wanglab/gogpt-training-data huggingface dataset:
Protein: Cyclic nucleotide-gated channel beta-3 (CNG channel beta-3) (Cone photoreceptor cGMP-gated channel subunit beta) (Cyclic nucleotide-gated cation channel beta-3) (Cyclic nucleotide-gated cation channel modulatory subunit) (Q9NQW8)
Organism: Homo sapiens (Human)
Function: Visual signal transduction is mediated by a G-protein coupled cascade using cGMP as second messenger. This protein can be activated by cGMP which leads to an opening of the cation channel and thereby causing a depolarization of rod photoreceptors. Induced a flickering channel gating, weakened the outward rectification in the presence of extracellular calcium, increased sensitivity for L-cis diltiazem and enhanced the cAMP efficiency of the channel when coexpressed with CNGA3 (By similarity). Essential for the generation of light-evoked electrical responses in the red-, green- and blue sensitive cones.
Subcellular location: Cell membrane {ECO:0000269|PubMed:12815043}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Cyclic nucleotide-gated channel alpha-3
- Guanine nucleotide-binding protein G
- Cone cGMP-specific 3',5'-cyclic phosphodiesterase subunit alpha'
- Cyclic nucleotide-gated channel alpha-1
- Cyclic nucleotide-gated channel alpha-2
- Cyclic nucleotide-gated channel alpha-4
- Retinal cone rhodopsin-sensitive cGMP 3',5'-cyclic phosphodiesterase subunit gamma
- Very long chain fatty acid elongase 4
- Retinal-specific phospholipid-transporting ATPase ABCA4
- Melanopsin
Sequence:
MFKSLTKVNKVKPIGENNENEQSSRRNEEGSHPSNQSQQTTAQEENKGEEKSLKTKSTPVTSEEPHTNIQDKLSKKNSSGDLTTNPDPQNAAEPTGTVPEQKEMDPGKEGPNSPQNKPPAAPVINEYADAQLHNLVKRMRQRTALYKKKLVEGDLSSPEASPQTAKPTAVPPVKESDDKPTEHYYRLLWFKVKKMPLTEYLKRIKLPNSIDSYTDRLYLLWLLLVTLAYNWNCCFIPLRLVFPYQTADNIHYWLIADIICDIIYLYDMLFIQPRLQFVRGGDIIVDSNELRKHYRTSTKFQLDVASIIPFDICYLFFGFNPMFRANRMLKYTSFFEFNHHLESIMDKAYIYRVIRTTGYLLFILHINACVYYWASNYEGIGTTRWVYDGEGNEYLRCYYWAVRTLITIGGLPEPQTLFEIVFQLLNFFSGVFVFSSLIGQMRDVIGAATANQNYFRACMDDTIAYMNNYSIPKLVQKRVRTWYEYTWDSQRMLDESDLLKTLPTTVQLALAIDVNFSIISKVDLFKGCDTQMIYDMLLRLKSVLYLPGDFVCKKGEIGKEMYIIKHGEVQVLGGPDGTKVLVTLKAGSVFGEISLLAAGGGNRRTANVVAHGFANLLTLDKKTLQEILVHYPDSERILMKKARVLLKQKAKTAEATPPRKDLALLFPPKEETPKLFKTLLGGTGKASLARLLKLKREQAAQKKENSEGGEEEGKENEDKQKENEDKQKENEDKGKENEDKDKGREPEEKPLDRPECTASPIAVEEEPHSVRRTVLPRGTSRQSLIISMAPSAEGGEEVLTIEVKEKAKQ
Protein: AT27794p (Q8MZ79)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MTAHTLGNISLTATTTTAAAPPAATPVAASTIAPPKKILNGHQRTNSLPSIVFPIETKSIITQQQLQQLQQQQQQQQQFQPVQQPKQQQLNQVDIKLAPAPPPQYEEATKQLAASKAAALNGLLPLVKIKEEPVQSPAPAAAPLPQTAPLCKRKTASIKSEQVSDVLDILIKQGELPESAALEPITPLTPLPELSMFNGATPTTAAGGASIVPLVPKLETPVTPVQNLDMAMDTNEQHVGFASNQAPNHVFIESIDMASPLQTDSSAIDAESVAKTLDIFLEQHHATPPPSTPPKSCHSGSEKPNSPDAKLNHFDEYELLELMSQQLEMDMGDDSSGYCHASAAKSSNNNGNLRRDLNPSLQPSINELLDASSSDNVLLNNNTGADVDFDADSFVAQLSQHVTGNGNSPGVNCNGSIESSSSAVNSHFGSHSTPMDCDDFESTLNSFMQAVTQPQAGQHVEYATSTSMANGTGGGMGVDNGTGGAVDAFNASGDIFDLFNMDDYKMNWAAGDFTV
Protein: Protein P7 (55 kDa core protein) (P22473)
Organism: Rice dwarf virus (isolate O) (RDV)
Function: Probable component of the transcriptional machinery present in the inner capsid. Displays dsRNA binding activity and may play an important role in the sorting of viral RNA and virion assembly. Together with the RNA-directed RNA polymerase P1 and capping enzyme P5, forms an transcriptional complex positioned near the channels situated at each of the five-fold vertices of the core.
Subcellular location: Virion {ECO:0000305|PubMed:20190042}. Host cytoplasm {ECO:0000250}. Note=Located inside the inner capsid. Found in the interior of spherical cytoplasmic structures, called virus factories, that appear early after infection and are the site of viral replication and packaging (By similarity). {ECO:0000250}.
Interaction partners:
Sequence:
MSAIVGLCLLSEKVVLSRSLTDEVSKLYKLNRGNVKEPRKYATERMSTQSKPVALQVPVSTIILDYKNEDFIKQNPTYSAMDIIGSPSNTAPQTAFQSIMPSLSALFNTPFIQGAFRHRIISSMGPEISYLVMVIGPPSGFMDTPNVSSAQSSVHTVSNADVDLNDIIAINSTMAKSTKLVSASTLQAMLVNDVYDRCMDLDGILLSQALPFFRNYVNVQSKGSLPPAVAACLNTPIKELFSMGSGKREPLALEFRKDNEGQCIGIVLPKGHEGDTLSSRYPAVFINESEPFSDKERSELSELKRTDSDAYEKLYSETISKHVSDGSYGNRVIISHKMSRLSNGGVKIIGRFKISDFNTVKKNLSSRSGEIDSAKEQWEALSGNGLVTDSNISMLHDKILDTITSNKPGVVLRDGNKKSENIVVCFKNGFPNKKHSLLQLTKNGISVVSLDELTDAGILVESTGPDRVRRSPKVLANKLSSFKGRKVTLDVDNMSTEALIQKLSTL
Protein: Phenylalanine--tRNA ligase, chloroplastic/mitochondrial (EC 6.1.1.20) (Phenylalanyl-tRNA synthetase) (PheRS) (Q94K73)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Is responsible for the charging of tRNA(Phe) with phenylalanine in mitochondrial translation.
Subcellular location: Plastid, chloroplast stroma {ECO:0000269|PubMed:16251277, ECO:0000269|PubMed:17433818, ECO:0000269|PubMed:18431481}. Mitochondrion matrix {ECO:0000269|PubMed:16251277, ECO:0000269|PubMed:17433818, ECO:0000269|PubMed:18431481}.
Interaction partners:
- Phenylalanine--tRNA ligase beta subunit, cytoplasmic
- Phenylalanine--tRNA ligase alpha subunit, cytoplasmic
- Tyrosine--tRNA ligase, chloroplastic/mitochondrial
- Lysine--tRNA ligase, chloroplastic/mitochondrial
- Tyrosine--tRNA ligase 1, cytoplasmic
- Putative methyltransferase At1g22800, mitochondrial
- Lysine--tRNA ligase, cytoplasmic
- Valine--tRNA ligase, chloroplastic/mitochondrial 2
- Putative glycine--tRNA ligase, cytoplasmic
- Tyrosine--tRNA ligase 2, cytoplasmic
Sequence:
MTVFSVQSTIFSRASVALLSSNGFKRFSFVSSFSSSAAYSPPKMRKRRYPIVSAVDIGGVAIARNDVVREDDPTNNVPDSIFSKLGMQLHRRDKHPIGILKNAIYDYFDSNYSNKFEKFEDLSPIVTTKQNFDDVLVPADHVSRSLNDTYYVDSQTVLRCHTSAHQAELLRKGHSRFLVTGDVYRRDSIDSTHYPVFHQMEGFCVFSPEDWNGSGKDSTLYAAEDLKKCLEGLARHLFGSVEMRWVDTYFPFTNPSFELEIYFKEDWLEVLGCGVTEQVILKQSGLENNVAWAFGLGLERLAMVLFDIPDIRFFWSSDERFTSQFGKGELGVKFKPYSKYPPCYKDISFWISDLFTENNFCEVVRGIAGDLVEEVKLIDQFTNKKKGLTSHCYRIVFRSMERSLTDEEVNDLQSKVRDEVQKKLNVELR
Protein: Complement C1q-like protein 2 (C1q and tumor necrosis factor-related protein 10) (C1q/TNF-related protein 10) (C1qTNF10) (CTRP10) (Q8CFR0)
Organism: Mus musculus (Mouse)
Function: May regulate the number of excitatory synapses that are formed on hippocampus neurons. Has no effect on inhibitory synapses.
Subcellular location: Secreted {ECO:0000269|PubMed:18783346}.
Interaction partners:
Sequence:
MALGLLIAVPLLLQAAPPGAAHYEMLGTCRMICDPYSVAPAGGPAGAKAPPPGPSTAALEVMQDLSANPPPPFIQGPKGDPGRPGKPGPRGPPGEPGPPGPRGPPGEKGDSGRPGLPGLQLTTSAAGGVGVVSGGTGGGGDTEGEVTSALSAAFSGPKIAFYVGLKSPHEGYEVLKFDDVVTNLGNHYDPTTGKFSCQVRGIYFFTYHILMRGGDGTSMWADLCKNGQVRASAIAQDADQNYDYASNSVVLHLDSGDEVYVKLDGGKAHGGNNNKYSTFSGFLLYPD
Protein: Rho-related BTB domain-containing protein 1 (O94844)
Organism: Homo sapiens (Human)
Interaction partners:
- Cullin-3
- Kelch-like ECH-associated protein 1
- Kelch-like protein 13
- Kelch-like protein 9
- Rho-related BTB domain-containing protein 2
- Rho-associated protein kinase 1
- NEDD8-conjugating enzyme Ubc12
- COP9 signalosome complex subunit 1
- COP9 signalosome complex subunit 6
- cGMP-specific 3',5'-cyclic phosphodiesterase
Sequence:
MDADMDYERPNVETIKCVVVGDNAVGKTRLICARACNTTLTQYQLLATHVPTVWAIDQYRVCQEVLERSRDVVDEVSVSLRLWDTFGDHHKDRRFAYGRSDVVVLCFSIANPNSLNHVKSMWYPEIKHFCPRTPVILVGCQLDLRYADLEAVNRARRPLARPIKRGDILPPEKGREVAKELGLPYYETSVFDQFGIKDVFDNAIRAALISRRHLQFWKSHLKKVQKPLLQAPFLPPKAPPPVIKIPECPSMGTNEAACLLDNPLCADVLFILQDQEHIFAHRIYLATSSSKFYDLFLMECEESPNGSEGACEKEKQSRDFQGRILSVDPEEEREEGPPRIPQADQWKSSNKSLVEALGLEAEGAVPETQTLTGWSKGFIGMHREMQVNPISKRMGPMTVVRMDASVQPGPFRTLLQFLYTGQLDEKEKDLVGLAQIAEVLEMFDLRMMVENIMNKEAFMNQEITKAFHVRKANRIKECLSKGTFSDVTFKLDDGAISAHKPLLICSCEWMAAMFGGSFVESANSEVYLPNINKISMQAVLDYLYTKQLSPNLDLDPLELIALANRFCLPHLVALAEQHAVQELTKAATSGVGIDGEVLSYLELAQFHNAHQLAAWCLHHICTNYNSVCSKFRKEIKSKSADNQEYFERHRWPPVWYLKEEDHYQRVKREREKEDIALNKHRSRRKWCFWNSSPAVA
Protein: LD06038p (Paxillin, isoform A) (Paxillin, isoform J) (Paxillin, isoform K) (Q9VIX2)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cell junction, focal adhesion {ECO:0000256|ARBA:ARBA00004246}. Cytoplasm, cytoskeleton {ECO:0000256|ARBA:ARBA00004245}.
Interaction partners:
Sequence:
MSSKLISSSFHSSPLSDCFKVGEFERRLDALLADLQNSVPGQPQQPQPQYGTVQPKHQALQQQQFVDNTPGYGSLRGKAQPQVYQEHYSVETRSPTAGHDFNGSSTTPGYANQGSLPRQAAGASTGLSELDSLLQDLQKIDVPVNYSTPVSKYNTMNSYATVEERPSVDSLLKELDNAHIYAVPNGSAHKSPTPGRHVTITVRETKTEKLTGPDGPVGTVEEQIVQQKDSYTPNHAVPGQQVHQAYTSQATKELDDLMASLSDFKVSNGTNGIGNGSHPQQHSSTVQHQTVTDYARPNKGSQQAHLTQTIEETTIVEDSREDQLDSMLGNLQANMSRQGVNTVQKGCCNACEKPIVGQVITALGKTWHPEHFTCNHCSQELGTRNFFERDGFPYCEPDYHNLFSPRCAYCNGAILDKCVTALDKTWHTEHFFCAQCGQQFGEEGFHERDGKPYCRNDYFEMFAPKCNGCNRAIMENYISALNSQWHPDCFVCRDCRQPFQGGSFFDHEGLPYCETHYHAKRGSLCAGCSKPITGRCITAMFKKFHPEHFVCAFCLKQLNKGTFKEQKDKPYCHTCFDKIFG
Protein: protein-lysine 6-oxidase (EC 1.4.3.13) (Q5FWS5)
Organism: Rattus norvegicus (Rat)
Subcellular location: Secreted, extracellular space {ECO:0000256|ARBA:ARBA00004239}.
Interaction partners:
- Fibulin-5
- Fibrillin-1
- NYN domain and retroviral integrase containing
- Latent-transforming growth factor beta-binding protein 2
- Metalloendopeptidase
Sequence:
MALAGAGSQLGTLVWGACLCVLVHGQQEQPGQGSDPGRWRQLIQWENNGQVYSLLNSGSEYVPAGPQRGESSSRVLLAGAPQTSQRRSQGGPRRRQAPNLPLPGRVGSDTVRGQTRHPFGFGQVPDNWREVAVGDSNGMARARTSVSQQRHGGSASSSVSASAFATTYRQPSSYPQQFPYPQAPFVNQYENYDPASRTYEQGYVYYRGAGGGMGAGAAAAAVASAGVIYPFQPRARYEEYGGGGEEQPEYPAQGFYPAPERPYAPQPQPQPQPQPQPQPQPSDGLDRRYSHSLYNEGTPGFEQAYPDPSTDVSQIPAGAGGTYGAAGDPRLGWYPPYAANVPPEAYVPPRAVEPQPPFRVLEPPYLPVRNSDAPSQGGERNGAQQGRLSVGSVYRPNQNGRGLPDLVPDPNYVQASTYVQRAHLYSLRCAAEEKCLASTAYAPEATDYDLRVLLRFPQRVKNQGTADFLPNRPRHTWEWHSCHQHYHSMDEFSHYDLLDASTGKKVAEGHKASFCLEDSTCDFGNLKRYACTSHTQGLSPGCYDTYNADIDCQWIDITDVQPGNYILKVHVNPKYIVLESDFTNNVVRCNIHYTGRFVSTTNCKIVQS
Protein: [histone H3]-trimethyl-L-lysine(9) demethylase (EC 1.14.11.66) (F1QNG0)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- Histone H3
- Histone H3.2
Sequence:
MASDMPVSRGIMTFHPTVEEFKNFSRYIAYMESQGAHKAGLAKIVPPKNWKPRGSYDDIDDLIIPAPIQQVVTGQSGLFTQYNIQKKAMTVKEFRKTANSDKFCSPRYDDFEELERKYWKNVTFNPPIYGADVNGTLYDPDIKEWNVGHLNTILDTVEHESGITIEGVNTPYLYFGMWKTTFAWHTEDMDLYSINYLHFGEPKSWYTVPPEHGKRLERLAKGFFPGSSQNCEAFLRHKMTLISPSILKKYGIPFEKITQEAGEFMVTFPYGYHAGFNHGFNCAESTNFATRRWIDYGKQAILCSCRKDMVKISMDVFVKKFQPERYELWLEGKDNAPIDHSKPTPEAAEFLGGEAGAQELRIENQSNEGQKKSLAKQRIGTKRHRVCLDFPEEVLPKTETNDEAEYGKKGRLTPYTEQCKEYTELKHEDRTLPLMGSTSLKMLPGSRSAEFSENVRGAGFSDADLDAKATSHISACAQPFPKHHLSIASVPTVPHCLSAVPRVSTKPGVASLLFHRTLSPTDALQVHSYAAKAALCKPQTPSPEKPREDLHIPDISLDVRPNTPTPPPDTPEHEIEGEKENNSMKRKLQPLSKLPRLHPLLRENSSDDEIQEPTAEPEETDPWAKILAPMWQSRQRNFQIEKEFNFRMGLHPPYCAVCSLFHTYNESDVISLGGFAAVGGNPQRTKPLIPEMCFTSSSEGHLSTPNLEADGTSQLISCSVCSVRVHTSCYGVSQDAKLDSWRCSRCEANAITQDCCLCSLRGGALQRANNDKWVHVLCAVAVLEARFVNIAERRPVDLSTIPFQRFKLKCQFCRKWVKKTTGCCVQCSHGRCSTSFHATCAQAAGVQMHPDDWPFVVYFTCWRHKGGTHIERNMASMRELEKGQKVICKHKNGRYYHCEVVELTKATFYEVIFDDGSFSDNLFPEDIVNRDCTRHGPPSEGEVVQVQWTDGLIYGAKFVSDHIIPMYQVEFEDDSQLTVKREDVFSLDEELPKRVKSRLSVASDMRFKGVFVEKEVKQDSKRQRVINSRYREDYIEPAIYRAILE
Protein: (Z)-3-hexen-1-ol acetyltransferase (EC 2.3.1.195) (Q9SRQ2)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Acyltransferase involved in the production of green leaf volatiles (GLVs). Uses acetyl-CoA as substrate, but not malonyl-CoA or benzoyl-CoA. Prefers primary, medium-chain-length, aliphatic alcohols.
Interaction partners:
- Alcohol dehydrogenase class-P
- NAC domain-containing protein 6
- Zinc knuckle
- Putative GEM-like protein 8
- Mitochondrial import inner membrane translocase subunit TIM23-3
- Kinectin-like protein
Sequence:
MDHQVSLPQSTTTGLSFKVHRQQRELVTPAKPTPRELKPLSDIDDQQGLRFQIPVIFFYRPNLSSDLDPVQVIKKALADALVYYYPFAGRLRELSNRKLAVDCTGEGVLFIEAEADVALAELEEADALLPPFPFLEELLFDVEGSSDVLNTPLLLVQVTRLKCCGFIFALRFNHTMTDGAGLSLFLKSLCELACGLHAPSVPPVWNRHLLTVSASEARVTHTHREYDDQVGIDVVATGHPLVSRSFFFRAEEISAIRKLLPPDLHNTSFEALSSFLWRCRTIALNPDPNTEMRLTCIINSRSKLRNPPLEPGYYGNVFVIPAAIATARDLIEKPLEFALRLIQETKSSVTEDYVRSVTALMATRGRPMFVASGNYIISDLRHFDLGKIDFGPWGKPVYGGTAKAGIALFPGVSFYVPFKNKKGETGTVVAISLPVRAMETFVAELNGVLNVSKG
Protein: Amine oxidase [copper-containing] gamma 1 (AtCuAO1) (AtCuAOgamma1) (Copper amine oxidase 1) (EC 1.4.3.21) (Primary amine oxidase 1) (Q8H1H9)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Copper amine oxidase that can use putrescine and spermidine as substrates. Required for abscisic acid- (ABA) and polyamine- (PA) and H(2)O(2)-dependent induced nitric oxide (NO) biosynthesis. Involved in ABA signal transduction and in responses to osmotic stress.
Subcellular location: Secreted, extracellular space, apoplast {ECO:0000269|PubMed:23915037}.
Interaction partners:
- Probable polyamine oxidase 5
- Polyamine oxidase 1
- Tyrosine decarboxylase 2
- Phenylacetaldehyde synthase
- Polyamine oxidase 2
- Probable aminotransferase TAT4
- Tyrosine aminotransferase
- Probable aminotransferase TAT1
- Tyrosine transaminase family protein
- Polyamine oxidase 3
Sequence:
MAEPSFARLFLLFFSFLLIFATYSWVFGPDSGFLFGTRVRKTLGSNRQVHVDHSLEKPHHPLDPLTVREINRVRTILSNHDPGFGSGSATIHSMALDEPEKSRVVQWKKGNKLLSRRAAVVAYWGGQTHEITVDLDSGRVVSDVINRTSGYPILTLNDVFAASQVPLKSLEFNRSIEARGVKFSDLACITPFAGWFGSEEEGRRVIRVQCFTLQGTTNYFMRPLEGLYVTVDLDKLEVIKIIDKGPIPIPKASGTEYRFGVQNKPVHMDRINPISMEQPDGPSFRVEDGHLVKWANWVFHVKADQRAGMIISQATVRDSETGEPRSVMYKGFPSELFVPYMDPEEGWYYKGYMDAGELGLGPTAMPLVPLNDCPRNSYYIDGVFASPDGKPIVQPNMICLFERYAGDISWRHSEILFANADIRESRPKVTLVARMATSVGNYDYIFDWEFQTDGLIRVTVAASGMLMVKGTPYDNVDDLGDREDDAGPLISENVIGVVHDHFITFHLDMDIDGPMNNSLVKVHLEKQRVPTGKSPRKSYLKVKKYIAKTEKDAQIKLSLYDPYEFHIVNPNRKSRVGNPAGYRIVPGGNAASLLDHDDPPQIRGAFTNNQIWVTPYNRSEQYAGGVLIYQSQGDDTLQVWSDRDRSIENKDIVLWYTLGFHHVPCQEDYPVMPTVAASFELKPANFFESNPILGSAPFFEKDLPVCRPFASS
Protein: Histone-lysine N-methyltransferase ASHH1 (EC 2.1.1.354) (ASH1 homolog 1) (Protein SET DOMAIN GROUP 26) (Q84WW6)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Histone methyltransferase involved in regulation of flowering time. Required for the expression of the SOC1/AGL20 gene. Required for histone H3 trimethylation on 'Lys-4' (H3K4me3) at the SOC1 locus. Prevents trimethylation on 'Lys-27' (H3K27me3) at the same locus.
Subcellular location: Nucleus {ECO:0000250}. Chromosome, centromere {ECO:0000250}. Note=Associates with centromeric constitutive heterochromatin. {ECO:0000250}.
Interaction partners:
- Histone H4
- Histone H3-like 5
- Histone H3.1
- Histone H3.3
- Histone H3-like 3
- Histone H3-like 2
- Histone H3-like 4
- Histone H3-like centromeric protein CENH3
- Histone H3-like 1
- Protein ANTHESIS POMOTING FACTOR 1
Sequence:
MQFSCDPDQEGDELPQYEHIYQNDFSYRKHKKQKEEDISICECKFDFGDPDSACGERCLNVITNTECTPGYCPCGVYCKNQKFQKCEYAKTKLIKCEGRGWGLVALEEIKAGQFIMEYCGEVISWKEAKKRAQTYETHGVKDAYIISLNASEAIDATKKGSLARFINHSCRPNCETRKWNVLGEVRVGIFAKESISPRTELAYDYNFEWYGGAKVRCLCGAVACSGFLGAKSRGFQEDTYVWEDGDDRYSVDKIPVYDSAEDELTSEPSKNGESNTNEEKEKDISTENHLESTALNIQQQSDSTPTPMEEDVVTETVKTETSEDMKLLSQNSQEDSSPKTAIVSRVHGNISKIKSESLPKKRGRPFSGGKTKNVAQKHVDIANVVQLLATKEAQDEVLKYEEVKKEAAVRLSSLYDEIRPAIEEHERDSQDSVATSVAEKWIQASCNKLKAEFDLYSSVIKNIASTPIKPQDTKTKVAEAGNEDHIKLLEAK
Protein: Synaptotagmin-8 (Synaptotagmin VIII) (SytVIII) (Q925B4)
Organism: Rattus norvegicus (Rat)
Function: Involved in the trafficking and exocytosis of secretory vesicles in non-neuronal tissues. Mediates Ca(2+)-regulation of exocytosis acrosomal reaction in sperm. May mediate Ca(2+)-regulation of exocytosis in insulin secreted cells (By similarity).
Subcellular location: Cell membrane {ECO:0000250}; Single-pass type III membrane protein {ECO:0000250}. Cytoplasmic vesicle, secretory vesicle, acrosome {ECO:0000250|UniProtKB:Q9R0N6}.
Interaction partners:
Sequence:
MQADRSMKMGHVSNPLSTSAPVDATAGPNLIPDLITKIPWPRWILFIAILAAGVLLVSCLLCVICYCCHRQRHRKQPKDKETVGLGSARNSTTTHLVQPDVECLEPCSGGDQPWGQLLLSLEYDFGSQEIRVGLRQAKNLKAEGTADPYARVSVSTQAGRRHETKVHRGTLCPMFEETCCFLVPPAELPKATLKVQLLDFKRFSEHEPLGELQLPLGTVDLQHVLESWYQLGPPGSTESEQMGELCFSLRYVPSSGRLTVVILEARGLNPGLAEAYVKVQLILNQRKWKKNKTSSKKGTTNPYFNEAFVFLVPVSQLQSMDLVLAVWARGLQLLAEPVGKVLLGPRASGQPLQHWADMLAHARRPIAQWHHLRSPREVDRALALQPRLPLLRPRS
Protein: Nuclear receptor subfamily 2 group F member 6 (V-erbA-related protein 2) (EAR-2) (P10588)
Organism: Homo sapiens (Human)
Function: Transcription factor predominantly involved in transcriptional repression. Binds to promoter/enhancer response elements that contain the imperfect 5'-AGGTCA-3' direct or inverted repeats with various spacings which are also recognized by other nuclear hormone receptors. Involved in modulation of hormonal responses. Represses transcriptional activity of the lutropin-choriogonadotropic hormone receptor/LHCGR gene, the renin/REN gene and the oxytocin-neurophysin/OXT gene. Represses the triiodothyronine-dependent and -independent transcriptional activity of the thyroid hormone receptor gene in a cell type-specific manner. The corepressing function towards thyroid hormone receptor beta/THRB involves at least in part the inhibition of THRB binding to triiodothyronine response elements (TREs) by NR2F6. Inhibits NFATC transcription factor DNA binding and subsequently its transcriptional activity. Acts as transcriptional repressor of IL-17 expression in Th-17 differentiated CD4(+) T cells and may be involved in induction and/or maintenance of peripheral immunological tolerance and autoimmunity. Involved in development of forebrain circadian clock; is required early in the development of the locus coeruleus (LC).
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00407, ECO:0000269|PubMed:10644740, ECO:0000269|PubMed:18701084}.
Interaction partners:
- Unconventional myosin-IXb
- Metallophosphoesterase MPPED2
Sequence:
MAMVTGGWGGPGGDTNGVDKAGGYPRAAEDDSASPPGAASDAEPGDEERPGLQVDCVVCGDKSSGKHYGVFTCEGCKSFFKRSIRRNLSYTCRSNRDCQIDQHHRNQCQYCRLKKCFRVGMRKEAVQRGRIPHSLPGAVAASSGSPPGSALAAVASGGDLFPGQPVSELIAQLLRAEPYPAAAGRFGAGGGAAGAVLGIDNVCELAARLLFSTVEWARHAPFFPELPVADQVALLRLSWSELFVLNAAQAALPLHTAPLLAAAGLHAAPMAAERAVAFMDQVRAFQEQVDKLGRLQVDSAEYGCLKAIALFTPDACGLSDPAHVESLQEKAQVALTEYVRAQYPSQPQRFGRLLLRLPALRAVPASLISQLFFMRLVGKTPIETLIRDMLLSGSTFNWPYGSGQ
Protein: Mitochondrial uncoupling protein 4 (UCP 4) (Solute carrier family 25 member 27) (O95847)
Organism: Homo sapiens (Human)
Function: UCP are mitochondrial transporter proteins that create proton leaks across the inner mitochondrial membrane, thus uncoupling oxidative phosphorylation from ATP synthesis. As a result, energy is dissipated in the form of heat. May play a role in thermoregulatory heat production and metabolism in brain.
Subcellular location: Mitochondrion inner membrane {ECO:0000269|PubMed:10025957}; Multi-pass membrane protein {ECO:0000255}. Note=Localizes to neuronal cell body and processes. Within mitochondrial inner membrane, it is mainly observed in the inner boundary membrane locally separated from F(1)F(0) ATP synthase, which is preferentially localized in cristae. {ECO:0000250|UniProtKB:Q9D6D0}.
Interaction partners:
Sequence:
MSVPEEEERLLPLTQRWPRASKFLLSGCAATVAELATFPLDLTKTRLQMQGEAALARLGDGARESAPYRGMVRTALGIIEEEGFLKLWQGVTPAIYRHVVYSGGRMVTYEHLREVVFGKSEDEHYPLWKSVIGGMMAGVIGQFLANPTDLVKVQMQMEGKRKLEGKPLRFRGVHHAFAKILAEGGIRGLWAGWVPNIQRAALVNMGDLTTYDTVKHYLVLNTPLEDNIMTHGLSSLCSGLVASILGTPADVIKSRIMNQPRDKQGRGLLYKSSTDCLIQAVQGEGFMSLYKGFLPSWLRMTPWSMVFWLTYEKIREMSGVSPF
Protein: Ras GTPase-activating protein 1 (GAP) (GTPase-activating protein) (RasGAP) (Ras p21 protein activator) (p120GAP) (P20936)
Organism: Homo sapiens (Human)
Function: Inhibitory regulator of the Ras-cyclic AMP pathway. Stimulates the GTPase of normal but not oncogenic Ras p21; this stimulation may be further increased in the presence of NCK1.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:8360177}.
Interaction partners:
- GTPase HRas
- Rho GTPase-activating protein 35
- Docking protein 1
- Ras GTPase-activating protein-binding protein 1
- Ras-related protein Ral-A
- Platelet-derived growth factor receptor beta
- GTPase NRas
- Docking protein 2
- Ras-related protein R-Ras
- Ephrin type-B receptor 2
Sequence:
MMAAEAGSEEGGPVTAGAGGGGAAAGSSAYPAVCRVKIPAALPVAAAPYPGLVETGVAGTLGGGAALGSEFLGAGSVAGALGGAGLTGGGTAAGVAGAAAGVAGAAVAGPSGDMALTKLPTSLLAETLGPGGGFPPLPPPPYLPPLGAGLGTVDEGDSLDGPEYEEEEVAIPLTAPPTNQWYHGKLDRTIAEERLRQAGKSGSYLIRESDRRPGSFVLSFLSQMNVVNHFRIIAMCGDYYIGGRRFSSLSDLIGYYSHVSCLLKGEKLLYPVAPPEPVEDRRRVRAILPYTKVPDTDEISFLKGDMFIVHNELEDGWMWVTNLRTDEQGLIVEDLVEEVGREEDPHEGKIWFHGKISKQEAYNLLMTVGQVCSFLVRPSDNTPGDYSLYFRTNENIQRFKICPTPNNQFMMGGRYYNSIGDIIDHYRKEQIVEGYYLKEPVPMQDQEQVLNDTVDGKEIYNTIRRKTKDAFYKNIVKKGYLLKKGKGKRWKNLYFILEGSDAQLIYFESEKRATKPKGLIDLSVCSVYVVHDSLFGRPNCFQIVVQHFSEEHYIFYFAGETPEQAEDWMKGLQAFCNLRKSSPGTSNKRLRQVSSLVLHIEEAHKLPVKHFTNPYCNIYLNSVQVAKTHAREGQNPVWSEEFVFDDLPPDINRFEITLSNKTKKSKDPDILFMRCQLSRLQKGHATDEWFLLSSHIPLKGIEPGSLRVRARYSMEKIMPEEEYSEFKELILQKELHVVYALSHVCGQDRTLLASILLRIFLHEKLESLLLCTLNDREISMEDEATTLFRATTLASTLMEQYMKATATQFVHHALKDSILKIMESKQSCELSPSKLEKNEDVNTNLTHLLNILSELVEKIFMASEILPPTLRYIYGCLQKSVQHKWPTNTTMRTRVVSGFVFLRLICPAILNPRMFNIISDSPSPIAARTLILVAKSVQNLANLVEFGAKEPYMEGVNPFIKSNKHRMIMFLDELGNVPELPDTTEHSRTDLSRDLAALHEICVAHSDELRTLSNERGAQQHVLKKLLAITELLQQKQNQYTKTNDVR
Protein: V-ral simian leukemia viral oncogene homolog Bb (Ras related) (EC 3.6.5.2) (Zgc:86798) (Q6IQE6)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004236}.
Interaction partners:
Sequence:
MAVNKSKAQSSLVLHKVIMVGSGGVGKSALTLQFMYDEFVEDYEPTKADSYRKKVVLDGEEVQIDILDTAGQEDYAAIRDNYFRSGEGFLLVFSITEPESFSASAEFREQILRVKAEEDKIPLLVVGNKSDLEERRQVSADEARSKADEWGVQYVETSAKTRANVDKVFFDLMREVRTKKMSENKEKNLKKGGKKKKSLKERCTLL
Protein: Protein cueball (Q95RU0)
Organism: Drosophila melanogaster (Fruit fly)
Function: Has a role in spermatogenesis and oogenesis. Might have a role in triglyceride homeostasis. Probably by regulating lipid storage and catabolism, plays a role in neuronal function.
Subcellular location: Cell membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}.
Interaction partners:
Sequence:
MIRIRFGMDVLLVLLLATCLLTPAHGTPLEWDFAVTLRTKIQFMDSSWQTIATAAHEFDELSALTFDESEELIYFNDLKHRNGSIFSLKRDLIAANHVAEQTIARTGNESVGGLAYDPLNMNLFWSDTEQRKIFFAPIHGSATPQVLVDLSAEGGRPDGVAVDVCRRKLYWTNSNVTHPTVERINLDGSNRTVIISSNIDMPRGIVVDQLSDRLFWIDDLKGVFFSVESSKLDGSDRQVVLKDKHHEPLNLAVTNDAIYWTDRTTRAVWSHPKVPVIKVTTTSKPDEEDSTDSTDFKDPEPVAEDCPLVRVANLSEEARGIVARTGFYQRLQKDHHCASIVRKVKERVDEQSRKFEIRSLLDQKIKVLEDERCMNDGEYRAATDLCICPTGFKGSRCEIRECHNYCVHGTCQMSELAYPKCYCQPGFKGERCELSVCSGLCLNGGHCRVSKDENEAPSCECPAKFGGARCEQNSTEICSLFCRLLKHEPEMYVPFGCHSICEELAQDNSTNIAIPQYQHLEVCLTPRVWTSSVIIILVVGIVSSLLLVAVIVQGIRRLYKPKRPRIRKTFVVRKQARTNSAGDTPLTNRPLATEQCEITIENCCNMNICETPCFDPKLVEQTLSKSSCKEDKKILIHNMEDDLY
Protein: IP08853p (Ladybird late, isoform B) (Q4V727)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MPQRTPSPANSDVSVGSPSPPPLRSLNMKRLRLLRSPISLEHDRQKSSPVRVKSFSIADILGRGHEEDRVEKKPERIAIPNALPGVPAPLALINERLQIPLVPNCPPPAALHTFLSPALLHSYEQRLAWDYQRQLQEHFQAQAQLLRQMTLNPAIIASEDGSSERSQRSSSSNGSTECCSPTQAEKVEKRSQEDRMEVPKKSPEEQPKGASKSSGDTPLDALFQLSTKNFDEEQVSTSKRHSALRWNIFETSPKSKGTKGITNAGMNGKLSDLEKQAQVGVIVDVDVAIYTQHD
Protein: P2X purinoceptor 7 (P2X7) (ATP receptor) (P2Z receptor) (Purinergic receptor) (Q99572)
Organism: Homo sapiens (Human)
Function: Receptor for ATP that acts as a ligand-gated ion channel. Responsible for ATP-dependent lysis of macrophages through the formation of membrane pores permeable to large molecules. Could function in both fast synaptic transmission and the ATP-mediated lysis of antigen-presenting cells. In the absence of its natural ligand, ATP, functions as a scavenger receptor in the recognition and engulfment of apoptotic cells.
Subcellular location: Cell membrane {ECO:0000269|PubMed:12107182, ECO:0000269|PubMed:23303206, ECO:0000269|PubMed:28326637}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q64663}.
Interaction partners:
- P2X purinoceptor 4
- Pannexin-1
- P2X purinoceptor 1
- P2X purinoceptor 3
- P2X purinoceptor 6
- P2X purinoceptor 5
- Glutamate receptor ionotropic, NMDA 2A
- Glutamate receptor ionotropic, NMDA 1
- Glutamate receptor ionotropic, NMDA 2C
- Glutamate receptor ionotropic, NMDA 2D
Sequence:
MPACCSCSDVFQYETNKVTRIQSMNYGTIKWFFHVIIFSYVCFALVSDKLYQRKEPVISSVHTKVKGIAEVKEEIVENGVKKLVHSVFDTADYTFPLQGNSFFVMTNFLKTEGQEQRLCPEYPTRRTLCSSDRGCKKGWMDPQSKGIQTGRCVVYEGNQKTCEVSAWCPIEAVEEAPRPALLNSAENFTVLIKNNIDFPGHNYTTRNILPGLNITCTFHKTQNPQCPIFRLGDIFRETGDNFSDVAIQGGIMGIEIYWDCNLDRWFHHCRPKYSFRRLDDKTTNVSLYPGYNFRYAKYYKENNVEKRTLIKVFGIRFDILVFGTGGKFDIIQLVVYIGSTLSYFGLAAVFIDFLIDTYSSNCCRSHIYPWCKCCQPCVVNEYYYRKKCESIVEPKPTLKYVSFVDESHIRMVNQQLLGRSLQDVKGQEVPRPAMDFTDLSRLPLALHDTPPIPGQPEEIQLLRKEATPRSRDSPVWCQCGSCLPSQLPESHRCLEELCCRKKPGACITTSELFRKLVLSRHVLQFLLLYQEPLLALDVDSTNSRLRHCAYRCYATWRFGSQDMADFAILPSCCRWRIRKEFPKSEGQYSGFKSPY