lhallee/plat_data huggingface dataset:
The following text describes a protein:
Function:
Cyclic nucleotide phosphodiesterase with specificity for the second messengers cAMP and cGMP, which are key regulators of many important physiological processes. Also has activity toward cUMP (By similarity). Independently of its catalytic activity it is part of an E2/17beta-estradiol-induced pro-apoptotic signaling pathway. E2 stabilizes the PDE3A/SLFN12 complex in the cytosol, promoting the dephosphorylation of SLFN12 and activating its pro-apoptotic ribosomal RNA/rRNA ribonuclease activity. This apoptotic pathway might be relevant in tissues with high concentration of E2 and be for instance involved in placenta remodeling (By similarity).
Subcellular Localization:
Membrane; Multi-pass membrane protein. Cytoplasm, cytosol.
Sequence:
MAVRGEAAQDLAKPGLGGASPARVARGNHRHRGESSPSPRGSGCCWRALALQPLRRSPQLSSALCAGSLSVLLALLVRLVGGEVGGELEKSQEAAAEEEEEEGARGGVFPGPRGGAPGGGAQLSPWLQPAALLFSLLCAFFWMGLCLLRAGVRLPLAVALLAACCAGEALVQLSLGVGDGRLLSLPAAGVLLSCLGGATWLVLRLRLGVLMVAWTSVLRTVALVSLERFKVAWRPYLAYLAAVLGLLLARYAEQILPQCSGPAPPRERFGSQLSARTKEEIPGWKRRRRSSSVVAGEMSGCSGKSHRRTSLPCIPREQLMGHSEWDHKRGPRGSQSGTSITVDIAVMGEAHGLITDLLADPSLPPNVCTSLRAVSNLLSTQLTFQAIHKPRVNPTVTFSENYTCSDSEEGLEKDKQAISKRLRRSLPPGLLRRVSSTWTTTTSATGLPTLEPAPVRRDRSASIKPHEAPSPSAVNPDSWNAPGLTTLTKSRSFTSSYAVSAANHVKAKKQNRPGGLAKISPVPSPSSSPPQGSPASSPVSNSASQQFPESPEVTIKRGPGSHRALTYTQSAPDLSPQIPPPSVICSSCGRPYSQGNPADGPSERSGPAMLKPNRTDDTSQVTSDYETNNNSDSSDILQNEEEAECQREPQRKASACGTYTSQTMIFLDKPILAPEPLVMDNLDSIMDQLNTWNFPIFDLMENIGRKCGRILSQVSYRLFEDMGLFEAFKIPVREFMNYFHALEIGYRDIPYHNRIHATDVLHAVWYLTTQPIPGLPSVIGDHGSASDSDSDSGFTHGHMGYVFSKMYHVPDDKYGCLSGNIPALELMALYVAAAMHDYDHPGRTNAFLVATSAPQAVLYNDRSVLENHHAAAAWNLFMSRPEYNFLVNLDHVEFKHFRFLVIEAILATDLKKHFDFVAKFNAKVNDDVGIDWTNENDRLLVCQMCIKLADINGPAKCKELHLRWTEGIASEFYEQGDEEASLGLPISPFMDRSAPQLANLQESFISHIVGPLCHSYDSAGLMPGKWVDDSDDSGDTDDPEEEEEEAETPHEDEACESSIAPRKKSFKRRRIYCQITQHLLQNHMMWKKVIEEEQCLSGTENQSLDQVPLQHPSEQIQAIKEEEEEKGKPRAEETLAPQPDL
The following text describes a protein:
Function:
A helicase with DNA-dependent ATPase activity. Unwinds DNA duplexes with 3'-5' polarity. Translocates on single-stranded DNA with 3'-5' polarity. Initiates unwinding more efficiently from a nicked substrate than double-stranded DNA. Involved in the post-incision events of nucleotide excision repair and methyl-directed mismatch repair, and probably also in repair of alkylated DNA (Probable).
Sequence:
MDVSYLLDSLNDKQREAVAAPRSNLLVLAGAGSGKTRVLVHRIAWLMSVENCSPYSIMAVTFTNKAAAEMRHRIGQLMGTSQGGMWVGTFHGLAHRLLRAHHMDANLPQDFQILDSEDQLRLLKRLIKAMNLDEKQWPPRQAMWYINSQKDEGLRPHHIQSYGNPVEQTWQKVYQAYQEACDRAGLVDFAELLLRAHELWLNKPHILQHYRERFTNILVDEFQDTNNIQYAWIRLLAGDTGKVMIVGDDDQSIYGWRGAQVENIQRFLNDFPGAETIRLEQNYRSTSNILSAANALIENNNGRLGKKLWTDGADGEPISLYCAFNELDEARFVVNRIKTWQDNGGALAECAILYRSNAQSRVLEEALLQASMPYRIYGGMRFFERQEIKDALSYLRLIANRNDDAAFERVVNTPTRGIGDRTLDVVRQTSRDRQLTLWQACRELLQEKALAGRAASALQRFMELIDALAQETADMPLHVQTDRVIKDSGLRTMYEQEKGEKGQTRIENLEELVTATRQFSYNEEDEDLMPLQAFLSHAALEAGEGQADTWQDAVQLMTLHSAKGLEFPQVFIVGMEEGMFPSQMSLDEGGRLEEERRLAYVGVTRAMQKLTLTYAETRRLYGKEVYHRPSRFIGELPEECVEEVRLRATVSRPVSHQRMGTPMVENDSGYKLGQRVRHAKFGEGTIVNMEGSGEHSRLQVAFQGQGIKWLVAAYARLESV
The following text describes a protein:
Function:
The 2-oxoglutarate dehydrogenase complex catalyzes the overall conversion of 2-oxoglutarate to succinyl-CoA and CO(2). It contains multiple copies of three enzymatic components: 2-oxoglutarate dehydrogenase (E1), dihydrolipoamide succinyltransferase (E2) and lipoamide dehydrogenase (E3).
Subcellular Localization:
Mitochondrion matrix.
Sequence:
MAWQRLLAAASRPGLRSARSLAARGFHAVGASAAPRAAESWSRVNHRSLGVLGSFGSRSIHGTGEKLQAAPIPQAVALSKLTDNFLDGTSSVYLEELQRAWEADPKSVDPSWDLFFRNFTGVADSAPGLSGQTIQESMRLLLLVRAYQVNGHMKAKLDPLGLDVRTPPVELDPALYGFTDADLDREFFLGVWRMAGFLSENRPVQTLRAILARLEQAYCGTIGYEYMHIPDREKCNWLRDQIETQVPGKYGSTRRAQILDRLVWGTNFESFIAQKWTAAKRFGLEGCETLIPGMKELIDYAADRGVENVVIGMPHRGRLNVLGNVVRKPLRQIFSEFSGGIKPPNEAGGYTGSGDVKYHLGTSYDRPTRSGKRIHLSLVANPSHLEAVSPVVIGKTRAKQYYSNDKDRGKNMAVLLHGDGSFSGQGVVYETLHLSDLPNYTTGGTIHLVVNNQVAFTTDPKSSRSSPYCTDVAKALNAPIFHVNGDDVEAVVHACELAAEWRCKFKSDVVVDIVCYRRFGHNEIDEPSFTQPKMYQVIRSHPTSLEIYEKKLVESGQLTQEEIKSIENRVFEILNDEFNNSKDYVPRTRDWLAAYWAGFKGPEQLSRIRNTGVKPEILKSVGKSLSTIPPDFSPHRAIKRIYEQRAQMIETGQGVDWATAEALAFATLLVEGNHVRLSGQDVERGTFSHRHSVLHDQQTGAKYCPLDHVMMDQEDEMFTVSNSSLSEFGVLGFELGYSMENPNSLVLWEAQFGDFANGAQVIFDQFLSSGEAKWLRQAGLVCLLPHGYDGQGPEHSSARLERYLQMSDDNPYVIPEMDPSLRKQIQEVNWQVVNVTTPANYFHVLRRQIHRDFRKPLIVMSPKNLLRHAACKSNLSEFDDVQGHDGFDKQGTRFKRLIKDYNFDSTREESVRRMILCSGKVYYELDDERQRSQLKDLAICRVEQLCPFPWDLILREINRYPNAEVVWCQEEPMNMGAYSYIAPRLATALRSAGRGSFEDIKYVGRPPSAATATGFGSMHVEEQKELLHKALQEAPIINGLSKAHSPLSA
The following text describes a protein:
Function:
Catalyzes the cleavage of L-kynurenine (L-Kyn) and L-3-hydroxykynurenine (L-3OHKyn) into anthranilic acid (AA) and 3-hydroxyanthranilic acid (3-OHAA), respectively.
Subcellular Localization:
Cytoplasm.
Sequence:
MANDVLFLGNSPKGILEDLAKEKGVTVFDEKLCEILDKNDELGHLKNEFCIPKVEPKCGKYGRDSWIDFCSNAVGRQPKKTKEMVLEMLEEWQNRTPFTATTTKMLGYDNLLLGGIGRLVGADPDEVAIMNSLTVNLNFLLISFYNPTKQRFKIIIERGAFPTTFYACESHVLQRGFKPEDSLVYWEPRPESKLLNTSDILDMIEREGDSVAVVLLCGVQYLTGQLLDMKVITAAAHAKGCKVGYDLAQGIGNVELHLHDWNVDFAVWGHHKFMNSCAGATGGAFMHKKHENNNFPKLLGWWGHSENTRFDFTSDHDFSPGIKGYHNSNPSVINLACIAASLEVYGKITMQDFRKKSILLNCYLESLLEPNLNKYGMNIITPSDYQQRGCQLSITFTKSFDIMPPCLLSHGVICVVSLGVLRVSPNPLHTSFRDVYRFVQALFQILDDLTEP
The following text describes a protein:
Function:
Specifically methylates the guanine-2535 in 23S ribosomal RNA. Confers resistance to antibiotic avilamycin, an orthosomycin antibiotic.
Sequence:
MSAYRHAVERIDSSDLACGVVLHSAPGYPAFPVRLATEIFQRALARLPGDGPVTLWDPCCGSGYLLTVLGLLHRRSLRQVIASDVDPAPLELAAKNLALLSPAGLTARELERREQSERFGKPSYLEAAQAARRLRERLTAEGGALPCAIRTADVFDPRALSAVLAGSAPDVVLTDLPYGERTHWEGQVPAQPVAGLLRSLASALPAHAVIAVTDRSRKIPVAPVKALERLKIGTRSAVLVRAADVLEAGP
The following text describes a protein:
Function:
Serine protease inhibitor which exhibits antifibrinolytic, antielastolytic and antimicrobial activities (By similarity). Displays antimicrobial activity against bacteria and fungi (By similarity). Likely functions in the innate immune response to microbial infection and possibly in the venom, as an antifibrinolytic agent (By similarity). Induces hyperalgesia and edema mediated by leukotrienes when injected into mice. Does not induce hemolytic activity, mast cell degranulation, or chemotactic activity for polymorphonucleated leukocytes (PMNL).
Subcellular Localization:
Secreted.
Sequence:
MKNYSKNATYLITVLLFSFVTMLLIIPSKCEAVSNDMQPLEARTADLVQQPRYIIDVPPRCPPGSKFVHKRCRVIVP
The following text describes a protein:
Function:
Single-stranded DNA-dependent ATP-dependent helicase. Involved in non-homologous end joining (NHEJ) DNA double strand break repair. DNA-binding is sequence-independent but has a high affinity to nicks in double-stranded DNA and to the ends of duplex DNA. Binds to naturally occurring chromosomal ends, and therefore provides chromosomal end protection. Required also for telomere recombination to repair telomeric ends in the absence of telomerase. ku70, of the ku70/ku80 heterodimer, binds to the stem loop of tlc1, the RNA component of telomerase. Required for mating-type switching (By similarity). Involved in telomere maintenance. Interacts with telomeric repeats and subtelomeric sequences thereby controlling telomere length and protecting against subtelomeric rearrangement. Maintains telomeric chromatin, which is involved in silencing the expression of genes located at the telomere.
Subcellular Localization:
Nucleus. Chromosome, telomere.
Sequence:
MENDEQIDETENFAIGKYAILFVIEVSPSMLDPVDEFTPSSLQMALICAYQLAAQRVITNPSDIMGVLLYGTESSTGRFANQMMLLDIDPPDAERIKSLQSFEKDFQFSKEKFKPCSCQVSLSSVLYHCSVIFTTKAENFEKRLFLITDNDHPAWDATERDIILQRAKDLRDLDIQVHPVFLDPPTHSFRINIFYSDFLYIVYGRQDVSNLVNRGQAQLQHMLNMITALQKPKRAHFHLKMDLGNDVRIGVEAFILLKRLESAKTNWVYAKGERFAVAVPQSKQVSFATKKELKKDEIRRSYSYGGSSVVFGSDELNKVRSFEPPTLRIIGFRDFSTLKPWHCLKPAVFLRPKDDEIIGSGAVFSAIHKKLLASNKIGIAWFVSRPNANPCFVAMLATPGSIHIRDDFELPLGIFLVQLPTADDIRSLPPINPNPISMPSNLIETMQRILRGMELRSYQPGKYNNPSLQWHYKVLQALALDEEIPTDFVDNTLPKYKAIQKRVGEYMGDVNNIVAEYRNDISDKNGIKEEEEDQGPIVKKARIEKSGKPIFAEDDRLKQLYIEGVLDKEIKALKVSQLKDILRDRGLRVSGKKADLLDNLTNYVKKL
The following text describes a protein:
Function:
Probable transcription repressor that functions as a negative regulator of phytochrome-mediated promotion of seed germination. Inhibits seed germination by regulating the expression of gibberellic acid (GA) and abscisic acid (ABA) metabolic genes. Does not regulate the expression of the DELLA genes RGA and RGA1. Activated by PIL5, a phytochrome-interacting basic helix-loop-helix transcription factor. Represses directly JMJ20 and JMJ22 expression in the absence of red light (R) and in far-red (FR) conditions.
Miscellaneous:
MISCELLANEOUS: Plants lacking SOM germinate in darkness, independently of various light regimens.
Subcellular Localization:
Nucleus.
Sequence:
MDVVCTEHQMRKPTVEIPPRKLLLSSKSFPSDSSSPRSPRKHNWNKSNKITSEHEEDNEDNNRENKEYCYDSDSDDPYASDHFRMFEFKIRRCTRSRSHDWTDCPFAHPGEKARRRDPRRFQYSGEVCPEFRRGGDCSRGDDCEFAHGVFECWLHPIRYRTEACKDGKHCKRKVCFFAHSPRQLRVLPPENVSGVSASPSPAAKNPCCLFCSSSPTSTLLGNLSHLSRSPSLSPPMSPANKAAAFSRLRNRAASAVSAAAAAGSMNYKDVLSELVNSLDSMSLAEALQASSSSPVTTPVSAAAAAFASSCGLSNQRLHLQQQQPSSPLQFALSPSTPSYLTNSPQANFFSDDFTPRRRQMNDFTAMTAVRENTNIEDGSCGDPDLGWVNDLLT
The following text describes a protein:
Function:
Confers freeze tolerance. Binds to the surface of ice crystals and inhibits their growth. Has low thermal hysteresis (TH) activity, which is the ability to lower the freezing point of an aqueous solution below its melting point. The TH activity of this protein is approximately 0.2 degrees Celsius at 50 uM and 0.3 degrees Celsius at 400 uM.
Subcellular Localization:
Secreted.
Sequence:
MSLLSIITIGLAGLGGLVNGQRDLSVELGVASNFAILAKAGISSVPDSAILGDIGVSPAAATYITGFGLTQDSSTTYATSPQVTGLIYAADYSTPTPNYLAAAVANAETAYNQAAGFVDPDFLELGAGELRDQTLVPGLYKWTSSVSVPTDLTFEGNGDATWVFQIAGGLSLADGVAFTLAGGANSTNIAFQVGDDVTVGKGAHFEGVLLAKRFVTLQTGSSLNGRVLSQTEVALQKATVNSPFVPAPEVVQKRSNARQWL
The following text describes a protein:
Function:
Conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles.
Sequence:
MPHFKFYYFDVRGRGEAIRLLFHLADEKFDDERFGMEQWGVLKSEMPLGQVPVLEIDGVKISQTTAIARYLGHQFHRAGTNAVDCARLDMIAEVIQEFMSSSGMGKFSRVLLGMIQANKEQFFKENVLPDVEKYAPIVEKFLLENGNNGLLLGDRETWVDVFAAESFSKLIDYGSPDALDAYPHILALINRVFNHPNIKKYVSQRKATPA
The following text describes a protein:
Function:
Involved in membrane remodeling.
Subcellular Localization:
Endoplasmic reticulum membrane; Multi-pass membrane protein. Vacuole membrane; Multi-pass membrane protein.
Sequence:
MEKTEESVGIRVYTTTTTQNPSPTSSRSPKPVPLSSLPMLPAGAAAGGGKGRKRRMVAKGVQKTVSKTSMLVNFLPTGTLLMFEMVLPTIYRDGDCNGINTLMIHLLLLLCAMSCFFFHFTDSFKASDGKIYYGFVTPRGLAVFMKPPSPGFGGGDVIAEKEIPVTDERYKLRVNDFVHSVMSVLVFMAIAFSDRRVTGCLFPGKEKEMDQVMESFPLMVGIVCSALFLVFPTSRYGVGCMST
The following text describes a protein:
Function:
TFIIIC mediates tRNA and 5S RNA gene activation by binding to intragenic promoter elements. Upstream of the transcription start site, TFIIIC assembles the initiation complex TFIIIB-TFIIIC-tDNA, which is sufficient for RNA polymerase III recruitment and function. Part of the tauA domain of TFIIIC that binds boxA DNA promoter sites of tRNA and similar genes. Sfc4 is the TFIIIB assembling subunit of TFIIIC.
Subcellular Localization:
Nucleus.
Sequence:
MIQNGGNSYVDSNMNETQNDTTDNFDAEMQDLNGYISEIVDEARNVSEVDAKFLGDTSALQAEGLWSDEESDYEGSDDESNFSKTASRTEDDIANEEWEENLKAVAGFRKVRKGHKGRGRVSRADMLPSVEVQQMLSLANHLFAQEGNFDEAQKLAEEIVRIDNNVIAAWKMLGECHRQRGNGRVNIEKCLIAWMAAAHLKPKDHELWFTCAKLSESLEFWDQADYCYNRAVSAKPPNKSELKKYIWNRSVLNKEHGSLKKAAEGFKFLLQSSPYNASILKNLAEIYIKIHAPREILKQFEIAWKYFYQYPAPPIGNDIFDLPTLNLYAELLLLDHQWSNLIRLINRGVRWFRGRKSESFWDEFDDDREWDVDERRREFPNASEEHTNKEAYLLPHLFRTKLGIARLKTGELPEAELHFSVIKNLPPDYAWGMLYDIAKAYMDIERLDLALEYFVLICNHEPAQNIGLWYNMGVCYLELKEYEHAQQCMEAILIVDNSNTNALIKLAEINELQDNRDAALEIVTNIFEQRRNINELEREQSQNEDHEKNVGSQLFVGNQKVPQDKWEKRARISRSKEEARQFTIWKTEETQRRFHKLDILRQSLKKEENVSESLNEWLAIASELIDEFVSIKAFFPSEKKARARAGLLTRRTRYASLNDQLTSMINRLNDSLTRTKYGDLDLDTILRTGYFRNVSIDAWYQLFVEFSLRLTKVGSVQQAYDVLTTAMGAILFDQDTIKRQNLRWCMLACSMYARDPQGALTPLRWVFTTFQFRQDTYRLFSAVLSQGYECSRAFVDSANQKFLLRLIKLMDQLMSNSLVSGAATLVKNDDGLATVPTSYDPVLVLLYGHIMARNRSWIPAINYYSRAFAINPDCPITNLSLGLAYLHRAMQRLSDNRHYQILQGFTFLYRYYDLRVNEGLGEKQEALYNLGKAYHFIGLEHYAVKYYEAVLGLSPMSQGDKMTSSESTVSTTYDFGFEAAYNLRLIYICSGNIKLAFQISSKYLIF
The following text describes a protein:
Function:
Probable disulfide isomerase, which participates in the folding of proteins containing disulfide bonds. May act as a dithiol oxidase. Acts as a regulator of endoplasmic reticulum-mitochondria contact sites via its ability to regulate redox signals.
Subcellular Localization:
Endoplasmic reticulum membrane; Single-pass membrane protein.
Sequence:
MSPNSMWIFGLISALLLTLGSTGLSSKVLELSDRFIDVRHEGQWLVMFYAPWCGYCKKTEPIFALVAQALHATNVRVGRLDCTKYPAAAKEFKVRGYPTIMFIKGNMEFTYNGDRGRDELVDYALRMSGPPVQLVTRTESVDMLKGSHTIFFIFVGQQEGVVWDTYYAAAEGYQEHGFFYATSEDIAAQHFDFEKLPAVIVYKEEQHHFYPHGHLAHEMDPNEVNETVFQWVNVERFTLFPKVTRFNIHQLLKTNKYLVLAVVQEDKLNQIATHELEFRDMVEGVIRKHRARYHDKFQFGWIGEPSIAHSIILDQLPTPHLIAINSSTQHHFIPEDDPMQMTPQALHLFLESIRNESAIAYGGDTYFVRLNRALFEVRRALRDMWLGNPVLTTVIFGLPLGFLSLIMYSIFCGDCLVTEEDPDEDHEKKE
The following text describes a protein:
Function:
Catalyzes the NADPH-dependent reduction of ketopantoate into pantoic acid.
Sequence:
MSPKARVLLVGAGGIGTIAALNLERGGLAEVTCVLRSNYEAVRSRGIEIISCEHGHIKNWRPTAVLNVIPRVCSEDHSTLFDYIVCTTKNIPGVTPSICETIAPAVRPGHTVIVLIQNGLNIEKPFLSRFPQNVILSGVSRCDAHEIAHGVIEQKEDDDLHIAAFHNPLLDQETQQKAAEQFVQIYGAGGKTNVRHEPNWERDRWSKLVYNATLNPICALTGVNTGDLQIAGGAFDRLVIPAMQEVVKVSKAVGVELPDDIIETTIRKNPVERKIAPSMQKDMEKGNLLEHENLIGEVVREAQKQGVAIPVLSVLYELCSAIQWRVAKERGMRIA
The following text describes a protein:
Function:
In association with mitochondrial contact site and cristae organizing system (MICOS) complex components and mitochondrial outer membrane sorting assembly machinery (SAM) complex components may regulate mitochondrial dynamics playing a role in determining mitochondrial length, distribution and motility.
Subcellular Localization:
Cytoplasm. Mitochondrion. Mitochondrion outer membrane. Note=Associates with the outer mitochondrion membrane, most likely through its C-terminus. Not integrated into the mitochondrial outer membrane.
Sequence:
MNSSTSTMSEEPDALSVVNQLRDLAADPLNRRAIVQDQGCLPGLILFMDHPNPPVVHSALLALRYLAECRANREKMKGELGMMLSLQNVIQKTTTPGETKLLASEIYDILQSSNMADGDSFNEMNSRRRKAQFFLGTTNKRAKTVVLHIDGLDDTSRRNLCEEALLKIKGVISFTFQMAVQRCVVRIRSDLKAEALASAIASTKVMKAQQVVKSESGEEMLVPFQDTPVEVEQNTELPDYLPEDESPTKEQDKAVSRVGSHPEGGASWLSTAANFLSRSFYW
The following text describes a protein:
Function:
Sigma factors are initiation factors that promote the attachment of RNA polymerase to specific initiation sites and are then released.
Subcellular Localization:
Cytoplasm.
Sequence:
MSLVMKILRKPKIEDIVCNIQNNEEDKEAFIVQYQPFIRKSISSVCRRYITEQDDEYSIGLFAFNEAIEQYSYTKGKSFLAFADLLIKRDVIDYIRKESKHNFVFLKEDEQEEMLEMQVSLTEYMKEMENSNRKEEILHFQSVLAEFKITFSELAKESPKHRDTREHLIEIVKIIIKEEEMMEELFRKKKLPLKHIEPRVRVSRKTLERHRKYIIAMCIIFANNYTYILDYIRGEKHDE
The following text describes a protein:
Function:
Involved in autophagic vesicle formation.
Subcellular Localization:
Preautophagosomal structure membrane; Peripheral membrane protein.
Sequence:
MEIGYMEVPNIKDINSNIEKSGLVLCVSLNQKESESLISPSYYYIYVHRYMYLSNIIPKCLEFFKSFILPFYGNKFGVYFECIKKEQKKSSNNNNNNNNNITYTSTNNYEEKIVLDWRLPIGVLFDIYCDLDKSQKEYIKTYEKFNDTNINMNNKKNITICSNNELFLNHINIVKLKGTDKNYDKKSNERQNQKNIYDANRNISTNTNNSSNVNHQQNCDRTDDDTLHKGDDILHKGDDILHKGDDILHKGDDILHKGDDILYKGNDILHKGDDILHKGDDILHTDAFINEKETKEGTDKKKQINRNIKNEERERGKEVKNIIVENYYEENYMKEKKIIVENGKGSTKNDVEENKKDINTHYDDIKLNNVDIYDDIKLNNVDIYDDTADFQYIQFIQNEKINNEWYNKQFVNISNKNIPWMLIVHFKGEEEYPLSIINKKYDEKNTHFKGDINILPYNNYIPLYKGFNNFEEYIINQLKKANCILNKNNRALEILPQRIQKDILYSLKHFHIEKICSLYREYIDYNMLNFINYFNNSYIKKVQQVCDLNRHKDNSIQINGKSSGKQNEENLCLLKMDLHEEESPVKITHCKDILNNDNENYDNENNNNENNNEHNCHRNSYDVHLNENFINDQSQKNHISNIRTSYNNDHVSDSLQTDIQNDFSSIILENTKEQGDHINFKNNLHNNEKYPNVYDILKDEKVLKDCPIILHIYGPPYNQILTKYPFLKLIHSNNNNNNNNNDNKDNNNNSNKYDGCKKYIQNVHLNTLGDFLHEQLPSFVRKIINKDEKNETSHILNKYDKDKYLNSETIYYFIEDDYLIFSPYMFIIVNGIQIPLNTPLYWLAANFSQFDHFLHITIRIPPY
The following text describes a protein:
Function:
Polycomb group (PcG) protein that specifically binds histone H3 trimethylated at 'Lys-36' (H3K36me3) and recruits the PRC2 complex, thus enhancing PRC2 H3K27me3 methylation activity. Regulates the transcriptional networks during embryonic stem cell self-renewal and differentiation. Promotes recruitment of the PRC2 complex to the inactive X chromosome in differentiating XX ES cells and PRC2 recruitment to target genes in undifferentiated ES cells. Required to repress Hox genes by enhancing H3K27me3 methylation of the PRC2 complex. In some conditions may act as an inhibitor of PRC2 activity: able to activate the CDKN2A gene and promote cellular senescence by suppressing the catalytic activity of the PRC2 complex locally. Binds to the metal-regulating-element (MRE) of MT1A gene promoter.
Subcellular Localization:
Nucleus.
Sequence:
MRDSTGAGNSLVHKRSPLRRNQKTPTSLTKLSLQDGHKVKKPACKFEEGQDVLARWSDGLFYLGTIKKINILKQSCFIIFEDSSKSWVLWKDIQTGATGSGEMVCTICQEEYSEAPNEMVICDKCGQGYHQLCHTPHIDSSVIDSDEKWLCRQCVFATTTKRGGALKKGPNAKALQVMKQTLPYSVADLEWDAGHKTNVQQCYCYCGGPGDWYLKMLQCCKCKQWFHEACVQCLQKPMLFGDRFYTFICSVCSSGPEYLKRLPLQWVDIAHLCLYNLSVIHKKKYFDSELELMTYINENWDRLHPGELADTPKSERYEHVLEALNDYKTMEVSNGIEKKGKKKSVGRPPGPYTRKMIQKTAEPPLDKESISENPTLDLPCSIGRTEGTAHSSNTSDVDFTGASSAKETTSSSISRHYGLSDSRKRTRTGRSWPAAIPHLRRRRGRLPRRALQTQNSEIVKDDEGKEDYQFDELNTEILNNLADQELQLNHLKNSITSYFGAAGRIACGEKYRVLARRVTLDGKVQYLVEWEGATAS
The following text describes a protein:
Function:
Transcriptional repressor. Acts as a component of the histone deacetylase NuRD complex which participates in the remodeling of chromatin. Enhances MBD2-mediated repression. Efficient repression requires the presence of GATAD2B.
Subcellular Localization:
Nucleus speckle. Nucleus. Chromosome. Note=Speckled nuclear localization requires both CR1 and CR2 regions. Localizes to sites of DNA damage in a manner partially dependent on ZMYND8.
Domain:
Both CR1 and CR2 regions are required for speckled nuclear localization.
Sequence:
MSEEACRTRSQKRTLEPDLTEDDVENKKMKMEKGSSELTVDGDSRVMPEPSAGSAQGLLRTTEAMGTGSGEGLLGDGPVDMRTSHSDMKSEKRPPSPDVIVLSDSEQPSSPRVNGLTTVALKDTSTEALLKSSPEERERMIKQLKEELRLEEAKLVLLKKLRQSQIQKEATAQKPTASSGSTVTTPPPLVRGTQNIPAGKTSLQTSSTRIPGSIIPPPLVRGGQQVSAKLGPQASSQVVMPPLVRGAQIHNIRQHSSTGPPPLLLAPRASVPSMQIQGQRIIQQGLIRVANVPNTSLLVNIPQPTAASMKGTAVASAQANSTPTSVASVVASAESPASRQAAAKLALRKQLEKTLLEIPPPKPPAPEMNFLPSAANNEFIYLVGLEEVVQNLLETQAGRISATAAAAVLSREPYMCVQCKTDFTCRWREKGGAVMCENCMTSNQKKALKVEHTSRLKAAFVKALQQEQEMEQRLLQQGVGTASIKAEPAAPHPTLKQVIKPRRKLAFRSGEARVWNNGSSLQASSQLSRGSATAPRGVLHTFSQSPKLQNAASATALVSRTGRHSERVVGTGKGTASNWKKTPLSTGGTLAFVSPSLAVHKTSSAVDRQREYLLDMIPPRSIPQSATWK
The following text describes a protein:
Function:
Functions as an intracellular leucine sensor that negatively regulates the mTORC1 signaling pathway through the GATOR complex. In absence of leucine, binds the GATOR subcomplex GATOR2 and prevents mTORC1 signaling. Binding of leucine to SESN2 disrupts its interaction with GATOR2 thereby activating the TORC1 signaling pathway. This stress-inducible metabolic regulator also plays a role in protection against oxidative and genotoxic stresses. May negatively regulate protein translation in response to endoplasmic reticulum stress, via mTORC1. May positively regulate the transcription by NFE2L2 of genes involved in the response to oxidative stress by facilitating the SQSTM1-mediated autophagic degradation of KEAP1. May also mediate TP53 inhibition of TORC1 signaling upon genotoxic stress. Moreover, may prevent the accumulation of reactive oxygen species (ROS) through the alkylhydroperoxide reductase activity born by the N-terminal domain of the protein. Was originally reported to contribute to oxidative stress resistance by reducing PRDX1. However, this could not be confirmed.
Subcellular Localization:
Cytoplasm.
Domain:
The N-terminal domain has an alkylhydroperoxide reductase activity; The C-terminal domain mediates interaction with GATOR2 through which it regulates TORC1 signaling.
Sequence:
MIVADSECRAELKDYLRFAPGGVGDSGPGEEQRESRARRGPRGPSAFIPVEEVLREGAESLEQHLGLEALMSSGRVDNLAVVMGLHPDYFTSFWRLHYLLLHTDGPLASSWRHYIAIMAAARHQCSYLVGSHMAEFLQTGGDPEWLLGLHRAPEKLRKLSEINKLLAHRPWLITKEHIQALLKTGEHTWSLAELIQALVLLTHCHSLSSFVFGCGILPEGDADGSPAPQAPTPPSEQSSPPSRDPLNNSGGFESARDVEALMERMQQLQESLLRDEGTSQEEMESRFELEKSESLLVTPSADILEPSPHPDMLCFVEDPTFGYEDFTRRGAQAPPTFRAQDYTWEDHGYSLIQRLYPEGGQLLDEKFQAAYSLTYNTIAMHSGVDTSVLRRAIWNYIHCVFGIRYDDYDYGEVNQLLERNLKVYIKTVACYPEKTTRRMYNLFWRHFRHSEKVHVNLLLLEARMQAALLYALRAITRYMT
The following text describes a protein:
Function:
Functions redundantly with tsp-14 isoform a to regulate body size, embryonic and vulva development. Functions redundantly with tsp-14 (isoforms a and b) to regulate cell fate specification in the postembryonic mesodermal M lineage and male development. May regulate BMP-like Sma/Mab signaling by mediating protease sup-17 trafficking to the cell surface. Together with tsp-14, functions redundantly to maintain cell surface levels of the BMP type II receptor daf-4 (but not BMP type I receptor sma-6), probably by regulating endosomal sorting of receptors and their targeting to degradative lysosomes. Together with tsp-14 involved in maintaining the structural and functional integrity of the endosomal network. Together with tsp-14, probably acts by modulating the activation of glp-1, a Notch-like receptor, to regulate germline maturation. Probably acts by modulating the activation of lin-12, a Notch-like receptor, to regulate cell fate specification such as the anchor cell/ventral uterine precursor cell decision.
Subcellular Localization:
Cell membrane; Multi-pass membrane protein. Cytoplasmic vesicle membrane; Multi-pass membrane protein. Endosome membrane; Multi-pass membrane protein. Early endosome membrane; Multi-pass membrane protein. Late endosome membrane; Multi-pass membrane protein. Recycling endosome membrane; Multi-pass membrane protein. Golgi apparatus, trans-Golgi network membrane; Multi-pass membrane protein. Note=Often in close juxtaposition to the retromer but not part of it, suggesting separate microdomains of the same endosome.
Sequence:
MANRRQPVQHRAQQRVYRQSQIRYAPGAGGESEISCCVKYSVFSFNVIFFLLGFGLLLFGVWAQIEKNTFVNMLSKASKLYLDPTWPLLIVGFLTFIIGFSGCVGSLRENTSFLTFYSTLLGLLLIAEFSAGVFAYACRDQLDNYIRNLLNDVVVGYRDDPDLQLLIDSMQETWMCCGINGADDWDRNTYFSIEAREVASPEAGGVPFSCCINSSKLEFKNYFCGHGVRLKPESHMAAHLAAQRVMAHTASIYTEGCLPKLQLWLNNNMLLVAVSMVIIAIIQVLGICFAQNLKSDILAQRAKWYYTH
The following text describes a protein:
Function:
GPI inositol-deacylase that catalyzes the remove of the acyl chain linked to the 2-OH position of inositol ring from the GPI-anchored protein (GPI-AP) in the endoplasmic reticulum. Initiates the post-attachment remodeling phase of GPI-AP biogenesis and participates in endoplasmic reticulum (ER)-to-Golgi transport of GPI-anchored protein; Involved in inositol deacylation of GPI-anchored proteins which plays important roles in the quality control and ER-associated degradation of GPI-anchored proteins.
Subcellular Localization:
Endoplasmic reticulum membrane; Multi-pass membrane protein.
Sequence:
MAAQNKILCCLVVALLGLGIYDVLTNFESNRCAMSFMWETPEYIDVLHMNETLQEKYPHYSLTVYGEGRYATNLEKGKYTGIPILFIPGNAGSHKQVRSLSSIALRKASDKYNFHFNYFSVDLDEELNAVYGGVLEGQTEYVHACVKHILELYKNNKNPPKQVVIIGHSKGGLVAKALFALPDFDASTVNTLITMGTPHVNAIVKPDIYMDQFTTSVNEFWSENWDSAELQDVTVLSIGGSYRDNMVRSGLVSMNGMVSPDRGLSVVVGSIPRVWLSTDHRCIVWCKELVLATNRALFDMVDKLTKQISVNPEYRMKVLNHHFVSHDGQSSYTPHTEDVVGFADENFKAISSGFHHVAGRHIEKAVHYTFPINPSDPNHALFTVTATIPSTSGWLYACTRSHEDRCIEGVDITRRARLMPPLKSNMRVAHLDLKNLGIDNVKQIVVKIPKTNKVNVIADLHGRSGRIMNATLPGFFSYKPKTVMKQHDSHTLFFNISLPDLDSVWKAYTAILEPAHCADPVRKDGNTTLHFHVPWYQEDEWSVAKATENNVMPLKLQSGRPADDLRSVQLHAYVYSRCHYRLRIAVSHREIPGQLMRFYGNLLPSFVVVVALLVVSFSLNNLVMQKPVESYIMTQSTHCKPFIVVPFITMLRKIIPHIYAPLDEADNFKVLDDQGINFGMLPIVFFVFGYGILTILAGLLEMDVLFFGKILSLVKGTSIDADSTPYTGSLGYSLLLYAILGGLMAVCVGSCGAVVLLVLVVLYLLKVVALQARVLVLKGCLNLTNDAIEKDKDVKEIEQEKDGKEIEKEKDGNEEETSVKSQEDETAASTAEPSPPTPPSPPTPLDVAQTSLHFHFALMVLTLLLALLNIPSLAFWVKNMQHDIYNLERDPALYPTLVVIAALTVLLDPAYTIPKKGLITKGLSWIVHAFTLIALLYASDAMYRLSYLLASAIFLVAVNQVMPL