lhallee/plat_data huggingface dataset:
The following text describes a protein:
Function:
The PE25/PPE41 dimer induces both a strong humoral and cellular immune response. The dimer induces necrosis, but not apoptosis, in mouse macrophage cells. It also induces activation and maturation of mouse dendritic cells and drives Th2-biased immune responses.
Subcellular Localization:
Secreted. Cell surface. Note=Secreted via the ESX-5 / type VII secretion system (T7SS).
Sequence:
MHFEAYPPEVNSANIYAGPGPDSMLAAARAWRSLDVEMTAVQRSFNRTLLSLMDAWAGPVVMQLMEAAKPFVRWLTDLCVQLSEVERQIHEIVRAYEWAHHDMVPLAQIYNNRAERQILIDNNALGQFTAQIADLDQEYDDFWDEDGEVMRDYRLRVSDALSKLTPWKAPPPIAHSTVLVAPVSPSTASSRTDT
The following text describes a protein:
Function:
Plays a major role to prevent cellular inhibition of viral genome replication. Assembles an SCF-like E3 ubiquitin ligase complex based on the cellular proteins ELOB, ELOC, CUL5 and RBX1, in cooperation with viral E4orf6. This viral RING-type ligase ubiquitinates cellular substrates and targets them to proteasomal degradation: TP53/p53, LIG4, MRE11-RAD50-NBS1 (MRN) complex, ITGA3, DAXX and BLM. E1B-55K probably acts as the substrate-specific adapter of the SCF-like E3 ubiquitin ligase complex. Degradation of host TP53/p53 activity is essential for preventing E1A-induced TP53 accumulation that would otherwise lead to cell apoptosis and growth arrest. E1B-55K also inactivates TP53 transcription-factor activity by binding its transactivation domain. E1B-55K also functions as a SUMO1 E3 ligase for TP53 which causes the latter to be sequestered in promyelocytic leukemia (PML) nuclear bodies thereby contributing to maximal inhibition of TP53 function.
Subcellular Localization:
Host nucleus. Host cytoplasm. Note=Colocalizes with host TP53 to host PML nuclear bodies. PML localization of E1B-55K is necessary for E1B-55K-dependent SUMOylation of TP53.
Domain:
Contains a PML interaction motif that allows the subnuclear PML localization.
Sequence:
MAQNNSDGVEGASPAKRRRLDQVTYSEICADFRSGSFSDFFMEKYNFAQVASYKMQPDDDWTDMIAQHAKIELDPTKEYVILSTVFIQSNCYIIGHGAKIVIVGEPGIAFKVLTKSFGPVITNMWAVSFTDCVFQRRDSYNGKVFTCASQVLFHNCFFVGFTGTCITSTAALTVRGCQFLACYRPIMFLAAFDLTVKHCVFDKCVIAISTEGDFEISSNLCTDSCCFLSAAGTGIFSYNSIVNPFTLQDSAEFSMVTCADAKVQLLHTIHIHSNPKLVYPQFMHNVLLRAKLFVGRRRGGFHPHFCSLKYSLLTLAKGSERKVNLSTCYPDGLKVYKVLNRNPNRLFTRLCECDASHQTADIVLGEVGLPATADPTLDSVDCLEFSSDEEW
The following text describes a protein:
Function:
Component of the RIX1 complex required for processing of ITS2 sequences from 35S pre-rRNA.
Subcellular Localization:
Nucleus.
Sequence:
MPKASKRQKEKKADFQKTKLKLGKGKQAANNATDVSFKAKTIALPQQSINVDKSGKLVNSRNLTIADLALQLRHYSAAVRRDAITGIKEILTLHPSLLMTDAASIVPELSRCIGDEDAAVRKQLHALIAWMLPQIPAQLLGTFQNTLLLFTTSALSHIYPEVRLDAVKILDVCLNVLPHAATTGWENAVHKMASAVSSASNRNRTTSSDTVGPSSATHQPHGERIMNCYLNLLGITQRSSSAASITATDLASASKLLIIRSLRTFLSHALRSTSDEDSDADFQHSCPTWFFRSAFACPAEFEYFQRILGRKSSSIQSRCVEVKHAKKHEVDGSTGVRESYSDWPPLASAATSLMDLDFTLGTSLHQSDLFDSLHMASTLEPSLSTASSVTLSAKPTQSAALSLYTLLDPALLASFLDTAPSAFQPDLDLSLPSRGQNVGLSTPAQLIFELISLMRALWRGSTVGCTQARTALANTLGHVSIYFPFSHRTSSSGLSARAKSAVVQVDLAYAELVALLALNDAKLQKVKSKFNVKVQIASVSSFIGELLSTPVTESGTVSLDTVSASAAGVLDPNTFRALLPTLWFLLGTEHETLLDSLLATFHTHTNQHRVKPVLFEFLARAFLLSKMRASTPFTNQENDRILESLLSTLPRSLWEAASSSAGFTFAGVQLEFLHFLLLSSSPPANLAYDKLGPFYFFRHPTKKVSGPGPFSRLPHTLRKLALDNIALLQGRDSKLDKAMSQALEFAQTSTSG
The following text describes a protein:
Function:
Transcription factor that can both stimulate and repress transcription. Binds to the consensus DNA sequence 5'-A/GCAGGTG-3'. Regulates cell motility and adhesion during tracheal morphogenesis by stimulating transcription of the DE-cadherin gene shg at branch tips, thereby promoting tracheal tube fusion. Maintains diploidy in imaginal cells by inhibiting the transcription of genes required for endoreplication. Required for development of the genital disk and acts as an intrinsic determinant of wing cell fate. The somatic protein is required for maintenance of male germ cells. Acts with other members of the snail protein family to control embryonic central nervous system development.
Subcellular Localization:
Nucleus.
Sequence:
MHTVEDMLVEKNYSKCPLKKRPVNYQFEAPQNHSNTPNEPQDLCVKKMEILEENPSEELINVSDCCEDEGVDVDHTDDEHIEEEDEDVDVDVDSDPNQTQAAALAAAAAVAAAAAASVVVPTPTYPKYPWNNFHMSPYTAEFYRTINQQGHQILPLRGDLIAPSSPSDSLGSLSPPPHHYLHGRASSVSPPMRSEIIHRPIGVRQHRFLPYPQMPGYPSLGGYTHTHHHHAPISPAYSENSYYSMRSMTPESSCSSSLPEDLSLKHKNLNLNLNTSQPGEQAAAKTGDMSPETMPNASAKKDKNQPPRYQCPDCQKSYSTFSGLTKHQQFHCPAAEGNQVKKSFSCKDCDKTYVSLGALKMHIRTHTLPCKCNLCGKAFSRPWLLQGHIRTHTGEKPFSCQHCHRAFADRSNLRAHLQTHSDIKKYSCTSCSKTFSRMSLLTKHSEGGCPGGSAGSSSSSELNYAGYAEP
The following text describes a protein:
Function:
With LigD forms a non-homologous end joining (NHEJ) DNA repair enzyme, which repairs dsDNA breaks with reduced fidelity. Stimulates rNTP addition to DSB and end joining (ligation) of linear DNA by LigD, on 3'-overhangs and probably also 5'-overhangs and blunt dsDNA breaks. Binds both ends of linear dsDNA protecting it from exonuclease activity.
Sequence:
MARAIWKGAISFGLVHIPVSLSAATSSQGIDFDWLDQRSMEPVGYKRVNKVTGKEIERENIVKGVEYEKGRYVVLSEEEIRAAHPKSTQTIEIFAFVDSQEIPLQHFDTPYYLVPDRRGGKVYALLRETLERTGKVALANVVLHTRQHLALLRPLQDALVLITLRWPSQVRSLDGLELDESVTEAKLDKRELEMAKRLVEDMASHWEPDEYKDSFSDKIMKLVEEKAAKGQLHAVEEEEEVAGKGADIIDLTDLLKRSLRSRAGGGKDKGSEKAGADAKGRAKSGASRSRRKA
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:
MHGRPREYKNKLKADPKAQEAYKKKVDAIRNGTALVLEYRRQKKYEPAIMDAAAKLLKVVPEIYTLWNYRREALEPVFAAGGEEAARASEGELALTQACLMENPKSYSAWHHRKWVVGQGLAPLERELQLVTRALDEDSRNFHAWNYRQFVCRKLGRSAQDELGYVEEKIIQNFSNYSAWHFRTMLLHQIYGTPGGPEAGVGTEAPASASSPAPGAGGTAGAAASGSASQRSPIPHEVLDAEYDMVHQAFATDARDESPWTYYRWLVGNTLAHLGPAAATAAAAAAAGSLEAASGAGADAAASGAPGTGGEASREGREGQEGQAEVDEEARARVAAVLEREAARLQEDHLAAEPDAKRPLLALARLREAQARLGLGDSAEAGAALLEEARGIYRRLMDIDPLRRGYYQDALEGRAFVVVQALGTV
The following text describes a protein:
Function:
Receptor for angiotensin II, a vasoconstricting peptide, which acts as a key regulator of blood pressure and sodium retention by the kidney. The activated receptor in turn couples to G-alpha proteins G(q) (GNAQ, GNA11, GNA14 or GNA15) and thus activates phospholipase C and increases the cytosolic Ca(2+) concentrations, which in turn triggers cellular responses such as stimulation of protein kinase C; Receptor for angiotensin II, a vasoconstricting peptide, which acts as a key regulator of blood pressure and sodium retention by the kidney. The activated receptor in turn couples to G-alpha proteins G(q) and thus activates phospholipase C and increases the cytosolic Ca(2+) concentrations, which in turn triggers cellular responses such as stimulation of protein kinase C.
Subcellular Localization:
Cell membrane; Multi-pass membrane protein. Membrane; Multi-pass membrane protein.
Sequence:
MDTAALNASIGSISNITSLTPSEKSPRNHCSSIPDDFEFIFILVPIFYIIIFIVGILGNMIIVIGLTCFLQAKTVANIYIVNLAIADLSFVATLPLWAVSMAAKYEWTFGSFMCKFCATMSSMNMFSSIFLLTCLSIDRYFGIVHPMRSLKWRTQAKAKIVTFIVWASACAASFPTMYFRETYYSKKHQIITCAMKYPKQRVFWPNFVDLMKNIFGFVIPFLIQGGCYCLIYKNVLASKKSKVKNAKSDNILKVVLAMVSAFIVCWLPFQIASFLKVLVRITWISNCKVAQIINAVMPVTVCIAFSNSCVNPILYFFASKRFRNQLAIALRKSFSQSYRTTRTR
The following text describes a protein:
Function:
May act as an effector of RAP2A in neuronal cells.
Sequence:
MEASFVQTTMALGLSSKKASSRNVAVERKNLITVCRFSVKTLLEKYTAEPIDDSSEEFVNFAAILEQILSHRFKGPVSWFSSDGQRGFWDYIRLACSKVPNNCVSSIENMENISTARAKGRAWIRVALMEKRMSEYITTALRDTRTTRRFYDSGAIMLRDEATILTGMLIGLSAIDFSFCLKGEVLDGKTPVVIDYTPYLKFTQSYDYLTDEEERHSAESSTSEDNSPEHPYLPLVTDEDSWYSKWHKMEQKFRIVYAQKGYLEELVRLRESQLKDLEAENRRLQLQLEEAAAQNQREKRELEGVILELQEQLTGLIPSDHAPLAQGSKELTTPLVNQWPSLGTLNGAEGASNSKLYRRHSFMSTEPLSAEASLSSDSQRLGEGTRDEEPWGPIGKDPTPSMLGLCGSLASIPSCKSLASFKSNECLVSDSPEGSPALSPS
The following text describes a protein:
Function:
Enhances Ca(2+)-mediated inhibition of inositol 1,4,5-triphosphate receptor (ITPR) Ca(2+) release.
Subcellular Localization:
Cell membrane; Single-pass type I membrane protein. Nucleus outer membrane; Single-pass type I membrane protein.
Sequence:
MEDTLLSVFVVVVSLILSKDHNVFHEQDDDIIVSMQDHEHFLLKEKAKLEQGEHPVAIELPYSNQEASQSHRKLPIEGHVSDVKQIEPNVETKVLHEEQMSSMGEQNEFRQKASDDQEILSIDKDKWTVHMASEGPTNEQVRLGSTVDQNVSQGEAEHPEEPKYDRIDTHREHQADEGFDQKIPTSSQRLTTRPQEKQPNDQDVTFIYFLWRTYSIISLFHFLKRFLKKGSKTQKMLRSTNVSKIVSNIDYKTLTSFHNQCVVLPRNHSWQTCEFVEGFVNDLLETVRNSSTAGADMEIEDFVGIGSFYEQWASRKSVVCDIHVPIIPPKSCSFEFTLLKENRGSTAQNSCRIKMVKNSGNCHCNSSNIDNPDDDDLLCLLHLDNKIDDHAPDKCINDLCQENTSYLAKTKVLKWFKSTVRKAWNEISHKYDFELIFRNRENPGSLKVRFRSGRVIQFRLTPVVRFKDSEAHLMSYLPSDVFSDTYWPVCFARYENALLQHLTNTLPDNACHIYVLQMLSFLHKHQTGLTGPCGLTSYHLKTALLHLLLKKTLHWEPEQIGCRLNDLFTFLLEKLNAKMLDHVLVANPLIPCVIGLPKEFTEGKPVNLFLPLLSDDKLYLKTNRHLLEMIKNMPVLIQEYGSVRNALQQNHL
The following text describes a protein:
Function:
Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) 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. F-type ATPases consist of two structural domains, F(1) - containing the extramembraneous catalytic core and F(0) - containing the membrane proton channel, linked together by a central stalk and a 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. Part of the complex F(0) domain. Minor subunit located with subunit a in the membrane.
Miscellaneous:
MISCELLANEOUS: Present with 14600 molecules/cell in log phase SD medium.
Subcellular Localization:
Mitochondrion. Mitochondrion inner membrane.
Sequence:
MIFKRAVSTLIPPKVVSSKNIGSAPNAKRIANVVHFYKSLPQGPAPAIKANTRLARYKAKYFDGDNASGKPLWHFALGIIAFGYSMEYYFHLRHHKGAEEH
The following text describes a protein:
Function:
May play a role in microtubule-mediated transport or vesicle function.
Subcellular Localization:
Cytoplasm. Nucleus.
Sequence:
MATTEKLLKAFESLKAFQQGNVTGEETSTASQTAPVGQMSNLLTTSPAEFTEVARDIVASLATGKKELAVGKKDRVAHLVTIADAMCASNFRTMAEFPKFLGISMEMFLASCDDKESDVRMVADECLNRTVKMLLETNLGRLQVELYKEIKKNGPARSLRAALWRFAELSHLIRPQKCRPYVVNLLPCFNRICRRQEDAVQETLANSLKKTFPVLGSFTNDAEIKVLLKTFLPNLRSASAVTRRTAASSLVTFCQHSRKPRHFFCWLLTVLLGMVIPIQEDRKSHTLLGVLLCLRHLVPHLATLQDLEDDSLKGSFGVTKKDPELSVSTEQLVQIFELVLHYSQHTDHNVVTASLETFQQLLRTPPPGLLPVLTRPGSITQSSIFKEGGQHRVGSSSQLSAAGVGEEDSGMEDDRSEVSSTATDDLPPIVKLNLDPTMQSMEQSSSAADLETLDSSAAESSGIGLLQTGGEGGIFNALEKADSLPDTPTTTEFPGNVQDFPEHAAADDVIINADGGSYSNVEIGSVTVEDDFPSESEVSPVGIVAEFIKTHQRADSNVSAGSQEAERQVTEEVSLAEEGSEVAASAERMMGDVGHYTDEEVPLIYCTRLLCSSFLLTGHEKGLIRDREVRVSVKALSLGCLAAIFNLHPRALSIKLFRPSQDTQGPESRQLVRDILLFSNHGDPQLKGNTAVLVGNFIHSALTEARLKYDLWIQAICEEQGTPPVLLESLVSCLQTCLTDQASVTCRMACVALKTCLVTLLQSSSGDLGLRLVLATLGQRDTSYWLGKVELLELLSQVDFKLVKYLEDSFPYMRKGDHSYLGAMNCQQRLLEDIVLHLMGDDDYRVRHAATAALGRLVPRLFYPVDHPQHDPVVASAKEYSSAHLEQEGQQQSEEPYRPPPCTMWGYETSGLVSASLESSLSRVVSAIMRRLNSSTSKSLTFGCLHALCQLSQQFPVCQYTTAWCCVGITTFTPKDSSGRTNLPRPGSRSRSLNGSLTSSMTSSLTSSITSTSSISSVSSQLSMEESITGSGGGPLPMVLSLLLSSWLPLDLAAHQDALLLAGNLLAGAASRSLKAPYDEEKPTGKDGVKEVGKEEEDGWHALQDRNLVPLAQQLLSHLARVVNVCSHVIEQVIPGPPAKTALPSLPNAPSLSPIKRKPKGKDGVDQGSATASPSKSSAKKGSDAGLPTEKEPDRPNKSNIGTFWQLPGYMKLYSVLKGAYSNYKVSLDPSATEKFLGLLKTVLNVLSQVLEIATFIDISKYVEELLSYLKSTVAMEPTSTIQCVEQLLKALFGTNLASQWDGSQTAETSRKPGKATRLSSNMKPGLYHYCFTAPYTQFTQSLAAASFRTSQAEGEEGGGILSWFKHRSSDKKVSPAIAKLVKGDKTPIHNYIRLFEPLVIKSLKLYTVTSSVTLQRQVLHLLAQLVQLRVNYCLLDSDQIFIGFVIKQFEYIEAGQIRGSETLIPPIFHFLVLLSYERYHSKSIIVMPRIIQLCDGVMASGQKATNHAIPALQPIVHDLFVLRGNSKADQGKELDTQREVVVSMLVRLIHYPEVLEMLTIVLQQCHKESEDRWKKLSRQVVDMVLPMLARQQICLSTPSALNTLHGLFESVTPSSLRPLDMLLKTLFSPPTDLTSPDSFLRWSSMVLSVLRVLISQSKEEVIMARLQELGLSANIFTNNVIYRAKGRAVDLDGDAPFEEVPEEALARFLLQVIGALAEEIAFRSNTSVLQREGCHSLAQQLAHLLLYVTYILKSGLLRKVLSAAMALPEESPTEAYYSVLH
The following text describes a protein:
Function:
Promotes the exchange of Ras-bound GDP by GTP. May also play a role in the activation of rasG.
Sequence:
MKEEEIANLGPQEYFNYLEGINKKIIIELKTVANIDTAKDTDNLQNILIESSLALEHNIRNLLYFVDKCPISYDQIVHYHSHFKEVVKIFFQVCQDLIKAAQALILNSCDYLTTSNFAKCRGEAIKTIKNTMATCSNFEKLYYNPDLQLEDEVDLVHQQQQKEQEQQQKEQEQYEQEQLILKQLKEQELKKQQEQQQQQQQQQQQQQQQQQQQQQKHQEEKEKNDQKEKEEKLKKQLLAEQQKQKQEELERQQQQLQQQQQLLQQQQQLLQQQQQQQRSDPIIIPPITLKTSQSDLLSGGLSPKVNSPGSPNLGKFTESAERVANFDRGTANIILNMNKIKEISLSGDSEQAPEIVTAARIISENIAIISKELRYKTLGTNLSEHFVSVVQVARLAIKNKSDQFYQDQLELAIEKFNDTMRKIIYSVKSISKSSMNLRQFGVDESSLGRSPVVSPEKSISPSFTSSTSERILSHEIKNHNNNNNNYNNSSTNNLQTSFSTPSLSSNHSQQPNQQPLQSPLLINQLQSTSSSSSSSSSNLSNSLNSIQLPQATTTTTTATSPSTSTSTSTSTSPNSSSLSISDQDKQLKRKEKQHQIVIPKDVKDSVANQQQQQQQQQNGTTSPRNNESSVTAATTTTTSTTASITTNVNTIPNFPPNKQLPATPTTGTPSTSTPTPQTPTSTSQNDKQNENNNKENFVDKQKTLGKLFSKFVHKKRTPLPGFDSSNSSSPSNNSNTTNSSSHSSTNSSPMETSPGVESPKITKSPSQNNILVDSLDIGSDNQQQQQDKLTTTTSTTTITINNNNNNNNNNNNNNNNNNNNIQQQQQQQQQIPTTPNKLSNSIAMNSSNRLMTPKKERSFTIGLVSGKHSCVVVETPKSKKLFQHESAKQILSIISMNFPSFEKEFQMQNSEVISNIIEQIGNVIKNYHDEVSESSSSSSSSTTSPNNINTPSDCSPILNSENSKDSHNLSSINNSSYDPVSPALRKMYENGSYDSKEHSRSSIQSKITRKLGTIRKKGPSPFNMLLNSSTGSLSSLYLDQLNGGNGDSSSSSSSSYNLVGGSGISGYDNQNEIDASEHLVSTSSLFTEEAIELVSKCFEASIIVNHSGGTSSEIKALFSSTLDHLESMLQSSVNFGKIDPSSFCMTFLKNIRQHIPTMKSKGGKCDPTLVTAATKLFRHTILSNLDKSIHSLCHSVRVLAIQMTIIVISISAKPWDISSQLQLFASAKSFIDSLVSLLDAVENKIYISTNTNIQDDVEVPTIDDTEDTNIWEEADSPLTFGWISDEGSKTGRYVPKAGTLNKLISALTQDNKHDISRYTKTFLLTYQSFTNPWKLMEKLIQRYNVPLDEKPDVRATTQLRVVSFMQTWIERNFNDFDDQLIGQLKEFRTRLLMDNNNDLAVILGGLIKKKEAERSLSKERSTNHLTFPELMIPDGQKSPTALFLLLNESEIARQLTLIDFNIFSKIQPTELLDQSWNKDSLKFKSPNVIEMINRANKFSFWVSSQILWQEDIEERVKVFEKFILISKYLREMNNFNTLLAIFTGLNTAPILRLKKTFALLSPNSLSIYNSLEKLMNSSGSYKNYRSVSKNPPLLPYLPVILSDLTFMEDGNPDKINNLINFQKRELICRVISEVQQCQQQTKYEFPVVEPIHTLLTELPSSTPSELYQLSLIREPRETNQSNANSSISSGSNFLSNSSNHNIGNNNGFDTLKKYYKSSNNN
The following text describes a protein:
Function:
Catalyzes the methyl esterification of L-isoaspartyl residues in peptides and proteins that result from spontaneous decomposition of normal L-aspartyl and L-asparaginyl residues. It plays a role in the repair and/or degradation of damaged proteins (By similarity).
Subcellular Localization:
Cytoplasm.
Sequence:
MVLVNAISEKDYIKDSRRRKKEEKEFEKLRKLLVEGLEDIVRDKKVLKAMFRVPRHRFVPEYEQRAAYTDRPLEIGHGQTISTPHTVALMCEILELSEGHKVLEIGTGSGYNAAVMAELVGKTGHIYSVERIEPLVNFARKNLEQMGYDNVTVLLENGSMGYPRYAPYDRIAVTCAAPTIPKALLEQLKPGGIMVIPVGDYSQELIRVKKDSNGNIYKKRKGEVIFVPMLGRHGFPRS
The following text describes a protein:
Function:
Controls stomatal patterning.
Subcellular Localization:
Secreted.
Sequence:
MSKHLHTSVLLLLLLLLIDPMTPASASVQPHQGLLMEEDKIRLGSTPPSCHRRCDQCNPCIAVQVPTLPVAGLRRNTDSFRGYPNYKPLGWKCRCQGRFFNP
The following text describes a protein:
Function:
Functions as a two-component phosphorelay mediators between cytokinin sensor histidine kinases and response regulators (B-type ARRs). Plays an important role in propagating cytokinin signal transduction.
Subcellular Localization:
Cytoplasm, cytosol. Nucleus.
Domain:
Histidine-containing phosphotransfer domain (HPt) contains an active histidine that mediates the phosphotransfer.
Sequence:
MQRQVALIKQSLFDQGYLDEQFIELEELQDDANPNFVEEVATLYFKDSARLISNIEQALERGSFDFNRLDNYMHQFKGSSTSIGASKVKTECTMFREYCRVGNAEGFLTIPYLRRVQMFEDFQATEERARNVEKEA
The following text describes a protein:
Function:
Required for recruitment of CENPA to centromeres and normal chromosome segregation during mitosis.
Subcellular Localization:
Chromosome, centromere. Nucleus.
Sequence:
MSSTPPRPAPRSRLRPGALRSRPRPGSSPVSPPEGRRGGVPGEGPPAPAPRLPTENQGSRGGLPETRVFNRSVFPGVTHDVVLEESLLVGIEGALTGSTYHRLSCRSCKLGLGFHLYSSSAALASWRGLFCLAKDKIVCYLLETKCTVEASEMTFPTVDIGENIEKVKFLNDVLPPPCVCSPAAKRLRNGGRAGGGPADFHPGPRMLCVTTTGKNKPSGPEGVAPEKFQPGKNLGGTPVGVGIDGLYISRSFIEPFLDAEHRTRRWGEHDITDPFPAHLGLRSQVLWGQGTRLPICQSRHPSSVVFIERPPCAEHCTEGLGEDNRVGRPRPLPKTV
The following text describes a protein:
Function:
A P subtype restriction enzyme that recognizes the double-stranded sequence 5'-CTGCAG-3' and cleaves after A-5.
Sequence:
MSSNNPTPNLEQLMLEARQLMKDLGLPDKMQGDTPIFVLLVMLDMKPAKSWSEANNQKWGITPLMNKMRELGFKNLAPNTRENIRDDCVGQLVDAELATENPDKPRPKNSPKYCYQINQEVLYLVKKIGSADYPIALNNFLSNYQTIKHKYQAKRQSQRLNVKIAHNFSVSIAPGGQGVLIKSVLQDFCKYFNIDKVLYIDNTVDTARGYSPFIDENLINYLGIDIDKFKNSYDKPDIVLYKSDNKYLIIIEAVKTGGAINVERRDRLLSLFENVDVKLSFVNAFESFKELKRLTKEITRETHAWIMEFPDHMIHFNGDQYLFH
The following text describes a protein:
Function:
Probably a niacin-binding protein that interacts with the energy-coupling factor (ECF) ABC-transporter complex. Unlike classic ABC transporters this ECF transporter provides the energy necessary to transport a number of different substrates. The substrates themselves are bound by transmembrane, not extracytoplasmic soluble proteins. Uptake of niacin into proteosomes containing EcfA1A2T and Niax has been demonstrated. Uptake requires hydrolyzable Mg-ATP and is substrate-specific; NiaX-containing proteosomes did not transport riboflavin.
Subcellular Localization:
Cell membrane; Multi-pass membrane protein.
Sequence:
MRNHDCPTVRFFKARVYKEKETQMTQTKKAKVRNLIIAAMLTALGILIPMMMPVKLIIGPASFTLAAHVPVMAAMFFSPLMTAFVALGTTLGFMISIPVPTIWLRALMHLPVMTVGAYVLKKYPEFVHQKVKIQIFNFILGIFHAGLETLVVYAFYSLGFANIEQGALLNFLLLIALGGLVHSMIDFNLALGLGNVLSKAFPIDIFDKAKNLVNKKKVKAEI
The following text describes a protein:
Function:
K(+) channel that conducts voltage-dependent outward rectifying currents upon membrane depolarization. Voltage sensing is coupled to K(+) electrochemical gradient in an 'ion flux gating' mode where outward but not inward ion flow opens the gate. Homo- and heterodimerizes to form functional channels with distinct regulatory and gating properties.
Subcellular Localization:
Membrane; Multi-pass membrane protein.
Domain:
The pore-forming domains 1 and 2 assemble to form a single pore in which M2 and M4 transmembrane helices line the central cavity and M1 and M3 face the lipid bilayer. The transmembrane helices are bridged by the selectivity filters 1 and 2 carrying a signature sequence TxTTxGYGD that coordinate the permeant ions. Up to four ions can simultaneously occupy the selectivity filter and at least two elementary charges must translocate across the filter to convert it into the open conformation.
Sequence:
MVDRGPLLTSAIIFYLAIGAAIFEVLEEPHWKEAKKNYYTQKLHLLKEFPCLGQEGLDKILEVVSDAAGQGVAITGNQTFNNWNWPNAMIFAATVITTIGYGNVAPKTPAGRLFCVFYGLFGVPLCLTWISALGKFFGGRAKRLGQFLTKRGVSLRKAQITCTVIFIVWGVLVHLVIPPFVFMVTEGWNYIEGLYYSFITISTIGFGDFVAGVNPSANYHALYRYFVELWIYLGLAWLSLFVNWKVSMFVEVHKAIKKRRRRRKESFESSPHSRKALQVKGSTASKDVNIFSFLSKKEETYNDLIKQIGKKAMKTSGGGETGPGPGLGPQGGGLPALPPSLVPLVVYSKNRVPTLEEVSQTLRSKGHVSRSPDEEAVARAPEDSSPAPEVFMNQLDRISEECEPWDAQDYHPLIFQDASITFVNTEAGLSDEETSKSSLEDNLAGEESPQQGAEAKAPLNMGEFPSSSESTFTSTESELSVPYEQLMNEYNKANSPKGT
The following text describes a protein:
Function:
One of the essential components for the initiation of protein synthesis. Protects formylmethionyl-tRNA from spontaneous hydrolysis and promotes its binding to the 30S ribosomal subunits. Also involved in the hydrolysis of GTP during the formation of the 70S ribosomal complex (By similarity).
Subcellular Localization:
Cytoplasm.
Sequence:
MKKNRAFNQVKKTKFDGRIKTSAKHQLRNVKTGVKDGVFIYKGPLTVSEFASKTNIAVANIIKHFFLNGLALTVNSVLTNEQLADACVNFGFDFKMETEVTHENIVANIQFEDSDDLLQPRPPIVTIMGHVDHGKTSLLDTIRKTNVTAKEFGGITQKIGAYQVKNHQNKTITFIDTPGHEAFTLMRARGAKVTDIVVLVVAADDGIKKQTEEAISHAKSANTPIIVFINKMDKPTANPDLVIQQLNKFDLVPEAWGGKTIFVMGSALTGQGINELLDNILLLGEVEGYQANYNAHSSGYAIEVQTSKGLGPIANVIVKRGTLKLGDIVVLGPAYGRVRTMHDENGNSLKQATPSKPVQISGFDIMPVAGEKFIVFDDEKDAKLIANKFKEQQKQKANNLTVNQTLKEQIKNKEIKILNLIFKADSDGSLQAIKQAVENINVAKISLSIIHAAVGQISESDIMLAKASGALLFSLNLGLSQTVKNIASLQGVKLEVHYHIPKLAEEIENILKGQLDPVYEEIEIGKAEVLQLWFHSKIGNIAGTIVKSGKIKRGNLCKLFRDKEIIFEGRIDSLKNEKTPVNLIETGKNCGIVINGCNDIKIGDIIVAYEKQIVKDGKL
The following text describes a protein:
Function:
Auxiliary protein of the large-conductance, voltage and calcium-activated potassium channel (BK alpha). Modulates gating properties by producing a marked shift in the BK channel's voltage dependence of activation in the hyperpolarizing direction, and in the absence of calcium.
Subcellular Localization:
Cell membrane; Single-pass membrane protein.
Sequence:
MDTASAPVGSLQYCCCQLPEMGDTWSQLPWPGPPHPAVLLVSLLLAAGVMHSDAGTSCPVLCTCHNQVVDCSSQRLFSVPPDLPRDTRNLSLAHNRIAAVPPGYLTCYMELRVLDLRNNSLMELPPGLFLHAKRLAHLDLSYNNLSHVPADMFQEAHGLVHIDLSHNPWLRRVHPQAFQGLVQLRDLDLSYGGLAFLSLEALEGLPGLVTLQIGGNPWVCGCTMEPLLKWLRNRIQRCTADSQLAECRGPPEVEGAPLFSLTEESFKACHLTLTLDDYLFIAFVGFVVSIASVATNFLLGITANCCHRWSKASEEEEI
The following text describes a protein:
Function:
The central subunit of the protein translocation channel SecYEG. Consists of two halves formed by TMs 1-5 and 6-10. These two domains form a lateral gate at the front which open onto the bilayer between TMs 2 and 7, and are clamped together by SecE at the back. The channel is closed by both a pore ring composed of hydrophobic SecY resides and a short helix (helix 2A) on the extracellular side of the membrane which forms a plug. The plug probably moves laterally to allow the channel to open. The ring and the pore may move independently.
Subcellular Localization:
Cell membrane; Multi-pass membrane protein. Endomembrane system; Multi-pass membrane protein. Membrane; Multi-pass membrane protein.
Sequence:
MAEGTVTTIIRKMVFKAEPYLPQVPKPKKKIPLSTRLLWCGVALLIYMVMGQTPLFGATTPEFDFLAFARVIFASQQGTLVELGIGPIVTAGLLMQLLRGSDILKFDFKKPEERGVFQTATKMVTYVVIVAESIVYGVAVYGPGVSDPSILYVMVGQLMAASIIIMFLDELIQKGWGLGSGISLFIMAGVAQQILWSLFSPLPAGDGGTIGIIPYIGQSIMAGDLSNIMFRSNQLPSIFGLCLTAGVILILVFTQGMKIEIPIVSTKYRGFSAVYPIKMMYVSNIPVILASALTANAVFIFQMLWANANPRNNNFFMNFIAQFDPTSPSTPIGGLIYYITPPRGLDVAALDPGRAVGYVLFMIGIVIVFGRLWVELGGLSPKSAAQNLLDADVQIPGFRRSNKPVEALLNKYIPSVTIIGSAILGLLAGASDVLGVFGSGIGVLLMVDILINYYTQLVREQVEVVMPRLGALLGRK
The following text describes a protein:
Function:
Catalyzes the methylthiolation of an aspartic acid residue of ribosomal protein uS12.
Subcellular Localization:
Cytoplasm.
Sequence:
MKYHIVTLGCPKNAVDSEGMDGLLSTQGHQAVASAEEADVIIVNTCSFIAAARAETLGVLKELAGRKRPGQRLIAAGCMAQSHPHEVAGVQGVDATLGTQQWTQINALVGQLERPVIPLTPGQPVATIPLTTTTNGQPTSYADWRTTQIRRTHQTPSAYLKISDGCNLRCAFCTIPSFKGDMRSKPVGAVLAEAQELVAGGVREIVLVAQHLTDYGRDLGLKDGLATLLAELCQVTPPETWIRLMYAYPHGISERLITTMASYPQICHYLDMPLQHAHPATLRRMRRPPDTDRTLRIIAELRAAMPDIAIRSTFIVGYPGETTAEFHALLEFLQTAQLDRVGAFRYSREPGTPAAELPDQVRPQVIERRWHELMRLQQTISYTRNQRWVGRTIKVLIEGNGTADDGSALSIGRSFRDAPEIDGQVFVWGNYPAGTMIPVQVTQATAYDLWGEALS
The following text describes a protein:
Function:
Catalyzes the hydrolysis of fructose 1,6-bisphosphate (Fru 1,6-P2) and sedoheptulose 1,7-bisphosphate (Sed 1,7-P2) to fructose 6-phosphate and sedoheptulose 7-phosphate, respectively.
Sequence:
MEKTLGLEIIEVVEQAAIASARLMGKGLRNEADGVAVKAMRDRMNQIYMRGRIVIGEGERDDAPMLYIGEQVGICTQPNAAQMCSIDELLEIDIAVDPCEGTNLVAEGRQGSMAVLAISEKGGLLGAPDLYMKKLAAPPQAKGKVHIDYPATKNLQIIAECLDRAIEDLVVIVMKRDRHKDLISEIRSTGARVRFIDDGDISAALSAGINGTGVHALMGIGAAPEGVISAAALRCLGSHFQGQLIYDPDVVQTGLLKGTKAEIEEQLKAQGVEQPDKVWEAEELASGKNVLFAACGITDGDFIKGVRFFTGSARTETMVISSQSNTVRFVDTVHILDPAHHASLVI
The following text describes a protein:
Function:
Component of the monoterpenoid indole alkaloids (MIAs, e.g. echitovenine, tabersonine, lochnericine, 19-hydroxytabersonine and horhammericine) biosynthetic pathway; MIAs are used in cancer treatment and other medical applications. Acyltransferase catalyzing the conversion of (+)-minovincinine to (+)-echitovenine.
Subcellular Localization:
Cytoplasm. Nucleus.
Sequence:
MDSITMVETETLSKTLIKPSSPTPQSLSHYNLSYNDQNIYPEYIFAGFFYSNPDGHEISTIREQLQNSLSKTLVSYYPFAGKVVKNDYIHCNDDGIEFVDVRIHCRMNDILKPELRSYASELIRPNRSTVGSEDSTALVQLSHFDCGGVAVAFGISHKVADAATILSFIKDWAASTCDLSSSHDVSTPVLVSDSIFPRQDNIICGQFPASPNCVRKRFLFSPEAIERLKSKAIEFGIEKPTRVEVLTAFLCRCATVAGKSAAKNNNCGQSLPFAVIQAVNLRPLLELPKNSVGNLISIYFSTIKENDTVNIEQEFTKLVIGELRKAKDKLKNLSQEKLNYVARMQDFANCLKELDISSFFDMENVDIDAYLFSSWCRFPFYDIDFGLGKPIWVCMFQPHFKNCIILMDYPFGDDYGIEALITLEQEKMPAFENNELLLSFASN