lhallee/plat_data huggingface dataset:
The following text describes a protein:
Function:
May be involved in transcriptional regulation.
Subcellular Localization:
Nucleus.
Sequence:
MSLVPGLTSIQPQPQLLDQLGIPRRCFQDWVDQNGLPGLSVTQQIRGITLLRRLECSNTIIAHCRHELLGPPTLSPSAWSSPASPPPRALPLGSCASKMLERGAESAAGATDPSPTGKEPVTKEAPHQGPPQKPSQSAPGPIASAGSPPRPRRRPPPQRLHRCPDCDKAFSYPSKLATHRLAHGGARPHPCPDCPKAFSYPSKLAAHRLTHSGARPHPCPHCPKSFGHRSKLAAHLWTHAPTRPYPCPDCPKSFCYPSKLAAHRHTHHATDARPYPCPHCPKAFSFPSKLAAHRLCHDPPTAPGSQATARHRCSSCGQAFGQRRLLLLHQRSHHQVEHKGERD
The following text describes a protein:
Function:
Synthesizes cyclic GMP (cGMP) from GTP (By similarity). May play a role in sensory neurons.
Miscellaneous:
MISCELLANEOUS: There are two types of guanylate cyclases: soluble forms and membrane-associated receptor forms.
Subcellular Localization:
Cytoplasm.
Sequence:
MIGWTHVCVSALILRKYGPEVLEEILRKAGYQEDIKFDIQCYYDDTETMRIFRVAATVLGLSVDDMWEMYGEFLITHACETGWQKMLFCMANNLQEFLDNLNSMHYFIDQIAFKSEMKGPTFQCEPFGESGLKLHYFSFRQGLFPIVKGLVRKTARTLFEMDVKVCMLERNQERRKSGMVEHVIFSVEPDDNHRKGKRLFHKFRNTKTTENAPSFTLSSTILVGLRDFKNIFPYHVCFNKQMIIEHIGIYLLREYGLENKKTLKVSDLMQLVQPSDIQLTYKNVLSYLNTLFIFQLKHHSKRNEVQEGSSEAFQQPLVLKGEMMPINDGNSIIFICSPHVTTVRDILNLKLYISDMPMHDATRDLVMLNQSRICQMELNKKLEETMKKMKKMTEELEVKKSQTDRLLFEFVPPVIAEALRAAKTVPAQEFSDCSVIFTDIPDFFTISVNCSPTEIITVVTDLFHRFDRIIEKHKGYKVLSLMDSYLIVGGVPNANQYHCEDSLNLALGLLFEAKQVVVPKLERSVRLRIGVHCGPVVAGIVSQQKPRFCVLGNTVNVTKSICSHSSPGKVLVSNAVRTMVTKHLKSIFVFNANGYLELQSGKVLTHFLEKNEKCSVWDIVDRDKATNDSIDGYRELHSDNGTEEWQEATVAAYRVISVVDALENKQSRTRKALTRLRSVKRKFRTIQSNDSGVSVSEPNVESAVCSIM
The following text describes a protein:
Function:
Responsible for the biosynthesis of pyroglutamyl peptides. Has a bias against acidic and tryptophan residues adjacent to the N-terminal glutaminyl residue and a lack of importance of chain length after the second residue. Also catalyzes N-terminal pyroglutamate formation. In vitro, catalyzes pyroglutamate formation of N-terminally truncated form of APP amyloid-beta peptides [Glu-3]-amyloid-beta. May be involved in the N-terminal pyroglutamate formation of several amyloid-related plaque-forming peptides.
Subcellular Localization:
Secreted.
Sequence:
MAGGRHRRVVGTLHLLLLVAALPWASRGVSPSASAWPEEKNYHQPAILNSSALRQIAEGTSISEMWQNDLQPLLIERYPGSPGSYAARQHIMQRIQRLQADWVLEIDTFLSQTPYGYRSFSNIISTLNPTAKRHLVLACHYDSKYFSHWNNRVFVGATDSAVPCAMMLELARALDKKLLSLKTVSDSKPDLSLQLIFFDGEEAFLHWSPQDSLYGSRHLAAKMASTPHPPGARGTSQLHGMDLLVLLDLIGAPNPTFPNFFPNSARWFERLQAIEHELHELGLLKDHSLEGRYFQNYSYGGVIQDDHIPFLRRGVPVLHLIPSPFPEVWHTMDDNEENLDESTIDNLNKILQVFVLEYLHL
The following text describes a protein:
Function:
Cytokine that acts as a physiological ligand for receptor tyrosine kinases LTK and ALK. Required for neural crest cell differentiation and iridophore development during embryonic iridophore development and adult stripe development by acting as a receptor for LTK.
Subcellular Localization:
Secreted. Cell membrane.
Sequence:
MRALRAPVLVMGLVLLICTAAQSDASANKVEKTLRRIMEIMRQVENSADDESAQKTESAPEPKDTHHLKTASGETILEIFPRDLSRKEKFITILTGRRLSNPLRHQSCVFETSDLVVFHPSGPLYFGPKCKKDVYRLYHNTRDCTIPAHYKRCARLLTRLAGTRKCQEG
The following text describes a protein:
Function:
Mitochondrial DNA endonuclease involved in intron homing. Cleaves only one strand of intronless DNA sequence at the site which coincides with the I-SceII cleavage recognition site.
Miscellaneous:
MISCELLANEOUS: The expression of ai2a in E.coli causes growth inhibition and degradation of genomic DNA.
Subcellular Localization:
Mitochondrion.
Sequence:
MKKEEKKENKKREQNQISSKKWNEWLAGLIDGAGKFTLSKSGYANLDILLELRDEKCHIELKQRFGGEIKRKETTLIRYRVHRLYGIRQLIACVNGHIRHPLRKIEFKEICMHYNVEYKEPETLTFANGWLSGYFDAVGLIEFSTEQDQLYLAFRHKKNTMLNELEIQKCLGVNLTCEQNGCSCESVTLYKINKKTVLSLYKYFKKYRLRSSIKTTQILLIPQFYEIQNETKEINDMQVKQKLWKQFFKKWYVDEMVKYESVKLANYYKSKTSPEKRVKKLIKLKFHRNERIRKRAERLELQKEKEKKA
The following text describes a protein:
Function:
Involved in mitochondrial or peroxisomal functions and amino acid signaling pathways.
Subcellular Localization:
Vacuole membrane; Peripheral membrane protein. Cytoplasmic vesicle membrane; Peripheral membrane protein. Preautophagosomal structure membrane; Peripheral membrane protein.
Domain:
May contain a beta-propeller domain involved in specific binding to phosphatidylinositol 3,5-bisphosphate (PIP2), leading to the association of the protein to the membrane.
Sequence:
MSTINTVSLNQDASCMSVALDTGYKIFQINPLKLRAQRQFNDGGLSIVKMLFRSNVLLLVGGGGNPKYAPNKLIVWDDVKERPVKELELNFEIKGICFDGKLLAIATASKLFLYQFGNNLKLQRCLDTQNPKGLCAMVTTVEKTAIVFPSRKVGQLQILFLFKDHMNTSIVPAHDSEISCLGISKTGSKIASSSTNGTLIRIWNSETGEKICEFRRGYQHTAVCQLAFSPDELLLACASKKETLHIFSLHGSPNTIRQLTSEEPYEEASEFKSSTTEPRQTHWKRKLLKLIDSGKRAHWRIQLYQSNPVLLHWLDEMTILICYKDAAYQKLKLTIEESSKSVEHANQHVCFHYDYTLEADGSLC
The following text describes a protein:
Function:
Probable RNA-binding protein that plays a role in meiosis and vegetative growth.
Sequence:
MEHHLQNSVSVLSYYFKTTFGSNLVDSQSNKQSVEGGSEDTHTVGDITNSLTGSMLPGDEDELLAGITDDFDLGDLPTQLEDLEDDLFESGGGMEMDFDSHDGIRFGLSNLTMSDGVPLISINRHELLNSGNTVVVGEHPYGEHPSRTLFVRNINSNVEDSELKSLFEEYGEIRNLYTACKHRGFVMISYYDIRHARIAMRELQNKPLRRRKLDIHFSIPKDNPSEKDINQGTLVVFNLDSSISSDDLRHIFSVYGEVKEIRETPNKRHHKFIEFYDVRAAEVALKALNGSEIAGKRIKLEHSRPGGARRSMMQQLSQELEQDEARALWHHVGSPVINSPPGSWSSGFGTLSPVNTTPLHGLASILPPHISNPMKISPIGKDQQSSSRSFPDHHNTSSSFLDSKFDPSSSIGTLSGTEFLWGSPTTYSDHQSNSWRASPVGPFSPSQHGTFLGPPHHHVGSAPPGIPLDRSERSFMYNGNQMGSFGKGQMLFGNVTSYQGRGGGLNDGLMVGNRTRRVDSSVTQLGNNNNNNNKQYQLDLDKIITGEDMRTTLMIKNIPNKYTSKMLLAAIDETHTGTYDFVYLPIDFKNKCNVGYAFINMVSPSHIISFYEAFNGKKWEKFNSEKVATLAYARIQGKVALITHFQNSSLMNEDKWCRPILFQSEAQGNDYLDSIPYHNMNICIRQPDGSYSVDSFDSSNSSLEENQS
The following text describes a protein:
Function:
Mitochondrial RNA cytosine C(5)-methyltransferase that methylates cytosine to 5-methylcytosine (m5C) in various RNAs, such as rRNAs, mRNAs and some long non-coding RNAs (lncRNAs). Involved in mitochondrial ribosome small subunit (SSU) maturation by catalyzing methylation of mitochondrial 12S rRNA.
Subcellular Localization:
Mitochondrion.
Sequence:
MGRFQKQVCQFVLDYFDRTYTKELGNAWSTVREVLTSPECWQYAVLLNNFTSPWALEKQLHLKGYRLLFQEIFCPQTLQCFINGNPGKFPSQRHRTGKLKEYYVLNASSLLPVLALDVRDGEKWLDMCAAPGGKSIAFLQCATPGRLHCNEPDLPRSRWLKQTLESFVPETDRNHIFFSELDGRLLGKFHSGFYDKVLVDAPCSNDRSWLFSSDVQQAAARISQRKSLPVLQTELLRSAVEALRPGGSLVYSTCTLSRAENTDVITNILNSCSNVVPMDLSSMASALSHEFTFAPGIPHGLLVLPDNGKSWGPMFVAKLLKV
The following text describes a protein:
Function:
Probable serine lipid hydrolase associated with lipid droplets. Has low cholesterol esterase activity. Appears to lack triglyceride lipase activity. Involved in cholesterol and triglyceride homeostasis; stimulates cellular triglyceride accumulation and cellular cholesterol release.
Subcellular Localization:
Lipid droplet.
Sequence:
MELIEEIINLDEAIQGETRTEIIYTKSQTPSNIKIIVIAGNPGIESFYQEFVKVLNLSFNSKYDIYGVGHIGHCGKIENKTFSVEEQIKHKELFLEYLLKNKYGDKDRKDIKFILIGHSVGSYISLKVVSRFSEKFEFLSVVNLFPTFKNLYDGLSPFIKMVVMRESTRNGLSTFLHYIPSIVVSNVLKWILPSDESRIAVQSKINYYSALNILYMAYTETEDIKEIDDECHSVFNSRLNQLLFIYGQTDSYTPKSFYDEMKQLYPAGNIEYSSSYVPHAFVLHHSQEVALRVSEWLSLNILKN
The following text describes a protein:
Function:
Involved in the regulation of glutamine synthetase GlnA, a key enzyme in the process to assimilate ammonia. When cellular nitrogen levels are high, the C-terminal adenylyl transferase (AT) inactivates GlnA by covalent transfer of an adenylyl group from ATP to specific tyrosine residue of GlnA, thus reducing its activity. Conversely, when nitrogen levels are low, the N-terminal adenylyl removase (AR) activates GlnA by removing the adenylyl group by phosphorolysis, increasing its activity. The regulatory region of GlnE binds the signal transduction protein PII (GlnB) which indicates the nitrogen status of the cell.
Sequence:
MSDNRLDTARRHSLFLARQLDNGKLKPEIFLPMLDKVLTEADFQAFADWGEIRAEENEEELARQLRELRRYVVSQIIVRDINRISDLNEVTRTITLFADFAVNTALDFAYAYYRDMYGTPIGRYTKSPQHLSVVAMGKAGGYELNVSSDIDLIFVYPESGDTDGRRERGNQEFFTKVGQKLIALLNDITADGQVFRVDMRLRPDGDSGALVLSETALEQYLITQGREWERYAWCKGRVVTPYPNDIKALVRPFVFRKYLDYGAYEAMRKLHRQISSEVSKKGMADNIKLGAGGIREVEFIAQIFQMIRGGQMRALQLKGTQETLKKLAELGIMLSEHVETLLAAYRFLRDVEHRLQYWDDQQTQTLPTSPEQRQLLAESMGFDSYSAFSDGLNVHRNKVNQLFNEILSEPEEQTQDNSEWQWAWQDKPDEEGRRCRLKAHGFDAETVAARLDQIRHGHKYRHLSAHAQPRFDAVVPLFVQAAAAQSNPTDTLMRLLDFLENISRRSAYLAFLNEHPQTLAQLAQIMGQSSWVAAYLNKYPILLDELISAQLLDTAFDWQALAAALSDDLKACGGDTEAQMDTLRRFQHAQVFRLAVQDLAGLWTVESLSDQLSALADTILAAALLCAWADMPKKHRDTPQFAVVGYGKLGGKELGYASDLDLVYLYDDPHPDAGDVYSRLARRLTNWLSAATGAGSLYETDLRLRPNGDAGFLAHSIAAFEKYQRENAWTWEHQSLTRARFICGTSEIQTAFDRIRTEILTAERDQTALAGEIIEMREKMFPTHPPADSNVKYARGGVVDVEFIVQYLILAHARQYPQLLDNYGNIALLNISADCGLIDKTLAGQSRTAYRFYRRQQHNTKLRDAAKTEVTGELLAHYGNVRKLWREVFGEEAATV
The following text describes a protein:
Function:
Histone chaperone involved in single-strand and double-strand DNA break repair (By similarity). Recruited to sites of DNA damage through interaction with branched poly-ADP-ribose chains, a polymeric post-translational modification synthesized transiently at sites of chromosomal damage to accelerate DNA strand break repair reactions (By similarity). Following recruitment to DNA damage sites, acts as a histone chaperone that mediates histone eviction during DNA repair and promotes recruitment of histone variant MACROH2A1. Also has a nuclease activity: displays apurinic-apyrimidinic (AP) endonuclease and 3'-5' exonuclease activities in vitro (By similarity). Also able to introduce nicks at hydroxyuracil and other types of pyrimidine base damage (By similarity). Together with PARP3, promotes the retention of the LIG4-XRCC4 complex on chromatin and accelerate DNA ligation during non-homologous end-joining (NHEJ). Also acts as a negative regulator of cell pluripotency by promoting histone exchange. Required for the embryo implantation during the epithelial to mesenchymal transition in females.
Subcellular Localization:
Nucleus. Chromosome. Cytoplasm, cytosol. Note=Localizes to DNA damage sites. Accumulates at single-strand breaks and double-strand breaks via the PBZ-type zinc fingers.
Domain:
The PBZ-type zinc fingers (also named CYR) mediate non-covalent poly-ADP-ribose-binding. Specifically recognizes branched poly-ADP-ribose chains generated by PARP2. Poly-ADP-ribose-binding is dependent on the presence of zinc and promotes its recruitment to DNA damage sites; The KBM (Ku-binding motif) mediates interaction with XRCC5/Ku80 and XRCC6/Ku70 and recruitment to DNA damage sites; The FHA-like domain mediates interaction with XRCC1 and XRCC4; The NAP1L motif is required for the histone chaperone activity.
Sequence:
MPSDFFLQPLDGGPRVPVGPGQTVIGRGPLLGITDKRVSRRHAILEVVDSQLRIKPIHRNPCFYQSSEKSQHSPMETQVWSQLHPGDSFSLLLDKYAFRVFSAESEVEMECTLRNSQMLDEDDILSEMQKSPVVNLPDKTTGASQLQGSPEITKTKCPTIDPMSSSGECRAFSEHQPRPTQRKRILPAWMLAESLSDQSLSTPAEGGDKDVIQRSGKAGTCEDRTPGNTSWHGKKRLSPSGNSKSVSAEQDPGKKCRKADQEGPGVSSENVPESSSSNIVKDPDVDIVKTNKQKDGILIEELGEVSKHKAATKPTTNEEGESCARVQSKSPPEKSQGCHPESSSAPSSPDALHTDTADPVLGCSEESKVRRTACMYGANCYRRNPLHFQHFSHPGDSDYGEVHGTDEGVIGDRPECPYGASCYRKNPQHKMEYRHSALPARVALDEDDDDVGQPSDDEDEEDYEPTDEDSDWHPGKDDEEQEDVDELLKEAKSSLHLKH
The following text describes a protein:
Function:
During fertilization, required on male gametes for their fusion with female gametes, and for subsequent ookinete formation in the host. Thereby, required for mosquito-mediated transmission to other animals. Probably initiates the fusion of gamete cell membranes by inserting part of its extracellular domain into the cell membrane of a female gamete.
Miscellaneous:
MISCELLANEOUS: HAP2/GCS1 family members mediate membrane fusion between gametes in a broad range of eukaryotes, ranging from algae and higher plants to protozoans and cnidaria, suggesting they are derived from an ancestral gamete fusogen. They function similar to viral fusogens, by inserting part of their extracellular domain into the lipid bilayer of an adjoining cell.
Subcellular Localization:
Cell membrane; Single-pass type I membrane protein.
Domain:
The N-terminal extracellular domain is important for gamete fusion.
Sequence:
MKNKLINLRSKHIYKLIIIIFFCIILKYYKWCDFKNKVFFIQLVYSFAKKSVCTSSLDDSTCHTVTFGELDVSNNSVVRLKVMRKGGKGYFLTIRRDYVTVSYYLKYVKDIPLEFREIIDIFNNHKFEQYTQEQINKYTYTCNVRKIEDIDKYDEKNPTKFHEYTRGEACRCQTYNYFKDDEFIKRAKLKCIYYNMLFTESATVYSRHCPIIDLMHFAVYDIEYPPIFNTIVNITIEEYYYNDVSSVLNNKSDLVTKEKKYQLNDTITEIRDDYFDLWLFLKGETHGKRTLVNLSNDYIVIPSSPINNRDVIASDITRNCGLSQNSPLLKGCNYSSICNIMHPCLRKAMMLPKYMFDLSGKTCGKLGVSLNTWRKSEGNFCGSEAGYCISNNLKKYYDIHNSASIKDGISLSKYKIKNIYNSEPQTKIYESYKLPDYLKDKIKNNNHAEMDENDLDNKIFYKPNVAAHSQFIDYKYNGNHSVEIKFETDAIEVYEIRPVSIATITHVTIPNDCASNNSNSNECVLIIHVWNNSKFVGSNFSCSIACTNKETDQLASHINPIAPVRAFIGPNKNYAFYFIIKFLINKEITTLCKAIVKDSNGKECSIEEFELQSKESVHIVESEVDETTDQVVVEHHTQSPDIKNPDEYVCKCTINLLCYVINFKTCSNYYINTVKTLIGKFAIIAILIILAPALIPLLPFFLNFFFLFISTILKLYQSIISTIGQIRIRNNDKPIIYKKKIHDMKTNYLSVSSYSSLSDSSSIYSTDSVSSMRKNKKKFNKNNISSNIKHKKGGKKVKQKEPNRNSNHTSHEYADTSPSGKSKIPPLR
The following text describes a protein:
Function:
Plays a role in intracellular trafficking and contributes to the macromolecular organization of group 1 metabotropic glutamate receptors (mGluRs) at synapses.
Subcellular Localization:
Cell membrane; Peripheral membrane protein; Cytoplasmic side. Cytoplasm, perinuclear region. Postsynaptic cell membrane.
Sequence:
MTFRRLRKLQHKEEYACPPDRTVYRDRDKLDPYSALTSYKQADMYKALAVSGGTLPRTKKGSTAGWKNVSQSSEYQRKILTLQKEDSESFGFEIQTYGLHHQDKNAVEMFTFVCRVQDGSPAQLCGLKVGDIIAGVNGLNMDGVRHRDIVELIKVSGNTIRLETVYGSAIRRAELEARIQYLKQTLYEKWEEYRSLMVQEQRLLHGIVVKDPSVYDTLESVRSYIYGTVNTCSKDPLTGTLAAGSMCSSASCLSTTEENEDAVYQTCYFSSDSTDEINSLPGKSNNNGKPYKSTLTRSSSVKCPGPATNWDKPKEQNNFVSLPRKKHKSFRKRLLKFIPGLNRNLEEEASPL
The following text describes a protein:
Function:
Involved in the lipid remodeling steps of GPI-anchor maturation.
Subcellular Localization:
Endomembrane system; Multi-pass membrane protein. Golgi apparatus membrane; Multi-pass membrane protein.
Sequence:
MTEAGRKMDAGRLWHLLLLLIFATGASANWHDSRFRSCLSTCETIGCVGKSCLPSCTYLNATAAGDDSQQDVTSPPLSRKWQTWICKTECDYHCTLSKETEEAGFSQEAIGYRDDWCLARSVDHHEESKKLYSHLLKTGLTRGFTLATVNEPASAAFCVLNILGNIIGLFAFFQSRQYSLPKRQSACAPYPYSSLWTGFGLLSILYWISRCMLHSREMAVDKHLESSFEILLSMYALCLAIMRVGKMKTEASRVIVAAPTLAFLYTHLMYINYCVYDYGLNMQLCLGLALVQYLIWISWVSVVKHPGRYQLGLSAITASLVVFLRLSVMNAKWPFFNGETEALWIASTLPLTFIWWSFAITDATYLTTLRSDKKATTESESKKDL
The following text describes a protein:
Function:
Converts the abundant, but inactive, zymogen plasminogen to plasmin by hydrolyzing a single Arg-Val bond in plasminogen. By controlling plasmin-mediated proteolysis, it plays an important role in tissue remodeling and degradation, in cell migration and many other physiopathological events. During oocyte activation, plays a role in cortical granule reaction in the zona reaction, which contributes to the block to polyspermy.
Subcellular Localization:
Secreted, extracellular space.
Domain:
Both FN1 and one of the kringle domains are required for binding to fibrin; Both FN1 and EGF-like domains are important for binding to LRP1; The FN1 domain mediates binding to annexin A2; The second kringle domain is implicated in binding to cytokeratin-8 and to the endothelial cell surface binding site.
Sequence:
MYALKRELWCVLLLCGAICTSPSQETHRRLRRGVRSYRVTCRDEKTQMIYQQHQSWLRPLLRGNRVEHCWCNDGQTQCHSVPVKSCSEPRCFNGGTCLQAIYFSDFVCQCPVGFIGRQCEIDARATCYEDQGITYRGTWSTTESGAECVNWNTSGLASMPYNGRRPDAVKLGLGNHNYCRNPDKDSKPWCYIFKAEKYSPDFCSTPACTKEKEECYTGKGLDYRGTRSLTMSGAFCLPWNSLVLMGKIYTAWNSNAQTLGLGKHNYCRNPDGDTQPWCHVLKDHKLTWEYCDLPQCVTCGLRQYKEPQFRIKGGLYADITSHPWQAAIFVKNRRSPGERFLCGGILISSCWVLSAAHCFQERFPPHHVRVVLGRTYRLVPGEEEQAFEVEKYIVHKEFDDDTYDNDIALLQLKSDSLTCAQESDAVRTVCLPEANLQLPDWTECELSGYGKHEASSPFYSERLKEAHVRLYPSSRCTSKHLFNKTITNNMLCAGDTRSGGDNANLHDACQGDSGGPLVCMKGNHMTLVGVISWGLGCGQKDVPGVYTKVTNYLNWIRDNTRP
The following text describes a protein:
Function:
May be involved in regulating transcriptional activation of cardiac genes during the aging process. May play a role in biosynthesis and/or processing of SLC2A4 in adipose cells.
Sequence:
MVKKVKKIDDSASIEMPMAQIDDADDVAEDYEVFDMSNIAAPVIEFELPNLVAKNAPKTMEKAENDRKSMKKPKKSVKIAPEAQKSDSEGEEGSDARRPENAQKSLRKEAKKAPEAQKLAEKDAETGRIQLTAEKLNNELVGLRATVTKAKDQWISKVIRKKKELEKKRKEGKGGKEEVVDAKLNRMMEEILALKTIDRDTIAKFASLNTKTLNELKIDGSTPMAEQVMYKLACHEVVVSRIQAIKQKYIEWNKTAAFFMQRLGRQYSTKPEKKEKKAKHSDETKGIQKAKTDSENVVDSGEESDVEEDALDDSEDVEKEEEEGEDAPDDYDQSDVEMVDSDDEDVGVEAAKKRRNMLLNLIGVKEDASRPALNPKKRKIVDDDSQDVTETTSSEPSKKQKTKEAMKAVLEKALKAEKVEKPKKMVPKKVEVSSEVESEDVEEEADDVEEEEDPNQQTLVMKIDLSQGGKIAKSTAAPKSTMAAHAPKKASEDVEEENSEDESSGFFLPASSKGTSSASKSKAVPESGGIAKKMEKLGVEEDLKMKKNKNTKKKGPVGKKNFQPPATTTENKKKGTSKNSTSSEGQMHPSWLASQAKKKELAAAKPAGKRILFNDED
The following text describes a protein:
Function:
Putative transcription factor. Positive regulator of the lin-12/Notch signaling pathway. Binds to specific DNA sequences in regulatory elements. Involved in cell fate decisions that require cell-cell interactions, such as the anchor cell (AC) / ventral uterine (VU) precursor cell fate decision. Heterochronic protein which controls the choice of stage specific cell fates, including the larval L3 stage-specific fate of seam cells. Involved in regulating the temporal expression pattern of hunchback-like protein hbl-1, thereby playing a role in the progression between larval stages L2 and L3.
Subcellular Localization:
Nucleus.
Sequence:
MAQPNQPTPQFQMAQIPLAAFFDNNESKTMLNSMNLRLNDMDLKLSLILELLATRLPDQRLPSIFTSPPQTVISEAPPQSFTPSATNSTSDKTSSSLKTELKTEDSDGDLDMEGEEDTEELFDNESQPSQRNQSPKETEVEDEKVLADGPFPEGAVKRAAEKAARSFQSTQPKVFAWQILRESVTDDELRNVQISLRTFHGETADHLLGRQLPKIRLVVEATMKYFKWDLLSTESQLSKAKLILSHLKNNAKVRNWTLREGRPNRVAPATPPVNVDLVWKRYLALLGPAGFTGILPNLPQNLCNGGTQSPSIPQIDPSLFKVDA
The following text describes a protein:
Function:
Arginine methyltransferase that can both catalyze the formation of omega-N monomethylarginine (MMA) and symmetrical dimethylarginine (sDMA), with a preference for the formation of MMA. Specifically mediates the symmetrical dimethylation of arginine residues in the small nuclear ribonucleoproteins Sm D1 (SNRPD1) and Sm D3 (SNRPD3); such methylation being required for the assembly and biogenesis of snRNP core particles. Specifically mediates the symmetric dimethylation of histone H4 'Arg-3' to form H4R3me2s. Plays a role in gene imprinting by being recruited by CTCFL at the H19 imprinted control region (ICR) and methylating histone H4 to form H4R3me2s, possibly leading to recruit DNA methyltransferases at these sites. May also play a role in embryonic stem cell (ESC) pluripotency. Also able to mediate the arginine methylation of histone H2A and myelin basic protein (MBP) in vitro; the relevance of such results is however unclear in vivo.
Miscellaneous:
MISCELLANEOUS: Confers resistance or sensitivity to DNA-damaging agents. Down-regulation confers increased sensitivity to the Top1 inhibitor camptothecin (CPT).
Subcellular Localization:
[Isoform 1]: Cytoplasm. Nucleus; [Isoform 2]: Cytoplasm.
Sequence:
MKVFCGRANPTTGSLEWLEEDEHYDYHQEIARSSYADMLHDKDRNIKYYQGIRAAVSRVKDRGQKALVLDIGTGTGLLSMMAVTAGADFCYAIEVFKPMADAAVKIVEKNGFSDKIKVINKHSTEVTVGPDGDLPCRANILVTELFDTELIGEGALPSYEHAHRHLVQENCEAVPHKATVYAQLVESRRMWSWNKLFPVHVQTSLGEQVIVPPSELERCPGAPSVYDIQLNQVPSTDFTALSDVLPMFSVDFSKQVSSSAACHSKQFVPLASGQAQVVLSWWDIEMDPEGKITCTMAPFWAQTNPQELQWRDHWMQCVYFLPQEEPVVQGSPRCLVAHHDDYCVWYSLQRTSADENEEVYQVRPVCDCQAHLLWNRPRFGEINDQDRTDQYAQALRTVLMPGTICLCVSDGSLLSLLAHHLGAEQVFTVESSAASYRLMKRIFKANHLEDKVSIIKKRPELLTSADLEGKKVSLLLGEPFFATSLLPWHNLYFWYARTSVDQHLEPGAVVMPQAASLYAMIVEFRDLWRIRSPCGDCEGFDVHIMDDMIKHSLDFRESREAEPHPLWEYPCRSLSEPQQILTFDFQQPVPQKPVHAEGSMELRRPGKSHGAVLWMEYHLTPDSTVSTGLMNPLEDKGDCCWNPHCKQAVYFLSTTVDPRVPLDGPQSVSYAVEFHPLTGDITMEFRLADTLN
The following text describes a protein:
Function:
Component of the intraflagellar transport complex A (IFT-A) involved in flagellar assembly.
Subcellular Localization:
Cell projection, cilium, flagellum. Cytoplasm, cytoskeleton, flagellum axoneme. Cytoplasm, cytoskeleton, flagellum basal body. Note=Localizes to the cytoplasmic and membrane-bound portions of each of the eight axonemes, localizing particularly at the flagellar pores and at the distal flagellar tips. Localizes to the basal bodies. Main cytoplasmic localization in the posteriolateral axonemes.
Sequence:
MIQITIDVILEDPTLCVVQLYTQVSSQTVFALLSDGSLAVLYPNDNNALVLASKTSMANQLPVDILRKVITTDEGQVQVPITALACHPFVENLVVVGFKDASFSIWFPTDSDPSYKTELHQEELCLIKWLSHGRILVTCDVSGQVILYKFSTDTYSFESITKTRKSGHVVDIVERTCCTDNIIYSIDQEHSDHPIDVSNYAGVGLCEFIVMWSKGDVAVLTDNGVIRHIGTVNLSAGHALLYKLYYWSCSDTCCAISTSGDMFLFGFKTLAVGAYKDILAKYKIEYKRENGIVQLPATKIAYMAPSDGQLRVLSLLTQEVAYIDLEDHIENFVGVNGGLAVIRDYGILIPLRGKNGYAVVSCHRSTGSCDSNGNEGMHILAASDHYLHANDMRFARVQDSNGPSSGPRIRPGSDEFIVTEQHFLHAENPRCSYANIYMSQIVVGDNSFSQTMITNYSITNRNVVSNKMLPIFHDEGGKPINLPPGFSPETASTPEGVDDATIDSFSAEIISSRGKFVSLLLFSFEPKDMQVAYANNTNSAIMAQDLTGEGLTHMKFLDQKFTDSRNSFISAVLIGARIIKVSVNTNANLLQEHTLEIKHPIKKISILTNPLTSVSSDNLSGFVLAFGDNVFTVFEVAIGKVPHLAGSFKLDERYTYVADCVLYGRYILASQNSRADLESDYLKVEIVKYSITGSKAGSLVLSDDPTHGATVERIARMTLVNQHLFMINNNLSLFYTDCKTFNSVVKITDIGQLMFNTNIYCAYLEEEDLDDIHLSTPDTGSPAVEAEESPQRQTREEKIKDLLLVENTMQINQQLHDRIKQERKEQNVISVYTTLPTLIPLDTICVQSCNATITLDNAHHVLFTVVFKGYNVVTGLPCLLPYVVALSIDTKILGEMISAGLTATPSQPTEKVGSRPTTGSDGGSAVLKSRIFDMAPYTVTNAIPDCFGNIGLELVLSTSLNLLFVGSSMLFALKTGTFTKRALSSKNLSAYLSWLDSKEKGSQRNADLVFQQEKYEDQISLLQSIYISSEQRAKVPLLVQSLAETTISMNDRIKGSWLDFNDKIFLSIQGVFAPYVNSKLETLMQPLSSTMLTLLSPAFVFSERSGKSEKPRTSNFVSINSDRLTIKNLTALGSSKKTGFQQSCTATYALNKFTICSSNGQLAEAYSHVLVSENLHVWRSLATLCIQNGYVDLLKTCTTHLKSPILSLLMRLVTNRKRSDAADTGQDQLKTKLAPQDELLLALLSIALGASAQGLDRLQGKPLLLSGVMNDIGLSIRYLMSDGAHSSLQQTGGLTSLAKKSSILSLANRLIHLNDLESSKICYSEVYKAPVAAQGEIDSLNANPQQLLQQNESVQFLNDEYKKKGVAACLTLAKKGTDPQFLYVAARMIESEAKSRDVKSDIPGKMKDELDQQTLWLEAARLYKRCSAFTHALACALKCEDDELIYNIGTTSQSQRLSLVAATYFSNKYKSGLITISEKGRDNVSEDFCDELQATIEHALVLYKSAGLGAQSLELCIKSNRMKELSNLLADILSEPSKSLDRELDDDVVLQEQSTTTQGTGDVLQGISSDLLLRAGRALLDVSPEDYSLNDYNSFIRTAVIALAKASAYQDALQAILDGKIQISERIADILTPASIEHDEEAVRVTETLGKLLHKAGLYQSAVKKFILAQNHTLAINSLIKQGDPMKVIKFANMARQKQVYIAASNFLQTLDWRSNPTYMKAIISFYEKANSLENIAKFFANCAAEEISEYHDYVKAKQAIIEAMNRQKVAIDYVEQNASSKESEKVATARAAKVASLKKTLQAYEQNGKLIHAFLQLCDFARDTSQAHDSSETLTTNSSKLLTAVRKMENCYVKPGDIMGLLAEFHGVRGEKARIVSIIKDMCNEGIDPENYLAADLYAAHAAEAGLTVVNKALELEDIDLTAEKSDH
The following text describes a protein:
Function:
O-methyltransferase that catalyzes the 2 O-methylation steps in the ubiquinone biosynthetic pathway.
Subcellular Localization:
Cytoplasm.
Sequence:
MNAEKSPVNHNVDHEEIAKFEAVASRWWDLEGEFKPLHRINPLRLGYIAERAGGLFGKKVLDVGCGGGILAESMAREGATVTGLDMGFEPLQVAKLHALESGIQVDYVQETVEEHAAKHAGQYDVVTCMEMLEHVPDPQSVVRACAQLVKPGGDVFFSTLNRNGKSWLMAVVGAEYILRMVPKGTHDVKKFIKPAELLGWVDQTSLKERHITGLHYNPITNTFKLGPGVDVNYMLHTQNK