lhallee/plat_data huggingface dataset:
The following text describes a protein:
Function:
Transcriptional activator of STAT3 involved in the regulation of immune homeostasis. Also able to activate STAT1 transcription.
Subcellular Localization:
Nucleus.
Sequence:
MAQAIFEALEGMDNQTVLAVQSLLDGQGAVPDPTGQSVNAPPAIQPLDDEDVFLCGKCKKQFNSLPAFMTHKREQCQGNAPALATVSLATNSIYPPSAAPTAVQQAPTPANRQISTYITVPPSPLIQTLVQGNILVSDDVLMSAMSAFTSLDQPMPQGPPPVQSSLNMHSVPSYLTQPPPPPPPPPPLPPPPPPQPPPPPPQSLGPPGRPNPGGNGVVEVYSAAAPLAGSGTVEIQALGMQPYPPLEVPNQCVEPPVYPTPTVYSPGKQGFKPKGPNPAAPMTSATGGTVATFDSPATLKTRRAKGARGLPEAAGKPKAQKLKCSYCDKSFTKNFDLQQHIRSHTGEKPFQCIACGRAFAQKSNVKKHMQTHKVWPPGHSGGTVSRNSVTVQVMALNPSRQEDEESTGLGQPLPGAPQPQALSTAGEEEGDKPESKQVVLIDSSYLCQFCPSKFSTYFQLKSHMTQHKNEQVYKCVVKSCAQTFPKLDTFLEHIKSHQEELSYRCHLCGKDFPSLYDLGVHQYSHSLLPQHSPKKDNAVYKCVKCVNKYSTPEALEHHLQTATHNFPCPHCQKVFPCERYLRRHLPTHGSGGRFKCQVCKKFFRREHYLKLHAHIHSGEKPYKCSVCESAFNRKDKLKRHMLIHEPFKKYKCPFSTHTGCSKEFNRPDKLKAHILSHSGMKLHKCALCSKSFSRRAHLAEHQRAHTGNYKFRCAGCAKGFSRHKYLKDHRCRLGPQKDKDLQTRRPPQRRAAPRSCGSGGRKVLTPLPDPLGLEELKDTGAGLVPEAVPGKPPFAEPDAVLSIVVGGAVGAETELVVPGHAEGLGSNLALAELQAGAEGPCAMLAVPVYIQASE
The following text describes a protein:
Function:
V region of the variable domain of T cell receptor (TR) beta chain that participates in the antigen recognition. Alpha-beta T cell receptors are antigen specific receptors which are essential to the immune response and are present on the cell surface of T lymphocytes. Recognize peptide-major histocompatibility (MH) (pMH) complexes that are displayed by antigen presenting cells (APC), a prerequisite for efficient T cell adaptive immunity against pathogens. Binding of alpha-beta TR to pMH complex initiates TR-CD3 clustering on the cell surface and intracellular activation of LCK that phosphorylates the ITAM motifs of CD3G, CD3D, CD3E and CD247 enabling the recruitment of ZAP70. In turn ZAP70 phosphorylates LAT, which recruits numerous signaling molecules to form the LAT signalosome. The LAT signalosome propagates signal branching to three major signaling pathways, the calcium, the mitogen-activated protein kinase (MAPK) kinase and the nuclear factor NF-kappa-B (NF-kB) pathways, leading to the mobilization of transcription factors that are critical for gene expression and essential for T cell growth and differentiation. The T cell repertoire is generated in the thymus, by V-(D)-J rearrangement. This repertoire is then shaped by intrathymic selection events to generate a peripheral T cell pool of self-MH restricted, non-autoaggressive T cells. Post-thymic interaction of alpha-beta TR with the pMH complexes shapes TR structural and functional avidity.
Subcellular Localization:
Cell membrane.
Sequence:
MGCRLLCCVVFCLLQAGPLDTAVSQTPKYLVTQMGNDKSIKCEQNLGHDTMYWYKQDSKKFLKIMFSYNNKELIINETVPNRFSPKSPDKAHLNLHINSLELGDSAVYFCASSQ
The following text describes a protein:
Function:
Catalyzes the epimerization of the C3' and C5'positions of dTDP-6-deoxy-D-xylo-4-hexulose, forming dTDP-6-deoxy-L-lyxo-4-hexulose.
Sequence:
MNVIKTEIPDVLIFEPKVFGDERGFFMESFNQKVFEEAVGRKVEFVQDNHSKSTKGVLRGLHYQLEPYAQGKLVRCVVGEVFDVAVDIRKSSPTFGKWVGVNLSAENKRQLWIPEGFAHGFCVLSDEAEFVYKTNNFYSKMQERGILWSDKSINIEWPVQNPLLSDKDINGQKFVDADYFI
The following text describes a protein:
Function:
Catalyzes the third of the four reactions of the long-chain fatty acids elongation cycle. This endoplasmic reticulum-bound enzymatic process, allows the addition of two carbons to the chain of long- and very long-chain fatty acids/VLCFAs per cycle. This enzyme catalyzes the dehydration of the 3-hydroxyacyl-CoA intermediate into trans-2,3-enoyl-CoA, within each cycle of fatty acid elongation. Thereby, it participates to the production of VLCFAs of different chain lengths that are involved in multiple biological processes as precursors of membrane lipids and lipid mediators.
Subcellular Localization:
Endoplasmic reticulum membrane; Multi-pass membrane protein. Membrane; Multi-pass membrane protein.
Sequence:
MPPKASTSRKASANAKPAKRGPAAPIKYYLILFNFVSFFGWVVVLSTLIKHLAMGPQTFSPSVKFASDLLARFRLAKIGIVKSYSHLFPEPIAQLLERASNSHTFVGPVVALVQSLAILEVVHAAIGWVRSPVTTTAIQVASRLFMVWGVTERYSQAWTSPFYASMVLAWAITECVRYPFYANQLLNSEGPGLLWARYTLFYVLYPIGAASEAMCILATLPNGLPFNKPAAWDLRAYVFAGLFVIWWPGLYVMYTYMIKQRRKVIGKGFWGNKLVDELREKKKQ
The following text describes a protein:
Function:
Monothiol glutaredoxin involved in the biogenesis of iron-sulfur clusters. Binds one iron-sulfur cluster per dimer. The iron-sulfur cluster is bound between subunits, and is complexed by a bound glutathione and a cysteine residue from each subunit.
Sequence:
MSVVEITSDSHFSELTSSLAPTTLVAVYFHTPWAAPCAQMNSVFKSLSTLHSSVLFLSVNADELPEISESFDISAVPYFVMLRDGTILKELSGADPKELAATISALSESDAKPAESESAAAAAPTSSTADAPASSSTDAPEPAEETEEELNARLAKLVKAAPVMLFMKGTPAAPQCGFSRQLVAILREHHVRFGFFDILKDDAVRQGLKKFSDWPTFPQLYIGGELQGGLDIVKESIQEDPEFFEKAVAE
The following text describes a protein:
Function:
Co-chaperone for Hsp70 protein HSPA5/BiP that acts as a key repressor of the ERN1/IRE1-mediated unfolded protein response (UPR). J domain-containing co-chaperones stimulate the ATPase activity of Hsp70 proteins and are required for efficient substrate recognition by Hsp70 proteins. In the unstressed endoplasmic reticulum, interacts with the luminal region of ERN1/IRE1 and selectively recruits HSPA5/BiP: HSPA5/BiP disrupts the dimerization of the active ERN1/IRE1 luminal region, thereby inactivating ERN1/IRE1. Also involved in endoplasmic reticulum-associated degradation (ERAD) of misfolded proteins. Required for survival of B-cell progenitors and normal antibody production.
Subcellular Localization:
Endoplasmic reticulum.
Sequence:
MATPQSVFIFAICILMITELILASKSYYDILGVPKSASERQIKKAFHKLAMKYHPDKNKSPDAEAKFREIAEAYETLSDANRRKEYDTLGHSAFTNGKGQKASGSPFEQSFNFNFDDLFKDFGFFGQNQNTRSKKHFENHFQTRQDGSSRQRHHFQEFSFGGGLFDDMFEDMEKMFSFTGFDTTTSRHTVQTENRFHGSSKHCRTVTQRRGNMVTTYTDCSGQ
The following text describes a protein:
Function:
May play a role in endocytic and/or exocytic pathways.
Miscellaneous:
MISCELLANEOUS: Present with 56 molecules/cell in log phase SD medium.
Subcellular Localization:
Cell membrane; Peripheral membrane protein. Vacuole membrane; Peripheral membrane protein. Note=Located at both the plasma and vacuolar membrane.
Sequence:
MSNEAYQHDHTVNPHQKIVVNSYDWLQFRDEQDHCKSKNPITHASPGVGSNAQNSDIAEAPQVFHPSYQSLVNVPSESPRPDQTSGSNPAVGLLHNAEDKASGQEEEGSQYEIQYSVFRPLHAYPTKGLAYEQLRRKEEQEQRENFNHLVSDCIEAVETFGRELERIQTGSSGSYFVYGTRADESVPVGVFKPKDEEPYGPFSPKWTKWAHRTFFPCLFGRSCLIPNLGYICESAASLLDRRLETHLVPYTDTASIESFNFYDNRKKWVLGYNLQKKKQKKLGSFQLFLKEYINADEFFHKYPLPGMYSDVKHSFHRKSSGEDINHKPETTRNLTDETEPSKQINSSPISTESEENSKFEWTESSLSQFRLELEKLIILDYIMRNTDRGLDNWMVKLIKLSNNKWRLKLAAIDNGLSFPWKHPDEWRLYPYGWLYLPLQLLAKPFSEQMRSHFLPILTSTNWWEESYQEFLALFSRDQDFNVRMWKKQWAVLKGQAFNVVETLKDPRQGPLELVRRTRCQVIDEKMQVPCCPPPVSIFKNAIDEPIGSYSTSPMVLPSTPSTIPFHAHNQSNSNPVYYDSTLHPFANKTVIAERLQIVNSTPVFTWC
The following text describes a protein:
Function:
Tumor suppressor serine/threonine-protein kinase involved in synaptic plasticity, centriole duplication and G1/S phase transition. Polo-like kinases act by binding and phosphorylating proteins that are already phosphorylated on a specific motif recognized by the POLO box domains. Phosphorylates CPAP, NPM1, RAPGEF2, RASGRF1, SNCA, SIPA1L1 and SYNGAP1. Plays a key role in synaptic plasticity and memory by regulating the Ras and Rap protein signaling: required for overactivity-dependent spine remodeling by phosphorylating the Ras activator RASGRF1 and the Rap inhibitor SIPA1L1 leading to their degradation by the proteasome. Conversely, phosphorylates the Rap activator RAPGEF2 and the Ras inhibitor SYNGAP1, promoting their activity. Also regulates synaptic plasticity independently of kinase activity, via its interaction with NSF that disrupts the interaction between NSF and the GRIA2 subunit of AMPARs, leading to a rapid rundown of AMPAR-mediated current that occludes long term depression. Required for procentriole formation and centriole duplication by phosphorylating CPAP and NPM1, respectively. Its induction by p53/TP53 suggests that it may participate in the mitotic checkpoint following stress.
Miscellaneous:
MISCELLANEOUS: There are indications that PLK2 might act as a tumor suppressor: PLK2 is significantly down-regulated in a wide range of acute myeloid leukemias (AMLs) and B-cell lymphomas due to aberrant cytosine methylation in the CpG island located at the 5' of the PLK2 gene. Moreover, miR-126, a microRNA that negatively regulates PLK2 is up-regulated in AMLs, suggesting that PLK2 down-regulation by miR-126 could also contribute to leukemogenesis.
Subcellular Localization:
Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole. Cell projection, dendrite. Note=Localizes to centrosomes during early G1 phase where it only associates to the mother centriole and then distributes equally to both mother and daughter centrioles at the onset of S phase.
Domain:
The POLO box domains act as phosphopeptide-binding module that recognizes and binds serine-[phosphothreonine/phosphoserine]-(proline/X) motifs. PLK2 recognizes and binds docking proteins that are already phosphorylated on these motifs, and then phosphorylates them (By similarity).
Sequence:
MELLRTITYQPAASTKMCEQALGKGCGADSKKKRPPQPPEESQPPQSQAQVPPAAPHHHHHHSHSGPEISRIIVDPTTGKRYCRGKVLGKGGFAKCYEMTDLTNNKVYAAKIIPHSRVAKPHQREKIDKEIELHRILHHKHVVQFYHYFEDKENIYILLEYCSRRSMAHILKARKVLTEPEVRYYLRQIVSGLKYLHEQEILHRDLKLGNFFINEAMELKVGDFGLAARLEPLEHRRRTICGTPNYLSPEVLNKQGHGCESDIWALGCVMYTMLLGRPPFETTNLKETYRCIREARYTMPSSLLAPAKHLIASMLSKNPEDRPSLDDIIRHDFFLQGFTPDRLSSSCCHTVPDFHLSSPAKNFFKKAAAALFGGKKDKARYIDTHNRVSKEDEDIYKLRHDLKKTSITQQPSKHRTDEELQPPTTTVARSGTPAVENKQQIGDAIRMIVRGTLGSCSSSSECLEDSTMGSVADTVARVLRGCLENMPEADCIPKEQLSTSFQWVTKWVDYSNKYGFGYQLSDHTVGVLFNNGAHMSLLPDKKTVHYYAELGQCSVFPATDAPEQFISQVTVLKYFSHYMEENLMDGGDLPSVTDIRRPRLYLLQWLKSDKALMMLFNDGTFQVNFYHDHTKIIICSQNEEYLLTYINEDRISTTFRLTTLLMSGCSSELKNRMEYALNMLLQRCN
The following text describes a protein:
Function:
Hydrolysis of the glycosidic linkage between oligosaccharides and ceramides of glycosphingolipids, optimal substrates appear to be the glycosphingolipids with a gangliotetraose structure.
Subcellular Localization:
Secreted. Note=Released from digestive cells into the gastric cavity, and eventually into the surrounding medium, during the digestive process.
Sequence:
MISVALIILFLAKVISGKSDDFISVNPETNMLIDGYGRERFFHGTNVVVKHFPFHPETTGFNKDTFSEDDMKILQKFGLNSIRLGMMLPGYVPKREEYNETYIKVIQSIVTTAAKYGIYTLLDMHQDVFSPKFCVEGMPDWIVNTQGAKDFPMPLHKPFNLDPKTGYPYPEDCAKFSWADYYFTEAAGQAFQNLYDNVDGLRDEWAQFWKKTADVFKEEPSVIGYELINEPFCGNVFKHPTLLIPGVADYLNLQPTYDALQKAIRQVDEEHNIFFEGVTWDFFEVGFTEVPGGKQYQNRSVLSYHYYEPPDFSKKLNFEARLLDLKRLKCGGFLTEMFTVGTDFNSMFEMFDLCDKFKQSWHGWMYKSYGCIEQNLGCLNMSSPGKESIQIANTSRTYPQAVAGRTQSYAFDIKTKVFTLVYETVGSCKSGRTIVYFNKNLHYPNGYRYEINPNFKVTPSENEYFLYLDEVNKVPNTVVTFKLFPLSFTDSEDIHPVTVMGDKHLSENHNENEKKKK
The following text describes a protein:
Function:
Phosphorylates both N-acetylglucosamine (GlcNAc) and N-acetylgalactosamine (GalNAc) at similar rates. Involved in the lacto-N-biose I/galacto-N-biose (LNB/GNB) degradation pathway, which is important for host intestinal colonization by bifidobacteria. Also accepts GTP and ITP as phosphate donors. In vitro, can phosphorylate several GlcNAc and GalNAc derivatives.
Sequence:
MTESNEDLFGIASHFALEGAVTGIEPYGDGHINTTYLVTTDGPRYILQQMNTSIFPDTVNLMRNVELVTSTLKAQGKETLDIVPTTSGATWAEIDGGAWRVYKFIEHTVSYNLVPNPDVFREAGSAFGDFQNFLSEFDASQLTETIAHFHDTPHRFEDFKAALAADKLGRAAACQPEIDFYLSHADQYAVVMDGLRDGSIPLRVTHNDTKLNNILMDATTGKARAIIDLDTIMPGSMLFDFGDSIRFGASTALEDEKDLSKVHFSTELFRAYTEGFVGELRGSITAREAELLPFSGNLLTMECGMRFLADYLEGDIYFATKYPEHNLVRTRTQIKLVQEMEQKASETRAIVADIMEAAR
The following text describes a protein:
Function:
May function as sodium-coupled metabolite transporter across the chloroplast envelope.
Subcellular Localization:
Membrane; Multi-pass membrane protein. Plastid, chloroplast envelope.
Sequence:
MDTDAAVNVTAAAFKAAADATATVKPVAAACYDNNLVNSQGMFLGDQPLRFSLPLLLIQVSLILLLSAAAHHVLRRLGQSRFVTHMLVGILLDPSVLGRNHELRGALFSERGTYILESVSLVALILFLFSMGVKTDMSLLRRPSGRAVAVGLAGSVVPLAITLPVFHMLQPTLPADLRGSSLITEIAVRLSLSSFPVIADALAELDLLNSELGRIALTASLITDVTSWFLRACFAAAFLVTEAKSPAFTTKILASFVGFVFFVAFVARPAGRYIAYKRTPAGDLLSEGSFVVVVIAALLSALVTDVIGFKYMIGPMMLGLAIPGGMPIGATMTERLDSFFIALFLPVYMALAGYRTDFSELGGHEEKWCALELFVALCVAGKMVGCIAAGLFFAMPIGEATALALMLNIRGIVEVAAINNWGDTMKATAEHYSTLTLSMVLITAAATPLIKLLYDPTGRFARAKRRTMEGARPNAELRVMACLYTEDHAAPLIDLLEASGANHDFPVSLIVLHLTELVGRAASVLKPHKKSSTASSPSDRIVNAFRHFEQQAAPGAVTVSPYVAQSPYSSMHHDVCSLAHSRKANLILLPFHKSSDGARSTANSAVRSANRAVLQYAPCSVAILVDHGLASGSACATASNRNLLQRVALYFLGGPDDREALAYAARMPESGGTSVTVVRIKLRNWVGMGGHDEVRDEEVLQEFWQRYREDERVVYVEKTVEDGEGTASVVRSMSDKFDLVIVGRRGEDRDVEGSALTSGLSEWSECPELGVLGDMLATAEFASKVSILVIQQQAGITTGGEADYQ
The following text describes a protein:
Function:
Participates in the regulation of gene transcription. Binds DNA in a non-specific manner, yet also specifically recognizes the core sequence CAC[GA]TG. Seems to activate the transcription of growth-related genes (By similarity).
Miscellaneous:
MISCELLANEOUS: This protein is synthesized as a Gag-vMyc chimeric protein. The sequence shown here corresponds to the Myc homolog fragment of the chimera.
Subcellular Localization:
Host nucleus.
Sequence:
MPLNVSFANRNYDLDYDSVQPYFYCDEEENFYQQQQQSELQPPAPSEDIWKKFELLPTPPLSPSRRSGLCSPSYVAFASFSPRGDDDGGGGSFSTADQLEMVTELLGGDMVNQSFICDPDDETFIKNIIIQDCMWSGFSAAAKLVSEKLASYQAARKDSGSPSPARGPGGCPTSSLYLQDLTAAASECIDPSVVFPYPLNDSSSPKPCASPDSAAFSPSSDSLLSSAESSPRASPKPLGLHEETPPTTSSDSEEEQEEEEEIDVVSVEKRQPPAKRSESGSPSAGGHSKPPHSPLVLKRCHVPTHQHNYAAPPSTRKDYPAAKRAKLDSGRVLKQISNNRKCISPRSSDTEENDKRRTDNVLERQRRNELKRSFFALRDQIPELENNEKAPKVVILKKATAYILSVQAGEQKLISEKDLLRKRREQLKHKLEQLRNS
The following text describes a protein:
Function:
Flippase that catalyzes the hydrolysis of ATP coupled to the transport of lysophosphatidylserine, phosphatidylethanolamine, and phosphatidylserine from the lumenal to the cytosolic leaflet of the Golgi apparatus membrane and ensures the maintenance of asymmetric distribution of phospholipids.
Subcellular Localization:
Endosome membrane; Multi-pass membrane protein. Golgi apparatus membrane; Multi-pass membrane protein.
Sequence:
MDSRLNRIQSKMKLWIKDKNLSNPSIPLKVLNKSFRSSRQSSVSNGHGLYSLDRDETESLMSSHEASNAGISLDSSFRVIQVGQPEPQYGNNAVTNTKYDLFTFLPKCLYEQFRYFYNMYFLLVSLSQLIPPLKIGYLSTYIAPLIFVLLITLTKEAVDDLKRRRRDSYANNEIYTVNDSPCAAQNIQAGDVVYIAKDQRIPADMILLETTVGNEAFIRTDQLDGETDWKLRIPCSNQHTEGIVHADAPIKSVHHFYGTFTLNNQKRPISVDHTLWANTVLASDGVYGVVVYTGKDTRQSMNSSKAKTKVGLLEKEINFYSKILCTFVLVLSIGLTFSHGIKTDWYISVFRYLILFSSIIPINLRVNLDLAKIVHSKNTESDPNLPGVVVRSSNIPEELGRIEYVLTDKTGTLTQNEMEMKKLHVGTMGFSAESMDVVQACIQNYSTPIPLSEDSKTLVRNLVLALSLCHNVTPSKGHDGVVSYQAASPDEVAIVKWTSTLGLVLTNRTRDAITLNNNVYKILNIFPFKSETKRMGIIVQSPDEKITFYLKGADSIMQNFVKPSFWLEEECGNLAREGLRTLVVAKKDLSAEEYSAFSLAHSDASLSFSNSRDKKMEEIVSRYLENDMDLLGLTGVEDKLQKDVKITLELLRNAGIHVWMLTGDKVETARCIAISSRLVSRGQYIHTINQLSSREEAHNHLLTLRNKPDSCLIIDGESMEFCIGYLQNEFIDIVSDLSSVVICRCTPTQKANMTRLIQEKKQASVCCIGDGGNDVGMIQVANVGIGIVGKEGQQASLAADYSVKEFSHVSRLLLWHGRISYKQTSKLAMFVIHRGLLISVCQVVYSVISAFEPIALFQGLLLVGYSTMYTMLPVFSIVYDRDVSEKLVFLFPELYKEMREQKCFSYKNFISCVLISVYQGLIIQLFTFYLIGFEEEGKMLAVCFSCLIFNELIMVALQINTWEQTIVMSELLTLMMYILSVPFLTNYFELKFLLGLKFYWVSALILFISLLPVWCGKALKRKLKPSSYAKLQR
The following text describes a protein:
Function:
Nonessential protein required for the fusion of transport vesicles derived from the endocytic pathway with the Golgi complex. Can be replaced by got1 (By similarity).
Subcellular Localization:
Golgi apparatus membrane; Multi-pass membrane protein.
Sequence:
MEGSFQSRLQSIIQRTGETTAESTNSWYNRLRTSMPWSNDYTEIPTNASGGNSYFQSSEFSLSRWERYMLFGICLLGSLACYAIACFMFPVLVLKPRKFVLLWTMGSLLAVLGFAIVQGFVAHFRQLTTMERLPITLSYFVTLLATIIATIKIKSTILSIVFGVLHILSFVAYLIAFFPFGTRTVSLGTRMASRSLSNWLP
The following text describes a protein:
Function:
Alpha-1,2-mannosyltransferase that catalyzes the transfer of the fourth mannose, via an alpha-1,2 bond, from a dolichol-phosphate-mannose (Dol-P-Man) to an alpha-D-Man-(1->2)-alpha-D-Man-(1->6)-2-PEtn-alpha-D-Man-(1->4)-alpha-D-GlcN-(1->6)-(1-radyl,2-acyl-sn-glycero-3-phospho)-2-acyl-inositol (also termed H6) intermediate and participates in the twelfth step of the glycosylphosphatidylinositol-anchor biosynthesis. The presence of a fourth mannose in GPI is facultative, suggesting that it only exists in some tissues.
Subcellular Localization:
Endoplasmic reticulum membrane; Multi-pass membrane protein.
Sequence:
MQICGSSVASVAAGTSFQVLGPVCWQQLDLKMAVRVLWGGLSLLRVLWCLLPQTGYVHPDEFFQSPEVMAEDILGVQAARPWEFYPSSSCRSVLFPLLISGSTFWLLRLWEELGPWPGLVSGYALLVGPRLLLTALSFALDGAVYHLAPPMGADRWNALALLSGSYVTLVFYTRTFSNTIEGLLFTWLLVLVSSHVTWGPTRKEPAPGPRWRSWLLGGIVAAGFFNRPTFLAFAVVPLYLWGTRGATNPGLKSLTREALVLLPGAALTAAVFVATDSWYFSSPATSRNLVLTPVNFLHYNLNPQNLARHGTHARLTHLAVNGFLLFGVLHAQALQAAWQRLQVGLQASAQMGLLRALGARSLLSSPRSYLLLLYFMPLALLSAFSHQEARFLIPLLVPLVLLCSPQTQPVPWKGTVVLFNALGALLFGCLHQGGLVPGLEYLEQVVHAPVLPSTPTHYTLLFTHTYMPPRHLLHLPGLGAPVEVVDMGGTEDWALCQTLKSFTRQPACQVAGGPWLCRLFVVTPGTTRRAVEKCSFPFKNETLLFPHLTLEDPPALSSLLSGAWRDHLSLHIVELGEET
The following text describes a protein:
Function:
May play a role in retrograde transport of proteins from the Golgi to the endoplasmic reticulum.
Miscellaneous:
MISCELLANEOUS: Present with 1630 molecules/cell in log phase SD medium.
Subcellular Localization:
Golgi apparatus membrane; Multi-pass membrane protein.
Sequence:
MQYSSRFLELNIPDSFLNINKIPDATKFITVTYICLTATLFCIRRSLYNKLVLEDPNLDYNLITSPLLQMVPSQIWRYPTSLVLSNFIDTKAWKVVVNLLNLIIGGSFIERNWNSSKEMFKFIIVLGSLTNVLIIMLTLLVSFFSNKVRLDIPLDGNYTILIGFPIIYRQLLPETTIIHLKTPQFLAKNFRFKLLPIFVMFTMTVTQIIWFHHFAQLFSIWVTFFASWSYLRFFQKLAPLNCPSLPTTNSQGGQEILVGDASDTFQLIYFFPDLIKPILRPIFNFIYNVVVVKFKVIKPFHDIDIDIGNTIAESRGAKKIMTVEERRRQLALQVLEERMVNP
The following text describes a protein:
Function:
Probable proto-oncogene that functions in the epidermal growth factor receptor/EGFR signaling pathway. Activates both the EGFR itself and downstream RAS/MAPK and PI3K/AKT/TOR signaling cascades.
Subcellular Localization:
Cytoplasm. Membrane.
Domain:
All members of the FAM83 family of proteins share a conserved N-terminal DUF1669 (domain of unknown function 1669) domain of about 300 amino acids. This domain mediates the interaction with casein kinase 1 (CK1) isoforms. Therefore, it has been proposed to rename DUF1669 the polypeptide anchor of CK1 domain.
Sequence:
METSSMLSSLNDECKSDNYIEPHYKEWYRVAIDILIEHGLEAYQEFLVQERVSDFLAEEEINYILKNVQKVAQSTAHGTDDSCDDTLSSGTYWPVESDVEAPNLDLGWPYVMPGLLGGTHIDLLFHPPRAHLLTIKETIRKMIKEARKVIALVMDIFTDVDIFKEIVEASTRGVSVYILLDESNFNHFLNMTEKQGCSVQRLRNIRVRTVKGQDYLSKTGAKFHGKMEQKFLLVDCQKVMYGSYSYMWSFEKAHLSMVQIITGQLVESFDEEFRTLYARSCVPSSFAQEESARVKHGKALWENGTYQHSVSSLASVSSQRNLFGRQDKIHKLDSSYFKNRGIYTLNEHDKYNIRSHGYKPHFVPNFNGPNAIRQFQPNQINENWKRHSYAGEQPETVPYLLLNRALNRTNNPPGNWKKPSDSLSVASSSREGYVSHHNTPAQSFANRLAQRKTTNLADRNSNVRRSFNGTDNHIRFLQQRMPTLEHTTKSFLRNWRIESYLNDHSEATPDSNGSALGDRFEGYDNPENLKANALYTHSRLRSSLVFKPTLPEQKEVNSCTTGSSNSTIIGSQGSETPKEVPDTPTNVQHLTDKPLPESIPKLPLQSEAPKMHTLQVPENHSVALNQTTNGHTESNNYIYKTLGVNKQTENLKNQQTENLLKRRSFPLFDNSKANLDPGNSKHYVYSTLTRNRVRQPEKPKEDLLKSSKSMHNVTHNLEEDEEEVTKRNSPSGTTTKSVSIAALLDVNKEESNKELASKKEVKGSPSFLKKGSQKLRSLLSLTPDKKENLSKNKAPAFYRLCSSSDTLVSEGEENQKPKKSDTKVDSSPRRKHSSSSNSQGSIHKSKEDVTVSPSQEINAPPDENKRTPSPGPVESKFLERAGDASAPRFNTEQIQYRDSREINAVVTPERRPTSSPRPTSSELLRSHSTDRRVYSRFEPFCKIESSIQPTSNMPNTSINRPEIKSATMGNSYGRSSPLLNYNTGVYRSYQPNENKFRGFMQKFGNFIHKNK
The following text describes a protein:
Function:
Telomerase is a ribonucleoprotein enzyme essential for the replication of chromosome termini in most eukaryotes. It elongates telomeres. It is a reverse transcriptase that adds simple sequence repeats to chromosome ends by copying a template sequence within the RNA component of the enzyme.
Subcellular Localization:
Nucleus. Chromosome, telomere.
Sequence:
MSASFPSIPGFAGPLSLKAFLEEYFGLHLTFAVETASPSPRAAATAATPSAAEFRALRDVVLPPNQSFLVVVYVALHASSSPPPTTAHASPTPPTPALGRAASATGFERLRQPLTHQTVASSAHDTCMTRCNPADRQNSSWSSSSFAGKHGSTRDPWRASAFRLLYTNTSHRPLTDALLRHPWWASFAACLGPAAMGFIEMYCPIVLQLEAMAGGVQVLGPALKHTAFERSFSAAAPSSEMKGPLPQGSGCISSRGVKRALDTRECSAPLPLQKQRRVEAPPKAKAGRRLQRGVAPDSRPCRDDPFSSSVNRAAMAATWAAALTRTDVPRTRLYSARISDGDGAGDGSGSALPLPAGFLEAQWLRRHPHSLHRALQAALPKRAAYGASTRRYSVGASERGTGCTSVEDIPMWHVTHVFRWLVLQPPQSSADASPTTPPKFDLPSHLRRLLSTVVDQCSRLDLRGAALKHTGYLEEAFRRQQQGVEPWDVQRLSTPVDVVVSYLRTLLSTLRWAPLKETDNGSFWGRDAAGSERVLDALMRAVRGWLIAGRHAVFPVSRFLDGVPVAQVPWLNGFYTTAPSLPFPAATSSAARHARRERSHVQQRVWLQFALFLTQDILPFLLRASFTITWSSKNTHKLLFFPAVVWRRLVRREVRRTRSCGAPRSQMPLAGESARRIGAEPAALSSAPSACGGVVTAALLTPHSAVSKASAAIAAPRDVWRAVRTGGALTHRGARATLATRGGGASCLYAGVRFRPDRRKLRPIAVVRSASLRSLKEMARGSPSPYSHASAIARLLRRLGCSDTDGQLPAATATLLRRVQARSRHNRRAGVHRFPHPLPPHLPHKAALRDALRCLVSGVEEQRVRDGLPRLSNLSHQDEYAELRSFCEEVRGRHALLCEGPAGTAPAVSSAPPPGSAACCFAPYVTLVRSDASRCYDNLPQERVLAAVASLVKHDAYRVLRFTAIHALDGEGACRGGCLLRRTFTTRTIPCAEAECGVLARIPRGHIYWEEEEEGHTQGGLHTTAAVSRTTDANRRCGANLISGAAVRALLSEHIRHHLVVVSGGSLFEQRVGILQGSPVAMLLCDRLFSDVVDTALSGILSEHAERSLLLRRVDDVLVATTSPAAAERCLRAMQCGWPSVGYVSNPSKLTLSTACGRLVPWCGLLLHDTTLEVSVEWRRIGVLLASLRVGDPHYVHRGDHDPLYLTQRFLAVLQLRVAPTALCGRMNSKTRQLQTFYEVGLLWSRVVLEKVQEALPVARNRCVAVLLLRPLAVCVGRLCRLLSGHQRFLAARQSACDVSAAEVRACVLTALHRTMQAKLRVLQARTVCVVTAQRGRTPRGTSLKGRRNHFCSHEALSAGRKCCERRRKGRNRRRNTRVCLRSFWWLAAAEVESQWRRSLSALHRAAPRLGEARGPTALSPSPGASASLLMDDGPLSMHARALSATRLSQT
The following text describes a protein:
Function:
Peptidoglycan polymerase that catalyzes glycan chain elongation from lipid-linked precursors.
Subcellular Localization:
Cell inner membrane; Single-pass membrane protein.
Sequence:
MISVRRGFSQLWYWGKRGVIGIIALWMAGILIFAFLPVPFSMVMIERQLGAWLTGDFAYVAHSDWVPMDEISPYMALAVMAAEDQKFPDHWGFDVGAIESALSHNQRNQKRIRGASTLSQQTAKNVFLWDGRSWVRKGLEVGLTAGIELIWTKRRILTVYLNIAEFGNGIFGVEAAARHFFNKPASKLSASEAALLAAVLPNPLRFKVNAPSGYVISRQQWILRQMHQLGGKTFLQENTLD
The following text describes a protein:
Function:
Specifically methylates the N1 position of guanosine-37 in various cytoplasmic and mitochondrial tRNAs. Methylation is not dependent on the nature of the nucleoside 5' of the target nucleoside. This is the first step in the biosynthesis of wybutosine (yW), a modified base adjacent to the anticodon of tRNAs and required for accurate decoding.
Subcellular Localization:
Mitochondrion matrix. Nucleus. Cytoplasm. Note=Predominantly in the mitochondria and in the nucleus.
Sequence:
MASQVAACVVDTAEASSSGREHATLDREAFKQILNLVALRVPARQCADMMKAFRGFTLDRPRLKCIVNDGDPPRKDTKLLLLEEGVTLESLTLELRGRVEADKLEVQTHQVTLEYSMLSADAVLKKLLPEGVDAPSSFETIGHIAHLNLRDEQLPYRHLIAQVLLDKNPHLKTIVNKVGSIENEFRVFNMEVIGGEQRLETEVTQHGARFKLDFSQVYWNSRLESEHLRLVGTMERGQVLVDMMAGIGPFAVPAAQKGLTVYANDLNPRSTHYLAVNVRLNRLGDGVRVFNMDGRAFLRLLCDTPSGPAADIRRQKQQQGQQPAEEPKQQQEPEPVSAGIAVPQAAAGAAAAAAAGTTAAAEGAAASPAVGQPAKRQRTKERVFEAQGPVPPVPESFTPPVGGIMFDHVVMNLPASAIEFLDAFNGAFDPVAWADRPLPTVHCYTFKRANETEADIVAKAEGYLGGPMEAGACVVHTVRDVAPNKLMLCLSFRVPKAVAFNSRS
The following text describes a protein:
Function:
Can inhibit both serine proteases and cysteine proteases. May be involved in the modulation of the proteases that participate in the hydrolysis of dietary proteins in the gut of spider mites.
Subcellular Localization:
Endoplasmic reticulum.
Sequence:
MSSLLYIFLLLAVFISHRGVTTEAAVEPVKDINGKSLLTGVNYYILPVIRGRGGGLTMSNLKTETCPTSVIQDQFEVSQGLPVKFSPYDKSRTIPVSTDVNIKFSPTSIWELANFDETTKQWFISTCGVEGNPGQKTVDNWFKIDKFEKDYKIRFCPTVCNFCKVICRDVGVFVQDGKRRLALSDVPLKVMFKRAY