wanglab/gogpt-training-data huggingface dataset:
Protein: LIM domain-containing protein PLIM2b (Pollen-expressed LIM protein 2B) (Q1ECF5)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Binds to actin filaments and promotes cross-linking into thick bundles. Has an actin-stabilizing activity. The actin regulatory activities are inhibited by pH > 6.8 but are [Ca(2+)] independent.
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000269|PubMed:20817848}.
Interaction partners:
- Uncharacterized GPI-anchored protein At5g19240
- Protein DA1-related 7
- Uncharacterized GPI-anchored protein At3g06035
- Uncharacterized GPI-anchored protein At5g19230
- Propionyl-CoA carboxylase
- Expansin-A13
- Fimbrin-5
- Actin cross-linking protein, putative
- Zinc finger CCCH domain-containing protein 52
- Uncharacterized GPI-anchored protein At5g19250
Sequence:
MSFTGTLDKCNVCDKTVYVVDMLSIEGMPYHKSCFRCTHCKGTLQMSNYSSMDGVLYCKTHFEQLFKESGNFSKNFQPGKTEKPELTRTPSKISSIFCGTQDKCAACEKTVYPLEKIQMEGECFHKTCFRCAHGGCTLTHSSYASLDSVLYCRHHFNQLFMEKGNYAHVLQAANHRRTASGNTLPPEPTEDVAVEAKEENGVSES
Protein: B-box domain protein 30 (AtBBX30) (Microprotein 1A) (Q1G3I2)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Developmental regulator acting by forming heterodimeric complexes, that sequester CO and CO-like (COL) proteins into non-functional complexes. Engages CO and the transcriptional repressor TPL in a tripartite complex. Involved in the CO-mediated long-day flowering-promotion pathway.
Subcellular location: Nucleus {ECO:0000269|PubMed:27015278}.
Interaction partners:
- Protein TOPLESS
- B-box zinc finger protein 19
- B-box zinc finger protein 23
- B-box zinc finger protein 24
- B-box zinc finger protein 21
- DNA-binding enhancer protein-like protein
- B-box zinc finger protein 25
- B-box zinc finger family protein
- B-box zinc finger protein 20
- B-box zinc finger protein 22
Sequence:
MCRGFEKEEERRSDNGGCQRLCTESHKAPVSCELCGENATVYCEADAAFLCRKCDRWVHSANFLARRHLRRVICTTCRKLTRRCLVGDNFNVVLPEIRMIARIEEHSSDHKIPFVFL
Protein: Tetratricopeptide repeat protein 19, mitochondrial (TPR repeat protein 19) (Q8CC21)
Organism: Mus musculus (Mouse)
Function: Required for the preservation of the structural and functional integrity of mitochondrial respiratory complex III by allowing the physiological turnover of the Rieske protein UQCRFS1. Involved in the clearance of UQCRFS1 N-terminal fragments, which are produced upon incorporation into the complex III and whose presence is detrimental for its catalytic activity.
Subcellular location: Mitochondrion inner membrane {ECO:0000269|PubMed:21278747}.
Interaction partners:
- Complex III assembly factor LYRM7
- Mitochondrial chaperone BCS1
- Ubiquinol-cytochrome c reductase complex assembly factor 1
Sequence:
MFRLLRWRLGRTLLRAAGRRCGGCTARLLPERTGDAGTGAERLRTRGAPARGHGVLPLLAALAWFSRPAATAEQPGEDASDEAEAEIIQLLKQAKLSIMKDEPEAAELILHDALRLAYESDNRKAITYTYDLMANLAFIRGQLENAEQLFKATMSYLLGGGMKQEDNAIIEISLKLANIYAAQNKQEFALAGYEFCISTLEGKIEREKELAEDIMSEETANTYLLLGMCLDSCARYLLFSKQLSQAQRMYEKALQICQEIQGERHPQTIVLMSDLATTLDAQGHFDDAYIYMQRASDLAREINHPELHMVLSNLAAILIHRERYTQAKEIYQEALKRAELKRDEVSVQHIREELAELSRKSRRLT
Protein: Serine/threonine-protein kinase PAK 4 (EC 2.7.11.1) (p21-activated kinase 4) (PAK-4) (O96013)
Organism: Homo sapiens (Human)
Function: Serine/threonine protein kinase that plays a role in a variety of different signaling pathways including cytoskeleton regulation, cell migration, growth, proliferation or cell survival. Activation by various effectors including growth factor receptors or active CDC42 and RAC1 results in a conformational change and a subsequent autophosphorylation on several serine and/or threonine residues. Phosphorylates and inactivates the protein phosphatase SSH1, leading to increased inhibitory phosphorylation of the actin binding/depolymerizing factor cofilin. Decreased cofilin activity may lead to stabilization of actin filaments. Phosphorylates LIMK1, a kinase that also inhibits the activity of cofilin. Phosphorylates integrin beta5/ITGB5 and thus regulates cell motility. Phosphorylates ARHGEF2 and activates the downstream target RHOA that plays a role in the regulation of assembly of focal adhesions and actin stress fibers. Stimulates cell survival by phosphorylating the BCL2 antagonist of cell death BAD. Alternatively, inhibits apoptosis by preventing caspase-8 binding to death domain receptors in a kinase independent manner. Plays a role in cell-cycle progression by controlling levels of the cell-cycle regulatory protein CDKN1A and by phosphorylating RAN.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:12356872}. Note=Seems to shuttle between cytoplasmic compartments depending on the activating effector. For example, can be found on the cell periphery after activation of growth-factor or integrin-mediated signaling pathways. {ECO:0000269|PubMed:12356872}.
Interaction partners:
- Cell division control protein 42 homolog
- Ras-related C3 botulinum toxin substrate 3
- LIM domain kinase 1
- Rho guanine nucleotide exchange factor 7
- Rho guanine nucleotide exchange factor 6
- Rho-related GTP-binding protein RhoU
- Ras-related C3 botulinum toxin substrate 2
- RAF proto-oncogene serine/threonine-protein kinase
- LIM domain kinase 2
- PAK4-inhibitor INKA1
Sequence:
MFGKRKKRVEISAPSNFEHRVHTGFDQHEQKFTGLPRQWQSLIEESARRPKPLVDPACITSIQPGAPKTIVRGSKGAKDGALTLLLDEFENMSVTRSNSLRRDSPPPPARARQENGMPEEPATTARGGPGKAGSRGRFAGHSEAGGGSGDRRRAGPEKRPKSSREGSGGPQESSRDKRPLSGPDVGTPQPAGLASGAKLAAGRPFNTYPRADTDHPSRGAQGEPHDVAPNGPSAGGLAIPQSSSSSSRPPTRARGAPSPGVLGPHASEPQLAPPACTPAAPAVPGPPGPRSPQREPQRVSHEQFRAALQLVVDPGDPRSYLDNFIKIGEGSTGIVCIATVRSSGKLVAVKKMDLRKQQRRELLFNEVVIMRDYQHENVVEMYNSYLVGDELWVVMEFLEGGALTDIVTHTRMNEEQIAAVCLAVLQALSVLHAQGVIHRDIKSDSILLTHDGRVKLSDFGFCAQVSKEVPRRKSLVGTPYWMAPELISRLPYGPEVDIWSLGIMVIEMVDGEPPYFNEPPLKAMKMIRDNLPPRLKNLHKVSPSLKGFLDRLLVRDPAQRATAAELLKHPFLAKAGPPASIVPLMRQNRTR
Protein: Bifunctional pinoresinol-lariciresinol reductase (PLR-Lc1) ((+)-lariciresinol reductase) (EC 1.23.1.2) ((+)-pinoresinol reductase) (EC 1.23.1.1) (B5KRH5)
Organism: Linum corymbulosum (Linum) (Linum strictum subsp. corymbulosum)
Function: Reductase involved in lignan (-)-hinokinin biosynthesis. Catalyzes the enantioselective conversion of (+)-pinoresinol into (+)-lariciresinol and of (+)-lariciresinol into (-)-secoisolariciresinol. Abstracts the 4R-hydride from the NADPH cofactor during catalysis. Has also a low phenylcoumaran benzylic ether reductase activity.
Interaction partners:
Sequence:
MGSLNESSKVLVIGGTGYLGKRLVKASLDAGHDTYVMHRPEIGVDIEKVQLLLSFKMQGAHLVSASFDDHRSLVDAVSLVDVVICAISGVHIRSHQILLQLKLVQAIKEAGNVKRFLPSEFGTDPARMGDAMEPGRVTFDDKMVVRRAIEEAAIPFTYVSANCFAGYFLGGLCQPGSILPSRDHVTLLGDGNQKGVYVDENDIAAYTLKAIDDPRTLNKTLYIKPPKNILSQRQVVGIWEKHIGKQLHKTLLSEQDFLAAMKEQDYAEQVGLTHYYHVCYEGCLTNFEVEQDQEASKLYPDVRYTTVEEYLKRYV
Protein: Fanconi-associated nuclease (EC 3.1.4.1) (A0A590UKC0)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus {ECO:0000256|RuleBase:RU365033}.
Interaction partners:
Sequence:
MTKLEYEEIALDLTPVIEELTNAGFLQTESELQELSEVLELLSAPELKSLAKTFHLVNPNGQKQQLVDAFLKLAKQRSVCTWGKNKPGIGAVILKRAKALAGQSVRICKGPRAVFSRILLLFSLTDSMEDEDAACGGQGQLSTVLLVNLGRMEFPSYTINRKTHIFQDRDDLIRYAAATHMLSDISSAMANGNWEEAKELAQCAKRDWNRLKNHPSLRCHEDLPLFLRCFTVGWIYTRILSRFVEILQRLHMYEEAVRELESLLSQRIYCPDSRGRWWDRLALNLHQHLKRLEPTIKCITEGLADPEVRTGHRLSLYQRAVRLRESPSCKKFKHLFQQLPEMAVQDVKHVTITGRLCPQRGMCKSVFVMEAGEAADPTTVLCSVEELALAHYRRSGFDQGIHGEGSTFSTLYGLLLWDIIFMDGIPDVFRNACQAFPLDLCTDSFFTSRRPALEARLQLIHDAPEESLRAWVAATWHEQEGRVASLVSWDRFTSLQQAQDLVSCLGGPVLSGVCRHLAADFRHCRGGLPDLVVWNSQSRHFKLVEVKGPNDRLSHKQMIWLAELQKLGAEVEVCHVVAVGAKSQSLS
Protein: Uncharacterized protein C19orf47 (Q8N9M1)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MVMAALSLVAACWGRAAADESVQLPAAPGSSVRARETMVSVTMATSEWIQFFKEAGIPPGPAVNYAVMFVDNRIQKSMLLDLNKEIMNELGVTVVGDIIAILKHAKVVHRQDMCKAATESVPCSPSPLAGEIRRGTSAASRMITNSLNHDSPPSTPPRRPDTSTSKISVTVSNKMAAKSAKATAALARREEESLAVPAKRRRVTAEMEGKYVINMPKGTTPRTRKILEQQQAAKGLHRTSVFDRLGAETKADTTTGSKPTGVFSRLGATPETDEDLAWDSDNDSSSSVLQYAGVLKKLGRGPAKASPQPALTVKAKATSSATTAAAPTLRRLALSSRSGLERKPESLSKVSIIKRLGAAALVPEAQDSQVTSTKSKSSAEVKVTIKRTLVGPRGSSSSEGLGAQMDHAGTVSVFKRLGRRTF
Protein: Helix-loop-helix protein 3 (Q22717)
Organism: Caenorhabditis elegans
Function: Probable transcriptional regulator. May mediate transcriptional activation by binding to the E-box motif 5'-CANNTG-3'. Plays a role in the differentiation of the hermaphrodite-specific motor neurons (HSN) that are required for normal egg laying. Might play a role in serotonin production by regulating expression of the tryptophan hydrolase tph-1 which catalyzes serotonin synthesis, in the HSN neurons. Also plays a role in HSN axon guidance towards the vulva and the ventral nerve cord, possibly by promoting the expression of the netrin receptor unc-40. Under feeding conditions, involved in the regulation of the srh-234 chemoreceptor encoding gene expression in the ADL sensory neurons. Together with hlh-2, involved in the induction of programmed cell death in the sister cells of the serotonergic neurosecretory motor (NSM) neurons, probably through the activation of egl-1 transcription.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00981, ECO:0000269|PubMed:18586090}.
Interaction partners:
- Helix-loop-helix protein hlh-2
Sequence:
MTASTSSTPSTSTKIPSSSKSSVTKQTKQKRNERERKRVDQVNQGFVLLQERVPKAAGNKAKLSKVETLREAARYIQELQKQLGMSSTSFHNSMPADFPTPEQSPVYPQSVCSMMAQTPSPSYTSPYYPPPQMMSSNQHDMSSHYYQESSSSSASTSGDHHSFYSHTETY
Protein: FI19405p1 (GATAd, isoform A) (GATAd, isoform B) (GATAd, isoform C) (Q9VKZ0)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- Zinc finger protein ush
- GATAe, isoform A
Sequence:
MNNVPHKFRQVCRLCLTLVNECDVAVLQIYDNSSHNNSAPDRISADFRGVANRANCFCSALSPNPCSCIVDNPLSANKNERRNQGTPVPVPIPIPVSVPVPVPSQQIQSQTLHHHQNQTKIHYTPSVPSAADAKSSERERQCQLESDIAERSTVFKSQSSSDHEHIEYSGETPSPSASLSQSQTKSEPMREEEEHQHNHNQQSGREETSVNTTNISGTDNYGKEHGRDDSSSPHLTFQIFNCLSIKALPNDGLPNVVCGDCRQKLDSFEKFRTMAHNSQIALKEFLNISKNLRPDPNDLETKLDAILKASSEAIAAKALTELSTFSKVKYDHSKLDSSIQPGLDRKIEISNQEMPAHSLYPSLFKSITMKSDQKSKAMSGSSHSQFDSKLQKDSDIEKYENLQQQLETAAVLMDISKKIVISPPCSNPQSPCFSAAVDTSIKSSVIKSKRPSNQNEIQDGVEIDLSVKKQKNDYSNQRNAAPIHHFCQTPMLDIQSHLRSEEDFQNYSITINQVGGSDFKSKAPKASTGSLLDSGDSSDSHKLEMDITSSINDRKTPDSLSSDHATDAATTQLWQALARSAAKSKEDNPASQIFRNMMSQPFAFPVPSTVSFTKVPEEPIALLKDLSEAQSSKSKPCRRKQSFPTKTDCIDVVNENVTDTYTTSEATPDDKKDKRNINLFNAIPGAQKDMSCSNCGTLTTTIWRRSVRGEMVCNACGLYFKLHGVNRPHSMRRDTIHTRRRRPKELERSKKKHKQMSSCSSIETTKQDFLTARESLAISGLVLNKFKKEIDDTETPAAAALKDILSRRKKSNSLPAFNDTCESADLSAPLNLVSSENNAKLT
Protein: Metastasis associated 1 (E7ESY4)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MAANMYRVGDYVYFENSSSNPYLIRRIEELNKTANGNVEAKVVCFYRRRDISSTLIALADKHATLSVCYKAGPGADNGEEGEIEEEMENPEMVDLPEKLKHQLRHRELFLSRQLESLPATHIRGKCSVTLLNETESLKSYLEREDFFFYSLVYDPQQKTLLADKGEIRVGNRYQADITDLLKEGEEDGRDQSRLETQVWEAHNPLTDKQIDQFLVVARSVGTFARALDCSSSVRQPSLHMSAAAASRDITLFHAMDTLHKNIYDISKAISALVPQGGPVLCRDEMEEWSASEANLFEEALEKYGKDFTDIQQDFLPWKSLTSIIEYYYMWKTTDRYVQQKRLKAAEAESKLKQVYIPNYNKPNPNQISVNNVKAGVVNGTGAPGQSPGAGRACESCYTTQSYQWYSWGPPNMQCRLCASCWTYWKKYGGLKMPTRLDGERPGPNRSNMSPHGLPARSSGSPKFAMKTRQAFYLHTTKLTRIARRLCREILRPWHAARHPYLPINSAAIKAECTARLPEASQSPLVLKQAVRKPLEAVLRYLETHPRPPKPDPVKSVSSVLSSLTPAKVAPVINNGSPTILGKRSYEQHNGVDGLANHGQARHMGPSRNLLLNGKSYPTKVRLIRGGSLPPVKRRRMNWIDAPDDVFYMATEETRKIRKLLSSSETKRAARRPYKPIALRQSQALPPRPPPPAPVNDEPIVIED
Protein: 1,8-cineole 2-endo-monooxygenase (EC 1.14.14.133) (cytochrome P450) (CYP176A1) (P450cin) (Q8VQF6)
Organism: Citrobacter braakii
Function: Involved in the degradation of cineol (eucalyptol). Catalyzes the initial hydroxylation of cineole exclusively at the pro-R carbon to give the (S)-6beta-hydroxycineole. Cineole is the natural substrate of CinA.
Interaction partners:
Sequence:
MTATVASTSLFTTADHYHTPLGPDGTPHAFFEALRDEAETTPIGWSEAYGGHWVVAGYKEIQAVIQNTKAFSNKGVTFPRYETGEFELMMAGQDDPVHKKYRQLVAKPFSPEATDLFTEQLRQSTNDLIDARIELGEGDAATWLANEIPARLTAILLGLPPEDGDTYRRWVWAITHVENPEEGAEIFAELVAHARTLIAERRTNPGNDIMSRVIMSKIDGESLSEDDLIGFFTILLLGGIDNTARFLSSVFWRLAWDIELRRRLIAHPELIPNAVDELLRFYGPAMVGRLVTQEVTVGDITMKPGQTAMLWFPIASRDRSAFDSPDNIVIERTPNRHLSLGHGIHRCLGAHLIRVEARVAITEFLKRIPEFSLDPNKECEWLMGQVAGMLHVPIIFPKGKRLSE
Protein: Altered inheritance rate of mitochondria protein 25 (P47140)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Subcellular location: Mitochondrion {ECO:0000269|PubMed:16823961}.
Interaction partners:
Sequence:
MHRTAIFLTYRSCMRNFSTLSKTLTVSSGKVIRNGPFRRVIREKNQITKAPSVKAFKENSNSGIIKVHDPIATTILNEPTVIIERQIEFMNVFLGFEQANRYAIMDVNGNKIASMMERDFSITKAIMRQFYRLHRPFLVDVFDNWGNVIMTIKRPFSFINSHIKTIIPPSAYVDNGSDSTHYHDGKEGTTVGETIQNWHLWRRRYELFQKDGVEGSTFDQFGKIDAPFLSFDFPVTDADGKIMASVDRNWVGLGREMFTDTGVYVVRFDSQRCFDNIYPTEMLSSQVLTLDQRAVLLANAVSIDFDYFSRHSRQTGGFLSFGGGYDE
Protein: Gelsolin (ADF) (Actin-depolymerizing factor) (G1U9R8)
Organism: Oryctolagus cuniculus (Rabbit)
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000256|ARBA:ARBA00004245, ECO:0000256|RuleBase:RU367130}.
Interaction partners:
Sequence:
MPLDVPSSMVVEHPEFLKAGKQPGLQIWRVEKFDLVPVPPNLYGDFFMGDAYVILKTVQLRNGNLQYDLHYWLGNECSQDESGAAAIFTVQLDDYLNGRAVQHRETQGFESATFLGYFKSGLKYKKGGVASGFKHVVPNEVVVQRLLQVKGRRVVRATEVPVSWDSFNNGDCFILDLGNDIYQWCGSKSNKFERLKATQVSKGIRDNERSGRAQVHVSEEGSEPEGMLQLLGPRPALPEGTDDTAKEDAANRKLAKLYKVSNGAGTMSVSLVADENPFAQGALKSEDCFILDHGSDGKIYVWKGKQANMEERKAALKTASDFISKMNYPKQTQVSVLPDGGETPLFKQFFKNWRDPDQTDGPGLAYLSSHIAHVERVPFDAATLHTSTAMAAQHGMDDDGTGQKQIWRIEGSNKVPVDPATYGQFYGGDSYIILYNYRHGGRQGQIIYNWQGAQSTQDEVAASAILTAQLDEELGGTPVQSRVVQGKEPAHLMSLFGGKPMIIYKGSTSREGGQTAPASTRLFQVRASSSGATRAVEVIPKAGALNSNDAFVLKTPSAAYLWVGAGASEAEKTGAQELLRVLRAQPVQVAEGSEPDGFWEALGGKAAYRTSPRLKDKKMDAHPPRLFACSNKIGRFVIEEVPGELMQEDLATDDVMLLDTWDQVFVWVGKDSQEDEKTEALTSAKRYIETDPANRDRRTPITVVKQGFEPPSFVGWFLGWDDNYWSVDPLDRALAELAA
Protein: Glutamine--tRNA ligase (EC 6.1.1.18) (Glutaminyl-tRNA synthetase) (GlnRS) (P47897)
Organism: Homo sapiens (Human)
Function: Glutamine--tRNA ligase. Plays a critical role in brain development.
Subcellular location: Cytoplasm, cytosol {ECO:0000269|PubMed:19289464}. Cytoplasm {ECO:0000269|PubMed:10791971, ECO:0000269|PubMed:24656866}.
Interaction partners:
- Methionine--tRNA ligase, cytoplasmic
- Aspartate--tRNA ligase, cytoplasmic
- Leucine--tRNA ligase, cytoplasmic
- Lysine--tRNA ligase
- Bifunctional glutamate/proline--tRNA ligase
- Aminoacyl tRNA synthase complex-interacting multifunctional protein 2
- Isoleucine--tRNA ligase, cytoplasmic
- Probable arginine--tRNA ligase, mitochondrial
- Aminoacyl tRNA synthase complex-interacting multifunctional protein 1
- Arginine--tRNA ligase, cytoplasmic
Sequence:
MAALDSLSLFTSLGLSEQKARETLKNSALSAQLREAATQAQQTLGSTIDKATGILLYGLASRLRDTRRLSFLVSYIASKKIHTEPQLSAALEYVRSHPLDPIDTVDFERECGVGVIVTPEQIEEAVEAAINRHRPQLLVERYHFNMGLLMGEARAVLKWADGKMIKNEVDMQVLHLLGPKLEADLEKKFKVAKARLEETDRRTAKDVVENGETADQTLSLMEQLRGEALKFHKPGENYKTPGYVVTPHTMNLLKQHLEITGGQVRTRFPPEPNGILHIGHAKAINFNFGYAKANNGICFLRFDDTNPEKEEAKFFTAICDMVAWLGYTPYKVTYASDYFDQLYAWAVELIRRGLAYVCHQRGEELKGHNTLPSPWRDRPMEESLLLFEAMRKGKFSEGEATLRMKLVMEDGKMDPVAYRVKYTPHHRTGDKWCIYPTYDYTHCLCDSIEHITHSLCTKEFQARRSSYFWLCNALDVYCPVQWEYGRLNLHYAVVSKRKILQLVATGAVRDWDDPRLFTLTALRRRGFPPEAINNFCARVGVTVAQTTMEPHLLEACVRDVLNDTAPRAMAVLESLRVIITNFPAAKSLDIQVPNFPADETKGFHQVPFAPIVFIERTDFKEEPEPGFKRLAWGQPVGLRHTGYVIELQHVVKGPSGCVESLEVTCRRADAGEKPKAFIHWVSQPLMCEVRLYERLFQHKNPEDPTEVPGGFLSDLNLASLHVVDAALVDCSVALAKPFDKFQFERLGYFSVDPDSHQGKLVFNRTVTLKEDPGKV
Protein: Single-stranded nucleic acid-binding protein (P10080)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Functions in the transition of mRNAs from translation to an mRNP complex destined for decapping. High-copy-number suppressor of decapping defects. Overexpression suppresses decapping defects in both DCP1-2 and DCP2-7 mutations. Acts to promote translational repression of mRNA in conjunction with DHH1 and subsequent mRNA localization to P bodies. Promotes translational repression of mRNA during glucose deprivation.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16782896, ECO:0000269|PubMed:23222640}. Nucleus, nucleolus {ECO:0000269|PubMed:16782896, ECO:0000269|PubMed:2121740}. Cytoplasm, P-body {ECO:0000269|PubMed:16782896, ECO:0000269|PubMed:23222640}. Cytoplasm, Stress granule {ECO:0000269|PubMed:23222640}.
Interaction partners:
- Eukaryotic initiation factor 4F subunit p150
- H/ACA ribonucleoprotein complex subunit CBF5
- Polyadenylate-binding protein, cytoplasmic and nuclear
- Protein arginine N-methyltransferase 1
- Zinc finger protein GIS2
- Eukaryotic initiation factor 4F subunit p130
- Eukaryotic translation initiation factor 4E
- Protein SCD6
- Pumilio homology domain family member 6
- ATP-dependent RNA helicase DHH1
Sequence:
MSAEIEEATNAVNNLSINDSEQQPRAPTHKTVIDPEDTIFIGNVAHECTEDDLKQLFVEEFGDEVSVEIPIKEHTDGHIPASKHALVKFPTKIDFDNIKENYDTKVVKDREIHIKRARTPGQMQRGGFRGRGGFRGRGGFRGGFRGGYRGGFRGRGNFRGRGGARGGFNGQKREKIPLDQMERSKDTLYINNVPFKATKEEVAEFFGTDADSISLPMRKMRDQHTGRIFTSDSANRGMAFVTFSGENVDIEAKAEEFKGKVFGDRELTVDVAVIRPENDEEEIEQETGSEEKQE
Protein: APC/C-CDH1 modulator 1 (Q08981)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Negative regulator of GDH1, the activator protein that regulates the ubiquitin ligase activity and substrate specificity of the anaphase promoting complex/cyclosome (APC/C), and which is required for exit from mitosis, cytokinesis and formation of prereplicative complexes in G1.
Interaction partners:
- APC/C activator protein CDH1
- APC/C activator protein CDC20
- Cyclin-dependent kinase 1
- Protein BMH1
- Protein BMH2
- Tyrosine-protein phosphatase CDC14
- Anaphase-promoting complex subunit DOC1
- G2/mitotic-specific cyclin-3
- S-phase entry cyclin-5
- Anaphase-promoting complex subunit MND2
Sequence:
MISPSKKRTILSSKNINQKPRAVVKGNELRSPSKRRSQIDTDYALRRSPIKTIQISKAAQFMLYEETAEERNIAVHRHNEIYNNNNSVSNENNPSQVKENLSPAKICPYERAFLREGGRIALKDLSVDEFKGYIQDPLTDETIPLTLPLGDKKISLPSFITPPRNSKISIFFTSKHQGQNPETKISRSTDDVSEKKVVRKLSFHVYEDE
Protein: Actin-related protein T3 (ARP-T3) (Actin-related protein M1) (Q8BXF8)
Organism: Mus musculus (Mouse)
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000250}. Cytoplasm {ECO:0000269|PubMed:18692047}. Nucleus {ECO:0000269|PubMed:18692047}. Note=The localization changes from the peripheral region to inside the nucleus during differentiation from round to elongated spermatid.
Interaction partners:
- Leucine-rich repeat and IQ domain-containing protein 4
- Profilin-3
- Myoneurin
- Dynactin subunit 2
- Leucine-rich repeat-containing protein 34
- Actin-related protein 10
Sequence:
MSGYQPPVVIDNGSGMIKAGLAGTREPQFVYPNILGRSKGHTADSRQELCVGDQAQERRSFLSISYPVERGLISSWGDMEIMWKHIYDYNLNLNASDGPVLVTEPALNPLADRQHISEVFFENLGVPAFYMSAQAVLALFAAGFTTGLVLNSGAGITQCVPIFEGYCLSHGVKQLNVAGSDLTSYLMMLLKGDGIMLLRTGDRKVVTDIKENACYVAMNYEDEMTKDSNLEKIYTLPDGKTVKLHKQLFHCPEALFSPYLVNVDAPGIDKMCFGSIMKCDTDLRNSFFSNIILSGGSTSFPGLDKRLIKDVAKLAPANTAVQVIAPPERKISVWMGGSILASLSAFQDMWITAAEFEEVGPNIVHQRCF
Protein: Small toxic polypeptide LdrA (P0DPD0)
Organism: Escherichia coli (strain K12)
Function: Toxic component of a type I toxin-antitoxin (TA) system. Inhibits ATP synthesis possibly due to its insertion in the cell inner membrane, ATP levels drop over 50% 2 minutes after induction. Overexpression is toxic leading to cell death, it inhibits cell growth within 30 minutes; C-terminally tagged versions of the protein are toxic while N-terminally tagged versions are not.
Subcellular location: Cell inner membrane {ECO:0000269|PubMed:24513967}; Single-pass membrane protein {ECO:0000305|PubMed:24513967}.
Interaction partners:
- Small toxic polypeptide LdrB
- Small toxic polypeptide LdrD
- Prophage tail fiber assembly protein homolog TfaQ
- H repeat-associated putative transposase YbfD
- Prophage tail fiber assembly protein homolog TfaR
Sequence:
MTLAQFAMIFWHDLAAPILAGIITAAIVSWWRNRK
Protein: Recombination signal binding protein for immunoglobulin kappa J region (A0A8I6AL64)
Organism: Rattus norvegicus (Rat)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MAWIKRKFGERPPPKRLTREAMRNYLKERGDQTVLILHAKVAQKSYGNEKRFFCPPPCVYLMGSGWKKKKEQMERDGCSEQESQPCAFIGIGNSDQEMQQLNLEGKNYCTAKTLYISDSDKRKHFMLSVKMFYGNSDDIGVFLSKRIKVISKPSKKKQSLKNADLCIASGTKVALFNRLRSQTVSTRYLHVEGGNFHASSQQWGAFYIHLLDDDESEGEEFTVRDGYIHYGQTVKLVCSVTGMALPRLIIRKVDKQTALLDADDPVSQLHKCAFYLKDTERMYLCLSQERIIQFQATPCPKEQNKEMINDGASWTIISTDKAEYTFYEGMGPVLAPVTPVPVVESLQLNGGGDVAMLELTGQNFTPNLRVWFGDVEAETMYRCGESMLCVVPDISAFREGWRWVRQPVQVPVTLVRNDGIIYSTSLTFTYTPEPGPRPHCSAAGAILRANSSQVPTNESNTNSEGNYTNASTNSTSVTSSTATVVS
Protein: H-2 class I histocompatibility antigen, TLA(B) alpha chain (MHC thymus leukemia antigen) (P14432)
Organism: Mus musculus (Mouse)
Function: Involved in the presentation of foreign antigens to the immune system.
Subcellular location: Membrane; Single-pass type I membrane protein.
Interaction partners:
- Beta-2-microglobulin
- T-cell surface glycoprotein CD8 alpha chain
- Tapasin
- Class II histocompatibility antigen, M alpha chain
- H-2 class II histocompatibility antigen, A-B alpha chain
- Natural killer cells antigen CD94
- H2-O alpha
- Protein disulfide-isomerase A3
- Histocompatibility 2, O region beta locus
- H2-M beta 2
Sequence:
MRMGTPVPGTLLILLAASQGQTQTCPGSHSLRYFYTALSRPAISEPWYIAVGYLDDTQFVRFNSSGETATYKLSAPWVEQEGPEYWARETEIVTSNAQFFRENLQTMLDYYNLSQNGSHTIQVMYGCEVEFFGSLFRAYEQHGYDGPDYIALNEDLKTWTAADTAAEITRSKWEQAGYTELRRTYLEGPCKDSLLRYLENRKKTQECTDPPKTHVTHHPRPEGYVTLRCWALRFYPADITLTWQLNGEELIQDTELVETRPAGDGTFQKWAAVVVPLGKEQKYTCHVYHEGLPEPLTLRWEPPQTSMPNRTTVRALLGAMIILGFMSGSVMMWMRKNNGGNGDDNTAAYQNEREHLSLDPRAESEALGVEAGMKDLPSAPPLVS
Protein: Hapless 2 (Generative cell specific-1) (Q4YCF6)
Organism: Plasmodium berghei (strain Anka)
Function: During fertilization, required on male gametes for their fusion with female gametes, and for subsequent ookinete formation in the host. Thereby, required for mosquito-mediated transmission to other animals. Probably initiates the fusion of gamete cell membranes by inserting part of its extracellular domain into the cell membrane of a female gamete.
Subcellular location: Cell membrane {ECO:0000269|PubMed:29212032, ECO:0000305|PubMed:18367645, ECO:0000305|PubMed:21209845}; Single-pass type I membrane protein {ECO:0000269|PubMed:29212032, ECO:0000305|PubMed:18367645, ECO:0000305|PubMed:21209845}.
Interaction partners:
Sequence:
MKNKLINLRSKHIYKLIIIIFFCIILKYYKWCDFKNKVFFIQLVYSFAKKSVCTSSLDDSTCHTVTFGELDVSNNSVVRLKVMRKGGKGYFLTIRRDYVTVSYYLKYVKDIPLEFREIIDIFNNHKFEQYTQEQINKYTYTCNVRKIEDIDKYDEKNPTKFHEYTRGEACRCQTYNYFKDDEFIKRAKLKCIYYNMLFTESATVYSRHCPIIDLMHFAVYDIEYPPIFNTIVNITIEEYYYNDVSSVLNNKSDLVTKEKKYQLNDTITEIRDDYFDLWLFLKGETHGKRTLVNLSNDYIVIPSSPINNRDVIASDITRNCGLSQNSPLLKGCNYSSICNIMHPCLRKAMMLPKYMFDLSGKTCGKLGVSLNTWRKSEGNFCGSEAGYCISNNLKKYYDIHNSASIKDGISLSKYKIKNIYNSEPQTKIYESYKLPDYLKDKIKNNNHAEMDENDLDNKIFYKPNVAAHSQFIDYKYNGNHSVEIKFETDAIEVYEIRPVSIATITHVTIPNDCASNNSNSNECVLIIHVWNNSKFVGSNFSCSIACTNKETDQLASHINPIAPVRAFIGPNKNYAFYFIIKFLINKEITTLCKAIVKDSNGKECSIEEFELQSKESVHIVESEVDETTDQVVVEHHTQSPDIKNPDEYVCKCTINLLCYVINFKTCSNYYINTVKTLIGKFAIIAILIILAPALIPLLPFFLNFFFLFISTILKLYQSIISTIGQIRIRNNDKPIIYKKKIHDMKTNYLSVSSYSSLSDSSSIYSTDSVSSMRKNKKKFNKNNISSNIKHKKGGKKVKQKEPNRNSNHTSHEYADTSPSGKSKIPPLR