wanglab/gogpt-training-data huggingface dataset:
Protein: Dynamin-binding protein (Scaffold protein Tuba) (E2RP94)
Organism: Canis lupus familiaris (Dog) (Canis familiaris)
Function: Plays a critical role as a guanine nucleotide exchange factor (GEF) for CDC42 in several intracellular processes associated with the actin and microtubule cytoskeleton. Regulates the structure of apical junctions in epithelial cells (By similarity). Participates in the normal lumenogenesis of epithelial cell cysts by regulating spindle orientation. Plays a key role in ciliogenesis and cyst formation. May play a role in membrane trafficking between the cell surface and the Golgi (By similarity).
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:Q6XZF7}. Golgi apparatus, Golgi stack {ECO:0000250|UniProtKB:Q6TXD4}. Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:Q6TXD4}. Synapse {ECO:0000250|UniProtKB:M0R4F8}. Cell junction {ECO:0000250|UniProtKB:Q6XZF7}. Note=Localizes to the apical junction, colocalizes with TJP1. {ECO:0000250|UniProtKB:Q6XZF7}.
Interaction partners:
- Zinc finger protein 768.
- Ubiquitin specific peptidase 36
- Rap guanine nucleotide exchange factor 1.
- FA complementation group I.
Sequence:
MEAGSVVRAIFDFCPSVSEELPLFVGDIIEVLAVVDEFWLLGKKEDVTGQFPSSFVEIVTIPSLKEGERLFVCISEFTSQELNSLPLHRGDLVILDDAPTASWLQGRSCWGARGFFPSSCVRELCLSSQSRRWHSQSALLQIPEYSMGQARALMGLSAQLDEELDFREGDVITIIGVPEPGWFEGELEGRRGIFPEGFVELLGPLRTVDELVSSGNHNDCIINGEEETPTGEEERGPEEDEEQPGTYGIALYRFQALEPNELDFEVGDKIRILGTLEDGWLEGSLKGRTGIFPYRFVKLFSKTRAEETMDLPKESSPTEIPDTSLDCRENPLVVEGRHKSPEYKAEKSNCVISETSASPLEHLTSECEVHKSSHQDEGTSRGPPRSPGWGHEQPLARHSPAEDPSETINGVSSQSQVPFRPRWQQNQYYSTTGRGHLSTEQYSDPLPLEAKAKDYSSRPPRGMYSPPKTFQKPVPSPHGSSCPLAPRVVRPSLLSSQLQSMVRGAKKYHTPKENASSFCSASERSEVKAGLQDRAFTADLIALGQGGGHTDLDSKLTQQLVEFEKSLSGPGAEPEAILRHFSIMNFNSEKDIVRGSSKSITPQELPERRRALRPPPPRPSTPASTSPHVLLDQNLKPEPPLAMRPSRPAPLPPSAQHRVTAVTPGLLTPGLFTHESCESPEKEGPENLDQTLDQTSQCPLVLVRIQEMEQDLDMCSPAPEEPNLTLEEKQDESLRAETPEDLEFYESNIESLNMELQQLREMTLLSSQSSSPVAPPGSMYTENPEQRMLEKRAKVIEELLQTERDYVRDLEMCIEHIMAPLQQTQIPNIDFEGLFGNMQMVIKVSKQLLADLEISDAVGPVFLDHRDELEGTYKVYCQNHDEAISLLEIYEKDEKIQKHLQDSLADLKSLYTEWGCTNYINLGSFLIKPVQRVMRYPLLLMELLNSTPESHPDKAPLTSAVLAVKEINVNINEYKRRKDLVLKYRKGDEDSLMEKISKLNIHSIIKKSNRVSSHLKHLTGFAPQIKDEAFEETEKNFRMQERLIKSFIRDLSLYLQHIRESACVKVVAAVSMWDVCMEKGHRDLEQFEKVHRYISDQLFTNFKERTERLVISPLNQLLSMFTGPHKLVQKRFDKLLDFYNCTERAEKLKDKKTLEELQSARNNYEALNAQLLDELPKFHQYAQGLFTNCIHGYAEAHCDFVRQALEQLKPLLSLLKVAGREGNLIAIFHEEHSRVLQQLQVFTFFPESLPAARKPFERKTLDRQSARKPLLGLPSYMLQSEELRASLLTRYPPEKLFQAERNFNAAQDLDVSLLEGDLVGVIKKKDPMGSQNRWLIDNGVSQGFVYSSFLKPYNTRRSHSDVSVGSHSSTESEQSSSSPRFPRQNSSGTLTFNPGSMAVSFTSGSCQKQPQDATSPKELGQEILSASSNLGCSESSPSRCPSDPDSSPQPRSWDSPEAARDISQPAPALRGYRNSRHPEIGGYSLPGRNGQGKDLTKGCARTTQALEDKNEEPESREAEGNQVYFAVYTFKARNPNELSVSANQRLKILEFKDVTGNTEWWLAEVNGKKGYVPSNYIRKAEYT
Protein: Serine/threonine-protein kinase 10 (EC 2.7.11.1) (Lymphocyte-oriented kinase) (O94804)
Organism: Homo sapiens (Human)
Function: Serine/threonine-protein kinase involved in regulation of lymphocyte migration. Phosphorylates MSN, and possibly PLK1. Involved in regulation of lymphocyte migration by mediating phosphorylation of ERM proteins such as MSN. Acts as a negative regulator of MAP3K1/MEKK1. May also act as a cell cycle regulator by acting as a polo kinase kinase: mediates phosphorylation of PLK1 in vitro; however such data require additional evidences in vivo.
Subcellular location: Cell membrane {ECO:0000269|PubMed:19255442}; Peripheral membrane protein {ECO:0000269|PubMed:19255442}.
Interaction partners:
- Transforming protein RhoA
Sequence:
MAFANFRRILRLSTFEKRKSREYEHVRRDLDPNEVWEIVGELGDGAFGKVYKAKNKETGALAAAKVIETKSEEELEDYIVEIEILATCDHPYIVKLLGAYYHDGKLWIMIEFCPGGAVDAIMLELDRGLTEPQIQVVCRQMLEALNFLHSKRIIHRDLKAGNVLMTLEGDIRLADFGVSAKNLKTLQKRDSFIGTPYWMAPEVVMCETMKDTPYDYKADIWSLGITLIEMAQIEPPHHELNPMRVLLKIAKSDPPTLLTPSKWSVEFRDFLKIALDKNPETRPSAAQLLEHPFVSSITSNKALRELVAEAKAEVMEEIEDGRDEGEEEDAVDAASTLENHTQNSSEVSPPSLNADKPLEESPSTPLAPSQSQDSVNEPCSQPSGDRSLQTTSPPVVAPGNENGLAVPVPLRKSRPVSMDARIQVAQEKQVAEQGGDLSPAANRSQKASQSRPNSSALETLGGEKLANGSLEPPAQAAPGPSKRDSDCSSLCTSESMDYGTNLSTDLSLNKEMGSLSIKDPKLYKKTLKRTRKFVVDGVEVSITTSKIISEDEKKDEEMRFLRRQELRELRLLQKEEHRNQTQLSNKHELQLEQMHKRFEQEINAKKKFFDTELENLERQQKQQVEKMEQDHAVRRREEARRIRLEQDRDYTRFQEQLKLMKKEVKNEVEKLPRQQRKESMKQKMEEHTQKKQLLDRDFVAKQKEDLELAMKRLTTDNRREICDKERECLMKKQELLRDREAALWEMEEHQLQERHQLVKQQLKDQYFLQRHELLRKHEKEREQMQRYNQRMIEQLKVRQQQEKARLPKIQRSEGKTRMAMYKKSLHINGGGSAAEQREKIKQFSQQEEKRQKSERLQQQQKHENQMRDMLAQCESNMSELQQLQNEKCHLLVEHETQKLKALDESHNQNLKEWRDKLRPRKKALEEDLNQKKREQEMFFKLSEEAECPNPSTPSKAAKFFPYSSADAS
Protein: Ammonium transporter (Q84R60)
Organism: Oryza sativa subsp. japonica (Rice)
Interaction partners:
Sequence:
MEDSSLFMEWAMETLQHLHPLPATPPPAGGGYAGDNATFPSLQALRESSVSQNGMAPPEPTAHEGHRASNSWSSGDTDSVSGGGGGAVMEHDGWSTSPNSVRCAAGGGGGGGGGGLWPVSWNFSSAMTQPCNDQATPSNPPTTTRARYGGGGVRYLPAAVSPSPSAQTRRASSKGNGGGGSGSSSAAPYAQEHIIAERKRREKINQRFIELSTVIPGLKKMDKATILSDAVRYVKEMQEKLSELEQHQNGGVESAILLKKPCIATSSSDGGCPAASSAVAGSSSSGTARSSLPEIEAKISHGNVMVRIHGENNGKGSLVRLLAAVEGLHLGITHTNVMPFSACTAIITIMAKE
Protein: Large ribosomal subunit protein uL16c (50S ribosomal protein L16, chloroplastic) (Q6END6)
Organism: Oryza nivara (Indian wild rice) (Oryza sativa f. spontanea)
Subcellular location: Plastid, chloroplast.
Interaction partners:
- Uncharacterized protein
- Large ribosomal subunit protein bL27c
- Large ribosomal subunit protein uL5c
- Large ribosomal subunit protein uL14c
- Uncharacterized protein
- Small ribosomal subunit protein uS12c
- Large ribosomal subunit protein uL23 N-terminal domain-containing protein
- Large ribosomal subunit protein uL23 N-terminal domain-containing protein
- Ribosomal protein L30 ferredoxin-like fold domain-containing protein
- Ribosomal protein L30 ferredoxin-like fold domain-containing protein
Sequence:
MLSPKRTRFRKQHRGRMKGKSYRGNCICFGRYALQALEPTWITARQIEAGRRAMTRYARRGGKIWVRIFPDKPVTIRPTETRMGSGKGSPEYWVAVVKPGRILYEMGGVSETVARVAISIAASKMPIRSQFLRLEI
Protein: At4g24330 (Q9STW1)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- Nicalin
- BOS complex subunit TMEM147
- Calcium load-activated calcium channel
- Calcium load-activated calcium channel
- Large ribosomal subunit protein eL38z/eL38y
- Large ribosomal subunit protein uL18y
- Protein Asterix
- SecY protein transport family protein
- AT2G34250 protein
- F9K20.24 protein
Sequence:
MNRLFSLFSIALIAFLCLHHHVLASSSSDFEGFDAEDDDVSEDSTELHHSLRPPLLTQSESTVLDLDPSPDSDSTPASKSDPPTQTVKPSSSISFDYWDEDEFEGLPEDEKSTESPVFSDDASSPADPQTPDLESASETPDTDIPKKMQSYTVEIVCVSILIGYAINYFTGKRENENLALAWASKFGLKDTIFEKNFSLLGVGEGEDSPLLLKEATNVFKFYASGRRYCHGLLATLELKSRHDLISRLFNSVVPCKDEISFEVYMNDEAMDHIVFAMARKKAAKTMHKELRDLQRFGGMVPSPGGRKWVTEELAVVSESKEVAGDMITDVVLDQVFGDKSFEKFGKYFISMHFSDQHPGKHRKMLLFKFALPDIKHMDDMVRLIALIPYYIDLIGRYKLSSQARNKTDGARQKAAQEAYKELENVRQEALQRKKAEKKKILEEAQAKLSSEALRKKEAKERARQMKKSMPKVKMSRGH
Protein: Nucleoporin NUP120 (Nuclear pore protein NUP120) (P35729)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Functions as a component of the nuclear pore complex (NPC). NPC components, collectively referred to as nucleoporins (NUPs), can play the role of both NPC structural components and of docking or interaction partners for transiently associated nuclear transport factors. NUP120 is involved in nuclear poly(A)+ RNA and pre-ribosome export, in GSP1 nuclear import, in NPC assembly and distribution, as well as in nuclear envelope organization.
Subcellular location: Nucleus, nuclear pore complex {ECO:0000269|PubMed:10684247}. Nucleus membrane; Peripheral membrane protein; Cytoplasmic side. Nucleus membrane; Peripheral membrane protein; Nucleoplasmic side. Note=Symmetric distribution.
Interaction partners:
- Nucleoporin NUP145
- Nucleoporin NUP84
- Nucleoporin NUP85
- Protein transport protein SEC13
- Nucleoporin NUP133
- Nucleoporin SEH1
- Nucleoporin NUP188
- Nucleoporin NUP100/NSP100
- Nucleoporin NUP116/NSP116
- Nucleoporin NUP157
Sequence:
MACLSRIDANLLQYYEKPEPNNTVDLYVSNNSNNNGLKEGDKSISTPVPQPYGSEYSNCLLLSNSEYICYHFSSRSTLLTFYPLSDAYHGKTINIHLPNASMNQRYTLTIQEVEQQLLVNVILKDGSFLTLQLPLSFLFSSANTLNGEWFHLQNPYDFTVRVPHFLFYVSPQFSVVFLEDGGLLGLKKVDGVHYEPLLFNDNSYLKSLTRFFSRSSKSDYDSVISCKLFHERYLIVLTQNCHLKIWDLTSFTLIQDYDMVSQSDSDPSHFRKVEAVGEYLSLYNNTLVTLLPLENGLFQMGTLLVDSSGILTYTFQNNIPTNLSASAIWSIVDLVLTRPLELNVEASYLNLIVLWKSGTASKLQILNVNDESFKNYEWIESVNKSLVDLQSEHDLDIVTKTGDVERGFCNLKSRYGTQIFERAQQILSENKIIMAHNEDEEYLANLETILRDVKTAFNEASSITLYGDEIILVNCFQPYNHSLYKLNTTVENWFYNMHSETDGSELFKYLRTLNGFASTLSNDVLRSISKKFLDIITGELPDSMTTVEKFTDIFKNCLENQFEITNLKILFDELNSFDIPVVLNDLINNQMKPGIFWKKDFISAIKFDGFTSIISLESLHQLLSIHYRITLQVLLTFVLFDLDTEIFGQHISTLLDLHYKQFLLLNLYRQDKCLLAEVLLKDSSEFSFGVKFFNYGQLIAYIDSLNSNVYNASITENSFFMTFFRSYIIENTSHKNIRFFLENVECPFYLRHNEVQEFMFAMTLFSCGNFDQSYEIFQLHDYPEAINDKLPTFLEDLKSENYHGDSIWKDLLCTFTVPYRHSAFYYQLSLLFDRNNSQEFALKCISKSAEYSLKEIQIEELQDFKEKQHIHYLNLLIHFRMFEEVLDVLRLGHECLSDTVRTNFLQLLLQEDIYSRDFFSTLLRLCNAHSDNGELYLRTVDIKIVDSILSQNLRSGDWECFKKLYCFRMLNKSERAAAEVLYQYILMQADLDVIRKRKCYLMVINVLSSFDSAYDQWILNGSKVVTLTDLRDELRGL
Protein: peptidylprolyl isomerase (EC 5.2.1.8) (Q38BD9)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- Calcineurin B subunit, putative
- Probable eukaryotic initiation factor 4A
- Serine/threonine-protein phosphatase
- Serine/threonine specific protein phosphatases domain-containing protein
- Serine/threonine-protein phosphatase
Sequence:
MPLQYDIITKGTGPCPKAGDSVTVRAAGFFPDGRIFWPAKGGTESFSFRVGLGHVIRGWDEAVLQMPLGEKAKIAMTSEYAYGTKGFPEWGIEPGASLVFEMELVAIN
Protein: Adenosine deaminase (EC 3.5.4.4) (Adenosine aminohydrolase) (P22333)
Organism: Escherichia coli (strain K12)
Function: Catalyzes the hydrolytic deamination of adenosine and 2-deoxyadenosine.
Interaction partners:
- Purine nucleoside phosphorylase DeoD-type
- Guanosine-inosine kinase
- Pyrimidine/purine nucleoside phosphorylase
- Protein UshA
- Pyrimidine 5'-nucleotidase YjjG
- 2',3'-cyclic-nucleotide 2'-phosphodiesterase/3'-nucleotidase
- Pyrimidine-specific ribonucleoside hydrolase RihB
- 5'/3'-nucleotidase SurE
- GMP/IMP nucleotidase YrfG
- Adenine phosphoribosyltransferase
Sequence:
MIDTTLPLTDIHRHLDGNIRPQTILELGRQYNISLPAQSLETLIPHVQVIANEPDLVSFLTKLDWGVKVLASLDACRRVAFENIEDAARHGLHYVELRFSPGYMAMAHQLPVAGVVEAVIDGVREGCRTFGVQAKLIGIMSRTFGEAACQQELEAFLAHRDQITALDLAGDELGFPGSLFLSHFNRARDAGWHITVHAGEAAGPESIWQAIRELGAERIGHGVKAIEDRALMDFLAEQQIGIESCLTSNIQTSTVAELAAHPLKTFLEHGIRASINTDDPGVQGVDIIHEYTVAAPAAGLSREQIRQAQINGLEMAFLSAEEKRALREKVAAK
Protein: Biotin synthase, mitochondrial (EC 2.8.1.6) (Q5AYI7)
Organism: Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Function: Biotin synthase; part of the cluster involved in the biosynthesis of biotin (also known as vitamin B8 or vitamin H), a water-soluble vitamin that functions as a prosthetic group of many carboxylases, such as acetyl-CoA carboxylase and pyruvate carboxylase. Catalyzes the conversion of dethiobiotin (DTB) to biotin by the insertion of a sulfur atom into dethiobiotin via a radical-based mechanism (By similarity).
Subcellular location: Mitochondrion {ECO:0000305|PubMed:20713166}.
Interaction partners:
- Bifunctional dethiobiotin synthetase/adenosylmethionine-8-amino-7-oxononanoate aminotransferase
- Biotin apo-protein ligase, putative
- Uroporphyrinogen decarboxylase
- 8-amino-7-oxononanoate synthase
- 5-aminolevulinate synthase, mitochondrial
- Acetylglutamate kinase
Sequence:
MSVSFTRSFPRAFIRSYGTVQSSPTAASFASRIPPALQEAVAATAPRTNWTRDEVQQIYETPLNQLTYAAAAVHRRFHDPSAIQMCTLMNIKTGGCSEDCSYCAQSSRYSTGLKATKMSPVDDVLEKARIAKANGSTRFCMGAAWRDMRGRKTSLKNVKQMVSGVREMGMEVCVTLGMIDADQAKELKDAGLTAYNHNLDTSREFYPTIITTRSYDERLKTLSHVRDAGINVCSGGILGLGEADSDRIGLIHTVSSLPSHPESFPVNALVPIKGTPLGDRKMISFDKLLRTVATARIVLPATIVRLAAGRISLTEEQQVACFMAGANAVFTGEKMLTTDCNGWDEDRAMFDRWGFYPMRSFEKETNAATPQQHVDSVAHESEKNPAAPAAEAL
Protein: Exocyst complex component Sec8 (Q38CI3)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MAWRYNSNSPPRGNVSANASLVSLSSANNNNRNFTDSADDNADTSALGNNNTFRRDRSAMDGAGAFLRSNAKGKMWSRQEGRDETPDDDVSSRDGTSPCSISFARPKLAPTESTTRPHRSLIFSRNPNRGVSGAATRSGMGSMSRLSVDSALNTPHRVASTRCVEGRVTSSSIANWRLPRHSGSPPINTGECNGEMTIISESGDFDEDATGGDPLLGCADRNLHRATEALLAEADPDLRATDFTPTKHVLQIVVKEDGTECSGAQIDERIAPLCGLQNRLDDMLGLHIQSHKDVFNKAIGRFSDIVLAVSDSNEVLGLLKQRLGMATSSLENRAEQLQVLRMRAAKALLMEESLKRMEAALASEREIKQLVASRHYLAAVRLLRQQKARLESPDMVNIRATQSMRDFANHTLETLHKNVLDGLMGCVFDKDRFSEADKQLMGRMVADGALENVAGTLSFMGDTCGALSSQCFTGGGGKNGDSDFVSLDGIVDDPCDEGMVKNHLHFIPLCVKTLKELGKLDQCCEAFRSGATRSIEQCVANFLSLYDTWRRDAESSKCVGNNDDMGSTVRILELQGRDVASCTVSHDEAVALIQQRDLCPLLNALFTELERVVRNADYLVRVVLLAYFPFLTDVPPRSEVFDDNFSCHEWDVTQSPLRTKNELRDIVVRTLAEAISRHSEDSVSSETPESRRLAALKRLMAKFDVDKALKGSSSHDAPTSKKGSLRQGSVDDGSIRCESNNAVCLGDVLTSLNAAAFLAVEEFPDGSEEVPACCERLSKAISSAVQDSFRSYMREIYLDWDLCALSSQLSYTVELVFKLICSNDAATSSKSDATAVNLSKQNLKHRRTTSRSWWQIDSIGGSHTNETFTSLDKMLSSHGSSGLLSAIEQIGGVSFSIVSTVNASSVEQVRAKDKKHLHSGAGTRIISSFGEVQGAAAPLKSAARLRNWFMFTPMNILACYDCTGHFFKRWKSYKLYFATVPVVEMTNFFQDFLERTYSPCLRAFHMMQLGKFLAEMPEPQGVHDGTESMGGPGDAGGTRANSSFATSTRQYMHHLKTQQEYMRWPTVTPGDNGCNGNAIHPVLTCVHYVGQVVQKLSRICRVLPSVLVDKIQQFLVQPLLIELNSFLKRKVQLITRGSLSHCLLNSDFDDAFHGTHTARWDALCDETRRGDSYEAIDMGLFRFYRYINARRTRAGADGDVEVVVPEEMQELFNHVRVKREKQHERSERRNEVFRSNGSLVSPISPRGAANGIQCEDVTAADLALQGDGIVVALALFCHSTEWLCGLLLRAFGPEGWCQHSDGDKLVPGAAFRERRRPPRKGVTPMQEGTEGWQHLGNFVDQLYTISQACLFHLLVEARFTAFQFIPQLSEHSYNIVAGAGTPDTFVQAYNRRMTNFFALLKPYLPSKRVKFVCLTVAKPLSDLFMLEISQLRDKVISTTGVSRLQVNLLAMEAALQLVLPTDDDVRESVKFHFARPATFVRYLSNGDVTDDLIASGDYKIFEVREMEELVRLVLKGDATASSVAEKIKLLHAGLEREQYDMISPLTTSPAITPNRKLPPVARGSSTGCKGHFPVSGSDAAAHEEPGELDNAKSPSSPQRRSANNKGTLKHVDPNSGGIIDPSLVNSDLKMPSSPGDAREVTESHSSGSEEGDEEEEYEEEYEEYEESDEYEESDDADNDDDDSSL
Protein: Coiled-coil domain-containing protein 172 (P0C7W6)
Organism: Homo sapiens (Human)
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:Q810N9}. Cell projection, cilium {ECO:0000250|UniProtKB:Q6AXT4}. Note=In spermatozoa, localized in the middle piece, predominantly concentrated at the mitochondrial sheath of the flagella and to a lesser extent with outer dense fibers (ODF) (By similarity). Colocalized with TEKT2 at the perinuclear region (By similarity). {ECO:0000250|UniProtKB:Q6AXT4, ECO:0000250|UniProtKB:Q810N9}.
Interaction partners:
Sequence:
MSLESLFQHIIFTEHQAEESRRLMREVRSEITRCREKIKKATEELNEEKIKLESKVQQFFEKSFFLQLLKAHENALEKQYSEITNHRNMLLQTFEAIKKQMIEEEDKFIKEITDFNNDYEITKKRELLMKENVKIEISDLENQANMLKSEMKSMEHDSSQLNELQKQKSELIQELFTLQRKLKVFEDEENESICTTKYLEAEKIKISEKPQNDTECLRLKKELELYKEDDMESVYEALQTEIEFLELTLAQKDLQESK
Protein: Protein mago nashi homolog (Ce-mago) (P49029)
Organism: Caenorhabditis elegans
Function: Core component of the splicing-dependent multiprotein exon junction complex (EJC) deposited at splice junctions on mRNAs (Probable). Positively regulates the nuclear export of spliced mRNAs including the sex determination gene tra-2. Promotes oogenesis and represses germline masculinization and spermatogenesis. Required for embryonic development, possibly through positively regulating the expression of pie-1. Not required for the spatial patterning of pie-1 in embryos.
Subcellular location: Nucleus {ECO:0000250|UniProtKB:P61326}.
Interaction partners:
- RNA-binding protein rnp-4
- RNA helicase
- Partner of Y14 and mago
- UPF3 domain-containing protein
- Protein CASC3
- Spliceosome RNA helicase DDX39B homolog
- Cleavage and polyadenylation specificity factor subunit 5
- Exportin-T
- Probable splicing factor, arginine/serine-rich 6
- RRM domain-containing protein
Sequence:
MSGEEEKAADFYVRYYVGHKGKFGHEFLEFEFRPNGSLRYANNSNYKNDTMIRKEATVSESVLSELKRIIEDSEIMQEDDDNWPEPDKIGRQELEILYKNEHISFTTGKIGALADVNNSKDPDGLRSFYYLVQDLKCLVFSLIGLHFKIKPI
Protein: Glucose-1-phosphate adenylyltransferase small subunit, chloroplastic/amyloplastic (EC 2.7.7.27) (ADP-glucose pyrophosphorylase) (ADP-glucose synthase) (AGPase B) (Alpha-D-glucose-1-phosphate adenyl transferase) (P23509)
Organism: Solanum tuberosum (Potato)
Function: This protein plays a role in synthesis of starch. It catalyzes the synthesis of the activated glycosyl donor, ADP-glucose from Glc-1-P and ATP.
Subcellular location: Plastid, chloroplast. Plastid, amyloplast. Note=Found in the chloroplast in leaf. Found in the plastid in the developing endosperm.
Interaction partners:
- Glucose-1-phosphate adenylyltransferase
- Granule-bound starch synthase 1, chloroplastic/amyloplastic
- Soluble starch synthase 3, chloroplastic/amyloplastic
- Sucrose synthase
- Sucrose-phosphate synthase
- sucrose-phosphate synthase
- Eukaryotic translation initiation factor
- Eukaryotic translation initiation factor 2 subunit beta
- sucrose synthase
- Sucrose synthase
Sequence:
MAASIGALKSSPSSNNCINERRNDSTRAVSSRNLSFSSSHLAGDKLMPVSSLRSQGVRFNVRRSPMIVSPKAVSDSQNSQTCLDPDASRSVLGIILGGGAGTRLYPLTKKRAKPAVPLGANYRLIDIPVSNCLNSNISKIYVLTQFNSASLNRHLSRAYASNMGGYKNEGFVEVLAAQQSPENPDWFQGTADAVRQYLWLFEEHTVLEYLILAGDHLYRMDYEKFIQAHRETDADITVAALPMDEKRATAFGLMKIDEEGRIIEFAEKPQGEQLQAMKVDTTILGLDDKRAKEMPFIASMGIYVISKDVMLNLLRDKFPGANDFGSEVIPGATSLGMRVQAYLYDGYWEDIGTIEAFYNANLGITKKPVPDFSFYDRSAPIYTQPRYLPPSKMLDADVTDSVIGEGCVIKNCKIHHSVVGLRSCISEGAIIEDSLLMGADYYETDADRKLLAAKGSVPIGIGKNCHIKRAIIDKNARIGDNVKIINKDNVQEAARETDGYFIKSGIVTVIKDALIPSGIII
Protein: Large ribosomal subunit protein uL15 (60S ribosomal protein L27a) (E9PLX7)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MPSRLRKTRKLRGHVSHGHGRIGKHRKHPGGRGNAGGLHHHRINFDKYEQTRVNAAKNKTGAAPIIDVVRSGYYKVLGKGKLPKQPVIVKAKFFSRRAEEKIKSVGGACVLVA
Protein: Breast cancer type 2 susceptibility protein homolog (dmbrca2) (Q9W157)
Organism: Drosophila melanogaster (Fruit fly)
Function: Involved in and required for double-strand break repair by meiotic and mitotic homologous recombination. During meiosis, has a dual role in the repair of meiotic double-stranded breaks and the efficient activation of the meiotic recombination checkpoint.
Subcellular location: Nucleus {ECO:0000269|PubMed:17822964}. Note=Brca2 and spn-A/Rad51 become recruited to nuclear foci after DNA damage. {ECO:0000269|PubMed:17822964}.
Interaction partners:
- DNA repair protein Rad51 homolog
- Fanconi anemia group D2 protein homolog
- FI03211p
- Rad51 recombinase D
- DNA repair protein RAD51 homolog 3
- Serine/threonine-protein kinase ATM
- Probable 26S proteasome complex subunit sem1
- Acyl carrier protein, mitochondrial
- Exonuclease 1
- Fanconi anemia group I protein homolog
Sequence:
MDQNGASGSHPNRLSQGRGAHARERGATVSAAANRSNIIDEMAKICEADRQTFAIARRTRGHERLAVDNSDFVAVEDLILSYAEPTPEDQVEMIMSDFCSSPTYAEDEDEPSHESEPWFRFRNKRIRTYSRKRDPKSHKAVQNEKRRGSSGLSVQRDLNTSFTSMACDFDASSQKIHEVLLNLSQYFSATATASGPTPVPSQIDLPTEARQDSGDECFNAELENLRDDLLQSGFTFEASFYENEHEQEGPGTMADTIYGDSMQSVPTTRLRLESGKRNVWSDADSTLKKADVEIAENKKLLMGQTQAKNVDIEENTNFILEGIPLSEWLTPMELPEISKDVIKHIPDKKLKLEPSSQKEQKSSKDSNASKVRGASKQSCDINTKNEGTTILDQPNAAEQENLLNDGELLEEFLFNDWQPMQCSNGPSTSKNAIQGPKENINSINLDDKEQPEKQTPNKSQTISSHQLNGIRKKSFKFIEVSEEMKIKGEEFVDKVVSGLYHFSHKCNLRTEEYSDNHSQVMESTQCAEFKSAPSKPIEILDGKETYNAIAKVDVGEINGKFSPLNNDTIAEPEFCGFRTASNKAIPISEKMKIKTAEFMAEFQSKETIQQNDYLVHQPNDKPTSVGLDTALKRSIESSEEMRSKASKLVVVDTTMREPHQPTLDPVCRDLNESQFFGFRTASNKAIEITEAMEKRGAMFLAQSKATDQLNGWQPSDFPDVLPTSPNNEIHSINVENNKAVNTKTVSETEFFGFRTASNKGIVISENTKIKVAQFMSEFQAADASTDSNQPTVISEESRNIDAKFVDEAAAEDSANKPTFCNVQSLKNTSDIEHFKHDFFVEHSAKEEHPLCSQPLVRTPRRSQEIHSSLSQLAGKSPLDQATKKSVIARRNLLSLKRKRKIILSTETSTSCALPTMERFAPKPSSTSTPLADRDLNRSKDCTKNRQDAEDMSPICMQPKKSRRLGLSRSRY
Protein: Auxin-responsive protein IAA20 (Indoleacetic acid-induced protein 20) (O24410)
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
- Auxin response factor 7
- Auxin-responsive protein IAA33
- Protein TRANSPORT INHIBITOR RESPONSE 1
- Auxin response factor 9
- Auxin transporter protein 1
- Auxin response factor 3
- SAUR-like auxin-responsive protein family
- Auxin response factor 22
- Putative auxin response factor 15
Sequence:
MGRGRSSSSSSIESSSKSNPFGASSSTRNLSTDLRLGLSFGTSSGTQYFNGGYGYSVAAPAVEDAEYVAAVEEEEENECNSVGSFYVKVNMEGVPIGRKIDLMSLNGYRDLIRTLDFMFNASILWAEEEDMCNEKSHVLTYADKEGDWMMVGDVPWEMFLSTVRRLKISRANYHY
Protein: RE70650p (RabX6, isoform A) (Q9W0N7)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MATMRIPKQKVILCGDYGVGKSSLFRRFATNTFITDTDRKSTLGLDHIDREYSVNEKQIKLQLWDTGGMERVASVTSSYYKFAEGAILVFALDNAASFHSLSQHLLDIVTYAENAKIFICGNKSDLDGREPEVSDEEVEAFCEQCHSLISATYKTSCRSGAGVEEMFRDISRQLVHANRSKMELQALEHKSFQVDTASSGAATNEEDASSCGC
Protein: Probable G-protein coupled receptor 142 (G-protein coupled receptor PGR2) (Q7Z601)
Organism: Homo sapiens (Human)
Function: Orphan receptor.
Subcellular location: Cell membrane; Multi-pass membrane protein.
Interaction partners:
- Rhodopsin
Sequence:
MSIMMLPMEQKIQWVPTSLQDITAVLGTEAYTEEDKSMVSHAQKSQHSCLSHSRWLRSPQVTGGSWDLRIRPSKDSSSFRQAQCLRKDPGANNHLESQGVRGTAGDADRELRGPSEKATAGQPRVTLLPTPHVSGLSQEFESHWPEIAERSPCVAGVIPVIYYSVLLGLGLPVSLLTAVALARLATRTRRPSYYYLLALTASDIIIQVVIVFAGFLLQGAVLARQVPQAVVRTANILEFAANHASVWIAILLTVDRYTALCHPLHHRAASSPGRTRRAIAAVLSAALLTGIPFYWWLDMWRDTDSPRTLDEVLKWAHCLTVYFIPCGVFLVTNSAIIHRLRRRGRSGLQPRVGKSTAILLGITTLFTLLWAPRVFVMLYHMYVAPVHRDWRVHLALDVANMVAMLHTAANFGLYCFVSKTFRATVRQVIHDAYLPCTLASQPEGMAAKPVMEPPGLPTGAEV
Protein: Prostacyclin synthase (EC 5.3.99.4) (Hydroperoxy icosatetraenoate dehydratase) (EC 4.2.1.152) (Prostaglandin I2 synthase) (PGIS) (F1RE08)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Function: Catalyzes the isomerization of prostaglandin H2 to prostacyclin (= prostaglandin I2).
Subcellular location: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q29626, ECO:0000255|PIRNR:PIRNR000047}; Single-pass membrane protein {ECO:0000255}.
Interaction partners:
- Prostaglandin E synthase 3b
- Prostaglandin E synthase 3
- Prostaglandin-endoperoxide synthase 2a.
- Prostaglandin-endoperoxide synthase 1.
- Prostaglandin E synthase 2
- Prostaglandin G/H synthase 2
- Lipocalin-type prostaglandin D synthase-like protein
- Thromboxane-A synthase
- Prostaglandin E synthase
- Prostaglandin D2 synthase b, tandem duplicate 2
Sequence:
MMWTALLLVGLSILVIVLYGRRTRRRNEPPLDKGMIPWLGHALEFGKDAAKFLTRMKEKHGDIFTVRAAGLYITVLLDSNCYDAVLSDVASLDQTSYAQVLMKRIFNMILPSHNPESEKKRAEMHFQGASLTQLSNSMQNNLRLLMTPSEMGLKTSEWKKDGLFNLCYSLLFKTGYLTVFGAENNDSAALTQIYEEFRRFDKLLPKLARTTINKEEKQIASAAREKLWKWLTPSGLDRKPREQSWLGSYVKQLQDEGIDAEMQRRAMLLQLWVTQGNAGPAAFWVMGYLLTHPEALRAVREEIQGGKHLRLEERQKNTPVFDSVLWETLRLTAAALITRDVTQDKKIRLSNGQEYHLRRGDRLCVFPFISPQMDPQIHQQPEMFQFDRFLNADRTEKKDFFKNGARVKYPSVPWGTEDNLCPGRHFAVHAIKELVFTILTRFDVELCDKNATVPLVDPSRYGFGILQPAGDLEIRYRIRF
Protein: Probable sulfate permease C3H7.02 (O74377)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: High affinity uptake of sulfate into the cell.
Subcellular location: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
- Probable sulfate permease C869.05c
- Vacuolar basic amino acid transporter vsb1
- GTP-binding protein ypt1
- Sulfate adenylyltransferase
- Putative glutamine amidotransferase PB2B2.05
- Protein isd11
- Adenylyl-sulfate kinase
Sequence:
MSFIKKIKHYFADPADLPQDEAPDSVPGLVPPPSNFVPVYPEPTYSDTVSKKGTIVRVVRHTASKLTKHGDSSQSLSTLPNNDISVGEYVEPLPSVPGWLKQNIFSHFGTRLLHYLRSLFPIMNWLPRYNWNWLVYDFIAGITVGCVVVPQGMSYAKVATLPAQYGLYSSFVGVAIYCIFATSKDVSIGPVAVMSLVTSKVIANVQAKDPNYDAAQIGTTLALLAGAITCGLGLLRLGFIIEFIPVPAVAGFTTGSALNIMAGQVSSLMGYKSRVHTNAATYRVIIQTLQNLPHTKVDAAFGLVSLFILYLVRYTCQHLIKRYTKFQRVFFLTNVLRSAVIIIVGTAISYGVCKHRRENPPISILGTVPSGFRDMGVPVISRKLCADLASELPVSVIVLLLEHISIAKSFGRVNDYKVIPDQELIAMGATNLIGVFFHAYPATGSFSRSAINAKSGVRTPLGGIFTAGVVVLALYCLTGAFYYIPNAVLSAVIIHSVFDLIIPWRQTLLFWRMQPLEALIFICAVFVSVFSSIENGIYTAVCLSAALLLFRIAKPSGSFLGILKIANKFDDDENSIDVVRDIYVPLNQKGMNPNLTVRDPPAGVLIFRLQESFTYPNAGHVNSMLTSKAKTVTRRGNANIYKKASDRPWNDPAPRKKKNAPEVEDTRPLLRAIILDFSAVNHIDTTGVQALVDTRKELEIYAGDEVEFHFTDINNDWIKRTLVAAGFGKARDATKYTSRSIEVGSAAPLRDIETPMAPGNSRIVMPSSVRVRPFDEEEAIESSIPAIVSEDGADSDTISVSDDKDKKVEGHRPSQDPTFSHHEYYPVISTTYPFFHVDVTSAVVDIQYRHVLDVNYKPKIVTNEVENENIEHSDGAA