wanglab/gogpt-training-data huggingface dataset:
Protein: Si:dkey-33i11.3 protein (A5D6S2)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
Sequence:
MSEKKVGRPGMSIFSPCRVVAAVSLILIILGGLGAAIWALVTYLRTTEDTGLFDVQVSAADQRLRVFDSTQWRWKYVCSSSVNQLIANITCEEMGFVRAVNFSVTCAPESGGDRDFFCVKESELTYGKKIKTALYPCKCDKGQILEVICQDCGRRMLPEERIVGGVDARQGSWPWQVSLQYDGVHQCGGSIISDRWIISAAHCFPERYRHASRWRVLMGSIYNTPIRKNVVIAEVKTVVYHSSYLPFVDANIDDNSRDIAVISLTKPLQFTDYIQPVCLPTYGQRLADGQMGTVTGWGNVEYYGTQANVLQEAHVPIISDAVCNGPDYYDNQVTTTMFCAGYEKGGTDSCQGDSGGPFVAADVLSKTSRYRLLGVVSWGTGCAMAKKPGVYTRVSRFLPWISTAMRMYENSPGVHKMARAATP
Protein: ARF GTPase-activating protein Git (ARF GAP GIT) (dGIT protein) (G protein-coupled receptor kinase interacting ArfGAP) (Q95RG8)
Organism: Drosophila melanogaster (Fruit fly)
Function: GTPase-activating protein for ADP ribosylation factor family members, including ARF1. Multidomain scaffold protein that interacts with numerous proteins and therefore participates in many cellular functions, including receptor internalization, focal adhesion remodeling, and signaling by both G protein-coupled receptors and tyrosine kinase receptors (By similarity). Through Pak activation, may positively regulate microtubule nucleation during interphase. May play a role in the regulation of cytokinesis (By similarity). During embryogenesis, promotes proper muscle morphogenesis and proper guidance and targeting of subsets of myotubes. Required for the recruitment of Pak to muscle attachments in the embryo, probably indirectly through pix/dPIX. May be important for brain development.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:18996366}. Synapse {ECO:0000250|UniProtKB:Q9Y2X7}. Cell junction, focal adhesion {ECO:0000250|UniProtKB:Q9Y2X7}. Cell projection, lamellipodium {ECO:0000250|UniProtKB:Q9Y2X7}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250|UniProtKB:Q9Y2X7}. Cytoplasm, cytoskeleton, spindle pole {ECO:0000250|UniProtKB:Q9Y2X7}. Note=Localizes to the leading edge of growing myotubes. {ECO:0000269|PubMed:18996366}.
Interaction partners:
- Rho-type guanine nucleotide exchange factor, isoform F
- Liprin-alpha, isoform E
- non-specific serine/threonine protein kinase
- Liprin-gamma, isoform C
- Paxillin, isoform F
- Uncharacterized protein, isoform A
- MIP06432p1
- FK506-binding protein 59
- G protein-coupled receptor kinase 2
- non-specific serine/threonine protein kinase
Sequence:
MCFASSIIEAHRKLFIAPPDLDHSDPATPTISTRSKMPRGKSRLQTEVCGDCGAGDPSWASINRGILLCADCCSVHRSLGRHISIVKSLRQGNWEPSVLNFVNSLNAHGANSVWEHHLLDGSTNSTGGKHVPRWRKPTPKDALHPTKSDFIKAKHVNLTFVLKPSLQDDDDGNGSAGCLEQELSRQLHASVRTSNLETSLRFLVQGADPNYYHEDKLSTPLHMAAKFGQASQIEMLLIYGADVNALDGNGMTPLELARANNHNTIAERLLDAMYDVTDRIITFLGGKKPDHASGRHMIIPDANGADISEQLKIARGKLQLVPNKMFEELVMDLYDEVDRRECEAIWSTSTLNADHATVPFLPANPFLSATRNQGRQKLARFNRAEFTGLLTDVLVDAMRRQNMANLRPMDAPVAGHQSLQSLPYANNSMLLGSFEQGGHDPNLSDDEPIYDPVASDDDYAPVPPMAQQAIVHTPPRSANSHNEMETLRKQLNDYKSEINQLKNVVQMLSSENTQLKSKFSSASNNSVYDEPLRIDLSLSSPDTEHEPLSLPEGGTANGESGSSNDSSNQSTIKRPASMYERRLVPNVAKGNTDIRNTTSMYQMAGDGKPFGEEVKVRSDLVTRRLKELIRAMQPVPEDQKQSIAPHGELIRSAVTDLIALYANLPPNASDPSRETLKLLTRQNILIQHECENLQKAIEADDKQAIQKNTLEVRDCAFHIASAIKTLVLQFY
Protein: Aldehyde oxidoreductase FAD-binding subunit PaoB (EC 1.2.99.6) (P77324)
Organism: Escherichia coli (strain K12)
Function: Oxidizes aldehydes to the corresponding carboxylic acids with a preference for aromatic aldehydes. It might play a role in the detoxification of aldehydes to avoid cell damage.
Subcellular location: Periplasm {ECO:0000305|PubMed:19368556}.
Interaction partners:
- Aldehyde oxidoreductase iron-sulfur-binding subunit PaoA
- Aldehyde oxidoreductase molybdenum-binding subunit PaoC
- Molybdenum cofactor insertion chaperone PaoD
- Putative xanthine dehydrogenase iron-sulfur-binding subunit XdhC
- Probable hypoxanthine oxidase XdhD
- Putative xanthine dehydrogenase molybdenum-binding subunit XdhA
- Putative xanthine dehydrogenase FAD-binding subunit XdhB
- Adenine deaminase
- Guanine deaminase
- Pyrimidine-specific ribonucleoside hydrolase RihB
Sequence:
MKAFTYERVNTPAEAALSAQRVPGAKFIAGGTNLLDLMKLEIETPTHLIDVNGLGLDKIEVTDAGGLRIGALVRNTDLAAHERVRRDYAVLSRALLAGASGQLRNQATTAGNLLQRTRCPYFYDTNQPCNKRLPGSGCAALEGFSRQHAVVGVSEACIATHPSDMAVAMRLLDAVVETITPEGKTRSITLADFYHPPGKTPHIETALLPGELIVAVTLPPPLGGKHIYRKVRDRASYAFALVSVAAIIQPDGSGRVALGGVAHKPWRIEAADAQLSQGAQAVYDTLFASAHPTAENTFKLLLAKRTLASVLAEARAQA
Protein: Plasmepsin III (EC 3.4.23.39) (Histo-aspartic protease) (Plasmepsin 3) (Q9Y006)
Organism: Plasmodium falciparum (isolate HB3)
Function: During the asexual blood stage, catalyzes the cleavage of denatured host hemoglobin (Hb) or globins. Digestion of host Hb is an essential step which provides the parasite with amino acids for protein synthesis, and regulates osmolarity (Probable).
Subcellular location: Membrane {ECO:0000255}; Single-pass type II membrane protein {ECO:0000305}. Vacuole lumen {ECO:0000269|PubMed:11782538}. Note=In trophozoites, localizes to the digestive (or food) vacuole, an acidic vacuole where host hemoglobin is digested. {ECO:0000269|PubMed:11782538}.
Interaction partners:
Sequence:
MNLTIKEEDFTNTFMKNEESFNTFRVTKVKRWNAKRLFKILFVTVFIVLAGGFSYYIFENFVFQKNRKINHIIKTSKYSTVGFNIENSYDRLMKTIKEHKLKNYIKESVKLFNKGLTKKSYLGSEFDNVELKDLANVLSFGEAKLGDNGQKFNFLFHTASSNVWVPSIKCTSESCESKNHYDSSKSKTYEKDDTPVKLTSKAGTISGIFSKDLVTIGKLSVPYKFIEMTEIVGFEPFYSESDVDGVFGLGWKDLSIGSIDPYIVELKTQNKIEQAVYSIYLPPENKNKGYLTIGGIEERFFDGPLNYEKLNHDLMWQVDLDVHFGNVSSKKANVILDSATSVITVPTEFFNQFVESASVFKVPFLSLYVTTCGNTKLPTLEYRSPNKVYTLEPKQYLEPLENIFSALCMLNIVPIDLEKNTFVLGDPFMRKYFTVYDYDNHTVGFALAKNL
Protein: Probable G-protein coupled receptor 132 (G2 accumulation protein) (Q9UNW8)
Organism: Homo sapiens (Human)
Function: May be a receptor for oxidized free fatty acids derived from linoleic and arachidonic acids such as 9-hydroxyoctadecadienoic acid (9-HODE). Activates a G alpha protein, most likely G alpha(q). May be involved in apoptosis. Functions at the G2/M checkpoint to delay mitosis. May function as a sensor that monitors the oxidative states and mediates appropriate cellular responses such as secretion of paracrine signals and attenuation of proliferation. May mediate ths accumulation of intracellular inositol phosphates at acidic pH through proton-sensing activity.
Subcellular location: Cell membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. Note=Internalized and accumulated in endosomal compartments. LPC triggers the relocalization from the endosomal compartment to the cell surface (By similarity). {ECO:0000250}.
Interaction partners:
- Mitogen-activated protein kinase kinase kinase 4
- G-protein coupled receptor 68
Sequence:
MCPMLLKNGYNGNATPVTTTAPWASLGLSAKTCNNVSFEESRIVLVVVYSAVCTLGVPANCLTAWLALLQVLQGNVLAVYLLCLALCELLYTGTLPLWVIYIRNQHRWTLGLLACKVTAYIFFCNIYVSILFLCCISCDRFVAVVYALESRGRRRRRTAILISACIFILVGIVHYPVFQTEDKETCFDMLQMDSRIAGYYYARFTVGFAIPLSIIAFTNHRIFRSIKQSMGLSAAQKAKVKHSAIAVVVIFLVCFAPYHLVLLVKAAAFSYYRGDRNAMCGLEERLYTASVVFLCLSTVNGVADPIIYVLATDHSRQEVSRIHKGWKEWSMKTDVTRLTHSRDTEELQSPVALADHYTFSRPVHPPGSPCPAKRLIEESC
Protein: Uncharacterized membrane protein C3H7.05c (O74380)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Subcellular location: Mitochondrion membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
- Uncharacterized transcriptional regulatory protein C139.03
- Uncharacterized protein UNK4,15
- Uncharacterized transporter C11D3.06
- Uracil phosphoribosyltransferase 2
- Putative uracil phosphoribosyltransferase urg2
- Uncharacterized transcriptional regulatory protein PB24D3.01
- Uncharacterized transcriptional regulatory protein C1399.05c
- Protein rds1
Sequence:
MYPFSFDPSSKLPVTGIYNILLFNLFPLATYLVETFCFFRRWKIACTLLCSITVILAYRMCAVYHHVGYKDVSTFGLAYGFLIMMSLRTCFLSWRDMVPSRNDPVQISAVKRRRPFIRNARWNFVDYALSLRKYGWTDDVVPPYCRKVLTYKSLGIRTAVYVGAFCFVNCFKTRLSNWMLLPISANPWYIQVAFCVTSGFFSYLFINALYYLFAIIFVPLGIWDIAEYPLMMGNVSKTTSVNDFWSRDWHVCTKPYFRVIAWDPTIALTGSKFLASCSCFFLSALFHDFAYWSISGRCSPAFFFQLLIQPFLINLEKRIPLLRKYHYWVLIIEMLINGTYGMGVVLLKFKWKTCSQI
Protein: At1g58220 (Homeodomain-like superfamily protein) (MYB transcription factor) (Putative MYB-family transcription factor) (Q8GZ96)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- GRR1-like protein 1
- At3g27340
Sequence:
MVDNSNNKKRKEFISEADIATLLQRYDTVTILKLLQEMAYYAEAKMNWNELVKKTSTGITSAREYQLLWRHLAYRDSLVPVGNNARVLDDDSDMECELEASPGVSVDVVTEAVAHVKVMAASYVPSESDIPEDSTVEAPLTINIPYSLHRGPQEPSDSYWSSRGMNITFPVFLPKAAEGHNGNGLASSLAPRKRRKKWSAEEDEELIAAVKRHGEGSWALISKEEFEGERTASQLSQRWGAIRRRTDTSNTSTQTGLQRTEAQMAANRALSLAVGNRLPSKKLAVGMTPMLSSGTIKGAQANGASSGSTLQGQQQPQPQIQALSRATTSVPVAKSRVPVKKTTGNSTSRADLMVTANSVAAAACMSGLATAVTVPKIEPGKNAVSALVPKTEPVKTASTVSMPRPSGISSALNTEPVKTAVAASLPRSSGIISAPKVEPVKTAASAASLPRPSGMISAPKVEPVKTTASVASLPRPSGIISAPKAEPVKTAASAASSPRPSGMISAPKVESVKTTASMPRPSGIISAPKAELVKSAASAASLPCTSGIISSPKAELVKSAASAASFPRPSSMLSAPKADPVKIVPAAATNTKSVGPLNLRHAVNGSPNHTIPSSPFTKPLHMAPLSKGSTIQSNSVPPSFASSRLVPTQRAPAATVVTPQKPSVVAAATVVTPQKPSVGAAATVVTPQKPSVGAAANVVTPQKPSVGSAATVVTPQKPSVGAAVTVTSKPVGVQKEQTQGNRASPLVTATLPPNKTIPANSVIGTAKAVAAKVETPPSLMPKKNEVVGSCTDKSSLDKPPEKESTTTVSPLAVAATKSKPKDEATVTGTGLKEL
Protein: Cyclin-L1 (Cyclin-L) (Q9UK58)
Organism: Homo sapiens (Human)
Function: Involved in pre-mRNA splicing. Functions in association with cyclin-dependent kinases (CDKs). Inhibited by the CDK-specific inhibitor CDKN1A/p21. May play a role in the regulation of RNA polymerase II (pol II). May be a candidate proto-oncogene in head and neck squamous cell carcinomas (HNSCC).
Subcellular location: Nucleus speckle {ECO:0000269|PubMed:18216018}. Nucleus, nucleoplasm {ECO:0000269|PubMed:18216018}. Note=Found in nuclear intrachromatin granules clusters (IGC), also called nuclear speckles, which are storage compartments for nuclear proteins involved in mRNA processing. {ECO:0000250}.
Interaction partners:
- Cyclin-dependent kinase 11A
- Cyclin-dependent kinase 19
- Cyclin-dependent kinase 11B
- Serine/arginine-rich splicing factor 2
Sequence:
MASGPHSTATAAAAASSAAPSAGGSSSGTTTTTTTTTGGILIGDRLYSEVSLTIDHSLIPEERLSPTPSMQDGLDLPSETDLRILGCELIQAAGILLRLPQVAMATGQVLFHRFFYSKSFVKHSFEIVAMACINLASKIEEAPRRIRDVINVFHHLRQLRGKRTPSPLILDQNYINTKNQVIKAERRVLKELGFCVHVKHPHKIIVMYLQVLECERNQTLVQTAWNYMNDSLRTNVFVRFQPETIACACIYLAARALQIPLPTRPHWFLLFGTTEEEIQEICIETLRLYTRKKPNYELLEKEVEKRKVALQEAKLKAKGLNPDGTPALSTLGGFSPASKPSSPREVKAEEKSPISINVKTVKKEPEDRQQASKSPYNGVRKDSKRSRNSRSASRSRSRTRSRSRSHTPRRHYNNRRSRSGTYSSRSRSRSRSHSESPRRHHNHGSPHLKAKHTRDDLKSSNRHGHKRKKSRSRSQSKSRDHSDAAKKHRHERGHHRDRRERSRSFERSHKSKHHGGSRSGHGRHRR
Protein: Complement factor H-related 4 (E9Q8B5)
Organism: Mus musculus (Mouse)
Interaction partners:
- Complement factor I
- Complement C3
- Mannose-binding protein C
- Ficolin-1
- Complement factor B
- Mannan-binding lectin serine protease 2
- Coagulation factor XI
- Vitamin K-dependent protein C
- Prothrombin
- Mannan-binding lectin serine protease 1
Sequence:
MGFCSMLLLSNILLTAWLSTAKGEVKSCEFPQFKYGRLYYEEILRPNFPVSIGNKYSYKCDNGFSPPSGIFWDYLRCTVQGWEPEVPCVRKCVFHYVENGQSAYWEKIYVQGQSLKVQCYNGYSLQNGQDTMTCTENGWSPPPKCIRIKTCSVSDIEIENGFFSESFRTYALNRETSYRCKQGYVTNTGETSGSITCLQNGWSPQPSCIKSCERPVFENSVTKNNSTWFKLNDKLDYECLIGYENEYKHTKGSITCTYYGWSDTPSCYEIECSVPILDRKLVVSPRKEKYRVGDLLEFSCRSGHRVGPDSVQCYHFGWSPSFPTCKAGQVASCAQPPEIPNGEINGAKRVEYSHGEVVGYDCKPRFLLKGPNKIQCVDGMWTTLPVCVEEERTCGDIPELEHGSVKFSVPPYHHGDSVEFTCAETFTMIGLGSVFCLSGKWTQLPKCVATDQLEKCRVLKSTDIEAIKPKRKEFQHNSTMYYKCRDKQEYEHSICINGKWNPEPNCIRKISCPPPPQIPNTQVIETTVKYLDGEKLSVLCQDNYLTQDPEEMMCKDGRWQSLPHCIEKIPCSQPPTIEHGSIKLPRTSEKRRKSIEFSSHEHGTTFSYVCDDGFRIPEENGVACYMGKWSTPPRCVGLPCGPPPSIPLGTVSLELESYQHGEEVTYHCSTGFGIDGPALIKCEGGKWSDPPKCIKTDCDILPTIENAIIRGKNKKSYRTGEQVTVRCQSPYQMNGSDTVTCINGRWIGKPVCKDSRGKCGPPPPIDNGDITSLSLPEYEPFSSVDYQCQKYYLLKGKKTITCRNGKWSEPPTCLHACIIPENIMEARKIILKWRHTKNIYSHSGEDIEFECKYGYHKARGSPPFRTKCISGTINYPICE
Protein: Limbic system associated membrane protein (H3BLU2)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
LRLLCLLPTGLPVRSVDFNRGTDNITVRQGDTAILRCVVEDKNSKVAWLNRSGIIFAGHDKWSLDPRVELEKRHSLEYSLRIQKVDVYDEGSYTCSVQTQHEPKTSQVYLIVQVPPKISNISSDVTVNEGSNVTLVCMANGRPEPVITWRHLTPTGREFEGEEEYLEILGITREQSGKYECKAANEVSSADVKQVKVTVNYPPTITESKSNEATTGRQASLKCEASAVPAPDFEWYRDDTRINSANGLEIKSTEGQSSLTVTNVTEEHYGNYTCVAANKLGVTNASLVLFKRVLPTIPHPIQEIGTTVHFKQKGPGSVRGINGSISLAVPLWLLAASLLCLLSKC
Protein: Histone-lysine N-methyltransferase SETD5 (EC 2.1.1.359) (EC 2.1.1.367) (SET domain-containing protein 5) (Q9C0A6)
Organism: Homo sapiens (Human)
Function: Chromatin regulator required for brain development: acts as a regulator of RNA elongation rate, thereby regulating neural stem cell (NSC) proliferation and synaptic transmission. May act by mediating trimethylation of 'Lys-36' of histone H3 (H3K36me3), which is essential to allow on-time RNA elongation dynamics. Also monomethylates 'Lys-9' of histone H3 (H3K9me1) in vitro. The relevance of histone methyltransferase activity is however subject to discussion.
Subcellular location: Nucleus {ECO:0000250|UniProtKB:Q5XJV7}. Chromosome {ECO:0000250|UniProtKB:Q5XJV7}. Note=Localizes to active transcribed genes. {ECO:0000250|UniProtKB:Q5XJV7}.
Interaction partners:
- tRNA
- Inactive histone-lysine N-methyltransferase 2E
Sequence:
MSIAIPLGVTTSDTSYSDMAAGSDPESVEASPAVNEKSVYSTHNYGTTQRHGCRGLPYATIIPRSDLNGLPSPVEERCGDSPNSEGETVPTWCPCGLSQDGFLLNCDKCRGMSRGKVIRLHRRKQDNISGGDSSATESWDEELSPSTVLYTATQHTPTSITLTVRRTKPKKRKKSPEKGRAAPKTKKIKNSPSEAQNLDENTTEGWENRIRLWTDQYEEAFTNQYSADVQNALEQHLHSSKEFVGKPTILDTINKTELACNNTVIGSQMQLQLGRVTRVQKHRKILRAARDLALDTLIIEYRGKVMLRQQFEVNGHFFKKPYPFVLFYSKFNGVEMCVDARTFGNDARFIRRSCTPNAEVRHMIADGMIHLCIYAVSAITKDAEVTIAFDYEYSNCNYKVDCACHKGNRNCPIQKRNPNATELPLLPPPPSLPTIGAETRRRKARRKELEMEQQNEASEENNDQQSQEVPEKVTVSSDHEEVDNPEEKPEEEKEEVIDDQENLAHSRRTREDRKVEAIMHAFENLEKRKKRRDQPLEQSNSDVEITTTTSETPVGEETKTEAPESEVSNSVSNVTIPSTPQSVGVNTRRSSQAGDIAAEKLVPKPPPAKPSRPRPKSRISRYRTSSAQRLKRQKQANAQQAELSQAALEEGGSNSLVTPTEAGSLDSSGENRPLTGSDPTVVSITGSHVNRAASKYPKTKKYLVTEWLNDKAEKQECPVECPLRITTDPTVLATTLNMLPGLIHSPLICTTPKHYIRFGSPFIPERRRRPLLPDGTFSSCKKRWIKQALEEGMTQTSSVPQETRTQHLYQSNENSSSSSICKDNADLLSPLKKWKSRYLMEQNVTKLLRPLSPVTPPPPNSGSKSPQLATPGSSHPGEEECRNGYSLMFSPVTSLTTASRCNTPLQFELCHRKDLDLAKVGYLDSNTNSCADRPSLLNSGHSDLAPHPSLGPTSETGFPSRSGDGHQTLVRNSDQAFRTEFNLMYAYSPLNAMPRADGLYRGSPLVGDRKPLHLDGGYCSPAEGFSSRYEHGLMKDLSRGSLSPGGERACEGVPSAPQNPPQRKKVSLLEYRKRKQEAKENSAGGGGDSAQSKSKSAGAGQGSSNSVSDTGAHGVQGSSARTPSSPHKKFSPSHSSMSHLEAVSPSDSRGTSSSHCRPQENISSRWMVPTSVERLREGGSIPKVLRSSVRVAQKGEPSPTWESNITEKDSDPADGEGPETLSSALSKGATVYSPSRYSYQLLQCDSPRTESQSLLQQSSSPFRGHPTQSPGYSYRTTALRPGNPPSHGSSESSLSSTSYSSPAHPVSTDSLAPFTGTPGYFSSQPHSGNSTGSNLPRRSCPSSAASPTLQGPSDSPTSDSVSQSSTGTLSSTSFPQNSRSSLPSDLRTISLPSAGQSAVYQASRVSAVSNSQHYPHRGSGGVHQYRLQPLQGSGVKTQTGLS
Protein: Pyruvate dehydrogenase complex repressor (P0ACL9)
Organism: Escherichia coli (strain K12)
Function: Transcriptional repressor for the pyruvate dehydrogenase complex genes aceEF and lpd.
Interaction partners:
- Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex
- Pyruvate dehydrogenase E1 component
- Dihydrolipoyl dehydrogenase
- Fatty acid metabolism regulator protein
Sequence:
MAYSKIRQPKLSDVIEQQLEFLILEGTLRPGEKLPPERELAKQFDVSRPSLREAIQRLEAKGLLLRRQGGGTFVQSSLWQSFSDPLVELLSDHPESQYDLLETRHALEGIAAYYAALRSTDEDKERIRELHHAIELAQQSGDLDAESNAVLQYQIAVTEAAHNVVLLHLLRCMEPMLAQNVRQNFELLYSRREMLPLVSSHRTRIFEAIMAGKPEEAREASHRHLAFIEEILLDRSREESRRERSLRRLEQRKN
Protein: Cdc42-interacting protein 4 (Thyroid receptor-interacting protein 10) (TR-interacting protein 10) (TRIP-10) (Q8CJ53)
Organism: Mus musculus (Mouse)
Function: Required to coordinate membrane tubulation with reorganization of the actin cytoskeleton during endocytosis. Binds to lipids such as phosphatidylinositol 4,5-bisphosphate and phosphatidylserine and promotes membrane invagination and the formation of tubules. Also promotes CDC42-induced actin polymerization by recruiting WASL/N-WASP which in turn activates the Arp2/3 complex. Actin polymerization may promote the fission of membrane tubules to form endocytic vesicles. Required for the formation of podosomes, actin-rich adhesion structures specific to monocyte-derived cells. May be required for the lysosomal retention of FASLG/FASL (By similarity). Required for translocation of GLUT4 to the plasma membrane in response to insulin signaling.
Subcellular location: Cytoplasm, cytoskeleton. Cytoplasm, cell cortex. Lysosome. Golgi apparatus {ECO:0000250}. Cell membrane. Cell projection, phagocytic cup {ECO:0000250}. Note=Localizes to cortical regions coincident with F-actin, to lysosomes and to sites of phagocytosis in macrophages. Also localizes to the Golgi, and this requires AKAP9 (By similarity). Translocates to the plasma membrane in response to insulin stimulation, and this may require active RHOQ. {ECO:0000250}.
Interaction partners:
- Actin nucleation-promoting factor WAS
- Cell division control protein 42 homolog
- Actin nucleation-promoting factor WASL
- Intersectin-2
- Rho-related GTP-binding protein RhoQ
- Rho GTPase-activating protein 17
- tRNA-splicing endonuclease subunit Sen2
Sequence:
MDWGTELWDQFEVLERHTQWGLDLLDKYVKFVKERAEVEQAYAKQLRSLVKKYLPKRPTKDDPEVKFSQQQSFVQLLQEVNDFAGQRELVAESLGIRVCLELAKYSQEMKQERKMHFQEGRRAQQQLENGFKQLENSKRKFERDCREAEKAAHTAERLDQDINATKADVEKAKQQAHLRNHMAEESKNEYAAQLQRFNRDQAHFYFSQMPQIFDKLQDMDERRATRLGAGYGLLSEAELQVVPIIGKCLEGMKVAAESVDAKNDSQVLIELHKSGFARPGDLEFEDFSQVINRVPSDSSLGTPDGRPELRAASSRSRAKRWPFGKKNKPRPPSLSLLGGHLPSTLSDGPSSPRSGRDPLAILSEISKSVKPRLASFRSFRGGRGTVATEDFSHLPPEQQRKRLQQQLEERNRELQKEEDQREALKKMKDVYEKTPQMGDPASLEPRIAETLGNIERLKLEVQKYEAWLAEAESRVLSNRGDSLSRHARPPDPPTTAPPDSSSSSTNSGSQDNKESSSEEPPSEGQDTPIYTEFDEDFEEPASPIGQCVAIYHFEGSSEGTVSMSEGEDLSLMEEDKGDGWTRVRRKQGAEGYVPTSYLRVTLN
Protein: Probable glutathione-independent glyoxalase HSP33 (EC 4.2.1.130) (Glyoxalase 3 homolog 3) (Heat shock protein 33) (Q08914)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Catalyzes the conversion of methylglyoxal (MG) to D-lactate in a single glutathione (GSH)-independent step. May play a role in detoxifying endogenously produced glyoxals. Involved in protection against reactive oxygen species (ROS) (By similarity). Important for viability in stationary phase. May negatively regulate TORC1 in response to nutrient limitation.
Subcellular location: Cytoplasm, P-body {ECO:0000250|UniProtKB:Q04432}. Note=Present in processing bodies (P-bodies) and stress granule (SG) foci upon glucose starvation and heat shock. {ECO:0000250|UniProtKB:Q04432}.
Interaction partners:
- NADPH-dependent methylglyoxal reductase GRE2
- D-2-hydroxyglutarate--pyruvate transhydrogenase DLD3
- Glyoxalase I
- D-2-hydroxyglutarate--pyruvate transhydrogenase DLD2
- Hydroxyacylglutathione hydrolase, mitochondrial
- D-lactate dehydrogenase [cytochrome] 1, mitochondrial
- Hydroxyacylglutathione hydrolase, cytoplasmic isozyme
- Catabolic L-serine/threonine dehydratase
- Threonine dehydratase, mitochondrial
- D-serine dehydratase
Sequence:
MTPKRALISLTSYHGPFYKDGAKTGVFVVEILRSFDTFEKHGFEVDFVSETGGFGWDEHYLPKSFIGGEDKMNFETKNSAFNKALARIKTANEVNASDYKVFFASAGHGALFDYPKAKNLQDIASKIYANGGVIAAICHGPLLFDGLIDIKTTRPLIEGKAITGFPLEGEIALGVDDILRSRKLTTVERVANKNGAKYLAPIHPWDDYSITDGKLVTGVNANSSYSTTIRAINALYS
Protein: Caspase 14, apoptosis-related cysteine peptidase (Caspase-14) (cDNA, FLJ94644, Homo sapiens caspase 14, apoptosis-related cysteine protease(CASP14), mRNA) (B2CIS9)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MSNPRSLEEEKYDMSGARLALILCVTKAREGSEEDLDALEHMFRQLRFESTMKRDPTAEQFQEELEKFQQAIDSREDPVSCAFVVLMAHGREGFLKGEDGEMVKLENLFEALNNKNCQALRAKPKVYIIQACRGEQRDPGETVGGDEIVMVIKDSPQTIPTYTDALHVYSTVEGYIAYRHDQKGSCFIQTLVDVFTKRKGHILELLTEVTRRMAEAELVQEGKARKTNPEIQSTLRKRLYLQ
Protein: Leucine-rich repeat neuronal protein 4 (Neuronal leucine-rich repeat protein 4) (NLRR-4) (Q8WUT4)
Organism: Homo sapiens (Human)
Function: May play an important role in hippocampus-dependent long-lasting memory.
Subcellular location: Membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}.
Interaction partners:
- Putative postmeiotic segregation increased 2-like protein 11
Sequence:
MRQTLPLLLLTVLRPSWADPPQEKVPLFRVTQQGPWGSSGSNATDSPCEGLPAADATALTLANRNLERLPGCLPRTLRSLDASHNLLRALSTSELGHLEQLQVLTLRHNRIAALRWGPGGPAGLHTLDLSYNQLAALPPCTGPALSSLRALALAGNPLRALQPRAFACFPALQLLNLSCTALGRGAQGGIAEAAFAGEDGAPLVTLEVLDLSGTFLERVESGWIRDLPKLTSLYLRKMPRLTTLEGDIFKMTPNLQQLDCQDSPALASVATHIFQDTPHLQVLLFQNCNLSSFPPWTLDSSQVLSINLFGNPLTCSCDLSWLLTDAKRTVLSRAADTMCAPAAGSSGPFSASLSLSQLPGVCQSDQSTTLGASHPPCFNRSTYAQGTTVAPSAAPATRPAGDQQSVSKAPNVGSRTIAAWPHSDAREGTAPSTTNSVAGHSNSSVFPRAASTTRTQHRGEHAPELVLEPDISAASTPLASKLLGPFPTSWDRSISSPQPGQRTHATPQAPNPSLSEGEIPVLLLDDYSEEEEGRKEEVGTPHQDVPCDYHPCKHLQTPCAELQRRWRCRCPGLSGEDTIPDPPRLQGVTETTDTSALVHWCAPNSVVHGYQIRYSAEGWAGNQSVVGVIYATARQHPLYGLSPGTTYRVCVLAANRAGLSQPRSSGWRSPCAAFTTKPSFALLLSGLCAASGLLLASTVVLSACLCRRGQTLGLQRCDTHLVAYKNPAFDDYPLGLQTVS
Protein: 2-oxoglutarate dehydrogenase, mitochondrial (EC 1.2.4.2) (2-oxoglutarate dehydrogenase complex component E1) (OGDC-E1) (Alpha-ketoglutarate dehydrogenase) (O61199)
Organism: Caenorhabditis elegans
Function: The 2-oxoglutarate dehydrogenase complex catalyzes the overall conversion of 2-oxoglutarate to succinyl-CoA and CO(2). It contains multiple copies of three enzymatic components: 2-oxoglutarate dehydrogenase (E1), dihydrolipoamide succinyltransferase (E2) and lipoamide dehydrogenase (E3) (By similarity).
Subcellular location: Mitochondrion matrix {ECO:0000250}.
Interaction partners:
- Dihydrolipoyllysine-residue succinyltransferase component of 2-oxoglutarate dehydrogenase complex, mitochondrial
- Dihydrolipoyl dehydrogenase, mitochondrial
- Probable isocitrate dehydrogenase subunit alpha, mitochondrial
- Isocitrate dehydrogenase
- Succinate--CoA ligase subunit alpha, mitochondrial
- Isocitrate dehydrogenase
- Succinate--CoA ligase subunit beta, mitochondrial
- Succinate--CoA ligase subunit alpha, mitochondrial
- Probable aconitate hydratase, mitochondrial
- Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex, mitochondrial
Sequence:
MHRASLICRLASPSRINAIRNASSGKSHISASTLVQHRNQSVAAAVKHEPFLNGSSSIYIEQMYEAWLQDPSSVHTSWDAYFRNVEAGAGPGQAFQAPPATAYAGALGVSPAAAQVTTSSAPATRLDTNASVQSISDHLKIQLLIRSYQTRGHNIADLDPLGINSADLDDTIPPELELSFYGLGERDLDREFLLPPTTFISEKKSLTLREILQRLKDIYCTSTGVEYMHLNNLEQQDWIRRRFEAPRVTELSHDQKKVLFKRLIRSTKFEEFLAKKWPSEKRFGLEGCEVLIPAMKQVIDSSSTLGVDSFVIGMPHRGRLNVLANVCRQPLATILSQFSTLEPADEGSGDVKYHLGVCIERLNRQSQKNVKIAVVANPSHLEAVDPVVMGKVRAEAFYAGDEKCDRTMAILLHGDAAFAGQGVVLETFNLDDLPSYTTHGAIHIVVNNQIGFTTDPRSSRSSPYCTDVGRVVGCPIFHVNVDDPEAVMHVCNVAADWRKTFKKDVIVDLVCYRRHGHNELDEPMFTQPLMYQRIKQTKTALEKYQEKILNEGVANEQYVKEELTKYGSILEDAYENAQKVTYVRNRDWLDSPWDDFFKKRDPLKLPSTGIEQENIEQIIGKFSQYPEGFNLHRGLERTLKGRQQMLKDNSLDWACGEALAFGSLLKEGIHVRLSGQDVQRGTFSHRHHVLHDQKVDQKIYNPLNDLSEGQGEYTVCNSSLSEYAVLGFELGYSMVDPNSLVIWEAQFGDFSNTAQCIIDQFISSGQSKWIRQSGLVMLLPHGYEGMGPEHSSARPERFLQMCNEDDEIDLEKIAFEGTFEAQQLHDTNWIVANCTTPANIYHLLRRQVTMPFRKPAVVFSPKSLLRHPMARSPVEDFQSGSNFQRVIPETGAPSQNPPDVKRVVFCTGKVYYDMVAARKHVGKENDVALVRVEQLSPFPYDLVQQECRKYQGAEILWAQEEHKNMGAWSFVQPRINSLLSIDGRATKYAGRLPSSSPATGNKFTHMQEQKEMMSKVFGVPKSKLEGFKA
Protein: Probable ATP-dependent RNA helicase DDX49 (EC 3.6.4.13) (DEAD box protein 49) (Q9Y6V7)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus, nucleolus {ECO:0000269|PubMed:29618122}.
Interaction partners:
- Activator of basal transcription 1
- Something about silencing protein 10
- Nucleolar protein 6
- Bystin
- Probable ATP-dependent RNA helicase DHX37
- Ribosomal RNA small subunit methyltransferase NEP1
- WD repeat-containing protein 46
- U3 small nucleolar RNA-associated protein 25 homolog
- Probable ATP-dependent RNA helicase DDX52
- Protein RRP5 homolog
Sequence:
MAGFAELGLSSWLVEQCRQLGLKQPTPVQLGCIPAILEGRDCLGCAKTGSGKTAAFVLPILQKLSEDPYGIFCLVLTPTRELAYQIAEQFRVLGKPLGLKDCIIVGGMDMVAQALELSRKPHVVIATPGRLADHLRSSNTFSIKKIRFLVMDEADRLLEQGCTDFTVDLEAILAAVPARRQTLLFSATLTDTLRELQGLATNQPFFWEAQAPVSTVEQLDQRYLLVPEKVKDAYLVHLIQRFQDEHEDWSIIIFTNTCKTCQILCMMLRKFSFPTVALHSMMKQKERFAALAKFKSSIYRILIATDVASRGLDIPTVQVVINHNTPGLPKIYIHRVGRTARAGRQGQAITLVTQYDIHLVHAIEEQIKKKLEEFSVEEAEVLQILTQVNVVRRECEIKLEAAHFDEKKEINKRKQLILEGKDPDLEAKRKAELAKIKQKNRRFKEKVEETLKRQKAGRAGHKGRPPRTPSGSHSGPVPSQGLV