wanglab/gogpt-training-data huggingface dataset:
Protein: 3-hydroxy-5-methyl-1-naphthoate 3-O-methyltransferase (EC 2.1.1.302) (Azinomycin biosynthesis protein B2) (B4XY98)
Organism: Streptomyces sahachiroi
Function: O-methyltransferase that mediates the formation of 3-methoxy-5-methyl-1-naphthoate from 3-hydroxy-5-methyl-1-naphthoate in the biosynthesis of the antitumor antibiotic azinomycin B.
Interaction partners:
Sequence:
MAAGSGSGTPPGTPPPTLLTDLATGLWKTQTLTAAIETGLFEALAAGDADAPETAQRLGIGKRPAEILLTACTALGLLEQRDGRYRNTAVAAHYLVPGLPDYFGGYVQMVARYTAPGWLRATEAVRTDAPTKPVPDPDRNMFEEGNRPESFWEGLFTFSTLTARQLAASVDLSGVRRIMDVGGGAGATLIELCRQHPHLSGTVVDLPHVCALAGERIAAAGMTGRIDTAAADFFADPLPSGHDAVLLSMILHDWDESQNRKILASCLDALPSGGTVLISELLVDDDKSGPVDAALMSMNMLVGTWGRNYTGAEYTDWLRDAGCSEVRTVRFASPGANGVVAGVKA
Protein: Dro3 protein (Q2UYI2)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Secreted {ECO:0000256|ARBA:ARBA00004613}.
Interaction partners:
Sequence:
MVQMKFLFAILAVMTIVLMEANTVSARDCLSGTFGGPCWAWSGEKCRRLCIEEGRVSGHCSGGMKCWCEGC
Protein: Maltodextrin glucosidase (EC 3.2.1.20) (Alpha-glucosidase) (P21517)
Organism: Escherichia coli (strain K12)
Function: May play a role in regulating the intracellular level of maltotriose. Cleaves glucose from the reducing end of maltotriose and longer maltodextrins with a chain length of up to 7 glucose units.
Subcellular location: Cytoplasm.
Interaction partners:
- 4-alpha-glucanotransferase
- Cytoplasmic alpha-amylase
- Periplasmic alpha-amylase
- Periplasmic beta-glucosidase
- Alpha-galactosidase
- Maltodextrin phosphorylase
- 6-phospho-beta-glucosidase BglB
- 6-phospho-beta-glucosidase BglA
- 6-phospho-beta-glucosidase AscB
- 6-phospho-beta-glucosidase
Sequence:
MLNAWHLPVPPFVKQSKDQLLITLWLTGEDPPQRIMLRTEHDNEEMSVPMHKQRSQPQPGVTAWRAAIDLSSGQPRRRYSFKLLWHDRQRWFTPQGFSRMPPARLEQFAVDVPDIGPQWAADQIFYQIFPDRFARSLPREAEQDHVYYHHAAGQEIILRDWDEPVTAQAGGSTFYGGDLDGISEKLPYLKKLGVTALYLNPVFKAPSVHKYDTEDYRHVDPQFGGDGALLRLRHNTQQLGMRLVLDGVFNHSGDSHAWFDRHNRGTGGACHNPESPWRDWYSFSDDGTALDWLGYASLPKLDYQSESLVNEIYRGEDSIVRHWLKAPWNMDGWRLDVVHMLGEAGGARNNMQHVAGITEAAKETQPEAYIVGEHFGDARQWLQADVEDAAMNYRGFTFPLWGFLANTDISYDPQQIDAQTCMAWMDNYRAGLSHQQQLRMFNQLDSHDTARFKTLLGRDIARLPLAVVWLFTWPGVPCIYYGDEVGLDGKNDPFCRKPFPWQVEKQDTALFALYQRMIALRKKSQALRHGGCQVLYAEDNVVVFVRVLNQQRVLVAINRGEACEVVLPASPFLNAVQWQCKEGHGQLTDGILALPAISATVWMN
Protein: Uncharacterized protein ycf76 (ORF85) (P0C471)
Organism: Oryza sativa (Rice)
Subcellular location: Plastid, chloroplast.
Interaction partners:
Sequence:
MKKILFSMFYSILVGEEPDSVFLKKEGKQNQVKMIWVAPSSCAKDLTISEGTGATFLFNFHSRVSYLFPRPFLRPRNMKWTNSFS
Protein: (S)-8-amino-7-oxononanoate synthase BioU (EC 2.6.1.121) (8-amino-7-oxononanoate carboxylating dehydrogenase) (I3R9K3)
Organism: Haloferax mediterranei (strain ATCC 33500 / DSM 1411 / JCM 8866 / NBRC 14739 / NCIMB 2177 / R-4) (Halobacterium mediterranei)
Function: A 'suicide' enzyme that participates in biotin synthesis. Catalyzes the formation of (S)-8-amino-7-oxononanoate (DAN-carbamic acid) from (7R,8S)-8-amino-7-(carboxyamino)nonanoate (DAN), a function equivalent to the cannonical BioA reaction and the first half-reaction of BioD. The cellular requirement for biotin is thought be low enough that this single turnover enzyme supplies a sufficient amount of the cofactor. Overall it catalyzes three reactions: formation of a covalent linkage with 8-amino-7-oxononanoate to yield a BioU-DAN conjugate at the epsilon-amino group of Lys124 of BioU using NAD(P)H, carboxylation of the conjugate to form BioU-DAN-carbamic acid, and release of DAN-carbamic acid using NAD(P)+ (By similarity). Complements a bioA deletion in E.coli.
Interaction partners:
Sequence:
MDEINFAVLGTGGIGRRTLEVSTYKDGLTPVAACDRHGVAVNHDGLDVEEILDATEGNIAGDGTGDTEDKRVTDGGAAVKQHGDGAGIVASAQGTSTETPIDEIIAESDEIDAVLLALPNLEHDFIPRIAERFAEAEFEGVLIDVLKRSRVIGMLDDREETLVESGITFVCGAGATPGLLTGAAALAAQSFVEVEEVEIWWGVGLKSGYEDNRGTVREDIAHLDGYDIETAREMDESEIEAVIEEHDGVLEFNDMEHADDVLLERAGICDAEDVTVGGILDIRKDEKPTTTTVRVTGRTFDGKRGTNTFQLDDATSMAANVNGPALGYLKSAVRRNRAGDYGVFGPAELMPGF
Protein: Endothelin-2 (ET-2) (Preproendothelin-2) (PPET2) (Vasoactive intestinal contractor) (VIC) (P23943)
Organism: Rattus norvegicus (Rat)
Function: Vasoconstrictor.
Subcellular location: Secreted.
Interaction partners:
- Endothelin-1 receptor
- Endothelin receptor type B
- Endothelin-1
- Endothelin-3
- Oxytocin receptor
- Endothelin-converting enzyme 1
- Beta-2 adrenergic receptor
Sequence:
MVSPAWCSIALALLLALHEGKGQAAATMEQPASAPKGRGPHLRFRRCSCNSWLDKECVYFCHLDIIWVNTAGQTAPYGLGNPPQRRRRSLPKRCECSSAGDSACATFCHRRPWPEAEVTSSSQGPAAVLETSKTWTAAGDLLQKLRDISAAKLQFVRLRPELTREAIPAHSRRRKR
Protein: Lipoxygenase 7, chloroplastic (EC 1.13.11.12) (P38419)
Organism: Oryza sativa subsp. japonica (Rice)
Function: Plant lipoxygenase may be involved in a number of diverse aspects of plant physiology including growth and development, pest resistance, and senescence or responses to wounding. This lipoxygenase introduces molecular oxygen exclusively into the C-13 position of linoleic and linolenic acids.
Subcellular location: Plastid, chloroplast {ECO:0000305}.
Interaction partners:
- hydroperoxide dehydratase
- Allene oxide synthase 1, chloroplastic
- Alpha-dioxygenase PIOX
- Allene oxide synthase 2
- Lipoxygenase
- Lipase family protein
- Os04g0589400 protein
- Allene oxide synthase 4
- Os09g0544500 protein
- ARID transcription factor
Sequence:
MLRPQLNPSSHTTTTSSSSSTQLFASSSCIASLRRPSSSSSSVVAAARRTRGQGSSRVVVVCASSSATASRGDSSSDMAAAAAVRVKAVATIKVTVGELINRSIDIRDLIGRSLSLELVSSELDAKTGKEKATVRSYAHNVDDDDHSVVTYEADFDVPSGFGPIGAIIVTNELRQEMFLEDINLTASDGAGNSTVLPIRCNSWVQPKSVGDEGTPSKRIFFANKTYLPGQTPAGLRSYRKNDLQQKRGDGTGEREADDRVYDYDVYNDLGNPDSNGDLARPVLGGNKQFPYPRRCRTGRPPSKKDPKSETRKGNVYVPRDEEFSPEKEDYFLRKTVGSVLQAAVPAAQSLLLDKLKWNLPFPSFFVIDKLFEDGVELPGVDKLNFLESVVPRLLEHLRDTPAEKILRFETPANIQKDKFAWLRDEEFARETLAGINPYAIELVREFPLKSKLDPAVYGPAESAITADLLEEQMRRVMTVEEAISQKRLFMLDFHDLFLPYVHKIRSLDHTTMYGSRTVFFLTDDGTLQLLAIELTRPASPSQPQWRQVFTPSTDATMSWLWRMAKAHVRAHDAGHHELITHWLRTHCAVEPYIIAANRQLSEMHPIYQLLRPHFRYTMRINARARSALISAGGIIERSFSPQKYSMELSSVAYDKLWRFDTEALPADLVRRGMAEEDPTAEHGLKLAIEDYPFANDGLLIWDAIKTWVQAYVARFYPDADSVAGDEELQAFWTEVRTKGHGDKKDAPWWPKLDSPESLAHTLTTIVWVAAAHHAAVNFGQYDFGGYFPNRPSIARTVMPVEEPVDGAAMERFLDNPDQALRECFPSQVQATVVMAVLDVLSSHSTDEEYLGGEQTRPWNSDAAVQAAYDGFAARLKEIEGVIDGRNKDRKLKNRCGAGILPYQLMKPFSDSGVTGMGIPNSTSI
Protein: Meiotically up-regulated gene 177 protein (Q9C110)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Has a role in meiosis.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16823372}.
Interaction partners:
Sequence:
MYPKIVARCMIVITKNRESERNVLICYRNVTNVYFSLRILLNRQNEGNNCKYKLVFSLYRVSFRRMRLNDRQLSCVESVTNGIGLLCLKQADQVCLFTPTVDSHL
Protein: Katanin_con80 domain-containing protein (Q9XTS3)
Organism: Caenorhabditis elegans
Interaction partners:
- Meiotic spindle formation protein mei-1
- Meiotic spindle formation protein 2
- WD_REPEATS_REGION domain-containing protein
- Protein KATNIP homolog
- Anaphase-promoting complex subunit 4-like WD40 domain-containing protein
- Kinesin-like protein
Sequence:
MALTSVSVYELSRLGPPQQPVRRRSNSTKVRRKDAELGSVDRKRNPKRNQIQPQHNESITITYMGRPRSPSVDLPTSPPIPSVIRQRRSSSTVAKKLPQSASNPSFLRKQGSSSSLSNGLWTDCIEVVNEIGVMAKMESRKIRRLRMAVYRRVRISDDEEMVLTASRALSKCHGWTLDTCHDYLPVIIDNIISMDTSNRIIAAEGLAAIADSLGERLVKFAGMNSHRIGVDIAAEERSEKAKACIQLLRSVVRKRDWYYRHLDVESIDRLDATMERLKSI
Protein: Protein PAXX (Paralog of XRCC4 and XLF) (XRCC4-like small protein) (Q9BUH6)
Organism: Homo sapiens (Human)
Function: Non-essential DNA repair protein involved in DNA non-homologous end joining (NHEJ); participates in double-strand break (DSB) repair and V(D)J recombination. May act as a scaffold required for accumulation of the Ku heterodimer, composed of XRCC5/Ku80 and XRCC6/Ku70, at double-strand break sites and promote the assembly and/or stability of the NHEJ machinery. Involved in NHEJ by promoting the ligation of blunt-ended DNA ends. Together with NHEJ1/XLF, collaborates with DNA polymerase lambda (POLL) to promote joining of non-cohesive DNA ends. Constitutes a non-essential component of classical NHEJ: has a complementary but distinct function with NHEJ1/XLF in DNA repair. Able to restrict infection by herpesvirus 1 (HSV-1) via an unknown mechanism.
Subcellular location: Nucleus {ECO:0000269|PubMed:25574025, ECO:0000269|PubMed:25670504, ECO:0000269|PubMed:29144403}. Chromosome {ECO:0000269|PubMed:25574025, ECO:0000269|PubMed:25670504}. Note=Predominantly localizes to the nucleus. Accumulates at sites of DNA damage generated by laser microirradiation. {ECO:0000269|PubMed:25574025, ECO:0000269|PubMed:25670504}.; SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:29144403}. Note=(Microbial infection) Upon infection by herpesvirus 1 (HSV-1), it is partially translocated into the cytoplasm in an HSV-1-dependent manner. {ECO:0000269|PubMed:29144403}.
Interaction partners:
- Non-homologous end-joining factor 1
- DNA repair protein XRCC4
- X-ray repair cross-complementing protein 6
- X-ray repair cross-complementing protein 5
- DNA-dependent protein kinase catalytic subunit
- DNA ligase 4
- Serine-protein kinase ATM
- Protein artemis
- DNA excision repair protein ERCC-1
- DNA mismatch repair protein Msh2
Sequence:
MDPLSPPLCTLPPGPEPPRFVCYCEGEESGEGDRGGFNLYVTDAAELWSTCFTPDSLAALKARFGLSAAEDITPRFRAACEQQAVALTLQEDRASLTLSGGPSALAFDLSKVPGPEAAPRLRALTLGLAKRVWSLERRLAAAEETAVSPRKSPRPAGPQLFLPDPDPQRGGPGPGVRRRCPGESLINPGFKSKKPAGGVDFDET
Protein: Thiosulfate sulfurtransferase TUM1 (EC 2.8.1.1) (Thiouridine modification protein 1) (tRNA-thiouridine modification protein 1) (Q08686)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Required for formation of the 2-thio group of the 5-methoxycarbonylmethyl-2-thiouridine modified base in some tRNAs.
Subcellular location: Mitochondrion {ECO:0000269|PubMed:14562095}. Cytoplasm {ECO:0000269|PubMed:14562095}.
Interaction partners:
- Cysteine desulfurase, mitochondrial
- Adenylyltransferase and sulfurtransferase UBA4
- Cytoplasmic tRNA 2-thiolation protein 1
- Ubiquitin-related modifier 1
- Sulfite reductase subunit beta
- Cytoplasmic tRNA 2-thiolation protein 2
- Cystathionine gamma-lyase
- Aspartate aminotransferase, cytoplasmic
- Aspartate aminotransferase, mitochondrial
- Cystathionine beta-lyase
Sequence:
MPLFDLISPKAFVKLVASEKVHRIVPVDATWYLPSWKLDNKVDFLTKPRIPNSIFFDIDAISDKKSPYPHMFPTKKVFDDAMSNLGVQKDDILVVYDRVGNFSSPRCAWTLGVMGHPKVYLLNNFNQYREFKYPLDSSKVAAFSPYPKSHYESSESFQDKEIVDYEEMFQLVKSGELAKKFNAFDARSLGRFEGTEPEPRSDIPSGHIPGTQPLPYGSLLDPETKTYPEAGEAIHATLEKALKDFHCTLDPSKPTICSCGTGVSGVIIKTALELAGVPNVRLYDGSWTEWVLKSGPEWIAENRD
Protein: Expansin-like A3 (At-EXPL3) (AtEXLA3) (AtEXPL3) (Ath-ExpBeta-2.3) (Q9LZT5)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Secreted {ECO:0000305}.
Interaction partners:
- At5g17640)
- Arabinogalactan protein 20
Sequence:
MRSFLYLIVVIFLFSSSVNACDRCLHRSKASYFSSASALSSGACAYGPMATSFFAGHIAAAIPSIYKDGAGCGACFQVRCKNPKLCNSKGTIVMVTDLNTSNQTDLVLSSRAFRAMAKPVVGVDKYLLKQGIVDVEYQRVPCNYGKRNLNVRVEEASKKPNYLAIKLLYQGGQTEVVGIDIAPVGSSQWSYMSRSHGAVWATDKVPTGALQFKFTVTGGYDGKTVWSKRVLPANWNSGRIYDAGVQITDIAQEGCDTCGHIWN
Protein: Histone deacetylase 6 (F8W4B7)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
- Transitional endoplasmic reticulum ATPase
- ubiquitinyl hydrolase 1
- Alpha-tubulin N-acetyltransferase 1
- NAD-dependent protein deacetylase sirtuin-2
- Heat shock factor protein 1 isoform X1
- Hematopoietic cell-specific Lyn substrate 1
- Cortactin.
- Prostaglandin E synthase 3
- Heat shock protein HSP 90-alpha 1
- Nuclear receptor corepressor 2
Sequence:
MDAVPDTKGSSGPPRGTPETKNNKKNLQEARRKGRMDRSKAEEEMSNELQNLDVQGKSKATGTGLVYVDAFTRFHCLWDASHPECPARVSTVMEMLETEGLLGRCVQVEARAVTEDELLLVHTKEYVELMKSTQNMTEEELKTLAEKYDSVYLHPGFFSSACLSVGSVLQLVDKVMTSQLRNGFSINRPPGHHAQADKMNGFCMFNNLAIAARYAQKRHRVQRVLIVDWDVHHGQGIQYIFEEDPSVLYFSVHRYEDGSFWPHLKESDSSSVGSGAGQGYNINLPWNKVGMESGDYITAFQQLLLPVAYEFQPQLVLVAAGFDAVIGDPKGGMQVSPECFSILTHMLKGVAQGRLVLALEGGYNLQSTAEGVCASMRSLLGDPCPHLPSSGAPCESALKSISKTISDLYPFWKSLQTFEGGPLSEVSPLPAPVCAEVKVSSPITGLVYDQRMMLHHNMWDSHHPELPQRISRIFSRHEELRLLSRCHRIPARLATEEELALCHSSKHISIIKSSEHMKPRDLNRLGDEYNSIFISNESYTCALLAAGSCFNSAQAILTGQVRNAVAIVRPPGHHAEKDTACGFCFFNTAALTARYAQSITRESLRVLIVDWDVHHGNGTQHIFEEDDSVLYISLHRYEDGAFFPNSEDANYDKVGLGKGRGYNVNIPWNGGKMGDPEYMAAFHHLVMPIAREFAPELVLVSAGFDAARGDPLGGFQVTPEGYAHLTHQLMSLAAGRVLIILEGGYNLTSISESMSMCTSMLLGDSPPSLDHLTPLKTSATVSINNVLRAHAPFWSSLRVNIPESLRLSLPSPKPKGKCTPGGKGKKSPRQSTPSQSPGQATHRPDQSGFDELTADLLSLNLNTSTSSNTSPESVAVGGARRKVKPNTHRVSAGLESESPLKLNPEKAGAGDDTDVKAETPNRSISEPVVTCDSSAVKDQESLVLEAAGGNTVQSVLERVFGAQATDVDTMYVVDPLPWCPHLESVRPVPAGGIDVFQPCEECGGEAENWICLFCYKVLCGRYVNQHMVTHGQESGHPVVLSFADLSVWCYACESYVHNKVLHEAKNAAHLVKFGEGIHPFN
Protein: Periodic tryptophan protein 1 (P21304)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Interaction partners:
- Ribosome biogenesis protein BRX1
- rRNA-processing protein EBP2
- Nucleolar protein 12
- Proteasome-interacting protein CIC1
- Ribosome biogenesis protein RPF2
- Nucleolar complex protein 2
- Ribosome biogenesis protein ERB1
- Nucleolar GTP-binding protein 1
- Ribosome biogenesis protein 15
- rRNA biogenesis protein RRP5
Sequence:
MISATNWVPRGFSSEFPEKYVLDDEEVERINQLAQLNLDDAKATLEEAEGESGVEDDAATGSSNKLKDQLDIDDDLKEYNLEEYDDEEIADNEGGKDVSMFPGLSNDSDVKFHEGEKGEDPYISLPNQEDSQEEKQELQVYPSDNLVLAARTEDDVSYLDIYVYDDGAGFHSSDIPVEEGDEADPDVARGLVRDPALYVHHDLMLPAFPLCVEWLDYKVGSNSEEAANYAAIGTFDPQIEIWNLDCVDKAFPDMILGEPLDNSMVSLKSKKKKKKSKTGHITTHHTDAVLSMAHNKYFRSVLASTSADHTVKLWDLNSGNAARSLASIHSNKNVSSSEWHMLNGSILLTGGYDSRVALTDVRISDESQMSKYWSAMAGEEIETVTFASENIILCGTDSGNVYSFDIRNNENRKPVWTLKAHDAGISTLCSNKFIPGMMSTGAMGEKTVKLWKFPLDDATNTKGPSMVLSRDFDVGNVLTSSFAPDIEVAGTMVIGGVNKVLKLWDVFTNRSVRKSFKSELENVQARAKEEAQKIGKSSRIARKYTSNDNPDTVITIDDQGEDEEEREGGDEHDDMA
Protein: StAR-related lipid transfer protein 13 (START domain-containing protein 13) (StARD13) (Q923Q2)
Organism: Mus musculus (Mouse)
Function: May function as a GTPase-activating protein.
Subcellular location: Cytoplasm. Membrane; Peripheral membrane protein; Cytoplasmic side. Mitochondrion membrane; Peripheral membrane protein; Cytoplasmic side. Lipid droplet {ECO:0000250}.
Interaction partners:
- Tensin-2
Sequence:
MFSQVPRTPAAGCYYLNPLTPESQEMYLRFDQTARRSPYRMSRILARHHLVTKIQQEIEAKEACDWLRAAGFPQYAQLYEDSQFPINIAAVKKDHDFLERDLVEPLCRRLNTLNKCASMRLDVNFQRKKGDDSDEEDLCISNKWTFQRTSRRWSRVDDLHTLFPVADRNGSPGGPRMRNTASSESVLTDLSEPEVCSIHSESSGGSDSRSQSGHHSADSTHALEATLVSSSLPQSTREGLNQSFHPKNEKPTRTRAKSFLKRMDTLRVKGALGRHKGPGRTGGLVISRPVLQQEPESFKTMQCVQIPNGDLQTSPPAACRKGLPCSSKSSGESSPLENSSTVSTPCMKERKCHHEANKRGGMYLEDLDVLAGTALPDTSDQNHMHGFHSQENLVVHIPKDHKPGTFPKALSIESLSPTDNSNGVNWRTGSISLGRQQGPGMREPRLMSSCHRASRVSIYDNVPSSHLYASTGDLLDLEKDGLLPQLDDILQHVNGIQEVVDDWSKNILPELQSHSTLAGDPGLSPFPSPNQVTLDFEGNSVSEGRTTPSDVERDRTSLNESEATGVRERRDSGVGASLTRPNRRLRWSSFQLSHQPQPSPATPHISSQTAAQLNLLQRFSLLRLTAIMEKYSMSNKHGWTWSVPKFMKRIKAPDYRDKAVFGVPLIVHVQRTGQPLPQSIQQALRYLRSNCLDQVGLFRKSGVKSRIHALRQMNENFPDNVSYEDQSAYDVADMVKQFFRDLPEPLFTNKLSETFLHIYQYVPKEQRLQAVQAAILLLADENREALQTLLCFLHDVVNLVDENQMTPMNLAVCLAPSLFHLNLLKKESSPKVIQKKYATGKPDQKDLNENLAAAQGLAHMITECNRLFEVPHEMVAQSRDSYLEAEIHVPSLEDLGAQLAESGATFHTYLEHLVQGLQKEAKEKFKGWVTCSSPDNTDLAFKKVGDGHPLKLWKASVEVEAPPSVVLNRVLRERHLWDEDFVQWKVVERLDKQTEIYQYVLNSMVPHPSRDFLVLRTWKTDLPKGMCTLVSLSVEYEEAQLMGGVRAVVMDSQYLIEPCGSGKSRLTHICRIDLKGHSPEWYSKGFGHLCAAEVTRIRNSFQPLVAEGPETKI
Protein: Octopamine receptor beta-3R (DmOct-beta-3R) (Q4LBB6)
Organism: Drosophila melanogaster (Fruit fly)
Function: Autoreceptor for octopamine, which is a neurotransmitter, neurohormone, and neuromodulator in invertebrates (By similarity). Probably also acts as a receptor for tyramine during ecdysone biosynthesis. Required for the biosynthesis of the steroid hormone ecdysone which is necessary for metamorphosis. Involved in activation of prothoracicotropic hormone and insulin-like peptide signaling which is required for the expression of ecdysone biosynthetic genes.
Subcellular location: Cell membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
Sequence:
MSGVNVADLLATTMTLPITAAAGAATSQAAATSATNASHLQPATLTGHISTTAAAKTTTTPTSSLPITSQFVDASLTSLSLTATSSDASYSSPFSSYLSSDSTFELLSTVGPNITANGSDIAVDNQAELEESWLDLSLLLLKGFIFSSIILAAVLGNALVIISVQRNRKLRVITNYFVVSLAMADMLVALCAMTFNASVELSGGKWMFGPFMCNVYNSLDVYFSTASILHLCCISVDRYYAIVRPLEYPLNMTHKTVCFMLANVWILPALISFTPIFLGWYTTEEHLREISLHPDQCSFVVNKAYALISSSVSFWIPGIVMLVMYWRIFKEAIRQRKALSRTSSNILLNSVHMGHTQQPTSLSYLHPSDCDLNATSAREETHSALSNLEDMLQPATDEDDDRDECDELRVPSPPPRRLSRSSIDLRDLEQERYEKVTHTDSAPSMMALQQQQPSHNQLQPPAPVFNPQIWTEGKMIPSKELDKEHSHPNGPQQQLSLTSGSGNSEPEPESTAYRVFGGLNSDESEGNDLYDTHLPLAEDNKELKRLIEDNYLYFKRQTGGTIISGPGGGKYAALSETDFIRLKAGAAACGRKAFASSDSEFLRTISESRALPEQPVPGKEKGFNILSLLSKTKRSSTECFTLEKKRHQANSEGSSFFRRSRNRKLSHSYNGCGGGKERKLERRQRQHSDTDSTPNKPDILLDINVLSEQSGASVIQQFSDGVQLIDFSELKTPPERIRSDDELAQLADCFGESPQQPATPPPSLSPPELPEPSGLLIASSSELAEIFRSLSFPLGRPAGAPQRLSTLSDQVCANYLMSPPNTPAPPAISVPNGGAMDSSASSNAQSASINVYFLSPPPHAAAPGYTPSDTSTVSLDVVTSLPMPVPVPQPNPQMASQSNISPKPEIILDSTLSPVEGCGDEHRDVTSPLFKRKDSAGDADVSVSGNGGAGGVGGVGGRQGRCSILAGYDGIQTVRKRQASVVTYDVNVINFSQENSDSRSYIPMGRVSTSSAKHEFSNKSSLIRRGGICIFVDEEEAEIIEQRPRGITFAAVPSPLPKCPLCGADISSTTGTTANATATANADSTIDTTVTTSSKRSIHEQTPDLGQRPASSSSSTRFWHKRTAAVTACWQQSKNRKRRFKTGCSHCGATGGSVRPAKGWKAEHKAARTLGIIMGVFLLCWLPFFLWYVITSLCGPACPCPDVLVVVLFWIGYFNSTLNPLIYAYFNRDFREAFRNTLECVLPCLEKRNPYNAYYV
Protein: Hpr1 (LD43883p) (Q9VNI8)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- THO complex subunit 2
- THO complex protein 7
- FI07663p
- THO complex subunit 6
- THO complex subunit 5
- LD24793p
- ATP-dependent RNA helicase WM6
- RNA and export factor binding protein 2, isoform A
- LD31448p
- Nuclear RNA export factor 1
Sequence:
MSTAVEVANTAPEKLANYFALQSAFEKALELAITDGKVELLVKEYNRFPANTEHDKRLPMDHAFRVLLMKRLDEDVSRIGELVRLSVEATRAEIVSNTIPVVLLIDTFDVVTLDKCQKIFQFVEDMVEVWKEEIFFSSCKNNILRMCNDLLRRLSRTQNTVFCGRIQLFLSKFFPFSERSGLNIVSEFNLDNFTEYGLDSKDHDESDNKELEDTAEDIPLKIDYDLYCKFWSLQDFFRNPNQCYNKPQWKMFQMHADNILQSFSSFKLEDVRQSSNENASGTDQAMDVDEEAVDTTAVSSVIKANHFFAKFLTNPKLLALQLSDANFRRAVLVQFLILFQYLQVSVKFKSDTQTLTADQADFIKETESRVYKLLEETPPYGKRFSRTVYHMLAREEMWNNWKNEGCKEFKKPEEPTLSEEDSKPTPNKRPRRPLGDALRDASRSGKFYLGNDNLTRLWNYSPDNLQACKSEQRNFLPLLETYLETPHEKVDPAFEWRALRLLARQTPHFFTSLSQPSSKISDYLEQVRKRLIRDKEPKPAALLSNNSSENNFGLSVNNVHTEGEQDATVALQDGEPEQDLEVEDNEPVVEEVDEVPAHEKPLMVTKEHIEEVAPLIGEPWMKVGKKIGFTNDELLFFQMEHPTANVACVKMLTNWISDDDDATLENWAYMLEGLEMNKAAEAVKAIIEREKSGSTAAFCLR
Protein: Cytidine and dCMP deaminase domain-containing protein 1 (EC 3.5.4.5) (Cytidine deaminase) (Testis development protein NYD-SP15) (Q9BWV3)
Organism: Homo sapiens (Human)
Function: Catalyzes the deamination of cytidine and deoxycytidine into uridine and deoxyuridine, respectively. May play an important role in testicular development and spermatogenesis.
Subcellular location: Cytoplasm {ECO:0000305|PubMed:26945630}. Nucleus {ECO:0000305|PubMed:26945630}.
Interaction partners:
- Thymidylate synthase
- Thymidine kinase, cytosolic
- Thymidine phosphorylase
- Fibronectin type-III domain-containing protein 3A
Sequence:
MKEAGQMQNLESARAGRSVSTQTGSMTGQIPRLSKVNLFTLLSLWMELFPAEAQRQKSQKNEEGKHGPLGDNEERTRVSTDKRQVKRTGLVVVKNMKIVGLHCSSEDLHAGQIALIKHGSRLKNCDLYFSRKPCSACLKMIVNAGVNRISYWPADPEISLLTEASSSEDAKLDAKAVERLKSNSRAHVCVLLQPLVCYMVQFVEETSYKCDFIQKITKTLPDANTDFYYECKQERIKEYEMLFLVSNEEMHKQILMTIGLENLCENPYFSNLRQNMKDLILLLATVASSVPNFKHFGFYRSNPEQINEIHNQSLPQEIARHCMVQARLLAYRTEDHKTGVGAVIWAEGKSRSCDGTGAMYFVGCGYNAFPVGSEYADFPHMDDKQKDREIRKFRYIIHAEQNALTFRCQEIKPEERSMIFVTKCPCDECVPLIKGAGIKQIYAGDVDVGKKKADISYMRFGELEGVSKFTWQLNPSGAYGLEQNEPERRENGVLRPVPQKEEQHQDKKLRLGIH
Protein: Type III secretion system effector delivery regulator TyeA domain-containing protein (G3XCT8)
Organism: Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Interaction partners:
- Type III secretion chaperone SycN
- Uncharacterized protein
- Type III secretion outer membrane protein PopN
- Type III secretion protein PcrV
- Type III secretory apparatus protein PcrD
- Uncharacterized protein
- Transcriptional regulator protein PcrR
- Translocation protein in type III secretion
- Regulatory protein PcrH
- Translocation protein in type III secretion
Sequence:
MAYGPSELTGAVIALLEKRWVGVAEVQALLEPLPLADVARQIHFFRELKRLYRLLPVEVFGDDEQRQNLLNACQMALDLAIEREEEQQHGLG
Protein: Ferredoxin-fold anticodon-binding domain-containing protein 1 (FDX-ACDB domain-containing protein 1) (Q9BRP7)
Organism: Homo sapiens (Human)
Interaction partners:
- Leucine-rich repeat-containing protein 47
- Phenylalanine--tRNA ligase beta subunit
- Polyribonucleotide nucleotidyltransferase 1, mitochondrial
- Adipocyte plasma membrane-associated protein
- Tyrosine--tRNA ligase, cytoplasmic
Sequence:
MAPRRLLLVGEGNFSFAAALSETLDQSTQLTATCLQRPAELARDPLAWENLQCLRERGIDVRFGVDCTQLADVFELHEREFDQIYFIFPHCGRKAGVAKNRELLAKFFQSCADVLAEEGEVHVALCRGQGGTPADKPQREWHNSWQVVAMAALGGLILSDVYPFSCKAVAGYKCTGYRSQDKSFHVEGALNHIFTRSLPFEGSQPRIFRIKLGNQWFSFPEPEALVGKLNRGFLEAPSCHPIKTINEKLIAELGKVFPLKRLKCSYPLLPQEGTSVLPFWNCDFLSAAFWISLHEDNSNSESLTGGTSQDVEDFLVSFSELSLLKNPGRDGKEEACEGTCGQAKICLRPSLLVHVQDVIEVPDFLSGSLHILSGPVFQKCHILPFTMPAFHETLFILGVNQNLKDGCLQSLLDHLKGILDSLLTQTLPESSKLSSLVKFVLQSNGKDYMIRVKTHNFSPDCTEDLIIGSVITSATSVIHKDQCFVFVSMNLDLLAMLVWCISDWRMLWTFDNRFLKNFVPGKIEPFKSHSLYPPCYVHDVSFWIDQKKGFDELEFHTVARAVSQDTIISIQFLSRFQHPKTQQVSLCYRLTYQTCDKALTQQQVASMQSQFRKEIQQHLYVIPR
Protein: C-type lectin domain-containing protein (O02343)
Organism: Caenorhabditis elegans
Interaction partners:
- VWFA domain-containing protein
- C-type LECtin
- C-type lectin domain-containing protein
- Alpha-mannosidase
- C-type lectin domain-containing protein
Sequence:
MLLFSAFLIFGFSIGFSEEASCRHPHERFIGTRCYAFVSKKHTYNTAKEYCDSHGYSLATVDNAITSNFLASSAATEFGSNNGQFWIGLSRKKDYELFNWDDGTIVSYTNFEAGFPNKQDFVAENVRNGRWQTLAEHKELEFVCSYDPTATTSAAPTTIPPTTTTTRAPTTTTVRKTTQTTATTMTTPKPTTTVSTTTTTTVPPTTTPKACPQGFVLFEPTQKCYIVLVYGNDSDYPDVPDDAPFLTRENQRCAKYGATVATIHSSDLNDLFRSLIYERFNDTRYATIGLRNIDMKTISGKWQWFDGTSPDYLNFGNMFPKTGDYIAQTSSQGFWVSYTHTAPNEGVVCSVDF
Protein: Cytoplasmic linker associated protein 1 (F1LNQ9)
Organism: Rattus norvegicus (Rat)
Subcellular location: Chromosome, centromere, kinetochore {ECO:0000256|ARBA:ARBA00004629}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000256|ARBA:ARBA00004300}. Cytoplasm, cytoskeleton, spindle {ECO:0000256|ARBA:ARBA00004186}. Golgi apparatus, trans-Golgi network {ECO:0000256|ARBA:ARBA00004601}.
Interaction partners:
Sequence:
MEPRMESCLAQVLQKDVGKRLQVGQELIDYFSDKQKSADLEHDQTMLDKLVDGLATSWVNSSNYKVVLLGMDILSALVTRLQDRFKAQIGTVLPSLIDRLGDAKDSVREQDQTLLLKIMDQAANPQYVWDRMLGGFKHKNFRTREGICLCLIATLNASGAQTLTLSKIVPHICNLLGDPNSQVRDAAINSLVEIYRHVGERVRADLSKKGLPQSRLNVIFTKFDEVQKSGNMIQSANDKNFDDEDSVDGNRPSSASSSSSKAPSSSRRNVSMGTTRRLMASSLGSKSSAAKEGAGAVDEEDFIKAFDDVPVVQIYSSRDLEESINKIREILSDDKHDWEQRVNALKKIRSLLLAGAAEYDNFFQHLRLLDGAFKLSAKDLRSQVVREACITLGHLSSVLGNKFDHGAEAIMPTIFNLIPNSAKIMATSGVVAVRLIIRHTHIPRLIPVITSNCTSKSVAVRRRCFEFLDLLLQEWQTHSLERHISVLAETIKKGIHDADSEARIEARKCYWGFHSHFSREAEHLYHTLESSYQKALQSHLKNSDSIVSLPQSDRSSSSSQESLNRPLSAKRSPTGSTASRGSTVSTKSMSTTGSLQRSRSDIDVNAAASAKSKVSSSSGSTAFSSAAALPPGSYASLGRIRTRRQSSGSTTNVASTSSDSRGRSRAKVVSQSQRSRSANPAGAGSRSSSPGKLLGSGYGGLAGGSSRGPPVTPSSEKRSKIPRSQGCSRETSPNRIGLARSSRIPRPSMSQGCSRDTSRESSRDTSPARGFTPLDRFGLGQSGRIPGSVSAMRVLSTSTDLEAAVADALKKPVRRRYEPYGMYSDDDANSDASSVCSERSYGSRNGGIPHYLRQTEDVAEVLNHCASSNWSERKEGLLGLQNLLKSQRTLSRVELKRLCEIFTRMFADPHSKRVFSMFLETLVDFIIIHKDDLQDWLFVLLTQLLKKMGADLLGSVQAKVQKALDVTRDSFPFDQQFNILMRFIVDQTQTPNLKVKVAILKYIESLARQMDPTDFVNSSETRLAVSRIITWTTEPKSSDVRKAAQIVLISLFELNTPEFTMLLGALPKTFQDGATKLLHNHLKNSSNAGVGSPSNTIGRTPSRHPSSRTSPLTSPTNCSHGGLSPSRLWGWSADGLSKPPPPFSQPNSIPTAPSHKTLRRSYSPSMLDYDTENLNSEEIYSSLRGVTEAIEKFSFRSQEDLNEPIKRDGKKDCDIVSRDGGAASPATEGRGGSEVEGGRMALDNKTSLLNTQPPRAFPGPRAREYNPYPYSDTINTYDKTALKEAVFDDDMEQLRDVPIDHSDLVADLLKELSNHNERVEERKGALLELLKITREDSLGVWEEHFKTILLLLLETLGDKDHSIRALALRVLREILRNQPARFKNYAELTIMKTLEAHKDSHKEVVRAAEEAASTLASSIHPEQCIKVLCPIIQTADYPINLAAIKMQTKVVERITKESLLQLLVDIIPGLLQGYDNTESSVRKASVFCLVAIYSVIGEDLKPHLAQLTGSKMKLLNLYIKRAQTTNSNSSSSSDVSTHS