lhallee/plat_data huggingface dataset:
The following text describes a protein:
Function:
Mediates nucleation of actin filaments and thereby promotes actin polymerization. Plays a role in the regulation of actin filament length. Required for normal sarcomere organization in the heart, and for normal heart function.
Subcellular Localization:
Cytoplasm, cytoskeleton. Cytoplasm, myofibril, sarcomere, M line.
Sequence:
MSTFGYRRELSKYEDIDEDELLASLTEEELKELERELEDIEPDRNLPVGQRQKSLTEKTPTGTFSREALMAYWERETRKLLEKERLGACEKDSEQEEDNSEDIQEECFTESNSEVSEEAYTEEDDEEEEEEEEEEEDEDDSDDEDEEKQNSAASERPVNCEDGRSSSHVRHKKCSNAKNSENLFNGHDGKDTENLSFKSSAIHPCGNPTVIEDALEKVRSNDPETTEVNLNNIENITSQMLIQFSQALRDNTVVKSFSLANTHADDNVAIAIAGMLKVNQHITSLNIESNFITGKGVLAIMRALQHNKVLTELRFHNQRHIMGSQVEMDIVKLLKENTTLVKLGYHFDLAGPRMSMTSILTRNMDKQRQKRMQEQRQQEYGCDGAINPKTKVLQKGTPRSSPYTSPKSSPWSSPKLPRKSAPAKSQPPAPAPPPPPPPPPPPPPPPPPVIPDKKAPTRNIAEVIKQQESSRKALQNGQKKKKGKKGKKHENSILKEIKDSLKSVSDRKSEEGSRPSTRPSTPQRSLHDNLMEAIRASSIKQLRRVSRRSYFSNWLWIRYRTSSINFRT
The following text describes a protein:
Function:
Involved in DNA double-strand break repair (DSBR). The Rad50/Mre11 complex possesses single-strand endonuclease activity and ATP-dependent double-strand-specific 3'-5' exonuclease activity. Rad50 provides an ATP-dependent control of Mre11 by unwinding and/or repositioning DNA ends into the Mre11 active site (By similarity).
Domain:
The two conserved Cys that bind zinc constitute the zinc-hook, which separates the large intramolecular coiled coil regions. The 2 Cys residues coordinate one molecule of zinc with the help of the 2 Cys residues of the zinc-hook of another Rad50 molecule, thereby forming a V-shaped homodimer (By similarity).
Sequence:
MRPLKLEVKGFTVYKKPQVIDFTPLKFFVIQGKTGAGKTSIIDAITYALYGKVPRYGASVATKYVLSRGEKELKVALDFSLRGRNYRVERYYREFPEDSQVRVYEEGRRLNIKANEVEKWLFKISGLDYKTFTKVILLPQGEFDRFLKESSERKKILINLLGLEELEKVRQLASETFKNLEGKREALKKEYELLKDYTPTKKEVLEKTLKNLEEELKELKETEEKLRQELKKAEEKDSLERELSQVVTKLKELENLEKEVEKLREKLEFSRKVAPYVPIAKRIEEIDKKLTELKVRKNKLTKELAVLKDELSFAQEELNRIEAEKEKFKEEKEREKELEHRLKKLQEIKEILKELSQLSSSLKEKEREYEQAKQEFEDLSERVEKGKKLVAETEEKLEKIKELFSEEEYTSLKMKERLLVELQRKLKELKEKEGQLENLTQKYKEKKKVHEKVLNELKELERELKERELHYHAHMVASYLSPGDTCPVCGGIYRGKALENVDAEGISELKHAKELKEKEEREIDTTLKLYAQKINSLKEEMEKLRNEVEELRKEIPENLKERIKKLEELRIEKEKLEHKLNKYRKALEDRQKQKEEAQAKLHKAQTELELLKEKIREKSRLVKEFKELYRVERLEDYEESLKEEINYINSKLQEIEEKEKKLRKHFEELSSRKSKLEGELSALNESINSLEEERKEKLKELANIYEVAKSPREVVELYLGDKEAELERKIKEFEESFQSLKLKKSEIEEKLKEYEGIRELSDIKGEYESVKTQLEEKHKKLGEVKRELEHLGERLKRKEELQKEISELEKKLEVYRVISNDFRGDRFQKYVSEIMLQKVVDRASEYFYKFTGNYFFELERATKGRDKDIVVVESSTSQRRPVSSLSGGETFLASLSFAFAVSDLLSGSANLESLFIDEGFGSLDQDMRERVSEILEAIKTNVNKMIGIVSHIPDFAERFTERIVVEKKGDYSEVRVIY
The following text describes a protein:
Function:
Converts adenosine-3',5'-bisphosphate (PAP) to AMP.
Subcellular Localization:
Cell inner membrane; Peripheral membrane protein; Cytoplasmic side.
Sequence:
MAAIDAALKAGEKILSIYEDPKSDFEIERKADNSPLTIADRKAHEAIVAILNETPFPVLSEEGKHMDYAVRRGWDTLWIVDPLDGTKEFIKRNGEFTVNIALVQNAVPVMGVIYVPVKKELYFAVEGTGAYKCSGIVGLEDEGVTLQQMIEKSERMPLADARDHFIAVASRSHLTPETETYIADLKKKHGNVELISSGSSIKICLVAEGKADVYPRFAPTMEWDTAAGHAIARAAGMEVYQAGKEEPLRYNKEDLLNPWFIVEAKRER
The following text describes a protein:
Function:
Component of the transcription regulatory histone acetylation (HAT) complex SAGA, a multiprotein complex that activates transcription by remodeling chromatin and mediating histone acetylation and deubiquitination. Within the SAGA complex, participates in a subcomplex that specifically deubiquitinates histone H2B. The SAGA complex is recruited to specific gene promoters by activators, where it is required for transcription.
Subcellular Localization:
Nucleus.
Domain:
The C-terminal SGF11-type zinc-finger domain forms part of the 'catalytic lobe' of the SAGA deubiquitination module; The long N-terminal helix forms part of the 'assembly lobe' of the SAGA deubiquitination module.
Sequence:
MSERRKSGTPATIRNFDTENLPRDQNVLDIDPNASPEAGIVYEIIDDVILSLCFDVHRSIKLGTFNIEDVDDEVIKQYEVVDSEGLDVFGQVPLKKPVDCICPNCQRNMAASRFAPHLEKCMGMGRNSSRIASRRLATGKMMDEDEEDVYFDDDWTWNTDRKPGKKNKRERPGNSPRRAKAPRRNGETGTPRPGTPSSVNSGEMPAARIGPTQAAFESLGIAEKKALMSQTCGVISEHTGRMCTRSQRCPQHTDEQRRLVRLRMLGPQETESALSRVRPDGSSFEPEDVIDVDGYEDGDGPSLRDTLSRLSWEEESNASTGDDHSPAAFGISAIVKKKRKKKAKHKRRPR
The following text describes a protein:
Function:
Functions as a zinc transporter.
Subcellular Localization:
Cytoplasmic vesicle, COPII-coated vesicle membrane; Multi-pass membrane protein. Cytoplasmic vesicle, secretory vesicle membrane; Multi-pass membrane protein. Golgi apparatus, Golgi stack membrane; Multi-pass membrane protein. Golgi apparatus, trans-Golgi network membrane; Multi-pass membrane protein.
Sequence:
ARTVHPGLPRAKLTKYIVLLCLTKCLKAVGLFESYDLLKAVHIVQFIFILKLGTAFFMVLFQKPFSSGKTVTKHQWIKIFKHAVAGCIISLLWFFGLTLCGPLRTLLLFEHSDIVVISLLSVLFTSSGGGPAKTRGAAFFIIAVICLLLFDNDDLMAKMAEHPEGHHDSALTHMLYTAIAFLGGVEYDSYGGVLLLVLALCCKVGFHTASRKLSIDVGGAKRLQALSQLVSVFLLCPWVIVLSVTTESKIESWFPLIMPFTTVIFFVMILDFYMDSVCSVKMEASKCARYGSFPIFISALLFGNFWTHPITDQLRAMNRAAHQESTEHVLSGGVVVSAVFFILSANILSSPSKRGQKGTLIGYSPEGTPLYHFMGDAFQHSSQSVPRFIKDSLKQILEESDSRQIFYFLCLNLLFTFVELFYGVLTNSLGLISDGFHMLFDCSALVMGLFAALVSRWKATRIFSYGYGRIEILSGFINGLFLIVIAFFVFLESVARLIDPPELDTNMLTPVSIGGLIVNLIGVCAFSHAHSHGHGPSQGHCHSDHGHSHHAHGHSDHGHSHGFTGGGMNANMRGVFLHVLADTLGSIGVIVSTVLIEQFGWFIADPLCSLFIAVLIFLSVIPLIKDACQVLLLRLPPDYEKELHIALEKVQKLEGLISYRDPHFWRHSASIVAGTIHIQVTSDVLEQRVVQQVTGILKDAGVNNLTIQVEKEAYFQHMSGLSTGFHDVLAMTQQMESMKYCKDGTYIM
The following text describes a protein:
Function:
TFIIF is a general transcription initiation factor that binds to RNA polymerase II and helps to recruit it to the initiation complex in collaboration with TFIIB. It promotes transcription elongation.
Subcellular Localization:
Nucleus.
Sequence:
MSSASKSTPSAASGSSTSAAAAAAASVASGSASSSANVQEFKIRVPKMPKKHHVMRFNATLNVDFAQWRNVKLERENNMKEFRGMEEDQPKFGAGSEYNRDQREEARRKKFGIIARKYRPEAQPWILKVGGKTGKKFKGIREGGVGENAAFYVFTHAPDGAIEAYPLTEWYNFQPIQRYKSLSAEEAEQEFGRRKKVMNYFSLMLRKRLRGDEEEEQDPEEAKLIKAATKKSKELKITDMDEWIDSEDESDSEDEEDKKKKEQEDSDDGKAKGKGKKGADKKKKKRDVDDEAFEESDDGDEEGREMDYDTSSSEDEPDPEAKVDKDMKGVAEEDALRKLLTSDEEEDDEKKSDESDKEDADGEKKKKDKGKDEVSKDKKKKKPTKDDKKGKSNGSGDSSTDFSSDSTDSEDDLSNGPPKKKVVVKDKDKEKEKEKESAASSKVIASSSNANKSRSATPTLSTDASKRKMNSLPSDLTASDTSNSPTSTPAKRPKNEISTSLPTSFSGGKVEDYGITEEAVRRYLKRKPLTATELLTKFKNKKTPVSSDRLVETMTKILKKINPVKHTIQGKMYLWIK
The following text describes a protein:
Function:
Induces bone resorption, acting probably through a signaling cascade which results in the secretion of factor(s) enhancing osteoclast formation and activity.
Subcellular Localization:
Cytoplasm.
Sequence:
MSKPPPKPAKPGQVKVFRALYNFDPRTPDELYFEEGDILYISDTSDSNWWKGTCRGRTGLIPSNYVAEQAESIDNPMHEAAKRGNLSWLRECVDNKVGINGLDKAGNTALYWGCHGGHKDVVELLLSQSNVELNQQNKLGDTPLHAAAWKGYSDIVEMLLNKDARTDIRNNENKLALDMATNAQSASLLKRKQASNVTRTLSNAEEYLDDEDSD
The following text describes a protein:
Function:
Negatively regulates stress-induced JNK activation and apoptosis by promoting MAP2K7 phosphorylation and inhibiting its ability to activate JNK. Following prolonged stress, anti-apoptotic effect stops because of degradation of RASSF7 protein via the ubiquitin-proteasome pathway. Required for the activation of AURKB and chromosomal congression during mitosis where it stimulates microtubule polymerization.
Subcellular Localization:
Cytoplasm, cytoskeleton, microtubule organizing center, centrosome. Note=Colocalizes with gamma-tubulin.
Sequence:
MLLGLAAMELKVWVDGIQRVVCGVSEQTTCQEVVIALAQAIGQTGRFVLVQRLREKERQLLPQECPVGAQATCGQFASDVQFVLRRTGPSLAGRPSSDSCPPPERCLIRASLPVKPRAALGCEPRKTLTPEPAPSLSRPGPAAPVTPTPGCCTDLRGLELRVQRNAEELGHEAFWEQELRREQAREREGQARLQALSAATAEHAARLQALDAQARALEAELQLAAEAPGPPSPMASATERLHQDLAVQERQSAEVQGSLALVSRALEAAERALQAQAQELEELNRELRQCNLQQFIQQTGAALPPPPRPDRGPPGTQGPLPPAREESLLGAPSESHAGAQPRPRGGPHDAELLEVAAAPAPEWCPLAAQPQAL
The following text describes a protein:
Function:
Nuclear phosphoprotein which forms a tight but non-covalently linked complex with the JUN/AP-1 transcription factor. On TGF-beta activation, forms a multimeric SMAD3/SMAD4/JUN/FOS complex, at the AP1/SMAD-binding site to regulate TGF-beta-mediated signaling. Has a critical function in regulating the development of cells destined to form and maintain the skeleton. It is thought to have an important role in signal transduction, cell proliferation and differentiation (By similarity). In growing cells, activates phospholipid synthesis, possibly by activating CDS1 and PI4K2A. This activity requires Tyr-dephosphorylation and association with the endoplasmic reticulum (By similarity).
Subcellular Localization:
Nucleus. Endoplasmic reticulum. Cytoplasm, cytosol. Note=In quiescent cells, present in very small amounts in the cytosol. Following induction of cell growth, first localizes to the endoplasmic reticulum and only later to the nucleus. Localization at the endoplasmic reticulum requires dephosphorylation at Tyr-10 and Tyr-30 (By similarity).
Sequence:
MMFSGFNADYEASSSRCSSASPAGDSLSYYHSPADSFSSMGSPVNAQDFCTDLAVSSVNFIPTVTAISISPDLQWLVQPTLVSSVAPSQTRAPHPYGVPTPSAGAYSRAGAVKTMPGGRAQSIGRRGKVEQLSPEEEEKRRIRRERNKMAAAKCRNRRRELTDTLQAETDQLEDEKSALQTEIANLLKEKEKLEFILAAHRPACKIPDDLGFPEEMSVASLDLSGGLPEAATPESEEAFTLPLLNDPEPKPSVEPVKKVSSMELKAEPFDDFLFPASSRPGGSETARSVPDMDLSGSFYAADWEPLHGGSLGMGPMATELEPLCTPVVTCTPSCTAYTSSFVFTYPEADSFPSCAAAHRKGSSSNEPSSDSLSSPTLLAL
The following text describes a protein:
Function:
Gluconolactonase with low activity towards other sugar lactones, including gulonolactone and galactonolactone. Can also hydrolyze diisopropyl phosphorofluoridate and phenylacetate (in vitro). Calcium-binding protein. Modulates Ca(2+) signaling, and Ca(2+)-dependent cellular processes and enzyme activities (By similarity).
Subcellular Localization:
Cytoplasm.
Sequence:
MSSIKIECVLPENCQCGESPVWEEASNSLLFVDIPAKKVCRWDSLTKQVQRVTVDAPVSSVALHRSGDYVATIGTKFCALNWKEQSAVVLATVDNDKKNNRFNDGKVDPAGRYFAGTMAEETAPAVLERHQGALYSLFPDHHVKKYFDQVDISNGLDWSLDHKIFYYIDSLSYSVDAFDYDLQTGQISNRRSVYKLEKEEQIPDGMCIDAEGKLWVACYNGGRVIRLDPVTGKRLHTVKLPVDKTTSCCFGGKNYSEMYVTCARDGMDPEGLLRQPEAGGIFKITGLGVKGIAPYSYAG
The following text describes a protein:
Function:
Required for the formation of a threonylcarbamoyl group on adenosine at position 37 (t(6)A37) in tRNAs that read codons beginning with adenine.
Subcellular Localization:
Cytoplasm.
Sequence:
MPPRILGTTQSELADAAGALQRGELVAIPTETVYGLAADALSEAACAKIFTLKQRPANDPLIVHISHISQLPMVAVVSVELSSIVDALAAAFWPGPLTMVLPAAPCVPSIVTAGSQTIGVRMPRHPVACAILELAARPLAAPSANMFGSISPTQAEDVAAEFVNSDLLIIDGGRCDIGIESTVLLVEKDCLTILRRGQVNEEMLVATLPTNALDYIRVETRALSSSGLQTKAVSSPGQFLRHYSPRTECYLVMKGGPMLPGAVRAILPARLDGFVVILDCNPALAELEPDALLRSLAGLLPEGTEPARILRAYSVPTLEAAAQSLFETLRRADKLGPACILALPPEPARGLADALLDRLFRAASGRWVE
The following text describes a protein:
Function:
Catalyzes two sequential steps in the biosynthesis of coenzyme A. In the first step cysteine is conjugated to 4'-phosphopantothenate to form 4-phosphopantothenoylcysteine. In the second step the latter compound is decarboxylated to form 4'-phosphopantotheine.
Sequence:
MLSGVNVAVGVTGSIAAVKVVEFVHELRRRGACVRAVMTESAQGIIHPWAVEFATENPVVTEITGTVPHVELCGRDGWADVFVVAPATANTVGKIAAAVDDSPVTTCVTTAVGADVPVVVVPAMHEPMYDHPGVRDAIDRVSSWGVSVVDPRIEEGKAKLPRESTIVHETARAAGEQPLAGTHVVVTSGATSEAIDPVRVLTNRASGRTGRAVAAACYVRGARVTLVHDASDGGAVPYADVRDVSSAAEMTAATLTACADADALVSAAAISDYTVEAADEKLRSGREDVALSLEPTRKLVGAVRDDNPDLPIVGFKAETPADDGTAGDDSMVAAARSLLQRDGLAFVVANDAGVMGNDETRALFVTADSVSEYAGHKRGLGARIAERLAVFA
The following text describes a protein:
Function:
Prosaposin: Behaves as a myelinotrophic and neurotrophic factor, these effects are mediated by its G-protein-coupled receptors, GPR37 and GPR37L1, undergoing ligand-mediated internalization followed by ERK phosphorylation signaling; Pulmonary surfactant-associated proteins promote alveolar stability by lowering the surface tension at the air-liquid interface in the peripheral air spaces. SP-B increases the collapse pressure of palmitic acid to nearly 70 millinewtons per meter; Saposins are specific low-molecular mass non-enzymic proteins, they participate in the lysosomal degradation of sphingolipids, which takes place by the sequential action of specific hydrolases.
Subcellular Localization:
Secreted, extracellular space, surface film.
Sequence:
VMCLTLSMCIFAPLAAASPLLGKEQCAKGPPYWCQNVKTASTCGAVTHCQQNVWNKPTAKTVPCDLCKEVLTVVGSLLKDNATEAEILGYLEKACQLIPDAGLSSECKEMVDNYYPVLMGILTGELEDPNAVCCAMGLCRSLQKEMAEAQILSNEIPQVDLAQRLSPFIANVPQLLYPQSTPKETPKPENGDVCKDCVTFIKDAQDQAKSNTSFVSALISQIETQCDLLGPGISDMCKQYVGQYGPLVIQQLMSMAPEDICSRAGFCSVHHSVPMETLVAAKLFPAKVVKPAELKPAKKLVKVGEPPQCTVCELVLKEIESILEGKTSEEAVVHAVEKVCSLLPSALSAQCRDLIEVYGKAVIELLVQEADPKTVCTLLGLCRGRPYIPVMDKAHFQLGGFCDVCKMAVRYIDGILEQNATEAQIEEAVRKVCNFLPETVRDECDQLVQQYEPLLVQLLLQMLDPDFVCTKVGACPDALKSLLGTEECSWGPSYWCKNMDTASRCDAVEHCRRHVWN
The following text describes a protein:
Function:
Catalyzes the carbon-carbon bond cleavage of the bicyclic beta-diketone 6-oxocamphor via a retro-Claisen reaction to yield the optically active (2R,4S)-beta-campholinic acid. It is also able to cleave 2,2-disubstituted cyclohexa-1,3-diones such as 2-methyl-2-propylcyclohexa-1,3-dione and 2-methyl-2-butylcyclohexa-1,3-dione which result in racemic keto acid products. Transformations of the bicyclic diketone substrates bicyclo[2.2.1]heptane 2,6-dione and bicyclo[2.2.2]octane-2,6-dione yield (S)-keto acid products.
Sequence:
MKQLATPFQEYSQKYENIRLERDGGVLLVTVHTEGKSLVWTSTAHDELAYCFHDIACDRENKVVILTGTGPSFCNEIDFTSFNLGTPHDWDEIIFEGQRLLNNLLSIEVPVIAAVNGPVTNHPEIPVMSDIVLAAESATFQDGPHFPSGIVPGDGAHVVWPHVLGSNRGRYFLLTGQELDARTALDYGAVNEVLSEQELLPRAWELARGIAEKPLLARRYARKVLTRQLRRVMEADLSLGLAHEALAAIDLGMESEQ
The following text describes a protein:
Function:
S-adenosyl-L-methionine-dependent 2'-O-ribose methyltransferase that catalyzes the formation of 2'-O-methylguanosine at position 18 (Gm18) in a subset of tRNA. Selectively mediates Gm18 methylation of tRNAGln-TTG/CTG and tRNASer-TGA/GCT. Gm18 modification can enhance the stability of modified tRNAs.
Sequence:
MAASQLLDCLGDLAQASGGQVASLRATVGAVINATLAISRTPPEKLLDDLLREFLKRGGGAEGAETIKDQEVGEGSVSGVSAFIVAAMLLLEKEGTTNDQLHRLITTVCLPALSPREKLPVATQAEIASSLGALISARGAWELAGGSLIPACKAALTEAPSAANVTQSELFKAEKADGGPGHRADFSDGLAPLAACHLASNLVQAALRTFKSPEHSNGPSKAHDGGFSLGSKEESKSAGAFLAESVSAMLPVAFAMLTDGDSPMRRRQAVSILLPSLLEASLQIKDQESDTSALGAKLWACCEKLLEGERGEKADGFSVIACFKAHLLPPRGAKGAASGAVIDVRGQPTFWEAIKNGLLDEDSLIRRQALQVLRLALPTPSDGATSAETGPWVERGADGPASTSARGPIQKKGEKGGGSLNKGGGSRSKNEVRKEWKEFYHSRKRDGYAEKEMASMMENKGDNGEGDAARWDAFLLLYENLDDYTLHLFEATWPAQMEVLHSGDHLPQPSASGSPPGPDFSWVSLLWQRGFQHRNPQVRQAVLTSFFDRQWDGDTWLSQIPQQFVLGPLWKALDDPVQHPAFGSRGVWASPITLRASDFFLSFVSALPAPHRLPFLCELTRVSLAGVVSRPGLLTLASCLVAASEPLAVSNPKRSSSAPENPLVVPADAPEQLQTEEALDRLRAVVQESRRFHNPGFRLAVCGKALEAAAGAAKPPGFTISALAKLLAAFPDDLLSPKGALRDDFVTWVAPALPPSGAAAERFSSWLSPGLALALEAFFQPTSGAALPSNKASLMPAVQDEGSTVGGAGSANETRGWEQEAQQWAAFLALELLPSGDVAALLEILEHRALDIYRRPYLPPGQAEKTFLVLRSLAATCPPDAPPRGSPKAQHPPPSSNGPHSNGASPRGTTLACHVANVLGACMDELTAYAGKASAVLWEGAGMLAGIPGAPTTNSGVGPLGRGTLVFGGGPRALTGNAATTVTRAVLSVTCVSECCIWLQQQNPSPHPESATNFLLAFLWHFVAFLRAHQALPATAAEAELWAAILEALSAVCRAAAAVSAAEARSKGRAALVVVTEEHYEQPVEGFTRALAVVADDVADDVSRAAANVLEFPSLPRGMRGTVSEHKWLCLDALLATCAAQPPPPPSAKPSPPKASRPSSPPKSARPSSPPKEPRPFLTEGQLLDVLDDISDGLESAAETYLTPMLRCTRFLIEMGMLRVAAQRKGLSETEVLQPLVESAWAATADLRKRRVSVTSSVLATFLHPSLFSRPEMHGSGEDPGPLRWLLTQMLQLGQKSPRTIRLAALQVCELWLRHPDIARLYVSEAVRMALHGSDAVDEELDEMLSEGQPAGGNYAALLQSRDPELTEVFHNSELYVRVSVAVMVHEMARLCTASETQPDVAERYRTFGQALLMDLLTLSARDADVSKNLYKKGSIAHRKKVRTWQMLCVLSPFLERADVAELQPLLAAAIQVQNMSSVRQYVEQFAVQVYLRFPHLVKDSLVPWLNDVNTRTQTAASLVMIAAHVVLHSSPGLVQQDMLRLLFPATLPYLTSHHHNLRTFTQVLVHRILTRFGPSLLGTSENEYLTRIAAYLEHNIDCHRVRVSVDRAWAQFDPQTSVTPRGIFCPSASLDDALSELPFECVPGALYDRVSFFIKEQRDALRAETAADMSALDVESAARSDRPSRSGDSADVAADVAADDEEEQGARAPRDYQRKIKGDMGALLPPETDLDEDVMLAFAEARTRALLDLRGNRQDLIVVASLVARIPNLAGLARTCEVFKAAALVVADKSVVDDRQFQLISVSADKWVPLLEVPESGLAAYLQRKQREGYSLVGLEQTANSVPLHTHRFPRKTVLVLGREKEGIPADLIHHLDACVEIPQLGVIRSLNVHVSGAIATWEYSRSQFQSS
The following text describes a protein:
Function:
Catalyzes the irreversible transfer of a propylamine group from the amino donor S-adenosylmethioninamine (decarboxy-AdoMet) to putrescine (1,4-diaminobutane) to yield spermidine.
Subcellular Localization:
Cytoplasm.
Sequence:
MSQKELWYETLHANFGQYFSVENVLFREKTEHQDLVIFENPELGRVMALDGVVQTTERDEFIYHEMMTHVPLLAHGQAKKVLIIGGGDGAMLREVSRHKNIEQITMVEIDAGVVEFCRQYLPNHSAGAYDDPRFKLVIDDGVNFVNQTTEKFDVIISDCTDPIGPGESLFTSVFYEGCARSLNEGGIFVAQNGVCFLQQDEAVNSHNKLSHYFSDVSFYQAAIPTYYGGIMTFAWATQNPALRQLDLATLQNRFAQAGLACRYYNPAIHVGSFALPQYLLDALTTIPKVIGVDSSE
The following text describes a protein:
Function:
Probable transcriptional regulator that is required in neural development for the normal formation of sublateral cholinergic motor neuron processes. Plays a role in regulating the expression of acetylcholine transporter protein unc-17 in the sublateral processes. In particular, it is required in sublateral motor neurons for a left-right turning behavior that occurs during the lethargus phase of the normal sleep process called 'flipping'. During 'flipping' animals rotate 180 degrees about their longitudinal axis.
Subcellular Localization:
Nucleus.
Sequence:
MSYSPKQTTSFSVADILTPLEESFRRSMLDSPGSAFPSVFSAAPSMQSAYRSPQHSAHQGMQVSPMNMASANNPYAHMHVPQLSHNYCNGSVGELSQHYSDHRPSAASWYHGASSDPRFTISRLMNHSSTMNMNMNMNMNMNMNMNMSTLSAVGSGDLGKPLLPSHRRKRRVLFSQAQVYELERRFKQQKYLSAPEREHLANLINLTPTQVKIWFQNHRYKMKRQTKEKNMQDNNTICHQSPRRVAVPVLVKDGKPCNGSSGGGGNTGGDLTDDDDRSLSGQVEGVSDQGVVGGPQQQQPQQQQQQGNVTQSMSSQQTAANHHASMKASPVEPSSCGIPISIPSSDSGIGLSPVSVHAHHQHPMSQASLHHQASAMHSLYSPSAGAAGMTHNGAVNNMSATAPFLLHGRTW
The following text describes a protein:
Function:
Part of the Ssh1 complex, which probably is the major component of a channel-forming translocon complex that may function exclusively in the cotranslational pathway of protein endoplasmic reticulum (ER) import.
Miscellaneous:
MISCELLANEOUS: Present with 704 molecules/cell in log phase SD medium.
Subcellular Localization:
Endoplasmic reticulum membrane; Multi-pass membrane protein.
Sequence:
MSGFRLIDIVKPILPILPEVELPFEKLPFDDKIVYTIFAGLIYLFAQFPLVGLPKATTPNVNDPIYFLRGVFGCEPRTLLEFGLFPNISSGLILQLLAGLKVIKVNFKIQSDRELFQSLTKVFAIVQYVILTNIFIFAGYFGDDLSVVQIGLINFQLVGAGIFTTLLAEVIDKGFGFSSGAMIINTVVIATNLVADTFGVSQIKVGEDDQTEAQGALINLIQGLRSKHKTFIGGIISAFNRDYLPNLTTTIIVLAIAIIVCYLQSVRVELPIRSTRARGTNNVYPIKLLYTGCLSVLFSYTILFYIHIFAFVLIQLVAKNEPTHIICKIMGHYENANNLLAVPTFPLSLLAPPTSFFKGVTQQPLTFITYSAFILVTGIWFADKWQAISGSSARDVALEFKDQGITLMGRREQNVAKELNKVIPIAAVTGASVLSLITVIGESLGLKGKAAGIVVGIAGGFSLLEVITIEYQQSGGQSALNQVLGVPGAM
The following text describes a protein:
Function:
Mg(2+)-dependent phosphatase that catalyzes the hydrolysis of the 1-position phosphate from inositol 1,4-bisphosphate and inositol 1,3,4-trisphosphate and participates in inositol phosphate metabolism.
Sequence:
MSDILRELLCVSEKAANIARACRQQEALFQLLIEEKKEGEKNKKFAVDFKTLADVLVQEVIKQNMENKFPGLEKNIFGEESNEFTNDWGEKITLRLCSTEEETAELLSKVLNGNKVASEALARVVHQDVAFTDPTLDSTEINVPQDILGIWVDPIDSTYQYIKGSADIKSNQGIFPCGLQCVTILIGVYDIQTGVPLMGVINQPFVSRDPNTLRWKGQCYWGLSYMGTNMHSLQLTISRRNGSETHTGNTGSEAAFSPSFSAVISASEKETIKAALSRVCGDRIFGAAGAGYKSLCVVQGLVDIYIFSEDTTFKWDSCAAHAILRAMGGGIVDLKECLERNPETGLDLPQLVYHVENEGAAGVDRWANKGGLIAYRSRKRLETFLSLLVQNLAPAETHT
The following text describes a protein:
Function:
Component of SCF(ASK-cullin-F-box) E3 ubiquitin ligase complexes, which may mediate the ubiquitination and subsequent proteasomal degradation of target proteins.
Subcellular Localization:
Nucleus.
Domain:
The F-box is necessary for the interaction with ASK proteins.
Sequence:
MLPSRKTKRVFSCDFTPGRKRRRCVVVPSSVSPVPENTTGADLLDSIPDDLVISILCKLGSTSRCPADFINVLLTCKRLKGLAMNPIVLSRLSPKAIAVKAHNWSEYSHRFLKRCVDAGSLEACYTLGMIRFYCLQNRGNGASLMAKAAISSHAPALYSLAVIQFNGSGGSKNDKDLRAGVALCARAAFLGHVDALRELGHCLQDGYGVPQNVSEGRRFLVQANARELAAVLSSGIQARSTWLSLSQPPPPVVPNHGQQTCPLLSDFGCNVPAPETHPANRFLADWFAVRGGDCPGDGLRLCSHAGCGRPETRKHEFRRCSVCGVVNYCSRACQALDWKLRHKMDCAPVQRWLEEGDGGEGNVQIDGNGNGDNVLLPMS
The following text describes a protein:
Function:
Accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), that is believed to be not involved in catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone.
Subcellular Localization:
Mitochondrion inner membrane; Peripheral membrane protein; Matrix side.
Sequence:
MRGITHQQRVLRLYRNCLRHSLSWIVDRQAWRKEALMIRAQFEANKHETDRKRIAMIMEQAEAEFERKKHPYPYTFPTAAEGSKWERNTPPPPHVRQQRMLFI
The following text describes a protein:
Function:
Initiates complex N-linked carbohydrate formation. Essential for the conversion of high-mannose to hybrid and complex N-glycans.
Subcellular Localization:
Golgi apparatus membrane; Single-pass type II membrane protein.
Sequence:
MMDNNSSRYQKAVASKFPLFISQDGTNGDVKNKALSYTQIRYMQHVDLEPVHTERPGEHIAYYKIANHYKWALDELFIKHDFRRVIILEDDMEIAPDFFDYFEAAAKLLDTDKSIMAVSSWNDNGQKQFVYDPKALYRSDFFPGLGWMLTKTTWMELSPKWPKAYWDDWVRLKEVRRDRQFIRPEVCRTYNFGEHGSSMGQFFDQYLKPIKLNDAHIDWTSEDLSYLTEDNFLIKFGKDVASATPVHGFDELLKAHNLDVDVRIQYDDQGDFERVARQFGVFEEWKDGVPRAAYKGVVVFRYKSSRRRIYLVGPDSLRQLGV
The following text describes a protein:
Function:
Hydrolyzes UDP-glucose to glucose 1-phosphate and UMP and ADP-ribose to ribose 5-phosphate and AMP. The physiological substrate is probably UDP-glucose. Poor activity on other substrates such as ADP-glucose, CDP-glucose, GDP-glucose and GDP-mannose.
Subcellular Localization:
Cytoplasm.
Sequence:
MNDLSDVTIVPLENSNFVQPFRMLFKHAGKDRLWDLVRVHESVAIIIFNISKKKLIFVRQFRPAVYINSIPQEDRTNPIDTEKYPAKLGFTLELCAGIVDKKKTLAEIAAEEVLEECGYKVDPDKLEYIIQFHSGVGLSGDPQTVFYAEVTDEMKVSSGGGNPEEGELIDVVEMSMSEVEEFLAQKRVPSPGGFLFGLQWFFNKKASLFVS
The following text describes a protein:
Function:
S-adenosyl-L-methionine-dependent 2'-O-ribose methyltransferase that catalyzes the formation of 2'-O-methylguanosine at position 18 (Gm18) in a subset of tRNA. Selectively mediates Gm18 methylation of tRNAGln-TTG/CTG and tRNASer-TGA/GCT. Gm18 modification can enhance the stability of modified tRNAs.
Sequence:
MSSKILRLLEGFGDDAQVGAILRKAVAQAQTALASKDHAHAVDLIAFCSENLQSNPHLLQTEEVEDIVQRLCFPVAAARMMGGKEEETQGREILQRVCEFLAGTMSSSFRKHHPKPCEIVMKACTQSLLTYRDEVYTRDQGCNEFDEDEERKKGDLSISSSITVLSIYTKKLKQSPEKPDRSDEAEDLWWRELTEIVLDILETGEALVCVQLAQIMVPKDKDLPLGGRTRSEMLEMIWGRLVAMHERGVVRLEGVNENIYLILCALSDAYFPTSTEESTVKANDTGLDCSRGLNLLELELFWKLIQQGLIHTNPLTRKRCSYLMKRAVDVAATSGRSIGQGSHGLDEQPLFSWNPAEKEKLLRLWFEFFLIYETLEEVQIHVVTPAMPRLAQLTKATYRLDGAGIPIMHSSWLCILYQRCFVHESKTITRLGVTQCLNLDLDKSSFLHQSGPRFIFGPLLTALHEEYLYTKPPETPPGSQPPIGLALKKFMVFCVSQLNDDTRKTFLSDLLALICEQAWGPVTISFVAEALASIPAFPAWGRSSLFLLRDKLSSGFVTCPPGYRSTIQCFFLRAALHLLDWSSISLHQLSSLLGVCNAAEVLKRGSSLWEEVCQAFHDNMLNPTSSDPDIQPRSPWQTCIQEIKGYLHVDPTKEALERDDLPNREEAQRVVITMLMVADSQALDHPQDSHISDLLQPLHEVLGRAGSHVYLPTQKADKALQILYALLQESQTSSQDQRYSEFCTSLTILLCETLGEIFQYLIRQLLGNRDVQVHDVNSITLYRSFLDALLSHAGREHEGQGRSFQGQGLTLKIIEGRKQLLKGCEALMNSQLQNEHYVKEMHHCYTMTSILTWILSSEAFSPGAMLPSTSNMLTSLLRVEASASARLKEVAEAGDMRGLDGSNRGRLQSDVIRTKWEAILAVIQHWDRHRGKAGSGLTQEDDPVAWQPVLSACLSDTSLVSALHTRPLLKCTALLIDKVADENIPLCLEGLSACWCAVLDGWRANSTFWNLYEAFIAVAYQPTLLQLGEGTEVYEALQKYTSKILSQGETRLGMLNTLMCHLDKVLSEHFFLQPPENHRHDAMTVIRNLSGILQEAALFGPCVSKSVRLMEDISAYLVRHEELLTVRPILQNNSNATNPCHPRVLVISILMKIGASNFQGKEEFFEDFLSSLLDKDQEIIPKKRSYIINSVVHRLKLRIWQAAIIILNFLSPDAAPRILARVLRSMRAENQTSVRHLMEVFVVRMIHLHPHLLQQFWQYASEVANCQDVSFSPLLMIIAHLGTVQPKDQQESFYLQAIPTVLPWTFVPSMALRVQSQVALFKMWKDCKEAGLITLMDRFPGVAVCMDFTQNNSALHSLRERMEGSFFLSYFHPIQHFSVETIFYIMPKLTLVTEDELVHPELFLVSDTSPWKQNSNHPIVPLYSETDTLRTCQVKEKQKNKSVKDAEIREELWTEDGSGDIQKKITPWKESHIPGFESSEGQKSPRGHLVVVASLISRVPNLGGLCRTCEIFGASCLVLGNLALKDHQDFLSLSVSAERWLPLREVKPSDLKDYMIEMKKHGYTLVGVEQTANSQSLTDFKFPQRTMLLLGKEREGIPVELIQFLDVCVEIPQLGFIRSLNVHVSGALMIWEYTRQKLLGLKN
The following text describes a protein:
Function:
One of the primary rRNA binding proteins, it binds directly to 16S rRNA central domain where it helps coordinate assembly of the platform of the 30S subunit.
Subcellular Localization:
Mitochondrion.
Sequence:
MFRSVPSVRSAPLPNLPRAPAAASATARGEEAERAAAAAALVVRDPTSGPAMGRRILNDALRTMVNADRRGNATALLQPISGVMVSFLNIMKHRGYIKNFEVIDPHRVGKINVELHGRIKDCKALTYRQDLRAKEIEQYRVRMLPTRQWGYVVITTPNGVLDHEEAIRQNVGGQVLGYFH
The following text describes a protein:
Function:
Vacuolar Fe(2+) uptake transporter.
Subcellular Localization:
Vacuole membrane; Multi-pass membrane protein.
Domain:
The cytoplasmic metal binding domain (MBD) is located between transmembrane 2 (TM2) and transmembrane 3 (TM3).
Sequence:
MDGHGHGDGRQPMLEKGPPSHRERHFTAGEVVRDVIMGVSDGLTVPFALAAGLSGASAPSSLVLTAGLAEVAAGAISMGLGGYLAAQSEADHYKREMKREQDEIIAVPDTEAAEIGDIMAEYGLEPHEYGPVVEGLRRNPQAWLEFMMRFELGLEKPDPRRALQSALTIALSYIIGGLVPLLPYMFISTVQDAMLTSVGVTLLALLFFGYIKGRFTGNRPFLSAVQTTIIGAVASAAAYGMAKAVQAR