lhallee/plat_data huggingface dataset:
The following text describes a protein:
Function:
Self-glucosylating initiator of glycogen synthesis. It catalyzes the formation of a short alpha (1,4)-glucosyl chain covalently attached via a glucose 1-O-tyrosyl linkage to internal tyrosine residues and these chains act as primers for the elongation reaction catalyzed by glycogen synthase. Capable of transferring glucosyl residues to unbound acceptors such as free oligoglucans or oligoglucan derivatives.
Subcellular Localization:
Cytoplasm. Vacuole.
Sequence:
MLVGIATLLYSADYLPGAFTLAFRVRELLVESREHRLVLLATPEVLDNVSEDVLRALHELYDEVIRLAGDESASKTALARHRTNLAALGRPELADTFHKLQLWKLTQFRKVLYLDCDAFPLHSGFLEAVDQVPDQAPRQLAAVPDCGWPDLFNSGVMVLVPSLAVHGELAAHVETALSIDGADQGLLNLFFNRACHRGTLPNEWRTLPFLYNVTVPNAGYQATPALDYFRRRIAVVHFIGHEKPWISRGVSDSFRELWWQTYNRFLARHFSCPAFSTGNASEGPDVSAPQADGTQSWAPAPESRQAARAFAARPAAPAHDPYSSAPVCESHAGTPVYESHAGAPAFESHSGAPAFESHSGAPAYESHAGAPAAEQQPQAYSQSWAPLPSPQPPAPAPKTHLWTPMQEPQLAVPSCPEPLPSAPCAWDGTKEPPSKDAPPEAYKLALVGTYSWSTASPTLVPEDALLAESASLGSPFHSCKSTDKLPLCNPSPGPPRPAPAAAPRPPGIHLPAPAAPARPRPVRSSLQPAPELLRPEPPAVAPAAASSSAAPAPPAAPAADPAPTEAPRASPAPAAAAAPPLFPWERYKPKSTRVFPE
The following text describes a protein:
Function:
Receptor which may mediate L-selectin-dependent lymphocyte rollings. Binds SELL in a calcium dependent manner. Binds lymphocyte (By similarity).
Subcellular Localization:
Apical cell membrane; Single-pass type I membrane protein. Basolateral cell membrane; Single-pass type I membrane protein. Endosome, multivesicular body membrane; Single-pass type I membrane protein. Note=Transcytoses across the cytoplasm.
Domain:
Ig-like V-type domain mediates binding to lymphocyte.
Sequence:
MRLLVLLWGCLLLPGYEALEGPEEISGFEGDTVSLQCTYREELRDHRKYWCRKGGILFSRCSGTIYAEEEGQETMKGRVSIRDSRQELSLIVTLWNLTLQDAGEYWCGVEKRGPDESLLISLFVFPGPCCPPSPSPTFQPLATTRLQPKAKAQQTQPPGLTSPGLYPAATTAKQGKTGAEAPPLPGTSQYGHERTSQYTGTSPHPATSPPAGSSRPPMQLDSTSAEDTSPALSSGSSKPRVSIPMVRILAPVLVLLSLLSAAGLIAFCSHLLLWRKEAQQATETQRNEKFCLSRLTAEEKEAPSQAPEGDVISMPPLHTSEEELGFSKFVSA
The following text describes a protein:
Function:
Binds the phosphorylated C-terminal domain (CTD) of the largest subunit of RNA polymerase II and functions as a scaffold for RNA processing machineries. May be involved in pre-mRNA splicing.
Subcellular Localization:
Nucleus.
Sequence:
MAGRGRAATLPAWMTSGSAPAPGAPGGAPVPAPSPGPGAPGAPPFGAPHGGHPPPGSHMHSGPPSGGAGPPQHLPPPPGSGPPPGGMQGPGGQGGAPPGQGPPMQGPPGMMVRPPAPGGPGAPPPGWQPGMGPPPPGMGFPPPGTHLPPPGMGLPPPGWQPGMGAPPPGMGLPPPPAGWHPGMGQPPGYPPRPGFPPPGMAPPGFPSGMAPPPGMHQGMHPGMHPGMPGMPGLPLPPGGPGGPQQQQQQQQLPAGQPPAGPGAGAPAPSSAGPAGASTPGAAGGGGAPGGPGAGVGGGGGGPAKEWTEHTAPDGRKYYYNAKTKQSSWEKPDELLSGAEKTDAPAWKEYTAPDGRKYYYNKATKESRWTMPEEMKAAAAGGGGGGAGAGAAPKSAGGVQVVSLTGASGAAAAAAAAPAGGGGDSRSSPSGADGPSASAQSGEPKNYNFATKEEAKDCFKELLAAVGCRSDWSWEQAMRHIVNDPRYSALKSLGERKQTFNEYVQARRNEEREEERRRQRQAREDFTAMLMSSDELKTTHPFRRARELFESDARWKAVPEREREELFHDAQRERDKRDKEERRQERKRRAGAFRDLLEREGVKQGAEWRKVSKRLEGEDEYEALDKVERLEVFQEYMKDMERREKEDKEREREERKRQERKARDAFKELLKKHRDEGLIGLRSRWKEYVDAAALTGEEAYRAVEANSSGSRPKELFEDVVEDMEEEYDKSIKPFFKALLKAAPADFALTPTTTYEATEEALAAAAAGEGAEPDAATRLNSLLPTYKRCFWEDAVAKARSREAEEAERRRRARDKLASYMRHARPVVREDSAWEQWLAEHEREPEVRALSLDEARAVFDEVQARARRKAEAAHSDDDSGGGGGSRRRRGSRSDDEDGYDGGRSKKSHKEKKSSKRHDRSDDDDEPVKSKKHKKDKDKDKDRERERSERAGGGSRGPPPPQPPPPAEDSDRDSGEIRE
The following text describes a protein:
Function:
Plays a role in the transport of the budded virion (BV) to the host nucleus and for occlusion of viral progeny.
Subcellular Localization:
Host cytoplasm. Host nucleus.
Sequence:
MECPFQIQVCISDRFFAFPHNLVEPQSDVGNKLIENLIVYVPTDDDRLYIDKKQFPKFNSVLVYRHEHDVNIDSRSPKKTASATIVYWNPLVPITEIGAGETRVFSVLLTNNLFYCNTMIVHHENPKCPIEFTYPETDMQSACSALLKNRNGQSVPPPIKSNLRPIACEIPLSHFKELVESNDFLLCFNLETSTMVKILSLKRIFCIFQYRKQPARYVINLPHEEIDNLYNKLNWERTRRLMKGDVPSNCATVNRSSLKYIKQAQSLLGIPDYSQTVVDFVKMFQKIIFPYQLVPNVIIKLNNFDQMVSSAPNKAEPYKKIRLFCKNDSIAISSSGIVPINMPDFSPPNTFDYSDYANRTNINFVTQRVLTDGGFSSGITVTPVKYNYYL
The following text describes a protein:
Function:
Component of the sarcoglycan complex, a subcomplex of the dystrophin-glycoprotein complex which forms a link between the F-actin cytoskeleton and the extracellular matrix.
Subcellular Localization:
Cell membrane, sarcolemma; Single-pass type II membrane protein. Cytoplasm, cytoskeleton.
Sequence:
LSIFVFLQALPSTLSMREKAMLKEEINKRHNGNFSAGYVPIFESTLHKTGLRGRKALLFYGLVVGLFIVSLANLAVTMMLVGVLRIGYGMESLEFLPGAQLVRFLNNADLGRVILHKGVIGAFKDSDLTITGNAHPASLKIFFVASGASLEVGPDRTVVSNVGEFRVRSPTTGRTIFSTEYQGFDLPKGIPNLNVKEAHVSRLTSAKQDSLLISSPYQIMLKGNAGLDMEGQNVTLSAGHNLFLRSNQSVTLDGRKGIRLSVDKLPISTDPSSGAQFQYKLCVCMPSGRLFRVPVREQGFGCNDVRFPESINPCS
The following text describes a protein:
Function:
Non-catalytic component of the RNA exosome complex which has 3'->5' exoribonuclease activity and participates in a multitude of cellular RNA processing and degradation events (By similarity). In the nucleus, the RNA exosome complex is involved in proper maturation of stable RNA species such as rRNA, snRNA and snoRNA, in the elimination of RNA processing by-products and non-coding 'pervasive' transcripts such as antisense RNA species, and of mRNAs with processing defects, thereby limiting or excluding their export to the cytoplasm (By similarity). In the cytoplasm, the RNA exosome complex is involved in general mRNA turnover and specifically degrades inherently unstable mRNAs containing AU-rich elements (AREs) within their 3' untranslated regions, and in RNA surveillance pathways, preventing translation of aberrant mRNAs (By similarity). The catalytic inactive RNA exosome core complex of 9 subunits is proposed to play a pivotal role in the binding and presentation of RNA for ribonucleolysis, and to serve as a scaffold for the association with catalytic subunits and accessory proteins or complexes (By similarity). Required generally for normal embryonic and neuronal development. Also plays a critical role in the maintenance of neuronal function in mature flies by controlling the levels of specific mRNAs such as the synaptic regulator Arc1.
Subcellular Localization:
Cytoplasm. Nucleus, nucleolus. Nucleus.
Sequence:
MSATSTIVMPGERIAAIEELAKSKRVILGPGLRRLDDTVVASKAGPLRHKEPGTFWVDNYQRRYIPARGDLILGIVRAKAGDLYRVDIGATDTASISYLAFEAASKKNRPDLIPGDLIYARVLNASADIEPELVCVNSVGKSGKLGVLTDGFFFKCSLNLGRMLLRENCPVLAALTRELPYEIAVGVNGRIWLKAHSLKETVALANAISALEQSGCAEIDKICGNLGDFLQA
The following text describes a protein:
Function:
Hydrolase that removes conjugated ubiquitin from target proteins and regulates various pathways such as the TGF-beta receptor signaling, NF-kappa-B and RNF41/NRDP1-PRKN pathways. Acts as a key regulator of TGF-beta receptor signaling pathway, but the precise mechanism is still unclear: according to a report, acts by promoting deubiquitination of monoubiquitinated R-SMADs (SMAD1, SMAD2 and/or SMAD3), thereby alleviating inhibition of R-SMADs and promoting activation of TGF-beta target genes. According to another reports, regulates the TGF-beta receptor signaling pathway by mediating deubiquitination and stabilization of TGFBR1, leading to an enhanced TGF-beta signal. Able to mediate deubiquitination of monoubiquitinated substrates, 'Lys-27'-, 'Lys-48'- and 'Lys-63'-linked polyubiquitin chains. May also regulate gene expression and/or DNA repair through the deubiquitination of histone H2B. Acts as an inhibitor of mitophagy by counteracting the action of parkin (PRKN): hydrolyzes cleavage of 'Lys-48'- and 'Lys-63'-linked polyubiquitin chains attached by parkin on target proteins such as MFN2, thereby reducing parkin's ability to drive mitophagy. Acts as an associated component of COP9 signalosome complex (CSN) and regulates different pathways via this association: regulates NF-kappa-B by mediating deubiquitination of NFKBIA and deubiquitinates substrates bound to VCP. Involved in endosome organization by mediating deubiquitination of SQSTM1: ubiquitinated SQSTM1 forms a molecular bridge that restrains cognate vesicles in the perinuclear region and its deubiquitination releases target vesicles for fast transport into the cell periphery. Acts as a negative regulator of antifungal immunity by mediating 'Lys-27'-linked deubiquitination of CARD9, thereby inactivating CARD9.
Subcellular Localization:
Cytoplasm. Nucleus. Mitochondrion.
Sequence:
MAEGGAADLDTQRSDIATLLKTSLRKGDTWYLVDSRWFKQWKKYVGFDSWDKYQMGDQNVYPGPIDNSGLLKDGDAQSLKEHLIDELDYILLPTEGWNKLVSWYTLMEGQEPIARKVVEQGMFVKHCKVEVYLTELKLCENGNMNNVVTRRFSKADTIDTIEKEIRKIFNIPDEKEARLWNKYMSNTFEPLNKPDSTIQDAGLYQGQVLVIEQKNEDGTWPRGPSAPNVKNSNYCLPSYTAYKNYDYSEPGRNNEQPGLCGLSNLGNTCFMNSAIQCLSNTPPLTEYFLNDKYQEELNFDNPLGMRGEIAKSYAELIKQMWSGKFSYVTPRAFKTQVGRFAPQFSGYQQQDCQELLAFLLDGLHEDLNRIRKKPYIQLKDADGRPDKVVAEEAWENHLKRNDSIIVDIFHGLFKSTLVCPECAKISVTFDPFCYLTLPLPMKKERSLEVYLVRMDPLAKPMQYKVIVPKIGNILDLCTALSALSGVPADKMIVTDIYNHRFHRIFAMDENLSSIMERDDIYVFEININRTEDTEHVVIPVCLREKFRHSSYTHHTGSSLFGQPFLMAVPRNNTEDKLYNLLLLRMCRYVKMSTETEETDGPLRCCEDQNINGNGPNGIHEEGSPSEMETDEPDDESSQDQELPSENENSQSEDSVGGDNDSENGLCTEETCKGRLTGHKKRLFTFQFNNLGNTDINYIKDDTRHIRFDDRQLRLDERSFLALDWDPDLKKRYFDENAAEDFEKHESVEYKPPKRPFVKLKDCIELFTTKEKLGAEDPWYCPNCKEHQQATKKLDLWSLPPVLVVHLKRFSYSRYMRDKLDTLVDFPISDLDMSEFLINPNAGPCRYNLIAVSNHYGGMGGGHYTAFAKNKDDGKWYYFDDSSVSSASEDQIVSKAAYVLFYQRQDTFSGTGFFPLDRETKGASAATGVPLESDEDSNDNDNDLENENCMHTN
The following text describes a protein:
Function:
Serine/threonine-protein kinase component of the WNK4-SPAK/OSR1 kinase cascade, which acts as a key regulator of ion transport in the distal nephron and blood pressure. The WNK4-SPAK/OSR1 kinase cascade is composed of WNK4, which mediates phosphorylation and activation of downstream kinases OXSR1/OSR1 and STK39/SPAK. Following activation, OXSR1/OSR1 and STK39/SPAK catalyze phosphorylation of ion cotransporters, such as SLC12A1/NKCC2, SLC12A2/NKCC1, SLC12A3/NCC, SLC12A5/KCC2 or SLC12A6/KCC3, regulating their activity. Acts as a molecular switch that regulates the balance between renal salt reabsorption and K(+) secretion by modulating the activities of renal transporters and channels, including the Na-Cl cotransporter SLC12A3/NCC and the K(+) channel, KCNJ1/ROMK. Regulates NaCl reabsorption in the distal nephron by activating the thiazide-sensitive Na-Cl cotransporter SLC12A3/NCC in distal convoluted tubule cells of kidney: activates SLC12A3/NCC in a OXSR1/OSR1- and STK39/SPAK-dependent process. Also acts as a scaffold protein independently of its protein kinase activity: negatively regulates cell membrane localization of various transporters and channels (CFTR, KCNJ1/ROMK, SLC4A4, SLC26A9 and TRPV4) by clathrin-dependent endocytosis. Also inhibits the activity of the epithelial Na(+) channel (ENaC) SCNN1A, SCNN1B, SCNN1D in a inase-independent mechanism. May also phosphorylate NEDD4L (By similarity).
Subcellular Localization:
Cell junction, tight junction. Note=Present exclusively in intercellular junctions in the distal convoluted tubule and in both the cytoplasm and intercellular junctions in the cortical collecting duct. WNK4 is part of the tight junction complex.
Domain:
The RFXV motif mediates recognition with downstream kinases OXSR1/OSR1 and STK39/SPAK.
Sequence:
MLAPRNTETGVPMSQTEADLALRPSPALTSTGPTRLGPPPRRVRRFSGKAEPRPRSSRPSRRSSVDLGLLSSWSQPASLLPEPPDPPDSAGPTRSPPSSSKEPPEGTWMGAAPVKAVDSACPELTGSSGGPGSREPPRVPDAAARERRREQEEKEDTETQAVATSPDGRYLKFDIEIGRGSFKTVYRGLDTDTTVEVAWCELQTRKLSRAERQRFSEEVEMLKGLQHPNIVRFYDSWKSVLRGQVCIVLVTELMTSGTLKTYLRRFREMKPRVLQRWSRQILRGLHFLHSRVPPILHRDLKCDNVFITGPSGSVKIGDLGLATLKRASFAKSVIGTPEFMAPEMYEEKYDEAVDVYAFGMCMLEMATSEYPYSECQNAAQIYRKVTSGTKPNSFYKVKMPEVKEIIEGCIRTDKNERFTIQDLLAHAFFREERGVHVELAEEDDGEKPGLKLWLRMEDARRGGRPRDNQAIEFLFQLGRDAAEEVAQEMVALGLVCEADYQPVARAVRERVAAIQRKREKLRKARELEVLPPDSGPPPATVSLAPGPPSAFPPEPEEPEADQHQSFLFRHASYSSTTSDCETDGYLSSSGFLDASDPALQPPGGLPSSPAESHLCLPSGFALSIPRSGPGSDFSPGDSYASDAASGLSDMGEGGQMRKNPVKTLRRRPRSRLRVTSVSDQSDRVVECQLQTHNSKMVTFRFDLDGDSPEEIAAAMVYNEFILPSERDGFLSRIREIIQRVETLLKRDAGPPEAAEDALSPQEEPAALPALPGPPNAEPQRSISPEQRSWAAFSTSPSSPGTPLSPGAPFSPGTPPVFPCPIFPITSPSCYPCPFSQVSSNPYPQAPSSLLPLSSSASQVPLPSSSLPISAPLPFSPSYPQDPLSPTSLPVCPSPPSLPSTTAAPLLSLASAFSLAVMTVAQSLLSPSPGLLSQSPPAPPGPLPSLPLSLASCDQESLSAQTAETENEASRNPAQPLLGDARLAPISEEGKPQLVGRFQVTSSKEPAEPPLQPASPTLSRSLKLPSPPLTSESSDTEDSAAGGPETREALAESDRAAEGLGVAVDDEKDEGKEPLLGGSSPILSHPSPVWMNYSYSSLCLSSEESESSGEDEEFWAELQNLRQKHLSEVEALQTLQKKEIEDLYSRLGKQPPPGIVAPAAMLSCRQRRLSKGSFPTSRRNSLQRSDLPGPGIMRRNSLSGSSTGSQEQRASKGVTFAGDIGRM
The following text describes a protein:
Function:
Transcription factor involved in the regulation of the insulin signaling pathway. Binds to insulin-response elements (IREs) and can activate transcription of IGFBP1. Down-regulates expression of HIF1A and suppresses hypoxia-induced transcriptional activation of HIF1A-modulated genes. Also involved in negative regulation of the cell cycle. Involved in increased proteasome activity in embryonic stem cells (ESCs) by activating expression of PSMD11 in ESCs, leading to enhanced assembly of the 26S proteasome, followed by higher proteasome activity (By similarity). Represses smooth muscle cell differentiation by inhibiting the transcriptional coactivator activity of myocardin.
Subcellular Localization:
Cytoplasm. Nucleus. Note=When phosphorylated, translocated from nucleus to cytoplasm. Dephosphorylation triggers nuclear translocation. Monoubiquitination increases nuclear localization. When deubiquitinated, translocated from nucleus to cytoplasm (By similarity).
Sequence:
MDPENKKSATGAAAILDLDPDFEPQSRPRSCTWPLPRPDLATEPHEPSEVEPSLGQKVPTEGHSEPILLPSRLPEPAGGPQPGILGAVTGPRKGGSRRNAWGNQSYAELISQAIESAPEKRLTLAQIYEWMVRTVPYFKDKGDSNSSAGWKNSIRHNLSLHSKFIKVHNEATGKSSWWMLNPDGGKGGKAPRRRAASMDSSSKLLRGRSKGPKKKPSVLPAPPEGATPRSPLGHFAKWSSSPCPRNREEADVWTTFRPRSSSNASTVSTRLSPMRPESEVLAEEEMPASASSYAGGVPPTLSEDLELLDGLNLASPHSLLSRSGLSGFSLQHPGLAGPLHSYGASLFGPIDGSLSAGEGCFSSSQSLEALLTSDTPPPPADVLMTQVDPILSQAPTLLLLGGMPSSSKLGTGVSLCPTPLEGPGPSNLVPNLSVMAPPPVMAGAPIPKVLGTPVLASPTEDSSHDRMPQDLDLDMYMENLECDMDNIISDLMDGEGLDFNFEPDP
The following text describes a protein:
Function:
Component of the transcription coactivator SAGA complex. SAGA acts as a general cofactor required for essentially all RNA polymerase II transcription. At the promoters, SAGA is required for transcription pre-initiation complex (PIC) recruitment. It influences RNA polymerase II transcriptional activity through different activities such as TBP interaction (via core/TAF module) and promoter selectivity, interaction with transcription activators (via Tra1/SPT module), and chromatin modification through histone acetylation (via HAT module) and deubiquitination (via DUB module). SAGA preferentially acetylates histones H3 (to form H3K9ac, H3K14ac, H3K18ac and H3K23ac) and H2B and deubiquitinates histone H2B. SAGA interacts with DNA via upstream activating sequences (UASs). Also identified in a modified version of SAGA named SALSA or SLIK. The cleavage of SPT7 and the absence of the SPT8 subunit in SLIK neither drive any major conformational differences in its structure compared with SAGA, nor significantly affect HAT, DUB, or DNA-binding activities. Component of the ADA histone acetyltransferase complex, which preferentially acetylates nucleosomal histones H3 (to form H3K14ac and H3K18ac) and H2B. Positioned at chromosomal termini to participate in both transcriptional repression and activation in response to nutrient signaling, promoting transcriptional silencing at telomeres and ribosomal DNA. May be involved in response to DNA damage by genotoxic agents.
Miscellaneous:
MISCELLANEOUS: Present with 1720 molecules/cell in log phase SD medium.
Subcellular Localization:
Nucleus.
Sequence:
MSNKFHCDVCSADCTNRVRVSCAICPEYDLCVPCFSQGSYTGKHRPYHDYRIIETNSYPILCPDWGADEELQLIKGAQTLGLGNWQDIADHIGSRGKEEVKEHYLKYYLESKYYPIPDITQNIHVPQDEFLEQRRHRIESFRERPLEPPRKPMASVPSCHEVQGFMPGRLEFETEFENEAEGPVKDMVFEPDDQPLDIELKFAILDIYNSRLTTRAEKKRLLFENHLMDYRKLQAIDKKRSKEAKELYNRIKPFARVMTAQDFEEFSKDILEELHCRARIQQLQEWRSNGLTTLEAGLKYERDKQARISSFEKFGASTAASLSEGNSRYRSNSAHRSNAEYSQNYSENGGRKKNMTISDIQHAPDYALLSNDEQQLCIQLKILPKPYLVLKEVMFRELLKTGGNLSKSACRELLNIDPIKANRIYDFFQSQNWM
The following text describes a protein:
Function:
Catalyzes the 6-electron oxidation of protoporphyrinogen-IX to form protoporphyrin-IX.
Subcellular Localization:
Plastid, chloroplast.
Sequence:
MTKPHYDPVGSVAVIGAGVSGLAAAYRLNKEGADVTIFEAGDHAGGAIQSFSKDGFVWERAANTMAENDPLIGQLIRDLNIEDKRIWPANANKRYIVKNGKAVQAPANPLALLTNNLLSPGAKLRALAEPLIWKRKKHAKQQKGEEAHGEAQEEDESIGDFLERHVGREPVEYLLDPFLAGTSGSDPQSTAVKYAYPNLYDWEESKGSLLIGAIAAQLSKKKPQSKAHGSSKVAPAGSQSDGHVADKGKKGKRHRGSFSFLDGMQTLPNALADHVGRHRLKTQTPVTRLDLTAAGPTRRGDWTVEYAARPGKSESRHFDAVLVTAPLEDVKNRMKISKGNRPFSLGFIPKITYQPMTALIQGFRAEDVKQPLEGFGVLVPSKETEFKTLGTLFNSYMFPNRAPSGFVTFTTFIGGSRHPELPGRPIDELKEVAARDLQRLLGVEGKPAFSQHIYWERAFPQYGKGYGEVLEAIRKLETDLPGLYVAGNHRDGLAVGKALVSGYDAAGRILTDLRGMVAAIPAVKLS
The following text describes a protein:
Function:
Probable methyltransferase required to silence rDNA.
Subcellular Localization:
Nucleus, nucleolus.
Sequence:
MFGKVKGNRSGNQQSISKKNKKELKAQRKWEQDEERIKGSKFRLLNEYMYTVNSEEAQKHFKNHPEEFKIYHTGYAQQIEKWPESPVGNIIKLLTESEQFQNKKLVVCDLGCGQGEIQEYFQKDKRLSKLITVKSFDLVAIKPYIIETDISNLPMDDCSCDAAIFSLSLMGINYLDYLGEAFRVLKKNGHLIIAEVKSRMNTIDNFVNLVTGMGMKILKRDEHNSHFVLFVFEKIMDVCQFNGPLNQKRVYQILGQKDPNLKDWQSLGQQILQPCVYKKR
The following text describes a protein:
Function:
Provides the precursors necessary for DNA synthesis. Catalyzes the biosynthesis of deoxyribonucleotides from the corresponding ribonucleotides (By similarity).
Sequence:
MHPTLISAPISSSANDAHAGTSQGSHQGHRIQVIRRDGSSTPLNIGKIRAVVDWACLGLEVNSIALEAGLTTRLREGISTREIQDNLISCALEMCSPNEPDWRYVAGRLHVWSLWKDTLVRRGYQYGQYLRTVQTKVTNGEYDSRILTYSEGELQEAGCWINSDWDTDYDYAGAVLLTSRYLLPNELPQEALLTCALLLASVEAPDRRLQWARRFYESIAARRISLATPILANLRVPGGSLTSCFIVAMEDNLESIFGEITNAARISKNGGGVGVNVSRIRATGSWVMGKPNASGGVIPWTKLLNDTAIAVNQGGRRAGAVTVGLDVWHLDVPEFLEMQAENGDQRRKAYDIFPQLILPDEFMRRVINKEDWTLVDPYEVREKMGIELAELWGEQFEGAYREIESNLDTTITLYKRINARELFKQIMRTQVETGMPYLSFKDTINKANPNKHLGYIPGTNLCCESFSNVTPGQDAHCCNLVSLNLANLDLQDIAGVSQIAVRMLDNTIELTAPPFADAKSHNNKYRTIGVGAMGLADWLAKRRLNYDELADINRLFEEIGYWCTQSSMELAKERGAYPAFPGSDWQKGLLIGSKPVSWFQANAAKPERWEKLSNDIQTHGIRNSHITAIAPNTSSSLVQGCTASILPVYSRFFYDKWAKGTVPIAPPFIGNCFWFYPENKTMDQRKVVKAVAAIQQWTDTGISMELLFNLNAGIYFPEEPERSLNAKDIFDTLVMAWEAGCKAIYYIRTVQKDDFKDSSDGCVACAN
The following text describes a protein:
Function:
Catalyzes the formation of N(7)-methylguanine at position 46 (m7G46) in tRNA.
Sequence:
MPHFLAKLDFKPLEYPLIEGDFCFHREFLSLKNPTKSCVYASFKDRIFLLQKIRRANDFLIKSEKATPLKREVLKQALRIYSQSFEVISHNLQENSKHASGKKTLDLGTFEDFIQKNQAPILIEIGFGSGRHLIELAKNNPTKTCLGIEIHTPSIAQALKQIELLDLKNLHILQGDGRLVLESMPNHRCEKIFVHFPVPWNEKKHRRVLSEKFLNEALRVLKPRGFLELRTDDSLYFEDSLKLALKNFQCEIEIKKNAQIPVVSKYEARWNKLKKDIYDLRIYSLEWNETPFDNHAFDFSFDTITISKKSVGTILKTKKIIQEGYFVHVCNIYENKGDFLVELSMGDFDWPVRLFVLLTENQIFYLNKSPLKTLNNHKAHLLLQNILSQKGIG
The following text describes a protein:
Function:
Catalyzes the conversion of a range of fructosamine 6-phosphates to glucose 6-phosphate and a free amino acid.
Sequence:
MLKFDEQKVRENMEGALKLRPQINEVVDQIHHRGFSNICWLGIGGTYASAMQAVVHMKEKTALETFYENAAVFLTTGNKRVTKDTLVVISSVTGSTQEVVDAVKKCNEIGATIFGFIDKAETELANLVDHLISYPLNEQLKFFMVADRFMYLAGEFEDYGAFYQEMDQHFAKGIVEVEKAADKFGQEFALKHHQDDIHYFVGAGNQWGATYSYAMCYWEEQHWIKTKSIESHEFFHGMFEIVERDTPITIYVTEDSQRSLSERVVNFIPQICANYTVIDAKDYDMPGISAKFRGALSPFIIHAVNNRIDVHVEKINCHPMEIRRYYRQLDY
The following text describes a protein:
Function:
APOE is an apolipoprotein, a protein associating with lipid particles, that mainly functions in lipoprotein-mediated lipid transport between organs via the plasma and interstitial fluids. APOE is a core component of plasma lipoproteins and is involved in their production, conversion and clearance. Apolipoproteins are amphipathic molecules that interact both with lipids of the lipoprotein particle core and the aqueous environment of the plasma. As such, APOE associates with chylomicrons, chylomicron remnants, very low density lipoproteins (VLDL) and intermediate density lipoproteins (IDL) but shows a preferential binding to high-density lipoproteins (HDL). It also binds a wide range of cellular receptors including the LDL receptor/LDLR and the very low-density lipoprotein receptor/VLDLR that mediate the cellular uptake of the APOE-containing lipoprotein particles. Finally, APOE also has a heparin-binding activity and binds heparan-sulfate proteoglycans on the surface of cells, a property that supports the capture and the receptor-mediated uptake of APOE-containing lipoproteins by cells.
Subcellular Localization:
Secreted. Secreted, extracellular space. Secreted, extracellular space, extracellular matrix. Extracellular vesicle. Endosome, multivesicular body. Note=In the plasma, APOE is associated with chylomicrons, chylomicrons remnants, VLDL, LDL and HDL lipoproteins. Lipid poor oligomeric APOE is associated with the extracellular matrix in a calcium- and heparan-sulfate proteoglycans-dependent manner. Lipidation induces the release from the extracellular matrix. Colocalizes with CD63 and PMEL at exosomes and in intraluminal vesicles within multivesicular endosomes.
Sequence:
MKVLWAALVVTLLAGCGADVEPGPEVQLGKEWATWQASQPWEQALGRFWNYLRWVQTLSEQVQEQLLSSQVTEELTALMDDTMKEVKACQSELEEQLGPVTEETKARVSKELQAAQARLGADMEEVRSRLAQYRGELQAMVGQSTEELRGRLSAHLRKMRKRLLRDAEDLQRRLAVYQAGIWEGAERSVNTLREHLGPLAEQAATVHTLVSKPLQERAEAWAQRLRGRLEKAGFPVGDRLDEVREQVQEVRAKVEEQANQVRLQAEAFQGRLKSWFEPLVQDMQQKWAELVEKVQLAVGAVPTSVPSEKQ
The following text describes a protein:
Function:
Tyrosine-protein kinase that acts as a cell-surface receptor for fibroblast growth factors and plays an essential role in the regulation of embryonic development, cell proliferation, differentiation and migration. Required for normal mesoderm patterning and normal skeletogenesis. Phosphorylates PLCG1, FRS2, GAB1 and SHB. Ligand binding leads to the activation of several signaling cascades. Activation of PLCG1 leads to the production of the cellular signaling molecules diacylglycerol and inositol-1,4,5-trisphosphate. Phosphorylation of FRS2 triggers recruitment of GRB2, GAB1, PIK3R1 and SOS1, and mediates activation of RAS, MAPK1/ERK2, MAPK3/ERK1 and the MAP kinase signaling pathway, as well as of the AKT1 signaling pathway. Promotes phosphorylation of SHC1, STAT1 and PTPN11/SHP2. In the nucleus, enhances RPS6KA1 and CREB1 activity and contributes to the regulation of transcription. FGFR1 signaling is down-regulated by ubiquitination, internalization and degradation (By similarity).
Subcellular Localization:
Cell membrane; Single-pass type I membrane protein. Nucleus. Cytoplasm, cytosol. Cytoplasmic vesicle. Note=After ligand binding, both receptor and ligand are rapidly internalized. Can translocate to the nucleus after internalization, or by translocation from the endoplasmic reticulum or Golgi apparatus to the cytosol, and from there to the nucleus (By similarity).
Domain:
The second and third Ig-like domains directly interact with fibroblast growth factors (FGF) and heparan sulfate proteoglycans. Isoforms lacking the first Ig-like domain have higher affinity for fibroblast growth factors (FGF) and heparan sulfate proteoglycans than isoforms with all three Ig-like domains (By similarity).
Sequence:
MFTWRCLILWAVLVTATLSAARPAPTLPDQALPKANIEVESHSAHPGDLLQLRCRLRDDVQSINWVRDGVQLPENNRTRITGEEVEVRDAVPEDSGLYACMTNSPSGSETTYFSVNVSDALPSAEDDDDEDDSSSEEKEADNTKPNQAVAPYWTYPEKMEKKLHAVPAAKTVKFKCPSGGTPNPTLRWLKNGKEFKPDHRIGGYKVRYATWSIIMDSVVPSDKGNYTCIVENKYGSINHTYQLDVVERSPHRPILQAGLPANKTVALGSNVEFVCKVYSDPQPHIQWLKHIEVNGSKIGPDNLPYVQILKTAGVNTTDKEMEVLHLRNVSFEDAGEYTCLAGNSIGISHHSAWLTVLEATEQSPAMMTSPLYLEIIIYCTGAFLISCMVVTVIIYKMKSTTKKTDFNSQLAVHKLAKSIPLRRQVTVSADSSSSMNSGVMLVRPSRLSSSGTPMLAGVSEYELPEDPRWELPRDRLILGKPLGEGCFGQVVLAEAIGLDKDKPNRVTKVAVKMLKSDATEKDLSDLISEMEMMKMIGKHKNIINLLGACTQDGPLYVIVEYASKGNLREYLQARRPPGMEYCYNPTRIPEEQLSFKDLVSCAYQVARGMEYLASKKCIHRDLAARNVLVTEDNVMKIADFGLARDIHHIDYYKKTTNGRLPVKWMAPEALFDRIYTHQSDVWSFGVLLWEIFTLGGSPYPGVPVEELFKLLKEGHRMDKPSNCTNELYMMMRDCWHAVPSQRPTFKQLVEDLDRIVAMTSNQEYLDLSVPLDQYSPGFPATRSSTCSSGEDSVFSHDPLPDEPCLPRCPPHSHGALKRH