wanglab/gogpt-training-data huggingface dataset:
Protein: DELLA protein GAI (GRAS family protein 3) (AtGRAS-3) (Gibberellic acid-insensitive mutant protein) (Restoration of growth on ammonia protein 2) (Q9LQT8)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Transcriptional regulator that acts as a repressor of the gibberellin (GA) signaling pathway. Transcription coactivator of the zinc finger transcription factors GAF1/IDD2 and ENY/IDD1 in regulation of gibberellin homeostasis and signaling. No effect of the BOI proteins on its stability. Probably acts by participating in large multiprotein complexes that repress transcription of GA-inducible genes. Positively regulates XERICO expression. In contrast to RGA, it is less sensitive to GA. Its activity is probably regulated by other phytohormones such as auxin and ethylene. Involved in the regulation of seed dormancy and germination, including glucose-induced delay of seed germination. Involved in the process leading to microtubules (MTs) dissociation in response to gibberellic acid (GA) probably by mediating the translocation of the prefoldin co-chaperone complex from the cytoplasm to the nucleus.
Subcellular location: Nucleus {ECO:0000269|PubMed:12492836, ECO:0000269|PubMed:23583555, ECO:0000269|PubMed:25035403}.
Interaction partners:
- Gibberellin receptor GID1A
- Gibberellin receptor GID1B
- Gibberellin receptor GID1C
- F-box protein GID2
- Transcription factor PIF3
- Transcription factor PIF4
- Transcription factor PIF5
- Protein BRASSINAZOLE-RESISTANT 1
- Transcription factor MYC2
- Gibberellin 3-beta-dioxygenase 1
Sequence:
MKRDHHHHHHQDKKTMMMNEEDDGNGMDELLAVLGYKVRSSEMADVAQKLEQLEVMMSNVQEDDLSQLATETVHYNPAELYTWLDSMLTDLNPPSSNAEYDLKAIPGDAILNQFAIDSASSSNQGGGGDTYTTNKRLKCSNGVVETTTATAESTRHVVLVDSQENGVRLVHALLACAEAVQKENLTVAEALVKQIGFLAVSQIGAMRKVATYFAEALARRIYRLSPSQSPIDHSLSDTLQMHFYETCPYLKFAHFTANQAILEAFQGKKRVHVIDFSMSQGLQWPALMQALALRPGGPPVFRLTGIGPPAPDNFDYLHEVGCKLAHLAEAIHVEFEYRGFVANTLADLDASMLELRPSEIESVAVNSVFELHKLLGRPGAIDKVLGVVNQIKPEIFTVVEQESNHNSPIFLDRFTESLHYYSTLFDSLEGVPSGQDKVMSEVYLGKQICNVVACDGPDRVERHETLSQWRNRFGSAGFAAAHIGSNAFKQASMLLALFNGGEGYRVEESDGCLMLGWHTRPLIATSAWKLSTN
Protein: Kiss1 receptor (B0F101)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004651}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}.
Interaction partners:
Sequence:
IANLAATDIIFLLCCVPFTATLYPLPGWIFGDFMCKFVAFLQQVTVQATCITLTAMSGDRCYVTVYPLKSLHHRTPRVAMIVSICIWIGSFILSIPIFLYQRLEDGYWYGPRKYCMERFPSKTHEKAFILYQFIAVYLLPVITISFCYSFMLKRVGQASVEPVDNNHQVHLLSERTISIRSKISKMVVVIVVLFTICWGPIQIFVLFQSFYPNFKANYATYKIKTWANCMSYANSSINPIVYGFMGASFRKSF
Protein: Ribosome-inactivating protein lychnin (EC 3.2.2.22) (P85101)
Organism: Silene chalcedonica (Maltese-cross) (Lychnis chalcedonica)
Function: Ribosome-inactivating protein of type 1, inhibits protein synthesis in animal cells. Inhibits cell-free translation in rabbit reticulocyte lysate system with an IC(50) of 0.17 nM.
Interaction partners:
Sequence:
RPSWTVDSDSAKYSSFLDSLREEFGRGTPKVCNIPVTKKANNDKFVLVNLVLPFNRNTITLAFRASDAYLVGFQDRDSKTNKLRANFFSDEYRALSGKYKSIFTDAEVLAPALPCASTYTDLQNKAGVSREKLSLGVSSLQTAFTAVYGKVFTGKNVAKFALISIQMVAEAARFKYIEDQVINRGMYSSFEAGARITLLENNWSKISEQYHKSCKLGGGQFTEEEMKLGLLLYN
Protein: Phosphatidylcholine:ceramide cholinephosphotransferase 2 (EC 2.7.8.27) (Sphingomyelin synthase 2) (SMS2) (Q8NHU3)
Organism: Homo sapiens (Human)
Function: Sphingomyelin synthase that primarily contributes to sphingomyelin synthesis and homeostasis at the plasma membrane. Catalyzes the reversible transfer of phosphocholine moiety in sphingomyelin biosynthesis: in the forward reaction transfers phosphocholine head group of phosphatidylcholine (PC) on to ceramide (CER) to form ceramide phosphocholine (sphingomyelin, SM) and diacylglycerol (DAG) as by-product, and in the reverse reaction transfers phosphocholine from SM to DAG to form PC and CER. The direction of the reaction appears to depend on the levels of CER and DAG in the plasma membrane. Does not use free phosphorylcholine or CDP-choline as donors. Can also transfer phosphoethanolamine head group of phosphatidylethanolamine (PE) on to ceramide (CER) to form ceramide phosphoethanolamine (CPE). Regulates receptor-mediated signal transduction via mitogenic DAG and proapoptotic CER, as well as via SM, a structural component of membrane rafts that serve as platforms for signal transduction and protein sorting. To a lesser extent, plays a role in secretory transport via regulation of DAG pool at the Golgi apparatus and its downstream effects on PRKD1. Required for normal bone matrix mineralization.
Subcellular location: Cell membrane {ECO:0000269|PubMed:14685263, ECO:0000269|PubMed:30779713}; Multi-pass membrane protein {ECO:0000255}. Golgi apparatus membrane {ECO:0000269|PubMed:14685263, ECO:0000269|PubMed:18370930}; Multi-pass membrane protein {ECO:0000255}. Note=Primarily localized at the plasma membrane with a small fraction at the Golgi apparatus. {ECO:0000269|PubMed:14685263}.
Interaction partners:
- Sphingomyelin phosphodiesterase
- Sphingomyelin phosphodiesterase 2
- Ceramide glucosyltransferase
- Ceramide synthase 6
- Sphingomyelin phosphodiesterase 3
- Ceramide synthase 2
- Sphingomyelin phosphodiesterase 4
- Ceramide synthase 4
- Ceramide kinase
- Acid ceramidase
Sequence:
MDIIETAKLEEHLENQPSDPTNTYARPAEPVEEENKNGNGKPKSLSSGLRKGTKKYPDYIQIAMPTESRNKFPLEWWKTGIAFIYAVFNLVLTTVMITVVHERVPPKELSPPLPDKFFDYIDRVKWAFSVSEINGIILVGLWITQWLFLRYKSIVGRRFCFIIGTLYLYRCITMYVTTLPVPGMHFQCAPKLNGDSQAKVQRILRLISGGGLSITGSHILCGDFLFSGHTVTLTLTYLFIKEYSPRHFWWYHLICWLLSAAGIICILVAHEHYTIDVIIAYYITTRLFWWYHSMANEKNLKVSSQTNFLSRAWWFPIFYFFEKNVQGSIPCCFSWPLSWPPGCFKSSCKKYSRVQKIGEDNEKST
Protein: Protein FAM13A (O94988)
Organism: Homo sapiens (Human)
Interaction partners:
- Iron-responsive element-binding protein 2
- Hedgehog-interacting protein
- Neuronal acetylcholine receptor subunit alpha-3
- Glutathione S-transferase C-terminal domain-containing protein
Sequence:
MGAGALAICQSKAAVRLKEDMKKIVAVPLNEQKDFTYQKLFGVSLQELERQGLTENGIPAVVWNIVEYLTQHGLTQEGLFRVNGNVKVVEQLRLKFESGVPVELGKDGDVCSAASLLKLFLRELPDSLITSALQPRFIQLFQDGRNDVQESSLRDLIKELPDTHYCLLKYLCQFLTKVAKHHVQNRMNVHNLATVFGPNCFHVPPGLEGMKEQDLCNKIMAKILENYNTLFEVEYTENDHLRCENLARLIIVKEVYYKNSLPILLTRGLERDMPKPPPKTKIPKSRSEGSIQAHRVLQPELSDGIPQLSLRLSYRKACLEDMNSAEGAISAKLVPSSQEDERPLSPFYLSAHVPQVSNVSATGELLERTIRSAVEQHLFDVNNSGGQSSEDSESGTLSASSATSARQRRRQSKEQDEVRHGRDKGLINKENTPSGFNHLDDCILNTQEVEKVHKNTFGCAGERSKPKRQKSSTKLSELHDNQDGLVNMESLNSTRSHERTGPDDFEWMSDERKGNEKDGGHTQHFESPTMKIQEHPSLSDTKQQRNQDAGDQEESFVSEVPQSDLTALCDEKNWEEPIPAFSSWQRENSDSDEAHLSPQAGRLIRQLLDEDSDPMLSPRFYAYGQSRQYLDDTEVPPSPPNSHSFMRRRSSSLGSYDDEQEDLTPAQLTRRIQSLKKKIRKFEDRFEEEKKYRPSHSDKAANPEVLKWTNDLAKFRRQLKESKLKISEEDLTPRMRQRSNTLPKSFGSQLEKEDEKKQELVDKAIKPSVEATLESIQRKLQEKRAESSRPEDIKDMTKDQIANEKVALQKALLYYESIHGRPVTKNERQVMKPLYDRYRLVKQILSRANTIPIIGSPSSKRRSPLLQPIIEGETASFFKEIKEEEEGSEDDSNVKPDFMVTLKTDFSARCFLDQFEDDADGFISPMDDKIPSKCSQDTGLSNLHAASIPELLEHLQEMREEKKRIRKKLRDFEDNFFRQNGRNVQKEDRTPMAEEYSEYKHIKAKLRLLEVLISKRDTDSKSM
Protein: Vitamin D3 dihydroxylase (EC 1.14.15.22) (CYP105A1) (Cytochrome P450-CVA1) (Cytochrome P450-SU1) (Vitamin D3 hydroxylase) (VD3 hydroxylase) (P18326)
Organism: Streptomyces griseolus
Function: Involved in the metabolism of vitamin D3 (calciol) and of a number of sulfonylurea herbicides. Catalyzes the two-step hydroxylation (25- and 1-alpha-hydroxylation) of vitamin D3 (VD3) to yield its active form 1-alpha,25-dihydroxyvitamin D3 (calcitriol). The first step is the hydroxylation of the C-25 position of VD3 to produce 25-hydroxyvitamin D3 (calcidiol). The second reaction is the hydroxylation of the C1-alpha-position of calcidiol to produce calcitriol. It can also hydroxylate vitamin D2.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:15207715}.
Interaction partners:
Sequence:
MTDTATTPQTTDAPAFPSNRSCPYQLPDGYAQLRDTPGPLHRVTLYDGRQAWVVTKHEAARKLLGDPRLSSNRTDDNFPATSPRFEAVRESPQAFIGLDPPEHGTRRRMTISEFTVKRIKGMRPEVEEVVHGFLDEMLAAGPTADLVSQFALPVPSMVICRLLGVPYADHEFFQDASKRLVQSTDAQSALTARNDLAGYLDGLITQFQTEPGAGLVGALVADQLANGEIDREELISTAMLLLIAGHETTASMTSLSVITLLDHPEQYAALRADRSLVPGAVEELLRYLAIADIAGGRVATADIEVEGHLIRAGEGVIVVNSIANRDGTVYEDPDALDIHRSARHHLAFGFGVHQCLGQNLARLELEVILNALMDRVPTLRLAVPVEQLVLRPGTTIQGVNELPVTW
Protein: Cyclin-C (P39947)
Organism: Rattus norvegicus (Rat)
Function: Component of the Mediator complex, a coactivator involved in regulated gene transcription of nearly all RNA polymerase II-dependent genes. Mediator functions as a bridge to convey information from gene-specific regulatory proteins to the basal RNA polymerase II transcription machinery. Mediator is recruited to promoters by direct interactions with regulatory proteins and serves as a scaffold for the assembly of a functional preinitiation complex with RNA polymerase II and the general transcription factors. Binds to and activates cyclin-dependent kinase CDK8 that phosphorylates the CTD (C-terminal domain) of the large subunit of RNA polymerase II (RNAp II), which may inhibit the formation of a transcription initiation complex (By similarity).
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
- Mediator complex subunit 12
- cyclin-dependent kinase
- Mediator of RNA polymerase II transcription subunit 13
- Mediator complex subunit 12L
- Mediator of RNA polymerase II transcription subunit 1
- Mediator of RNA polymerase II transcription subunit 18
- Mediator of RNA polymerase II transcription subunit 14
- Mediator of RNA polymerase II transcription subunit 7
- Mediator of RNA polymerase II transcription subunit 28
- Mediator of RNA polymerase II transcription subunit 13
Sequence:
MAGNFWQSSHYLQWILDKERQKDLKFLSEEEYWKLQIFFTNVIQALGEHLKLRQQVIATATVYFKRFYARYSLKSIDPVLMAPTCVFLASKVEEFGVVSNTSLIAATTSVLKTRFSYASPKEFPYRMNHILECEFYLLELMDCCLIVYHPYRPLLQYVQDMGQEDVLLPLAWRIVNDTYRTDLCLLYPPFMIALACLHVACVVQQKDARQWFAELSVDMEKILEIIRVILKLYEQWKNFDERKEMATILSKMPKPKPPPNSEGEQGPNGSQNSSYSQS
Protein: Gem-associated protein 7 (Gemin-7) (Q9CWY4)
Organism: Mus musculus (Mouse)
Function: The SMN complex catalyzes the assembly of small nuclear ribonucleoproteins (snRNPs), the building blocks of the spliceosome, and thereby plays an important role in the splicing of cellular pre-mRNAs. Most spliceosomal snRNPs contain a common set of Sm proteins SNRPB, SNRPD1, SNRPD2, SNRPD3, SNRPE, SNRPF and SNRPG that assemble in a heptameric protein ring on the Sm site of the small nuclear RNA to form the core snRNP (Sm core). In the cytosol, the Sm proteins SNRPD1, SNRPD2, SNRPE, SNRPF and SNRPG are trapped in an inactive 6S pICln-Sm complex by the chaperone CLNS1A that controls the assembly of the core snRNP. To assemble core snRNPs, the SMN complex accepts the trapped 5Sm proteins from CLNS1A forming an intermediate. Binding of snRNA inside 5Sm triggers eviction of the SMN complex, thereby allowing binding of SNRPD3 and SNRPB to complete assembly of the core snRNP (By similarity).
Subcellular location: Nucleus, nucleoplasm {ECO:0000250|UniProtKB:Q9H840}. Nucleus, gem {ECO:0000250|UniProtKB:Q9H840}. Cytoplasm {ECO:0000250|UniProtKB:Q9H840}. Note=Found both in the nucleoplasm and in nuclear bodies called gems (Gemini of Cajal bodies) that are often in proximity to Cajal (coiled) bodies. Also found in the cytoplasm (By similarity). {ECO:0000250}.
Interaction partners:
- Gem-associated protein 8
- Gem-associated protein 2
- Probable ATP-dependent RNA helicase DDX20
- Serine-threonine kinase receptor-associated protein
- Gem
- Gem-associated protein 5
- Gem-associated protein 6
- Survival motor neuron protein
- Small nuclear ribonucleoprotein Sm D3
- Small nuclear ribonucleoprotein-associated protein B
Sequence:
MQSPLTIPVPVPVLRLPRGPDGFSRGFASDGRRTILRPEVGEGHIQDPPESQEQRARATLRERYLRSLLAMVGHPVSFTLHEGVHVTAQFGATDLDVANFYVSQLQTPIGVQAEALLRCSDIISYSFKL
Protein: Transcription factor AP-2, isoform F (M9PFX8)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MSFLATLDASAWQERLSGHGSLGLSSGSAAYTTHSGGHTGRSGPATGHSGHSSTHGSAATMHHQSLQSDFQPPYFPPPFHHSTQSPPQQQISGYLQNHGALEYLGTDPYGQPLSSLHHAPLHHYNQLAGLRSTQDQLGIHRTHREAELQGHVTQLSHGFPYTDRRSDYGSAISAGAAHGTRLGHEHESLALHQALQNAVDDVQAPALDDNVAFMSDLPLIKSMKSGKEAGNIGSGSPSEVFCAVPGRLSLLSSTSKYKVTIAEVQRRLSPPECLNASLLGGVLRRAKSKNGGRLLREKLEKIGLNLPAGRRKAANVTLLTSLVEGEATHLAKDFHFVCETEFPARQLAEYIVRHQTEPQDSYRRKELILHSQQITKELMQILSQDRTTHFGTRSQHLLEPSMQRHLTHFSLITHGFGSPAIMAVLHAFQTFLNESLNYLEKLYPSNGGGMVSSSLDKSKIDNEKK
Protein: Geranylgeranyl transferase type-2 subunit beta 1 (EC 2.5.1.60) (Geranylgeranyl transferase type II subunit beta 1) (Rab geranylgeranyl transferase beta subunit 1) (AtRGTB1) (Rab-GGT beta 1) (Q84J75)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Catalyzes the transfer of a geranylgeranyl moiety from geranylgeranyl diphosphate to both cysteines of Rab proteins with the C-terminal sequence -CCXX, CXXX, -XCCX and -XCXC, such as RABA1A, RABA2A, RABF2A and RABG2. Involved in the geranylgeranylation of RABA2A. In vitro, can prenylate PGGTI targets with the C-terminal sequence Cys-aliphatic-aliphatic-X (CaaX) with leucine in the terminal position. Substrates with the C-terminal sequence -CSIL such as ARAC11/ROP1 or GG2/AGG2 are prenylated independently of REP and when the beta subunit is associated with the alpha subunit RGTA1.
Interaction partners:
- Rab escort protein 1
- Geranylgeranyl transferase type-2 subunit alpha 1
- Geranylgeranyl transferase type-2 subunit alpha 2
- Protein prenylyltransferase superfamily protein
- Ras-related protein RABD2b
- Ras-related protein RABD2c
- Geranylgeranyl transferase type-2 subunit beta 2
- Ras-related protein RABH1a
- Ras-related protein RABG3c
- Ras-related protein RABC2b
Sequence:
MSSTSSSQMVQLVADKHVRYILMAEKKKESFESVVMDHLRMNGAYWGLTTLDLLDKLGCVSEEEVISWLMTCQHESGGFAGNTGHDPHILYTLSAVQILALFDKINILDIGKVSSYVAKLQNEDGSFSGDMWGEIDTRFSYIAICCLSILKCLDKINVEKAVKYIVSCKNLDGGFGCTPGAESHAGQIFCCVGALAITGSLHHVDKDSLGWWLCERQLKAGGLNGRPEKLADVCYSWWVLSSLIMIDRVHWIDKAKLVKFILDCQDLDNGGISDRPEDAVDIFHTYFGVAGLSLLEYPGVKVIDPAYALPVDVVNRIIFTK
Protein: Catalase (EC 1.11.1.6) (Q6FM56)
Organism: Candida glabrata (strain ATCC 2001 / BCRC 20586 / JCM 3761 / NBRC 0622 / NRRL Y-65 / CBS 138) (Yeast) (Nakaseomyces glabratus)
Interaction partners:
- Superoxide dismutase
- Superoxide dismutase
- Peroxisomal hydratase-dehydrogenase-epimerase
- thioredoxin-dependent peroxiredoxin
- Acyl-coenzyme A oxidase
- Peptide-methionine
- 2-hydroxyacyl-CoA lyase
- Transcription factor
- Candida glabrata strain CBS138 chromosome J complete sequence
- Candida glabrata strain CBS138 chromosome A complete sequence
Sequence:
MSANPTNTSDVRGDRVVTNSTGYPYNDPFATQRVGQHGPLLMQDANLIDSLAHFNRERIPERNPHAHGSGAFGYFEVTDDITDICGSAMFSEIGKRTRFLTRFSTVGGEKGSADTARDPRGFATKFYTEEGNLDWVYNNTPIFFIRDPSKFPHFIHTQKRNPQTNLKDPNMFWDYLTTPENQVAVHQLMILFSDRGTPASYRHMNGYSGHTYKWSNKKGEWHYVQVHILTDQGIKNLTNDEAVEIAGKNPDYCQQDLYENIAKGNYPSWTVYIQTMTEEQAKKLPFSVFDLTKVWPHKDFPLRRVGKMVMNENPLNYFASIEQAAFSPANTVPYQEPSADPVLQSRLFAYADAHRYRLGANFHQIPVNCPYASKFFNPVIRDGPMNVDGNFGNEPNYYASNKQYQIPNQDRPIQQHQEVWNGPAQPFHWATSPGDIDFVQARDLYKVLGKQKDQQEHLAYNIGTHVAGADPEIQQRVIDMFSRVDEGLGANIRKEIEKNASAPTAKI
Protein: Uncharacterized transporter C36.02c (O59699)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Subcellular location: Endoplasmic reticulum {ECO:0000269|PubMed:16823372}. Membrane {ECO:0000255}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Putative uncharacterized protein C1347.14c
- Coiled-coil domain-containing protein 124 homolog
- Putative inorganic phosphate transporter C23D3.12
- 40 kDa peptidyl-prolyl cis-trans isomerase
Sequence:
MSSTPTAEELALQNTVSQSASAHPELYHTVSHASNNSYQLPQLSRSATSNFSTSARFAARYPTTAGESFQNLTPVNSNPSNQNSKTEPNPDDVEKCIQDPLLQVFPVVEEPERFVFSIDPKSPLIAVNWPFKRKLKTTCILAYVALCSSFASSVFAVPAEAITTVFHISLTVSLLTMTVFLLGYCSGPIIWAPLSELSGRKPPILIGMLGFGIFNISVAVGKDIQTIMMCRFFAGFFASAPLTVVAAALADMYSNKYRGTAITLFSAMVFDGPLVSPIVGGFLTKSYLGWRWTEYITSFMGFFALIIVYLFCDETYSKAIIQGKAKEYRAITGNYFVHAKSEEEVLTLSDIAKNYLLVPMKLLFTEPICFLITLYSSFVYAILYLLLEAYPIIFGEKRHFSMGVAELPYIGLLVGVFIGSGINIAFEPWYYRKCLAQGGKPDPEARLPPMMIGCFMFPAGIFWLSWSGHYSYVNWVVPALSGLATGCGILLIFLQCINYLIDAYLFRAASAIAANTIMRSAMAAGFPLFAVQMFHNMGVGWAGSLLGFIATALIPMPFVFFFFGRKIRRMSKMAVDF
Protein: ATP-dependent RNA helicase DBP5 (EC 3.6.4.13) (DEAD box protein 5) (Helicase CA5/6) (Ribonucleic acid-trafficking protein 8) (P20449)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: ATP-dependent RNA helicase associated with the nuclear pore complex and essential for mRNA export from the nucleus. May participate in a terminal step of mRNA export through the removal of proteins that accompany mRNA through the nucleopore complex. Contributes to the blocking of bulk poly(A)+ mRNA export in ethanol-stressed cells. May also be involved in early transcription.
Subcellular location: Cytoplasm. Nucleus, nuclear pore complex. Nucleus membrane; Peripheral membrane protein; Cytoplasmic side. Note=Nuclear pore complex cytoplasmic fibrils. Accumulates in the nucleus rapidly and reversibly in response to ethanol stress.
Interaction partners:
- Nucleoporin NUP159
- mRNA export factor GLE1
- Nucleoporin NUP42
- Nuclear mRNA export protein SAC3
- mRNA export factor MEX67
- mRNA transport factor GFD1
- Nucleoporin NUP116/NSP116
- Nucleoporin NUP2
- Nucleoporin NUP82
- RNA annealing protein YRA1
Sequence:
MSDTKRDPADLLASLKIDNEKEDTSEVSTKETVKSQPEKTADSIKPAEKLVPKVEEKKTKQEDSNLISSEYEVKVKLADIQADPNSPLYSAKSFDELGLAPELLKGIYAMKFQKPSKIQERALPLLLHNPPRNMIAQSQSGTGKTAAFSLTMLTRVNPEDASPQAICLAPSRELARQTLEVVQEMGKFTKITSQLIVPDSFEKNKQINAQVIVGTPGTVLDLMRRKLMQLQKIKIFVLDEADNMLDQQGLGDQCIRVKRFLPKDTQLVLFSATFADAVRQYAKKIVPNANTLELQTNEVNVDAIKQLYMDCKNEADKFDVLTELYGLMTIGSSIIFVATKKTANVLYGKLKSEGHEVSILHGDLQTQERDRLIDDFREGRSKVLITTNVLARGIDIPTVSMVVNYDLPTLANGQADPATYIHRIGRTGRFGRKGVAISFVHDKNSFNILSAIQKYFGDIEMTRVPTDDWDEVEKIVKKVLKD
Protein: Cold acclimation protein (O50054)
Organism: Spinacia oleracea (Spinach)
Interaction partners:
Sequence:
MEHPSGHTRHTTHVEDDLQDASIQTGHNEDEKPEKKTMMMKVKAKARKIRDSIKNVGHSHDHDHDHDENDDDDDEEEEVEMDMDSEIQGTHTAQTGTPGEEVTRQKLHEPKLVERTIGEDIQVRNRLGDYQTFDPTSETFTPGHDQTLGWSRTDTGKPKEYGGSHSTEASDKEMNAAAPVNLGGVVVGCDHQVPKDVGEDSHSANYQSEVIEPTVTGFEFPVAQSHSPANKPQGDFQTFNPRTDTERLNKSVEMFNESNNAPISAHSGHESHERTAMEGVVDAPGNKTEGDYQTFDPKSTSYVPGQEETLGWSRTDTGGLNKSEELSNLSNNTSTETHSGDEETRIIQILNQMDLMNVNEESQQKPTAPDDSHLNKTEHHNPPDEKISTESHHDQFFAKPDTSETGPVVQATTTPATDGNSYTGMISNAAAMVADKAMLATSAVTSKLGYGGPSTGPTSPDQQHSTTDVTSEMHDNNPSDKPVGTTYGERMSSATAVVTDKAIQAKDVVATKLGYGGNPDQQHSTDVTSEMHDNPSEQPVGTTYGEKISSATTVVTDKAIQAKDVVAAKLGYGGPSTGPSTGPITGPSKGPITGPSTGPITWGDKGVAVKEYLVEKLKPGEDDKALSEVITEALPSPLHKPKEEGVTIIGRVAEPKEVVQMIDHIEEKNDDGIVMGEDDKAVFEAVVGKVGGGDEVAERLGWGEEKKEDGSDNGGAGVVSPGKGVMERIKDAASGWFQSSDEFPSQDTGTGTGHITQGTESFPISSMESEQKRIGGAGSL
Protein: Basic phospholipase A2 9 (svPLA2) (EC 3.1.1.4) (Cdc-9) (Phosphatidylcholine 2-acylhydrolase) (P86805)
Organism: Crotalus durissus cumanensis (South American rattlesnake)
Function: Snake venom phospholipase A2 (PLA2) that has a strong dose-dependent anticoagulant effect. Intramuscular and intervenal injection causes muscle necrosis. Induces moderate edema in the mouse foot pad. PLA2 catalyzes the calcium-dependent hydrolysis of the 2-acyl groups in 3-sn-phosphoglycerides.
Subcellular location: Secreted {ECO:0000269|PubMed:19747981}.
Interaction partners:
Sequence:
SLVQFNKMIKFETRKSGLPFYAAYGCYCGWGGQRPKDATDRCCFVHDCCYGKVAKCNTKWDIYSYSLKSGYITCGKGTWCKEQICECDRVAAECLRRSLSTYKNEYMFYPDSRCREPPEYTC
Protein: Uncharacterized protein (Q586C7)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MGRQRALFLLGLLQRQHPEAHKNLTREVERVEREARSDGDLVRLRESCRVVLHLLNEHREFLPFVAQGCPSCLSAVLSQVGKGGITDNAGDADRNDGDESCMEDIDMLRLAALLSTSGSPVDALADGVSKSLEPMTRLVFSTNSEVGELALSLLGRAVRLSADSERLAGSLLGNEKFWVRFARAFFGDSSRANHLDKEARLCTTSSPPSVLASVLGLLRRCCMVSRVGRDASFRSLLVRVCTAVTLKNDARLREEAVLLLYTLRITSSTDETECLRECIAVLAPATPGSEDDCANVARNGSDPGFVDRLVGDRNIMYANSLMNALISLQKNQFESSARLRDLERIAKLLFDPHVPCGAAAALVLLPGAVTSVFAAASDVEEKISAFACALFSSAIEGLEEMLSSPMNLGATEQEGALRESDICSYRRCLVEDFLSLGGMVLLEDLLLDYSSGVVSTATRLVRSLMRFSSGTRNLVLASRCFPNLYKALEGVSGESNISESLRCGAEDGVCAMLHIALDTFSLLGSDTAWVLPESAVGCVSMIATESRNNVSVLAAALRTLSVLAASHPMAATVVLDYDYINSVLGMEGDAAVNSDGEEAKEPWVLNDTDAAYICGSFDIMSAVVSQEPSCVTFEWIETLIMATKRAQHWQDEVPRFARPLWNVVVKTVTISEEGRTYLLEDTEFVDVLLNTMASCCSYMTRGCESERIRHSAENIGTDNKVVGTPYGDCSSVVARLLPLLVRVARFLPALQQSQPLEGACDLVEALAILLSMRGAEASVDLLVNVALFAYDNETTLISVFDLFVKVGLRASQELQQRALASLSVLEGADPAVVEGDMRCAEALGDFERATAALGALLARCRAGEGSDLDNEVVEEVSALILAALKAPSDHPPLLFALPPTGAPPLLSRHRRILSSTVDLLRSGHQIFDHTAQQLWCEHQVFQRVSRFFGAIRDSEGAEELLDEICDLLSIMYGLHNPWASAEDSGVESSDYTPSCDVGDLLVFVVEYILNERLSRSSSCRSLFTRLCECAPFRHGMLAAHREIYHSSLEVVSNCSGEAEEREVFDRWINEKLDGTVHATVA
Protein: Histone H2B type 1-F/J/L (H2B 291A) (P10853)
Organism: Mus musculus (Mouse)
Function: Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling.
Subcellular location: Nucleus. Chromosome.
Interaction partners:
- Histone H3.1
- Histone H3.2
- Histone H3.3
- Histone H4
- Plasminogen
- E3 ubiquitin-protein ligase BRE1A
- Histone H2A type 1-K
- E3 ubiquitin-protein ligase BRE1B
- Histone H2A type 1-B
- Histone H2AX
Sequence:
MPEPAKSAPAPKKGSKKAVTKAQKKDGKKRKRSRKESYSVYVYKVLKQVHPDTGISSKAMGIMNSFVNDIFERIASEASRLAHYNKRSTITSREIQTAVRLLLPGELAKHAVSEGTKAVTKYTSSK
Protein: 26S proteasome non-ATPase regulatory subunit 2 (Q9VW54)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- 26S proteasome non-ATPase regulatory subunit 11
- 26S proteasome non-ATPase regulatory subunit 4
- 26S proteasome regulatory complex subunit p50
- Probable 26S proteasome non-ATPase regulatory subunit 3
- 26S proteasome non-ATPase regulatory subunit 1
- 26S proteasome regulatory subunit 7
- 26S proteasome non-ATPase regulatory subunit 6
- 26S proteasome non-ATPase regulatory subunit 14
- 26S proteasome non-ATPase regulatory subunit 13
- 26S proteasome regulatory subunit 8
Sequence:
MTGETKLEKKPLKPAASEGDAKDPKAKKDEKKDGKDKEQQPELSDEDQQLQEELELLVQHLQEPDAKLYQPTLESMAKLIRASTTSMTSVPKPLKFMRPHYETMKTVYKHMPNEQARQLCADIISVLSMTMGSGKDCLAYRFLCDRKQRIGDWGHEYVRHLSGEISAHYHDTTGDFRVQLIELVKQIIPYNMEHNAEADACDLLIEIDHLHLLSDFVDESAYPRVCLYLQSCYPYVPDPDNTIILETALQLSRKFNQYTQAMRLALMLNDMDKIGEIFKEPKEPAMQKQLAFMLARQQICLELDELVPDYDDLMEIMSNANLNKHFLNLARELDIMEPKTPEDIYKSHLDNSRSRFASIQVDSAKQNLAASFVNGFVNAGFGVDKLLSEDGNKWLYKNKEHGMLSATASLGLILLWDVDGGLTMIDKYLYSTDDNIKSGALLACGIVNCGIRNEVDPAHALLSDYIDNQNSCMRVGAILGLGIAYAGSNRSIVIDTLKTVFSFGSNNKSSASVEILGITALSLGLISVGSCNSEITEILLQTIMGLTKADLKDTYTRFLFLGLGLLYLGRQKSTEAVMMTLEVLEEPYRSMATTMVDICAYAGTGNVLKIQQLLHICSDHYETSSADDEKEKSKKDKGKDKEKEKEKEKEKEREKDLSATQSIAVLGIALIAMGEDIGAEMAYRSFGNLLRYCEPAIRRAVPLALGLISASNPKLNIIDTLSKFSHDSDAEVAHNAIFAMGLVGAGTNNARLASMLRQLAQYHSKDPSNLFMVRIAQSLTHLGKGTLSLSPYHSDRQLMNPMAVAGLMATLVSLLDVKNLILNRSHYLLYTLVPAMQARMLITFDEELNQLQVPVRVGIAIDVVGQAGKPKTITGFQTHTTPVLLAIGERAELATDEYLALTPVMEGFVILKKNPNFVK
Protein: Adenylate kinase 2 (PfAK2) (EC 2.7.4.3) (Q8IB06)
Organism: Plasmodium falciparum (isolate 3D7)
Function: Catalyzes the reversible transfer of the terminal phosphate group between ATP and AMP. Has very low activity with CTP, GTP, ITP and UTP and no activity with GMP, UMP or IMP in vitro.
Subcellular location: Parasitophorous vacuole membrane {ECO:0000269|PubMed:25909331}; Lipid-anchor {ECO:0000269|PubMed:25909331}. Note=Localizes to the vacuolar side of the parasitophorous vacuole. {ECO:0000269|PubMed:25909331}.
Interaction partners:
- Adenylosuccinate lyase
- Ribonucleoside-diphosphate reductase
- Nucleoside diphosphate kinase
- nucleoside-diphosphate kinase
- Ribonucleoside-diphosphate reductase small chain, putative
- Ribonucleoside-diphosphate reductase small chain, putative
- Pyruvate kinase
- pyruvate kinase
- Adenylate kinase 1
- AMP deaminase
Sequence:
MGSCYSRKNKVSTISLDEEEKKKEKKKKKKIYILNGASGSGKDTQCRLLEKKYNYKIICISKLLKEYKEEYNKENVLNEEENYFDEIEKCMIDGSLVNDQIVIEIFHKQLNKYINDDKYNGIIINGFPRNYEQALLIIQNNISITKFINIQVGKDTLWTRINNRIIDPITNISYNENIIQIIKKKREGQELSDKEQKQLIIDNHLYNNLSNDILERLTKRKDDEEQVFNKRFQLYIESEQKINSLFKNICKNVDGEKSINDIFDQICSIIDDNPN