ids stringlengths 6 10 | seqs stringlengths 11 1.02k | texts stringlengths 108 11.1k |
|---|---|---|
Q9Y0B7 | MSSDLDRQIEQLKRCEIIKESEVRALCSKAREILLEEGNVQRVDSPVTICGDIHGQFYDLKELFKVGGDCPQTNYLFMGDFVDRGFYSVETFLLLLALKVRYPDRITLIRGNHESRQITQVYGFYEECVRKYGSVTVWKYCTEIFDYLSLSALVDGKIFCVHGGLSPSINTLDQIRAIDRKQEVPHEGPMCDLMWSDPEDIPGWNGSPRGAGFLFGEDVVQKFNHDNNLEFICRAHQLVMEGFKYMFNETLVTVWSAPNYCYRCGNVAAILQLDENLKKNFAIFEAAPQESRGAPAKKPAPEYFL | Cofactor: Binds 2 manganese ions per subunit.
Function: Required for development, chemotaxis and the expression of numerous genes.
Catalytic Activity: H2O + O-phospho-L-seryl-[protein] = L-seryl-[protein] + phosphate
Sequence Mass (Da): 34862
Sequence Length: 305
Subcellular Location: Cytoplasm
EC: 3.1.3.16
|
O76932 | MSDYSDLDRQIEQLKRCEIIKENEVKALCAKAREILVEEGNVQRVDSPVTVCGDIHGQFYDLKELFKVGGDVPEKNYLFMGDFVDRGYYSVETFLLLLALKVRYPDRITLIRGNHESRQITQVYGFYDECLRKYGSTAVWRYCTEIFDYLSLSAIIDGKIFCVHGGLSPSIQYLDQIRSIDRKQEVPHDGPMCDLLWSDPEDQTGWGVSPRGAGYLFGSDVVSQFNRTNDIDMICRAHQLVMEGFKWHFNETVLTVWSAPNYCYRCGNVAAILELNEYLHRDFVIFEAAPQESRGIPSKKPQADYFL | Cofactor: Binds 2 manganese ions per subunit.
Function: Protein phosphatase that regulates many processes such as microtubule organization at centrosomes. The probable PP4 complex Pp4-19C-PPP4R2r-flfl (PPP4C-PPP4R2-PPP4R3) is required to prevent caspase-induced cell death (in vitro).
PTM: Reversibly methyl esterified o... |
P60510 | MAEISDLDRQIEQLRRCELIKESEVKALCAKAREILVEESNVQRVDSPVTVCGDIHGQFYDLKELFRVGGDVPETNYLFMGDFVDRGFYSVETFLLLLALKVRYPDRITLIRGNHESRQITQVYGFYDECLRKYGSVTVWRYCTEIFDYLSLSAIIDGKIFCVHGGLSPSIQTLDQIRTIDRKQEVPHDGPMCDLLWSDPEDTTGWGVSPRGAGYLFGSDVVAQFNAANDIDMICRAHQLVMEGYKWHFNETVLTVWSAPNYCYRCGNVAAILELDEHLQKDFIIFEAAPQETRGIPSKKPVADYFL | Cofactor: Binds 2 manganese ions per subunit.
Function: Protein phosphatase that is involved in many processes such as microtubule organization at centrosomes, maturation of spliceosomal snRNPs, apoptosis, DNA repair, tumor necrosis factor (TNF)-alpha signaling, activation of c-Jun N-terminal kinase MAPK8, regulation o... |
P32345 | MMDLDKIIASLRDGKHIPEETVFRLCLNSQELLMNEGNVTQVDTPVTICGDIHGQLHDLLTLFEKSGGVEKTRYIFLGDFVDRGFYSLESFLLLLCYKLRYPDRITLIRGNHETRQITKVYGFYDEVVRKYGNSNVWRYCCEVFDYLSLGAIINNSIFCVHGGLSPDMTTVDEIRTIDRKQEVPHEGAMCDLLWSDPEDVDTWSLSPRGAGFLFGKREVDQFLEKNNVELIARAHQLVMEGYKEMFDGGLVTVWSAPNYCYRCGNVAAVLKIDDDLNREYTIFEAVQAQNEVGNAIIPTKKSQMDYFL | Cofactor: Binds 2 manganese ions per subunit.
Function: Forms the histone H2A phosphatase complex in association with the regulatory subunits PSY2 and PSY4, which dephosphorylates H2AS128ph (gamma-H2A) that has been displaced from sites of DNA lesions in the double-stranded DNA break repair process. Dephosphorylation i... |
Q86T03 | MAADGERSPLLSEPIDGGAGGNGLVGPGGSGAGPGGGLTPSAPPYGAAFPPFPEGHPAVLPGEDPPPYSPLTSPDSGSAPMITCRVCQSLINVEGKMHQHVVKCGVCNEATPIKNAPPGKKYVRCPCNCLLICKVTSQRIACPRPYCKRIINLGPVHPGPLSPEPQPMGVRVICGHCKNTFLWTEFTDRTLARCPHCRKVSSIGRRYPRKRCICCFLLGLLLAVTATGLAFGTWKHARRYGGIYAAWAFVILLAVLCLGRALYWACMKVSHPVQNFS | Function: Catalyzes the hydrolysis of phosphatidylinositol-4,5-bisphosphate (PtdIns-4,5-P2) to phosphatidylinositol-4-phosphate (PtdIns-4-P) . Does not hydrolyze phosphatidylinositol 3,4,5-trisphosphate, phosphatidylinositol 3,4-bisphosphate, inositol 3,5-bisphosphate, inositol 3,4-bisphosphate, phosphatidylinositol 5-... |
Q3TWL2 | MAADGERSPLLSEAGDGGAGGNGLAGPGGSATGPGGGLTPSAPPYGAGKHAPPQAFPPFPEGHPAVLPGEDPPPYSPLTSPDSGSAPMITCRVCQSPINVEGKMHQHVVKCGVCNEATPIKNAPPGKKYVRCPCNCLLICKVTSQRIACPRPYCKRIINLGPVHPGPLSPEPQPMGVRVICGHCKNTFLWTEFTDRTLARCPHCRKVSSIGRRYPRKRCICCFLLGLLLAVTATGLAFGTWKHAQQYGGIYAAWAFVILLAVLCLGRALYWACMKVSHPVQNFS | Function: Catalyzes the hydrolysis of phosphatidylinositol-4,5-bisphosphate (PtdIns-4,5-P2) to phosphatidylinositol-4-phosphate (PtdIns-4-P) (By similarity). Does not hydrolyze phosphatidylinositol 3,4,5-trisphosphate, phosphatidylinositol 3,4-bisphosphate, inositol 3,5-bisphosphate, inositol 3,4-bisphosphate, phosphat... |
Q3SZ48 | MAADGVDERSPLLSASHSGSVTPTAPPYLQDSSPRAELPPPYTAIVSPDASGIPVINCRVCQSLINLDGKLHQHVVKCTVCNEATPIKNPPAGKKYVRCPCNCLLICKDTSRRIGCPRPNCRRIINLGPVMLVSEEQPAQPALPVQPEGTRVVCGHCGNTFLWMELRFNTLAKCPHCKKISSVGSALPRRRCCAYITIGMMCIFIGIGLTVGTQDFARRFHATYVSWAIAYLLGLVCLIRACYWGAIRVSYPEHSFA | Function: Catalyzes the hydrolysis of phosphatidylinositol-4,5-bisphosphate (PtdIns-4,5-P2) to phosphatidylinositol-4-phosphate (PtdIns-4-P) (By similarity). Does not hydrolyze phosphatidylinositol 3,4,5-trisphosphate, phosphatidylinositol 3,4-bisphosphate, inositol 3,5-bisphosphate, inositol 3,4-bisphosphate, phosphat... |
Q8N4L2 | MAADGVDERSPLLSASHSGNVTPTAPPYLQESSPRAELPPPYTAIASPDASGIPVINCRVCQSLINLDGKLHQHVVKCTVCNEATPIKNPPTGKKYVRCPCNCLLICKDTSRRIGCPRPNCRRIINLGPVMLISEEQPAQPALPIQPEGTRVVCGHCGNTFLWMELRFNTLAKCPHCKKISSVGSALPRRRCCAYITIGMICIFIGVGLTVGTPDFARRFRATYVSWAIAYLLGLICLIRACYWGAIRVSYPEHSFA | Function: Catalyzes the hydrolysis of phosphatidylinositol-4,5-bisphosphate (PtdIns-4,5-P2) to phosphatidylinositol-4-phosphate (PtdIns-4-P) . Does not hydrolyze phosphatidylinositol 3,4,5-trisphosphate, phosphatidylinositol 3,4-bisphosphate, inositol 3,5-bisphosphate, inositol 3,4-bisphosphate, phosphatidylinositol 5-... |
Q9CZX7 | MAADGVDERSPLLSASHSGNVTPTAPPYLQESSPRAELPPPYTAIASPGTSGIPVINCRVCQSLINLDGKLHQHVVKCTVCNEATPIKTPPTGKKYVRCPCNCLLICKDTSRRIGCPRPNCRRIINLGPVMLISEEQPAQPALPIQPEGTRVVCGHCGNTFLWMELRFNTLAKCPHCKKISSVGSALPRRRCCAYVTIGMICIFIAVGLTVGTQDFSRRFHATYVSWAIAYLLGLICLIRACYWGAIRVSYPEHGFA | Function: Catalyzes the hydrolysis of phosphatidylinositol-4,5-bisphosphate (PtdIns-4,5-P2) to phosphatidylinositol-4-phosphate (PtdIns-4-P) (By similarity). Does not hydrolyze phosphatidylinositol 3,4,5-trisphosphate, phosphatidylinositol 3,4-bisphosphate, inositol 3,5-bisphosphate, inositol 3,4-bisphosphate, phosphat... |
Q9JMQ2 | MSDKQVTTILFDLDGTLINTNELIIASFLHTLEHYYPSKYKREDVLAFIGPSLFDTFSSMDPDKCEDMIAMYRAYNHDMHDSLVTEYETVYETLDALKKAGFTLGIVTTKLRDTVNMGLKLTGIGEFFETVVTLDDVTNAKPDPEPVLLALKQLGSEPAEAIMVGDNYHDVLAGKNAGTKTAGVAWTIKGPEMLAKHEPDFMLEKMSDLLQIVGVK | Function: Hydrolyzes pyrophosphate formed during P-Ser-HPr dephosphorylation by HPrK/P. Might play a role in controlling the intracellular pyrophosphate pool.
Catalytic Activity: diphosphate + H2O = H(+) + 2 phosphate
Sequence Mass (Da): 24004
Sequence Length: 216
EC: 3.6.1.1
|
P9WI42 | MAAPIWMASPPEVHSALLSNGPGPGSLVAAATAWSQLSAEYASTAAELSGLLGAVPGWAWQGPSAEWYVAAHLPYVAWLTQASADAAGAAAQHEAAAAAYTTALAAMPTLAELAANHVIHTVLVATNFFGINTIPITLNEADYVRMWLQAAAVMGLYQAASGAALASAPRTVPAPTVMNPGGGAASTVGAVNPWQWLLALLQQLWNAYTGFYGWMLQLIWQFLQDPIGNSIKIIIAFLTNPIQALITYGPLLFALGYQIFFNLVGWPTWGMILSSPFLLPAGLGLGLAAIAFLPIVLAPAVIPPASTPLAAAAVAAGSVW... | Function: Important for the siderophore-mediated iron-acquisition function of ESX-3.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 51788
Sequence Length: 513
Subcellular Location: Cell membrane
|
Q8YHB5 | MSFIRSALAAAAFVALSIGAVQTASAADPENTVILKLKDGDVALELRPDLAPKHVAQIKKLVREGAYNGVAFHRVIPGFMAQTGDVKFGNMDKGFDAARVGTGGSNYPDLPAEFSKEPFVRGTVGMARSQNPNSANSQFFIMFDDGPFLNGQYTVVGKVVSGMDAVDKIKKGSEAENGAVKNPDKIIKATIEADTK | Function: PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides (By similarity).
Catalytic Activity: [protein]-peptidylproline (omega=180) = [protein]-peptidylproline (omega=0)
Sequence Mass (Da): 20751
Sequence Length: 196
Subcellular Loca... |
Q2FIC1 | MANYPQLNKEVQQGEIKVVMHTNKGDMTFKLFPNIAPKTVENFVTHAKNGYYDGITFHRVINDFMIQGGDPTATGMGGESIYGGAFEDEFSLNAFNLYGALSMANSGPNTNGSQFFIVQMKEVPQNMLSQLADGGWPQPIVDAYGEKGGTPWLDQKHTVFGQIIDGETTLEDIANTKVGPQDKPLHDVVIESIDVEE | Function: PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides (By similarity).
Catalytic Activity: [protein]-peptidylproline (omega=180) = [protein]-peptidylproline (omega=0)
Sequence Mass (Da): 21619
Sequence Length: 197
EC: 5.2.1.8
|
Q4L4W9 | MTNYPQLNKEIQDNEIKVAMHTNKGDMTFKLFPDIAPKTVENFVTHAKNGYYDGITFHRVINDFMIQGGDPTATGMGGESIYGGSFEDEFSLEAFNLYGALSMANAGPNTNGSQFFVVQMKEVPESMVNQLVDGGWPEPIAKAYADNGGTPWLDQKHTVFGQLIEGEATLEDIANTKVGAQDKPVHDVVIESIDVEDK | Function: PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides (By similarity).
Catalytic Activity: [protein]-peptidylproline (omega=180) = [protein]-peptidylproline (omega=0)
Sequence Mass (Da): 21726
Sequence Length: 198
EC: 5.2.1.8
|
Q49W93 | MTNYPQLNTEINGNEIKLIMHTNKGDMTFKLLPDVAPKTVENFVTHAKNGYYNGVTFHRVINDFMVQGGDPTATGMGGESIYGEPFEDEFSKEAFNIYGALSMANAGPHTNGSQFFIVQMNEVPESMLSQLADGGWPEPIVKAYAETGGTPWLDQKHTVFGQLIEGKDTLEDIANTKVGPQDKPLHDITIDSIEIVE | Function: PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides (By similarity).
Catalytic Activity: [protein]-peptidylproline (omega=180) = [protein]-peptidylproline (omega=0)
Sequence Mass (Da): 21683
Sequence Length: 197
EC: 5.2.1.8
|
P72704 | MRILPNISRATWFVGIFFVVNILLTACNQPSANSSAEPSPTETNSPVAQVTTDPYKDYKPRLNGKATVEMMVNGQPIIIEVDGENAPITAGNFVDLVEQGFYNGLTFHRVVDGFVAQGGDPKGDGTGGYVDKNTQRPRNIPLEIKVDPAVENAPETPVYSRALGNQAGFPVMLPHKTGAVAMARSQMPDSASSQFYFTLSDETGFLDGDYAVFGYVTQGMDVVLKIKQGDKIQSAKVITGQNNLEK | Function: PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides.
Catalytic Activity: [protein]-peptidylproline (omega=180) = [protein]-peptidylproline (omega=0)
Sequence Mass (Da): 26580
Sequence Length: 246
EC: 5.2.1.8
|
B3H4K7 | MGAQIILSEGFEVVPPPEMNDLVLFGSNQSVSSCDVSTVTTEDGTVFSGDSSPGGATEEDFPEEKPFSFYFVKQPAYDDPEIKAKIDEAGHEINRYNKDRIVVSNAQESEKAEILSLFGQMKSLVSKSEGYRVVIEEKKMEFDALHESLRNLRCSTSDQLCFSKEELDHLIYIAHYQIEHGSIGFEEEDWVLKETEKADGIVLSEDSLAEKEASINRVKSMAVELNEVKKELDAITWKINHLSDKVGKSQNNLRVLDVKKAHILEERDRSYERIKMLRIQRDKGKAAFYQSLPVMRKARELAASGNVRDLEVFASSEADR... | Function: May regulate plasma membrane ATPase activity.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 67324
Sequence Length: 589
Subcellular Location: Cell membrane
|
O66105 | MNTQVWRVCVGVMLFCFVGRIGCAEEKMVREEGLAVADGIYAVMETNRGTIVLSLFFEKAPLTVCNFVGLAEGTLAVCKGRPFYQGLTFHRVIKDFMIQGGDPQGNGTGGPGYQFPDECDPALRHDSPGVLSMANAGPGTNGSQFFITHVATPWLDGKHTVFGKVVEGMEVVHAIIAGDTIRSLKIVRRGAAAKRFVCDQAQFDQLRKRVSAASK | Function: PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides (By similarity).
Catalytic Activity: [protein]-peptidylproline (omega=180) = [protein]-peptidylproline (omega=0)
Sequence Mass (Da): 23272
Sequence Length: 215
EC: 5.2.1.8
|
Q6C4W6 | MKLFATIGVLLVALLAFFVQPAQAEPDAEITHKVYFDIKQGEESLGKIVMGLYGDVVPKTVENFRALCTGETGKGYKGSKFHRVIKNFMIQGGDFTRGDGTGGESIYGRKFPDENFQLKHTKPYKLSMANAGRDTNGSQFFITTVVTSWLDGKHVVFGEVLEGQDIVDAIENAPTGARSNPKVDITIADAGEIPVEKSETKEAEPAKEDAKEPKEDVKKKGKSDKDEL | Function: PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides (By similarity).
Catalytic Activity: [protein]-peptidylproline (omega=180) = [protein]-peptidylproline (omega=0)
Sequence Mass (Da): 24946
Sequence Length: 228
Subcellular Loca... |
P0A9L7 | MAKTAAALHILVKEEKLALDLLEQIKNGADFGKLAKKHSICPSGKRGGDLGEFRQGQMVPAFDKVVFSCPVLEPTGPLHTQFGYHIIKVLYRN | Function: PPIases accelerate the folding of proteins. It prefers amino acid residues with hydrophobic side chains like leucine and phenylalanine in the P1 position of the peptides substrates (By similarity).
Catalytic Activity: [protein]-peptidylproline (omega=180) = [protein]-peptidylproline (omega=0)
Sequence Mass (D... |
P45877 | MGPGPRLLLPLVLCVGLGALVFSSGAEGFRKRGPSVTAKVFFDVRIGDKDVGRIVIGLFGKVVPKTVENFVALATGEKGYGYKGSKFHRVIKDFMIQGGDITTGDGTGGVSIYGETFPDENFKLKHYGIGWVSMANAGPDTNGSQFFITLTKPTWLDGKHVVFGKVIDGMTVVHSIELQATDGHDRPLTNCSIINSGKIDVKTPFVVEIADW | Function: PPIase that catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides and may therefore assist protein folding.
Catalytic Activity: [protein]-peptidylproline (omega=180) = [protein]-peptidylproline (omega=0)
Sequence Mass (Da): 22763
Sequence Length: 212
Subcellular Location: Cyto... |
Q4WIF3 | MAETQRRPRVYFDIQIGSQKAGRIALELVRLPFNDVVPKTAENFRALCTGEKGVGKQRKPLSYKGSIFHRVIKQFMIQGGDFTNFNGTGGESIYGEKFPDENFELKHDRPFLLSMANSGPGTNGSQFFITTVPTPHLDGKHVVFGEVINGKSIVRKIENMPTQADKPTTDVTIVDCGELSGEDYENATKQVADATGDPYEDYPDDHQGEELNAQVCFKIASELKNFGNTAFKSGDVALGLDKYQKGLRYLNEFPDPDENDPKDLEPQMKSLRFTLHSNSSLLANKLGQYKNAQNWATYALEVADAANAKEADRAKAYYRR... | Function: PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides (By similarity).
Catalytic Activity: [protein]-peptidylproline (omega=180) = [protein]-peptidylproline (omega=0)
Sequence Mass (Da): 41808
Sequence Length: 377
Subcellular Loca... |
P57550 | MTKYSQARLNSIIVKFILGVIILSLILSTISIYINRDFEKYIATVNGEKISFNLFKKMYFIEREKQKKILGKNFFKFSHNENFTKETYNYVLSQLINNVLLEQYAKNMNYLEVNDNTIKKIIYNSPIFQKNNKFSKERYLNYLTSINSTNHEYINIIKKKINTENLIHTISKSNFILKKEEKNIIKLLSQKRIIKKAIVKIDPSIYKKNITNQEAQIYFKKNQDNFYIPEKFKINFVELKTDNFKIHCENKEIYDWYIRNITQYSTKEKRRYSIIQVKNKQQAISILSRLHNTPEDFSKIAQEQSTDPISSKKDGDIGWI... | Function: Chaperone that functions as a gatekeeper on the periplasmic side of the SecYEG translocon. Facilitates the translocation of precursor proteins across SecYEG by interacting with the translocating substrate. Also plays a role in the release of newly synthesized secreted proteins at the periplasmic exit site of ... |
Q89A98 | MHKLTSKLSNLILLLLIIIIFISLILTNFNNYLLENLSEYEIKINNTEISREEFIQRYNLECFYNDKNFKNDIITNPKNPKYISEIYNITLSNIIYESLLQQYVHQLHFNIDYSHVKNYIYKQTIFRQNQKFNKEKYYEYLKKLQISSNEYIKKVMTYLEIKEFIKTLTNTDFILNNEKNNILKLFEQGRIVNKSYVNLNNLKLIEHISNKELKRYYINHKHQFLSPKKFKISYFLINKNNVFVPCIKKFYFKNKDNTFQHELFLQHKKSKKQNDNIIKKLLTTHTNTSQFKNIIQKNNICIHHTPWLTQTLYKHEKLPK... | Function: Chaperone that functions as a gatekeeper on the extracellular side of the Sec translocon. Facilitates the translocation of precursor proteins across Sec by interacting with the translocating substrate. Also plays a role in the release of newly synthesized secreted proteins at the extracellular exit site of th... |
Q5ACI8 | MTATPVYFDISCNGKPKGRVVFKLYDDVVPKTAANFRSLCTGDKGISPKSGKPLSYKDSIFHRVIKDFMCQGGDFTAPSDHLGTGGESIYGEKFEDENFKLNHNKPFLLSMANSGPNTNGSQFFITTVPTPHLDGKHVVFGEVIEGKSIVRQLERSEKGANDRPVEDWKIADCGELPANYEPVASGADDGTGDTYEEILTDNDTIDINNPQSVFAAVSKIKDIGTKLLKEGKLEKSYEKYTKANSYLNDYFPEGLSPEDLSTLHGLKLSCYLNAALVALKLKHGKDAIAAANNALEVEQIDDKSKTKALYRKGMGYILVK... | Function: PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides (By similarity).
Catalytic Activity: [protein]-peptidylproline (omega=180) = [protein]-peptidylproline (omega=0)
Sequence Mass (Da): 40740
Sequence Length: 369
Subcellular Loca... |
Q9URY1 | MKKNEKANISASYNDLIATICNPRISDVGTYRIESVVGEGSFGKVYLAAHLLTNTKVVLKSSCRKQAIILAREIHHHRRLLHPNITRLYEVVCTEDRIYLAMEYCPNGELYDWVAREKRLDEKTTCRIMWQLCCAIQYLHRQGCVHRDLKLENIFLDKAYNVKLGDFGFSRDSDCSRRTFMNTRCGTVAYCAPELVQGHKYIGECVDIWSLGIIMYALLIGRLPFDEDDVSLTEQKIINECPQYPETLSKNSSSLLKSLLCKDYRLRPSIDQIISHPYFKENGYHSSSIRDPRPSSKAEEKVRKRLEFVGVDMDQLNASI... | Function: Has a role in meiosis.
Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Sequence Mass (Da): 75841
Sequence Length: 672
Subcellular Location: Cytoplasm
EC: 2.7.11.1
|
Q9VAJ3 | MLLYTKELVIPRPRPGLLRFRNNPRGIKFREKLCNSFAHSNIHGMQHVFGEQHLWQRCLWLAIVLGAVITGFSLYTVLMHRHSEQLLVSLIETTQLPVYHIDFPAVAVCPWNHFNWQRAPSAFIRFLPRHPNAELRETFRQLLASMDIMNFSNFNRIRILTKRNLTGISYLKMTDLMNFMTYRCDELFVADSCVFDETPYDCCKLFVREQTVKGQCLVFNSMISENSRKKHLINQFYPHKLSTAGEDSGLKFTINASYSFMNNIDALTPFGMNLMIKEPRQWSNEMMYHLYPDTENFVAVHPLVTETSPNTYEMSPKKRR... | Function: Part of a complex that plays a role in tracheal liquid clearance. In both larvae and adults, contributes to the behavioral response to salt. Probable role in sodium transport.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 59461
Sequence Length: 511
Subcellular Location: Membrane
|
B7GXW8 | MNTAITATTPTEYSYNDRYINRELSILDFHLRVLEQAVDPLHPLLERMNFLLIFSRNLDEFFEIRVAGVMEQFALGNESRSPDGLTPRQVLQKISETAHTAIERQYRILNEEILPKLREEDICFLRRGELTPAQSAWVKKYFQEQVAPVLTPISLDPAHPFPRLVNKSLNFIVTLEGKDAFGRQIDLAVVPAPRSLPRVVRLPDELTGGKEHHVMLSAIIHEHVSDLFPGMTATGCYQFRVTRNADLALNEDVEDLAKALKGELSSRRFGRAVRLEVTQNCPQHIYEYLLEEFDLNEEQLYKVDGPVNLARLVSNFKRPH... | Function: Catalyzes the reversible transfer of the terminal phosphate of ATP to form a long-chain polyphosphate (polyP).
PTM: An intermediate of this reaction is the autophosphorylated ppk in which a phosphate is covalently linked to a histidine residue through a N-P bond.
Catalytic Activity: [phosphate](n) + ATP = [ph... |
A5G1J3 | MDQETLPRTATEPMPAGDSDRFINRELSWLAFNSRVVAAAENPRYPLLERLRFISISGSNLDEFYSVRVAGLIGQARAGLALRSSDGLTPTQQLGEINRCARALMETQQRVLGTVLAELAGAGLTIIAPHELNEADRAFLDQHFMERVFPVLTPLAIDPAHPFPFVQNMGLVLALKLIRQEDSGVMRALIPLPAQIRRFIRLPDPSPETIRFVKLEDLVILFLDRLFHGFRLAGSGLFRVCRDTDVEFEEEAEDLVQSYETALKRRRRGAAIELTLAADLPDDLRTLVIDEVEAPEDQLFVEPGMLGLVDLKEMIVDDRP... | Function: Catalyzes the reversible transfer of the terminal phosphate of ATP to form a long-chain polyphosphate (polyP).
PTM: An intermediate of this reaction is the autophosphorylated ppk in which a phosphate is covalently linked to a histidine residue through a N-P bond.
Catalytic Activity: [phosphate](n) + ATP = [ph... |
Q93AK9 | VFHGGVAGLKQQVEATVNLLTTDGRTPQKQLDDIRLHLHPQLKKQNTEFQEVLQPLLRQQGICILDYIELNQQQRNYLDNYFQEQIFPVLTPLAVDPSHPFPHISNLSLNLAVVVKNPDTEEEFFARVKVPQVLPRFLPLPPELRTEDNGKTANWSGIPLEQAIAHNLESLFPGMSIQEYHPFRITRDADLELEEDEAEDLLLAIEQELRKRGMGGTPVRLEIRSQTPESIRSRLLQDLGLTENDIYEVDGLLGLRDLMYFLLLPLPDLKDPPRQSVVPSRLQRLKEPCINPDVPEPEDGKDFFSVIREKDLLVHHPYQS... | Function: Catalyzes the reversible transfer of the terminal phosphate of ATP to form a long-chain polyphosphate (polyP).
PTM: An intermediate of this reaction is the autophosphorylated ppk in which a phosphate is covalently linked to a histidine residue through a N-P bond.
Catalytic Activity: [phosphate](n) + ATP = [ph... |
Q81MN9 | MELSKGNIVNLNDTAYYNNRELSWLAFNERVLQEAQDETNPLLERLKFISIFSSNLDEFFMVRVAGLKDQVSAGFNQPENKAGLTPKKQLNKIAIKAHELMTVQYGTFKNYVLPALELEGIERLTFHDLTKEQREFIEEYFDEQIFPVLTPVAIDAYRPFPMLLNKSLNLATLLYDEKQVEEENRTKLGIVQVPSLLERFIFLPSEGQKHKFILLEDVISSFTHKLFTGYKVSSVTRFRITRNADLTIHEEGARDLLKVIEKELKKRKWGAAVRLEVGKEHIDERVLALLYEVLEVKDEDVYIMDGPLDLTCLFSLYKKL... | Function: Catalyzes the reversible transfer of the terminal phosphate of ATP to form a long-chain polyphosphate (polyP).
PTM: An intermediate of this reaction is the autophosphorylated ppk in which a phosphate is covalently linked to a histidine residue through a N-P bond.
Catalytic Activity: [phosphate](n) + ATP = [ph... |
Q6G327 | MEKTVADQISLSDITMKNPARFINREFSWLQFNNRVLMEAANSKNPLLERLQFLSISATNLDEFFMVRVAGLAAQIRAGVTACSADGRTPQEQLDFVLAEISCLQDNQLRELSILRHELKQNNIEIICSAGLSETEKSWIEKYFLDTIFPVLTPLSVDPVRPFPFIPNLGFSIALQLSRCADQHSFIALLPLPTTLRRFIPLPQKDNRFRFIACEDVINLFMRHVFPDYEVEGIGTFRVIRDSDIEVEEEAEDLVHFFETALKRRRRGQVIRIEFEAKMPDHLRQFITNGLAVPEYCINVLDGFLALNTVSEIVSIPRND... | Function: Catalyzes the reversible transfer of the terminal phosphate of ATP to form a long-chain polyphosphate (polyP).
PTM: An intermediate of this reaction is the autophosphorylated ppk in which a phosphate is covalently linked to a histidine residue through a N-P bond.
Catalytic Activity: [phosphate](n) + ATP = [ph... |
Q9UTH3 | MSQDVFKHLTSKQVQRTRARSFGASFERPLASFLPKKENKNLLSNAARVKLLTFSSSSPYSFSYSPVLSRDANDGYIPLDTSSRANLWESVTDYDLQHANEPLVGNYYISTEALGDGLNRSPFTINPEKRRSLSDISYVPIPHKEHSNWPVHCSSQAIVTTSNTTFSIWSANDYFCLLFGYAGSQLNRHSVFDIFPKSFSSHLSNLIVSFPIDNEHERILFCGDVFPVITVDGVRLMDFWVKEKQGKLIWILEFVEESYIDIKLQDGVAVDERTEQPLTSDLLPSRLPKTWDQRLYLTTKTTEGYYCPSMIYPLSKSSFQ... | Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Sequence Mass (Da): 88614
Sequence Length: 775
Subcellular Location: Cytoplasm
EC: 2.7.11.1
|
Q09792 | MAVITEENSNNLFCTDSLELTSNKQDDQVISNYLKPVRSYPYIKYSRSSLLLTASTTLPENFVISFTNSIESEESDKSDYLLDHAHSLQELSTTHSSLSSTLTSMSEESSSTESKFATLNDGINGGNPYSRLYRKNPSSDPNDIPPQFHFKKKSKSFYSSMYDKMKIRINILPNGNDNFIKKRNSGFALAPIACYNHTSDLRKLLKHKVTGSNASIFKRINPRSRKRVVNPECSVTDTPYGKLNNVIGEGASSFIRVINDRNKLPIYVAKVFRPPLDTSLLRRYVRYFIAEYTFASTLRHPNIIKVLDIIYKRHTILQII... | Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Sequence Mass (Da): 58547
Sequence Length: 513
Subcellular Location: Cytoplasm
EC: 2.7.11.1
|
Q2SC73 | MLKVNEYFNGRVKSIAFQTATLPATVGVMIPGDYEFSTSQHETMTVVSGALSVKLPESESWTRFNAGDRFEIPANATFNLKVAVDTAYLCTYG | Function: Catalyzes the phosphorolysis of diverse nucleosides, yielding D-ribose 1-phosphate and the respective free bases. Can use uridine, adenosine, guanosine, cytidine, thymidine, inosine and xanthosine as substrates. Also catalyzes the reverse reactions.
Catalytic Activity: a purine D-ribonucleoside + phosphate = ... |
Q5YZH4 | MSKFENVSVAKKANVYFDGACVSHSIEFPDGTAKSVGVILPATLTFGTTAPEVMELVEGHCRVTLPGADAPVTFRGGESFEVPADSEFTIEVLETVHYVCHYG | Function: Catalyzes the phosphorolysis of diverse nucleosides, yielding D-ribose 1-phosphate and the respective free bases. Can use uridine, adenosine, guanosine, cytidine, thymidine, inosine and xanthosine as substrates. Also catalyzes the reverse reactions.
Catalytic Activity: a purine D-ribonucleoside + phosphate = ... |
Q8E927 | MELIEQVAVAKKANIYFEGKVASRSVFFSDGSKQTLGVVLPGEYEFSTSQGEIMHVTSGSFEVLLPNSSTWQAFSEGSQFELAANVSFKIRNNAIAEYCCRYL | Function: Catalyzes the phosphorolysis of diverse nucleosides, yielding D-ribose 1-phosphate and the respective free bases. Can use uridine, adenosine, guanosine, cytidine, thymidine, inosine and xanthosine as substrates. Also catalyzes the reverse reactions.
Catalytic Activity: a purine D-ribonucleoside + phosphate = ... |
Q2FUA9 | MIPESHPRYKSLITREKLAQYTKTGIVSLEGLTAHGRGEAFDYLLGEETTESALRAEKIAAALLLSANHPVISVNGNTAALAAKEIAQLQLASKARVEVNLFHRTDERVQAISGLLKEHGITLVEGTVSRYIPLDHDRGLCHFDGMHSADVVLVPLEDGDRAQALIDLGKKVIAIDLNPLSRTSKVATVPVIDEVTRALANIARFCTELDQDEITGLTREIHGTGFIRDALEYIRERLLNVLD | Function: Catalyzes the condensation of (R)-4-phosphopantoate and beta-alanine to 4'-phosphopantothenate in the CoA biosynthesis pathway.
Catalytic Activity: (R)-4-phosphopantoate + ATP + beta-alanine = (R)-4'-phosphopantothenate + AMP + diphosphate + H(+)
Sequence Mass (Da): 26633
Sequence Length: 243
Pathway: Cofacto... |
Q57662 | MLSVMRMQIPKTHPRYESLMKREKIIEALDKGILAKAGLIAHGRGETFDYLIGEKTAPIALEAIKAAAALLILAENPVISVNGNTVALAIDEVVELAKELNGKIEVNLFYRTKERELAIKRAFEEKFKDDIETGKIKILGIDDANKQIPNLDSLRGKVSEEGIFTADVVLVPLEDGDRAEALVNMGKKVIAIDLNPLSRTARKSTITIVDELTRAMPLLIKYVKEFKNKDREELLKIVEDFDNKKNLKDMIDYIAERLKNLSLDEL | Function: Catalyzes the condensation of (R)-4-phosphopantoate and beta-alanine to 4'-phosphopantothenate in the CoA biosynthesis pathway.
Catalytic Activity: (R)-4-phosphopantoate + ATP + beta-alanine = (R)-4'-phosphopantothenate + AMP + diphosphate + H(+)
Sequence Mass (Da): 29853
Sequence Length: 266
Pathway: Cofacto... |
Q5JIZ8 | MVNIPKSHPRYWSLYYREKIIEGMEKGMTAKAGLIAHGRGEAFDYLIGERTIEPAERAMRAAVAKFLLAEHPVISVNGNVAALVPKETIELAKALNAKLEINLFYRTEERVRTIAEELRKYDPEIEILGINPTKRIPGLEHERGKVDENGIWKADVVLVPLEDGDRTEALVRMGKFVVTVDLNPLSRSARMADITIVDNIVRAYPRMVELAREMKDYSREELLKIVGEYDNGKTLSDVLLHIRDRLTRLAEEGIWRRKELE | Function: Catalyzes the condensation of (R)-4-phosphopantoate and beta-alanine to 4'-phosphopantothenate in the CoA biosynthesis pathway . Cannot use (R)-pantoate as substrate and thus does not display pantothenate synthetase (PS) activity . Displays strict specificity for its natural substrates, 4-phosphopantoate, ATP... |
Q8RXN3 | MQSSAVFSLSPSLPLLKPRRLSLRHHPITTAASSSDLNVSPNVVSIPSLSRRSWRLASSDSPLRAWSGVPSPISHSLDTNRFRTAATAVPESAEEGDNSGKLTKVLELGLLFAMWYLFNIYFNIYNKQVLKALHAPMTVTLVQFAVGSVLITIMWVLNLYKRPKISGAQLAAILPLAVVHTLGNLFTNMSLGKVSVSFTHTIKAMEPFFSVLLSAMFLGEKPTPWVLGAIVPIVGGVALASISEVSFNWAGFSSAMASNLTNQSRNVLSKKVMVKKDDSLDNITLFSIITLMSLVLMAPVTFFTEGIKFTPSYIQSAGVN... | Function: Phosphoenolpyruvate/phosphate translocator that transports phosphoenolpyruvate (PEP), 2-phosphoglycerate, 3-phosphoglycerate and dihydroxyacetone phosphate. Imports PEP to the chloroplast stroma as one substrate of the shikimate pathway, from which aromatic amino acids and a variety of secondary products deri... |
Q20390 | MRYFPLLLCLLAITTAEFRNATKQVPVVMWHGMGDCCCNPLSMGSVKKLFEEQIPGVYVHSLQLGSSITKDIEHGFYANTNELVYMACIKIKNDPELKNGYNAIGFSQGAQFLRAVAQRCPNPPMKNLVSVGGQHQGVFGAPYCIGDNIMCNGVRRLIDLGAYLPFVQKRVVQAQYWHDPNQVEEYKKRSIFLADINNENNNNPTYKRNLLSLKNLVLVKFNQDHMVVPKDSSWFGFYKDGDIDTILPMNETDLYKEDRIGLKKLHESGRIHFMDVDGDHLQIPRSVLVNDIIKKYFM | Function: Removes thioester-linked fatty acyl groups such as palmitate (hexadecanoate) from modified cysteine residues in proteins or peptides.
Catalytic Activity: H2O + S-hexadecanoyl-L-cysteinyl-[protein] = H(+) + hexadecanoate + L-cysteinyl-[protein]
Sequence Mass (Da): 33984
Sequence Length: 298
EC: 3.1.2.22
|
Q9W3C7 | MISICCSRFSCILFLLFLIFSLVLSYIWWSPTKGGTNPEVLPVVLWHGMGDTCCVPFSLGAIMNLIVEQTKGGYVRSLQIGGNVLIDWQSGFFIHPNEQVDYVCKQLLQDEHLAKGYHAIGFSQGGQFLRAVAERCPNPPMRNLITLGGQHQGIFGLPMCPTLTEKPCDYITRLLDNAAYAPEVQKALVQATYWHDPIMENKYRLGSTFLADINNELFINKFYIENLQKLKKFVMVQFLNDTIVQPKESQWFQYYTTGQNKVIQPFTESKVYQDLGLDKMHRQGQLVFLGVEGDHLAISKAWFIQNIVPLLLEK | Function: Cleaves thioester-linked long fatty acyl groups such as palmitate from modified cysteine residues in proteins or peptides.
Catalytic Activity: H2O + S-hexadecanoyl-L-cysteinyl-[protein] = H(+) + hexadecanoate + L-cysteinyl-[protein]
Sequence Mass (Da): 35780
Sequence Length: 314
Subcellular Location: Lysosome... |
A0A1L7T8M0 | MSRAQSSPTVIQWVIDTHPLWPSALKTKDLTSAASRALSLLTEEEQSSVLRYYHVRDAKLALASALLKRYAISRFCHVPWFQAKTTRDSRTKPVFVLPSGDEPLIFNVSHQAGLAVFLAVRDPPKGLAVGVDVVCPSERRDRDLSSLEEDGWASFVDIHADVFGAGEVSALKSMNPVPTVQGRDRALRYFYALWCLREAYVKMTGDALLASWLKDLEMHKFAPPEDMKEAQEVRLRGKKVEGVDVRLMPLLEEYMVSTAIRNGDNGERVELGEFQSLDMEEILAFGEKASKP | Function: Transfers the 4'-phosphopantetheine moiety from coenzyme A to a Ser of an acyl-carrier-protein (Ref.2). The enzyme is able to transfer the cofactor to a broad range of enzymes with acyl- or peptidyl-carrier protein domains (Probable). Required for primary biological processes such as growth and asexual/sexual... |
P50897 | MASPGCLWLLAVALLPWTCASRALQHLDPPAPLPLVIWHGMGDSCCNPLSMGAIKKMVEKKIPGIYVLSLEIGKTLMEDVENSFFLNVNSQVTTVCQALAKDPKLQQGYNAMGFSQGGQFLRAVAQRCPSPPMINLISVGGQHQGVFGLPRCPGESSHICDFIRKTLNAGAYSKVVQERLVQAEYWHDPIKEDVYRNHSIFLADINQERGINESYKKNLMALKKFVMVKFLNDSIVDPVDSEWFGFYRSGQAKETIPLQETSLYTQDRLGLKEMDNAGQLVFLATEGDHLQLSEEWFYAHIIPFLG | Function: Removes thioester-linked fatty acyl groups such as palmitate from modified cysteine residues in proteins or peptides during lysosomal degradation. Prefers acyl chain lengths of 14 to 18 carbons .
PTM: Glycosylated.
Catalytic Activity: H2O + S-hexadecanoyl-L-cysteinyl-[protein] = H(+) + hexadecanoate + L-cyste... |
O43049 | MAKEALELKNEANKFLKEGHIVQAIDLYTKAIELDSTNAILYSNRSLAHLKSEDYGLAINDASKAIECDPEYAKAYFRRATAHIAIFQPKEAVGDFRKALALAPSDPAARKKLRECEQLVKRIRFQEAIHNTEPPSPLANINIEDMDIPSDYDGVILEKQITKEFVEDMKERFCQGKKLPLKFAYSILRDLKELLEKTPSLIDIPVKGDETLVICGDTHGQYFDLLNIFKLHGPPSPTNKYLFNGDFVDRGSWSTEVAFTLYAYKLLYPDAVFINRGNHETDDMNKVYGFEGECRSKYNERTFNIFSETFSLLPLGSLIS... | Cofactor: Binds 2 manganese ions per subunit.
Function: Protein phosphatase that specifically binds to and dephosphorylates the molecular chaperone Hsp90. Dephosphorylation positively regulates the Hsp90 chaperone machinery (By similarity).
Catalytic Activity: H2O + O-phospho-L-seryl-[protein] = L-seryl-[protein] + pho... |
P53043 | MSTPTAADRAKALERKNEGNVFVKEKHFLKAIEKYTEAIDLDSTQSIYFSNRAFAHFKVDNFQSALNDCDEAIKLDPKNIKAYHRRALSCMALLEFKKARKDLNVLLKAKPNDPAATKALLTCDRFIREERFRKAIGGAENEAKISLCQTLNLSSFDANADLANYEGPKLEFEQLYDDKNAFKGAKIKNMSQEFISKMVNDLFLKGKYLPKKYVAAIISHADTLFRQEPSMVELENNSTPDVKISVCGDTHGQFYDVLNLFRKFGKVGPKHTYLFNGDFVDRGSWSCEVALLFYCLKILHPNNFFLNRGNHESDNMNKIY... | Cofactor: Binds 2 manganese ions per subunit.
Function: Protein phosphatase that specifically binds to and dephosphorylates the molecular chaperone Hsp90 (HSC82 and HSP82). Dephosphorylation positively regulates the Hsp90 chaperone machinery.
Catalytic Activity: H2O + O-phospho-L-seryl-[protein] = L-seryl-[protein] + p... |
Q6PCJ9 | MTASRPKALQTFCLLLPLLVWMVDRSLCYKPVIVVHGLFDSSANFKNLLQYINESHPGTNVTVLDLFDNKESLQPLWKQVQGFKEAIYPIMQNAGRDGVHLLCYSQGGLICRGLLQTMPDHNVDTFISLSSPQMGQYGDTDYLRYLFPTYVKSNLYRLCYTQMGQTFSICNFWNDPHHHGIYVNVSDFLAPLNSERPEPNATDWKKNFLRLRKMVLIGGPDDGVITPWESSHFGFYDENETVLEMKYQMVYQDDTFGLRSMDYRGAITVYGVPGVVHTMWHSNQTVFKNCIEKWLT | Function: Removes thioester-linked fatty acyl groups from various substrates including S-palmitoyl-CoA. Has the highest S-thioesterase activity for the acyl groups palmitic and myristic acid followed by other short- and long-chain acyl substrates. However, because of structural constraints, may be unable to remove palm... |
Q6GNY7 | MRGYLLLLPLLLCLVDNSVSYKPVILVHGLLSSSKSFDKLIQFIKKAHPGTDIYPVDMFNHLKSLNPMWKQVYEIRKYISPIIKNAGLKGVHLICYSQGGLICRGLLETMPEHNVDTFIALSSPLMGQYGMTLYVQKALPLVNISALQEVCYRKFFKEISICGYWRDPHRYEKYLEYSAFLPKLNNELLDSNSTERKRNFLRLRKLVLIGGPDDEVIAPWQSSHFGFYNEKEEVVNMKDQMVYQKDTFGLQSLDGRGAITIYSVPGVLHASWPNNQTVFKNYIEKWLT | Function: Removes thioester-linked fatty acyl groups from various substrates including S-palmitoyl-CoA. Has the highest S-thioesterase activity for the acyl groups palmitic and myristic acid followed by other short- and long-chain acyl substrates. However, because of structural constraints, may be unable to remove palm... |
Q8H0T6 | MFALTFLNPNPRLPSPLFLAKSTPESALSRRSRAFSSSNSYPWRPNLRFNGFKLKSATVPENVEGGDLESGSLVKGLKLGGMFGVWYLLNIYYNIFNKQVLRVYPYPATVTAFQLGCGTLMIAIMWLLKLHPRPKFSPSQFTVIVQLAVAHTLGNLLTNVSLGRVNVSFTHTIKAMEPFFTVLLSVLLLGEWPSLWIVCSLLPIVAGVSLASFTEASFNWIGFCSAMASNVTNQSRNVLSKKFMVGKDALDNINLFSIITIISFILLVPLAILIDGFKVTPSHLQVATSQGLSVKEFCIMSLLAGVCLHSYQQVSYMILE... | Function: Phosphoenolpyruvate/phosphate translocator that transports phosphoenolpyruvate (PEP), 2-phosphoglycerate and 3-phosphoglycerate.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 42054
Sequence Length: 383
Subcellular Location: Plastid
|
P07782 | MTEGVGLPLWLLAELTYRCPLQCPYCSNPLDYAQHKNELTTQEWFDVFDQARQMGAVQLGFSGGEPLVRQDLEQLVAHAHQQGFYTNLITSGMGLTEQRIADLKQAGLDHIQVSFQASDPVVNDALAGSKHAFEQKYEMCRLVKKYDYPMVLNFVIHRHNIDQIEQIIELCLELNADTVELAICQFYGWAFLNRQGLLPTQEQLTRAERITNEYREKLKAQNHPCKLIFVVPDYYEERPKACMNGWGKIFFTVAPDGMALPCHAARQLPISFPNVREHKLSDIWYKSTGFNHFRGDAWMPEGCRSCPDKDRDFGGCRCQA... | Cofactor: Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine.
Function: Catalyzes the cross-linking of a glutamate residue and a tyrosine residue in the PqqA protein as part of the biosynthesis of pyrroloquinoline quinone (PQQ).
Catalytic Activity: [PQQ pre... |
Q9FF29 | MVEGFSLSLMFLLVSHFFVSGVMSRNFTIENKCDYTVWPGFLTMTTAVSLPTNGFSLKKGESRVINVPPSWSGRLWGRSFCSTSSTGNFSCATGDCGSGKIECSDSGARPPTTLIDFTLDATDGQDFYDVSVVDGYNLPLVVVPQRLGSGRTCSNVGCVVNLNKTCPSELKVMGSSNKEHPIACMNACQKFGLPEFCCYGEYGKPAKCQPTLYSTNFKNECPLAYSYAYDNENNTFRCSNSPNYVITFCPNDISSMSQPSKETNGGTKQKSSWKLKLIVGVSAALTLMILIVVVIIVRTKNMRNSEWNDQNVEAVAMLKR... | Function: Possesses kinase activity in vitro.
PTM: Autophosphorylated in vitro.
Location Topology: Single-pass type I membrane protein
Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Sequence Mass (Da): 73952
Sequence Length: 665
Subcellular Location: Membrane
EC: 2.7.11.1
|
P03319 | MPRLQQKWLNSRECPTPRGEAAKGLFPTKDDPSAHKRVSPSDKDIFILCCKLGIALLCLGLLGEVAVRARRALTLDSFNSSSVQDYNLNNSENSTFLLRQGPQPTSSYKPHRFCPSEIEIRMLAKNYIFTNKTNPIGRLLVTMLRNESLSFSTIFTQIQKLEMGIENRKRRSTSIEEQVQGLLTTGLEVKKGKKSVFVKIGDRWWQPGTYRGPYIYRPTDAPLPYTGRYDLNWDRWVTVNGYKVLYRSLPFRERLARARPPWCMLSQEEKDDMKQQVHDYIYLGTGMHFWGKIFHTKEGTVAGLIEHYSAKTYGMSYYE | Function: Superantigen.
Location Topology: Single-pass type II membrane protein
Sequence Mass (Da): 36853
Sequence Length: 319
Subcellular Location: Membrane
|
Q9QZP2 | MNDMNLSPVGMEQLSSSSVSNALPVSGSHLGLAASPSHSAIPAPGLPVAIPNLGPSLSSLPSALSLMLPMGIGDRGVMCGLPERNYTLPPPPYPHLESSYFRTILPGILSYLADRPPPQYIHPNSINVDGNTALSITNNPSALDPYQANGNVGLELGIVSIDSRSVNTHGAQSLHPNDGHEVALDTTITMENVSRVTSPISTDGMAEELTMDGVTGEHSQIPNGSRSHEPLSVDSVSNNLTADTVGHGGVIPIHGNGLELPVVMETDHIANRVNGISDSVLSDSIHTVAMSTNSVSVALSTSHNFASLESVSLQEVGLSL... | Function: May function as a transcription factor involved in cell differentiation.
Sequence Mass (Da): 87392
Sequence Length: 798
Subcellular Location: Nucleus
EC: 2.1.1.-
|
Q9NQX1 | MLGMYVPDRFSLKSSRVQDGMGLYTARRVRKGEKFGPFAGEKRMPEDLDENMDYRLMWEVRGSKGEVLYILDATNPRHSNWLRFVHEAPSQEQKNLAAIQEGENIFYLAVEDIETDTELLIGYLDSDMEAEEEEQQIMTVIKEGEVENSRRQSTAGRKDRLGCKEDYACPQCESSFTSEDILAEHLQTLHQKPTEEKEFKCKNCGKKFPVKQALQRHVLQCTAKSSLKESSRSFQCSVCNSSFSSASSFEQHQETCRGDARFVCKADSCGKRLKSKDALKRHQENVHTGDPKKKLICSVCNKKCSSASSLQEHRKIHEIF... | Function: Sequence-specific DNA-binding transcription factor. Represses transcription at least in part by recruitment of the histone methyltransferase EHMT2/G9A and histone deacetylases such as HDAC1. Regulates hematopoiesis-associated protein-coding and microRNA (miRNA) genes. May regulate the expression of proteins i... |
Q9CXE0 | MLGMYVPDRFALKSSRVQDGMGLYTARRVRKGEKFGPFAGEKRMPEDLDENMDYRLMWEVRGSKGEVLYILDATNPRHSNWLRFVHEAPSQERKNLAAIQEGENIFYLAVDDIETDTELLIGYLDSDVEAEEEEQQALTMTKEGKVDHSKGQLAAGSKGHLGCEEDFACPQCESSFPSEEVLTEHLQSLHQKPTGEKEFKCENCGKKFPVRQALQRHFEQHRKACRGEARFVCKADSCGKRLKSKDALRRHQENVHTGDPKRKLICSVCNRKCTSVSSLQEHRKIHEIFDCQECMKKFISANQLKRHMITHSEKRPYNCE... | Function: Sequence-specific DNA-binding transcription factor. Represses transcription at least in part by recruitment of the histone methyltransferase EHMT2/G9A and histone deacetylases such as HDAC1. Regulates hematopoiesis-associated protein-coding and microRNA (miRNA) genes (By similarity). May regulate the expressi... |
Q9NQX0 | MLKPGDPGGSAFLKVDPAYLQHWQQLFPHGGAGPLKGSGAAGLLSAPQPLQPPPPPPPPERAEPPPDSLRPRPASLSSASSTPASSSTSASSASSCAAAAAAAALAGLSALPVSQLPVFAPLAAAAVAAEPLPPKELCLGATSGPGPVKCGGGGGGGGEGRGAPRFRCSAEELDYYLYGQQRMEIIPLNQHTSDPNNRCDMCADNRNGECPMHGPLHSLRRLVGTSSAAAAAPPPELPEWLRDLPREVCLCTSTVPGLAYGICAAQRIQQGTWIGPFQGVLLPPEKVQAGAVRNTQHLWEIYDQDGTLQHFIDGGEPSKS... | Function: Putative histone methyltransferase that acts as a transcriptional repressor of smooth muscle gene expression. Promotes the transition from differentiated to proliferative smooth muscle by suppressing differentiation and maintaining the proliferative potential of vascular smooth muscle cells. Also plays a role... |
Q9NQW5 | MSPERSQEESPEGDTERTERKPMVKDAFKDISIYFTKEEWAEMGDWEKTRYRNVKMNYNALITVGLRATRPAFMCHRRQAIKLQVDDTEDSDEEWTPRQQVKPPWMAFRGEQSKHQKGMPKASFNNESSLRELSGTPNLLNTSDSEQAQKPVSPPGEASTSGQHSRLKLELRRKETEGKMYSLRERKGHAYKEISEPQDDDYLYCEMCQNFFIDSCAAHGPPTFVKDSAVDKGHPNRSALSLPPGLRIGPSGIPQAGLGVWNEASDLPLGLHFGPYEGRITEDEEAANSGYSWLITKGRNCYEYVDGKDKSSANWMRYVN... | Function: Histone methyltransferase that selectively methylates 'Lys-4' of dimethylated histone H3 (H3K4me2) to produce trimethylated 'Lys-4' histone H3 (H3K4me3). May play a role in epigenetic regulation of gene expression by defining an active chromatin state.
Catalytic Activity: N(6),N(6)-dimethyl-L-lysyl(4)-[histon... |
Q9NQV8 | MEDTGIQRGIWDGDAKAVQQCLTDIFTSVYTTCDIPENAIFGPCVLSHTSLYDSIAFIALKSTDKRTVPYIFRVDTSAANGSSEGLMWLRLVQSARDKEEQNLEAYIKNGQLFYRSLRRIAKDEELLVWYGKELTELLLLCPSRSHNKMNGSSPYTCLECSQRFQFEFPYVAHLRFRCPKRLHSADISPQDEQGGGVGTKDHGGGGGGGKDQQQQQQEAPLGPGPKFCKAGPLHHYPSPSPESSNPSAAAGGSSAKPSTDFHNLARELENSRGGSSCSPAQSLSSGSGSGGGGGHQEAELSPDGIATGGGKGKRKFPEEA... | Function: Probable histone methyltransferase, preferentially acting on 'Lys-9' of histone H3 (By similarity). Involved in the control of steroidogenesis through transcriptional repression of steroidogenesis marker genes such as CYP17A1 and LHCGR (By similarity). Forms with BHLHE22 a transcriptional repressor complex co... |
Q8BZ97 | MEDSGIQRGIWDGDAKAVQQCLTDIFTSVYTTCDIPENAIFGPCVLSHTSLYDSIAFVALKSTDKRTVPYIFRVDTSAANGSSEGLMWLRLVQSARDKEEQNLEAYIKNGQLFYRSLRRIAKDEELLVWYGKELTELLLLCPSRAHKMNGSSPYTCLECSQRFQFEFPYVAHLRFRCPKRLHSTDANPQDEQGGGLGTKDHGGGGGGKEQQQQQQQQQQEAPLIPGPKFCKAGPIHHYPASSPEASNPPGSAGAGSAKPSTDFHNLARELENSRGSSSCVAAPGVGSGGSGHQEAELSPDGVATGGCKGKRRFPEEAAAE... | Function: Probable histone methyltransferase, preferentially acting on 'Lys-9' of histone H3 . Histone methyltransferase activity has not been confirmed in other species. Involved in the control of steroidogenesis through transcriptional repression of steroidogenesis marker genes such as CYP17A1 and LHCGR . Forms with ... |
Q6P2A1 | MSLSPDLPPSEEQNLEIQGSATNCYSVVIIEEQDDTFNDQPFYCEMCQQHFIDQCETHGPPSFTCDSPAALGTPQRALLTLPQGLVIGRSSISHAGLGVFNQGQTVPLGMHFGPFDGEEISEEKALDSANSWVICRGNNQYSYIDAEKDTHSNWMKFVVCSRSETEQNLVAFQQNGRILFRCCRPISPGQEFRVWYAEEYAQGLGAIWDKIWDNKCISQGSTEEQATQNCPCPFCHYSFPTLVYLHAHVKRTHPNEYAQFTQTHPLESEAHTPITEVEQCLVASDEALSTQTQPVTESPQEQISTQNGQPIHQTENSDEP... | Function: Histone methyltransferase that sequentially mono-, di-, and tri-methylates both 'Lys-4' (H3K4) and 'Lys-36' (H3K36) of histone H3 to produce respectively trimethylated 'Lys-4' (H3K4me3) and trimethylated 'Lys-36' (H3K36me3) histone H3 and plays a key role in meiotic prophase by determining hotspot localizatio... |
Q9NQV7 | MSPEKSQEESPEEDTERTERKPMVKDAFKDISIYFTKEEWAEMGDWEKTRYRNVKRNYNALITIGLRATRPAFMCHRRQAIKLQVDDTEDSDEEWTPRQQVKPPWMALRVEQRKHQKGMPKASFSNESSLKELSRTANLLNASGSEQAQKPVSPSGEASTSGQHSRLKLELRKKETERKMYSLRERKGHAYKEVSEPQDDDYLYCEMCQNFFIDSCAAHGPPTFVKDSAVDKGHPNRSALSLPPGLRIGPSGIPQAGLGVWNEASDLPLGLHFGPYEGRITEDEEAANNGYSWLITKGRNCYEYVDGKDKSWANWMRYVN... | Function: Histone methyltransferase that sequentially mono-, di-, and tri-methylates both 'Lys-4' (H3K4) and 'Lys-36' (H3K36) of histone H3 to produce respectively trimethylated 'Lys-4' (H3K4me3) and trimethylated 'Lys-36' (H3K36me3) histone H3 and plays a key role in meiotic prophase by determining hotspot localizatio... |
Q96EQ9 | MNTNKLEENSPEEDTGKFEWKPKVKDEFKDISIYFSKEEWAEMGEWEKIRYRNVKRNYKMLISIGLRAPRPAFMCYQRQAMKPQINDSEDSDEEWTPKQQVSPPWVPFRVKHSKQQKESSRMPFSGESNVKEGSGIENLLNTSGSEHVQKPVSSLEEGNTSGQHSGKKLKLRKKNVEVKMYRLRERKGLAYEEVSEPQDDDYLYCEKCQNFFIDSCPNHGPPLFVKDSMVDRGHPNHSVLSLPPGLRISPSGIPEAGLGVWNEASDLPVGLHFGPYEGQITEDEEAANSGYSWLITKGRNCYEYVDGQDESQANWMRYVN... | Function: Histone methyltransferase that sequentially mono-, di-, and tri-methylates both 'Lys-4' (H3K4) and 'Lys-36' (H3K36) of histone H3 to produce respectively trimethylated 'Lys-4' (H3K4me3) and trimethylated 'Lys-36' (H3K36me3) histone H3 and plays a key role in meiotic prophase by determining hotspot localizatio... |
Q8PTX6 | MISEVDMDDNFLGLRARDEFYSGKHIHRASQLILLDPENRILLQKRSPGKFWFPNRYTYSVSGTVADESYEACIAREMLEEIGISVPFRRLFKIPCIRENKGAYHTIFSGRCSEEAASLIRHDLEEATSIEWVELEELHRAVKAEPGNYTPALREGIIKIFKEGCEKYLF | Function: Hydrolyzes homoallylic isopentenyl diphosphate (IPP), its allylic isomer dimethylallyl diphosphate (DMAPP) and short-chain prenyl diphosphates geranyl diphosphate (GPP) and farnesyl diphosphate (FPP) to their corresponding monophosphate forms with high activity. The preferred substrate is IPP. ADP, NADPH, Ap5... |
Q5E947 | MSSGNAKIGHRAPQFKATAVMPDGQFKDISLADYKGKYVVFFFYPLDFTFVCPTEIIAFSDRAEEFKKLNCQVIGASVDSHFCHLAWINTPKKQGGLGPMNIPLISDPKRTIAQDYGVLKADEGISFRGLFIIDDKGILRQITINDLPVGRSVDETLRLVQAFQFTDKHGEVCPAGWKPGSDTIKPDVQKSKEYFSKQK | Function: Thiol-specific peroxidase that catalyzes the reduction of hydrogen peroxide and organic hydroperoxides to water and alcohols, respectively. Plays a role in cell protection against oxidative stress by detoxifying peroxides and as sensor of hydrogen peroxide-mediated signaling events. Might participate in the s... |
P0CB50 | MSSGKAFIGKPAPDFTATAVMPDGQFKDIKLSDYRGKYVVFFFYPLDFTFVCPTEIIAYSDRADEFKKINCEIIGASVDSHFCHLAWINTPKKQGGLGTMKIPLVSDTKRVIAKDYGVLKEDEGIAYRGLFIIDEKGILRQITINDLPVGRSVDETLRLVQAFQFTDKHGEVCPAGWKPGSDTIKPDVQKSKEYFSKQK | Function: Thiol-specific peroxidase that catalyzes the reduction of hydrogen peroxide and organic hydroperoxides to water and alcohols, respectively. Plays a role in cell protection against oxidative stress by detoxifying peroxides and as sensor of hydrogen peroxide-mediated signaling events. Might participate in the s... |
Q6DV14 | MSSGNAYIGKLAPDFQATAVMPDGQFKEIKLSDYKGKYVVLFFYPLDFTFVCPTEIIAFSDRSEEFRKINCEVIGASVDSHFCHLAWINTPKKQGGLGSMHIPLVSDTKRVIAKDYGILKEDEGISYRGLFIIDDKGTLRQITINDLPVGRSVDETLRLVQAFQFTDKHGEVCPAGWQPGSDTIKPDVQKSKEYFSKHK | Function: Thiol-specific peroxidase that catalyzes the reduction of hydrogen peroxide and organic hydroperoxides to water and alcohols, respectively. Plays a role in cell protection against oxidative stress by detoxifying peroxides and as sensor of hydrogen peroxide-mediated signaling events. Might participate in the s... |
P03193 | MSAPVVIKALVASNTDIAEAILDAILSRPDEGFRLFCLCHNASPLHHVAGSLVELQLHLPKKRLTSQSRCGLVLTLHLPAEEAFPFLRGLTPLTADRLSTYLDRAGALRSLTPLVELLTLSAKKQPQGDARGRVAWLRPKIVGCLRRIYRVNISARWFISTFGSHEAQFVLVTAAYYFWGIPCTIETLAHLTELFTSESGQSLAAVTSLAELGEVFGSSAWAEQTEAFAHFAHEKLRRDSREIRAVARTIDAYRGRLPLASADLVRYVYLAHAQCFNEGTFKRYSQLTSMGEIGCLPSGGVVLPSLLDRGFAEHMRTYFT... | Function: Essential component of the helicase/primase complex. Unwinds the DNA at the replication forks and generates single-stranded DNA for both leading and lagging strand synthesis. The primase initiates primer synthesis and thereby produces large amount of short RNA primers on the lagging strand that the polymerase... |
Q66658 | MATGRSTSTESSEKTCQQRDPLPEYRALCGTDGDAAEILTDVLTNTDSDGVVFCLAHNCYSYNIGGGEALLTLCLPAKRPWGAEKCLPVIQFRCDASRAQEFLFQGRPIPVRYIQTNLNHRAVKKFFKPILSVLTCSDKKGGGGEGAHADLKSTIFWFRAKFVAAVRKTFKITASPFWMISTFGCTEAQFVLVSSCYFFERHECTIDTLSHLSRLFDGSRGRQLTTVNTFSDLAGMFGTSAWLGRVPEFSAYVGKKLARDDLESAAVDEAVNAFRGQLMLSNADLIHYIYLSFFQCLNKEKFLEYSLRTNPHNIDGVPPE... | Function: Essential component of the helicase/primase complex. Unwinds the DNA at the replication forks and generates single-stranded DNA for both leading and lagging strand synthesis. The primase initiates primer synthesis and thereby produces large amount of short RNA primers on the lagging strand that the polymerase... |
Q18LF7 | MTIQVLFATEYDSANIVISLLCGVEVDHDLYPILYKRINYNNGASNNDGSRSGAINFDDRVNDEDSRLNAPVDDTIEFCLQTQSCEDSIRIRPVFYCHAHALNFETRYRTHEVLGSATLLQCLDESRTLTMYRRILSEIITEPSSASEKRNPAPTNLRHLVYFHRDVLVKYLTENFIMPTSPAWFISVFGSYEASLVLTMHYYLLERQYSTVQTTQHYAKCFTGDMGKPLVSCYSMKDFMIMIQSSAFLGKTAKFTHYCKLKNDRDLQELMAIDASINAFRQNVCLTEAEHVHFMYLAFGTALAKTKFLDYTLKTSLLSN... | Function: Essential component of the helicase/primase complex. Unwinds the DNA at the replication forks and generates single-stranded DNA for both leading and lagging strand synthesis. The primase initiates primer synthesis and thereby produces large amount of short RNA primers on the lagging strand that the polymerase... |
P17149 | MTLVLFATEYDSAHIVANVLSQTPTDHCVFPLLVKHQVSRRVYFCLQTQKCSDSRRVAPVFAVNNETLQLSRYLAARQPIPLSALIASLDEAETQPLYRHLFRTPVLSPEHGGEVREFKHLVYFHHAAVLRHLNQVFLCPTSPSWFISVFGHTEGQVLLTMAYYLFEGQYSTISTVEEYVRSFCTRDLGTIIPTHASMGEFARLLLGSPFRQRVSAFVAYAVARNRRDYTELEQVDTQINAFRERARLPDTVCVHYVYLAYRTALARARLLEYRRVVAYDADAAPEAQCTREPGFLGRRLSTELLDVMQKYFSLDNFLHD... | Function: Essential component of the helicase/primase complex. Unwinds the DNA at the replication forks and generates single-stranded DNA for both leading and lagging strand synthesis. The primase initiates primer synthesis and thereby produces large amount of short RNA primers on the lagging strand that the polymerase... |
P52540 | MTIVVFATEYDAANVIFSILCRSPSEHLIFPIIVKYKPSNNVSFCLQTQKCKNSKRIDTVFVCHAEKLNLSHYIQTASPIKAEDVANSLNDKETELLYVDMILSQTGKEKEDVEFKYMAYFHKSLIIKYLTGKFLLPTSPFWFLSTYGQTEGLLLLTMYYYLFEEQKSTITTTKNYVQCFTENTGSMVFTYSSMSEFINITLKSKFRKLFADFATYARQKNLRDKEEFKYLDTQINLFRKSSHLTNTFRVHYIYIAYNTALETTKFVNYCNITSYDSNLPIGQQCQRNVHILGNSLHENLLCIMKQYFNADCYFKTYIDI... | Function: Essential component of the helicase/primase complex. Unwinds the DNA at the replication forks and generates single-stranded DNA for both leading and lagging strand synthesis. The primase initiates primer synthesis and thereby produces large amount of short RNA primers on the lagging strand that the polymerase... |
F5HIN0 | METTYRREALTVRVIFCTSGDSAETIADVLTGAPTSASFFSVLHDLFYSQILAPRVTLKLCLPARRPGNGTRCSPVLVLRTDASVASGFLGGRPLEASDIKYMLLSDQTAGLFKPLLEIIGGARAPPNQDACTFQSQVAWLRTKFVTALRKLYKMTPSPYWMLSAFGAQEAQFVLTSSFYFFEHTVVCTTETVSHLSRLFSPQQGQTLVSVTSHEELGQLYGTSPFRRRVPAFVAYVKEKLARDSLETEAIDRTIDQIRGKLMLSNQDLVHFIYISFYQCLNKRAFLRYSRQTSSSSALRELGEDPQLCGALHGEFRDHV... | Function: Essential component of the helicase/primase complex. Unwinds the DNA at the replication forks and generates single-stranded DNA for both leading and lagging strand synthesis. The primase initiates primer synthesis and thereby produces large amount of short RNA primers on the lagging strand that the polymerase... |
Q69153 | MTVVLFATEYDTPNIVVNMLSETPTEHHLFPLMIKYKPSNRIEFVLQTQRCPDSTRVRPVFICDARRLSLSEYVSTNTPLPARVICAGIDADATRELYEHLFDRKKDETGHDEENGSAARHLFSNLTSTLKCLVHYNRSAILRYLNNTFLSPTFPSWFLSTYGTHEGTLILTMSYYLFERTYSTIQTTRDYTKCFTADPGRNLFTYINMRDFMATMNGSRFRKQTVLFAVFAKARNARDRCELEYVDAKINAFREESRLAADSCVYYVYLAYRTALCREKFLQYCEHTAYDKNLPDDQQCAAEENYLGRSLDAELISIMN... | Function: Essential component of the helicase/primase complex. Unwinds the DNA at the replication forks and generates single-stranded DNA for both leading and lagging strand synthesis. The primase initiates primer synthesis and thereby produces large amount of short RNA primers on the lagging strand that the polymerase... |
P14346 | MNEATEAWPKFKVLFATDGDSAEIITDILTGTDTNAFIYSVLHNCYIYPTEVKIVLILCLPAKKPGGGDKCLEVFQLHIDTELAIPFLFYTKPLKANDLHKYIDFKAARKNFKPILDIISTNKPSPKTHNSDIKSKIVWFRAKFVNSLRKLYKISSSPYWMITTFGSFEVPFLLTAIFYFFEQHNCTINTIFHLSSLFEKKLGTSLIAITTFEELGGVCSTSDYLKTAPAFINYCHIKLARDSLESQAIDTSIDTLRGQLMLSNQDLVHYIYLSFFQCLNKDIFIKYSHLTNSDNIHFVPETEVLAQSLDENFRKDMLTY... | Function: Essential component of the helicase/primase complex. Unwinds the DNA at the replication forks and generates single-stranded DNA for both leading and lagging strand synthesis. The primase initiates primer synthesis and thereby produces large amount of short RNA primers on the lagging strand that the polymerase... |
Q5A961 | MPQPPPNAYKAGTRLTVGSHKVSIIKYISEGGFAHVYTCTIDPPFQGSTVACLKRVVVPSKWQLSLLRQEVDAMRRLRGNKHIVSYIDSHASRLGDSNTSGTNHSQQQQYEVFLLMEYCENNGLIDFMNTRLVNKLTEKEIIDIMYQVTIGVAMCHHLRPPLIHRDIKIENVLIDGKGVFKLCDFGSSVNYLPPPRNPQELQLMKDDLMQHTTPQYRAPEMIDLSKGFPIDDKSDIWALGIFLYKLCYYTTPFERPNQSSLQELEHTILNCSETLRFSDQPGSIFSPRLKNAIKVCLRADPRRRPNAVQLLGEIAAMKGE... | Function: Protein kinase involved in regulation of actin cytoskeleton organization and endocytosis. Phosphorylates the endocytic protein SLA1. The CDC28-CLN3 complex phosphorylation of SLA1 enhances its further phosphorylation by PRK1, weakening SLA1 association with PAN1, an activator of the actin-nucleating ARP2/3 co... |
Q40902 | MMTEVHDAGRPRVVIFNGSQLQREAIIPFASRSSCFHHQLCSRGHLLIIFLLLVSPFNDAAVDVDGDDNDNLIIDHVPDAKSSSEALLNFKSSLSTSSPRGHEVLGSWIPSNSPCSGNNGNWLGVLCYEGDVWGLQLENLDLSGVIDIDSLLPLHFLRTLSFMNNSFKGQCLIGISLEPSSHCTCPIIASPVRSRMMLPGYDLSQEALFGKQPIQRQHPHLPGYLLPQVFELSLENNRFTGSIPHFPPNVLKVLNLSNNQLEGPIPPALSLMDPTTFSGNKGLCGKPLESACNSPSQEANNPDSRNSSTISGQSSTDVIR... | Function: Dual-specificity kinase with both serine/threonine and tyrosine kinase activities . Required for postmeiotic development of microspores (Ref.2). Involved in embryo sac development at the late stages of megagametogenesis (Ref.3). Involved in the phosphorylation of KIP1 .
PTM: Autophosphorylated.
Location Topol... |
P40494 | MNTPQISLYEPGTILTVGSHHAKIIKYLTSGGFAQVYTAEISPPDPYSNANIACLKRVIVPHKQGLNTLRAEVDAMKLLRNNKHVVSYIDSHAARSVNGIAYEVFVLMEFCERGGLIDFMNTRLQNRLQESEILEIMSQTVQGITAMHALQPPLIHRDIKIENVLISHDGLYKVCDFGSVSGVIRPPRNTQEFNYVQHDILTNTTAQYRSPEMIDLYRGLPIDEKSDIWALGVFLYKICYYTTPFEKSGEAGILHARYQYPSFPQYSDRLKNLIRLMLMEAPSQRPNICQVLEEVSRLQNKPCPIRNFYLLRAMNQNANT... | Function: Protein kinase involved in the regulation of actin cytoskeleton organization and endocytosis . Phosphorylates PAN1 which disrupts the interaction between PAN1 and END3, and between PAN1 and SLA1 . Phosphorylates SCD5 . Preferentially, phosphorylates substrates on threonine residues in a [L/I/V/M]-x-x-[Q/N/T/S... |
Q9W735 | MLWKTALIFLCWGLTSGELQNGLSATPAAPARRTLDFGFVPSGVYDTVAYYEPGAIGILFNMMHAFLFVVQPNPFPEDLVISAAKDKFGAIQSEYQKVIYYELGFVVCAALGLLFTVLLPLVGLLFCLCRCCDNCGGEMHQRQRKNADCLRGLLTTLLLTTTFIITAGVLCAYAANQNLSSQLKGMRRLVKSNLKDLHTFANQTPAQIDYLISRYGTVKEQVLHDLENVGVILGGRIHEELGKEVKPALDATLSMTGTMRDTKDALENVSLTLETLQEGTVKLQANLSVVRNSLRNALNDPVCVDAPAPEICRNIRNSIP... | Function: May play a role in cell differentiation, proliferation and apoptosis. Binds cholesterol in cholesterol-containing plasma membrane microdomains and may play a role in the organization of the apical plasma membrane in epithelial cells. Involved in regulation of MAPK and Akt signaling pathways (By similarity).
L... |
A6QWA0 | MKFSRFIPRSRTPGLPAYGEQEPNTFENGYRPSPPPGAITPYLGLRSRLSQIWFNRWTILLLLILARVLVAIGSLDGNLVSAKREALSACSSVESVGSTMASMPHYMAQGVNELTATGVEKAINGLMSMLELTVTGVEEIFVFFVNVMTQTYLCLITLVVSGMMNAAIDVLKKATEFLDDITGKLGNAIGDGISDFEDAINGFGDVINMFGTKLPKLNLDGPIKELENLSLPDGLTDDLNKLKEKIPNFEDVNNFTNNALRMPFELVKKLIRDEIDDYKFDRSVFPVPAKEQLQFCNEEGGIHSFFNKLASLTSTAKKIF... | Function: Involved in cell fusion during mating by stabilizing the plasma membrane fusion event.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 81106
Sequence Length: 736
Subcellular Location: Cell membrane
|
B9MJY9 | MRWYEISIKTTEEAEDAISNILYELGANGVVIEDNEIVTRPNLWDYIDENQFTKKDYARVCAYFPESSNILELTHTIEERLKETAKYIDIGEGKISVSEVNEKDWAEEWKKYYKPVEIGNIVIVPSWEDYKAEGNKTIVKLDPGMAFGTGTHESTILCLEAIQKYVKPGMDVLDVGTGSGILAIAAKKFLARRVLAVDIDEVAVKVAEENARLNGVEIEIKKNDLVEGIEEKFDVVVANIVADIIMRLSRDVKKVLKDDRIFISSGIIEDRLEDVLKSFEKNSLEIVEVKKLGTWCLVVSKKTV | Function: Methylates ribosomal protein L11.
Catalytic Activity: L-lysyl-[protein] + 3 S-adenosyl-L-methionine = 3 H(+) + N(6),N(6),N(6)-trimethyl-L-lysyl-[protein] + 3 S-adenosyl-L-homocysteine
Sequence Mass (Da): 34366
Sequence Length: 304
Subcellular Location: Cytoplasm
EC: 2.1.1.-
|
Q8RB66 | MKWLEIQVTTSQEAEEAVTGILYDLGAGGVVIKNPNDVKELAQTSEWDYFDPSLLEEGEEVKISAYFLITTDITDKVNFLKERIWELKSFGINVGNVKVEVSEVDEEDWADSWKKYYKPLKVGKRIVVRPLWEEYSPKEGEIVIDLDPGMAFGTGTHETTKMCLQFLEDIVKPGAIVFDVGCGSGILSIAASKLGASYVYGADVDEMAVKIARENVKLNGLENVEIFQSDLLKNFRGKADVIVANIIADAIIRLIPDVLPHLKEEGLFLASGIIKDRFEEVKERAEEFFEIIDMKEEKEWLSILMKKKG | Function: Methylates ribosomal protein L11.
Catalytic Activity: L-lysyl-[protein] + 3 S-adenosyl-L-methionine = 3 H(+) + N(6),N(6),N(6)-trimethyl-L-lysyl-[protein] + 3 S-adenosyl-L-homocysteine
Sequence Mass (Da): 34776
Sequence Length: 309
Subcellular Location: Cytoplasm
EC: 2.1.1.-
|
A7ZES6 | MKDKFYELSIKTSNFYDEILELVFSFGVTCVEELDHEIIIREEYDLKDIAWGVEEYAKGLSSVRKISNDLKISLNLKENKDWLGEYKRAVKPILVDKIYIRPSWEESLSGVTNIIIDPALAFGSGHHESTNSCLQLLQKYAKSGDTALDVGCGSGILSIALAKLGCKVDACDTDEQATQSSLSNAQLNEVKFNKIWTGSIANLEQKYDIVVANIIADVIFMLSNDLKKSLKKGGYLVLSGILNKYEDRIKDTFKDLELVEIKQANDWVSFVYKEMDE | Function: Methylates ribosomal protein L11.
Catalytic Activity: L-lysyl-[protein] + 3 S-adenosyl-L-methionine = 3 H(+) + N(6),N(6),N(6)-trimethyl-L-lysyl-[protein] + 3 S-adenosyl-L-homocysteine
Sequence Mass (Da): 31218
Sequence Length: 277
Subcellular Location: Cytoplasm
EC: 2.1.1.-
|
Q9PNH7 | MQKKYYELFFIVEEQYKNLFLDFAFDLGIEAIEEKDNGVYIRSHESLEEFSWALEIFAQKLTTTFNLNHKIISNLSLVEKENKDWIQEYKKGIKPILVDNVYIHTTWQEEKKNCINIKINPALAFGSGHHESTYSCVKFLQKFSKSKLRALDLGCGSGILGIIMAKFGCNVEICDTDELAIDSSLENARLNGVDFHKAWCGSIDKANGLYNLIVANIIADVILILEKDIKNHLEDNAILILSGILDKYSTRIKEKFQDLELIDEMQINEWCSFVYKNNKKG | Function: Methylates ribosomal protein L11.
Catalytic Activity: L-lysyl-[protein] + 3 S-adenosyl-L-methionine = 3 H(+) + N(6),N(6),N(6)-trimethyl-L-lysyl-[protein] + 3 S-adenosyl-L-homocysteine
Sequence Mass (Da): 32323
Sequence Length: 281
Subcellular Location: Cytoplasm
EC: 2.1.1.-
|
Q133Y8 | MTETASTRASFVIGDEAAARRVTDLLGESFDDGELAIAAFERPDRSWEVSLHFGEMPNLDGVRALVAQAAGDAAAAAMTVESIAAKDWVAASLEGLVPVPAGRFVVHGSHDRARIPSNKLGIEIEAALAFGTGHHGTTRGCLTLLDLVLRAGPPRSVLDLGTGTGVLAIAAAKALRQPVLATDIDRQSVAVAKENARLNGVGNLVEAVHATGFSAPVFAAWGPFDLVLANILANPLRQLSTPMSQHLAPSALVILSGLLQPQAQSVIAAYRARGCVLLRQIVIEGWSSLLLAKTF | Function: Methylates ribosomal protein L11.
Catalytic Activity: L-lysyl-[protein] + 3 S-adenosyl-L-methionine = 3 H(+) + N(6),N(6),N(6)-trimethyl-L-lysyl-[protein] + 3 S-adenosyl-L-homocysteine
Sequence Mass (Da): 30814
Sequence Length: 295
Subcellular Location: Cytoplasm
EC: 2.1.1.-
|
B8I303 | MKWYEVRVSTTDEASDAVSEMLTTMGAGGVAIKDPFDIKKEILKPNSLDYADDEFLESLGEDVVIQAYFQSGNDIDKLLKQINEGLVNISQFLNIGKGLEGYNEVDDEDWSTAWKKYYKPLQLTDRIVIKPTWEDYSPNADEIVIQMDPGMAFGTGTHETTQMCSILLDKYMKDDTEVLDIGCGTGILSIIAAKLGAKQVEAIDIDEVAVKVARENIELNQEITKVSARKAVLSDLKAEEHKYDIIVANIIANVIIDLSSQIPYYLKKESLFITSGIIKERKQEVIDACEKNGMSRIETLEMGEWVAMVFKCPDTL | Function: Methylates ribosomal protein L11.
Catalytic Activity: L-lysyl-[protein] + 3 S-adenosyl-L-methionine = 3 H(+) + N(6),N(6),N(6)-trimethyl-L-lysyl-[protein] + 3 S-adenosyl-L-homocysteine
Sequence Mass (Da): 35371
Sequence Length: 316
Subcellular Location: Cytoplasm
EC: 2.1.1.-
|
Q7ULT2 | MAETSNDTPWTVMRLLEWTTDFFRKKGSESPRLDAEILLAHARGCQRIELYTSFDKVPEEEQRVAFRELVRRRGEGAPVAQLVGYREFYSISIRVDENVLVPRPETEHLVIEAIDQIKGRLSDRPSPTVLDIGTGSGAIAVAIAKSLPKTQVTAVDISLTALDIAKWNVENLKLSDRVTLLQSDLFDGLEPDQTFDVICSNPPYISQSEYDELPTTVREFEPRGALLSGPDGTEIIARLLNDSVQRLNDGGQLIIELSPMIAGVSKTLAEQNGGYKEIHLIKDLAGHERILSMQKA | Function: Methylates the class 1 translation termination release factors RF1/PrfA and RF2/PrfB on the glutamine residue of the universally conserved GGQ motif.
Catalytic Activity: L-glutaminyl-[peptide chain release factor] + S-adenosyl-L-methionine = H(+) + N(5)-methyl-L-glutaminyl-[peptide chain release factor] + S-a... |
Q2RWE0 | MSDGDGGGEQGGGGPAEAEESALVLGRLLDRGAWRLKVAGVEKPRRDARLLAGHVLGLSPGAVLLADDRVVTPEEAQALEAVIARRETREPVSRILGHRGFWRFDLALGADTLDPRPDTETLVEAGLAVLEGCGGRILDLGTGSGCILLALLADRPGAIGLGIDIAPGAVRVALRNARALGLERRALFAVGDWAAAVAGPFDLIVSNPPYIPSADIAALEPEVARFDPSRALDGGADGLDPYRILAAQVPALLAPAGVLAVEFGQGQARDVAGLLEVGGLCPYEIKKDLSGEERCLLARRRAAGPLPPIHIDAKPSAPGN... | Function: Methylates the class 1 translation termination release factors RF1/PrfA and RF2/PrfB on the glutamine residue of the universally conserved GGQ motif.
Catalytic Activity: L-glutaminyl-[peptide chain release factor] + S-adenosyl-L-methionine = H(+) + N(5)-methyl-L-glutaminyl-[peptide chain release factor] + S-a... |
Q2S0V8 | MEHPPGSDAETAEASPTRLELIDRAARRLGAADRSAPRRTAEWLLAELLDCDRAHLYAHPDRTVAAAAAEQFHRMVGRRVQGEPLQHILGYASFYGLRLRVSPDVMVPRPETETVVDRALTCIEEVSRPRVLDAGTGSGCIALALKHERPDAEVHACDVSTDALAVARANAQDLGLDVRFFEGDLCAEVPAATPRDVDLLVSNPPYIPDAEAESLPPVVREYDPDRSLFAGRDPLRFYRALVRWVSACCVPGGSFVLEVHAEHAAEVERLFRGEEGVGAVHTEEDLSGRPRIVWGRTERATAS | Function: Methylates the class 1 translation termination release factors RF1/PrfA and RF2/PrfB on the glutamine residue of the universally conserved GGQ motif.
Catalytic Activity: L-glutaminyl-[peptide chain release factor] + S-adenosyl-L-methionine = H(+) + N(5)-methyl-L-glutaminyl-[peptide chain release factor] + S-a... |
Q8EAR4 | MADQSCIAEALQWAYVQLAASSESAHLDAEVLLLYCLNKNRAYLYTWPEKALSVEQWKRFQQMVQRRQQGVPVAHIVGEREFWSLPFIVNDTTLIPRPDTEILVESALNLPLESNAKVLDLGTGTGAIALALASERAAWQITAVDKVEDAVALAKANRTNLKLEQVEILQSDWFSAVTSHDFDLIVSNPPYIDEADEHLHQGDVRFEPQSALTAADEGFADLYYIAKTARDYLKPNGYILLEHGFEQAVKLRAKLIELGYQNVATVRDFGSNDRCTMGKWMGLIGI | Function: Methylates the class 1 translation termination release factors RF1/PrfA and RF2/PrfB on the glutamine residue of the universally conserved GGQ motif.
Catalytic Activity: L-glutaminyl-[peptide chain release factor] + S-adenosyl-L-methionine = H(+) + N(5)-methyl-L-glutaminyl-[peptide chain release factor] + S-a... |
Q2FWE1 | MVNYKEKLDEAIHLTQQKGFEQTRAEWLMLDVFQWTRTDFVVHMHDDMPKAMIMKFDLALQRMLLGEPIQYIVGFASFYGRTFDVNSNCLIPRPETEEVMLHFLQQLEDDATIVDIGTGSGVLAITLKCEKPDLNVIATDISLEAMNMARNNAEKHQSQIQFLTGDALKPLINEGIKLNGLISNPPYIDEKDMVTMSPTVTRFEPHQALFADNHGYAIYESIIEDLPHVMEKGSPVVFEIGYNQGEALKSIILNKFPDKKIDIIKDINGHDRIVSFKW | Function: Methylates the class 1 translation termination release factors RF1/PrfA and RF2/PrfB on the glutamine residue of the universally conserved GGQ motif.
Catalytic Activity: L-glutaminyl-[peptide chain release factor] + S-adenosyl-L-methionine = H(+) + N(5)-methyl-L-glutaminyl-[peptide chain release factor] + S-a... |
Q9K4E3 | MNLLLAEVAQATQRLADAGVPSPRTDAEELAAYLHGVKRGELHTVPDADFDARYWEVVARREAREPLQHITGRAYFRYLELQVGPGVFVPRPETESVVGWAIDAVRAMDVVEPCIVDLCTGSGAIALALAQEVPRSRVHAVELSEDALKWTRRNMEGSRVDLRQGDALTAFPDLDGQVDLVVSNPPYIPLTEWEYVAPEARDHDPELALFSGEDGLDLIRGLERTAHRLLRPGGVVVVEHADTQGGQVPWIFTEERGWADAADHPDLNNRPRFATARKALP | Function: Methylates the class 1 translation termination release factors RF1/PrfA and RF2/PrfB on the glutamine residue of the universally conserved GGQ motif.
Catalytic Activity: L-glutaminyl-[peptide chain release factor] + S-adenosyl-L-methionine = H(+) + N(5)-methyl-L-glutaminyl-[peptide chain release factor] + S-a... |
Q8DPZ3 | MKLAQLFSNFEEELIRQGEEAESLSFVYRSLKNLSFTDFIFALQQEVTTEEEKQFVEDIYQQLAAHKPAQYIIGQADFYGMHLKVDERVLIPRPETEELVELILTENLETNLSVLDIGTGSGAIALALAKNRPDWSVTAADISQEALDLARENAKNQNLQIFLKKSDCFTEISEKYDIIVSNPPYISREDESEVGLNVLYSEPHLALFADEDGLAIYRRIAEDATDYLKDSGKIYLEIGYKQGQCVPELFRKHLPEKRVRTLKDQFGQNRMVVVDDGQD | Function: Methylates the class 1 translation termination release factors RF1/PrfA and RF2/PrfB on the glutamine residue of the universally conserved GGQ motif.
Catalytic Activity: L-glutaminyl-[peptide chain release factor] + S-adenosyl-L-methionine = H(+) + N(5)-methyl-L-glutaminyl-[peptide chain release factor] + S-a... |
P74003 | MNKGFVSGEEFARWYATARQMAIAHGIETGELNWLLQGWTDLDRLTLRLQDFAHREIALQETWENIQRGWRRRVEEKYPVQYLLGQTQWRDFVIKVTDDVLIPRPETELIIDIVQHEHSALSPSNCADHWVDLGTGSGAIALGLAATFPQALVHAVDCSGSALAIARENAQLNQFGDRIQFHQGYWWEPLEHLKGQVQGMVSNPPYIPQRELAQLQPEVIKHEPLLALDGGPDGLQAVEQLIRRSPTYLKPGGFWLVEIMTGQAPMVAELLRASGAYQDIQIHRDLASIERFVSARTLS | Function: Methylates the class 1 translation termination release factors RF1/PrfA and RF2/PrfB on the glutamine residue of the universally conserved GGQ motif.
Catalytic Activity: L-glutaminyl-[peptide chain release factor] + S-adenosyl-L-methionine = H(+) + N(5)-methyl-L-glutaminyl-[peptide chain release factor] + S-a... |
Q9WYV8 | MDTRKNVSGAERKIWSLIRDCSGKLEGVTETSVLEVLLIVSRVLGIRKEDLFLKDLGVSPTEEKRILELVEKRASGYPLHYILGEKEFMGLSFLVEEGVFVPRPETEELVELALELIRKYGIKTVADIGTGSGAIGVSVAKFSDAIVFATDVSSKAVEIARKNAERHGVSDRFFVRKGEFLEPFKEKFASIEMILSNPPYVKSSAHLPKDVLFEPPEALFGGEDGLDFYREFFGRYDTSGKIVLMEIGEDQVEELKKIVSDTVFLKDSAGKYRFLLLNRRSS | Function: Methylates the class 1 translation termination release factors RF1/PrfA and RF2/PrfB on the glutamine residue of the universally conserved GGQ motif.
Catalytic Activity: L-glutaminyl-[peptide chain release factor] + S-adenosyl-L-methionine = H(+) + N(5)-methyl-L-glutaminyl-[peptide chain release factor] + S-a... |
Q8DHV7 | MSGEALQRWWHWAQGIIPAPERESGLRELKQFLRAFTGLSPLEITLRRFPPQIHLKLPLTELQERWQRRWQERVPLQYLIGVAHWHDLELVVTPSVLIPRPETEELLAVVAATVPPWQQQGHWLDLGTGSGAIAIGLARLFPAALIHAVDCSSEALEVAQVNIQKYALGDRVRCYVGNWFDPIVPLQGQVQGIVSNPPYIPTSVVATLQPEVQYHEPLLALDGGTDGLQAIRQILETAPEYLQPQGWLFIELMATQGKAVAALAMATQAYERVEILRDLSGHDRFLLAQTP | Function: Methylates the class 1 translation termination release factors RF1/PrfA and RF2/PrfB on the glutamine residue of the universally conserved GGQ motif.
Catalytic Activity: L-glutaminyl-[peptide chain release factor] + S-adenosyl-L-methionine = H(+) + N(5)-methyl-L-glutaminyl-[peptide chain release factor] + S-a... |
B5YIQ8 | MKALDKIREIVNKFSFNIREAQEIICHVLKIDKIQLYTENPEITSEQAHTIKSLIERRLKKEPLQYIIGECYFYNIKIKVGRGVLIPRPETEILVEQVLERQKLISNTGNRILDLCTGSGCIALAIGKNAPEFQIFGIDKSEKAVKYATENKALNNIKNVIFLVGDMFNPFKEKIFACITANPPYVKTDEISKLQPEIKNYEPLEALNGGEDGLNFYRKIIENAEKYLLNSGLIFLEIGQGQAKAVQNIALMSGFNVIEVVKDIAGIDRVMILQKSKSL | Function: Methylates the class 1 translation termination release factors RF1/PrfA and RF2/PrfB on the glutamine residue of the universally conserved GGQ motif.
Catalytic Activity: L-glutaminyl-[peptide chain release factor] + S-adenosyl-L-methionine = H(+) + N(5)-methyl-L-glutaminyl-[peptide chain release factor] + S-a... |
Q9KQ26 | MSVTIEAALKAATEQLQQSGSDSPALDAAVLLCHVLAKPRSYLLTWPDKILEKPTLASLELLLARRRAGEPMAYILGEREFWSLPLKVSPSTLIPRPDTERLVELALDKAALIDGELLDLGTGTGAIALALASELPTRQVTGIDLRPEAAELARENATRLAIHNAQFFQGSWFSPLADGTKFALIVSNPPYIEENDPHLSLGDVRFEPKSALVAAENGLADIRHISTHAPHFLLDGGWLLFEHGYDQGVAVRTILRDLGYQNIITEQDYAGHDRVTLGQYKTEREA | Function: Methylates the class 1 translation termination release factors RF1/PrfA and RF2/PrfB on the glutamine residue of the universally conserved GGQ motif.
Catalytic Activity: L-glutaminyl-[peptide chain release factor] + S-adenosyl-L-methionine = H(+) + N(5)-methyl-L-glutaminyl-[peptide chain release factor] + S-a... |
Q9PD67 | MPSPIALLTAATERIERVDAEALLLHALDCDRAWLFTHGDIPLAAAATESFQALVEQRARGIPVAYLIGRRGFWTLDVMVSSATLIPRAETETLVEQALQRLDHASERRVADLGTGSGAIALAIACERPQAQVLATDNSAAALDIAARNASAHGLNHVVFREGDWYEALLGERFDLIVSNPPYIAVTDPHLTQGDLRFEPPSALISGGDGLDALRILTAGAPAYLRPGGWLVMEHGWDQGAAMRTLLHTAGLVAVATVQDLEARDRVTVGRCPGF | Function: Methylates the class 1 translation termination release factors RF1/PrfA and RF2/PrfB on the glutamine residue of the universally conserved GGQ motif.
Catalytic Activity: L-glutaminyl-[peptide chain release factor] + S-adenosyl-L-methionine = H(+) + N(5)-methyl-L-glutaminyl-[peptide chain release factor] + S-a... |
Q3Z6Z9 | MEKALLEIEEKARLAKAASRPLSYASSAQKDAALKNIAACLLNNAPAILEANLKDQTEAKAAGMTAAMLDRLIITQSRLEGIAKDTLAIAALPDPVGEIFDMNTMPNGLVIGKKRVPLGVIAAIYESRPNVTVDIAALCLKAGNAVILRGGKETIHSNTILARLIRQAVEEAGLPQEAVQFIENTEHSLVNHLLKLSDQIDLVIPRGGAGLISYVKQNSFIPVVAGGIGVVHIYVDADANIADAVNIAYNSKVQRPTVCNAMDTLLVHKDIAAAFLPVVAAEWSKAGVEIRADKTAMEILENASSCKLIPAAADDWGKEF... | Function: Catalyzes the NADPH-dependent reduction of L-glutamate 5-phosphate into L-glutamate 5-semialdehyde and phosphate. The product spontaneously undergoes cyclization to form 1-pyrroline-5-carboxylate.
Catalytic Activity: L-glutamate 5-semialdehyde + NADP(+) + phosphate = H(+) + L-glutamyl 5-phosphate + NADPH
Sequ... |
Subsets and Splits
No community queries yet
The top public SQL queries from the community will appear here once available.