wanglab/gogpt-training-data huggingface dataset:
Protein: Dedicator of cytokinesis protein 4 (P59764)
Organism: Mus musculus (Mouse)
Function: Functions as a guanine nucleotide exchange factor (GEF) that promotes the exchange of GDP to GTP, converting inactive GDP-bound small GTPases into their active GTP-bound form. Involved in regulation of adherens junction between cells. Plays a role in cell migration.
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:Q8N1I0}. Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q8N1I0}. Note=Colocalizes with EPHA2, RHOG and CTTN/cortactin at the tip of protrusions in migrating cells. {ECO:0000250|UniProtKB:Q8N1I0}.
Interaction partners:
- Ubiquitin-like protein FUBI
- Engulfment and cell motility protein 2
- Small ribosomal subunit protein uS17
- Small ribosomal subunit protein eS6
- Small ribosomal subunit protein eS1
- Large ribosomal subunit protein eL19
- Small ribosomal subunit protein eS7
- Large ribosomal subunit protein eL21
- Small ribosomal subunit protein eS24
- Large ribosomal subunit protein eL6
Sequence:
MWIPTEHEKYGVVIASFRGTVPYGLSLEIGDTVQILEKCDGWYRGFALKNPNIKGIFPSSYVHLKNACVKNKGQFEMVIPTEDSVITEMTSTLRDWGTMWKQLYVRNEGDLFHRLWHIMNEILDLRRQVLVGHLTHDRMKDVKRHITARLDWGNEQLGLDLVPRKEYAMVDPEDISITELYRLMEHRHRKKDTPVQASSHHLFVQMKSLMCSNLGEELEVIFSLFDSKENRPISERFFLRLNRNGLPKAPDKPERHCSLFVDLGSSELRKDIYITVHIIRIGRMGAGEKKNACSVQYRRPFGCAVLSIADLLTGETKDDLVLKVYMCNTESEWYQIHENIIKKLNARYNLTGSNAGLAVSLQLLHGDIEQIRREYSSVFSHGVSITRKLGFSDIIMPGEMRNDLYITVERGEFEKGGKSVARNVEVTMFIVDSNGQPLKDFISFGSGEPPASEYHSFVLYHNNSPRWSELLKLPIPVDKFRGSHIRFEFRHCSTKEKGEKKLFGFSFVPLMQEDGRTLPDGTHELIVHKCEENTNLQDTTRYLKLPFSKVIFLGNNNQTMKATKESFWITSFLCSTKLTQNGDMLDLLKWRTHPDKITGCLSKLKEIDGSEIVKFLQDTLDTLFGILDENSQKYGSKVFDSLVHIINLLQDSKFHHFKPVMDTYIESHFAGALAYRDLIKVLKWYVDRITEAERQEHIQEVLKAQEYIFKYIVQSRRLFSLATGGQNEEEFRCCIQELLMSVRFFLSQESKGTGALSQSQAVFLSSFPAVYSELLKLFDVREVANLVQDTLGSLPTIMHVDDSLQAIKLQCIGKTVESQLYTNPDSRYILLPVVLHHLHIHLQEQKDLIMCARILSNVFCLIKKNSSEKSVLEEIDVIVASLLDILLRTILEITSRPQASSSAMRLQFQDVTGEFVACLLSLLRQMTDRHYQQLLNSFSTKEELRDFLLQIFTVFRILIRPEMFPKDWTVMRLVANNVIITTVLYLSDALRKNFLNENFDYKIWDSYFYLAVIFINQLCLQLEMFTPSKKKKVLEKYGDMRVTMGCEIFSMWQNLGEHKLHFIPALIGPFLEVTLIPQPDLRNVMIPIFHDMMDWEQRRSGNFKQVEAKLIDKLDSLMSEGKGDETYRELFNSIIPLFGPYPSLLKKIERETWRESGVSLIATVTRLMERLLDYRDCMKIGEVDGKKIGCTVSLLNFYKTELNKEEMYIRYIHKLYDLHLKAQNFTEAAYTLLLYDELLEWSDRPLREFLTYPMQTEWQRKEHLHLTIIQNFDRGKCWENGIILCRKIAEQYESYYDYRNLSKMRMMEASLYDKIMDQQRLEPEFFRVGFYGKKFPFFLRNKEFVCRGHDYERLEAFQQRMLNEFPHAIAMQHANQPDETIFQAEAQYLQIYAVTPIPESQEVLQREGVPDNIKSFYKVNHIWKFRYDRPFHKGAKDKENEFKSLWVERTSLYLVQSLPGISRWFEVEKREVVEMSPLENAIEVLENKNQQLKTLISQCQTRQMQNINPLTMCLNGVIDAAVNGGVSRYQEAFFVKDYILSHPEDGEKIARLRELMLEQAQILEFGLAVHEKFVPQDMRPLHKKLVDQFFVMKSSFGIQEFPACIQASPVHFPNGSPRVCRNSAPASMSPDGTRVIPRRSPLSYPAVNRYSSSSLSSQASAEVSNITGQSESSDEVFNMQPSPSTSSLSSTHSASPNVTSSAPSSARASPLLSDKHKHSRENSCLSPRDRPCSAIYPTPVEPSQRMLFNHIGDGALPRSDPNLSAPEKAVNPTPSSWSLDSGKEAKNMSDSGKLISPPVPPRPTQTASPARHTTSVSPSPAGRSPLKGSVQSFTPSPVEYNSPGLSSNSPVLSGSYSSGISSLSRCSTSETSGFENQANEQSVPVPVPVPVPVPVPSFSGSEEPVRKESKTPPPYSVYERTLRRPVPLPHSLSIPVTSEPPALPPKPLAARSSHLENGTRRTEPGPRPRPLPRKVSQL
Protein: Guanine nucleotide-binding protein subunit alpha-14 (G alpha-14) (G-protein subunit alpha-14) (G-protein subunit GL1 alpha) (P38408)
Organism: Bos taurus (Bovine)
Function: Guanine nucleotide-binding proteins (G proteins) are involved as modulators or transducers in various transmembrane signaling systems.
Interaction partners:
- 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase beta-1
- 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase beta-4
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein subunit beta-5
- Guanine nucleotide-binding protein subunit beta-5
- Chaperone Ric-8A
- Guanine nucleotide-binding protein G
- GNB4 protein
- Gastrin/cholecystokinin type B receptor
- Cholecystokinin A receptor
Sequence:
MAGCCCLSAEEKESQRISAEIERQLRRDKKDARRELKLLLLGTGESGKSTFIKQMRIIHGSGYSDEDRKGFTKLVYQNIFTAMQAMIRAMDTLKIQYVCEQNKENAQLIREVEVDKVSTLSRDQVEAIKQLWQDPGIQECYDRRREYQLSDSAKYYLTDIDRIAMPAFVPTQQDVLRVRVPTTGIIEYPFDLENIIFRMVDVGGQRSERRKWIHCFESVTSIIFLVALSEYDQVLAECDNENRMEESKALFKTIITYPWFLNSSVILFLNKKDLLEEKIMYSHLISYFPEYTGPKQDVKAARDFILKLYQDQNPDKEKVIYSHFTCATDTENIRFVFAAVKDTILQLNLREFNLV
Protein: High mobility group protein B3 (Q32L31)
Organism: Bos taurus (Bovine)
Function: Multifunctional protein with various roles in different cellular compartments. May act in a redox sensitive manner. Associates with chromatin and binds DNA with a preference for non-canonical DNA structures such as single-stranded DNA. Can bend DNA and enhance DNA flexibility by looping thus providing a mechanism to promote activities on various gene promoters. Proposed to be involved in the innate immune response to nucleic acids by acting as a cytoplasmic promiscuous immunogenic DNA/RNA sensor. Negatively regulates B-cell and myeloid cell differentiation. In hematopoietic stem cells may regulate the balance between self-renewal and differentiation. Involved in negative regulation of canonical Wnt signaling (By similarity).
Subcellular location: Nucleus {ECO:0000250|UniProtKB:P40618, ECO:0000255|PROSITE-ProRule:PRU00267}. Chromosome {ECO:0000305}. Cytoplasm {ECO:0000250|UniProtKB:O54879}.
Interaction partners:
Sequence:
MAKGDPKKPKGKMSAYAFFVQTCREEHKKKNPEVPVNFAEFSKKCSERWKTMSGKEKSKFDEMAKADKVRYDREMKDYGPAKGGKKKKDPNAPKRPPSGFFLFCSEFRPKIKSANPGISIGDVAKKLGEMWNNLSDSEKQPYINKAAKLKEKYEKDVADYKSKGKFDGAKGAAKVARKKVEEEDEEDEEEEEEEEEEEDE
Protein: Solute carrier family 46 member 2 (Thymic stromal cotransporter homolog) (Q9BY10)
Organism: Homo sapiens (Human)
Function: May act as a transporter.
Subcellular location: Endosome membrane {ECO:0000269|PubMed:28539433}; Multi-pass membrane protein {ECO:0000255}. Cell membrane {ECO:0000269|PubMed:34235268}; Multi-pass membrane protein. Note=Localizes in acidic vesicles likely late endosomes and/or endolysosomes. {ECO:0000269|PubMed:28539433}.
Interaction partners:
Sequence:
MSPEVTCPRRGHLPRFHPRTWVEPVVASSQVAASLYDAGLLLVVKASYGTGGSSNHSASPSPRGALEDQQQRAISNFYIIYNLVVGLSPLLSAYGLGWLSDRYHRKISICMSLLGFLLSRLGLLLKVLLDWPVEVLYGAAALNGLFGGFSAFWSGVMALGSLGSSEGRRSVRLILIDLMLGLAGFCGSMASGHLFKQMAGHSGQGLILTACSVSCASFALLYSLLVLKVPESVAKPSQELPAVDTVSGTVGTYRTLDPDQLDQQYAVGHPPSPGKAKPHKTTIALLFVGAIIYDLAVVGTVDVIPLFVLREPLGWNQVQVGYGMAAGYTIFITSFLGVLVFSRCFRDTTMIMIGMVSFGSGALLLAFVKETYMFYIARAVMLFALIPVTTIRSAMSKLIKGSSYGKVFVILQLSLALTGVVTSTLYNKIYQLTMDMFVGSCFALSSFLSFLAIIPISIVAYKQVPLSPYGDIIEK
Protein: Putative indole-3-acetic acid-amido synthetase GH3.9 (EC 6.3.2.-) (Auxin-responsive GH3-like protein 9) (AtGH3-9) (O82243)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Catalyzes the synthesis of indole-3-acetic acid (IAA)-amino acid conjugates, providing a mechanism for the plant to cope with the presence of excess auxin.
Interaction partners:
- Auxin transporter protein 1
- Alpha/beta-Hydrolases superfamily protein
- Two-component response regulator ARR16
- Serine/threonine-protein kinase SRK2J
Sequence:
MDVMKLDHDSVLKELERITSKAAEVQDNILRGILERNKDTEYLSKYMNGSKDVLEFKRAVPIIIYKDIYPYIQRIANGEDSSLITGHSITEILCSSGTSAGEPKLMPTIPEDLDRRTFLYNLIIPIVNKYITGLDKGKAMYLNFVKAETSTPCGLPIRAVLTSYYKSKHFQCRPYDPFNDLTSPIQTILCEDSNQSMYCQLLAGLIHRHKVMRLGAVFASAFLRAISYLEKKWSQLCEDIRTGSLNPMITDPGCQMAMSCLLMSPNPELASEIEEICGRSSWKGILCQLWPKAKFIEAVVTGSMAQYIPALEFFSQGKIPLVCPMYASSETYFGVNVEPLSKPSDVVFTLLPNMCYFEFIPLGKNGTLSFDLDDDEQVPCDKVVDLVNVKLGRYYELVVTTFAGLYRYRIGDVLQVAGFYNGAPQFRFICRRNVVLSIDLDKTNEEDLHRSITLAKKKLGSNAFLAEYTSYADTSSVPGHYVLFWEIQGHLEPKLMEECCVAVEEELDYIYRQCRTKERSIGALEIRVVKPGTFEKLMDLIISQGGSFNQYKTPRCVKSNSATFKLLNGHVMASFFSPRDPTWVP
Protein: Serine/threonine-protein phosphatase with EF-hands 2 (PPEF-2) (EC 3.1.3.16) (O14830)
Organism: Homo sapiens (Human)
Function: May play a role in phototransduction. May dephosphorylate photoactivated rhodopsin. May function as a calcium sensing regulator of ionic currents, energy production or synaptic transmission.
Subcellular location: Cytoplasm {ECO:0000305}. Cell projection, cilium, photoreceptor outer segment. Photoreceptor inner segment. Note=Localized to photoreceptors, PPEF-2(L) is at least 2 fold more abundant in rod inner segments than in the outer segments.
Interaction partners:
- Neurensin-1
- Rhodopsin
Sequence:
MGSGTSTQHHFAFQNAERAFKAAALIQRWYRRYVARLEMRRRCTWSIFQSIEYAGQQDQVKLHDFFSYLMDHFIPSSHNDRDFLTRIFTEDRFAQDSEMKKCSDYESIEVPDSYTGPRLSFPLLPDHATALVEAFRLKQQLHARYVLNLLYETKKHLVQLPNINRVSTCYSEEITVCGDLHGQLDDLIFIFYKNGLPSPERSYVFNGDFVDRGKDSVEILMILFAFMLVYPKEFHLNRGNHEDHMVNLRYGFTKEVMNKYKVHGKEILRTLQDVFCWLPLATLIDEKVLILHGGVSDITDLELLDKIERSKIVSTMRCKTRQKSEKQMEEKRRANQKSSAQGPIPWFLPESRSLPSSPLRLGSYKAQKTSRSSSIPCSGSLDGRELSRQVRSSVELELERCRQQAGLLVTGEKEEPSRSASEADSEAGELRKPTQEEWRQVVDILWSDPMAQEGCKANTIRGGGCYFGPDVTQQLLQKYNMQFLIRSHECKPEGYEFCHNRKVLTIFSASNYYEVGSNRGAYVKLGPALTPHIVQYQANKVTHTLTMRQRISRVEESALRALREKLFAHSSDLLSEFKKHDADKVGLITLSDWAAAVESVLHLGLPWRMLRPQLVNSSADNMLEYKSWLKNLAKEQLSRENIQSSLLETLYRNRSNLETIFRIIDSDHSGFISLDEFRQTWKLFSSHMNIDITDDCICDLARSIDFNKDGHIDINEFLEAFRLVEKSCPEGDASECPQATNAKDSGCSSPGAH
Protein: Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) (EC 1.2.1.12) (Peptidyl-cysteine S-nitrosylase GAPDH) (EC 2.6.99.-) (P00356)
Organism: Gallus gallus (Chicken)
Function: Has both glyceraldehyde-3-phosphate dehydrogenase and nitrosylase activities, thereby playing a role in glycolysis and nuclear functions, respectively. Glyceraldehyde-3-phosphate dehydrogenase is a key enzyme in glycolysis that catalyzes the first step of the pathway by converting D-glyceraldehyde 3-phosphate (G3P) into 3-phospho-D-glyceroyl phosphate (By similarity). Participates in nuclear events including transcription, RNA transport, DNA replication and apoptosis. Nuclear functions are probably due to the nitrosylase activity that mediates cysteine S-nitrosylation of nuclear target proteins such as SIRT1, HDAC2 and PRKDC (By similarity).
Subcellular location: Cytoplasm, cytosol {ECO:0000250|UniProtKB:P04797}. Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:P04797}. Nucleus {ECO:0000250|UniProtKB:P04797}.
Interaction partners:
- Triosephosphate isomerase
- Phosphoglycerate kinase
- Transketolase
- Actin, cytoplasmic 1
- Transaldolase
- Fructose-bisphosphate aldolase B
- Fructose-bisphosphate aldolase C
- Uncharacterized protein.
- Peroxidasin.
- Hexose-6-phosphate dehydrogenase/glucose 1-dehydrogenase.
Sequence:
MVKVGVNGFGRIGRLVTRAAVLSGKVQVVAINDPFIDLNYMVYMFKYDSTHGHFKGTVKAENGKLVINGHAITIFQERDPSNIKWADAGAEYVVESTGVFTTMEKAGAHLKGGAKRVIISAPSADAPMFVMGVNHEKYDKSLKIVSNASCTTNCLAPLAKVIHDNFGIVEGLMTTVHAITATQKTVDGPSGKLWRDGRGAAQNIIPASTGAAKAVGKVIPELNGKLTGMAFRVPTPNVSVVDLTCRLEKPAKYDDIKRVVKAAADGPLKGILGYTEDQVVSCDFNGDSHSSTFDAGAGIALNDHFVKLVSWYDNEFGYSNRVVDLMVHMASKE
Protein: Heat shock factor protein 4 (Q5CZP2)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Function: Heat-shock transcription factor that specifically binds heat shock promoter elements (HSE). Required for denucleation and organelle rupture and degradation that occur during eye lens terminal differentiation, when fiber cells that compose the lens degrade all membrane-bound organelles in order to provide lens with transparency to allow the passage of light. In this process, may regulate denucleation of lens fiber cells in part by activating dnase1l1l and dnase2b transcription. May be involved in DNA repair through the transcriptional regulation of rad51. May up-regulate TP53 protein in lens fiber cells, possibly through protein stabilization. In the eye lens, controls the expression of alpha-crystallin B chain/CRYAB and consequently may be involved in the regulation of lysosomal acidification.
Subcellular location: Nucleus {ECO:0000250|UniProtKB:Q9ULV5}.
Interaction partners:
Sequence:
MQENPGSIGVDGGYASNVPAFLTKLWTLVEDPETNHLICWSATGTSFHVFDQGRFAKEVLPKYFKHNNMASFVRQLNMYGFRKVVNIEQSGLVKPERDDTEFQHLYFLQGHEHLLEHIKRKVSIVKSEETKVRQEDLSKLLYEVQVLRSQQENMEMQMQDMKQQNDVLWREVVSLRQNHTQQQKVMNKLIQFLFSQMQSNSPSTVGMKRKLPLMLDDGCSTPPASKFSHNHSMESLQESFYIQSPSTESASCSTSSVMTGGPIISDVTEIPQSSSMALQMQAEESREKCLMLIKEEPVSPGVQGRAEGVPLGSCEVCAEPPVLPVAMVQSVLEGRGSNLGERRAKRPMLERPEIPDGVENVDMSLEDLQLLLRSHQQSMENNAAAMDQFTFSLPLNEWNFAEMDPNLKSELANALIPAAVSQYMFQGQEGELYPTAGYEEQ
Protein: Trifunctional (S)-stylopine synthase/(S)-nandinine synthase/(S)-canadine synthase (STS) (EC 1.14.19.64) (EC 1.14.19.68) (EC 1.14.19.73) (Cytochrome P450 719A13) (B1NF19)
Organism: Argemone mexicana (Mexican prickly poppy)
Function: Methylenedioxy bridge-forming cytochrome P450 involved in the biosynthesis of isoquinoline alkaloids. Converts (S)-cheilanthifoline to (S)-stylopine, (S)-scoulerine to (S)-nandinine and (S)-tetrahydrocolumbamine to (S)-canadine. Can be involved in both sanguinarine and berberine biosynthesis. Catalyzes an oxidative reaction that does not incorporate oxygen into the product.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}.
Interaction partners:
Sequence:
MEEKIMTNNSPWILTSSTTTTTTILLSLLFTIFIILRRNKSSSSKMVWPTGPKTLPIIGNMNILGGTALHVVLHNLAKTYGNVMTIWIGSWRPVIVVSDIDRAWEVLVNKSSDYSARDMPEITKLATADWKTISSSDSGPFWTNLRKGLQNVALSPQNLSSQSKFQERDIIKTIQNLKEEAKMNNGIVKPLDHLKKAMVRLISRLIYGQDFDNDEYVEEMHHTIEELIRVSGYARLAEAFYYAKYLPSHKKAVREVLQANQRVQNLVRPLLSLNSPTNTYLHFLRSQNYEDEVIIFAIFEAYLLGVDSTSSTTAWALAYLIREPNVQEKLYEELKNFTNDNDRKMVKFEDLNKLQYLQAVVKETMRMKPIAPLAIPHKACRETSLMGRKVNQGTRVMVNIYALHHNQNVWKEPYKFNPERFLQKNQDGVDGKAMEQSLLPFSAGMRICAGMELGKLQFSFALANLVNAFKWSCVSDGVFPDMSDQLGFVLLMKTPLEAGIVPRM
Protein: Mas-related G-protein coupled receptor member F (Mas-related gene F protein) (G-protein coupled receptor 140) (G-protein coupled receptor 168) (Q96AM1)
Organism: Homo sapiens (Human)
Function: Orphan receptor. May bind to a neuropeptide and may regulate nociceptor function and/or development, including the sensation or modulation of pain (By similarity).
Subcellular location: Cell membrane; Multi-pass membrane protein.
Interaction partners:
- Pro-FMRFamide-related neuropeptide FF
Sequence:
MAGNCSWEAHPGNRNKMCPGLSEAPELYSRGFLTIEQIAMLPPPAVMNYIFLLLCLCGLVGNGLVLWFFGFSIKRNPFSIYFLHLASADVGYLFSKAVFSILNTGGFLGTFADYIRSVCRVLGLCMFLTGVSLLPAVSAERCASVIFPAWYWRRRPKRLSAVVCALLWVLSLLVTCLHNYFCVFLGRGAPGAACRHMDIFLGILLFLLCCPLMVLPCLALILHVECRARRRQRSAKLNHVILAMVSVFLVSSIYLGIDWFLFWVFQIPAPFPEYVTDLCICINSSAKPIVYFLAGRDKSQRLWEPLRVVFQRALRDGAELGEAGGSTPNTVTMEMQCPPGNAS
Protein: CALM1 protein (Calmodulin 1) (Calmodulin 2) (Calmodulin 3) (LP7057 protein) (Q96HY3)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MRSLGQNPTEAELQDMINEVDADGNGTIDFPEFLTMMARKMKDTDSEEEIREAFRVFDKDGNGYISAAELRHVMTNLGEKLTDEEVDEMIREADIDGDGQVNYEEFVQMMTAK
Protein: Phospholipid-transporting ATPase DNF2 (EC 7.6.2.1) (Flippase DNF2) (Q12675)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: This magnesium-dependent enzyme catalyzes the hydrolysis of ATP coupled with the transport of phospholipids. Required for protein transport from Golgi to vacuoles.
Subcellular location: Cell membrane {ECO:0000269|PubMed:12221123, ECO:0000269|PubMed:12631737, ECO:0000269|PubMed:18199685, ECO:0000269|PubMed:27235400, ECO:0000269|PubMed:33060204}; Multi-pass membrane protein {ECO:0000269|PubMed:12221123, ECO:0000269|PubMed:18199685}.
Interaction partners:
- Phospholipid-transporting ATPase accessory subunit LEM3
- Phospholipid-transporting ATPase DNF1
- Phospholipid-transporting ATPase accessory subunit CDC50
- Flippase kinase 1
- Serine/threonine-protein kinase KIN82
- Phospholipid-transporting ATPase accessory subunit CRF1
Sequence:
MSSPSKPTSPFVDDIEHESGSASNGLSSMSPFDDSFQFEKPSSAHGNIEVAKTGGSVLKRQSKPMKDISTPDLSKVTFDGIDDYSNDNDINDDDELNGKKTEIHEHENEVDDDLHSFQATPMPNTGGFEDVELDNNEGSNNDSQADHKLKRVRFGTRRNKSGRIDINRSKTLKWAKKNFHNAIDEFSTKEDSLENSALQNRSDELRTVYYNLPLPEDMLDEDGLPLAVYPRNKIRTTKYTPLTFFPKNILFQFHNFANIYFLILLILGAFQIFGVTNPGFASVPLIVIVIITAIKDGIEDSRRTVLDLEVNNTRTHILSGVKNENVAVDNVSLWRRFKKANTRALIKIFEYFSENLTAAGREKKLQKKREELRRKRNSRSFGPRGSLDSIGSYRMSADFGRPSLDYENLNQTMSQANRYNDGENLVDRTLQPNPECRFAKDYWKNVKVGDIVRVHNNDEIPADMILLSTSDVDGACYVETKNLDGETNLKVRQSLKCSKIIKSSRDITRTKFWVESEGPHANLYSYQGNFKWQDTQNGNIRNEPVNINNLLLRGCTLRNTKWAMGMVIFTGDDTKIMINAGVTPTKKSRISRELNFSVILNFVLLFILCFTAGIVNGVYYKQKPRSRDYFEFGTIGGSASTNGFVSFWVAVILYQSLVPISLYISVEIIKTAQAIFIYTDVLLYNAKLDYPCTPKSWNISDDLGQIEYIFSDKTGTLTQNVMEFKKCTINGVSYGRAYTEALAGLRKRQGVDVESEGRREKEEIAKDRETMIDELRSMSDNTQFCPEDLTFVSKEIVEDLKGSSGDHQQKCCEHFLLALALCHSVLVEPNKDDPKKLDIKAQSPDESALVSTARQLGYSFVGSSKSGLIVEIQGVQKEFQVLNVLEFNSSRKRMSCIIKIPGSTPKDEPKALLICKGADSVIYSRLDRTQNDATLLEKTALHLEEYATEGLRTLCLAQRELTWSEYERWVKTYDVAAASVTNREEELDKVTDVIERELILLGGTAIEDRLQDGVPDSIALLAEAGIKLWVLTGDKVETAINIGFSCNVLNNDMELLVVKASGEDVEEFGSDPIQVVNNLVTKYLREKFGMSGSEEELKEAKREHGLPQGNFAVIIDGDALKVALNGEEMRRKFLLLCKNCKAVLCCRVSPAQKAAVVKLVKKTLDVMTLAIGDGSNDVAMIQSADVGVGIAGEEGRQAVMCSDYAIGQFRYVTRLVLVHGKWCYKRLAEMIPQFFYKNVIFTLSLFWYGIYNNFDGSYLFEYTYLTFYNLAFTSVPVILLAVLDQDVSDTVSMLVPQLYRVGILRKEWNQTKFLWYMLDGVYQSVICFFFPYLAYHKNMVVTENGLGLDHRYFVGVFVTAIAVTSCNFYVFMEQYRWDWFCGLFICLSLAVFYGWTGIWTSSSSSNEFYKGAARVFAQPAYWAVLFVGVLFCLLPRFTIDCIRKIFYPKDIEIVREMWLRGDFDLYPQGYDPTDPSRPRINEIRPLTDFKEPISLDTHFDGVSHSQETIVTEEIPMSILNGEQGSRKGYRVSTTLERRDQLSPVTTTNNLPRRSMASARGNKLRTSLDRTREEMLANHQLDTRYSVERARASLDLPGINHAETLLSQRSRDR
Protein: GTPase-activating protein skywalker (Q9VIH7)
Organism: Drosophila melanogaster (Fruit fly)
Function: GTPase-activating protein (GAP) for Rab35 which regulates synaptic vesicle (SV) protein recycling and turnover at the neuromuscular junction boutons and possibly ventral nerve cord via endosomal trafficking. Inhibits Rab35-mediated endosomal sorting which traffics old or dysfunctional SV proteins through a degradative endolysosomal route that involves the ESCRT pathway and the HOPS complex members dor, vps39 and rab7. This function is essential for preventing excessive degradation and turnover of vesicles from the readily releasable pool which leads to increased neurotransmission and eventually neurodegeneration. Preferentially binds phosphoinositides phosphorylated at the D5 position of the inositol ring, such as phosphatidylinositol 4,5-bisphosphate (PIP2) and phosphatidylinositol 3,4,5-trisphosphate (PIP3). Binding to phosphoinositides and thus membrane-association, is required for its function in regulating the turnover of synaptic-vesicle proteins. It is therefore likely that it is recruited to vesicle membranes with high phosphoinositide content and thereby selectively prevents endolysosomal degradation of these vesicles.
Subcellular location: Cytoplasmic vesicle, secretory vesicle, synaptic vesicle membrane {ECO:0000269|PubMed:21458671, ECO:0000269|PubMed:27669036}; Peripheral membrane protein {ECO:0000269|PubMed:21458671, ECO:0000269|PubMed:27669036}. Endosome membrane {ECO:0000269|PubMed:21458671}; Peripheral membrane protein {ECO:0000269|PubMed:21458671}. Note=Detected at the synapses of neuromuscular junction boutons, where it displays co-localization with Rab35 (PubMed:21458671). Associates with certain types of membrane phosphoinositides such as phosphatidylinositol 4,5-bisphosphate (PIP2) and phosphatidylinositol 3,4,5-trisphosphate (PIP3) (PubMed:27669036). {ECO:0000269|PubMed:21458671, ECO:0000269|PubMed:27669036}.
Interaction partners:
- LD21953p
- Cell division cycle 16
Sequence:
MPYHRGGDASSQADKLSGIVEESDLYEGFAPHVETSEIKTLDFYNLPKQTGKEPALRSYTEIQQLLQQGKKRDVKNILRENSWPINSPIRAQLWPMLCGQHQTKQQMLDGFYWEMVHQVFGTTELSEKPIMLPAFVDATHCLPYHLTSTGRAVADRIVNVLGYDCPDITYSPVLYPITSILLHFMSEEEAYICLAGLVGSKEKVFINQTKLQHEVTWKTVMQIAKKHTKSATSYFQRICPGLKLERIFMDWCWWILAGLPFQHLVRIMDCYFHEGIKVLYRVALVILNLFHKECQSNNEWSPDNIKNDIGNALIKFCKKIPVSPAKLLHAAFSIRGLSTQYISRIFIKTEMLLKSRSVLTSGSKQLIKSRSSDNLPTSQSQVNIQMMSHTLTIREHFGLPGTKNFIKTWTDRQFLFTLWSWLPVRITMYQPVLLYTTEEHGCSLTTFYVRVEQHEPTLLMIKTCNNEVFGAYCSSRWFERNVKDDKGQRQAYFGTGETFLFSLYPERAKYPWVGIEGDKDLGHSSELFMAADSKMITIGGGEGQAIWMDENIRFGKTDSCKTFNNPPLCPSGDFEIRVLEVYGFVGI
Protein: Superoxide dismutase [Cu-Zn] (EC 1.15.1.1) (P00442)
Organism: Bos taurus (Bovine)
Function: Destroys radicals which are normally produced within the cells and which are toxic to biological systems.
Subcellular location: Cytoplasm. Nucleus {ECO:0000250}.
Interaction partners:
- Superoxide dismutase, mitochondrial
- Apoptosis regulator Bcl-2
- Parkinson disease protein 7 homolog
- Peroxisome proliferator-activated receptor gamma coactivator 1-alpha
- Endoplasmic reticulum chaperone BiP
- Non-selective voltage-gated ion channel VDAC1
- Neurofilament light polypeptide
- Calcineurin subunit B type 1
- Glutathione peroxidase 1
- Mitochondrial import receptor subunit TOM40 homolog
Sequence:
MATKAVCVLKGDGPVQGTIHFEAKGDTVVVTGSITGLTEGDHGFHVHQFGDNTQGCTSAGPHFNPLSKKHGGPKDEERHVGDLGNVTADKNGVAIVDIVDPLISLSGEYSIIGRTMVVHEKPDDLGRGGNEESTKTGNAGSRLACGVIGIAK
Protein: Keratin-associated protein 5-5 (Q2TA51)
Organism: Mus musculus (Mouse)
Function: In the hair cortex, hair keratin intermediate filaments are embedded in an interfilamentous matrix, consisting of hair keratin-associated protein (KRTAP), which are essential for the formation of a rigid and resistant hair shaft through their extensive disulfide bond cross-linking with abundant cysteine residues of hair keratins. The matrix proteins include the high-sulfur and high-glycine-tyrosine keratins.
Interaction partners:
Sequence:
MTCCGCSGGCGSSCGGCGCSGGCGSSCGGCGSSCCCKPVCCCKPVCCCVPACSCSSCGGCKGGCGSCGGCKGSCGSCGGCKGGCGSCGGCGSCGGCKPSCCQSSCCKPCCCQSSCCKPCCSSGCGSSCCQSSCCKPCCCQSSCCKPCCSSGCGSSCCQSSCCKPCCCQSSCCKPCCCQSSCCKPCCCQSSCCKPCCCQSSCCKPCCCQSSCCKPCCCQSSCCKPCCCQSSCCAPVCCQCKI
Protein: Mediator of RNA polymerase II transcription subunit 12 (Mediator complex subunit 12) (Suppressor of RNA polymerase B srb8) (Q9P6L8)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Component of the srb8-11 complex. The srb8-11 complex is a regulatory module of the Mediator complex which is itself involved in regulation of basal and activated RNA polymerase II-dependent transcription. The srb8-11 complex may be involved in the transcriptional repression of a subset of genes regulated by Mediator. It may inhibit the association of the Mediator complex with RNA polymerase II to form the holoenzyme complex.
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
- Mediator of RNA polymerase II transcription subunit 13
- Serine/threonine-protein kinase srb10
- RNA polymerase II holoenzyme cyclin-like subunit
- Mediator of RNA polymerase II transcription subunit 7
- Mediator of RNA polymerase II transcription subunit 31
- Mediator of RNA polymerase II transcription subunit 14
- Mediator of RNA polymerase II transcription subunit 27
- Mediator of RNA polymerase II transcription subunit 20
- Mediator of RNA polymerase II transcription subunit 19
- Mediator of RNA polymerase II transcription subunit 1
Sequence:
MSNRDSANPPGFNDAVPLAICYIDSSTSSHDEYLTLLQSKVSAPDKNFRDETVDGAPFLAGDAISKGHRYSPPVRSDRASAQGLLQQHLEKSSTLENLKRYSSTLLGRQNDAVIDEPFAPFRPPPRVTLSESRRDRWLQGLSDPMVPLSSLIKTIPHGLWGEDILRMLVKFRVPFTRAIWFIRCAGVNEARSFLRKVQTTDITEWVKNWTDVAAGFLISFISSFLNADIYSFADDYTYLLKLFGRLLAEELVSPKHFLLRIVSFSGDSSLKSFSLHFFALQFFSTSLIQYTHICRKCVITILQSYQQLIVDQPANLLKFSLLSKKVSHFLFTLAQKNIESFFFPTEWDKLKPTIILLWKDFPNYSTLLSIMQERNSKAMYMYKPVTSSIRFLQIISCLSFPVGWRTLAKDLFKLLPVYTGVPLLLHWCINCRSIFSGDRNFIVSSIFDNANFDRNLIVDLTLSFVLKLHPLEYNECVAAAQLLDHLAACGYFFFSKYIARLASLGYLRESMLNSSFMDDQRKILVQLPILRMSQQLKNKIYYILSKGNYFVDWSICDEYVKRFKEDHFSFMFKKEENYAIITLSLVKIASTPMSKLYEDYLVMLFAFHYSMFQVMTKLIADNLVHFSFQSCACQTLFFICSVVPKTESQKLLLNEMGKLFQVELNFSYDSPDVNLLIEQFYEITSYESNYDDAFVEYKDATVANRKDFIEFLFHNITVSSKHTAVIFTSDLLMVLKIALNHPPYFDDLATTTFSSLLKRDECTILSFFKILQFYGCKLLSVDQIWAVVSDVYEAQDNNTTLKQFFNYLLDESTWPEGYLEERHWRSILCKEARKHDSGLKLFKLGIKLCTRNEQIMKTIWSFIHVHDCNVISEVIPDQRFLRTLTEHFMIDLRQLDIVTCLKKALVTLDEFSAPLYATWLTTLDDDELSELTDDVVQKKVLESLDNYKSGIWKLVLSGLPNCKTVFEHLLLFSLEERLDLPAAFLQDLIGASAYVMEQVPDSWFLEKLPCPLTQSLQSFSHLSNHIEVLDSTRQSRLTFLCHLILHMHGFVELTDQLATLESLTIRKCIYRNQELLDLLLFSIHLVKPNVETNDEVCNTLKAWENIESRPYTIDFPEALQQYSPRIVLYEPTFW
Protein: Glutathione peroxidase (Q8I5T2)
Organism: Plasmodium falciparum (isolate 3D7)
Interaction partners:
- Glutathione reductase
- 1-cys peroxiredoxin
- Glutathione S-transferase
- Glutathione synthetase
- Glutaredoxin-1
- Glutathione reductase.
- Superoxide dismutase
- Superoxide dismutase
- Endoplasmic reticulum oxidoreductin, putative
- Thioredoxin reductase
Sequence:
MFFSMFIKFILPISFICYNFGKKFNMFSYFQKIKVSEQELLSSIYDYEVKDLSGSNVSMSKFKNKVLIIFNSASKCGLTKNHVEQFNKLHEKYNARGLEILAFPTSQFLNQEFDNTKDICTFNEKNKIKYNMFSPIEVNGDNTHPLFKYLKKNCDSMHDENGTLKSIGWNFGKFLVDKNGEVVNYFSPKTNPLDLEKIIIQLLQK