lhallee/plat_data huggingface dataset:
The following text describes a protein:
Function:
Substrate recognition component of a DCX (DDB1-CUL4-X-box) E3 protein ligase complex that mediates the ubiquitination and subsequent proteasomal degradation of target proteins. Has an essential role in mediating growth by negatively regulating insulin signaling. It also has a role in maintaining presynaptic function in the neuromuscular junction synapses of third-instar larvae.
Subcellular Localization:
Cytoplasm. Nucleus.
Sequence:
MDERILENERLQMEQIRELDLEELQVEEVDDTHNSSDDDSDPSRHGDGGIGSHGGLTFDACLASLHTYLGEVEDTHRRLAFLDGGAILNLPMFYLEGAVLFPEATLPLRVIQPRFIAAVERALNQADAPYTIGVVRVHRGPDDQRLHFATIGTTAEIRQYRRLEDGSLNVVTRGQQRFYLQRRWIDVEGALCAEVQIIQEDLPLRTPRNAFGELASVSNLWSRSLSCSRNSRAKWHKSQCEENDSESMSETSFESDLSPTEMRMHKSAIDSTNSFDRIDEMMSSDDEGFELVSGSQLGRYHSNEFRGSSQHCIIDRGSESEDTSPGIGNQFTPGKISHQSCKGERWKKKGLLSDSNWAYRVPKSYWPNWVYQMYDSYYLARRAADMWRQIIGVPSMDDLVKKPDLLSFFIASKIPISDSTRQELLEIHGISYRLRREIELLECFDRVRCKNCQTVIAKRSDMLVMSSDGPLGAYVNPYGFVHEIMTLQKANGLALMGRPHTEYSWFPGYAWTIATCATCESQMGWLFTATNKKLKPRSFWGIRSSQVADDMRSSQVADDRR
The following text describes a protein:
Function:
Scaffold protein that serves as a bridging partner between the PRC2/EZH2 complex and the elongin BC complex: required to fine-tune the transcriptional status of Polycomb group (PcG) target genes in embryonic stem cells (ESCs). Plays a key role in genomic regions that display both active and repressive chromatin properties in pluripotent stem cells by sustaining low level expression at PcG target genes: acts by recruiting the elongin BC complex, thereby restricting excessive activity of the PRC2/EZH2 complex. Interaction with USP7 promotes deubiquitination of H2B at promoter sites. Acts as a regulator of neuronal differentiation.
Subcellular Localization:
Nucleus. Chromosome. Note=Localizes at both PRC2/EZH2 sites (H3K27me3) and broad H3K4me3 sites on chromatin of embryonic stem cells (ESCs).
Domain:
The BC-box, which mediates binding to the elongin BC complex.
Sequence:
METLCPPPRLAVPASPRGSPCSPTPLKPRRGTPEFSPLCLRALAFCALAKPRPSSLGLGPGELAPRTPVLLGPPASPCTGGWAADGLKHLGGQAGRPSDVSSPAREDADVAVCPGGGEEEEGGGGFPHFGAGSCAPPGRCPAPLRPQDSPTNPAWSPPRPARGLDAASSPPLEPGSPPPSPPAGLSPEPAPSEQPVPASEAPGGGDPAPTAPEAPALSPSTADAAPDPPRDLRQEHFNRLIRRSKLWCYAKGFALDTPSLRRGPERPAAKARGAAKKRRRPAPPPPSVQPRRPVPTLPTSSTFSLLDCFPCPPALVVEENGDLGPASSLRLQGDAKPPPAHPLWKWQMGGPAVPEPPGLKSWWVNLEEL
The following text describes a protein:
Function:
DNA-dependent ATPase involved in processing of recombination intermediates, plays a role in repairing DNA breaks. Stimulates the branch migration of RecA-mediated strand transfer reactions, allowing the 3' invading strand to extend heteroduplex DNA faster. Binds ssDNA in the presence of ADP but not other nucleotides, has ATPase activity that is stimulated by ssDNA and various branched DNA structures, but inhibited by SSB. Does not have RecA's homology-searching function; Plays a role in repairing double-strand DNA breaks, probably involving stabilizing or processing branched DNA or blocked replication forks.
Domain:
The middle region has homology to RecA with ATPase motifs including the RadA KNRFG motif, while the C-terminus is homologous to Lon protease.
Sequence:
MKPKLKRVFQCQSCGYISPKWIGKCPDCGAWNSFVEEVIEAESISKKAETARLKTLEDIQPVPISSIKITLSDRLSTGISELDRVLGGGVVRGSLVLIGGDPGIGKSTLLLQATDNLAKKYGRVLYVSGEESLTQIKLRAERLGAISENILLLSETLVEKILDWASEEELNALVVDSIQTVYTEEAMSAPGSVSQIRESATKFINFAKQKGIPVFLIGHVTKEGAIAGPRVLEHLVDTVLYFEGDRGYAYRILRSVKNRFGPTNEIGVFEMTGTGLIEVENPSLIFLSEHSQNSGSAITATIEGTRAILTEIQALVAPSNFGMPRRNFIGVDYQRVNLLVAVLEKRGRINLAGADIFVNVVGGLKITEPSSDLAVISAIVSSFRDIPLHEGMVIFGEVGLSGEIRAISQTEMRLKEASRIGMKHAIIPKSNLERLKEKFNLKIKGVGSINELIEIIGS
The following text describes a protein:
Function:
Catalyzes the reversible oxidation of 3-phospho-D-glycerate to 3-phosphonooxypyruvate, the first step of the phosphorylated L-serine biosynthesis pathway. Also catalyzes the reversible oxidation of 2-hydroxyglutarate to 2-oxoglutarate.
Sequence:
MDINPLQDSFQRAMNLSRSPGAVSTSPTQSFMNTLPRRLSVSKQQKALKPFSTGDMRILLLENVNQTAVDIFKDQGYQVEFYKSSLPEEELIEKIKDVHAIGIRSKTKLTANILKHAKNLVVIGCFCIGTNQVDLDYAASIGVAVFNSPFSNSRSVAELVIAEIISLARQLGDRSIELHTGTWNKVSQKCWEVRGKTLGVVGYGHIGSQLSVLAESMGMHVLYYDIVTIMALGTAKQVSTLDELLNKSDFVTLHVPETPETKNLLSAPQFAAMKDGAYVINASRGTVVDIPSLIQAMKAGKIAGAALDVYPNEPAKNGADAFSDKLNNWTSELVSLPNVILTPHIGGSTEEAQSAIGIEVAHALSKYINEGISVGSVNFPEVSLRSLDLDQENTVRVLYIHKNVPGVLKTVNNILSNHNIEKQFSDSCGEIAYLMADISDVNQSDIKQIYDELDKTSSKISIRLLY
The following text describes a protein:
Function:
DNA-binding protein that specifically binds heat shock promoter elements (HSE) and activates transcription.
Subcellular Localization:
Nucleus.
Sequence:
MDVTPATSGGGGPAPFLIKTYEMVDDSVTDEIVSWSTKGNSFVVWNPPEFARLLLPTYFKHNNFSSFIRQLNTYGFRKIDPERWEFANEEFIKDKKHLLKNIHRRKPIHSHSNNPQSSTADPERAAFEEQIDTLTREKNSLEKNIQRFKQQQPSTKLQLEDLTQRVNNMEQKQDTLLNFLKKASQNPEFVERLAQKLESMDFSADNKKRRLPGSRVSPEDSLVDNHSPSRPDFGNVFHHDFSNKLRLELSPAVSDVNFVSNSTQSSNEDGGSPQIRLTEDCRTNNELTPGGPQELSDTCTSFGFNMESSFMHKTGPCLDANEEPEGHLSCQLNLTLASCVSQINRSPDTDTIPESFEGVAKPSGQNVSLSSARDDPAKNAAAPASVQPRVNDVFWEQFLTERPGSSDVEDTGSNLRSMAYEQEDRRSGHGNSRNLRNLTL
The following text describes a protein:
Function:
Component of the cytochrome c oxidase, the last enzyme in the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII) and cytochrome c oxidase (complex IV, CIV), that cooperate to transfer electrons derived from NADH and succinate to molecular oxygen, creating an electrochemical gradient over the inner membrane that drives transmembrane transport and the ATP synthase. Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Electrons originating from reduced cytochrome c in the intermembrane space (IMS) are transferred via the dinuclear copper A center (CU(A)) of subunit 2 and heme A of subunit 1 to the active site in subunit 1, a binuclear center (BNC) formed by heme A3 and copper B (CU(B)). The BNC reduces molecular oxygen to 2 water molecules using 4 electrons from cytochrome c in the IMS and 4 protons from the mitochondrial matrix.
Subcellular Localization:
Mitochondrion inner membrane; Single-pass membrane protein.
Sequence:
MSALTPLLLRGLTGPARRLLVPRAQVHSKPPREQLGSMDVTIALTACFVSFLLPAGWVLSHLDSYKKRE
The following text describes a protein:
Function:
Glycosyltransferase that generates the core 1 O-glycan Gal-beta1-3GalNAc-alpha1-Ser/Thr (T antigen), which is a precursor for many extended O-glycans in glycoproteins.
Subcellular Localization:
Membrane; Single-pass type II membrane protein.
Sequence:
DEKGRDLGDQVRVLCWILTSPENHETRALAVKETWGKRCNILLFMSSANDSTLPSVELAVREGRNGLWGKTREAFRYAWDRYQDEVDWFLKADDDTYVIVENLRYFLSAFNTSLPLWFGHKFKAIVKSGYFSGGAGYVLSKEATRRFVKEGYFNALLCRHDHEGAEDAEMGKCMENLKVLTMDTRDSKGRGRFHPFVPDNVYFPGNITQDYWYWKNIYYAPKKGRECCSDSTISFHYVDTKMMRLLDFFLYQIRPYGI
The following text describes a protein:
Function:
Catalyzes the phosphorylation of thiamine to thiamine pyrophosphate (TPP). TPP is an active cofactor for enzymes involved in glycolysis and energy production. Plant leaves require high levels of TPP for photosynthesis and carbohydrate metabolism.
Sequence:
MTTATAGGTGTPQPASASSSHGAKPASDDRPPPQPLNGNASAPASNSTLPTPAAGPPPAATPLYSASASAAAAAAAAAAAAAAAARLREPGAALGPPYSQTICSDFLGPGPLPPGRRLYLVILNYTLPAGLPHVWEQACFRVCADGGCNRLHDELPSLAPPPPPPPTSALSAAATEPLASASAAAAGTSAASPATAPATAPAAASCTPAATAAAAGAGAAATADPELALRLAHLPDLVLGDLDSLRPDTREFYTRHNVPFLDLSHDQDSTDLTKAVALVEQRFIACDPHPDPDPDRHQILVLGALGGRLDHTLGNLNTVHMFPHLNICLWGDGNLVRLLRPGTARIEPDTRFEGPECGLVPLAGPATATSTGLLYNVDDTPLRVGGLVSTSNQIVGQGPVEVLTDAPLLWTTSLRADPRPEPAELWGRVWGAAGAAGAAPGQP
The following text describes a protein:
Function:
Probably acts as a heme chaperone, transferring heme to an unknown acceptor. Binds one molecule of heme per monomer, possibly covalently. Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine.
Subcellular Localization:
Cytoplasm.
Sequence:
MRHLYLHIPFCHRRCSYCDFNTYANMEHRIEAYVDALCQELAMLRDQLPPLPASPEAAALRPSIFFGGGTPSMLSPAQIERILQAAAEIVPLTGAEISLEANPGTVLGRDYLRDLRSLGINRLSMGVQSLHDPTLRMLGRIHTAAEAYASFNDARAVGFESINLDFIFGLPGQDIEQWRATLTEIIRWEVDHIALYSLILEENTPLYAQVTAGRLQIPDDDLTGAMYELAMEMLGAAGYRHYEISNWVRPSVSDRPDAPPALACQHNLAYWLNSDYLAAGAGAHGHVFPQRYANLRPIDSYITAVQSGRRPIAETTLLTSADLAAETMFMGLRLDIGVGFAHFAARVGQSLLDYYGPTLEQLSQQGLIECSAQRVYLTPRGRMLGNQVFAHFV
The following text describes a protein:
Function:
Catalyzes the transfer of a geranyl-geranyl moiety from geranyl-geranyl pyrophosphate to cysteines occuring in specific C-terminal amino acid sequences.
Sequence:
MHGRIKVRTSEEQKLQKQKEQQKKLVAYRMGMKQILSTRNKENYDPASLLLSGQLLSVNPDIYTLWNYRKEATLMELKENHSDAENGDEKSIEFCENELRLTEQCLLSNPKSYGSWHHRYWILNHHPKPNWQREFDLCTKYLSMDDRNFHCWDFRRLLVNKIGITLTDEIAFSTERININFSNYSSWHYRSTLQFLTDAESVAKELTLVQNAVFTDPIDTSAWFYLRWVLSNPNLRKTQKDELLEALEQLQELEPDCKWIVMAKCWLSGNITVLDKEHVENNVHYYKELIKLDPLRRGHYEDCLKIVETKID
The following text describes a protein:
Function:
G protein-coupled receptor activated by secretin (SCT), which is involved in different processes such as regulation of the pH of the duodenal content, food intake and water homeostasis. Ligand binding causes a conformation change that triggers signaling via guanine nucleotide-binding proteins (G proteins) and activates cAMP-dependent pathway. Upon binding to secretin, regulates the pH of the duodenum by (1) inhibiting the secretion of gastric acid from the parietal cells of the stomach and (2) stimulating the production of bicarbonate (NaHCO(3)) from the ductal cells of the pancreas (By similarity). In addition to regulating the pH of the duodenal content, plays a central role in diet induced thermogenesis: acts as a non-sympathetic brown fat (BAT) activator mediating prandial thermogenesis, which consequentially induces satiation. Mechanistically, secretin released by the gut after a meal binds to secretin receptor (SCTR) in brown adipocytes, activating brown fat thermogenesis by stimulating lipolysis, which is sensed in the brain and promotes satiation. Also able to stimulate lipolysis in white adipocytes. Also plays an important role in cellular osmoregulation by regulating renal water reabsorption. Also plays a role in the central nervous system: required for synaptic plasticity (By similarity).
Subcellular Localization:
Cell membrane; Multi-pass membrane protein. Basolateral cell membrane; Multi-pass membrane protein.
Sequence:
MRPHLSPPLQQLLLPVLLACAAHSTGALPRLCDVLQVLWEEQDQCLQELSREQTGDLGTEQPVPGCEGMWDNISCWPSSVPGRMVEVECPRFLRMLTSRNGSLFRNCTQDGWSETFPRPNLACGVNVNDSSNEKRHSYLLKLKVMYTVGYSSSLVMLLVALGILCAFRRLHCTRNYIHMHLFVSFILRALSNFIKDAVLFSSDDVTYCDAHRAGCKLVMVLFQYCIMANYSWLLVEGLYLHTLLAISFFSERKYLQGFVAFGWGSPAIFVALWAIARHFLEDVGCWDINANASIWWIIRGPVILSILINFILFINILRILMRKLRTQETRGNEVSHYKRLARSTLLLIPLFGIHYIVFAFSPEDAMEIQLFFELALGSFQGLVVAVLYCFLNGEVQLEVQKKWQQWHLREFPLHPVASFSNSTKASHLEQSQGTCRTSII
The following text describes a protein:
Function:
Subunit e, of the mitochondrial membrane ATP synthase complex (F(1)F(0) ATP synthase or Complex V) that produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. ATP synthase complex consist of a soluble F(1) head domain - the catalytic core - and a membrane F(1) domain - the membrane proton channel. These two domains are linked by a central stalk rotating inside the F(1) region and a stationary peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation (By similarity). In vivo, can only synthesize ATP although its ATP hydrolase activity can be activated artificially in vitro (By similarity). Part of the complex F(0) domain (By similarity).
Subcellular Localization:
Mitochondrion. Mitochondrion inner membrane.
Sequence:
MVPPVQVSPLIKLGRYSALVLGMAYGAKRYSYLKPRAEEERRVAAEEKKRLDELKRIERELAEGDTILK
The following text describes a protein:
Function:
Putative negative growth factor. Antagonist of dpp, a protein involved in patterning the dorsal region and in the development of the neuroectoderm; dpp inhibition is enhanced by tsg. Required for establishment of a narrow stripe of peak levels of BMP signaling in the dorsal midline of early embryos, that will give rise to the amnioserosa. During pupal development, plays a role in specification of the posterior crossvein in the wing. Exhibits both agonist and antagonist activities towards BMP signaling during pupal wing patterning.
Subcellular Localization:
Golgi apparatus membrane; Single-pass type II membrane protein. Cell membrane; Single-pass type I membrane protein. Secreted.
Sequence:
MANKLRKSNAIEWATATGTVPLLERSCCHSEDAALEPQASKTSHREQAPILRHLSQLSHLLIIAGLLIVCLAGVTEGRRHAPLMFEESDTGRRSNRPAVTECQFGKVLRELGSTWYADLGPPFGVMYCIKCECVAIPKKRRIVARVQCRNIKNECPPAKCDDPISLPGKCCKTCPGDRNDTDVALDVPVPNEEEERNMKHYAALLTGRTSYFLKGEEMKSMYTTYNPQNVVATARFLFHKKNLYYSFYTSSRIGRPRAIQFVDDAGVILEEHQLETTLAGTLSVYQNATGKICGVWRRVPRDYKRILRDDRLHVVLLWGNKQQAELALAGKVAKYTALQTELFSSLLEAPLPDGKTDPQLAGAGGTAIVSTSSGAASSMHLTLVFNGVFGAEEYADAALSVKIELAERKEVIFDEIPRVRKPSAEINVLELSSPISIQNLRLMSRGKLLLTVESKKYPHLRIQGHIVTRASCEIFQTLLAPHSAESSTKSSGLAWVYLNTDGSLAYNIETEHVNTRDRPNISLIEEQGKRKAKLEDLTPSFNFNQAIGSVEKLGPKVLESLYAGELGVNVATEHETSLIRGRLVPRPVADARDSAEPILLKRQEHTDAQNPHAVGMAWMSIDNECNLHYEVTLNGVPAQDLQLYLEEKPIEAIGAPVTRKLLEEFNGSYLEGFFLSMPSAELIKLEMSVCYLEVHSKHSKQLLLRGKLKSTKVPGHCFPVYTDNNVPVPGDHNDNHLVNGETKCFHSGRFYNESEQWRSAQDSCQMCACLRGQSSCEVIKCPALKCKSTEQLLQRDGECCPSCVPKKEAADYSAQSSPATNATDLLQQRRGCRLGEQFHPAGASWHPFLPPNGFDTCTTCSCDPLTLEIRCPRLVCPPLQCSEKLAYRPDKKACCKICPEGKQSSSNGHKTTPNNPNVLQDQAMQRSPSHSAEEVLANGGCKVVNKVYENGQEWHPILMSHGEQKCIKCRCKDSKVNCDRKRCSRSTCQQQTRVTSKRRLFEKPDAAAPAIDECCSTQCRRSRRHHKRQPHHQQRSSS
The following text describes a protein:
Function:
Transcriptional regulator that binds CpG islands in promoters where the DNA is methylated at position 5 of cytosine within CpG dinucleotides. May directly affect chromatin structure by inducing intra- and inter- chromatin compaction via bridging over multiple methylated CpG sites. Acts as an anti-silencing factor that prevents DNA hypermethylation and gene repression. Requires high mCG density for binding. Recognizes preferentially mCGs located in transposable elements. Required for active DNA demethylation. Prefers to target genomic loci around chromocenters.
Subcellular Localization:
Nucleus. Chromosome. Note=Associated with heterochromatin, at all chromocenters. Excluded from nucleolus.
Domain:
The methyl-CpG-binding domain (MBD) functions both in binding to methylated DNA and in protein interactions (By similarity). The number of MBD domains may affect binding affinity, mobility within the nucleus, and subnuclear localization (By similarity). The C-terminal domain (232-306) has a very strong chromatin binding affinity and thus is coined 'sticky-C' (StkC). StkC confers intranuclear immobility, but has no effect on subnuclear localization. It is necessary for the interaction with IDM2 and IDM3, and for the anti-silencing function.
Sequence:
MQTRSSSSPSANHRRETQLQIADPTSFCGKIMPGWTVVNRPRSSNNGVVDTYFIEPGTGRQFSSLEAIHRHLAGEVNDRRLTRAGSFFQDKTRVYEGSRTKQDHCGVEYASKGFRLPRGWSVEEVPRKNSHYIDKYYVERKTGKRFRSLVSVERYLRESRNSIEQQLRVLQNRRGHSKDFRLPDGWIVEEKPRRSSSHIDRSYIEPGTGNKFRSMAAVERYLISVGNITLDSVSMVHSERLPLLMNRNGIRFQSEVIDPNPPKKVKWVLTGSGGNMFTANVRGSNVSSLVKHTWSEAFVSLIEDRS
The following text describes a protein:
Function:
Electroneutral sodium and chloride ion cotransporter, which acts as a key mediator of sodium and chloride reabsorption in kidney distal convoluted tubules. Also acts as a receptor for the pro-inflammatory cytokine IL18, thereby contributing to IL18-induced cytokine production, including IFNG, IL6, IL18 and CCL2. May act either independently of IL18R1, or in a complex with IL18R1.
Subcellular Localization:
Apical cell membrane; Multi-pass membrane protein.
Sequence:
FQPGPTAIPFLHSPPPQAGVWGRRRPPWEAHAARVDLPGTALQVQEDAAAPSLSGGADRGGVAAAAGDGLGRPLGPTPSQSRFQVDLVTENAGRAAAAAAAAAAAAAAVAGSPAEPPRDGRASGENGAGKSSEEAKGRFRVNFVDPAASSSADESPSDAAGVGGEGANVSFQNGGDTVLSEGSSLHSGSGGGGGHHHHYYYDTHTNTYYLRTFGHNTMDAVPRIDHYRQTAANLGEKLLRPSLAELHDELEKEPFEDGFANGEEGTPTREAVVTYTAESKGVVKFGWIKGVLVRCMLNIWGVMLFIRLSWIVGQAGIGLSVLVIAMATVVTTITGLSTSAIATNGFVRGGGAYYLISRSLGPEFGGAIGLIFAFANAVAVAMYVVGFAETVVELLKEHSILMVDEINDIRIIGAITVVLLLGISVAGMEWEAKAQIVLLVILLLAIVDFVIGTFIPMESKRSKGFFSYQNEIFTENFGPDFREDESFFSVFAIFFPAATGILAGANISGDLADPQSAIPKGTLLAILITTLVYIGIAVSVGSCVVRDATGNANDTLTVELANCSSAACSLGFDFSACERSPCGYGLMNNFQVMSMVSGFAPLISAGIFSATLSSALASLVSAPKIFQALCKDNIYPAFQMFIKAMEEQRATPSPKKTQKHALQHSIRLSGVEDHVKNFRPQCLVMTGSPNSRPALLHLVHAFTKNVGLMVCGHVHMGPRRQAMKEISIDQTKYQRWLIKNKMKAFYAPVHADDLRDGAQYLMQAAGLGRMKPNTLVLGFKKDWLQADMRDVDTYMNIFHDAFDLQFGVVVIRLKEGLDISHLQGQEELLSSQEKSPGSKDVVLSVEYSRKGDVDPSKPSDEKSPVMQKDEEEDGKTPTQPLLKKEPKGPVAPLNVADQRLLEASTQFQKKQGKNTIDVWWLFDDGGLTLLIPYLLTTKKKWKDCKIRVFIGGKINRIDHDRRAMATLLSKFRIDFSDIMVLGDINTKPKKENIAAFEEMIEPLRLHEDDKEQDVSDKMKEDEPWRITDNELELYKTKTYRQIRLNELLKEHSSTANIIVMSLPVARKGGVSSALYMAWLEVLSRDVPPVLLVRGNHQSVLTFYS
The following text describes a protein:
Function:
Tubulin-binding protein that acts as a negative regulator of Notch signaling pathway. Shuttles between the cytoplasm and the nucleus and mediates the nuclear export of RBPJ/RBPSUH, thereby preventing the interaction between RBPJ/RBPSUH and NICD product of Notch proteins (Notch intracellular domain), leading to down-regulate Notch-mediated transcription. May play a role in neurogenesis (By similarity).
Subcellular Localization:
Cytoplasm. Nucleus. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome. Note=Shuttles rapidly between the cytoplasm and the nucleus. The function of centrosome localization is still unclear (By similarity).
Sequence:
MQALHLQHRNPRSYRVKARASYVDETLFGSPTGTRPTLPDFDPPWVQNCNRSRGVSPGPPKVSLAKRDCESPSSRGSTPNLTPRKKNKYRLIGHTPSYCDESLFGSRPQGTSKERSRTAVEDAAKLRTLFWTPPATPRGSHSPRPRETPLRAIHPTGPPRTEPRVATGSQMVSRDGLDAPRSLGQRRSYSLTHLAVPSTGHPASTAPQTNGPWSPRPYTSGATVQSPLVTRKVCSGSVSGPTTPQRGACPQKPKPPWK
The following text describes a protein:
Function:
Catalyzes the opening of the heme ring to form the open-chain tetrapyrrole biliverdin IX with the release of iron and carbon monoxide (CO). Produces specifically the biliverdin IX-alpha isomer. Plays a minor role in phytochrome assembly and photomorphogenesis.
Subcellular Localization:
Plastid, chloroplast.
Sequence:
MATSRLNASCRFPASRRLDCESYVSLRAKTVTIRYVRTIAAPRRHLVRRANEDQTLVVNVVAAAGEKPERRYPREPNGFVEEMRFVVMKIHPRDQVKEGKSDSNDLVSTWNFTIEGYLKFLVDSKLVFETLERIINESAIQAYAGLKNTGLERAENLSRDLEWFKEQGYEIPESMVPGKAYSQYLKNIAEKDPPAFICHFYNINFAHSAGGRMIGTKVAEKILDNKELEFYKWDGQLSELLQNVSEELNKVAELWTREEKNHCLEETEKSFKFYWEIFRYLLS
The following text describes a protein:
Function:
Sequence-specific transcription factor which is part of a developmental regulatory system that provides cells with specific positional identities on the anterior-posterior axis.
Subcellular Localization:
Nucleus.
Sequence:
MNSYHGFRDTTSLFIKGYHATGVMRLHQDHGSTADFPSREDVNNEADFLQYHFTNLCATATGACSKPCEDPGRANSTRPPFPQNQDFYRPVHPNRPQVPSFQSCREQGLSRKGFSPSSDTFRTFSSAHCELGPVNNTQTEVRTYDGPVRHSAVEDDNTGHGALNTLNETLHSGKTFEWMRVRRNQSRAAKIQLGKCSDRELKTNHGRDSDEDTSSGGSRTNFTTKQLTELEKEFHFNKYLTRARRIEIANPLQLSETQVKIWFQNRRMKQKKMLREGLAQGLMLISGCDEDSKKSDTCSSPD
The following text describes a protein:
Function:
Plays a role in the recruitment of the exosome to pre-rRNA to mediate the 3'-5' end processing of the 5.8S rRNA.
Subcellular Localization:
Cytoplasm. Nucleus, nucleolus. Nucleus.
Sequence:
MVNDMETDIGTPVDDYGVLKGDLVFIRNNENLMQAIDQIQVTLANVNREYEKYPNFTAEEKVRFDTLCAFCVNSLFWMHEKMLGRPNTVMDDIKADLDRVREAMKRLQTIHDNLTKRPRLDQPAAQRFVRAGLYDANNAESDKQNDAPPNKKKRREKKAEPE
The following text describes a protein:
Function:
An L-glutamate ligase that catalyzes the ATP-dependent post-translational addition of glutamate residues to the C-terminus of ribosomal protein bS6 (RpsF). Is also able to catalyze the synthesis of poly-alpha-glutamate in vitro, via ATP hydrolysis from unprotected glutamate as substrate. The number of glutamate residues added to either RpsF or to poly-alpha-glutamate changes with pH.
Sequence:
MKIAILSRDGTLYSCKRLREAAIQRGHLVEILDPLSCYMNINPAASSIHYKGRKLPHFDAVIPRIGTAITFYGTAALRQFEMLGSYPLNESVAIARARDKLRSMQLLARQGIDLPVTGIAHSPDDTSDLIDMVGGAPLVVKLVEGTQGIGVVLAETRQAAESVIDAFRGLNAHILVQEYIKEAQGCDIRCLVVGDEVVAAIERRAKEGDFRSNLHRGGAASVASITPQEREIAIKAARTMALDVAGVDILRANRGPLVMEVNASPGLEGIEKTTGIDIAGKMIRWIERHATTEYCLKTGG
The following text describes a protein:
Function:
Functions in inorganic phosphate uptake, although probably not the main uptake protein under phosphate starvation. Binds phosphate; probably able to bind both H(2)PO(4)(-) and HPO(4)(2-). Part of the ABC transporter complex PstSACB involved in phosphate import (Probable); A host TLR2 agonist (toll-like receptor), shown experimentally for human and mouse. Requires both host TLR1 and TLR2 as coreceptors to elicit host response in mouse (TLR6 may also play a role) neither CD14 or CD36 function as accessory receptors. Protein purified from culture filtrate induces host (human) monocytes to produce TNF-alpha, IL-6 and IL-12 p40 (IL12B) via ERK1/2 (MAPK3 and MAPK1) and p38 MAPK pathways; MEK inhibitors U0126 and PD98059 and p38 inhibitor SB203580 block most cytokine production. Host ERK1/2 and p38 MAPK activation is mediated mainly by TLR2, but also partially by TLR4, and unlike the case for lipoprotein LpqH the protein moiety of PstS1 seems to be the antigenic agent. Greater activation of ERK1/2 and p38 MAPK is seen in patients with active pulmonary tuberculosis than in tuberculin-negative patients. Induces apoptosis when incubated with human monocyte-derived macrophages via TLR2. Protein purified from culture filtrate acts via TLR2 and TLR4 to induce host macrophage (shown for mouse) endoplasmic reticulum stress-mediated apoptosis via MAPK (at least JNK), C-C motif chemokine 2 (MCP-1, Ccl2) and ZC3H12 endoribonucleases (MCPIP, Zc3h12). Functions as an adhesin, binds to human and mouse macrophages via mannose residues, binds to the mouse macrophage mannose receptor (possibly Mrc1) and mediates bacterial phagocytosis.
Subcellular Localization:
Cell membrane; Lipid-anchor. Cell surface. Secreted, cell wall. Secreted. Note=A soluble cell wall-associated protein. Also found in culture filtrate in increasing quantities during growth.
Sequence:
MKIRLHTLLAVLTAAPLLLAAAGCGSKPPSGSPETGAGAGTVATTPASSPVTLAETGSTLLYPLFNLWGPAFHERYPNVTITAQGTGSGAGIAQAAAGTVNIGASDAYLSEGDMAAHKGLMNIALAISAQQVNYNLPGVSEHLKLNGKVLAAMYQGTIKTWDDPQIAALNPGVNLPGTAVVPLHRSDGSGDTFLFTQYLSKQDPEGWGKSPGFGTTVDFPAVPGALGENGNGGMVTGCAETPGCVAYIGISFLDQASQRGLGEAQLGNSSGNFLLPDAQSIQAAAAGFASKTPANQAISMIDGPAPDGYPIINYEYAIVNNRQKDAATAQTLQAFLHWAITDGNKASFLDQVHFQPLPPAVVKLSDALIATISS
The following text describes a protein:
Function:
The coatomer is a cytosolic protein complex that binds to dilysine motifs and reversibly associates with Golgi non-clathrin-coated vesicles, which further mediate biosynthetic protein transport from the ER, via the Golgi up to the trans Golgi network. The coatomer complex is required for budding from Golgi membranes, and is essential for the retrograde Golgi-to-ER transport of dilysine-tagged proteins.
Subcellular Localization:
Cytoplasmic vesicle, COPI-coated vesicle membrane; Peripheral membrane protein; Cytoplasmic side. Golgi apparatus membrane; Peripheral membrane protein; Cytoplasmic side.
Sequence:
MDSDQDFHVKTLFYQGSYSASHDAISSINDPSFQLVLFSARCLICLKKPGEAIKLLKQHHDSEPAARALTLLAKFYQDSPSSKAEIDKFGEAAEALIEEIADEENDGPDSVLRVTLATILTLAENLSLAIFILKQGVQLKSLEAVAALISLYLSPRLRRPDLARSLYTSAKAWADDAILLQMAEAWIGATTGSAAGNSNGREPGGYQSAFYVFDEVTNTAVTKPNQVNVVGLNGKAITQLAMGHVEEAQANLTEALKADPENENTLANSIVISARLESPPSEIATSIQKLKTLNPKHPLIVDLDRQSALFDEAASQFVASTA
The following text describes a protein:
Function:
Has an organic peroxide-dependent peroxidase activity. Exhibits strong peroxidase activity using organic hydroperoxides as cosubstrates, weak peroxidase activity using hydrogen peroxide and negligible catalase activity. May have a role in elimination of reactive oxygen species, in particular by deactivating hydroperoxides.
Sequence:
MSGGLTPDQAIDAIRGTGGAQPGCRALHAKGTLYRGTFTATRDAVMLSAAPHLDGSTVPALIRFSNGSGNPKQRDGAPGVRGMAVKFTLPDGSTTDVSAQTARLLVSSTPEGFIDLLKAMRPGLTTPLRLATHLLTHPRLLGALPLLREANRIPASYATTEYHGLHAFRWIAADGSARFVRYHLVPTAAEEYLSASDARGKDPDFLTDELAARLQDGPVRFDFRVQIAGPTDSTVDPSSAWQSTQIVTVGTVTITGPDTEREHGGDIVVFDPMRVTDGIEPSDDPVLRFRTLVYSASVKLRTGVDRGAQAPPV