lhallee/plat_data huggingface dataset:
The following text describes a protein:
Function:
Subunit of non-clathrin- and clathrin-associated adaptor protein complex 3 (AP-3) that plays a role in protein sorting in the late-Golgi/trans-Golgi network (TGN) and/or endosomes. The AP complexes mediate both the recruitment of clathrin to membranes and the recognition of sorting signals within the cytosolic tails of transmembrane cargo molecules. AP-3 appears to be involved in the sorting of a subset of transmembrane proteins targeted to lysosomes and lysosome-related organelles. In concert with the BLOC-1 complex, AP-3 is required to target cargos into vesicles assembled at cell bodies for delivery into neurites and nerve terminals.
Subcellular Localization:
Cytoplasmic vesicle, clathrin-coated vesicle membrane; Peripheral membrane protein; Cytoplasmic side. Golgi apparatus.
Sequence:
MSAAPAYSEDKGGSAGPGEPEYGHDPASGGIFSSDYKRHDDLKEMLDTNKDSLKLEAMKRIVAMIARGKNASDLFPAVVKNVACKNIEVKKLVYVYLVRYAEEQQDLALLSISTFQRGLKDPNQLIRASALRVLSSIRVPIIVPIMMLAIKEAASDMSPYVRKTAAHAIPKLYSLDSDQKDQLIEVIEKLLADKTTLVAGSVVMAFEEVCPERIDLIHKNYRKLCNLLIDVEEWGQVVIISMLTRYARTQFLSPTQNESLLEENPEKAFYGSEEDEAKGPGSEEAATAALPARKPYVMDPDHRLLLRNTKPLLQSRSAAVVMAVAQLYFHLAPKAEVGVIAKALVRLLRSHSEVQYVVLQNVATMSIKRRLEVLTNLANETNIPTVLREFQTYIRSMDKDFVAATIQAIGRCATNIGRVRDTCLNGLVQLLSNRDELVVAESVVVIKKLLQMQPAQHGEIIKHLAKLTDNIQVPMARASILWLIGEYCEHVPKIAPDVLRKMAKSFTAEEDIVKLQVINLAAKLYLTNSKQTKLLTQYVLSLAKYDQNYDIRDRARFTRQLIAPSEQGGALSRHAKKLFLAPKPAPILESSFKDRDHFQLGSLSHLLNAKATGYQELPDWPEEAPDPSVRNVEVPEWTKCSNREKRKEKEKPFYSDSEGESGPTESADSEPESESESGSKSSSESGSGESSSESDNEDDDEEKGEGSESEQSEEEGEKKKKTKKKKASEGHREGSSSEEGSDSSSSSESEVTSESEEEQVEPASWRKKTPPSSKSTPAAKEISLLDLEDFTSPSVQPVSPPMVVSTSLAADLEGLTLTDSSLVPSLLSPVSSIGRQELLHRVAGEGLAVDYAFSRQPFSGDPHMVSLHIYFSNNSETPIKGLHVGTPKLPAGISIQEFPEIGTEGLGQESLAPGESTTTVMGINFCDSTQAANFQLCTQTRQFYVSIQPPVGELMAPVFMSENEFKKEQGKLTGMNEITEKLTLPDTCRSDHMVVQKVTATANLGRVPCGASDEYRFAGRTLTSGSLVLLTLDARGTGAAQLTVNSEKMVIGTMLVKDVIQALTQ
The following text describes a protein:
Function:
May be involved in transcriptional regulation.
Subcellular Localization:
Nucleus.
Sequence:
MEPRRLEGKWENEEPDTEEPLPTIKREMDPVPGADSPVMESEILQIKIKEEEPDYEDDPNPMESLEGSLTDGDGCDNEEWKWQSQISGGFSDTLDTSEGPGILIGETAPYKAESDSDCDSLTSWGAEEEDKTLGFICFKCGIRFSAHRDLLTHLCGQYEEGQEGQQQDFAGEKPFAPIDCGQIQKTIITGEKPFTCAECGKAFSSKRNLCNHHQVHTGERHFTCTQCGKNFFSKSNLHAHQNIHTGLKTFTCTECGKSFFRESHLRRHQNVHAGEKRFSCVECGESFATKKHCNVHQKSHVMGKSFSCKECSKTFSLKNLLQRHQKIHTGEKPFTCSECGKRFLRKSHLQRHRKIHTADKPLPDTEFATTIIQCGPRRKRLKPRAGEKRFSCTECSKAFSRKSNLQSHQKLHSGQELFTCTECDKSFSYKSNLLNHQKIHTGEKPFTCTECGKSFSHKWNLFNHQKIHTGEKPFACAECGKRFSLKNNLKNHQKIHTGEKPFACAECGKCFSLKSHLHSHQRTHTGEKPFTCNECGNSFSSKSYLEAHQNIHAGVKPFSCAVCGKSFFRESHLNRHRNIHTREKPFTCTDCSKCFPTKSHLQRHQNIHTGLRPFQCTDCGKSFPTKSHLHTHKNVHTGLKPFLCTECGKCFSRKSHLQKHQRTHTGERRYTFEEFEKSLMQESHRLQLSLPLQEPPSPSAETPQGWMGSHKQLPQPPDSLGFKEKKRALRALAPPLTACFRTCAEGEAEPGQPITTQDKMSAPQPHNRSHKPADEEEDPLDHMIGRTGCAAAHYAVQECMAEQQDWRKCQAQMESSAAPLTDGGSPEPQPEILQIKIKEEEPDLEDHQIPMKSSAAPLTDGGKENVGAGDKQQDAELGEDFPLVTEQRIQPREKPFKCTECGKGFLHNRSLVSHQSTVHKGHKPFSCPECGKCFTRKHSLKYHQAAHTHVKRFKCRNCRKCFSHWREFQEHCVTHTAEKPFTCTECGKSFTLKCALCSHQRIHTGKKPFSCTECGTGFSCNLSLQLHVKRHRGEKPFRCTECGKEYAYSSSLRLHMKLHTGDKLFICTECGKRFLQRSLFLLHVKVHTGEKPFICTECGKSFTQKKLLIGHQSVHTGEKPFTCSECGKHFSNKGDLLTHQRRHTGVKPFKCAECGKSFLASSNFRAHQRIHTGEKPFTCTECGKGFALRSYLRVHQRTHTGERPYSCDVCGKSYAQSGALAVHKRSHCR
The following text describes a protein:
Function:
Dioxygenase that acts on nucleic acids, such as DNA and tRNA. Requires molecular oxygen, alpha-ketoglutarate and iron. A number of activities have been described for this dioxygenase, but recent results suggest that it mainly acts on tRNAs and mediates their demethylation or oxidation depending on the context and subcellular compartment. Mainly acts as a tRNA demethylase by removing N(1)-methyladenine from various tRNAs, with a preference for N(1)-methyladenine at position 58 (m1A58) present on a stem loop structure of tRNAs. Acts as a regulator of translation initiation and elongation in response to glucose deprivation: regulates both translation initiation, by mediating demethylation of tRNA(Met), and translation elongation, N(1)-methyladenine-containing tRNAs being preferentially recruited to polysomes to promote translation elongation. In mitochondrion, specifically interacts with mt-tRNA(Met) and mediates oxidation of mt-tRNA(Met) methylated at cytosine(34) to form 5-formylcytosine (f(5)c) at this position. mt-tRNA(Met) containing the f(5)c modification at the wobble position enables recognition of the AUA codon in addition to the AUG codon, expanding codon recognition in mitochondrial translation. Specifically demethylates DNA methylated on the 6th position of adenine (N(6)-methyladenosine) DNA. N(6)-methyladenosine (m6A) DNA is present at some L1 elements in embryonic stem cells and probably promotes their silencing (By similarity). Demethylates mRNAs containing N(3)-methylcytidine modification. Also able to repair alkylated single-stranded DNA by oxidative demethylation, but with low activity. Also has DNA lyase activity and introduces double-stranded breaks at abasic sites: cleaves both single-stranded DNA and double-stranded DNA at abasic sites, with the greatest activity towards double-stranded DNA with two abasic sites. DNA lyase activity does not require alpha-ketoglutarate and iron and leads to the formation of an irreversible covalent protein-DNA adduct with the 5' DNA product. DNA lyase activity is not required during base excision repair and class switch recombination of the immunoglobulin heavy chain during B lymphocyte activation. May play a role in placental trophoblast lineage differentiation (By similarity).
Subcellular Localization:
Nucleus. Mitochondrion. Note=Mainly localizes in euchromatin, largely excluded from heterochromatin and nucleoli (By similarity).
Sequence:
MGKMAAAVGSVATLATEPGEDAFRKLFRFYRQSRPGTADLEGVIDFSAAHAARGKGPGAQKVIKSQLNVSSVSEQNAYRAGLQPVSKWQAYGLKGYPGFIFIPNPFLPGYQWHWVKQCLKLYSQKPNVCNLDKHMSKEETQDLWEQSKEFLRYKEATKRRPRSLLEKLRWVTVGYHYNWDSKKYSADHYTPFPSDLGFLSEQVAAACGFEDFRAEAGILNYYRLDSTLGIHVDRSELDHSKPLLSFSFGQSAIFLLGGLQRDEAPTAMFMHSGDIMIMSGFSRLLNHAVPRVLPNPEGEGLPHCLEAPLPAVLPRDSMVEPCSMEDWQVCASYLKTARVNMTVRQVLATDQNFPLEPIEDEKRDISTEGFCHLDDQNSEVKRARINPDS
The following text describes a protein:
Function:
Cargo-receptor protein involved in the cytoplasm to vacuole transport (Cvt) and in autophagy. Recognizes cargo proteins, such as APE4, LAP3, LAP4 and AMS1 and delivers them to the pre-autophagosomal structure for eventual engulfment by the autophagosome and targeting to the vacuole. Involved in the organization of the preautophagosomal structure (PAS). ATG19 association with cargo protein is required to localize ATG11 to the PAS. Also involved in endoplasmic reticulum-specific autophagic process, in selective removal of ER-associated degradation (ERAD) substrates, and is essential for the survival of cells subjected to severe ER stress. Also plays a role in regulation of filamentous growth.
Miscellaneous:
MISCELLANEOUS: Present with 1250 molecules/cell in log phase SD medium.
Subcellular Localization:
Preautophagosomal structure membrane; Peripheral membrane protein. Note=Also found in other perivacuolar punctate structures.
Domain:
The coiled coil domain is required for the interaction with LAP4; The C-terminal WXXL motif is crucial for ATG8-binding and Cvt pathway.
Sequence:
MNNSKTNQQMNTSMGYPLTVYDECNKFQLIVPTLDANIMLWCIGQLSLLNDSNGCKHLFWQPNDKSNVRILLNNYDYGHLFKYLQCQRKCSVYIGEGTLKKYNLTISTSFDNFLDLTPSEEKESLCREDAHEDPVSPKAGSEEEISPNSTSNVVVSRECLDNFMKQLLKLEESLNKLELEQKVTNKEPNHRISGTIDIPEDRSELVNFFTELKTVKQLEDVFQRYHDYERLSQECDSKTEIASDHSKKETKIEVEPPNERSLQITMNQRDNSLYFQLFNNTNSVLAGNCKLKFTDAGDKPTTQIIDMGPHEIGIKEYKEYRYFPYALDLEAGSTIEIENQYGEVIFLGKYGSSPMINLRPPSRLSAESLQASQEPFYSFQIDTLPELDDSSIISTSISLSYDGDDNEKALTWEEL
The following text describes a protein:
Function:
Component of the signal peptidase complex (SPC) which catalyzes the cleavage of N-terminal signal sequences from nascent proteins as they are translocated into the lumen of the endoplasmic reticulum. Dispensable for SPC enzymatic activity.
Subcellular Localization:
Endoplasmic reticulum membrane; Multi-pass membrane protein.
Sequence:
MNHLPPLIQRTLEGRIDPQSQQLVTSYTQTTFIVLTALSFVLSYLSGSVLLGVESFAAGFAVLIIATVPPWPYLKRYPVKFLPVRKLHAL
The following text describes a protein:
Function:
Component of the heterotrimeric replication protein A (RPA) and holoenzyme telomerase ribonucleoprotein complexes. As part of the heterotrimeric RPA complex, binds and stabilizes single-stranded DNA intermediates that form during DNA replication or upon DNA stress (By similarity). It prevents their reannealing and in parallel, recruits and activates different proteins and complexes involved in DNA metabolism (By similarity). Thereby, it plays an essential role both in DNA replication and the cellular response to DNA damage (By similarity). In the cellular response to DNA damage, the RPA complex controls DNA repair and DNA damage checkpoint activation (By similarity). Also part of a subcomplex of the holoenzyme telomerase ribonucleoprotein complex: this subcomplex that contains TEB1, RPA2/TEB2, RPA3/TEB3, but not RPA1, mediates the recruitment of telomerase to telomeric DNA via specific interaction between TEB1 and telomeric ssDNA. In the holoenzyme telomerase ribonucleoprotein complex, RPA2/TEB2 and RPA3/TEB3 act as assembly factors for TEB1 incorporation into telomerase holoenzyme. In the holoenzyme telomerase ribonucleoprotein complex, RPA3/TEB3 does not contribute to ssDNA affinity, while it contributes to ssDNA affinity in the RPA complex.
Subcellular Localization:
Nucleus. Chromosome, telomere.
Sequence:
MDAEQEQVMYPRILFEQMAQFRGKKVTVVGNVCNEDQNDSLVIEFGPTGLNQHVVIDNYRRVDLNNTTKFVEIRGVVLNQNIVSCEELTEFEQKDPFDFDTYSKLIHLSQSDKLSSLFTDQ
The following text describes a protein:
Function:
PDI acts by binding stoichiometrically to cyclic nucleotide phosphodiesterase, changing the KM of the enzyme for cAMP from 10 uM to 2 mM.
Sequence:
MAKIIISLILLLSLFSFSYGAYNCNKLNCSSKNTKCRTFSCTSVVGCYYTDKCTSPDLCHNSACNASTGNCTLTTISCNDNNPCTDDFCHPGYGCYSVPNSCDPGVICQQNCNDNDPCTYDFCDALNICRHSETYCNDGDACTLNTCGVNGCNFTKISCDDNDPCTADYCSTLYGCYHEPIECSIKVPCNIDSDCNRNNGCETFTCNLSTNTCDYYAKNCGGWPCINNQCTTGSISN
The following text describes a protein:
Function:
Binds both single-stranded and double-stranded DNA with higher affinity for the single-stranded form. Specifically binds to scaffold/matrix attachment region DNA. Also binds single-stranded RNA. Enhances RNA unwinding activity of DDX39A. May participate in important transcriptional or translational control of cell growth, metabolism and carcinogenesis. Component of the TREX complex which is thought to couple mRNA transcription, processing and nuclear export, and specifically associates with spliced mRNA and not with unspliced pre-mRNA. The TREX complex is recruited to spliced mRNAs by a transcription-independent mechanism, binds to mRNA upstream of the exon-junction complex (EJC) and is recruited in a splicing- and cap-dependent manner to a region near the 5' end of the mRNA where it functions in mRNA export to the cytoplasm via the TAP/NXF1 pathway. Associates with DDX39B, which facilitates RNA binding of DDX39B and likely plays a role in mRNA export; Regulates the export of target proteins, such as DRD1, from the endoplasmic reticulum to the cell surface.
Subcellular Localization:
Endoplasmic reticulum membrane; Multi-pass membrane protein. Nucleus speckle.
Sequence:
XPALQRCLTLLRDSRPWQRLVRIVQWGWLELPWVKQNINRQGNAPVASGRYCQPEEEVARLLTMAGVPEDELNPFHVLGVEATASDVELKKAYRQLAVMVHPDKNHHPRAEEAFKVLRAAWDIVSNAEKRKEYEMKRMAENELSRSVNEFLSKLQDDLKEAMNTMMCSRCQGKHRRFEMDREPKSARYCAECNRLHPAEEGDFWAESSMLGLKITYFALMDGKVYDITEWAGCQRVGISPDTHRVPYHISFGSRIPGTRGRQRATPDAPPADLQDFLSRIFQVPPGQMPNGNFFAAPQPAPGAAAASKPNSTVPKGEAKPKRRKKLAELKQECLARGLETKGIKQDLIHRLQAYLEEHAEEEANEEDVLGDETEEEETKPIELPVKEEEPPEKTVDVAAEKKVVKITSEIPQTERMQKRAERFNVPVSLESKKAARAARFGISSVPTKGLSSDNKPMVNLDKLKERAQRFGLNVSSISRKSEDDEKLKKRKERFGIVTSSAGTGTTEDTEAKKRKRAERFGIA
The following text describes a protein:
Function:
Covalently attaches a chromophore to Cys residue(s) of phycobiliproteins (By similarity). Required for plastid division, and involved in cell differentiation and regulation of the cell division plane. Maintenance of plastid homeostasis controls plant preconditioning to stress and stress acclimation; Confers sensitivity to cabbage leaf curl virus (CaLCuV), probably by supporting viral movement.
Subcellular Localization:
Plastid, chloroplast outer membrane; Single-pass membrane protein.
Sequence:
MGTESGSDPESSSNGWSRARGLVVKTLVLIGGALLIKRLTKSTTRRDHARVVSRSLTGEKFTREQASRDPDNYFNIRMLSCPAAEMVDGSEVLYLEQAFWRTPQKPFRQRLYMVKPCPKELKCDVEVSSYAIRDAEEYKNFCDRPKDQRPLPEEVIGDIGEHLTTIHLNCCDRGKRCLYEGSTSPGGFPNSWNGASYCTSDLAVLKNNEIHLWDRGFDENRNQVWGPKEGPYEFKPATSSSINENLSALNILYQSSIDKPIQGSLILQD
The following text describes a protein:
Function:
Required for fertility. Involved in chromatid cohesion establishment, in chromosome structure during male and female meiosis (e.g. the synapse formation between homologous chromosomes, the recombination, and the cohesion of both chromatid arm and centromere), and in axial element formation. Regulates the switch from mitosis to the reductional meiosis division of megaspores prior to the female gametogenesis (megasporogenesis).
Subcellular Localization:
Nucleus. Note=Localized in meiocyte nuclei just before meiosis, exclusively in meiotic G1 and S phase (at protein level).
Sequence:
MSSTMFVKRNPIRETTAGKISSPSSPTLNVAVAHIRAGSYYEIDASILPQRSPENLKSIRVVMVSKITASDVSLRYPSMFSLRSHFDYSRMNRNKPMKKRSGGGLLPVFDESHVMASELAGDLLYRRIAPHELSMNRNSWGFWVSSSSRRNKFPRREVVSQPAYNTRLCRAASPEGKCSSELKSGGMIKWGRRLRVQYQSRHIDTRKNKEGEESSRVKDEVYKEEEMEKEEDDDDGNEIGGTKQEAKEITNGNRKRKLIESSTERLAQKAKVYDQKKETQIVVYKRKSERKFIDRWSVERYKLAERNMLKVMKEKNAVFGNSILRPELRSEARKLIGDTGLLDHLLKHMAGKVAPGGQDRFMRKHNADGAMEYWLESSDLIHIRKEAGVKDPYWTPPPGWKLGDNPSQDPVCAGEIRDIREELASLKRELKKLASKKEEEELVIMTTPNSCVTSQNDNLMTPAKEIYADLLKKKYKIEDQLVIIGETLRKMEEDMGWLKKTVDENYPKKPDSTETPLLLEDSPPIQTLEGEVKVVNKGNQITESPQNREKGRKHDQQERSPLSLISNTGFRICRPVGMFAWPQLPALAAATDTNASSPSHRQAYPSPFPVKPLAAKRPLGLTFPFTIIPEEAPKNLFNV
The following text describes a protein:
Function:
Catalyzes the formation of methylglyoxal from dihydroxyacetone phosphate.
Sequence:
MTVKKIALVAHDRMKKELIEWIKKHQNLLKHHELYATGSTGQAIEKTLNVTVTKMESGPLGGDLQLGAKIVNKEIDILIFFWDPLEAQPHDPDVRALLRIAVVWNLPVACNASTADYLLTSPLFDSDYHPETPDYEAYRNRII
The following text describes a protein:
Function:
2/mitotic-specific cyclin essential for the control of the cell cycle at the G2/M (mitosis) transition. G2/M cyclins accumulate steadily during G2 and are abruptly destroyed at mitosis. Degradation is necessary for the cell to exit from mitosis. Plays a role in morphogenesis by negatively regulating polarized growth. Through binding to CDC28 regulates cytokinesis, partly by phosphorylation of the actomyosin ring component IQG1. Also involved in the phosphorylation of CDC6 and CDC54.
Sequence:
MPQVTKTNNENEFRLTRSKVQHQESISTIKNTTISNSQHKQQTQQQISSPPQVSVTSSEGVSHVNTRQYLGDVSNQYITNAKPTNKRKPLGGDNAPLQKQQHRPSRPIPIASDNNNNGSTSSSSNSSNNNNNDANRLASLAVPSRLPQKRQATESSTNLVEKLRVPQPEVGERSQSYHKKSRLIDYEWQDLDEEDSDDQLMVSEYVNEIFSYYYELETRMLPDPQYLFKQTLLKPRMRSILVDWLVEMHLKFKLLPESLFLAVNVMDRFMSVEVVQIDKLQLLATAALFTAAKYEEVFSPSVKNYAYFTDGSYTPEEVVQAEKYMLTILNFDLNYPNPMNFLRRISKADDYDVQSRTLGKYLLEITIVDYKFIGMRPSLCCASAMYLARLILGKLPVWNGNLIHYSGGYRISDMRECIELMFQYLIAPIEHDEFFKKYAMRKFMRASTLCRNWAKKFQASGRDLFDERLSTHRLTLEDDDEEEEIVVAEAEE
The following text describes a protein:
Function:
Involved in the biosynthesis of phosphatidyl-myo-inositol mannosides (PIM) which are early precursors in the biosynthesis of lipomannans (LM) and lipoarabinomannans (LAM). Catalyzes the addition of a mannosyl residue from GDP-D-mannose (GDP-Man) to the position 2 of the carrier lipid phosphatidyl-myo-inositol (PI) to generate a phosphatidyl-myo-inositol bearing an alpha-1,2-linked mannose residue (PIM1).
Subcellular Localization:
Cell membrane; Peripheral membrane protein; Cytoplasmic side.
Sequence:
MRVGLVCPYSFARPGGVQNHVLGLGGWLKEQGHDVSIIAPGQASRSLLAETGLVPSEFVSAGRAVPVTFNGSVARINFGVGPALKVKKWLDQGNFDVVHLHEPIAPTICLLALYLTDRPVTATFHTATPELTAIRFANRVLPRMVSRIDAAIAVSSEAADVAHHYSGVNPVVIGNGIHLADYPLVRATSRWRGGEHPLITFLGRYDEPRKGFEVLTAALPLVRATYPDLEVVVIGSGTARSVEGVRFLGGLDDEERNAWLGRSDIYIAPQTGRESFGIVLLEAMACGAPVVAANLRAFLDVLTDDEGLVGHTFRVGNSASASRAMLRSLSEPRDLRLERGRALAANYDWSVIGPQVVAMYTVAGQNYATSRGIKNRELKGH
The following text describes a protein:
Function:
Acetyltransferase; part of the gene cluster that mediates the biosynthesis of mannosylerythritol lipids (MELs), surface-active substances that enhance the availability of water-insoluble substrates. Mannosylerythritol lipid production is responsible for hemolytic activity of Ustilago maydis. Depending on the number of acetyl groups, mannosylerythritol lipids can be differentiated into MEL A (fully acetylated), MEL B and MEL C (monoacetylated at R-6 and R-4, respectively), and the fully deacetylated MEL D. The first step in the pathway is the generation of mannosylerythritol by the glycosyltransferase EMT1 which catalyzes the transfer of GDP-mannose to the C-4 atom of meso-erythritol. This reaction has to be stereospecific, since only mannosyl-D-erythritol is generated. The produced disaccharide is subsequently acylated with fatty acids of various lengths derived from the peroxisomal beta-oxidation by the peroxisomal acyltransferases MAC1 and MAC2 at positions C-2 and C-3, repectively. The existence of MEL derivatives which carry an acetyl group at C-2 implies that at least MAC1 also accepts acetyl-CoA as a donor. The final step of MEL biosynthesis is the acetylation of the fully acylated mannosylerythritol lipids catalyzed by the acetyl-CoA-dependent acetyltransferase MAT1. MAT1 displays a relaxed regioselectivity and is able to transfer acetylgroups to both positions C-4 and C-6 of the mannosyl moiety.
Subcellular Localization:
Cell membrane; Peripheral membrane protein.
Sequence:
MKSNVDTVLDGYTSVPVGVLDSTLANTDILTRITLVFPSSLSLSALQESWYALVRSWPILAARVRATPSTPSGLSYLIPTPATLESLETRSRNSASKPLEKHIVLLDQSSRSFSDYHPIVAKAVHSNLDRNNISIGGAPLVEHEKATICSNACTSWKQLIKQDQAFVTAQATKFADATTVTISFSHILGDAFTIKHIFQGWQTALNGQAVQELQDVGKDPFIKYLPKDTNDKKHKKNKKSEPAPDLPLQWFRYGLARKIKLISLLLWEVKVKKPEKTLGQYYIYLPQAKVDELMAQARSDLEQLRSSSATSATERDLNVSTFNVLFAWLLQNIHASTAIKPSKTSSVICIINAKTRPPAGHVPADYPRHQLWGGALGAPLRPLSAAEYVTLPLGQLALHIRESITEQVDPENIRKSVVMALKHSMWKKPSGELLFFSQNPNTYWCGCTEWRSAKFHTIDFSAAATPHHDAIQPTAAPAASVNPVAITTNMETPMTKRNRWALLGEANNGIWFTGGLTANEASNKNGFGRYIFVE
The following text describes a protein:
Function:
Non-catalytic subunit of the queuine tRNA-ribosyltransferase (TGT) that catalyzes the base-exchange of a guanine (G) residue with queuine (Q) at position 34 (anticodon wobble position) in tRNAs with GU(N) anticodons (tRNA-Asp, -Asn, -His and -Tyr), resulting in the hypermodified nucleoside queuosine (7-(((4,5-cis-dihydroxy-2-cyclopenten-1-yl)amino)methyl)-7-deazaguanosine).
Subcellular Localization:
Cytoplasm.
Sequence:
MASLNALKQALKHASAHIDYSSRRTLSDDQYAGGFSNFNEAPNDRMYRAFITPTLTSVLGPLFDSRLAISVLEIGPGPKTILASLPEGMKRKIKRYKAFEPNEVFAKRLDDQLGCVVRREAYELHDETQTEKFDVVLFCHSMYGMHPKRAFIEQALESLGDVGDEMVVVFHRDGKLDFGGLVCYRTATWLDLTLQVPVEDERLDEFVSFIVGFDVEASDVRKKCRDICHALGTRTGNHLVFYAREIMVAFNKHATALPRLLAQVPAAMSATAIKNREPNVVGVDMSAFNDLHVLQDGSWIKGDDVKDGPLVIMGAGCTTGQVVSETLKSGMTIPLGSRPSVGAGLWLQGRYRSPIAAPRTVLSISVLGVVMVSPTGEILHIGHVPPLYLPRDTIRPDNEAELLWAVKGAGTNFGIVISVVFRAYNAPKFLVREWVVSLGNREEAVDKLAKFNEIADKLERSQSADPCLHWDDGGLRLGVTMYECSNSDPDRAPTPFDTLFGKPQDVQTVDCKGLFDTDMYMSRMHGGHAGGKTSSFKRCVFLKDIGNHQIADLLVKAIENRPTPTCYLHLLQGGGAIRGVADTSTAFGCRDWDFACVITGIWPRDEDGNEISRSTIQWVYNFTTALLPLSQGIYGADLGPDPRDKLLVSEAFGPNRQRLARLKKVMDPQNVLAYACPLPKNRPGPKLIFLVTGNHGAGKDYCAEQWASEVKDHARERLEVHISSISDATKRAYAASTGADLARLLNDRAYKEQHRAAMTAFFKAQVQQRPNLPEEHFLDVVYGAAEADVLFITGMRDPAPVAMFSHLVPGSRVIEVRVRASEEIIYNRRCCDGPGVAERETASALLDWCPDFDFDNNVKGPRAARSFAEKHLSLFLHGDAQRLADMVRAIPDFPVADTQFRHVLGIAQEPDDLALCLSLLKSLYPGDMSQVDAMVCCEAGGFLFASPLASSLSVPLVIVRNGGKLPPPTLSVTKLNSHISSYGNVKEETIEIERDAISKGASVLVVDDVLASGQTLCAVLQLLDQTGIQPEKIQALVVAEFPIHGGRALLRSRGFGTVSVTATKRTLKEGTIDRGTTLADGGKERDVTRRDAISRARPATTLKIGIVTPPCQKSSRVHEDPRIAITVYPDVREQHWTRQMAEQAAMRNLDQLPPEMIEFTLLKTTGALAPRLGRISLVGRKTIQTPAFIGNTSRGVISHISPDNFRKSVHVNGVYVPLEDFVEKHPKQIPPIFKYEVPEPLRKFIALPEDTLLILGARRNPPIPVPVPNTNTEIALSTSVGFKAMSSEYYAAAVRKLQPDIVVGLADIPFGQESIGTKRKDKMSDRTELWLQDIIARKESLDKGEKSWSIFAPILPIERDLQSWYLEHLLDDMVDKISGVAIYDTYLLDDLPDQLHLLPRLSFHAPIGLGMDLFTVPFLADATDAGIVLDFAFPPPAKDETSSTRCTLGIDMWHEDHATSVTPLSTDCTCYACIKHHRAYLQHLLAAKEMLGWVLIQIHNHAILSAFFAGVRTSIEAGTFDTDVAAFEAYYEPSLPEKTGQGPRVRGYQFRSEEHAKKGRKNPRVYKKFDEGKIAELKAAHGQQPNRKPEMRDVIDDEALLGLMGMDEEPSRQMEELVIEDDKGV
The following text describes a protein:
Function:
Participates in the conversion of CDP-6-deoxy-D-glycero-L-threo-4-hexulose to 3,6-dideoxy-D-glycero-D-glycero-4-hexulose together with CDP-6-deoxy-D-glycero-L-threo-4-hexulose-3-dehydrase (E1) in two consecutive steps. The detailed mechanism of E3 is not yet resolved (By similarity).
Sequence:
MSLNVKLHPSGIIFTSDGTSTILDAALDSNIHIEYSCKDGTCGSCKAILISGEVDSAENTFLTEEDVAKGAILTCCSKAKSDIELDVNYYPELSHIQKKTYPCKLDSIEFIGEDIAILSLRLPPTAKIQYLAGQYIDLIINGQRRSYSIANAPGGNGNIELHVRKVVNGVFSNIIFNELKLQQLLRIEGPQGTFFVREDNLPIVFLAGGTGFAPVKSMVEALINKNDQRQVHIYWGMPAGHNFYSDIANEWAIKHPNIHYVPVVSGDDSTWTGATGFVHQAVLEDIPDLSLFNVYACGSLAMITAARNDFINHGLAENKFFSDAFVPSK
The following text describes a protein:
Function:
Plays a role as an alternative splicing regulator. Regulates its own expression at the level of RNA processing. Also regulates the splicing of fibronectin and CD45 genes. May act, at least in part, by interaction with other R/S-containing splicing factors. Represses the splicing of MAPT/Tau exon 10 (By similarity).
Subcellular Localization:
Nucleus.
Sequence:
MYGAGGGRAKPERKGGVKEEAGPGGTGTGGNRVELLVFGYACKLFRDDERALAQEQGQHLIPWMGDPKILIDRYDGRGHLHDLSAYDAEYATWNRDYQLSEEEARVEALCDEERYLALHTDLLEEEARQEEEYKRLSEALAEDGNYSAVGFTYGSDYYDPSEPTEEEEPSKQREKNEAENLEENEEPFIAPLGLSVPSDVELPPTAKMHAIIERTANFVCKQGAQFEIMLKAKQARNSQFDFLRFDHYLNPYYKFIQKAMKEGRYTVLAESKNEEKKKSGPTSDNEEEDDEEDGSYLHPSLFASKKSSRLEELMKPLKVVDPDHPLAALVRKAQADSSAPAPPTADGTPAQPSQVEYTADSTVAAMYYSYYMLPDGTYCLAPPPPGIDVATYYSTLPAGVTVSSSPGVTTTVPPPPGTTPPPPPTTAEPSSGVTSTTTTTSALAPVAIIPPPPDIQPVIDKLAEYVARNGLKFETSVRAKNDQRFEFLQPWHQYNAYYEFKKQFFLQKEGGGSTQAASTAEEAPTETAVEESGEAGEDGAPEGMAETGGRGSGKKEAGSSKSTVDGKLVKASFAPISFAIKAKENDLLPLEKNRVKLDDDSEEDEESRECQESTSSVANPSPAAAPPSVAVEEKKPQLTQEELEAKQAKQKLEDRLAAAAREKLAQASKESKEKQLQAERKRKAALFLQTLKNPLPEAEVGKLEESTFGVEDTGVMPCPLLVGGRTLPILEGKPPERPSNRCRDPPREEEREKKKKKHKKRSRTRSRSPKYHSSSKPRSRSHSKAKHSLPSAYRTVRRSRSRSRSPRRRAHSPERRREERSVPTAYRMSGSPGVSRKRTRSRSPHEKKKKRRSRSRTKAKARSQSTSPSKQAAQRPSAHSAHSASISPVESRGSSQERSRGVSQEKDGQISSAIVSSVQSKITQDLMAKVRAMLAASKNLQTSAS
The following text describes a protein:
Function:
Catalyzes the specific phosphorylation of the 3-hydroxyl group of shikimic acid using ATP as a cosubstrate.
Subcellular Localization:
Cytoplasm.
Sequence:
MNAKRAIPVRERNIVLIGFMGVGKTTIGQLVAKKLYRDFIDIDQQIEKDFNMSIPEIFEKKGEDFFRKTEKEYILDICHHKRFKIVSLGGGSFKQEEIRNCCLENCLVLHLDLSWENWKQRADLLIESRPVLHNRSMDEMEQLFNERKVIYDKHNSKVATDNLSPEEVADYIVETLKIGWDLYQPM
The following text describes a protein:
Function:
Plays a continuous role in plant development probably in the structural organization of compartments.
Sequence:
MFGRAPKKSDNTKYYEILGVPKTASQDDLKKAYRKAAIKNHPDKGGDPEKFKELAQAYEVLSDPEKREIYDQYGEDALKEGMGGGGGAHDPFDIFQSFFGGNPFGGGGSSRGRRQRRGEDVIHPLKVSLEDLYNGISKKLSLSRNIICSKCKGKGSKSGASMKCSGCQGSGMKVSIRHLGPSMIQQMQHPCNDCKGTGETINDKDLCPQCKGEKVVQEKKVLEVNVEKGMQNGQKITFPGEADEAPDTVTGDIVFVLQQKDHPKFKRKGDDLFVEHTLTLTEAVCGFQFILTHLDGRQLLIKTHPGEVVKPDQCKAINDEGMPMYQRPFMRGKLYIHFTVDFPDSLAPEQCKALEAVLPSRASVQLTDMELDECEETTLYDVNIEEEMRRKQAQAAQEAYEEDDDMHGGAQRVQCAQQ
The following text describes a protein:
Function:
Necessary for sperm flagellar function. Plays a role in motile ciliogenesis. May help to recruit STK36 to the cilium or apical surface of the cell to initiate subsequent steps of construction of the central pair apparatus of motile cilia.
Subcellular Localization:
Cytoplasm, cytoskeleton, flagellum axoneme.
Sequence:
MAAQRGMPSSAVRVLEEALGMGLTAAGDARDTADAVAAEGAYYLEQVTITEASEDDYEYEEIPDDNFSIPEGEEDLAKAIQMAQEQATDTEILEQKTVLPSKHAVPEVIEDFLCNFLIKMGMTRTLDCFQSEWYELIQKGVTELRTVENVPDVYTQIMLLENENKNLKKDLKHYKQAADKAREDLLKIQKQRDFHRMHHKRIVQEKNKLINDLKGLKLHYASYEPTIRVLHEKHHTLLKEKMLTSLERDKVVGQISGLQETLKKLQRGHSYHAPQIKVDHSREKENAPEGPTQKGLREAREQNKCKTKMKGNTKDSEFPIDMQPNPNLNVSKESLSPAKFDYKLKNIFRLHELPVSCVSMHPHKDILVSCGEDRLWKVLGLPKCNVLLTGFGHTDWLSDCCFHPSGNKLATSSGDTTVKLWDLCKGDCILTFEGHSRAVWSCTWHSCGNFVASSSLDKTSKIWDVNSERCRCTLYGHTDSVNSIEFFPFSNTLLTSSADKTLSIWDARTGICEQSLYGHMHSINDAIFDPRGHMIASCDACGVTKLWDFRKLLPIVSIDIGPSPGNEVNFDSSGRVLAQASGNGVIHLLDLKSGEIHKLMGHENEAHTVVFSHDGEILFSGGSDGTVRTWS