wanglab/gogpt-training-data huggingface dataset:
Protein: Divisome-associated membrane protein Blr (Beta-lactam resistance protein) (P56976)
Organism: Escherichia coli (strain K12)
Function: Component of the cell division machinery, which is probably involved in the stabilization of the divisome under certain stress conditions.
Subcellular location: Cell inner membrane {ECO:0000269|PubMed:10931331, ECO:0000269|PubMed:22885295}; Single-pass membrane protein {ECO:0000269|PubMed:10931331, ECO:0000269|PubMed:22885295}. Note=Localizes to the division septum. Localization requires FtsQ and FtsN.
Interaction partners:
- Inner membrane protein YmgF
- Uncharacterized oxidoreductase YdgJ
Sequence:
MNRLIELTGWIVLVVSVILLGVASHIDNYQPPEQSASVQHK
Protein: tRNA wybutosine-synthesizing protein 4 (EC 2.1.1.290) (EC 2.3.1.231) (Leucine carboxyl methyltransferase 2) (tRNA(Phe) (7-(3-amino-3-(methoxycarbonyl)propyl)wyosine(37)-N)-methoxycarbonyltransferase) (tRNA(Phe) (7-(3-amino-3-carboxypropyl)wyosine(37)-O)-methyltransferase) (Q38DD6)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MFPPSLCSCSLRAVSSSHTPALGLIISTQLRVVARNKAVATSQNTLMSIAVEESSVSTDAAVQRTNDDSVVSKRSAVHKGYFDDPYLRFFVKKLSRRSPLINRGYYLRMLVITDVIERCIHHLRCLKIRCTVNTPPLPPTGNAVALPVQVISLGAGYDTLAMRLKQRPDYGNVHFYEVDFPAVMQSKSMLVKMAPFGSFPEDIVADPGGELVKLYGNNYWAVGTDLRSTNRDLVTCLREVSPQFSTDNPTVLYAECVMQYMPPVAASHLIKQIASAFPCAIFVAYDQLHPSDSFGTVMLSALRTKNSPLLSIGECPSGAAMVRRAIQQGMCKARFANFHDLSKFYISGDNHDRVEALEPFDEWEEWCEMCEHYGITMATTLSDEEMPDHSCFKEIMEQKEEELCAGLPCKSQGNEQNALRLENWPTGRFGFEGWGNGGAVAERLFSGDVLIISFGGFSVTRGHQRTNTLHVHSLRSGDRKVLQSSLSVEPPSLVFHSMSRVSRGSYVVFGGRTNPQDVASDAYLLRLELPTDGYGEEANIVATWSKLQQTADDGKLPVARYRHAATSVTNSGCDENTDMRNIFVFGGRCATGEFLNDAWLGSVGDGIIHWKLLRLSGDIPPPCCSSGVVDATMGSIVLLSGGLLRGGVSDSSLWSIDWVTGVCNKRDAIVGPRFSHTMCRVSVNGVTGVLVVGGSSTEPSASFQATQILLLDPVSGEITEALKLPPMCPTWTRHSCVALEDGAVGVLGSGFTCFSFGTFATKPLLLLLGGKRGGRNAHSWDVSKLESTSTSAAANAFSICCTVQRRPVEEQSLSVGSFSVLVNHPFKPVVFRDVDMGCCVKAWSDPAYLNRVEGNTRVSVHVARNTELLDFVTKNFSFQHVSFNELLDHCLASSAALAESGNLPGKLNEERETWYLRAVASNMKSERANIWRDFQGLKDDFVLPSATVDHIKPRMHQACLRISAPPLQLWTHYDTLDNVLCQIVGRKRVVLFPPSEYNNLYISGSSSAVTNIDKPDYMRFPRFIDASRHALEVEIGPGDMLFIPALWFHHITTLEGSYSMSVNVFFERLPHADYDKKDLYGNKDIPAASRLRAGIVKKVKEMISETAVERTSDGKALTPDLVEFALRQALQDLMEVADDMCTALR
Protein: Tubulin-specific chaperone D (Beta-tubulin cofactor D) (Tubulin-folding cofactor D) (Q28205)
Organism: Bos taurus (Bovine)
Function: Tubulin-folding protein implicated in the first step of the tubulin folding pathway and required for tubulin complex assembly. Involved in the regulation of microtubule polymerization or depolymerization, it modulates microtubule dynamics by capturing GTP-bound beta-tubulin (TUBB). Its ability to interact with beta tubulin is regulated via its interaction with ARL2. Acts as a GTPase-activating protein (GAP) for ARL2. Induces microtubule disruption in absence of ARL2. Increases degradation of beta tubulin, when overexpressed in polarized cells. Promotes epithelial cell detachment, a process antagonized by ARL2. Induces tight adherens and tight junctions disassembly at the lateral cell membrane. Required for correct assembly and maintenance of the mitotic spindle, and proper progression of mitosis. Involved in neuron morphogenesis.
Subcellular location: Cell junction, tight junction {ECO:0000269|PubMed:17704193}. Lateral cell membrane {ECO:0000269|PubMed:17704193}. Cytoplasm {ECO:0000269|PubMed:17704193}. Cell junction, adherens junction {ECO:0000269|PubMed:17704193}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250|UniProtKB:Q9BTW9}. Note=Localized in cell-cell contacts. {ECO:0000269|PubMed:17704193}.
Interaction partners:
- Tubulin-specific chaperone E
- ADP-ribosylation factor-like protein 2
- Tubulin-folding cofactor B
- Tubulin-specific chaperone C
- ADP ribosylation factor like GTPase 13A
- Tubulin-specific chaperone cofactor E-like protein
- Tubulin-specific chaperone A
- Small ArfGAP 1
- ADP-ribosylation factor-like protein 3
Sequence:
MALSEEPAAGAAEDPVEDPVEDAGEDAALACGAALESFGESAETRELLGHLPAVLADRSAREGALERFRVIMDKYQEQPHLLDPHLEWMLNLLLEFVQNKTSPADLVHLAFKFLYIISKVRGYKTFLRLFPHEVADVQPVLDMFTNQNPKDHETWETRYMLLLWLSVTCLIPFDFSRLDGNLSQPGQERASTMDRILQVAESYLVVSDKARDAAAVLVSKFVTRPDVKQKKMASFLDWSLCTLARSSFQTIEGVIAMDGTLQALAQIFKHGKREDCLPYAATVLQCLDSCRLPDSNQTLLRKLGVKLVQRLGLTFLKPQVAKWRYQRGCRSLAESLQHSIQNPREPVTQAETPDSDGQDDVPEEVESVIEQLLVGLKDKDTIVRWSAAKGIGRMAGRLPKELADDVTGSVLDCFSFQETDSAWHGGCLALAELGRRGLLLPSRLSDVVPVILRALTYEEKRGACSVGSNVRDAACYVCWAFARAYEPQELKPFVAAISSALVIATVFDRDVNCRRAASAAFQENVGRQGTFPHGIDILTTADYFAVGNRSNCFLVISMFIAGFPEYTQPMIEHLVTMKVGHWDGTIRELSAKALRNLAQRAPEHTAREVFPRLLSMTQSPDLHTRHGAVLACAEVARSLHTLATQQGRPVSDFLDEKAMHGLKQIHQQLYDRQLYRGLGGELMRQAVCILIENVALSKMPFRGDAVIDGWQWLINDTLKNLHLISSHSRQHIKEAAVSALAALCSEYHAQEPGEAEAAAQEELVKLYLAELQSPEEMTRCGCALALGALPAFFLKGRLRQVLAGLRAVTHISPKDVSFAEARRDALKAISRICQTVGVRAEGPPDEAVCRENVSQIYCTLLDCLKDYTTDSRGDVGAWVREAAMTSLMDLTLLLGRNQPELIEAPLCQQLMCCLAQQASEKIDRFRAHAARVFLALLHADSPAIPHVPARPELERLFPRAAVASVNWGAPSQAFPRMARLLGLPAYRYHVLLGLAVSVGGLTESTVRYSTQGLFEYMKEIQNDPAALEDFGGTLLQVFEDNLLNDRVSVPLLKTLDQMLANGCFDIFTAQENHPFCVKLLALCKEEIKKSKDVQKLRSSIAVFCGLVQFPGDVRRKVLLQLFLLLCHPFPVIRKNTASQVYEMVLTYDVVPTAVLDEVMAVLSSTAWDAELPVVRAQRNRLCDLLGVPRPQLVPKPAVR
Protein: Polymerase basic protein 2 (RNA-directed RNA polymerase subunit P3) (P03428)
Organism: Influenza A virus (strain A/Puerto Rico/8/1934 H1N1)
Function: Plays an essential role in transcription initiation and cap-stealing mechanism, in which cellular capped pre-mRNAs are used to generate primers for viral transcription. Recognizes and binds the 7-methylguanosine-containing cap of the target pre-RNA which is subsequently cleaved after 10-13 nucleotides by the viral protein PA. Plays a role in the initiation of the viral genome replication and modulates the activity of the ribonucleoprotein (RNP) complex. In addition, participates in the inhibition of type I interferon induction through interaction with and inhibition of the host mitochondrial antiviral signaling protein MAVS.
Subcellular location: Virion {ECO:0000255|HAMAP-Rule:MF_04062}. Host nucleus {ECO:0000255|HAMAP-Rule:MF_04062, ECO:0000269|PubMed:15308710, ECO:0000269|PubMed:20538852}. Host mitochondrion {ECO:0000255|HAMAP-Rule:MF_04062, ECO:0000269|PubMed:15308710, ECO:0000269|PubMed:16242167, ECO:0000269|PubMed:20538852}.
Interaction partners:
Sequence:
MERIKELRNLMSQSRTREILTKTTVDHMAIIKKYTSGRQEKNPALRMKWMMAMKYPITADKRITEMIPERNEQGQTLWSKMNDAGSDRVMVSPLAVTWWNRNGPITNTVHYPKIYKTYFERVERLKHGTFGPVHFRNQVKIRRRVDINPGHADLSAKEAQDVIMEVVFPNEVGARILTSESQLTITKEKKEELQDCKISPLMVAYMLERELVRKTRFLPVAGGTSSVYIEVLHLTQGTCWEQMYTPGGEVRNDDVDQSLIIAARNIVRRAAVSADPLASLLEMCHSTQIGGIRMVDILRQNPTEEQAVDICKAAMGLRISSSFSFGGFTFKRTSGSSVKREEEVLTGNLQTLKIRVHEGYEEFTMVGRRATAILRKATRRLIQLIVSGRDEQSIAEAIIVAMVFSQEDCMIKAVRGDLNFVNRANQRLNPMHQLLRHFQKDAKVLFQNWGVEPIDNVMGMIGILPDMTPSIEMSMRGVRISKMGVDEYSSTERVVVSIDRFLRIRDQRGNVLLSPEEVSETQGTEKLTITYSSSMMWEINGPESVLVNTYQWIIRNWETVKIQWSQNPTMLYNKMEFEPFQSLVPKAIRGQYSGFVRTLFQQMRDVLGTFDTAQIIKLLPFAAAPPKQSRMQFSSFTVNVRGSGMRILVRGNSPVFNYNKATKRLTVLGKDAGTLTEDPDEGTAGVESAVLRGFLILGKEDKRYGPALSINELSNLAKGEKANVLIGQGDVVLVMKRKRDSSILTDSQTATKRIRMAIN
Protein: Aspartate--tRNA ligase, mitochondrial (EC 6.1.1.12) (Aspartyl-tRNA synthetase) (AspRS) (P15179)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Catalyzes the attachment of aspartate to tRNA(Asp) in the mitochondrion.
Subcellular location: Mitochondrion matrix {ECO:0000305|PubMed:2668951}.
Interaction partners:
- Glutamyl-tRNA
- Aspartate--tRNA ligase, cytoplasmic
- Valine--tRNA ligase, mitochondrial
- Tyrosine--tRNA ligase, mitochondrial
- Histidine--tRNA ligase, mitochondrial
- Glutamyl-tRNA
- Glutamate--tRNA ligase, mitochondrial
- eIF-2-alpha kinase GCN2
- Leucine--tRNA ligase, mitochondrial
- Alanine--tRNA ligase, mitochondrial
Sequence:
MLARSRVCLQTITRRLADFPEANAIKKKFLFRKDTSTIKQLKGLSSGQKIVLNGWIEQKPKRVGKNLIFGLLRDSNGDIIQLVDNKSLLKGFTLEDVVQAVGILSLKRKLSNEDADEYEVQLEDITVLNASNKKPAQMQDFKLSAIYPPEFRYLQLRNPKYQDFLKKRSSISKEIRNSFNNFDFTEVETPMLFKATPEGAREFLVPTRTKRSDGKPSFYALDQSPQQYKQLLMASGVNKYYQMARCFRDEDLRADRQPEFTQVDMEMAFANSEDVMKIIEKTVSGVWSKFSKKRGLLTLDSKGTLVPAKKENGTVSIFRMTYEQAMTSYGIDKPDLRAPDLKIINLGEFNAFSHLNKKFPVFEVIILRSAFSNMEEYKERWSFLTNNSNYNYRVPIVLPIENDEQANSNWFENFHAIATFENPHLITKFLKLKKGDIVCGCTREPNHSIFENPTPLGRLRQLVLQSEHGKNIYHAVNKDVASWIVDFPLFSPVIIEDKSGKKEKLAYPEYEKDRLCSTHHPFTMVKLKDYEKLEKTPEKCLGRHYDLVVNGVELGGGSTRIHDPRLQDYIFEDILKIDNAYELFGHLLNAFDMGTPPHAGFAIGFDRMCAMICETESIRDVIAFPKSITGADLVVKSPSVIPESILEPYNIKYSNSKK
Protein: Probably inactive leucine-rich repeat receptor-like protein kinase At5g48380 (Q9ASS4)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Cell membrane {ECO:0000269|PubMed:14506206, ECO:0000305|PubMed:17644812}; Single-pass type I membrane protein {ECO:0000269|PubMed:14506206, ECO:0000305|PubMed:17644812}.
Interaction partners:
- BRASSINOSTEROID INSENSITIVE 1-associated receptor kinase 1
- Protein BONZAI 1
- Guanine nucleotide-binding protein subunit gamma 1
- Guanine nucleotide-binding protein alpha-1 subunit
- Guanine nucleotide-binding protein subunit gamma 2
- Extra-large guanine nucleotide-binding protein 2
- Guanine nucleotide-binding protein subunit beta
- Lipase-like PAD4
- Somatic embryogenesis receptor kinase 4
- Stromal cell-derived factor 2-like protein
Sequence:
MMMGRLVFVIWLYNCLCLLLLSSLVDADQANIDCLRTFKSQVEDPNRYLSTWVFGNETAGYICKFSGVTCWHDDENRVLSIKLSGYGLRGVFPPAVKLCADLTGLDLSRNNFSGPLPANISTLIPLVTILDLSYNSFSGEIPMLISNITFLNTLMLQHNQFTGTLPPQLAQLGRLKTFSVSDNRLVGPIPNFNQTLQFKQELFANNLDLCGKPLDDCKSASSSRGKVVIIAAVGGLTAAALVVGVVLFFYFRKLGAVRKKQDDPEGNRWAKSLKGQKGVKVFMFKKSVSKMKLSDLMKATEEFKKDNIIATGRTGTMYKGRLEDGSLLMIKRLQDSQRSEKEFDAEMKTLGSVKNRNLVPLLGYCVANKERLLMYEYMANGYLYDQLHPADEESFKPLDWPSRLKIAIGTAKGLAWLHHSCNPRIIHRNISSKCILLTAEFEPKISDFGLARLMNPIDTHLSTFVNGEFGDFGYVAPEYSRTMVATPKGDVYSFGVVLLELVTGQKATSVTKVSEEKAEEENFKGNLVEWITKLSSESKLQEAIDRSLLGNGVDDEIFKVLKVACNCVLPEIAKQRPTMFEVYQLLRAIGESYNFTADDDILIPSESGEGDFIEELIVAR
Protein: Regulator of G-protein signaling 9 (RGS9) (O46469)
Organism: Bos taurus (Bovine)
Function: Inhibits signal transduction by increasing the GTPase activity of G protein alpha subunits thereby driving them into their inactive GDP-bound form. Binds to GNAT1. Involved in phototransduction; key element in the recovery phase of visual transduction.
Subcellular location: Membrane; Peripheral membrane protein. Note=Targeted to the membrane via its interaction with RGS9BP. {ECO:0000250}.
Interaction partners:
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein subunit beta-5
- Regulator of G-protein signaling 9-binding protein
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein G
- Guanine nucleotide binding protein
- Guanine nucleotide-binding protein G
- Retinal rod rhodopsin-sensitive cGMP 3',5'-cyclic phosphodiesterase subunit gamma
Sequence:
MTIRHQGQQYRPRMAFLRKIEALVKDMQDPDTGVRVQNQKVKVVSIPHAMTGSDVLQWISQRLWISGLEAQNLGNFIVKYGYIYPLQDPRNLTLKPDSSLYRFQTPYFWPTQQWPAEDVDYAIYLAKRNIKKKGILEEYEKENYNFLNKKINYKWDFVIMQAREQYRAGKERNKVDRCALDCQEKAYWLVHRCPPGANNVLDYGLDRVTNPNEDQKQTVVSVRKEIMYYRQALMRSTVKSSVSLGGIVKYSEQFSSNDAIMSGCLPSNPWITDDTQFWDLNAKLVDIPTKMRVERWAFNFSELIRDPKGRQSFQHFLRKEFSGENLGFWEACEDLKYGDQSKVKEKAEEIYKLFLAPGARRWINIDGKTMDITVKGLKHPHRYVLDAAQTHIYMLMKKDSYARYLKSPIYKEMLAKAIEPQGTTRKSSSLPFMRRHLRSSPSPVILRQLEEEAKAREAATTVDITQVMSKLDRRSQLRKEPPPK
Protein: Putative major capsid protein (H9C196)
Organism: Pectobacterium phage ZF40 (Bacteriophage ZF40)
Interaction partners:
Sequence:
MAKSVFDVSPVSALSFLVNQAAHIESEIYRIEYPQFKYGTLLPLDNSAPDWAQAVMFRSIDARGELQLFGPNSTDVPTVDIAMSQGFKDINTAALGYTYSIEEIGFAMLNNVNLDAERGQAVRDVVEQGLNKIYLLGDKGVGEGLYTSPNVSVEAATSTFVALVAAIPTNGTQPIIDFFGNAYNTVYLDNTLTVHRPNTFVLPPAQFQLLARTLLSTQNASNVTLLQFLRTNFPDITFEDDILLKGAGVAGADRMAVYKKEIRIVKGHDVMPLRFLAPATADNVNFKVPAILRTGGTEWRIPKAGHYVDGV
Protein: Aryl-hydrocarbon-interacting protein-like 1 (Q9NZN9)
Organism: Homo sapiens (Human)
Function: May be important in protein trafficking and/or protein folding and stabilization.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:12374762}. Nucleus {ECO:0000269|PubMed:12374762}.
Interaction partners:
- NEDD8 ultimate buster 1
- Retinal guanylyl cyclase 1
- X-linked retinitis pigmentosa GTPase regulator-interacting protein 1
- Spermatogenesis-associated protein 7
- Cone-rod homeobox protein
- Tubby-related protein 1
- AH receptor-interacting protein
- Retinoid isomerohydrolase
- Retinol dehydrogenase 12
- Lecithin retinol acyltransferase
Sequence:
MDAALLLNVEGVKKTILHGGTGELPNFITGSRVIFHFRTMKCDEERTVIDDSRQVGQPMHIIIGNMFKLEVWEILLTSMRVHEVAEFWCDTIHTGVYPILSRSLRQMAQGKDPTEWHVHTCGLANMFAYHTLGYEDLDELQKEPQPLVFVIELLQVDAPSDYQRETWNLSNHEKMKAVPVLHGEGNRLFKLGRYEEASSKYQEAIICLRNLQTKEKPWEVQWLKLEKMINTLILNYCQCLLKKEEYYEVLEHTSDILRHHPGIVKAYYVRARAHAEVWNEAEAKADLQKVLELEPSMQKAVRRELRLLENRMAEKQEEERLRCRNMLSQGATQPPAEPPTEPPAQSSTEPPAEPPTAPSAELSAGPPAEPATEPPPSPGHSLQH
Protein: Chloride channel protein 1 (ClC-1) (Chloride channel protein, skeletal muscle) (Q64347)
Organism: Mus musculus (Mouse)
Function: Voltage-gated chloride channel (By similarity). Plays an important role in membrane repolarization in skeletal muscle cells after muscle contraction (Probable).
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:P35523}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P35523}. Cell membrane, sarcolemma {ECO:0000269|PubMed:18008009, ECO:0000269|PubMed:21078869, ECO:0000305|PubMed:21149546}; Multi-pass membrane protein {ECO:0000255}. Cell membrane, sarcolemma, T-tubule {ECO:0000305|PubMed:21149546}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- CUGBP Elav-like family member 1
- Muscleblind-like protein 1
- Muscleblind-like protein 2
- Sodium channel protein type 4 subunit alpha
- Muscleblind-like protein 3
- Sarcoplasmic/endoplasmic reticulum calcium ATPase 1
- Barttin
- Myotonin-protein kinase
- Voltage-dependent L-type calcium channel subunit alpha-1S
Sequence:
MERSQSQRHGGEQSWWGSAPQYQYMPFEHCTSYGLPSENGGLQHRPRKDMGPRHNAHPTQIYGHQKEQYSYKAQDGGMPKKMGSSSTMDSLDEDHYSKCQDCVHRLGRVLRRKLGEDWIFLVLLGLLMALVSWCMDYVSAKSLQAYKWTYAQMKPSLPLQYLAWVTFPLILILFSALFCQLISPQAVGSGIPEMKTILRGVVLKEYLTLKAFVAKVVALTAGLGSGIPVGKEGPFVHIASICAAVLSKFMSMFSGVYEQPYYYTDILTVGCAVGVGCCFGTPLGGVLFSIEVTSTYFAVRNYWRGFFAATFSAFVFRVLAVWNKDAVTITALFRTNFRMDFPFDLKELPAFAVIGICCGFLGAVFVYLHRQVMLGVRKHKCLSQFLAKHRLLYPGIVTFVIASLTFPPGMGQFMAGELMPREAISTLFDNNTWVKHIGDPQSLGQSAVWLHPQVNVIIIILLFFVMKFWMSIVATTMPIPCGGFMPVFVLGAAFGRLVGEIMAMLFPEGILFDDIIYKILPGGYAVIGAAALTGAVSHTVSTAVICFELTGQIAHILPMMVAVILANMVAQSLQPSLYDSIIQVKKLPYLPDLGWNQLSKFTIFVEDIMVRDVKFVSASCTYGELRNLLQATTVKTLPLVDSKDSMILLGSVERSELQSLLQRHLCAERRLKAAQDMARKLSELPYNGKAQLAGDWHPGGRPESFAFVDEDEDEDLSRKMELPLTPAPPPPSPPPPPSQFPIAPSNPEEPNGPLPSHKQPPEASDSADQRSSTFQRLLHCLLGKAHSKKKKITQDSTDLVDNMSPEEIEAWEREQLSQPVCFDCCCIDQSPFQLVEQTTLHKTHTLFSLLGLHLAYVTSMGKLRGVLALEELQKAIEGHTKSGVQLRPPLASFRNTTSIRKTPGGPPPPAEGWNVPEDGDGAPGREVMVPTMPETPVPPPSPEAPSCLAPARAEGELEELEMVGSLEPEEELADILHGPSLRSTDEEDEDELIL
Protein: Elongator complex protein 4 (A0A1W2PR08)
Organism: Homo sapiens (Human)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}. Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MAAVATCGSVAASTGSAVATASKSNVTSFQRRGPRASVTNDSGPRLVSIAGTRPSVRNGQLLVSTGLPALDQLLGGGLAVGTVLLIEEDKYNIYSPLLFKYFLAEGIVNGHTLLVASAKEDPANILQELPAPLLDDKCKKEFDEDVYNHKTPESNIKMKIAWRYQLLPKMEIGPVSSSRFGHYYDASKRMPQELIEASNWHGFFLPEKISSTLKVEPCSLTPGYTKLLQFIQNIIYEEGFDGSNPQKKQRNILRIGIQNLGSPLWGDDICCAENGGNSHSLTKFLYVLRGLLRTSLSACIITMPTHLIQNKAIIARVTTLSDVVVGLESFIGSERETNPLYKDYHGLIHIRQIPRLNNLICDESDVKDLAFKLKRKLFTIEAEVQKGVSTATFLLDGPRKKLFPCLFQLLEVACIPWLMASSSVFKASNIGFESLCYQLSGFFSASLLHF
Protein: 5'-3' exonuclease PLD3 (EC 3.1.16.1) ((S,S)-bis(monoacylglycero)phosphate synthase PLD3) (EC 3.1.4.-) (HindIII K4L homolog) (Hu-K4) (Phospholipase D3) (Q8IV08)
Organism: Homo sapiens (Human)
Function: 5'->3' DNA exonuclease which digests single-stranded DNA (ssDNA). Regulates inflammatory cytokine responses via the degradation of nucleic acids, by reducing the concentration of ssDNA able to stimulate TLR9, a nucleotide-sensing receptor in collaboration with PLD4 (By similarity). May be important in myotube formation. Plays a role in lysosomal homeostasis. Involved in the regulation of endosomal protein sorting.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:15794758, ECO:0000269|PubMed:22428023}; Single-pass type II membrane protein {ECO:0000269|PubMed:15794758, ECO:0000269|PubMed:22428023}. Lysosome lumen {ECO:0000269|PubMed:29386126, ECO:0000269|PubMed:30312375, ECO:0000305|PubMed:39423811}. Early endosome membrane {ECO:0000269|PubMed:29386126}; Single-pass type II membrane protein {ECO:0000269|PubMed:15794758, ECO:0000269|PubMed:22428023}. Late endosome membrane {ECO:0000269|PubMed:29386126}; Single-pass type II membrane protein {ECO:0000269|PubMed:15794758, ECO:0000269|PubMed:22428023}. Golgi apparatus membrane {ECO:0000269|PubMed:29368044}; Single-pass type II membrane protein {ECO:0000269|PubMed:29368044}. Endosome membrane {ECO:0000269|PubMed:29368044}; Single-pass type II membrane protein {ECO:0000269|PubMed:29368044}. Note=Localizes to ER-associated vesicles in differentiating myotubes (PubMed:22428023). Sorted into intralumenal vesicles (ILVs) in lysosomes. The soluble form in lysosome arises by proteolytic processing of the membrane-bound form (PubMed:29386126). Colocalizes with APP in endosomes (PubMed:29368044). {ECO:0000269|PubMed:22428023, ECO:0000269|PubMed:29368044, ECO:0000269|PubMed:29386126}.
Interaction partners:
- Phospholipase D2
- Cholinephosphotransferase 1
- Phospholipase D1
- Choline/ethanolaminephosphotransferase 1
- Membrane-bound glycerophospholipid O-acyltransferase 2
- Membrane-bound glycerophospholipid O-acyltransferase 1
- Lysophospholipid acyltransferase 5
- Phosphatidylcholine-sterol acyltransferase
- Lysophosphatidylcholine acyltransferase 1
- Phosphatidylserine decarboxylase proenzyme, mitochondrial
Sequence:
MKPKLMYQELKVPAEEPANELPMNEIEAWKAAEKKARWVLLVLILAVVGFGALMTQLFLWEYGDLHLFGPNQRPAPCYDPCEAVLVESIPEGLDFPNASTGNPSTSQAWLGLLAGAHSSLDIASFYWTLTNNDTHTQEPSAQQGEEVLRQLQTLAPKGVNVRIAVSKPSGPQPQADLQALLQSGAQVRMVDMQKLTHGVLHTKFWVVDQTHFYLGSANMDWRSLTQVKELGVVMYNCSCLARDLTKIFEAYWFLGQAGSSIPSTWPRFYDTRYNQETPMEICLNGTPALAYLASAPPPLCPSGRTPDLKALLNVVDNARSFIYVAVMNYLPTLEFSHPHRFWPAIDDGLRRATYERGVKVRLLISCWGHSEPSMRAFLLSLAALRDNHTHSDIQVKLFVVPADEAQARIPYARVNHNKYMVTERATYIGTSNWSGNYFTETAGTSLLVTQNGRGGLRSQLEAIFLRDWDSPYSHDLDTSADSVGNACRLL
Protein: L-fucose kinase (Fucokinase) (EC 2.7.1.52) (Q7TMC8)
Organism: Mus musculus (Mouse)
Function: Takes part in the salvage pathway for reutilization of fucose from the degradation of oligosaccharides.
Interaction partners:
- Fucose-1-phosphate guanylyltransferase
- GDP-mannose 4,6 dehydratase
- GDP-L-fucose synthase
- Hexokinase HKDC1
- Hexokinase-1
- Sorbitol dehydrogenase
- Hexokinase-2
- Hexokinase-3
- Bifunctional polynucleotide phosphatase/kinase
- Meiotic recombination protein REC114
Sequence:
MEQSEGVNWTVIILTCQYKDSVQVFQRELEVRQRREQIPAGTMLLAVEDPQTRVGSGGATLNALLVAAEHLSARAGFTVVTSDVLHSAWILILHMGRDFPFDDCGRAFTCLPVENPQAPVEALVCNLDCLLDIMTHRLGPGSPPGVWVCSTDMLLSVPPNPGISWDGFRGARVIAFPGSLAYALNHGVYLTDSQGLVLDIYYQGTKAEIQRCVGPDGLVPLVSGVVFFSVETAEHLLATHVSPPLDACTYMGLDSGAQPVQLSLFFDILLCMARNMSRENFLAGRPPELGQGDMDVASYLKGARAQLWRELRDQPLTMVYVPDGGYSYMTTDATEFLHRLTMPGVAVAQIVHSQVEEPQLLEATCSVVSCLLEGPVHLGPRSVLQHCHLRGPIRIGAGCFVSGLDTAHSEALHGLELHDVILQGHHVRLHGSLSRVFTLAGRLDSWERQGAGMYLNMSWNEFFKKTGIRDWDLWDPDTPPSDRCLLTARLFPVLHPTRALGPQDVLWMLHPRKHRGEALRAWRASWRLSWEQLQPCVDRAATLDFRRDLFFCQALQKARHVLEARQDLCLRPLIRAAVGEGCSGPLLATLDKVAAGAEDPGVAARALACVADVLGCMAEGRGGLRSGPAANPEWIQPFSYLECGDLMRGVEALAQEREKWLTRPALLVRAARHYEGAEQILIRQAVMTARHFVSTQPVELPAPGQWVVTECPARVDFSGGWSDTPPIAYELGGAVLGLAVRVDGRRPIGAKARRIPEPELWLAVGPRQDEMTMRIVCRSLDDLRDYCQPHAPGALLKAAFICAGIVHLHSELPLLEQLLHSFNGGFELHTWSELPHGSGLGTSSILAGAALAALQRAAGRAVGTEALIHAVLHLEQVLTTGGGWQDQVSGLMPGIKVGRSRAQLPLKVEVEEITVPEGFVQKINDHLLLVYTGKTRLARNLLQDVLRNWYARLPVVVQNARRLVRQTEKCAEAFRQGNLPLLGQYLTSYWEQKKLMAPGCEPLAVQRMMDVLAPYAYGQSLAGAGGGGFLYLLTKEPRQKETLEAVLAKAEGLGNYSVHLVEVDPQGLSLQLLGHDTRLCGAGPSEVGTT
Protein: Flavin-containing monooxygenase 1 (EC 1.14.13.148) (EC 1.14.13.8) (Dimethylaniline monooxygenase [N-oxide-forming] 1) (Dimethylaniline oxidase 1) (Hepatic flavin-containing monooxygenase 1) (FMO 1) (Trimethylamine monooxygenase) (Q95LA2)
Organism: Canis lupus familiaris (Dog) (Canis familiaris)
Function: Broad spectrum monooxygenase that catalyzes the oxygenation of a wide variety of nitrogen- and sulfur-containing compounds including xenobiotics (By similarity). Catalyzes the S-oxygenation of hypotaurine to produce taurine, an organic osmolyte involved in cell volume regulation as well as a variety of cytoprotective and developmental processes (By similarity). In vitro, catalyzes the N-oxygenation of trimethylamine (TMA) to produce trimethylamine N-oxide (TMAO) and could therefore participate to the detoxification of this compound that is generated by the action of gut microbiota from dietary precursors such as choline, choline containing compounds, betaine or L-carnitine (By similarity).
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:11792679}; Single-pass membrane protein {ECO:0000255}.
Interaction partners:
Sequence:
MAKRVAIVGAGVSGLASIKCCLEEGLEPTCFERSDDLGGLWRFTEHVEEGRASLYKSVVSNSCKEMSCYSDFPFPEDYPNYVPNSQFLEYLKMYANRFSLLKCIRFKTKVCKVTKCPDFTVTGQWEVVTQHEGKQESAIFDAVMVCTGFLTNPHLPLDCFPGINTFKGQYFHSRQYKHPDIFKDKRVLVIGMGNSGTDIAVETSRLAKKVFLSTTGGAWVMSRVFDSGYPWDMVFMTRFQNMFRNSLPTPIVTWLMARKMNSWFNHANYGLVPEDRTQLREPVLNDELPGCIITGKVLIKPSIKEVKENSVVFNNTPKEEPIDIIVFATGYTFAFPFLDETVVKVENGQASLYKYIFPVHLPKPTLAVIGLIKPLGSMIPTGETQARWAVRVLKGINKLPPQSAMTEEVNARKENKPSGFGLCYCKALQSDYITYIDELLTNINAKPNLFSLLLTDPRLALTIFFGPCTPYQFRLTGPGKWKGARNAILTQWDRTFKVTKTRIVQESPTPFASLLKLLSLLALLMAIFLIFL
Protein: Nuclear factor 1 (Q5VW28)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123, ECO:0000256|RuleBase:RU000690}.
Interaction partners:
Sequence:
MMYSPICLTQDEFHPFIEALLPHVRAIAYTWFNLQARKRKYFKKHEKRMSKDEERAVKDELLSEKPEIKQKWASRLLAKLRKDIRQEYREDFVLTVTGKKHPCCVLSNPDQKGKIRRIDCLRQADKVWRLDLVMVILFKGIPLESTDGERLMKSPHCTNPALCVQPHHITVSVKELDLFLAYYVQEQDSGQSGSPSHNDPAKNPPGYLEDSFVKSGVFNVSELVRVSRTPITQGTGVNFPIGEIPSQPYYHDMNSGVNLQRSLSSPPSSKRPKTISIDENMEPSPTGDFYPSPSSPAAGSRTWHERDQDMSSPTTMKKPEKPLFSSASPQDSSPRLSTFPQHHHPGIPGVAHSVISTRTPPPPSPLPFPTQAILPPAPSSYFSHPTIRYPPHLNPQDTLKNYVPSYDPSSPQTSQSWYLG
Protein: Protein O-mannosyl-transferase TMTC2 (EC 2.4.1.109) (Transmembrane O-mannosyltransferase targeting cadherins 2) (Transmembrane and tetratricopeptide repeat-containing 2) (Q8N394)
Organism: Homo sapiens (Human)
Function: Transfers mannosyl residues to the hydroxyl group of serine or threonine residues. The 4 members of the TMTC family are O-mannosyl-transferases dedicated primarily to the cadherin superfamily, each member seems to have a distinct role in decorating the cadherin domains with O-linked mannose glycans at specific regions. Also acts as O-mannosyl-transferase on other proteins such as PDIA3.
Subcellular location: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. Endoplasmic reticulum {ECO:0000305}.
Interaction partners:
Sequence:
MIAELVSSALGLALYLNTLSADFCYDDSRAIKTNQDLLPETPWTHIFYNDFWGTLLTHSGSHKSYRPLCTLSFRLNHAIGGLNPWSYHLVNVLLHAAVTGLFTSFSKILLGDGYWTFMAGLMFASHPIHTEAVAGIVGRADVGASLFFLLSLLCYIKHCSTRGYSARTWGWFLGSGLCAGCSMLWKEQGVTVLAVSAVYDVFVFHRLKIKQILPTIYKRKNLSLFLSISLLIFWGSSLLGARLYWMGNKPPSFSNSDNPAADSDSLLTRTLTFFYLPTKNLWLLLCPDTLSFDWSMDAVPLLKTVCDWRNLHTVAFYTGLLLLAYYGLKSPSVDRECNGKTVTNGKQNANGHSCLSDVEYQNSETKSSFASKVENGIKNDVSQRTQLPSTENIVVLSLSLLIIPFVPATNLFFYVGFVIAERVLYIPSMGFCLLITVGARALYVKVQKRFLKSLIFYATATLIVFYGLKTAIRNGDWQNEEMLYRSGIKVNPAKAWGNLGNVLKSQSKISEAESAYRNALYYRSNMADMLYNLGLLLQENSRFAEALHYYKLAIGSRPTLASAYLNTGIILMNQGRTEEARRTFLKCSEIPDENLKDPHAHKSSVTSCLYNLGKLYHEQGHYEEALSVYKEAIQKMPRQFAPQSLYNMMGEAYMRLSKLPEAEHWYMESLRSKTDHIPAHLTYGKLLALTGRKSEAEKLFLKAIELDPTKGNCYMHYGQFLLEEARLIEAAEMAKKAAELDSTEFDVVFNAAHMLRQASLNEAAEKYYDLAARLRPNYPAALMNLGAILHLNGRLQKAEANYLRALQLKPDDVITQSNLRKLWNIMEKQGLKTSKT