lhallee/plat_data huggingface dataset:
The following text describes a protein:
Function:
RNA polymerase that catalyzes the synthesis of short RNA molecules used as primers for DNA polymerase during DNA replication.
Domain:
Contains an N-terminal zinc-binding domain, a central core domain that contains the primase activity, and a C-terminal DnaB-binding domain.
Sequence:
MVGEYVRLTPAGKGRLKGLCPFHKEKTPSFQVDTEKGYYHCFGCKASGDVFGFVQQMEHLSFGDALRKLADRAGIQIDAKYGEKVSRDLYEVNAFALDYFRSHLPGPALDYLRGRGLSDETIAAFELGYAPDGWDGLLKLARTKGVSEKQLLEAGLLTENPENGRVYDRFRGRVMFPIRDHLGRLVGFGGRVLDDSKPKYLNTPETAAFKKGELLYGLDKARSGLGGGAELVVVEGYMDVISMHQHGFTGAVASLGTALTAEHAQLLERLGAQSIVLMFDQDGAGLKATLAGLDQVIGAKFRVRATSVPSGKDPADALLAGDDAGIREALAGGLDEVKYRVQAATEKYGVDTNEGKRRVLMELLPRMQNLDPLDAIAQDMRGAACELLGIRPEALLDWITSKAKRRTLTDTHLAGMSQSSGEEEHELALLRQLLVDPSLLAKLDGSLPWRNEAVRKVMLAAQGARSPDDILDIFRGQPEEQLLIRLMFEGRDSGSLSRASSQEYEQKVTTYAAHAVDDIQVTLNIDALKTEVDLLKKQLLSTPPAEQLALLSQIQELQRAIEAEKRARRGS
The following text describes a protein:
Function:
Stabilizer subunit of the dolichol-phosphate mannose (DPM) synthase complex; tethers catalytic subunit to the ER.
Subcellular Localization:
Endoplasmic reticulum membrane; Multi-pass membrane protein.
Sequence:
MTKLLEWLTVSAVLSLIWAALVTDSLSFQVSDQIKDVLMPITILQSLTYISPYTTINNDNVTAANDRIRVTAYLPIDCLRCKYAVDILVRTCYSLASVGYGVMTFNDCIEAHNSLKMEVSEAIDDLKKKGLTM
The following text describes a protein:
Function:
Functions in the biosynthesis of the anionic phospholipids phosphatidylglycerol and cardiolipin.
Subcellular Localization:
Mitochondrion.
Sequence:
DTTSLVATPSEFHSQLCHKIRHAKDRVVLASLYIGSTIQCKEDELLQALQITASNPNVQKIQVLLDANRAMRKVSYTMTTATNSNKHSAQFHERTSVFLFQVKDERLCSILPSPLDEVAGVFHIKAYIVDNELILSGANLSEEYFTNRLDRYMLFTNGEWLVDFYANLCEVLSSYSIRYKGEPENSPSPSFIFSSQDEQCRKEQLESSLMKLFDGSKHSNESNDSKDTIAYAIPTFQMPNSFLQRPLNLPSDTKMTRELLLTASKYDQSASVRLSSAYLNLTPRLLSALTTFGAPYILTAGMISHGFAPKPKIKASIPEAFLTLVKETAVSILAKGGKVLMYERLGWTFHAKGVWITAGDDKRQAIGDPDTIIGSGNYGARSEDLDVESNCIIVFNDSTTD
The following text describes a protein:
Function:
Plays a role in the regulation of phosphate uptake.
Subcellular Localization:
Cytoplasm.
Sequence:
MPKKFEEILKEVENDLIEMAELCAEQTENAVKAFIESDRELAKQVRKRDTTIDLMEMKIEEKCIKAIALYQPVSGDLRELMTAIKISSKLEKVGDNASKICKILLKSDVEGNRKNELLIVMKDYLINMLKNAMIAFKTRDESLARDVYNMDKRLDDLYEQLYRSMISKIIENPKNLTLYTEIIFAGKYLERSGNIVASIGDRIVYMITGERIKEEEIEEELKKEKDIEKNIDQIND
The following text describes a protein:
Function:
Mediates both low-affinity uptake and efflux of sugar across the membrane; Mediates both low-affinity uptake and efflux of sugar across the plasma membrane.
Subcellular Localization:
Cell membrane; Multi-pass membrane protein.
Sequence:
MTWVIEPGVKTALGVIGNITALGLFLAPVKTFVRILRVRGVEDFSCLPYLVTFLNCSLWTFYGLPVVTRSAILVATINAVGTALALSYCLIYITHAPPPQQRRTGALLAAEGLGLAAVVLIVLLAFPFHMRTTVVGIVAVVVTIGMYCAPLGKLRQVVRDRSVEYMPFLLSLNVLLNATAWTVYAVYAHDIYVLIPNALGVLLGTAQLVLYAWYCKERPAPVADTESGRGGSSTRGGAALHKNLSARQLLGRTLSTGEKGGGEEIEIGNGLDSK
The following text describes a protein:
Function:
Absolutely required for transposition of IS1.
Sequence:
MWIAVDRVGKKFINCSFGSRGTKTGQLLWEKLKKKEIREVVTDHWRAYAEFIPENIHTQSKAETYTVEGYNGILRHFLPRLRRKTKCYTKSLEMLKYSVLLLMKHRNKKLSIFN
The following text describes a protein:
Function:
Constituent of pre-60S ribosomal particles. Required for large subunit rRNA maturation, in particular processing of the 27S pre-rRNA at the A3 and B1 sites to yield 5.8S and 25S rRNA.
Miscellaneous:
MISCELLANEOUS: Present with 6200 molecules/cell in log phase SD medium.
Subcellular Localization:
Nucleus, nucleolus.
Sequence:
MGSKHRVDTKDKKRTRKNAEFGREKRNSGNQELSNEPEKDTIMEGDEAEEDEQNSSSDESSKIIDNEQSDAEEDDDEEEEDDDFPRKKKSKNSKHDDGSTGFSAAVNAILSSHLKAYDRKDPIMARNKKVLKQSESEKLEYKAKKALLAEKKKLLGKARKTDIIPIASGEDRSENIRKVLEKETALRKIAQKGAVKLFNAILATQVKTEKEVSENLSEIKNKEEKKELITEVSKEKFLDLVKAAAGSDNE
The following text describes a protein:
Function:
Mediates the voltage-dependent sodium ion permeability of excitable membranes. Assuming opened or closed conformations in response to the voltage difference across the membrane, the protein forms a sodium-selective channel through which Na(+) ions may pass in accordance with their electrochemical gradient.
Subcellular Localization:
Cell membrane; Multi-pass membrane protein.
Sequence:
MASPNNLTYFTRKSLTKEYRADRKKDEEEEELEPSSDLEAGEQLAFIYGDVPSEMVSEPLEDLDPYYKDKKTFLVLNEGRIIFRFSATSALYILTPFNLIRRLCIKVLVNLYPFAKIHWQGCLSVIIDMSFFHLMYLWILAFSLPFLGLYTFEILIKILARGFCIGPFTFLSDPWNWFDIPILTMALFVNLGSFPYLGIFSVLRIMKAVSLNIGKSVVRTLTQSMKMFQQTVMLIVFCLSVFAVMGMQLFMGKLKQKCVINKLFHSYSFQIDYFYYLEGQKDALLCGNSSYSGDCPEGYMCVKAGMNPDHNYTSFDHFGWSLLTLFRLMTLDCWENLYQQILRAAGKTYVIFFIVVLLFCSFYLVTLILAMVILAYEKQNQITIKAAKRRQIKYQAMSYWHKRKVKQGRTARKEQEERQIDFCCISKDILDDPTIRSTCTNWWHRFGTTFTIWNCSTLWIKFKDFIYAVVMDPFFDLAIAICIIINITFMAMEHYPMTEKFYNVLSVGYLVFIGIYIAEMFLKIIALHPYNYFQRGWNIFDTVIVILALADIYMKEAYGLSLFGWFRLLLVFKVAKYWPTWEKLIKIINYSVDALKGLFLLLFITMFTFAVVGMKLFGQGCQEYLCKTDVDCPFKRWHMHDFFHSFLLMFRVLCGEWIDSMWDCMNTEGQKECLIFFVVVIIIGKMQLLVLFVALLSSFSPENFAAIQVSPESNNLQLAMARIQKGIYYVKRTLFDLVAKGFSKKQMISNDIQGEENLNLEKRNHTINGMSKKIWESQDRLHSNGCRLEKYVRDKSHFPSLVPNSNYSTLAPIALGESDFENVIKEARNELDIGSSKEVTNITGFYIYNFLLLSFNIGKQCGCIRRFPYCKASKKSRKGKIWWNLRKTCYRTVNHGCFEISIVFIVLLSCFALIFEDIYIEKRKTIKIILEYGNMIFTYIFILEMLLKWMAYGYKTYFSNVWCWLEFLVVNVCIIHLLQMLSTNNHLLKTFYTPEIMMVVLHIFLKAIPSILEALLVWLICWLLFSLMGVNLFAGKFFKCINITTGERLPWTLIIDVIDCKMLSNSSGDVQWKNPKANFDNIGNGYFSLLQLLLHEITIFNKQPKNESNVYIYLYFVIFVILGLCFPFVFFVRVVINHLKQQIIFVTLMIIPLLQNKFQGYIFDLITKEAFEITIIVLICLNTVVMMVETDTQDTYKRNILYQINLVFIGLFAGECLLKLIGLRLYYFTIGWNIFDFVVIHLSIMVVLLPHLTVKYLLTYSQVQVIRLIRCGRVLNFIKGTKVLGPLIYALMLSLPTLLNIVLLLLLIMFIYAILGMSHFAYIKKDAGINDMFNFETFGNSMLCLFQITTFAGWNGLLEPVLSTGPPDCDPEKIHPGSSVKGDCGSPSFGVFYFVSYIIISFLVLVNLFIVVILEICNVVTEENAQLLSEEVFDNFYEVWKQFDPDGTHFIDYSQLSEFAASLDPPFLIAKPNKIQLTAMDLPMVKGDRVFCADVLIAFTKCVMRESEEFNHICLPLRKHFLSSCLFQVSYEPVTTTLKRKQEEVSALVIQRAFRRFCLRQNESGIYNIKGEAREKLTIEEAIVIDKIPENSTLEKVSFLSPPSNSLYLDSVIEIVSQI
The following text describes a protein:
Function:
Acts as a cytosolic iron-sulfur (Fe-S) cluster assembly factor that facilitates [2Fe-2S] cluster insertion into a subset of cytosolic proteins. Acts together with the monothiol glutaredoxin GLRX3.
Subcellular Localization:
Cytoplasm. Nucleus.
Sequence:
MASAKSLDRWKARLLEGGSTALTYALVRAEVSFPAEVAPVRQQGSVAGVRAGVVSLLGCRSSWTVAMELSAEYLREKLQRNLEAEHVEVEDTTLNRCACSFRVLVVSAKFEGKPLLQRHRLVNACLAEELPHIHAFEQKTLTPDQWARERQK
The following text describes a protein:
Function:
Coreceptor required for the peroxisomal import of proteins containing a C-terminal PTS2-type peroxisomal targeting signal, such as 3-oxoacyl-CoA thiolase. Acts via its interaction with PEX7, promoting association between PEX7 bound to cargo proteins and the PEX13-PEX14 docking complex. PEX20 along with PEX7 and PTS2-containing cargo proteins are tranlocated into peroxisomes by passing through the PEX13-PEX14 docking complex. PEX20 coreceptor is then retrotranslocated into the cytosol, leading to release of bound cargo in the peroxisome matrix, and reset for a subsequent peroxisome import cycle. Also mediates peroxisomal import of proteins that do not contain PTS1- or PTS2-type peroxisomal targeting signals, such as acyl-CoA oxidases (Aox) izozymes (By similarity). Import of acyl-CoA oxidases (Aox) izozymes is independent of PEX7 (By similarity). Required for PEX7 ubiquitination.
Subcellular Localization:
Cytoplasm, cytosol. Peroxisome matrix. Note=Cycles between the cytosol and the peroxisome matrix. Following binding to cargo proteins in the cytosol, recruited to the docking complex, composed of PEX13 and PEX14, leading to translocation into the peroxisome matrix along with cargo proteins. Export and recycling to the cytosol is initiated by binding to the PEX2-PEX10-PEX12 retrotranslocation channel. Cys-8 of PEX20 is then monoubiquitinated by PEX2, promoting its extraction from peroxisomal membrane by the PEX1-PEX6 AAA ATPase complex. Extraction is accompanied by release of bound cargo in the peroxisome matrix (By similarity).
Domain:
The WxxxF/Y motifs mediate interaction with PEX14, promoting association with the PEX13-PEX14 docking complex.
Sequence:
MFTSNGSCGPATALDNLSKRVGQDRTLENDHVARFRDQNSSQNRAFRAESSFNTTAGAEFGQFQNTSVQRNYFPSAELIRKNTRFGDNWSSEFRQQQENNKWVEDFGAMNLENVRMEQEQSFQTMDQRTNMQAMSSTANAWTQEFNHMQHNKEMEYEMRIRETQRLVNAPAREVFSMVNQHSQQHNQNFTHNQTQLGDQSHYMTNLAFERQFETVQNEIDGMDMFSDSEQVEQQKELQKEDDNNDIETTKFAEIAQQVFNQMNNVDTTVSQNTEHKFKQSNFLRLMDKVAQREVEINGSGDRFIDKTGNDIRDYLPDPLSDLR
The following text describes a protein:
Function:
Iron-sulfur subunit of the cytochrome bc1 complex, an essential component of the respiratory electron transport chain required for ATP synthesis. The bc1 complex catalyzes the oxidation of menaquinol and the reduction of cytochrome c in the respiratory chain. The bc1 complex operates through a Q-cycle mechanism that couples electron transfer to generation of the proton gradient that drives ATP synthesis.
Sequence:
MPGRPAPSRRTVLRSAAATPVAGLGLAACSPGDDGAAPARPTAPVDLGADGDVAKGATKLFPDGNVVVSRAADGSLKAFSTVCTHAGCPIRKLEGTKLVCNCHGSEFDARTGEVLHAPATVPLVELPVSVEQGRIVASPGT
The following text describes a protein:
Function:
This enzyme scavenges exogenous and endogenous cytidine and 2'-deoxycytidine for UMP synthesis. Functions as a conventional cytidine deaminase. Has no affinity for RNA and is not involved in RNA-editing by C-to-U deamination.
Sequence:
MDKPSFVIQSKEAESAAKQLGVSVIQLLPSLVKPAQSYARTPISKFNVAVVGLGSSGRIFLGVNVEFPNLPLHHSIHAEQFLVTNLTLNGERHLNFFAVSAAPCGHCRQFLQEIRDAPEIKILITDPNNSADSDSAADSDGFLRLGSFLPHRFGPDDLLGKDHPLLLESHDNHLKISDLDSICNGNTDSSADLKQTALAAANRSYAPYSLCPSGVSLVDCDGKVYRGWYMESAAYNPSMGPVQAALVDYVANGGGGGYERIVGAVLVEKEDAVVRQEHTARLLLETISPKCEFKVFHCYEA
The following text describes a protein:
Function:
Component of clathrin-coated vesicles. Component of the aftiphilin/p200/gamma-synergin complex, which plays roles in AP1G1/AP-1-mediated protein trafficking including the trafficking of transferrin from early to recycling endosomes, and the membrane trafficking of furin and the lysosomal enzyme cathepsin D between the trans-Golgi network (TGN) and endosomes.
Miscellaneous:
MISCELLANEOUS: [Isoform 3]: May be due to intron retention.
Subcellular Localization:
Cytoplasm. Cytoplasm, perinuclear region. Cytoplasmic vesicle, clathrin-coated vesicle. Note=Co-localizes with AP1G1/AP-1 in the cytoplasm. Recruited to the perinuclear region by AP1G1/AP-1.
Domain:
The WXXF motifs mediate binding of accessory proteins to the ear-domain of AP-1, GGAs and AP-2 through hydrophobic interactions. Selective binding to the GAE domains of AP-1 or to the alpha-ear domain of AP-2 is tuned by the acidic context surrounding the motif and the properties of the second residue of the motif itself (By similarity).
Sequence:
MEPDIIRMYSSSPPPLDNGAEDDDDDEFGEFGGFSEVSPSGVGFVDFDTPDYTRPKEEFVPSNHFMPIHEFSENVDSLTSFKSIKNGNDKDITAELSAPVKGQSDVLLSTTSKEIISSEMLATSIDGMERPGNLNKVVEQRQNVGTLESFSPGDFRTNMNVVHQNKQLESCNGEKPPCLEILTNGFAVLETVNPQGTDDLDNVADSKGRKPLSTHSTEYNLDSVPSPAEEFADFATFSKKERIQLEEIECAVLNDREALTIRENNKINRVNELNSVKEVALGRSLDNKGDTDGEDQVCVSEISIVTNRGFSVEKQGLPTLQQDEFLQSGVQSKAWSLVDSADNSEAIRREQCKTEEKLDLLTSKCAHLCMDSVKTSDDEVGSPKEESRKFTNFQSPNIDPTEENDLDDSLSVKNGDSSNDFVTCNDINEDDFGDFGDFGSASGSTPPFVTGTQDSMSDATFEESSEHFPHFSEPGDDFGEFGDINAVSCQEETILTKSDLKQTSDNLSEECQLARKSSGTGTEPVAKLKNGQEGEIGHFDSVPNIQDDCNGFQDSDDFADFSSAGPSQVVDWNAFEDEQKDSCSWAAFGDQQATESHHRKEAWQSHRTDENIDTPGTPKTHSVPSATSKGAVASGHLQESATSVQTALLNRLERIFEACFPSILVPDAEEEVTSLKHLLETSTLPIKTREALPESGELLDVWTELQDIHDAHGLRYQWGGSHSNKKLLSSLGIDTRNILFTGNKKQPVIVPMYAAGLGMLEPTKEPLKPLSAAEKIASIGQTATMSPDMNTCTSDQFQESLPPVQFDWSSSGLTNPLDASGGSTLLNLDFFGPVDDSSSSSSTTIPGVDPELYELTTSKLEISTSSLKVTDAFARLMSTVEKTSTSTRKPKREEHLSEEAIKVIAGLPDLTFMHAKVLMFPATLTPSTSSQEKADG
The following text describes a protein:
Function:
Associates with cyclin G and CDK5. Seems to act as an auxilin homolog that is involved in the uncoating of clathrin-coated vesicles by Hsc70 in non-neuronal cells. Expression oscillates slightly during the cell cycle, peaking at G1. May play a role in clathrin-mediated endocytosis and intracellular trafficking, and in the dynamics of clathrin assembly/disassembly.
Subcellular Localization:
Cell junction, focal adhesion. Cytoplasm, perinuclear region. Cytoplasmic vesicle, clathrin-coated vesicle. Golgi apparatus, trans-Golgi network.
Sequence:
MSEFLKSAINYFNATPANGLDNDFVGQTVEVANVKLRIKRVIAEGGFAYVYVAQDVQSNTEYALKRLLGTDKEECNNIIREINFHKQVSGHPNVVKFVAATFIDRTQSANSQRRAEYLLVSELCKGGSLYDCLEQDLAPETVLRVFYQATKAVAHLHSQPKPINHRDIKIENFLIGSDGLLKLCDFGSASTDSYAPDVTWNAQQRDTLEDALTRCTTPMYRAPEQLDTWANYPIGIKMDVWALGCILYCLCYRKHPFEDSAKLRIINANYTIPANDARYACFSDVIRGCLQVDPNQRFDTATVLERLAAIAETKGWPLKAPLGLLGKPLNSPPTGMTPAPSPSHSRPNGGLVPDRPAPPRPVCPPGGPVPVSSDGSLRNKYPQRPPDPVRMGHANAPPLHSVPSPYPTPPAQQFSQPAAPPATGGGGLFSSIKGGAGSFLKNLKDTSSKVMQTVQQSIVRTDLDMSYITQRILVMPCPSEGIESAYRTNNIDDVKLFLDSRYQPTKLSVYNLVGRNGCPRLPPPVRTVDAGFIYAPAPQQGGKAPVLTGLYSLVEDIYGFLSADPKTVVIVQSPDGGRALAATVVCALLVYASLVTEPEDAMQMFAIKRTPPNMRPSELRYLYYLGDIVRSVPHLPHYKPVTLVSLAVTPVPRMTKARDGCRMYVEVATADRTVFCTLQDYERMRLYHTSEGKIALAMNVTVCGDVTISLYHARNALGGMGRPQGLKICQLQFHTGFIPEEETLINYDRAELDEVPDLEHVPQKFSVALSVFVGDSERPPATQPPWRTPKASRDPRTLFASQLEYEENVDNFVTKPSSSARATAGESTAPQKPPPPRPAPPSPQPMHRVLGDDIPRRGSSGTPPVVAAAEEREADLLNLNKSSQGRPAPEESPAPVPKIEETYDLLGGLSPPVVKGGAFAGSGVRSTPTSSAVLDDIFGTLDDAGAPTGSTLPTTKSSSDLSGLNLNFDHFGGVAQPASGAAPFTNGAGQSDASASNANNSFGFDAFAGVAPQSIYNSAAPAGVPSQPAPAAAAASKDPFADIGNLAAGLGGGISAGASAAGWGGKPGTTPSPRSTQFSSPTHQFSGASTANPSPRAPSTPNHQMRSPNDPSQAQSRPDYSRSHFEPPKNGSNGSAKDAPGAGVGGGRSGDIFGDILGQQGYSFGSTKNQGPRTMNDMRKEELVREMDPERVKLMEWTEGKKNNIRALLCTVHTVLWPGAKWTKCEMHQLVSAADVKKIYRKACLAVHPDKHTGTENESMAKMIFMELNNAWTEFESDATQQNLFAN
The following text describes a protein:
Function:
Transcription factor involved in skull and limb development.
Subcellular Localization:
Nucleus.
Sequence:
MNAETCVSYCESPAAAMDAYYSPVSQSREGSSPFRGFPGGDKFGTTFLSAGAKGQGFGDAKSRARYGAGQQDLAAPLESSSGARGSFNKFQPQPPTPQPPPAPPAPPAHLYLQRGACKTPPDGSLKLQEGSGGHNAALQVPCYAKESNLGEPELPPDSEPVGMDNSYLSVKETGAKGPQDRASAEIPSPLEKTDSESNKGKKRRNRTTFTSYQLEELEKVFQKTHYPDVYAREQLAMRTDLTEARVQVWFQNRRAKWRKRERFGQMQQVRTHFSTAYELPLLTRAENYAQIQNPSWIGNNGAASPVPACVVPCDPVPACMSPHAHPPGSGASSVSDFLSVSGAGSHVGQTHMGSLFGAAGISPGLNGYEMNGEPDRKTSSIAALRMKAKEHSAAISWAT
The following text describes a protein:
Function:
E3 ubiquitin-protein ligase.
Subcellular Localization:
Endomembrane system. Endoplasmic reticulum membrane; Single-pass type IV membrane protein.
Domain:
The RING-type zinc finger domain is responsible for E3 ligase activity.
Sequence:
MEEVDGIPRAYIHRACSGKEKPEEKDLSTKSGISDDAASPASSMNGCFDCNICLDFVVDPVVTLCGHLYCWPCIYKWMQVESMSPRQCPVCKASLSQDTLVPLYGRGGQSPVADSEVPHRPTLHRDHAVFTSVVDHRPRGTEDAAYVDRYQPTQQPQFRRHQHDYSGYASLLGTSYTSGGSSSLLFAPLFRSTAGGVLGGLAILPWAQRNHGMNTYYASPYPFASGSNNPRLLRHQMQVESSLHQICLFLFFCALLCLLLF
The following text describes a protein:
Function:
Involved in the biosynthesis of glucosylglycerate. Catalyzes the dephosphorylation of glucosyl-3-phosphoglycerate (GPG) and mannosyl-3-phosphoglycerate (MPG) to glucosylglycerate (GG) and mannosylglycerate (MG), respectively.
Sequence:
MVIFTDLDGTLLNHEDYSFKDAIPSLERIKKKGIPLVIVTSKTKKEVELIQKELGIEEPFIVENGAAVFFPKGYRGFNIRCDQENRYCIIKLGRDYREIRDFIEKIKDKFKIKGFGDMTVEEIVRLTDLPYDRAELAKERDFTEPFIIEDEKDIKDLEEIAEKEGFKITKGGRFYHLIGKGQDKGRAVQIVKKVFEENYGEVPLTVGLGDSRNDIPMLREVDIPILIPHINKKYESVNLPGIIKAEYPGSKGWNESIWRILNEIERGCC
The following text describes a protein:
Function:
Component of the elongator complex which is required for multiple tRNA modifications, including mcm5U (5-methoxycarbonylmethyl uridine), mcm5s2U (5-methoxycarbonylmethyl-2-thiouridine), and ncm5U (5-carbamoylmethyl uridine). The elongator complex catalyzes formation of carboxymethyluridine in the wobble base at position 34 in tRNAs. It functions as a gamma-toxin target (TOT); disruption of the complex confers resistance to Kluyveromyces lactis toxin zymocin (pGKL1 killer toxin). May also be involved in sensitivity to Pichia inositovora toxin.
Miscellaneous:
MISCELLANEOUS: Present with 3870 molecules/cell in log phase SD medium.
Subcellular Localization:
Cytoplasm. Nucleus.
Sequence:
MASSSHNPVILLKRILSLTESSPFILCLDSIAQTSYKLIQEFVHQSKSKGNEYPIVYISFETVNKPSYCTQFIDATQMDFVHLVKQIISYLPAATATQAKKHMVIIDSLNYISTEYITRFLSEIASPHCTMVATYHKDIKDENRTVIPDWNNNYPDKLTLLQFMATTIVDIDVVLTGTLDTEEVSELLNEFRIPRGLNNDIFQLRLVNKRKSGRSLEYDFIVNSNTHEYELLSTTKQEEESSSNGLETPEMLQGLTTFNLGTSNKQKLAKDQVALPFLEAQSFGQGGAIVYEYEKDDDYDEEDPYEDPF
The following text describes a protein:
Function:
Catalyzes the transfer of sulfate to the C2-position of selected hexuronic acid residues within the maturing heparan sulfate (HS). Involved in cell adhesion and guidance by specifically modifying proteoglycans in the extracellular matrix and on the cell surface that are essential for axon migrations.
Subcellular Localization:
Golgi apparatus membrane; Single-pass type II membrane protein.
Sequence:
MLWKKRKVLYFAGISVFILILLLLKLNSKPKANVWPTSSKIVIYNRIPKTGSTTFTNAIAYDLYKENGFSVLHVNMTKNRQVMSLPDQYTFVNNITTWTERLPAFYHGHVAFIDFQRFGIANPIYINIIREPLERLLSHYYFLRYGDNYRIGLKRSRAGNNETFDECYSRGGKDCDMKQMWIQIPYFCGHYHFCTEVGNPEALRVAKQNVLEKYLLVGTTSRMRDMIALLEVTVPDFFKGALGHFDSLDANRAHLRYTKKKIPPNDQTLSMIRRDEVYKMEREFYDFINNLFDAVFKKATNGISKADDLVKLPLQYHFEKIKPS
The following text describes a protein:
Function:
Catalyzes the NADPH-dependent reduction of glutamyl-tRNA(Glu) to glutamate 1-semialdehyde (GSA).
Miscellaneous:
MISCELLANEOUS: During catalysis, the active site Cys acts as a nucleophile attacking the alpha-carbonyl group of tRNA-bound glutamate with the formation of a thioester intermediate between enzyme and glutamate, and the concomitant release of tRNA(Glu). The thioester intermediate is finally reduced by direct hydride transfer from NADPH, to form the product GSA.
Domain:
Possesses an unusual extended V-shaped dimeric structure with each monomer consisting of three distinct domains arranged along a curved 'spinal' alpha-helix. The N-terminal catalytic domain specifically recognizes the glutamate moiety of the substrate. The second domain is the NADPH-binding domain, and the third C-terminal domain is responsible for dimerization.
Sequence:
MSLLVVGLSHRSAPVSVLERASLNADAQLKLLQDTVAAEPAAEAAVLATCNRIELYADVDKFHAGVAELSTLLAQHSGVGLEELTPYLYVHYEDRAVHHLFSVACGLDSMVVGEGQILGQIKDSLARAQDLHTAGRLLNDLFQQALRVGKRAHSETGIDRAGQSLVTFGLEQLSAGADVEQWARGKKALVIGAGSMSSLAAATLARAGVAEIVVANRTFERAERLALLLEEQYGQRLSEGDDTDVLARAVPMDAVPGELTRADVAVSCTGATGLVLTADSVAATVEGRTGAPAVEDTAVQETAVREAGETPLPGAGSAADENCPLDLSSVSSVPSGFSVMGEAAVAGMDAATLEQHGAWAAGGTAVDRTREAGRSGPEADAELIGALAATATRVGRIPERRRPEPVAEAPRPQPVLFLLDLAMPRDVDAAVHRLAGVRLVDIESLADASADAPMAADVDMVRRIVADEVAAFGAAQRAAHITPTVVALRSMAADVVAGEIARLEGRLPGLDDKHRAEITQTVKRVVDKLLHAPTVRVKQLAAEPGGAGYADALRTLFDLDQETVASVSRAENSTEKNRGPA
The following text describes a protein:
Function:
CD2 interacts with lymphocyte function-associated antigen CD58 (LFA-3) and CD48/BCM1 to mediate adhesion between T-cells and other cell types. CD2 is implicated in the triggering of T-cells, the cytoplasmic domain is implicated in the signaling function.
Subcellular Localization:
Cell membrane; Single-pass type I membrane protein.
Sequence:
MSFPCKFVASFLLIFNVSSKGAVSEEITNALETWGALGQDINLDIPSFQMSDDIDDIKWEKTSDKKKIAQFRKEKETFKEKDTYKLFKNGTLKIKHLKTDDQDIYKVSIYDTKGKNVLEKIFDLKIQERVSKPKISWTCINTTLTCEVMNGTDPELNLYQDGKHLKLSQRVITHKWTTSLSAKFKCTAGNKVSKESSVEPVSCPEKGLDIYLIIGICGGGSLLMVFVALLVFYITKRKKQRSRRNDEELETRAHRVATEERGRKPHQIPASTPQNPAASQHPPPPPGHRSQAPSHRPPPPGHRVQHQPQKRPPAPSGTQVHQQKGPPLPRPRVQPKPPHGAAENSLSPSSN
The following text describes a protein:
Function:
Acts in maintaining the cortical microtubules organization essential for anisotropic cell growth.
Sequence:
MSRACRGESSGGGRSSLGYLFEPEPEDIIPDHSTKSVQGTNKAPKGNIVLGDKMASDEADQEHQAAAPLKKEDSNPIVSSRSASNIYHTNQVGNNSGLLITDRPSTRVRCAPGGPSSLGFLFGDEDA
The following text describes a protein:
Function:
Cytoskeletal linker protein involved in tethering membrane bound organelles to the cytoskeleton.
Subcellular Localization:
Cytoplasm, cytoskeleton.
Domain:
The large coiled coil domain may mediate homodimerization.
Sequence:
MIETSFIKWINSFKDLSNSIEDLKELSNGTIFNEICCQIAPKYFDIDSLRKDGLDNWIFREENIKNIVERVDEFYIEEMGLNDQISSINCEEIANENIDEIILLIEAILGMAMESENNEAVIENILSLDQDTQNDLMVVVAKIQQSHQPNTVDNSKSFDKDGSILSQSPSQSNNSISNNNNNNNIDSSNISKSNISSNNNNNNSSNNNKEEILNLQNEIEKLKREKQEIQNDLDESNIQLSNVTMDRDRITIDKQKTEEVCSSLHESIIGLQKQLDETMAQTTTMNALNDETYKTEINDLHMQVESKEKQLSELKKKVDEANRLANENRSLRDEIDILREKAANAEATEEKLKKHQKKIEEIGDLKKKIKELEDQNDSYIQQTLDLEEQLSKNNTYRTQADSGKQQISSLKIELAKLELSLKSIKEDRDKLSESLNTVELERDSLQSQVTNLRNTIDNQQQEYETKFVDLQSSISLNSGGSGGLGDEVIDGSTKERIARLERDNKRLKEVAEKASELENQLEDANQSKELLTIQIKQLEEQKQQSNNTNNNNNNNNMVDSSEIESLKQQLKEKEKEISTLKRKLEESNLSLDENRKQLVELSQRPTTQSPGDIEKLENYENLLKENDGLEGRLRAARNIIKDLREKHKSYSNQETQLATKDEVITKLEGLVKKKTDINEDLRKQLEEGREESQREINLMLSAFLKIGLEMEQVKIQNISSSKEPRSFLNKKRAD
The following text describes a protein:
Function:
Leucine-rich repeat protein that likely mediates protein interactions, possibly in the context of signal transduction.
Sequence:
MDPAPQSHPILSYVLSRLPTLSKPRPTAGADFDIEQPPVHTPSPRSPSVGEFELVERMPGLRHASVLHAMTRAVADVSAARSALQELGPRPDHELVDSSRAVVAAAAAGDVAPRVTEEDLEACRTVVRLEEAHETYEALLHEAEGRLEKVYRSAMEGRDLEEAEGKDESAAGDEGVAVQEEVVAVLKQAQEGKPVESVLLVDRQLRYLPEAFGRILGLRVLDVSHNQLQVIPDAIGGLEHLEELRLASNALVSLPDTVGFLSNLKILNVSTNKLRTLPDSISKCRSLVELDASYNGLTYLPTNIGYELINLRKLWVHMNKLRSLPSSICEMQSLYLLDAHFNELCGLPSAIGKLSSLEILDLSSNFSDMKELPFSFGDLLNLREVDLSNNQIHALPDSFGRLDKLEKLNLEQNPLSMPPAEVVKEGVDAVKEYMSKRWLDALLEEEQRSMAAAAAESPQASTPKAWLARSVSWVSDVGGSLVGYVSGGQTKSEKDSILDQQF
The following text describes a protein:
Function:
Component of the MRN complex, which plays a central role in double-strand break (DSB) repair, DNA recombination, maintenance of telomere integrity and meiosis. The MRN complex is involved in the repair of DNA double-strand breaks (DSBs) via homologous recombination (HR), an error-free mechanism which primarily occurs during S and G2 phases. The complex (1) mediates the end resection of damaged DNA, which generates proper single-stranded DNA, a key initial steps in HR, and is (2) required for the recruitment of other repair factors and efficient activation of ATM and ATR upon DNA damage. The MRN complex possesses single-strand endonuclease activity and double-strand-specific 3'-5' exonuclease activity, which are provided by MRE11, to initiate end resection, which is required for single-strand invasion and recombination. Within the MRN complex, nbn acts as a protein-protein adapter, which specifically recognizes and binds phosphorylated proteins, promoting their recruitment to DNA damage sites. Recruits mre11 and rad50 components of the MRN complex to DSBs in response to DNA damage. Promotes the recruitment of PI3/PI4-kinase family members atm, atr, and probably DNA-PKcs to the DNA damage sites, activating their functions. Mediates the recruitment of phosphorylated rbbp8/CtIP to DSBs, leading to cooperation between the MRN complex and rbbp8/CtIP to initiate end resection.
Subcellular Localization:
Chromosome, telomere. Nucleus, PML body.
Sequence:
MWILSPLENGGETHYIFCGKEYVVGRKNCAILLPSDQSISRAHANLTATDQTLTLKDSSKYGTFVRNQRVTSPVNLTPGDEVTFGVFHSKFRVIHQKLVVCSSCLDNDGKASLTEALLALGGKLVNSWSLDCTHLAMPTVKVTIKTISALLCCCPIVKPEFFSELNSAVQQKRPPPKPESFNPEIDEPVLSDENVNLGAVSARKQLFRGKTFIFLNAKQLKRLSGAVRFGGGSSQLLEEGALPCNLLQSPNTCVVDILTASSQILLPASITEWANSVKNLLARKGLRVIPESEIGLAAIYASCDQYCNPSCPILDLDSAPKVTPRIPSASLSQNIAVDETVLPAASQNITAYAVNTEPSQRKEVCEMTGVGVAVEETQEKIEFQNSRRFSGSKLSAHTKTPQFVVPETIPSTFNNTDSLKKTLQSRATEEGHADVRPPPSASRTSAQSVLHKQSPRKPKTSPQTSPQKQMTLTNFFQSVNKKRPLEDEPSAVTPEPKRAATETSIATQAQNSSPPFTVPKAQSQTPALLDVRSEASSEKPQSRKRKEMEIELEELESIMSEDMDLFDGQISTSRGQQEEPNVPKARISPKEKHDLQAVDPSSKRQRIHHQQNKMNTPQLQGGLEKDHHLQNKYSEHNTVSKTSKMLTGGQDLKKPPEASPSSTTEEMKHFEEDEGSFIEDAELLEINVCQEKKETPAEKPVPIKQEAQESKIDEDLPKKLILVEFRSLTVSAPPKTQPKLMQQNGHAKNFKCFRKRQAPGVGSIPIIGGSDLLVHNRGKNTDLDEWLRDAVEEERQSRRDESMGDDLFRYNPTKLSRRR