lhallee/plat_data huggingface dataset:
The following text describes a protein:
Function:
Together with LptD, is involved in the assembly of lipopolysaccharide (LPS) at the surface of the outer membrane. Required for the proper assembly of LptD. Binds LPS and may serve as the LPS recognition site at the outer membrane.
Subcellular Localization:
Cell outer membrane; Lipid-anchor.
Sequence:
MLIKRLAFAIMTLVIMTSAGCGFKLQRSYQIPEQLNQLSLSSSDEYSELTRLVRERLRLNNVKIVDAANDVPVLRLITDSLERSTLSLYPTGNVAEYELIYFVEFAVALPGKEAQPFKIEIRRDYLDDPRTALAKSREMELLVKEMRIQAADRILQSMASTEVN
The following text describes a protein:
Function:
This proteoglycan is a major component of extracellular matrix of cartilagenous tissues. A major function of this protein is to resist compression in cartilage. It binds avidly to hyaluronic acid via an N-terminal globular region. May play a regulatory role in the matrix assembly of the cartilage.
Subcellular Localization:
Secreted, extracellular space, extracellular matrix.
Domain:
Two globular domains, G1 and G2, comprise the N-terminus of the proteoglycan, while another globular region, G3, makes up the C-terminus. G1 contains Link domains and thus consists of three disulfide-bonded loop structures designated as the A, B, B' motifs. G2 is similar to G1. The keratan sulfate (KS) and the chondroitin sulfate (CS) attachment domains lie between G2 and G3.
Sequence:
MTTLLLVFVTLRVITAAISVEVSEPDNSLSVSIPEPSPLRVLLGSSLTIPCYFIDPMHPVTTAPSTAPLAPRIKWSRISKEKEVVLLVATEGRVRVNSAYQDKVTLPNYPAIPSDATLEIQNMRSNDSGILRCEVMHGIEDSQATLEVVVKGIVFHYRAISTRYTLDFDRAQRACLQNSAIIATPEQLQAAYEDGFHQCDAGWLADQTVRYPIHTPREGCYGDKDEFPGVRTYGIRDTNETYDVYCFAEEMEGEVFYATSPEKFTFQEAANECRRLGARLATTGQLYLAWQGGMDMCSAGWLADRSVRYPISKARPNCGGNLLGVRTVYLHANQTGYPDPSSRYDAICYTGEDFVDIPESFFGVGGEEDITIQTVTWPDVELPLPRNITEGEARGSVILTAKPDFEVSPTAPEPEEPFTFVPEVRATAFPEVENRTEEATRPWAFPRESTPGLGAPTAFTSEDLVVQVTLAPGAAEVPGQPRLPGGVVFHYRPGSSRYSLTFEEAKQACLRTGAIIASPEQLQAAYEAGYEQCDAGWLQDQTVRYPIVSPRTPCVGDKDSSPGVRTYGVRPPSETYDVYCYVDRLEGEVFFATRLEQFTFWEAQEFCESQNATLATTGQLYAAWSRGLDKCYAGWLADGSLRYPIVTPRPACGGDKPGVRTVYLYPNQTGLLDPLSRHHAFCFRGVSAAPSPEEEEGSAPTAGPDVEEWMVTQVGPGVAAVPIGEETTAIPGFTVEPENKTEWELAYTPAGTLPLPGIPPTWPPTGEATEEHTEGPSATEVPSASEKPFPSEEPFPPEEPFPSEKPFPPEELFPSEKPFPSEKPFPSEEPFPSEKPFPPEELFPSEKPIPSEEPFPSEEPFPSEKPFPPEEPFPSEKPIPSEEPFPSEKPFPSEEPFPSEEPSTLSAPVPSRTELPSSGEVSGVPEISGDFTGSGEISGHLDFSGQPSGESASGLPSEDLDSSGLTSTVGSGLPVESGLPSGEEERITWTSAPKVDRLPSGGEGPEVSGVEDISGLPSGGEVHLEISASGVEDISGLPSGGEVHLEISASGVEDLSRIPSGEGPEISASGVEDISGLPSGEEGHLEISASGVEDLSGIPSGEGPEVSASGVEDLIGLPSGEGPEVSASGVEDLSRLPSGEGPEVSASGVEDLSGLPSGEGPEVSVSGVEDLSRLPSGEGPEVSASGVEDLSRLPSGEGPEISVSGVEDISILPSGEGPEVSASGVEDLSVLPSGEGHLEISTSGVEDLSVLPSGEGHLETSSGVEDISRLPSGEGPEVSASGVEDLSVLPSGEDHLEISASGVEDLGVLPSGEDHLEISASGVEDISRLPSGEGPEVSASGVEDLSVLPSGEGHLEISASGVEDLSRLPSGGEDHLETSASGVGDLSGLPSGREGLEISASGAGDLSGLTSGKEDLTGSASGALDLGRIPSVTLGSGQAPEASGLPSGFSGEYSGVDLESGPSSGLPDFSGLPSGFPTVSLVDTTLVEVVTATTAGELEGRGTIDISGAGETSGLPFSELDISGGASGLSSGAELSGQASGSPDISGETSGLFGVSGQPSGFPDISGETSGLLEVSGQPSGFYGEISGVTELSGLASGQPEISGEASGILSGLGPPFGITDLSGEAPGIPDLSGQPSGLPEFSGTASGIPDLVSSAVSGSGESSGITFVDTSLVEVTPTTFKEEEGLGSVELSGLPSGELGVSGTSGLADVSGLSSGAIDSSGFTSQPPEFSGLPSGVTEVSGEASGAESGSSLPSGAYDSSGLPSGFPTVSFVDRTLVESVTQAPTAQEAGEGPSGILELSGAPSGAPDMSGDHLGSLDQSGLQSGLVEPSGEPASTPYFSGDFSGTTDVSGESSAATSTSGEASGLPEVTLITSELVEGVTEPTVSQELGQRPPVTYTPQLFESSGEASASGDVPRFPGSGVEVSSVPESSGETSAYPEAEVGASAAPEASGGASGSPNLSETTSTFHEADLEGTSGLGVSGSPSAFPEGPTEGLATPEVSGESTTAFDVSVEASGSPSATPLASGDRTDTSGDLSGHTSGLDIVISTTIPESEWTQQTQRPAEARLEIESSSPVHSGEESQTADTATSPTDASIPASAGGTDDSEATTTDIDECLSSPCLNGATCVDAIDSFTCLCLPSYQGDVCEIQKLCEEGWTKFQGHCYRHFPDRATWVDAESQCRKQQSHLSSIVTPEEQEFVNNNAQDYQWIGLNDKTIEGDFRWSDGHSLQFENWRPNQPDNFFATGEDCVVMIWHEKGEWNDVPCNYQLPFTCKKGTVACGEPPVVEHARIFGQKKDRYEINALVRYQCTEGFIQGHVPTIRCQPSGHWEEPRITCTDPATYKRRLQKRSSRPLRRSHPSTAH
The following text describes a protein:
Function:
[Capsid polyprotein VP90]: The capsid polyprotein VP90 self-assembles and undergoes a proteolytic cleavage by host caspases to yield the immature VP70 virion; [Capsid polyprotein VP70]: The immature virion is composed of 180 VP70 subunits with 90 dimeric spikes and displays a T=3 icosahedral symmetry. During maturation, VP70 undergoes a loss of 60 peripentonal spikes, which likely plays an important role in viral infectivity; [Core protein VP34]: Self-assembles to form an icosahedral capsid with a T=3 symmetry, about 43 nm in diameter. This forms contains only 30 spikes located on the icosahedral 2-fold axes; [Spike protein VP27]: VP25 and VP27 Forms the spikes at the surface of the virion. This forms contains only 30 spikes located on the icosahedral 2-fold axes. Plays a role in the attachment to target host cell (Probable). This attachment induces virion internalization through clathrin-dependent endocytosis; [Spike protein VP25]: VP25 and VP27 Forms the spikes at the surface of the virion. This forms contains only 30 spikes located on the icosahedral 2-fold axes. Plays a role in the attachment to target host cell. This attachment induces virion internalization through clathrin-dependent endocytosis.
Subcellular Localization:
[Capsid polyprotein VP90]: Virion. Note=Immature capsid; [Capsid polyprotein VP70]: Virion. Note=Immature capsid after cleavage by host caspases; [Core protein VP34]: Virion. Note=Capsid; [Spike protein VP27]: Virion. Note=Capsid; [Spike protein VP25]: Host extracellular space. Virion. Note=Capsid (By similarity). Spike protein VP25 that lacks the core attachment region may need to dimerize with spike protein VP27 to remain stably bound to the viral particle (Probable).
Domain:
[Spike protein VP27]: Contains the core attachment region and the P2 globular region; [Spike protein VP25]: Contains the P2 globular region. The core attachment region is lost by cleavage; [Capsid polyprotein VP70]: Contains a lipid disrupting region that is exposed after trypsin treatment.
Sequence:
MASKSDKQVTVEVNNNGRSRSKSRARSQSRGRGRSVKITVNSHNKGRRQNGRNKYQSNQRVRKIVNKQLRKQGVTGPKPAICQTATATLGTIGSNTTGATEIEACILLNPVLVKDATGSTQFGPVQALGAQYSMWKLKYLNVRLTSMVGASAVNGTVVRISLNPTSTPSSTSWSGLGARKHLDVTVGKNAVFKLKPSDLGGPRDGWWLTNTNDNASDTLGPSIEIHTLGQTMSSYQNTQFTGGLFLVELSSAWCFTGYAANPNLVNLVKSTDKSVNVTFEGSAGTPLIMNVPEHSHFARTAVEHSSLSTSLSRAGGESSSDTVWQVLNTAVSAAELVTPPPFNWLVKGGWWFVKLIAGRARTGARRFYVYLSYQDALSNKPALCTGGVPASARQSNPVRTTLQFTQMNQPSLGHGATPMTFGRSIPEPGEQFRVLLTVGPPMAPNTANSQNWVNKTIVPPENQYTVKIGIDLEHYTTMQGFTPVESVSWYTADFQPSDEPSPIPGLYARVNNTKKADVYGVQQFKSSHTNNRHQITSVFLVRVTTSFQVINYTSYFIRGAESGSNVSNLKIRDQTYHTPLQFTQGKWYLLTSTVMHDGPTSSGWVWMNQELTNNIAYRVDPGMMYLITPPPAASQLYFELHTVLPQARSEEPETYVDAPLPEEPPIEEEETDSDFESTEDENDEVDRFDLHPSSESDDDDVENDRATLLSTLLNQGISVERATRITNGAFPTRAARVRRSVYNDLLVSGLSPGAAWSHACEQARRAGDNHDLQLSGSRDHAE
The following text describes a protein:
Function:
May be involved in cooperative interactions with calmodulins or calmodulin-like proteins (By similarity). Recruits calmodulin proteins to microtubules, thus being a potential scaffold in cellular signaling and trafficking (By similarity). May associate with nucleic acids and regulate gene expression at the transcriptional or post-transcriptional level (By similarity).
Subcellular Localization:
Cell membrane. Nucleus.
Sequence:
MGKASRWFRSLFGVKKPDPGYPDLSVETPSRSTSSNLKRRWSFVKSKREKESTPINQVPHTPSLPNSTPPPPSHHQSSPRRRRKQKPMWEDEGSEDSDKHAIAVAAATAAVAEAAVAAANAAAAVVRLTSTSGRSTRSPVKARFSDGFDDVVAHGSKFYGHGRDSCELAVIKIQSIFRGYLAKRALRALKGLVRLQAIVRGHIERKRMSVHLRRMHALVRAQARVRATRVIVTPESSSSQSNNTKSSHFQNPGPPTPEKLEHSISSRSSKLAHSHLFKRNGSKASDNNRLYPAHRETFSATDEEEKILQIDRKHISSYTRRNRPDMFYSSHLILDNAGLSEPVFATPFSPSSSHEEITSQFCTAENSPQLYSATSRSKRSAFTASSIAPSDCTKSCCDGDHPSYMACTESSRAKARSASAPKSRPQLFYERPSSKRFGFVDLPYCGDTKSGPQKGSALHTSFMNKAYPGSGRLDRLGMPIGYRY
The following text describes a protein:
Function:
Upstream regulator of interferon-induced serine/threonine protein kinase R (PKR). May block the PKR-inhibitory function of DNAJC3, resulting in restoration of kinase activity and suppression of cell growth.
Sequence:
MPNFCAAPNCTRKSTQSDLAFFRFPRDPARCQKWVENCRRADLEDKTPDQLNKHYRLCAKHFETSMICRTSPYRTVLRDNAIPTIFDLTSHLNNPHSRHRKRIKELSEDEIRTLKQKKIEETSEQEQETNTNAQNPSAEAVNQQDANVLPLTLEEKENKEYLKSLFEILVLMGKQNIPLDGHEADEVPEGLFAPDNFQALLECRINSGEEVLRKRFEATAVNTLFCSKTQQRHMLEICESCIREETLREVRDSHFFSIITDDVVDIAGEEHLPVLVRFVDDAHNLREEFVGFLPYEADAEILAVKFHTTITEKWGLNMEYCRGQAYIVSSGFSSKMKVVASRLLEKYPQAVYTLCSSCALNAWLAKSVPVIGVSVALGTIEEVCSFFHRSPQLLLELDSVISVLFQNSEERAKELKEICHSQWTGRHDAFEILVDLLQALVLCLDGIINSDTNVRWNNYIAGRAFVLCSAVTDFDFIVTIVVLKNVLSFTRAFGKNLQGQTSDVFFAASSLTAVLHSLNEVMENIEVYHEFWFEEATNLATKLDIQMKLPGKFRRAQQGNLESQLTSESYYKDTLSVPTVEHIIQELKDIFSEQHLKALKCLSLVPSVMGQLKFNTSEEHHADMYRSDLPNPDTLSAELHCWRIKWKHRGKDIELPSTIYEALHLPDIKFFPNVYALLKVLCILPVMKVENERYENGRKRLKAYLRNTLTDQRSSNLALLNINFDIKHDLDLMVDTYIKLYTNKSELPTINSETIENT
The following text describes a protein:
Function:
Transcription factor involved in glucosinolates biosynthesis.
Subcellular Localization:
Nucleus.
Sequence:
MVRTPCCRAEGLKKGAWTQEEDQKLIAYVQRHGEGGWRTLPDKAGLKRCGKSCRLRWANYLRPDIKRGEFSQDEEDSIINLHAIHGNKWSAIARKIPRRTDNEIKNHWNTHIKKCLVKKGIDPLTHKSLLDGAGKSSDHSAHPEKSSVHDDKDDQNSNNKKLSGSSSARFLNRVANRFGHRINHNVLSDIIGSNGLLTSHTTPTTSVSEGERSTSSSSTHTSSNLPINRSITVDATSLSSSTFSDSPDPCLYEEIVGDIEDMTRFSSRCLSHVLSHEDLLMSVESCLENTSFMREITMIFQEDKIETTSFNDSYVTPINEVDDSCEGIDNYFG
The following text describes a protein:
Function:
Controls stomatal patterning.
Subcellular Localization:
Secreted.
Sequence:
MAEWGLAGTYKKLGLKLKEGKISFNNNYLDKHVVFVFDKCDSGRYQAYNSSLSEKILISVTHHPSSFHPSHNYTYISLSFPLFPPVSQMGTCSFSLNIQSSTAFFIFFLIFNSTHSRFMPQGGSNFSLIDKNAQMKRASLFIGSRPPRCEKIYCRNCSHCDAVQVPVVPKYISSTQQASGTTLRNIFNSRGDDISNYKPMCWKCKCGDFLFNP
The following text describes a protein:
Function:
Essential component of the TIM23 complex, a complex that mediates the translocation of transit peptide-containing proteins across the mitochondrial inner membrane.
Subcellular Localization:
Mitochondrion inner membrane; Single-pass membrane protein.
Sequence:
MKIKEEEKILIDIYKVLNMSTLVRRKLIRSNLYTSFNQSPQEVKIIKQKTFLLPQKVDDKLTIVFDLDETLIHTHVTSQNLSDDLITIEFQGKQYFVSVRPGARELLKSLAGKYELILFTASTEGYATQIINNLERDGQIFDYKLYCHNCKEKFGQLFKDVHKLGRDLDRVLIFDDSTIVWTTSENLFVCKRYEGGNEDNEIETIKKVIEEFKRTRSSQSVVRFIL
The following text describes a protein:
Function:
Involved in the regulation of gamete interactions during the double fertilization and to prevent multiple-pollen tube attraction; mediates the redistribution of the gamete fusogen HAP2/GCS1 to the cell surface after secretion upon sperm arrival.
Subcellular Localization:
Cytoplasmic vesicle. Secreted. Note=Secreted via vesicle exocytose upon sperm arrival, especially in the apical region of the degenerating synergid cell.
Sequence:
MATKSTSKPLLLSFLMMSYLISTFHVITVAEGRTLQFTKMATDHSGAGNLMDCWNAGLELKSCTDEIVKFFLSQTGTSEPPVKGGIDKDCCGAIGLVVKDCWSVMFTSLGLTTMEGNNLREYCEFQAEKSELSPSPAPETLALSPVEITYPGLDY
The following text describes a protein:
Function:
Dispensable for autophagy but essential for efficient targeting and degradation of biosynthetic and endocytic cargo to the vacuole. Required for seedling development and plant growth as well as for seed storage proteins (SSPs) vacuolar trafficking. Controls multiple aspects of development by affecting late endosome morphology and by regulating vacuolar and endocytic cargos (e.g PIN1 and PIN2) trafficking and distributions (e.g. polarity), thus influencing auxin transport orientation.
Subcellular Localization:
Late endosome membrane; Peripheral membrane protein. Endosome, multivesicular body membrane; Peripheral membrane protein. Prevacuolar compartment membrane; Peripheral membrane protein. Cytoplasm. Endosome. Note=Colocalizes with and mobilizes VPS29 at late endosomes, probably in a PI3K complex-dependent manner.
Sequence:
MERVSERSLSENLRRSDREDGKIIEWEEFDHELTRLWSLSSAMKLATERKQILQPKLESLIQVSTESLRRTNELEEMRQRLEARKLLVDKTSVACKVTEQDVKKKEENLSTEVRSLLVGGTTLSIAKSKLQESNCQLEGESGYAHLKIVTNKLRKRQQFMVSQVSFIYPLKIEAGPSQDQELESFPGGSRLGTKPLSQGSVRILGLPFSMAPFTKMSFFTDKKEVQKSATALGYVAHAVSLIAPYLRVPIRYPLCLGGSKTYIRDYAPYIEPSPSDMSPITTLSQNINFVEFPLFLDGQDTTRAAYAVFLLNKNIEQLLNFVGENSLGPRQVLANLKELIRIIQSPDYIDYL
The following text describes a protein:
Function:
Involved in the biosynthesis of tetrahydrobiopterin, an essential cofactor of aromatic amino acid hydroxylases. Catalyzes the transformation of 7,8-dihydroneopterin triphosphate into 6-pyruvoyl tetrahydropterin.
Sequence:
MAPPAARLARLSRTASFSACHRLHSKSLSDEENLKLFGKCNNPNGHGHNYKVIVTVRGEIDPVSGMVINLTDLKEYMQQAIMEPLDHKNLDKDVPYFAEVVRWVEVWGAAGSGCSLRGSDLSWGSAVSAIADGSESAAVSLSAPQRTLQCSSGKTSRGSCLRECFIKSKCMKRTRTLWSIKEKKQFLRGEMSRSSAGQKLTPAHVSDTVSPACCVLKQSLGYALQKNQPR
The following text describes a protein:
Function:
Kinetochore- and microtubule-binding protein that plays a key role in spindle assembly. ZNF207/BuGZ is mainly composed of disordered low-complexity regions and undergoes phase transition or coacervation to form temperature-dependent liquid droplets. Coacervation promotes microtubule bundling and concentrates tubulin, promoting microtubule polymerization and assembly of spindle and spindle matrix by concentrating its building blocks. Also acts as a regulator of mitotic chromosome alignment by mediating the stability and kinetochore loading of BUB3. Mechanisms by which BUB3 is protected are unclear: according to a first report, ZNF207/BuGZ may act by blocking ubiquitination and proteasomal degradation of BUB3. According to another report, the stabilization is independent of the proteasome.
Subcellular Localization:
Nucleus. Chromosome, centromere, kinetochore. Cytoplasm, cytoskeleton, spindle. Note=Localizes primarily to the nucleus in interphase, concentrates at kinetochores prior to nuclear envelope breakdown and during early prometaphase, and disappears from kinetochores upon microtubule-binding.
Domain:
The GLEBS region mediates interaction with BUB3; The microtubule-binding region is required for efficient loading of BUB3 onto kinetochores and proper mitosis; Mainly composed of disordered low-complexity regions outside of the C2H2-type zinc fingers. Coacervation depends on hydrophobic and aromatic Phe and Tyr in the disordered low-complexity region, that may promote coacervation by forming intermolecular hydrophobic interactions.
Sequence:
MGRKKKKQLKPWCWYCNRDFDDEKILTQHQKAKHFKCHICHKKLYTGPGLAIHCMQVHKETIDAVPNAIPGRTDIELEIYGMEGIPEKDMDEGRRLLEQKTQESQKKKQQDDSDEYDDDDSAASTSFQPQPVQPQQGYIPPMAQPGLPPVPGAPGMPPGIPPLMPGVPPLMPGMPPVMPGMPPGLHHQRKYTQSFCGENIMMPMGGMMPPGPGIPPLMPGMPPGMPPPVPRPGIPPMTQAQAVSAPGILNRPPAPTATVPAPQPPVTKPLFPSAGQMGTPVTSSSTASSNSESLSASSKAPFPSTAQAQVAVQGPVGTDFKPLNSTPATSTEPPKPTFPAYTQSTASTTSTTNSTAAKPAASITSKPATLTTTSATSKLIHPDEDISLEERRAQLPKYQRNLPRPGQAPIGNPPVGPIGGMMPPQPGIPQQQGMRPPMPPHGQYGGHHQGMPGYLPGAMPPYGQGPPMVPPYQGGPPRPPMGMRPPVMSQGGRY
The following text describes a protein:
Function:
Histone H1-like DNA-binding protein involved in the organization and segregation of kinetoplast DNA (kDNA). The mitochondrial DNA of kinetoplastid protozoa consists of about 5,000 minicircles and 20 to 30 maxicircles. These circular DNAs are held together by catenation into a highly organized compact disk structure referred to as a kinetoplast DNA (kDNA) network. Binds preferentially to a specific fragment of minicircle DNA and is able to compact kDNA networks through DNA charge neutralization and condensation.
Subcellular Localization:
Mitochondrion matrix, kinetoplast. Mitochondrion matrix. Note=Present both within the kDNA disk and in the mitochondrial matrix at opposite edges of the kDNA disk.
Sequence:
MLRFVPRRLAIGAYTLFMMEQKNNPKLKGLKIADRGKMTSKLYKALNPNDKAALEKRAAAHPGFKRKEKEPKELKAAKAAKTSTPRAPSEYAKFVQANIGRFEKLPHLDRMKAVAKLWKQQQMRTGKP
The following text describes a protein:
Function:
Nuclease that specifically cleaves and resolves four-way DNA Holliday junctions into linear duplex products.
Sequence:
MIICSVDIGIKNPAYAIFNYDNTSNTIKLIAIEKSDWTKNWERSVARDLTRYNPDVVILEKQGFKSPNSKIIYFIKGFFYNSNTKVIVRNPTFKGGSYRNRKKQSIDVFIQKISEYTDYKNDILNKYTKLDDIADSFNLGLSYMESLLKKCKISKD
The following text describes a protein:
Function:
Ubiquitin-binding adapter that links a subset of NEDD8-associated cullin ring ligases (CRLs) to the segregase VCP/p97, to regulate turnover of their ubiquitination substrates.
Subcellular Localization:
Nucleus.
Sequence:
MSLRKPCGEVGEGVPCVSVLLFGGSGGGGKMAAHGGSAASSALKGLIQQFTAITGASESVGKHMLEACNNNLEMAVTMFLDGGGIAEEPSTSSASVSTVRPHTEEEVRAPIPQKQEILVEPEPLFGAPKRRRPARSIFDGFRDFQTETIRQEQELRNGGAIDKKLTTLADLFRPPIDLMHKGSFETAKECGQMQNKWLMINIQNVQDFACQCLNRDVWSNEAVKNIIREHFIFWQVYHDSEEGQRYIQFYKLGDFPYVSILDPRTGQKLVEWHQLDVSSFLDQVTGFLGEHGQLDGLSSSPPKKCARSESLIDASEDSQLEAAIRASLQETHFDSTQTKQDSRSDEESESELFSGSEEFISVCGSDEEEDIENLAKSRKSPHKDLGHRKEENRRSLTEPPARTEPGTATNHQGLPSVDSEILEMSPEKSDGVVEGIDVNGPKAQLMLRYPDGKREQITLPEQAKLLALVKHVQSKGYPNERFELLTNFPRRKLSHLDYDITLQEAGLCPQETVFVQERN
The following text describes a protein:
Function:
Involved in the processing of the 20S pre-rRNA. Required for survival upon K1 Killer toxin exposure.
Miscellaneous:
MISCELLANEOUS: Present with 1460 molecules/cell in log phase SD medium.
Subcellular Localization:
Nucleus, nucleolus.
Sequence:
MGTAKQNQNRKKFTREYKVKEIQRSITKKTRLRKEYLKALKDEGYAVPEKEPKTVAKESVRKIKEARAIEGKKKLDEKKEIKKQRKRMQKDELNKQRNEQLERIRVSKEKFQRREDRKKKLTQRTRTGQPLMGPKIEDLLDKIKTDDTYTS
The following text describes a protein:
Function:
Involved in beta-(1-->2)glucan export. Transmembrane domains (TMD) form a pore in the inner membrane and the ATP-binding domain (NBD) is responsible for energy generation.
Sequence:
MLEVKDINLFYGAAQALRGVSIAAEPGKVTCVLGRNGVGKTSLLRAMVGQYPISSGAIVFDGSDITGLKPYERARKGIGFVPQGREIFPLLTVEENLKTGFGPLKREDRHIPDDVFSLFPVLQSMLGRRGGDLSGGQQQQLAIGRALVMRPKLLLLDEPTEGIQPSIIKDIGRAISYLRNLGNIAIVLVEQYLDFACELGDSFAVMDRGAVKFTCDRTNLDASEISRQMAL
The following text describes a protein:
Function:
Mediates bacterial resistance to the antibiotic spectinomycin but not streptomycin.
Sequence:
MSNLINGKIPNQAIQTLKIVKDLFGSSIVGVYLFGSAVNGGLRINSDVDVLVVVNHSLPQLTRKKLTERLMTISGKIGNTDSVRPLEVTVINRSEVVPWQYPPKREFIYGEWLRGEFENGQIQEPSYDPDLAIVLAQARKNSISLFGPDSSSILVSVPLTDIRRAIKDSLPELIEGIKGDERNVILTLARMWQTVTTGEITSKDVAAEWAIPLLPKEHVTLLDIARKGYRGECDDKWEGLYSKVKALVKYMKNSIETSLN
The following text describes a protein:
Function:
Arginine hydroxylase that mediates hydroxylation of 'Arg-111' of NDUFS7 and is involved in the assembly of mitochondrial NADH:ubiquinone oxidoreductase complex (complex I, MT-ND1) at early stages. May also have methyltransferase activity.
Subcellular Localization:
Mitochondrion.
Sequence:
MLRPAGLWRLCRRPWAARVPVENLGRREVTSGVSPRGSTSPRTLNIFDRDLKRKQKNWAARQPEPTKFDYLKEEVGSRIADRVYDIPRNFPLALDLGCGRGYIAQYLNKETIGKFFQADIAENALKNSSETEIPTVSVLADEEFLPFKENTFDLVVSSLSLHWVNDLPRALEQIHYILKPDGVFIGAMFGGDTLYELRCSLQLAETEREGGFSPHISPFTAVNDLGHLLGRAGFNTLTVDTDEIQVNYPGMFELMEDLQGMGESNCAWNRKALLHRDTMLAAAAVYREMYRNEDGSVPATYQIYYMIGWKYHESQARPAERGSATVSFGELGKINNLMPPGKKSQ
The following text describes a protein:
Function:
Probably plays a role in facilitating the assembly of multimeric protein complexes inside the ER.
Subcellular Localization:
Endoplasmic reticulum lumen.
Sequence:
DTAEAYLGKKINDAVVTVPAYFNDAQRQATKDAGVIAGLNVARIINEPTAAAIAYGLDKKGGEKNILVFDLGGGTFDVSILTIDNGVFEVLATNGDTHLGGEDFDQRIMEYFIKLIKKKYNKDINKDNRALGKLRREAERAKRALSNQHQVRVEIESLFDGTDFSEPLTHARFEELNNDLFRKTMGPAKKAMEDAGLEKSQIHEIVLVGGSTRIPKVQQLLKDYFNGKEPNKGVNHDEVVAFGAAVQGSILSGEGGDETKGSVLFH
The following text describes a protein:
Function:
Widely expressed membrane-bound protein which acts as a ligand to stimulate an activating receptor KLRK1/NKG2D, expressed on the surface of essentially all human natural killer (NK), gammadelta T and CD8 alphabeta T-cells. Up-regulated in stressed conditions, such as viral and bacterial infections or DNA damage response, serves as signal of cellular stress, and engagement of KLRK1/NKG2D by MICA triggers NK-cells resulting in a range of immune effector functions, such as cytotoxicity and cytokine production.
Miscellaneous:
MISCELLANEOUS: Recognized by antibodies in the sera of some organ transplant recipients and may be a target molecule in allograft rejection; MISCELLANEOUS: [Isoform 2]: Found in about 10% of examined clones.
Subcellular Localization:
Cell membrane; Single-pass type I membrane protein. Cytoplasm. Note=Expressed on the cell surface in gastric epithelium, endothelial cells and fibroblasts and in the cytoplasm in keratinocytes and monocytes. Infection with human adenovirus 5 suppresses cell surface expression due to the adenoviral E3-19K protein which causes retention in the endoplasmic reticulum.
Sequence:
MGLGPVFLLLAGIFPFAPPGAAAEPHSLRYNLTVLSWDGSVQSGFLTEVHLDGQPFLRCDRQKCRAKPQGQWAEDVLGNKTWDRETRDLTGNGKDLRMTLAHIKDQKEGLHSLQEIRVCEIHEDNSTRSSQHFYYDGELFLSQNLETKEWTMPQSSRAQTLAMNVRNFLKEDAMKTKTHYHAMHADCLQELRRYLKSGVVLRRTVPPMVNVTRSEASEGNITVTCRASGFYPWNITLSWRQDGVSLSHDTQQWGDVLPDGNGTYQTWVATRICQGEEQRFTCYMEHSGNHSTHPVPSGKVLVLQSHWQTFHVSAVAAAAIFVIIIFYVRCCKKKTSAAEGPELVSLQVLDQHPVGTSDHRDATQLGFQPLMSDLGSTGSTEGA
The following text describes a protein:
Function:
Regulatory subunit of the condensin complex, a complex required for conversion of interphase chromatin into mitotic-like condense chromosomes.
Subcellular Localization:
Chromosome. Cytoplasm.
Sequence:
MSSFTSTPLRKSDASRLFRTPQSVVVREAANDDEAERRSRRSEVTLNDSTSAVEENENIKMCLKLYSDNKMSKENAWSLTIIDSFATLMSRHSKSLQNFQVAGSTLEASTKVYGLRVDSVHTDVMRMCSELTRQTARAMNNNAADQDDEEAGGEGNAGDQSMVEGGDGGGNKENEQTVTQQPKARKKRTRKVVSTITKSKDSINGPLDTNPFMDPFFAKLNSVVGDVNSSSRLMQNIVPTKQSELRLGMDYAFWDPAPSPELDLDGVPEAYEGLECSTMRFLPLGPNNLLRTLRSGYLITDAPAEADEDEEDARTNRTSLDAHMDDVEARDHSAALLNRSALDVHFDINAEVEPVPSGDAFILDYDAKDIDGNDDFAEDDELALEQCKGLMRKTVVIEDMRPLDTTSSHLEYSYRPLDNISQFWAGPAHWKFKRSMRPRSTMAPPPSDTASQTSSTTAKGRAVGRRKKTFEPDTLDDVLSVTETLFQEYNPNRPIRGITHLKSLVCKKWESKKLKLPTDYKIDPKRFDLYKYARGLSMPDYGAPNHAPSEEYNCDGGDDQISCSNDTNDGGDNDMMMNHDDGGFSQMDHDNGGPVEEQHEKDKTMNATVGLEAISTEFLGAPDKVHKINIAYAKTAKVIDMKQLKYNCWRVISSHVQAEVGPPPTQQPAASQQPDVTMPPPTQPEETRITFSALYRKVPQLLSKTMSENISKSLAFYAVLHLANEKSLLLGRQEDLNDFTIRKEDDGDAD
The following text describes a protein:
Function:
Involved in pre-mRNA splicing and required for cell cycle progression at G2/M.
Subcellular Localization:
Cytoplasm. Nucleus.
Sequence:
MSVTATSHDILKSIDDSILPPEDTLSEAMYNNVKLDHYFNKLPKSSEENNINDQTNQLIVSAAPESEDSPAAEWKLLRTLAGAHQGWIRAIALDEITNKWYVTGSADSTIKIWDFENNSLKAVLTGHVLGIRSLCISKRHPYLFSGGEDKSLRCWDLERSNSDAGCQIRSYHGHLGGVYSIGLHPELDVLFSGGKDCVVRVWDIRSRVEAMTLLGHTNDITSIETDYNDPQVITSSMDGTIRLWDLRKSKTELLITNHSKSIRSMKSHPKEATFVSGDSNGEIKQWLLPKGELLNEFGTSQLSPNQRDNSRIINTLAINPVTNTLFSGYDDGKLEFYNYTTGNLQQSGQSPSLAGPEQSAIYASTFDMSGLRLLTCHGDKSIRIWGTSY
The following text describes a protein:
Function:
Hydrolyzes the ester bond at the sn-1 position of glycerophospholipids and produces 2-acyl lysophospholipids, being phosphatidylinositol (PI) its major substrate. PI is a versatile lipid that not only serves as a structural component of cellular membranes, but also plays important roles in signal transduction through distinct phosphorylated derivatives of the inositol head group. Catalyzes the hydrolysis of phosphatidylcholine at sn-2 position in vitro. Regulates asymmetric division, an important property of stem cells in C.elegans, by controlling the subcellular localizations of beta-catenin.
Sequence:
MSGSEEEHLVSLTFRKNEEDMDEDEGKVKQKEKPKEKQMEFVNQNFVESTEDESEVSTPTAVGLPIGTSTPDGDETPTQPDPNGKYTMAQTKDADLSRPSGLPSNGNPGSSTTVPPASKSGPVAPPRPSGTPVAPQRNRRRKVTELKCSEVRWFFQEPKGTLWNPFNGRDSIMLEIKYRKEKGIELDEAMQEIYDESLTHYKMEMKDEPEIENGNIGMEQEKPMVVVMNGQYKVNKDNSKIDPIYWKDDSKEIRRGSWFSPDYQPLEMPLSDQIEKNHLQCFRNQMIPEGTTVFSKSETSNKPVLAELHVDGYDIRWSSVIDISLHQKGNAILRYLWAKSTPLRRGYEKEADWNDAAAEISHLILVVHGIGQKGYENLIAQNANQVRDGVVSAMEKVYPEEKSRPMFLPVEWRSALKLDNGLTDNITIPKMSSMRASLNSTAMDVMYYQSPLFRTEIVRGVVSQLNRTYKLFKANNPQFNGHVSVFGHSLGSVICYDVLTQYSPLMLFDKYVTKSIDEYLKRDDTNASEEARKALEAMKLAREQLRDNLEGGIHKLLVTKEEQLEFKVKYLFAVGSPLGVFLTMRGGESTDLLSKATNVERVFNIFHPYDPVAYRLEPFFAPEYRHIRPIKLFSNTDLRARASYENLPLDVYKHYLKKLKNLNKAKKNKDDKTADARSGGDDENEDEDECDSDEDARSGCSSPRSMTPPPFETAAANAAAAAKETKAVKKGWFSFGTSSNPKKTQSTASLGSVNATSTENIEFAKEAAEELPLAEKILGSGVRVPHRIDFQLQPALTEKSYWSVLKSHFAYWTNADLALFLANVLYCKPLKPEEAKPTWA
The following text describes a protein:
Function:
Demethylates proteins that have been reversibly carboxymethylated.
Sequence:
MCPRLAGAVMPSFASPLDTPFSILPQTVLLLPAQAPTASMEPAPLSSLQEDGEPEESPSSPSPSAFSADAVPPRPATHRSLHKYEPLDWSAYFDEERPVVIPDTEDVFNVYMAGSEGPVVFCLHGGGYSGLSFALAANRIKEKSHVVAMDLRGHGKSTTSDDLDLSIETLTNDVISVIRTMYGDSTPAIILVGHSMGGSVAVHVAARKVFRNLHGLVVVDVVEGTAMASLVHMQKILANRAHHFPNIEKAIEWSVKGGSLRNIESARISVPPTLKYDESRECYTYRTPLEKTEKYWKGWYEGLSDKFLSCPVQKILLLAGTDRLDRALTIGQMQGKFQMVVVRHTGHAIQEDVPEEFASHILTFISRNKIGPNGVEIPGLAKTWQH