTHNWTYWQCGQYLGVGPGAHGRFMPQGAGGHTREARIQTLEPDNWMKEVMLFGHGTRKRVPLGRLELLEEVLALGLRTDVGITHQHWQQFEPQLTLWDVFGANKEVQELLERGLLQLDHRGLRCSWEGLAVLDSLLLTLLPQLQEAWQQRTPSPVPGG
Protein: Large ribosomal subunit protein mL37 (39S ribosomal protein L37, mitochondrial) (Q9VGW9)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Mitochondrion {ECO:0000256|ARBA:ARBA00004173}.
Interaction partners:
Sequence:
MRLTNTLCAQHIGWHFKKHWLVQGRRVPKETGAAAELLKLGVLVKNPEDLLNAKVEKKLVDIVGAREKPVPEDSRHPDWHPTVCNTYSDNSVLIGGLPQAQVLTNSIVIQTFPKHIEDAIASQQLPNSVDKSVRHAILASHVLDAEQVKLPKVRLPERPAFNLPRSYGISHERVNRLLVNKLLHESEKLAGRSVSVRRKLIDNASFKTFLSKDGDLLGFSINAEKVVFANRAIEGVKGKFEGDLPDLYPMKSTISIPKYHIYQAKNLYPLRSDITCSHPHTIFTVFNKHQVKNSHGSEVTTSQLQARTLVKAFVVAAARAKQLHGDSVGALPKPIVVQSVQTDGRTFHFGVLQLNTLDLGANSTAKNYWFHRQNYNLFAECSYEGGRTHLDNYNGEVFRIFNAFYNNS
Protein: Alpha-1-syntrophin (59 kDa dystrophin-associated protein A1 acidic component 1) (59-1 DAP) (Syntrophin-1) (Q28626)
Organism: Oryctolagus cuniculus (Rabbit)
Function: Adapter protein that binds to and probably organizes the subcellular localization of a variety of membrane proteins. May link various receptors to the actin cytoskeleton and the extracellular matrix via dystrophin glycoprotein complex. Plays an important role in synapse formation and in the organization of UTRN and acetylcholine receptors at the neuromuscular synapse. Binds to phosphatidylinositol 4,5-bisphosphate (By similarity).
Subcellular location: Cell membrane, sarcolemma {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Cell junction {ECO:0000250}. Cytoplasm, cytoskeleton {ECO:0000250}. Note=In skeletal muscle, it localizes at the cytoplasmic side of the sarcolemmal membrane and at neuromuscular junctions. {ECO:0000250}.
Interaction partners:
- Dystrophin
- Dystroglycan 1
- Caveolin
- Utrophin
- Dystrobrevin
- Alpha-sarcoglycan
- Sarcospan
- Sodium channel protein
- FERM and PDZ domain containing 2
- ZZ-type domain-containing protein
Sequence:
MASGRRAPRTGLLELRAGTGAGAGGERWQRVLVSLAEDALTVSPADGEPGPEPGAVREPEPAQINGAAEPGAAPPQLPEALLLQRRRVTVRKADAGGLGISIKGGRENKMPILISKIFKGLAADQTEALFVGDAILSVNGEDLSSATHDEAVQALKKTGKEVVLEVKYMKEVSPYFKNSAGGTSVGWDSPPASPLQRQPSSPGPQTRNLSEAKHVPLKMAYVSRRCTPSDPEHRYLEICSADGQDTIFLRAKDEASARSWAGAIQAQINALLPWVKDELQALLAASSPAGSQDIKQIGWLTEQLPSGGTAPTLALLTEKELLLYGGLPQTREALSRPARTAPLIATRLVHSGPSKGSVPYDAELSFALRTGTRHGVDTHLFSVESPQELAAWTRQLVDGCHRAAEGVQEVSTACTWNGRPCNLSVHIDKGFTLWAAEPGAARAVLLRQPFEKLQMSSDDGASLLFLDFGGAEGEIQLDLHSCPKTMVFIIHSFLSAKVTRLGLLA