ids stringlengths 6 10 | seqs stringlengths 11 1.02k | texts stringlengths 108 11.1k |
|---|---|---|
Q1Q0T3 | MAREMRLGGKERMKTGVVKIGLVAALGVVGLISAGGVYAGQPRVISTIQTGATWEPLGREEPLTVPEVHFRVKHSPFKSELVRYGQFQFNDAAWSLQGSYSCASCHYERGQTTGLIWDLGDEGWGSWKNTKYIRGGRYLPPFRHEGFTGHPDEIVGATSSLDRVCGRDPGFVFRSENFSPMRLEALICYIRALEFTGSPFRNADGSLTEAQKRGQKIFEDPKVGCLECHPGDPMDPRALFSDAQTHDVGTGRVGVNGFRSTPGKVFNISALEAGEDPYGVESNTPIIGLDLVKEFDTPTLRDIYASGTYFHDGGARTLMD... | Cofactor: Binds two heme c groups per subunit. Heme 1 appears to be in the active site, whereas heme 2 probably functions in electron transfer.
Function: Component of the hydrazine synthase complex that catalyzes the condensation of nitric oxide (NO) with ammonium to form hydrazine . The gamma subunit catalyzes the fir... |
Q13651 | MLPCLVVLLAALLSLRLGSDAHGTELPSPPSVWFEAEFFHHILHWTPIPNQSESTCYEVALLRYGIESWNSISNCSQTLSYDLTAVTLDLYHSNGYRARVRAVDGSRHSNWTVTNTRFSVDEVTLTVGSVNLEIHNGFILGKIQLPRPKMAPANDTYESIFSHFREYEIAIRKVPGNFTFTHKKVKHENFSLLTSGEVGEFCVQVKPSVASRSNKGMWSKEECISLTRQYFTVTNVIIFFAFVLLLSGALAYCLALQLYVRRRKKLPSVLLFKKPSPFIFISQRPSPETQDTIHPLDEEAFLKVSPELKNLDLHGSTDSG... | Function: Cell surface receptor for the cytokine IL10 that participates in IL10-mediated anti-inflammatory functions, limiting excessive tissue disruption caused by inflammation. Upon binding to IL10, induces a conformational change in IL10RB, allowing IL10RB to bind IL10 as well . In turn, the heterotetrameric assembl... |
Q08334 | MAWSLGSWLGGCLLVSALGMVPPPENVRMNSVNFKNILQWESPAFAKGNLTFTAQYLSYRIFQDKCMNTTLTECDFSSLSKYGDHTLRVRAEFADEHSDWVNITFCPVDDTIIGPPGMQVEVLADSLHMRFLAPKIENEYETWTMKNVYNSWTYNVQYWKNGTDEKFQITPQYDFEVLRNLEPWTTYCVQVRGFLPDRNKAGEWSEPVCEQTTHDETVPSWMVAVILMASVFMVCLALLGCFALLWCVYKKTKYAFSPRNSLPQHLKEFLGHPHHNTLLFFSFPLSDENDVFDKLSVIAEDSESGKQNPGDSCSLGTPPG... | Function: Shared cell surface receptor required for the activation of five class 2 cytokines: IL10, IL22, IL26, IL28, and IFNL1. The IFNLR1/IL10RB dimer is a receptor for the cytokine ligands IFNL2 and IFNL3 and mediates their antiviral activity. The ligand/receptor complex stimulate the activation of the JAK/STAT sign... |
Q14626 | MSSSCSGLSRVLVAVATALVSASSPCPQAWGPPGVQYGQPGRSVKLCCPGVTAGDPVSWFRDGEPKLLQGPDSGLGHELVLAQADSTDEGTYICQTLDGALGGTVTLQLGYPPARPVVSCQAADYENFSCTWSPSQISGLPTRYLTSYRKKTVLGADSQRRSPSTGPWPCPQDPLGAARCVVHGAEFWSQYRINVTEVNPLGASTRLLDVSLQSILRPDPPQGLRVESVPGYPRRLRASWTYPASWPCQPHFLLKFRLQYRPAQHPAWSTVEPAGLEEVITDAVAGLPHAVRVSARDFLDAGTWSTWSPEAWGTPSTGTI... | Function: Receptor for interleukin-11 (IL11). The receptor systems for IL6, LIF, OSM, CNTF, IL11 and CT1 can utilize IL6ST for initiating signal transmission. The IL11/IL11RA/IL6ST complex may be involved in the control of proliferation and/or differentiation of skeletogenic progenitor or other mesenchymal cells (Proba... |
Q64385 | MSSSCSGLTRVLVAVATALVSSSSPCPQAWGPPGVQYGQPGRPVMLCCPGVSAGTPVSWFRDGDSRLLQGPDSGLGHRLVLAQVDSPDEGTYVCQTLDGVSGGMVTLKLGFPPARPEVSCQAVDYENFSCTWSPGQVSGLPTRYLTSYRKKTLPGAESQRESPSTGPWPCPQDPLEASRCVVHGAEFWSEYRINVTEVNPLGASTCLLDVRLQSILRPDPPQGLRVESVPGYPRRLHASWTYPASWRRQPHFLLKFRLQYRPAQHPAWSTVEPIGLEEVITDAVAGLPHAVRVSARDFLDAGTWSAWSPEAWGTPSTGPL... | Function: Receptor for interleukin-11. The receptor systems for IL6, LIF, OSM, CNTF, IL11 and CT1 can utilize IL6ST for initiating signal transmission. The IL11/IL11RA/IL6ST complex may be involved in the control of proliferation and/or differentiation of skeletogenic progenitor or other mesenchymal cells. Essential fo... |
Q5RF19 | MSSSCSGLSRVLVAVATALVSASSPCPQAWGPPGVQYGQPGRSVKLCCPGVTAGDPVSWFRDGEPKLLQGPDSGLGHELVLAQADSTDEGTYICRTLDGALGGTVTLQLGYPPARPVVSCQAADYENFSCTWSPSQISGLPTRYLTSYRKKTVLGADSQRRSPSTGPWPCPQDPLGAARCVVHGAEFWSQYRINVTEVNPLGASTRLLDVSLQSILRPDPPQGLRVESVPGYPRRLRASWTYPASWPRQPHFLLKFRLQYRPAQHPAWSTVEPAGLEEVITDAVAGLPHAVRVSARDFLDAGTWSTWSPEAWGTPSTGTV... | Function: Receptor for interleukin-11 (IL11). The receptor systems for IL6, LIF, OSM, CNTF, IL11 and CT1 can utilize IL6ST for initiating signal transmission. The IL11/IL11RA/IL6ST complex may be involved in the control of proliferation and/or differentiation of skeletogenic progenitor or other mesenchymal cells. Essen... |
P42701 | MEPLVTWVVPLLFLFLLSRQGAACRTSECCFQDPPYPDADSGSASGPRDLRCYRISSDRYECSWQYEGPTAGVSHFLRCCLSSGRCCYFAAGSATRLQFSDQAGVSVLYTVTLWVESWARNQTEKSPEVTLQLYNSVKYEPPLGDIKVSKLAGQLRMEWETPDNQVGAEVQFRHRTPSSPWKLGDCGPQDDDTESCLCPLEMNVAQEFQLRRRQLGSQGSSWSKWSSPVCVPPENPPQPQVRFSVEQLGQDGRRRLTLKEQPTQLELPEGCQGLAPGTEVTYRLQLHMLSCPCKAKATRTLHLGKMPYLSGAAYNVAVIS... | Function: Functions as an interleukin receptor which binds interleukin-12 with low affinity and is involved in IL12 transduction. Associated with IL12RB2 it forms a functional, high affinity receptor for IL12. Associates also with IL23R to form the interleukin-23 receptor which functions in IL23 signal transduction pro... |
Q60837 | MDMMGLAGTSKHITFLLLCQLGASGPGDGCCVEKTSFPEGASGSPLGPRNLSCYRVSKTDYECSWQYDGPEDNVSHVLWCCFVPPNHTHTGQERCRYFSSGPDRTVQFWEQDGIPVLSKVNFWVESRLGNRTMKSQKISQYLYNWTKTTPPLGHIKVSQSHRQLRMDWNVSEEAGAEVQFRRRMPTTNWTLGDCGPQVNSGSGVLGDIRGSMSESCLCPSENMAQEIQIRRRRRLSSGAPGGPWSDWSMPVCVPPEVLPQAKIKFLVEPLNQGGRRRLTMQGQSPQLAVPEGCRGRPGAQVKKHLVLVRMLSCRCQAQTS... | Function: Functions as an interleukin receptor which binds interleukin-12 with low affinity and is involved in IL12 transduction. Associated with IL12RB2 it forms a functional, high affinity receptor for IL12. Associates also with IL23R to form the interleukin-23 receptor which functions in IL23 signal transduction pro... |
Q5P5Z3 | MKRRTVLSMEQALSMPYATLRFAQLGWRVIRLESTPSRGGLPGDPNRYIGANVVDDDRRTYFIAPNVGKEAIAINLKEPDGQALLRRLLVELDVDVFCCNTVPRRYEQLGIDYETLSRTKPDLIWAGISAMGPDYPDAPGYDPVLQAMAGYMELTGDADGPPTLAGVPIVDLKAGDEVFANVMLALLERAETGKGSRIDVSMLQAAASWLITTLPLLDFDCQPAEITRCGNAHRKFIPTNVYPTADGFIYMAIGSDVQWRRLTEIPKFASLGAAPRATNEGRHKERDAIHRDMAAVTTRFATAEIAADFRDATIPHAPIH... | Function: Involved in degradation of indoleacetate, the most common member of the auxin class of plant hormones . CoA-transferase that catalyzes the succinyl-CoA-dependent activation of phenylsuccinate to phenylsuccinyl-CoA . Acts as a rather unspecific CoA-transferase that shows a broad substrate specificity for C4-di... |
P18204 | MTAYDMEKEWSRISITAAKIHQNNDFEGFTYQDFRTHVPIMDKDGFAAQTERCLERNERNCLIGFTSGTSGNIKRCYYYYDCEVDEDSSLSNVFRSNGFILPGDRCANLFTINLFSALNNTITMMAGNCGAHVVSVGDITLVTKSHFEALNSIKLNVLLGVPSTILQFINAMQHNGVHINIEKVVFTGESLKTFQKKIIRQAFGEQVSIVGVYGSSEGGILGFTNSPCHTEYEFLSDKYFIEKEGDSILITSLTRENFTPLLRYRLGDTATLSMKGDKLYLTDIQREDMSFNFMGNLIGLGIIQQTIKQTLGRSLEIQVH... | Function: Conversion of IAA to IAA-lysine.
Catalytic Activity: (indol-3-yl)acetate + ATP + L-lysine = ADP + H(+) + N(6)-[(indole-3-yl)acetyl]-L-lysine + phosphate
Sequence Mass (Da): 44624
Sequence Length: 395
EC: 6.3.2.20
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P16969 | MASDHRRFVLSGAVLLSVLAVAAATLESVKDECQLGVDFPHNPLATCHTYVIKRVCGRGPSRPMLVKERCCRELAAVPDHCRCEALRILMDGVRTPEGRVVEGRLGDRRDCPREEQRAFAATLVTAAECNLSSVQAPGVRLVLLADG | Function: Alpha-amylase/trypsin inhibitor.
PTM: Five disulfide bonds, which are essential for the inhibitor activity, are probably present.
Sequence Mass (Da): 15965
Sequence Length: 147
Subcellular Location: Secreted
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P83048 | SEDCTPWTATPITVLAGCRDYVGEQ | Function: Inhibits alpha-amylases but not trypsin. Is more effective against insect alpha-amylases than those of mammals.
PTM: May exist both in a glycosylated and in an unglycosylated form.
Sequence Mass (Da): 2713
Sequence Length: 25
Subcellular Location: Secreted
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P94531 | MKKARMIVDKEYKIGEVDKRIYGSFIEHMGRAVYEGIYEPDHPEADEDGFRKDVQSLIKELQVPIIRYPGGNFLSGYNWEDGVGPVENRPRRLDLAWQTTETNEVGTNEFLSWAKKVNTEVNMAVNLGTRGIDAARNLVEYCNHPKGSYWSDLRRSHGYEQPYGIKTWCLGNEMDGPWQIGHKTADEYGRLAAETAKVMKWVDPSIELVACGSSNSGMPTFIDWEAKVLEHTYEHVDYISLHTYYGNRDNNLPNYLARSMDLDHFIKSVAATCDYVKAKTRSKKTINLSLDEWNVWYHSNEADKKVEPWITARPILEDIY... | Function: Involved in the degradation of arabinan and is a key enzyme in the complete degradation of the plant cell wall. Catalyzes the cleavage of terminal alpha-(1->5)-arabinofuranosyl bonds in different hemicellulosic homopolysaccharides (branched and debranched arabinans). It acts preferentially on arabinotriose, a... |
P94552 | MSEHQAVIQTDIAKGTINKNIYGHFAEHLGRGIYEGIWVGTDSDIPNINGIRKDVLEALKQLHIPVLRWPGGCFADEYHWANGVGDRKTMLNTHWGGTIESNEFGTHEFMMLCELLECEPYICGNVGSGTVQEMSEWIEYMTFEEGTPMSDWRKQNGREEPWKLKYFGVGNENWGCGGNMHPEYYADLYRRFQTYVRNYSGNDIYKIAGGANVDDFNWTDVLMKKAAGLMDGLSLHYYTIPGDFWKGKGSATEFTEDEWFITMKKAKYIDELIQKHGTIMDRYDPEQRVGLIIDEWGTWFDPEPGTNPGFLYQQNTIRDA... | Function: Involved in the degradation of arabinan and is a key enzyme in the complete degradation of the plant cell wall. Catalyzes the cleavage of terminal alpha-L-arabinofuranosyl residues in different hemicellulosic homopolysaccharides (branched and debranched arabinans) and heteropolysaccharides (arabinoxylans). It... |
Q59219 | MKAKLLVSTAFLAASVSLSAQKSATITVHADQGKEIIPKEIYGQFAEHLGSCIYGGLWVGENSDIPNIKGYRTDVFNALKDLSVPVLRWPGGCFADEYHWMDGIGPKENRPKMVNNNWGGTIEDNSFGTHEFLNLCEMLGCEPYVSGNVGSGTVEELAKWVEYMTSDGDSPMANLRRKNGRDKAWKLKYLGVGNESWGCGGSMRPEYYADLYRRYSTYCRNYDGNRLFKIASGASDYDYKWTDVLMNRVGHRMDGLSLHYYTVTGWSGSKGSATQFNKDDYYWTMGKCLEVEDVLKKHCTIMDKYDKDKKIALLLDEWGT... | Function: Involved in the degradation of arabinan and is a key enzyme in the complete degradation of the plant cell wall. Catalyzes the cleavage of terminal alpha-L-arabinofuranosyl residues in different hemicellulosic homopolysaccharides (branched and debranched arabinans) and heteropolysaccharides (arabinoxylans) (By... |
Q841V6 | MTTHNSQYSAETTHPDKQESSPAPTAAGTTASNVSTTGNATTPDASIALNADATPVADVPPRLFGSFVEHLGRCVYGGIYEPSHPTADENGFRQDVLDLVKELGVTCVRYPGGNFVSNYNWEDGIGPRENRPMRRDLAWHCTETNEMGIDDFYRWSQKAGTEIMLAVNMGTRGLKAALDELEYVNGAPGTAWADQRVANGIEEPMDIKMWCIGNEMDGPWQVGHMSPEEYAGAVDKVAHAMKLAESGLELVACGSSGAYMPTFGTWEKTVLTKAYENLDFVSCHAYYFDRGHKTRAAASMQDFLASSEDMTKFIATVSDA... | Function: Involved in the degradation of arabinan and is a key enzyme in the complete degradation of the plant cell wall. Catalyzes the cleavage of terminal alpha-(1->5)-arabinofuranosyl bonds in different hemicellulosic homopolysaccharides (branched and debranched arabinans). It is active with sugar beet arabinan and ... |
H7FWB6 | MKILKRIPVLAVLLVGLMTNCSNDSDSSSLSVANSTYETTALNSQKSSTDQPNSGSKSGQTLDLVNLGVAANFAILSKTGITDVYKSAITGDVGASPITGAAILLKCDEVTGTIFSVDAAGPACKITDASRLTTAVGDMQIAYDNAAGRLNPDFLNLGAGTIGGKTLTPGLYKWTSTLNIPTDITISGSSTDVWIFQVAGNLNMSSAVRITLAGGAQAKNIFWQTAGAVTLGSTSHFEGNILSQTGINMKTAASINGRMMAQTAVTLQMNTVTIPQ | Function: Has antifreeze activity for survival in a subzero environment. Binds to the surface of ice crystals and inhibits their growth. Has high thermal hysteresis (TH) activity, which is the ability to lower the freezing point of an aqueous solution below its melting point, and thus the freezing of the cell fluid can... |
C7F6X3 | MSLLSIITIGLAGLGGLVNGQRDLSVELGVASNFAILAKAGISSVPDSAILGDIGVSPAAATYITGFGLTQDSSTTYATSPQVTGLIYAADYSTPTPNYLAAAVANAETAYNQAAGFVDPDFLELGAGELRDQTLVPGLYKWTSSVSVPTDLTFEGNGDATWVFQIAGGLSLADGVAFTLAGGANSTNIAFQVGDDVTVGKGAHFEGVLLAKRFVTLQTGSSLNGRVLSQTEVALQKATVNSPFVPAPEVVQKRSNARQWL | Function: Confers freeze tolerance. Binds to the surface of ice crystals and inhibits their growth. Has low thermal hysteresis (TH) activity, which is the ability to lower the freezing point of an aqueous solution below its melting point . The TH activity of this protein is approximately 0.2 degrees Celsius at 50 uM an... |
A0A7D5JNZ7 | MLKINRKYAIILAIVAFSSFQTEAKAASISMLGTASNFGVLGGSTVTNTGPSVITESLGVSTGSSATGFPPAIVNGTIFTSDTVAAQAQVDNATAYNKLASLIPNKDLTGLDLGGLTLTPGVYSFSSSAQLTGILTLDNLGDPNALFVFQIGSTLTTASNSSIVTTNGDAPNVFFQIGSSATLGTGTQFMGNILALTSITLTTGVNIDCGRALAQNGAVTMDTNKVSNACYTKPQEKAVVPEPDSSLAVLGSGLVSLLFAFRKRFRKGW | Function: A probable ice-binding protein that has ice-structuring activities in vitro. Thought not to anchor the cyanobacterium to ice surfaces, as its habitat is shallow puddles fed by glacier meltwater.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 27596
Sequence Length: 269
Domain: The ice-bind... |
Q8RWZ3 | MGSSTGDLVTRIQSAHRFDHDALFRFAADNVSGFPTNPSQFKVSQFGHGQSNPTFLIEVGSGSSLKRYVLRKKPPGKLLQSAHAVDREFQVLRALGEHTQVPVPKVFCLCTDPAVIGTAFYIMEFMEGRIFIDPKLPNVAPERRNAIYRATAKALASLHSADVDAIGLEKYGRRGNYCKRQIDRWFKQYLASTSEGKPERNPKMFELVDWLRKNIPAEDSTGATSGLVHGDFRIDNLVFHPSEDRVIGIIDWELSTLGNQMCDVAYSCMHYIVNVQLDKEHVSEGFETTGLPEGMLSMPEFLLEYCSASGKPWPAANWKF... | Function: Involved with IBR1 and IBR10 in the peroxisomal beta-oxidation of indole-3-butyric acid (IBA) to form indole-3-acetic acid (IAA), a biologically active auxin . May be responsible for catalyzing the first step in IBA-CoA beta-oxidation . May play a role in defense response to pathogenic bacteria .
Catalytic Ac... |
Q84JU4 | MRKRERENPCSICGHYHKYEEGEVCGVCGHCMPVSSDTVAPQQVHVSAFPSEILPEFLYLGSYDNASRSELLKTQGISRVLNTVPMCQNLYRNSFTYHGLDNEKVLQFDDAIKFLDQCEKDKARVLVHCMSGKSRSPAVVVAYLMKRKGWRLAESHQWVKQRRPSTDISPEFYQQLQEFEQGIFGSEMMSAMNINDAPTFGFGFPKIDNQAQAPVFNNAPTSSIFSSPASSIPPQEFTFGATPPKPTTGGDIAMDGS | Function: Required for the transduction of auxin and abscisic acid (ABA) signaling pathways. Dephosphorylates and inactivates the MAP kinase MPK12.
Catalytic Activity: H2O + O-phospho-L-tyrosyl-[protein] = L-tyrosyl-[protein] + phosphate
Sequence Mass (Da): 28690
Sequence Length: 257
Subcellular Location: Nucleus
EC: 3... |
C1P616 | MMKLVIILIVLLLVSFAAY | Function: Toxic component of a type I toxin-antitoxin (TA) system.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 2151
Sequence Length: 19
Subcellular Location: Membrane
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P09255 | MFCTSPATRGDSSESKPGASVDVNGKMEYGSAPGPLNGRDTSRGPGAFCTPGWEIHPARLVEDINRVFLCIAQSSGRVTRDSRRLRRICLDFYLMGRTRQRPTLACWEELLQLQPTQTQCLRATLMEVSHRPPRGEDGFIEAPNVPLHRSALECDVSDDGGEDDSDDDGSTPSDVIEFRDSDAESSDGEDFIVEEESEESTDSCEPDGVPGDCYRDGDGCNTPSPKRPQRAIERYAGAETAEYTAAKALTALGEGGVDWKRRRHEAPRRHDIPPPHGV | Function: Immediate early (EI) protein that functions as a transcriptional regulator of cellular and viral mRNAs mainly by interacting with several general transcription factors thereby disorganizing the preinitiation complex at certain promoters. May additionally help to regulate levels of histones in virus-infected c... |
Q04360 | MVPSQRLSRTSSISSNEDPAESHILELEAVSDTNTDCDLDPMEGSEEHSTDGEISSSEEEDEDPTPAHAIPARPSSVVITPTSASFVIPRKKWDLQDKTVTLHRSPLCRDEDEKEETGNSSYTRGHKRRRGEVHGCTDESYGKRRHLPPGARAPRAPRAPRVPRAPRSPRAPRSNRATRGPRSESRGAGRSTRKQARQERSQRPLPNKPWFDMSLVKPVSKITFVTLPSPLASLTLEPIQDPFLQSMLAVAAHPEIGAWQKVQPRHELRRSYKTLREFFTKSTNKDTWLDARMQAIQNAGLCTLVAMLEETIFWLQEITY... | Function: Promotes the nuclear export of a subset of early and late viral mRNAs by interacting with mRNAs and cellular export proteins. Additionally may prevent the establishment of cellular antiviral state, by acting as an alternative splicing factor for cellular RNAs such as STAT1, resulting in a STAT1 mRNA incapable... |
Q05906 | MALSSVSSCEPMEDEMSIMGSDTEDNFTGGDTCAEATRGLVNKSAFVPTQTVGTVSALRNVVGNPPKSVVVSFSASPQRAQPSNPKSERPAFGHGRRNRRRPFRRNNWKQQQRGWEKPEPENVPARQSAGSWPKRSSLPVHMRLGQRGGDSSSADSGHGGAGPSDRWRFKTRTQSVARVHRNRRRGNANHGSNTPGRSAGDRLNAAAARSIADVCRRVTSSRIGEMFHGARETLTTPVKNGGFRAENSSPWAPVLGFGSDQFNPEARRITWDTLVEHGVNLYKLFEVRSHAAEAARSLRDAVMRGENLLEALASADETLS... | Function: Multifunctional regulator of the expression of viral genes that mediates nuclear export of viral intronless mRNAs. This immediate early (EI) protein promotes the nuclear export of viral intronless mRNAs by interacting with mRNAs and host NXF1/TAP (By similarity).
Sequence Mass (Da): 51389
Sequence Length: 470... |
P16749 | MELHSRGRHDAPSLSSLSERERRARRARRFCLDYEPVPRKFRRERSPTSPSTRNGAAASEHHLAEDTVGAASHHHRPCVPARRPRYSKDDDTEGDPDHYPPPLPPSSRHALGGTGGHIIMGTAGFRGGHRASSSFKRRVAASASVPLNPHYGKSYDNDDGEPHHHGGDSTHLRRRVPSCPTTFGSSHPSSANNHHGSSAGPQQQQMLALIDDELDAMDEDELQQLSRLIEKKKRARLQRGAASSGTSPSSTSPVYDLQRYTAESLRLAPYPADLKVPTAFPQDHQPRGRILLSHDELMHTDYLLHIRQQFDWLEEPLLRK... | Function: Immediate early (EI) protein that plays many roles during productive infection including regulation of host cell cycle progression, regulation of viral gene expression or nuclear export of intronless viral RNAs. Acts as a transcriptional transactivator via interaction with the cellular transcription elongatio... |
P10238 | MATDIDMLIDLGLDLSDSDLDEDPPEPAESRRDDLESDSSGECSSSDEDMEDPHGEDGPEPILDAARPAVRPSRPEDPGVPSTQTPRPTERQGPNDPQPAPHSVWSRLGARRPSCSPEQHGGKVARLQPPPTKAQPARGGRRGRRRGRGRGGPGAADGLSDPRRRAPRTNRNPGGPRPGAGWTDGPGAPHGEAWRGSEQPDPPGGQRTRGVRQAPPPLMTLAIAPPPADPRAPAPERKAPAADTIDATTRLVLRSISERAAVDRISESFGRSAQVMHDPFGGQPFPAANSPWAPVLAGQGGPFDAETRRVSWETLVAHGP... | Function: Multifunctional regulator of the expression of viral genes that contributes to the shutoff of host protein synthesis and mediates nuclear export of viral intronless mRNAs. Early in infection, this immediate early (EI) protein mediates the inhibition of cellular splicing. This results in the accumulation of un... |
Q2HR75 | MVQAMIDMDIMKGILEDSVSSSEFDESRDDETDAPTLEDEQLSEPAEPPADERIRGTQSAQGIPPPLGRIPKKSQGRSQLRSEIQFCSPLSRPRSPSPVNRYGKKIKFGTAGQNTRPPPEKRPRRRPRDRLQYGRTTRGGQCRAAPKRATRRPQVNCQRQDDDVRQGVSDAVKKLRLPASMIIDGESPRFDDSIIPRHHGACFNVFIPAPPSHVPEVFTDRDITALIRAGGKDDELINKKISAKKIDHLHRQMLSFVTSRHNQAYWVSCRRETAAAGGLQTLGAFVEEQMTWAQTVVRHGGWFDEKDIDIILDTAIFVCN... | Function: Early protein that promotes the accumulation and nuclear export of viral intronless RNA transcripts by interacting with mRNAs and cellular export proteins. Probably acts as a viral splicing factor that regulates viral RNA splicing. Functions as a multifunctional regulator of the expression of viral lytic gene... |
Q9USP8 | MSMLSTLRTAGSLRTFSRSACYSFQRFSSTKAAAGTYEGVKNANGNYTVTMIAGDGIGPEIAQSVERIFKAAKVPIEWERVKVYPILKNGTTTIPDDAKESVRKNKVALKGPLATPIGKGHVSMNLTLRRTFGLFANVRPCVSITGYKTPYDNVNTVLIRENTEGEYSGIEHEVIPGVVQSIKLITRAASERVIRYAFQYARQTGKNNITVVHKATIMRMADGLFLECAKELAPEYPDIELREEILDNACLKIVTDPVPYNNTVMVMPNLYGDIVSDMCAGLIGGLGLTPSGNIGNQASIFEAVHGTAPDIAGKGLANPT... | Cofactor: Binds 1 Mg(2+) or Mn(2+) ion per subunit.
Function: Performs an essential role in the oxidative function of the citric acid cycle and is involved in glutamate biosynthesis . Also binds RNA; specifically to the 5'-untranslated leaders of mitochondrial mRNAs .
Catalytic Activity: D-threo-isocitrate + NAD(+) = 2... |
P28241 | MLRNTFFRNTSRRFLATVKQPSIGRYTGKPNPSTGKYTVSFIEGDGIGPEISKSVKKIFSAANVPIEWESCDVSPIFVNGLTTIPDPAVQSITKNLVALKGPLATPIGKGHRSLNLTLRKTFGLFANVRPAKSIEGFKTTYENVDLVLIRENTEGEYSGIEHIVCPGVVQSIKLITRDASERVIRYAFEYARAIGRPRVIVVHKSTIQRLADGLFVNVAKELSKEYPDLTLETELIDNSVLKVVTNPSAYTDAVSVCPNLYGDILSDLNSGLSAGSLGLTPSANIGHKISIFEAVHGSAPDIAGQDKANPTALLLSSVMM... | Cofactor: Binds 1 Mg(2+) or Mn(2+) ion per subunit.
Function: Performs an essential role in the oxidative function of the citric acid cycle. Also binds RNA; specifically to the 5'-untranslated leaders of mitochondrial mRNAs.
Catalytic Activity: D-threo-isocitrate + NAD(+) = 2-oxoglutarate + CO2 + NADH
Sequence Mass (Da... |
Q93714 | MLGKCIKKASSTVGQSIRYSSGDVRRVTLIPGDGIGPEISASVQKIFEAADAPIAWDPVDVTPVKGRDGVFRIPSRCIELMHANKVGLKGPLETPIGKGHRSLNLAVRKEFSLYANVRPCRSLEGHKTLYDNVDVVTIRENTEGEYSGIEHEIVPGVVQSIKLITETASRNVASFAFEYARQNGRKVVTAVHKANIMRQSDGLFLSICREQAALYPDIKFKEAYLDTVCLNMVQDPSQYDVLVMPNLYGDILSDLCAGLVGGLGVTPSGNIGKGAAVFESVHGTAPDIAGQDKANPTALLLSAVMMLRYMNLPQHAARIE... | Cofactor: Binds 1 Mg(2+) or Mn(2+) ion per subunit.
Catalytic Activity: D-threo-isocitrate + NAD(+) = 2-oxoglutarate + CO2 + NADH
Sequence Mass (Da): 38466
Sequence Length: 358
Subcellular Location: Mitochondrion
EC: 1.1.1.41
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P54836 | AIEVQTVTLIPGD | Function: Catalytic subunit of the enzyme which catalyzes the decarboxylation of isocitrate (ICT) into alpha-ketoglutarate. The heterodimer composed of the alpha (IDH3A) and beta (IDH3B) subunits and the heterodimer composed of the alpha (IDH3A) and gamma (IDH3G) subunits, have considerable basal activity but the full ... |
Q9VWH4 | MAARFIQKILNQLGLIAARDAPAVTATPAVSQVNATPAASRSYSSGTKKVTLIPGDGIGPEISAAVQKIFTAANVPIEWEAVDVTPVRGPDGKFGIPQAAIDSVNTNKIGLKGPLMTPVGKGHRSLNLALRKEFNLYANVRPCRSLEGYKTLYDDVDVVTIRENTEGEYSGIEHEIVDGVVQSIKLITEEASKRVAEYAFQYAKNNNRKKVTVVHKANIMRMSDGLFLRCVRDMAQKFPEIQFEEKYLDTVCLNMVQNPGKYDVLVMPNLYGDILSDMCAGLVGGLGLTPSGNMGLNGALFESVHGTAPDIAGKDLANPT... | Cofactor: Binds 1 Mg(2+) or Mn(2+) ion per subunit.
Function: Probable catalytic subunit of the enzyme which catalyzes the decarboxylation of isocitrate (ICT) into alpha-ketoglutarate.
Catalytic Activity: D-threo-isocitrate + NAD(+) = 2-oxoglutarate + CO2 + NADH
Sequence Mass (Da): 40844
Sequence Length: 377
Subcellula... |
P50213 | MAGPAWISKVSRLLGAFHNPKQVTRGFTGGVQTVTLIPGDGIGPEISAAVMKIFDAAKAPIQWEERNVTAIQGPGGKWMIPSEAKESMDKNKMGLKGPLKTPIAAGHPSMNLLLRKTFDLYANVRPCVSIEGYKTPYTDVNIVTIRENTEGEYSGIEHVIVDGVVQSIKLITEGASKRIAEFAFEYARNNHRSNVTAVHKANIMRMSDGLFLQKCREVAESCKDIKFNEMYLDTVCLNMVQDPSQFDVLVMPNLYGDILSDLCAGLIGGLGVTPSGNIGANGVAIFESVHGTAPDIAGKDMANPTALLLSAVMMLRHMGL... | Cofactor: Divalent metal cations; Mn(2+) or Mg(2+). Activity higher in presence of Mn(2+) than of Mg(2+). Binds 1 Mg(2+) or Mn(2+) ion per subunit.
Function: Catalytic subunit of the enzyme which catalyzes the decarboxylation of isocitrate (ICT) into alpha-ketoglutarate. The heterodimer composed of the alpha (IDH3A) an... |
P86225 | MRPGVAAVAAVRIFDAAKAPIQWEERNVTAIQGPGGKWMIPPEAKGPLKTPIAAGHPSMNLLLRKTFDLYANVRPCVSIEGYKTPYTDVNIVTIRRIAEFAFEYARDMANPTALLLSAVMMLRCSDFTEEICRR | Cofactor: Divalent metal cations; Mn(2+) or Mg(2+). Activity higher in presence of Mn(2+) than of Mg(2+). Binds 1 Mg(2+) or Mn(2+) ion per subunit.
Function: Catalytic subunit of the enzyme which catalyzes the decarboxylation of isocitrate (ICT) into alpha-ketoglutarate. The heterodimer composed of the alpha (IDH3A) an... |
Q9D6R2 | MAGSAWVSKVSRLLGAFHNTKQVTRGFAGGVQTVTLIPGDGIGPEISASVMKIFDAAKAPIQWEERNVTAIQGPGGKWMIPPEAKESMDKNKMGLKGPLKTPIAAGHPSMNLLLRKTFDLYANVRPCVSIEGYKTPYTDVNIVTIRENTEGEYSGIEHVIVDGVVQSIKLITEEASKRIAEFAFEYARNNHRSNVTAVHKANIMRMSDGLFLQKCREVAENCKDIKFNEMYLDTVCLNMVQDPSQFDVLVMPNLYGDILSDLCAGLIGGLGVTPSGNIGANGVAIFESVHGTAPDIAGKDMANPTALLLSAVMMLRHMGL... | Cofactor: Divalent metal cations; Mn(2+) or Mg(2+). Activity higher in presence of Mn(2+) than of Mg(2+). Binds 1 Mg(2+) or Mn(2+) ion per subunit.
Function: Catalytic subunit of the enzyme which catalyzes the decarboxylation of isocitrate (ICT) into alpha-ketoglutarate. The heterodimer composed of the alpha (IDH3A) an... |
Q5R678 | MAGPAWISKVSRLLGAFHNPKQVTRGFTGGVQTVTLIPGDGIGPEISAAVMKIFDAAKAPIQWEERNVTAIQGPGGKWMIPSEAKESMDKNKMGLKGPLKTPIAAGHPSMNLLLRKTFDLYANVRPCVSIEGYKTPYTDVNIVTIRENTEGEYSGIEHVIVDGVVQSIKLITEGASKRIAEFAFEYARNNHRSNVTAVHKANIMRMSDGLFLQKCREVAENCKDIKFNEMYLDTVCLNMVQDPSQFDVLVMPNLYGDILSDLCAGLIGGLGVTPSGNIGANGVAIFESVHGTAPDIAGKDMANPTALLLSAVMMLRHMGL... | Cofactor: Divalent metal cations; Mn(2+) or Mg(2+). Activity higher in presence of Mn(2+) than of Mg(2+). Binds 1 Mg(2+) or Mn(2+) ion per subunit.
Function: Catalytic subunit of the enzyme which catalyzes the decarboxylation of isocitrate (ICT) into alpha-ketoglutarate. The heterodimer composed of the alpha (IDH3A) an... |
Q93353 | MLSRTVSSLSRVAPQTLGAVNAASSRQYSITAPRPPTELNQKLKVTIIPGDGVGPELIYTVQDIVKQTGIPIEFEEIFLSEVHYTRSSSIENAVESIGRNNNVALKGAIEESAVLHTEGELQGLNMRLRRSLDLFANVVHIKTLDGIKTRHGKQLDFVIVREQTEGEYSSLEHELVPGVIECLKISTRTKAERIAKFAFDYATKTGRKKVTAVHKANIMKLGDGLFLRTCEGVAKQYPKIQFESMIIDNTCMQLVSKPEQFDVMVMPNLYGNIIDNLAAGLVGGAGVVPGQSVGRDFVIFEPGSRHSFQEAMGRSIANPT... | Cofactor: Binds 1 Mg(2+) or Mn(2+) ion per subunit.
Catalytic Activity: D-threo-isocitrate + NAD(+) = 2-oxoglutarate + CO2 + NADH
Sequence Mass (Da): 41553
Sequence Length: 379
Subcellular Location: Mitochondrion
EC: 1.1.1.41
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Q92HM7 | MLKDQNLDIERKQDHIEINLTKNVESTLKSGFESIHFIHNALPEINYDSVNTTTTFLGKSLQAPILISSMTGGTTRARDINYRLAQVAQKAGIAMGLGSMRVLLTEPDTIKTFAVRHIAPDIPLLANIGAVQLNYGVTPKECQYLVDAIKADALILHLNVLQELTQPEGNRNWEKLLPKIREVVNYLSIPVIVKEVGYGLSKKVAESLIDAGVKVLDIAGSGGTSWSQVEAYRATNSLQNRIASSFINWGIPTLDSLKMVREVSKDIPIITSGGFKSGIDGAKAIRIGANIFGLAGQFLKAADTSESLLSEEIQLIIEQL... | Function: Involved in the biosynthesis of isoprenoids. Catalyzes the 1,3-allylic rearrangement of the homoallylic substrate isopentenyl (IPP) to its allylic isomer, dimethylallyl diphosphate (DMAPP).
Catalytic Activity: isopentenyl diphosphate = dimethylallyl diphosphate
Sequence Mass (Da): 37336
Sequence Length: 342
S... |
Q9ZD90 | MPKEQNLDIERKQEHIEINLKQNVNSTLKSGLESIKFIHNALPEINYDSIDTTTTFLGKDMKAPILISSMTGGTARARDINYRLAQAAQKSGIAMGLGSMRILLTKPDTIKTFTVRHVAPDIPLLANIGAVQLNYGVTPKECQYLIDTIKADALILHLNVLHELTQPEGNKNWENLLPKIKEVINYLSVPVIVKEVGYGLSKQVAKKLIKAGVKVLDIAGSGGTSWSQVEAYRAKNSMQNRIASSFINWGITTLDSLKMLQEISKDITIIASGGLQSGIDGAKAIRMGANIFGLAGKLLKAADIAESLVLEEIQVIIEQL... | Function: Involved in the biosynthesis of isoprenoids. Catalyzes the 1,3-allylic rearrangement of the homoallylic substrate isopentenyl (IPP) to its allylic isomer, dimethylallyl diphosphate (DMAPP).
Catalytic Activity: isopentenyl diphosphate = dimethylallyl diphosphate
Sequence Mass (Da): 37364
Sequence Length: 342
S... |
P61615 | MPDIVNRKVEHVEIAAFENVDGLSSSTFLNDVILVHQGFPGISFSEINTKTKFFRKEISVPVMVTGMTGGRNELGRINKIIAEVAEKFGIPMGVGSQRVAIEKAEARESFAIVRKVAPTIPIIANLGMPQLVKGYGLKEFQDAIQMIEADAIAVHLNPAQEVFQPEGEPEYQIYALEKLRDISKELSVPIIVKESGNGISMETAKLLYSYGIKNFDTSGQGGTNWIAIEMIRDIRRGNWKAESAKNFLDWGVPTAASIMEVRYSVPDSFLVGSGGIRSGLDAAKAIALGADIAGMALPVLKSAIEGKESLEQFFRKIIFE... | Function: Involved in the biosynthesis of isoprenoids. Catalyzes the 1,3-allylic rearrangement of the homoallylic substrate isopentenyl (IPP) to its allylic isomer, dimethylallyl diphosphate (DMAPP).
Catalytic Activity: isopentenyl diphosphate = dimethylallyl diphosphate
Sequence Mass (Da): 40427
Sequence Length: 368
S... |
Q53479 | MTEVLDILRKYSEVADKRIMECISDITPDTLLKASEHLITAGGKKIRPSLALLSCEAVGGNPEDAAGVAAAIELIHTFSLIHDDIMDDDEMRRGEPSVHVIWGEPMAILAGDVLFSKAFEAVIRNGDSERVKDALAVVVDSCVKICEGQALDMGFEERLDVTEDEYMEMIYKKTAALIAAATKAGAIMGGASEREVEALEDYGKFIGLAFQIHDDYLDVVSDEESLGKPVGSDIAEGKMTLMVVKALEEASEEDRERLISILGSGDEGSVAEAIEIFERYGATQYAHEVALDYVRMAKERLEILEDSDARDALMRIADFV... | Cofactor: Binds 2 Mg(2+) ions per subunit.
Sequence Mass (Da): 35636
Sequence Length: 325
Subcellular Location: Cytoplasm
EC: 2.5.1.-
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P22304 | MPPPRTGRGLLWLGLVLSSVCVALGSETQANSTTDALNVLLIIVDDLRPSLGCYGDKLVRSPNIDQLASHSLLFQNAFAQQAVCAPSRVSFLTGRRPDTTRLYDFNSYWRVHAGNFSTIPQYFKENGYVTMSVGKVFHPGISSNHTDDSPYSWSFPPYHPSSEKYENTKTCRGPDGELHANLLCPVDVLDVPEGTLPDKQSTEQAIQLLEKMKTSASPFFLAVGYHKPHIPFRYPKEFQKLYPLENITLAPDPEVPDGLPPVAYNPWMDIRQREDVQALNISVPYGPIPVDFQRKIRQSYFASVSYLDTQVGRLLSALDD... | Cofactor: Binds 1 Ca(2+) ion per subunit.
Function: Lysosomal enzyme involved in the degradation pathway of dermatan sulfate and heparan sulfate.
PTM: Synthesized as a 75-kDa precursor form in the endoplasmic reticulum (ER), and then processed by proteolytic cleavage through various intermediates to yield a 55-kDa matu... |
Q08890 | MSPPPPPPIWRQLSFSLLLGSFCIALESAAQGNSATDALNILLIIVDDLRPSLGCYGDKLVRSPNIDQLASHSVLFQNAFAQQAVCAPSRVSFLTGRRPDTTRLYDFNSYWRVHSGNFSTIPQYFKENGYVTMSVGKVFHPGISSNHSDDYPYSWSFPPYHPSSEKYENTKTCKGQDGKLHANLLCPVDVADVPEGTLPDKQSTEEAIRLLEKMKTSASPFFLAVGYHKPHIPFRYPKEFQKLYPLENITLAPDPHVPDSLPPVAYNPWMDIREREDVQALNISVPYGPIPEDFQRKIRQSYFASVSYLDTQVGHVLSAL... | Cofactor: Binds 1 Ca(2+) ion per subunit.
Function: Lysosomal enzyme involved in the degradation pathway of dermatan sulfate and heparan sulfate.
PTM: Synthesized as a 75-kDa precursor form in the endoplasmic reticulum (ER), and then processed by proteolytic cleavage through various intermediates to yield a 55-kDa matu... |
J7FIJ6 | MDGFSILHEPPAAYKEVKWMADTFVAGMGLGWIVNYALMIRFSWKGRPHCMALLPLCNNIAWELTYTIVYPSANRVELLVFAIGLTLNFFIMVGARRSARVEWRHSPLLSEHAGFILLVGTLLCFTGHVALAMEIGPGLAYSWGAVVCQLALSIGGLFQLLQRNSTAGTSWTLWSSRFLGSCCTVAFAGLRCKYWPEVFGWLASPLVLWSLVTFLLADSAYGFCLYRVSHAETKARKKH | Function: Terpene cyclase; part of the gene cluster that mediates the biosynthesis of paspalitrems, indole-diterpene (IDT) mycotoxins that are potent tremorgens in mammals . The geranylgeranyl diphosphate (GGPP) synthase idtG is proposed to catalyze the first step in IDT biosynthesis via catalysis of a series of iterat... |
J7FJH2 | MTTLAWFAGRSMVLDLAALTSAFTVGYLLKSTSTPTSTPTSTDKAGTPPGSTIHHYGYPQGSVTKPNNSKTEKENGSPKDSKGNVPDCPYKYLVGLYGHHHFAGFVEALQPTLKDEDPEKYTLVLDIMDAVHLCLILVDDICDDSPKRKNQTTAHLLFGSCETANRAYLVLTKVINRAMRTRPVLGAELVRALELILEGQDLSLVWRRDGLAAFDAEEGGDKVSVYKKMAQLKTGTLFVLLGRLLNDGGAQLDDVLLRLGWYSQLQNDCKNIYSGEYANNKGAIAEDLRNGEMSFPVVVALGDQTTSSQIRKAFGSHSDG... | Cofactor: Binds 3 Mg(2+) ions per subunit.
Function: Prenyltransferase; part of the gene cluster that mediates the biosynthesis of paspalitrems, indole-diterpene (IDT) mycotoxins that are potent tremorgens in mammals . The geranylgeranyl diphosphate (GGPP) synthase idtG is proposed to catalyze the first step in IDT bio... |
J7FIP8 | MFLLHILAIGACLLWYFVRSDKRKQGSNIPTIRRWPALFPEFLDRLSYNSCAARLVENGYREHKDRPFRLLKMDMDLVVIPLKYAQEMRALTSDELDPLTAVFDDNVGKVTGILLDSQLHTHAIQRRLTPRLPNIIPAMMDELNYAFQQVIPSEAGERLQTSWVPINPYDMVLELSTRAAARLFVGEPICRDEVFLKTSAAYSRNIFDTIHVSRSLGHIITPYLGSLIPSVRQFHQQFEYIQNLVLGEIAHRKQHSEDNKADDFLQWCMELARTKEESTPTALAQRTVGILSMAVVHTSAMATTHLLFDMISNQELREQL... | Function: Cytochrome P450 monooxygenase; part of the gene cluster that mediates the biosynthesis of paspalitrems, indole-diterpene (IDT) mycotoxins that are potent tremorgens in mammals . The geranylgeranyl diphosphate (GGPP) synthase idtG is proposed to catalyze the first step in IDT biosynthesis via catalysis of a se... |
J7FJH1 | MLTEQFDPSTFYSPKTVAIAGLILGCVLIYVYNDYPTNVNVPVIGVGVRYTKWLAAVRNVFYARDSVAEGYKKANFAFQIPTLNRMEIFICDRKMTREYQNLDSDRMSLDAVVVEEFEFDLLSPGHGHGHRRGPDSVPIPVVAKALAWQRRRTANTNDPFFQEFMAEVSYGFQQEVQRLSQDPRSSTTTPVFTVPCFSFALQVVGRITTFALFGRPMCRDRAFLDLCGKYSDGLPRGAMLLRPWPKWMRPFIAKHMEAPQVLAKLKEIIGAEIERRKASDGESPMENIMDYFVDWAYKGRDTVPADADDTVAHVLANLIF... | Function: Cytochrome P450 monooxygenase; part of the gene cluster that mediates the biosynthesis of paspalitrems, indole-diterpene (IDT) mycotoxins that are potent tremorgens in mammals . The geranylgeranyl diphosphate (GGPP) synthase idtG is proposed to catalyze the first step in IDT biosynthesis via catalysis of a se... |
J7FIP9 | MSRTEASGWGFSLLQILLVLAGMVWKAREGFPIVDFLDTSGDTCSWLNPCIVPPALSCWNNWPWFALHLFLYTTQLVGLSAIILPPVYLIRMLGLSTALPLISLWVLHRRRRTGKGWATTFPPRHGEEAFLWRVLWFTGLAHVASFLVATAASFLGREDMAPWHLTNTLLGTPDCSYLPCSQIAERQARLRQINEMTGTSSGFFLAVALFSQHLEMNGARLGAGLLARLFFVSLIAGPAAGAADALLLRSAFMRTRRST | Function: Part of the gene cluster that mediates the biosynthesis of paspalitrems, indole-diterpene (IDT) mycotoxins that are potent tremorgens in mammals . The geranylgeranyl diphosphate (GGPP) synthase idtG is proposed to catalyze the first step in IDT biosynthesis via catalysis of a series of iterative condensations... |
Q9VKJ8 | MLSLLLVLTTLARIHAHYTSGDVVYHTMPHFWTGVGFCPAGRIDHEGISAALGDPALRLNLRLIAALPVGAVTHIRIHWLLELIQFWQYDPSGIPIYDFSKFDDFIDFLHEELRLSPVLEWMGNLGGVFSENPMQQSFYWEHLVKTTINHQIARHGSSRLVNWRYETWNEPDLRGYNKQNFTAHTFLDYVQAVRRGLSKAGNLDNQDGKVPLPMYRSLRGPAGLFKDSNHPLCWNLLELCSQRVVYCPIDILTFHRKGIEGTATEIVNGSLSLMAKIYEEYPNLKQLPVANDEADPVAGWSTSRDFQADVRYGITLISTV... | Function: Essential lysosomal hydrolase responsible for the degradation of the glycosaminoglycans (GAG) heparan sulfate and dermatan sulfate (Probable). Required for lysosome function and autophagy . Consequently, has an essential role in the development, maintenance and function of various cells, tissues, and organs, ... |
P35475 | MRPLRPRAALLALLASLLAAPPVAPAEAPHLVHVDAARALWPLRRFWRSTGFCPPLPHSQADQYVLSWDQQLNLAYVGAVPHRGIKQVRTHWLLELVTTRGSTGRGLSYNFTHLDGYLDLLRENQLLPGFELMGSASGHFTDFEDKQQVFEWKDLVSSLARRYIGRYGLAHVSKWNFETWNEPDHHDFDNVSMTMQGFLNYYDACSEGLRAASPALRLGGPGDSFHTPPRSPLSWGLLRHCHDGTNFFTGEAGVRLDYISLHRKGARSSISILEQEKVVAQQIRQLFPKFADTPIYNDEADPLVGWSLPQPWRADVTYAA... | PTM: N-glycosylation at Asn-372 contributes to substrate binding and is required for full enzymatic activity.
Catalytic Activity: Hydrolysis of unsulfated alpha-L-iduronosidic linkages in dermatan sulfate.
Sequence Mass (Da): 72670
Sequence Length: 653
Subcellular Location: Lysosome
EC: 3.2.1.76
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P11138 | MTQINFNASYTSASTPSRASFDNSYSEFCDKQPNDYLSYYNHPTPDGADTVISDSETAAASNFLASVNSLTDNDLVECLLKTTDNLEEAVSSAYYSESLEQPVVEQPSPSSAYHAESFEHSAGVNQPSATGTKRKLDEYLDNSQGVVGQFNKIKLRPKYKKSTIQSCATLEQTINHNTNICTVASTQEITHYFTNDFAPYLMRFDDNDYNSNRFSDHMSETGYYMFVVKKSEVKPFEIIFAKYVSNVVYEYTNNYYMVDNRVFVVTFDKIRFMISYNLVKETGIEIPHSQDVCNDETAAQNCKKCHFVDVHHTFKAALTS... | Function: Regulatory transcriptional protein, which trans-activates gene expression from early baculovirus promoters. Can also trans-activate its own promoter, suggesting an autoregulation during infection of host cells. Promotes also viral DNA genome replication via the N-terminal region.
PTM: Phosphorylated.
Sequence... |
Q9NZI8 | MNKLYIGNLNESVTPADLEKVFAEHKISYSGQFLVKSGYAFVDCPDEHWAMKAIETFSGKVELQGKRLEIEHSVPKKQRSRKIQIRNIPPQLRWEVLDSLLAQYGTVENCEQVNTESETAVVNVTYSNREQTRQAIMKLNGHQLENHALKVSYIPDEQIAQGPENGRRGGFGSRGQPRQGSPVAAGAPAKQQQVDIPLRLLVPTQYVGAIIGKEGATIRNITKQTQSKIDVHRKENAGAAEKAISVHSTPEGCSSACKMILEIMHKEAKDTKTADEVPLKILAHNNFVGRLIGKEGRNLKKVEQDTETKITISSLQDLTL... | Function: RNA-binding factor that recruits target transcripts to cytoplasmic protein-RNA complexes (mRNPs). This transcript 'caging' into mRNPs allows mRNA transport and transient storage. It also modulates the rate and location at which target transcripts encounter the translational apparatus and shields them from end... |
Q0GRC4 | MVVEDTPKSIITDDQITTNPNRVIEDDNNLEEGEILDEDDSSATSKPVVHQPHLLENSWTFLFDTPAAKSKQDDWGSSMRPIYTFSTVEEFWSIYNNIHHPGKLAVRADFYCFKHKIEPKWEDPICANGGKWTANYPKGKSDTSWLYTLLAMIGEQFDHGDEICGAVVKVRGRAEKISIWTKNASNEAAQVSIGKQWKEFLDYNETMGFIFHDDARKLDRNAKNKYVV | Function: Component of the protein complex eIF4F, which is involved in the recognition of the mRNA cap, ATP-dependent unwinding of 5'-terminal secondary structure and recruitment of mRNA to the ribosome . Recognizes and binds the 7-methylguanosine-containing mRNA cap during an early step in the initiation of protein sy... |
M1JJT8 | MVVEDALKTSASEDQAKTETNPKPREEDDEPEEGEIVGDEESASKPSKGIAPESHALEHSWTFWFDSPAAKSAKTKQEDWGSSIRPIYTFSTVEEFWSIYNNIRHPSKLAIGTDFHCFKYKIEPKWEDPVCANGGKWTVTLPKGKSDTSWLYTLLGMIGEQFDHGDEICGAVVNVRNRQEKISIWTKNAINEAAQLSIGKQWKGLLDYNETIGFIFHEDAMRHERSAKNKYVV | Function: Component of the protein complex eIF4F, which is involved in the recognition of the mRNA cap, ATP-dependent unwinding of 5'-terminal secondary structure and recruitment of mRNA to the ribosome (By similarity). Recognizes and binds the 7-methylguanosine-containing mRNA cap during an early step in the initiatio... |
Q4VQY3 | MAAAEMERTMSFDAAEKLKAADGGGGEVDDELEEGEIVEESNDTASYLGKEITVKHPLEHSWTFWFDNPTTKSRQTAWGSSLRNVYTFSTVEDFWGAYNNIHHPSKLIMGADFHCFKHKIEPKWEDPVCANGGTWKMSFSKGKSDTSWLYTLLAMIGHQFDHGDEICGAVVSVRAKGEKIALWTKNAANETAQVSIGKQWKQFLDYSDSVGFIFHDDAKRLDRNAKNRYTV | Function: Component of the protein complex eIF4F, which is involved in the recognition of the mRNA cap, ATP-dependent unwinding of 5'-terminal secondary structure and recruitment of mRNA to the ribosome . Recognizes and binds the 7-methylguanosine-containing mRNA cap during an early step in the initiation of protein sy... |
A0A075QQ08 | MVDEVEKPASLEESKTNTREVEEGAEEVIESDDTMSSLGNPCKAMKHPLEHSWTFWFDNPSGKSKQAAWGSSIRPIYTFSTVEDFWSVYNNIHHPSKLAVGADFHCFKNKIEPKWEDPVCASGGKWTMSFSRGKSDTCWLYTLLAMIGEQFDCGDEICGAVINVRVRQEKIALWTRNAANETAQVSIGKQWKEFLDYNDSIGFIFHDDAKKLDRAAKNRYSV | Function: Component of the protein complex eIF4F, which is involved in the recognition of the mRNA cap, ATP-dependent unwinding of 5'-terminal secondary structure and recruitment of mRNA to the ribosome . Recognizes and binds the 7-methylguanosine-containing mRNA cap during an early step in the initiation of protein sy... |
O60573 | MNNKFDALKDDDSGDHDQNEENSTQKDGEKEKTERDKNQSSSKRKAVVPGPAEHPLQYNYTFWYSRRTPGRPTSSQSYEQNIKQIGTFASVEQFWRFYSHMVRPGDLTGHSDFHLFKEGIKPMWEDDANKNGGKWIIRLRKGLASRCWENLILAMLGEQFMVGEEICGAVVSVRFQEDIISIWNKTASDQATTARIRDTLRRVLNLPPNTIMEYKTHTDSIKMPGRLGPQRLLFQNLWKPRLNVP | Function: Recognizes and binds the 7-methylguanosine-containing mRNA cap during an early step in the initiation. Acts as a repressor of translation initiation . In contrast to EIF4E, it is unable to bind eIF4G (EIF4G1, EIF4G2 or EIF4G3), suggesting that it acts by competing with EIF4E and block assembly of eIF4F at the... |
A0A3Q7FGP1 | MADELNKAALEEYKSSSVEDRGEEGEIVGESDDTASSLGKQITMKHPLEHSWTFWFDNPSGKSKQAAWGSSIRPIYTFSTAEDFWSVYNNIHHPSKLAVGADFHCFKNKIEPKWEDPVCANGGKWTMNFSRGKSDTCWLYTLLALIGEQFDYGDEICGAVINVRVRQEKIALWTRNAANETAQVSIGKQWKEFLDYNDTIGFIFHDDAKKLDRAAKNRYSV | Function: Component of the protein complex eIF4F, which is involved in the recognition of the mRNA cap, ATP-dependent unwinding of 5'-terminal secondary structure and recruitment of mRNA to the ribosome (By similarity). Recognizes and binds the 7-methylguanosine-containing mRNA cap during an early step in the initiatio... |
Q5A7R7 | MLLSNLVIPLLATSATVSATFDVTSSLTKYAAFDFGVGDISIQKSASFSLINTFDCAFQGDINIEKDCEFLIASTAKALKLTFNNIFHKIENKGKWIVHTLESAAASTCNIIVKSFVNTGEIILAFKGHVLAPIINIAASHWVNHGCLHLFQEIKSISVAILGVVGGTIENHGTICLTNQLCKQVTKIIGSGCIALEKSSSFFISNSFLSIDAQHTFYLGEGNPTIQAQAVSLPQTFKVANFGANGSHKIGLNLPLLSITIAGKKGWSYDTKTGILTLTANGFISQKFDIGLGYDPSKFEVCTDNSVGIVSVIKGSIKYN... | Function: GPI-anchored cell wall protein involved in cell wall organization, hyphal growth, as well as in host-fungal interaction and virulence.
PTM: O-glycosylated.
Sequence Mass (Da): 53359
Sequence Length: 511
Subcellular Location: Secreted
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Q59XB0 | MLFTLSILSTLLFSTSISAIEITQNRVDHGTITTSIGDITIDSGAYWSIIDNSISTFIGNLDIKSNAGLYISSTISNLPLLVLLNSGSASITNDGIVSLDARTSTQGSSQFNLVGGSFENNGEFYLAASGAIPMTMGLTGKSWNNNGLIVAYQNERSSGSVKFGVIGQTITNKGQICLTNQVYQQTSKIDGSGCVTAKKNASIYISNVLDPQSVSTEQNYFLADDKSSIITQAVGFNTQVINVFGFGNGNKIGLTLPLKSGNGGQAYSYDSDSGVLSLSSGLFGQKFNIGPGYDSKLFSIVTDNSEGIPSVNNGAVSYSG... | Function: GPI-anchored cell wall protein involved in cell wall organization, hyphal growth, as well as in host-fungal interaction and virulence.
PTM: The GPI-anchor is attached to the protein in the endoplasmic reticulum and serves to target the protein to the cell surface. There, the glucosamine-inositol phospholipid ... |
Q5A6U1 | MQLFQNILVSIALLTQIVFAIEITENKVDRGTVTLNLSDITIYPGASWSIIDNAYTSFVGKLDVRDGAGLYISSTSHLLALQVSLTALLHSITNNGVVSFDSRISRTSSSYDLRGVSFTNNGEMYFAASGEFSSPTALTSASWTNTGLLSFYQNQRTSGTVSLGMPLGSITNTGQVCLNNQVYEQTTQIKGSGCFTANGDSTIYISNVLLAVSPKQNFYLTDKGSSMIVQAVSTTQTFNVYGFGEGNKIGLTIPLMGNLWNSAYAYDTTSGILTLRNLLLEQKFNIGTGYDPSKFQVVTDSGSGIPSTILGSVAYYGRVP... | Function: GPI-anchored cell wall protein involved in cell wall organization, hyphal growth, as well as in host-fungal interaction and virulence.
PTM: The GPI-anchor is attached to the protein in the endoplasmic reticulum and serves to target the protein to the cell surface. There, the glucosamine-inositol phospholipid ... |
Q18235 | MEDLNFEERGSTQIPASLQQHFSAKLGRQNELEKTPSRGGLGLVVNSSKTPGGKSLQSLASACKVPPSTKKNTIPIAFECYEDETDDQIADVATIKKTEKHPCSPIDTANRCETFDSLAADIEDDMLNLEDQDVVLSEDRPYGDVIDPAESEAEALAELGVEEWDSYPPIDPASRIGDDFNYVLRTEDFAEEGDVKLEETRHRTVIADIDEVKMSKAERNELFSMLADDLDSYDLLAEEANLPL | Function: Acts as a chaperone and as an inhibitor for separase sep-1 . Plays an essential role in maintaining chromosome cohesion prior to meiotic and mitotic anaphase, in cytokinesis and in organizing the spindle and the centrosome . Ubiquitination-dependent degradation at the onset of anaphase is likely to activate s... |
Q9LPU5 | MGYLFQETLSSNPKTPIVVDDDNELGLMAVRLANAAAFPMVLKAALELGVFDTLYAAASRTDSFLSPYEIASKLPTTPRNPEAPVLLDRMLRLLASYSMVKCGKALSGKGERVYRAEPICRFFLKDNIQDIGSLASQVIVNFDSVFLNTWAQLKDVVLEGGDAFGRAHGGMKLFDYMGTDERFSKLFNQTGFTIAVVKKALEVYEGFKGVKVLVDVGGGVGNTLGVVTSKYPNIKGINFDLTCALAQAPSYPGVEHVAGDMFVDVPTGDAMILKRILHDWTDEDCVKILKNCWKSLPENGKVVVIELVTPDEAENGDINA... | Function: Involved in indole glucosinolate biosynthesis. Catalyzes methoxylation reactions of the glucosinolate indole ring. Converts the hydroxy intermediates 4-hydroxy-indol-3-yl-methylglucosinolate (4OH-I3M) and 1-hydroxy-indol-3-yl-methylglucosinolate (1OH-I3M) to 4-methoxy-indol-3-yl-methylglucosinolate (4MO-I3M) ... |
Q9P305 | MSEDLSPTSSRVDLSNPHGFTKEGVDLSKLSPQELKLYKMYGKLPSKKDLLRHKMQDRQYFDSGDYALKKAGVIKSDDVIVNNSSNNLPVTNPSGLRESIIRRRMSSSSGGDSISRQGSISSGPPPRSPNK | Function: Required for TORC1 to properly control gene expression and chronological life span. Plays an essential role in initiation of the G0 program by preventing the degradation of specific nutrient-regulated mRNAs via the 5'-3' mRNA decay pathway.
PTM: Phosphorylated by RIM15.
Sequence Mass (Da): 14395
Sequence Leng... |
Q08DK1 | MTCRGSPLAPLLLFSLHGVAASLEVSESPGSVQVARGQTAVLPCTFTTSAALINLNVIWMVIPLSNANQPEQVILYQGGQMFDGAPRFHGRVGFTGTMPATNVSIFINNTQLSDTGTYQCLVNNLPDRGGRNIGVTGLTVLVPPSAPHCQIQGSQDIGSDVILLCSSEEGIPRPTYLWEKLDNTLKLPPTATQDQVQGTVTIRNISALSSGLYQCVASNAIGTSTCLLDLQVISPQPRSIGLIAGAIGTGAVIIIFCIALILGAFFYWRSKNKEEEEEEIPNEIREDDLPPKCSSSAKAFHMEISSSENNTLTSSNTYNS... | Function: Functions as a cell adhesion molecule through homophilic interaction. Stimulates cell growth (By similarity).
PTM: N-glycosylated.
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 46530
Sequence Length: 437
Subcellular Location: Cell membrane
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Q5DX21 | MTSQRSPLAPLLLLSLHGVAASLEVSESPGSIQVARGQPAVLPCTFTTSAALINLNVIWMVTPLSNANQPEQVILYQGGQMFDGAPRFHGRVGFTGTMPATNVSIFINNTQLSDTGTYQCLVNNLPDIGGRNIGVTGLTVLVPPSAPHCQIQGSQDIGSDVILLCSSEEGIPRPTYLWEKLDNTLKLPPTATQDQVQGTVTIRNISALSSGLYQCVASNAIGTSTCLLDLQVISPQPRNIGLIAGAIGTGAVIIIFCIALILGAFFYWRSKNKEEEEEEIPNEIREDDLPPKCSSAKAFHTEISSSDNNTLTSSNAYNSR... | Function: Functions as a cell adhesion molecule through homophilic interaction. Stimulates cell growth.
PTM: N-glycosylated.
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 46120
Sequence Length: 431
Subcellular Location: Cell membrane
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Q15GI3 | MTTGKGKILILGATGYLGKYMVKASISLGHPTYAYVMPLKKNSDDSKLQLLKEFESLGVTIFYGELSEHDKLVAVFKEVDIVISTLAVPQYLEQLKVIEAIKEAGNIKRFVPSEFGNEVDRVRALPRFQAVLDNKKKIRRATEAAGIPFTFVSANSLTAYFVDYLLHPRQKSEQVTIYGSGDAKAVLNYEEDVAAYTIKAADDPRAANRVLIIKPPKNIVSQLDLVSSWEKTTGSTLKMTHISEQEIIKLSESINFPENIHASILHNIFIAGAQLSFELTQDHDLEASELYPNYNYTSVDEYLKICLVNPPKPKLATYAQ... | Function: Involved in the biosynthesis of the floral volatile isoeugenol . Catalyzes the synthesis of the phenylpropene isoeugenol from coniferyl acetate . Phenylpropenes are the primary constituents of various essential plant oils . They are produced as antimicrobial and antianimal compounds, or as floral attractants ... |
Q9KXR9 | MALPPLTPEQRAAALEKAAAARRERAEVKNRLKHSGASLHEVIKQGQENDVIGKMKVSALLESLPGVGKVRAKQIMERLGISESRRVRGLGSNQIASLEREFGSTGS | Function: A nucleoid-associated protein (NAP) that probably plays a role in chromosome compactation. Contributes to development and secondary metabolism, but is dispensable for growth and viability . Binds to the promoter region of a number of genes (including itself); multiple molecules of the protein bind to the DNA ... |
P79693 | VMNLWPGVRLRVTEGWDEDGHHSEESLHYEGRAVDITTSDRDRNKYAMLARLAVEAGF | Function: Intercellular signal essential for a variety of patterning events during development.
PTM: The C-terminal domain displays an autoproteolysis activity and a cholesterol transferase activity. Both activities result in the cleavage of the full-length protein and covalent attachment of a cholesterol moiety to the... |
Q14623 | MSPARLRPRLHFCLVLLLLLVVPAAWGCGPGRVVGSRRRPPRKLVPLAYKQFSPNVPEKTLGASGRYEGKIARSSERFKELTPNYNPDIIFKDEENTGADRLMTQRCKDRLNSLAISVMNQWPGVKLRVTEGWDEDGHHSEESLHYEGRAVDITTSDRDRNKYGLLARLAVEAGFDWVYYESKAHVHCSVKSEHSAAAKTGGCFPAGAQVRLESGARVALSAVRPGDRVLAMGEDGSPTFSDVLIFLDREPHRLRAFQVIETQDPPRRLALTPAHLLFTADNHTEPAARFRATFASHVQPGQYVLVAGVPGLQPARVAAV... | Function: The C-terminal part of the indian hedgehog protein precursor displays an autoproteolysis and a cholesterol transferase activity (By similarity). Both activities result in the cleavage of the full-length protein into two parts followed by the covalent attachment of a cholesterol moiety to the C-terminal of the... |
P97812 | MSPAWLRPRLRFCLFLLLLLLVPAARGCGPGRVVGSRRRPPRKLVPLAYKQFSPNVPEKTLGASGRYEGKIARSSERFKELTPNYNPDIIFKDEENTGADRLMTQRCKDRLNSLAISVMNQWPGVKLRVTEGWDEDGHHSEESLHYEGRAVDITTSDRDRNKYGLLARLAVEAGFDWVYYESKAHVHCSVKSEHSAAAKTGGCFPAGAQVRLENGERVALSAVKPGDRVLAMGEDGTPTFSDVLIFLDREPNRLRAFQVIETQDPPRRLALTPAHLLFIADNHTEPAAHFRATFASHVQPGQYVLVSGVPGLQPARVAAV... | Function: The C-terminal part of the indian hedgehog protein precursor displays an autoproteolysis and a cholesterol transferase activity (By similarity). Both activities result in the cleavage of the full-length protein into two parts followed by the covalent attachment of a cholesterol moiety to the C-terminal of the... |
Q5VWK5 | MNQVTIQWDAVIALYILFSWCHGGITNINCSGHIWVEPATIFKMGMNISIYCQAAIKNCQPRKLHFYKNGIKERFQITRINKTTARLWYKNFLEPHASMYCTAECPKHFQETLICGKDISSGYPPDIPDEVTCVIYEYSGNMTCTWNAGKLTYIDTKYVVHVKSLETEEEQQYLTSSYINISTDSLQGGKKYLVWVQAANALGMEESKQLQIHLDDIVIPSAAVISRAETINATVPKTIIYWDSQTTIEKVSCEMRYKATTNQTWNVKEFDTNFTYVQQSEFYLEPNIKYVFQVRCQETGKRYWQPWSSLFFHKTPETVP... | Function: Associates with IL12RB1 to form the interleukin-23 receptor. Binds IL23 and mediates T-cells, NK cells and possibly certain macrophage/myeloid cells stimulation probably through activation of the Jak-Stat signaling cascade. IL23 functions in innate and adaptive immunity and may participate in acute response t... |
Q13007 | MNFQQRLQSLWTLARPFCPPLLATASQMQMVVLPCLGFTLLLWSQVSGAQGQEFHFGPCQVKGVVPQKLWEAFWAVKDTMQAQDNITSARLLQQEVLQNVSDAESCYLVHTLLEFYLKTVFKNYHNRTVEVRTLKSFSTLANNFVLIVSQLQPSQENEMFSIRDSAHRRFLLFRRAFKQLDVEAALTKALGEVDILLTWMQKFYKL | Function: Multifunctional cytokine mainly produced by T-cells that plays a regulatory role in immune response, tissue homeostasis, host defense, and oncogenesis . Possesses antiviral functions and induces the type I intereferon response during influenza infection . Signals through two receptor complexes IL20RA/IL20RB o... |
Q8NEV9 | MGQTAGDLGWRLSLLLLPLLLVQAGVWGFPRPPGRPQLSLQELRREFTVSLHLARKLLSEVRGQAHRFAESHLPGVNLYLLPLGEQLPDVSLTFQAWRRLSDPERLCFISTTLQPFHALLGGLGTQGRWTNMERMQLWAMRLDLRDLQRHLRFQVLAAGFNLPEEEEEEEEEEEEERKGLLPGALGSALQGPAQVSWPQLLSTYRLLHSLELVLSRAVRELLLLSKAGHSVWPLGFPTLSPQP | Function: Associates with EBI3 to form the IL-27 interleukin, a heterodimeric cytokine which functions in innate immunity. IL-27 has pro- and anti-inflammatory properties, that can regulate T-helper cell development, suppress T-cell proliferation, stimulate cytotoxic T-cell activity, induce isotype switching in B-cells... |
Q8K3I6 | MGQVTGDLGWRLSLLLLPLLLVQAGSWGFPTDPLSLQELRREFTVSLYLARKLLSEVQGYVHSFAESRLPGVNLDLLPLGYHLPNVSLTFQAWHHLSDSERLCFLATTLRPFPAMLGGLGTQGTWTSSEREQLWAMRLDLRDLHRHLRFQVLAAGFKCSKEEEDKEEEEEEEEEEKKLPLGALGGPNQVSSQVSWPQLLYTYQLLHSLELVLSRAVRDLLLLSLPRRPGSAWDS | Function: Associates with EBI3 to form the IL-27 interleukin, a heterodimeric cytokine which functions in innate immunity. IL-27 has pro- and anti-inflammatory properties, that can regulate T-helper cell development, suppress T-cell proliferation, stimulate cytotoxic T-cell activity, induce isotype switching in B-cells... |
P30740 | MEQLSSANTRFALDLFLALSENNPAGNIFISPFSISSAMAMVFLGTRGNTAAQLSKTFHFNTVEEVHSRFQSLNADINKRGASYILKLANRLYGEKTYNFLPEFLVSTQKTYGADLASVDFQHASEDARKTINQWVKGQTEGKIPELLASGMVDNMTKLVLVNAIYFKGNWKDKFMKEATTNAPFRLNKKDRKTVKMMYQKKKFAYGYIEDLKCRVLELPYQGEELSMVILLPDDIEDESTGLKKIEEQLTLEKLHEWTKPENLDFIEVNVSLPRFKLEESYTLNSDLARLGVQDLFNSSKADLSGMSGARDIFISKIVH... | Function: Neutrophil serine protease inhibitor that plays an essential role in the regulation of the innate immune response, inflammation and cellular homeostasis . Acts primarily to protect the cell from proteases released in the cytoplasm during stress or infection. These proteases are important in killing microbes b... |
Q12905 | MRGDRGRGRGGRFGSRGGPGGGFRPFVPHIPFDFYLCEMAFPRVKPAPDETSFSEALLKRNQDLAPNSAEQASILSLVTKINNVIDNLIVAPGTFEVQIEEVRQVGSYKKGTMTTGHNVADLVVILKILPTLEAVAALGNKVVESLRAQDPSEVLTMLTNETGFEISSSDATVKILITTVPPNLRKLDPELHLDIKVLQSALAAIRHARWFEENASQSTVKVLIRLLKDLRIRFPGFEPLTPWILDLLGHYAVMNNPTRQPLALNVAYRRCLQILAAGLFLPGSVGITDPCESGNFRVHTVMTLEQQDMVCYTAQTLVRI... | Function: Chromatin-interacting protein that forms a stable heterodimer with interleukin enhancer-binding factor 3/ILF3 and plays a role in several biological processes including transcription, innate immunity or cell growth . Essential for the efficient reshuttling of ILF3 (isoform 1 and isoform 2) into the nucleus. T... |
Q7TP98 | MVSTHLTSTTLPDCYRSLIVNSELGSSALMDLNSPSFLYPLLHTPADKGTLCTYQAALGKVYASLEVIGVGDDKLQAVHGLNGGKPHRDILGSRITRPTGIKPLCLPRHILAYDWLAQSLLGIVIGSISLAYNELLMMEKLKGFRPFVPHIPFDFYLCEMAFPRVKPAPDETSFSEALLKRNQDLAPNSAEQQIEEVRQVGSYKKGTMTTGHNVADLVVILKILPTFLTMLTNETGFEISSSDATVKILITTVPPNLRKLDPELHLDIKVLQSALAAIRHARWFEENASQSTVKVLIRLLKDLRIRFPGFEPLTPWILDL... | Function: Chromatin-interacting protein that forms a stable heterodimer with interleukin enhancer-binding factor 3/ILF3 and plays a role in several biological processes including transcription, innate immunity or cell growth. Essential for the efficient reshuttling of ILF3 (isoform 1 and isoform 2) into the nucleus. To... |
Q91550 | MRPMRIFLNDDRHVMAKHSVVYPTQEELEAVQNMVSHTERALKAVSDWIDQQEKDCSGEQEQPMAEETETTEEGKDSEMKTGENPTRTLRGVMRVGLVAKGLLLKGDLDLELVLLCRDKPTISLLKRVADNLVLQFETVSEDKYEVIQNIREALIVVKSTKEPPLTLNIRLTSPLVREEMEKLSAGETLTVSDPPDVLDRHKCLAALASLRHAKWFQARANGLKSCVIVIRVLRDLCTRVPTWEPLRGWPLELLCEKAIGTANRPMGAGEALRRVLECLSSGILMPDGSGLYDPCEKDASDALEHLERQQREDITQSAQH... | Function: RNA-binding protein that plays an essential role in the biogenesis of circular RNAs (circRNAs) which are produced by back-splicing circularization of pre-mRNAs. Within the nucleus, promotes circRNAs processing by stabilizing the regulatory elements residing in the flanking introns of the circularized exons (B... |
Q12906 | MRPMRIFVNDDRHVMAKHSSVYPTQEELEAVQNMVSHTERALKAVSDWIDEQEKGSSEQAESDNMDVPPEDDSKEGAGEQKTEHMTRTLRGVMRVGLVAKGLLLKGDLDLELVLLCKEKPTTALLDKVADNLAIQLAAVTEDKYEILQSVDDAAIVIKNTKEPPLSLTIHLTSPVVREEMEKVLAGETLSVNDPPDVLDRQKCLAALASLRHAKWFQARANGLKSCVIVIRVLRDLCTRVPTWGPLRGWPLELLCEKSIGTANRPMGAGEALRRVLECLASGIVMPDGSGIYDPCEKEATDAIGHLDRQQREDITQSAQH... | Function: RNA-binding protein that plays an essential role in the biogenesis of circular RNAs (circRNAs) which are produced by back-splicing circularization of pre-mRNAs. Within the nucleus, promotes circRNAs processing by stabilizing the regulatory elements residing in the flanking introns of the circularized exons. P... |
Q9AQ97 | KKNSILKKNHSWMNAIKNNFQVDDYESLIPNADLVINLTPDKEHHNVIKILQQLMKKNSCLGYSHGFNIVEFGEKIREDITVIMVAPKCPGTEVREEYNRGFGVPTLIAVHDANDIHKQGLEIAKAWSFSIGGHRAGVLESSFIAEVKSDLMGEQTILCGMLQTASLLCYEKLITDKHNPAYAAKLIQNGWETITESLKHGGITLMMDRLSNSSKIRAYNLSENIKKILAPLFQKHMDDIISGEFSAEMMKDWKNHDQKLLFWRQKIKNTSFETAPMYNKKIPEQEYYDHGILMVAILKSGIELSFEKMINAGIIAESAY... | Cofactor: Binds 2 magnesium ions per subunit.
Function: Involved in the biosynthesis of branched-chain amino acids (BCAA). Catalyzes an alkyl-migration followed by a ketol-acid reduction of (S)-2-acetolactate (S2AL) to yield (R)-2,3-dihydroxy-isovalerate. In the isomerase reaction, S2AL is rearranged via a Mg-dependent... |
Q03UU4 | MTTKMFYDKDIDTTPLENKKIAVIGYGAQGHAQANNLRDSGFDVIMGLRPGKSFDSAKKDGFEVYSAAEATAQADVVMMETPDELQAAVWEKEVEPNLKAGSYLGFSHGFNIVYGLIKPNADINVMIIAPKGPGNIERRQFVEGGGIPSLYGVHQDPTGDTAEVAKAYAKGIGSGRAGILETTFEEETTEDLFGEQAVLCGGLTQLIEAGFNTLVEAGYSPELAYFETSHEMKMIVDLIFEGGFEKMRHDCSNTCEYGEMLNGPRIITEESKQGMRDVLKDIQDGTYAKKWLAEYNSGLKDLEKMRTEYKSGLYEQTGKK... | Cofactor: Binds 2 magnesium ions per subunit.
Function: Involved in the biosynthesis of branched-chain amino acids (BCAA). Catalyzes an alkyl-migration followed by a ketol-acid reduction of (S)-2-acetolactate (S2AL) to yield (R)-2,3-dihydroxy-isovalerate. In the isomerase reaction, S2AL is rearranged via a Mg-dependent... |
Q9PJ98 | MRSDAIKKGHLRAPNRSLLRACGLKDEDFDKPFIGVANSYIDIIPGHYFLNDYAKIIKDEIRKNGCVPFEFNTIGVDDGIAMGHEGMLYSLPSRELIANSIETVMNAHQLDALICIPNCDKITPGMLMGALRVNVPTIFVSGGPMASGVTKKGEKISLSSVFEAVGAYESKKISEEEFKDIECSACPSGGSCSGMFTANSMNTLCEAMGIALEGNGTILALSKEREELLRKAARRICEIALDERFKIRNIITQKAVRNAMVVDMAMGGSSNTVLHMLAISREAGVALDIKDLNFISSKVAHIAKIAPSLNSVYMDDIHKA... | Cofactor: Binds 1 [2Fe-2S] cluster per subunit. This cluster acts as a Lewis acid cofactor.
Function: Functions in the biosynthesis of branched-chain amino acids. Catalyzes the dehydration of (2R,3R)-2,3-dihydroxy-3-methylpentanoate (2,3-dihydroxy-3-methylvalerate) into 2-oxo-3-methylpentanoate (2-oxo-3-methylvalerate)... |
A7I7L0 | MTDLRSDTIRKGYERAPNRSLLRSLGVTDREIELPFIGIANAFNTIVPGHTHLRQLSDKVKEGIAAAGGVPFEFGVIGICDGIAMGHEGMRYSLPSRENIADSIELMVQAHRFDGLVCVGTCDKIVPGMLMAAVRTNIPTIVVTGGAMLPGSSGGKDLSLIDVFEGVGKVAAGTMEEDALKELECCAMPGCGSCQGLYTANTMACMTETMGMSLPGCAAVPAVEAAKLRIARESGEAIIPLVKKNSTARDIVTKKSLENAIRVDMALGGSTNTVLHLMAIATEAEIPLSLADFNRIADEIPHICHMLPAGPYSMQALYRA... | Cofactor: Binds 1 [2Fe-2S] cluster per subunit. This cluster acts as a Lewis acid cofactor.
Function: Functions in the biosynthesis of branched-chain amino acids. Catalyzes the dehydration of (2R,3R)-2,3-dihydroxy-3-methylpentanoate (2,3-dihydroxy-3-methylvalerate) into 2-oxo-3-methylpentanoate (2-oxo-3-methylvalerate)... |
Q58672 | MISDRVKKGLKRAPNRSLLKACGYTDEELERPFIGVVNSFTEVVPGHIHLRDIAEAVKKGIYANGGTAFEFNTMAICDGIAMGHEGMKYSLPSREIIADTVESMAKAHGFDGLVLIPSCDKIVPGMIMGAIRTGLPFIVVTGGPMFPGELRGKKYDLISVFEGVGACAAGKITEEELKEIEDIACPGAGSCAGLFTANTMACLTEAMGLSLPYCATSHATTAEKIRIAKRSGMRIVDLVRNNITPDKILTKEAFENAILVDLALGGSTNTTLHIPAIANEVKPKFITLDDFDRLSGEVPHIASLRPGGEHFIIDLHRAGG... | Cofactor: Binds 1 [2Fe-2S] cluster per subunit. This cluster acts as a Lewis acid cofactor.
Function: Functions in the biosynthesis of branched-chain amino acids. Catalyzes the dehydration of (2R,3R)-2,3-dihydroxy-3-methylpentanoate (2,3-dihydroxy-3-methylvalerate) into 2-oxo-3-methylpentanoate (2-oxo-3-methylvalerate)... |
A7X4M5 | MRSDMIKKGDHQAPARSLLHATGALKSPTDMNKPFVAICNSYIDIVPGHVHLRELADIAKEAIREAGAIPFEFNTIGVDDGIAMGHIGMRYSLPSREIIADAAETVINAHWFDGVFYIPNCDKITPGMILAAMRTNVPAIFCSGGPMKAGLSAHGKALTLSSMFEAVGAFKEGSISKEEFLDMEQNACPTCGSCAGMFTANSMNCLMEVLGLALPYNGTALAVSDQRREMIRQAAFKLVENIKNDLKPRDIVTREAIDDAFALDMAMGGSTNTVLHTLAIANEAGIDYDLERINAIAKRTPYLSKIAPSSSYSMHDVHEA... | Cofactor: Binds 1 [2Fe-2S] cluster per subunit. This cluster acts as a Lewis acid cofactor.
Function: Functions in the biosynthesis of branched-chain amino acids. Catalyzes the dehydration of (2R,3R)-2,3-dihydroxy-3-methylpentanoate (2,3-dihydroxy-3-methylvalerate) into 2-oxo-3-methylpentanoate (2-oxo-3-methylvalerate)... |
P00894 | MRRILSVLLENESGALSRVIGLFSQRGYNIESLTVAPTDDPTLSRMTIQTVGDEKVLEQIEKQLHKLVDVLRVSELGQGAHVEREIMLVKIQASGYGRDEVKRNTEIFRGQIIDVTPSLYTVQLAGTSGKLDAFLASIRDVAKIVEVARSGVVGLSRGDKIMR | Catalytic Activity: H(+) + 2 pyruvate = (2S)-2-acetolactate + CO2
Sequence Mass (Da): 17977
Sequence Length: 163
Pathway: Amino-acid biosynthesis; L-isoleucine biosynthesis; L-isoleucine from 2-oxobutanoate: step 1/4.
EC: 2.2.1.6
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P45260 | MRRILSVLLENESGALSRVVGLFSQRAFNIESLTVAPTDDPTLSRMTIEAVGDAQALEQIEKQLHKLVDVFKVVNLSEQEHIEREIVLAKVRAVGSSRDEIKRLADIFRGQIVDVTPKSYTIQLSGTNDKVDAFISALKEETTLLEIVRSGLISVSRGEKNIL | Catalytic Activity: H(+) + 2 pyruvate = (2S)-2-acetolactate + CO2
Sequence Mass (Da): 18087
Sequence Length: 163
Pathway: Amino-acid biosynthesis; L-isoleucine biosynthesis; L-isoleucine from 2-oxobutanoate: step 1/4.
EC: 2.2.1.6
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Q02140 | MRRMIIAKLHNVTGIMNRFTAVLNRRQVNILSITAGVTESQDLTHTTFVIEVDHLDEVEQIIKQLNRLIDVIEVADITDLPHVEREVVLIKVSAPPTIRAEIFTMIEPFRVNVVDVNLENVTIQLTGDSAKIEALIDVVSPYGILNMARTGSAGFERG | Catalytic Activity: H(+) + 2 pyruvate = (2S)-2-acetolactate + CO2
Sequence Mass (Da): 17641
Sequence Length: 158
Pathway: Amino-acid biosynthesis; L-isoleucine biosynthesis; L-isoleucine from 2-oxobutanoate: step 1/4.
EC: 2.2.1.6
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Q57625 | MVNIMEHRHVISALVLNKPGVLQRISGLFTRRGFNISSITVGITENPQISRVTIVVNGDDKILEQVIKQLNKLIDVIKVSELEEKKSVQRELCLIKIYAPTESAKSQVIQYTSIFRGNVVDLSPESLIVEITGSEDKINAFIDLVKPLGIKEMARTGITALARGPKILKPKS | Catalytic Activity: H(+) + 2 pyruvate = (2S)-2-acetolactate + CO2
Sequence Mass (Da): 19057
Sequence Length: 172
Pathway: Amino-acid biosynthesis; L-isoleucine biosynthesis; L-isoleucine from 2-oxobutanoate: step 1/4.
EC: 2.2.1.6
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Q59499 | MSPQTHTLSVLVEAKPGVLARVAALFSRRGFNIESLAVGATEQKDMSRMTIVVSAEETPLEQITKQLNKLINVIKIVELEDGNSVSRELALIKVRADAGTRSQVIEAVNLFRAKVIDVSPEALTIEATGDRGKIEALLRVLEPSVSVRSSNREWCRCPGPRGIGTAK | Catalytic Activity: H(+) + 2 pyruvate = (2S)-2-acetolactate + CO2
Sequence Mass (Da): 18131
Sequence Length: 167
Pathway: Amino-acid biosynthesis; L-isoleucine biosynthesis; L-isoleucine from 2-oxobutanoate: step 1/4.
EC: 2.2.1.6
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P65162 | MSPKTHTLSVLVEDKPGVLARVAALFSRRGFNIESLAVGATECKDRSRMTIVVSAEDTPLEQITKQLNKLINVIKIVEQDDEHSVSRELALIKVQADAGSRSQVIEAVNLFRANVIDVSPESLTVEATGNRGKLEALLRVLEPFGIREIAQSGMVSLSRGPRGIGTAK | Catalytic Activity: H(+) + 2 pyruvate = (2S)-2-acetolactate + CO2
Sequence Mass (Da): 18187
Sequence Length: 168
Pathway: Amino-acid biosynthesis; L-isoleucine biosynthesis; L-isoleucine from 2-oxobutanoate: step 1/4.
EC: 2.2.1.6
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O33113 | MVGLPTHTLSVLVEDTPGVLARVAALFSRRGFNIESLAVGATECKTMSRMTIVVSAEETPLEQVTKQLHKLINVIKVVEQEADNSLSRELALIKVRAEAGTRSQVIEAVHLFRARVIDVSLESLTVEATGDCSKIEALLRVLEPFGVREIVQSGVVSLSRGPRGIGTVR | Catalytic Activity: H(+) + 2 pyruvate = (2S)-2-acetolactate + CO2
Sequence Mass (Da): 18284
Sequence Length: 169
Pathway: Amino-acid biosynthesis; L-isoleucine biosynthesis; L-isoleucine from 2-oxobutanoate: step 1/4.
EC: 2.2.1.6
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A0QUX7 | MSNGTPTHTLSVLVEDKPGVLARVSSLFSRRGFNIQSLAVGATEQKDMSRMTIVVSVEDSPLEQITKQLNKLINVIKIVEQEEDNSVSRELALIKVRADATTRGQIIEAVNLFRAKVVDVSTESLTIEATGTPEKLEALLRVLEPYGIREIAQSGVVSVSRGPRGIGAAK | Catalytic Activity: H(+) + 2 pyruvate = (2S)-2-acetolactate + CO2
Sequence Mass (Da): 18395
Sequence Length: 170
Pathway: Amino-acid biosynthesis; L-isoleucine biosynthesis; L-isoleucine from 2-oxobutanoate: step 1/4.
EC: 2.2.1.6
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Q9SMC2 | MEHIQTRTTLSQLSTLPSDKRLGAIRFKCLLVMKVEMINRIAGVFARRGYNIESLAVGLNKDKALFTIVVSGTERVLQQVMEQLQKLVNVIKVEDLSKEPQVERELMLIKISADPKYRAEVMWLVDVFRAKIVDISDQSLTIEVTGDPGKMVAVQRNLSKFGIREIARTGKIALRREKMGESAPFWRFSAASYPDLEGAMSAGTISRTIKRTPNGESMSMAEGDVYPVETDDNSGVSQVLDAHWGVLNDEDTSGLRSHTLSMLVNDTPGVLNIVTGVFARRGYNIQSLAVGHAEVEGLSRITTVVPGTDESVSKLVQQLY... | Function: Regulatory subunit of acetohydroxy-acid synthase. Probably involved in feedback inhibition by branched-chain amino acids. Not involved in herbicide tolerance.
Sequence Mass (Da): 50113
Sequence Length: 449
Pathway: Amino-acid biosynthesis; L-isoleucine biosynthesis; L-isoleucine from 2-oxobutanoate: step 1/4.... |
Q55141 | MKHTLSVLVEDEAGVLTRIAGLFARRGFNIESLAVGSAEQGDVSRITMVVPGDENTIEQLTKQLYKLVNVIKVQDITETPCVERELMLVKVSANAPNRAEVIELAQVFRARIVDISEDTVTIEVVGDPGKMVAILQMLAKFGIKEVARTGKIALVRESGVNTEYLKSLESKF | Catalytic Activity: H(+) + 2 pyruvate = (2S)-2-acetolactate + CO2
Sequence Mass (Da): 18871
Sequence Length: 172
Pathway: Amino-acid biosynthesis; L-isoleucine biosynthesis; L-isoleucine from 2-oxobutanoate: step 1/4.
EC: 2.2.1.6
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O58045 | MGKFVEKLEKAIKGYTFDDVLLIPQATEVEPKDVDVSTRITPNVKLNIPILSAAMDTVTEWEMAVAMAREGGLGVIHRNMGIEEQVEQVKRVKRAERLIVEDVITIAPDETVDFALFLMEKHGIDGLPVVEDEKVVGIITKKDIAAREGKLVKELMTKEVITVPESIEVEEALKIMIENRIDRLPVVDERGKLVGLITMSDLVARKKYKNAVRDENGELLVAAAVSPFDIKRAIELDKAGVDVIVVDTAHAHNLKAIKSMKEMRQKVDADFIVGNIANPKAVDDLTFADAVKVGIGPGSICTTRIVAGVGVPQITAVAMV... | Function: Catalyzes the conversion of inosine 5'-phosphate (IMP) to xanthosine 5'-phosphate (XMP), the first committed and rate-limiting step in the de novo synthesis of guanine nucleotides, and therefore plays an important role in the regulation of cell growth.
Catalytic Activity: H2O + IMP + NAD(+) = H(+) + NADH + XM... |
Q9KH33 | MARIIETSTGLDALTFDDVLLQPGHSEVMPGQTNIATRIAQDIELNVPILSAAMDTVTESRLAIAMAQAGGMGVIHRNLTPVQQAEEVRQVKKFESGMVVNPVTIGPDATLAEALSLDEGPRHFRASPVVEKSHRLVGILTNRDVRFASDPEQKIYELMTRENLVTVKDGVQQHEAKRLLHTHRIEKXLVVDADSRFVGLITVKDIEKSQLNPHASKDAQGRLRAAAAISVGDDGYERAERLIDAGVDLLVVDTAHGHSQRVLDAVTRVKKLSNSVRIMAGNVATYDGTRALIDAGADAVKVGIGPGSICTTRIVAGVGV... | Function: Catalyzes the conversion of inosine 5'-phosphate (IMP) to xanthosine 5'-phosphate (XMP), the first committed and rate-limiting step in the de novo synthesis of guanine nucleotides, and therefore plays an important role in the regulation of cell growth.
Catalytic Activity: H2O + IMP + NAD(+) = H(+) + NADH + XM... |
Q7UJL3 | MGASTRFRRQSGKVPYNSTAASVIIARFPHRITFGCPRPRGNENGMFDDKIGDLGVTFDDVLLQPRYSEVVPSEVDVSSQMTQRIRLQIPLISSPMDTVTESEMAIALAKEGGLGIVHKNLSVRRQTEEVLKVKRSANGIIVNPVTLNPAQKVSAAAELMDRANVSGIPIVEDDRTLAGILTRRDLRFLEDPDMPISQVMTRENLVTAVGNVTLAQAEKILTEKRVEKLLLIDEERKLTGLITIRDIDMMKRYPRACKDPQGRLRVGAAIGVGDYERAESLIGKGVDVLVVDSAHGHSRNVIETVREIKQNKSWDIDVVA... | Function: Catalyzes the conversion of inosine 5'-phosphate (IMP) to xanthosine 5'-phosphate (XMP), the first committed and rate-limiting step in the de novo synthesis of guanine nucleotides, and therefore plays an important role in the regulation of cell growth.
Catalytic Activity: H2O + IMP + NAD(+) = H(+) + NADH + XM... |
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