lhallee/plat_data huggingface dataset:
The following text describes a protein:
Function:
Probable oxidoreductase; part of the gene cluster that mediates the biosynthesis of patulin, an acetate-derived tetraketide mycotoxin produced by several fungal species that shows antimicrobial properties against several bacteria. PatJ acts with patO in the vacuole to convert gentisyl alcohol to isoepoxydon. The pathway begins with the synthesis of 6-methylsalicylic acid by the polyketide synthase (PKS) patK via condensation of acetate and malonate units. The 6-methylsalicylic acid decarboxylase patG then catalyzes the decarboxylation of 6-methylsalicylic acid to yield m-cresol (also known as 3-methylphenol). These first reactions occur in the cytosol. The intermediate m-cresol is then transported into the endoplasmic reticulum where the cytochrome P450 monooxygenase patH converts it to m-hydroxybenzyl alcohol, which is further converted to gentisyl alcohol by the cytochrome P450 monooxygenase patI. The oxidoreductases patJ and patO further convert gentisyl alcohol to isoepoxydon in the vacuole. PatN catalyzes then the transformation of isoepoxydon into phyllostine. The cluster protein patF is responsible for the conversion from phyllostine to neopatulin whereas the alcohol dehydrogenase patD converts neopatulin to E-ascladiol. The steps between isoepoxydon and E-ascladiol occur in the cytosol, and E-ascladiol is probably secreted to the extracellular space by one of the cluster-specific transporters patC or patM. Finally, the secreted patulin synthase patE catalyzes the conversion of E-ascladiol to patulin (Probable).
Subcellular Localization:
Vacuole lumen. Cytoplasmic vesicle lumen.
Sequence:
MAPFVPYHYSAGQSTIVKFGGLLTTEFLEPPPGRCFLFRQTYRHTIEGSIPENLRKLINSPDRPKGPPPHFHQFQTEYFRVENGVLGISVDGVVRRITPEDGEISVKAGSVHNFFIHPDSPENMTVYLSASDSGNDYQLDRVFFENWYGYWHDALLHDGGIDWIQFLAIQDGGDAYTPAPAWVPFRRQVGYWTCVIVGRWIGGLLGYKPFFREYTTDWDFAVAKMKGSFFQRHLVHAAFEEEKSWTKQAELEPKGKPENAEFEPWTEDMSPAPLSLGPVAYEQGLFHGVQPGSVNGSNGHSTGVESKLEQLGSRAQRRVVIDDAGK
The following text describes a protein:
Function:
Calcium- and integrin-binding protein (By similarity). Plays a role in intracellular calcium homeostasis. Critical for proper photoreceptor cell maintenance and function. Required for prevention of light-dependent retinal degeneration.
Miscellaneous:
MISCELLANEOUS: The binding of either calcium or magnesium significantly increases the structural stability of the protein in comparison to apo-CIB (calcium- and magnesium-free form).
Subcellular Localization:
Cytoplasm.
Sequence:
MGNKVVTFTEQELDDYQDCTFFTRKEILRVHKRFRELRPDLVPRQMTEGQASSVKVPCECIEKMPELRENPFRRRICEAFSRDGQGNLSFEDFLDALSVFSEQAPRDIKVFYAFKIYDFDQDGFIGHADLMSCLTTMTKNELSPEEHQQIADKVIEEADVDGDGKLSILEFEHVILRAPDFLSTFHIRI
The following text describes a protein:
Function:
Catalyzes the hydrolysis of ATP coupled with the transport of calcium.
Subcellular Localization:
Endomembrane system; Multi-pass membrane protein. Membrane; Multi-pass membrane protein.
Sequence:
MVAANRYRSVPTSESDVQTAPIPPSTSQLPPSDQFAFSTTLRKAHSDDPYFGAASDHGAYPPFSSPSRTTAHKPNASDASFRQAASTDLYGGSLHSVAVSASAHYTHLSVQQCLDSLHCPSLDTGLSPLLVHEARREAGGYNEFAVRAGDEPWKKFLAQFQEPLILLLLGSAAVSLLIGQIDDAVSITIAIIIVISVAFYQEQKSEKSLEALNKLVPHYCHLIRDGVNSSVLANELVPGDVVTFSTGDRIPADVRICECVSLEVDESTLTGEIKPRRKHAGVVPRASNGSAAANGNANGTNANASVPATVNGSNADDAVATTSINERENIAFMGTLVKSGHGKGIVVGTGATTEFGMIFSMVDEVIEKRTPLQLSMDELAKKLSMISFAVIAVICLMGVWQRRPWLEMFTIGVSLAVAAIPEGLPIVVTVTLALGVLRMSHRKAIVKKLPSVETLGSVSVVCSDKTGTLTTNEMTVTKCWTAEDEIIDVAQHMSHRHTQALSRLLLTANLCNNSHRNELGTNVGQATDVALVNILKVFGLEDQRPYFKRSTEIAFDSESKFMAVTGVLSTADAGSTAETVYVKGAFEVVLAKSSAVLGADGSPQRLDERWRNRISQAAEKLSSQGLRVVGCASGASGSLEQRTLTFSGLQAMHDPPRPGVKEAIASLACGGVQVVMITGDSQVTAVAMARQLGILPASTSSSSTSSVLTGRQIDALSERQLQERIPSISVFARTTPRHKMSIISALQSCGAVVAMTGDGVNDAPALKMADIGISMGKGGTDVAKEAADVILVDDNFATILAAVEEGKGIFYNIQNFLSFQLSTAVAALTLITLSTAFRMKLPLNAMQILFINILMDGPPSQSLGVDPVDRKSVMSRAPRAKNAPVLNNRLLYRIAFSATMVVLGTLYVYIHELVPVDIEAPPAPDGMHTFDVKPQEKVADQRDSTMTFTCFVFLDLVSAVQNRGLYTRITANRMLGLTVGISLLAQLSMVYLPPLQGVFQTTPLAFADLVFLAFIAALSFGLHELRRMWERTTADHDLAEFSATAAGECA
The following text describes a protein:
Function:
Plays a critical role in eye formation by regulating the initial specification of retinal cells and/or their subsequent proliferation.
Subcellular Localization:
Nucleus.
Sequence:
MRLVGSQYKDMEDRLSPSARLVRSPGSQTRIHSIESILGFKGETLFHPAFPYGSGKTGKDTEHLSPKKDSNKHFDGVCRSTVMVSPDLPDADGGKLSDDENPKKKHRRNRTTFTTFQLHELERAFEKSHYPDVYSREELALKVNLPEVRVQVWFQNRRAKWRRQEKLEVSSIKLQESSMLSIPRSGPLSLGSGLPLEPWLTGPISTSSSPLQSLPSFITPQQAVPASYTPPQFLSSSTLNHSLPHIGAVCPPYQCSGFMDKFSLQEADPRNTSIASLRMKAKEHIQSIGKTW
The following text describes a protein:
Function:
Required for the assembly of the V0 complex of the vacuolar ATPase (V-ATPase) in the endoplasmic reticulum.
Subcellular Localization:
Endoplasmic reticulum membrane; Multi-pass membrane protein. Endoplasmic reticulum-Golgi intermediate compartment membrane; Multi-pass membrane protein. Cytoplasmic vesicle, COPII-coated vesicle membrane; Multi-pass membrane protein.
Sequence:
MSKSKQNRNTISKAEQRAEYRTFKTVFLYCILIIALPVLTFFTSKHWIFDQLLQLSSVSSNIYSAVSAVVALHGALFLFIYKAYFAVSNESVDGRGDKVAQKED
The following text describes a protein:
Function:
May be involved in transcriptional regulation.
Subcellular Localization:
Nucleus.
Sequence:
MMAKPTLRGNGTNPETFRQRFRRFHYQEVAGPREAFSQLWELCCRWLRPEVRTKEQIVELLVLEQFLTILPGEIQNWVQEQCPESGEEAVALVEDLEREPGRPGRSVTVSVKGQEVRLEKMTPLKSSRELLSVRQESVEPQPRGVTKKERARSPDLGPQEQMNPKEKLRPFQRSGFPFPKSGVVSRLEQGEPWVPDLGSKEKELPRGSHTGDKQMHADLLSPKRERRSWVDQDYWGFEDEKVAGVHWGYEETRTLLAILSQTEFYEALRNCHRNSQVYGAVAERLREYGFFRTLEQCRTKFKGLQKSYRKVKSGHPPETCPFFEEMEALMSAQVIALPSNGLEEAASHSGLVGSDPETEEPGQGGWQHEEAEEALAEESGSDEMGQEALPQDPENSTAPVLFRSPSGVHWGYEETKTYLAILSETQFYEALRNCHRNSQLYGAVAERLWEYGFLRTPEQCRTKFKSLQTSYRKVKNGQAPETCPFFEEMDALVSARVVAPPSDSQEEETASCPIQETSETEAEKQADMAEETIEEDSEDDEEDTEVPLEVVMTRAPVLFQSPSGFEAGFDNEENLKRDISEEVQLHRTLLARSERKVSRRLTQGKGGESEYRSGQQWENTPEERRGKPAFPERSLGKVLNHQRPYLGEKPCKYLRYSKSFGPNSHLVHQISHQVENPYKCADCGKSFSRSARLIRHRRIHTGEKPYKCLDCGKSFRDSSNFITHRRIHTGEKPYQCGECGKRFNQSSSLIIHQRTHTGEKPYQCEECGKSFNNSSHFSAHRRIHTGERPHVCPDCGKSFSKSSDLRAHHRTHTGEKPYGCHDCGKCFSKSSALNKHREIHTREKLLSQSTPKQ
The following text describes a protein:
Function:
Part of the spliceosome which catalyzes two sequential transesterification reactions, first the excision of the non-coding intron from pre-mRNA and then the ligation of the coding exons to form the mature mRNA. Plays a role in stabilizing the structure of the spliceosome catalytic core and docking of the branch helix into the active site, producing 5'-exon and lariat intron-3'-intermediates.
Subcellular Localization:
Nucleus.
Sequence:
MSERKVLNKYYPPDFDPAKIPRRKLAKDRQQVVRLMAPFSMQCLSCTEFIYKGKKFNARKEAAAGEHYFGIKIFRFYIKCPRCSNEITFKTDPKHSDYVAEHGAQRNFEPWREEEAAKNAGSDSEDDVERLLAVEQAELEEEQEDSMRSLEKNQIESKREMEILDKLQEIRTRNARLERSANGRGADGVLASVSSRIQSGLAGAKEVLEQERQLKELEEDEAEVAKYFTKFAALPNKSMPSIQEHDDNDDDDGPKPSGSGSHLEQEAGEKDDRQHSAINQTRETITQPTPESITIKRKFTDVEPDVHSLLSEKSREMLANASGFTKLPPKKKKNATVNAFGVKIIKKS
The following text describes a protein:
Function:
Involved in the structural organization of the epidermis (By similarity). Involved in the mineralization and structural organization of enamel.
Subcellular Localization:
Secreted. Note=Secreted at a very early stage of enamel formation, and tightly bound to the surface of the growing crystallites.
Sequence:
SLRKTVQDLLVQLQEAERQHQSERVDFEATLSRYQREAEQSHVALQRAEDRVEQKEAEVEELQKRLLGMETEHQALLAKVREGVTALEELRGKNSDCRAEQEKAANLEKEVAGLREKIHHLDDMLKSQQRKVRQMIEQLQNSKTVIQSKDTAIQELKEKIAYLEAENLEMHDRMEHLIEKQISHGNFS
The following text describes a protein:
Function:
Maybe involved in both the vernalization and photoperiod pathways by regulating gene expression. Binds preferentially to dimethylated histone H3 'Lys-9' (H3K9me2). Promotes flowering in non-inductive photoperiods (e.g. short days) through the maintenance of the epigenetically repressed state of MAF5 via H3K9me2 and plant homeodomain / polycomb repressive complex 2 (PHD-PRC2)-dependent H3K27me3.
Subcellular Localization:
Nucleus. Note=Probably DNA-associated.
Sequence:
MDSSLDGAAGDSSKCSEMSVDEKRQLVYELSKQSHLAAEVLQAWSRQEILQILCAEMGKERKYTGLTKVKIIETLLKIVSEKNSGECEGKKRDSDCLPIQRNTKRQRKVDNPSRYVIPATNIVTSNNASGSCSSVNTKGESTTIYCKNLACRAVLRQEDSFCRRCSCCICRKYDDNKDPSLWLTCSSDPPFEGESCGFSCHLECAFNTEKSGLGKDKQSEGCCFYCVSCGKANSLLECWKKQLTIAKETRRVEVLCYRLFLVQKLLKSSTKYRNLCEVVDEAVKTLEADVGPLTGLPMKMGRGIVNRLHSGPDVQKLCSSALESLETIATTPPDVAALPSPRSSKMQQDCSYVLSNEISADTATTGSTKIRFEDVNATSLTVVLASNEIPSPPNIVHYSIWHRKVPEKDYPEKSTCTLFIPNTRFVVSGLAPASEYCFKVVSYSGTREMGVDEINVLTRSAEEGANCSSAVERSVSPLTNCSTLSSNPSSVEAESNNDYIVPKKPSSKNEDNNSPSVDESAAKRMKRTTDSDIVQIEKDVEQIVLLDDEEQEAVLDKTESETPVVVTTKSLVGNRNSSDASLPITPFRSDEIKNRQARIEISMKDNCNNGDHSANGGTESGLEHCVKIIRQLECSGHIDKNFRQKFLTWYSLRATSQEIRVVKIFIDTFIDDPMALAEQLIDTFDDRVSIKRSAVGGSGASAVVPSGFCMKLWH
The following text describes a protein:
Function:
Sodium-independent anion exchanger which mediates the electroneutral exchange of chloride for bicarbonate ions across the cell membrane. Plays an important role in osteoclast differentiation and function (By similarity). Regulates bone resorption and calpain-dependent actin cytoskeleton organization in osteoclasts via anion exchange-dependent control of pH (By similarity). Essential for intracellular pH regulation in CD8(+) T-cells upon CD3 stimulation, modulating CD8(+) T-cell responses (By similarity).
Subcellular Localization:
Apical cell membrane; Multi-pass membrane protein. Basolateral cell membrane; Multi-pass membrane protein.
Sequence:
MSSAPRRPASGADSLHTPEPESLSPGTPGFPEQEEEDELRTLGVERFEEILQEAGSRGGEEPGRSYGEEDFEYHRQSSHHIHHPLSTHLPPDARRRKTPQGPGRKPRRRPGASPTGETPTIEEGEEDEDEVGEAEGFRAPPQQPSPASSPSAVQFFLQEDEGTDRKAERTSPSPPTQTPHQEAAPRASKGAQTGTLVEEMVAVASGTAGGDDGGAAGRPLTKAQPGHRSYNLQERRRIGSMTGVEQALLPRVPTDESEAQTLATADLDLMKSHRFEDVPGVRRHLVRKNAKGSTQAAREGREPGPTPRARPRAPHKPHEVFVELNELQLDKNQEPQWRETARWIKFEEDVEEETERWGKPHVASLSFRSLLELRRTLAHGAVLLDLDQQTLPGVAHQVVEQMVISDQIKAEDRANVLRALLLKHSHPSDEKEFSFPRNISAGSLGSLLGHHHAQGTESDPHVTEPLIGGVPETRLEVDRERELPPPAPPAGITRSKSKHELKLLEKIPENAEATVVLVGCVEFLSRPTMAFVRLREAVELDAVLEVPVPVRFLFLLLGPSSANMDYHEIGRSISTLMSDKQFHEAAYLADERDDLLTAINAFLDCSVVLPPSEVQGEELLRSVAHFQRQMLKKREEQGRLLPPGAGLEPKSAQDKALLQMVEVAGAAEDDPLRRTGRPFGGLIRDVRRRYPHYLSDFRDALDPQCLAAVIFIYFAALSPAITFGGLLGEKTQDLIGVSELIMSTALQGVIFCLLGAQPLLVIGFSGPLLVFEEAFFSFCKSNQLEYLVGRVWIGFWLVLLALLMVALEGSFLVRFVSRFTQEIFAFLISLIFIYETFYKLIKIFQEHPLHGCSVSNDSEADSSSNNMTWAATTLAPDNSSASGQERPRGQPNTALLSLVLMAGTFFIAFFLRKFKNSRFFPGRIRRVIGDFGVPIAILIMVLVDYSIEDTYTQKLSVPSGFSVTAPDKRGWVINPLGEKTPFPVWMMVASLLPAVLVFILIFMETQITTLIISKKERMLQKGSGFHLDLLLIVAMGGICALFGLPWLAAATVRSVTHANALTVMSKAVAPGDKPKIQEVKEQRVTGLLVALLVGLSMVIGDLLRQIPLAVLFGIFLYMGVTSLNGIQFYERLHLLLMPPKHHPDVTYVKKVRTMRMHLFTALQLLCLALLWAVMSTAASLAFPFILILTVPLRMVVLTRIFTEREMKCLDANEAEPVFDECEGVDEYNEMPMPV
The following text describes a protein:
Function:
Synthesizes nicotianamine, a polyamine which serves as a sensor for the physiological iron status within the plant, and/or might be involved in the transport of iron.
Sequence:
MGNQEERLVQRVTEIYECVSKLPTLSPSKEVNELFTELVNICIPVIAIDVSKLSSEVQAMRSELIMLCGEAEGLLESHHSDLLASYDNPLDHLRLFPYYSNYLKLSLLEYTLLARHVSSRPGRVAFVGSGPLPLTSIVLAKRHMPVAEFHNYDLDPTANDRASRLVRSDPDMAARMAFHTADVLSVTDELRGFDVVFLAALVGVGHDEKVRVIEHLARHMAPGAVLVARSAHSARAFLYPVVEPAELTGFEVLTVHHPVDEVINSVIVARKPKDDHAAGAAAVTRPCKCCEMVQGFHHFRHGSVMGDAAPEELPS
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. This sigma factor is involved in regulation of expression of heat shock genes. Intracellular concentration of free RpoH protein increases in response to heat shock, which causes association with RNA polymerase (RNAP) and initiation of transcription of heat shock genes, including numerous global transcriptional regulators and genes involved in maintaining membrane functionality and homeostasis. RpoH is then quickly degraded, leading to a decrease in the rate of synthesis of heat shock proteins and shut-off of the heat shock response.
Miscellaneous:
MISCELLANEOUS: May only be involved in heat shocks that occur during exponential phase of growth under aerobic conditions. Different mechanisms may play a prime role during stationary phase and anaerobic growth.
Subcellular Localization:
Cytoplasm.
Domain:
The sigma-70 factor domain-2 mediates sequence-specific interaction with the -10 element in promoter DNA, and plays an important role in melting the double-stranded DNA and the formation of the transcription bubble. The sigma-70 factor domain-2 mediates interaction with the RNA polymerase subunits RpoB and RpoC (By similarity); The sigma-70 factor domain-4 contains a helix-turn-helix (H-T-H) motif that mediates interaction with the -35 element in promoter DNA. The domain also mediates interaction with the RNA polymerase subunit RpoA (By similarity).
Sequence:
MTDKMQSLALAPVGNLDSYIRAANAWPMLSADEERALAEKLHYHGDLEAAKTLILSHLRFVVHIARNYAGYGLPQADLIQEGNIGLMKAVRRFNPEVGVRLVSFAVHWIKAEIHEYVLRNWRIVKVATTKAQRKLFFNLRKTKQRLGWFNQDEVEMVARELGVTSKDVREMESRMAAQDMTFDLSSDDDSDSQPMAPVLYLQDKSSNFADGIEDDNWEEQAANRLTDAMQGLDERSQDIIRARWLDEDNKSTLQELADRYGVSAERVRQLEKNAMKKLRAAIEA
The following text describes a protein:
Function:
Inactive carboxypeptidase that may play a role in cell wall organization and biogenesis.
Subcellular Localization:
Secreted.
Sequence:
MLIALLWGSHVQPSLQYILPQSVFTSPELPVDGENTLKEEEFNEPVAFAANVPEYFSQYADDTVVRVFLDSREEKGVLMNELSGYNLDVWKDEGDEIDVRIHRDGLPRLEREGWKFTVVISNVTETLLRSVSHEHEREHEREHEREHEHEHFHNGADNDNSDDADPAFTPSPFSSYDRFFSDYQRLESFNTWMRLQASLFPDLSELFSLGTSSEGRTIMALRLHGHRSRQIPVNEKRPAIVVFAGVHAREWIANPTVVYAAQRLMSSYDSDPQSRRLLDSFDWIFVPVVNVDGYEYTWTNDRLWRKNRQSFNYSSCVGIDLDHNFDFAFDYSKRARNPCSEMYQGKYAFEAPEAAALAKLLSETLPNSGYYTAGLIDVHSYSQSVLWPYASSCDIVPRDEENFEELAIGMVKELHSVHHHVYMYGQACTSAGIYSEFEETGTALDWSYELAGVKWPYVVKLRDTGNYGFLLPAHHIIPTAEEFYAMLRYYGDFISQF
The following text describes a protein:
Function:
Component of the MICOS complex, a large protein complex of the mitochondrial inner membrane that plays crucial roles in the maintenance of crista junctions, inner membrane architecture, and formation of contact sites to the outer membrane.
Subcellular Localization:
Mitochondrion inner membrane; Single-pass membrane protein.
Sequence:
MWRVPTNLPKCLARTHVAVAVKRNIRTSKVLQSQDVNSAGGGGGGILKKLIALTFAGAGGVVGYSWYDPEFKKLVEENVPYAKECYDAVFQYLPESASTIEDAVKRLPIKTTEITTVPPPVQAPIQEDSKPEVKAEEKVKTKKEREKEKKEEAEKLLKLREENEINQNKALEALLMRTFTESASVMEAAMKSAHSAAEAVKEHTVKLKEALQKVDAKEGEWEAVTRAHDAKVKAMQHFEEVNEKAKQELAKLREVISTGKSNKVTKKNKLLWSTEDEANKLNRSFNTALNEVSKAEADSKVFKEYRDLIKKGKEQFKKELESIMPDVKKATTSVAKLTEDELNALIAHAHKRIDQLQRQLAEQQALEQLRINEALSRQREEDAAILLVSINKEKELWDNEINLIKAKWDIDARVNFEEELKLQLTRQAAAHSDHISEVLRAQQRELEAKFSLMLSEHVENERREFQRQVAGWVARLHGIEDAIDKRASLEKQGHQVQKLWLACESLQTVLNTGKLGATSWEGRLKPLAADVELIRSASTGQPAVEIILDSIPEVALNRGVWTEAALIERFKRVCKISKRVAMIDETTGVSGSLFKYGLSYLQSMFVVTGVGRIYDSSDLEIDPDEIKDTFVLLDNAQACLDRGDFAQAVRFVNHLSGEAKTAASDWLAEARLLLETKQAAVALLATASAAGFTSIAGCT
The following text describes a protein:
Function:
Tumor suppressor serine/threonine-protein kinase involved in mTORC1 signaling and post-transcriptional regulation. Phosphorylates FOXO3, ERK3/MAPK6, ERK4/MAPK4, HSP27/HSPB1, p53/TP53 and RHEB. Acts as a tumor suppressor by mediating Ras-induced senescence and phosphorylating p53/TP53. Involved in post-transcriptional regulation of MYC by mediating phosphorylation of FOXO3: phosphorylation of FOXO3 leads to promote nuclear localization of FOXO3, enabling expression of miR-34b and miR-34c, 2 post-transcriptional regulators of MYC that bind to the 3'UTR of MYC transcript and prevent MYC translation. Acts as a negative regulator of mTORC1 signaling by mediating phosphorylation and inhibition of RHEB. Part of the atypical MAPK signaling via its interaction with ERK3/MAPK6 or ERK4/MAPK4: the precise role of the complex formed with ERK3/MAPK6 or ERK4/MAPK4 is still unclear, but the complex follows a complex set of phosphorylation events: upon interaction with atypical MAPK (ERK3/MAPK6 or ERK4/MAPK4), ERK3/MAPK6 (or ERK4/MAPK4) is phosphorylated and then mediates phosphorylation and activation of MAPKAPK5, which in turn phosphorylates ERK3/MAPK6 (or ERK4/MAPK4). Mediates phosphorylation of HSP27/HSPB1 in response to PKA/PRKACA stimulation, inducing F-actin rearrangement.
Subcellular Localization:
Cytoplasm. Nucleus. Note=Translocates to the cytoplasm following phosphorylation and activation. Interaction with ERK3/MAPK6 or ERK4/MAPK4 and phosphorylation at Thr-182, activates the protein kinase activity, followed by translocation to the cytoplasm. Phosphorylation by PKA/PRKACA at Ser-115 also induces nuclear export.
Sequence:
MSEDSDMEKAIKETSILEEYSINWTQKLGAGISGPVRVCVKKSTQERFALKILLDRPKARNEVRLHMMCATHPNIVQIIEVFANSVQFPHESSPRARLLIVMEMMEGGELFHRISQHRHFTEKQASQVTKQIALALQHCHLLNIAHRDLKPENLLFKDNSLDAPVKLCDFGFAKVDQGDLMTPQFTPYYVAPQVLEAQRRHQKEKSGIIPTSPTPYTYNKSCDLWSLGVIIYVMLCGYPPFYSKHHSRTIPKDMRKKIMTGSFEFPEEEWSQISEMAKDVVRKLLKVKPEERLTIEGVLDHPWLNSTEALDNVLPSAQLMMDKAVVAGIQQAHAEQLANMRIQDLKVSLKPLHSVNNPILRKRKLLGTKPKDGIYIHDHENGTEDSNVALEKLRDVIAQCILPQAGKGENEDEKLNEVMQEAWKYNRECKLLRDALQSFSWNGRGFTDKVDRLKLAEVVKQVIEEQTLPHEPQ
The following text describes a protein:
Function:
Serine/threonine-protein kinase involved in the process of chromatin assembly and probably also DNA replication, transcription, repair, and chromosome segregation. Phosphorylates the chromatin assembly factors ASF1A and ASF1B. Phosphorylation of ASF1A prevents its proteasome-mediated degradation, thereby enhancing chromatin assembly. Negative regulator of amino acid starvation-induced autophagy.
Subcellular Localization:
Nucleus. Nucleus, nucleoplasm. Cytoplasm, perinuclear region. Cytoplasm, cytoskeleton. Note=Colocalizes with the cytoplasmic intermediate filament system during the G1 phase of the cell cycle. Present in the perinuclear region at S phase and in the nucleus at late G2.
Sequence:
MMEELHSLDPRRQELLEARFTGVGVSKGPLNSESSNQSLCSVGSLSDKEVETPEKKQNDQRNRKRKAEPYETSQGKGTPRGHKISDYFEFAGGSAPGTSPGRSVPPVARSSPQHSLSNPLPRRVEQPLYGLDGSAAKEATEEQSALPTLMSVMLAKPRLDTEQLAQRGAGLCFTFVSAQQNSPSSTGSGNTEHSCSSQKQISIQHRQTQSDLTIEKISALENSKNSDLEKKEGRIDDLLRANCDLRRQIDEQQKMLEKYKERLNRCVTMSKKLLIEKSKQEKMACRDKSMQDRLRLGHFTTVRHGASFTEQWTDGYAFQNLIKQQERINSQREEIERQRKMLAKRKPPAMGQAPPATNEQKQRKSKTNGAENETPSSGNTELKDTAPALGAHSLLRLTLAEYHEQEEIFKLRLGHLKKEEAEIQAELERLERVRNLHIRELKRIHNEDNSQFKDHPTLNDRYLLLHLLGRGGFSEVYKAFDLTEQRYVAVKIHQLNKNWRDEKKENYHKHACREYRIHKELDHPRIVKLYDYFSLDTDSFCTVLEYCEGNDLDFYLKQHKLMSEKEARSIIMQIVNALKYLNEIKPPIIHYDLKPGNILLVNGTACGEIKITDFGLSKIMDDDSYNSVDGMELTSQGAGTYWYLPPECFVVGKEPPKISNKVDVWSVGVIFYQCLYGRKPFGHNQSQQDILQENTILKATEVQFPPKPVVTPEAKAFIRRCLAYRKEDRIDVQQLACDPYLLPHIRKSVSTSSPAGAAIASTSGASNNSSSN
The following text describes a protein:
Function:
With SRT1 or RER2, forms the dehydrodolichyl diphosphate synthase (DDS) complex, an essential component of the dolichol monophosphate (Dol-P) biosynthetic machinery. Adds multiple copies of isopentenyl pyrophosphate (IPP) to farnesyl pyrophosphate (FPP) to produce dehydrodolichyl diphosphate (Dedol-PP), a precursor of dolichol which is utilized as a sugar carrier in protein glycosylation in the endoplasmic reticulum (ER).
Subcellular Localization:
Endoplasmic reticulum membrane; Single-pass membrane protein. Lipid droplet. Nucleus membrane; Single-pass membrane protein.
Sequence:
MPTMIKKDDKAMEPPNEKPHRKIERDDVPESSNHIPPPESGVLKGGKVNSKTRALKAVTSIIADADENPQKKVNNETNGVQKQKTEDLSKRIGKFEYLFYKFLLVLLYICFGLFRYGQYQYNKMKLRIFSIIYNHAYTPQLIRQDVIPLKKIPKRLAAILEVKPVGDVGGGVTGLLNDASEIVCWTVSAGIKHLMLYDYDGILQRNVPELRMEIHSNLAKYFGPAHVPNYAVKIPHSNKIFYNLDGIETETDVGNEIEANQEKDKIAIEISLLSNRDGRETIVDLTKTMAELCAVNELSVSDITMDLVDSELKQLVGPEPDLLLYFGPSLDLQGFPPWHIRLTEFYWEKDNNEVIYSVFIRGLRQYAGCKVNVGK
The following text describes a protein:
Function:
Creatine:sodium symporter which mediates the uptake of creatine. Plays an important role in supplying creatine to the brain via the blood-brain barrier.
Subcellular Localization:
Apical cell membrane; Multi-pass membrane protein.
Sequence:
MAKKSAENGIYSVSGDEKKGPLIAPGPDGAPAKGDGPAGLGAPGGRLAVPPRETWTRQMDFIMSCVGFAVGLGNVWRFPYLCYKNGGGVFLIPYVLIALVGGIPIFFLEISLGQFMKAGSINVWNICPLFKGLGYASMVIVFYCNTYYIMVLAWGFYYLVKSFTTTLPWATCGHTWNTPDCVEIFRHEDCANASLANLTCDQLADRRSPVIEFWENKVLRLSGGLEVPGALNWEVTLCLLACWVLVYFCVWKGVKSTGKIVYFTATFPYVVLVVLLVRGVLLPGALDGIIYYLKPDWSKLGSPQVWIDAGTQIFFSYAIGLGALTALGSYNRFNNNCYKDAIILALINSGTSFFAGFVVFSILGFMATEQGVHISKVAESGPGLAFIAYPRAVTLMPVAPLWAALFFFMLLLLGLDSQFVGVEGFITGLLDLLPASYYFRFQREISVALCCALCFVIDLSMVTDGGMYVFQLFDYYSASGTTLLWQAFWECVVVAWVYGADRFMDDVACMIGYRPCPWMKWCWSFFTPLVCMGIFIFNVVYYKPLVYNNTYVYPWWGEAVGWGFALSSMLCVPLHLLGCLLRAKGTMAEVSVPCATPPRPRAEASAPKCPVSHPLGCTSALEVSGPAGGGWHGGDADPPGPEVVAGGAEVCPRPPTPSLVRERGAVSPHSRRGPCPQAAAGGGQRTGQGPACVPPRPPWPGDSTRPFLPQRWQHLTQPVWGLHHLEYRAQET
The following text describes a protein:
Function:
Member of the granin protein family that regulates the biogenesis of secretory granules (By similarity). Acts as a sorting receptor for intragranular proteins including chromogranin A/CHGA (By similarity). May also play a role in angiogenesis. Promotes endothelial proliferation, migration and tube formation through MEK/ERK signaling pathway (By similarity).
Subcellular Localization:
Cytoplasmic vesicle, secretory vesicle. Cytoplasmic vesicle, secretory vesicle membrane; Peripheral membrane protein. Secreted. Note=Associated with the secretory granule membrane through direct binding to cholesterol-enriched lipid rafts.
Sequence:
MGFLWTGTWIVVLMLHSSPIQAFPKPAGSQDKPLHNRELSAERPLNEQIAEAEADEIKKTYPPENKPGESNYSFVDNLNLLKAITEKEKNEKERQSVKISPNDNKLNVEDVDSTKNRRLIDDYDSTKSGLDRKFQDDPDGLHQLDGTPLTAEDIVQKIATRIYEENDRGVFDRIVSKLLNLGLITESQAHTLEDEVAEVLQKLISKEANNYEEELNKPTSKTESQTGKIPEKVTPMAAIQDAFTNGENDETVSNTLTLTNGLERRTKTYSEDNFEELQYFPNFYALLKSIDSEKEAKEKETLITIMKTLIDFVKMMVKYGTISPEEGVSYLENLDETIALQTKNKLEKNVTDNKSKLFAVPSEKSHEETDSTKEEAAKMEKEYGTLKDSTKDDDSNPRGKTDEHKGKTEAYLEAIRKNIDWLKKHNKKENKEDYDLSKMRDFINQQADAYVEKGILDKEEADAIKRIYSSL
The following text describes a protein:
Function:
Catalytic subunit of the glycosylphosphatidylinositol-N-acetylglucosaminyltransferase (GPI-GnT) complex that catalyzes the transfer of N-acetylglucosamine from UDP-N-acetylglucosamine to phosphatidylinositol and participates in the first step of GPI biosynthesis.
Subcellular Localization:
Endoplasmic reticulum membrane; Single-pass membrane protein.
Sequence:
MACSGGGGPSQPPSPALSSVSPGSLPTCRSCSHNICMVSDFFYPNMGGVESHIYQLSQCLIERGHKVIIVTHAYGNRKGIRYLTNGLKVYYLPLKVMYNQSTATTLFHSLPLLRYIFVRERVTIIHSHSSFSAMAHDALFHAKTMGLQTVFTDHSLFGFADVSSVLTNKLLTVSLCDTNHIICVSYTSKENTVLRAALNPEIVSVIPNAVDPTDFTPDPFRRHDSVITIVVVSRLVYRKGTDLLSGIIPELCQKYPDLNFVIGGEGPKRIILEEVRERYQLHDRVRLLGALEHKDVRNVLVQGHIFLNTSLTEAFCMAIVEAASCGLQVVSTRVGGIPEVLPESLIILCEPSVKSLCEGLEKAISQLKSGALPPPESIHNIVKTFYTWRNVAERTEKVYDRVAGEAVLPMDKRLDRLISHCGPVTGCIFALLAVFNFLFLVFLRWMTPDSIIDVAIDATGPKGAWTRQYPSHANGDENNEESETR
The following text describes a protein:
Function:
Repressor of jasmonate responses.
Subcellular Localization:
Nucleus.
Domain:
The jas domain is required for interaction with COI1.
Sequence:
MVQGGERSVRKTSHFSLTCRLLSQYLKKKKKKNGNRGELALRQQAKENSLVPNTVSFEPGVDVSGKNHHRHAENSILTKEESNMATNTKEKRKDQFTVFYGGKVVVFDNIPADRAKDLMLMASKDTTCNLMTLQPQANNSSDMPIARRNSLHRFLEKRKDRMGKAPYQVHGGSEVAKTEEDQPWLSLGRRVPEAGSTCHV
The following text describes a protein:
Function:
Exoribonuclease involved in ribosome biosynthesis. Involved in the processing of ITS1, the internal transcribed spacer localized between the 18S and 5.8S rRNAs (By similarity).
Subcellular Localization:
Nucleus.
Sequence:
MAKLSQNWKKLSSKIQDKPKNGSVKKPTLKGKISKKVKASISEKLSTTNNTTTTTTTTTSTTDVVPIASSTKPTATPLEYTLWTQNHTINVSHIPKTPKPLPLSRNDSRKLDPGKYVAIDCEFVGIGKDGEESALARISIINYYGVVLLDTYVRPQERVTDWRTWVSGIQSYHMQDAIDFKTAQLKTMELINNKILVGHAVNNDLDILFLSHPKSMIRDTCKFPKFREIAGGKSPSLKKLIKHFIQVDIQIGQHSSVEDARATMLLFRLFKREIEQSMRNRNKRQ
The following text describes a protein:
Function:
Component of an histone acetyltransferase complex.
Subcellular Localization:
Nucleus.
Domain:
The PHD-type zinc finger mediates the binding to H3K4me3.
Sequence:
MVMADYNDEDGGVILDGPFDPDAQATVTDFIDYTEYLPADLIRSLTLIRGLDERYLEATQNVHELTKTWGQLPDLPSHERPDAQTLRKNISAQLDQAINARECAYAEACRLYDVVDRHFNRLECIKQKLHALPKPESREPTPPETQTTLNKRGRSSKKGEAAAPTTTRIKLRLDGAANAGTRPEQRSRSRRGKLAADHLAGLHPDSPIASTEHSDVEAGTKPTRSAAPEELAVAKGKKEKQTRRSRTSAPLTNGHGHGAAMSTSNALAMLKPPPEDAKPGSEDLPWLRLTEWEMTKLRKKMKKNAVWQPSEVMIHRELALRGRGWDAYRRAKAEAEANGTEFLDCDDIMNNYVPGMLTRLTDANGIEGVVETKLSNRGMKLNEAKKLKRENMAREQAAAAAAAAAEAKRLAESGTTGAAAPDQSQVESSLAARKPSRALKKRKVDESVAAQAAPAPPVDSETRGSLRSSAKRRKMSKTPVEADEAMVDETADQAAKIESSKASPVPSAASTVAAAQTKEIKTSTPPVSRPPSRHLAPGGASAEVAALAPGKDLRRKSTTPARRTPVPEASQAGGRRRKRPAPGPVSSGQDGGAAVSYGRRKAKPAKKRFGPREQGQKDGTTREDIRIDEDGVLEEIDPNEPRYCLCGDVSFGTMICCENQDCDKEWFHLECVGLSEVPSRTAKWYCPDCRVKFHKGNDGIVRPSSRR