wanglab/gogpt-training-data huggingface dataset:
Protein: Alpha-amylase 1 (EC 3.2.1.1) (1,4-alpha-D-glucan glucanohydrolase 1) (Salivary and hepatic alpha-amylase) (P00687)
Organism: Mus musculus (Mouse)
Subcellular location: Secreted.
Interaction partners:
- Glycogen phosphorylase, liver form
- Glycogen phosphorylase, muscle form
- Glycogen phosphorylase, brain form
- 1,4-alpha-glucan-branching enzyme
- Glycogen debranching enzyme
- Sucrase-isomaltase, intestinal
- Sucrase-isomaltase, intestinal
- Lysosomal alpha-glucosidase
- Neutral alpha-glucosidase C
- Pancreatic alpha-amylase 2a5
Sequence:
MKFFLLLSLIGFCWAQYDPHTQYGRTAIVHLFEWRWVDIAKECERYLAPNGFAGVQVSPPNENIVVHSPSRPWWERYQPISYKICSRSGNEDEFRDMVNRCNNVGVRIYVDAVINHMCGVGAQAGQSSTCGSYFNPNNRDFPGVPYSGFDFNDGKCRTASGGIENYQDAAQVRDCRLSGLLDLALEKDYVRTKVADYMNHLIDIGVAGFRLDASKHMWPGDIKAILDKLHNLNTKWFSQGSRPFIFQEVIDLGGEAVSSNEYFGNGRVTEFKYGAKLGKVMRKWDGEKMSYLKNWGEGWGLMPSDRALVFVDNHDNQRGHGAGGASILTFWDARLYKMAVGFMLAHPYGFTRVMSSYYWPRNFQNGKDVNDWVGPPNNNGKTKEVSINPDSTCGNDWICEHRWRQIRNMVAFRNVVNGQPFANWWDNDSNQVAFGRGNKGFIVFNNDDWALSETLQTGLPAGTYCDVISGDKVDGNCTGIKVYVGNDGKAHFSISNSAEDPFIAIHAESKI
Protein: Large ribosomal subunit protein bL9m (39S ribosomal protein L9, mitochondrial) (A0A1W2PQB6)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
XNRGTVIVERWWKVPLAGEGRKPRLHRRHRVYKLVEDTKHRPKENLELILTQSVENVGVRGDLVSVKKSLGRNRLLPQGLAVYASPENKKLFEEEKLLRQEGKLEKIQTKAGEATQEWEKGEVLWLPHKT
Protein: Fatty acyl-CoA reductase (EC 1.2.1.84) (Q8MMC6)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MTVDLSPVQEYYKDKTIFITGASGFMGKVLLEKLLYSCHSLKEVIIICRPKRGKAPETRLEEMFKLPIFQRIKDERPEMLKRVTIYQGDVTFDQLGLSGESLKHVTENTNIVFHMAATLKLEGNLRDAIDMNLLGTRRALNVAKEMKQLEAFIHLSTAFCNCDQDVMYEKVYEFPHKPEDLMRLAEWMDVKTLDAITPDLLKPHPNTYTYSKRLAELLVRDHYESMPVIIARPSIVTPAVAEPLPGWVDNMNGPTGVLIGAGKGVIRSMICNGELKSEVIPVDIAINGLILLPYHNSLAEKRPLQIPVYNLTVDDAKKRTWKWIMDVGRDLGIKYPFEVGLWYPDGNMTSSKFYHTICTILFMWLPAYLIDFLLLIFGQRRFMIRVQTKIAVGLEVLQFFTTRSWDFKSTHFEQIYKELGSTDRRIFKINTDDVDDYEYMKVSILGGRQYVMKEPLTSLPKSRIQLRFMYVLDRICKTMIISGLLYWVSQKLRVVDLFRSVFHSST
Protein: LP06731p (Q8MT71)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MILNQEQNQDQSQQPTVPPQEQQQQQRSFVRTRRKCRGNQLQLEEQEELTVAEESLSWSLPPVAVRQSLFNPSLLDSSRVLLFVITNETRSLAPMTLAAHCIGLMYNVVLAVQMLPEDCVLGDEKLTVAAIKDYNRGRSYLIDLAKRQGVPVFSDIRAALECTVAKVKAYNNRDRC
Protein: RH55021p (Q8SWZ1)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004236}. Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
- pH-sensitive chloride channel 2
- pH-sensitive chloride channel 2
Sequence:
MLDKFNTNAFISFGLGFILMWLSEATEAHMNYTAKPRVVLPPNYVKEIRPPSKKGSPVIVDFSIFVVDINSINVEDMDFRVDMFIHQRWLESRLEIPDDIFEEGDDYVTLLPEVFENFWQPDPYFLNSKIAEIATLTHKFTSVTLYKNKTVRYAARMHAIIACQMEFQLYPMDIQVCPIYIESFSSNNQKVKLRWSDSGVTLNPELKLLQYNLGQPLELEESDGYMPEKVGNFSRLTVYFRFERQIGHHLIQTFAPSSLVVMLSWFSFWLGLDAIPGRVTLLVTCMLTLVTMFTGADIPPVAYVKALDLWMAGCMLSVFAALAEFVVVKVLDVQYQYQVNRIPKVLPMRISNMEKGQCATVASWEGGAVRSRKATQTPTTPGQTSLQGNGGPPKPARRQSLLSVAWTDTDTGVEKIMWREIDKVSRAVFPILFFVFVLLYWPILLMKSS
Protein: Gastrin/cholecystokinin type B receptor (Cholecystokinin-2 receptor) (Q7M3J6)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004651}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}.
Interaction partners:
- Cholecystokinin-like receptor at 17D1
- Drosulfakinins
Sequence:
MFNYEEGDADQAAMAAAAAYRALLDYYANAPSAAGHIVSLNVAPYNGTGNGGTVSLAGNATSSYGDDDRDGYMDTEPSDLVTELAFSLGTSSSPSPSSTPASSSSTSTGMPVWLIPSYSMILLFAVLGNLLVISTLVQNRRMRTITNVFLLNLAISDMLLGVLCMPVTLVGTLLRNFIFGEFLCKLFQFSQAASVAVSSWTLVAISCERYYAICHPLRSRSWQTISHAYKIIGFIWLGGILCMTPIAVFSQLIPTSRPGYCKCREFWPDQGYELFYNILLDFLLLVLPLLVLCVAYILITRTLYVGMAKDSGRILQQSLPVSATTAGGSAPNPGTSSSSNCILVLTATAVYNENSNNNNGNSEGSAGGGSTNMATTTLTTRPTAPTVITTTTTTTVTLAKTSSPSIRVHDAALRRSNEAKTLESKKRVVKMLFVLVLEFFICWTPLYVINTMVMLIGPVVYEYVDYTAISFLQLLAYSSSCCNPITYCFMNASFRRAFVDTFKGLPWRRGAGASGGVGGAAGGGLSASQAGAGPGAYASANTNISLNPGLAMGMGTWRSRSRHEFLNAVVTTNSAAAAVNSPQL
Protein: RE55842p (Q8SYK0)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MQVSSDVFAHPPPAVRPPPHYADNVSINASLDGMKSSSSSNSLDRYLGAPPSVALAGPSFATSVLVSSKGSKYEISGPVNFQHVSGDVTRDRTRNAFDLNADPNDKVLRKYMMERGITEADISDMRRQEVIKKIIHSNFTWMPPKSDLQAQPKVQDHARPLLYATISTNNQITPPPSPPPPPIATISRPTEAPNFSNYASLTSRFVDISDMDLPAPTPAAPTPFQPAEVGSVIPVQVQPQQSVKPKVPPPPSAVMAKNAHGYPAAIDIRQVRPSVAPKVANETYATISPQRKVGSMRVPPPAPPKPTIVPHTNSTISNGSLYAVSPVQYAPVAKPAPPAAPAKPTSRSSAVYMTPLSAQKTQISSTPVPVSPPPPTAASVGVPPPPPAPPAGVPPAPPPMPVFGAGGAPPPPPPPSSGMAGVPPPPPMQKSQPKAVSAASTGGDPRDAFLESIRQGVKLKKVDQKAATISGIKPRPERKPVTTDFLSELKLGITLRRVKNPADNPYSEESESQA
Protein: Ras-related protein Rab-40C (Rar-like protein) (Ras-like protein family member 8C) (SOCS box-containing protein RAR3) (Q96S21)
Organism: Homo sapiens (Human)
Function: Probable substrate-recognition component of a SCF-like ECS (Elongin-Cullin-SOCS-box protein) E3 ubiquitin ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of target proteins.
Subcellular location: Cell membrane {ECO:0000305}; Lipid-anchor {ECO:0000305}; Cytoplasmic side {ECO:0000305}.
Interaction partners:
- Cullin-5
- Elongin-B
- Ras-related protein Rab-40B
- Geranylgeranyl transferase type-2 subunit beta
Sequence:
MGSQGSPVKSYDYLLKFLLVGDSDVGKGEILESLQDGAAESPYAYSNGIDYKTTTILLDGRRVKLELWDTSGQGRFCTIFRSYSRGAQGILLVYDITNRWSFDGIDRWIKEIDEHAPGVPRILVGNRLHLAFKRQVPTEQARAYAEKNCMTFFEVSPLCNFNVIESFTELSRIVLMRHGMEKIWRPNRVFSLQDLCCRAIVSCTPVHLIDKLPLPVTIKSHLKSFSMANGMNAVMMHGRSYSLASGAGGGGSKGNSLKRSKSIRPPQSPPQNCSRSNCKIS
Protein: Protein COBRA (Cell expansion protein) (Q94KT8)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Involved in determining the orientation of cell expansion, probably by playing an important role in cellulose deposition. May act by recruiting cellulose synthesizing complexes to discrete positions on the cell surface.
Subcellular location: Lateral cell membrane {ECO:0000305|PubMed:11331607}; Lipid-anchor, GPI-anchor {ECO:0000305|PubMed:11331607}; Extracellular side {ECO:0000305|PubMed:11331607}. Note=Located on the longitudinal sides of the cell rather than on the apical or basal sides.
Interaction partners:
- Chitinase-like protein 1
- Protein CELLULOSE SYNTHASE INTERACTIVE 1
- Cellulose synthase A catalytic subunit 6
- Receptor-like protein kinase THESEUS 1
- Peptidase C13 family
Sequence:
MESFFSRSTSIVSKLSFLALWIVFLISSSSFTSTEAYDALDPEGNITMKWDVMSWTPDGYVAVVTMFNFQKYRHIQSPGWTLGWKWAKKEVIWSMVGAQTTEQGDCSKYKGNIPHCCKKDPTVVDLLPGTPYNQQIANCCKGGVMNSWVQDPATAASSFQISVGAAGTTNKTVRVPRNFTLMGPGPGYTCGPAKIVRPTKFVTTDTRRTTQAMMTWNITCTYSQFLAQRTPTCCVSLSSFYNETIVGCPTCACGCQNNRTESGACLDPDTPHLASVVSPPTKKGTVLPPLVQCTRHMCPIRVHWHVKQNYKEYWRVKITITNFNYRLNYTQWNLVAQHPNLDNITQIFSFNYKSLTPYAGLNDTAMLWGVKFYNDFLSEAGPLGNVQSEILFRKDQSTFTFEKGWAFPRRIYFNGDNCVMPPPDSYPFLPNGGSRSQFSFVAAVLLPLLVFFFFSA
Protein: Transforming acidic coiled-coil containing protein 2 (E9PGB3)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MAYASWQRWSPVEWARWMWTAVTSSGDSSLLVLQGDSGKRSSDSEEAFETPESTTPVKAPPAPPPPPPEVIPEPEVSTQPPPEEPGCGSETVPVPDGPRSDSVEGSPFRPPSHSFSAVFDEDKPIASSGTYNLDFDNIELVDTFQTLEPRASDAKNQEGKVNTRRKSTDSVPISKSTLSRSLSLQASDFDGASSSGNPEAVALAPDAYSTGSSSASSTLKRTKKPRPPSLKKKQTTKKPTETPPVKETQQEPDEESLVPSGENLASETKTESAKTEGPSPALLEETPLEPAVGPKAACPLDSESAEGVVPPASGGGRVQNSPPVGRKTLPLTTAPEAGEVTPSDSGGQEDSPAKGLSVRLEFDYSEDKSSWDNQQENPPPTKKIGKKPVAKMPLRRPKMKKTPEKLDNTPASPPRSPAEPNDIPIAKGTYTFDIDKWDDPNFNPFSSTSKMQESPKLPQQSYNFDPDTCDESVDPFKTSSKTPSSPSKSPASFEIPASAMEANGVDGDGLNKPAKKKKTPLKTDTFRVKKSPKRSPLSDPPSQDPTPAATPETPPVISAVVHATDEEKLAVTNQKWTCMTVDLEADKQDYPQPSDLSTFVNETKFSSPTEELDYRNSYEIEYMEKIGSSLPQDDDAPKKQALYLMFDTSQESPVKSSPVRMSESPTPCS
Protein: RE02250p (Q8SY28)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MQRRMSITIREYKFFRSFSQKFENWPKRKAEALWRKMRERKIAEIEAVEACKWLRAAGFPQYAQMYEDHQFPIDLNNVAKDHTNLENDQLQSLYRRLCVLNRCATMRLDQSHKPQTPQQKEESDDENFALSEHWTFQPHIRRWSRIGEMGLELPPPGLLSLNVEKTESSSKESSPDRFEEDGAGITLVTPGCSKAGGIPNDGSSLGEGSDSGRLRRSGSERIKDQAKALLRRVESIKSRRRKRQNRENVVISGPTVLDLSQFGQRSSLRKPDAVYSTPPSPSALSPMHTFPKAPFFGNDLKVPSHSDNFLSPNRSSPKRTPTTPRSMRTSPLHFFSSPMSQLKEGKSDDSSSYYSDSQESSTGGKLSLRKPSKARRFLQRTGKVDDIGAHSDSECHQGRKLLIKDANSNTTEVKVKKLTRGGSLNLGKDPKKRDGFRSSSFRSRSTSRKEAKNDEDTAGATTNGGSKRQPVVRWHSFQMEERPNMIFRKCFSKKIEPLQEDAGGMPFAAMSAGQLQIIRKLALVTLTGHMERYCPSHRSGWNWELPKFIKKIKMPDYKDKKVFGVPLLMILQRSGQTLPLAVRAAFRWLQLNALDQVGIFRKSGGKSRIMKLREQIEVTDSTAECMDVFDLQQAYDVADMLKQYFRELPESLLTTKMSETFVAIFQHLPAEVRLDAVQCAVLLLPDENREILYVLLEFLTIVAANSQQNQMTSNNLGVCLAQSIFHSSISTGSASVSASPRRKGKGSGMPDMKELAEAKASHECLSFMIEHYKQIYTAAKEKLSKCNFSYMEESKPLPLEALGEGMQFHNWRGYLYECTSATIKEGREKTRGWFSINSLNDSSVDIAYKKVGDGHPLRLWRCSTEIEGPPKEVLEFVIKQRASWDTNLLQCQTVKKLDDRTEIYQYALDGQLTTDFCVLRSWQTDLPRGACVIVETSIDHAKAKPLFGAVRGVVLASRYLIEPCGSGRSKVMHLARVDVKGKTPEWYNKNYGHICSHYLSRIRLAFKHVADGPESKV
Protein: Aquaporin PIP1-1 (Plasma membrane intrinsic protein 1-1) (MaPIP1-1) (MaPIP1;1) (S5ZH89)
Organism: Musa acuminata (Banana) (Musa cavendishii)
Function: Water channel required to facilitate the transport of water across cell membrane; mercury-insensitive (By similarity). Promotes primary root elongation and root hair formation. Contributes to the tolerance to multiple abiotic stresses including salt (NaCl), cold and water deprivation, by modulating cytosolic K(+)/Na(+) ratio, maintaining osmotic balance, and reducing membrane injury (e.g. oxidative injury). Regulates also the expression of abscisic acid (ABA)-responsive genes during dehydration and salt stresses.
Subcellular location: Cell membrane {ECO:0000269|PubMed:24606771}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
Sequence:
MEGKEEDVRLGANKFSERQPIGTAAQSDKGYKEPPPAPLFEPGELTSWSFYRAGIAEFMATFLFLYITILTVMGVVKSNSKCSTVGIQGIAWAFGGMIFALVYCTAGISGGHINPAVTFGLFLARKLSLTRALFYMVMQCLGAICGAGVVKGYQKGLYESNGGGANVVAPGYTKGDGLGAEIVGTFILVYTVFSATDAKRNARDSHVPILAPLPIGFAVFLVHLATIPITGTGINPARSLGAAIIYNKKHAWDDHWIFWVGPFIGAALAAIYHQIVIRAIPFKSRP
Protein: NudC domain-containing protein 1 (Chronic myelogenous leukemia tumor antigen 66) (Tumor antigen CML66) (Q96RS6)
Organism: Homo sapiens (Human)
Subcellular location: [Isoform 1]: Cytoplasm. Nucleus.; SUBCELLULAR LOCATION: [Isoform 2]: Cytoplasm.; SUBCELLULAR LOCATION: [Isoform 3]: Cytoplasm. Nucleus.
Interaction partners:
- Nuclear migration protein nudC
- Putative pre-mRNA-splicing factor ATP-dependent RNA helicase DHX32
- ATP-dependent RNA helicase DHX15
- Coatomer subunit gamma-2
- Coatomer subunit alpha
- Transcription and mRNA export factor ENY2
- Scavenger receptor cysteine-rich domain-containing group B protein
- Coatomer subunit beta
Sequence:
MEVAANCSLRVKRPLLDPRFEGYKLSLEPLPCYQLELDAAVAEVKLRDDQYTLEHMHAFGMYNYLHCDSWYQDSVYYIDTLGRIMNLTVMLDTALGKPREVFRLPTDLTACDNRLCASIHFSSSTWVTLSDGTGRLYVIGTGERGNSASEKWEIMFNEELGDPFIIIHSISLLNAEEHSIATLLLRIEKEELDMKGSGFYVSLEWVTISKKNQDNKKYEIIKRDILRGKSVPHYAAIEPDGNGLMIVSYKSLTFVQAGQDLEENMDEDISEKIKEPLYYWQQTEDDLTVTIRLPEDSTKEDIQIQFLPDHINIVLKDHQFLEGKLYSSIDHESSTWIIKESNSLEISLIKKNEGLTWPELVIGDKQGELIRDSAQCAAIAERLMHLTSEELNPNPDKEKPPCNAQELEECDIFFEESSSLCRFDGNTLKTTHVVNLGSNQYLFSVIVDPKEMPCFCLRHDVDALLWQPHSSKQDDMWEHIATFNALGYVQASKRDKKFFACAPNYSYAALCECLRRVFIYRQPAPMSTVLYNRKEGRQVGQVAKQQVASLETNDPILGFQATNERLFVLTTKNLFLIKVNTEN
Protein: Ribonucleoprotein PTB-binding 2 (Protein raver-2) (Q7TPD6)
Organism: Mus musculus (Mouse)
Function: May bind single-stranded nucleic acids.
Subcellular location: Nucleus {ECO:0000269|PubMed:16051233}. Cytoplasm {ECO:0000269|PubMed:16051233}. Note=May shuttle between the nucleus and the cytoplasm.
Interaction partners:
Sequence:
MAARGGGAGGAGSGSGPSAGTAGEAAEPALRPGEVAALHPQEVAARLQRMRRELSNRRKILVKNLPQDSSSQEVHELLQDYELKYCYVDRNKRTAFVTLLNGEQAQSAIQRFHQFSFRGRELTVQLQPTDALLCITNLPISFTLEEFEELVRAYGNIERCFLVYSEVTGHSKGYGFVEYMKKDFAAKARLELLGRQMGASALFAQWMDVNLLASELIHSKCLCIDKLPSDYSDSEELLQLFSGIHKPVFCQLAQDEGSHGGGFAVVEYSTAEHAEEVQQVADGITIKGSQVQLSFCAPGAPGRSTLAVLIAAQRAMHSNQKGLLPEPNPVQIMKSLNNPAMLQVLLQPQLCGRAMKPVLGVAPSLSHLLSPSLPSAILHFSKAQQSSAVGNTSSLILQNLSPLPLIQQQLMKFDNAHTNNKPGLLGEPPAMVLQPALAIGPPLPLKTDLGHHGEAHKTSNLIPPQTTLAAGLGMLPFFSNQLPAGQAGPGRGTTQEKQSASVSISEASFSGSQHYLQTFPGLPAGGPLTGNQKTPQSQPKGTEVASKNQTSLLGEPPKEIRLSKNPYLNLASVLPSVCLSTAGKGMPPKTGIASNILDAISQGSESQHALEKCIAYSPSIEDYAQASSLRNEKRGSSYLISAPEGGPVELAGQHPQDTGVSYTETYLKKKRVY
Protein: Protein EXORDIUM-like 2 (Q9FE06)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: May play a role in a brassinosteroid-dependent regulation of growth and development.
Subcellular location: Secreted. Secreted, extracellular space. Secreted, extracellular space, apoplast {ECO:0000305}.
Interaction partners:
- Putative cysteine-rich receptor-like protein kinase 32
- Phloem protein 2-A10
- At5g54130
- Uncharacterized calcium-binding protein At1g02270
- Type IV inositol polyphosphate 5-phosphatase 9
Sequence:
MASNYRFAIFLTLFFATAGFSAAALVEEQPLVMKYHNGVLLKGNITVNLVWYGKFTPIQRSVIVDFIHSLNSKDVASSAAVPSVASWWKTTEKYKGGSSTLVVGKQLLLENYPLGKSLKNPYLRALSTKLNGGLRSITVVLTAKDVTVERFCMSRCGTHGSSGSNPRRAANGAAYVWVGNSETQCPGYCAWPFHQPIYGPQTPPLVAPNGDVGVDGMIINLATLLANTVTNPFNNGYYQGPPTAPLEAVSACPGIFGSGSYPGYAGRVLVDKTTGSSYNARGLAGRKYLLPAMWDPQSSTCKTLV
Protein: Heterocyst specific ABC-transporter, membrane fusion protein (Q7A2B0)
Organism: Nostoc sp. (strain PCC 7120 / SAG 25.82 / UTEX 2576)
Interaction partners:
- Alr3648 protein
- Alr4281 protein
- Heterocyst specific ABC-transporter, membrane spanning subunit
- Heterocyst specific ABC-transporter, ATP-binding subunit
- Alr3649 protein
- Alr4282 protein
- Alr2887 protein
- All5346 protein
- All0808 protein
- ABC transporter permease protein
Sequence:
MSRVTEERRSREQPLDLEQPKIWWGLAVALPVAVAAGLLATAKFEQLKRLGPSVPVKPVITSVSAVGRLEPQGEVIKLSAPVGGMQSASRVKQLFVKEGERVRKGQVIAILDNHDTQLAAVEEAKAKLLESRANLAQVRVGSPRDIQAQTAVIARLQAQLVGEMGAQQASITRIASQLSGEKVAQQALVNRLEAELVGQQDSLRATLNRIRAEQRNAQVDAGRYDFLYREGAISQQERDRRRLTATTANQQVIESQAALRQALATLRQQVAEARANQMKTLASLQQQLIEARVTRDKTITTLQRQIDEEKARLKRLVEVSPTDVQMAQAQVSNAIANVRRAEAELKLSYIQAPSAGEILKIYSKSGEAITADGIAEMGETEQMMIIAEVPEDSIGRVRIGQTVTANSDNGAFSGEIRGTVTEIGRKIGKKDVLNTDPAADVDARVVEVKIALSPEDSQKVSGLTYAKVVVDINK
Protein: EKC/KEOPS complex subunit cgi121 (Q9P7J3)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Component of the EKC/KEOPS complex that is required for the formation of a threonylcarbamoyl group on adenosine at position 37 (t(6)A37) in tRNAs that read codons beginning with adenine. The complex is probably involved in the transfer of the threonylcarbamoyl moiety of threonylcarbamoyl-AMP (TC-AMP) to the N6 group of A37. Cgi121 acts as an allosteric effector that regulates the t(6)A activity of the complex. The EKC/KEOPS complex also promotes both telomere uncapping and telomere elongation. The complex is required for efficient recruitment of transcriptional coactivators. Cgi121 is not required for tRNA modification (By similarity).
Subcellular location: Nucleus {ECO:0000250}. Chromosome, telomere {ECO:0000250}.
Interaction partners:
- EKC/KEOPS complex subunit SPAP27G11.07c
- tRNA N6-adenosine threonylcarbamoyltransferase
- EKC/KEOPS complex subunit SPAC4H3.13
- Threonylcarbamoyl-AMP synthase
- tRNA N6-adenosine threonylcarbamoyltransferase, mitochondrial
- EKC/KEOPS complex subunit gon7
Sequence:
MILPLFPETQVHVFVYENVSNCAAIHEQLISQNPIYDYAFLDAATILYKKQVYSAIIRALEDRRDEQMKTKTIHSEVILSLSPKTEISSAFRQFSMTKKSKNIVVVKIDSKLTEEEEFERLDKLVEGNRVEFSDEELQKLIDFKVLKKNYKLDPSTLENPLASILSSIALRGYS
Protein: Disks large homolog 4 (Postsynaptic density protein 95) (PSD-95) (Synapse-associated protein 90) (SAP-90) (SAP90) (P78352)
Organism: Homo sapiens (Human)
Function: Postsynaptic scaffolding protein that plays a critical role in synaptogenesis and synaptic plasticity by providing a platform for the postsynaptic clustering of crucial synaptic proteins. Interacts with the cytoplasmic tail of NMDA receptor subunits and shaker-type potassium channels. Required for synaptic plasticity associated with NMDA receptor signaling. Overexpression or depletion of DLG4 changes the ratio of excitatory to inhibitory synapses in hippocampal neurons. May reduce the amplitude of ASIC3 acid-evoked currents by retaining the channel intracellularly. May regulate the intracellular trafficking of ADR1B. Also regulates AMPA-type glutamate receptor (AMPAR) immobilization at postsynaptic density keeping the channels in an activated state in the presence of glutamate and preventing synaptic depression (By similarity). Under basal conditions, cooperates with FYN to stabilize palmitoyltransferase ZDHHC5 at the synaptic membrane through FYN-mediated phosphorylation of ZDHHC5 and its subsequent inhibition of association with endocytic proteins.
Subcellular location: Cell membrane {ECO:0000269|PubMed:12151521}; Lipid-anchor {ECO:0000269|PubMed:12151521}; Cytoplasmic side {ECO:0000269|PubMed:12151521}. Postsynaptic density {ECO:0000250|UniProtKB:P31016}. Synapse {ECO:0000269|PubMed:12151521}. Cytoplasm {ECO:0000250|UniProtKB:P31016}. Cell projection, axon {ECO:0000250|UniProtKB:P31016}. Cell projection, dendritic spine {ECO:0000250|UniProtKB:P31016}. Cell projection, dendrite {ECO:0000250|UniProtKB:P31016}. Presynapse {ECO:0000250|UniProtKB:P31016}. Note=High levels in postsynaptic density of neurons in the forebrain. Also in presynaptic region of inhibitory synapses formed by cerebellar basket cells on axon hillocks of Purkinje cells. Suppression of neuronal activity induces synaptic accumulation and clustering of DLG4. {ECO:0000250|UniProtKB:P31016}.
Interaction partners:
- Disks large-associated protein 1
- Voltage-dependent calcium channel gamma-2 subunit
- Neuroligin-1
- Glutamate receptor ionotropic, NMDA 2A
- Glutamate receptor ionotropic, NMDA 2B
- Glutamate receptor ionotropic, kainate 2
- Glutamate receptor ionotropic, NMDA 1
- Receptor tyrosine-protein kinase erbB-4
- Neuroligin-2
- Potassium voltage-gated channel subfamily A member 4
Sequence:
MDCLCIVTTKKYRYQDEDTPPLEHSPAHLPNQANSPPVIVNTDTLEAPGYELQVNGTEGEMEYEEITLERGNSGLGFSIAGGTDNPHIGDDPSIFITKIIPGGAAAQDGRLRVNDSILFVNEVDVREVTHSAAVEALKEAGSIVRLYVMRRKPPAEKVMEIKLIKGPKGLGFSIAGGVGNQHIPGDNSIYVTKIIEGGAAHKDGRLQIGDKILAVNSVGLEDVMHEDAVAALKNTYDVVYLKVAKPSNAYLSDSYAPPDITTSYSQHLDNEISHSSYLGTDYPTAMTPTSPRRYSPVAKDLLGEEDIPREPRRIVIHRGSTGLGFNIVGGEDGEGIFISFILAGGPADLSGELRKGDQILSVNGVDLRNASHEQAAIALKNAGQTVTIIAQYKPEEYSRFEAKIHDLREQLMNSSLGSGTASLRSNPKRGFYIRALFDYDKTKDCGFLSQALSFRFGDVLHVIDASDEEWWQARRVHSDSETDDIGFIPSKRRVERREWSRLKAKDWGSSSGSQGREDSVLSYETVTQMEVHYARPIIILGPTKDRANDDLLSEFPDKFGSCVPHTTRPKREYEIDGRDYHFVSSREKMEKDIQAHKFIEAGQYNSHLYGTSVQSVREVAEQGKHCILDVSANAVRRLQAAHLHPIAIFIRPRSLENVLEINKRITEEQARKAFDRATKLEQEFTECFSAIVEGDSFEEIYHKVKRVIEDLSGPYIWVPARERL
Protein: ATP-dependent zinc metalloprotease FTSH 12, chloroplastic (AtFTSH12) (EC 3.4.24.-) (Q9SAJ3)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Probable ATP-dependent zinc metallopeptidase.
Subcellular location: Plastid, chloroplast thylakoid membrane {ECO:0000269|PubMed:14630971}; Multi-pass membrane protein {ECO:0000269|PubMed:14630971}; Stromal side {ECO:0000269|PubMed:14630971}.
Interaction partners:
- Probable inactive ATP-dependent zinc metalloprotease FTSHI 4, chloroplastic
- Protein Ycf2
- Probable inactive ATP-dependent zinc metalloprotease FTSHI 1, chloroplastic
- Probable inactive ATP-dependent zinc metalloprotease FTSHI 2, chloroplastic
- Probable inactive ATP-dependent zinc metalloprotease FTSHI 5, chloroplastic
- Malate dehydrogenase, chloroplastic
- Protein TIC 100
- Protein TIC 56, chloroplastic
- Protein TIC110, chloroplastic
- Protein TIC 40, chloroplastic
Sequence:
MEIAISYKPNPLISSSTQLLKRSKSFGLVRFPAKYGLGATRKKQLFRVYASESSSGSSSNSDGGFSWVRLAQSIRLGAERIGEKIGESVKTEIGFDSEEASGRVNEYVARVKDSVHKGHHELTRFKNETVPSFIDWNKWEHWKDIRNWDGKRVAALFIYAFALLLSCQRVYVAIQAPRVERERRELTESFMEALIPEPSPGNIEKFKRNMWRKATPKGLKLKRFIEAPDGTLVHDSSYVGENAWDDDLETTEGSLKKIIGRNARIQTEAKKKLSQDLGVSGEIGDSVGNWRERLATWKEMLEREKLSEQLNSSAAKYVVEFDMKEVEKSLREDVIGRTSETEGTRALWISKRWWRYRPKLPYTYFLQKLDSSEVAAVVFTEDLKRLYVTMKEGFPLEYIVDIPLDPYLFETICNAGVEVDLLQKRQIHYFMKVFIALLPGILILWFIRESAMLLLITSKRFLYKKYNQLFDMAYAENFILPVGDVSETKSMYKEVVLGGDVWDLLDELMIYMGNPMQYYEKDVAFVRGVLLSGPPGTGKTLFARTLAKESGLPFVFASGAEFTDSEKSGAAKINEMFSIARRNAPAFVFVDEIDAIAGRHARKDPRRRATFEALIAQLDGEKEKTGIDRFSLRQAVIFICATNRPDELDLEFVRSGRIDRRLYIGLPDAKQRVQIFGVHSAGKNLAEDIDFGKLVFRTVGFSGADIRNLVNEAAIMSVRKGRSYIYQQDIVDVLDKQLLEGMGVLLTEEEQQKCEQSVSYEKKRLLAVHEAGHIVLAHLFPRFDWHAFSQLLPGGKETAVSVFYPREDMVDQGYTTFGYMKMQMVVAHGGRCAERVVFGDNVTDGGKDDLEKITKIAREMVISPQSARLGLTQLVKKIGMVDLPDNPDGELIKYRWDHPHVMPAEMSVEVSELFTRELTRYIEETEELAMNALRANRHILDLITRELLEKSRITGLEVEEKMKDLSPLMFEDFVKPFQINPDDEELLPHKDRVSYQPVDLRAAPLHRS
Protein: Insulin-like growth factor 1.S (Insulin-like growth factor 1-A) (Insulin-like growth factor I-A) (IGF-I') (IGF-IA) (xIGF-1) (Somatomedin) (P16501)
Organism: Xenopus laevis (African clawed frog)
Function: The insulin-like growth factors, isolated from plasma, are structurally and functionally related to insulin but have a much higher growth-promoting activity. Promotes head development by inhibiting Wnt signaling during embryogenesis. Acts as a ligand for IGF1R. Binds to the alpha subunit of IGF1R, leading to the activation of the intrinsic tyrosine kinase activity which autophosphorylates tyrosine residues in the beta subunit thus initiatiating a cascade of down-stream signaling events leading to activation of the PI3K-AKT/PKB and the Ras-MAPK pathways. Binds to integrins. Its binding to integrins and subsequent ternary complex formation with integrins and IGFR1 are essential for IGF1 signaling (By similarity).
Subcellular location: Secreted.
Interaction partners:
Sequence:
METNNNLSTQLFKCYFCDILKLKMHKMSCIHLLYLVLCFLTLTHSAAAGPETLCGAELVDTLQFVCGDRGFYFSKPTGYGSNNRRSHHRGIVDECCFQSCDFRRLEMYCAPAKQAKSARSVRTQRHTDMPKAQKEVHPKNTSRGNTGSRGFRM
Protein: polynucleotide adenylyltransferase (EC 2.7.7.19) (Q9NDU1)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
LDHRSVRSLNGCRVTDEILALVPNIENFRLALRTIKLWAKKHGIYSNSLGYFGGVTWAMLVARTCQLYPNAAAATLVHKFFLVFSRWKWPNPVLLKHPDNVNLRFQVWDPRVNASDRYHPMPIITPAYPQQNSTFNVSESTKKVILTEFNRGMNITDEIMLGRIPWERLFEAPSFFYRYRHFIVLLVNSQTADDHLEWCGLVESKVRLLIGNLERNPHIALAHVNPKCFEFKKGQSANNSQNNSGNEDDLKQSQGNQSAVTSAPFCSMWFIGLEFERSENLNVDLTESIQNFTEHVMMHGVNIKMLKEGMTIDARHVKRKQLSLYLDSDFLKRERKSMESHNNFNNTLLANRKRLSTELAQSQDPLPPGQQPSSGNRGRDSGAKIQRLSDSLTEENSNASSDMGAGTPTTPTTAQLSAPSFKSSGKNGSEIDVVEQEPTQPHNNGNASSNTTTTEVACS
Protein: Protein MUK1 (Q02866)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Putative GTPase-activating protein.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:14562095}.
Interaction partners:
- Translation initiation factor eIF2B subunit beta
- Vacuolar protein sorting-associated protein 9
- Vacuolar protein sorting-associated protein 21
- GTP-binding protein YPT52
- GTP-binding protein YPT53
- Vacuolar protein sorting-associated protein 35
- Vacuolar protein sorting-associated protein 5
- Vacuolar protein sorting-associated protein 29
- UPF0507 protein YML002W
- UPF0507 protein YML003W
Sequence:
MARQLFTPPITNPRFDPNQSIRESYKNTTGGMQFQQNLHEDQNDNERSSCDGDENSTTGERLENNKSPILTKQEIDEALNTVTNLPPELSKLIDIFIDDLKQPKYVRPLSVLQLSSLFQSFYIKFDKASFQHVSSANNNGYYFSGGGSSSFLAAKETLSSGLSGIFGRSRSSSGNSLMRPRRSSSLFSNESISNSTNATQMLSPEEIKKQLKINELNNMKIEKYMELCERDVFKKILIVGTSVSSPNKMKTFKPHQLQTFKVGNLFRNSVEFTEYNKLLNEKILCLSKLSTMNKINLIKFLSLNNGIDPEPKFEEIKDILYEFTYHSISPCEKIKALLKLHEIMTYSQEMSNDDYLSLLIYYIITIVPRDIFLNAEFIRLFRYKKKLVETESFALTNLEAALVFVEGLTKNDFSNELQDKLTVNESKILENSISSRVSLPSKTAIMHKNNGNNGSNLGDIVTPTIQRPDVTRSNSYDGFRTVFDSSLKNIIGKIRSYTPPHPNNTSNNNLHSSNNLNIPRSSSQLSMELSNRDTTEMSRDGSRSTSSSSRSSASLEHGNREFTGDLTVTASINGADKKEFQKSWKKYKGYKFEDLTICELRDLFEIYQKMMQ
Protein: HECT-type ubiquitin ligase-interacting protein apyA (Arrestin and PY motif-containing protein A) (Q6SCL4)
Organism: Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Function: May be involved in signaling by recognizing appropriately phosphorylated substrates via its arrestin domains and then recruit a HECT-type ubiquitin ligase such as hulA, leading to ubiquitination of the substrate, providing a link between ubiquitination and phosphorylation in protein regulation and stability.
Interaction partners:
- E3 ubiquitin-protein ligase RSP5
Sequence:
MALHRLKGHGANVGNRVGIQLDKDFVLFQGSEQEALAVYLSGILSLRLKETTTIKYIRLHLRGVRRVSSDTQSSLPARTGRKRFCSENEFYSRTWNFFDGYREAPMTVPAGEYKYPFDVVMEGSLPASVEGMKEASISYLFTVEIGRRHGRDITFDKPLRVIRVPDLEPCSHDFALDEVWANKIAYRIGIQNRTVALGTRIDVDYVFAPLLRDMKIAFIESQLLEVRDLSVEPNDGGSAHAARTETIVCSDRYTLGEEYSSKALESYQFSRTLQLPQALGHCVQDTEDMGVRVSHKLKIHVRMHNPDGHESELRLAIPVLIYLSPYYRVWEDSFCGETIPLPETLNPSDECPPAYGMHELDQLYMPQD