lhallee/plat_data huggingface dataset:
The following text describes a protein:
Function:
Involved in ligand-dependent receptor mediated endocytosis of the EGF and insulin receptors as part of the Ral signaling pathway. By controlling growth factor receptors endocytosis may regulate cell survival. Through ASAP1 may regulate cell adhesion and migration.
Subcellular Localization:
Cytoplasm.
Sequence:
MEAAAAAAAAAAAAAAAGGGCGSGPPPLLLSEGEQQCYSELFARCAGAAGGGPGSGPPEAARVAPGTATAAAGPVADLFRASQLPAETLHQITELCGAKRVGYFGPTQFYIALKLIAAAQSGLPVRIESIKCELPLPRFMMSKNDGEIRFGNPAELHGTKVQIPYLTTEKNSFKRMDDEDKQQETQSPTMSPLASPPSSPPHYQRVPLSHGYSKLRSSAEQMHPAPYEARQPLVQPEGSSSGGPGTKPLRHQASLIRSFSVERELQDNSSYPDEPWRITEEQREYYVNQFRSLQPDPSSFISGSVAKNFFTKSKLSIPELSYIWELSDADCDGALTLPEFCAAFHLIVARKNGYPLPEGLPPTLQPEYLQAAFPKPKWDCQLFDSYSESLPANQQPRDLNRMEKTSVKDMADLPVPNQDVTSDDKQALKSTINEALPKDVSEDPATPKDSNSLKARPRSRSYSSTSIEEAMKRGEDPPTPPPRPQKTHSRASSLDLNKVFQPSVPATKSGLLPPPPALPPRPCPSQSEQVSEAELLPQLSRAPSQAAESSPAKKDVLYSQPPSKPIRRKFRPENQATENQEPSTAASGPASAATMKPHPTVQKQSSKQKKAIQTAIRKNKEANAVLARLNSELQQQLKEVHQERIALENQLEQLRPVTVL
The following text describes a protein:
Function:
RNA-binding protein required for the maturation of box H/ACA snoRNPs complex and ribosome biogenesis. During assembly of the H/ACA snoRNPs complex, it associates with the complex and disappears during maturation of the complex and is replaced by GAR1 to yield mature H/ACA snoRNPs complex (By similarity).
Subcellular Localization:
Nucleus. Note=Absent from the nucleolus.
Sequence:
MYPHLPCKIPGLSLIYDDESKVEKSKQLSTNASSSNFVKEDQIPSNLSIDNINTPQGDPIDKNNLNTNTENNLPNIVNFQNISSANSGEIKQKDNEILFSSTEDINQHKENYQDENKIDLLDVALANPKDCVVPSSGLLMPKEEFISNEEVGIPATNSSEKSNVKIADEIAEVTHSNSSIGKSSADLSSDSSSDSESNTSFSETDVEEEKAEEKSDAESMAPSTPPKTVNELPEQIYEKPEIVLQPNSLIEPLGKIIQVLKREVVVKSDIDDEKIVFDEKTVLCFEDRSIIGYIHETFGPVSSPYYIVRFSTEEECSAINACMGRPVFYVPTMANKIDPEPLKYIKGSDASNVYDEEINPSEQEFSDDEAEVAAKQLKKKRKRKAKSMVSGNQALPGEANFQSLNQNNVRNYPFYQTNQGSNPPAKRFTQEPPSSSLYSLSESSINYSTQSPMYYNYNYPQPSFPPFHPIYNDSIGYYSQANPQMYYANQVSAPPPQGSFDPNSKFYRNSSDSYRK
The following text describes a protein:
Function:
Involved in normal synaptic function through regulation of Ca(2+) influx and neurotransmitter release in photoreceptor synaptic terminals and in auditory transmission. Modulator of CACNA1D and CACNA1F, suppressing the calcium-dependent inactivation and shifting the activation range to more hyperpolarized voltages.
Subcellular Localization:
Cytoplasm. Presynapse. Note=Found in rod spherules and cone pedicles of the presynapses from both types of photoreceptors.
Sequence:
MATEHNVQLVPGSQKIPKGVVSPRSAAEGPALTRRRSKKESWHPGSQKASSGDQSSSQGSEASGSSKHPPRTKVGQEEPSSAPARPASHRHSHRHRSDPQQDAAQRTYGPLLNRMFGKDRELGPEELEELQAAFEEFDTDQDGYIGYRELGDCMRTLGYMPTEMELLEVSQHVKMRMGGFVDFEEFVELISPKLREETAHMLGVRELRIAFREFDKDRDGRITVAELRQAAPALLGEPLEGTELDEMLREMDLNGDGTIDFDEFVMMLSTG
The following text describes a protein:
Function:
Catalyzes the reduction of glutathione disulfide (GSSG) to reduced glutathione (GSH). Constitutes the major mechanism to maintain a high GSH:GSSG ratio in the cytosol.
Miscellaneous:
MISCELLANEOUS: [Isoform 1]: Produced by alternative initiation at Met-47 of isoform 2; MISCELLANEOUS: The active site is a redox-active disulfide bond.
Subcellular Localization:
[Isoform 1]: Cytoplasm; [Isoform 2]: Plastid, apicoplast.
Sequence:
MYKHRYFHFFFFFFFFLVSTKIIRSFTFLNNNTNLSNPVYFKKKANMVYDLIVIGGGSGGMAAARRAARHNAKVALVEKSRLGGTCVNVGCVPKKIMFNAASVHDILENSRHYGFDTKFSFNLPLLVERRDKYIQRLNNIYRQNLSKDKVDLYEGTASFLSENRILIKGTKDNNNKDNGPLNEEILEGRNILIAVGNKPVFPPVKGIENTISSDEFFNIKESKKIGIVGSGYIAVELINVIKRLGIDSYIFARGNRILRKFDESVINVLENDMKKNNINIVTFADVVEIKKVSDKNLSIHLSDGRIYEHFDHVIYCVGRSPDTENLNLEKLNVETNNNYIVVDENQRTSVNNIYAVGDCCMVKKSKEIEDLNLLKLYNEETYLNKKENVTEDIFYNVQLTPVAINAGRLLADRLFLKKTRKTNYKLIPTVIFSHPPIGTIGLSEEAAIQIYGKENVKIYESKFTNLFFSVYDIEPELKEKTYLKLVCVGKDELIKGLHIIGLNADEIVQGFAVALKMNATKKDFDETIPIHPTAAEEFLTLQPWMK
The following text describes a protein:
Function:
Component of the RNF20/40 E3 ubiquitin-protein ligase complex that mediates monoubiquitination of 'Lys-120' of histone H2B (H2BK120ub1). H2BK120ub1 gives a specific tag for epigenetic transcriptional activation and is also prerequisite for histone H3 'Lys-4' and 'Lys-79' methylation (H3K4me and H3K79me, respectively). It thereby plays a central role in histone code and gene regulation. The RNF20/40 complex forms a H2B ubiquitin ligase complex in cooperation with the E2 enzyme UBE2A or UBE2B; reports about the cooperation with UBE2E1/UBCH are contradictory. Required for transcriptional activation of Hox genes.
Subcellular Localization:
Nucleus.
Sequence:
MSGPGNKRAAGDGGSGPPEKKLSREEKTTTTLIEPIRLGGISSTEEMDLKVLQFKNKKLAERLEQRQACEDELRERIEKLEKRQATDDATLLIVNRYWAQLDETVEALLRHHESQGELSSGTEAPGTQEGPTRDETPLTEPGTSELREPLPMQLRPPLSEPALAFVVALGASSSEEVELQLQGRMEFSKAAVSRVVEASDRLQRRVEELCQRVYSRGDSEPPGEAARARTRELGRENRRLQDLATQLQEKHHRISLEYSELQDKVTSAETKVLEMETTVEDLQWDIEKLRKREQKLNKHLAEALEQLNSGYYVSGSSSGFQGGQITLSMQKVALRSLPEEVVRETGEYRMLQAQFSLLYNESLQVKTQLDEARGLLLATKNSHLRHIEHMESDELGLQKKLRTEVIQLEDTLAQVRKEYEMLRIEFEQNLAANEQAGPINREMRHLISSLQNHNHQLKGDAQRYKRKLREVQAEIAKLRAQASGSTHSIPSLGHPEDSSLSAPVPGKEEGGPGPVGAPDTRKEMASMPGAALTTSSAKKEDVVASEEETQALTPGAQGPSSRGRELEARPKRELREREGPVLGPPSVASALSRADREKAKVEEVKRKESELLKGLRVELKKAQESQKEMKLLLDMYKSAPKEQRDKVQLMAAERKAKAEVDELRGRIRELEERDRRESKKIADEDALRRIRQAEEQIEHLQRKLGATKQEEEALLSEMDVTGQAFEDMQEQNGRLLQQLREKDDANFKLMSERIKANQIHKLLREEKDELGEQVLGLKSQVDAQLLTVQKLEEKERALQGSLGGVEKELTLRSQALELNKRKAVEAAQLAEDLKVQLEHVQTRLREIQPCLAESRAAREKESFNLKRAQEDISRLRRKLEKQRKVEVYADADEILQEEIKEYKARLTCPCCNTRKKDAVLTKCFHVFCFECVRGRYEARQRKCPKCNAAFGAHDFHRVYIS
The following text describes a protein:
Function:
Involved in the regulation of the intracellular balance of NAD and NADP, and is a key enzyme in the biosynthesis of NADP. Catalyzes specifically the phosphorylation on 2'-hydroxyl of the adenosine moiety of NAD to yield NADP.
Subcellular Localization:
Cytoplasm.
Sequence:
MIKLSIIYNEDKEDAIKIYKELLKYLKSKKEFEVLDDKNISQAEYIVVIGGDGTLLRGFKKIKDKKVKIIAINSGTLGYLTEIRKDGYKKIFENILKGKINIEERYFFTVKIGKKKYNALNEVFLTKDNIKRNIVSSEIYVDDKFLGKFKGDGVIIATPTGSTAYSLSAGGPIVTPELKLFLITPIAPHNLNTRPIILSGDVKIVLTLVGPSEFGIVNVDGHTHNKINIEDKVEISYSKESLKIVLPDDRNYYNVLREKLKWGENLC
The following text describes a protein:
Function:
Monacolin J acid methylbutanoyltransferase; part of the gene cluster that mediates the biosynthesis of lovastatin (also known as mevinolin, mevacor or monacolin K), a hypolipidemic inhibitor of (3S)-hydroxymethylglutaryl-coenzyme A (HMG-CoA) reductase (HMGR). The first step in the biosynthesis of lovastatin is the production of dihydromonacolin L acid by the lovastatin nonaketide synthase lovB and the trans-acting enoyl reductase lovC via condensation of one acetyl-CoA unit and 8 malonyl-CoA units. Dihydromonacolin L acid is released from lovB by the thioesterase lovG. Next, dihydromonacolin L acid is oxidized by the dihydromonacolin L monooxygenase lovA twice to form monacolin J acid. The 2-methylbutyrate moiety of lovastatin is synthesized by the lovastatin diketide synthase lovF via condensation of one acetyl-CoA unit and one malonyl-CoA unit. Finally, the covalent attachment of this moiety to monacolin J acid is catalyzed by the transesterase lovD to yield lovastatin. LovD has broad substrate specificity and can also convert monacolin J to simvastatin using alpha-dimethylbutanoyl-S-methyl-3-mercaptopropionate (DMB-S-MMP) as the thioester acyl donor, and can also catalyze the reverse reaction and function as hydrolase in vitro. LovD has much higher activity with LovF-bound 2-methylbutanoate than with free diketide substrates.
Miscellaneous:
MISCELLANEOUS: Directed evolution toward higher catalytic activity with free diketides led to an enzyme with 1000-fold higher activity in simvastatin synthesis, due to numerous mutations that affect protein folding and promote optimal alignment of the residues that are important for substrate binding and catalysis.
Sequence:
MGSIIDAAAAADPVVLMETAFRKAVKSRQIPGAVIMARDCSGNLNYTRCFGARTVRRDECNQLPPLQVDTPCRLASATKLLTTIMALQCMERGLVDLDETVDRLLPDLSAMPVLEGFDDAGNARLRERRGKITLRHLLTHTSGLSYVFLHPLLREYMAQGHLQSAEKFGIQSRLAPPAVNDPGAEWIYGANLDWAGKLVERATGLDLEQYLQENICAPLGITDMTFKLQQRPDMLARRADQTHRNSADGRLRYDDSVYFRADGEECFGGQGVFSGPGSYMKVLHSLLKRDGLLLQPQTVDMMFQPALEPRLEEQMNQHMDASPHINYGGPMPMVLRRSFGLGGIIALEDLDGEDWRRKGSLTFGGGPNIVWQIDPKAGLCTLAFFQLEPWNDPVCRDLTRTFEHAIYAQYQQG
The following text describes a protein:
Function:
Cysteine protease that plays a key role in autophagy by mediating both proteolytic activation and delipidation of ATG8 family proteins.
Subcellular Localization:
Cytoplasm.
Sequence:
MNTQVVSRERSIFLSKLSFPTSSSDSRLQDEGNNSDVEGKVKNRLLSMWNNVKYGMKLKTNFSKESPVWLLGKCYRRIESPSSDSTELGTDVAAFQSQSEIASSDDEGFEGFKKDFISRLWLTYRREFPILNGSNYSSDCGWGCMLRSGQMLIAQALVCHILGRDWRWQPDHQPTTRESFIEVVNHRKIIKWFGDKPSRNSPFSIHTLVALGEASGKKAGDWYGPGFVAHLFRQAFKRASEDNYEFDSLTVCVAQDCAVYIKDVMEECTDKNGKWKSLILLIPVRLGAEKFNSIYAPCLTTLFSLKQCIGIIGGRPKHSLYFVGYQDDKLIHLDPHYCQEVVDVWAVDFPLTSFHCRSPRKIHLSKMDPSCCIGFYCPTKESFFNLIEIVQPLVIPPGRTDSPGSEYPMFIFCDGYSRDAQLSPKKLPPSELEYSMDSSTDGDDMGTEAFEIL
The following text describes a protein:
Function:
Catalyzes the initial reaction in the xylose utilization pathway by reducing D-xylose into xylitol. Xylose is a major component of hemicelluloses such as xylan. Most fungi utilize D-xylose via three enzymatic reactions, xylose reductase (XR), xylitol dehydrogenase (XDH), and xylulokinase, to form xylulose 5-phosphate, which enters pentose phosphate pathway.
Sequence:
MTTFKLNTGATIPALGFGTWQDADAQETAVLEALRAGYRHIDTARVYGTEAAVGRAIKKSGIPRNQIFLTTKIWNNKHHPDDVAQALQDSLNDLDQDYVDLLLIHWPVAFKRGTEQFPKTEDGKPAVADTDYLDTYKALEKLLSTGKVKAIGVSNFSKAEMERILANATVPPAVHQLEGHPWLQQREFAEWHKKHGIHITHYSPFGNQNEVYSREGTIGRLIEDPVLVEIGKKYNKSAAQVALAWGVTEGHSVLPKSKTPERIKANLEGDFKLEEEDLKKIRGIDRKLRFNDSSKDFGYDFFKDLDGKK
The following text describes a protein:
Function:
Endonuclease that specifically degrades the RNA of RNA-DNA hybrids.
Sequence:
MPPRSQPLTLDYIDCSIMAEKETPPVVTGTRPPPSVTIAEPLLSSYLYSTSDRKDITEEEEQLKRDNWIMGIDEAGRGPVLGPMVYGAAFCTQAFAEDKLLDLGFADSKTLTHRRREELLEMIVHPPADQPLNERVEWNVKVLTPADISQGMNRRSPYNLNAQAFDATCEIIQHALDLQYNLQHIYVDTLGPPKTHQMKLEQSFPGIKFTVCSKADSIYPIVGAASVVAKVTRDAIVSHWIHPESTHPQKRKSSQEDEDATTSLGSGYPSDPNTVKWLSENFNTIFGFGQLVRFSWGTVKTLLADRGPAFSWNDEPSIQKWLKPVSQCQAETAPVGFCQDLGLRSVDSL
The following text describes a protein:
Function:
Transcription factor which may be involved in developmental processes.
Subcellular Localization:
Nucleus.
Sequence:
MWTMGYNEGGADSFNGGRKLRPLIPRLTSCPTAAVNTNSDHRFNMAVVTMTAEQNKRELMMLNSEPQHPPVMVSSRWNPTPDQLRVLEELYRQGTRTPSADHIQQITAQLRRYGKIEGKNVFYWFQNHKARERQKRRRQMETGHEETVLSTASLVSNHGFDKKDPPGYKVEQVKNWICSVGCDTQPEKPSRDYHLEEPANIRVEHNARCGGDERRSFLGINTTWQMMQLPPSFYSSSHHHHQRNLILNSPTVSSNMSNSNNAVSASKDTVTVSPVFLRTREATNTETCHRNGDDNKDQEQHEDCSNGELDHQEQTLELFPLRKEGFCSDGEKDKNISGIHCFYEFLPLKN
The following text describes a protein:
Function:
Acts as a 5'-hydroxyl kinase, a 3'-phosphatase and a 2',3'-cyclic phosphodiesterase. Catalyzes the transfer of the terminal phosphate of ATP to the 5'-hydroxyl termini of ribo- and deoxyribonucleotides. In the presence of ADP the enzyme also catalyzes an exchange reaction. In the exchange reaction, an excess ADP causes the enzyme to transfer the 5' terminal phosphate from phosphorylated DNA to ADP. Involved in countering a host defense mechanism which activates T4-induced anticodon nuclease and shuts off viral translation. The polynucleotide kinase modifies the ends of nicked tRNA generated by the antiviral response of the host bacteria and facilitates repair by T4 RNA ligase.
Sequence:
MKKIILTIGCPGSGKSTWAREFIAKNPGFYNINRDDYRQSIMAHEERDEYKYTKKKEGIVTGMQFDTAKSILYGGDSVKGVIISDTNLNPERRLAWETFAKEYGWKVEHKVFDVPWTELVKRNSKRGTKAVPIDVLRSMYKSMREYLGLPVYNGTPGKPKAVIFDVDGTLAKMNGRGPYDLEKCDTDVINPMVVELSKMYALMGYQIVVVSGRESGTKEDPTKYYRMTRKWVEDIAGVPLVMQCQREQGDTRKDDVVKEEIFWKHIAPHFDVKLAIDDRTQVVEMWRRIGVECWQVASGDF
The following text describes a protein:
Function:
Probable disulfide isomerase, which participates in the folding of proteins containing disulfide bonds. May act as a dithiol oxidase. Acts as a regulator of endoplasmic reticulum-mitochondria contact sites via its ability to regulate redox signals.
Subcellular Localization:
Endoplasmic reticulum membrane; Single-pass membrane protein.
Sequence:
MRLPRLLSVTFSLSALLTTATATITDLDDDFQLRELTEDNFKSSVSQGVWLVEHFSPKCAHCRAFAPTWTQLARDKRHLERLTGFHMAQINCLAQGDLCNSNGIKFYPQIIMYTDGKPSPHYTGDRSYEELSKYIDEHAHTYAETILDPAVQSQEALVIGPANSEGKVQEVDERGLEALKAEGPVLVEYFAPWCGHCKALRPTYEQLALELQGQLNVAAVNCDDHRALCVNSGIKAYPTIRLLHHGTSAEYSGARSLAKLKEFSQRAEKPASLTSIKAGDFDKIVSANEAFFLYLQTFDTTVAEVDSVKKAFEPLLGTVPAYTSADVALYQRLHVVNPPTSTLFAFSSYSTRPVGTMGLPASPNDLRKFINLHRFPTLVRLDASNFQSLMRSDTRAIVVLAGVHKGEEGKKERDKFADVARAWKRGGRRFEQPVWFVWVEGETSRWANWLKRFYGIKKRDLPGVVVIDTPLEEYYDTTIEGTKIEFEGSSIFSVLEGFYQHFLRPKRIESTLEWGSRSASETLISVGESAVEHPFLFLTVLVGTVALFVYLLQKCLVKDPKDGYSPSRLD
The following text describes a protein:
Function:
Component of the post-replicative DNA mismatch repair system (MMR). Heterodimerizes with mlh1 to form MutL alpha. DNA repair is initiated by MutS alpha (msh2-msh6) or MutS beta (msh2-msh3) binding to a dsDNA mismatch, then MutL alpha is recruited to the heteroduplex. Assembly of the MutL-MutS-heteroduplex ternary complex in presence of rfc and pcna is sufficient to activate endonuclease activity of pms1. It introduces single-strand breaks near the mismatch and thus generates new entry points for the exonuclease exo1 to degrade the strand containing the mismatch (By similarity).
Subcellular Localization:
Nucleus.
Sequence:
MIKAIDKESINNICSGQVIFDLSIAVKELIENSIDAGATTVEIRLKEYGEEFIEVIDNGSGVEPSNFVALTMKHCTSKLESFSDLLSIETYGFRGEALSSLCSLSNCIITTRTKNQVTAQRLVFDKEGKIQTQTPVAREVGTTVQLSNLFKGLPVRYQEFKRNIKKEYAKLLTILQAYALISTNTRITCYNQAGKSPRSCVLSTTSGSTIRDNLINVFGTKMSQSLDEFTASDSLFKVNGLISKIGIGSGTGQSISNSSSSSSQSSSQLSSSSSSSSSSQSSQLSIGSLSRSCADRQFFFVNSRPFEHSKLAKEINSLYQSFHKRGSYPVVIFNIEMPTNNYDVNVTPDKRTIFIQKEQQLLLLITDGLKTMWETAQSVFDTNQLGQFTFNDENENDNSNNNKQSKISSFPNLYTLKTEEDENNNKITTPIKKHSTTTTTSSLNSPSSNKKSSNSTSSSSSSNNKNNRNNLEEDGDDSFDITDQQPLKRAKYDGNYNNSNKKPELPKTPYPNKKKNNENEDEDEDEDNYVQPVFSNVNKSKNSSNSGSSNSLDDIIDDNEFISRSNGNSSNFMDDFEFKGSSNNIGSSSNGIKLKTISNNNNSNNSNNSNKIIDDINKTIDKMKQQQQPQQKMGLNDDGDDEEQQKQKQQQQQQKRKQQQQQQQIEEEEEETIDGYKQKNSKTFDITIKTDLNTISKQYLIRNGTFDKDNNPIIPNTALVVSNDDMVVNNNNSNEFDQNSIITTTSEKCCIVDKSIPQLDGKFSTSLGGIGAKQQQKAATQVTSQLQQQPSQTNQKTAEEELTKFFKKEYFKQMIVIGQFNLGFIIAKLGNDLFIIDQHAADEKYNFEILSKSVESSINSQPLLKPDTLSDLTSEEELIIIENVDLFKKNGFKFIIDHDAPTRFKIKLSAFPIIHGQSFGIKDIYEWIFMIKESSIPGSVNKIPRLNSLLASKACRKSIMVGTTLTHKEMKDVLNNLSTLDNPWCCPHGRPTMRHLVDLSIKDKLKQQQQQQQQKQQQQQQQ
The following text describes a protein:
Function:
May play a role in the regulation of cytokinesis.
Sequence:
MDDSEPTSLNALLGSTVDADIRAQLALNEELWHSLLQTQQIASSSDCSHLRAKVVRNLLSAGPEAQKTAEKCGLLVWFHHVLPNPSVSEDPNDRFFWQAFANASAGTSPISRQLWQFLFETDGSTPGLIMQDRTPRVYVSDGLHSAFTVALWSLELSLEKDPQTDPIQDLCLTERGQTLLYILFCMDGVLEIGHRETALLKGFVEKIFQQGFTSKLISVSQDCGHRTLYFVLNTLNELLEDASAKSAIALAPETFQTATASFLEKGSSLRLMLSDLSTSSFSSDLSLTTFAEHVSVFLTCIKFYSLFLDVANDDLERDTFKPCIVPDHPDLISPAANASDGSLKPLVKLLVDVLGLASNLFPAKTLVATSAASAQDPVRNEFAEAAAGLKRECLRLITFLLHLHPTLQDEVRELGAIPLILQQCNIDDHNPYIREITILCIRQLLFNNVENQSLVARLQPQQPVQSTVVNEAGYEVCLNSEGKPYLQSIHADTGTAEMNETNGSASS
The following text describes a protein:
Function:
May play a role in pre-mRNA splicing as component of the spliceosome. Acts as an important regulator of the cell cycle that participates in the maintenance of genome integrity. During cell cycle progression in embryonic fibroblast, prevents replication fork collapse, double-strand break formation and cell cycle checkpoint activation. Controls mitotic cell cycle progression and cell survival in rapidly proliferating intestinal epithelium and embryonic stem cells. During the embryo preimplantation, controls different aspects of M phase. During early oocyte growth, plays a role in oocyte survival by preventing chromosomal breaks formation, activation of TP63 and reduction of transcription.
Subcellular Localization:
Chromosome. Nucleus speckle.
Sequence:
MASSASARPPAGKRVVNQDELRRLMKEKQRLSTNRKRIESPFAKYNRLGQLSCALCNTPVKSELLWQTHVLGKQHREKVAELKGAKEAAQGPSASAVPQSTKRKAPDSESQDAKRAKASLVPQVQPSTSALPTNFDKAGKESTRATVGKASGLGLLPDYDDEEDEEEEKGGGGGEGKKGDACKQPSTSQSKEHSLSSSREATGSRLPSNFSDTNPPKAPLIPHSGSIEKAEIHEKVVERRENTAEALPEGFFDDPEIDARVRKVDAPKDQMDKEWDEFQKAMRQVNTISEAIVAEEDEEGRLDRQIGEIDEQIECYRRVEKLRNRQDEIKNKLKEVLTIKELQKKEEENVDSDDEGELQDLLSQDWRVKGALL
The following text describes a protein:
Function:
Catalyzes the decarboxylation of L-3,4-dihydroxyphenylalanine (DOPA) to dopamine and L-5-hydroxytryptophan to serotonin.
Sequence:
MNASEFRRRGKEMVDYVANYMEGIEGRQVYPDVEPGYLRPLIPAAAPQEPDTFEDIINDVEKIIMPGVTHWHSPYFFAYFPTASSYPAMLADMLCGAIGCIGFSWAASPACTELETVMMDWLGKMLELPKAFLNEKAGEGGGVIQGSASEATLVALLAARTKVIHRLQAASPELTQAAIMEKLVAYSSDQAHSSVERAGLIGGVKLKAIPSDGNFAMRASALQEALERDKADGLIPFFMVATLGTTTCCSFDNLLEVGPICNKEDMWLHVDAAYAGSAFICPEFRHLLNGVEFADSFNFNPHKWLLVNFDCSAMWVKKRTDLTGAFRLDPTYLKHSHQDSGLITDYRHWQIPLGRRFRSLKMWFVFRMYGVKGLQAYIRKHVQLSHEFESLVRQDPRFEICVEVILGLVCFRLKGSNKVNEALLQRINSAKKIHLVPCHLRDKFVLRFAICSRTVESAHVQRAWEHIKELAADVLRAERE
The following text describes a protein:
Function:
Protein-arginine N-methyltransferase that catalyzes both the monomethylation and asymmetric dimethylation of the guanidino nitrogens of arginine residues in target proteins, and therefore falls into the group of type I methyltransferases.
Subcellular Localization:
Cytoplasm, cytosol.
Sequence:
MEPSREVKDEAEERLRSDEEEEEEEGEEGWDDWCSDGDDAGGGLLCLFCSSRFDADSSLFAHCSAEHRFDFHRIVKELRLDFYGCIRLINFVRSKVAENKCWSCGQAFSSNTELCSHLHALENYLIEGKVPWEDDVYLKPFMEDDSLLHSLFMDDDEEDEECGTSMERGQCSAGDRVLAEPLGNKLSTLSEGNSSEISAQFEKGCTIGSTQAEDRESLAHETNDSQLKIARASVNAKAIKTVDDNYFGSYSSFGIHREMLGDKVRTDAYRDALLGNPSLLRGAAVLDVGCGTGILSLFAAKAGASRVVAVDGSAKMASVATQVAKNNGLLYDENLKAEQKRGAQVISVVHTKAEELNQKIQVPQHGFDVLVSEWMGYCLLFESMLSSVIYARDHFLKPGGAILPDTATIVGAGFGKGGTSLPFWENVYGFDMSCIGKEVTSTSARFPVVDVIASQDIVTETAVLHSFDLATMKESEMDFTASFELRLSESATVVPGVTWCYGIVLWFDTGFTDRFCKEKPVVLSTSPFSTPTHWSQTIFTFEEPIAMVKEESTLGSSASVGTDECPATMLRSRISIVRASEHRSIDISVETTAFSSDGWKRSWPIQIFNL
The following text describes a protein:
Function:
Plays a structural role to facilitate the assembly and ensure the full activity of the enzyme catalyzing the decarboxylation of isocitrate (ICT) into alpha-ketoglutarate. The heterodimer composed of the alpha (IDH3A) and beta (IDH3B) subunits and the heterodimer composed of the alpha (IDH3A) and gamma (IDH3G) subunits, have considerable basal activity but the full activity of the heterotetramer (containing two subunits of IDH3A, one of IDH3B and one of IDH3G) requires the assembly and cooperative function of both heterodimers.
Subcellular Localization:
Mitochondrion.
Sequence:
MRAGRAPLPGGRDVTSGGAQRPLGEHGLAEQDRPAAAGGVAGVKGHGADGPAPPAGPRTPPGPAHLRPGLPAPAGEHGPPGKPRGAAGRRRPRAILGERGPPGGGGSGAPLPWPQGEPVQVEGAFPVTMLPGDGVGPELMHAVKEVFKAAAVPVEFQEHHLSEVQNMASEEKLDQVLDSMKQNKVALIGKIHTPMEYKGELASYDMRLRRKLDLFANVVHVKSLPGYKTRHNNLDLVIIREQTEGEYSSLEHESARGVIECLKIVTRAKSQRIAKFAFDYATKQGRCKVTAVHKANIMKLGDGLFLQCCEEVAELYPKVQFETMIIDNCCMQLVQNPYQFDVLVMPNLYGNIIDNLAAGLVGGAGVVPGESYSAEYAVFETGARHPFAQAVGRNIANPTAMLLSATNMLRHLNLEYHSNLISDAVKKVIKVGKVSEGAPKGDWVGGWVLGGSPGPFPTPPTALLSRLHPCGSRCGHGTWAGTAPPPTSSSLSSTTCTPSLGSNWGTPGGPPTPHPLGKQHIPPQHHPLPPPTTFPSRTASVCSVAK
The following text describes a protein:
Function:
Component of ribonuclease P, a protein complex that generates mature tRNA molecules by cleaving their 5'-ends.
Subcellular Localization:
Nucleus.
Sequence:
MVRFKNRYLLCEIIFENGKISESLNLYQILNAIKESLSTNFGVFGLGVLAISLQVKYFNPFTGLAIVRVNRDYMRLVWACVSLITAINKRICMVKVVHVGGTIKLVQSQAIKYNQTIISKLRSDLVLSGN
The following text describes a protein:
Function:
Contributes to cell growth, probably by hydrolyzing exogenous lipids. Catalyzes the hydrolysis of monoacylglycerols (MAG) with fatty acid chains ranging from C14 to C18, with a maximum activity on monoolein. Is unable to hydrolyze long-chain diacylglycerol (DAG).
Subcellular Localization:
Secreted, cell wall.
Sequence:
MVSSTRSEHSFAGVGGVRIVYDVWTPDTDPRGVVVLAHGYAEHAGRYHHVAQRFGAAGLLVYALDHRGHGRSGGKRVHLRDLSEFVEDFRTLVGIAANDHPTLPRIVLGHSMGGGIVFAYGARYPGEYSAMVLSGPAVNAHDGVSPVLVAVAKVLGKLAPGIPVENLDADAVSRDPEVVAAYKADPMVHHGKLPAGIARALIGLGQSMPQRAAALTAPLLVVHGDKDRLIPVAGSRLLVDRVASEDVHLKVYPGLYHEVFNEPEQKLVLDDVTSWIVSHL
The following text describes a protein:
Function:
Cell-surface glycoprotein having a role in immunoadhesion. Mediates in the adhesion of blood neutrophils in cytokine-activated endothelium through interaction with SELPLG/PSGL1. May have a role in capillary morphogenesis (By similarity).
Subcellular Localization:
Cell membrane; Single-pass type I membrane protein.
Sequence:
MIASQFLSALTLVLLIKESGAWSYSASTTNMTFDEASAYCQQRYTHLVAIQNQEEIKYLNSIFNHSPSYYWIGIRKVNDKWVWIGTQKPLTEEAKNWAPGEPNNKQNEDCVEIYIKRYKDAGKWNDENCNKKKLALCYTAACTHTSCSGHGECVETINNYTCQCHPGFTGLRCEQVVTCQAQEAPEHGRLVCTHPLGNFSYNSSCSVSCEEGYLPSRTEAMQCTSSGEWSAPPPACHVVECDALTNPANGVMQCSQSPGSFPWNTTCTFDCQEGFELTGPQHLQCTPSGNWDNEKPTCKAVTCGAGGHPQNGFVNCSHSSAGEFTFNSSCNFTCEEGFVLQGPAQVECTAQGQWTQQVPVCKALQCKALSRPERGYMSCRPSTSGSFQSGSSCEFSCEQGFVLKGSKKLRCGPTGEWDSEKPTCEAVRCDAVRQPQGGLVRCTHSAAGEFTYKSSCAFSCEEGFELRGSAQLECTLQGQWTQEVPSCQVVQCASLAVPGKVSMSCSGEPVFGAVCTFACPEGWTLNGSAALTCGATGHWSGMLPTCEATAKSNIPLTVGLSAAGTSLLTLASFLFWLLKRLRRKAKKFVPASSYQSLQSDGSYQMPSESA
The following text describes a protein:
Function:
Catalyzes the NAD(+)-dependent oxidation of L-threonine to 2-amino-3-ketobutyrate. To a lesser extent, also catalyzes the oxidation of D-allo-threonine and L-threonine amide, but not that of D-threonine and L-allothreonine. Cannot utilize NADP(+) instead of NAD(+).
Subcellular Localization:
Cytoplasm.
Sequence:
MKALSKLKAEEGIWMTDVPVPELGHNDLLIKIRKTAICGTDVHIYNWDEWSQKTIPVPMVVGHEYVGEVVGIGQEVKGFKIGDRVSGEGHITCGHCRNCRGGRTHLCRNTIGVGVNRPGCFAEYLVIPAFNAFKIPDNISDDLAAIFDPFGNAVHTALSFDLVGEDVLVSGAGPIGIMAAAVAKHVGARNVVITDVNEYRLELARKMGITRAVNVAKENLNDVMAELGMTEGFDVGLEMSGAPPAFRTMLDTMNHGGRIAMLGIPPSDMSIDWTKVIFKGLFIKGIYGREMFETWYKMAALIQSGLDLSPIITHRFSIDDFQKGFDAMRSGQSGKVILSWD
The following text describes a protein:
Function:
Involved in regulation of actin and microtubule organization. Part of a WAVE complex that activates the Arp2/3 complex.
Subcellular Localization:
Cytoplasm, cytoskeleton.
Sequence:
MTLTRYQIRNEYGLADKELYSDKEDAEVLLEGSSMAGLVGLLRQLGDLAEFAGEVFHNLHEELMTTSARGQGLAIRLQQLEAQVPNSVEIPILSQTDHSIFFYDPGKSCNISGLEWHSTLKTEEHLISPHKLPHCIIDSYEECRGPPQLYLLDKFDVDGSGSCLKRYSDPSLLKKLTASQLSKDERPSKPKKKASHISNGERTLGDSQTSHAKLNQLFLMDHAEDPEITVKLKRRHLNGPPPINSSSGTGYMEKFLKNSLPYCEIVHETLDQSSSAMETDEVATCNVRVDLSTPSLVYPNNGETRKEREMEAIADDEREGGGAMVYNDTDAPPASTETEADKADVTQTGVLAANVLHHSTEEGASEGTKDVQTNDGEDDHSQHVFSVETGSEMSLTGLVEDQFCSLTNQETEKEPDCLLIQNQHISTFDNFEDLSVDADAIHDSAVPKEEDETSSQDGYSVNTEHAGHASTFEISSEAETLMLDTPRDVQTGNITPSASYWQEDALANSDLAEISSYSGKEDPQNMPIIAAGSSDGTDTQRDGAGDNHTSLNDKASETVPEVALEVDPEECLLGTQECLSPEYYIQTHSQGGQESLSETDSENTTAEAAAESLPPQDVPLGVQYSTSEETLTCNENEAEVEALNAPHQGDITSLNGNIPESVLSMDPTDQENCLDVPMAPFSTSLHVTPMEDLEITPPLPPLPPTQWWMGKLVDSVKTTETQFSPVPSLGNNSFYIHRDEKIHNGLVQGTEALDQSEASVTADESHNTDVDPVEAVLTSAKTTLNEPSKATEEEQSPSESVAWESLLTPEATPEAESTEGLEALEWFSQNLKEHTNPNLTKLEEEPQLDHPLEPPGETEGDNKSYEYNEKVEKLPRDKESLVLGIDRSMLRKVSERNRTQLGARVDENDSLLEIIRSKSFNLRPADASVRHNFHVAAPITNLKVAAILEKANSLRHAMAGSDDDHDSDSWSEQRRTNLYFPLNYQYWFVHTYDMT
The following text describes a protein:
Function:
Serine/threonine kinase that acts as positive regulator of brassinosteroid (BR) signaling downstream of the receptor kinase BRI1.
Subcellular Localization:
Cell membrane; Lipid-anchor. Endomembrane system.
Sequence:
MGGCCFSTPLDNNQQPPQQPQIPPGERKNDGFVNWPVTEFFLSDITTATNNFSSDEIISENAEESSNVVYKGCLLENLGFVAVKRFKNTPWDDPDYFTEDAKTAGELKHKRLVKLLGYCCEEDEGLLVAEFMPNDTLAKRLFQEKNMEWSMRLRVAYHIVEALDYCNSVRFDEYDNLSAYTVLFDKDGDACLSSFGLVKEIIRYNRREGGNVRTGNVTYRFGTILVNLLTGLQISPSHAPEMINGKDVTELMDPNLKGKFSTEEATIVLKLASECLQWKGYIENGITKKLVATLKALQAKKEISSSEMHEVTKQHDVASSSSQQQLPP