lhallee/plat_data huggingface dataset:
The following text describes a protein:
Function:
Tyrosine phosphatase enzyme that plays important roles in controlling immune signaling pathways and fundamental physiological processes such as hematopoiesis. Dephosphorylates and negatively regulate several receptor tyrosine kinases (RTKs) such as EGFR, PDGFR and FGFR, thereby modulating their signaling activities. When recruited to immunoreceptor tyrosine-based inhibitory motif (ITIM)-containing receptors such as immunoglobulin-like transcript 2/LILRB1, programmed cell death protein 1/PDCD1, CD3D, CD22, CLEC12A and other receptors involved in immune regulation, initiates their dephosphorylation and subsequently inhibits downstream signaling events. Modulates the signaling of several cytokine receptors including IL-4 receptor. Additionally, targets multiple cytoplasmic signaling molecules including STING1, LCK or STAT1 among others involved in diverse cellular processes including modulation of T-cell activation or cGAS-STING signaling. Within the nucleus, negatively regulates the activity of some transcription factors such as NFAT5 via direct dephosphorylation. Also acts as a key transcriptional regulator of hepatic gluconeogenesis by controlling recruitment of RNA polymerase II to the PCK1 promoter together with STAT5A.
Subcellular Localization:
Cytoplasm. Nucleus. Note=In neurons, translocates into the nucleus after treatment with angiotensin II. Shuttles between the cytoplasm and nucleus via its association with PDPK1 (By similarity).
Domain:
The N-terminal SH2 domain functions as an auto-inhibitory domain, blocking the catalytic domain in the ligand-free close conformation.
Sequence:
MVRWFHRDLSGPDAETLLKGRGVPGSFLARPSRKNQGDFSLSVRVDDQVTHIRIQNSGDFYDLYGGEKFATLTELVEYYTQQQGILQDRDGTIIHLKYPLNCSDPTSERWYHGHISGGQAESLLQAKGEPWTFLVRESLSQPGDFVLSVLNDQPKAGPGSPLRVTHIKVMCEGGRYTVGGSETFDSLTDLVEHFKKTGIEEASGAFVYLRQPYYATRVNAADIENRVLELNKKQESEDTAKAGFWEEFESLQKQEVKNLHQRLEGQRPENKSKNRYKNILPFDHSRVILQGRDSNIPGSDYINANYVKNQLLGPDENSKTYIASQGCLDATVNDFWQMAWQENTRVIVMTTREVEKGRNKCVPYWPEVGTQRVYGLYSVTNSREHDTAEYKLRTLQISPLDNGDLVREIWHYQYLSWPDHGVPSEPGGVLSFLDQINQRQESLPHAGPIIVHCSAGIGRTGTIIVIDMLMESISTKGLDCDIDIQKTIQMVRAQRSGMVQTEAQYKFIYVAIAQFIETTKKKLEIIQSQKGQESEYGNITYPPAVRSAHAKASRTSSKHKEEVYENVHSKSKKEEKVKKQRSADKEKNKGSLKRK
The following text describes a protein:
Function:
Component of the replication protein A complex (RPA) required for DNA recombination, repair and replication. The activity of RPA is mediated by single-stranded DNA binding and protein interactions. Probably involved in repair of double-strand DNA breaks (DSBs) induced by genotoxic stresses.
Subcellular Localization:
Nucleus.
Sequence:
MAQPSLTPNAIVALLGGDLELRPIVQVLDVKQIGSNQNVQERYRLVLSDGTAVQQAMLATQLNEVVKNGTLMKSSIVKLQEYICNTVKDRKIVIVLNLDVLVSNAEMSDQPPGAVVDPPGPSGNQTASAVSSYGGRPAEVSSFGGRPTEVSSFGGRQAEATSFGGRPTETNSLGGRAAEGSSIGGRTPEPGSFGGQATPAVSPYGRPAEPGSFGGQATPAVSPYGRPAEARRETVAYGGRPAESIGSYAPNPPYGPPPTYTNRGPIARNEGPPGLVPIAALNPYHGRWTIKARITSKSDLRRFNNARGDGRVFSFDLLDAEGGEIRVTCFNNVADEFYERAQVGRLYMVSKGSLRAAQKQFNHLKNDWEIMFEKDSVLDPCPEDSSVPQQVFDFKQVSEIENLPNNAMVDAIGVVVGVNQTTTIMRKNGTETQRRTLQLRDRSGKSVEITMWGNFCTQEGQHLQELCDSGQSPILAIKAGRVSDFSGKSLGTISSTRFQINPDHPEARSLQLWFEREGRHAQAQSISREGAGGGGRTENRKTVSQIKDEGLGRSEKPDFVTIRATIHFIKTDSFCYTACPLQIGDRQCSKKVTNNGDGTWRCERCDRTVPECDYRYMLSIQVMDHTGATWLTGFQEAAEELLGVKAKDLFMWKQEDNGRFLDHIASIQFTQHHFKVRIKEESFNDEQRVKVNIQRAEKLDFVAESKYMIDAIGKLRRGEPINNTASFSAQTMSGMSGADAGYRATTGGGGYGGSASGYAGGGGYGGNAGGGGSSGGGYSGYVGNSGGGRSGFGANSGSGYGGGGGFSANTGGGWL
The following text describes a protein:
Function:
Tubulin binding protein that inhibits microtubule nucleation and growth, resulting in shorter microtubules.
Subcellular Localization:
Cytoplasm, cytoskeleton. Cytoplasm, cytoskeleton, spindle. Note=Colocalizes with the microtubule cytoskeleton. Colocalizes with the mitotic spindle.
Domain:
Contains a tandem atypical propeller in EMLs (TAPE) domain. The N-terminal beta-propeller is formed by canonical WD repeats; in contrast, the second beta-propeller contains one blade that is formed by discontinuous parts of the polypeptide chain (By similarity).
Sequence:
MSSFGAGKTKEVIFSVEDGSVKMFLRGRPVPMMIPDELAPTYSLDTRSELPSCRLKLEWVYGYRGRDCRANLYLLPTGEIVYFVASVAVLYSVEEQRQRHYLGHNDDIKCLAIHPDMVTIATGQVAGTTKEGKPLPPHVRIWDSVSLSTLHVLGLGVFDRAVCCVGFSKSNGGNLLCAVDESNDHMLSVWDWAKETKVVDVKCSNEAVLVATFHPTDPTVLITCGKSHIYFWTLEGGSLSKRQGLFEKHEKPKYVLCVTFLEGGDVVTGDSGGNLYVWGKGGNRITQAVLGAHDGGVFGLCALRDGTLVSGGGRDRRVVLWGSDYSKLQEVEVPEDFGPVRTVAEGHGDTLYVGTTRNSILQGSVHTGFSLLVQGHVEELWGLATHPSRAQFVTCGQDKLVHLWSSDSHQPLWSRIIEDPARSAGFHPSGSVLAVGTVTGRWLLLDTETHDLVAIHTDGNEQISVVSFSPDGAYLAVGSHDNLVYVYTVDQGGRKVSRLGKCSGHSSFITHLDWAQDSSCFVTNSGDYEILYWDPATCKQITSADAVRNMEWATATCVLGFGVFGIWSEGADGTDINAVARSHDGKLLASADDFGKVHLFSYPCCQPRALSHKYGGHSSHVTNVAFLWDDSMALTTGGKDTSVLQWRVV
The following text describes a protein:
Function:
Potent tight-binding inhibitor of several G1 cyclin/CDK complexes (cyclin E-CDK2, cyclin D2-CDK4, and cyclin A-CDK2) and, to lesser extent, of the mitotic cyclin B-CDC2. Negative regulator of cell proliferation. May play a role in maintenance of the non-proliferative state throughout life.
Subcellular Localization:
Nucleus.
Sequence:
MERLASSDTFPVIARSSACRSLFGPVDHEELGRELRMRLAELNAEDQNRWDFNFQQDVPLRGPGRLQWMEVDSESVPAFYRETVQVGRCRLQLGPRPPPVAVAVIPRSGPPAGEGPDGLEEAPEQPPSAPASAVVAEPTPPATPAPASDLTSDPIPDVTPVATSDSTPDPIPDVATQDGEEQVPEQVSEQVSEQGEESGAEPGDELGAEPVSEQGKQQGAEPVEEKDEEPVEEQGAEPVEEKDEEPVEGQNGELVEEQDENQELKDQPLSGIPGRPAAGTAAANANGAIKKLSGPLISGEPRTAPPRPGLALSGRPGSPSPSGASPGPRLLPWH
The following text describes a protein:
Function:
Specifically methylates the N4 position of cytidine in position 1402 (C1402) of 16S rRNA.
Subcellular Localization:
Cytoplasm.
Sequence:
MEEIEIIHKPVMLKEVIHYLKLSPGKIVVDATLGLGGHSSEILRELKGEGLLIGIDRDEEVLNLARERLRKIANNFVLFNTTYDKVQEILKELKLSFIDAILFDLGFSSFHIEKSERGFSFMRPEEPLDMRYSKDTTLTAADILNSFNELELSNLFWEYGEEPLSRKLAKKIVERRKEKKFVYVKDLLEVVEEVIPKRKRHEATKVFQALRIVVNDEVNILKRALDQIPFILAPRGRIVVLTYHSIEDRVVKNFFKSHSDKIFPVNKKVIRPSVNEIRENRRARSAKLRVGERRE
The following text describes a protein:
Function:
Mediator of diverse signals that repress RNA polymerase III transcription. Inhibits the de novo assembly of TFIIIB onto DNA.
Subcellular Localization:
Nucleus.
Sequence:
MKVRAGRDKAYLDLCALHEVNLALNFDTQDTAIIGGCDLWTVKAAGSDKKLYKRIEKTLEERHKDLLAFVADHSAQSAAQFADELDVARDTPFGSFSESSNRHTFAYLIATLNATHIDYDFANTLNPDEFRRESQNSFKHRIDQTMYYLRPQVYSAGLPIGAVTPLGSPIWSPRSWQLLDSEMDMANCEYYAWEPSDDPFADDGAIWSHHFFLYNKDRKRVCYFYLRGISALSDSPSVAMSLMSKFKQTKFESSANAGSRKRAEYWLGDRAKKGLEAYGDSDELDNMVIDHPGDVVDADQNVWVPVREMSTDADYYESDDDSDVEILVDRERGKSRVRTMSEGVMDRMEL
The following text describes a protein:
Function:
Component of the mitochondrial ribosome (mitoribosome), a dedicated translation machinery responsible for the synthesis of mitochondrial genome-encoded proteins, including at least some of the essential transmembrane subunits of the mitochondrial respiratory chain. The mitoribosomes are attached to the mitochondrial inner membrane and translation products are cotranslationally integrated into the membrane.
Miscellaneous:
MISCELLANEOUS: Present with 1550 molecules/cell in log phase SD medium.
Subcellular Localization:
Mitochondrion. Note=Mitoribosomes are tethered to the mitochondrial inner membrane and spatially aligned with the membrane insertion machinery through two distinct membrane contact sites, formed by the 21S rRNA expansion segment 96-ES1 and the inner membrane protein MBA1.
Sequence:
MSYKQYFDSLPLKLKSFFQRYPPSIKYSPVSTSTKAINANPFLPNKHPVTQRFHDPKYSLRRMSDVYKLALRYGVEEFLPPIENTKKLFFEEKYNKKTLMKGVLLPKGHKHELKLNEKLKKREEALKKVDELIASKKGSKYAKRVEKMKKNQSIGWF
The following text describes a protein:
Function:
Metalloprotease essential for chloroplast and plant development. May be involved in regulated intramembrane proteolysis (RIP).
Subcellular Localization:
Plastid, chloroplast inner membrane; Multi-pass membrane protein.
Sequence:
MLLNISSSPISHRNPHFLSNFNNPISYFPRRSKTHLSKSHFFPKFTPLSNQSLKNRVLFGNKRYPDGERFDFRSRAISGIDLGSFESVLEAIAVLTTIIVVHESGHFLAASLQGIHVSKFAIGFGPILAKFDYNNVEYSLRAFPLGGFVGFPDNDPDSEIPIDDENLLKNRPTLDRSIVVSAGIIANVIFAYAIIFVQVLSVGLPVQEAFPGVLVPEVKTFSAASRDGLLSGDVILAVDGTELSKTGPDAVSKIVDIVKRNPKSNVVFRIERGGEDFDIRVTPDKNFDGTGKIGVQLSPNVRITKVRPRNIPETFRFVGREFMGLSSNVLDGLKQTFFNFSQTASKVAGPVAIIAVGAEVARSNIDGLYQFAALLNINLAVINLLPLPALDGGTLALILLEAVRGGKKLPVEVEQGIMSSGIMLVIFLGLFLIVKDTLSLDFIKEML
The following text describes a protein:
Function:
Nematode cuticles are composed largely of collagen-like proteins. The cuticle functions both as an exoskeleton and as a barrier to protect the worm from its environment. Mutations in dpy-13 affects the body shape.
Sequence:
MDIDTKIKAYRFVAYSAVVFSVIAVLSVCITLPIVYNYVHTVRRQLHNEALTCKGSMKDVWADVHHLRVDAASNRTARAVRYGRDDAAAGNGPNFDSGCEGCCQPGPQGAPGAPGKPGRPGKPGAPGFPGNPGKAPQKPCEEITPPPCKPCPQGPPGAPGLPGDQGDKGEAGQPGQPGSDAAPGEQGPKGPNGAPGKPGAPGAPGDEGLPAVCEPVQKGEPGSTGEPGPVGPPGPSGQPGNDGTPGQPGPKGPPGPDGKPGADGNPGQPGPVGPPGTPGERGICPKYCAIDGGIFFEDGTRR
The following text describes a protein:
Function:
Repressor of jasmonate responses.
Subcellular Localization:
Nucleus.
Domain:
The jas domain is required for interaction with COI1.
Sequence:
MERDFMGLNSKEEAIEAVLRKSSSVQWSLSNGPEDLNNRQWAENQKNINLHGPTQLTIFYKGMVNVYDDMSPEKAHAIMSLARNEARAQAHAATPRTPVVDVVHAGQPMTTSSPVSIGTSTARDAPKEMSSFRRVIQSDVPQMREASLARFLQKRRERVMASAPYSSKPASSSAPNKDDHK
The following text describes a protein:
Function:
May participate in the coupling of lysosomes to microtubule plus-end-directed kinesin motor.
Subcellular Localization:
Lysosome membrane.
Sequence:
MPDPSSTPNRTREIESRSRIISERICESVRLLDNEPSLALYRLQEHTVRSLPGLVNRRIMLTQQSATLSGAQFDLENTLSTTTSMQNATSAFDNCIELLRNCMFYKQQLDFDSTRKATSSAESSTVKGRSKSLHNVATRVHSTEASTSNDA
The following text describes a protein:
Function:
Together with COR27, involved in central circadian clock regulation and in flowering promotion, by binding to the chromatin of clock-associated evening genes TOC1, PRR5, ELF4 and cold-responsive genes in order to repress their transcription. Negative regulator of freezing tolerance.
Subcellular Localization:
Nucleus.
Sequence:
MENDCTVNIVSLEKDRDVSEASAESQSESTLSNSLDSGVTAETSRSDADSKLDECTAWTNEKHNSYLDYLESSFVRQLYSLLGGGTQRLSRTRDVQSNSHKSADQFTVLQNGCWQKVNFGKKQSCLETSSEFRFHRNSLRNKPENSNGNYTMGTTVQGDVLCHDETKHSEASGQNFREEEEEEEKGEVSKKREREANNDDSSLKEDQVVPVRMVKPRT
The following text describes a protein:
Function:
Acts as a component of the outer kinetochore KNL1 complex that serves as a docking point for spindle assembly checkpoint components and mediates microtubule-kinetochore interactions. 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. Targets the RZZ complex to the kinetochore at prometaphase (By similarity). Recruits MAD2L1 to the kinetochore, but is not required for BUB1B localization. In addition to orienting mitotic chromosomes, it is also essential for alignment of homologous chromosomes during meiotic metaphase I. In meiosis I, required to activate the spindle assembly checkpoint at unattached kinetochores to correct erroneous kinetochore-microtubule attachments (By similarity).
Subcellular Localization:
Nucleus. Chromosome, centromere, kinetochore. Note=Localizes to kinetochores from late prophase to anaphase (By similarity). Localizes to kinetochores both during mitosis and meiosis (By similarity).
Sequence:
MGAAESEVETAAREVLAKVADILEPVGFQEEAELPAQILAEFVMDSRKKDKLLCSQLQVVDFLQNFLVQEGTAQDQNPLASEDTSRQKALEAKEQWKELKATYQEHVEVITNSLTEALPKVEEAQIKQAQLQEALKQLQAKKQMAMEKLRIAQKQWQLEQEKHLQNLAEASSEVRERQTGAQQELQRLYQELGTLKQQAGQEKDKLQRHQTFLQLLYTLQGKQLFNEAEAEIPQELDLPKDKLQQVTQPQEQNTQDTMGREADNPQPVGDAGLPWLPGRQQHKEES
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:
MSYFQKLVQHGSYNILSKFYNQIGHEDEQKPIFVGGCSFYILGVEFKTKQMDKQLAEQPPEVYLQYSSAATFFRISNLFWMTYRSGYEKLPNSSLTTDVGWGCTIRAMQMMIANAMETIVYSGALNNTQTPYIPTKQEVMNVLIPFIDSPNSTTPLSIHHVYESRFVVEKNKSGVNYLAPSVVAKAYSGLVNSWKLCPIRCVMCSNVSIPTHELSKLPFKPTLVFLPIVLNHLIHSKLQQIYKSKLFAGIVGGMGDRAIFVFGFHALQFLYLDPHIVQPSFKSFTEIDTKSYSPIGTNRFSVHTIDPTKLDDFCTFGFLIKNLHEVDDFMKLAKDVFEISNDKELRTSHDLNGFEVLDF
The following text describes a protein:
Function:
Participates in the translocation of lipoproteins from the inner membrane to the outer membrane. Only forms a complex with a lipoprotein if the residue after the N-terminal Cys is not an aspartate (The Asp acts as a targeting signal to indicate that the lipoprotein should stay in the inner membrane) (By similarity).
Subcellular Localization:
Periplasm.
Sequence:
MNKWLALLFCSFSAIAAPKDTLSERLAMSEGFSATFNQQVLSPEGKVILTGNGKVDIARPSLFRWETETPDENLLVSDGTTLWHFDPFVEQVTLYRAEEALEQTPFVLLTRNKASDWDAYHVEEKGDVFTLTPTALDSNQGRFQITISEKGVVQGFKVIEQDGQQSEFTFSKVKQQKPNASVFNYKVPKGVEVDDQRN
The following text describes a protein:
Function:
Together with BOLA2, acts as a cytosolic iron-sulfur (Fe-S) cluster assembly factor that facilitates [2Fe-2S] cluster insertion into a subset of cytosolic proteins. Acts as a critical negative regulator of cardiac hypertrophy and a positive inotropic regulator. Required for hemoglobin maturation. Does not possess any thyoredoxin activity since it lacks the conserved motif that is essential for catalytic activity.
Subcellular Localization:
Cytoplasm, cytosol.
Sequence:
MLSKAGRHECTGAALSAGLGARPVLAGAGGGGEGREARRAVRRGSTGSAWRGEALGARRSSGAAWRGRGVRVLGSGFGVRGSGPGMASGPAMSGPQEVTSPPQLEELLRRRDKSLVVIHFWAPWAPQCAPMNDVMAELAKEHPQAAFAKLEAEAVPEVSEKYEISSVPTFLFFKDSRRVDRLDGAHAPELTRKVRRHLTSAAPLLPPGAAGHGEDLAARLKRLIHAAPCMLFMKGSPQEPRCGFSRQMVEILTRHNIQYGSFDIFSDEEVRQGLKAYSNWPTYPQLYVAGELVGGLDIVKELEASQELETICPKVPSLEKRLQELTNKASVMLFMKGNKQMAKCGFSKQILEILNDSGVEYETFDILEDEEVRQGLKTYSNWPTYPQLYVKGELVGGLDIVKELKETGELLSTLKGEN
The following text describes a protein:
Function:
Catalytic subunit of the poly(A)-nuclease (PAN) deadenylation complex, one of two cytoplasmic mRNA deadenylases involved in general and miRNA-mediated mRNA turnover. PAN specifically shortens poly(A) tails of RNA and the activity is stimulated by poly(A)-binding protein (PABP). PAN deadenylation is followed by rapid degradation of the shortened mRNA tails by the CCR4-NOT complex. Deadenylated mRNAs are then degraded by two alternative mechanisms, namely exosome-mediated 3'-5' exonucleolytic degradation, or deadenlyation-dependent mRNA decaping and subsequent 5'-3' exonucleolytic degradation by XRN1.
Subcellular Localization:
Cytoplasm, P-body. Nucleus. Note=Shuttles between nucleus and cytoplasm.
Domain:
Contains a pseudo-UCH domain. This ubiquitin C-terminal hydrolase (UCH)-like or ubiquitin specific protease (USP)-like domain is predicted to be catalytically inactive because it lacks the active site catalytic triad characteristic of thiol proteases, with residues at the equivalent structural positions that are incompatible with catalysis, and it cannot bind ubiquitin. It functions as a structural scaffold for intra- and intermolecular interactions in the complex; The linker, or PAN3 interaction domain (PID), between the WD40 repeats and the pseudo-UCH domain mediates interaction with PAN3.
Sequence:
MEFNTSTGGGITPNPYAPQFSPAAATTTTTASTFSPDAPPFAPSPGPHAPPFAPSPVPHAPQTPQHHPEIFVDGHVPILDGSFNGSGDASVHFGHNSSGFEEGFHPSDPNSQHHSGQHQEHGIMQGGRGISNPPVGNEEYHELHTIVADGGDRYGVSAVAFDLHQELLWMGNQGGHVTSYYGPGMQKYSSFQPLPVGTEMRQVLSIDNGVLLLGNNRMRCSERGGLTIFDFSGEDMHDMQVMTMVDPTTLLIGGHQDKVIEFDLNSGQQVNLLEVGDPGVAIFRHTNRFICCGDTSGQVTLRDMNTFKTEHILKAHSGSLSDFDVHGNLLVTAGFSTRRGSLAVDRFLMIYDLRVMRAMAPMQLSIDPMFLRFVPTYTPRIVAVSQAGQFQILDLAGVMTPASMAIHQLNTHGHMCMGFDISTSCEAFSFGDNGGLLHLWTDREEVLYNNYSSPTEFADHPEHLPAMSIVDPLTPLASIPMLYENCHGPLLSDWPEDCMKYVKRRMPPVDPEILASMKIVQFIGYAPNPRVKKRNQVPYRAKDLAITIPTSSTGATSTVPESPGARGESPRWYMVPTRYRKVEIKYTKLGVDSFDFRHYNRTNFAGLETNIPNSYCNAMLQVLYFIEPLRCAAQSHLCEKEFCLTCELGFLFHMLDMSKGENCQASNFLRAFRTIPEASALGLVLGDHEEATGKVNLGRLIQSWNRFIVQQVHQDILEPKEEDSEKKEPEEPEPPKEVEKTPIEKMFSSEVTISSKCRCGKETTKETNSMVYGLNYPDISDPELKKKQYSFAEVLKSSMSSEQVTHAWCEDCNRYQPTTQSRKLKSLPDILSINCHLDSERDQLFWQAQEEKMPNYVPWDQVMKQKEGNSSKPSSSQSRTVRPCRYGSQCTRSDCKFSHGSQDKEQTPCRYGDMCTRPDCKFSHRSNTERQQATVLSSAEILEMSLQEEAQAHWLPCGLKMALVDGHLKIEGLPEMEDVEKEKPSEEWAVYELTSSVCHVQESRLGGNLDVEKEKPSEEWAVYELTSSVCHVQESRLGGNLVAHIKGGIPYHKRKEGITATQWYLVNDFAIAPMDKLDAVQYGMAWKVPCVLYFSRKDLNKRHDCQIHNPISEKVLFPEASLSSRVLKRHITFQPLAAEEMPKDGDLVALDAEFVTLNQEEAELHSDGTRSTIKPSHMSVARITVIRGQGPQEGTPFIDDYISTQEQVVDYLTKFSGIKPGDLDANISSKHLTTLKSTYLKLRYLIDRGVKMVGHGLKKDFRVINLFVPKDQIVDTVLLFHLTNKRMMSLRFLAWYFLKLRIQSDTHDSIEDARTALQLHKKYKQLKDEQEPDEFHKTLRKMYEEGRKVGWKPPDE
The following text describes a protein:
Function:
Mediates the nuclear export of proteins (cargos) with broad substrate specificity.
Subcellular Localization:
Nucleus. Cytoplasm. Nucleus, nuclear pore complex. Note=Shuttles between the nucleus and the cytoplasm.
Sequence:
MSIQSEQDFFKFEELCKDFYLKPEETIKIDDILHQYFLNPNFLIEYKQILSFTKNSYVVAQVIRGLIKCVTSFWTSLTPNQKNDMSKSIEHHCIGLRILKDIISEFNEYIGEHLTVLQHRNISISLRDNILLDIFCISLESLNYALANSMDEKFKSIKELALDLSYSCLSFDFIKTTSIDSSEEILTVQIPSQWKSTFDENNPLELFFKIYKQYHSTKSLECILQIVSIRRSFFTTEDERVKFLASIVQYTTEILKSNIGFNEPNNHLVFSRVIERLKTNYHLNNLVTVVGYNDWISNLSTFTIDTLKNPQFSPNSIYFLLTLWAKLVSSIIYVKGDPSKTYLEKYSPIIMESFINSKIDNSYSDEEDEHLMDYEKMVEILEGIPHLGRITYQATCRQIILLFDSISSKFLNETNPTQLEVYERQCAWLVYIIGCLILGRTSINSSEEHDKIDGELSVRVFILIGYNDKKLSAESNTQYQYRTSRISLELSFIYFMQNFRRIYIGENSISSSKIYQRISELSGPTDHTSVLFSIVQKIGFNFKYWAENDEIIKKSLDMFWESVNGHSTSKMLIDNKITKDILKTHSSQVFPFLEKNSNPRNRTSLYKTIGKLLFTDENMGFFDEFIAPFDDTIKHLLNISTPEQFRTEEIKRKVIGLLRDLRGIITSANSKRSYLLFFEWIHLNFSEVLIKIINVWVDSPEVTTSLLKFISEFVFNRQSRLIFDSSSANGFIIFRDTSKILVSYASLILKANISKQDLYKFKIKGIQTSMLLFTRCLVGGYCNFGVFELYGDPSFTSAIDYIFQLCLSVSLDELMSFPKASKAYVTMLEALCLGHTLSIIQLNQQYFIHIMKSLHRCLDSQDVTMSSSSCTSIEKIITVCYYHLKKKNSQCLQAIHQNFFSNSNILYEIIDKIISIIIYEDNFNQFMFSKLLLTCIIFHQDTFTTLKQKYIHSFNSQCPEKVEKAFVQLMENTLDNLETKNKDKFTSNVSIFRKEMKLISSSTGRYL
The following text describes a protein:
Function:
Glutamate-gated receptor that probably acts as non-selective cation channel.
Subcellular Localization:
Membrane; Multi-pass membrane protein.
Sequence:
MGCLARLTRPLIEGSEALTSHQRVLDLIENEEVHAILGPKWSSQAKFVIDLGGKAQVPIISFSATSPSLSPTHSPYFVRTAYDDSSQVDALAAVVQAYGWREITLVYEDTDYGNGLVPYLVDAFQKVDARISYRSVIPPSPEDVDIVKELNNLLTRQTRVFLVHMTAMIGSRFFALAHNAGMMSEEFAWIVTDGLSSSLDPVISKALDSMQGVVGVRPHVPRSESRINFEERWRKLYNERNPHYEIADLGLFGLWAYDTVSALALAGEMAWDPAKSRYLKPNTSRKNLDFSSIEISEMGPKLLDKILSIKFQGLTGEFKLLNGALHPIAFEIFNVVGQNEKTIGYWTLAQGLSPDLNLSTREVYKALANDLKPPTWSGDTLKPPKGWVMPILGKKLRIGVPMKDGFSEFFKIKWDPHTGVPSYSGFAHDMFMAVRDALPFAIPYEYIPYVDASRQSAGTYDDMLNEIKCQKFDAVVGDTTIVAYRSSDVDFTLPYSESGLAMVVAIKDDERRNTWIFIKPLSWNLWLTTVLASIFTGSVVWLLERRTNEEFRGRPRQQIGLIFLFSLSTLVFAHSKSIQICRASFVIMIFIIKLPFTLIHVDVGEKTANNLTRPVLIVWVFVVLILTQSYTASLASILTVQRFTPKFVDVQDLIRNRHFVGYQKGSYVREFLVTQLNFNASKLIPYGSPEEYHEALSKGSENGGVAAIFDDLPCIKLFLARYCNKYKVVGATYKTGGFGFAFPLGSPLVSHVSRAILNVTQDKAKMDAMEGKHFGGQSSCQDQDAAIFSDDLSLSVYSFGGLFIITGVVSVSSVLIYVVSFFYSHWPSSSAAHAADCSLWSKFLETTDNFFREHGLFGCLERNRSTMIPTSHIPSSEASPNSDVELIARTPE
The following text describes a protein:
Function:
Potentially plays a role in the Ras signal transduction pathway. Capable of suppressing v-Ras transformation in vitro.
Sequence:
MRDLQPTRTFPQQKTQPRVKQGAAGVRFPAKRQLCNSTARTPSPLRPPVTVHPLYRKVAGKGLAPDWLPVEERGGALFADWFCPVHSGEGTSVWGGIRLIWRVSYFTAPGGFLWGFIMSKSLKKIVEESREKNVPDIDMCDRGIANMLDVPGLFTLSHITQLILSHNKLTTVPPNIADLKNLEVLNFFNNQIEELPTQISSLQKLKHLNLGMNRLNSLPRGFGSLPALEVLDLTYNNMNENSLPGNFFYLTTLRALYLSDNDFEILPPDIGKLTKLQIISLRDNDLISLPKEIGDLTQLKELHIQGNRLTVLPPELGNLDLTGQKQVFKAENNPWVTPIADQFQVGVSHVFEYIRSETYKYLYGRHMQANPEPPKKNNDKSKKISRKPLAAKNK
The following text describes a protein:
Function:
Catalyzes the attachment of valine to tRNA(Val). As ValRS can inadvertently accommodate and process structurally similar amino acids such as threonine, to avoid such errors, it has a 'posttransfer' editing activity that hydrolyzes mischarged Thr-tRNA(Val) in a tRNA-dependent manner.
Subcellular Localization:
Cytoplasm.
Domain:
ValRS has two distinct active sites: one for aminoacylation and one for editing. The misactivated threonine is translocated from the active site to the editing site; The C-terminal coiled-coil domain is crucial for aminoacylation activity.
Sequence:
MSEIPTRFEHAEEADKIAQAWTDAKCSHADPESSKPPFSVVIPPPNVTGALHLGHGLNNTLQDIVVRRKRMQGFETLWMPGTDHAGIATQAVVERRLKEQEDKTRHDLGREALVDRIWQWKDQYEERIIGQLKRMGTSCDWERLRFTLDPICAAAVRATFFDLFGKRRIYRGKRLVNWDTFLQTAVSDDEVFNETKKGHFYHFRYPVIDPKPGEPEFVTIATTRPETMLGDTAVAVHPDPAAALDAVEAGLREKLSDANEKEAVDLNKQIEALQKRREERLPELIQLRDMAADGRKLMLPLVDREIDLVADEWAKPEMGSGCVKITPAHDPNDYEVGIRQDLPMINILNSDGTLNGEGGQFAGLTIPKARKAVVAALEELGLMGDIEDREIELPHSDRSKTPIEPYLADQWFVAMDELAQSAMDAVSDERVQIFPARYRKGYLDWLSEKRDWPVSRQLWWGHRIPIWSVGGLSQQEANELSSELEKLAERHPDQIAQRIDSDGVDAAGEPTKAVFVCIRSEDETVEADVEALGLQQDPDVLDTWFSSALWPHSTLGWPAQTPELAKFYPTATLITSRDILTLWVARMVLMGLNNVGEVPFSEVFIHPKILDGLGETMSKSKGNGVDPIDVIDKFGPDALRFGLARLATETQDVRMPVQYECPSCEKLIDQTKKNRALPSMDCPACGKPFSTQWAETEADKSLPKAAVVSERFETARNFVNKLWNASRFVMMNLDGFEPTSLDVASLPIEDRWLLSRLSTVTQTVGDAIERYQFGEAARVLYDFAWDEFCSFYVEIAKPRLSDDSQRQIAQNVIAHGLDQLLRLLHPIMPFVTESVWNHLGQIAPKRGVPEPAEVGPFVMTASFPVADESHHDSKIERQFSEFQQIVAAIRQIRASQNIAPKETVPAAIRCSASSQELLQPMTAYFEALAGAEVQSLGPDTTAFETDAHLALPDVDVDVHVDLEKFIDVEAELARLEKLQGQLTGQITGKQNKLSNESFVSRAPADIVQKERESLAGLQTQLEAVAQDILKLQSKK
The following text describes a protein:
Function:
Phospholipid scramblase involved in autophagy and cytoplasm to vacuole transport (Cvt) vesicle formation. Cycles between the preautophagosomal structure/phagophore assembly site (PAS) and the cytoplasmic vesicle pool and supplies membrane for the growing autophagosome. Lipid scramblase activity plays a key role in preautophagosomal structure/phagophore assembly by distributing the phospholipids that arrive through atg2 from the cytoplasmic to the luminal leaflet of the bilayer, thereby driving autophagosomal membrane expansion. Required for mitophagy. Also involved in endoplasmic reticulum-specific autophagic process and is essential for the survival of cells subjected to severe ER stress. Different machineries are required for anterograde trafficking to the PAS during either the Cvt pathway or bulk autophagy and for retrograde trafficking (By similarity).
Subcellular Localization:
Preautophagosomal structure membrane; Multi-pass membrane protein. Cytoplasmic vesicle membrane; Multi-pass membrane protein. Golgi apparatus membrane; Multi-pass membrane protein. Endoplasmic reticulum membrane; Multi-pass membrane protein.
Domain:
Forms a homotrimer with a solvated central pore, which is connected laterally to the cytosol through the cavity within each protomer. Acts as a lipid scramblase that uses its central pore to function: the central pore opens laterally to accommodate lipid headgroups, thereby enabling lipid flipping and redistribution of lipids added to the outer leaflet of ATG9-containing vesicles, thereby enabling growth into autophagosomes.
Sequence:
MSSSSYNPYKNNVNDRLINNSTDSFQDNDQGIPNNNDTFLSRIFGLNSIYNQLQDNYQYYDPEFDSSLNQQLQQSIQENDEAEDESLLPQHQQQQQQAAPMDLSIQDKSAKQKSKSSSLLNSDSDSDLSSSEDSYVRPNIPQIPSTPIETENQGSSSKIKFSIPQRAKNFVGKLHPHHEPTLPVYQTPQEFRRNLPQQQRASATVNTNYQRTRNNNRRFIIPPKERALYLWANITNMDEFLSDVYYYYRGRGLLNIVLSRGFDLIILIFILIFTVFLKWGIDYSIFFDNLHQEESKHITLNDMIIPNYFATIPLSIKFILFGFSVYILLRSVQLYLDYNYKLKELKNFYHYLLDVTDDELMTISWKTIVEKLMLLKDYNSLTSTTKSNNFSENHYVNDLSSKVRLNAHDIANRIMRRENYMIALINKDILDLSVLFMNEKSLLTKTLEWNLKLCIDNFIYNQQGQINGKILKEYNRNQLARELTSRFKLAAIINLILSPFIVIYFVLLYFFRYFNEYKSNPASILGLRQYTPYAEWKLREYNELSHLFNKRLIMSMGPANTYIDQFPKGFLVVNLMRLINFISGSILAVLVIMGILLEDENHSFWSFEITDGRSALFYISIFGTIWAITASSATGTSHESTISTTSQSSNSNSNSNAASTFVYDPEASLRYVAQFTHYLPSSWNKKLHTIQVKNEFCQLYCLKIIIIINEILSSVLTPFILWFKISHNSGNIIDFYREYSIHVDGLGYVCYFAMFNFEEKDKNMMSDLNKSKKRRKRMKNKMNKYGKTKMVNPISGKTVNSEIEMTKISKSESERSSDDESGNEQDYDNDEELDYLSYKKDDKMIKSYMYFLESYGGSKQPQPQPPQQQQHPQNQNQTVGGLRNRNPIQSIDPAIMTGNYYDQQSLNSSIYNINYKFDDSGLLQDETMNSSSRKKGGVLGMLNQFYKQDINR