wanglab/gogpt-training-data huggingface dataset:
Protein: Krev interaction trapped protein 1 (Krev interaction trapped 1) (Cerebral cavernous malformations 1 protein homolog) (Santa) (F1REV3)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Function: Component of the CCM signaling pathway which is a crucial regulator of heart and vessel formation and integrity. Negative regulator of angiogenesis. Inhibits endothelial proliferation, apoptosis, migration, lumen formation and sprouting angiogenesis in primary endothelial cells. Plays a role in integrin signaling. Plays an important role in the maintenance of the intracellular reactive oxygen species (ROS) homeostasis to prevent oxidative cellular damage. Facilitates the down-regulation of cyclin-D1 (CCND1) levels required for cell transition from proliferative growth to quiescence by preventing the accumulation of intracellular ROS. Probable microtubule-associated protein that may bind to phosphatidylinositol 4,5-bisphosphate (PIP2)-containing membranes (By similarity). Required for correct endothelial cell polarity and cell junction stabilization in cardiovascular development. May play a role in the regulation of macroautophagy through the down-regulation of the mTOR pathway (By similarity).
Subcellular location: Cytoplasm, cytoskeleton. Cell membrane; Peripheral membrane protein. Cell junction. Note=KRIT1 and CDH5 reciprocally regulate their localization to endothelial cell-cell junctions (By similarity). Association with RAP1 relocalizes KRIT1 from microtubules to cell junction membranes. {ECO:0000250}.
Interaction partners:
- Cerebral cavernous malformations protein 2 homolog
- Protein HEG
- Sorting nexin-17
- Programmed cell death protein 10-A
- Integrin beta-1-binding protein 1
- CCM2-like scaffold protein.
- Ras-related protein Rap-1b
- Ras-interacting protein 1
- Ras-related protein Rap-1b
- Ras-related protein Rap-1b
Sequence:
MGNQELEEVFVAVIRPKNTTSLNSKEYRAKSYEILLIEVPLEGKEKKRKKVLLGTKIHADSDRTKSILEFVDETTKPISNNQGIIGKRVVHMRKFLLDGDSGGKEASLFIVPINVKDNSKSVHHPGSPSFYCLQDIMRVCSETSAHFSSSTSKMLLALDKWLAEQHTVPHAIPALFRPAPVDRVKTNVSNPAYAVEKQTDGTLHMGYTALEIKSKLMSLEKADLCIQNPLYGSDLQYTNRVDKVIINPYFGLGAPDYSKIQIPKRDKWQHSMTSVTEDKERQWVDDFPLHRSACEGDTELLSKLLDGGFSVKQLDSDHWAPIHYACWHGKVEATKLLLEKGNCNPNLLNGQLSSPLHFAAIGGHAEIVQLLLQHPEIDRHIEDQQKRSPLQVCEENKQNNWEETVNLLQQASNKPYEKVRIYRMDGSYRSVELKHGNNTTVQQIMEGMRLSQETQQYFTIWICSENLSLQLKPYHKPLQHLRMWSEIVTDLTALDPQRESPQLFLRRDVRLPLEVEKKVEDPLSILILFDEARHCLLKGFLSTSDNKLITLASLLLQIIYGNYDSKKHKQGFLNEENLKSIVPISKVKSKAHHWTNRILHEYKSLSTSEGVSKEMHHLQRLFLQNCWDIPTYGAAFFTGQVFTKASSSTHKVIRVYVGVNTKGLHLMNMETKVLHLSLEYGTFMWQLGQADQYVQIHSLENKKNFVVHTKQAGLIVKLLMKLSGQIAPNDRAVSDKYAYG
Protein: GH12726p (Q95SN6)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MKPSAPVQNGNGNANGTHIEAPCCRDIHGKEPPDGGARAWLVMVSAFLCNGIIFGFINTYGVIHSLLTDRLTKLGDPEASSKAALIGALAIGTTFLFSTMAGCLTDKIGLRLTTFAGGVLSAGGLLLSSFCTENIGALYFTYGIMFGLGAALAYTPTLAILGHYFKRYLGKVSGFVTAGSSVFTVILPPCLDKLLGSYGLEGTLRIMSLVSAFIILCSFVYKPLHPPPEPPKKKPGRSRINLFLRSIINVEIWKRKRFVIWALCVPLALFGYFVPYVHMMQFVKTTFPGEDVNLPVMCIGITSGIGRLIFGVIADMPGVNRMYLQQLSLVSIGLVTLLLPLTNSYVILVSFTLVMGLFDGCFISLLGPIAYEICGPSGATQAIGFLLGLSSIPLTVGPPVAGMIFDSTNSYTLPLILAGLPPLLGSSLLFLIKCVKEEENGVSAPRAVVLANGDIEIAGNGHYRSAGTKSSAPLMGATNGINGSAPASPTIQSNGHVDNGTGKLAVTNGSAS
Protein: Succinate dehydrogenase assembly factor 1, mitochondrial (SDH assembly factor 1) (SDHAF1) (LYR motif-containing protein 8) (Q3U276)
Organism: Mus musculus (Mouse)
Function: Plays an essential role in the assembly of succinate dehydrogenase (SDH), an enzyme complex (also referred to as respiratory complex II) that is a component of both the tricarboxylic acid (TCA) cycle and the mitochondrial electron transport chain, and which couples the oxidation of succinate to fumarate with the reduction of ubiquinone (coenzyme Q) to ubiquinol. Promotes maturation of the iron-sulfur protein subunit Sdhb of the SDH catalytic dimer, protecting it from the deleterious effects of oxidants. May act together with SDHAF3. Contributes to iron-sulfur cluster incorporation into SDHB by binding to SDHB and recruiting the iron-sulfur transfer complex formed by HSC20, HSPA9 and ISCU through direct binding to HSC20.
Subcellular location: Mitochondrion matrix {ECO:0000250|UniProtKB:A6NFY7}.
Interaction partners:
- Succinate dehydrogenase iron-sulfur subunit, mitochondrial
- Succinate dehydrogenase flavoprotein subunit, mitochondrial
- Succinate dehydrogenase assembly factor 3, mitochondrial
- Succinate dehydrogenase assembly factor 2, mitochondrial
- Succinate dehydrogenase cytochrome b small subunit, mitochondrial
- Succinate dehydrogenase cytochrome b560 subunit, mitochondrial
- Succinate dehydrogenase assembly factor 4, mitochondrial
- LYR motif-containing protein 4
- Complex III assembly factor LYRM7
Sequence:
MSRPSRLQRQVLSLYRELLRAGRGTPGAEARVRAEFRQHASLPRTDVLRIEYLYRRGRRQLQLLRSGHATAMGTFVRPRGPAEEPGDATAPGTRLDDGGAPKNSCEDTGARETRSDGR
Protein: Transcription factor MYC2 (LeMYC2) (SlMYC2) (Basic helix-loop-helix protein 147) (Transcription factor bHLH147) (bHLH transcription factor bHLH147) (A0A3Q7HRZ6)
Organism: Solanum lycopersicum (Tomato) (Lycopersicon esculentum)
Function: Transcriptional activator that binds to the G-box motif (5'-AACGTG-3') found in the promoter of the jasmonate-induced gene LAPA1. Acts as negative regulator of blue light-mediated photomorphogenesis and positively regulates root growth. Promotes growth in response to the phytohormones abscisic acid (ABA) and jasmonate (JA). Binds to the G-box motif (5'-CACGTG-3') of the RBCS-3A gene promoter. Acts downstream of the jasmonate (JA) receptor to orchestrate JA-mediated activation of plant responses. Positively regulates both wound-responsive and pathogen-responsive genes through MYC2-targeted transcription factors (MTFs) involved in early response to JA. With JA2L forms a transcription module that regulates wounding-responsive genes. With ERF.C3 forms a transcription module that regulates pathogen-responsive genes. Plays a critical role in orchestrating JA-mediated defense gene expression during Botrytis cinerea infection. Regulates negatively defense responses to root-knot nematodes, potentially by mediating crosstalk among the hormones strigolactones, abscisic acid (ABA) and jasmonate (JA). Regulates the termination of JA-mediated defense responses by specifically binding the G-box (5'-CACATG-3') motifs in the promoters of MTB1, MTB2 and MTB3, which are transcription factors that negatively regulates JA signaling. May be involved in JA-induced chilling tolerance, possibly by ameliorating the antioxidant enzyme system of fruit and increasing proline and lycopene levels.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00981}.
Interaction partners:
- Protein TIFY
- Protein TIFY
- Tify domain-containing protein
- Coronatine-insensitive 1
- Protein TIFY
- Protein JAZ7
- Protein TIFY
- Protein TIFY
- Mitogen-activated protein kinase
- Mitogen-activated protein kinase
Sequence:
MTEYSLPTMNLWNNSTSDDNVSMMEAFMSSDLSFWATNNSTSAAVVGVNSNLPHASSNTPSVFAPSSSTSASTLSAAATVDASKSMPFFNQETLQQRLQALIDGARETWTYAIFWQSSVVDFSSPSVLGWGDGYYKGEEDKAKRKLSVSSPAYIAEQEHRKKVLRELNSLISGAPPGTDDAVDEEVTDTEWFFLISMTQSFVNGSGLPGQALYSSSPIWVAGTEKLAASHCERVRQAQGFGLQTIVCIPSANGVVELGSTELIVQSSDLMNKVRVLFNFSNDLGSGSWAVQPESDPSALWLTDPSSSGMEVRESLNTVQTNSVPSSNSNKQIAYGNENNHPSGNGQSCYNQQQQKNPPQQQTQGFFTRELNFSEFGFDGSSNRNGNSSVSCKPESGEILNFGDSTKKSASSANVNLFTGQSQFGAGEENNNKNKKRSATSRGSNEEGMLSFVSGTVLPSSGMKSGGGGGEDSEHSDLEASVVKEADSSRVVEPEKRPRKRGRKPANGREEPLNHVEAERQRREKLNQRFYALRAVVPNVSKMDKASLLGDAISYINELKSKLQNTESDKEDLKSQIEDLKKESRRPGPPPPPNQDLKMSSHTGGKIVDVDIDVKIIGWDAMIRIQCNKKNHPAARLMAALMELDLDVHHASVSVVNDLMIQQATVKMGSRHYTEEQLRVALTSKIAETH
Protein: Protein O-GlcNAcase (OGA) (EC 3.2.1.169) (Beta-N-acetylhexosaminidase) (Beta-hexosaminidase) (Bifunctional protein NCOAT) (Meningioma-expressed antigen 5) (N-acetyl-beta-D-glucosaminidase) (N-acetyl-beta-glucosaminidase) (Q9EQQ9)
Organism: Mus musculus (Mouse)
Function: Cleaves GlcNAc but not GalNAc from O-glycosylated proteins. Can use p-nitrophenyl-beta-GlcNAc and 4-methylumbelliferone-GlcNAc as substrates but not p-nitrophenyl-beta-GalNAc or p-nitrophenyl-alpha-GlcNAc (in vitro). Does not bind acetyl-CoA and does not have histone acetyltransferase activity.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:24563466}. Nucleus {ECO:0000250|UniProtKB:Q8VIJ5}.
Interaction partners:
- UDP-N-acetylglucosamine--peptide N-acetylglucosaminyltransferase 110 kDa subunit
- Hydrocephalus-inducing protein
- Aurora kinase B
- Glutamine--fructose-6-phosphate aminotransferase 1
- Tumor necrosis factor
Sequence:
MVQKESQAALEERESERNANPAAASGASLEQSVAPAPGEDNPSGAGAAAVVGAAGGARRFLCGVVEGFYGRPWVMEQRKELFRRLQKWELNTYLYAPKDDYKHRMFWREMYSVEEAEQLMTLISAAREYEIEFIYAISPGLDITFSNPKEVSTLKRKLDQVSQFGCRSFALLFDDIDHNMCAADKEVFSSFAHAQVSITNEIYQYLGEPETFLFCPTEYCGTFCYPNVSQSPYLRTVGEKLLPGIEVLWTGPKVVSKEIPVESIEEVSKIIKRAPVIWDNIHANDYDQKRLFLGPYKGRSTELIPRLKGVLTNPNCEFEANYVAIHTLATWYKSNMNGVRKDVVMTDSEDSTVSIQIKLENEGSDEDIETDVLYSPQMALKLALTEWLQEFGVPHQYSSRQVAHSGAKTSVVDGTPLVAAPSLNATTVVTTVYQEPIMSQGAALSGEPSVLTKEEEKKQPDEEPMDMVVEKQEEAEHKNDNQILTEIVEAKMAEELRPMDTDKESMAESKSPEMSMQEDCIPDVAPMQTDEQTQKEQFVPGPNEKPLYTAEPVTLEDLQLLADLFYLPYEHGPKGAQMLREFQWLRANSSVVSVNCKGKDSEKIEEWRSRAAKFEEMCALVMGMFTRLSNCANRTILYDMYSYVWDIKSIMSMVKSFVQWLGCRSHSSAQFLIGDQEPWAFRGGLAGEFQRLLPIDGANDLFFQPPPLTPTSKVYTIRPYFPKDEASVYKICREMYDDGVGFPFQSQPDLIGDKLVGGLLSLSLDYCFVLEDEDGICGYALGTVDVTPFIKKCKISWIPFMQEKYTKPNGDKELSEAEKIMLSFHEEQEVLPETFLANFPSLIKMDIHKKVTDPSVAKSMMACLLSSLKANGSRGAFCEVRPDDKRILEFYSKLGCFEIAKMEGFPKDVVILGRSL
Protein: DENN domain-containing protein 4C (Q5VZ89)
Organism: Homo sapiens (Human)
Function: Guanine nucleotide exchange factor (GEF) activating RAB10. Promotes the exchange of GDP to GTP, converting inactive GDP-bound RAB10 into its active GTP-bound form. Thereby, stimulates SLC2A4/GLUT4 glucose transporter-enriched vesicles delivery to the plasma membrane in response to insulin.
Subcellular location: Cytoplasmic vesicle membrane. Cell membrane. Cytoplasm, cytosol. Note=Associates with SLC2A4/GLUT4 storage vesicles.
Interaction partners:
- Ras-related protein Rab-10
Sequence:
MIEDKGPRVTDYFVVAGLTDTSTLLDQEINRLDTKSTGPKAPITDIAIIIKSAGETVPEGYTCVEATPSALQANLNYGSLKSPELFLCYKRGRDKPPLTDIGVLYEGKERLIPGCEVILATPYGRCANVNNSSTTSQRIFITYRRAPPVRPQNSLAVTDICVIVTSKGETPPHTFCKVDKNLNCGMWGSSVFLCYKKSVPASNAIAYKAGLIFRYPEEDYESFPLSESDVPLFCLPMGATIECWDPETKYPLPVFSTFVLTGSSAKKVYGAAIQFYEPYSRELLSEKQLMHLGLLTPVERKMVSKSINTNKCICLLSHWPFFEAFRKFLMFIYKLSVSGPHPLPIEKHISHFMQNIPFPSPQRPRILVQLSVHDALILSQPVSTPLPLSGANFSTLLMNLGPENCATLLLFVLLESKILLHSLRPAVLTGVAEAVVAMIFPFQWQCPYIPLCPLSLAAVLSAPLPFIVGVDSRYFDLHDPPQDVVCIDLDTNMLYVSDEKKNMNWKQLPKKPCKNLLSTLKKLYPQLSSVHQKTQEGSAIDMTPIEADFSWQKKMTQLEMEIQEAFLRFMASILKGYRTYLRPITEAPSNKATAADSLFDRQGFLKSRDRAYAKFYTLLSKTQIFIRFIEECSFVSDKDTGLAFFDDCIEKLFPDKGTEKTDKVDFDSAEDTRLIELDDSQKSEHTVFIMPPEPPPDDGKDLSPKYSYKYFPRLDLKLFDRPQELKLCFSRHPTGNSITKSPPLMAKRTKQEIKTAHKLAKRCYTNPPQWAKCLFSHCYSLWFICLPAYVRVSHPKVRALQQAYDVLIKMRKTDVDPLDEVCYRVVMQLCGLWGHPVLAVRVLFEMKTARIKPNAITYGYYNKVVLESPWPSSTRSGIFLWTKVRNVVRGLAQFRQPLKKTVQRSQVSSISGGQSDQGYGSKDELIKDDAEIHVPEEQAARELITKTKMQTEEVCDASAIVAKHSQPSPEPHSPTEPPAWGSSIVKVPSGIFDVNSRKSSTGSISNVLFSTQDPVEDAVFGEATNLKKNGDRGEKRQKHFPERSCSFSSESRAGMLLKKSSLDSNSSEMAIMMGADAKILTAALTCPKTSLLHIARTHSFENVSCHLPDSRTCMSESTWNPEHRSSPVPEMLEESQELLEPVVDDVPKTTATVDTYESLLSDSNSNQSRDLKTVSKDLRNKRSSLYGIAKVVQREDVETGLDPLSLLATECTGGKTPDSEDKLFSPVIARNLADEIESYMNLKSPLGSKSSSMELHREENRESGMTTAFIHALERRSSLPLDHGSPAQENPESEKSSPAVSRSKTFTGRFKQQTPSRTHKERSTSLSALVRSSPHGSLGSVVNSLSGLKLDNILSGPKIDVLKSGMKQAATVASKMWVAVASAYSYSDDEEETNRDYSFPAGLEDHILGENISPNTSISGLVPSELTQSNTSLGSSSSSGDVGKLHYPTGEVPFPRGMKGQDFEKSDHGSSQNTSMSSIYQNCAMEVLMSSCSQCRACGALVYDEEIMAGWTADDSNLNTACPFCKSNFLPLLNIEFKDLRGSASFFLKPSTSGDSLQSGSIPLANESLEHKPVSSLAEPDLINFMDFPKHNQIITEETGSAVEPSDEIKRASGDVQTMKISSVPNSLSKRNVSLTRSHSVGGPLQNIDFTQRPFHGISTVSLPNSLQEVVDPLGKRPNPPPVSVPYLSPLVLRKELESLLENEGDQVIHTSSFINQHPIIFWNLVWYFRRLDLPSNLPGLILTSEHCNEGVQLPLSSLSQDSKLVYIQLLWDNINLHQEPREPLYVSWRNFNSEKKSSLLSEEQQETSTLVETIRQSIQHNNVLKPINLLSQQMKPGMKRQRSLYREILFLSLVSLGRENIDIEAFDNEYGIAYNSLSSEILERLQKIDAPPSASVEWCRKCFGAPLI
Protein: Piwi-like protein 1 (EC 3.1.26.-) (Q96J94)
Organism: Homo sapiens (Human)
Function: Endoribonuclease that plays a central role in postnatal germ cells by repressing transposable elements and preventing their mobilization, which is essential for the germline integrity. Acts via the piRNA metabolic process, which mediates the repression of transposable elements during meiosis by forming complexes composed of piRNAs and Piwi proteins and governs the methylation and subsequent repression of transposons. Directly binds methylated piRNAs, a class of 24 to 30 nucleotide RNAs that are generated by a Dicer-independent mechanism and are primarily derived from transposons and other repeated sequence elements. Strongly prefers a uridine in the first position of their guide (g1U preference, also named 1U-bias). Not involved in the piRNA amplification loop, also named ping-pong amplification cycle. Acts as an endoribonuclease that cleaves transposon messenger RNAs. Besides their function in transposable elements repression, piRNAs are probably involved in other processes during meiosis such as translation regulation. Probable component of some RISC complex, which mediates RNA cleavage and translational silencing. Also plays a role in the formation of chromatoid bodies and is required for some miRNAs stability. Required to sequester RNF8 in the cytoplasm until late spermatogenesis; RNF8 being released upon ubiquitination and degradation of PIWIL1.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:Q9JMB7}. Note=Component of the meiotic nuage, also named P granule, a germ-cell-specific organelle required to repress transposon activity during meiosis. Also present in chromatoid body. {ECO:0000250|UniProtKB:Q9JMB7}.
Interaction partners:
- Tudor domain-containing protein 6
- Tudor and KH domain-containing protein
- Pirin
- Tudor domain-containing protein 1
- Staphylococcal nuclease domain-containing protein 1
- Endoribonuclease Dicer
- Trinucleotide repeat-containing gene 6A protein
- ATP-dependent RNA helicase TDRD9
- Tudor domain-containing protein 5
- RNA helicase Mov10l1
Sequence:
MTGRARARARGRARGQETAQLVGSTASQQPGYIQPRPQPPPAEGELFGRGRQRGTAGGTAKSQGLQISAGFQELSLAERGGRRRDFHDLGVNTRQNLDHVKESKTGSSGIIVRLSTNHFRLTSRPQWALYQYHIDYNPLMEARRLRSALLFQHEDLIGKCHAFDGTILFLPKRLQQKVTEVFSKTRNGEDVRITITLTNELPPTSPTCLQFYNIIFRRLLKIMNLQQIGRNYYNPNDPIDIPSHRLVIWPGFTTSILQYENSIMLCTDVSHKVLRSETVLDFMFNFYHQTEEHKFQEQVSKELIGLVVLTKYNNKTYRVDDIDWDQNPKSTFKKADGSEVSFLEYYRKQYNQEITDLKQPVLVSQPKRRRGPGGTLPGPAMLIPELCYLTGLTDKMRNDFNVMKDLAVHTRLTPEQRQREVGRLIDYIHKNDNVQRELRDWGLSFDSNLLSFSGRILQTEKIHQGGKTFDYNPQFADWSKETRGAPLISVKPLDNWLLIYTRRNYEAANSLIQNLFKVTPAMGMQMRKAIMIEVDDRTEAYLRVLQQKVTADTQIVVCLLSSNRKDKYDAIKKYLCTDCPTPSQCVVARTLGKQQTVMAIATKIALQMNCKMGGELWRVDIPLKLVMIVGIDCYHDMTAGRRSIAGFVASINEGMTRWFSRCIFQDRGQELVDGLKVCLQAALRAWNSCNEYMPSRIIVYRDGVGDGQLKTLVNYEVPQFLDCLKSIGRGYNPRLTVIVVKKRVNTRFFAQSGGRLQNPLPGTVIDVEVTRPEWYDFFIVSQAVRSGSVSPTHYNVIYDNSGLKPDHIQRLTYKLCHIYYNWPGVIRVPAPCQYAHKLAFLVGQSIHREPNLSLSNRLYYL
Protein: Expression site-associated gene (ESAG) protein, putative (Q57YD5)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004609}; Lipid-anchor, GPI-anchor {ECO:0000256|ARBA:ARBA00004609}.
Interaction partners:
Sequence:
MRFWFVLLALLGKETRANYYERNALNATAANKVCELSTYLKGVAHRVNSGSAAVMKKLSDLKIKSAQLQLSVMRNSVPSSEKDCKDIRTLLKTVLKNEFTFQQELEEMRNASALAAAAAGLAAGRLEEWIFAFAQAARTTSQFCISVGGSRPAVHDKLQECFRGTIGPETLYKIEDSHVTKSAEKNLQLHEALSSISFSSLGAESIIERNEDRGCNLMRTATDGLLKGGSLSHSFTWGGGVMNFASSVEGKLNVKGGEYGDVTSYGAVRWTEDPNKVSIFGDVIRLFARFEEAKNAVMEKIKTTADELTKCIGHKEAELTNDQLHEELIGEILNSLELSRRVNEESTSRGQEEVRLKSNYSAEPARRPVMRAESNPAAHSGVRAAALCSAVLLLRML
Protein: POTE ankyrin domain family member J (P0CG39)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MVAEVDSMPAASSVKKPFVLRSKMGKWCRHCFPCCRGSGKSNVGTSGDQDDSTMKTLRSKMGKWCCHCFPCCRGSGKSNVGAWGDYDDSAFVEPRYHVRREDLDKLHRAAWWGKVARKDLIVMLRDTDVNKQDKQKRTALHLASANGNSGVVKLLLDRRCQLNVLDNKKRTALTKAVQCQEDECALMLLEHGTDPNIPDEYGNTTLHYAIYNEDKLMAKALLLYGADIESKNKHGLTPLLLGVHEQKQQVVKFLIKKKANLNALDRYGRTALILAVCCGSASIVSLLLEQNIDVSSQDLSGQTAREYAVSSHHHVICQLLSDYKEKQMLKISSENSNPEQDLKLTSEEESQRFKGSENSQPEKMSQEPEINKDGDREVEEEMKKHESNNVGLLENLSNGVTAGNGDDGLIPQRKSRTPENQQFPDNESEEYHRICELVSDYKEKQMPKYSSENSNPEQDLKLTSEEESQRLKGSENGQPEKRSQEPEINKDGDRELENFMAIEEMKKHGSTHVGFPENLTNGATAGNGDDGLIPPRKSRTPESQQFPDTENEEYHSDEQNDTQKQFCEEQNTGILHDEILIHEEKQIEVVEKMNSELSLSCKKERDFLHENSMLREEIAMLRLELDTMKHQSQLRKKKYLEDIESVKKKNDNLLKALQLNELTMDDDTAVLVIDNGSGMCKAGFAGDDAPRAVFPSIVGCPRQQGMMGGMHQKESYVGKEAQSKRGILTLKYPMEHGIITNWDDMEKIWHHTFYNELRVAPEEHPILLTEAPLNPKANREKMTQIMFETFNTPAMYVAIQAMLSLYTSGRTTGIVMDSGDGVTHTVPIYDGNALPHATLRLDLAGRELTDYLMKILTERGYRFTTMAEREIVRDIKEKLCYVALDFEQEMAMVASSSSLEKSYELPDGQVITISNEWFRCPEALFQPCFLGMESCGIHETTFNSIMKSDVDIRKDLYTNTVLSGGTTMYPGMAHRMQKEIAALAPSMMKIRIIAPPKRKYSVWVGGSILASLSTFQQMWISKQEYDESGPSIVHRKCF
Protein: Protein aveugle (Q8ML92)
Organism: Drosophila melanogaster (Fruit fly)
Function: Required for normal photoreceptor differentiation between Ras and Raf for EGFR signaling in the eye and for mitogen-activated protein kinase phosphorylation. Probably acts together with Cnk to promote Raf activation, perhaps by recruiting an activating kinase.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16600911}. Membrane {ECO:0000269|PubMed:16600911}; Peripheral membrane protein {ECO:0000269|PubMed:16600911}.
Interaction partners:
- Connector enhancer of KSR protein CNK
- AT08303p
- Raf homolog serine/threonine-protein kinase Raf
- MAP/microtubule affinity-regulating kinase 3
- Dual specificity mitogen-activated protein kinase kinase dSOR1
- Tyrosine-protein kinase Src42A
- Ras-like protein 1
Sequence:
MGEETINSTQNKTRTKTTRPKAVYLWTVSDVLKWYRRHCGEYTQYEQLFAQHDITGRALLRITDSSLQRMGVTDNRDREAIWREIVKQRLKTDIMEIRDMERLNIY
Protein: Muscarinic acetylcholine receptor M2 (Q9ERZ4)
Organism: Mus musculus (Mouse)
Function: The muscarinic acetylcholine receptor mediates various cellular responses, including inhibition of adenylate cyclase, breakdown of phosphoinositides and modulation of potassium channels through the action of G proteins. Primary transducing effect is adenylate cyclase inhibition. Signaling promotes phospholipase C activity, leading to the release of inositol trisphosphate (IP3); this then triggers calcium ion release into the cytosol (By similarity).
Subcellular location: Cell membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Postsynaptic cell membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Note=Phosphorylation in response to agonist binding promotes receptor internalization. {ECO:0000250}.
Interaction partners:
- Proteinase-activated receptor 1
- Guanine nucleotide-binding protein G
- Muscarinic acetylcholine receptor M1
- Guanine nucleotide-binding protein subunit gamma
- Lysophosphatidic acid receptor 5
- Lysophosphatidic acid receptor 4
- Lysophosphatidic acid receptor 1
- Lysophosphatidic acid receptor 2
- Kininogen-1
- Lysophosphatidic acid receptor 3
Sequence:
MNNSTNSSNNGLAITSPYKTFEVVFIVLVAGSLSLVTIIGNILVMVSIKVNRHLQTVNNYFLFSLACADLIIGVFSMNLYTLYTVIGYWPLGPVVCDLWLALDYVVSNASVMNLLIISFDRYFCVTKPLTYPVKRTTKMAGMMIAAAWVLSFILWAPAILFWQFIVGVRTVEDGECYIQFFSNAAVTFGTAIAAFYLPVIIMTVLYWHISRASKSRIKKEKKEPVANQDPVSPSLVQGRIVKPNNNNMPGGDGGLEHNKIQNGKAPRDGGTENCVQGEEKESSNDSTSVSAVASNMRDDEITQDENTVSTSLGHSKDDNSRQTCIKIVTKTQKGDACTPTSTTVELVGSSGQNGDEKQNIVARKIVKMTKQPAKKKPPPSREKKVTRTILAILLAFIITWAPYNVMVLINTFCAPCIPNTVWTIGYWLCYINSTINPACYALCNATFKKTFKHLLMCHYKNIGATR
Protein: Thiol-specific monooxygenase (EC 1.14.13.-) (Flavin-dependent monooxygenase) (P38866)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Flavin-dependent oxidation of thiol-containing compounds. Probably required for the correct folding of disulfide-bonded proteins.
Interaction partners:
- Ubiquinone biosynthesis monooxygenase COQ6, mitochondrial
Sequence:
MTVNDKKRLAIIGGGPGGLAAARVFSQSLPNFEIEIFVKDYDIGGVWHYPEQKSDGRVMYDHLETNISKKLMQFSGFPFEENVPLYPSRRNIWEYLKAYYKTFIANKDAISIHFSTEVTYLKKKNSQWEITSKDELRTTKSDFDFVIVASGHYSVPKLPTNIAGLDLWFDNKGAFHSKDFKNCEFAREKVVIVVGNGSSGQDIANQLTTVAKKVYNSIKEPASNQLKAKLIETVQTIDSADWKNRSVTLSDGRVLQNIDYIIFATGYYYSFPFIEPSVRLEVLGEGVTGDKHSSVNLHNLWEHMIYVKDPTLSFILTPQLVIPFPLSELQAAIMVEVFCKSLPITTTFDSNACGTHNFPKGKDLEYYAELQELLNSIPRRVGHFEPVVWDDRLIDLRNSSYTDKEERNVLLAEHAQALKKKKAPYFLPAPHT
Protein: DNA-directed RNA polymerases I, II, and III subunit RPABC3 (RNA polymerases I, II, and III subunit ABC3) (ABC14.4) (ABC14.5) (DNA-directed RNA polymerases I, II, and III 14.5 kDa polypeptide) (P20436)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: DNA-dependent RNA polymerases catalyze the transcription. of DNA into RNA using the four ribonucleoside triphosphates as substrates. Common component of RNA polymerases I, II and III which synthesize ribosomal RNA precursors, mRNA precursors and many functional non-coding RNAs, and small RNAs, such as 5S rRNA and tRNAs, respectively.
Subcellular location: Nucleus {ECO:0000269|PubMed:14562095}.
Interaction partners:
- DNA-directed RNA polymerases I and III subunit RPAC2
- DNA-directed RNA polymerase I subunit RPA49
- DNA-directed RNA polymerase II subunit RPB2
- DNA-directed RNA polymerase I subunit RPA135
- DNA-directed RNA polymerases I, II, and III subunit RPABC2
- DNA-directed RNA polymerase II subunit RPB3
- DNA-directed RNA polymerase I subunit RPA43
- DNA-directed RNA polymerase II subunit RPB9
- DNA-directed RNA polymerases I and III subunit RPAC1
- DNA-directed RNA polymerase III subunit RPC6
Sequence:
MSNTLFDDIFQVSEVDPGRYNKVCRIEAASTTQDQCKLTLDINVELFPVAAQDSLTVTIASSLNLEDTPANDSSATRSWRPPQAGDRSLADDYDYVMYGTAYKFEEVSKDLIAVYYSFGGLLMRLEGNYRNLNNLKQENAYLLIRR
Protein: Poly(rC)-binding protein 4 (Alpha-CP4) (P57724)
Organism: Mus musculus (Mouse)
Function: Single-stranded nucleic acid binding protein that binds preferentially to oligo dC.
Subcellular location: Cytoplasm {ECO:0000250}.
Interaction partners:
Sequence:
MSSSDAGLEEGPELSITLTLRMLMHGKEVGSIIGKKGETVKRIREQSSARITISEGSCPERITTITGSTAAVFHAVSMIAFKLDEDLCAAPANGGSVSRPPVTLRLVIPASQCGSLIGKAGTKIKEIRETTGAQVQVAGDLLPNSTERAVTVSGVPDAIILCVRQICAVILESPPKGATIPYHPSLSLGTVLLSANQGFSVQGQYGAVTPAEVTKLQQLSGHAVPFASPSVVPGMDPSTQTSSQEFLVPNDLIGCVIGRQGSKISEIRQMSGAHIKIGNQAEGAGERHVTITGSPVSIALAQYLITACLETAKSTSGGTPGSAPADLPTPFSPPLTALPTAPPGLLGTPYAISLSNFIGLKPVPFLALPPASPGPPPGLAAYTAKMAAANGSKKAERQKFSPY
Protein: Serine/threonine-protein kinase BSK2 (EC 2.7.11.1) (Brassinosteroid-signaling kinase 2) (Q9LS26)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Probable serine/threonine kinase that acts as positive regulator of brassinosteroid (BR) signaling downstream of the receptor kinase BRI1. Mediates signal transduction from BRI1 by functioning as substrate of BRI1.
Subcellular location: Cell membrane {ECO:0000269|PubMed:18653891}; Lipid-anchor {ECO:0000305|PubMed:12912986}.
Interaction partners:
- Serine/threonine-protein phosphatase BSU1
- Protein BRASSINOSTEROID INSENSITIVE 1
- BRASSINOSTEROID INSENSITIVE 1-associated receptor kinase 1
- Shaggy-related protein kinase eta
- BRI1 kinase inhibitor 1
- Protein BRASSINAZOLE-RESISTANT 1
- Putative acyl-activating enzyme 19
- Serine carboxypeptidase 24
Sequence:
MGCLHSKTANLPSSDDPSAPNKPESVNGDQVDQEIQNFKEFELNELRKATNGFSPSCIVSEGGEKAPNVVYRGKLEGNHLVAIKRFSRQSWPDAQQFVVEATGVGKLRNKRIVSLIGCCAEGDERLLVAEYMPNDTLSKHLFHWEKQPLPWDMRVRIADYIAEALDYCNIENRKIYHDLNAYRILFDEEGDPRLSTFGLMKNSRDGKSYSTNLAYTPPEFLRTGRVIPESVIFSYGTILLDLLSGKHIPPSHALDIIRGKNALLLMDSSLEGQYANDDATKLVDLASKCLQSEAKDRPDTKFLLSAVAPLQKQEEVASHVLMGLPKNTVILPTMLSPLGKACAKMDLATFHDILLKTGYRDEEGAENELSFQEWTQQVQEMLNTKKFGDIAFRDKDFKNSIEYYSKLVGMMPVPSATVFARRAFSYLMTDQQELALRDAMQAQVCIPEWPTAFYLQALALSKLGMETDAQDMLNDGAAYDAKRQNSWRC