ids stringlengths 6 10 | seqs stringlengths 11 1.02k | texts stringlengths 108 11.1k |
|---|---|---|
Q9GZV4 | MADEIDFTTGDAGASSTYPMQCSALRKNGFVVLKGRPCKIVEMSTSKTGKHGHAKVHLVGIDIFTGKKYEDICPSTHNMDVPNIKRNDYQLICIQDGYLSLLTETGEVREDLKLPEGELGKEIEGKYNAGEDVQVSVMCAMSEEYAVAIKPCK | Function: Translation factor that promotes translation elongation and termination, particularly upon ribosome stalling at specific amino acid sequence contexts . Binds between the exit (E) and peptidyl (P) site of the ribosome and promotes rescue of stalled ribosome: specifically required for efficient translation of p... |
Q6IS14 | MADDLDFETGDAGASATFPMQCSALRKNGFVVLKGWPCKIVEMSASKTGKHGHAKVHLVGIDIFTGKKYEDICPSTHNMDVPNIKRNDFQLIGIQDGYLSLLQDSGEVPEDLRLPEGDLGKEIEQKYDCGEEILITVLSAMTEEAAVAIKAMAK | Function: Translation factor that promotes translation elongation and termination, particularly upon ribosome stalling at specific amino acid sequence contexts (By similarity). Binds between the exit (E) and peptidyl (P) site of the ribosome and promotes rescue of stalled ribosome: specifically required for efficient t... |
Q64282 | MGENADGDQVMENLLQLRCHFTWKLLFENNDIPDLEVRISEQVQFLDIKNPLGMHNLLAYVRHLKGQQDEALQSLKEAEALIQSEQLSKRSLATWGNCAWLHYHRGSLAEAQIYLDKVEKVCKEFSSPFRYRLECAEMDCEEGWALLKCGGGNYKQAMACFAKALKVEPENPEYNTGYAVVAYRQDLDDNFISLEPLRKAVRLNPEDPYLKVLLALKLQDLGEHVEAEAHIEEALSSTSCQSYVIRYAAKYFRRKHRVDKALHLLNRALQASPSSGYLHYQKGLCYKQQISQLRTSRNRQPRRQDNVQELAQQAIHEFQE... | Function: Interferon-induced antiviral RNA-binding protein that specifically binds single-stranded RNA bearing a 5'-triphosphate group (PPP-RNA), thereby acting as a sensor of viral single-stranded RNAs and inhibiting expression of viral messenger RNAs. Single-stranded PPP-RNAs, which lack 2'-O-methylation of the 5' ca... |
Q60462 | MSTTTKKSLESKLQQLKCHFTWNLMAGDESLDEFEDKVFNKDEFQKRECKATMCNILAFVKHRRGQNASALKELEKAEQFIQQQHPDHVEIRNIVTWGNYAWVYYHMGQLEKAQAYLDKVRQVCEKFSSPYRIESPELDCEEGWARLKCTRNQNERVKVCFEKALEKDPKNPEFTSGWAISNYRLDFWPAQQNAVDSLKQAIRMSPNSPYVKVLLALKLEMNQENQGKELVEEALREAPGETDVLRSAARFYYKTHDKDRAIQLLSQALELLPNNAYVYYYIGCFYRSKVLQIDSRRETSQNENREQLLKQAIYYLKKAE... | Function: IFN-induced antiviral protein which inhibits expression of viral messenger RNAs lacking 2'-O-methylation of the 5' cap. The ribose 2'-O-methylation would provide a molecular signature to distinguish between self and non-self mRNAs by the host during viral infection. Viruses evolved several ways to evade this ... |
P09913 | MSENNKNSLESSLRQLKCHFTWNLMEGENSLDDFEDKVFYRTEFQNREFKATMCNLLAYLKHLKGQNEAALECLRKAEELIQQEHADQAEIRSLVTWGNYAWVYYHMGRLSDVQIYVDKVKHVCEKFSSPYRIESPELDCEEGWTRLKCGGNQNERAKVCFEKALEKKPKNPEFTSGLAIASYRLDNWPPSQNAIDPLRQAIRLNPDNQYLKVLLALKLHKMREEGEEEGEGEKLVEEALEKAPGVTDVLRSAAKFYRRKDEPDKAIELLKKALEYIPNNAYLHCQIGCCYRAKVFQVMNLRENGMYGKRKLLELIGHAV... | Function: IFN-induced antiviral protein which inhibits expression of viral messenger RNAs lacking 2'-O-methylation of the 5' cap. The ribose 2'-O-methylation would provide a molecular signature to distinguish between self and non-self mRNAs by the host during viral infection. Viruses evolved several ways to evade this ... |
Q64112 | MSTTSKESLVCNLRQLKCHFTWNLIAEDESLDEFEDRVFNKDEFQNSEFKATMCNILAYVKHCRGLNEAALQCLGEAEGFIQQQHPDQVEIRSLVTWGNYAWVYYHMGQFSKAQAYLDKVKQVCKKFSSPYRIENPALDCEEGWARLKCTKNQNERVKVCFQKALEKDPKNPEFTSGWAIAFYRLDDWPARNYCIDSLEQAIQLSPDNTYVKVLLALKLDAVHVHKNQAMALVEEALKKDPSAIDTLLRAARFYCKVYDTDRAIQLLRKALEKLPNNAYVHYYMGCCYRSKVHHMLNRREMVFSGDRKKLEELIQLAVNH... | Function: IFN-induced antiviral protein which inhibits expression of viral messenger RNAs lacking 2'-O-methylation of the 5' cap. The ribose 2'-O-methylation would provide a molecular signature to distinguish between self and non-self mRNAs by the host during viral infection. Viruses evolved several ways to evade this ... |
Q13325 | MSEIRKDTLKAILLELECHFTWNLLKEDIDLFEVEDTIGQQLEFLTTKSRLALYNLLAYVKHLKGQNKDALECLEQAEEIIQQEHSDKEEVRSLVTWGNYAWVYYHMDQLEEAQKYTGKIGNVCKKLSSPSNYKLECPETDCEKGWALLKFGGKYYQKAKAAFEKALEVEPDNPEFNIGYAITVYRLDDSDREGSVKSFSLGPLRKAVTLNPDNSYIKVFLALKLQDVHAEAEGEKYIEEILDQISSQPYVLRYAAKFYRRKNSWNKALELLKKALEVTPTSSFLHHQMGLCYRAQMIQIKKATHNRPKGKDKLKVDELI... | Function: Interferon-induced RNA-binding protein involved in the human innate immune response. Has a broad and adaptable RNA structure recognition important for RNA recognition specificity in antiviral defense. Binds precursor and processed tRNAs as well as poly-U-tailed tRNA fragments . Specifically binds single-stran... |
Q6K0P9 | MANNYKKIVLLKGLEVINDYHFRIVKSLLSNDLKLNPKMKEEYDKIQIADLMEEKFPGDAGLGKLIEFFKEIPTLGDLAETLKREKLKVANKIESIPVKGIIPSKKTKQKEVYPATPACTPSNRLTAKGAEETLGPQKRKKPSEEETGTKRSKMSKEQTRPSCSAGASTSTAMGRSPPPQTSSSAPPNTSSTESLKPLANRHATASKNIFREDPIIAMVLNATKVFKYESSENEQRRMFHATVATQTQFFHVKVLNINLKRKFIKKRIIIISNYSKRNSLLEVNEASSVSEAGPDQTFEVPKDIIRRAKKIPKINILHKQ... | Function: Major mediator of the tumor suppressor activity of IFN in breast cancer cells. Promotes ubiquitination and subsequent degradation of MDM2, which leads to p53/TP53 stabilization. Promotes ubiquitination and subsequent degradation of HDAC1, which in turn enhances maspin expression, and impairs invasive activity... |
P13164 | MHKEEHEVAVLGPPPSTILPRSTVINIHSETSVPDHVVWSLFNTLFLNWCCLGFIAFAYSVKSRDRKMVGDVTGAQAYASTAKCLNIWALILGILMTIGFILLLVFGSVTVYHIMLQIIQEKRGY | Function: IFN-induced antiviral protein which inhibits the entry of viruses to the host cell cytoplasm, permitting endocytosis, but preventing subsequent viral fusion and release of viral contents into the cytosol. Active against multiple viruses, including influenza A virus, SARS coronaviruses (SARS-CoV and SARS-CoV-2... |
Q9D103 | MPKEQQEVVVLGSPHISTSATATTINMPEISTPDHVVWSLFNTLFMNFCCLGFVAYAYSVKSRDRKMVGDTTGAQAFASTAKCLNISSLFFTILTAIVVIVVCAIR | Function: IFN-induced antiviral protein which inhibits the entry of viruses to the host cell cytoplasm, permitting endocytosis, but preventing subsequent viral fusion and release of viral contents into the cytosol. Active against multiple viruses, including influenza A virus, SARS coronavirus (SARS-CoV), Marburg virus ... |
Q99J93 | MSHNSQAFLSTNAGLPPSYETIKEEYGVTELGEPSNSAVVRTTVINMPREVSVPDHVVWSLFNTLFFNACCLGFVAYAYSVKSRDRKMVGDVVGAQAYASTAKCLNISSLIFSILMVIICIIIFSTTSVVVFQSFAQRTPHSGF | Function: IFN-induced antiviral protein which inhibits the entry of viruses to the host cell cytoplasm, permitting endocytosis, but preventing subsequent viral fusion and release of viral contents into the cytosol. Active against multiple viruses, including influenza A virus, SARS coronavirus (SARS-CoV), Marburg virus ... |
Q05688 | NAIFVPRPERKRREVMQIANTTMSSRSRNTTVLDTYNITDPEELETEYPFFESRVDNKERTVISNLRPFTLYRIDIHSCNHEAEKLGCSASNFVFARTMPAEGADDIPGPVTWEPRPENSIFLKWPEPENPNGLILMYEIKYGSQVEDQRECVSRQEYRKYGGAKLNRLNPGNYTARIQATSLSGNGSWTDPVFFYVQAKTTYENFIHLMIALPIAVLLIVGGLVIMLYVFHRKRNSSRLGNGVLYASVNPEYFSAADVYVPDEWEVAREKITMSRELGQGSFGMVYEGVAKGVVKDEPETRVAIKTVNEAASMRERIEF... | Function: Receptor tyrosine kinase which mediates actions of insulin-like growth factor 1 (IGF1). Binds IGF1 with high affinity and IGF2 and insulin (INS) with a lower affinity. The activated IGF1R is involved in cell growth and survival control. IGF1R is crucial for tumor transformation and survival of malignant cell.... |
Q29000 | ERTVISNLRPFTLYRIDIHSCNHEAEKLGCSASNFVFARTMPAEGADDIPGPVTWEPRPENSIFLKWPEPENPNGLILMYEIKYGSQVEDQRECVSRQEYRKYGGAKLNRLNPGNYTARIQATSLSGNGSWTEPVFFYVQAKTTYENFIHLIIALPVAVLLIVGGLVIMLYVFHRKRNNSRLGNGVMLFELMRMCWQYNPKMRPSFLEIISSIKDEMEPGFREVSFYYSEENKPPEPEELDLEPENMESVPLDPSASSSSLPLPDRHSGHKAENGPGPGVLVLRASFDERQPYAHMNGGRKNER | Function: Receptor tyrosine kinase which mediates actions of insulin-like growth factor 1 (IGF1). Binds IGF1 with high affinity and IGF2 and insulin (INS) with a lower affinity. The activated IGF1R is involved in cell growth and survival control. IGF1R is crucial for tumor transformation and survival of malignant cell.... |
Q61730 | MGLLWYLMSLSFYGILQSHASERCDDWGLDTMRQIQVFEDEPARIKCPLFEHFLKYNYSTAHSSGLTLIWYWTRQDRDLEEPINFRLPENRISKEKDVLWFRPTLLNDTGNYTCMLRNTTYCSKVAFPLEVVQKDSCFNSAMRFPVHKMYIEHGIHKITCPNVDGYFPSSVKPSVTWYKGCTEIVDFHNVLPEGMNLSFFIPLVSNNGNYTCVVTYPENGRLFHLTRTVTVKVVGSPKDALPPQIYSPNDRVVYEKEPGEELVIPCKVYFSFIMDSHNEVWWTIDGKKPDDVTVDITINESVSYSSTEDETRTQILSIKK... | Function: Coreceptor for IL1RL2 in the IL-36 signaling system. Coreceptor with IL1R1 in the IL-1 signaling system. Associates with IL1R1 bound to IL1B to form the high affinity interleukin-1 receptor complex which mediates interleukin-1-dependent activation of NF-kappa-B and other pathways. Signaling involves the recru... |
P08831 | MAKVPDLFEDLKNCYSENEDYSSEIDHLSLNQKSFYDASYEPLREDQMNKFMSLDTSETSKTSKLSFKENVVMVAASGKILKKRRLSLNQFITDDDLEAIANNTEEEIIKPRSAHYSFQSNVKYNFMRVIHQECILNDALNQSIIRDMSGPYLTATTLNNLEEAVKFDMVAYVSEEDSQLPVTLRISKTQLFVSAQNEDEPVLLKEMPETPKIIKDETNLLFFWEKHGSMDYFKSVAHPKLFIATKQEKLVHMASGPPSITDFQILEK | Function: Cytokine constitutively present intracellularly in nearly all resting non-hematopoietic cells that plays an important role in inflammation and bridges the innate and adaptive immune systems. After binding to its receptor IL1R1 together with its accessory protein IL1RAP, forms the high affinity interleukin-1 r... |
Q60480 | FEDLKNCYSENEEYASAIDHLSLNQKSFYDTNYDPLHENRVDEPVSPNPYENSEESNFTLEDSSDSSAVVLTSAHGEVLKKRRLSLNQTMSNEDLEAIANDSEEEIIEPWSVPYSFQSNLKFKYQRSIKKGAVITDAMHQSLIRESNGQHLKAMHVVDRKHEVKFDIDGYVSTATRIRPVTLKISKTQLYVCAQEEGQPVLLKE | Function: Produced by activated macrophages, IL-1 stimulates thymocyte proliferation by inducing IL-2 release, B-cell maturation and proliferation, and fibroblast growth factor activity. IL-1 proteins are involved in the inflammatory response, being identified as endogenous pyrogens, and are reported to stimulate the r... |
P01583 | MAKVPDMFEDLKNCYSENEEDSSSIDHLSLNQKSFYHVSYGPLHEGCMDQSVSLSISETSKTSKLTFKESMVVVATNGKVLKKRRLSLSQSITDDDLEAIANDSEEEIIKPRSAPFSFLSNVKYNFMRIIKYEFILNDALNQSIIRANDQYLTAAALHNLDEAVKFDMGAYKSSKDDAKITVILRISKTQLYVTAQDEDQPVLLKEMPEIPKTITGSETNLLFFWETHGTKNYFTSVAHPNLFIATKQDYWVCLAGGPPSITDFQILENQA | Function: Cytokine constitutively present intracellularly in nearly all resting non-hematopoietic cells that plays an important role in inflammation and bridges the innate and adaptive immune systems . After binding to its receptor IL1R1 together with its accessory protein IL1RAP, forms the high affinity interleukin-1 ... |
P18430 | MAKVPDLFEDLKNCYSENEEYSSDIDHLSLNQKSFYDASYEPLPGDGMDKFMPLSTSKTSKTSRLNFKDSVVMAAANGKILKKRRLSLNQFITDDDLEAIANDTEEEIIKPRSATYSFQSNMKYNFMRVINHQCILNDARNQSIIRDPSGQYLMAAVLNNLDEAVKFDMAAYTSNDDSQLPVTLRISETRLFVSAQNEDEPVLLKELPETPKTIKDETSLLFFWEKHGNMDYFKSAAHPKLFIATRQEKLVHMAPGLPSVTDFQILENQS | Function: Cytokine constitutively present intracellularly in nearly all resting non-hematopoietic cells that plays an important role in inflammation and bridges the innate and adaptive immune systems. After binding to its receptor IL1R1 together with its accessory protein IL1RAP, forms the high affinity interleukin-1 r... |
Q8R460 | MFSKHPFSTHISGRETPDFGEVFDLDQQVWIFRNQALVTVPRSHRVTPVSVTILPCKYPESLEQDKGIAIYLGIQNPDKCLFCKEVNGHPTLLLKEEKILDLYHHPEPMKPFLFYHTRTGGTSTFESVAFPGHYIASSKTGNPIFLTSKKGEYYNINFNLDIKS | Function: Functions as an agonist of NF-kappa B activation through the orphan IL-1-receptor-related protein 2/IL1RL2. Part of the IL-36 signaling system that is thought to be present in epithelial barriers and to take part in local inflammatory response; similar to the IL-1 system with which it shares the coreceptor IL... |
Q9NZH6 | MSFVGENSGVKMGSEDWEKDEPQCCLEDPAGSPLEPGPSLPTMNFVHTSPKVKNLNPKKFSIHDQDHKVLVLDSGNLIAVPDKNYIRPEIFFALASSLSSASAEKGSPILLGVSKGEFCLYCDKDKGQSHPSLQLKKEKLMKLAAQKESARRPFIFYRAQVGSWNMLESAAHPGWFICTSCNCNEPVGVTDKFENRKHIEFSFQPVCKAEMSPSEVSD | Function: Immune regulatory cytokine that acts as a suppressor of innate inflammatory and immune responses involved in curbing excessive inflammation. Signaling can occur via two mechanisms, intracellularly through nuclear translocation with SMAD3 and extracellularly after secretion and binding to its receptor composed... |
P26951 | MVLLWLTLLLIALPCLLQTKEDPNPPITNLRMKAKAQQLTWDLNRNVTDIECVKDADYSMPAVNNSYCQFGAISLCEVTNYTVRVANPPFSTWILFPENSGKPWAGAENLTCWIHDVDFLSCSWAVGPGAPADVQYDLYLNVANRRQQYECLHYKTDAQGTRIGCRFDDISRLSSGSQSSHILVRGRSAAFGIPCTDKFVVFSQIEILTPPNMTAKCNKTHSFMHWKMRSHFNRKFRYELQIQKRMQPVITEQVRDRTSFQLLNPGTYTVQIRARERVYEFLSAWSTPQRFECDQEEGANTRAWRTSLLIALGTLLALVC... | Function: Cell surface receptor for IL3 expressed on hematopoietic progenitor cells, monocytes and B-lymphocytes that controls the production and differentiation of hematopoietic progenitor cells into lineage-restricted cells . Ligand stimulation rapidly induces hetrodimerization with IL3RB, phosphorylation and enzyme ... |
P26952 | MAANLWLILGLLASHSSDLAAVREAPPTAVTTPIQNLHIDPAHYTLSWDPAPGADITTGAFCRKGRDIFVWADPGLARCSFQSLSLCHVTNFTVFLGKDRAVAGSIQFPPDDDGDHEAAAQDLRCWVHEGQLSCQWERGPKATGDVHYRMFWRDVRLGPAHNRECPHYHSLDVNTAGPAPHGGHEGCTLDLDTVLGSTPNSPDLVPQVTITVNGSGRAGPVPCMDNTVDLQRAEVLAPPTLTVECNGSEAHARWVARNRFHHGLLGYTLQVNQSSRSEPQEYNVSIPHFWVPNAGAISFRVKSRSEVYPRKLSSWSEAWG... | Function: Cell surface receptor for IL3 expressed on hematopoietic progenitor cells, monocytes and B-lymphocytes that controls the production and differentiation of hematopoietic progenitor cells into lineage-restricted cells (By similarity). Ligand stimulation rapidly induces hetrodimerization with IL3RB, phosphorylat... |
P32927 | MVLAQGLLSMALLALCWERSLAGAEETIPLQTLRCYNDYTSHITCRWADTQDAQRLVNVTLIRRVNEDLLEPVSCDLSDDMPWSACPHPRCVPRRCVIPCQSFVVTDVDYFSFQPDRPLGTRLTVTLTQHVQPPEPRDLQISTDQDHFLLTWSVALGSPQSHWLSPGDLEFEVVYKRLQDSWEDAAILLSNTSQATLGPEHLMPSSTYVARVRTRLAPGSRLSGRPSKWSPEVCWDSQPGDEAQPQNLECFFDGAAVLSCSWEVRKEVASSVSFGLFYKPSPDAGEEECSPVLREGLGSLHTRHHCQIPVPDPATHGQYI... | Function: Cell surface receptor that plays a role in immune response and controls the production and differentiation of hematopoietic progenitor cells into lineage-restricted cells. Acts by forming an heterodimeric receptor through interaction with different partners such as IL3RA, IL5RA or CSF2RA . In turn, participat... |
Q8S9S4 | MAAASSSRVLLAAVAVLAAALAGCGAGAALDDPAGLLRRAKEAEFAGWMVGLRRRIHENPELGYEEFATSELVRRELDALGIPYRHPFAVTGVVATVGTGGPPFVALRADMDALPMQESVEWEHKSKVPGKMHGCGHDAHVAMLLGSARILQEHRDELKGTVVLVFQPAEEGGGGAKKMIDDGAVENIEAIFGVHVADVVPIGVVASRPGPVMAGSGFFEAVISGKGGHAALPHHTIDPILAASNVIVSLQQLVSREADPLDSQVVTVGKFQGGGAFNVIPDSVTIGGTFRAFLKESFNQLKQRIEEVIVSQASVQRCNA... | Function: Hydrolyzes certain amino acid conjugates of the plant growth regulator indole-3-acetic acid (IAA).
Sequence Mass (Da): 47135
Sequence Length: 442
Subcellular Location: Endoplasmic reticulum lumen
EC: 3.5.1.-
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O04373 | MSFFKWVSFVLILHLLNPTLISCSSNGLSQIPSKFLTLAKRNDFFDWMVGIRRRIHENPELGYEEVETSKLVRAELEKMGVSYKYPVAVTGVVGYVGTGHAPFVALRADMDALAMQEMVEWEHKSKVPGKMHACGHDAHTTMLLGAAKLLKEHEEELQGTVVLVFQPAEEGGGGAKKIVEAGVLENVSAIFGLHVTNQLALGQVSSREGPMLAGSGFFKAKISGKGGHAALPQHTIDPILAASNVIVSLQHLVSREADPLDSQVVTVAKFEGGGAFNVIPDSVTIGGTFRAFSTKSFMQLKKRIEQVITRQASVNMCNAT... | Cofactor: The Mn(2+) ion enhances activity.
Function: Hydrolyzes certain amino acid conjugates of the plant growth regulator indole-3-acetic acid (IAA), including IAA-Ala, IAA-Asn, IAA-Cys, IAA-Glu, IAA-Met, IAA-Ser and IAA-Gly . Has a lower efficiency with IAA-Phe, IAA-Leu and IAA-Val and no activity with IAA-Ile . Im... |
Q8VYX0 | MDNLRKLNLLSVSLTIIFVSLTIATNLPFFEVKYPNNNPFGMLLRPTPIKNQSLGLPAHVGSDECRVWTKACSDEILRLTYQPDNVAWLKRVRRTIHENPELAFEEYETSRLIRSELDRMGIMYRYPLAKTGIRAWIGSGGPPFVAVRADMDALPIQEAVEWEHISKVAGKMHACGHDAHVTMLLGAAHILKAREHLLKGTVVLLFQPAEEAGNGAKNMIEDGALDDVEAIFAVHVSHIHPTGVIGSRSGPLLAGCGIFRAVITSEDSRGAANLLLAASSAVISLQGIVSREASPLDSQVVSVTSFDGGHSLDVAPDTVV... | Function: Hydrolyzes certain amino acid conjugates of the plant growth regulator indole-3-acetic acid (IAA). Also hydrolyzes amino acid conjugates of jasmonic acid and 12-hydroxy jasmonic acid.
Catalytic Activity: a jasmonyl-L-amino acid + H2O = a jasmonate + an L-alpha-amino acid
Sequence Mass (Da): 50820
Sequence Len... |
Q9FNN3 | MGSNRPKNFRRRGDDGGDEIDGKVATPSSKPTSTLSSSKPKTLSASAPKKKLLSFADDEEEEEDGAPRVTIKPKNGRDRVKSSSRLGVSGSSHRHSSTKERRPASSNVLPQAGSYSKEALLELQKNTRTLPYSRSSANAEPKVVLKGLIKPPQDHEQQSLKDVVKQVSDLDFDEEGEEEQHEDAFADQAAIIRAKKERMRQSRSAPAPDYISLDGGIVNHSAVEGVSDEDADFQGIFVGPRPQKDDKKGVFDFGDENPTAKETTTSSIYEDEDEEDKLWEEEQFKKGIGKRMDEGSHRTVTSNGIGVPLHSKQQTLPQQQ... | Function: Transcriptional repressor regulating endoreduplication through control of A-type cyclins expression . Does not bind to promoter sequences (in vitro) and may act by interacting with tissue-specific transcription factors . Enhances the endocycle in endoreduplicating cells in seedlings . Required for efficient s... |
Q4X099 | MLLSQTRGRLPSTLRSFSRRALSTTLPRGKDSEETALNKVSRNVTQPISQGASQAMLYATGLTEEDMNKAQVGISSVWYNGNPCNMHLLDLSNRVREGVQKAGLVGFQFNTVGVSDAISMGTKGMRYSLQSRDLIADSIETVMGGQWYDANISIPGCDKNMPGVLMAMGRVNRPSLMVYGGTIKPGCARTQNNADIDIVSAFQAYGQFLTGEITENQRFDIIRNACPGGGACGGMYTANTMATAIEVMGMTLPGSSSNPAESKAKDLECLAAGEAIKRLLKEDIRPSDILTRQAFENAMIVVNITGGSTNAVLHLIAIAD... | Cofactor: Binds 1 [2Fe-2S] cluster per subunit.
Function: Dihydroxyacid dehydratase that catalyzes the third step in the common pathway leading to 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-methylpentan... |
C1DFH7 | MKVYYDKDCDLSIIQSKKVAIIGYGSQGHAHACNLKDSGVDVYVGLRAGSASVAKAEAHGLTVKSVKDAVAAADVVMILTPDEFQGRLYKDEIEPNLKKGATLAFAHGFSIHYNQVVPRADLDVIMIAPKAPGHTVRSEFVRGGGIPDLIAVYQDASGNAKNLALSYACGVGGGRTGIIETTFKDETETDLFGEQAVLCGGCVELVKAGFETLVEAGYAPEMAYFECLHELKLIVDLMFEGGIANMNYSISNNAEYGEYVTGPEVINEQSRQAMRNALKRIQDGEYAKMFITEGAANYPSMTAYRRNNAAHQIEVVGEKL... | 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... |
P37253 | MVKVYYNGDIKENVLAGKTVAVIGYGSQGHAHALNLKESGVDVIVGVRQGKSFTQAQEDGHKVFSVKEAAAQAEIIMVLLPDEQQQKVYEAEIKDELTAGKSLVFAHGFNVHFHQIVPPADVDVFLVAPKGPGHLVRRTYEQGAGVPALFAIYQDVTGEARDKALAYAKGIGGARAGVLETTFKEETETDLFGEQAVLCGGLSALVKAGFETLTEAGYQPELAYFECLHELKLIVDLMYEEGLAGMRYSISDTAQWGDFVSGPRVVDAKVKESMKEVLKDIQNGTFAKEWIVENQVNRPRFNAINASENEHQIEVVGRKL... | 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... |
Q0BS26 | MRVYYDRDADLNLIKGKKVAVIGYGSQGHAHVLNMRDSGVKDLVVGLRKGSSAVAKAEGEGLKVMEPAEAAAWADVVMILTPDESQADLYREHLHANLRPGAALAFAHGLNIHFNLIEPRSDIDVFMIAPKGPGHTVRGEYQKGGGVPCLVAVAQNASGNALEIALSYASAVGGGRAGIIETTFKEECETDLFGEQAVLCGGLVELIRAGFETLVEAGYAPEMAYFECLHEVKLIVDLIYEGGIANMNYSISNTAEYGEYVTGPRIVTPETKAEMKRVLEDIQSGRFVRDFMLEMKVNGASFKSIRRRNNEHQIEQVGER... | 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... |
Q5V520 | MSDELTTTVYYDEDADVSTINDETVAVLGYGSQGHAHALNLHESGVDVIVGLRQDSSSWADAEDAGLRVETPDVAAGEADRVVMLVPDTIQPAVYEAIEDELDAGDTLQFAHGFNIHYGQIEPPEDVDVTMVAPKSPGHLVRRTYERGEGTPGLIAVYQDATGNAKQESLAYAKGIGCTRAGVIETSFQEEVETDLFGEQAVLCGGVTEMVKAGFETLVDAGYAPEMAYFECLNELKLIVDLMYEGGHMGMWNSVSDTAEYGGLTRGEEVIDREGMEKILEEVQNGEFAREWINENQANRPAYKQYRDAEQNHQIEAVGE... | 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... |
Q18GT4 | MTETKTQTETETDEEEGTDTDTALDTTIYYDDDADREYIDDKTVAVLGYGSQGHAHAQNLADSGIDVIVGLYEGSSSRDAARADGLRVETPATAADEADIVSVLVPDTVQPDVFEAIQDGLDAGDTLQFAHGFNIHYNQIQPPADVDVTMVAPKAPGHLVRRNYEAGEGTPGLVAVYQNTTGTARKEAVAYAHAIGCTRAGAIETTFREETETDLFGEQAVLCGGATALVKQGYETLVDAGYSPEMAYFECLNELKLIVDLMYEGGLSEMWNSVSDTAEYGGLTRGNQVIDESVREEMESILEGVQDGTFAREWISENQA... | 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... |
Q89HA2 | MKLRCPAAYGTSHVDDANMKKLRSRITTDGLDRAPHRAFMRAMGLDDAAIAKPMVGIVSMKGEQTPCNMTHDFQVAAAKTGIEEAGGTPREFSTVSVSDGISMNHEGMKFSLFSRELIADSIEAVVHGLAYDALIGYGGCDKTLPGVMMGMVRCNVPSIFIYGGSSLPGRVDGRTLTVLDSYEAVGSFMTGEIDSATLERIERACLPTIGACAGQFTANTMGMVSEAMGLTIPNVSMVPGVYAERAQISRRAGRLIMEMLERGGPLPRDIVTRKSLENGAAIVAATGGSTNAALHLPAIANEAGIAFTIDDVGEVFARTP... | 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)... |
B9DMJ2 | MRSDQIKKGDQQAPARSLLHATGQIKEPTDMNKPFVAICNSYIDIVPGHVHLRELANIAKEAIREAGAIPFEFNTIGVDDGIAMGHIGMRYSLPSREIIADAAETVINAHWFDGVFYIPNCDKITPGMLMAAVRTNVPAIFCSGGPMKAGLSAQGKALTLSSMFEAVGAFKGGSMTQEEFLDMEQNACPTCGSCAGMFTANSMNCLMEVLGLALPYNGTALAVSDQRREMIRQAAFQLVENIKNDLKPRDIVTKEALDDAFALDMAMGGSTNTVLHTLAIANEAGVDYDLKRINEIAKRTPYLSKIAPSSSYSMHDVHEA... | 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)... |
O76357 | MFVKSLVFLTIAVAYASADCLHCICMRESGCKPIGCNMDVGSLSCGYYQIKLPYYEDCGQPTKKSGETTEAAWKRCANDLSCATTCVENYYNRYKSQCAGTGQGACEVMARNHNGGPQGCKHSGTLGYWNGIKSCCGCS | Function: Has bacteriolytic activity against Gram-positive bacteria. Plays a role in defense against bacterial pathogens. Involved in pharyngeal grinder function by enabling proper lysis of ingested bacteria.
Catalytic Activity: Hydrolysis of (1->4)-beta-linkages between N-acetylmuramic acid and N-acetyl-D-glucosamine ... |
Q557F4 | MSSRDKQDSRKKEFKKSLDSETARRKREENSIGIRKNAREELMLKRRGIVQPNPSTSYQIIVPPEVQEQFQKYENETMENKIKNLPGLVTALNSNDQAYVYSSLVQFRKLLSIHAYPPIDQVIECGIIPKLNQLLQCNNPKVQFESAWALTNIASGNNRQTQTVMESGSVPIFIQLLCAETTDEVKEQCAWALGNIAGDTVDSRNYLLKYGAMNALIPLLHYGEDNGATTTSANSERKIGLIQNVVWTISNLCRGKPQPDFSVVSQCLPAINELIRIENLPSEIYGDLCWALSYLCDGPNTKIQAVIDSGVVPRLVKLLE... | Function: Functions in nuclear protein import via a substrate-importin alpha-beta transport complex that passes though the nuclear pore complexes (NPC). Binds specifically and directly to substrates containing either a simple or bipartite NLS motif (By similarity).
Sequence Mass (Da): 61592
Sequence Length: 550
Domain:... |
Q22560 | MGDEFRPSHEERSKMYKSNVRDQNEMRRKRREDEVQIRKNRRDEKFERNRQITVQRSLSHEETSELLKSVADGLQSMQETTIHEALTVLHENLNNTVWTIHVLVKVQILHKLSDVYCNRVISQTTRLLISRTLLKISGIDEVKYERYSSDDRCIQSLVFNISTYGSSEDILCDTFQSIACFIIRSITYRNLALDCAIVSELIDASTINMSIILHRSLMWLVFLFCEKLDRCSPHVDEIAPLLEIISNGIQSTDAMVQTDAASSCASLAEWPPIYHYMSDLKLCSKLVANLRNDKGNARPKVKAGINSIIQATGYFTEEMI... | Function: Binds specifically and directly to substrates containing either a simple or bipartite NLS motif. Promotes docking of import substrates to the nuclear envelope. Seems to act as a cytosolic receptor for both simple and bipartite NLS motifs (By similarity).
Sequence Mass (Da): 59925
Sequence Length: 524
Domain: ... |
P52292 | MSTNENANTPAARLHRFKNKGKDSTEMRRRRIEVNVELRKAKKDDQMLKRRNVSSFPDDATSPLQENRNNQGTVNWSVDDIVKGINSSNVENQLQATQAARKLLSREKQPPIDNIIRAGLIPKFVSFLGRTDCSPIQFESAWALTNIASGTSEQTKAVVDGGAIPAFISLLASPHAHISEQAVWALGNIAGDGSVFRDLVIKYGAVDPLLALLAVPDMSSLACGYLRNLTWTLSNLCRNKNPAPPIDAVEQILPTLVRLLHHDDPEVLADTCWAISYLTDGPNERIGMVVKTGVVPQLVKLLGASELPIVTPALRAIGNI... | Function: Functions in nuclear protein import as an adapter protein for nuclear receptor KPNB1. Binds specifically and directly to substrates containing either a simple or bipartite NLS motif. Docking of the importin/substrate complex to the nuclear pore complex (NPC) is mediated by KPNB1 through binding to nucleoporin... |
P52293 | MSTNENANLPAARLNRFKNKGKDSTEMRRRRIEVNVELRKAKKDEQMLKRRNVSSFPDDATSPLQENRNNQGTVNWSVEDIVKGINSNNLESQLQATQAARKLLSREKQPPIDNIIRAGLIPKFVSFLGKTDCSPIQFESAWALTNIASGTSEQTKAVVDGGAIPAFISLLASPHAHISEQAVWALGNIAGDGSAFRDLVIKHGAIDPLLALLAVPDLSTLACGYLRNLTWTLSNLCRNKNPAPPLDAVEQILPTLVRLLHHNDPEVLADSCWAISYLTDGPNERIEMVVKKGVVPQLVKLLGATELPIVTPALRAIGNI... | Function: Functions in nuclear protein import as an adapter protein for nuclear receptor KPNB1. Binds specifically and directly to substrates containing either a simple or bipartite NLS motif. Docking of the importin/substrate complex to the nuclear pore complex (NPC) is mediated by KPNB1 through binding to nucleoporin... |
Q02821 | MDNGTDSSTSKFVPEYRRTNFKNKGRFSADELRRRRDTQQVELRKAKRDEALAKRRNFIPPTDGADSDEEDESSVSADQQFYSQLQQELPQMTQQLNSDDMQEQLSATVKFRQILSREHRPPIDVVIQAGVVPRLVEFMRENQPEMLQLEAAWALTNIASGTSAQTKVVVDADAVPLFIQLLYTGSVEVKEQAIWALGNVAGDSTDYRDYVLQCNAMEPILGLFNSNKPSLIRTATWTLSNLCRGKKPQPDWSVVSQALPTLAKLIYSMDTETLVDACWAISYLSDGPQEAIQAVIDVRIPKRLVELLSHESTLVQTPAL... | Function: Functions in nuclear protein import as an adapter protein for importin beta nuclear receptors . Binds specifically and directly to substrates containing either a simple or bipartite NLS motif . Promotes docking of import substrates to the nuclear envelope . Together with importin beta KAP95, mediates nuclear ... |
C5DYQ1 | MLRVLPTSFKSISTRSAFRACQLSPLTVYCPLKSSQGTDIKSLEDLTKLKSLEGVDPELIRKLINERTIELNVQNELEMLKNLNKQEKMSQEVSLKRFVRPLWVFFLMSSTVYLILHYVWWKLEVVEKEKELQSHVESLEMELDQTLKSQNQNVSSSQNNGNNKTNDKPWYRKWFF | Function: Component of the INA complex (INAC) that promotes the biogenesis of mitochondrial F(1)F(0)-ATP synthase. INAC facilitates the assembly of the peripheral stalk and promotes the assembly of the catalytic F(1)-domain with the membrane-embedded F(0)-domain.
Location Topology: Single-pass membrane protein
Sequence... |
P40576 | MFMARQVLRNGLFLRSLAPIKITARTVASANAGIKRKSRFDKTMIKPLLLVMIFGSILNAVIAEKRNIIDMERKYKLKLDKLKELIRRVHDNNGKVDFDADDELKLVNLRLGIVGKNATGMKEDETDIVVPKEESLEEIWQSIIDEAKKEVIEKTPDAGVKNKEGIVTDLNVLKDLEKSKKEDEKVYLSGDVHMMMNQPGDLNEIAKEHDKIPKFL | Function: Component of the INA complex (INAC) that promotes the biogenesis of mitochondrial F(1)F(0)-ATP synthase. INAC facilitates the assembly of the peripheral stalk and promotes the assembly of the catalytic F(1)-domain with the membrane-embedded F(0)-domain.
Location Topology: Single-pass membrane protein
Sequence... |
Q24008 | MVQFLGKQGTAGELIHMVTLDKTGKKSFGICIVRGEVKDSPNTKTTGIFIKGIVPDSPAHLCGRLKVGDRILSLNGKDVRNSTEQAVIDLIKEADFKIELEIQTFDKSDEQQAKSDPRSNGYMQAKNKFNQEQTTNNNASGGQGMGQGQGQGQGMAGMNRQQSMQKRNTTFTASMRQKHSNYADEDDEDTRDMTGRIRTEAGYEIDRASAGNCKLNKQEKDRDKEQEDEFGYTMAKINKRYNMMKDLRRIEVQRDASKPLGLALAGHKDRQKMACFVAGVDPNGALGSVDIKPGDEIVEVNGNVLKNRCHLNASAVFKNV... | Function: Involved in the negative feedback regulation of the light-activated signaling cascade in photoreceptors through a calcium-mediated process. Interacts with tetrapeptide ligand located in C-terminal sequence of 3 key components of the visual cascade, tethering them and forming a macromolecular signaling phototr... |
P17181 | MMVVLLGATTLVLVAVAPWVLSAAAGGKNLKSPQKVEVDIIDDNFILRWNRSDESVGNVTFSFDYQKTGMDNWIKLSGCQNITSTKCNFSSLKLNVYEEIKLRIRAEKENTSSWYEVDSFTPFRKAQIGPPEVHLEAEDKAIVIHISPGTKDSVMWALDGLSFTYSLVIWKNSSGVEERIENIYSRHKIYKLSPETTYCLKVKAALLTSWKIGVYSPVHCIKTTVENELPPPENIEVSVQNQNYVLKWDYTYANMTFQVQWLHAFLKRNPGNHLYKWKQIPDCENVKTTQCVFPQNVFQKGIYLLRVQASDGNNTSFWSE... | Function: Together with IFNAR2, forms the heterodimeric receptor for type I interferons (including interferons alpha, beta, epsilon, omega and kappa) . Type I interferon binding activates the JAK-STAT signaling cascade, resulting in transcriptional activation or repression of interferon-regulated genes that encode the ... |
Q8I3Y8 | METYKGIQFFSNKGTVKNAFKKSNLGYEVMLDRKEDENFIYSNYEHVETQVEKDSKGMVVCKKYKNTYEILVEKVKEKRLGVLLVGIGGNNATTMLGGICANAKDLSYMNKCDLKRSNYLGSVFLSSNIRLGYNEKDKEHAYAPIYKLIDIYNPENIVYGGWDINNMNLKDCLVRNKVFDNEVIEKIKDDLDYVPLKSVYFKGNFIAGNQQRRVNNILYGKNKLEILEQVREQIRNFKKQNNLNELIVLWSGNTEKNIPHIPGVNDTFLNILHACKKNHESVSPSVIYALAAILENSPFINSSPQNTLVSAVVQLAQQKG... | Function: Key enzyme in myo-inositol biosynthesis pathway that catalyzes the conversion of glucose 6-phosphate to 1-myo-inositol 1-phosphate in a NAD-dependent manner (By similarity). Rate-limiting enzyme in the synthesis of all inositol-containing compounds (By similarity). De novo-synthesized myo-inositol is essentia... |
Q6AYK3 | MEPAAEILVDSPDVIFGPEAIEARYEYRTTRVSREGGVLRVRPTATRFTFRTARQVPRLGVMLVGWGGNNGSTLTAAVLANRLRLTWPTRTGRKEANYYGSLTQAGTVNLGLDGDGREVFVPFSALLPMVAPNDLVFDGWDISSLNLAEAMRRAQVLDCGLQEQLWPHMESLRPRPSVYIPEFIAANQTARADNLIPGTRAQQLEQIRKDIRDFRSSAGLDKVIVLWTANTERFCEVVPGRNDTAENLLRTIQLGLEVSPSTLFAVASILEGCAFLNGSPQNTLVPGALELASQRHVFVGGDDFKSGQTKVKSVLVDFLI... | Function: Key enzyme in myo-inositol biosynthesis pathway that catalyzes the conversion of glucose 6-phosphate to 1-myo-inositol 1-phosphate in a NAD-dependent manner . Rate-limiting enzyme in the synthesis of all inositol-containing compounds (By similarity).
PTM: Phosphorylation at Ser-524 does not appear to affect e... |
P42803 | MFIEKFRVESPNVKYGDGEIESVYSYETTELVHEVRNGSYQWVVKPKSVQYQFKTDTRVPRLGVMLVGWGGNNGSTLTAGVIANREGISWVTKEKVQQANYFGSLTQSSSIRVGSFNGEEIYAPFKSLLPMVNPDEIVFGGWDISDMNLADAMGRAKVLDIDLQKQLRPYMESMVPLPGIYNPDFIAANQGSRANNVIKGPKKQQVQRIIDDIREFKEREKVEKVVVLWTANTERYSDLVVGLNDTMENLLAAVERDEAEISPSSLYALACIMEGVPFVNGSPQNTFVPGLIEMAIKRNSLIGGDDFKSGQTKMKSVLVD... | Function: Key enzyme in myo-inositol biosynthesis pathway that catalyzes the conversion of glucose 6-phosphate to 1-myo-inositol 1-phosphate in a NAD-dependent manner.
Catalytic Activity: D-glucose 6-phosphate = 1D-myo-inositol 3-phosphate
Sequence Mass (Da): 56386
Sequence Length: 510
Pathway: Polyol metabolism; myo-i... |
Q5QQ46 | MPAVRTKSGHGVEYTDEAITATYSYNTTRVEKEANGDVTVQPIQLHLKFRTQRKVQRTGVMLIGWGGNNGTTVTAALMAHKHRXSWRTKTGTKQPDYLGSITQSSTMSVGLTSEMEEVFVPMKALVPMINPAELVIGGWDCSGMNIADAMRRAQVLDVTLQDALYNYLKDMHPLPAAFDLDFVAENQLSRADNIMQTKNKWESVEQLRADIRNFREKNSLEEVIVLWTANTERFSEHITGVHDTADHLIDAIRRNENEIAPSVLYATAAIMEGCSYVNGAPQNTLCAGLIELARRHGVFVVGDDFKSGQTKVKSGLVEFF... | Function: Key enzyme in myo-inositol biosynthesis pathway that catalyzes the conversion of glucose 6-phosphate to 1-myo-inositol 1-phosphate in a NAD-dependent manner . Rate-limiting enzyme in the synthesis of all inositol-containing compounds (By similarity). De novo-synthesized myo-inositol is essential for incorpora... |
P11986 | MTEDNIAPITSVKVVTDKCTYKDNELLTKYSYENAVVTKTASGRFDVTPTVQDYVFKLDLKKPEKLGIMLIGLGGNNGSTLVASVLANKHNVEFQTKEGVKQPNYFGSMTQCSTLKLGIDAEGNDVYAPFNSLLPMVSPNDFVVSGWDINNADLYEAMQRSQVLEYDLQQRLKAKMSLVKPLPSIYYPDFIAANQDERANNCINLDEKGNVTTRGKWTHLQRIRRDIQNFKEENALDKVIVLWTANTERYVEVSPGVNDTMENLLQSIKNDHEEIAPSTIFAAASILEGVPYINGSPQNTFVPGLVQLAEHEGTFIAGDD... | Function: Key enzyme in myo-inositol biosynthesis pathway that catalyzes the conversion of glucose 6-phosphate to 1-myo-inositol 1-phosphate in a NAD-dependent manner (Ref.6, Ref.8, PubMed:23902760, PubMed:14684747). Rate-limiting enzyme in the synthesis of all inositol-containing compounds (By similarity).
PTM: Phosph... |
Q38862 | MFIESFKVESPNVKYTENEINSVYDYETTEVVHENRNGTYQWVVKPKTVKYDFKTDTRVPKLGVMLVGWGGNNGSTLTAGVIANKEGISWATKDKVQQANYFGSLTQASSIRVGSYNGEEIYAPFKSLLPMVNPEDVVFGGWDISDMNLADAMARARVLDIDLQKQLRPYMENMIPLPGIYDPDFIAANQGSRANSVIKGTKKEQVDHIIKDMREFKEKNKVDKLVVLWTANTERYSNVIVGLNDTTENLLASVEKDESEISPSTLYAIACVLEGIPFINGSPQNTFVPGLIELAISKNCLIGGDDFKSGQTKMKSVLVD... | Function: Key enzyme in myo-inositol biosynthesis pathway that catalyzes the conversion of glucose 6-phosphate to 1-myo-inositol 1-phosphate in a NAD-dependent manner.
Catalytic Activity: D-glucose 6-phosphate = 1D-myo-inositol 3-phosphate
Sequence Mass (Da): 56337
Sequence Length: 510
Pathway: Polyol metabolism; myo-i... |
Q9Y5U4 | MAEGETESPGPKKCGPYISSVTSQSVNLMIRGVVLFFIGVFLALVLNLLQIQRNVTLFPPDVIASIFSSAWWVPPCCGTASAVIGLLYPCIDRHLGEPHKFKREWSSVMRCVAVFVGINHASAKVDFDNNIQLSLTLAALSIGLWWTFDRSRSGFGLGVGIAFLATVVTQLLVYNGVYQYTSPDFLYVRSWLPCIFFAGGITMGNIGRQLAMYECKVIAEKSHQE | Function: Oxysterol-binding protein that mediates feedback control of cholesterol synthesis by controlling both endoplasmic reticulum to Golgi transport of SCAP and degradation of HMGCR . Acts as a negative regulator of cholesterol biosynthesis by mediating the retention of the SCAP-SREBP complex in the endoplasmic ret... |
Q91WG1 | MAEGETESPRPKKCGPYISSVTSQSVNVVIRGVVLFFIGVFLALVLNLLQIQRNVTLFPPDVITSIFSSAWWVPPCCGTASAVIGLLYPCIDRHLGEPHKFKREWSSVMRCVAVFVGINHASAKVDFDNNFQFSLTLAALSVGLWWTFDRSRSGFGLGVGIAFLATVVTQLLVYNGVYQYTSPDFLYVRSWLPCIFFAGGITMGNIGRQLAMYECKVIAEKSHQE | Function: Oxysterol-binding protein that mediates feedback control of cholesterol synthesis by controlling both endoplasmic reticulum to Golgi transport of SCAP and degradation of HMGCR . Acts as a negative regulator of cholesterol biosynthesis by mediating the retention of the SCAP-SREBP complex in the endoplasmic ret... |
Q80UA9 | MAEGETESPRPKKRGPYISSVTSQSVNVVIRGVVLFFIGVFLALVLNLLQIQRNVTLFPPDVITSIFSSAWWVPPCCGTASAVIGLLYPCIDRHLGEPHKFKREWSSVMRCVAVFVGINHASAKVDFDNNFQFSLTLAALSVGLWWTFDRSRSGFGLGVGIAFLATVVTQLLVYNGVYQYTSPDFLYVRSWLPCIFFAGGITMGNIGRQLAMYECKVIAEKSHQE | Function: Oxysterol-binding protein that mediates feedback control of cholesterol synthesis by controlling both endoplasmic reticulum to Golgi transport of SCAP and degradation of HMGCR. Acts as a negative regulator of cholesterol biosynthesis by mediating the retention of the SCAP-SREBP complex in the endoplasmic reti... |
A1T557 | MRLRISEAVVLFLLGAVAALIGDHSHVVTGTTVYHTDAVPFVWSSPFWFPILVGAATASLAELRLHLPAPRDGVTARQALGGVAAVVGTYVTTALVHAFPVVPVTALVCAAAAITWCVLGDGPGAACGVVIAVIGPAVEIALVQLGVFAYHPDSDGLFGVAPFLAPLYFAFGVVAALLGELAVARRPQLGPPVCDTVSRGPGAG | Function: Diacylglycerol-binding protein.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 20710
Sequence Length: 204
Domain: The KxHxx motif mediates association with the coatomer complex.
Subcellular Location: Membrane
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O23492 | MVEGGIAKADKTEFTECWRTTWKTPYIMRLALSAGIGGLLFGYDTGVISGALLFIKEDFDEVDKKTWLQSTIVSMAVAGAIVGAAVGGWINDKFGRRMSILIADVLFLIGAIVMAFAPAPWVIIVGRIFVGFGVGMASMTSPLYISEASPARIRGALVSTNGLLITGGQFFSYLINLAFVHTPGTWRWMLGVAGVPAIVQFVLMLSLPESPRWLYRKDRIAESRAILERIYPADEVEAEMEALKLSVEAEKADEAIIGDSFSAKLKGAFGNPVVRRGLAAGITVQVAQQFVGINTVMYYSPSIVQFAGYASNKTAMALSL... | Function: Plasma membrane inositol-proton symporter. Mediates high-affinity myoinositol-proton symport across the plasma membrane. Active with myoinositol, scylloinositol and D-chiroinositol. Low activity with mucoinositol and alloinositol.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 62892
Sequen... |
Q9VFS6 | MLRQNLLDQLKHFIETVSNGHSCPQLLTSPNLIKLALGFLEELPATRDIVFEYFALLAEISVQLYVSPEMADPKTGMPVSQVKLAGNRQQQQRAPEYEAFNLVKTALQSLVWKGPPAWSPLIANWSLELVAKLSDKYTQRRMTITASCNYWLECSAMHGLMTLINSCFRKLTQPEEEACVEIMLNAFHRFPMTFDWIVARLGGCFPYKIIMQILQCGIKRFVDDYRCHLDSEAGILDYMTSCHEQHLRAAFREMLREGFAPKKPLDVAVVPFLLITTNYSDTILQSLVNVLVEIYTEDMCEVIVQKAPLWLSNKMFAGMQ... | Function: Component of the Integrator complex, a complex involved in the transcription of small nuclear RNAs (snRNA) and their 3'-box-dependent processing . Involved in the 3'-end processing of the U7 snRNA, and also the spliceosomal snRNAs U1, U2, U4 and U5 . May mediate recruitment of cytoplasmic dynein to the nuclea... |
Q6P9B9 | MSALCDPPGAPGPPGPAPATHGPAPLSAQELSQEIKAFLTGVDPILGHQLSAREHARCGLLLLRSLPPARAAVLDHLRGVFDESVRAHLAALDETPVAGPPHLRPPPPSHVPAGGPGLEDVVQEVQQVLSEFIRANPKAWAPVISAWSIDLMGQLSSTYSGQHQRVPHATGALNELLQLWMGCRATRTLMDIYVQCLSALIGSCPDACVDALLDTSVQHSPHFDWVVAHIGSSFPGTIISRVLSCGLKDFCVHGGAGGGAGSSGGSSSQTPSTDPFPGSPAIPAEKRVPKIASVVGILGHLASRHGDSIRRELLRMFHDS... | Function: Component of the Integrator (INT) complex, a complex involved in the small nuclear RNAs (snRNA) U1 and U2 transcription and in their 3'-box-dependent processing. The Integrator complex is associated with the C-terminal domain (CTD) of RNA polymerase II largest subunit (POLR2A) and is recruited to the U1 and U... |
Q8UVX8 | MGLLSVDLLITLQILPWFFSNCLFLALYDSVVLLKHVILLLSCSKSSRGEWRRMLTSEGLRTVWNSFLLDAYKQVKLGGDAPNSKVVRVTSGCCRRRSFSGKGESECHLLDFASSNRPLVVNFGSATUPPFISQLPTFRKLVEEFSDVADFLLVYIDEAHPADGWAAPGVATKSFEVKKHRSQEERCVAAHKLLEHFSLPPQCQVVADCMDNNTNVAYGVSFERVCIVQRQKIAYLGGKGPFFYNLKEVRHWLEQTYRKRUVPTCELIM | Function: Responsible for the deiodination of T4 (3,5,3',5'-tetraiodothyronine) into T3 (3,5,3'-triiodothyronine).
Catalytic Activity: 3,3',5-triiodo-L-thyronine + A + H(+) + iodide = AH2 + L-thyroxine
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 30513
Sequence Length: 269
Subcellular Location: M... |
P70551 | MGLLSVDLLITLQILPVFFSNCLFLALYDSVILLKHVALLLSRSKSTRGEWRRMLTSEGLRCVWNSFLLDAYKQVKLGEDAPNSSVVHVSNPEAGNNCASEKTADGAECHLLDFASAERPLVVNFGSATUPPFTRQLPAFRQLVEEFSSVADFLLVYIDEAHPSDGWAVPGDSSMSFEVKKHRNQEDRCAAAHQLLERFSLPPQCQVVADRMDNNANVAYGVAFERVCIVQRRKIAYLGGKGPFSYNLQEVRSWLEKNFSKRUILD | Function: Catalyzes the deiodination of T4 (3,5,3',5'-tetraiodothyronine) into T3 (3,5,3'-triiodothyronine). Essential for providing the brain with appropriate levels of T3 during the critical period of development.
PTM: Ubiquitinated by MARCHF6, leading to its degradation by the proteasome. Deubiquitinated by USP20 an... |
P55073 | MPRQATSRLVVGEGEGSQGASGPAATMLRSLLLHSLRLCAQTASCLVLFPRFLGTAFMLWLLDFLCIRKHFLGRRRRGQPEPEVELNSEGEEVPPDDPPICVSDDNRLCTLASLKAVWHGQKLDFFKQAHEGGPAPNSEVVLPDGFQSQHILDYAQGNRPLVLNFGSCTUPPFMARMSAFQRLVTKYQRDVDFLIIYIEEAHPSDGWVTTDSPYIIPQHRSLEDRVSAARVLQQGAPGCALVLDTMANSSSSAYGAYFERLYVIQSGTIMYQGGRGPDGYQVSELRTWLERYDEQLHGARPRRV | Function: Responsible for the deiodination of T4 (3,5,3',5'-tetraiodothyronine) into RT3 (3,3',5'-triiodothyronine) and of T3 (3,5,3'-triiodothyronine) into T2 (3,3'-diiodothyronine). RT3 and T2 are inactive metabolites. May play a role in preventing premature exposure of developing fetal tissues to adult levels of thy... |
P49898 | MLPAPHTCCRLLQQLLACCLLLPRFLLTVLLLWLLDFPCVRRRVIRGAKEEDPGAPEREDPPLCVSDTNRMCTLESLKAVWYGQKLDFFKSAHLGGGAPNTEVVTLEGQRLCRILDFSKGHRPLVLNFGSCTUPPFMARLQAYQRLAAQRLDFADFLLVYIEEAHPCDGWLSTDAAYQIPTHQCLQDRLRAAQLMLQGAPGCRVVADTMTNASNAAYGAYFERLYVILDGKVVYQGGRGPEGYKIGELRNWLDQYQTRATGNGALVIQV | Function: Responsible for the deiodination of T4 (3,5,3',5'-tetraiodothyronine) into RT3 (3,3',5'-triiodothyronine) and of T3 (3,5,3'-triiodothyronine) into T2 (3,3'-diiodothyronine). May play a major role in regulating intracellular T3 levels in developing tadpoles.
Catalytic Activity: 3,3',5'-triiodo-L-thyronine + A ... |
Q6U6H1 | MHNLLEIKIIRFLRNVFYFLHVLFNECLDTLKAYYKRWRGMKSEKPLDPSSRRARIIQATGVDLSRDPAMQSLRGVYHMAKSILYADVLRTAVRGGNAPNSSLVNYRTKEKCNILDFMKPGRPLVVNFGSCSUPPFMASFEIFSRIIDSYHERADFLTVYIEEAHSSDLWALKNNKYSIPSHITFEDRMEAAAIFKKSVSFECAFAVDTMKDETNLSYGALPERTAIILDGKVQYIGGIGPFNYDLVELEKELIAVLKK | Function: Responsible for the deiodination of T4 (3,5,3',5'-tetraiodothyronine) into T3 (3,5,3'-triiodothyronine). Can also produce 3,3'-diiodothyronine from reverse T3 (rT3, 3,3',5'-triiodothyronine). Does not have significant inner-ring deiodination activity for T4, T3 or rT3.
Catalytic Activity: 3,3',5-triiodo-L-thy... |
Q8NTY7 | MSKSLRVGVVGAGAMGADHIDRINNRTSGAHISAIIEPDAARAAAAAEDAPGAQAFTRIEDAIAADAVDAVLIAVPGQFHEPVLVPALEAGLPILCEKPLTPDSESSLRIVELEQKLDKPHIQVGFMRRFDPEYNNLRKLVESGEAGELLMLRGLHRNPSVGESYTQSMLITDSVVHEFDVIPWLAGSRVVSVEVKYPKTSSLAHSGLKEPILVIMELENGVLVDVEMNVNIQFGYQVATEAVFEKGLARIGQPSGMQRWRDGEFLINEHTDFTTRFATAYDRQIQSWVDAVHEGTLVAGPNAWDGYLVALSCEAGVKAL... | Function: Involved in the oxidation of myo-inositol (MI) to 2-keto-myo-inositol (2KMI or 2-inosose).
Catalytic Activity: myo-inositol + NAD(+) = H(+) + NADH + scyllo-inosose
Sequence Mass (Da): 36431
Sequence Length: 337
EC: 1.1.1.18
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A6WFC5 | MRVAVLGVGMMGQDHARRLATLTKGAQLVAVSDVDAARTDAVAAELGVRAVHDPAAAIADPEVDAVVIATPGFTHEGLVLEAIAAGKPTLCEKPLTTSPETARAVVEAERALGRPLVQVGFMRRFDAEYEQLRALVASRELGRPLFLHCVHRNATTPPNFNSEMLILDSVVHEVDIARFLLGEEITAITVLTPGRTAHAPEGLQDPQFVLMETASGTLVDVEIFVNTTFGYEVRTELVAERGSAMTGLGVGLVQHSAAGWGGRIAADFKQRFGAAYDTEFQRWVDAVRSGAGVDGPGVWDGYAAAAVCAAGVQSLRTGRR... | Function: Involved in the oxidation of myo-inositol (MI) to 2-keto-myo-inositol (2KMI or 2-inosose).
Catalytic Activity: myo-inositol + NAD(+) = H(+) + NADH + scyllo-inosose
Sequence Mass (Da): 34862
Sequence Length: 329
EC: 1.1.1.18
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A5YBJ7 | MVVKVGVIGTGAMGRAHIDRLTNVLTGAEVVAVTDIDHEAAEAAVRDFHLNAKVYPDDTSLLQDPDIDAVFVVSFGGAHEATVLKALDTDKFIFTEKPLATTLEGAKRIVDKELTKSKKVIQVGFMRRYDQGIRALKEKLDTGIIGAPLVVRASHINPNVASNYSNEMAITDTLIHEIDEMHWLLDDEYTSIQITYPRQSAEVRNEGLHDPQLATLTTKKGTVIQVLVHVTAQYGYEVKLEVIGETGELQLPNYGLGPILRSNANQQTAVEMSWINRFIQAYNTEVQEFIDQVAKSEPPVGPSAWDGYIAAITAAAANRS... | Function: Involved in the oxidation of myo-inositol (MI) and D-chiro-inositol (DCI) to 2-keto-myo-inositol (2KMI or 2-inosose) and 1-keto-D-chiro-inositol (1KDCI), respectively.
Catalytic Activity: myo-inositol + NAD(+) = H(+) + NADH + scyllo-inosose
Sequence Mass (Da): 37964
Sequence Length: 346
Pathway: Polyol metabo... |
Q88S38 | MAEAHVTKVGIVGIGFIGSDHLHRLTKTVANVDVTAVCDIVPGKAQKALDQQGLTATTYEDYHDLVNDPNVEVVVCTANNEAHYEIVMAALKAGKFTFCEKPLALDAKQCMDIIDSEKKLGRRMLQVGFMRHYAPEYVQMKKMIDDGVIGKPLMMDQRHYNQTQPEEYDSSRSIIETAIHEIDIDHWLVNDDYANIRVFSPKQTRHVQNAKIQDPQIVMIETKSGINIINEVFVRCQYGYDIKCDVIGEEGVLELPTVPQVATRLNAQYSTAILTDWKARFESAYDIEFRDFINHVSQNESPVGPSAWDGYIAAVTADAA... | Function: Involved in the oxidation of myo-inositol (MI) and D-chiro-inositol (DCI) to 2-keto-myo-inositol (2KMI or 2-inosose) and 1-keto-D-chiro-inositol (1KDCI), respectively.
Catalytic Activity: myo-inositol + NAD(+) = H(+) + NADH + scyllo-inosose
Sequence Mass (Da): 39180
Sequence Length: 350
Pathway: Polyol metabo... |
Q6WAU1 | MAEVQRYALVTGANKGIGFEICRQLAEKGIIVILTSRNEKRGLEARQKLLKELNVSENRLVFHQLDVTDLASVAAVAVFIKSKFGKLDILVNNAGVSGVEMVGDVSVFNEYIEADFKALQALEAGAKEEPPFKPKANGEMIEKFEGAKDCVVTNYYGPKRLTQALIPLLQLSPSPRIVNVSSSFGSLLLLWNEWAKGVLGDEDRLTEERVDEVVEVFLKDIKEGKLEESQWPPHFAAERVSKAALNAYTKIAAKKYPSFRINAICPGYAKTDITFHAGPLSVAEAAQVPVKLALLPDGGPSGCFFPRDKALALY | Function: Monoterpene synthase that catalyzes the specific reduction of the 1(2)-double bond of (-)-isopiperitenone to produce (+)-cis-isopulegone. Does not catalyze the reverse reaction. Unable to reduce (+)-pulegone, (+)-cis-isopulegone, (-)-menthone or the 1,2-double bond of (-)-carvone. Able to utilize NADH with 20... |
Q75EW5 | MVKIIGKGGANYVLAFGNDNDDLYRICVRGRSLRENNRSTVDNYHYALEVVKPQLGEFVCRMELVDLPVCDSLRQVLKSKIEVWDATTVTCLKMPNLVPAGSLSHTVDHFTKIHIGERAIVWEFKPKWLSGNDKYCRNCTLNLLRGQTSISYCHAQLLNPGQAGPILKSLFAGLNVPPAFIEDMEAYIAQPCSVLQRLRVAQEQVDASLGPLDQPDTAASPERCLSMTLKDVSCFVSWHKDASPVAVVVDLDMKPAAKSAHWTALQEQLDRFQPQVRH | Function: Has kinase activity and phosphorylates inositol-1,3,4,5,6-pentakisphosphate (Ins(1,3,4,5,6)P5) to produce 1,2,3,4,5,6-hexakisphosphate (InsP6), also known as phytate.
Catalytic Activity: 1D-myo-inositol 1,3,4,5,6-pentakisphosphate + ATP = 1D-myo-inositol hexakisphosphate + ADP + H(+)
Sequence Mass (Da): 31047... |
Q59KN8 | MEISKITSPEDWEYFAKGAANILFKYTGNNDYLKRKLLRLRLLKQEEEYISTCELYDFIELRCKDLFPNQIIDIQLTVLDSNFTNKLNSQGNKLMLNERYGLLLPNILDGDYRKISLSQKCQLYFNDNDQDINSVIFEIKPKWLYDNYTDNYCRTCSLNQLKKVPRHFCPLDLLYTETIEQGLNDLFAPIPQDIYAKIEKLIPLKKLTTIYFNNPDNVFQKLKQYQKINNKNDLIKNLTSYSDVSQNLSLVMTLRDVGLFIKIEKFDKNNHIHTSHNNIKNVYRINDNKSNGTKDQDQEIGTNDEEDNDEKFLITCNIYD... | Function: Has kinase activity and phosphorylates inositol-1,3,4,5,6-pentakisphosphate (Ins(1,3,4,5,6)P5) to produce 1,2,3,4,5,6-hexakisphosphate (InsP6), also known as phytate.
Catalytic Activity: 1D-myo-inositol 1,3,4,5,6-pentakisphosphate + ATP = 1D-myo-inositol hexakisphosphate + ADP + H(+)
Sequence Mass (Da): 42920... |
Q6FRN1 | MLVAEGGANILLELDHRGVLYRCNVRDKSLKVNNEYTYKNYRYINQVVRPLLGDCIPEMELVDIPYDRISGIIGDFVGDPDSDHVSALTIKNLRPTNVYGEKIRYDDHFTKVYHDDTMEHILVEIKPKWLHHAKFCRNCTHNNLKNRKIPYCYALMVVDPSHVSDMLLHTGIAFPRKFLIKFVDYFSKSDNILAKLHDIQKNLDSNVSMNDIKSIDDVSDAFLLNMTLKDVSCFIEWTREPDSLEVNVVDVDMKLVSKLDHWVNTHIQLSNSSNLVHH | Function: Has kinase activity and phosphorylates inositol-1,3,4,5,6-pentakisphosphate (Ins(1,3,4,5,6)P5) to produce 1,2,3,4,5,6-hexakisphosphate (InsP6), also known as phytate.
Catalytic Activity: 1D-myo-inositol 1,3,4,5,6-pentakisphosphate + ATP = 1D-myo-inositol hexakisphosphate + ADP + H(+)
Sequence Mass (Da): 32200... |
Q6CNG8 | MTLLFVGRGNANVCYLLSGEVYRISLRHQKLSRNNAYVQDNFQFIDSKIRSLPMLADVVVSMRLEEVFVDTKWINVLKDENILIDDSHMQCIVMPLLHAKDSTCEQLDHFNQIYRCSLNDAITWEFKPKWLYQSSDYCRNCTHNSLKGRDIEYCFLHDPELIIETLFAGRQVPEEFLDDILQYLQSSDSITQRLYAAQRFVKDDLSTLMTLRDVTCFLTWSRNTRSVKATIIDVDQKPANKLRHWQSTESALASFPGKKKAHFNHQ | Function: Has kinase activity and phosphorylates inositol-1,3,4,5,6-pentakisphosphate (Ins(1,3,4,5,6)P5) to produce 1,2,3,4,5,6-hexakisphosphate (InsP6), also known as phytate.
Catalytic Activity: 1D-myo-inositol 1,3,4,5,6-pentakisphosphate + ATP = 1D-myo-inositol hexakisphosphate + ADP + H(+)
Sequence Mass (Da): 31066... |
B8AVX5 | MEVVLHEGDAKDWVYKGEGAANLILSYTGSSPSMLGKVLRVKKILKDKGQPAPNCIVFSSHEEHLWGKIPGLLESVKNDCLPQAYATIVMSQHLGANHVDGGVRVRVSKNFFELAGKNVLDNRPAWRVNASAIDAGADSALLISDHTLFSGNPRGSSCIAVEIKAKCGFLPSSEYISKENSIKKQVTRYKMHQHLKFHLGEISKTSEYDPLDLFSGSKERIHMAIKSFFSTPQNNFRIFVDGSLVFGGMGGGADSVHPNETEKCLEDLSKVTGLQLSDFIELLSEAIFKSGVLGKLLATQKLDDHDIEGAIHLYYNIISQ... | Cofactor: Binds 1 zinc ion per subunit.
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). Phytate is a regulator of intracellular signaling, a highly abundant animal antinutrient, and a phosphate store in plant seeds. Also phosphorylates Ins(1,3,4,6)P4 and Ins(1,4,5,... |
Q9USK0 | MPLKNYTKTTSKKEPKQLDIAASDQQIEQWSDQIHKLDKAIRSTIDNSRLFYDAWRCMVCIAPSVTASWISLYRQLPPEKQPAASVGTLVDWNKALERQRREVLLALQNFHVIVIAPCKEVKGYVKKAVEMIKRRDKKVKELEKIQKELLVVYELPDPETKKSKIKALQSQLVRVNGELDDLQKHLTLSFPTLIAKSRVFFGQLMKHFYCLQLQMFRKMHNIVRPWDCFQDDIPQTWLVEFSSVCQAAESISLIAVNNNRPPVELPKSGDVLSNREWEAGKIDAMNSLIAQNLHTSASQVSLSPMASTASSSVTNSPVDT... | Function: Has kinase activity and phosphorylates inositol-1,3,4,5,6-pentakisphosphate (Ins(1,3,4,5,6)P5) to produce 1,2,3,4,5,6-hexakisphosphate (InsP6), also known as phytate.
Catalytic Activity: 1D-myo-inositol 1,3,4,5,6-pentakisphosphate + ATP = 1D-myo-inositol hexakisphosphate + ADP + H(+)
Sequence Mass (Da): 72766... |
Q6C6Q7 | MSSLPTPLPPYKWTLLTAGNANVVYKSDETDLLLRLRRNRNAPSTAEVDEYLTGTIRPAIGPFLFHYTVVNLPLGFLESLPEAENLDLGEPLGLLMENLGPKPNETNVLKSHAVKINYSDNWESYTVELKPKWLLQSPTAPKDSINCRTCALQLKREKPRICPLKLFNEDEQTSLQALEDVFPGTQKQFEPLAKFFSNSELFAEIRHMQHGDELGILGYANYVQVPPQFVTAMTMRDVSLFVHVQGDSVNGKIVDADLKSVSEKRDYWASLETDLIEGGWYEKPGTNCLLRN | Function: Has kinase activity and phosphorylates inositol-1,3,4,5,6-pentakisphosphate (Ins(1,3,4,5,6)P5) to produce 1,2,3,4,5,6-hexakisphosphate (InsP6), also known as phytate.
Catalytic Activity: 1D-myo-inositol 1,3,4,5,6-pentakisphosphate + ATP = 1D-myo-inositol hexakisphosphate + ADP + H(+)
Sequence Mass (Da): 32942... |
Q06667 | MQVIGRGGANILIDYGDPTWLWRCCIRWPDLLSSNNSYTIKNISYIKDYVEPLLHGLLCPMYLIDVDIEAIRPILSDFILNLDDKVVKVIKIKNLTNNTSNLILNNHFLKSYCSQNLQTVILELKPKWLYYDTDYCRNCTHNAFKGRGTKYCYNQLLMNPAHLELIFGECNIFPVKFKDAMHEYLRNDNNIFKILYDLQKKLTKNTTPISDIKSINDVNDEHLLLMTLRDVTCFIEWNSAENALHVNIIDVDLKPKEKWTHWTKTYSQLTSSQKIYHTSNK | Function: Has kinase activity and phosphorylates inositol-1,3,4,5,6-pentakisphosphate (Ins(1,3,4,5,6)P5) to produce 1,2,3,4,5,6-hexakisphosphate (InsP6), also known as phytate.
Catalytic Activity: 1D-myo-inositol 1,3,4,5,6-pentakisphosphate + ATP = 1D-myo-inositol hexakisphosphate + ADP + H(+)
Sequence Mass (Da): 32918... |
A2X5H5 | MASDLRPPEHQVAGHRASADKLGPLVDGEGLFYKPLQAGERGEHEAAFYAAFTAHPAVPPRVRGAFFPRFHGTRFLPAPASPGGAPYPHIVLDDLLAGLPSPCVADVKIGACTWPPRSPDPYVAKCLAKDRETTSALLGFRVSGVRVVDARGGAVWRPDRSELKGIDAAGVRRVLRRYVSTGGGDGLDCALAAAVYGGEGGVLAQLRELKAWFEEQTLYHFYSASILFGYDANAAAAAAPGGGSGGVRVKLVDFAHVDDGDGVIDHNFLGGLCSLIKFIGDIVAEVTEKASSDHS | Function: Inositol phosphate kinase with a broad substrate specificity. Phosphorylates inositol 1,4,5-trisphosphate (Ins(1,4,5)P3), inositol 1,4,5,6-tetrakisphosphate (Ins(1,4,5,6)P4), inositol 1,3,4,5-tetrakisphosphate (Ins(1,3,4,5)P4), inositol 1,3,4,6-tetrakisphosphate (Ins(1,3,4,6)P4) and inositol 1,2,3,4,6-pentaki... |
Q9PLF1 | MSKTPLSIVHPWHGPVLTRDDYESLCCYIEITPSDSVKFELDKETGLLKVDRPQKFSNFCPCLYGLLPKTYCGDLSGEYSGQQSNRDNIKGDGDPLDICVLTEKNITQGNILLQARPIGGIRILDSGEADDKIIAVLEDDLVYGAMEDISDCPGSVLDMIQHYFLTYKATPESLIQAKPAKIEIIGLYGKKEAQKVIRLAHEDYCNLFM | Function: Catalyzes the hydrolysis of inorganic pyrophosphate (PPi) forming two phosphate ions.
Catalytic Activity: diphosphate + H2O = H(+) + 2 phosphate
Sequence Mass (Da): 23310
Sequence Length: 209
Subcellular Location: Cytoplasm
EC: 3.6.1.1
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Q9Z6Y8 | MSKKPLYVAHPWHSPTLTQDNYESLCCYIEITPYDSVKFELDKATGLLKVDRPQKFSNFCPCLYGLLPQTYCGTASGNYSGEQTRREGIQGDKDPLDVCVLTEKNIHHGNILLQARPIGGLRIIDSGEADDKIIAVLEDDLVFAEIEDISDCPGTVLDMIQHYFLTYKATPNHLIKGSPAKIEIVGIYGKKEAQKVIQLAHEDYLSYIGDTAEVN | Function: Catalyzes the hydrolysis of inorganic pyrophosphate (PPi) forming two phosphate ions.
Catalytic Activity: diphosphate + H2O = H(+) + 2 phosphate
Sequence Mass (Da): 23981
Sequence Length: 215
Subcellular Location: Cytoplasm
EC: 3.6.1.1
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Q8XIQ9 | MKDVIYITGHKNPDSDSICAALAYAEFKNKTQDTPAIPVRLGNVSQETQYILDYFGVEAPQFLETVKLKVEDLEMDKIAPLAPEVSLKMAWNIMRDKNLKSIPVADGNNHLLGMLSTSNITATYMDIWDSNILAKSATSLDNILDTLSAEAQNINEERKVFPGKVVVAAMQAESLKEFISEGDIAIAGDRAEIQAELIELKVSLLIVTGGHTPSKEIIELAKKNNITVITTPHDSFTASRLIVQSLPVDYVMTKDNLVAVSTDDLVEDVKVTMSETRYSNYPVIDENNKVVGSIARFHLISTHKKKVIQVDHNERGQSVH... | Cofactor: Binds tightly a transition metal ion; prefers Co(2+) over Mn(2+).
Catalytic Activity: diphosphate + H2O = H(+) + 2 phosphate
Sequence Mass (Da): 60528
Sequence Length: 549
EC: 3.6.1.1
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Q8NM79 | MSIEVTVEIPKGSRNKYEIDHETGKVYLDRYLFTPMAYPLDYGYIDHTLGEDGDPLDALVILPESVFPAVVVKSRIIGVFKMTDEAGGDDKLLSVLDDPRYDHIQDISDVSDFLKDEIEHFFVHYKDLEKGKHVDGSGWGDKAEAEKIHAEAIDRYKA | Function: Catalyzes the hydrolysis of inorganic pyrophosphate (PPi) forming two phosphate ions.
Catalytic Activity: diphosphate + H2O = H(+) + 2 phosphate
Sequence Mass (Da): 17905
Sequence Length: 158
Subcellular Location: Cytoplasm
EC: 3.6.1.1
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P19371 | NYTIGNDNVLTEPLSEIKTAGLMYKMGVQ | Function: Inorganic pyrophosphatase is an essential enzyme for the activation of sulfate by sulfate reducing bacteria. This is a high activity pyrophosphatase.
Catalytic Activity: diphosphate + H2O = H(+) + 2 phosphate
Sequence Mass (Da): 3201
Sequence Length: 29
Subcellular Location: Periplasm
EC: 3.6.1.1
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O77460 | MLAKITRSSFYASRAVGRLSGSIPTSPAALASNCRYIQIERKRTKSHEMALYETVEKGAKNSPSYSLYFKNKCGNVISPMHDIPLYANEEKTIYNMVVEVPRWTNAKMEISLKTPMNPIKQDIKKGKLRFVANCFPHKGYIWNYGALPQTWENPDHIEPSTGCKGDNDPIDVIEIGYRVAKRGDVLKVKVLGTIALIDEGETDWKIIAIDVNDPLASKVNDIADVDQYFPGLLRATVEWFKIYKIPDGKPENQFAFNGDAKNADFANTIIAETHKFWQNLVHQSPASGSISTTNITNRNSEHVIPKEEAEKILAEAPDGG... | Function: Component of NURF (nucleosome remodeling factor), a complex which catalyzes ATP-dependent nucleosome sliding and facilitates transcription of chromatin . NURF is required for homeotic gene expression, proper larval blood cell development, normal male X chromosome morphology, ecdysteroid signaling and metamorp... |
A2X8Q3 | MAGEADGKAPLGSRYPPAALNERILSSMSQKHVAAHPWHDLEIGPGAPAVFNCVVEIPRGSKVKYELDKATGLIKVDRVLYSSVVYPHNYGFIPRTLCEDGDPMDVLVLMQEQVVPGCFLRARAIGLMPMIDQGEKDDKIIAVCADDPEYRHFRDIKEIPPHRLQEIRRFFEDYKKNENKEVAVNEFLPAEDAINAIKYSMDLYGAYIIESLRK | Catalytic Activity: diphosphate + H2O = H(+) + 2 phosphate
Sequence Mass (Da): 24160
Sequence Length: 214
Subcellular Location: Cytoplasm
EC: 3.6.1.1
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Q5R8T6 | MSGFSTEERAAPFSLEYRVFLKNEKGQYISPFHDIPIYADKDVFHMVVEVPRWSNAKMEIATKDPLNPIKQDVKKRKLRYVANLFPYKGYIWNYGAIPQTWEDPGHNDKHTGCCGDNDPIDVCEIGSKVCARGEIIGVKVLGILAMIDEGETDWKVIAINMDDPDAANYNDINDVKRLKPGYLEATVDWFRRYKVPDGKPENEFAFNAEFKDKDFAIDIIKSTHDHWKALVTKKTNGKGISCMNTTVSESPLKCDPDAARAIVDALPPPCESACTVPTDVDKWFHHQKN | Catalytic Activity: diphosphate + H2O = H(+) + 2 phosphate
Sequence Mass (Da): 32743
Sequence Length: 289
Subcellular Location: Cytoplasm
EC: 3.6.1.1
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Q9HWZ6 | MSYSKIPAGKDLPNDIYVAIEIPANHAPIKYEIDKDTDCLFVDRFMATPMFYPANYGFIPNTLADDGDPLDVLVVTPYPVAPGSVIRARPVGVLHMTDEAGGDAKLIAVPHDKLSVLYKDVKEYTDLPALLLEQIKHFFENYKDLEKGKWVKVEGWGNADAARAEITKAVAAFQK | Function: Catalyzes the hydrolysis of inorganic pyrophosphate (PPi) forming two phosphate ions.
Catalytic Activity: diphosphate + H2O = H(+) + 2 phosphate
Sequence Mass (Da): 19396
Sequence Length: 175
Subcellular Location: Cytoplasm
EC: 3.6.1.1
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P58733 | MDLSRIPPQPKAGILNVLIEIPAGSKNKYEFDKDLNAFALDRVLYSSVQYPYDYGFVPITNNLADDGDPLDGMVIMVPPTFPGVATARPIGMLQMVDGGDRDEKFLCVPAKDPRYTYVKSANDLAGHRLDEIFEFFRSYKNLFKKPTEFFGWKGDVAGLPLVEECVKNYYKTYCKNDHGK | Function: Hydrolyzes PPi generated in anabolic reactions.
Catalytic Activity: diphosphate + H2O = H(+) + 2 phosphate
Sequence Mass (Da): 20332
Sequence Length: 180
Subcellular Location: Cytoplasm
EC: 3.6.1.1
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Q8U438 | MNPFHDLEPGPDVPEVVYAIIEIPKGSRNKYELDKKTGLLKLDRVLYSPFFYPVDYGIIPRTWYEDDDPFDIMVIMREPVYPLTIIEARPIGLFKMIDSGDKDYKVLAVPVEDPYFKDWKDIDDVPKAFLDEIAHFFKRYKELQGKEIIVEGWEGAEAAKREILRAIEMYKEKFGKKE | Function: Catalyzes the hydrolysis of inorganic pyrophosphate (PPi) forming two phosphate ions.
Catalytic Activity: diphosphate + H2O = H(+) + 2 phosphate
Sequence Mass (Da): 20913
Sequence Length: 178
Subcellular Location: Cytoplasm
EC: 3.6.1.1
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Q8XWX1 | MSFNNVSPGKDIPNDFNVIIEIPAQSDPVKYEADKETGLLHVDRFVGTGMRYPANYGFIPQTLAGDGDPVDVLVVTPFPLVHGCVVRCRTLGMLKMTDESGQDAKLVAVPVNKLSPATAHMTDLSDIGQNLLDQIKHFFEQYKALEPGKWVKVEGWGGIEEAHKEIVDGVANYKK | Function: Catalyzes the hydrolysis of inorganic pyrophosphate (PPi) forming two phosphate ions.
Catalytic Activity: diphosphate + H2O = H(+) + 2 phosphate
Sequence Mass (Da): 19224
Sequence Length: 175
Subcellular Location: Cytoplasm
EC: 3.6.1.1
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Q9N1F0 | MVKAPQSEERLAGGGKGNNSVLACGAQASWSIFGADAAEVPGTRSHSRQEAAMPHIPEDEEPPGEPQAAQSPAGQDPATTGISCSPPTIILTGDASSPEGETDKNPVNRAHSPHRRLSHRHLKVSTASLTSVDPAGHVIDLVNDQLPDISISEEDKKKNLALLEEAKLVSERFLTRRGRKSRSSPGESSPAVSPNLSPGASPASSQSNSLTVPTPPGLDVCSGPPSPLPGAPPQKGDEAEVPSPHLGESNVLKGLADRKQNDQRTLSQGRLTARSPTVEKSKEITIEQKENFDPLQRPEAIPKGPASGPGSGGKMALNSP... | Function: Plays a role as NO/PRKG1-dependent regulator of IP3-induced calcium release; its phosphorylation by PRKG1 inhibits bradykinin and IP3-induced calcium release from intracellular stores. Recruits PRKG1 to the endoplasmic reticulum and may mediate the assembly of PRKG1 and ITPR1 in a macrocomplex. Involved in PR... |
Q9Y6F6 | MGMDLTCPFGISPACGAQASWSIFGADAAEVPGTRGHSQQEAAMPHIPEDEEPPGEPQAAQSPAGQGPPAAGVSCSPTPTIVLTGDATSPEGETDKNLANRVHSPHKRLSHRHLKVSTASLTSVDPAGHIIDLVNDQLPDISISEEDKKKNLALLEEAKLVSERFLTRRGRKSRSSPGDSPSAVSPNLSPSASPTSSRSNSLTVPTPPGLDVCSGPPSPLPGAPPQQKGDEADVSSPHPGEPNVPKGLADRKQNDQRKVSQGRLAPRPPPVEKSKEIAIEQKENFDPLQYPETTPKGLAPVTNSSGKMALNSPQPGPVES... | Function: Plays a role as NO/PRKG1-dependent regulator of IP3-induced calcium release; its phosphorylation by PRKG1 inhibits bradykinin and IP3-induced calcium release from intracellular stores. Recruits PRKG1 to the endoplasmic reticulum and may mediate the assembly of PRKG1 and ITPR1 in a macrocomplex. Involved in PR... |
Q9C5S2 | MPPRCPFLRHLFFLLLLLSPWIMSPCGGAADDVTYPIVPSSPGRRSILQIRREPPTEPNTKLVVDRDGKVFLKQQPKETPYWSFSTGSPMHSLYQAPANNNTENATEITRPHIIVEYLNNSKAATTVDGYHNWTVQEFFRQKPLVTDDGVTLGSETTSAYLVDGRSGRLIHVYKSTGDTKITNALVKPASTEDFVNEPLLIRRTDSKLEHFSKTTGKLVWNLTVSHFRAALLCDPVFNSGYDLGPKLQTGIYMPLLCGSQIDVRGPEIVIRVLHDQPMNVKMLPSPSLNHFESENSIMPFGKARESRKLQEQHKQKYTYL... | Function: Senses unfolded proteins in the lumen of the endoplasmic reticulum via its N-terminal domain which leads to enzyme auto-activation. The active endoribonuclease domain splices bZIP60 mRNA to generate a new C-terminus, converting it into a potent unfolded-protein response transcriptional activator which then in... |
Q93VJ2 | MRGSALLDLILFLLVSPLAHSFKGSEISKFYDKSISNQISQSDRESGYVLVSTVDGSISLVDMSSQKLDWTFHTNEPIYSSYQAPHYHYTTDEERSSVLGDDFYMDCDKDWRLYNSSVRKGKRVNEIVDASEFIGTLPYTSTDRIVLGKKDTSVFLLDWKTGKLVKRYRMDELYSNTVVENDKEKAIVLSKEAPLLFGSGFKKSEDFPELVYIERKDFKIQCISKFGDVLWSVSYAKMEAKLQNHESVQFISGLSSSVGKNQFPLSYTTSVPMVQLRNVKYETLFPRLGFLDEALYLPFQDRKPNQLAIGDGNQLTLPGN... | Function: Senses unfolded proteins in the lumen of the endoplasmic reticulum via its N-terminal domain which leads to enzyme auto-activation. The active endoribonuclease domain splices bZIP60 mRNA to generate a new C-terminus, converting it into a potent unfolded-protein response transcriptional activator which then in... |
Q09499 | MRATFHLFTFIFLLLFSSVICISTPGFRNDHESIGDDEEKTSSTILVSTIDGRLRALDSETGEIKWTLQEEPVLRSPSAVKQGFTFLPNPLDGSLYVLKNSSLKKLPFNIPQLVHASPCKGNDGILYAGSKKDVWFGIDPKTGLKVETLSSASADRICPANQKQTIFLGRTEYRVSMFDEKNRGKTWNATFNDYSAHLLPEVNTWPFKHYASSSHGYILTFDRETGEMRWEQDLKQPVVALYLLRDDGLHKLPFEVMGKETMENVAKNIFTVDQWPTVLGVNAADPQTTSLTNQFFPALFVGESSFGLYAIEALVDHQTI... | Function: Senses unfolded proteins in the lumen of the endoplasmic reticulum via its N-terminal domain which leads to enzyme auto-activation . The active endoribonuclease domain splices xbp-1 precursor mRNA to produce the mature form which then induces transcription of UPR target genes . Unfolded protein response (UPR)... |
Q7XIT1 | MRSLRRVLLQLVLLAGVAFRGVRFDDAADAAAAAQGSSDLFELPSPSPTLALPGGGDEGASTEIIAAPWPGRHGLFTPPRSTSQPARAVVQPAADFGSQLQFYDNGTIQLVDLLSKLPRWQFSTGPPLSKHITTSKPDLNYVIYLDGSETSDLIEVHNGSGVRLPWKLEEFIAETPYIRDSFVTIGSKVSTTFVVNADSGEIIYKHSLPVALNEVGGPLVEEIPSKLDAARSGTSANIIVVVRTDYSISASDLGEHLFNWTRTSFTANYYARYGHQDMLAQSSCLRGNIPCIRTEGPPIKLYLPDSSSDNAIVLRPVNEV... | Function: Involved in endoplasmic reticulum (ER) stress response. Senses unfolded proteins in the lumen of the ER via its N-terminal domain which leads to enzyme auto-activation. The active endoribonuclease domain splices bZIP50 mRNA to generate a new C-terminus, converting it into a potent unfolded-protein response (U... |
Q55GJ2 | MTFSKTRNKIIFLLFLIIINIFNINAYIKDENEDDLSLLISTLDGNIYSFNYESGELNWDLKPNGGDSLYSTSQFDRKQQQSTSTSTEITKSSPSILIPTLDGSGLLFQYSNDRLHQVPFSLQELVNTSPLFLKELEDKSSTSSTSTTSESSKDENKVTMFIGNKKTSITVVDSQTGEIIKSMSKDGLWLTDEDDCPVNIIPDEALMFTRSDYQIIALDPKSGVEKWNLSVGEYIPHSTKSFYNSEISLNFEGLIEVASLSQRMYKIYIKKPEKTVVGISHNYWEHILTSSPVSIYAYSSKKHILKKLDFHRKVSPYSNS... | Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 112801
Sequence Length: 984
Subcellular Location: Membrane
EC: 2.7.11.1
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Q5ZLQ4 | MDALRPGSPYQPIIEELRNYPQKRFYNVSKLGGTKYDVLPYSIRVLFESSIRNCDGFLVKETDAMNILDWKTKQNDVEVPFCPARVVLQDFTGIPAMVDFAAMREAVRNAGGDPVKVNPACPTDLTVDHSLQIDFSKCAIQNAPNPGGGEAQKPTAKLSPLKGQPRKLPCRGQSSCKGPCSAGELSRASGQFSAQIENTPILCPFHLQPVPEPETVLKNQEMEFGRNRERLQFFKWSSKVFKNTSIIPPETGMAHQVNLEYLSRVVFDVEDFLYPDSVVGTDSHTTMVNGLGILGWGVGGIETEAVMLGMPVTLTLPEVV... | Cofactor: Binds 1 [4Fe-4S] cluster per subunit. [4Fe-4S]-binding affects RNA-binding activity, thereby inhibiting activity of the protein.
Function: RNA-binding protein that binds to iron-responsive elements (IRES), which are stem-loop structures found in the 5'-UTR of ferritin, and delta aminolevulinic acid synthase m... |
P48200 | MDAPKAGYAFEYLIETLNDSSHKKFFDVSKLGTKYDVLPYSIRVLLEAAVRNCDGFLMKKEDVMNILDWKTKQSNVEVPFFPARVLLQDFTGIPAMVDFAAMREAVKTLGGDPEKVHPACPTDLTVDHSLQIDFSKCAIQNAPNPGGGDLQKAGKLSPLKVQPKKLPCRGQTTCRGSCDSGELGRNSGTFSSQIENTPILCPFHLQPVPEPETVLKNQEVEFGRNRERLQFFKWSSRVFKNVAVIPPGTGMAHQINLEYLSRVVFEEKDLLFPDSVVGTDSHITMVNGLGILGWGVGGIETEAVMLGLPVSLTLPEVVGC... | Cofactor: Binds 1 [4Fe-4S] cluster per subunit. [4Fe-4S]-binding affects RNA-binding activity, thereby inhibiting activity of the protein.
Function: RNA-binding protein that binds to iron-responsive elements (IRES), which are stem-loop structures found in the 5'-UTR of ferritin, and delta aminolevulinic acid synthase m... |
Q9ZUV3 | MTTHKHRRTEKNLCFKQYYKWILCFILTLYFFASFFVDHDQDHRSSTSISKHLLTNHKPKLFASRAMFESKIHDHKLGFTSQQPNIKTDVFNNLKIYVYDLPSKFNKDWLANDRCTNHLFAAEVALHKAFLSLEGDVRTEDPYEADFFFVPVYVSCNFSTINGFPAIGHARSLINDAIKLVSTQYPFWNRTSGSDHVFTATHDFGSCFHTMEDRAIADGVPIFLRNSIILQTFGVTFNHPCQEVENVVIPPYISPESLHKTQKNIPVTKERDIWVFFRGKMELHPKNISGRFYSKRVRTNIWRSYGGDRRFYLQRQRFAG... | Function: Involved in the synthesis of the hemicellulose glucuronoxylan, a major component of secondary cell walls. Probably involved in the synthesis of the glycosyl sequence at the glucuronoxylan reducing end.
Location Topology: Single-pass type II membrane protein
Sequence Mass (Da): 51694
Sequence Length: 448
Subce... |
Q9SXC4 | MASIRRTLSPMYHDRSHENGGSHKGFTIGGSSSKHNSSQFLSYLTKLLGVTSDPKSSRRGPWRRPFYQFLVFFLLGFVLGLTPFGKMEDVNGSDRFSFEIKQPYVEERLENRKREEAAVDAVSFVAETENGKKEVNFVPKKLLIVVTPTYNRAMQAYYLNRVAQTLRLVESPVLWIVVEGNVASFETSEILRKTGVMYRHLVCKRNMTSIKDRGVHQRNTALEHIELHKLDGIVYFADDDNIYSLELFQSLRQISRFGTWPVAMLAQSKNKAILEGPVCNGSQVIGWHTNEKSKRLRRFHVDMSGFAFNSTILWDPKRWR... | Function: Involved in the synthesis of the hemicellulose glucuronoxylan, a major component of secondary cell walls. Probably involved in the elongation of glucuronoxylan xylosyl backbone.
Location Topology: Single-pass type II membrane protein
Sequence Mass (Da): 45187
Sequence Length: 394
Subcellular Location: Golgi a... |
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