lhallee/plat_data huggingface dataset:
The following text describes a protein:
Function:
Could have a role in patterning the central nervous system during embryogenesis. Has a key role in regulating the distinct phenotypic features that distinguish two major classes of ventral interneurons, V0 and V1 neurons. Regulates the transcription factor profile, neurotransmitter phenotype, intraspinal migratory path and axonal trajectory of V0 neurons, features that differentiate them from an adjacent set of V1 neurons.
Subcellular Localization:
Nucleus.
Sequence:
MMFPSLIAPPAVYPNLLRPTPTLTLPQSLQSAFSSHSSFLVEDLIRISRPGSYLPRSVPQPSLSPPTSGTTSAMTDTVTSDLVSSSASSSRRGCSPQTSASQANEATFLKFGVNAILSSSPRTETSPALLQSVPPKSFSFPYFEGSFQPFIRSSYFPASSSVVPIPGTFSWPLAARGKPRRGMLRRAVFSDVQRKALEKMFQKQKYISKPDRKKLAAKLGLKDSQVKIWFQNRRMKWRNSKERELLSNGGCREQTLPTKLNPHPDLSDVGKKCPGDEDEEEDEEDENSALGSASPRHSLAFHRSPEHLHLRDRLAAQLPPSPSHSSSPSKPSDFSDSEEEEEEGEGEEEEITVS
The following text describes a protein:
Function:
Protein O-mannose kinase that specifically mediates phosphorylation at the 6-position of an O-mannose of the trisaccharide (N-acetylgalactosamine (GalNAc)-beta-1,3-N-acetylglucosamine (GlcNAc)-beta-1,4-mannose) to generate phosphorylated O-mannosyl trisaccharide (N-acetylgalactosamine-beta-1,3-N-acetylglucosamine-beta-1,4-(phosphate-6-)mannose). Phosphorylated O-mannosyl trisaccharide is a carbohydrate structure present in alpha-dystroglycan (DAG1), which is required for binding laminin G-like domain-containing extracellular proteins with high affinity. Only shows kinase activity when the GalNAc-beta-3-GlcNAc-beta-terminus is linked to the 4-position of O-mannose, suggesting that this disaccharide serves as the substrate recognition motif.
Subcellular Localization:
Endoplasmic reticulum membrane; Single-pass type II membrane protein.
Sequence:
MEKQPQNSRRGLAPREVPPAVGLLLIMALMNTLLYLCLDHFFIAPRQSTVDPTHCPYGHFRIGQMKNCSPWLSCEELRTEVRQLKRVGEGAVKRVFLSEWKEHKVALSQLTSLEMKDDFLHGLQMLKSLQGTHVVTLLGYCEDDNTMLTEYHPLGSLSNLEETLNLSKYQNVNTWQHRLELAMDYVSIINYLHHSPVGTRVMCDSNDLPKTLSQYLLTSNFSILANDLDALPLVNHSSGMLVKCGHRELHGDFVAPEQLWPYGEDVPFHDDLMPSYDEKIDIWKIPDISSFLLGHIEGSDMVRFHLFDIHKACKSQTPSERPTAQDVLETYQKVLDTLRDAMMSQAREML
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. Coatomer complex is required for budding from Golgi membranes, and is essential for the retrograde Golgi-to-ER transport of dilysine-tagged proteins.
Miscellaneous:
MISCELLANEOUS: Present with 77900 molecules/cell in log phase SD medium.
Subcellular Localization:
Cytoplasm. Golgi apparatus membrane; Peripheral membrane protein; Cytoplasmic side. Cytoplasmic vesicle, COPI-coated vesicle membrane; Peripheral membrane protein; Cytoplasmic side. Endosome. Note=The coatomer is cytoplasmic or polymerized on the cytoplasmic side of the Golgi, as well as on the vesicles/buds originating from it.
Sequence:
MSAHTYKKFENSTSGDLPDKMTIYQDCMNTFNESPVNSKRCRLLISRLLRLLAQGETFPQNEATALFFSISKLFQHQNDPLRQAVYLAIKELSGISEDVLMATSSIMKDVQNGSDLIKPDAIRSLTYVLDESTAFSAERLLKSAVVSRHPSISSAALCTSYHLLPISEVTIRRFTNETQEAVLDLKQFPNQHGNSEYYPNSTYISQYHALGLLYQLKKTDKMALLKLVRHFSENNSMKNQLAKVELVKIVNDLIYRDPQLFSQFRPLLSDWLSNKFESVQLETAKLITSFATRNSRLVAPELYAAAISALQSLLTVPRVSSRFAALRILNRISMVSPEKIVVCNPELESLINDSNRNISTYAITTLLKTGTSKNISSLISTITNFIHDVSDDFKIIIIDAVRTLSLNFPQEWKSILNFLIDVLKNSEGGFKFKNSIVEALIDIVSFVPQSKELALENLCDFIEDCEFNEILVRILHLLGKEGPSAPNPSLYVRHIYNRVVLENSIIRSAAVVALSKFALTKNDPTLYESIISLLKRIANDKDDEVRDRATIALEFIDSARNKDDVIAQNLIESKYFYDIPSLESKLSSYISSNTDSFATAFDVNQVRKFTEDEMKAINLKRKQEQIFNQKSETTLDTTPEAESVPEKRADANSFAGPNLDDHQEDLLATKYADELLSIEQIKPFGQLVNSSRAISLTEPEAEFVVRGVKHLFKDNVVLQFNITNTLTDIALDNVSVVCTPEISDEAELEELFTLQVDRLLPSEEAACYVAFKKLDEIVMEGFLNNLTFTTKEINPDTNEPFDGDEGFQDEYEIDSIFLNAGDYVKSSFTGNFSATFDELPCEEVAVFNIQEDLSIQEVVDKIILNSSCLPVESTQFAPSDSNSHTLKLFGKSALTGSKVALQIKMIKSSKGLALKVHGKGEDSLLCSDLVNGLMQ
The following text describes a protein:
Function:
Aminotransferase, part of the diffuse TOX2 gene cluster that mediates the biosynthesis of the HC-toxin, cyclic tetrapeptide of structure cyclo(D-Pro-L-Ala-D-Ala-L-Aeo), where Aeo stands for 2-amino-9,10-epoxi-8-oxodecanoic acid. HC-toxin is a determinant of specificity and virulence in the interaction between the producing fungus and its host, maize. TOXF contributes to the synthesis of 2-amino-9,10-epoxi-8-oxodecanoic acid, an essential precursor for the production of the major forms of HC-toxin by the non-ribosomal peptide synthetase HTS1.
Miscellaneous:
MISCELLANEOUS: The genes involved in HC-toxin biosynthesis, called collectively TOX2, are organized into a diffuse cluster that spans >500 kb. All of the known genes are duplicated or triplicated within this region, with some variation in copy number and chromosomal location among different race 1 strains.
Sequence:
MAIPLPAFYKWDVYDSKLNNVHGHVECRYTAQTGYWSDPCFVQSPFLSVHGLAPGLNYGQQVYEGIQARRTARNEILIFRPGASADRMAKSATAVSMPPVPYELFVRSVHMAVALNADYVPPHDFHGSMYIRPCQFGSSCQIGLQPPDEFIFCVFVQPHIALHGHGSLRALIAEDFDRAATRGTGHVKIGGNYAPVIRWTQSAKKEENGGWDVLLHVDSKTQTRIDEFSTSAFIGTKYAEEQNEPPQIILPESAAAIQSITSDSVAWLAKSFGWNIVKQPVTIDELASLSEVMAVGTAAGLVPVSCIRHNSTNRTFEFPSAGPMYRQLKETLDNIQRGRSSDSFGWCEKLRYAEFVQ
The following text describes a protein:
Function:
Cofactor for serine ADP-ribosylation that confers serine specificity on PARP1 and PARP2 and plays a key role in DNA damage response. Initiates the repair of double-strand DNA breaks: recruited to DNA damage sites by PARP1 and PARP2 and switches the amino acid specificity of PARP1 and PARP2 from aspartate or glutamate to serine residues, licensing serine ADP-ribosylation of target proteins. Serine ADP-ribosylation of target proteins, such as histones, promotes decompaction of chromatin and the recruitment of repair factors leading to the reparation of DNA strand breaks. Serine ADP-ribosylation of proteins constitutes the primary form of ADP-ribosylation of proteins in response to DNA damage. HPF1 acts by completing the active site of PARP1 and PARP2: forms a composite active site composed of residues from HPF1 and PARP1 or PARP2. While HPF1 promotes the initiation of serine ADP-ribosylation, it restricts the polymerase activity of PARP1 and PARP2 in order to limit the length of poly-ADP-ribose chains. HPF1 also promotes tyrosine ADP-ribosylation, probably by conferring tyrosine specificity on PARP1.
Subcellular Localization:
Chromosome. Nucleus. Note=Localizes to DNA damage sites; chromatin localization is dependent on PARP1 and PARP2.
Sequence:
MVGGGGKRRTAGAGPQCEKTVEVKKSKFSEADVSSDLRKEVENLYKLSLPEDFYHFWKFCEELDPEKPADALATSLGLRLVGPYDILAGKHKMKKKPTGLNCNLHWRFYYDPPEFQTIIIGDNKTQYHMGYFRDSPDELPVYVGTNEAKKNCIIIQNGDNVFAAIKLFLMKKLKEVTDRKKISILKNIDEKLTEAARKLGYSLEQRTVKMRQRDKKVVTKTFHGAGLVVPVDKNDVGYRELPETDADLKRICKAVVDAASDEERLKAFAPIQEMMTFVQFANDECDYGMGLELGMDLFCYGSHYFHKVAGQLLPLAYNLLKRDLFAKIIEDHLASRSEENIDQLAG
The following text describes a protein:
Function:
Plays a role in the normal development of the peripheral and central nervous system. Required for the correct localization of aurora kinase AURKA and the microtubule minus end-binding protein NUMA1 as well as a subset of AURKA targets which ensures proper spindle formation and timely chromosome alignment.
Subcellular Localization:
Cytoplasm, cytoskeleton, spindle pole. Nucleus, nuclear pore complex.
Sequence:
MCSLGLFPPPPPRDQVTLYEHNNELVTGGRYESPPPDFRGQWINLPVLQLTKDPLKTPGRLDHGTRTAFIHHREQVWKRCINIWRDVGLFGVLNEIANSEEEVFEWVKTASGWALALCRWASSLHGSLFPHLSLRSEDLIAEFAQVTNWSSCCLRVFAWHPHTNKFAVALLDDSVRVYNASSTIVPSLKHRLQRNVAALAWKPLSASVLAVACQSCILIWTLDPTSLSTRPSSGCAQVLSHPGHTPVTSLAWAPSGGRLLSASPVDAAIRVWDVSTETCVPLPWFRGGGVTNLLWSPDGSKILATTPSAVFRVWEAQMWTCERWPTLSGRCQTGCWSPDGSRLLFTVLGEPLIYSLSFPERCGEGKGCVGGAKSATIVADLSETTIQTPDGEERLGGEAHSMVWDPSGERLAVLMKGNPRVQDGKPVILLFRTRNSPVFELLPCGIIQGEPGAQPQLITFHPSFNKGALLSVGWSTGRIAHIPLYFVNAQFPRFSPVLGRAQEPPAGGGGSIHDLPLFTETSPTSAPWDPLPGPPPVLPHSPHSHL
The following text describes a protein:
Function:
Cationic peptide that possesses multiple functions. It acts as a cell-penetrating peptide (CPP), and as a potent voltage-gated potassium channel (Kv) inhibitor. It exhibits antimicrobial activities, hind limb paralysis, and severe muscle necrosis by a non-enzymatic mechanism.
Subcellular Localization:
Secreted.
Sequence:
YKRCHKKEGHCFPKTVICLPPSSDFGKMDCRWKWKCCKKGSVNNA
The following text describes a protein:
Function:
Endolysin that degrades host peptidoglycans and participates in the sequential events which lead to the programmed host cell lysis releasing the mature viral particles (Probable). Exhibits lytic activity against Staphylococcus aureus. The CHAP activity cleaves the peptidic bond between the D-alanine of the tetra-peptide stem and the first glycine of the penta-glycine cross-bridge. The N-acetyl-muramidase activity cleaves between N-acetylmuramic acid and N-acetylglucosamine bonds.
Domain:
Contains a cysteine-histidine dependent amido-hydrolase/peptidase domain (peptidase C51/CHAP domain) at the N-terminus, a central amidase domain and a SH3b cell wall-binding domain at the C-terminus. The CHAP domain contains a tightly bound structural Ca(2+) ion and it is present at the N-terminus and is associated with the endopeptidase activity. The SH3b domain increases the CHAP domain activity.
Sequence:
MAKTQAEINKRLDAYAKGTVDSPYRVKKATSYDPSFGVMEAGAIDADGYYHAQCQDLITDYVLWLTDNKVRTWGNAKDQIKQSYGTGFKIHENKPSTVPKKGWIAVFTSGSYEQWGHIGIVYDGGNTSTFTILEQNWNGYANKKPTKRVDNYYGLTHFIEIPVKAGTTVKKETAKKSASKTPAPKKKATLKVSKNHINYTMDKRGKKPEGMVIHNDAGRSSGQQYENSLANAGYARYANGIAHYYGSEGYVWEAIDAKNQIAWHTGDGTGANSGNFRFAGIEVCQSMSASDAQFLKNEQAVFQFTAEKFKEWGLTPNRKTVRLHMEFVPTACPHRSMVLHTGFNPVTQGRPSQAIMNKLKDYFIKQIKNYMDKGTSSSTVVKDGKTSSASTPATRPVTGSWKKNQYGTWYKPENATFVNGNQPIVTRIGSPFLNAPVGGNLPAGATIVYDEVCIQAGHIWIGYNAYNGNRVYCPVRTCQGVPPNQIPGVAWGVFK
The following text describes a protein:
Function:
Functions as an ATP-dependent nucleosome disassembly factor that helps evict canonical histone H3 from the 5'-end of genes upon their induction. Also contributes to kinetochore assembly by cooperating with SCM3 to load the histone H3 variant CSE4/CENP-A at centromeres. Provides a chromatin boundary function at the 5'-end of genes that restricts access by RTT106 and thus prevents ectopic spreading of repressive chromatin into coding regions. Also prevents heterochromatin spreading downstream of the silent mating-type locus HMR, this function is independent of the tRNA boundary element. Contributes to appropriate cell cycle regulation of histone gene expression by recruiting RNA polymerase II to histone genes, and subsequent CDK1- and casein kinase II-dependent eviction from chromatin is required to promote transcriptional elongation.
Miscellaneous:
MISCELLANEOUS: Present with 172 molecules/cell in log phase SD medium.
Subcellular Localization:
Chromosome, centromere. Nucleus. Chromosome. Note=Binds near the 5'-end within protein-coding genes. Localizes to the negative regulatory element NEG and promoter of the HTA1 gene during G2 and M-phase, and its open reading frame during G1/S.
Sequence:
MARNLRNRRGSDVEDASNAKVGYETQIKDENGIIHTTTRSLRKINYAEIEKVFDFLEDDQVMDKDETPVDVTSDEHHNNNQKGDDEDDDVDLVSPHENARTNEELTNERNLRKRKAHDPEEDDESFHEEDVDDDEEEEEADEFEDEYLDEDSKDNNRRRRAADRKFVVPDPDDDEEYDEDDEEGDRISHSASSKRLKRANSRRTRSSRHPETPPPVRRALRSRTRHSRTSNEENDDENDNSRNEALTLADEIRELQEDSPIREKRFLRERTKPVNYKLPPPLTASNAEEFIDKNNNALSFHNPSPARRGRGGWNASQNSGPTRRLFPTGGPFGGNDVTTIFGKNTNFYNQVPSAFSDNNNNKLILDSDSSDDEILPLGVTPKTKKENTQKKKKKKPEIADLDPLGVDMNVNFDDIGGLDNYIDQLKEMVALPLLYPELYQNFNITPPRGVLFHGPPGTGKTLMARALAASCSSDERKITFFMRKGADILSKWVGEAERQLRLLFEEAKKHQPSIIFFDEIDGLAPVRSSKQEQIHASIVSTLLALMDGMDNRGQVIVIGATNRPDAVDPALRRPGRFDREFYFPLPDVKARFKILQIQTRKWSSPLSTNFIDKLAFLTKGYGGADLRSLCTEAALISIQRSFPQIYRSNDKLLVDPSKIKVKVSDFMLALKKIVPSSARSTGSSPQPLPELIKPLLADQLNNLKNKLDYMLNIKDTTFQRNTSLLQNFIDYEEYSGEEEEHDKYGGNEDTSSFRSYEFFESMAESQICKPRLLINGPKGNGQQYVGAAILNYLEEFNVQNLDLASLVSESSRTIEAAVVQSFMEAKKRQPSVVFIPNLDIWINTIPENVILVLSGLFRSLQSNEKILLLCLAENLDISEVKNGILSDFAFDKNIFQLHKPSKENITRYFSNLIELLKTKPSDIPMKKRRVKPLPELQKVTSNAAPTNFDENGEPLSEKVVLRRKLKSFQHQDMRLKNVLKIKLSGLMDLFKNRYKRFRKPPIDDAFLVHLFEPETSNDPNWQPAYIKDENMILEVSTGRKFFNMDLDIVEERLWNGYYSEPKQFLKDIELIYRDANTIGDRERVIKASEMFANAQMGIEEISTPDFIQECKATRQRDLERQELFLEDEEKRAAMELEAKEQSQENILQEPDLKDNKANEFGVAAGNQLQAQLQTTINTASIVNNSEVPQPIDTNLYKKEIPAAIPSAVDKEKAVIPEDSGANEEYTTELIQATCTSEITTDDDERARKEPKENEDSLQTQVTEENFSKIDANTNNINHVKEIQSVNKPNSLHETVEKRERSPIPKEVVEPEQGKKSDKELILTPEQIKKVSACLIEHCQNFTVSQLEDVHSSVAKIIWKSKSAWDKTGTVDEIIKFLSE
The following text describes a protein:
Function:
ESCRT-III-like protein involved in cytokinesis, nuclear envelope reassembly and endosomal tubulation. Is required for efficient abscission during cytokinesis. Involved in recruiting VPS4A and/or VPS4B to the midbody of dividing cells. During late anaphase, involved in nuclear envelope reassembly and mitotic spindle disassembly together with the ESCRT-III complex: IST1 acts by mediating the recruitment of SPAST to the nuclear membrane, leading to microtubule severing. Recruited to the reforming nuclear envelope (NE) during anaphase by LEMD2. Regulates early endosomal tubulation together with the ESCRT-III complex by mediating the recruitment of SPAST.
Sequence:
MFSSPFKADRLRVNLQLVVNRLKLLEKKKTEQAQKARKEVADHLAAGKDERAGIRVEHIIREDYLVEAMEILELYCDLLLARFGLIQATKELDSGLAEAISTLIWAAPRLQSEVPELKIVSLKNFNCLYNECR
The following text describes a protein:
Function:
Substrate recognition component of the SCF(CCNF) E3 ubiquitin-protein ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of target proteins. The SCF(CCNF) E3 ubiquitin-protein ligase complex is an integral component of the ubiquitin proteasome system (UPS) and links proteasome degradation to the cell cycle. Mediates the substrate recognition and the proteasomal degradation of various target proteins during G2 phase involved in the regulation of cell cycle progression and in the maintenance of genome stability.
Subcellular Localization:
Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole. Cytoplasm, perinuclear region. Nucleus.
Sequence:
MKGGGLHCRCSKCFAAPPRRRIKRRPRVLTLLSLPEDVLLYVLECLPAVDILSMREVHPHLRSLVDSHSSVWARASFQDVWPSSENLNLFERAAECGNFEACVKLGIAYLYNEGLSVSDDGRAEVNGLKASRFFSLTERLNAGADPFVWLFIRPPWSSSGSCCKAVVFDSLNEECGTVTSGEGATGALKGSIQYCLAKVLSLFEDDDKKREALGMLESSASNGCLHSAYLLWETKQKTALSDPGRYLQSFRQLRDYAARGCWDAQISLAKACGHKNPLNQEQRSAGELVNQVFQSSLPINKSSIFTTQKGMNDTMRYILIDWLVEVATMKDFSSLCLHMTVGLVDRYLKLRSVPRAKLQLVGIACMVICTRFISKEILTIREAVWLTDNTYKYEDLVRMMGEIISALEGKIRMPTVVDYKDVLSHLIPLDRNTLHLCSYISELSLLYTELSMYSPAQLAAGALLLARILHRQARPWPAQLAETTGFTLEHLTPCVVLLHKKCFHDDAPRDYRQVSLTAVKQRFQDDLYDQISKEKQVMDHTHLCELLGVPCHDSESPATCPNAADFHQFLCSPSGNKTKRRREESIQEDRGSFVTTPTAELSNQEEDLLGDFLDWSLETSCSGYEGDRESEGEREGEVTAPSGVLDLSLLLTEHPQCQDSTTDDDSITLHPIPLLSKAENGTDSIEGCVEKSSGYSSVSSGGSPTSSSSPGLPFTPTPGLNHSKLTPIPFPQPCSPLLKASRRQVKRKNQAQHSEDNLSDEL
The following text describes a protein:
Function:
Type II glyoxalase that catalyzes the hydrolysis of (R)-S-lactoylglutathione to (R)-lactate and glutathione. Is more efficient than the isozyme GloC, and plays a major contribution to methylglyoxal (MG) detoxification in E.coli. The two isoenzymes have additive effects and ensure maximal MG degradation.
Sequence:
MNLNSIPAFDDNYIWVLNDEAGRCLIVDPGDAEPVLNAIAANNWQPEAIFLTHHHHDHVGGVKELVEKFPQIVVYGPQETQDKGTTQVVKDGETAFVLGHEFSVIATPGHTLGHICYFSKPYLFCGDTLFSGGCGRLFEGTASQMYQSLKKLSALPDDTLVCCAHEYTLSNMKFALSILPHDLSINDYYRKVKELRAKNQITLPVILKNERQINVFLRTEDIDLINVINEETLLQQPEERFAWLRSKKDRF
The following text describes a protein:
Function:
Required for correct meiotic chromosome segregation and recombination.
Subcellular Localization:
Nucleus.
Sequence:
MENQVSSFLIDSPMEWKTYMKSLSDDNPSFGDVTVNLTKISVSSKNAKSYAEEMYNYVTQEMVFISERSRLLLRAKRRLYKNQSLMKKTSVSTSNTVKMVFMSLAKQIEQMLKFCMMVYSKLCEAFETTLKVAKEFQICDSSQEWFFQFQLGYHRKQMELQMLSFVAEWLVLTQHYTDALNDSAKTLYDIMESSHKAAQKV
The following text describes a protein:
Function:
Repressor of the lactose catabolism operon. Galactose-6-phosphate is the inducer.
Sequence:
MIKDERVLELIEIIKKKKRIAVKELAEITFSSTSTLRRDLIFLENQGLIKRKHGYVTLSSMNTIELSHQIREGESTRQKRLIASLAKDFIRSGMCIYLDSSTTVYELCPYLSELDNLIIFTNGLHTAQTLSETVKDSSKIFITSGEVKHQSCSVVNYDKENSLLDHFNIDLAFCSARGIDDQYVYEASLSQAISKKNIIDKAHETILLIDSSKFYKTGFFKINPLSKYTTFISDTLPDQKLLDAVELFDGEWVSDIQ
The following text describes a protein:
Function:
Catalyzes the decarboxylation of 3-octaprenyl-4-hydroxy benzoate to 2-octaprenylphenol, an intermediate step in ubiquinone biosynthesis.
Subcellular Localization:
Cell membrane; Peripheral membrane protein.
Sequence:
MKYKDLRDFIAMLEQQGKLKRVAHPISPYLEMTEIADRVLRAEGPALLFENPIKPDGTRYGYPVLANLFGTPERVAMGMGADSVSKLREIGQTLAYLKEPEPPKGIKDAFSKLPLLKDIWSMAPNVVKNAPCQEIVWEGEDVDLYQLPIQHCWPEDVAPLVTWGLTVTRGPHKKRQNLGIYRQQLIGKNKLIMRWLSHRGGALDYQEFRKLNPDTPYPVAVVLGCDPATILGAVTPVPDTLSEYQFAGLLRGSRTELVKCIGNDLQVPARAEIVLEGVIHPNETALEGPYGDHTGYYNEQDYFPVFTVERITMRENPIYHSTYTGKPPDEPAVLGVALNEVFVPLLQKQFPEITDFYLPPEGCSYRMAVVSMKKQYAGHAKRVMMGCWSFLRQFMYTKFIIVVDDDVNVRDWKEVIWAVTTRMDPVRDTVLVENTPIDYLDFASPVSGLGGKMGLDATNKWPGETDREWGRVIKKDPAVTAKIDGIWEELGL
The following text describes a protein:
Function:
Catalyzes the NADPH-dependent reduction of ketopantoate into pantoic acid.
Sequence:
MLSVAIIGPGAVGTTIAYELQQSLPHTTLIGRHAKTITYYTVPHAPAQDIVVKGYEDVTNTFDVIIIAVKTHQLDAVIPHLTHLAHEDTLIILAQNGYGQLEHISFKNVCQAVVYISGQKKGDVVTHFRDYQLRIQDNALTRQFRDLVQDSQIDIVLEANIQQAIWYKLLVNLGINSITALGRQTVAIMHNPEIRTLCRQLLLDGCRVAQAEGLNFSEQTVDTIMTIYQGYPDEMGTSMYYDIAHQQPLEVEAIQGFIYRRAREHILDTPYLDTIYSFLRAYQQNM
The following text describes a protein:
Function:
Metalloprotease.
Subcellular Localization:
Secreted.
Sequence:
MLFVSILISQFVTCLTQPDFFERPPPPDWFFPGPLRPWGPPPPWHRNRGPPPFGPPPPWDRPPPPWRRPPWHRRPPWGLPPPPPPPEPEPQQDQPQVMFSQDIDKVVNSVNQNTAAFQRPGESYDKVIQIMSSYFNRKSGSQYDINTVIPSSGIYNNEMAANSKIAAVMFESDMALTVSQMNKVAQNGFRVKRKMNLNGTTWSRNIPYRFLDTDGNWQSQITNGLRHYERNTCIRFSLNGGGSDYLVFSKGEGCYSSVGRLGGPQEISIGDGCETLGIITHEVGHALGFWHEQARPERDSYVRINRQNAINGLEGQFDKRSWSEVNEYSLPYDYGSVMHYGPKSFSKSSTMNTVEPVDPAFINTIGNRVEPSFLDLKLLNTAFCSNICTNRINCQHGGYADPNNCGQCTCPTGLEGTYCERLQTSNCGVELPRADYSWRNISYSGSSDCYWRIVSANGGNVRFELTYVMYRCSPVCEEFVEMKAEYSHEATGYRQCCKAVLGERISKGNSVLIISKATQNSQFVLRYREDGTAPTQRPPPVRVAAPRSYSLLWSGWTRCSENCGSCGTQYRERCTSTTNCLRSAKQTRVCNTQPCAQGTTRGKRSVLQTQISHRVKRLNGWCCARFVLSRGVCVPVRTGVTHPN
The following text describes a protein:
Function:
Acts as a component of the translation initiation factor 2B (eIF2B) complex, which catalyzes the exchange of GDP for GTP on eukaryotic initiation factor 2 (eIF2) gamma subunit. Its guanine nucleotide exchange factor activity is repressed when bound to eIF2 complex phosphorylated on the alpha subunit, thereby limiting the amount of methionyl-initiator methionine tRNA available to the ribosome and consequently global translation is repressed.
Subcellular Localization:
Cytoplasm, cytosol.
Sequence:
MSKNDKKNKQSGSSNMDQLKSEDILQAVVLGDSFDRKFAPITLEKPRTLLPLVNIPLLDYTLEFLAASGVQQIFVFCCAHASQIKEYIQSSRWHDLPGVQVICMTGSNCRTTGDALRGVYDAQVIQSDFILISGDVVSNMNLQKALQIHKDRRELDKNNIMTMVYKQASSTHRTRSKQDDTVIWCNRDTMQVVCYDNSPSKKKSSISVELFQKHPSIQMRYDLIDCHIDICSPEVLALFNDNFDFADIRKDFIHDILTSDLLDYKLSAYVLQGEYAARVKDLRTYHSVSKDIIHRWTFPMVPDNNFMCNSSYSLSRQMIYKEKNVKLLGDCLISDETVIGTQTEIGAGSIVSHSTIGRNCIIGKNVKINGSYIWDDVTIQDNAIIDHSIICNGSIIKSSSIIGRGSIIGFNVYIGQSKTLEPFSKITMAQYNEDEDDEELLEEYFKEINLNDDNNNNNNNNNENNKTNRWLMENELYNELVPRINDSIHDDIESDESGDEGDKSGGKIKNNKNNDDNPIEPDSVKFHREVGDTIRRGIIEKLPLENIQLEINGLKFAYDRDGLDCLTSILPVLLESSSSSSSTTDSVTPKELQQFIAGRISAFSPLLVKFSSEDSMVDLIFKIQDFCDENEKFKVVFQPILHQLYENDVISEEAIFEWAEEIEGDEEDDGFYLKKCKGFIDWLKSAEEESDDSDDSDDDDDDSDESD
The following text describes a protein:
Function:
Functions in trans to edit the amino acid moiety from incorrectly charged tRNA(Ala).
Subcellular Localization:
Cytoplasm.
Sequence:
MVFRCQRDSWARQFATRVVSCREAELRPESGGEPMRGFQVVLEDTILFPEGGGQPDDRGLIGAVPVLRVTRRGAEAVHFVETALEPGSAVLLSLDWERRFDHMQQHSGQHLITAIAEQMFGFKTTSWELGRQQSVIELDTPSMTTEQMEALEQSVNEKIRERIPVTVRELAADDPEVETVRSRGLPGDHTGPVRVVDIEGIDSNMCCGTHVSNLSDLQVIKLICTEKGKKNKTNLVFLAGNRVLKSVEQSHRTEKALTSLLKNGPGEHVEAVKRLQSSVKLLQKNNLNLLRDIAVLIARDFKSKPVQSPLFVLHRKEGDSEFMNIIANEIGKEETLLFLTVGDEKEAGLFLLAGSVEAVENLGPRVAELLEGKGAGKRGRYQGKATKMSRRGEVQALLQEFISQQTDEA
The following text describes a protein:
Function:
Transcription activator. Binds the promoter core sequence 5'-GGNCC-3'.
Subcellular Localization:
Nucleus.
Sequence:
MEAAVGDGEGGGGGGGRGKRGRGGGGGEMVEAVWGQTGSTASRIYRVRATGGKDRHSKVYTAKGIRDRRVRLSVATAIQFYDLQDRLGFDQPSKAIEWLINAASPAIDTLPSLDPAAFAAIPHAAADAAPTRRRSQQQQQQLSNKSGCSSTSETSKGSDKEVTVASAPAQAASFTELLIAGVAASSAGGGAIGNGADCVGIAHPGKGGAEGASTYGFSAASSFGDAPPIGMVPAPPFNFSAPGADMAAHYSLAQDQLAAPPPPAGGDYNLNFSMSSGFLGANRGTLQSNSPSNMSGHHHHHHQQQLQRLDGSTISFLLGHAAAAAHPAASEGQITSTAALQLWDGFRHSGMKEKSKN
The following text describes a protein:
Function:
Catalyzes the condensation of 2 farnesyl pyrophosphate (FPP) moieties to form squalene.
Subcellular Localization:
Endoplasmic reticulum membrane; Multi-pass membrane protein.
Sequence:
MGSLGTLLRYPDDIYPLLKMKRAIERAEKQIPPEPHWGFCYSMLHKVSRSFSLVIQQLRPELRNAVCVFYLVLRALDTVEDDTSIPTDEKLPILIAFHRGTKEYKVLMDQFHHVSAAFLELDKGYQEAIEEITKRMGAGMAKFICQEVETVDDYDEYCHYVAGLVGLGLSKLFLASGSEVLTPDWDHISNSMGLFLQKTNIIRDYLEDINEIPKSRMFWPRKIWGKYADKLEDLKYEENSTKAVNCLNEMVTNALTHIEDCLKYMAALRDPSIFRFCAIPQIMAIGTLALCYNNVQLFRGVVKLRRGLTAKVIDRTKTMADVYGAFYDFSCMLKTKVDKNDPNASNTLNRLEAVEKVCKDTGVLQKRKSYVNDEGQSNVYIVMLVILLAIVFAYLRAN
The following text describes a protein:
Function:
Component of SUN-protein-containing multivariate complexes also called LINC complexes which link the nucleoskeleton and cytoskeleton by providing versatile outer nuclear membrane attachment sites for cytoskeletal filaments (By similarity). Required for nucleus structure organization (e.g. size and shape).
Subcellular Localization:
Nucleus membrane; Peripheral membrane protein. Nucleus, nucleoplasm. Cytoplasm. Nucleus lamina. Note=Recruited to the nucleus envelope (NE) by SUN proteins and is immobilised therein (By similarity). Mostly localized in the nucleoplasm and, to a lesser extent, at the nuclear periphery. During prometaphase to anaphase, localized diffusely in the cytoplasm. A small population is later transferred from the cytoplasm to the chromatin surface. Relocalized to the nuclear periphery during late telophase.
Sequence:
MTPRSETHKIGGVTNPRNADRKGKAVAFSDDLVIPTLPPPPIGTLTGQGVSRGHTDDMDMGDWRRFREVGLLNEASMEKKDQEALLEKISTLEKELYGYQHNMGLLLMENKELVSKHEQLNQAFQEAQEILKREQSSHLYALTTVEQREENLRKALGLEKQCVQELEKALREIQEENSKIRLSSEAKLVEANALVASVNGRSSDVENKIYSAESKLAEATRKSSELKLRLKEVETRESVLQQERLSFTKERESYEGTFQKQREYLNEWEKKLQGKEESITEQKRNLNQREEKVNEIEKKLKLKEKELEEWNRKVDLSMSKSKETEEDITKRLEELTTKEKEAHTLQITLLAKENELRAFEEKLIAREGTEIQKLIDDQKEVLGSKMLEFELECEEIRKSLDKELQRKIEELERQKVEIDHSEEKLEKRNQAMNKKFDRVNEKEMDLEAKLKTIKEREKIIQAEEKRLSLEKQQLLSDKESLEDLQQEIEKIRAEMTKKEEMIEEECKSLEIKKEEREEYLRLQSELKSQIEKSRVHEEFLSKEVENLKQEKERFEKEWEILDEKQAVYNKERIRISEEKEKFERFQLLEGERLKKEESALRVQIMQELDDIRLQRESFEANMEHERSALQEKVKLEQSKVIDDLEMMRRNLEIELQERKEQDEKDLLDRMAQFEDKRMAELSDINHQKQALNREMEEMMSKRSALQKESEEIAKHKDKLKEQQVEMHNDISELSTLSINLKKRREVFGRERSRFLAFVQKLKDCGSCGQLVNDFVLSDLQLPSNDEVAILPPIGVLNDLPGSSNASDSCNIKKSLDGDASGSGGSRRPSMSILQKCTSIIFSPSKRVEHGIDTGKPEQRLSSSVAVGMETKGEKPLPVDLRLRPSSSSIPEEDEEYTDSRVQETSEGSQLSEFQSSRRGRGRPRKAKPALNPTSSVKHASLEESSKDELSGHVSVTSKKTTGGGGRKRQHIDDTATGGKRRRQQTVAVLPQTPGQRHYNLRRKKTVDQVPADVEDNAAAGEDDADIAASAPSKDTVEETVVETLRARRIETNADVVSAENNGDVPVANVEPTVNEDTNEDGDEEEDEAQDDDNEENQDDDDDDDGDDDGSPRPGEGSIRKKLWTFLTT
The following text describes a protein:
Function:
Catalyzes the removal of transit peptides required for the targeting of proteins from the mitochondrial matrix, across the inner membrane, into the inter-membrane space. Known to process the nuclear encoded protein DIABLO.
Subcellular Localization:
Mitochondrion inner membrane; Single-pass membrane protein.
Sequence:
MLGEAIEARRHFLNLRCQPGRISLRLKKCISEVKDKVGSAQCHPLEQRAGIPSGEWRQLKERSPKNPEQKIIKRVIALEGDIVRTIGHKNRYVKVPRGHIWVEGDHHGHSFDSNSFGPVSLGLLHAHATHILWPPERWQKLESVLPPERLPVQREEE