wanglab/gogpt-training-data huggingface dataset:
Protein: 5-hydroxytryptamine receptor 2B (5-HT-2B) (5-HT2B) (Serotonin receptor 2B) (Q8UUG8)
Organism: Dichotomyctere fluviatilis (Green pufferfish) (Tetraodon fluviatilis)
Function: G-protein coupled receptor for 5-hydroxytryptamine (serotonin). Also functions as a receptor for various ergot alkaloid derivatives and psychoactive substances. Ligand binding causes a conformation change that triggers signaling via guanine nucleotide-binding proteins (G proteins) and modulates the activity of down-stream effectors. Beta-arrestin family members inhibit signaling via G proteins and mediate activation of alternative signaling pathways. Signaling activates a phosphatidylinositol-calcium second messenger system that modulates the activity of phosphatidylinositol 3-kinase and down-stream signaling cascades and promotes the release of Ca(2+) ions from intracellular stores. Plays a role in the regulation of dopamine and 5-hydroxytryptamine release, 5-hydroxytryptamine uptake and in the regulation of extracellular dopamine and 5-hydroxytryptamine levels, and thereby affects neural activity (By similarity).
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:P41595}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P41595}. Synapse, synaptosome {ECO:0000250|UniProtKB:Q02152}.
Interaction partners:
Sequence:
MFQAAVGPLQTNISLPEETPGLELNWAALLIVMVIIPTIGGNILVILAVWLEKKLQNATNFFLMSLAVADLLVGLLVMPIALITILYDSDWPLPEPLCPIWLFLDVLFSTASIMHLCAISLDRYIAIKKPIQHSQYKSRAKVMLKIALVWLISICIAIPIPIKGLRNYPHPNNITFTSNHTCVLKTDTFQEFIIFGSLVAFFIPLTIMMIIYFLTVRVLRKKVYLLRSKVTQRFSYPIISTVFQREQAANPPQPEQPDSTGNSLARIQEKTDTDGMSSPTGDEKSFRRLSTMGKKSMQTLTNEQRASKVLGIVFLLFVVMWCPFFITNITSALCGPCDANIIGRLMEIFSWVGYVSSGINPLVYTLFNKTFRQAFTRYITCNYRNFASKEQGRSFRASTVDRMLTHISPRSSVAENAKLFTKQEIKNETTDYRSPLGCLQPSAQTSTGVVLDKILLTHTENCKQEERVSCV
Protein: Nitroalkane oxidase (NAO) (EC 1.7.3.1) (Q8X1D8)
Organism: Fusarium oxysporum (Fusarium vascular wilt)
Function: Catalyzes the oxidative denitrification of neutral nitroalkanes, including 3-nitro-2-pentanol, 1-nitropropane, 2-nitropropane, nitroethane and nitrocyclohexane, and may thereby protect the organism against toxic compounds. Has no detectable acyl-CoA dehydrogenase activity.
Interaction partners:
Sequence:
MVDFKLSPSQLEARRHAQAFANTVLTKASAEYSTQKDQLSRFQATRPFYREAVRHGLIKAQVPIPLGGTMESLVHESIILEELFAVEPATSITIVATALGLMPVILCDSPSLQEKFLKPFISGEGEPLASLMHSEPNGTANWLQKGGPGLQTTARKVGNEWVISGEKLWPSNSGGWDYKGADLACVVCRVSDDPSKPQDPNVDPATQIAVLLVTRETIANNKKDAYQILGEPELAGHITTSGPHTRFTEFHVPHENLLCTPGLKAQGLVETAFAMSAALVGAMAIGTARAAFEEALVFAKSDTRGGSKHIIEHQSVADKLIDCKIRLETSRLLVWKAVTTLEDEALEWKVKLEMAMQTKIYTTDVAVECVIDAMKAVGMKSYAKDMSFPRLLNEVMCYPLFDGGNIGLRRRQMQRVMALEDYEPWAATYGSSKVDKSRL
Protein: Capsid assembly protease C (EC 3.4.21.-) (Gene product C) (GPC) (Minor capsid protein C) (P03711)
Organism: Escherichia phage lambda (Bacteriophage lambda)
Function: Assembly protease promotes icosahedral procapsid assembly. Autocatalytic cleavage may release the capsid scaffolding protein. The protease domain catalyzes the cleavage of the capsid scaffolding protein after complete procapsid formation. Assembly protease and cleavages products are evicted from the capsid before or during DNA packaging.
Subcellular location: [Isoform Capsid assembly protease C]: Virion. Host cytoplasm.; SUBCELLULAR LOCATION: [Isoform Capsid scaffolding protein Nu3]: Host cytoplasm.
Interaction partners:
Sequence:
MTAELRNLPHIASMAFNEPLMLEPAYARVFFCALAGQLGISSLTDAVSGDSLTAQEALATLALSGDDDGPRQARSYQVMNGIAVLPVSGTLVSRTRALQPYSGMTGYNGIIARLQQAASDPMVDGILLDMDTPGGMVAGAFDCADIIARVRDIKPVWALANDMNCSAGQLLASAASRRLVTQTARTGSIGVMMAHSNYGAALEKQGVEITLIYSGSHKVDGNPYSHLPDDVRETLQSRMDATRQMFAQKVSAYTGLSVQVVLDTEAAVYSGQEAIDAGLADELVNSTDAITVMRDALDARKSRLSGGRMTKETQSTTVSATASQADVTDVVPATEGENASAAQPDVNAQITAAVAAENSRIMGILNCEEAHGREEQARVLAETPGMTVKTARRILAAAPQSAQARSDTALDRLMQGAPAPLAAGNPASDAVNDLLNTPV
Protein: Putative inactive cysteine synthase 2 (Beta-substituted Ala synthase 1;2) (ARAth-Bsas1;2) (O-acetylserine (thiol)-lyase 4) (Q9LJA0)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Cytoplasm {ECO:0000250}.
Interaction partners:
- Assimilatory sulfite reductase
- L-cysteine desulfhydrase
- Probable L-cysteine desulfhydrase, chloroplastic
- Probable cystathionine gamma-synthase 2
- Cystathionine gamma-synthase 1, chloroplastic
- Cystathionine beta-lyase, chloroplastic
- Methionine gamma-lyase
- Serine acetyltransferase 5
- Serine acetyltransferase 3, mitochondrial
- Phosphoserine aminotransferase 1, chloroplastic
Sequence:
MASVAPKIAKDVTELIGNTPLVYLNKVAKDCVGHVAAKLEMMEPCSSVKDRIGYSMIADAEAKGLIKPGESVLIEPTSGNTGVGLAFTAAAKGYKLVITMPASMSIERRIILLAFGAELILTDPAKGMKGAVAKAEEILAKTPNGYMLQQFENPANPKIHYETTGPEIWKGSGGKVDGFVSGIGTGGT
Protein: Cysteine sulfinate desulfinase/cysteine desulfurase and related enzymes (F4IT21)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- Transcription factor SCREAM2
Sequence:
MSSSLPLRLLLPLTTSLISPPPPPPDSFHAPSSFRSKNPNFKRRLSSSSCCSSQSQLFSGRCRSYSRCVTMCLPEHMRNQENTEILTDKDDHIECVLESDEDSGLRIPTQAQAIVEGSGSVAVSELKPAADVDYIQELLAIQQQGPRSIGFFGTRNMGFMHQELIEILSYAMVITKNHIYTSGASGTNAAVIRGALRAERPELLTVILPQSLKKQPPESQELLSKVQNVVEKPHNDHLPLLEASRLCNMDIISQVQQVICFAFHDSKLLMETCQEAKNLRKIVTLFYLD
Protein: Beta-enolase (EC 4.2.1.11) (2-phospho-D-glycerate hydro-lyase) (Phosphopyruvate hydratase) (P07322)
Organism: Gallus gallus (Chicken)
Function: Glycolytic enzyme that catalyzes the conversion of 2-phosphoglycerate to phosphoenolpyruvate.
Subcellular location: Cytoplasm.
Interaction partners:
Sequence:
MSIQKIHAREILDSRGEPTVEVDLHTAKGHFRAAVPSGASTGIHEALEPRDGDKKRFLGKGVLKAVEHINKTIGPALIEKKISVVEQEKIDKVMIEMDGTENKSKFGANAILGVSLAVCKAGAAEKGVPLYRHIADLAGNTELILPVPAFNVINGGSHAGNKLAMQEFMVLPVGAASFHDAMRVGAEVYHSLKGVIKAKYGKDATNVGGEGGFAPNILDNHEALELLKAAIAQAGYTDKVVIGMDVAASEFCRDGRYHLDFKSPPHTKRYITGEQLGEIYRGFIKDYPVVSIEDPFDQDDWEAWKRFVFHVDIQVVGDDLTVTNPKRIAHGAEQHACNCLLLKVNQIGSVTESIQACKLAQSHGWGVMVSHRSGETEDTFIADLVVGLCTGQIKTGAPCRSERLAKYNQLMRIEEALGDKAKFAGRKFRNPKAK
Protein: Large ribosomal subunit protein mL37 (39S ribosomal protein L37, mitochondrial) (L37mt) (MRP-L37) (Q921S7)
Organism: Mus musculus (Mouse)
Subcellular location: Mitochondrion {ECO:0000250|UniProtKB:Q9BZE1}.
Interaction partners:
- Large ribosomal subunit protein uL2m
- Large ribosomal subunit protein mL65
- Large ribosomal subunit protein mL49
- Large ribosomal subunit protein mL50
- Large ribosomal subunit protein mL46
- Large ribosomal subunit protein uL16m
- Large ribosomal subunit protein mL45
- 39S ribosomal protein L40
- Large ribosomal subunit protein uL3m
- Large ribosomal subunit protein mL55
Sequence:
MALASGPALRALAGSGRLGLGGYGTPKRGAYEWGVRSTRKPEPRPLDRVYEIPGLEPITYEGKKHFVPWLARPIFPPWERGWNDPRFHRAAPIHEQTLYKEEPCYIFHQRCRLLEGMKQALWLTKTKLIEGLPKKVLSLVDDPANHIENQEQRVLDIISHARLWHSTEDIPKRETYCPLIVDSLIQLCKSQILKHPSLARRTSAQNCTLATTWNRESLLLQVRGTSSTILSAKDPLPVIASREEVEATRSHVLETFYPISPTIDLQECHVYEVKDDTGFQEGYPYPHPHTLYFLEKANLRPQRFLPEQLRAKMLLFAFANALAQARLLYGNTAKVLEQPIVVQSVGTDGRVFQFLVLQLNTTDLASSEGVKNLVWTDSDQLLYRHFWCRPVIKKKVVVEPVGPVDFQPETFRKFLALYLHGVV
Protein: IP19042p (IP19242p) (IP19348p) (Q9VQ11)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Cathepsin B, isoform A)
- Cathepsin L1
- cathepsin L
- FI04419p
- Cathepsin F
- MIP16848p
- Uncharacterized protein, isoform A
- Femcoat
- IP19005p
- Peptidase A1 domain-containing protein
Sequence:
MQSSPKLALALTLVLIWCLAQSHVESRRWRKSVQLKLHRETNHTKILSSFHNQKLRLKEKLSPTSDLAISSVSVYQTTVSKENLINSHNTEYYVTAGFGTPKSQPVTLLVDTASANLLVYSSEFVKQSCLHHDGYNSSESQTYQANGSPFQIQFASQEILTGILSTDTFTLGDLVIKNQTFAEINSAPTDMCKRSNFDGIIGLGFSEIALNGVETPLDNILEQGLIDEPIFSLYVNRNASDASNGGVLLLGGSDPTLYSGCLTYVPVSKVGFWQITVGQVEIGSKKLCSNCQAIFDMGTSLIIVPCPALKIINKKLGIKETDRKDGVYIIDCKKVSHLPKIVFNIGWKDFTLNPSDYILNYSGTCVSGFSSLSDCNGTQTNDDSEDLNNIWVFGDVFFGAIFTLFDFGLKLVGMAPKV
Protein: G-protein coupled receptor dmsr-1 (Dromyosuppressin receptor related 1) (Q20929)
Organism: Caenorhabditis elegans
Function: G-protein coupled receptor.
Subcellular location: Cell membrane {ECO:0000269|PubMed:28094002}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- FMRFamide-like neuropeptides 13
Sequence:
MEFTECKTTFIHLPDKSFLYDVFVSVYNFYHPIHAYLSIFLCVLGTIANFCNIVVLTRRTMRTPVNMILTAMASCDTVVLFSNLIYTTHYSFVAFKFCHPKHWSYSWALFLIAHAHLSLVAHSSSVWLSVMLALVRYVTLRSRGNMGGMQVTLRHSYYAVAVTVSLVAVLNAPNFLNYKINEQPLNETCTDLDPMFWNSPAYLPGIADIAKANSCLVFRLSYWISGMVFKVLPCALLSLFVWLLLRILREVRENRQRLLKNSQHRPPNQTTTRNGQRLSISVAGNEKLGRNGSLRGRGERVDRTTHMLLAIVAVMLVTELPQGIMAVLSGMCSEEFRIYIYNNLGDILDLFSLCGSCCSFIIYCSMSGQFRNEFHRVFVPAKVRCLRMSSPSIRRPSDAYSTTKMTFLKPNEKNGNGMNGNGTYSEDTRSASVKMVGIQVRRNSTEITRMTGCDSITPCSPMPTSFPSSPLPPIRSGEDESTDETSHLLNSSGPNSTASADGIRGHFQNI
Protein: Fatty acid synthase (EC 1.1.1.100) (EC 1.3.1.39) (EC 2.3.1.41) (EC 2.3.1.85) (EC 3.1.2.14) (Q9VQL7)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MPARFAEEVITAEPAQRAAPQLDLGGGHYVPRQQHLNDEIAITGFSGRLPESSTIEEFKQNLFDGVDMVNDDPRRWERGLYGLPDRIGKLKDSDLENFDQQFFGVHQKQAECMDPLLRMLLELTHEAIIDAGLNPSDLRGSRTGVYIGVSNSETEQHWCSDADRVNGYGLTGCARAMFANRISFTFDFKGPSYSIDTACSSSLYALEQAFSDMREGKVDNALVAGAGLILKPTMSLQFKRLNMLSPDGSCKAFDESGNGYVRSDGCVVLLLQRTSAARRVYASILNVRTNTDGFKEQGITYPIGKMQNRLIRETYEEIGLNPADVVYVEAHGTGTKVGDPQEVNSITDFFCKDRTTPLLIGSVKSNMGHSEPASGVCSVAKILIAMEEGVIPGNLHYNKPNPDLYGLVDGRLKVVDRNLPWNGGIIGLNSFGFGGANAHVILKSNPKPKALTPKDGALKVVLASGRTFEAVEQLLESASTNADDDEYLQLINEIHSKAIPNHFFRGYGVVSSKGTHQREVIESNDDKRPIWYIYSGMGSQWASMAKDLMKIEAFAKTIQRCADVLKPEGVDLIDVLTRSTDKSFENILNSFISIAAMQVALTDLLSSLGIHPDGIVGHSVGELGCAYADGCFTPEQTVLAAYWRGKSILDTQLAKGKMAAVGLSWEDAHSRVPSDCFPVCHNSEDNCTISGPEASIEALVAKLNAEGVFAKAVNSSGYAFHSKYIAEAGPKLRKSLEKIIPNAKNRTARWISTSIPESAWNTPVAKQSSAAYHVNNLLSPVLFHEALQHVPKNAISVEIAPHGLLQAILKRALGPDATNLSLVKRGHENNVEFFLTNVGKLFAAGAQPQVLTLVRPISYPVGRGTPMLNSKVGWDHTQKWLVAKFGKETSSGETIVEVDLSKEDDAFLAGHTIDGRILFPATGYMTLAWQTFAKMQGSEFHKTPVVMENLVFHRATILNKNAVVKFGINFFDGTGAFEICESGSLAVSGKITIPESIDNEELPLEEQTPSAVAKELGTNDVYKELRLRGYDYGGIFRGIVRSDTVASTGKLQWVDNWISFMDTMLQFSILSKNLRELYLPTRIERAVINPAKHFELLSALTKEEQVETGLPVQWYSDINVIKSAGVELRGLKANLAQRRPGTQAPPTLERYQFVPNINTTDLNENSEKARLHALDVAIQVIIENSSGAVKLKGVELANGRNPDVLVANRLLQIIEGEPVLTGDVAVVTSNNNEETITAALGDSGVRVVSKDVLKEPVEQNCHFVFGIDVLSRPDTKTLENSIASIRENGFLILEETLPTYTKTGRALLTKFGFVAVQEQSLGATRVLVLARKAVDLKTRKSVVVVATEQNFNWVDDLKAALATAATEEQYVYVVCQGEELFGAVGLMTCIKNENGGKLARLVFVQDAKAEKFSLTSTLYRQQLEKDLISNVLKNGAWGTFRHLKLETQQATLQVEHAYVNALVKGDLASLKWIEAAQADTAATVDKNLETCTVYYAPINFRDVMLTSGKLAADALPGDLAEQDCVLGLEFAGRDTQGRRVMAMVPAKSLATTCVASKRMMWQIPEKWTMEEASTVPCVYSTVYYALVVRGQMKKGEKILIHAGSGGVGQAAISVALAHGLTVFTTVGSKEKREFLLKRFPKLQERNIGNSRDTSFEQLVLRETKGRGVDLVLNSLSEEKLQASIRCLGLNGRFLEIGKFDLSNNSPLGMSVFLKNTSFHGILLDSVMEGEEEMQNQVVSLVAEGIKTGAVVPLPTSVFNDQQVEQAFRFMASGKHIGKVVIKVRDEEAGKKALQPKPRLINAIPRTYMHPEKSYILVGGLGGFGLELTNWLVTRGARYIVLTSRSGVKTGYQGLMIRRWQERGVKVVIDTSDVTTAAGAKKLLENSNKLALVGGIFNLAAVLRDALIEDQTAKDFKTVADPKVTATKYLDQFSRDICTELDYFICFSSVSCGRGNIGQTNYGLANSAMERICEQRQVSGFPGTAIQWGAIGDTGLVLENLGDNDTVIGGTLPQRMPSCLQTIDLFLQQPHPVVASMVVAEKRKSDQSAGVSLIATIANILGLRDTKNIQDGASLADLGMDSLMSAEIKQTLERNFDIVLSAQEIRQLTFGALKAMDGGADVKPAAAAPAAAAGVPEANITSGGSSRTASPMGDGTQVVFTTSLIPTEAIVQLDTKAPANSKQSPIFFISPIEGFASALEPLAKRLEVPAYGLQYTEAVPSDSLESAAKFFIKQLRTVQPKGPYKLAGYSFGCLLTYVMAGILEETNEVANVIMLDGAPSYVNWYTSSFKQRYTDGTNADNDNQSYGLAYFGIVLANIDYKALVRLLIVIPTWEEKLERFAELMSNEITQPVETIKKSATLFYKKLELADGYQPTLKLKTNVTLVKPTDNSAKLDEDYRLKEVCTKPVEVHTVEGNHRTFLIEDQSLKTIQSILKRLFN
Protein: Cytosolic enolase 3 (EC 4.2.1.11) (2-phospho-D-glycerate hydro-lyase 3) (2-phosphoglycerate dehydratase 3) (Q9ZW34)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Cytoplasm {ECO:0000269|PubMed:19223001}. Nucleus {ECO:0000269|PubMed:19223001}.
Interaction partners:
- 2,3-bisphosphoglycerate-independent phosphoglycerate mutase 1
- Probable 2,3-bisphosphoglycerate-independent phosphoglycerate mutase 2
- Phosphoglycerate mutase-like protein 4
- 2,3-bisphosphoglycerate-dependent phosphoglycerate mutase 1
- 2,3-bisphosphoglycerate-dependent phosphoglycerate mutase 2
- Pyruvate kinase
- Pyruvate kinase
- Pyruvate kinase
- Pyruvate kinase
- Plastidial pyruvate kinase 1, chloroplastic
Sequence:
MSVQEYLDKHMLSRKIEDAVNAAVRAKTSDPVLFIANHLKKAVSSVITKVKARQILDSRGIPTVEVDLHTNKGVFRASVPSGDSSGTYEAIELRDGDKGMYLGNSVAKAVKNINEKISEALIGMDPKLQGQIDQAMIDLDKTEKKSELGANAILAVSIAACKAGAAEKEVPLCKHLSDLSGRANMVLPVPAFTVLSGGKHASNTFAIQEIMILPIGASRFEEALQWGSETYHHLKAVISEKNGGLGCNVGEDGGLAPDISSLKEGLELVKEAINRTGYNDKIKIAIDIAATNFCLGTKYDLDIKSPNKSGQNFKSAEDMIDMYKEICNDYPIVSIEDPFDKEDWEHTKYFSSLGICQVVGDDLLMSNSKRVERAIQESSCNALLLKVNQIGTVTEAIEVVKMARDAQWGVVTSHRCGETEDSFISDLSVGLATGVIKAGAPCRGERTMKYNQLLRIEEELGDQAVYAGEDWKLSL
Protein: Protein BEX3 (Brain-expressed X-linked protein 3 homolog) (rBex3) (Nerve growth factor receptor-associated protein 1) (p75NTR-associated cell death executor) (Q6PDU5)
Organism: Rattus norvegicus (Rat)
Function: May be a signaling adapter molecule involved in p75NTR-mediated apoptosis induced by NGF. Plays a role in zinc-triggered neuronal death.
Subcellular location: Nucleus {ECO:0000250|UniProtKB:Q9WTZ9}. Cytoplasm, cytosol {ECO:0000269|PubMed:15958283}. Note=Shuttles between the cytoplasm and the nucleus. Associates with replicating mitochondria. {ECO:0000250|UniProtKB:Q9WTZ9}.
Interaction partners:
- Tumor necrosis factor receptor superfamily member 16
- 14-3-3 protein epsilon
- Transcription elongation factor A like 9
- Melanoma-associated antigen D1
- Beta-nerve growth factor
- Protein BEX1
Sequence:
MANIHQENEEMEQPLQNGQEDRPVGGGEGHQPAANNNNHNHNHNHNHNHNHNHHRRGQARRLAPNFRWAIPNRQMNDGLGGDGDDMEMFMEEMREIRRKLRELQLRNCLRILMGELSNHHDHHDEFCLMP
Protein: Transketolase (EC 2.2.1.1) (Q4QAC4)
Organism: Leishmania major
Interaction partners:
- Transaldolase
- fructose-bisphosphatase
- Glucose-6-phosphate isomerase
- ribulose-phosphate 3-epimerase
- Ribulose-phosphate 3-epimerase
- Pyruvate kinase
- phosphoglucomutase
- Pyruvate kinase
- Ribokinase
- Triosephosphate isomerase
Sequence:
MAAIEKVANCIRCLAADIVQGGKSGHPGTPMGMAPVSAVLWTEVMKYNSQDPNWVDRDRFIMSNGHGCALHYALLHMAGYDLTMDDLKGFRQYGSRTPGHPERFVTPGVEVTTGPLGQGIANAVGLAMAESHLAATFNRPGHELVNHYTYVYCGDGCLMEGVCQEALSLAGHLALEKLIIIYDSNYICIDGATNLSFTEQSHQKYVAMGFHVIEVENGDTDYDGLRKALAEAKATKGKPKMIVQTTTIGFGSSKQGTEKVHGAPLGEEDIANVKTKFGRDPNKKYDVDEDVRAVFRTHVEKCSAEQRAWEERLAKYTAAFPAEGAAFVAQMKGELPPGWEAKLPTNSSAIATRKASENCLAALFPAIPALMGGSADLTPSNLTRPASANLVDFSSTSQEGRYIRFGVREHAMCAILNGLDAHGGVIPFGGTFLNFIGYALGAVRLAAISHHRVIYVATHDSIGVGEDGPTHQPVELVAALRAMPNLQVIRPSDQTETSGAWAVALSSAHTPTVLCLSRQNTVPQSGSSIEGVKRGAYAVVEVSDPQLVIVASGSEVSLAVDAAKALSGELCVRVVSMPCQELFDAQTDVYRKSVLAEGVPVVSVEAYVSFGWEKYSHAHVGMSGFGASAPAGVLYNKFGITVEEVVETARRLAARFPNGTAPLKNSSFSKM
Protein: Rifin (Q8IFQ3)
Organism: Plasmodium falciparum (isolate 3D7)
Interaction partners:
Sequence:
MKLHYTKILLFFFPLYILVTSYHVYSKNKPSITSHHTQTNRSLCECDTQSSNYDKDTGMKSVMQQFVDRTSQCFEEYDERMNEKRQKSKEQRDKNVQKIIEKDKIEKSLAEKVETGCLKYGCGLGGVAGSVGIFGTVAVKELTKAAITTATELAKEAAKDGAMAATIKAAGAEAGKKFVIAGLGKLHVSTLDNQILESYFATTKYTNVTKIARAINEQYNPSSCLTGGSGADNSICPWAMENFFAARKIPGKVSSTYNSIEVAVKSIVSDAEPVATAAAQQATEEAIKNSIAVVDAKYVICQNAIIASVVALLIIVLIMIIIYLVLRYRRKNKMNKKAHYTKLLKE
Protein: RNA-binding protein 7 (RNA-binding motif protein 7) (Q9CQT2)
Organism: Mus musculus (Mouse)
Function: RNA-binding subunit of the trimeric nuclear exosome targeting (NEXT) complex, a complex that functions as an RNA exosome cofactor that directs a subset of non-coding short-lived RNAs for exosomal degradation. NEXT is involved in surveillance and turnover of aberrant transcripts and non-coding RNAs. Binds preferentially polyuridine sequences and associates with newly synthesized RNAs, including pre-mRNAs and short-lived exosome substrates such as promoter upstream transcripts (PROMPTs), enhancer RNAs (eRNAs), and 3'-extended products from small nuclear RNAs (snRNAs). Participates in several biological processes including DNA damage response (DDR) and stress response. During stress response, activation of the p38MAPK-MK2 pathway decreases RBM7-RNA-binding and subsequently the RNA exosome degradation activities, thereby modulating the turnover of non-coding transcriptome. Participates in DNA damage response (DDR), through its interaction with MEPCE and LARP7, the core subunits of 7SK snRNP complex, that release the positive transcription elongation factor b (P-TEFb) complex from the 7SK snRNP. In turn, activation of P-TEFb complex induces the transcription of P-TEFb-dependent DDR genes to promote cell viability.
Subcellular location: Nucleus, nucleoplasm {ECO:0000250|UniProtKB:Q9Y580}. Nucleus {ECO:0000269|PubMed:25525152}. Note=Excluded from the nucleolus. {ECO:0000250|UniProtKB:Q9Y580}.
Interaction partners:
- Zinc finger CCHC domain-containing protein 8
- Exosome RNA helicase MTR4
- ATP-dependent RNA helicase A
- Serrate RNA effector molecule homolog
- Exosome complex component RRP43
- RNA-binding protein 25
- Exosome complex component RRP40
- RNA-binding protein 39
- Probable ATP-dependent RNA helicase DDX5
- Serine/arginine repetitive matrix protein 2
Sequence:
MGAAAAEADRTLFVGNLETKVTEELLFELFHQAGPVIKVKIPKDKDGKLKQFAFVNFKHEVSVPYAMNLLNGIKLFGRPIKIQFRSGSSHASQDASVSYPQHHVGNLSPTSTSPNSYERTVGNVSPTAQMVQRSFSSPEDYQRQAVMNSVFRQMSYAGKFGSPHADQLGFSPSAQPHGHTFNQSSSSQWRQDALSSQRKRQNSHPYLADRHYSREQRYSDHGSDYHYRGSREDFYYDDRNHDGWSHDYDNRRDSSRGGKWPSSRH
Protein: Chromodomain helicase DNA binding protein 3 (B0QZH7)
Organism: Mus musculus (Mouse)
Interaction partners:
Sequence:
LKIKLGLLGGKRKKAGSSEEGHEPEAEESDLDSGSVHSASGWPDGPVRAKKLKRGRPGRKKKKVLGCPAVTGEEEVDGYETDHQDYCEVCQQGGEIILCDTCPRAYHLVCLDPELDRAPEGKWSCPHCEKEGVQWEAKEEEEEYEEEGEEG
Protein: Carotenoid 3,4-desaturase (EC 1.3.99.37) (1-hydroxy-2-isopentenylcarotenoid 3,4-desaturase) (A0A0A1GKA2)
Organism: Haloarcula japonica (strain ATCC 49778 / DSM 6131 / JCM 7785 / NBRC 101032 / NCIMB 13157 / TR-1)
Function: Involved in the biosynthesis of the acyclic C50 carotenoid bacterioruberin (BR). CrtD is involved in the desaturation reactions that form double bonds at C-3,4 of dihydroisopentenyldehydrorhodopin (DH-IDR) and C-3',4' of dihydrobisanhydrobacterioruberin (DH-BABR) to yield isopentenyld ehydrorhodopin (IDR) and bisanhydrobacterioruberin (BABR), respectively.
Interaction partners:
Sequence:
MSDLSGEDVTVVGGGIGGLSAACYLADAGADVSLLEKNEQLGGRASRLEVDGFRFDMGPSWYLMPDVFERFFAYFGKEPRDYYDLQRLDPHYRIFFKDGDQIDVTGDNDEMAQKFEEYEPGAGEAFEEYLSTSERHYETAMNKFVYQDRSELRDWVDLDVMTAAPVGLQLIGTMQSHVEDYFEHPKLQQIMQYTLVFLGGSPRTTPALYNMMSHVDFNLGVYYPDGGVGAVVDGLVELGEELGVTYETDAEVEEISRRKEGFLVETVHGDTTHPDEVVVNADYAHAERELLPDHERQYDDDYWDDKTYAPSAFLMYMGVEGDVEPLEHHTLVLPTDWDPHFDDIFDEPAWPDDPAYYLCVPSKTDDSVAPDGHSNLFVLVPIAPGLHDGDEIRQEYREKVLADIADNTGVDLRDRIVYEKQFAVSDFGERYNATEGTALGLAHTLRQTALLRPNNRSSAVDGLYFTGSFTTPGIGVPMCLISGEHTAEALIEDIA
Protein: Peroxiredoxin-5 (EC 1.11.1.24) (Q960M4)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Thioredoxin-dependent peroxide reductase, mitochondrial
- Thioredoxin-2
- Peroxiredoxin 2
- Ubiquitin-related modifier 1 homolog
- Glutathione peroxidase
- Glutathione peroxidase
- GEO01508p1
- thioredoxin-dependent peroxiredoxin
- thioredoxin-dependent peroxiredoxin
- E3 ubiquitin-protein ligase ariadne-1
Sequence:
MRVLSCKFLGRVVNSALPQQIISLRSLSKTSAAMVKVGDSLPSVDLFEDSPANKINTGDLVNGKKVIIFGVPGAFTPGCSKTHLPGYVSSADELKSKQGVDEIVCVSVNDPFVMSAWGKEHGAAGKVRLLADPAGGFTKALDVTIDLPPLGGVRSKRYSLVVENGKVTELNVEPDGTGLSCSLANNIGKK
Protein: Alpha-(1,6)-fucosyltransferase (Alpha1-6FucT) (EC 2.4.1.68) (Fucosyltransferase 8) (GDP-L-Fuc:N-acetyl-beta-D-glucosaminide alpha1,6-fucosyltransferase) (GDP-fucose--glycoprotein fucosyltransferase) (Glycoprotein 6-alpha-L-fucosyltransferase) (G5EFE7)
Organism: Caenorhabditis elegans
Function: Catalyzes the addition of fucose in alpha 1-6 linkage to the first GlcNAc residue, next to the peptide chains in N-glycans. The addition is prevented if the GlcNAc residue is already fucosylated. Involved in susceptibility to the nematotoxic C.cinerea galectin Cgl2, likely by contributing to the synthesis of core alpha-1,6-fucosylated N-glycans to which Cgl2 binds.
Subcellular location: Golgi apparatus, Golgi stack membrane {ECO:0000255|PIRNR:PIRNR000472}; Single-pass type II membrane protein {ECO:0000305}. Note=Membrane-bound form in trans cisternae of Golgi. {ECO:0000305}.
Interaction partners:
- Beta-1,4-galactosyltransferase galt-1
- Fucosyltransferase
- Alpha-mannosidase
- Alpha-1,6-mannosyl-glycoprotein 2-beta-N-acetylglucosaminyltransferase
- Beta-1,4-N-acetylgalactosaminyltransferase bre-4
- Alpha-
- Alpha-
- beta-N-acetylhexosaminidase
- beta-N-acetylhexosaminidase
- GDP-fucose transporter
Sequence:
MLKCIAAVGTVVWMTMFLFLYSQLSNNQSGGDSIRAWRQTKEAIDKLQEQNEDLKSILEKERQERNDQHKKIMEQSHQLPPNPENPSLPKPEPVKEIISKPSILGPVQQEVQKRMLDDRIREMFYLLHSQTIENSTKILLETQMISLMGLSAQLEKLEGSEEERFKQRTAITQRIFKSIEKLQNPKACSEAKTLVCNLDKECGFGCQLHHVTYCAITAFATQRMMVLKRDGSSWKYSSHGWTSVFKKLSKCSFDEAVGNTEAKPFAEPSPARVVSLGIVDSLITKPTFLPQAVPEQLLESLTSLHSHPPAFFVGTFISYLMRFNSATQEKLDKALKSIPLDKGPIVGLQIRRTDKVGTEAAFHALKEYMEWTEIWFKVEEKRQGKPLERRIFIASDDPTVVPEAKNDYPNYEVYGSTEIAKTAQLNNRYTDASLMGVITDIYILSKVNYLVCTFSSQVCRMGYELRQPSGADDGSKFHSLDDIYYFGGQQAHEVIVIEDHIAQNNKEIDLKVGDKVGIAGNHWNGYSKGTNRQTYKEGVFPSYKVVNDWRKFKFEALLD
Protein: Exo-poly-alpha-D-galacturonosidase (EC 3.2.1.82) (E0SKR2)
Organism: Dickeya dadantii (strain 3937) (Erwinia chrysanthemi (strain 3937))
Interaction partners:
- Pectinesterase A
- Pectin acetylesterase
- Xylosidase/arabinosidase
- 4-deoxy-L-threo-5-hexosulose-uronate ketol-isomerase
Sequence:
MKAIRLSQCHALALTATVCLFTSQALAMPTNEQTPPALEALTPSLDNHSVVLVWKAPEDTSDIIDYQIYQDNQFVGLASQNSNQHSPAQPYINMFYKNDTGNFQHRIVIQSAKIDGLQPSTDYHFTVRAVYTDSSVTADSNTVDITTTAVPQIIDITRYGAKGNGTTLNTSAIQKAIDACPSGCQVNVPAGVFKTGALWLKSNMTLNLSPGATLLGSENAADYPGGYTIGKSSTDMRPASLLNVTDKTSSKGGVFQNIRITGKGAIDGSGWKRSADGQDELGNKLPQYVKSDNANVNNDGILAKNQVAAARAKGIDLKTAYRQYRSSLITLRGANNVYIADITIRNPADHGIVFMKSQNVIENGVIHQTFDANNGDGVEFSNSQDITVLNSVFDTGDDCINFAAGLGQEGQKQSPTQNARLFNNYFRHGHGAIVMGSHTAATIANILAENNVMNKTDIGLRAKSSPDIGGGAHHVVFRNNAMANLAMQAVFVTLNYVDVNGSGVYTPADVPAHFYDFTVKNITVLNSADISPSIQIEGNSNKQVWNSNFNFCDMKLSGIMPASVSDLEDSEFNNIAFSDLRGGTSPWKFGAVKNVTLDGKIVSPNP
Protein: Inositol monophosphatase 1 (IMP 1) (IMPase 1) (EC 3.1.3.25) (D-galactose 1-phosphate phosphatase) (EC 3.1.3.94) (Inositol-1(or 4)-monophosphatase 1) (Lithium-sensitive myo-inositol monophosphatase A1) (P97697)
Organism: Rattus norvegicus (Rat)
Function: Responsible for the provision of inositol required for synthesis of phosphatidylinositol and polyphosphoinositides and has been implicated as the pharmacological target for lithium action in brain. Has broad substrate specificity and can use myo-inositol 1,3-diphosphate, myo-inositol 1,4-diphosphate, scyllo-inositol-phosphate, glucose-1-phosphate, glucose-6-phosphate, fructose-1-phosphate, beta-glycerophosphate, and 2'-AMP as substrates (By similarity). Is equally active with myo-inositol monophosphate and D-galactose 1-phosphate.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:P29218}.
Interaction partners:
- Inositol-3-phosphate synthase 1
- Inositol oxygenase
- Inositol monophosphatase 2
- Inositol polyphosphate-1-phosphatase.
- CDP-diacylglycerol--inositol 3-phosphatidyltransferase
- Myotubularin
- Inositol polyphosphate-4-phosphatase type I A
- Type II inositol 3,4-bisphosphate 4-phosphatase
- Transcription termination factor 2
- Glucose-6-phosphate isomerase
Sequence:
MADPWQECMDYAVILARQAGEMIREALKNKMDVMIKSSPADLVTVTDQKVEKMLMSSIKEKYPYHSFIGEESVASGEKTVFTEQPTWIIDPIDGTTNFVHRFPFVAVSIGFVVNKEMEFGVVYSCVEDKMYTGRKGKGAFCNGQKLRVSQQEDITKSLLVTELGSSRKPETLRIVLSNMERLCSIPIHGIRSVGTAAVNMCLVATGGADAYYEMGIHCWDMAGAGIIVIEAGGVLLDVTGGPFDLMSRRIIAASNIALAERIAKELEIIPLQRDDES
Protein: Inner membrane protein YbaN (P0AAR5)
Organism: Escherichia coli (strain K12)
Subcellular location: Cell inner membrane; Multi-pass membrane protein.
Interaction partners:
- Uncharacterized protein YncE
- Uncharacterized protein YdiE
- Biopolymer transport protein ExbB
- NADPH-dependent ferric-chelate reductase
Sequence:
MQRIILIIIGWLAVVLGTLGVVLPVLPTTPFILLAAWCFARSSPRFHAWLLYRSWFGSYLRFWQKHHAMPRGVKPRAILLILLTFAISLWFVQMPWVRIMLLVILACLLFYMWRIPVIDEKQEKH