wanglab/gogpt-training-data huggingface dataset:
Protein: Arachidonate 5-lipoxygenase (A0A087X109)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MPSYTVTVATGSQWFAGTDDYIYLSLVGSAGCSEKHLLDKPFYNDFERGAVDSYDVTVDEELGEIQLVRIEKRKYWLNDDWYLKYITLKTPHGDYIEFPCYRWITGDVEVVLRDGREMDGVEPWLPLEHRCQMPQGFTP
Protein: Rap GTPase activating protein 1, isoform E (Q9VM02)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MGVLRWRDSPGSRISGSIGNSSGNSNNNHHHSSNSNSSSGNNNAHQQQHNNNHINNNMNNNNNRENHHRGSNASEERVPQPHSPHDSHAHPHNGGLQHSGSRATLRHSMNHSSSSTVSGSACSSTPASPQLSGVVSASGCQLLSNGHHYQSQSSVSSNSSIVSAIPASQRLLEEALAKPAPYPMILLPLHGGYWMDGTEHECGYDARGNPLLPQTTWMAKFETDDTAKCYRRFYAAREHSNLIGLDEQLGPILLSIKTENVANQEHMRILMRLRTGTMHELLPVSCLLPQPSPAKMAHTLNENITVEHFMPILCPKASQLISVYDEHVLVSHFKFGVLYQRYGQTTEEELFGNQQTSPAFDEFLDVLGQRIRLKDHKGYRGGLDIQNGHTGDTAVYEVFKEREIMFHVSTLLPHTEGDPQQLQRKRHIGNDIVAIVFQETNTPFSPDMIASHFLHAFIVVQPIEPNTPHTRYKVSVTARDDVPFFGPTLPNPAVFRKGQEFKEFILTKLINAENACYKAEKFAKLEQRTRTSLLQNLCEELREKTRDFLGTDLSQTSAGSPTPETPKAESGSGGNAGSRFIDTVKKALIMRVRSQSVDTGNGHGPGQTDKFSVNTKLGTLNSKKETHPEMQTPNLNTCSRTASKSSSKSKSSNESTSSSPDITSRQANNNNTNSIGGHLPQNGTGGGVVAAAVSAAQNGVVAVATMSETSDDSSLNSVDLDPMMAHLDGGATYIDSDTGLESMSSAEATTKACSLCLDGVQSTIMGSSPSNETIVKIENLRQEVTRLKCDKLDLLRQNVTCQRDIKRLRERELSLQGDLSAAGREILRLRDLLKEYMPDTASAPLSISPI
Protein: AT1G60000 protein (Nucleic acid-binding protein, putative) (Putative nucleic acid-binding protein) (RNA-binding (RRM/RBD/RNP motifs) family protein) (T2K10.5 protein) (Q9ZUJ3)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Plastid, chloroplast {ECO:0000256|ARBA:ARBA00004229}.
Interaction partners:
Sequence:
MAASSVLLSCFKSHHQPNLLHGCNYSSNQTLLRFNFSTPKPLLISSRSCSRRFRVLSETITVKLEEEEKDDGASAVLDPPAAVNTKLYFGNLPYNVDSATLAQIIQDFANPELVEVLYNRDTGQSRGFAFVTMSNVEDCNIIIDNLDGTEYLGRALKVNFADKPKPNKEPLYPETEHKLFVGNLSWTVTSESLAGAFRECGDVVGARVVFDGDTGRSRGYGFVCYSSKAEMETALESLDGFELEGRAIRVNLAQGKKF
Protein: Small ribosomal subunit protein eS30 (40S ribosomal protein S30) (O96269)
Organism: Plasmodium falciparum (isolate 3D7)
Function: Component of the ribosome, a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell (Probable). The small ribosomal subunit (SSU) binds messenger RNAs (mRNAs) and translates the encoded message by selecting cognate aminoacyl-transfer RNA (tRNA) molecules (Probable). The large subunit (LSU) contains the ribosomal catalytic site termed the peptidyl transferase center (PTC), which catalyzes the formation of peptide bonds, thereby polymerizing the amino acids delivered by tRNAs into a polypeptide chain (Probable). The nascent polypeptides leave the ribosome through a tunnel in the LSU and interact with protein factors that function in enzymatic processing, targeting, and the membrane insertion of nascent chains at the exit of the ribosomal tunnel (Probable).
Subcellular location: Cytoplasm {ECO:0000269|PubMed:24913268}.
Interaction partners:
- 60S ribosomal protein L30e, putative
- Small ribosomal subunit protein uS10
- 40S ribosomal protein S17, putative
- 60S acidic ribosomal protein P0
- 40S ribosomal protein S7
- Ribosomal protein S27a, putative
- 40S ribosomal protein S8
- Large ribosomal subunit protein P2
- 60S ribosomal protein L13, putative
- 40S ribosomal protein S9, putative
Sequence:
MGKVHGSLARAGKVKNQTPKVPKLDKKKRLTGRAKKRQLYNRRFSDNGGRKKGPNSKA
Protein: Insulin-like peptide 6 (dILP6) (Insulin-related peptide 6) [Cleaved into: Insulin-like peptide 6 A chain; Insulin-like peptide 6 B chain] (Q9W4Z4)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Secreted {ECO:0000305}.
Interaction partners:
- Insulin-like peptide 5
- Insulin-like peptide 1
- Insulin-like peptide 7
- Insulin-like peptide 3
- Insulin-like receptor
- Insulin-like peptide 2
- Insulin-like peptide 4
- Neural/ectodermal development factor IMP-L2
- Death-associated inhibitor of apoptosis 2
- Insulin receptor substrate 1
Sequence:
MVLKVPTSKVLLVLATLFAVAAMISSWMPQVAASPLAPTEYEQRRMMCSTGLSDVIQKICVSGTVALGDVFPNSFGKRRKRDLQNVTDLCCKSGGCTYRELLQYCKG
Protein: Protein ZPS1 (Q12512)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Interaction partners:
- Zinc-regulated transporter 1
- VEL1-related protein YOR387C
- Zinc-regulated transporter 2
- Zinc-responsive transcriptional regulator ZAP1
- Zinc-regulated transporter 3
- Protein VEL1
Sequence:
MKFSSGKSIIFATIASLALSAPVTYDTNSTAELQSPSSQEILGWSHATFPTIYQTCNETNARMLNAAFKDTAEITAYGKDRLLNYGVDDVYYKRWFGNGSIFTVMGVFEQLMEASKGAMLMRCDDIDGLCAANPNYYAGHHRQSAPAETVICDYFYTSKKPLSTICFEGTIVDVGPKHYAGIDMLHRYLHVPTMSMDGYVGEYAETLEEVVDYTQNNATYAVRNTDNYLYYLADVYSASVIPGGCLGNL
Protein: Cyclin-SDS-like (Protein SOLO DANCERS-like) (OsSDS) (Q10PQ9)
Organism: Oryza sativa subsp. japonica (Rice)
Function: Meiosis-specific cyclin. Required for normal homolog synapsis and recombination in early to mid-prophase 1.
Interaction partners:
- Wee1-like protein kinase
- Cell division control protein 6 homolog
- Cyclin-dependent kinases regulatory subunit 1
- Cyclin-dependent kinase A-1
- Anaphase-promoting complex subunit 10
- Os09g0242300 protein
- Fizzy-related protein, putative, expressed
- Os04g0600000 protein
- Os04g0599800 protein
- Os02g0700100 protein
Sequence:
MPPTMLASVPTRPRSHPFRRRRGAAAAAPPLLPDQIAAAAAAAAKRPAESSTSASSCFHSEVISATSTTCPTSLAAAQRPEKRPRYQDVDEEQPAASECSEIIGGARPRAAEVEVSESSCLASVLESYLACPEQLANDAETTAYSSAREDLTLSETEEEEEEEEVRSGPCICTDCSFSPLHESSSSSDDDNAVPSPTFSLFLALAEQFVPFTHPKTPTATDVALQAGEGKRFEDLDNEVSYERFRRRERRGVVARDYIEVYSSMLGSYGRAVVEQRVVMVNWIMEHSQAMKLQPETVFMGIGLMDRFLTRGYVKGSRNLQLLGIACTTLATRIEENQPYNCILQKAFKVGINTYSRSEVVAMEWLVQEVLDFQCFVTTTHHFLWFYLKAANADDRVEDLAKYLALLSLLDHKHLSFWPSTVAAAVVALACLATNNESSCHLVMETHMRTKNDDLPECLMSLEWLTNYAS
Protein: Lysozyme 2 (EC 3.2.1.17) (1,4-beta-N-acetylmuramidase 2) (Invertebrate-type lysozyme 2) (cv-lysozyme 2) (Q1XG90)
Organism: Crassostrea virginica (Eastern oyster)
Function: The main role of this lysozyme is in digestion. Has antibacterial activity against the Gram-positive bacterium P.cerevisiae and the Gram-negative bacteria E.coli and V.vulnificus. Shows some chitinase activity but no isopeptidase activity.
Subcellular location: Secreted.
Interaction partners:
Sequence:
MNFLILFCVVASASVVYSSISDQCLRCICEVESGCRAIGCHWDVYSNSCGYFQIKQGYWTDCGSPGHSMESCADNYNCASGCVRSYMDHYIKYNGCADTCESYARMHNGGPNGCKSSHHHATDNYWRLVQAKGCS
Protein: Intraflagellar transport-associated protein (Protein HEPIS) (Q86VG3)
Organism: Homo sapiens (Human)
Function: Seems to play a role in ciliary BBSome localization, maybe through interaction with IFT-A complex.
Interaction partners:
- Intraflagellar transport protein 122 homolog
- Intraflagellar transport protein 43 homolog
- WD repeat-containing protein 19
- Intraflagellar transport protein 140 homolog
- WD repeat-containing protein 35
Sequence:
MSAHMSGLEIMDEDQLIKDVLDKFLNCHEQTYDEEFLNTFTHLSQEDHVSKRGVFGTDSSENIFTSAKVTHKNEADDYHLRNKTIFLRTSSQCLEEQVDNFLDLEDLDMDEEIKPQMSEDLLLLPGEVEQDVSTSIPSCIPFVAQPPTCEVKPKPSVKRMDKQTEEILGDEVQLFSLDEEFDYDNVMLTSKFSPAEIENIKELCKQQKRKDTSPDLEKSCD
Protein: 2'-5'-oligoadenylate synthase 3 ((2-5')oligo(A) synthase 3) (2-5A synthase 3) (EC 2.7.7.84) (2',5'-oligoadenylate synthetase-like 10) (Q8VI93)
Organism: Mus musculus (Mouse)
Function: Interferon-induced, dsRNA-activated antiviral enzyme which plays a critical role in cellular innate antiviral response. In addition, it may also play a role in other cellular processes such as apoptosis, cell growth, differentiation and gene regulation. Synthesizes preferentially dimers of 2'-5'-oligoadenylates (2-5A) from ATP which then bind to the inactive monomeric form of ribonuclease L (RNase L) leading to its dimerization and subsequent activation. Activation of RNase L leads to degradation of cellular as well as viral RNA, resulting in the inhibition of protein synthesis, thus terminating viral replication. Can mediate the antiviral effect via the classical RNase L-dependent pathway or an alternative antiviral pathway independent of RNase L.
Subcellular location: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
Interaction partners:
- Antiviral innate immune response effector IFIT1
- Interferon regulatory factor 7
- Interferon-induced protein 44
- Interferon-induced, double-stranded RNA-activated protein kinase
- S-adenosylmethionine-dependent nucleotide dehydratase RSAD2
- 2-5A-dependent ribonuclease
- Ubl carboxyl-terminal hydrolase 18
- Interferon-induced protein with tetratricopeptide repeats 3
- DExD/H box helicase 60
- Interferon-induced protein with tetratricopeptide repeats 2
Sequence:
MDLFHTPAGALDKLVAHNLHPAPEFTAAVRGALGSLNITLQQHRARGSQRPRVIRIAKGGAYARGTALRGGTDVELVIFLDCFQSFGDQKTCHSETLGAMRMLLESWGGHPGPGLTFEFSQSKASRILQFRLASADGEHWIDVSLVPAFDVLGQPRSGVKPTPNVYSSLLSSHCQAGEYSACFTEPRKNFVNTRPAKLKNLILLVKHWYHQVQTRAVRATLPPSYALELLTIFAWEQGCGKDSFSLAQGLRTVLALIQHSKYLCIFWTENYGFEDPAVGEFLRRQLKRPRPVILDPADPTWDVGNGTAWRWDVLAQEAESSFSQQCFKQASGVLVQPWEGPGLPRAGILDLGHPIYQGPNQALEDNKGHLAVQSKERSQKPSNSAPGFPEAATKIPAMPNPSANKTRKIRKKAAHPKTVQEAALDSISSHVRITQSTASSHMPPDRSSISTAGSRMSPDLSQIPSKDLDCFIQDHLRPSPQFQQQVKQAIDAILCCLREKSVYKVLRVSKGGSFGRGTDLRGSCDVELVIFYKTLGDFKGQKPHQAEILRDMQAQLRHWCQNPVPGLSLQFIEQKPNALQLQLASTDLSNRVDLSVLPAFDAVGPLKSGTKPQPQVYSSLLSSGCQAGEHAACFAELRRNFINTCPPKLKSLMLLVKHWYRQVVTRYKGGEAAGDAPPPAYALELLTIFAWEQGCGEQKFSLAEGLRTILRLIQQHQSLCIYWTVNYSVQDPAIRAHLLCQLRKARPLVLDPADPTWNVGQGDWKLLAQEAAALGSQVCLQSGDGTLVPPWDVTPALLHQTLAEDLDKFISEFLQPNRHFLTQVKRAVDTICSFLKENCFRNSTIKVLKVVKGGSSAKGTALQGRSDADLVVFLSCFRQFSEQGSHRAEIISEIQAHLEACQQMHSFDVKFEVSKRKNPRVLSFTLTSQTLLDQSVDFDVLPAFDALGQLRSGSRPDPRVYTDLIHSCSNAGEFSTCFTELQRDFITSRPTKLKSLIRLVKYWYQQCNKTIKGKGSLPPQHGLELLTVYAWEQGGQNPQFNMAEGFRTVLELIVQYRQLCVYWTINYSAEDKTIGDFLKMQLRKPRPVILDPADPTGNLGHNARWDLLAKEATVYASALCCVDRDGNPIKPWPVKAAV
Protein: Beta-D-glucan exohydrolase-like protein (Glycosyl hydrolase family protein) (Q9SD68)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- Beta-glucosidase 19
- Beta-glucosidase 24
- Beta-glucosidase 44
- Beta-fructofuranosidase, insoluble isoenzyme CWINV6
- Putative serine carboxypeptidase-like 30
- F8A5.27 protein
- Beta-fructofuranosidase, insoluble isoenzyme CWINV5
- Beta-fructofuranosidase, insoluble isoenzyme CWINV3
- Beta-fructofuranosidase, insoluble isoenzyme CWINV2
- Beta-fructofuranosidase, insoluble isoenzyme CWINV4
Sequence:
MVDNEKSYVYKNREAPVEARVKDLLSRMTLAEKIGQMTLIERSVASEAVIRDFSIGSVLNRAGGWPFEDAKSSNWADMIDGFQRSALESRLGIPIIYGIDAVHGNNDVYGATIFPHNIGLGATRDADLVKRIGAATALEVRACGAHWAFAPCVAVVKDPRWGRCYESYGEVAQIVSEMTSLVSGLQGEPSKDHTNGYPFLAGRKNVVACAKHFVGDGGTNKAINEGNTILRYEDLERKHIAPYKKCISQGVSTVMASYSSWNGDKLHSHYFLLTEILKQKLGFKGYVVSDWEGLDRLSDPPGSNYRNCVKIGINAGIDMVMVPFKYEQFRNDLIDLVESGEVSMARVNDAVERILRVKFVAGLFEFPLTDRSLLPTVGCKEHRELAREAVRKSLVLLKNGRYGEFLPLNCNAERILVVGTHADDLGYQCGGWTKTMYGQSGRITDGTTLLDAIKAAVGDETEVIYEKSPSEETLASGYRFSYAIVAVGESPYAETMGDNSELVIPFNGSEIITTVAEKIPTLVILFSGRPMFLEPQVLEKAEALVAAWLPGTEGQGIADVIFGDYDFRGKLPATWFKRVDQLPLDIESNGYLPLFPLGFGLNGDSVENSDTV
Protein: Uncharacterized protein (A0A1D8PHY0)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Interaction partners:
- NADH-ubiquinone oxidoreductase
- Uncharacterized protein
- Complex 1 LYR protein domain-containing protein
- Nuc2p
- Uncharacterized protein
- NADH dehydrogenase 1 beta subcomplex subunit 9
- NADH dehydrogenase iron-sulfur protein 4
- NADH-ubiquinone oxidoreductase B12 subunit
- 4Fe-4S ferredoxin-type domain-containing protein
- Zinc finger CHCC-type domain-containing protein
Sequence:
MISRIGLRTPAKALSLSSRGVAGYTSRIALTRSYATQKATIYDQSTGQTIELADPEHPELADFKNPPFVLKQYLDPYAKYDDPQNRRNKNDPMHIDEDMLDLWSPDYYDHVSDSTALKHNAIFFGLIFGISAVIAYFQLNPEKPAMIRSFPYNGLADALGATSEETAPFYQNKPDLTAEKECGILPADNDITNNQAAYEKENSEFIKSGTA
Protein: Dual 3',5'-cyclic-AMP and -GMP phosphodiesterase 11 (EC 3.1.4.35) (EC 3.1.4.53) (cAMP and cGMP phosphodiesterase 11) (PDE11) (Q9VJ79)
Organism: Drosophila melanogaster (Fruit fly)
Function: Plays a role in signal transduction by regulating the intracellular concentration of cyclic nucleotides cAMP and cGMP. Dual-specificity phosphodiesterase that catalyzes the hydrolysis of both cAMP and cGMP to 5'-AMP and 5'-GMP, respectively.
Interaction partners:
- Dual specificity calcium/calmodulin-dependent 3',5'-cyclic nucleotide phosphodiesterase 1
- Adenylate kinase 2
- AMP deaminase
- 7-methylguanosine phosphate-specific 5'-nucleotidase
- 5'-nucleotidase
- 5'-Nucleotidase C-terminal domain-containing protein
- apyrase
- Apyrase
- 5'-nucleotidase
- Uncharacterized protein, isoform C
Sequence:
MGQAASMCRFRGCRYKNKNKSSKQQQQQQQQQQQQQQQHQQQQQQTPSHSPQIQHHSEIIPATTGLHLRSIEEPATTPLQFQPTGRMNTEQGGTGYGGYGSSEHSLLIATRHAGVPLPLAQHQPLPAHYQPLNHSGAAPPSSSNGSSSSGGGVQTSATPQQQQQYQVQQPYQYQYQHHYHHQANSPQHHRPYDPEHARMEAWLDENQEFVQDYFIRKATRQTVDAWLVSHATSAGNDVVSSTSPTHANGQTSSSRGGSGATTPVRKISAHEFERGGLLKPIVNTIDGTPTFLSIGPPMDNGSVGGSCSNLQNVGGVVAGQYQYNHQQHHHNHAHLHHSQHSHYQAGGAVGSSSLGSTGGASGAGGAPSLGGSGGAGNGHQYPYYHCHQRPQRLSRNELKQLDEKELIFELVKDICNELEVRTLCHKILQNVSILLNADRGSLFLVQGRCNGPDGLKKCLVSKLFDVCPRSTVEEMEQQDEVRVAWGTGIAGHVAESGEPVNIPDAYQDERFNCEIDSLTGYRTKALLCMPIKDSSGDVIGVAQVINKMNGECFSEIDEKVFSSYLQFCGIGLRNAQLYEKSQLEIKRNQVLLDLARMIFEEQSTIEHMVFRILTHMQSLIQCQRVQILLVHEADKGSFSRVFDFEANDLSEEEATSRTSPYESRFPINIGITGHVATTGETVNVPNAYEDDRFDASVDENSCFKHRSILCMAIKNSLGQIIGVIQLINKFNELDFTKNDENFVEAFAIFCGMGIHNTHMYEKAIVAMAKQSVTLEVLSYHASATMDEAHRLRRLRVPSAVHFRLHDFKFDDIHFEDDDTLKACLRMFLDLDFVERFHIDYEVLCRWLLSVKKNYRNVTYHNWRHAFNVAQMMFAILTTTQWWKIFGEIECLALIIGCLCHDLDHRGTNNSFQIKASSPLAQLYSTSTMEHHHFDQCLMILNSPGNQILANLSSDDYCRVIRVLEDAILSTDLAVYFKKRGPFLESVSQPTSYWVAEEPRALLRAMSMTVCDLSAITKPWEIEKRVADLVSSEFFEQGDMEKQELNITPIDIMNREKEDELPMMQVNFIDSICLPIYEAFATLSDKLEPLVEGVRDNRGHWIDLADVVKTKTSQDQEPEEEQQQQNVISNGDCKAMSDDDVAASEAEVAVDSPSEKASVNGSNVANNSSNTNKKIAVASHPTSTQPSDDDNDVDADADDVDEQAAEENGHDAEVDEASCRSNSTCSSSTASSCLSTPPPTGEDDSTPVSPLKTLQAKLVAANLNALQRQTSNQAQTQKQRCKSCDHSRSGLQVRKTSSLRGAQELDLDSKTRNGTHAALCKSTPVINNHSHHHNHSHSHNHNHHHHHHHHSHHNHSQHGIGIGSASIGGSGLISLTTPLLAMDSDRIPKIVGKIGNLDGLPFANGIGGPQNGHGLPFGSYQHHHHHQHHHHLLARRHSETNSNGATAMAVEK
Protein: Lachesin (Q24372)
Organism: Drosophila melanogaster (Fruit fly)
Function: Required for normal tracheal development and maintenance of the trans-epithelial diffusion barrier. Functions as a homophilic cell-adhesion molecule. May play a role in early neuronal differentiation and axon outgrowth.
Subcellular location: Cell membrane {ECO:0000269|PubMed:14681183, ECO:0000269|PubMed:8223276}; Lipid-anchor, GPI-anchor {ECO:0000269|PubMed:14681183, ECO:0000269|PubMed:8223276}; Extracellular side {ECO:0000269|PubMed:14681183, ECO:0000269|PubMed:8223276}. Note=Located at the extracellular face of the membrane and becomes associated with septate junctions.
Interaction partners:
- Sinuous
- Neurexin-4
- Kune-kune
- Contactin
- Neuroglian
- Sodium/potassium-transporting ATPase subunit beta-2
- Fasciclin-3
- Transferrin 2
Sequence:
MWRPSISNCVWSTLLLAIFVQQTLAQRTPTISYITQEQIKDIGGTVEFDCSVQYAKEYNVLFLKTDSDPVFLSTGSTLVIKDSRFSLRYDPNSSTYKLQIKDIQETDAGTYTCQVVISTVHKVSAEVKLSVRRPPVISDNSTQSVVASEGSEVQMECYASGYPTPTITWRRENNAILPTDSATYVGNTLRIKSVKKEDRGTYYCVADNGVSKGDRRNINVEVEFAPVITVPRPRLGQALQYDMDLECHIEAYPPPAIVWTKDDIQLANNQHYSISHFATADEYTDSTLRVITVEKRQYGDYVCKATNRFGEAEARVNLFETIIPVCPPACGQAYIAGAEDVSATSFALVGILAALLFAR
Protein: Heat shock cognate 70 kDa protein 1 (HSC70-1) (P36415)
Organism: Dictyostelium discoideum (Social amoeba)
Function: Affects actin polymerization through interaction with the actin-binding protein CAP32/34 (acpA/acpB). Acts as a chaperone by stimulating the refolding of denaturated acpA and acpB, but neither stimulates nor inhibits the capping activity of native CAP32/34.
Subcellular location: Cytoplasm. Note=Found in F-actin-rich regions of the cell cortex and cell protrusions.
Interaction partners:
- Heat shock cognate 90 kDa protein
- DnaJ homolog subfamily A member 1 homolog
- Heat shock protein
- Cell division cycle 5-like protein
- Pre-mRNA-processing factor 19
- Pre-mRNA-splicing factor spf27
- Armadillo-like helical domain-containing protein
- WD40 repeat-containing protein
- GrpE protein homolog, mitochondrial
- Luminal-binding protein 1
Sequence:
MSSIGIDLGTTYSCVGVWQNDRVEIIANDQGNRTTPSYVAFTDTERLIGDAAKNQVAMNPTNTVFDAKRLIGRKFSDKEVQSDMKHWPFKVIPKDGDKPHIQVEFKGETKVFSPEEISSMVLLKMKETAEAYLGKTINNAVITVPAYFNDSQRQATKDAGTISKLNVQRIINEPTAAAIAYGLEKKGSGEKNILIFDLGGGTFDVSLLTIEDGVFEVKATAGDTHLGGEDFDNRLVSHFVDEFKRKHKKDIMGNQRAVRRLRTACERAKRTLSSSAQASIEIDSLFEGIDFYTSITRARFEELCADLFRGCLDPVEKVLKDSKLDKKSIHEIVLVGGSTRIPKVQQLLQEFFNGKELNKSINPDEAVAYGAAVQAAILSNEGGAKVADLLLLDVAPLSMGLETAGGVMTTLIPRNTTIPCKKTQTFSTYSDNQPGVLIQVYEGERAMTKDNNLLGKFELSGIPPAPRGVPQVEVTFDVDANGILNVSAEDKSTGNKQKITITNDKGRLSKEEIEKMVADAEKFKQQDEQQKDRVESKNKLENYAFTVKNSIKDEKVAAKISDSDKSTIESETESVLKWLESNQTAEKDEYEDKMKALEAVVNPIMSKLYQEGGMPQGGGMPGGMSNDSPKSSNNKVDELD
Protein: 3',5'-cyclic-AMP phosphodiesterase 4D (EC 3.1.4.53) (DPDE3) (PDE43) (cAMP-specific phosphodiesterase 4D) (Q08499)
Organism: Homo sapiens (Human)
Function: Hydrolyzes the second messenger cAMP, which is a key regulator of many important physiological processes.
Subcellular location: Apical cell membrane {ECO:0000269|PubMed:14500724}. Cytoplasm {ECO:0000250}. Membrane {ECO:0000250}. Cytoplasm, cytoskeleton {ECO:0000250}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250}. Note=Found in the soluble fraction, associated with membranes, and associated with the cytoskeleton and the centrosome (By similarity). Colocalized with SHANK2 to the apical membrane of colonic crypt cells. {ECO:0000250}.
Interaction partners:
- Myomegalin
- cAMP-dependent protein kinase catalytic subunit alpha
- A-kinase anchor protein 6
- Beta-arrestin-2
- Deoxycytidine kinase
- Adenosine kinase
- cAMP-dependent protein kinase catalytic subunit beta
- cAMP-dependent protein kinase catalytic subunit gamma
- Alpha-aminoadipic semialdehyde dehydrogenase
- Ectonucleotide pyrophosphatase/phosphodiesterase family member 1
Sequence:
MEAEGSSAPARAGSGEGSDSAGGATLKAPKHLWRHEQHHQYPLRQPQFRLLHPHHHLPPPPPPSPQPQPQCPLQPPPPPPLPPPPPPPGAARGRYASSGATGRVRHRGYSDTERYLYCRAMDRTSYAVETGHRPGLKKSRMSWPSSFQGLRRFDVDNGTSAGRSPLDPMTSPGSGLILQANFVHSQRRESFLYRSDSDYDLSPKSMSRNSSIASDIHGDDLIVTPFAQVLASLRTVRNNFAALTNLQDRAPSKRSPMCNQPSINKATITEEAYQKLASETLEELDWCLDQLETLQTRHSVSEMASNKFKRMLNRELTHLSEMSRSGNQVSEFISNTFLDKQHEVEIPSPTQKEKEKKKRPMSQISGVKKLMHSSSLTNSSIPRFGVKTEQEDVLAKELEDVNKWGLHVFRIAELSGNRPLTVIMHTIFQERDLLKTFKIPVDTLITYLMTLEDHYHADVAYHNNIHAADVVQSTHVLLSTPALEAVFTDLEILAAIFASAIHDVDHPGVSNQFLINTNSELALMYNDSSVLENHHLAVGFKLLQEENCDIFQNLTKKQRQSLRKMVIDIVLATDMSKHMNLLADLKTMVETKKVTSSGVLLLDNYSDRIQVLQNMVHCADLSNPTKPLQLYRQWTDRIMEEFFRQGDRERERGMEISPMCDKHNASVEKSQVGFIDYIVHPLWETWADLVHPDAQDILDTLEDNREWYQSTIPQSPSPAPDDPEEGRQGQTEKFQFELTLEEDGESDTEKDSGSQVEEDTSCSDSKTLCTQDSESTEIPLDEQVEEEAVGEEEESQPEACVIDDRSPDT
Protein: DUNC-115m (SD03267p) (Uncoordinated 115b, isoform A) (Uncoordinated 115b, isoform E) (Q9VH92)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MNLMSGSTNRSSPFVFVPFSPQTGKQKIYCAKCTKKCSGEVLRVADNHFHKACFQCCQCKKSLATGGFFTKDNAYYCIPDYQRLYGTKCANCQQYVEGEVVSTMGKTYHQKCFTCSKCKQPFKSGSKVTNTGKEVLCEQCVTGAPVSPSRQATGGGVSSPAPPAESPTRATAHQQHGSVISHKAHLKEDYDPNDCAGCGELLKEGQALVALDRQWHVSCFRCKACQAVLNGEYMGKDAVPYCEKCYQKGFGVKCAYCSRFISGKVLQAGDNHHFHPTCARCTKCGDPFGDGEEMYLQGSAIWHPRCGPGPSESGIILNGGGGTSSVVGGASNGNFTDTECDRMSSSALSEMYIRSRTPSFNGSLYSSSRKHYRTVSPGLILREYGRPNAEDISRIYTYSYLTDAPHYLRKPIDPYDKTPLSPHFHRPSSYATTASNAGSVAGSRPPSRPHSRTRSAMKVLVDAIRSETPRPKSPGMNNEEPIELSHYPAAKKPPPGEQPKIERDDFPAPPYPYTDPERRRRYSDTYKGVPASDDEDENVENGKPNGKVKNGEEQQRLQREAEQLEKLNSGIGSAIAKDLKEHAKYRKWKQNNLDPRNASRTPSASKEPLYKLRYESPIGASPSRNLDHQKPFYEDEMFDRSTSYRGSLGKSLGNAPSYNAIHSYRSPPKPGYGFKTTTLPYIRNGFSSDFSYGGLGDKTHSTDLSCGKSEASVDSITEGDRRALMGGDLPASSTYSGALSYHYPQAGLIRRSLPNMSHSIISCANAKL
Protein: Solute carrier family 35 member E2A (Q8C811)
Organism: Mus musculus (Mouse)
Function: Putative transporter.
Subcellular location: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
Sequence:
MSAAAKSQVPEEAAPGCEEEPKGKTLLTWGSLFGHRSEKIVFTKGDGSPEESLLTVTITETTVIESDLGVWSSRALIYLTLWFFFSFCTLFLNKYILSLLEGEPSMLGAVQMLSTTLIGCVKIFVPCCLYQHKTRLSYPPNFIMTMLFVGLMRFATVVLGLVSLKNVAVSFAETVKSSAPIFTVIMSRMILGEYTGLLVNLSLIPVMGGLALCTATEISFNILGFSAALSTNIMDCLQNVFSKKLLSGDKYRFSAPELQFYTSAAAVALLIPAWTFFMDIPVIGRSGKSFSYSQDIVLLLLTDGALFHLQSVTAYALMGKISPVTFSVASTVKHALSIWLSIIVFGNKITSLSAIGTILVTLGVLLYNKARQYQQETMQSLVTATSRNPEDDTEPLVPQDSRQHH
Protein: NAD-dependent protein lipoamidase sirtuin-4, mitochondrial (EC 2.3.1.-) (NAD-dependent ADP-ribosyltransferase sirtuin-4) (EC 2.4.2.-) (NAD-dependent protein biotinylase sirtuin-4) (EC 2.3.1.-) (NAD-dependent protein deacetylase sirtuin-4) (EC 2.3.1.286) (Regulatory protein SIR2 homolog 4) (SIR2-like protein 4) (Q1JQC6)
Organism: Bos taurus (Bovine)
Function: Acts as NAD-dependent protein lipoamidase, biotinylase, deacetylase and ADP-ribosyl transferase. Catalyzes more efficiently removal of lipoyl- and biotinyl- than acetyl-lysine modifications. Inhibits the pyruvate dehydrogenase complex (PDH) activity via the enzymatic hydrolysis of the lipoamide cofactor from the E2 component, DLAT, in a phosphorylation-independent manner. Catalyzes the transfer of ADP-ribosyl groups onto target proteins, including mitochondrial GLUD1, inhibiting GLUD1 enzyme activity. Acts as a negative regulator of mitochondrial glutamine metabolism by mediating mono ADP-ribosylation of GLUD1: expressed in response to DNA damage and negatively regulates anaplerosis by inhibiting GLUD1, leading to block metabolism of glutamine into tricarboxylic acid cycle and promoting cell cycle arrest. In response to mTORC1 signal, SIRT4 expression is repressed, promoting anaplerosis and cell proliferation. Acts as a tumor suppressor. Also acts as a NAD-dependent protein deacetylase: mediates deacetylation of 'Lys-471' of MLYCD, inhibiting its activity, thereby acting as a regulator of lipid homeostasis. Does not seem to deacetylate PC. Controls fatty acid oxidation by inhibiting PPARA transcriptional activation. Impairs SIRT1-PPARA interaction probably through the regulation of NAD(+) levels. Down-regulates insulin secretion (By similarity).
Subcellular location: Mitochondrion matrix {ECO:0000255|HAMAP-Rule:MF_03161}.
Interaction partners:
- Nicotinamide phosphoribosyltransferase
- Nicotinamide/nicotinic acid mononucleotide adenylyltransferase 1
- Glutamine-dependent NAD
- Nicotinamide/nicotinic acid mononucleotide adenylyltransferase 2
- NAD kinase.
- NAD-capped RNA hydrolase NUDT12
- ADP-ribosyl cyclase/cyclic ADP-ribose hydrolase 1
- Nicotinamide N-methyltransferase
- Purine nucleoside phosphorylase
- ADP-ribosyl cyclase/cyclic ADP-ribose hydrolase
Sequence:
MRMSFGLTFKRTAKVHWRANFSQQCSLRSTGLFVPPSPPLDPEKVKELQRFITLSKRLLVMTGAGISTESGIPDYRSEKVGLYARTDRRPIQHGDFVRSAPVRQRYWARNFVGWPQFSSRQPNPAHWALSNWERLGKLHWLVTQNVDALHTKAGSQRLTELHGCMHRVLCLDCGEQTPRGVLQERFQVLNPTWSAEAHGLAPDGDVFLTEEEVQSFQVPSCSRCGGPLKPDVVFFGDTVKPDKVDFVHKRVKEADSLLVVGSSLQVYSGYRFILTAREKKLPIVILNIGPTRSDDLASLKLDSRCGELLPLIDPR
Protein: Transmembrane protein 106C (Endoplasmic reticulum membrane protein overexpressed in cancer) (Q9BVX2)
Organism: Homo sapiens (Human)
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|Ref.1}; Multi-pass membrane protein {ECO:0000269|Ref.1}. Membrane {ECO:0000305}; Lipid-anchor {ECO:0000305}.
Interaction partners:
Sequence:
MGSQHSAAARPSSCRRKQEDDRDGLLAEREQEEAIAQFPYVEFTGRDSITCLTCQGTGYIPTEQVNELVALIPHSDQRLRPQRTKQYVLLSILLCLLASGLVVFFLFPHSVLVDDDGIKVVKVTFNKQDSLVILTIMATLKIRNSNFYTVAVTSLSSQIQYMNTVVSTYVTTNVSLIPPRSEQLVNFTGKAEMGGPFSYVYFFCTVPEILVHNIVIFMRTSVKISYIGLMTQSSLETHHYVDCGGNSTAI
Protein: Os07g0676600 protein (cDNA, clone: J075101F12, full insert sequence) (Q8LII5)
Organism: Oryza sativa subsp. japonica (Rice)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MMSRERKKAAALHEKLQILRSITHSHALSNTSIITDASEYIKELKQKVVRLNKEIACAEAAALRQNSIPTVTVETLGHGFLINVFSDKSCPGLLVSILEAFDELGLNVLEATASCDDTFRLEAVGGENQVDEHVIKQTVLQAISNSNCSESSGDQEG
Protein: Calcium/calmodulin-dependent protein kinase II inhibitor 2 (Q6DHN6)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Cytoplasm, cytosol {ECO:0000256|ARBA:ARBA00004514}. Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- Syntaxin-binding protein 6
- Si:ch73-287m6.1.
- RIMS-binding protein 2.
- RIMS-binding protein 2.
Sequence:
MSEVLPYNEGKMNGYGADSEVSQISFSCRLQDTNSFFGTSQSKRPPKLGQIGRAKHVVIEDDRIDEVLKGMTDKSSPGV