wanglab/gogpt-training-data huggingface dataset:
Protein: NmrA-like domain-containing protein (G4NE58)
Organism: Pyricularia oryzae (strain 70-15 / ATCC MYA-4617 / FGSC 8958) (Rice blast fungus) (Magnaporthe oryzae)
Interaction partners:
- NADH:ubiquinone oxidoreductase 30kDa subunit domain-containing protein
- Cytochrome b-c1 complex subunit Rieske, mitochondrial
- 4Fe-4S ferredoxin-type domain-containing protein
- NADH-quinone oxidoreductase subunit D domain-containing protein
- NADH-ubiquinone oxidoreductase
- quinol--cytochrome-c reductase
- NADH dehydrogenase flavoprotein 1, mitochondrial
- NADH dehydrogenase 1 beta subcomplex subunit 9
- NADH dehydrogenase 1 alpha subcomplex subunit
- NADH-ubiquinone oxidoreductase 24 kDa subunit
Sequence:
MASKKIITVFGATGKQGGSIVEKFISDPKLKDEWAVRGVTRDVSKDSAKALASRGVEVVSADMDDKESVFKAVAGSHTVFSVTNYWEKLSKDGETQQGKNIADAAKEAGVQHFIWSTLINVTNVSKGKLTKVYHFDSKAEVDAYVRSLGIPTTFFLAGFYLSNFEAPMWFRQTGPDNAWTFSMPGPITSPVPLYDVRDTGKYVKAIVLNRDALLGGRVLAATEYQTFEEMLVDFRRTFPKDGANARFYELSDEQYLEGVRSAGMPDFVGEELLQNIQLLSQFGYYGGESLDETRKLVEGVGERLTTWAEWLPQSEVFKNLQ
Protein: Regulator of liu genes (Q9I295)
Organism: Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Interaction partners:
- Isovaleryl-CoA dehydrogenase, mitochondrial
- Biotin carboxylase
- Methylcrotonyl-CoA carboxylase, beta-subunit
- Expressed protein with apparent function in citronellol catabolism
- 3-methylglutaconyl-CoA hydratase
- 3-hydroxy-3-isohexenylglutaryl-CoA/hydroxy-methylglutaryl-CoA lyase
- Aromatic amino acid transport protein AroP2
- Probable transcriptional regulator
- Very-long chain acyl-CoA synthetase
- Z-ring associated protein G
Sequence:
MSITYTISDLARELDITTRAIRFYEEQGLLSPERRGQERIYSPRDKVSLKLILRGKRIGFSLAECRELIELYDPDPSSGNQKQLNTMLEKIAERRAQLEQQLLDIEQMQLELDTAEERCRAALIKSYNKHTVET
Protein: Homer protein homolog 3 (Homer-3) (Q99JP6)
Organism: Mus musculus (Mouse)
Function: Postsynaptic density scaffolding protein. Binds and cross-links cytoplasmic regions of GRM1, GRM5, ITPR1, DNM3, RYR1, RYR2, SHANK1 and SHANK3. By physically linking GRM1 and GRM5 with ER-associated ITPR1 receptors, it aids the coupling of surface receptors to intracellular calcium release. Isoforms can be differently regulated and may play an important role in maintaining the plasticity at glutamatergic synapses (By similarity). Negatively regulates T cell activation by inhibiting the calcineurin-NFAT pathway. Acts by competing with calcineurin/PPP3CA for NFAT protein binding, hence preventing NFAT activation by PPP3CA.
Subcellular location: Cytoplasm {ECO:0000250}. Postsynaptic density {ECO:0000250}. Synapse {ECO:0000250}. Note=Postsynaptic density of neuronal cells. {ECO:0000250}.
Interaction partners:
- SH3 and multiple ankyrin repeat domains protein 1
- Homer protein homolog 1
- Inositol 1,4,5-trisphosphate-gated calcium channel ITPR1
- Metabotropic glutamate receptor 5
- Metabotropic glutamate receptor 1
- Disks large-associated protein 1
- SH3 and multiple ankyrin repeat domains protein 3
- Alpha-actinin-1
Sequence:
MSTAREQPIFSTRAHVFQIDPTTKRNWIPAGKHALTVSYFYDATRNVYRIISIGGAKAIINSTVTPNMTFTKTSQKFGQWADSRANTVYGLGFASEQQLTQFAEKFQEVKEAARLAREKSQDGGEFTSTGLALASHQVPPSPLVSTNGPGEEKLFRSQSADTPGPTERERLKKMLSEGSVGEVQWEAEFFALQDSNQRLAGALREANAAATQWRQQLEVQRAEAELLRQRVAELEAQVAVEPVRAGEKEATSQSVEQLEARVQTKDQTLKNQSTGTREAPDTAEREETQQQVQDLETRNAELEQQLRSMECNLEEARAERERARAEVGRAAQLLDVRLFELSELREGLARLAEAAP
Protein: Beta-1,3-N-acetylglucosaminyltransferase lunatic fringe (EC 2.4.1.222) (O-fucosylpeptide 3-beta-N-acetylglucosaminyltransferase) (Q8NES3)
Organism: Homo sapiens (Human)
Function: Glycosyltransferase that initiates the elongation of O-linked fucose residues attached to EGF-like repeats in the extracellular domain of Notch molecules. Modulates NOTCH1 activity by modifying O-fucose residues at specific EGF-like domains resulting in inhibition of NOTCH1 activation by JAG1 and enhancement of NOTCH1 activation by DLL1 via an increase in its binding to DLL1 (By similarity). Decreases the binding of JAG1 to NOTCH2 but not that of DLL1. Essential mediator of somite segmentation and patterning (By similarity).
Subcellular location: Golgi apparatus {ECO:0000250|UniProtKB:O09010}. Golgi apparatus membrane {ECO:0000305}; Single-pass type II membrane protein {ECO:0000305}.
Interaction partners:
- Neurogenic locus notch homolog protein 2
- Neurogenic locus notch homolog protein 1
- Neurogenic locus notch homolog protein 3
- Neurogenic locus notch homolog protein 4
- Mesoderm posterior protein 2
- Beta-1,3-N-acetylglucosaminyltransferase manic fringe
- Beta-1,3-N-acetylglucosaminyltransferase radical fringe
- Delta-like protein 1
- Delta-like protein 3
- Protein jagged-1
Sequence:
MLKRCGRRLLLALAGALLACLLVLTADPPPPPLPAERGRRALRSLAGPAGAAPAPGLGAAAAAPGALVRDVHSLSEYFSLLTRARRDAGPPPGAAPRPADGHPRPLAEPLAPRDVFIAVKTTKKFHRARLDLLLETWISRHKEMTFIFTDGEDEALARHTGNVVITNCSAAHSRQALSCKMAVEYDRFIESGRKWFCHVDDDNYVNLRALLRLLASYPHTRDVYVGKPSLDRPIQAMERVSENKVRPVHFWFATGGAGFCISRGLALKMSPWASGGHFMNTAERIRLPDDCTIGYIVEALLGVPLIRSGLFHSHLENLQQVPTSELHEQVTLSYGMFENKRNAVHVKGPFSVEADPSRFRSIHCHLYPDTPWCPRTAIF
Protein: Medium/long-chain-fatty-acid--[acyl-carrier-protein] ligase FadD10 (EC 6.2.1.20) (EC 6.2.1.47) (FAAL10) (P9WQ55)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: Catalyzes the activation of medium/long-chain fatty acids as acyl-adenylates (acyl-AMP), which are then transferred to the phosphopantetheine arm of the acyl carrier protein (ACP) Rv0100. Can use octanoate (C8), decanoate (C10), dodecanoate (C12), tetradecanoate (C14) and hexadecanoate (C16), but not hexanoate (C6). Long chain saturated fatty acids are the preferred substrates. Cannot use coenzyme A to form acyl-CoA.
Subcellular location: Cytoplasm {ECO:0000305}.
Interaction partners:
- Acyl carrier protein Rv0100
- (3R)-3-[(carboxymethyl)amino]fatty acid oxygenase/decarboxylase
- Isonitrile lipopeptide synthase
- 
- Uncharacterized PPE family protein PPE1
- Probable fatty-acid-CoA ligase FadD18
- Probable fatty-acid-CoA ligase FadD34
- Probable multifunctional mycocerosic acid synthase membrane-associated Mas
- Polyketide synthase Pks13
- Phthioceranic/hydroxyphthioceranic acid synthase
Sequence:
MGGKKFQAMPQLPSTVLDRVFEQARQQPEAIALRRCDGTSALRYRELVAEVGGLAADLRAQSVSRGSRVLVISDNGPETYLSVLACAKLGAIAVMADGNLPIAAIERFCQITDPAAALVAPGSKMASSAVPEALHSIPVIAVDIAAVTRESEHSLDAASLAGNADQGSEDPLAMIFTSGTTGEPKAVLLANRTFFAVPDILQKEGLNWVTWVVGETTYSPLPATHIGGLWWILTCLMHGGLCVTGGENTTSLLEILTTNAVATTCLVPTLLSKLVSELKSANATVPSLRLVGYGGSRAIAADVRFIEATGVRTAQVYGLSETGCTALCLPTDDGSIVKIEAGAVGRPYPGVDVYLAATDGIGPTAPGAGPSASFGTLWIKSPANMLGYWNNPERTAEVLIDGWVNTGDLLERREDGFFYIKGRSSEMIICGGVNIAPDEVDRIAEGVSGVREAACYEIPDEEFGALVGLAVVASAELDESAARALKHTIAARFRRESEPMARPSTIVIVTDIPRTQSGKVMRASLAAAATADKARVVVRG
Protein: Toucan, isoform F (A8DYU0)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MFENFEFTNENLSAQTMDLDIDLISWTVPSTPTSTTFTDNFNFAQAFEEQQLDAVACKENKHQCARTKGTLEKTILLLQHTQKDCERLREDLEDKGLEWIQRQQEKEYLHRTELKQAEEKLMEVQLRAKLKFCELESQLRAKDEESKQAQEAYRMEVSHKLALKQEHLRTAEQKIQELQTRLQQVETEEQGHREELIRKENIHTARLAEANQREQDLIDRVKSLTKELNTLKANKEHNERDLRDRLALSQDEISVLRTSSQRRSPCTSLPDNASAELNRLTSEADSLRCVLELKQAEISALSKAKADLIHESEERLKLSNRVALLEAQNEMLRTELEAKTEKEKEIQQKMEELQKAYKYESIKRTRLTYDKEELQYHLKQRSLQLQSAESKLQDLSTGSHDNSLSSHSRCSLGRSGLEIAVTTSSPTSPVMKGMIERNDSVSWTLEIEDESFKGNTSKIVRRAGSLRSNNERCPIQRRQTLTSNGHSNGSATNGGSSPAHPNPLSQSMSATALLRSSSNSGESEGRPLSRARSKSMCIKASATSSAVCESSGQRKKPQDELSLADWPEDIPLCSSSPQAPGIEMRPRSSTMKLMSSEAKKFQEIQESAGEAMVSGANSEDESCSASSEDIMRSSSASSTASGGSLSKRPKQPPSRMSIEEALPCTPMEVSWSEDAADANGLA
Protein: 3-methyl-2-oxobutanoate hydroxymethyltransferase (EC 2.1.2.11) (Ketopantoate hydroxymethyltransferase) (KPHMT) (Q5F9F9)
Organism: Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090)
Function: Catalyzes the reversible reaction in which hydroxymethyl group from 5,10-methylenetetrahydrofolate is transferred onto alpha-ketoisovalerate to form ketopantoate.
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00156}.
Interaction partners:
- Pantothenate synthetase
- Aspartate 1-decarboxylase
- Dihydroxy-acid dehydratase
- branched-chain-amino-acid transaminase
- Probable nicotinate-nucleotide pyrophosphorylase [carboxylating]
Sequence:
MITVNTLQKMKAAGEKIVMLTAYESSFAALMDDAGVDVLLVGDSLGMAVQGRQSTLPVSLRDMCYHTECVARGAKNAMIVSDLPFGAYQQSKEQAFAAAAELMAAGAHMVKLEGGVWMAETTEFLQMRGIPVCAHIGLTPQSVFAFGGYKVQGRGGKAQALLNDAKAHDEAGAAVVLMECVPAELAKKVTETVSCPTIGIGAGADCDGQVLVMHDMLGIFPGKTAKFVKNFMRGQSSIQAAVRAYVAEVKAKTFPAAEHIFAD
Protein: MAP3K12 binding inhibitory protein 1 (S4R2X9)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
XTELNRPSSGDRNLERRCRPNLSREVLYEIFRSLHTLVGQLDLRDDVVKITIDWNKLQSLSAFQPALLFSALEQHILYLQPFLAKLQSPIKEENTTAVEEIGRTEMGNKNEVNDKFSIGDLQEEEKHKESDLRDVKKTQIHFDPEVVQIKAGKAEIDRRISAFIERKQAEINENNVREFCNVIDCNQENSCARTDAIFTPYPGFKSHVKVSRVVNTYGPQTRPEGIPGSGHKPNSMLRDCGNQAVEERLQNIEAHLRLQTGGPVPRDIYQRIKKLEDKILELEGISPEYFQSVVSISVF
Protein: Single-stranded DNA-binding protein 4 (Q9BWG4)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus {ECO:0000250}.
Interaction partners:
- LIM domain-binding protein 1
- Insulin gene enhancer protein ISL-1
- Single-stranded DNA-binding protein 3
- LIM/homeobox protein Lhx1
- LIM domain transcription factor LMO4
- Insulin gene enhancer protein ISL-2
- Single-stranded DNA-binding protein 2
- Isopentenyl-diphosphate delta-isomerase 2
- LIM/homeobox protein Lhx4
- LIM/homeobox protein Lhx9
Sequence:
MYAKGGKGSAVPSDSQAREKLALYVYEYLLHIGAQKSAQTFLSEIRWEKNITLGEPPGFLHSWWCVFWDLYCAAPDRREACEHSGEAKAFQDYSAAAAPSPVMGSMAPGDTMAAGSMAAGFFQGPPGSQPSPHNPNAPMMGPHGQPFMSPRFPGGPRPTLRMPSQPPAGLPGSQPLLPGAMEPSPRAQGHPSMGGPMQRVTPPRGMASVGPQSYGGGMRPPPNSLAGPGLPAMNMGPGVRGPWASPSGNSIPYSSSSPGSYTGPPGGGGPPGTPIMPSPGDSTNSSENMYTIMNPIGQGAGRANFPLGPGPEGPMAAMSAMEPHHVNGSLGSGDMDGLPKSSPGAVAGLSNAPGTPRDDGEMAAAGTFLHPFPSESYSPGMTMSV
Protein: Mannan polymerase complex subunit mnn9 (O36022)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Required for the addition of the long alpha 1,6-mannose backbone of N-linked glycans on cell wall and periplasmic proteins.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:16823372}; Single-pass type II membrane protein {ECO:0000269|PubMed:16823372}. Golgi apparatus membrane {ECO:0000269|PubMed:16823372}; Single-pass type II membrane protein {ECO:0000269|PubMed:16823372}. Note=Cis-Golgi. Recycles between endoplasmic reticulum and Golgi. {ECO:0000250|UniProtKB:P39107, ECO:0000269|PubMed:16823372}.
Interaction partners:
- Uncharacterized alpha-1,2-galactosyltransferase C637.06
- Initiation-specific alpha-1,6-mannosyltransferase
- Mannan polymerase II complex anp1 subunit
- Uncharacterized alpha-1,2-galactosyltransferase C8D2.17
- Inositol phosphoceramide mannosyltransferase 2
- Inositol phosphoceramide mannosyltransferase 1
- Alpha-1,2-galactosyltransferase
- Dolichol phosphate-mannose biosynthesis regulatory protein
- Dolichol-phosphate mannosyltransferase subunit 3
- Dolichol-phosphate mannosyltransferase
Sequence:
MRVYNKSRIVGQLLFVALGITFIYYLFTPSVNSNAKVQIENRGGNSYEIYDMNKITESSDPIRNKEEVLILTPIARFYPQYWKNLLELDYPRNLISLGFIVPSSKDGAKVHRELRNAINAVQKGPGDKRFADVKILIQDSDLSSGQSEAERHKFSAQKERRGKLAATRNTLLLSTLKPSTSWVLWLDSDIVETPSTLIQDLAEHNEDVLVANCFQKQGDKLTPYDFNSWVDSQTAQELASHMDRDEILLEGYAELPTYRMLMAKIYEEHKDPSTIMALDGVGTTALLVKASVHRDGALFPTFPFYHLIESEGFAKMAKRLGHGVYGLPYYLVFHHNE
Protein: Actin-related protein 2/3 complex subunit 1B-B (Q6GNU1)
Organism: Xenopus laevis (African clawed frog)
Function: Component of the Arp2/3 complex, a multiprotein complex that mediates actin polymerization upon stimulation by nucleation-promoting factor (NPF). The Arp2/3 complex mediates the formation of branched actin networks in the cytoplasm, providing the force for cell motility (By similarity). In addition to its role in the cytoplasmic cytoskeleton, the Arp2/3 complex also promotes actin polymerization in the nucleus, thereby regulating gene transcription and repair of damaged DNA. The Arp2/3 complex promotes homologous recombination (HR) repair in response to DNA damage by promoting nuclear actin polymerization, leading to drive motility of double-strand breaks (DSBs) (By similarity).
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:Q7ZXD5}. Nucleus {ECO:0000250|UniProtKB:O15143}.
Interaction partners:
- Actin-related protein 2/3 complex subunit 4
- Actin-related protein 3-A
- Actin-related protein 3-B
- Actin-related protein 2/3 complex subunit 2-B
- Actin-related protein 2/3 complex subunit 2-A
- Actin-related protein 2/3 complex subunit 3-B
- Actin-related protein 2/3 complex subunit 3-A
- Actin-related protein 2
- Actin-related protein 2
- Actin-related protein 2/3 complex subunit 3
Sequence:
MAFHSFLLEPITCHAWNKDATQIAFCPNSHDVHIYKKDGVKWTKIHELKEHNGQVTGIDWAPESNRIVTCGTDRNAYVWTLRNNVWKPTLVILRINRAARCVKWSPKENKFAVGSGSRLISICYFEQENDWWVCKHIKKPIRSTVLSLDWHPNNVLLAAGSSDFKSRIFSSYIKEVEERPAPTPWGSKMPFGELMFESSSSCGWVHSVCFSNSGDRMAWVSHDSTICIADATKKMRVTSLITDTLPLLCVTFITENSLVAAGHDCYPVLYTYDEAQGTLSFGGKLDVPKQSSQRGMTARERFQNLDKKASSDTNNITLDSLHKNSISQISVLSGGKAKCSKFCTTGLDGGMCIWDVKSLESALKDLKIK
Protein: Fanconi anemia complementation group G isoform 3 (A0A0S2Z4A7)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MSRQTTSVGSSCLDLWREKNDRLVRQAKVAQNSGLTLRRQQLAQDALEGLRGLLHSLQGLPAAVPVLPLELTVTCNFIILRASLAQGFTEDQAQDIQRSLERVLETQEQQGPRLEQGLRELWDSVLRASCLLPELLSALHRLVGLQAALWLSADRLGDLALLLETLNGSQSGASKDLLLLLKTWSPPAEELDAPLTLQDAQGLKDVLLTAFAYRQGLQELITGNPDKALSSLHEAASGLCPRPVLVQVYTALGSCHRKMGNPQRALLYLVAALKEGSAWGPPLLEASRLYQQLGDTTAELESLELLVEALNVPCSSKAPQFLIEVELLLPPPDLASPLHCGTQSQTKHILASRCLQTGRAGDAAEHYLDLLALLLDSSEPRFSPPPSPPGPCMPEVFLEAAVALIQAGRAQDALTLCEELLSRTSSLLPKMSRLWEDARKGTKELPYCPLWVSATHLLQGQAWVQLGAQKVAISEFSRCLELLFRATPEEKEQGAAFNCEQGCKSDAALQQLRAAALISRGLEWVASGQDTKALQDFLLSVQMCPGLSPCT
Protein: Acyclic carotenoid 1,2-hydratase (EC 4.2.1.131) (Hydroxyneurosporene synthase) (Lycopene hydratase) (Neurosporene hydratase) (P17058)
Organism: Rhodobacter capsulatus (strain ATCC BAA-309 / NBRC 16581 / SB1003)
Function: Involved in the biosynthesis of carotenoids spheroidene and spirilloxanthin. Catalyzes the hydration of neurosporene to the corresponding hydroxylated carotenoids 1-HO-neurosporene and that of lycopene to 1-HO-lycopene. It exhibits negligible activity in converting HO-neurosporene, HO-lycopene, or any other derivative such as spheroidene, 1-HO-3,4-didehydrolycopene.
Interaction partners:
- Hydroxyneurosporene desaturase
- Demethylspheroidene O-methyltransferase
- Phytoene desaturase
- Spheroidene monooxygenase
- Phytoene synthase
- Geranylgeranyl diphosphate synthase
- Chlorophyllide reductase 52.5 kDa chain
- 2-desacetyl-2-hydroxyethyl bacteriochlorophyllide A dehydrogenase
- Light-independent protochlorophyllide reductase subunit N
- Chlorophyllide reductase subunit Z
Sequence:
MIAFIGSVFSPWYRWSGRREPQNHCCINMVTTGTDGRFTMTDRGRSALRQSRDSFQVGPSKLTWTGKELVIDVDEWGALPKLGKLKGRVVLTPRAVTGVEVRLTPDAGHTWRPFAPIADVEVDLAPGHKWTGHGYFDANFGTRALEEDFSFWTWGRFPLKDRTVCFYDATRLDRTKVALAVQINPDGSVCEIDSPPPLVKMKRTPWFVRRETRCDAGAHPAGVYSLLEAPFYSRALMRTQIDGEETVGMHEALDLVRFRQPVLKPMLAVRVPRRAGWKHKD
Protein: Mitochondrial import inner membrane translocase subunit Tim8 A (Deafness dystonia protein 1 homolog) (Q9WVA2)
Organism: Mus musculus (Mouse)
Function: Mitochondrial intermembrane chaperone that participates in the import and insertion of some multi-pass transmembrane proteins into the mitochondrial inner membrane. Also required for the transfer of beta-barrel precursors from the TOM complex to the sorting and assembly machinery (SAM complex) of the outer membrane. Acts as a chaperone-like protein that protects the hydrophobic precursors from aggregation and guide them through the mitochondrial intermembrane space. The TIMM8-TIMM13 complex mediates the import of proteins such as TIMM23, SLC25A12/ARALAR1 and SLC25A13/ARALAR2, while the predominant TIMM9-TIMM10 70 kDa complex mediates the import of much more proteins (By similarity).
Subcellular location: Mitochondrion inner membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Intermembrane side {ECO:0000250}.
Interaction partners:
- Mitochondrial import inner membrane translocase subunit Tim13
- Mitochondrial import inner membrane translocase subunit Tim10
- Mitochondrial import inner membrane translocase subunit Tim9
- Mitochondrial import inner membrane translocase subunit Tim10 B
- Mitochondrial import inner membrane translocase subunit TIM50
- Putative mitochondrial import inner membrane translocase subunit Tim8 A-B
- Mitochondrial import inner membrane translocase subunit Tim23
Sequence:
MESSTSSSGSALGAVDPQLQHFIEVETQKQRFQQLVHQMTELCWEKCMDKPGPKLDSRAEACFVNCVERFIDTSQFILNRLEQTQKSKPVFSESLSD
Protein: tRNA (guanine(9)-N(1))-methyltransferase (EC 2.1.1.221) (C9JVB6)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MAAFLKMSVSVNFFRPFTRFLVPFTLHRKRNNLTILQRYMSSKIPAVTYPKNESTPPSEELELDKWKTTMKSSVQEECVSTISSSKDEDPLAATREFIEMWRLLGREVPEHITEEELKTLMECVSNTAKKKYLKYLYTKEKVKKARQIKKEMKAAAREEAKNIKLLETTEEDKQKNFLFLRLWDRNMDIAMGWKGAQAMQFGQPLVFDMAYENYMKRKELQNTVSQLLESEGWNRRNVDPFHIYFCNLKIDGALHRELVKRYQEKWDKLLLTSTEKSHVDLFPKDSIIYLTADSPNVMTTFRHDKVYVIGSF
Protein: U2 snRNP component prp10 (Q10178)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Contacts pre-mRNA on both sides of the branch site early in spliceosome assembly.
Subcellular location: Nucleus {ECO:0000269|PubMed:10759889, ECO:0000269|PubMed:16823372, ECO:0000269|PubMed:9837997}.
Interaction partners:
- U2 small nuclear ribonucleoprotein A'
- Splicing factor 3B subunit 6-like protein
- Spliceosome-associated protein 49
- Pre-mRNA-splicing factor sap62
- Uncharacterized protein C211.05
- Pre-mRNA-splicing factor cdc5
- Pre-mRNA-processing factor 19
- Pre-mRNA-splicing factor dre4
- Pre-mRNA-splicing factor cwf10
- Pre-mRNA-splicing factor prp1
Sequence:
MSTGTYPYKMFKMDVTNLNKVEDVEIERLRAERELLRRQKEAAKNSSTNGSVNIEGTQDSNDLQYNAHLFKSSNPKEEYDSAIDVRNDISQDEDDYKRTNDVNDSYRLVRQYEAPKELLNEYADESYDPMQERQSKKQIQDRESDYQKQRYDRQLTPTRVDAFQPDGTQSNGRSYAEVMRQVELEKEERRVHMELNQRRREGTLKEVEEEESISDKKRELELNNTEISQKPKRSRWDQAPPSVTQVSTTKRRSRWDKAPENFTISEHVIENGISEDLINKEVNVVEEKLRPPVRLLTEEELNELLPSEGYAILEPPPGYLESIHPELLQKGTTLDTYHVPQEQELPLEKELPAALPTEIPGVGDLAFFKQEDVKYFGKLLKVEDEAKLTIAELRERKILRLLLKVKNGTPPMRKSALRQLTDQARDFGAAALFNQILPLLMERTLEDQERHLLVKVIDRILYKLDDLVRPFTHKILVVIEPLLIDEDYYARAEGREIISNLAKASGLAHMIATMRPDIDHVDEYVRNTTARAFSVVASALGVPALLPFLKAVCRSKKSWQARHTGVRIIQQIALLLGCSILPHLKNLVDCIGHGLEDEQQKVRIMTALSLSALAEAATPYGIEAFDSVLKPLWSGVQRHRGKSLAAFLKATGFIIPLMEPEYASHFTRRIMKILLREFNSPDEEMKKIVLKVVSQCASTDGVTPEYLRTDVLPEFFHCFWSRRMASDRRSYKQVVETTVVLAQQVGSRQIVERVVNNFKDESEPYRKMTAETVDKVIGSLGVSEIDERLEELLLDGVLFAFQEQSVEEKVILTCFSTVVNALGTRCKPYLPQIVSTILYRLNNKSANVREQAADLVSSITIVLKACGEEALMRKLGVVLYEYLGEEYPEVLGSILGAIKAIVSVVGMSSMQPPIRDLLPRLTPILRNRHEKVQENTIDLVGKIADRGSEYVSAREWMRICFELIDMLKAHKKSIRRAAVNTFGYISKAIGPQDVLATLLNNLKVQERQNRVCTTVAIAIVAETCMPFTVVPALMADYRTPEMNVQNGVLKSLAFMFEYIGEQARDYVYAITPLLADALMDRDAVHRQTAASVIKHLSLGCVGLGVEDAMIHLLNILWPNILEESPHVINAVREGIDGIRNCIGVGPIMAYLVQGLFHPSRKVRNTYWTSYNSAYVQSADAMVPYYPHVDDDQFNNYDMKTLHICI
Protein: Ras/Rap GTPase-activating protein SynGAP (Neuronal RasGAP) (Synaptic Ras GTPase-activating protein 1) (Synaptic Ras-GAP 1) (p135 SynGAP) (Q9QUH6)
Organism: Rattus norvegicus (Rat)
Function: Major constituent of the PSD essential for postsynaptic signaling. Inhibitory regulator of the Ras-cAMP pathway. Member of the NMDAR signaling complex in excitatory synapses, it may play a role in NMDAR-dependent control of AMPAR potentiation, AMPAR membrane trafficking and synaptic plasticity. Regulates AMPAR-mediated miniature excitatory postsynaptic currents. Exhibits dual GTPase-activating specificity for Ras and Rap. May be involved in certain forms of brain injury, leading to long-term learning and memory deficits.
Subcellular location: Membrane; Peripheral membrane protein. Synapse. Note=Mostly in excitatory glutamatergic synapses.
Interaction partners:
- Disks large homolog 4
- Disks large homolog 3
- Glutamate receptor ionotropic, NMDA 2B
- SH3 and multiple ankyrin repeat domains protein 1
- Disks large-associated protein 1
- Glutamate receptor 1
- SH3 and multiple ankyrin repeat domains protein 3
- Disks large homolog 2
- Disks large homolog 1
- Glutamate receptor ionotropic, NMDA 1
Sequence:
MSRSRASIHRGSIPAMSYAPFRDVRGPPMHRTQYVHSPYDRPGWNPRFCIISGNQLLMLDEDEIHPLLIRDRRSESSRNKLLRRTVSVPVEGRPHGEHEYHLGRSRRKSVPGGKQYSMEAAPAAPFRPSQGFLSRRLKSSIKRTKSQPKLDRTSSFRQILPRFRSADHDRARLMQSFKESHSHESLLSPSSAAEALELNLDEDSIIKPVHSSILGQEFCFEVTTSSGTKCFACRSAAERDKWIENLQRAVKPNKDNSRRVDNVLKLWIIEARELPPKKRYYCELCLDDMLYARTTSKPRSASGDTVFWGEHFEFNNLPAVRALRLHLYRDSDKKRKKDKAGYVGLVTVPVATLAGRHFTEQWYPVTLPTGSGGSGGMGSGGGGGSGGGSGGKGKGGCPAVRLKARYQTMSILPMELYKEFAEYVTNHYRMLCAVLEPALNVKGKEEVASALVHILQSTGKAKDFLSDMAMSEVDRFMEREHLIFRENTLATKAIEEYMRLIGQKYLKDAIGEFIRALYESEENCEVDPIKCTASSLAEHQANLRMCCELALCKVVNSHCVFPRELKEVFASWRLRCAERGREDIADRLISASLFLRFLCPAIMSPSLFGLMQEYPDEQTSRTLTLIAKVIQNLANFSKFTSKEDFLGFMNEFLELEWGSMQQFLYEISNLDTLTNSSSFEGYIDLGRELSTLHALLWEVLPQLSKEALLKLGPLPRLLSDISTALRNPNIQRQPSRQSERARSQPMVLRGPSAEMQGYMMRDLNSSIDLQSFMARGLNSSMDMARLPSPTKEKPPPPPPGGGKDLFYVSRPPLARSSPAYCTSSSDITEPEQKMLSVNKSVSMLDLQGDGPGGRLNSSSVSNLAAVGDLLHSSQASLTAALGLRPAPAGRLSQGSGSSITAAGMRLSQMGVTTDGVPAQQLRIPLSFQNPLFHMAADGPGPPAGHGGSSGHGPPSSHHHHHHHHHHRGGEPPGDTFAPFHGYSKSEDLSTGVPKPPAASILHSHSYSDEFGPSGTDFTRRQLSLQDNLQHMLSPPQITIGPQRPAPSGPGGGSGGGSGGGGGGQPPPLQRGKSQQLTVSAAQKPRPSSGNLLQSPEPSYGPARPRQQSLSKEGSIGGSGGSGGGGGGGLKPSITKQHSQTPSTLNPTMPASERTVAWVSNMPHLSADIESAHIEREEYKLKEYSKSMDESRLDRVKEYEEEIHSLKERLHMSNRKLEEYERRLLSQEEQTSKILMQYQARLEQSEKRLRQQQVEKDSQIKSIIGRLMLVEEELRRDHPAMAEPLPEPKKRLLDAQRGSFPPWVQQTRV
Protein: Spanin, outer lipoprotein subunit (o-spanin) (gene product 23.1) (gp23.1) (P0DTL7)
Organism: Escherichia phage Mu (Bacteriophage Mu)
Function: Component of the spanin complex that disrupts the host outer membrane and participates in cell lysis during virus exit. The spanin complex conducts the final step in host lysis by disrupting the outer membrane after holin and endolysin action have permeabilized the inner membrane and degraded the host peptidoglycans. Host outer membrane disruption is possibly due to local fusion between the inner and outer membrane performed by the spanin complex.
Subcellular location: Host cell outer membrane {ECO:0000305}; Lipid-anchor {ECO:0000305}; Periplasmic side {ECO:0000305}.
Interaction partners:
Sequence:
MMQKKKLQPPLLVTIAALVLCLPLLLTGCGNSKNAPVPSVVILPEIDTELTEATPVPPMPQPLTWGASLLWNADLLMALGQCNRDKASVREQEIRRKEIYERRPEPGGGAAAR
Protein: Probable RNA-binding protein EIF1AD (Eukaryotic translation initiation factor 1A domain-containing protein) (Q23646)
Organism: Caenorhabditis elegans
Interaction partners:
- Ubiquitin-like domain-containing protein
- Serine/threonine-protein kinase RIO1
- Small ribosomal subunit protein uS13
- Small ribosomal subunit protein uS19
- Signal transducer and activator of transcription 1
Sequence:
MSAATKKRYITNKVGSEFYELVDEDIIAQVRQSRGNNLHEVLDQNGDSYVVSMPTKFRKSVWLRRDQFVVVRPITEGDKVKGEIEYILDQDNVLYIRELGKWPTCFEENALKMTREAKRGQTSDKMIDDDMLPPSESEEEDESEGEETYDEDDVDDEEEEEFDTYNPNRMQAPSK
Protein: Protein RER1 (Q5T092)
Organism: Homo sapiens (Human)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
Sequence:
MSEGDSVGESVHGKPSVVYRFFTRLGQIYQSWLDKSTPYTAVRWVVTLGLSFVYMIRVYLLQGWYIVTYALGIYHLNLFIAFLSPKVDPSLMEDSDDGPSLPTKQNEEFRPFIRRLPEFKFWHAATKGILVAMVCTFFDAFNVPVFWPILVMYFIMLF
Protein: Paired box protein Pax-7 (HuP1) (P23759)
Organism: Homo sapiens (Human)
Function: Transcription factor that is involved in the regulation of muscle stem cells proliferation, playing a role in myogenesis and muscle regeneration.
Subcellular location: Nucleus {ECO:0000250|UniProtKB:P47239}.
Interaction partners:
- Myogenin
- Myoblast determination protein 1
- Forkhead box protein O1
- Paired box protein Pax-3
- Myogenic factor 5
- Set1/Ash2 histone methyltransferase complex subunit ASH2
- Myogenic factor 6
- Homeobox protein SIX1
- Transcription factor SOX-10
- Zinc finger protein SNAI2
Sequence:
MAALPGTVPRMMRPAPGQNYPRTGFPLEVSTPLGQGRVNQLGGVFINGRPLPNHIRHKIVEMAHHGIRPCVISRQLRVSHGCVSKILCRYQETGSIRPGAIGGSKPRQVATPDVEKKIEEYKRENPGMFSWEIRDRLLKDGHCDRSTVPSGLVSSISRVLRIKFGKKEEEDEADKKEDDGEKKAKHSIDGILGDKGNRLDEGSDVESEPDLPLKRKQRRSRTTFTAEQLEELEKAFERTHYPDIYTREELAQRTKLTEARVQVWFSNRRARWRKQAGANQLAAFNHLLPGGFPPTGMPTLPPYQLPDSTYPTTTISQDGGSTVHRPQPLPPSTMHQGGLAAAAAAADTSSAYGARHSFSSYSDSFMNPAAPSNHMNPVSNGLSPQVMSILGNPSAVPPQPQADFSISPLHGGLDSATSISASCSQRADSIKPGDSLPTSQAYCPPTYSTTGYSVDPVAGYQYGQYGQTAVDYLAKNVSLSTQRRMKLGEHSAVLGLLPVETGQAY