lhallee/plat_data huggingface dataset:
The following text describes a protein:
Function:
Involved in plastid gene expression.
Subcellular Localization:
Plastid, chloroplast.
Sequence:
MNLAIPNPNSHHLSFLIQNSSFIGNRRFADGNRLRFLSGGNRKPCSFSGKIKAKTKDLVLGNPSVSVEKGKYSYDVESLINKLSSLPPRGSIARCLDIFKNKLSLNDFALVFKEFAGRGDWQRSLRLFKYMQRQIWCKPNEHIYTIMISLLGREGLLDKCLEVFDEMPSQGVSRSVFSYTALINAYGRNGRYETSLELLDRMKNEKISPSILTYNTVINACARGGLDWEGLLGLFAEMRHEGIQPDIVTYNTLLSACAIRGLGDEAEMVFRTMNDGGIVPDLTTYSHLVETFGKLRRLEKVCDLLGEMASGGSLPDITSYNVLLEAYAKSGSIKEAMGVFHQMQAAGCTPNANTYSVLLNLFGQSGRYDDVRQLFLEMKSSNTDPDAATYNILIEVFGEGGYFKEVVTLFHDMVEENIEPDMETYEGIIFACGKGGLHEDARKILQYMTANDIVPSSKAYTGVIEAFGQAALYEEALVAFNTMHEVGSNPSIETFHSLLYSFARGGLVKESEAILSRLVDSGIPRNRDTFNAQIEAYKQGGKFEEAVKTYVDMEKSRCDPDERTLEAVLSVYSFARLVDECREQFEEMKASDILPSIMCYCMMLAVYGKTERWDDVNELLEEMLSNRVSNIHQVIGQMIKGDYDDDSNWQIVEYVLDKLNSEGCGLGIRFYNALLDALWWLGQKERAARVLNEATKRGLFPELFRKNKLVWSVDVHRMSEGGMYTALSVWLNDINDMLLKGDLPQLAVVVSVRGQLEKSSAARESPIAKAAFSFLQDHVSSSFSFTGWNGGRIMCQRSQLKQLLSTKEPTSEESENKNLVALANSPIFAAGTRASTSSDTNHSGNPTQRRTRTKKELAGSTA
The following text describes a protein:
Function:
An RNase that has 5'-3' exonuclease and possibly endonuclease activity. Involved in maturation of rRNA and in some organisms also mRNA maturation and/or decay.
Subcellular Localization:
Cytoplasm.
Sequence:
MDTAPADITDNGGLRIIPLGGLGEIGLNMMAYEHGEDIIVADCGLMFPEPQMLGIDLVIPDITYLRERAGRVRGILLTHGHEDHIGALPYVLQELSLPLYGTALTLGFIREKLKEFDLESEVELNVVKPRDVVTLGCFSVEFIRVSHSIVDGCALAIRTPEGVVIHTGDFKIDQTPVDGELTDLATFSRYGDEGVLALLADSTNVEREGYTLSERVVGEAFDEIFPRCEGRIIVAAFSSNIHRVQQAVDAAVRCGRKVLLNGRSMVANVAIARQLGYLRMPEGVLTDLKELQHLPKEQVCMITTGSQGEPMSSLARIAMDDHKQIKLEAGDTVILSSRFIPGNEKTISDLINHLYRRGAEVFHEKVSEVHVSGHASQEELKLMLNLTRPRHFVPVHGEYRHLVKHARLAQRVGVPAERCLVAVNGDVIRFADGRGEIAGAVESGRVYIDGKGIGDVGEVVLKDRKHLSEDGMVVVIIAINQASGEVIYGPDIVSRGFVFEDESQQYLDETKKIVLDLLAGMSIETLGEWGEVKQEVRRILRRFFNKTIERRPVILPVILEM
The following text describes a protein:
Function:
Adaptins are components of the adapter complexes which link clathrin to receptors in coated vesicles. Clathrin-associated protein complexes are believed to interact with the cytoplasmic tails of membrane proteins, leading to their selection and concentration. The AP-1 complex interacts directly with clathrin. Component of the AP-1-related (AP-1R) complex, an adapter protein complex that mediates sorting of cargo SNARE SNC1. In contrast to the APM1-containing AP-1 complex, AP-1R is incapable of sorting CHS3.
Miscellaneous:
MISCELLANEOUS: Present with 4850 molecules/cell in log phase SD medium.
Subcellular Localization:
Cytoplasm. Golgi apparatus membrane; Peripheral membrane protein; Cytoplasmic side. Cytoplasmic vesicle, clathrin-coated vesicle membrane; Peripheral membrane protein; Cytoplasmic side. 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:
MGSSLRSFIKDVRGAKTLADERAIITKQSAKIRTKLRDDHLPHEKRRVNIQKLLYLYILGEKTHFGQVESINLIASDDFVDKRLGYLAATLLLDESEDLLTLLTNMLNNDLHHPNKYAVSLALTSLGFLSSPELARDLYPDVENIIKNSRDPFLLKKALQCAAKLIFKDVSLLEIFNIEDITKILSSHSICTHGVLLGVTKIIQSILLIGLNRKKDEDEDEDGIDYSNDILSPLSLLLRDFFIRLENMNSKNIEPGYDVQGICDPFLQCEIIYTLKLYFQVGELLNSNNVLDYKDNFCDLLTRIATNTDSTKNSGQAILYETVKTIFSLDLNQPLRVLGINILAKFLAGKDNNTKYVSLNTLLKVVPQEPTAVQRHRKFISHCLQDTDVSIRMRALELSFAILDDSNLVELVNELMKFLAKQDEDSKDLIIYTIDHLIDTFDTRVVKDESWKLDVFFNILKLVGSFINYEKINDILIIINNTSQLSDKSEFLRKMLTISLNGTSAEISEENIGWQLVLIWCIGEYGDLVLNEGNKNGADIINESSITDYLLTLQELYTATNLKIINYILTAALKLSVRFHDAKNIEKLRQLILSYTDSTDLSLQMKSNQYEIFFNQSISVKKIILETMPKFEKITEEQDNGKALSKNLISNEPVDLLSDLLGEDSKAESKASTGDNVKPIDILEEIFGEKNDIAQVPKNANKEESINHSSAVEANSGVTLPLDANKIYDSSSLNVYASLLSANSGLAHLDLYFQAKSLISDLKTFCAVPKAQKLTLGQLYPSSTINASQICKQSLKISGSGKLKLRVKLDFHLNGSSSITNEQFDHKFDETL
The following text describes a protein:
Function:
ATP-dependent low-affinity peptide transporter which translocates a broad spectrum of peptides from the cytosol to the lysosomal lumen for degradation. Displays a broad peptide length specificity from 6-mer up to at least 59-mer peptides with an optimum of 23-mers. Binds and transports smaller and larger peptides with the same affinity. Favors positively charged, aromatic or hydrophobic residues in the N- and C-terminal positions whereas negatively charged residues as well as asparagine and methionine are not favored.
Subcellular Localization:
Lysosome membrane; Multi-pass membrane protein.
Sequence:
MQLWKAVVVTLAFMSLDIGMTTAIYVLSHVDRSLLEDIRHFNIFDSVLDLWAACLYRSCLLLGATIGVAKNSALGPRRLRASWTVIALVCLFAGIYTMVKLLLFSEVRKPVRDPWFWALFVWTYISLAASFLLWWLLSTVQPDAKALEPGTGAEAEAEGFPAEDQSPPEQASGATLQKLLSYTKPDVAFLMAASFFLIVAALGETFLPYYTGRAIDGIIIQKSMEQFSTAVIVMCLLALGSSFAAGIRGGIFTLVFARLNIRLRNRLFRSLVSQEMSFFDENRTGDLISRLTSDTTMVSDLVSQNINIFLRNTVKVTGVVAFMFSLSWQLSLVTFMGFPIIMMVSDIYGRYYKRLSKDVQSALARASNTAEETISAMKTVRSFANEEEEAEVYSRKLQQVYKLNRKEAAAYTYYVWGSGLTLLVVQVSILYYGGHLIISGQMTSGNLISFIIYEFVLGDCMESMGSVYSGLMQGVGAAEKVFEFIDRQPTMVHDGKLAPDHLVGRVDFENVTFTYRTRPHTQVLQNVSFSLSPGKVTALVGPSGSGKSSCVNILENFYPLEGGRVLLDGQPIGAYDHKYLHRAISLVSQEPVLFARSITDNISYGLPSVPFETVVEAAQKANAHGFIMELQDGYNTETGEKGAQLSGGQKQRVALARALVRNPPLLILDEATSALDAESEYLVSGQVAGWCRNREQLQWSSPPSTRQTGAGKGSPRPPASGTGVSQSRWGAGERSPGPGLQLCERVVQERGPGAPPCHAEHEQVSSPL
The following text describes a protein:
Function:
Component of the COP9 signalosome (CSN) complex that acts as an regulator of the ubiquitin (Ubl) conjugation pathway by mediating the deneddylation of the cullin subunit of SCF-type E3 ubiquitin-protein ligase complexes (By similarity). The CSN complex seems to link protein degradation to sexual development. May be required for sporulation only at elevated temperatures.
Subcellular Localization:
Cytoplasm. Nucleus.
Sequence:
MDQVHHRALDALQSFIALTDSSSATSPRYIASIITNATSSPHTYVFAELLERPAVQALRSPDTPAEFQSYLTLLEIFAWGTWQDYQQTPNLPPLSEEQARKLRLLTLLSLASTIKPLTYEALMTSLSLSAPSELESLVTTAIYSSLITGRLSPATNPPTVNVTSVAPLRDVKPSSLPTMISTLTAWEARCGSVISDIETEIAKIRADSAQRRQKEHARAVAIEKTLEKWNAEGGEQLQGGNPGQGQGQGQGGLGKNAGWKPRDLSTAMFERGFFGGGSNKREFDDDGYFDGGSSDFDQHGSGMDIDEGAGARASGARHSKRFLGKKS
The following text describes a protein:
Function:
Non-functional DHOase.
Sequence:
METQCRPQVRCLDPIQGKETRVTVIVRGRAIVAVEDDSYPIPADAAVIPGENLLLAPSLADLYSYSGEPGYEDRETLSQLVKTAIAGGFGDVAILPNTDPPLDQPQTLQWLKQRLNQIEGVNAHHQPPGDPQAENRPDSAPVQCHWWGSVTQGNQGKQLTEWGELDQAGVIGFSDGGAIQDWRLLQRALEYGAIAGKPLALVPLNLSLRGNGVMREGPLAIQLGLPPDPVMSEAAVIASLLELLPHYGTPVHFMRISTARGVELIVQAKSQGLNCTASVNWHHLLLSNEAIAHGLPPHTPHYDPNLRFDPPLGNEGDRLALIEGVKSGVIDAIAVDHQAFTYEEKTQTFAETPPGAIGYELVLPCLWQGLVEKNLITPMALWRALSTNPRRCLGLPEVSNSRILFDPDQAWTLKRGTLQTSAYNSPWWNHSLKGRVVAWES
The following text describes a protein:
Function:
Reduces glyoxal and methylglyoxal (2-oxopropanal). Is not involved in the vitamin B6 biosynthesis.
Sequence:
MPTSLKDTVKLHNGVEMPWFGLGVFKVENGNEATESVKAAIKNGYRSIDTAAIYKNEEGVGIGIKESGVAREELFITSKVWNEDQGYETTLAAFEKSLERLQLDYLDLYLIHWPGKDKYKDTWRALEKLYKDGKIRAIGVSNFQVHHLEELLKDAEIKPMVNQVEFHPRLTQKELRDYCKGQGIQLEAWSPLMQGQLLDNEVLTQIAEKHNKSVAQVILRWDLQHGVVTIPKSIKEHRIIENADIFDFELSQEDMDKIDALNKDERVGPNPDELLF
The following text describes a protein:
Function:
Transcriptional activator that specifically binds 5'-GATA-3' or 5'-GAT-3' motifs within gene promoters. May be involved in the regulation of some light-responsive genes.
Subcellular Localization:
Nucleus.
Sequence:
MSNQPPHASLQDDLPDCDGDDPLALAIRLFPAHTTGAGLSPAALGIGRVAEPPRREQEPLANSTYGVRGAGPDPWGLRLSRSVLGGLDGFDVDTFFADDALDGGGEATEGDSPPAHVTAAARGSLANDDASPLPAAMPAVALEAYDACSAPVPAACGGAPPVLVANNSTPPASCLGARCTLHFMPDGGNGGNNRSAALPVALAPPSGSTGGAVRRRRPVPRPRNREVQRTCSHCQSSKTPQWREGPDGRRTLCNACGLRYKSHRLVPEYRTAESMTPRDLHPNAGLSSGPSSRPSSSSTTTPSQSQIDFPFHALPAVAPPPAMPDGGNGGNNRSSALPVALAPPSGSTGGAVRRRRPVPRPRNRQVQRTCSHCQSSETPQWREGPDGRRTLCNACGLRYRSHRLVPEYRPTTSPSFQIGQHSNRHRRIMQIREQNGTAGS
The following text describes a protein:
Function:
The Set1 complex specifically methylates 'Lys-4' of histone H3.
Subcellular Localization:
Nucleus.
Sequence:
MDSTAQQFPLNHDLQVQKDQKGVVEEDEEQIHKRIRNYESHSGFSEYCTLFGHEKSVTCVSVSPNKRWIATSSSDGTIKIWSALTFRLECTLFGHYRGISQVKWATGSKYLASASDDKTIRIWDFEKRCSVRCLKGHTNYVSSIDFNPLGTLLVSGSWDETVRIWNLQDGTCLRMLPAHSEPIISVSISADGTLCATASYDGMARIWDVLSGQCLKTLVEPINVPLSNLQFTENRKYLLVSNLNSQIRLWDYRRNRVVRIFDSHVNTRYSMSWDCYSSKNIPKNTEALPNNDSSYPDDAESFMHDAYLLIPSEDGTIQITDPSTKIIIDDSIRHSDDPETSLLNVTSLGPFIITSGTDPYVRVWAPSLLLSKHEKDGFSP
The following text describes a protein:
Function:
High-affinity urea-proton symporter involved in the active transport of urea across the plasma membrane into root cells. May play an important role in urea uptake by plant cells at low external urea concentrations.
Subcellular Localization:
Membrane; Multi-pass membrane protein.
Sequence:
MASSSKCPPLGFAGEYYTTNSGSEAGCVRHSSFFNDETVLNQAVGYSVILGFGAFFAVFTSFLVWLEKRYVGSSHTSEWFNTAGRNVKTGLIASVIVSQWTWAATILQSSNVAWEYGVSGPFWYASGATIQVLLFGIIAIEIKRKAPYAHTVCEILRARWGTAAHIVFLGFCFLTNIIVTAMLLLGGSAVVNALTGVNIYAASFLIPLGVIVYTLAGGLKATFLASYIHSVIVHLVLVIFVFLVYTTSSKLGSPRVVYDHLLEVASKSRICQDPFSHEGQACGPVNGNHNGSYLTMLSSGGLVFGIINIIGNFGTVFVDNGYWVSAIAARPSSTHKGYLLGGLVWFAVPFSLATSLGLGALALDLPLTESEASHGLVPPATAIALMGKGGSILLLTMLFMAVTSAGSSELIAVSSLCTYDIYRTYVNPNATGKQILKVSRAVVLGFGCFMGVLAVILNKAGVSLGWMYLAMGVLIGSAVLPIAFMLLWRKANAKGAIIGALLGCFSGIITWLSVTKVEYGRVNLDTTGRNAPMLAGNLVSILFGGLVHALCSFIWPQNYDWETTKQITVVEKDKGDLPAEEFKEEKLVKAKAWIVKWGVGFTIVIVILWPLLSLPAGEFSIGYFTFWAVVAITWGTVGSAVIIVLPLVESWQTLQMVFLGMFTNDRLMEKLEQMNTKMQAIIMALPEAERLYLLERDNAKKKDILEEKSNLV
The following text describes a protein:
Function:
Probable essential component of SCF (SKP1-CUL1-F-box protein) E3 ubiquitin-protein ligase complexes, which mediate the ubiquitination and subsequent proteasomal degradation of target proteins. Regulates cell proliferation during embryonic and larval development.
Sequence:
MADQQAGPAPAAAQPAQAPTLPAPKPEPSFYFFLESFDKETVKISDLAVPQLVTINNLVSGLGYDAEKAAKNVMPIDNITGVTLKRVVAWSSSWRGVPGGEERRLPTPDQHSRVGHELFEGVGGQGAGGVDAAANYLESKQLLRYCCKKIAIMAQGKTPEELRVLFEIPTDEEDAIAEQELKERLEREAKEEAERQLVEGPSTSDGKR
The following text describes a protein:
Function:
Negative regulator of epidermal growth factor receptor (EGFR) signaling.
Sequence:
MCLTPVVIVRRHQRRLSDSSLKGFPMELHSHEDAACQPSPSKHSCPDLVSEPSPGGPAVVLGSGAEDDGPREGPANEAPSIDGSTDTLVNEIGQQSSSVGADDGVLQKTMPEPAELSPAQLDQQLSNTASTSTTDLRSSAGAVLGGGYSELPLEEVAPGKCVVCLSRKNGHENLLAATRSSLARSAAAATTNGGRFSHYSTPMHSRTPSSGFPATPCDDRLLLDPMASRTQSSQASCQQQFDVDGLNTPVDALQQRIHQMVLDHEAKIENLENELRRARFALDQRSLHHNGKEASEALEDAVSLFWNSPCLQHLCSGAMEMELGLDCACSGEPPWGGCQDGSSSSELSWEQVDEREARATLWVPDHAASHCTACGAEFWIGRRKHHCRNCGNVFCSQCASQMHPVPHEQLYQPVRVCSSCFEALRSRPCRPSALLAAPGPHSERILAKTSPAVTAASN
The following text describes a protein:
Function:
Antiviral protein which inhibits the replication of viruses by recruiting the cellular RNA degradation machineries to degrade the viral mRNAs. Binds to a ZAP-responsive element (ZRE) present in the target viral mRNA, recruits cellular poly(A)-specific ribonuclease PARN to remove the poly(A) tail, and the 3'-5' exoribonuclease complex exosome to degrade the RNA body from the 3'-end. It also recruits the decapping complex DCP1-DCP2 through RNA helicase p72 (DDX17) to remove the cap structure of the viral mRNA to initiate its degradation from the 5'-end. Its target viruses belong to families which include retroviridae: human immunodeficiency virus type 1 (HIV-1) and moloney and murine leukemia virus (MoMLV), filoviridae: ebola virus (EBOV) and marburg virus (MARV), togaviridae: sindbis virus (SINV) and Ross river virus (RRV). Specifically targets the multiply spliced but not unspliced or singly spliced HIV-1 mRNAs for degradation. Isoform 1 is a more potent viral inhibitor than isoform 2. Isoform 2 acts as a positive regulator of RIG-I signaling resulting in activation of the downstream effector IRF3 leading to the expression of type I IFNs and IFN stimulated genes (ISGs).
Subcellular Localization:
Cytoplasm. Nucleus. Note=Localizes in the cytoplasm at steady state, but shuttles between nucleus and cytoplasm in a XPO1-dependent manner.
Domain:
The N-terminal domain is sufficient to bind to viral RNAs and promote their degradation. The second and fourth zinc fingers are involved in binding to specific viral RNAs. Contains a divergent PARP homology ADP-ribosyltransferase domain which lacks the structural requirements for NAD[+] binding. It is therefore inactive.
Sequence:
MTDPEVFCFITKILCAHGGRMTLEELLGEISLPEAQLYELLKAAGPDRFVLLETGDQAGITRSVVATTRARVCRRKYCQRPCDSLHLCKLNLLGRCHYAQSQRNLCKYSHDVLSEQNFQVLKNHELSGLNQEELAVLLVQSDPFFMPEICKSYKGEGRKQICGQPQPCERLHICEHFTRGNCSYLNCLRSHNLMDRKVLAIMREHGLSSDVVQNIQDICNNKHTRRNPPSMRAPHPHRRGGAHRDRSKSRDRFHHNSLEVLSTVSPLGSGPPSPDVTGCKDPLEDVSADVTQKFKYLGTQDRAQLSSVSSKAAGVRGPSQMRASQEFLEDGDPDGLFSRNRSDSSTSRTSAAGFPLVAAQRNEAGAMKMGMPSGHHVEVKGKNEDIDRVPFLNSYIDGVTMEEATVSGILGKRATDNGLEEMILSSNHQKSVAKTQDPQTAGRITDSGQDTAFLHSKYEENPAWPGTSTHNGPNGFSQIMDETPNVSKSSPTGFGIKSAVTGGKEAVYSGVQSLRSHVLAMPGETTTPVQGSNRLPPSPLSSSTSHRVAASGSPGKSSTHASVSPASEPSRMMMMMSDPAEYSLCYIVNPVSPRMDDHGLKEICLDHLYRGCQQVNCNKNHFHLPYRWQLFILPTWMDFQDMEYIERAYCDPQIEIIVIEKHRINFKKMTCDSYPIRRLSTPSFVEKTLNSVFTTKWLWYWRNELNEYTQYGHESPSHTSSEINSAYLESFFHSCPRGVLQFHAGSQNYELSFQGMIQTNIASKTQRHVVRRPVFVSSKDVEQKRRGPDHQPVMPQADALTLFSSPQRNASTVSSNEYEFIELNNQDEEYAKISEQFKASMKQFKIVTIKRIWNQKLWDTFERKKQKMKNKTEMFLFHAVGRIHMDYICKNNFEWILHGNREIRYGKGLCWRRENCDSSHAHGFLEMPLASLGRTASLDSSGLQRK
The following text describes a protein:
Function:
Pre-ribosomal factor involved in 60S ribosomal protein subunit export from the nucleus.
Subcellular Localization:
Nucleus, nucleolus. Nucleus. Cytoplasm. Note=Shuttles between the nucleus and the cytoplasm.
Sequence:
MAKKQSIRSRNFRRSDPAYDLDSSTAIENETKLSVKEKVAKEIANIALRSGGSESNGISKKKKNKKQTSKKAKDKLAAALKAQAREERLDTKISKSLQKQEKLKARKQGDE
The following text describes a protein:
Function:
Histone deubiquitinating enzyme component of the transcription coactivator SAGA complex. SAGA acts as a general cofactor required for essentially all RNA polymerase II transcription. At the promoters, SAGA is required for transcription pre-initiation complex (PIC) recruitment. It influences RNA polymerase II transcriptional activity through different activities such as TBP interaction (via core/TAF module) and promoter selectivity, interaction with transcription activators (via Tra1/SPT module), and chromatin modification through histone acetylation (via HAT module) and deubiquitination (via DUB module). SAGA preferentially acetylates histones H3 (to form H3K9ac, H3K14ac, H3K18ac and H3K23ac) and H2B and deubiquitinates histone H2B. SAGA interacts with DNA via upstream activating sequences (UASs). Also identified in a modified version of SAGA named SALSA or SLIK. The cleavage of SPT7 and the absence of the SPT8 subunit in SLIK neither drive any major conformational differences in its structure compared with SAGA, nor significantly affect HAT, DUB, or DNA-binding activities. Within the DUB module, the correctly positioned zinc finger domains of SGF11 and SGF73 are both required to fully activate the ubiquitin hydrolase UBP8. The DUB module is also linked to the splicing efficiency of many transcripts.
Miscellaneous:
MISCELLANEOUS: Present with 1030 molecules/cell in log phase SD medium.
Subcellular Localization:
Nucleus.
Domain:
The UBP-type zinc finger domain is required for the interaction with the SAGA complex; The USP domain is the catalytic domain, but it is only active when in complex with the other DUB module subunits.
Sequence:
MSICPHIQQVFQNEKSKDGVLKTCNAARYILNHSVPKEKFLNTMKCGTCHEINSGATFMCLQCGFCGCWNHSHFLSHSKQIGHIFGINSNNGLLFCFKCEDYIGNIDLINDAILAKYWDDVCTKTMVPSMERRDGLSGLINMGSTCFMSSILQCLIHNPYFIRHSMSQIHSNNCKVRSPDKCFSCALDKIVHELYGALNTKQASSSSTSTNRQTGFIYLLTCAWKINQNLAGYSQQDAHEFWQFIINQIHQSYVLDLPNAKEVSRANNKQCECIVHTVFEGSLESSIVCPGCQNNSKTTIDPFLDLSLDIKDKKKLYECLDSFHKKEQLKDFNYHCGECNSTQDAIKQLGIHKLPSVLVLQLKRFEHLLNGSNRKLDDFIEFPTYLNMKNYCSTKEKDKHSENGKVPDIIYELIGIVSHKGTVNEGHYIAFCKISGGQWFKFNDSMVSSISQEEVLKEQAYLLFYTIRQVN
The following text describes a protein:
Function:
Acts as a component of the outer kinetochore KNL1 complex that facilitates microtubule-kinetochore interactions and the spindle assembly checkpoint. Kinetochores, consisting of a centromere-associated inner segment and a microtubule-contacting outer segment, play a crucial role in chromosome segregation by mediating the physical connection between centromeric DNA and spindle microtubules. The outer kinetochore is made up of the ten-subunit KMN network, comprising the MIS12, NDC80 and KNL1 complexes, and auxiliary microtubule-associated components; together they connect the outer kinetochore with the inner kinetochore, bind microtubules, and mediate interactions with mitotic checkpoint proteins that delay anaphase until chromosomes are bioriented on the spindle. The KNL1 complex is required for kinetochore binding by the kMAPs (kinetochore-bound microtubule-associated proteins) BIM1, BIK1 and SLK19, and motors CIN8 and KAR3. Required during meiosis.
Miscellaneous:
MISCELLANEOUS: Present with 377 molecules/cell in log phase SD medium.
Subcellular Localization:
Nucleus. Chromosome, centromere, kinetochore.
Sequence:
MDTGSASIKDYETVLTDIEDSIAVSSEEVLNNQELRLKNTLHEITSSILAINEENKFVNPLRNDESLDVEGKEVFVNPKILSAKIKEFNKLMELLKLTYLEQETLDYFFRFTLSSTKPLQLDSEKDPQFVKLNERVNDLKEEISNVQESKIEQIKAEIQETGHNFAERQDLINELYLEATGDIENCWDSLNELKNLTNKEDKNMMGEKDTILNSSDSDDFVEETYTNWQKLLFLQKQNQRLTKELKEMHEVKNQIIRKGEQSKKEDSGHLMANESELCQSINLLTKFWEKHFLLKGSKTTILNFEIFTQLGKVQFEIKDMQYIIAISLSDLKRPMIKDITILQKAGGNIVTDIEASSKFNNKYRNNTKVQIFEVMDDIISELTNE
The following text describes a protein:
Function:
Essential for proper morphogenesis of the vacuole. May exist as structural reinforcement on the surface of the vacuolar membrane and be required for maintenance against rupture by osmotic pressure.
Subcellular Localization:
Vacuole.
Sequence:
MHQGAPHQRPATTKIHKMDISIPTYTVSSPTSFTVQVDLEGGGDVRHRGEENKYTLTKRYSDFVALVSQLEDEVGRTVEVALPPKSWFKSKNVEFLDDRRRGLEVFLRRLVKIPHFYSSAALLEFLQLQKVGPCKGGAGGSGVTAPVSWDDQVASITQMLKTARSNVVAGTAERYENQKLVLTAQTRFAQLEKSLNEPAGEKTSDNEHRRRRTLLMDLQKLLKQVVAQLSAQAGSETSSGTSTPLTGTVRSSQRGSGRKGRVLGETDKTRQLNNSGLVQLQKDSFQEQDESLRQMLGTIQRQKELGEAIRQEVDLQNEQLDELNGEVELTGARLKNAQRQVGKFT
The following text describes a protein:
Function:
Acts as an activator of both RNA and protein methyltransferases.
Subcellular Localization:
Nucleus, nucleoplasm. Cytoplasm, perinuclear region.
Sequence:
MKILTHNMMACTKKQCMGKGFPLKVESTEQIVLEQEFNYEFTKNIYPKLDWLGIAEISIKFNIPIQLDTTKHSLEDEEFLKTLHNLLCNLKVITGSLTCPNCQRVYPIDKGIPNMLLREDEIYQEIKE
The following text describes a protein:
Function:
Catalyzes the degradation of hydrogen peroxide (H(2)O(2)) generated by peroxisomal oxidases to water and oxygen, thereby protecting cells from the toxic effects of hydrogen peroxide.
Subcellular Localization:
Peroxisome matrix.
Sequence:
MAESREKSCDQMKIWKESRGSQKAETLTTGAGIPLGDKLNAQTAGPRGPLLVQDVVFTDEMAHFDRERIPERVVHAKGAGAFGYFEVTHDITKYTKAKVFEHVGKRTPTAVRFSTVAGESGSADTVRDPRGFAVKFYTEEGNWDLTGNNIPIFFIRDPMLFPSFIHSQKRNPQTHLKDPDMVWDFWSLRPESLHQVTFLFSDRGIPDGHRHMNGYGSHTFKLVNAAGEAVYCKFHFKTDQGIKNLSPEQAELLAATDPDYSIKDLYNAIANGNYPSWTFYIQVMTFEQAESFPFNPFDLTKVWSHKDYPLIPVGKLVLNRNPVNYFSEVEQIAFDPSNMPPGVEPSPDKMLQGRLFSYPDTHRHRLGANYLQLPVNCPYRTRVANYQRDGPMCMFDNQGGAPNYYPNSFSAPEAQPRFLESKFKVSIDVARYNSSDEDNVTQVRTFYTQVLSEEERQRLCQNLAGHLRGAQLFIQKRMLQNLMAVHPDYGNRVRALLDKYNAEADKNVIRVYSPTSQSLAASKMSNL
The following text describes a protein:
Function:
Catalyzes the specific phosphorylation of the 3-hydroxyl group of shikimic acid using ATP as a cosubstrate.
Subcellular Localization:
Cytoplasm.
Sequence:
MAQDLIKEQLQGVNLFLIGMMGSGKSTVGPLLAEQLGYRFFDADVLIERVAGKAIADIFAEDGEDTFRDLETEVLGHLAAQTRSVIATGGGVVLRRQNWSYLHHGLVIWLDGSLELLLARLQGDEARPLLQVENLEERLGNLLAQRQPLYAQADLRFPLQADQDPLAIAGELLATIPGLLKPQCSAEQN
The following text describes a protein:
Function:
Inner nuclear membrane protein. Involved in the attachment of membrane vesicles to chromatin during nuclear assembly, and is probably required for centrosome maturation and cell cycle progression during mitosis. Essential for differentiation of certain tissues and the maintenance of progenitor cell populations. Required for the differentiation and maintenance of male and female germline stem cells (GSCs), as well as the maintenance of somatic cells in the GSC niche. This role is likely to be independent of the BMP (Dpp) pathway that negatively regulates bam transcription during GSC differentiation. During development, plays essential and redundant functions with the other LEM domain proteins; bocks and MAN1. Also has a redundant but important role with bocks during larval development.
Subcellular Localization:
Nucleus inner membrane; Peripheral membrane protein; Nucleoplasmic side. Nucleus, nucleoplasm. Cytoplasm. Chromosome. Cytoplasm, cytoskeleton, spindle pole. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome. Note=Component of the spindle envelope during early mitotic cycles. Following nuclear envelope breakdown, becomes dispersed in the cytoplasm and concentrated at the spindle poles. At anaphase (when the nuclear envelope begins to reassemble), locates to the chromosomes accumulating first in areas adjacent to centrosomes and at the peripheral sites of the chromosomes. At telophase, expressed as a continuous rim around the chromatin and increased expression in the midspindle area. During cytokinesis, locates to the nuclear periphery with some remaining in the cytoplasm and at the mid-body. At stage 4 of egg development, expression in the oocyte nuclear envelope is higher than in the nurse nuclear envelope. Expression in oocyte cytoplasm increases after stages 6 to 7 of egg development.
Sequence:
MADVDDFDSLSNAELRAKMLAQGLPNIPVTDSSRKVLVKRLRASIGGQASPAASPKKTNRRETLAPAPGAPSAPAAASTPVDKLDGNKVAPATKARRTITAAEAKEPVRRLPEEAIRRRPDEADRLRSEEPVAARKPTTAPAAQPVQTRRTSTSSGSERKVVEPLRKPETIVEQPASSKRADREENYLKVNSLIVLESDEEEDEQLVQAADLVEQEHAARQKTTKLASSGTTTYEYKSKVVEPPRRQVYEATAAPVLPPSVPSARAQTTSSTRSYDYASNPAPGRYSSFVRTAAQGYVTAEAPPVASYSSSYKRTYANELSDDTDSKEDQYESTFARNLARLRAERIGDRISPYSRRTLASGNAGSGSLGYEPRARRSLRPNDNSVSEAFNRWLNSLEQKYHIKSKLFIVLLVLLLIGVYYIFY
The following text describes a protein:
Function:
Potential calcium sensor.
Sequence:
MDRKIRLLGLSINLDQSMGFIGSFLTKAKSTTKIIRWRRNPSPRIVLVTKTDEITDHRFLQSSSSNGSRRNIRLPRTVLEHFLFRLGVGESESSQVAEVVAEAGCDEEGKINLDDFLRPEISEEEELKQAFGMYDVNGDGVISPEELLRVLLTLEDNSCSINDCRRMIAVVDSDGDGFICFSDFKRMMSVG
The following text describes a protein:
Function:
Catalyzes the NADPH-dependent reduction of glyoxylate and hydroxypyruvate into glycolate and glycerate, respectively. Inactive towards 2-oxo-D-gluconate, 2-oxoglutarate, oxaloacetate and pyruvate. Only D- and L-glycerate are involved in the oxidative activity with NADP. Activity with NAD is very low.
Subcellular Localization:
Cytoplasm.
Sequence:
MDIIFYHPTFDTQWWIEALRKAIPQARVRAWKSGDNDSADYALVWHPPVEMLAGRDLKAVFALGAGVDSILSKLQAHPEMLNPSVPLFRLEDTGMGEQMQEYAVSQVLHWFRRFDDYRIQQNSSHWQPLPEYHREDFTIGILGAGVLGSKVAQSLQTWRFPLRCWSRTRKSWPGVQSFAGREELSAFLSQCRVLINLLPNTPETVGIINQQLLEKLPDGAYLLNLARGVHVVEDDLLAALDSGKVKGAMLDVFNREPLPPESPLWQHPRVTITPHVAAITRPAEAVEYISRTIAQLEKGERVCGQVDRARGY
The following text describes a protein:
Function:
Promotes loss of intracellular domain (ICD) of Notch1 in embryos. By down-regulating ICD levels, could function as a negative feedback regulator of Notch signaling that attenuates ICD-mediated transcription. Involved in angiogenesis. May be involved in somitogenesis (By similarity).
Sequence:
MSQAEMSTCSMPHTQRVFQEAVRNGNTKELHSLLQNMTNCEFNVNSFGPEGQTALHQSVIDGNLELVKLLVKFGADIRLANRDGWSALHIAAYGGHQDIVLYLITKAKYSSSSR
The following text describes a protein:
Function:
Catalyzes the conversion of butyryl-CoA through butyryl phosphate to butyrate.
Subcellular Localization:
Cytoplasm.
Sequence:
MYRLLIINPGSTSTKIGIYDDEKEIFEKTLRHSAEEIEKYNTIFDQFQFRKNVILDALKEANIEVSSLNAVVGRGGLLKPIVSGTYAVNQKMLEDLKVGVQGQHASNLGGIIANEIAKEINVPAYIVDPVVVDELDEVSRISGMADIPRKSIFHALNQKAVARRYAKEVGKKYEDLNLIVVHMGGGTSVGTHKDGRVIEVNNTLDGEGPFSPERSGGVPIGDLVRLCFSNKYTYEEVMKKINGKGGVVSYLNTIDFKAVVDKALEGDKKCALIYEAFTFQVAKEIGKCSTVLKGNVDAIILTGGIAYNEHVCNAIEDRVKFIAPVVRYGGEDELLALAEGGLRVLRGEEKAKEYK
The following text describes a protein:
Function:
Suggested to be part of an ABC transporter complex YydIJ involved in export of the modified peptide YydF (Probable). Responsible for energy coupling to the transport system (By similarity).
Sequence:
MNIANYTLKVKGKTLLQDTDLHFSSGKINHVVGKNGVGKSQLAKDFLLNNSKRIGRDIRQNVSLISSSSNIPNDVSKDFLLHFLSKKFDAKMIDKIAYLLNLDNIDGKVLIKNLSDGQKQKLKLLSFLLEDKNIIVLDEITNSLDKKTVIEIHGFLNKYIQENPEKIIINITHDLSDLKAIEGDYYIFNHQEIQQYHSVDKLIEVYINE