wanglab/gogpt-training-data huggingface dataset:
Protein: DELTA-actitoxin-Afr1a (DELTA-AITX-Afr1a) (Alpha-helical pore-forming toxin) (PFT) (Cytolysin) (Fragaceatoxin C) (fraC) (B9W5G6)
Organism: Actinia fragacea (Strawberry anemone)
Function: Pore-forming toxin (PFT) that consists of a crown-shaped octamer or nonamer that forms cation-selective hydrophilic pores of about 1.5 nm (inside) and 13 nm (outside). It causes cardiac stimulation and cytolysis (EC(50)=1.6 nM on erythrocytes). Interestingly, the Phe-16 is crucial for hemolysis. Pore formation is a multi-step process that involves specific recognition of membrane sphingomyelin (but neither cholesterol nor phosphatidylcholine) using aromatic rich region and adjacent phosphocholine (POC) binding site, firm binding to the membrane (mainly driven by hydrophobic interactions) accompanied by the transfer of the N-terminal region to the lipid-water interface and finally pore formation after oligomerization of monomers. It is probable that a dimeric form is an assembly intermediate before the complete oligomerization. The formation of stable pores occurs only in vesicles composed of DOPC/SM (there is no oligomerization when the PFT is treated with vesicles of DOPC or SM alone). The transmembrane pore displays 8 lateral perforations, one at each subunit-subunit interface, partially occupied by the acyl-chain region of a bridging lipid. Each pore contains 24 lipid molecules, firmly bound to each subunit, that is, 3 lipids (L1, L2, L3, L4 and/or L5) are associated to each subunit. Lipid L1 bridges 2 subunits, whereas lipids L2 and L3 bind to sites at single subunit.
Subcellular location: Secreted {ECO:0000269|PubMed:19563820}. Nematocyst {ECO:0000250|UniProtKB:P07845}. Target cell membrane {ECO:0000269|PubMed:19563820, ECO:0000269|PubMed:21300287, ECO:0000269|PubMed:25716479}. Note=Forms an alpha-helical membrane channel in the prey. {ECO:0000269|PubMed:19563820, ECO:0000269|PubMed:21300287, ECO:0000269|PubMed:25716479}.
Interaction partners:
Sequence:
SADVAGAVIDGAGLGFDVLKTVLEALGNVKRKIAVGIDNESGKTWTAMNTYFRSGTSDIVLPHKVAHGKALLYNGQKNRGPVATGVVGVIAYSMSDGNTLAVLFSVPYDYNWYSNWWNVRVYKGQKRADQRMYEELYYHRSPFRGDNGWHSRGLGYGLKSRGFMNSSGHAILEIHVTKA
Protein: non-specific serine/threonine protein kinase (EC 2.7.11.1) (Q9SD64)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004370}.
Interaction partners:
- Probable protein S-acyltransferase 20
- C2H2 and C2HC zinc fingers superfamily protein
- Putative terpenoid synthase 16
Sequence:
MRLFLLLAFNALMQLEAYGFTDESDRQALLEIKSQVSESKRDALSAWNNSFPLCSWKWVRCGRKHKRVTRLDLGGLQLGGVISPSIGNLSFLIYLDLSNNSFGGTIPQEMGNLFRLKYLAVGFNYLEGEIPASLSNCSRLLYLDLFSNNLGDGVPSELGSLRKLLYLYLGLNDLKGKFPVFIRNLTSLIVLNLGYNHLEGEIPDDIAMLSQMVSLTLTMNNFSGVFPPAFYNLSSLENLYLLGNGFSGNLKPDFGNLLPNIHELSLHGNFLTGAIPTTLANISTLEMFGIGKNRMTGSISPNFGKLENLHYLELANNSLGSYSFGDLAFLDALTNCSHLHGLSVSYNRLGGALPTSIVNMSTELTVLNLKGNLIYGSIPHDIGNLIGLQSLLLADNLLTGPLPTSLGNLVGLGELILFSNRFSGEIPSFIGNLTQLVKLYLSNNSFEGIVPPSLGDCSHMLDLQIGYNKLNGTIPKEIMQIPTLVHLNMESNSLSGSLPNDIGRLQNLVELLLGNNNLSGHLPQTLGKCLSMEVIYLQENHFDGTIPDIKGLMGVKNVDLSNNNLSGSISEYFENFSKLEYLNLSDNNFEGRVPTEGIFQNATLVSVFGNKNLCGSIKELKLKPCIAQAPPVETRHPSLLKKVAIGVSVGIALLLLLFIVSLSWFKKRKNNQKINNSAPFTLEIFHEKLSYGDLRNATDGFSSSNIVGSGSFGTVFKALLQTENKIVAVKVLNMQRRGAMKSFMAECESLKDIRHRNLVKLLTACASIDFQGNEFRALIYEFMPNGSLDKWLHPEEVEEIHRPSRTLTLLERLNIAIDVASVLDYLHVHCHEPIAHCDLKPSNILLDDDLTAHVSDFGLARLLLKFDQESFFNQLSSAGVRGTIGYAAPEYGMGGQPSIHGDVYSFGVLVLEMFTGKRPTNELFGGNFTLNSYTKAALPERVLDIADKSILHSGLRVGFPVLECLKGILDVGLRCCEESPLNRLATSEAAKELISIRERFFKTRRTARR
Protein: Cyclin-dependent kinase 14 (EC 2.7.11.22) (Cell division protein kinase 14) (Serine/threonine-protein kinase PFTAIRE-1) (hPFTAIRE1) (O94921)
Organism: Homo sapiens (Human)
Function: Serine/threonine-protein kinase involved in the control of the eukaryotic cell cycle, whose activity is controlled by an associated cyclin. Acts as a cell-cycle regulator of Wnt signaling pathway during G2/M phase by mediating the phosphorylation of LRP6 at 'Ser-1490', leading to the activation of the Wnt signaling pathway. Acts as a regulator of cell cycle progression and cell proliferation via its interaction with CCDN3. Phosphorylates RB1 in vitro, however the relevance of such result remains to be confirmed in vivo. May also play a role in meiosis, neuron differentiation and may indirectly act as a negative regulator of insulin-responsive glucose transport.
Subcellular location: Cell membrane; Peripheral membrane protein. Cytoplasm. Nucleus. Note=Recruited to the cell membrane by CCNY.
Interaction partners:
- Cyclin-Y
- G1/S-specific cyclin-D3
- Cyclin-dependent kinase inhibitor 1
- Cyclin-dependent kinase 17
- 14-3-3 protein eta
Sequence:
MCDLIEPQPAEKIGKMKKLRRTLSESFSRIALKKDDTTFDEICVTKMSTRNCQGMDSVIKPLDTIPEDKKVRVQRTQSTFDPFEKPANQVKRVHSENNACINFKTSSTGKESPKVRRHSSPSSPTSPKFGKADSYEKLEKLGEGSYATVYKGKSKVNGKLVALKVIRLQEEEGTPFTAIREASLLKGLKHANIVLLHDIIHTKETLTLVFEYVHTDLCQYMDKHPGGLHPDNVKLFLFQLLRGLSYIHQRYILHRDLKPQNLLISDTGELKLADFGLARAKSVPSHTYSNEVVTLWYRPPDVLLGSTEYSTCLDMWGVGCIFVEMIQGVAAFPGMKDIQDQLERIFLVLGTPNEDTWPGVHSLPHFKPERFTLYSSKNLRQAWNKLSYVNHAEDLASKLLQCSPKNRLSAQAALSHEYFSDLPPRLWELTDMSSIFTVPNVRLQPEAGESMRAFGKNNSYGKSLSNSKH
Protein: Magnetosome protein MamA (MM24.3) (Q93DY9)
Organism: Magnetospirillum gryphiswaldense (strain DSM 6361 / JCM 21280 / NBRC 15271 / MSR-1)
Function: Probably forms a large homooligomer on which other magnetosome subunits assemble. Required for formation of functional magnetosomes from pre-existing vesicles.
Subcellular location: Magnetosome membrane {ECO:0000269|PubMed:11571158, ECO:0000269|PubMed:14766587}; Peripheral membrane protein {ECO:0000305|PubMed:14766587}. Note=Purified magnetosomes remain attached to each other (PubMed:11571158). Probably a peripheral membrane protein, it is solubilized by Tween 20 (PubMed:14766587). Forms oligomers that cover the surface of the magnetosome (By similarity). {ECO:0000250|UniProtKB:Q2W8Q0, ECO:0000269|PubMed:11571158, ECO:0000269|PubMed:14766587}.
Interaction partners:
- Probable membrane transporter protein MamO
- Multi-heme protein MamP
- TPR repeat-containing protein
- Magnetosome formation protease MamE
Sequence:
MSSKPSNMLDEVTLYTHYGLSVAKKLGANMVDAFRSAFSVNDDIRQVYYRDKGISHAKAGRYSEAVVMLEQVYDADAFDVEVALHLGIAYVKTGAVDRGTELLERSIADAPDNIKVATVLGLTYVQVQKYDLAVPLLVKVAEANPVNFNVRFRLGVALDNLGRFDEAIDSFKIALGLRPNEGKVHRAIAYSYEQMGSHEEALPHFKKANELDERSAV
Protein: Epididymis secretory sperm binding protein (A0A024RB53)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MSKSESPKEPEQLRKLFIGGLSFETTDESLRSHFEQWGTLTDCVVMRDPNTKRSRGFGFVTYATVEEVDAAMNARPHKVDGRVVEPKRAVSREDSQRPGAHLTVKKIFVGGIKEDTEEHHLRDYFEQYGKIEVIEIMTDRGSGKKRGFAFVTFDDHDSVDKIVIQKYHTVNGHNCEVRKALSKQEMASASSSQRGRSGSGNFGGGRGGGFGGNDNFGRGGNFSGRGGFGGSRGGGGYGGSGDGYNGFGNDGSNFGGGGSYNDFGNYNNQSSNFGPMKGGNFGGRSSGPYGGGGQYFAKPRNQGGYGGSSSSSSYGSGRRF
Protein: Tyrosine-protein kinase fyna (EC 2.7.10.2) (Proto-oncogene c-Fyna) (Q6EWH2)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Function: Tyrosine-protein kinase implicated in the control of cell growth. Plays a role in the regulation of intracellular calcium levels. Required in brain development and mature brain function with important roles in the regulation of axon growth, axon guidance, and neurite extension. Role in cntn1-mediated signaling (By similarity). Required for convergent extension cell movements during gastrulation, acting with yes via rhoa. May be required for epiboly to occur, possibly through its effects in calcium signaling.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:10993948}. Nucleus {ECO:0000269|PubMed:10993948}. Note=Transiently expressed in the nucleus at mid-blastula stage (3.3 hpf) in a large subset of cells. Nuclear localization is not observed from late blastula stage onward.
Interaction partners:
- Caveolin
- Catenin beta-1
- Caveolin
- Caveolin
- Caveolin
- Caveolin
- Tyrosine-protein kinase yes
- SHC-transforming protein 1
- SHC adaptor protein 3.
- Catenin
Sequence:
MGCVQCKDKEATKLTDERETSVSQHAGYRYGSDPTPQHYPSFGVTAIPNYNNFHAPVSQGVTVFGGVNSSSHSGTLRSRGGTGVTLFVALYDYEARSEDDLSFRKGEKFQILNSTEGDWWEARSLTTGGTGYIPSNYVAPVDSIQAEDWYFGKLGRKDAERQLLSNGNPRGTFLIRESETTKGAYSLSIQDWDETKGDHVKHYKIRKLDNGGYYITTRAQFETLQQLVHHYSARAAGLCCRLIVPCHKGMPRLADLSVKTKDVWEIPRESLQLIKRLGNGQFGEVWMGTWNGNTKVAVKTLKPGTMSPESFLEEAQIMKKLRHDKLVQLYAVVSEEPIYIVTEYMSKGSLLDFLKDGEGRGLKLPNLVDMAAQVAAGMAYIERMNYIHRDLRSANILVGDSLVCKIADFGLARLIEDNEYTARQGAKFPIKWTAPEAALYGRFTIKSDVWSFGILLTELVTKGRVPYPGMNNREVLEQVERGYRMPCPQDCPSSLHELMLQCWKRDPEERPTFEYLQAFLEDYFTATEPQYQPGDNL
Protein: RE19601p (Q8SXJ5)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MNEDHLEDTHLCIRCNATILGLSKYIDHRKRNCLITGKQNASPKTDGRTRISADTHVSATLISSSNLDHSYDGFHFTEPEAPSSYLRKTAASHGGKTSKSLTEAYDLPYELGADLFFSSLQLQSVATGGKIGSVPRQERSKDESWSAPAGDPLLKAVRENDETVFKPLHFDHEYPEASDEEDDEDEHEEFDAEEDEEEYDARRHSPPIVPASHTGGKWKPEQRPQLRHPHIERLSPSWDEPPEENYTHPPADHTKGKWVPGSKQLEYRENLDLTKLDQPGASYWCNICCRRLKSRLYYNQHLRSGYHIKRAEAECELEQATLGRELTLSKDFSIKDDADKNEPKPPKRQRRANLLRCDLCRHTMARHLIGKHLISHYHFRRLQQQSRIRRQACLQEILKHMGSIVRQSPFQCMPCRFYANTEETFLYHWKSHEHLELTKRLGGTFWCSFCQFNSNTNNSMLLHLLDSSHKEVLLALNRSVPICIAQRIRIQCSRCGMEFLYNIQLRQHSITEHPGLALTGTAADEYQSRFRCNLCGSSQKSRLALQRHKKHKHHLARYFCAICRLEFDNSLDARRHRSLVIHKQKARPQTSIPQPENEIEHMLREVLEETVPSPPAKRSADVNAKCSNSRKTIESSQRLAQHQAEVHSSDNHLCLSCGISFESAQALGRHTRSCQPLASTSTPADLSQAQKKSMYSCDQCRFQSQYESDLVYHRIFHTRSGTIGKNEVLQCPLCPKNFKKHSLRAHLRNHTNEKIFECTECLQKFARRHNLKNHVITKHAKVGDKEKKKYAAKDVEQSKPKYQCGTCGKLLAKKYSLKLHEISHSKAVERNYLCHFADCSYAGRTPESLKTHLVSHSQENHKCARINCSYVGKSELHLKRHLKSAHSTEKNGEEWFSCDQCDFRARIKGHLRRHSLRHSGQKPHQCPHCDFQCSTIDNLRKHIIKTGKHPGMFIYHCAKCSDEEAGEIFKSNSYKEYQHHLKTHKAG
Protein: Malectin (Q14165)
Organism: Homo sapiens (Human)
Function: Carbohydrate-binding protein with a strong ligand preference for Glc2-N-glycan. May play a role in the early steps of protein N-glycosylation (By similarity).
Subcellular location: Endoplasmic reticulum membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}.
Interaction partners:
- Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit 1
- Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit 2
- Dolichyl-diphosphooligosaccharide--protein glycosyltransferase 48 kDa subunit
- Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit STT3B
- Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit TMEM258
- Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit DAD1
- Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit 4
- Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit MAGT1
- Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit STT3A
- Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit KCP2
Sequence:
MLGAWAVEGTAVALLRLLLLLLPPAIRGPGLGVAGVAGAAGAGLPESVIWAVNAGGEAHVDVHGIHFRKDPLEGRVGRASDYGMKLPILRSNPEDQILYQTERYNEETFGYEVPIKEEGDYVLVLKFAEVYFAQSQQKVFDVRLNGHVVVKDLDIFDRVGHSTAHDEIIPMSIRKGKLSVQGEVSTFTGKLYIEFVKGYYDNPKVCALYIMAGTVDDVPKLQPHPGLEKKEEEEEEEEYDEGSNLKKQTNKNRVQSGPRTPNPYASDNSSLMFPILVAFGVFIPTLFCLCRL
Protein: Receptor-like cytoplasmic kinase 1 (EC 2.7.11.1) (Q9LUT0)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Receptor-like cytoplasmic kinase (RLCK) that triggers abscisic acid (ABA) signaling by phosphorylating and activating ABA receptors (e.g. PYL8/RCAR3 and PYR1/RCAR11), which in turn repress ABI1, a negative regulator of ABA responses. Promotes drought tolerance.
Subcellular location: Cytoplasm, cytosol {ECO:0000269|PubMed:29928509}.
Interaction partners:
- AT3g47210/F13I12_260
- Plant intracellular Ras-group-related LRR protein 5
- Abscisic acid receptor PYL8
- Abscisic acid receptor PYR1
Sequence:
MGCFGCCGGGEDFRRVSETGPKPVHNTGGYNGGHHQRADPPKNLPVIQMQPISVAAIPADELRDITDNYGSKSLIGEGSYGRVFYGILKSGKAAAIKKLDSSKQPDQEFLAQVSMVSRLRQENVVALLGYCVDGPLRVLAYEYAPNGSLHDILHGRKGVKGAQPGPVLSWHQRVKIAVGAARGLEYLHEKANPHVIHRDIKSSNVLLFDDDVAKIADFDLSNQAPDMAARLHSTRVLGTFGYHAPEYAMTGTLSTKSDVYSFGVVLLELLTGRKPVDHTLPRGQQSVVTWATPKLSEDKVKQCVDARLNGEYPPKAVAKLAAVAALCVQYEADFRPNMSIVVKALQPLLNPPRSAPQTPHRNPY
Protein: Nuclear pore complex subunit Nup133, putative (AFU_orthologue AFUA_5G14040) (Q5B9U1)
Organism: Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Interaction partners:
- Ubiquitin-like domain-containing protein
- Polynucleotide 5'-hydroxyl-kinase grc3
- Importin beta-3 subunit, putative
- Importin subunit alpha
- Ulp1 protease family protein
- Ran specific GTPase activating protein An-RanGAP
- Pre-rRNA-processing protein IPI3
- Pre-rRNA-processing protein ipi1
- Importin-95
- Nuclear pore complex protein An-Nup133
Sequence:
MDFVTNGQPSPKDTVMNDASPYDALHHQRTNRQFTSEDLADPNYVPNPVPFGAKKITPDETHRPFYHIHSRKPSQRPDMVLKHQKTAYSTTRRRYDSLSPPQFQFTRGRTGSQHEQAPLVLPRVNEIQPYRLTATTASRLNATTYSSSLMNPMRSSGHDSILGAGLRGRDRPLSLFGSEASRQAAMIRPRKRDREGNILDTTGSIFVRNNNANDGRNNDQQHIASADADSPVLKYCRGGTESSFSAAVDNIKKVNGDPVQPLAQRPSFHWQRALPSKTTDPATPGKQTGSSTATGRIPGCWPSASKHGSMPLLPEPQQTAQTQHQTESPVTSQEICGQVDLPSNANPEPATVNPDQAILDETPSWTQHYSGVYGTLRIAYSFQCGMVQTVANAFHVALAAASTITHQTQQALGTVTQRVMAMYRQRRFDRARSRARASPAAPARQPPTTIASPARVNVATLPPGQQERVRINQWRRRRGFPVNEELPFPNMTTPMGALFYDPQIITTSSPSVQRSLDLVVDNASGATLHRHPAQRRTSVNDRDDKNRPQAPKAGILKKNSLVPTMSPATRRRLLPGYITPRDRRLGLQHRVRFRSPIVQPSPLRLRQWANSSAESGPGLDELLRTQLNGADAPSTVASDQRTGPDEQLYAQLAASLEPYVDPWAQPRDFTKGTPRSAVKLVKPKIEPVPDGRSESIYAKEYEEMQKMKKLEYGPVGRQVPEGVAVRPLPDNWKARLKDLKKKAHWVEVATTPSGESLTRDDIDTCLTPMAWLNDEVINSYLGLIVNHMRHENGNAGRHDKPRYHAFNTFFFSNLRDKGYDSVKRWAKRAKIGGKDLLDVDTVFIPVHNKAHWTLIVVKPSARTIEHFDSLGSLSRRHVETVKGWLRGELGDLYDDDEWEVLPSESPQQDNGSDCGVFLLTTAKAVALNIEPLAYGARDTPLLRQKIVAELINGGFEGDFTPDGAL
Protein: DNA-directed RNA polymerase I subunit RPA43 (A43) (DNA-directed DNA-dependent RNA polymerase 36 kDa polypeptide) (P46669)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: DNA-dependent RNA polymerases catalyze the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. Component of RNA polymerase I (Pol I) which synthesizes ribosomal RNA precursors. Besides, RNA polymerase I has intrinsic RNA cleavage activity. Through its association with RRN3 is involved in recruitment of Pol I to rDNA promoters. In vitro, the A13-A43 subcomplex binds single-stranded RNA.
Subcellular location: Nucleus, nucleolus {ECO:0000269|PubMed:14562095}.
Interaction partners:
- DNA-directed RNA polymerases I, II, and III subunit RPABC2
- DNA-directed RNA polymerase I subunit RPA135
- DNA-directed RNA polymerases I and III subunit RPAC2
- DNA-directed RNA polymerase I subunit RPA49
- DNA-directed RNA polymerases I, II, and III subunit RPABC4
- DNA-directed RNA polymerases I and III subunit RPAC1
- DNA-directed RNA polymerases I, II, and III subunit RPABC1
- DNA-directed RNA polymerases I, II, and III subunit RPABC3
- DNA-directed RNA polymerase I subunit RPA34
- DNA-directed RNA polymerase I subunit RPA12
Sequence:
MSQVKRANENRETARFIKKHKKQVTNPIDEKNGTSNCIVRVPIALYVSLAPMYLENPLQGVMKQHLNPLVMKYNNKVGGVVLGYEGLKILDADPLSKEDTSEKLIKITPDTPFGFTWCHVNLYVWQPQVGDVLEGYIFIQSASHIGLLIHDAFNASIKKNNIPVDWTFVHNDVEEDADVINTDENNGNNNNEDNKDSNGGSNSLGKFSFGNRSLGHWVDSNGEPIDGKLRFTVRNVHTTGRVVSVDGTLISDADEEGNGYNSSRSQAESLPIVSNKKIVFDDEVSIENKESHKELDLPEVKEDNGSEIVYEENTSESNDGESSDSD
Protein: Transmembrane protein 115 homolog (Q12239)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: May play a role in retrograde transport of proteins from the Golgi to the endoplasmic reticulum.
Subcellular location: Golgi apparatus membrane {ECO:0000269|PubMed:14562095}; Multi-pass membrane protein {ECO:0000269|PubMed:14562095}.
Interaction partners:
Sequence:
MQYSSRFLELNIPDSFLNINKIPDATKFITVTYICLTATLFCIRRSLYNKLVLEDPNLDYNLITSPLLQMVPSQIWRYPTSLVLSNFIDTKAWKVVVNLLNLIIGGSFIERNWNSSKEMFKFIIVLGSLTNVLIIMLTLLVSFFSNKVRLDIPLDGNYTILIGFPIIYRQLLPETTIIHLKTPQFLAKNFRFKLLPIFVMFTMTVTQIIWFHHFAQLFSIWVTFFASWSYLRFFQKLAPLNCPSLPTTNSQGGQEILVGDASDTFQLIYFFPDLIKPILRPIFNFIYNVVVVKFKVIKPFHDIDIDIGNTIAESRGAKKIMTVEERRRQLALQVLEERMVNP
Protein: Polynucleotide kinase 3'-phosphatase (Q6AXV0)
Organism: Rattus norvegicus (Rat)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MSELGSRGRLWLQSPTGGPPPIFLPSDGQALVLGRGPLTQVMDRKCSRNQVELIADPETRTVAVKQLGVNPSTVGVQELKPGVSGSLSVGDVLYLVNGLYPLTLRWEEISTPGSPPDTPPGNPVDPEEGKDTEPQKKRMRKSSPGWESFKQLLVFTASGVKPRGKVAAFDLDGTLITTRSGKVFPTSPSDWRILYPEIPKKLQELAAEGYKLVILTNQMGIGRGKLPAEVFKAKVEAVLEKLGVPFQVLVATHAGLNRKPVSGMWDHLQEKGNEGIPISIGDSVFVGDAAGRPANWAPGKKKKDFSCADRLFALNVGLPFATPEEFFLKWPAARFELPAFDPRTISSAGPLYLPESSFLLSPNPEVVVAVGFPGAGKSTFIQKHLVSAGYVHVNRDTLGSWQRCVNSCQAALRQGKQVVIDNTNPDIQSRARYIQCAKDAGVPCRCFSFCATIEQARHNNRFREMTDPSHAPVSDMVMFSYRKQFEPPTLAEGFLEILQVPFRLQEHLDPALQRLYCQFSEG
Protein: ARP2/3 complex subunit, putative (Q38BE7)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000256|ARBA:ARBA00004245}.
Interaction partners:
- Arp2/3 complex 41 kDa subunit
- Arp2/3 complex 34 kDa subunit
- Actin-like protein 3, putative
- Actin-like protein 2, putative
- Actin-related protein 2/3 complex subunit 4
- Actin-related protein 2/3 complex subunit 5
- Actin, putative
- WASH1 WAHD domain-containing protein
Sequence:
MESQWNGYEESTLLGCGVYPLRRTSLDTPNGPSRPMSEVIDPIEGEGEPQDIVDEALYFLKTHLVRRAFPIRGAGDRVILYLTWYLHECIKSLVGLNRNEAQKAMLNRAVEGVVAPVDEGFVFSRFFSPGDDSEQDRWKSYATQLRVEAGSRLVEKIFLFPEEDGTGNKFWMAFAKRPFLLGG
Protein: Max-interacting protein 1 (Max interactor 1) (Class C basic helix-loop-helix protein 11) (bHLHc11) (P50539)
Organism: Homo sapiens (Human)
Function: Transcriptional repressor. MXI1 binds with MAX to form a sequence-specific DNA-binding protein complex which recognizes the core sequence 5'-CAC[GA]TG-3'. MXI1 thus antagonizes MYC transcriptional activity by competing for MAX.
Subcellular location: Nucleus.
Interaction partners:
- Protein max
- Cell division cycle protein 20 homolog
- Anaphase-promoting complex subunit 4
- Mitotic checkpoint serine/threonine-protein kinase BUB1 beta
- Cell division cycle protein 27 homolog
- Myc proto-oncogene protein
- Paired amphipathic helix protein Sin3a
- Paired amphipathic helix protein Sin3b
- Forkhead box protein O3
- Double-strand-break repair protein rad21 homolog
Sequence:
MERVKMINVQRLLEAAEFLERRERECEHGYASSFPSMPSPRLQHSKPPRRLSRAQKHSSGSSNTSTANRSTHNELEKNRRAHLRLCLERLKVLIPLGPDCTRHTTLGLLNKAKAHIKKLEEAERKSQHQLENLEREQRFLKWRLEQLQGPQEMERIRMDSIGSTISSDRSDSEREEIEVDVESTEFSHGEVDNISTTSISDIDDHSSLPSIGSDEGYSSASVKLSFTS
Protein: (+)-epi-alpha-bisabolol synthase (EC 4.2.3.138) (Terpene synthase 8) (LdTPS8) (J7LH11)
Organism: Phyla dulcis (Aztec sweet herb) (Lippia dulcis)
Function: Sesquiterpene synthase involved in the biosynthesis of (+)-epi-alpha-bisabolol, a precursor of the natural sweetner hernandulcin.
Interaction partners:
Sequence:
MNSTSRRSANYKPTIWNNEYLQSLNSIYGEKRFLEQAEKLKDEVRMLLEKTSDPLDHIELVDVLQRLAISYHFTEYIDRNLKNIYDILIDGRRWNHADNLHATTLSFRLLRQHGYQVSPEVFRNFMDETGNFKKNLCDDIKGLLSLYEASYLLTEGETIMDSAQAFATHHLKQKLEENMNKNLGDEIAHALELPLHWRVPKLDVRWSIDAYERRQDMNPLLLELAKLDFNIAQSMYQDELKELSRWYSKTHLPEKLAFARDRLVESYLWGLGLASEPHHKYCRMMVAQSTTLISIIDDIYDVYGTLDELQLFTHAVDRWDIKYLEQLPEYMQICFLALFNTVNERSYDFLLDKGFNVIPHSSYRWAELCKTYLIEANWYHSGYKPSLNEYLNQGLISVAGPHALSHTYLCMTDSLKEKHILDLRTNPPVIKWVSILVRLADDLGTSTDELKRGDNPKSIQCHMHDTGCNEEETRAYIKNLIGSTWKKINKDVLMNFEYSMDFRTAAMNGARVSQFMYQYDDDGHGVPEGKSKERVCSLIVEPIPLP
Protein: Arsenical pump membrane protein (Arsenic efflux pump protein) (P0AB93)
Organism: Escherichia coli (strain K12)
Function: Involved in arsenical resistance. Thought to form the channel of an arsenite pump (By similarity).
Subcellular location: Cell inner membrane; Multi-pass membrane protein.
Interaction partners:
- Arsenical resistance operon repressor
- Arsenate reductase
Sequence:
MLLAGAIFVLTIVLVIWQPKGLGIGWSATLGAVLALVTGVVHPGDIPVVWNIVWNATAAFIAVIIISLLLDESGFFEWAALHVSRWGNGRGRLLFTWIVLLGAAVAALFANDGAALILTPIVIAMLLALGFSKGTTLAFVMAAGFIADTASLPLIVSNLVNIVSADFFGLGFREYASVMVPVDIAAIVATLVMLHLYFRKDIPQNYDMALLKSPAEAIKDPATFKTGWVVLLLLLVGFFVLEPLGIPVSAIAAVGALILFVVAKRGHAINTGKVLRGAPWQIVIFSLGMYLVVYGLRNAGLTEYLSGVLNVLADNGLWAATLGTGFLTAFLSSIMNNMPTVLVGALSIDGSTASGVIKEAMVYANVIGCDLGPKITPIGSLATLLWLHVLSQKNMTISWGYYFRTGIIMTLPVLFVTLAALALRLSFTL
Protein: Dual specificity calcium/calmodulin-dependent 3',5'-cyclic nucleotide phosphodiesterase 1B (Cam-PDE 1B) (EC 3.1.4.17) (Q64395)
Organism: Cricetulus griseus (Chinese hamster) (Cricetulus barabensis griseus)
Function: Cyclic nucleotide phosphodiesterase with a dual specificity for the second messengers cAMP and cGMP, which are key regulators of many important physiological processes. Has a preference for cGMP as a substrate.
Subcellular location: Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q01064}.
Interaction partners:
Sequence:
MELSPRSPPEMLESDCPSPLELKSAPSKKMWIKLRSLLRYMVKQLENGEVNIEELKKNLEYTASLLEAVYIDETRQILDTEDELRELRSDAVPSEVRDWLASTFTQQTRAKGRRAEEKPKFRSIVHAVQAGIFVERMFRRTYTAVGPTYSTAVHNCLKNLDLWCFDVFSLNRAADDHALRTIVFELLTRHSLISRFKIPTVFLMSFLEALETGYGKYKNPYHNQIHAADVTQTVHCFLLRTGMVHCLSEIEVLAIIFAAAIHDYEHTGTTNSFHIQTKSECAILYNDRSVLENHHISSVFRMMQDDEMNIFINLTKDEFVELRALVIEMVLATDMSCHFQQVKSMKTALQQLERIDKSKALSLLLHAADISHPTKQWSVHSRWTKALMEEFFRQGDKEAELGLPFSPLCDRTSTLVAQSQIGFIDFIVEPTFSVLTDVAEKSVQPLADDDSKSKSQPSFQWRQPSLDVDVGDPNPDVISFRSTWTKYIQENKQKWKERAASGITNQMSIDELSPCEEEAPPSPAEDEHNQNGNLD
Protein: Glucose-6-phosphate 1-dehydrogenase (G6PD) (EC 1.1.1.49) (P11413)
Organism: Homo sapiens (Human)
Function: Catalyzes the rate-limiting step of the oxidative pentose-phosphate pathway, which represents a route for the dissimilation of carbohydrates besides glycolysis. The main function of this enzyme is to provide reducing power (NADPH) and pentose phosphates for fatty acid and nucleic acid synthesis.
Subcellular location: Cytoplasm, cytosol {ECO:0000269|PubMed:35122041, ECO:0000269|PubMed:743300}. Membrane; Peripheral membrane protein {ECO:0000269|PubMed:743300}.
Interaction partners:
- Glucose-6-phosphate isomerase
- 6-phosphogluconate dehydrogenase, decarboxylating
- 6-phosphogluconolactonase
- Cellular tumor antigen p53
- GDH/6PGL endoplasmic bifunctional protein
- Glyceraldehyde-3-phosphate dehydrogenase
- Hexokinase-4
- L-lactate dehydrogenase A chain
- Hexokinase-2
- Glucose-6-phosphatase 3
Sequence:
MAEQVALSRTQVCGILREELFQGDAFHQSDTHIFIIMGASGDLAKKKIYPTIWWLFRDGLLPENTFIVGYARSRLTVADIRKQSEPFFKATPEEKLKLEDFFARNSYVAGQYDDAASYQRLNSHMNALHLGSQANRLFYLALPPTVYEAVTKNIHESCMSQIGWNRIIVEKPFGRDLQSSDRLSNHISSLFREDQIYRIDHYLGKEMVQNLMVLRFANRIFGPIWNRDNIACVILTFKEPFGTEGRGGYFDEFGIIRDVMQNHLLQMLCLVAMEKPASTNSDDVRDEKVKVLKCISEVQANNVVLGQYVGNPDGEGEATKGYLDDPTVPRGSTTATFAAVVLYVENERWDGVPFILRCGKALNERKAEVRLQFHDVAGDIFHQQCKRNELVIRVQPNEAVYTKMMTKKPGMFFNPEESELDLTYGNRYKNVKLPDAYERLILDVFCGSQMHFVRSDELREAWRIFTPLLHQIELEKPKPIPYIYGSRGPTEADELMKRVGFQYEGTYKWVNPHKL
Protein: Ponticulin-like protein C1 (Q54LC2)
Organism: Dictyostelium discoideum (Social amoeba)
Subcellular location: Cell membrane {ECO:0000305}; Lipid-anchor, GPI-anchor {ECO:0000305}.
Interaction partners:
- CMP/dCMP-type deaminase domain-containing protein
- PhoPQ-activated pathogenicity-related protein
- Probable phosphoglycerate mutase
- Secreted protein A
Sequence:
MKFTKSLLLLIVAVFASSNAAETFSNFQVTNSDANSPCVTTPVELKVNTCQSACGSILNVLPVTGSTSKFTFNQFGAQDTKCAATPTSSNEFTCVDGKSKVAIGTTTYSVVCVPDKTNSSESDSSDSTRIGASFALAASVLLSMLAI
Protein: At1g53640/F22G10.8 (Hydroxyproline-rich glycoprotein family protein) (Q9C8L9)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
Sequence:
MRSAIGRRFSNPNGFTIASLVKQTPFLTQSTSHFSSSSDSSGRGRGRGSGEDGGFPAAGRGQFGVNREPVVPGREPSSAGGYGHGRGRPIQSDSISPAFTSFVKSDSPSIGRGRGSVGSDTVSPFAAEPPRQSPPPPQQQQSQSQQQRSQPQQQQPRSQPQQQPNDESQGSPVFVKLQEMQDATSSPPPPESKPGQADPPDNIFNALGNEFSHPSGAGRGKPLVESAPIRQEDNRQIRRPPPPPQQQRVQPQQKRAPTVKDGTPKPQLSAEEAGRRARSELSRGEAEGSSVGGRGGRGRGRGRGARGRGRGRGGDGWRDDKKEEEGEQEAMRIFAGDSADGEKFAEKMGPELMKTLAEGFEEICEKALPSTTHDAIIDAYDTNLMIECEPEYIMPDFGSNPDIDEKPPMSLRECLEKVKPFIVAYEGIKDQEEWEEAINEAMTQAPLMKEIVDHYSGPDRVTAKKQNEELDRIATTLPASAPDSVKRFADRAALTLKSNPGWGFDKKYQFMDKLVLEVSQSYK