lhallee/plat_data huggingface dataset:
The following text describes a protein:
Function:
Filament-forming cytoskeletal GTPase (By similarity). May play a role in cytokinesis (Potential). May play a role in platelet secretion (By similarity).
Miscellaneous:
MISCELLANEOUS: In a heterologous system, SEPTIN5 overexpression has been shown to exert dopamine-dependent neurotoxicity. As wild-type PRKN, but not familial-linked PRKN mutants, ubiquitinates mouse SEPTIN5 and promotes its degradation, it has been suggested that a deficiency in SEPTIN5 degradation may contribute to the development of early onset Parkinson disease 2 (PARK2).
Subcellular Localization:
Cytoplasm. Cytoplasm, cytoskeleton. Note=In platelets, found in areas surrounding alpha-granules.
Sequence:
MSTGLRYKSKLATPEDKQDIDKQYVGFATLPNQVHRKSVKKGFDFTLMVAGESGLGKSTLVHSLFLTDLYKDRKLLSAEERISQTVEILKHTVDIEEKGVKLKLTIVDTPGFGDAVNNTECWKPITDYVDQQFEQYFRDESGLNRKNIQDNRVHCCLYFISPFGHGLRPVDVGFMKALHEKVNIVPLIAKADCLVPSEIRKLKERIREEIDKFGIHVYQFPECDSDEDEDFKQQDRELKESAPFAVIGSNTVVEAKGQRVRGRLYPWGIVEVENQAHCDFVKLRNMLIRTHMHDLKDVTCDVHYENYRAHCIQQMTSKLTQDSRMESPIPILPLPTPDAETEKLIRMKDEELRRMQEMLQRMKQQMQDQ
The following text describes a protein:
Function:
Cyclin-dependent kinase binding protein. Enhances cyclin-dependent kinase tyrosine phosphorylation by nonreceptor tyrosine kinases, such as that of CDK5 by activated ABL1, which leads to increased CDK5 activity and is critical for neuronal development, and that of CDK2 by WEE1, which leads to decreased CDK2 activity and growth inhibition. Positively affects neuronal outgrowth. Plays a role as a regulator for p53/p73-induced cell death (By similarity).
Subcellular Localization:
Nucleus. Cytoplasm. Note=Located in the cell body and proximal region of the developing axonal shaft of immature neurons. Located in axonal growth cone, but not in the distal part of the axon shaft or in dendritic growth cone of mature neurons (By similarity).
Sequence:
MAAAAAAATTAACSSGSAGTDAAGASGLQQPPPQPQPQPAAAAPAQPPPEPPRKPRMDPRRRQAALSFLTNISLDGRLPPQDAEWGGGEEGGAAKPGAGGACGARTRFSLLAAAERGGCIALAAPGTPAAGLAAGSGPCLPQPSSLPPLIPGGHATVSGPGVARGFASPLGAGRASGEQWQPPRPAPLAACAQLQLLDGSGAAGQEELEEDDAFISVQVPAAAFLGSGTPGSGSGSRGRLNSFTQGILPIAFSRPTSQNYCSLEQPGQGGSTSAFEQLQRSRRRLISQRSSLETLEDIEENAPLRRCRTLSGSPRPKNFKKIHFIKNMRQHDTRNGRIVLISGRRSFCSIFSVLPYRDSTQVGDLKLDGGRQSTGAVSLKEIIGLEGVELGADGKTVSYTQFLLPTNAFGARRNTIDSTSSFSQFRNLSHRSLSIGRASGTQGSLDTGSDLGDFMDYDPNLLDDPQWPCGKHKRVLIFPSYMTTVIDYVKPSDLKKDMNETFKEKFPHIKLTLSKIRSLKREMRKLAQEDCGLEEPTVAMAFVYFEKLALKGKLNKQNRKLCAGACVLLAAKIGSDLKKHEVKHLIDKLEEKFRLNRRELIAFEFPVLVALEFALHLPEHEVMPHYRRLVQSS
The following text describes a protein:
Function:
Thiol protease. Has dipeptidylpeptidase activity. Active against a broad range of dipeptide substrates composed of both polar and hydrophobic amino acids. Proline cannot occupy the P1 position and arginine cannot occupy the P2 position of the substrate. Can act as both an exopeptidase and endopeptidase. Activates serine proteases such as elastase, cathepsin G and granzymes A and B.
Subcellular Localization:
Membrane.
Sequence:
MILIFQLFLINILFLNFIKCDIPVHCLSRHVEGKWEIHLGLLKKKKNSKQKNVEGVILNDKVTGGNVWNISGDIKKNETTAYDNNYDNNYDYQCGYKRPDNADYHDDLNPENEDTKERFEEKEKRYIVFNEDRSLNILNEEGDINSRYSGYWKIIYDEGLYIEVYKEDDSKEVYFSFFKFKQKGDVSYSYCNNLIMGVMNKYSLDNNIWDMRYEENIEENIRSDDKNNNIHMIKDEKKSVLNIDEKNREISNNISHIYMIRKNVTFFGLRNNKIKKPKRKKMKDKIIISKGNNNINEIQNDDNYNKIIKEKNFFQLIDYYNDNYISSGRFNIDKFCWYGKKVQEHSEQPTNKIPVQNISPLSVNADEYNKLYDEKKKIINNLQKSQDDQLSHSSDNNNNNDNNDNNDNNDNNDNNDNNDNNNNVQNVVYLRRHKDVFRKYNKGLLLMNRNNKYEKRNSLFYKYIDKNIDLKNFDWNNKEDIKMRLGHYIKILDDAIDQKDCGSCYANSASFIINSRVRIKYNYIKNIDSLFFSNEQLILCDIFNQGCNGGYIYLSLKYAYENYLYTQKCFEKYKKKINYNTDDLEIKSSLMSQDDNSLLCDQFDVFKIKNEKKKNNEINIKEQITMNINNDSNKNQEYTNNDHDHLLILSYQIQTDPNKKDDNKKNINIYGLNEDYILIDEQKYNNNHNNNDDDEEYDIFKSNSCDVKINVSKFEYLDIQDEELLKKYIYYNGPVAAAIEPSSEFIGYKKGIILGNFIKMYDGTKNNAYIWNKVDHAVVIVGWGEDTLPNFVKKNKLSKETMEHILTTWKENNKDNGDSNNNGDSNNNGDSNNNGDSNNNGDSNNNGDSNDNGDNKDNGDSNDNGDNNNDNGDNNDNGDNNIINNNNNVIIKYWKVLNSWGTNWGNSGYFYILRNNNSFNIKSYILACDVNLFVKQKET
The following text describes a protein:
Function:
Catalyzes the conversion of homogentisate to maleylacetoacetate.
Sequence:
MAGLKYMSGFGNEFSSEDPRCPGSLPEGQNNPQVCPYGLYAEQLSGSAFTCPRSSNKRSWLYRILPSVRHKPFTRMSCGDLTENWNEVEPDPNQLRWKPFNIPKSSEKKVDFVSGLHTVCGAGDSKSRNGIAIHMYSCNTSMTDKCFQNADGDFLIVPQQGEILITTEFGKMMVEPNEICVIQQGMRFSVDVFGETRGYILEVFGAHFELPDLGPIGANGLANPRDFQTPVAWYEDRTIATGYTIVNKYQGKLFSCQQDFSPFNVVAWHGNYAPYKYNLENFMVINCVAFDHADPSIFTVLTAKSTRPGVAIADFVIFPPRWGVADHTFRPPYYHRNCMSEFMGLIKGHYEAKEEGFQPGGGSLHSIMTPHGPDVDCFEKNSTALLKPERVAEGTMAFMFESSFSMAVTKWGLETCQRLDKNYYKCWEALKSHFNPNWKPSSK
The following text describes a protein:
Function:
Pump for glutathione S-conjugates.
Subcellular Localization:
Membrane; Multi-pass membrane protein.
Sequence:
MRWLSSTWLSDLSCSSSSVIEPSSSLPAPIQWLRFILLSPCPQRLLSSTVDVLFLLILFFFAIQKLCSSSSSRTNGEADITKPLLGRRTRTRTTGLFKTTVVVTIVLSFCSLVLCVSAFFTTRTKLKLVDTLFWLIHAVTNVVIAVLVLHLKRFASPSHPLTLRIYWVFNFVVTTLFTVSGILHLLSDDPAAASLRADDVASFISFPLTAVLLLVSIKGSTGVVVTTSNVTAPAKSNDVVVEKSENVSLYASASFISKTFWLWMNPLLRKGYKSPLNLDQVPTLSPEHRAEKLATLFESKWPKPQENSRNPVRTTLIRCFWKEIAFTAVLAIIRLSVIYVGPVLIQSFVDFTSGKRSSPSQGYYLVLILLIAKFVEVLSTHQFNFNSQKLGMLIRSTLITALYKKGLKLTGSARQNHGVGQIVNYMAVDAQQLSDMMLQLHAIWLMPLQVAAAIVLLYNTLGPSVVTTVIGLTGIFVFILLGTKRNNRYQFSLMMNRDSRMKATNEMLNYMRVIKFQAWEDHFNERILKFREMEFGWLSKFLYSIAGNIIVLWSTPVLISALTFTTAVFLGVKLDAGTVFTTTTIFKILQEPIRTFPQSMISLSQAMISLGRLDAYMMSRELSEETVERSQGCDGNVAVEIKDGSFSWDDEDDEPAIENINFEVKKGELAAIVGTVGSGKSSLLASVLGEMHKLSGKVRVCGTTAYVAQTSWIQNGTVQDNILFGLPMNRSKYNEVLKVCCLEKDMQIMEFGDQTEIGERGINLSGGQKQRIQLARAVYQESDVYLLDDVFSAVDAHTGSDIFKKCVRGALKGKTILLVTHQVDFLHNVDRILVMRDGMIVQSGKYDELVSSGLDFGELVAAHETSMELVEAGSASATAANVPMASPITQRSISIESPRQPKSPKVHRTTSMESPRVLRTTSMESPRLSELNDESIKSFLGSNIPEDGSRLIKEEEREVGQVSFQVYKLYSTEAYGWWGMILVVFFSVAWQASLMASDYWLAYETSAKNEVSFDATVFIRVYVIIAAVSIVLVCLRAFYVTHLGLKTAQIFFKQILNSLVHAPMSFFDTTPSGRILSRASTDQTNVDIFIPFMIGLVATMYTTLLSIFIVTCQYAWPTVFFIIPLGWLNIWYRGYYLASSRELTRLDSITKAPVIHHFSESIAGVMTIRAFKKQPMFRQENVKRVNANLRMDFHNNGSNEWLGFRLELIGSWVLCISALFMVMLPSNIIKPENVGLSLSYGLSLNGVLFWAIYLSCFIENKMVSVERIKQFTDIPAEAKWEIKESRPPPNWPYKGNIRLEDVKVRYRPNTPLVLKGLTIDIKGGEKIGVVGRTGSGKSTLIQVLFRLVEPSGGKIIIDGIDICTLGLHDLRSRFGIIPQEPVLFEGTVRSNIDPTEKYSDEEIWKSLERCQLKDVVASKPEKLDSLVADNGENWSVGQRQLLCLGRVMLKRSRILFLDEATASVDSQTDAMIQKIIREDFSDCTIISIAHRIPTVMDCDRVLVIDAGKAKEYDSPVRLLERQSLFAALVQEYALRSAGI
The following text describes a protein:
Function:
Involved in histone pre-mRNA 3' processing. Required for chromosome condensation, progression of cell death and morphogenesis.
Sequence:
MAQKTPTKGTRSSPRKKAWGSPIKATAKFQSDIFSVEDFADLSNRSWAEVTEEDDELASRLEEERRCKSESRRKGQPKRAQNSQNKPKFVRSLELTNEVFQSTSSRRSQRSKSRTRNGDTITTVEEHTETVVMESSSGPISRKRCLSNASTINEGASPSKRRPETGKSNRKAPRGRLFTNGGSDSSSVASSPSRRDHWEEPTLGWCTDEAVLKRRSREIDRAKEKAVYQRYTSEVPLRDRIKGQHPRTPNKLINFSRRSWDTQIKKWKRSLYEYCGEEPSDSVNTSFCYSDSDALSEAGDNDKEIENRSVLRDLVIPVTMRPEVDSMASLLGKFDVDSQMGMDESTLKASTNTDPSAPTDFSKMSSH
The following text describes a protein:
Function:
Phosphorylates Ins(1,3,4,5,6)P5 at position 2 to form Ins(1,2,3,4,5,6)P6 (InsP6 or phytate).
Domain:
The EXKPK motif is conserved in inositol-pentakisphosphate 2-kinases of both family 1 and 2.
Sequence:
MVSISNTGSENGFVGTDSADKPHFQVVRGMKLCEEDAEDWSYRGEGAANIVLAYDGEKPSFVGRVLRIRKASRNPSGLIDNGTQNQVKKDAKPVLTEHEIKLWREWPSMCEATTSAALAHAYACEIMQPLLGKDHIDAGMLVFLTTGFLEAVSKEVNANQPEWRRKDAQMDMTGGLALMIADHSSFPALRSSARDLPQTITVELKPKWGFLPTAATISDKNNVKRHVPRFTMLQHLKLQQGKAKAISKYSPLDLFSGSDERIIKALVDLFETPQNNVRVFLEGEQVFGAPADGQSIDEEVSSLEEKLAAVSVAPEGERVSVFQRLVASALNKSKALDQLLRVQKLDTYDIEGAILAYDKFMEMADNADADDSSEAVSTSSENGKSINGSCFTRIDNLALEAEGELKNRDKEWIKSLTWEQSCCVVRNFLIAGTAKDCGLMLTLRPLHNRQGKAFPVPSAPIVACPTTGQQYIFKVAFLDLDPKRLKKMPFYHSLDQQIVDTYKASLT
The following text describes a protein:
Function:
Component of the MICOS complex, a large protein complex of the mitochondrial inner membrane that plays crucial roles in the maintenance of crista junctions, inner membrane architecture, and formation of contact sites to the outer membrane.
Subcellular Localization:
Mitochondrion inner membrane; Single-pass membrane protein.
Sequence:
MSAPAPAASIPTPPAPVAAPIPSEDQIARKFDNCVADLLVNAGLGFGVGVVASVLLFRRRGWPVALSTGFGAGVAYSNCNYSLNPYVLPGTKVLPSNRP
The following text describes a protein:
Function:
Subunit of the replication factor C (RFC) complex which acts during elongation of primed DNA templates by DNA polymerases delta and epsilon, and is necessary for ATP-dependent loading of proliferating cell nuclear antigen (PCNA) onto primed DNA.
Subcellular Localization:
Nucleus.
Sequence:
MRANSKCKGTRTGLRWSLSRPLGGRDDPSGPDHLRLLFMETSAPEQQQSAATAKIRNLPWVEKYRPQTLNDLISHQDILSTIQKFISEDRLPHLLLYGPPGTGKTSTILACAKQLYKDKEFGSMVLELNASDDRGIDIVRGPILSFASTRTIFKKGFKLVILDEADAMTQDAQNALRRVIEKFTENTRFCLICNYLSKIIPALQSRCTRFRFGPLTPELMVPRLQHVVEEENLNHSRPSRSLGECLCSQGPLCPFCLFPFRVAISEDGMKALVTLSSGDMRRALNILQSTNMAFGKVTEETVYTCTGHPLKSDIANILDWMLNQDFTTAYRNITELKTLKGLALHDILTEIHLFVHRVDFPTSVRIHLLTKMADIEYRLSVGTNEKIQLSSLIAAFQVTRDLIVSEA
The following text describes a protein:
Function:
Displays enzymatic activity both for medium-chain fatty acid (MCFA) ethyl ester synthesis and hydrolysis (esterase activity). MCFA are toxic for yeast and this enzyme could thus be involved in their detoxification by esterification.
Sequence:
MGLPTFAPRSWGYRGTITHRPHEEGLVKLPLKDKEKEPVTLSDLLNEHVPELKDGARFYLHPYLYNGILQTMYLYGADFSQQYKPFYGREIVSYSDGGVSTADWAMREWDDLYAAPEGYNKEKFDADAAKTHPENWPRLQPNTRFLDEEELAKIPKDTRPLIVVAHGLAGGSHENIIRALVTELLSVGNGQFNVVVLNSRGCARSKIANKKLFSAFHTMDIREFINREHARQPERKIYGLGFSFGSVIFGNYLGEEGDKSPLSGAVCCAGPWDMFASSKMLNDDFWISRLFGKNLVKHLSRLLHVNRKELEYDGSKGDDVEDASPTNPASHIFTKENLARASTMACTRDFDNFFTAPALGFKNANDYYKAASPVNIVGKIRVPTLLINALDDPMVGAEGFLPIEKLRSNKHILLCTTDIGGHLAYLDKNYTPWMAGRVAEFLSKMDTLVA
The following text describes a protein:
Function:
Thioredoxin reductase; part of the gene cluster that mediates the biosynthesis of gliotoxin, a member of the epipolythiodioxopiperazine (ETP) class of toxins characterized by a disulfide bridged cyclic dipeptide. The first step in gliotoxin biosynthesis is the condensation of serine and phenylalanine to form the cyclo-L-phenylalanyl-L-serine diketopiperazine (DKP) by the NRPS gliP. GliP is also able to produce the DKP cyclo-L-tryptophanyl-L-serine, suggesting that the substrate specificity of the first adenylation (A) domain in gliP is sufficiently relaxed to accommodate both L-Phe and L-Trp. The cytochrome P450 monooxygenase gliC has been shown to catalyze the subsequent hydroxylation of the alpha-carbon of L-Phe in cyclo-L-phenylalanyl-L-serine whereas the second cytochrome P450 enzyme, gliF, is presumably involved in the modification of the DKP side chain. The glutathione S-transferase (GST) gliG then forms a bis-glutathionylated biosynthetic intermediate which is responsible for the sulfurization of gliotoxin. This bis-glutathionylated intermediate is subsequently processed by the gamma-glutamyl cyclotransferase gliK to remove both gamma-glutamyl moieties. Subsequent processing via gliI yields a biosynthetic intermediate, which is N-methylated via the N-methyltransferase gliN, before the gliotoxin oxidoreductase gliT-mediated disulfide bridge closure. GliN-mediated amide methylation confers stability to ETP, damping the spontaneous formation of tri- and tetrasulfides. Intracellular dithiol gliotoxin oxidized by gliT is subsequently effluxed by gliA. GliT is required for self-protection against gliotoxin. GliT plays a role in preventing dysregulation of the methyl/methionine cycle to control intracellular S-adenosylmethionine (SAM) depletion and S-adenosylhomocysteine (SAH) homeostasis during gliotoxin biosynthesis and exposure.
Sequence:
MSIGKLLSNGALLVDVLIIGAGPAGLSTATGLARQLHTAVVFDSGVYRNAKTQHMHNVLGWDHRNPAELRAAGRADLTTRYSTIQFQNSTIEAIRQVETNQLFEARDNEGHSWYGRKVVLATGVRDIPLDIEGYSECWANGIYHCLFCDGYEERGQETVGVLALGPIANPARALHLARMALRLSESVTIYTNGNEQLAKEIQQAAEESPVGASGLKFEARPIRRFEKGDVAKTVIVHLGESESKTEGFLVYNPQTEVNGPFAKQLALNMTEGGDILTTPPFYETSVPGVFAVGDCATPLKAVTPAVSMGSLAAGGLVAQLQAQALPEFRLDQEL
The following text describes a protein:
Function:
This is a copper-containing oxidase that functions in the formation of pigments such as melanins and other polyphenolic compounds. Catalyzes the rate-limiting conversions of tyrosine to DOPA, DOPA to DOPA-quinone and possibly 5,6 dihydroxyindole to indole-5'6 quinone. Binds to the surface of hemocytes and is involved in hemocyte melanization.
Subcellular Localization:
Secreted.
Sequence:
MADIFDSFELLYDRPGEPMINTKGEDKVLFELTEQFLTPEYANNGLELNNRFGDEEEVSRKIILKNLDKIPEFPKAKQLPNDADFSLFLPSHQEMANEVIDVLMSVTENQLQELLSTCVYARINLNPQLFNYCYTVAIMHRRDTGKVRVQNYAEIFPAKFLDSQVFTQAREAAAVIPKTIPRTPIIIPRDYTATDLEEEHRLAYWREDLGINLHHWHWHLVYPFSASDEKIVAKDRRGELFFYMHQQIIARYNCERLCNSLKRVKKFSDWREPIPEAYYPKLDSLTSARGWPPRQAGMRWQDLKRPVDGLNVTIDDMERYRRNIEEAIATGNVILPDKSTKKLDIDMLGNMMEASVLSPNRDLYGSIHNNMHSFSAYMHDPEHRYLESFGVIADEATTMRDPFFYRVHAWVDDIFQSFKEAPHNVRPYSRSQLENPGVQVTSVAVESAGGQQNVLNTFWMQSDVNLSKGLDFSDRGPVYARFTHLNHRPFRYVIKANNTASARRTTVRIFIAPKTDERNLPWALSDQRKMFIEMDRFVVPLSAGENTITRQSTESSLTIPFEQTFRDLSIQGSDPRRSELAAFNYCGCGWPQHMLVPKGTVGGVAYQLFVMLSNYELDKIEQPDGRELSCVEASMFCGLKDKKYPDARPMGYPFDRPSNSATNIEDFSAMSNMGLQDIVIKLSDVTEPNPRNPPA
The following text describes a protein:
Function:
Proton-dependent permease that transports di- and tripeptides.
Subcellular Localization:
Cell inner membrane; Multi-pass membrane protein.
Sequence:
MNTTAPTGLLQQPRPFFMIFFVELWERFGYYGVQGILAVFFVKQLGFSQEQAFITFGAFAALVYGLISIGGYVGDHLLGTKRTLVLGAIVLAIGYFMTGMSLLNPDLIFIALGTIAVGNGLFKANPASLLSKCYQPKDPRLDGAFTLFYMSINIGSLLSLSLAPVIADKFGYAVTYNLCGAGLIVALLVYFACRGMVKNIGSEPDHKPLRFRNLLLVLLGTVVMIFLCAWLMHNVKIANLVLIVLSIVVTIFFFREAFRLDKTGRNKMFVAFILMIEAVLFYILYAQMPTSLNFFAINNVHHEILGFAINPVSFQALNPFWVVVASPVLAAIYTRLGSKGKDLTMPMKFTLGMFLCALGFLTAAAGMWFADAQGLTSPWFIVLVYLFQSLGELLISALGLAMVAALVPQHLMGFILGMWFLTQAAAFLLGGYVATFTAVPENITDPLQTLPIYTGVFSKIGLVTLAVTVVMAIMVPWLNRMINTPGTEQ
The following text describes a protein:
Function:
RNA polymerase that catalyzes the synthesis of short RNA molecules used as primers for DNA polymerase during DNA replication.
Domain:
Contains an N-terminal zinc-binding domain, a central core domain that contains the primase activity, and a C-terminal DnaB-binding domain.
Sequence:
MIDQVTIDRILDAAQIVDVVSEFVTLRKRGVNYVGLCPFHNEKTPSFSVSPAKGLCKCFSCGKGGNSVHFIMEHEQMSYYEALKYLAKKYNIEIKERELTNEEKQAQTTRESMFIVNNFARDYFQNILKNHVDGRSIGLAYFRQRGFRDDIIEKFQLGYCTESHDAMSQEALRKGYKKEFLVKTGICYETDDHRLRDRFWGRVIFPVHTLSGKVVAFGGRVLSTATKGVKVKYVNSPESEIYHKSNELYGIYFAKQAIVRQDRCFLVEGYTDVISMHQSGIENVVASSGTALTPGQIRLIHRFTNNITVLYDGDVAGIKASIRGIDMLLEEGMNIKVCLLPDGDDPDSFARKHNSEEFQAFIREHEKDFIRFKTDLLMEDAGRDPIKRAELISNIVRSISVIPEAIIRDVYIKECSQHLRIEEKLLVAEVAKLREAQAEKANRPSYNHSSSTTGDTSGTAAASGTPAYSGAPTYSTPSSPYANAGMPPEPEYDDDGNIVSFADPMSAATGGAAGFPPGNAPASTTDTTVPGDSYTSFIPQEGKEGQEFYKFERLILQAVVRYGEKVMCNLTDEEGNEIPVTVIEYVVNDLKEDDLAFHNPLHRQILTEAATHIHDAGFIAERYFLAHPDQTISRLSVDLINVRYQLSKYHSKSQKIVTDEERLYELVPMLMINFKYAIVTEELKHMLYALQDPALAHDNEKCNSLMQRYNEMREVQSLMAKRLGDRVVLR
The following text describes a protein:
Function:
Key player in the regulation of energy balance and body weight control. Once released into the circulation, has central and peripheral effects by binding LEPR, found in many tissues, which results in the activation of several major signaling pathways.
Subcellular Localization:
Secreted.
Sequence:
MQYIHLSFWGIFWMLLPVSQGRAIKADRVKNDAKLLASTLITRIQEHPIQFLFPSNLKISGLDFIPDEQLLESLEHMDETLEVFQKILSSLPMENVDQMLSDMENLRSLLQSLSTIMGCTARKHSQCDTQVNLTEEYAKAPYTTEKVALDRLQKSLHSIVKHLDHITDC
The following text describes a protein:
Function:
Mediates sugar transport across membranes.
Subcellular Localization:
Cell membrane; Multi-pass membrane protein. Golgi apparatus membrane; Multi-pass membrane protein.
Sequence:
MSFGFGELLENFTIGLTLILHLSGLSACQCMVRSKSTKGVPYLIFIFSTISCIIMIKYACILEQPKLIFLNSVGLVLYVIYISLYLMYADNKAYDLAILGSLLAVPISLLFFTSGWISANNGGDKNGDGDASGKGDVLNVLGSALTINALFLISIPSIEVYHNLVNRNREGMPLVMIISGLACFISWLAYGIMLNDIFIYLPNGIGMMVQALKLYAFVAFDDDGGDDVGEGGGGGGGGGGRGGARKKKK
The following text describes a protein:
Function:
Involved in the assembly of mitochondrial iron-sulfur proteins. Probably involved in the binding of an intermediate of Fe/S cluster assembly.
Sequence:
MAATRASKLFAAAAESVGSSARKQVLDLTDTAATRIRHLLQQRQRPFLRLGVKARGCNGLSYTLNYADEKGRFDELVADKGVKILIDPKALMHVIGTKMDFVDDKLRSEFVFINPNSQGQCGCGESFMTTSSSETAKRGGS
The following text describes a protein:
Function:
Potential calcium sensor.
Sequence:
MKFFSSSSKKSKKTINISDRPPSSFSSASSDTSGTPTTPTTVLSAPPVCRRYIGRNASCLDPEYDPPREITATTIAGRCKLSSCNYSSSSLRRDEDGKLTCEELRHVLWRLDGGVVDDVSGILAELDRDGDGRINLEELLKAREEDKAREEEELRVAFGVYDADGDGKISAEELWNVFQILGDETCRIEDCRKMIGSVDSDGDGYVCFKDFAKMMSNSTITS
The following text describes a protein:
Function:
Involved in resistance to GST substrate o-dinitrobenzene (o-DNB).
Domain:
The PY-motifs are required for the interaction with RSP5 ubiquitin-ligase.
Sequence:
MGFSSGKSTKKKPLLFDIRLKNVDNDVILLKGPPNEAPSVLLSGCIVLSINEPMQIKSISLRLYGKIQIDVPLERPQDASSSSLSSSPPKIRKYNKVFYNYAWDNVNLKEYLSGLRGQSGLAGSSSSSNILGTRQRAQSTSSLKSLKGSSSPSSCTLDKGNYDFPFSAILPGSLPESVESLPNCFVTYSMESVIERSKNYSDLICRKNIRVLRTISPAAVELSETVCVDNSWPDKVDYSISVPNKAVAIGSATPINISIVPLSKGLKLGSIKVVLFENYQYCDPFPPVISENRQVTELNLEDPLNESSGEFNGNGCFVNNPFFQPDHSFQDKWEIDTILQIPNSLSNCVQDCDVRSNIKVRHKLKFFIILINPDGHKSELRASLPIQLFISPFVALSIKPLSSSNLYSLFSTTNQKDENSSQEEEEEYLFSRSASVTGLELLADMRSGGSVPTISDLMTPPNYEMHVYDRLYSGSFTRTAVETSGTCTPLGSECSTVEDQQQDLEDLRIRLTKIRNQRDNLGLPPSASSAAASRSLSPLLNVPAPEDGTERILPQSALGPNSGSVPGVHSNVSPVLLSRSPAPSVSAHEVLPVPSGLNYPETQNLNKVPSYGKAMKYDIIGEDLPPSYPCAIQNVQPRKPSRVHSRNSSTTLSSSIPTSFHSSSFMSSTASPISIINGSRSSSSGVSLNTLNELTSKTSNNPSSNSMKRSPTRRRATSLAGFMGGFLSKGNKR
The following text describes a protein:
Function:
Catalyzes the biosynthesis of phosphatidylinositol (PtdIns) as well as PtdIns:inositol exchange reaction. May thus act to reduce an excessive cellular PtdIns content. The exchange activity is due to the reverse reaction of PtdIns synthase and is dependent on CMP, which is tightly bound to the enzyme.
Subcellular Localization:
Membrane; Multi-pass membrane protein.
Sequence:
MAKKERPRPEKLSVYLYIPNIVGYMRVLLNCVAFAVCFSNKPLFSVLYFFSFCCDAVDGWVARRFNQVSTFGAVLDMVTDRVSTACLLVILSQIYRPSLVFLSLLALDIASHWLQMYSTFLAGKSSHKDVKDSTSWLFRLYYGNRIFMCYCCVSCEVLYIILLLIAKNQSENLLNVVVATLTQISPLSFLLALTLFGWSMKQTINVIQMKTAADVCVLYDIEKQQKP
The following text describes a protein:
Function:
Plays a role in signal transduction by regulating the intracellular concentration of cyclic nucleotides. Can hydrolyze both cAMP and cGMP, but has higher affinity for cAMP and is more efficient with cAMP as substrate. May play a critical role in regulating cAMP and cGMP levels in the striatum, a region of the brain that contributes to the control of movement and cognition.
Subcellular Localization:
Cytoplasm, cytosol.
Domain:
The tandem GAF domains bind cAMP, and regulate enzyme activity. The binding of cAMP stimulates enzyme activity (By similarity); Composed of a C-terminal catalytic domain containing two divalent metal sites and an N-terminal regulatory domain which contains one cyclic nucleotide-binding region.
Sequence:
MSNDSTEGTVGSCNATGLTDEKVKAYLSLHPQVLDEFVSESVSAETVEKWLKRKTNKAKDEPSPKEVSRYQDTNMQGVVYELNSYIEQRLDTGGDNHLLLYELSSIIRIATKADGFALYFLGECNNSLCVFIPPGMKEGQPRLIPAGPITQGTTISAYVAKSRKTLLVEDILGDERFPRGTGLESGTRIQSVLCLPIVTAIGDLIGILELYRHWGKEAFCLSHQEVATANLAWASVAIHQVQVCRGLAKQTELNDFLLDVSKTYFDNIVAIDSLLEHIMIYAKNLVNADRCALFQVDHKNKELYSDLFDIGEEKEGKPIFKKTKEIRFSIEKGIAGQVARTGEVLNIPDAYADPRFNREVDLYTGYTTRNILCMPIVSRGSVIGVVQMVNKISGSAFSKTDENNFKMFAVFCALALHCANMYHRIRHSECIYRVTMEKLSYHSICTSEEWQGLMRFNLPARICRDIELFHFDIGPFENMWPGIFVYMIHRSCGTSCFELEKLCRFIMSVKKNYRRVPYHNWKHAVTVAHCMYAILQNNNGLFTDLERKGLLIACLCHDLDHRGFSNSYLQKFDHPLAALYSTSTMEQHHFSQTVSILQLEGHNIFSTLSSSEYEQVLEIIRKAIIATDLALYFGNRKQLEEMYQTGSLNLHNQSHRDRVIGLMMTACDLCSVTKLWPVTKLTANDIYAEFWAEGDEMKKLGIQPIPMMDRDKRDEVPQGQLGFYNAVAIPCYTTLTQILPPTEPLLKACRDNLNQWEKVIRGEETAMWISGPGPAPSKSTPEKLNVKVED
The following text describes a protein:
Function:
Essential for the control of the cell cycle at the G2/M (mitosis) transition. Interacts with the CDC2 protein kinase to form MPF. G2/M cyclins accumulate steadily during G2 and are abruptly destroyed at mitosis.
Miscellaneous:
MISCELLANEOUS: Present with 339 molecules/cell in log phase SD medium.
Sequence:
MSNPIENTENSQNTSSSRFLRNVQRLALNNVTNTTFQKSNANNPALTNFKSTLNSVKKEGSRIPQFTRESVSRSTAAQEEKRTLKENGIQLPKNNLLDDKENQDPSSQQFGALTSIKEGRAELPANISLQESSSAKEIIQHDPLKGVGSSTEVVHNSVENEKLHPARSQLQVRNTESETDSGKKRPISTIVEQELPKKFKVCDENGKEEYEWEDLDAEDVNDPFMVSEYVNDIFEYLHQLEVITLPKKEDLYQHRNIHQNRDILVNWLVKIHNKFGLLPETLYLAINIMDRFLGKELVQLDKLQLVGTSCLFIASKYEEVYSPSIKHFASETDGACTEDEIKEGEKFILKTLKFNLNYPNPMNFLRRISKADDYDIQSRTLAKFLLEISLVDFRFIGILPSLCAAAAMFMSRKMLGKGKWDGNLIHYSGGYTKEELAPVCHMIMDYLVSPIVHDEFHRKYQSRRFMKASIISVQWALKVRKNGYDIMTLHE
The following text describes a protein:
Function:
Probable catalytic subunit of the gamma-secretase complex, an endoprotease complex that catalyzes the intramembrane cleavage of integral membrane proteins such as Notch receptors. Requires the other members of the gamma-secretase complex to have a protease activity.
Subcellular Localization:
Endoplasmic reticulum membrane; Multi-pass membrane protein. Golgi apparatus membrane; Multi-pass membrane protein.
Sequence:
MGKKVGIHTFLEFYARKVAKIAVPVVLTLILDAVCIRFIERTHGSAELNRNFVDTMSRNDSGISVTASIWSAVGIIFMIIVVTAILLTLYYFGCMKIIFGWLILAVSLLLSMYFLVGFGTYPSIVNIPVDYLSLAVFLLNLVVVGNMSIFWRAPQRITQAFLVLISILTSIVFRYLPDWTVWILLVLLIIYDACVVLCPNGLLILLLKKSEERGDAIPALLYSAAAWEEADPEKGNQNNEEGDGNEGNQEDPAEQADNQDNNEEEEEEEEAENNQPQENANGEAQNGNQNNNKKKKNMSKRDNEGIKLGLGDFVFYGILVSRAARIGWDITILCIFAVILGLSLTLVCLAVWERPLPALPFSLALGIVFFIIGAMTFRQFCEHMRWGLVAF
The following text describes a protein:
Function:
Proteolytically removes the C-terminal three residues of farnesylated proteins.
Subcellular Localization:
Endoplasmic reticulum membrane; Multi-pass membrane protein.
Sequence:
MVFPYMEAVVGFMILMYFFETYLDLRQHAALKLPKLPKTLEGVISQEKFEKSRGYSLDKSHFHFVHEFVTILMDSAILLFRILPWFWKKSGNFLVLVGLDAENEILHTLSFLAGVMLWSQLTDLPFSLYSTFVIEARHGFNKQTIWLFFRDMIKGMILAIVLGPPIVSAIIIIVQKGGPYLAIYLWAFMFVLSLVMMTLYPVLIAPLFNKFTPLPEGELREKIEKLASSLKFPLKKLFVVDGSTRSSHSNAYMYGFFKNKRIVLYDTLIQQCKNDEEIVAVIAHELGHWKLNHTMYSFIAVQVLTLLQFGGYTLVRNSTDLFRSFGFDTQPVLIGLIIFQHTVIPIQHLVSFGLNLVSRSFEFQADAFAKKLGYASALRAGLVKLQEENLSAMNTDPWYSAYHYSHPPLVERLAAIDEPDKKEK
The following text describes a protein:
Function:
Component of the CHS5/6 complex which mediates export of specific cargo proteins, including chitin synthase CHS3. Also involved in targeting FUS1 to sites of polarized growth.
Miscellaneous:
MISCELLANEOUS: Present with 172 molecules/cell in log phase SD medium.
Subcellular Localization:
Golgi apparatus, trans-Golgi network membrane; Peripheral membrane protein. Note=Trans-Golgi network location requires interaction with myristoylated GTP-bound ARF1 for the recruitment to the membranes.
Sequence:
MSSVDVLLTVGKLDASLALLTTQDHHVIEFPTVLLPENVKAGSIIKMQVSQNLEEEKKQRNHFKSIQAKILEKYGTHKPESPVLKIVNVTQTSCVLAWDPLKLGSAKLKSLILYRKGIRSMVIPNPFKVTTTKISGLSVDTPYEFQLKLITTSGTLWSEKVILRTHKMTDMSGITVCLGPLDPLKEISDLQISQCLSHIGARPLQRHVAIDTTHFVCNDLDNEESNEELIRAKHNNIPIVRPEWVRACEVEKRIVGVRGFYLDADQSILKNYTFPPVNEEELSYSKENEPVAEVADENKMPEDTTDVEQVASPNDNESNPSEAKEQGEKSGHETAPVSPVEDPLHASTALENETTIETVNPSVRSLKSEPVGTPNIEENKADSSAEAVVEEPNEAVAESSPNEEATGQKSEDTDTHSNEQADNGFVQTEEVAENNITTESAGENNEPADDAAMEFGRPEAEIETPEVNESIEDANEPAEDSNEPVEDSNKPVKDSNKPVEDSNKPVEDSNKPVEDSNKPVEDANEPVEDTSEPVEDAGEPVQETNEFTTDIASPRHQEEDIELEAEPKDATESVAVEPSNEDVKPEEKGSEAEDDINNVSKEAASGESTTHQKTEASASLESSAVTEEQETTEAEVNTDDVLSTKEAKKNTGNSNSNKKKNKKNKKKGKKK
The following text describes a protein:
Function:
Antimicrobial peptide. Active against a variety of Gram-negative and Gram-positive bacterial strains. Active against fungus C.glabrata 090902 but not against C.albicans ATCC 10231. Shows hemolytic activity against human erythrocytes.
Subcellular Localization:
Secreted.
Sequence:
MFTLKKPLLLLVFLGMISLSLCQDERGADEDDGGEMTEEEKRGAFGNLLKGVAKKAGLKILSIAQCKLSGTC
The following text describes a protein:
Function:
Catalyzes the conversion of 3-deoxy-D-arabino-heptulosonate 7-phosphate (DAHP) to dehydroquinate (DHQ).
Subcellular Localization:
Cytoplasm.
Sequence:
MAQQIQVDLGERSYPIYIGQSLMSDSETLSRYLLKKRILIVTNETVAPLYLKQVQDTMASFGEISSVILSDGEQFKDLTHLDSIFTALLQRNYGRDSVLVALGGGVIGDMTGFAAACYQRGIDFIQIPTTLLSQVDSSVGGKTAVNHPLGKNMIGAFYQPQIVIIDTECLQTLPAREFAAGMAEVIKYGIMWDADFFQWLENNVQALKSLDTQALVYAISRCCEIKADVVSQDETEQGVRALLNLGHTFGHAIEAEMGYGNWLHGEAVAAGTVLAAQTAKSLGLIDESIVCRIVQLLQAFDLPVKAPESMDFESFIQHMRRDKKVLGGQIRLVLPTAIGRAEVFSQVPESTLEQVICCA