lhallee/plat_data huggingface dataset:
The following text describes a protein:
Function:
One of five 2-oxo acid decarboxylases (PDC1, PDC5, PDC6, ARO10, and THI3) involved in amino acid catabolism. The enzyme catalyzes the decarboxylation of amino acids, which, in a first step, have been transaminated to the corresponding 2-oxo acids (alpha-keto-acids). In a third step, the resulting aldehydes are reduced to alcohols, collectively referred to as fusel oils or alcohols. Its preferred substrates are the transaminated amino acids derived from phenylalanine (phenylpyruvate), tryptophan (3-(indol-3-yl)pyruvate), and probably tyrosine (4-hydroxyphenylpyruvate), but also isoleucine ((3S)-3-methyl-2-oxopentanoate, also alpha-keto-beta-methylvalerate) and methionine (4-methylthio-2-oxobutanoate), whereas transaminated leucine (4-methyl-2-oxopentanoate, also alpha-keto-isocaproate) is a low efficiency substrate and transaminated valine and pyruvate are no substrates. In analogy to the pyruvate decarboxylases the enzyme may in a side-reaction catalyze condensation (or carboligation) reactions leading to the formation of 2-hydroxy ketone, collectively called acyloins.
Miscellaneous:
MISCELLANEOUS: Present with 6560 molecules/cell in log phase SD medium.
Subcellular Localization:
Cytoplasm.
Sequence:
MAPVTIEKFVNQEERHLVSNRSATIPFGEYIFKRLLSIDTKSVFGVPGDFNLSLLEYLYSPSVESAGLRWVGTCNELNAAYAADGYSRYSNKIGCLITTYGVGELSALNGIAGSFAENVKVLHIVGVAKSIDSRSSNFSDRNLHHLVPQLHDSNFKGPNHKVYHDMVKDRVACSVAYLEDIETACDQVDNVIRDIYKYSKPGYIFVPADFADMSVTCDNLVNVPRISQQDCIVYPSENQLSDIINKITSWIYSSKTPAILGDVLTDRYGVSNFLNKLICKTGIWNFSTVMGKSVIDESNPTYMGQYNGKEGLKQVYEHFELCDLVLHFGVDINEINNGHYTFTYKPNAKIIQFHPNYIRLVDTRQGNEQMFKGINFAPILKELYKRIDVSKLSLQYDSNVTQYTNETMRLEDPTNGQSSIITQVHLQKTMPKFLNPGDVVVCETGSFQFSVRDFAFPSQLKYISQGFFLSIGMALPAALGVGIAMQDHSNAHINGGNVKEDYKPRLILFEGDGAAQMTIQELSTILKCNIPLEVIIWNNNGYTIERAIMGPTRSYNDVMSWKWTKLFEAFGDFDGKYTNSTLIQCPSKLALKLEELKNSNKRSGIELLEVKLGELDFPEQLKCMVEAAALKRNKK
The following text describes a protein:
Function:
IFN-induced dsRNA-dependent serine/threonine-protein kinase that phosphorylates the alpha subunit of eukaryotic translation initiation factor 2 (EIF2S1/eIF-2-alpha) and plays a key role in the innate immune response to viral infection. Inhibits viral replication via the integrated stress response (ISR): EIF2S1/eIF-2-alpha phosphorylation in response to viral infection converts EIF2S1/eIF-2-alpha in a global protein synthesis inhibitor, resulting to a shutdown of cellular and viral protein synthesis, while concomitantly initiating the preferential translation of ISR-specific mRNAs, such as the transcriptional activator ATF4. Exerts its antiviral activity on a wide range of DNA and RNA viruses including west nile virus (WNV), sindbis virus (SV), foot-and-mouth virus (FMDV), semliki Forest virus (SFV) and lymphocytic choriomeningitis virus (LCMV). Also involved in the regulation of signal transduction, apoptosis, cell proliferation and differentiation: phosphorylates other substrates including p53/TP53, PPP2R5A, DHX9, ILF3, and IRS1. In addition to serine/threonine-protein kinase activity, also has tyrosine-protein kinase activity and phosphorylates CDK1 at 'Tyr-4' upon DNA damage, facilitating its ubiquitination and proteasomal degradation (By similarity). Either as an adapter protein and/or via its kinase activity, can regulate various signaling pathways (p38 MAP kinase, NF-kappa-B and insulin signaling pathways) and transcription factors (JUN, STAT1, STAT3, IRF1, ATF3) involved in the expression of genes encoding pro-inflammatory cytokines and IFNs. Activates the NF-kappa-B pathway via interaction with IKBKB and TRAF family of proteins and activates the p38 MAP kinase pathway via interaction with MAP2K6 (By similarity). Can act as both a positive and negative regulator of the insulin signaling pathway (ISP) (By similarity). Negatively regulates ISP by inducing the inhibitory phosphorylation of insulin receptor substrate 1 (IRS1) at 'Ser-312' and positively regulates ISP via phosphorylation of PPP2R5A which activates FOXO1, which in turn up-regulates the expression of insulin receptor substrate 2 (IRS2) (By similarity). Can regulate NLRP3 inflammasome assembly and the activation of NLRP3, NLRP1, AIM2 and NLRC4 inflammasomes. Plays a role in the regulation of the cytoskeleton by binding to gelsolin (GSN), sequestering the protein in an inactive conformation away from actin.
Subcellular Localization:
Cytoplasm. Nucleus. Cytoplasm, perinuclear region.
Sequence:
MASDTPGFYMDKLNKYRQMHGVAITYKELSTSGPPHDRRFTFQVLIDEKEFPEAKGRSKQEARNAAAKLAVDILDNENKVDCHTSASEQGLFVGNYIGLVNSFAQKKKLSVNYEQCEPNSELPQRFICKCKIGQTMYGTGSGVTKQEAKQLAAKEAYQKLLKSPPKTAGTSSSVVTSTFSGFSSSSSMTSNGVSQSAPGSFSSENVFTNGLGENKRKSGVKVSPDDVQRNKYTLDARFNSDFEDIEEIGLGGFGQVFKAKHRIDGKRYAIKRVKYNTEKAEHEVQALAELNHVNIVQYHSCWEGVDYDPEHSMSDTSRYKTRCLFIQMEFCDKGTLEQWMRNRNQSKVDKALILDLYEQIVTGVEYIHSKGLIHRDLKPGNIFLVDERHIKIGDFGLATALENDGKSRTRRTGTLQYMSPEQLFLKHYGKEVDIFALGLILAELLHTCFTESEKIKFFESLRKGDFSNDIFDNKEKSLLKKLLSEKPKDRPETSEILKTLAEWRNISEKKKRNTC
The following text describes a protein:
Function:
Promotes microtubule growth, possibly through interactions with the microtubule end, and is important for establishing and maintaining polarized growth along the long axis of the cell. Acts as a kinesin motor protein that moves along microtubules and is required for proper localization of tea1 and tip1 to the cell tips and microtubules, respectively. ATPase activity stimulated via interaction with mal3.
Subcellular Localization:
Cytoplasm, cytoskeleton. Note=Localized in large clusters at cell tips and also in punctate dots within the cell that are coincident with the ends of cytoplasmic microtubules.
Sequence:
MSSSSSKPVNTGLVTPRRYSTMTGIRTGPSQSGTGSIPYSPTSPLSRNFSNYSIPMLRSNSTQTNVNGPTAFDLGVTEKLMSPGTLDRYTRPALYPSKDLDYLKNEYVNYESTTSQQTNSKGLKESNFVGSGIITSIRIRPIGKNQGVWSHGKLSNDPYGREYIRQQTSTSSSTIQQEYLFNNVFGMESKNYDIYKRSVKSVVRNVFSGYNGIVFAYGMTGTGKTYSMQGTENEPGIIPLAMNDLFEMVENNSDDDTFQIRISYLEIYNERIRDLIGNSDEEPRIRENASGEVNVTPLTRVLVTSPEEVSQVIEQCNAIRKTAATDFNTYSSRSHAILQVFLIRNNPTAHTSQISSLSLVDLAGSERASAHHERRKEGAFINKSLLTLGTVISRLSAAANPSLTSNSGHIPYRESKLTRLLQQSLSGQSQISLLATISIESNHTMETTNTLKFASRAQNLPQDIRQAEAVTNVQAELASLHSALEKNAQEVEYYASLVKQLTSDLEERDTYIAMLEAERSQGTAISRARLRMEELLSDHNFEIADLRDELQDKEQIIYALRYAQKQRDIADFNQSLAKFPHKILKKNVTRGSRSSSDQFSNETKTEILPDDQQQSKKDSVTQETQLLS
The following text describes a protein:
Function:
Potential multifunctional C-type lectin receptor that may play roles in endocytosis and phagocytosis as well as in cell adhesion and migration.
Subcellular Localization:
Cell projection, filopodium. Cytoplasm, cell cortex. Membrane; Single-pass type I membrane protein.
Sequence:
MLRAALPALLLPLLGLAAAAVADCPSSTWIQFQDSCYIFLQEAIKVESLEDVRNQCTDHGADMISIHNEEENAFILDTLKKQWKGPDDILLGMFYDTDDASFKWFDNSNMTFDKWTDQDNDEDLVDTCAFLHIKTGEWKKGNCEVSSVEGTLCKTAIPYKRKYLSDNHILISALVIASTVILTVLGAIIWFLYKKHSDSRFTTVFSTAPQSPYNEDCVLVVGEENEYPVQFD
The following text describes a protein:
Function:
Part of the phosphoribosylformylglycinamidine synthase complex involved in the purines biosynthetic pathway. Catalyzes the ATP-dependent conversion of formylglycinamide ribonucleotide (FGAR) and glutamine to yield formylglycinamidine ribonucleotide (FGAM) and glutamate. The FGAM synthase complex is composed of three subunits. PurQ produces an ammonia molecule by converting glutamine to glutamate. PurL transfers the ammonia molecule to FGAR to form FGAM in an ATP-dependent manner. PurS interacts with PurQ and PurL and is thought to assist in the transfer of the ammonia molecule from PurQ to PurL.
Subcellular Localization:
Cytoplasm.
Sequence:
MTARIGVVTFPGTLDDVDAARAARQVGAEVVSLWHADADLKGVDAVVVPGGFSYGDYLRAGAIARFAPVMDEVVAAADRGMPVLGICNGFQVLCEAGLLPGALTRNVGLHFICRDVWLRVASTSTAWTSRFEPDADLLVPLKSGEGRYVAPEKVLDELEGEGRVVFRYHDNVNGSLRDIAGICSANGRVVGLMPHPEHAIEALTGPSDDGLGLFYSALDAVLTG
The following text describes a protein:
Function:
Involved in the biosynthesis of a unique class of isonitrile lipopeptides (INLPs) that seem to function as virulence factors in M.tuberculosis and to play a role in metal acquisition. Catalyzes a Michael addition of glycine to the beta-position of an alpha,beta-unsaturated fatty acyl-[ACP], producing a (3R)-3-[(carboxymethyl)amino]fatty acid. Acts on the (2E)-decenoyl moiety loaded on the acyl-carrier protein (ACP) Rv0100, forming the product (3R)-3-[(carboxymethyl)amino]decanoate released from the ACP (By similarity). Displays thioesterase activity with a preference for long chain fatty acyl groups; in vitro, cleaves the thioester linkage of palmitoyl-CoA, stearoyl-CoA, lauroyl-CoA and hexanoyl-CoA. Contains low levels of trans-enoyl hydratase activity.
Sequence:
MSHTDLTPCTRVLASSGTVPIAEELLARVLEPYSCKGCRYLIDAQYSATEDSVLAYGNFTIGESAYIRSTGHFNAVELILCFNQLAYSAFAPAVLNEEIRVLRGWSIDDYCQHQLSSMLIRKASSRFRKPLNPQKFSARLLCRDLQVIERTWRYLKVPCVIEFWDENGGAASGEIELAALNIP
The following text describes a protein:
Function:
Required for formation of the RNA induced silencing complex (RISC). Component of the RISC loading complex (RLC), also known as the micro-RNA (miRNA) loading complex (miRLC), which is composed of DICER1, AGO2 and TARBP2. Within the RLC/miRLC, DICER1 and TARBP2 are required to process precursor miRNAs (pre-miRNAs) to mature miRNAs and then load them onto AGO2. AGO2 bound to the mature miRNA constitutes the minimal RISC and may subsequently dissociate from DICER1 and TARBP2. May also play a role in the production of short interfering RNAs (siRNAs) from double-stranded RNA (dsRNA) by DICER1. Binds in vitro to the PRM1 3'-UTR. Seems to act as a repressor of translation. For some pre-miRNA substrates, may also alter the choice of cleavage site by DICER1. Negatively regulates IRF7-mediated IFN-beta signaling triggered by viral infection by inhibiting the phosphorylation of IRF7 and promoting its 'Lys'-48-linked ubiquitination and degradation.
Subcellular Localization:
Cytoplasm. Cytoplasm, perinuclear region. Nucleus.
Sequence:
MSEEEQGSGITTGCGLPSIEQMLAANPGKTPISLLQEYGTRIGKTPVYDLLKAEGQAHQPNFTFRVTVGDTSCTGQGPSKKAAKHKAAEVALKHLKGGSMLEPALEDSSSFSPLDSSLPEDIPIFTAAAAATPVPSVVLTRSPPMELQPPVSPQQSECNPVGALQELVVQKGWRLPEYTVTQESGPAHRKEFTMTCRVERFIEIGSGTSKKLAKRNAAAKMLLRVHTVPLDARDGNEVEPDDDHFSIGVGSRLDGLRNRGPGCTWDSLRNSVGEKILSLRSCSLGSLGALGPACCRVLSELSEEQAFHVSYLDIEELSLSGLCQCLVELSTQPATVCHGSATTREAARGEAARRALQYLKIMAGSK
The following text describes a protein:
Function:
Probably not involved in the transport of molybdenum into the cell.
Subcellular Localization:
Cell inner membrane; Peripheral membrane protein.
Sequence:
MSSLQILQGTFRLSDTKTLQLPQLTLNAGDSWAFVGSNGSGKSALARALAGELPLLKGERQSQFSHITRLSFEQLQKLVSDEWQRNNTDMLGPGEDDTGRTTAEIIQDEVKDAPRCMQLAQQFGITALLDRRFKYLSTGETRKTLLCQALMSEPDLLILDEPFDGLDVASRQQLAERLASLHQSGITLVLVLNRFDEIPEFVQFAGVLADCTLAETGAKEELLQQALVAQLAHSEQLEGVQLPEPDEPSARHALPANEPRIVLNNGVVSYNDRPILNNLSWQVNPGEHWQIVGPNGAGKSTLLSLVTGDHPQGYSNDLTLFGRRRGSGETIWDIKKHIGYVSSSLHLDYRVSTTVRNVILSGYFDSIGIYQAVSDRQQKLVQQWLDILGIDKRTADAPFHSLSWGQQRLALIVRALVKHPTLLILDEPLQGLDPLNRQLIRRFVDVLISEGETQLLFVSHHAEDAPACITHRLEFVPDGGLYRYVLTKIY
The following text describes a protein:
Function:
Required for the formation of a threonylcarbamoyl group on adenosine at position 37 (t(6)A37) in tRNAs that read codons beginning with adenine. Is involved in the transfer of the threonylcarbamoyl moiety of threonylcarbamoyl-AMP (TC-AMP) to the N6 group of A37, together with TsaD and TsaE; this reaction does not require ATP in vitro. TsaB seems to play an indirect role in the t(6)A biosynthesis pathway, possibly in regulating the core enzymatic function of TsaD (By similarity).
Subcellular Localization:
Cytoplasm.
Sequence:
MNVLALDTSQRIRIGLRKGEDLFEISYTGEKKHAEILPVVVKKLLDELDLKVKDLDVVGVGIGPGGLTGLRVGIATVVGLVSPYDIPVAPLNSFEMTAKSCPADGVVLVARRARKGYHYCAVYLKDKGLNPLKEPSVVSDEELEEITKEFSPKIVLKDDLLISPAVLVEESERLFREKKTIHYYEIEPLYLQKSIAELNWEKKKRG
The following text describes a protein:
Function:
Functions as a two-component phosphorelay mediators between cytokinin sensor histidine kinases and response regulators (B-type ARRs). Plays an important role in propagating cytokinin signal transduction.
Subcellular Localization:
Cytoplasm, cytosol. Nucleus.
Domain:
Histidine-containing phosphotransfer domain (HPt) contains an active histidine that mediates the phosphotransfer.
Sequence:
MALPALKAQLQYSVQSMFDEGLLDGQFAQIQALQDESNPNFISEVITSFCNDAEKIITELNKHLTNEQNVDFFKLESRVHQLKGSSSSIGARRLKLACADLLQAFDCKNKGGCLEALNIITREYCLIGAKFQTLIQLEKRILAIESNQQQQDSYQATGSI
The following text describes a protein:
Function:
Promotes the exchange of Ras-bound GDP by GTP. This protein positively controls the level of cellular cAMP at start, the stage at which the yeast cell division cycle is triggered.
Miscellaneous:
MISCELLANEOUS: Present with 319 molecules/cell in log phase SD medium.
Subcellular Localization:
Membrane; Single-pass membrane protein.
Sequence:
MSDTNTSIPNTSSAREAGNASQTPSISSSSNTSTTTNTESSSASLSSSPSTSELTSIRPIGIVVAAYDFNYPIKKDSSSQLLSVQQGETIYILNKNSSGWWDGLVIDDSNGKVNRGWFPQNFGRPLRDSHLRKHSHPMKKYSSSKSSRRSSLNSLGNSAYLHVPRNPSKSRRGSSTLSASLSNAHNAETSSGHNNTVSMNNSPFSAPNDASHITPQSSNFNSNASLSQDMTKSADGSSEMNTNAIMNNNETNLQTSGEKAGPPLVAEETIKILPLEEIEMIINGIRSNIASTWSPIPLITKTSDYKLVYYNKDLDIYCSELPLISNSIMESDDICDSEPKFPPNDHLVNLYTRDLRKNANIEDSSTRSKQSESEQNRSSLLMEKQDSKETDGNNNSINDDDNNNENNKNEFNEAGPSSLNSLSAPDLTQNIQSRVVAPSRSSILAKSDIFYHYSRDIKLWTELQDLTVYYTKTAHKMFLKENRLNFTKYFDLISDSIVFTQLGCRLMQHEIKAKSCSKEIKKIFKGLISSLSRISINSHLYFDSAFHRKKMDTMNDKDNDNQENNCSRTEGDDGKIEVDSVHDLVSVPLSGKRNVSTSTTDTLTPMRSSFSTVNENDMENFSVLGPRNSVNSVVTPRTSIQNSTLEDFSPSNKNFKSAKSIYEMVDVEFSKFLRHVQLLYFVLQSSVFSDDNTLPQLLPRFFKGSFSGGSWTNPFSTFITDEFGNATKNKAVTSNEVTASSSKNSSISRIPPKMADAIASASGYSANSETNSQIDLKASSAASGSVFTPFNRPSHNRTFSRARVSKRKKKYPLTVDTLNTMKKKSSQIFEKLNNATGEHLKIISKPKSRIRNLEINSSTYEQINQNVLLLEILENLDLSIFINLKNLIKTPSILLDLESEEFLVHAMSSVSSVLTEFFDIKQAFHDIVIRLIMTTQQTTLDDPYLFSSMRSNFPVGHHEPFKNISNTPLVKGPFHKKNEQLALSLFHVLVSQDVEFNNLEFLNNSDDFKDACEKYVEISNLACIIVDQLIEERENLLNYAARMMKNNLTAELLKGEQEKWFDIYSEDYSDDDSENDEAIIDDELGSEDYIERKAANIEKNLPWFLTSDYETSLVYDSRGKIRGGTKEALIEHLTSHELVDAAFNVTMLITFRSILTTREFFYALIYRYNLYPPEGLSYDDYNIWIEKKSNPIKCRVVNIMRTFLTQYWTRNYYEPGIPLILNFAKMVVSEKIPGAEDLLQKINEKLINENEKEPVDPKQQDSVSAVVQTTKRDNKSPIHMSSSSLPSSASSAFFRLKKLKLLDIDPYTYATQLTVLEHDLYLRITMFECLDRAWGTKYCNMGGSPNITKFIANANTLTNFVSHTIVKQADVKTRSKLTQYFVTVAQHCKELNNFSSMTAIVSALYSSPIYRLKKTWDLVSTESKDLLKNLNNLMDSKRNFVKYRELLRSVTDVACVPFFGVYLSDLTFTFVGNPDFLHNSTNIINFSKRTKIANIVEEIISFKRFHYKLKRLDDIQTVIEASLENVPHIEKQYQLSLQVEPRSGNTKGSTHASSASGTKTAKFLSEFTDDKNGNFLKLGKKKPPSRLFR
The following text describes a protein:
Function:
Catalyzes the addition of a phosphoethanolamine moiety to the lipid A. The phosphoethanolamine modification is required for resistance to polymyxin.
Subcellular Localization:
Cell inner membrane; Multi-pass membrane protein.
Sequence:
MLKRLLKRPSLNLLAWLLLAAFYISICLNIAFFKQVLQALPLDSLHNVLVFLSMPVVAFSVINIVLTLSSFLWLNRPLACLFILVGAAAQYFIMTYGIVIDRSMIANIIDTTPAESYALMTPQMLLTLGFSGVLAALIACWIKIKPATSRLRSVLFRGANILVSVLLILLVAALFYKDYASLFRNNKELVKSLSPSNSIVASWSWYSHQRLANLPLVRIGEDAHRNPLMQNEKRKNLTILIVGETSRAENFSLNGYPRETNPRLAKDNVVYFPNTASCGTATAVSVPCMFSDMPREHYKEELAQHQEGVLDIIQRAGINVLWNDNDGGCKGACDRVPHQNVTALNLPDQCINGECYDEVLFHGLEEYINNLQGDGVIVLHTIGSHGPTYYNRYPPQFRKFTPTCDTNEIQTCTKEQLVNTYDNTLVYVDYIVDKAINLLKEHQDKFTTSLVYLSDHGESLGENGIYLHGLPYAIAPDSQKQVPMLLWLSEDYQKRYQVDQNCLQKQAQTQHYSQDNLFSTLLGLTGVETKYYQAADDILQTCRRVSE
The following text describes a protein:
Function:
The production of the second messenger molecules diacylglycerol (DAG) and inositol 1,4,5-trisphosphate (IP3) is mediated by activated phosphatidylinositol-specific phospholipase C enzymes.
Sequence:
MSCIPFRRTAKKKKEKPSFMRRMTTMKIASPSQPTSALFMASLLSSAQVFNAIHKPMYIHDAFKKHAVKVWKEARGSDKLLTHEKLLRFFEITQGVTTTALPVKDVYTFEEFFWAWSSNKAAWNAVRPLDPTEIDLTYPISNYFISSSHNTYLEGNQLSSKSSAEAYKAVLRNGCRCIEIDVWNGAPSRTPSKSPNGEHRRHISNVSAMSRTSVRHGSSLSVDQPGLYTMRTPRDSGTSLDPKELSDRMDRSTSSSSGSVKRGEPIVHHHGTMTTTVPFREVCKAVREEAFVTNHLPIIVSLEVGADREQQEMMVEIMKEEWAGLLLEEPFENCDRLTQQPRLEQLLDKILIKVKRLDDCNGEIQEAQRGRSLHVSSLRSKPPICEMLAALAIYTRSEHFNDVNSLASTTPSHIFSVNEDKFIDMISQDEALSKIMDHNRQYFMRIYPKGLRFDSSNPDPTIPWRRGVQMVAMNWQNTDEGTMLNDAMFADTNGWILKPTGFLKNQDEIPTKTVDLRITVLAGQSIPVPEGRQAKKLRTRVKVELHVENPDKARDLTRITQPQSTENPDWERNPHPLEFLGVSGVVEELSFVRFKVEEPSSSGFGNELLAWACIRLDRLQRGYRCLDLYHPLTRRPLRRHGGHSASQLFIRVEKNVRQGFPTNRTHAETAVGSK
The following text describes a protein:
Function:
mRNA decapping enzyme that specifically removes the nicotinamide adenine dinucleotide (NAD) cap from a subset of mRNAs by hydrolyzing the diphosphate linkage to produce nicotinamide mononucleotide (NMN) and 5' monophosphate mRNA. The NAD-cap is present at the 5'-end of some RNAs; in contrast to the canonical N7 methylguanosine (m7G) cap, the NAD cap promotes mRNA decay. Preferentially acts on NAD-capped transcripts in response to nutrient stress (By similarity). Also acts on free nicotinamide adenine dinucleotide molecules: hydrolyzes NAD(H) into NMN(H) and AMP, and NADPH into NMNH and 2',5'-ADP. May act to regulate the concentration of peroxisomal nicotinamide nucleotide cofactors required for oxidative metabolism in this organelle (By similarity). Regulates the levels of circadian clock components PER1, PER2, PER3 and CRY2 in the liver (By similarity).
Subcellular Localization:
Cytoplasm. Peroxisome. Cytoplasmic granule. Note=Localizes to cytoplasmic granules in the presence of BLMH.
Sequence:
MSSVKRTPKQEIVTQFHCSAAEGDIAKLTGILSHSPSLLNETSENGWTALMYAARNGHPEIVQFLLEKGCDRSIVNKSRQTALDIAVFWGYKHIANLLATAKGGKKPWFLTNEVEECENYFSKTLLDRKSEKRNNSDWLLAKESHPATVFILFSNLNPLVTLGGNKESFQQPEVRLCQLNYTDIKDYLAQPEKITLIFLGVELEIKDKLFNYAGEVPREEEDGLVAWFALGIDPIAAEEFKQRHENCYFLHPPMPALLQLKEKEAGVVAQARSVLAWYSRYKFCPTCGNATKIEEGGYKRVCLKEDCPSLNGVHNTSYPRVDPVVIMQVIHPDGTKCLLGRQKRFPPGMFTCLAGFIEPGETIEDAVRREVEEESGVKVGHVQYVACQPWPMPSSLMIGCLALAVSTEIKVDKNEIEDAHWFTREQVLDVLTKGKQQAFFVPPSRAIAHQLIKHWIRINPNL
The following text describes a protein:
Function:
May act as a guanine nucleotide exchange factor (GEF).
Sequence:
MPAPVFWMTSPRRRWLNERPREGGCRHVAKLRLQSFGLAASQGTVPSRPGLTPGAANRKQPGSRKTINKGWRPATPSRRTHAGSCVGIAAPASALGGHSHPERRGCRELGDAPLLPRLRCCSGGRPPCVSAGRHLARAEPADMAKHGADEPSSRSGSPDGEGRASEDRSLLHQRLAVRELIDTEVSYLHMLQLCASDIRSRLQQLPQGDLDVLFSNIDDIIKVNSRFLHDLQETASKEEEQVQLVGNIFLEFQEELEQVYKVYCASYDQALLLVDTYRKEPELQRHIQGIVEAVVPQAGSSGLSFLLVIPLQRITRYPLLLQKILENTVPDASAYPVLQRAVSALQDVNTNINEYKMRKEVASKYTKVEQLTLRERLARINTHTLSKKTTRLSQLLKQEAGLIPRTEDKEFDDLEERFQWVSLCVTELKNNVAAYLDNLQAFLYFRPHEYNLDIPEGPAVQYCNLARDLHLEAFLKFKQRLEGLVWQPLCSLAKALLGPQNLIKKRLDKLLDFERVEEKLLEVGSVTYQEEAARHTYQALNSLLVAELPQFNQLVMQWLGQILRTFVTLQRDLAKQVLQRAEGSMAQLPHHHVPEPAFRKLVEDALGRTSNQLRSFQETFEKVLPPPTTQPLLPGSERQVQALLSRHGPGKLYQVTSNISGTGTLDLTLPRGQIVAILQNKDTKGNSGRWLVDTGGHRGYVPAGKLQLYHVVPSAEELRRQAGLNKDPRCLTPEPSPAPVPSIPTVNQVIAAYPFVARSSHEVSLQAGQPVTILEAQDKKGNPEWSLVEVNGQRGYVPSGFLARARSPVLWGWSVPS
The following text describes a protein:
Function:
Lipid particle-localized triacylglycerol (TAG) lipase. The lipid droplet/particle is a lipid storage compartment which serves as a depot of energy and building blocks for membrane lipid biosynthesis. Involved in the mobilization of the non-polar storage lipids triacylglycerols (TAGs) from lipid particles by hydrolysis of TAGs, releasing and supplying specific fatty acids to the appropriate metabolic pathways. Also has steryl ester (SE) hydrolase and phospholipase A(2) (PLA(2)) activities, and catalyzes the acylation of lysophosphatidic acid (LPA). Contributes to early bud formation in late G1 phase of the cell cycle upon phosphorylation and activation by cyclin-dependent kinase 1 (Cdk1/CDC28).
Miscellaneous:
MISCELLANEOUS: Present with 195 molecules/cell in log phase SD medium.
Subcellular Localization:
Lipid droplet. Note=Partially retained in the endoplasmic reticulum in cells lacking triacylglycerols.
Sequence:
MSSKISDLTSTQNKPLLVTQQLIEKYYEQILGTSQNIIPILNPKNKFIRPSKDNSDVERVEEDAGKRLQTGKNKTTNKVNFNLDTGNEDKLDDDQETVTENENNDIEMVETDEGEDERQGSSLASKCKSFLYNVFVGNYERDILIDKVCSQKQHAMSFEEWCSAGARLDDLTGKTEWKQKLESPLYDYKLIKDLTSRMREERLNRNYAQLLYIIRTNWVRNLGNMGNVNLYRHSHVGTKYLIDEYMMESRLALESLMESDLDDSYLLGILQQTRRNIGRTALVLSGGGTFGLFHIGVLGTLFELDLLPRVISGSSAGAIVASILSVHHKEEIPVLLNHILDKEFNIFKDDKQKSESENLLIKISRFFKNGTWFDNKHLVNTMIEFLGDLTFREAYNRTGKILNITVSPASLFEQPRLLNNLTAPNVLIWSAVCASCSLPGIFPSSPLYEKDPKTGERKPWTGSSSVKFVDGSVDNDLPISRLSEMFNVDHIIACQVNIHVFPFLKLSLSCVGGEIEDEFSARLKQNLSSIYNFMANEAIHILEIGSEMGIAKNALTKLRSVLSQQYSGDITILPDMCMLFRIKELLSNPTKEFLLREITNGAKATWPKVSIIQNHCGQEFALDKAISYIKGRMIVTSSLKTPFQFADSVIGLIKAPEQTSDESKNPENSTLLTRTPTKGDNHISNVLDDNLLESESTNSLLLLRENASTYGRSPSGFRPRYSITSASLNPRHQRRKSDTISTSRRPAKSFSFSVASPTSRMLRQSSKINGHPPPILQKKTSMGRLMFPMDAKTYDPESHELIPHSASIETPAMVDKKLHFGRKSRYLRHMNKKWVSSSNILYTDSDKEDHPTLRLISNFDSDAMIHSDLAGNFRRHSIDGRPPSQATKSSPFRSRPSSSTQHKSTTSFTQ
The following text describes a protein:
Function:
Double-stranded RNA (dsRNA) endoribonuclease playing a central role in short dsRNA-mediated post-transcriptional gene silencing. Cleaves naturally occurring long dsRNAs and short hairpin pre-microRNAs (miRNA) into fragments of twenty-one to twenty-three nucleotides with 3' overhang of two nucleotides, producing respectively short interfering RNAs (siRNA) and mature microRNAs. SiRNAs and miRNAs serve as guide to direct the RNA-induced silencing complex (RISC) to complementary RNAs to degrade them or prevent their translation. Gene silencing mediated by siRNAs, also called RNA interference, controls the elimination of transcripts from mobile and repetitive DNA elements of the genome but also the degradation of exogenous RNA of viral origin for instance. The miRNA pathway on the other side is a mean to specifically regulate the expression of target genes.
Subcellular Localization:
Cytoplasm.
Sequence:
MKSPALQPLSMAGLQLMTPASSPMGPFFGLPWQQEAIHDNIYTPRKYQVELLEAALDHNTIVCLNTGSGKTFIAVLLTKELSYQIRGDFNRNGKRTVFLVNSANQVAQQVSAVRTHSDLKVGEYSNLEVNASWTKEKWNQEFTKHQVLVMTCYVALNVLKNGYLSLSDINLLVFDECHLAILDHPYREIMKLCENCPSCPRILGLTASILNGKCDPEELEEKIQKLEKILKSNAETATDLVVLDRYTSQPCEIVVDCGPFTDRSGLYGRLLVELEEALNFINDCNISVHSKERDSTLISKQILSDCRAVLVVLGPWCADKVAGMMVRELQKYIKHEQEELHRKFLLFTDTFLRKIHALCEEHFSPASLDLKFVTPKVIKLLEILRKYKPYERQQFESVEWYNNRNQDNYVSWSDSEDDDEDEEIEEKEKPETNFPSPFTNILCGIIFVERRYTAVVLNRLIKEAGKQDPELAYISSNFITGHGIGKNQPRNKQMEAEFRKQEEVLRKFRAHETNLLIATSIVEEGVDIPKCNLVVRFDLPTEYRSYVQSKGRARAPISNYIMLADTDKIKSFEEDLKTYKAIEKILRNKCSKSVDTGETDIEPVVDDDDVFPPYVLRPDDGGPRVTINTAIGHINRYCARLPSDPFTHLAPKCRTRELPDGTFYSTLYLPINSPLRASIVGPPMSCVRLAERVVALICCEKLHKIGELDDHLMPVGKETVKYEEELDLHDEEETSVPGRPGSTKRRQCYPKAIPECLRDSYPKPDQPCYLYVIGMVLTTPLPDELNFRRRKLYPPEDTTRCFGILTAKPIPQIPHFPVYTRSGEVTISIELKKSGFTLSLQMLELITRLHQYIFSHILRLEKPALEFKPTDADSAYCVLPLNVVNDSSTLDIDFKFMEDIEKSEARIGIPSTKYSKETPFVFKLEDYQDAVIIPRYRNFDQPHRFYVADVYTDLTPLSKFPSPEYETFAEYYKTKYNLDLTNLNQPLLDVDHTSSRLNLLTPRHLNQKGKALPLSSAEKRKAKWESLQNKQILVPELCAIHPIPASLWRKAVCLPSILYRLHCLLTAEELRAQTASDAGVGVRSLPVDFRYPNLDFGWKKSIDSKSFISVANSSSAENENYCKHSTIVVPENAARQGANRTSSLENHDQMSVNCRTLFSESPGKLQIEVVTDLTAINGLSYNKNLANGSYDLANRDFCQGNQLNYYKQEIPVQPTTSYPIQNLYNYENQPKPSDECTLLSNKYLDGNANKSTSDGSPTTAAMPGTTEAVRALKDKMGSEQSPCPGYSSRTLGPNPGLILQALTLSNASDGFNLERLEMLGDSFLKHAITTYLFCTYPDAHEGRLSYMRSKKVSNCNLYRLGKKKGLPSRMVVSIFDPPVNWLPPGYVVNQDKSNADKWEKDEMTKDCMLANGKLDEDFEEDDEEEEDLMWRAPKEDADYEDDFLEYDQEHIKFIDNMLMGSGAFVKKISLSPFSTTDSAYEWKMPKKSSLGSMPFSSDFEDFDYSSWDAMCYLDPSKAVEEDDFVVGFWNPSEENCGVDTGKQSISYDLHTEQCIADKSIADCVEALLGCYLTSCGERAAQLFLCSLGLKVLPVMKRTDREKTMCPPRENFSSQQKNLSGGRAAASVASLRPSVLKDLEYGCLKIPPRCMFDHPDADKTLNHLISGFENFEKKINYRFKNKAYLLQAFTHASYHYNTITDCYQRLEFLGDAILDYLITKHLYEDPRQHSPGVLTDLRSALVNNTIFASLAVKYDYHKYFKAVSPELFHVIDDFVQFQLEKNEMQGMDSELRRSEEDEEKEEDIEVPKAMGDIFESLAGAIYMDSGMSLEMVWQVYYPMMRPLIEKFSANVPRSPVRELLEMEPETAKFSPAERTYDGKVRVTVEVVGKGKFKGVGRSYRIAKSAAARRALRSLKANQPQWNTVLLALSAPLTPRETPLHVCMERAVRCFF
The following text describes a protein:
Function:
Cleaves peptide substrates after methionine, leucine, and norleucine. Physiological substrates include EZR, alpha-tubulins and the apoptosis inhibitor BIRC5/Survivin. Promotes caspase activation and subsequent apoptosis of target cells.
Subcellular Localization:
Secreted.
Sequence:
MKALHILLLAAAFISLTFNATHGEEIINGKKAKKNSFQYMASVQSKGKHICGGFLISPSYVLTAAHCFQSNLSVVLGTQNIDAKRNELRRYAVKSMHIHPSYKENPRYGSDIMLLKFSGKVNLNKDLKVIKISSNHKRVKPNTKCQVAGWGKTETQKTVNDLMVTDVSTIDITVCKKQWNKENVELPAKILCAGGYGTKSGACQGDSGGPLVCSGLAVGIVSFNLHDNCSYPNVPNVYTEISAYADWINKVIKRDA