wanglab/gogpt-training-data huggingface dataset:
Protein: Bifunctional peptidase and arginyl-hydroxylase JMJD5 (EC 1.14.11.73) (EC 3.4.-.-) (JmjC domain-containing protein 5) (Jumonji C domain-containing protein 5) (L-arginine (3R)-hydroxylase KDM8) (Lysine-specific demethylase 8) (Q9CXT6)
Organism: Mus musculus (Mouse)
Function: Bifunctional enzyme that acts both as an endopeptidase and 2-oxoglutarate-dependent monooxygenase. Endopeptidase that cleaves histones N-terminal tails at the carboxyl side of methylated arginine or lysine residues, to generate 'tailless nucleosomes', which may trigger transcription elongation. Preferentially recognizes and cleaves monomethylated and dimethylated arginine residues of histones H2, H3 and H4. After initial cleavage, continues to digest histones tails via its aminopeptidase activity. Upon DNA damage, cleaves the N-terminal tail of histone H3 at monomethylated lysine residues, preferably at monomethylated 'Lys-9' (H3K9me1). The histone variant H3F3A is the major target for cleavage. Additionnally, acts as Fe(2+) and 2-oxoglutarate-dependent monooxygenase, catalyzing (R)-stereospecific hydroxylation at C-3 of 'Arg-137' of RPS6 and 'Arg-141' of RCCD1, but the biological significance of this activity remains to be established. Regulates mitosis through different mechanisms: Plays a role in transcriptional repression of satellite repeats, possibly by regulating H3K36 methylation levels in centromeric regions together with RCCD1. Possibly together with RCCD1, is involved in proper mitotic spindle organization and chromosome segregation. Negatively regulates cell cycle repressor CDKN1A/p21, which controls G1/S phase transition. Required for G2/M phase cell cycle progression. Regulates expression of CCNA1/cyclin-A1, leading to cancer cell proliferation. Also, plays a role in regulating alpha-tubulin acetylation and cytoskeletal microtubule stability involved in epithelial to mesenchymal transition (By similarity). Regulates the circadian gene expression in the liver. Represses the transcriptional activator activity of the CLOCK-BMAL1 heterodimer in a catalytically-independent manner (By similarity). Negatively regulates the protein stability and function of CRY1; required for AMPK-FBXL3-induced CRY1 degradation.
Subcellular location: Nucleus {ECO:0000250|UniProtKB:Q8N371}. Chromosome {ECO:0000250|UniProtKB:Q8N371}. Note=Colocalizes with trimethylated 'Lys-9' of histone H3 (H3K9me3). {ECO:0000250|UniProtKB:Q8N371}.
Interaction partners:
- RCC1 domain-containing protein 1
- Small ribosomal subunit protein eS6
- Pyruvate kinase PKM
- Bifunctional arginine demethylase and lysyl-hydroxylase JMJD6
Sequence:
MSEDTTEPLVGSSTLWKELRTLLPDKEEELKLDLGEKVDRSVAALLRQAVGLFYAGHWQGCLQASEAVLDYSWEKLNTGPWRDVDKEWRRVYSFGCLLKALCLCQAPQKATTVVEALRVCDMGLLMGAAILEDILLKVVAVLQTHQLPGKQPARGPHQDQPATKKAKCDASPAPDVMLERMVPRLRCPPLQYFKQHFLVPGRPVILEGVADHWPCMKKWSLQYIQEIAGCRTVPVEVGSRYTDEDWSQTLMTVDEFIQKFILSEAKDVGYLAQHQLFDQIPELKRDISIPDYCCLGNGEEEEITINAWFGPQGTISPLHQDPQQNFLVQVLGRKYIRLYSPQESEAVYPHETHILHNTSQVDVENPDLEKFPKFTEAPFLSCILSPGDTLFIPAKYWHYVRSLDLSFSVSFWWS
Protein: Induced myeloid leukemia cell differentiation protein Mcl-1 (Bcl-2-like protein 3) (Bcl2-L-3) (Bcl-2-related protein EAT/mcl1) (mcl1/EAT) (Q07820)
Organism: Homo sapiens (Human)
Function: Involved in the regulation of apoptosis versus cell survival, and in the maintenance of viability but not of proliferation. Mediates its effects by interactions with a number of other regulators of apoptosis. Isoform 1 inhibits apoptosis. Isoform 2 promotes apoptosis.
Subcellular location: Membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}. Cytoplasm. Mitochondrion. Nucleus, nucleoplasm. Note=Cytoplasmic, associated with mitochondria.
Interaction partners:
- Bcl-2-like protein 11
- Apoptosis regulator BAX
- Phorbol-12-myristate-13-acetate-induced protein 1
- Bcl-2-binding component 3, isoforms 3/4
- Bcl-2 homologous antagonist/killer
- Beclin-1
- E3 ubiquitin-protein ligase HUWE1
- BH3-interacting domain death agonist
- Bcl-2-like protein 1
- Bcl-2-like protein 2
Sequence:
MFGLKRNAVIGLNLYCGGAGLGAGSGGATRPGGRLLATEKEASARREIGGGEAGAVIGGSAGASPPSTLTPDSRRVARPPPIGAEVPDVTATPARLLFFAPTRRAAPLEEMEAPAADAIMSPEEELDGYEPEPLGKRPAVLPLLELVGESGNNTSTDGSLPSTPPPAEEEEDELYRQSLEIISRYLREQATGAKDTKPMGRSGATSRKALETLRRVGDGVQRNHETAFQGMLRKLDIKNEDDVKSLSRVMIHVFSDGVTNWGRIVTLISFGAFVAKHLKTINQESCIEPLAESITDVLVRTKRDWLVKQRGWDGFVEFFHVEDLEGGIRNVLLAFAGVAGVGAGLAYLIR
Protein: Calcium-dependent phosphotriesterase superfamily protein (Expressed protein) (Q9SLE2)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
Sequence:
MSPSFCSGRCTAALFLVISAVPIAYLISLELAVPSTHVFSYQSSGFFRECAKWDDVGRRFLVSFMDGGGVGEIVPKDSDDVLEEVTLVKDVDLAGNASLGIAIDHVRNRLLVAVADLLGNRYSALAAYDLSTWRRLFLAELSGQSKEKTFADDVAVDEQGNAYVTDAKASKIWKVDVNGKLVNTITSPLFTPPGWYNNLVALNGIVYHPDGFLIVIHTFSGYLYKIDLTNGDVSNQVSVIDVSGGTLRFGDGLELLSPTKIVVAGSSSTKLVESSDGWRTASVTGWFSSGMVHRVVSSATVKEGRVYLNHIVGFGSKKKHVLVEAVF
Protein: ATP-dependent 6-phosphofructokinase (ATP-PFK) (Phosphofructokinase) (EC 2.7.1.11) (Phosphohexokinase) (A0A060WI24)
Organism: Oncorhynchus mykiss (Rainbow trout) (Salmo gairdneri)
Subcellular location: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03184}.
Interaction partners:
- Glucose-6-phosphate isomerase
- Glucose-6-phosphate isomerase
- glucose-6-phosphate isomerase
- Glucose-6-phosphate isomerase
- Phosphotransferase
- Phosphotransferase
- Phosphotransferase
- Transaldolase
- Transaldolase
- Phosphofructokinase domain-containing protein
Sequence:
MAHPKDHSKMGFGRSIAVLTSGGDAQGMNAAVRATVRVGIYTGAKVYFVHEGYQGLVDGGDNIKPATWESVSMMLQLGGTVIGSARCMDFKEKWGRLKAACNLVKLGITNLCVIGGDGSLTGANQFRTEWSELLADLIKQGKITAEEAKRSSHLNIVGMVGSIDNDFCGTDMTIGTDSALHRIIEVVDAITTTAQSHQRTFILEVMGRHCGYLALVTALACGADWVFIPEMPPEDNWEEHLCKRLIAQRERGSRLNVIIMAEGAQDRKQKPITCDQVKNLVSKKLGFDTRSTILGHVQRGGTPSAFDRILGSRMGVEAVMALLEATPETPACVVSLSGNMAIRLPLMECVQVTKDVTVAMAEGRFEDAVNLRGKSFQNNWNTYKMLAHVNPPEVKSNINIAIVNVGAPCAGMNAAVRSAVRAGLIQGHQMLAIHDGFDGLANGQIEPITWAQVGGWTGKGGSNLGTKRNLPGKNIEQISLNIAKFNIHSLIIIGGFEAYLGGLELVTAREKYEELCIPMVVIPATVSNNVPGSDFSIGADTALNTITMTCDRIKQSAAGTKRRVFIIETMGGYCGYLATMAGLSSGADAAYIYEEPFHIHDLELNVVHLIEKMKTSVKRGLILRNSNANDNYTTQFLYNLYSEEGKGTFDCRMNILGHMQQGGTPTPFDRNFGTKMGAKSVLWLTDKLKECYRHGRIFANTPDSACVLGMKRRSLIFQPLTSLKEDTDFEHRIPKTEWWLKLRPILKILARYEAVEIDTSEVAAMEHIIKKTGEIKGGKI
Protein: Gamma-aminobutyraldehyde dehydrogenase (ABALDH) (EC 1.2.1.19) (1-pyrroline dehydrogenase) (4-aminobutanal dehydrogenase) (5-aminopentanal dehydrogenase) (EC 1.2.1.-) (P77674)
Organism: Escherichia coli (strain K12)
Function: Catalyzes the oxidation 4-aminobutanal (gamma-aminobutyraldehyde) to 4-aminobutanoate (gamma-aminobutyrate or GABA). This is the second step in one of two pathways for putrescine degradation, where putrescine is converted into 4-aminobutanoate via 4-aminobutanal, which allows E.coli to grow on putrescine as the sole nitrogen source. Also functions as a 5-aminopentanal dehydrogenase in a a L-lysine degradation pathway to succinate that proceeds via cadaverine, glutarate and L-2-hydroxyglutarate. Can also oxidize n-alkyl medium-chain aldehydes, but with a lower catalytic efficiency.
Interaction partners:
- Putrescine aminotransferase
- 4-aminobutyrate aminotransferase GabT
- Inner membrane ABC transporter permease protein YdcV
- Gamma-glutamyl-gamma-aminobutyrate hydrolase PuuD
- Bifunctional polyhydroxybutyrate synthase / ABC transporter periplasmic binding protein
- 4-aminobutyrate aminotransferase PuuE
- tRNA pseudouridine synthase D
- Methionyl-tRNA formyltransferase
- Inner membrane ABC transporter permease protein YdcU
- Uncharacterized ABC transporter ATP-binding protein YdcT
Sequence:
MQHKLLINGELVSGEGEKQPVYNPATGDVLLEIAEASAEQVDAAVRAADAAFAEWGQTTPKVRAECLLKLADVIEENGQVFAELESRNCGKPLHSAFNDEIPAIVDVFRFFAGAARCLNGLAAGEYLEGHTSMIRRDPLGVVASIAPWNYPLMMAAWKLAPALAAGNCVVLKPSEITPLTALKLAELAKDIFPAGVINILFGRGKTVGDPLTGHPKVRMVSLTGSIATGEHIISHTASSIKRTHMELGGKAPVIVFDDADIEAVVEGVRTFGYYNAGQDCTAACRIYAQKGIYDTLVEKLGAAVATLKSGAPDDESTELGPLSSLAHLERVGKAVEEAKATGHIKVITGGEKRKGNGYYYAPTLLAGALQDDAIVQKEVFGPVVSVTPFDNEEQVVNWANDSQYGLASSVWTKDVGRAHRVSARLQYGCTWVNTHFMLVSEMPHGGQKLSGYGKDMSLYGLEDYTVVRHVMVKH
Protein: Receptor-type tyrosine-protein phosphatase F (EC 3.1.3.48) (Leukocyte common antigen related) (LAR) (P10586)
Organism: Homo sapiens (Human)
Function: Possible cell adhesion receptor. It possesses an intrinsic protein tyrosine phosphatase activity (PTPase) and dephosphorylates EPHA2 regulating its activity.
Subcellular location: Membrane; Single-pass type I membrane protein.
Interaction partners:
- Liprin-alpha-1
- Liprin-alpha-3
- Leucine-rich repeat-containing protein 4B
- Catenin beta-1
- Liprin-beta-1
- Insulin receptor
- Insulin receptor substrate 1
- Tyrosine-protein phosphatase non-receptor type 1
- Tyrosine-protein phosphatase non-receptor type 11
- Insulin receptor substrate 2
Sequence:
MAPEPAPGRTMVPLVPALVMLGLVAGAHGDSKPVFIKVPEDQTGLSGGVASFVCQATGEPKPRITWMKKGKKVSSQRFEVIEFDDGAGSVLRIQPLRVQRDEAIYECTATNSLGEINTSAKLSVLEEEQLPPGFPSIDMGPQLKVVEKARTATMLCAAGGNPDPEISWFKDFLPVDPATSNGRIKQLRSGALQIESSEESDQGKYECVATNSAGTRYSAPANLYVRVRRVAPRFSIPPSSQEVMPGGSVNLTCVAVGAPMPYVKWMMGAEELTKEDEMPVGRNVLELSNVVRSANYTCVAISSLGMIEATAQVTVKALPKPPIDLVVTETTATSVTLTWDSGNSEPVTYYGIQYRAAGTEGPFQEVDGVATTRYSIGGLSPFSEYAFRVLAVNSIGRGPPSEAVRARTGEQAPSSPPRRVQARMLSASTMLVQWEPPEEPNGLVRGYRVYYTPDSRRPPNAWHKHNTDAGLLTTVGSLLPGITYSLRVLAFTAVGDGPPSPTIQVKTQQGVPAQPADFQAEVESDTRIQLSWLLPPQERIIMYELVYWAAEDEDQQHKVTFDPTSSYTLEDLKPDTLYRFQLAARSDMGVGVFTPTIEARTAQSTPSAPPQKVMCVSMGSTTVRVSWVPPPADSRNGVITQYSVAYEAVDGEDRGRHVVDGISREHSSWDLVGLEKWTEYRVWVRAHTDVGPGPESSPVLVRTDEDVPSGPPRKVEVEPLNSTAVHVYWKLPVPSKQHGQIRGYQVTYVRLENGEPRGLPIIQDVMLAEAQWRPEESEDYETTISGLTPETTYSVTVAAYTTKGDGARSKPKIVTTTGAVPGRPTMMISTTAMNTALLQWHPPKELPGELLGYRLQYCRADEARPNTIDFGKDDQHFTVTGLHKGTTYIFRLAAKNRAGLGEEFEKEIRTPEDLPSGFPQNLHVTGLTTSTTELAWDPPVLAERNGRIISYTVVFRDINSQQELQNITTDTRFTLTGLKPDTTYDIKVRAWTSKGSGPLSPSIQSRTMPVEQVFAKNFRVAAAMKTSVLLSWEVPDSYKSAVPFKILYNGQSVEVDGHSMRKLIADLQPNTEYSFVLMNRGSSAGGLQHLVSIRTAPDLLPHKPLPASAYIEDGRFDLSMPHVQDPSLVRWFYIVVVPIDRVGGSMLTPRWSTPEELELDELLEAIEQGGEEQRRRRRQAERLKPYVAAQLDVLPETFTLGDKKNYRGFYNRPLSPDLSYQCFVLASLKEPMDQKRYASSPYSDEIVVQVTPAQQQEEPEMLWVTGPVLAVILIILIVIAILLFKRKRTHSPSSKDEQSIGLKDSLLAHSSDPVEMRRLNYQTPGMRDHPPIPITDLADNIERLKANDGLKFSQEYESIDPGQQFTWENSNLEVNKPKNRYANVIAYDHSRVILTSIDGVPGSDYINANYIDGYRKQNAYIATQGPLPETMGDFWRMVWEQRTATVVMMTRLEEKSRVKCDQYWPARGTETCGLIQVTLLDTVELATYTVRTFALHKSGSSEKRELRQFQFMAWPDHGVPEYPTPILAFLRRVKACNPLDAGPMVVHCSAGVGRTGCFIVIDAMLERMKHEKTVDIYGHVTCMRSQRNYMVQTEDQYVFIHEALLEAATCGHTEVPARNLYAHIQKLGQVPPGESVTAMELEFKLLASSKAHTSRFISANLPCNKFKNRLVNIMPYELTRVCLQPIRGVEGSDYINASFLDGYRQQKAYIATQGPLAESTEDFWRMLWEHNSTIIVMLTKLREMGREKCHQYWPAERSARYQYFVVDPMAEYNMPQYILREFKVTDARDGQSRTIRQFQFTDWPEQGVPKTGEGFIDFIGQVHKTKEQFGQDGPITVHCSAGVGRTGVFITLSIVLERMRYEGVVDMFQTVKTLRTQRPAMVQTEDQYQLCYRAALEYLGSFDHYAT
Protein: Uncharacterized protein (Q382S8)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- Flagellar attachment zone protein 1 conserved domain-containing protein
- Flagellar attachment zone protein 1 conserved domain-containing protein
Sequence:
MSTSLVTLASVLASDCTHYAGDPNLLKADRYADRVMKLLQSEQADLLAVRVAIHAQLRDAFRDDSVQKMLRPYLRSDENIADLIEDPKARAKFFMNKQQELQAVVMDSAEQVALRDAHRELAIWERENAVLLRHQMFMPYKPSLALLLESAATIALYRQYATLEEGHCSSDSSSGEVPEQLVKMGGVPLFTLKSEQKPFEVDEHTKMYSQQVLQNKRVEYEEKRGLVARHRKALEECPSLFRLQEFINVRNEIMRKFGIDRLVSLRARRDKALAEPFEGGEDVSTRGLPADNEIVKSRRVAQYSLPKIVQQCHKNYVTIVGGGPSDTEEGGVQVSGAIATKSAAGPLKDLEVFRYWFLACITADAPQIGPNKLVGKTFPTLEEYKKMWQVQKTSYVPSLNTTHRQSFVKNVAEQRGLPHIVVLSPVTYSYMQNNSRDTVVKGELDMIVYDATNEKVLLMVADSHDDRRPRTAFLNAQEERYRFAAVIRAAIVNDNELHDFQCEGVLAEYFFDPDSGSEENYYTIMAPTKISQKVGTKINVPLKALQPFTTCPPRYFILGSNWGVSSGNSKNPHAMSFSHAKLNEEAISLQSHIPEGFIKKNVMPKLLSRKEGLELLENAKRQRIKEQQLQKYQQQQQQQLNSARPAGGAQSTSRLTRSVTNTPRPTSDLEAAAAAELQEEENGILPEEEDPLGPVVPEDVLHPVRDLLLSKRFLQPDFLQRRSKDPEVHQLPATKDGKIRTPLTVFNELIKSRFGEEPPKASPQTLAGRRGSTSNSGIAAQGRASPYTRAASLQSDRLTSRAQRRQ
Protein: Initiator protein NS1 (NS1) (EC 3.1.21.-) (EC 3.6.4.12) (NCVP1) (Non-capsid protein NS-1) (Non-structural protein NS1) (P03134)
Organism: Murine minute virus (strain MVM prototype) (MVM) (Murine minute virus (strain MVM(p)))
Function: Multifunctional protein which displays endonuclease and helicase activities required for initiating and directing viral DNA replication. Also plays a role in viral packaging and transactivation of several promoters. Binds site-specifically to 2-3 approximate tandem copies of the tetranucleotide 5'TGGT3' within the origins of replication (Ori), unwinds this hairpin region and nicks one DNA strand thereby initiating the rolling circle replication (RCR). Cooperatively binds Ori with host PIF and probably other host factors, which activate the nickase function of NS1. Becomes covalently attached to the 5' end of the nick and provides a 3'OH for priming DNA synthesis. The helicase activity unwinds DNA in a 3'-5' direction on the longer strand. Participates in the transcriptional regulation of several promoters including the viral p38 promoter that regulates the expression of VP1 and VP2 transcripts. Inhibits the host cell cycle during the G1/S transition, the S-phase, and the G2/M transition. These arrests may provide essential cellular factors for viral DNA replication. Promotes apoptosis in host cell.
Subcellular location: Host nucleus {ECO:0000250|UniProtKB:D0EZM8}.
Interaction partners:
Sequence:
MAGNAYSDEVLGATNWLKEKSNQEVFSFVFKNENVQLNGKDIGWNSYKKELQEDELKSLQRGAETTWDQSEDMEWETTVDEMTKKQVFIFDSLVKKCLFEVLNTKNIFPGDVNWFVQHEWGKDQGWHCHVLIGGKDFSQAQGKWWRRQLNVYWSRWLVTACNVQLTPAERIKLREIAEDNEWVTLLTYKHKQTKKDYTKCVLFGNMIAYYFLTKKKISTSPPRDGGYFLSSDSGWKTNFLKEGERHLVSKLYTDDMRPETVETTVTTAQETKRGRIQTKKEVSIKTTLKELVHKRVTSPEDWMMMQPDSYIEMMAQPGGENLLKNTLEICTLTLARTKTAFDLILEKAETSKLTNFSLPDTRTCRIFAFHGWNYVKVCHAICCVLNRQGGKRNTVLFHGPASTGKSIIAQAIAQAVGNVGCYNAANVNFPFNDCTNKNLIWVEEAGNFGQQVNQFKAICSGQTIRIDQKGKGSKQIEPTPVIMTTNENITVVRIGCEERPEHTQPIRDRMLNIHLTHTLPGDFGLVDKNEWPMICAWLVKNGYQSTMASYCAKWGKVPDWSENWAEPKVPTPINLLGSARSPFTTPKSTPLSQNYALTPLASDLEDLALEPWSTPNTPVAGTAETQNTGEAGSKACQDGQLSPTWSEIEEDLRACFGAEPLKKDFSEPLNLD
Protein: Baseplate central spike complex protein gp27 (Gene product 27) (gp27) (Hub protein 27) (P17172)
Organism: Enterobacteria phage T4 (Bacteriophage T4)
Function: Baseplate central spike complex-associated protein involved in the tail assembly.
Subcellular location: Virion {ECO:0000269|PubMed:12837775, ECO:0000269|PubMed:15342608, ECO:0000269|PubMed:2403438, ECO:0000269|PubMed:27193680}. Note=Present in 3 copies in the baseplate. {ECO:0000303|PubMed:21129200}.
Interaction partners:
Sequence:
MSMLQRPGYPNLSVKLFDSYDAWSNNRFVELAATITTLTMRDSLYGRNEGMLQFYDSKNIHTKMDGNEIIQISVANANDINNVKTRIYGCKHFSVSVDSKGDNIIAIELGTIHSIENLKFGRPFFPDAGESIKEMLGVIYQDRTLLTPAINAINAYVPDIPWTSTFENYLSYVREVALAVGSDKFVFVWQDIMGVNMMDYDMMINQEPYPMIVGEPSLIGQFIQELKYPLAYDFVWLTKSNPHKRDPMKNATIYAHSFLDSSIPMITTGKGENSIVVSRSGAYSEMTYRNGYEEAIRLQTMAQYDGYAKCSTIGNFNLTPGVKIIFNDSKNQFKTEFYVDEVIHELSNNNSVTHLYMFTNATKLETIDPVKVKNEFKSDTTTEESSSSNKQ
Protein: Adenosine 3'-phospho 5'-phosphosulfate transporter 1 (PAPS transporter 1) (Protein slalom) (Q9VEI3)
Organism: Drosophila melanogaster (Fruit fly)
Function: Mediates the transport of adenosine 3'-phospho 5'-phosphosulfate (PAPS), from cytosol into Golgi. PAPS is a universal sulfuryl donor for sulfation events that take place in the Golgi. Required for the dorsoventral patterning, suggesting that it mediates the transport of the sulfate donor required for the sulfotransferase activity of pip (pipe).
Subcellular location: Golgi apparatus membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}.
Interaction partners:
- UDP-sugar transporter UST74c
- Endoplasmic reticulum GDP-fucose transporter
- Exostosin-2
- Large ribosomal subunit protein eL15
Sequence:
MYAYNKMGRVPELVICSFIVVTLLVIHFFSDLLRASLGGYYNQDVTLSQLVESQNSDYAWFLKLLVNCFGYSCVFVPGFLIYKYVGRINYLERGNKTFLHKAINMCITGNSGYDQLDAGTSTADKDRPAASTAPKRTSSQEAVQLLWCFGGLMISYLTWGVLQEKIMTQNYLNFTGESAKFKDSQFLVFSNRLLAFLVALAYLQWQPSPVRHRAPLYKYSYASFSNIMSAWFQYEALKFVNFPTQVLAKSCKIIPVMLMGKIMSKAKYESYEYVTALLISLGMIFFMSGSSDSSKASGVTTLTGIFLLSMYMVFDSFTANWQGSLFKSYGMTPLQMMCGVNLFSSIFTGASLSMQGGFMDSLAFATEHPKFVFDMVVLSVCSAVGQLFIYHTIDVFGPVVFTIIMTLRQAVAIMLSCFIYQHSISLLGIFGVLIVFVAIFLRVYCTQRLRAIRKRAEANKPKMAV
Protein: Tegument protein UL43 (Q6SW89)
Organism: Human cytomegalovirus (strain Merlin) (HHV-5) (Human herpesvirus 5)
Subcellular location: Virion tegument {ECO:0000250}.
Interaction partners:
Sequence:
MEKTPAETTAVSAGNVPRDSIPCITNVSADTRGRTRPSRPATVPQRRPARIGHFRRRSASLSFLDWPDDSVTEGVRTTSASVAASAARFDEIRRRRQSINDEMKERTLEDALAVELVNETFRCSVTSDARKDLQKLVRRVSGTVLRLSWPNGWFFTYCDLLRVGYFGHLNIKGLEKTFLCCDKFLLPVGTVSRCEAIGRPPLPVLIGEGGRVYVYSPVVESLYLVSRSGFRGFVQEGLRNYAPLREELGYVRFETGGDVGREFMLARDLLALWRLCMKREGSIFSWRDGNEALTTVVLNGSQTYEDPAHGNWLKETCSLNVLQVFVVRAVPVESQQRLDISILVNESGAVFGVHPDTRQAHFLARGLLGFFRVGFLRFCNNYCFARDCFTHPESVAPAYRATGCPRELFCRRLRKKKGLFARR
Protein: Transcriptional activator protein anr (P23926)
Organism: Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Function: Transcriptional activator of anaerobic gene expression.
Interaction partners:
- Oxygen-independent coproporphyrinogen III oxidase
- Two-component response regulator NarL
- RNA polymerase sigma factor RpoS
- Arginine deiminase
- UspA domain-containing protein
- Nitrite reductase
- Sensor protein
- Adenine phosphoribosyltransferase
- Transcriptional activator protein LasR
- Denitrification regulatory protein NirQ
Sequence:
MAETIKVRALPQAHCKDCSLAPLCLPLSLTVEDMDSLDEIVKRGRPLKKGEFLFRQGDPFGSVFAVRSGALKTFSITDAGEEQITGFHLPSELVGLSGMDTETYPVSAQALETTSVCEIPFERLDELSEQLPQLRRQLMRLMSREIRDDQQMMLLLSKKTADERIATFLVNLSARFRARGFSAQQFRLAMSRNEIGNYLGLAVETVSRVFTRFQQNGLISAEGKEVHILDSIELCALAGGQLEG
Protein: Cation channel sperm-associated protein 2 (CatSper2) (Q96P56)
Organism: Homo sapiens (Human)
Function: Voltage-gated calcium channel that plays a central role in calcium-dependent physiological responses essential for successful fertilization, such as sperm hyperactivation, acrosome reaction and chemotaxis towards the oocyte.
Subcellular location: Cell projection, cilium, flagellum membrane {ECO:0000250|UniProtKB:A2ARP9}; Multi-pass membrane protein {ECO:0000250|UniProtKB:A2ARP9}.
Interaction partners:
- Stereocilin
- Cation channel sperm-associated auxiliary subunit delta
- Cation channel sperm-associated protein 3
- Cation channel sperm-associated protein 1
- Cation channel sperm-associated auxiliary subunit epsilon
- Cation channel sperm-associated protein 4
- Cation channel sperm-associated auxiliary subunit beta
- EF-hand calcium-binding domain-containing protein 9
- Creatine kinase U-type, mitochondrial
- Cation channel sperm-associated auxiliary subunit zeta
Sequence:
MAAYQQEEQMQLPRADAIRSRLIDTFSLIEHLQGLSQAVPRHTIRELLDPSRQKKLVLGDQHQLVRFSIKPQRIEQISHAQRLLSRLHVRCSQRPPLSLWAGWVLECPLFKNFIIFLVFLNTIILMVEIELLESTNTKLWPLKLTLEVAAWFILLIFILEILLKWLSNFSVFWKSAWNVFDFVVTMLSLLPEVVVLVGVTGQSVWLQLLRICRVLRSLKLLAQFRQIQIIILVLVRALKSMTFLLMLLLIFFYIFAVTGVYVFSEYTRSPRQDLEYHVFFSDLPNSLVTVFILFTLDHWYALLQDVWKVPEVSRIFSSIYFILWLLLGSIIFRSIIVAMMVTNFQNIRKELNEEMARREVQLKADMFKRQIIQRRKNMSHEALTSSHSKIEDSSRGASQQRESLDLSEVSEVESNYGATEEDLITSASKTEETLSKKREYQSSSCVSSTSSSYSSSSESRFSESIGRLDWETLVHENLPGLMEMDQDDRVWPRDSLFRYFELLEKLQYNLEERKKLQEFAVQALMNLEDK
Protein: Aconitate hydratase (Aconitase) (EC 4.2.1.3) (B0RSR5)
Organism: Xanthomonas campestris pv. campestris (strain B100)
Interaction partners:
Sequence:
MSDSFSTRTSLEVNGQRYDYYSLPKLGERFDVARLPYSMKILLENLLRHEDGGVTVGKDHIEAVAKWDPAAEPDIEIAFMPARVVLQDFTGVPCVVDLAAMRDAVVKLGGNADQINPQIPSELVIDHSVQVDVFGKPEALDLNGKIEFQRNQERYGFLRWGQKAFDNFKVVPPNTGIVHQVNLENLARVVMSADKDGTQIAYPDTVFGTDSHTTMINGIGVLGWGVGGIEAEAAMLGQPSSMLIPQVVGFKLTGKLPEGATATDLVLTVTQMLRKHGVVGKFVEFYGEGLQHLPLADRATIGNMAPEYGATCGIFPVDNESLTYLRLSGRSEEQIALVEAYAKAQGLWHDADTPHAQYSATLELDMGDVKPSLAGPKRPQDRVLLEDMQSNYRESLKPFAEARSKRLADTKQEDRLKNEGGGGTAVGAKASQAESAGDSGAGWQLRDGSVVIAAITSCTNTSNPAVMLGAGLLARNAAAKGLKAQPWVKTSLGPGSRVVTDYLTKAGVLADLEQLGFYVVGYGCTTCIGNSGPLPEDVSAAIAKDDLVVTSVLSGNRNFEGRVHPEVKMNYLASPPLVVAYAIAGTTDIDLTRDPLGTGSDGQPVYLRDIWPSNKEIGDTIAATVGPEMFKQNYADVFKGDTRWNTIASPDGALYEWDAGSTYIKNPPYFEGMTMQVGHVDDVHGARIMGLFGDSITTDHISPAGNIKKDSPAGRFLQERGVQPADFNSYGSRRGNDDVMVRGTFANIRIKNLMFGGEEGGNTLYFGKDGATPEKLAIYDAAMKYKADGVPLVVLAGKEYGTGSSRDWAAKGTNLLGVKAVVAESFERIHRSNLVGMGVLPLQFLEGENAQTLGLDGSEVLDITGLQDGASRRATIDAKKSDGSVKQFQVKVLLLTPKEVEYFKHGGLLQYVLRQLAARKAA
Protein: Snail family transcriptional repressor 1 (A0A8J8YBT6)
Organism: Rattus norvegicus (Rat)
Interaction partners:
Sequence:
MPRSFLVRKPSDPRRKPNYSELQDACVEFTFQQPYDQAHLLAAIPPPEVLNPAASLPTLIWDSLLVPQVQPVAWATLPLRESPRAAELTSLSDEDSGKSSQPPSPPSPAPSSFSSTSASSLEAEAFIAFPGLGQLPKQLARLSVAKDPQSRKAFNCKYCNKEYLSLGALKMHIRSHTLPCVCTTCGKAFSRPWLLQGHVRTHTEAFLLLPLQPCLCRPLQPTCPPPDPLGCEEIPVSGLRPNLLPNVLAPQTPRVWLLRRPSLTLLPPHPHWHLPGALELLTARIPSSLSPGTCGVHVWPWFLLGSLGGLCCRWLMEGRVPLYPPRASCPSVFMRCSLWTQLLRAIELKPTHWLGSLNPTQGTPLPYLPQGPFQATFLEVQQTMQ
Protein: Spermidine synthase 2 (SPDSY 2) (EC 2.5.1.16) (Putrescine aminopropyltransferase 2) (O48661)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- S-adenosylmethionine decarboxylase proenzyme 1
- S-adenosylmethionine decarboxylase proenzyme 4
- S-adenosylmethionine decarboxylase proenzyme 2
- S-adenosylmethionine decarboxylase proenzyme 3
- N-carbamoylputrescine amidase
- Probable polyamine oxidase 4
- Polyamine oxidase 3
- Polyamine oxidase 1
- Polyamine oxidase 2
- Probable polyamine oxidase 5
Sequence:
MSSTQEASVTDLPVKRPREAEEDNNGGAMETENGGGEIKEPSCMSSIIPGWFSEISPMWPGEAHSLKVEKILFQGKSDYQDVIVFQSATYGKVLVLDGVIQLTERDECAYQEMITHLPLCSISNPKKVLVIGGGDGGVLREVARHSSVEQIDICEIDKMVVDVAKQYFPNVAVGYEDPRVNLIIGDGVAFLKNAAEGTYDAVIVDSSDPIGPAKELFEKPFFESVNRALRPGGVVCTQAESLWLHMDIIEDIVSNCRDIFKGSVNYAWTSVPTYPSGVIGFMLCSSEGPQVDFKKPVSLIDTDESSIKSHCPLKYYNAEIHSAAFCLPSFAKKVIDSKAN
Protein: Myeloproliferative leukemia virus oncogene, like (Thrombopoietin receptor c-mpl) (Thrombopoietin receptor precursor) (Q6EIY6)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004251}; Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004251}.
Interaction partners:
Sequence:
MDPVFIWWILHFCLYKQVNSVPRQPKPELLAMDEDPKCFTRNLEDFTCFWDAPVEKSYDFLYIIEGLMEEKRCDVKQQTFEEKILNICTFPPSDVYLYVETHIRVIDKDTNTTIYSRAVSVEDQLLLYPPSNISLHPTEEVGQMLVKWKRTSNEHEIRYSFKNTSTVKSVSENDYKLVSLVPGENCTVQMRVKPSGDFKRFWSDWSNPVTAMVPQTAGDIEFRCHTSDLIQIICKWRGDLYKDNTYSFYYKQLNRSSWSSWKLCPNCNNSIHQCVLYGQKSNVFKFYLNTGLQPFSRTFYAETFYMNSKVQTRPPEGLKVQIGEERLCLTWDSPFLIISKHLMYQIRYQHHEENQWKGFKASGSKTSTCLDVHRGGRYTIQVRAQPNGSVYSGNWSDWSKPVTTNLPLSKEWIIFVCIPVALIIFATAVISFFSRYFRKVKRSLWPPVPNLNKVLENILTDISGSHWEPTFNIKQCDDDTATSVVEVLTEGESVVKTCKNTCPLLSEHSEKHGEHFREDLEMAQDYVILNNNIISCLTGNDYVYKDVASTHLANEKQHSCSSTSYNSLPERTTDILNQSYLLLAEQSDLETYQTTCGQYTNLEITAVSCVAIGE
Protein: G protein alpha i subunit (Guanine nucleotide-binding protein G(i) subunit alpha 65A) (P20353)
Organism: Drosophila melanogaster (Fruit fly)
Function: Guanine nucleotide-binding proteins (G proteins) are involved as modulators or transducers in various transmembrane signaling systems. Plays a role in glial cell differentiation during embryogenesis; loco, Galphao and the G-protein coupled receptor, moody, are required in the surface glia to achieve effective insulation of the nerve cord.
Subcellular location: Cell membrane {ECO:0000269|PubMed:15937221}. Apical cell membrane {ECO:0000269|PubMed:15937221}. Note=Colocalizes with loco and raps/pins at the apical cortex throughout mitosis in neuroblasts.
Interaction partners:
- LD33695p
- G protein beta subunit 5
- Inscuteable
- Regulator of G-protein signaling loco
- Mushroom body defect, isoform H
- Guanine nucleotide-binding protein subunit beta-1
- Chaperone Ric-8
- Double hit, isoform B
- LP21163p
- Atypical protein kinase C
Sequence:
MGCAVSTARDKEAIERSKNIDRALRAEGERAASEVKLLLLGAGESGKSTIVKQMKIIHDTGYSQEECEEYRRVVFSNTVQSLMVIIRAMGRLKIEFADPSRTDIARQFFTHASAADEGILLPEIVLLMKKLWADGGVQQSFARSREYQLNDSAGYYLNSLDRIAQPNYIPTQQDVLRTRVKTTGIIETHFSCKQLHFKLFDVGGQRSERKKWIHCFEGVTAIIFCVALSGYDLVLAEDEEMNRMIESLKLFDSICNSKWFVETSIILFLNKKDLFEEKIKRSPLTICFPEYTGTNTFEEAANYIRMKFENLNKRKDQKEIYTHLTCATDTNNVKFVFDAVTDVIIKNNLKQIGLF