ids stringlengths 6 10 | seqs stringlengths 11 1.02k | texts stringlengths 108 11.1k |
|---|---|---|
A3PDP9 | MKLKSLLSVFTISIVALTSACSTKNAGPSADPDKLIVALIPDENAATVIQDNQGLKDYLTEAFDKEIELVVTTDYSSMIEAARNDRLDLAYFGPLSYVLAKAVSDIEPFAARIKGGTKTYNSCIIGNTKKGVTSFDDIKGTTFALGDPASTSSRLFPELTLAENGLTKGKDFQGVFLGSHDAVALAVQNGNAQAGGMACPILKSLKKKGVIDPSKVTTIAQSSPIPQYPWTMRSTLSPELKEKIRFTFLDLDSDKVLKPFNADGFASITDSDYDGIRKAGKLLGLDLSKFVK | Function: Probably part of the ABC transporter complex PhnC2D2E2. Binds strongly to methylphosphonate (MPn), ethylphosphonate (EPn) and inorganic phosphite.
Location Topology: Lipid-anchor
Sequence Mass (Da): 31304
Sequence Length: 292
Subcellular Location: Cell membrane
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A0QQ71 | MKIRAHHKIATAAACVALLASACSGSDKPQSTTAEGFPETITLAAIPAENSSDLKASYDPLIKMLEKQTGSKVEFVQASDYAGVVEGMIAGNVDLAFFGPFAYVVAGVNGAKMTPLGAVIKDEGGAPGYQSYGLARADEDNINGLKDFAGKKVCFVDPGSTSGFLYPTAGLIEEGVVKSGSEADISAAMSPIFAGGHDSSALAIANGDCDAGFAFDTMVDKTMIDKGDLKPGQLKTVWKSDMIAGSVFAANDALGPEVIDKLKTMFAQDANVKSFEEEGFCEGDACRITDERAWGVVPVTDADYDGVRHVCDVTGSEKCK... | Function: Part of the ABC transporter complex PhnCDE involved in phosphate import. Responsible for phosphate binding.
Location Topology: Lipid-anchor
Sequence Mass (Da): 33385
Sequence Length: 321
Subcellular Location: Cell membrane
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A0A142C7A2 | MYAFTILGFKRDDMTEDEYHNYISTVHSAHLKALLAQNDIVSYTMQHNTSQTRDDLLNKVYQGQMPAEKVFECDAIIQVVFKTVEDYLRVREDPHFQTVVNPDHVNFAHPTKTRFVMGWHEVHVADGKVVS | Function: Dehydratase; part of the gene cluster that mediates the biosynthesis of phenalenones such as herqueinone, compounds that have been reported to treat tumors, bacterial infections and/or mycoses, and rheumatic diseases . The non-reducing polyketide synthase phnA synthesizes the heptaketide backbone and cyclizes... |
P0DP69 | MPDAVQAPYPAYRPEPNMQTITIAPPKRSWFSLLSWAVVLAVLVVSWQGAEMAPLTLIKDGGNMATFAADFFPPDFSQWQDYLTEMAVTLQIAVWGTALAVVLSIPFGLMSAENLVPWWVYQPVRRLMDACRAINEMVFAMLFVVAVGLGPFAGVLACWRCLSTPPACSPSCFPKRWKRLSPARWKAFAPPVPTSSKRSSTACCHR | Function: N-terminal fragment of the PhnE protein, part of a phosphonate usage operon that is cryptic in K12 strains. Growth of K12 strains on phosphonate can be observed when it is used as the sole phosphorus source after a 60 hour lag period, suggesting the operon is activated . An intact PhnE in strain B is (AC A0A1... |
P0DP70 | MLALFIHTTGVLSKLLSEAVEAIEPGPVEGIRATGANKLEEILYGVLPQVMPLLISYSLYRFESNVRSATVVGMVGAGGIGVTLWEAIRGFQFQQTCALMVLIIVTVSLLDFLSQRLRKHFI | Function: C-terminal fragment of the PhnE protein, part of a phosphonate usage operon that is cryptic in K12 strains. Growth of K12 strains on phosphonate can be observed when it is used as the sole phosphorus source after a 60 hour lag period, suggesting the operon is activated . An intact PhnE in strain B is (AC A0A1... |
Q7ZAP3 | MNRIHAVILDWAGTTVDFGSFAPTQIFVEAFRQAFDVEITLAEARVPMGLGKWQHIEALGKLPAVDARWQAKFGRSMSAADIDAIYAAFMPLQIAKVVDFSSPIAGVIDTIAALRAEGIKIGSCSGYPRAVMERLVPAAAGHGYRPDHWVATDDLAAGGRPGPWMALQNVIALGIDAVAHCVKVDDAAPGISEGLNAGMWTVGLAVSGNEFGATWDAYQTMSKEDVAVRREHAASKLYAAGAHYVVDSLADLPGVIAHINARLAQGERP | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Involved in phosphonate degradation.
Catalytic Activity: H2O + phosphonoacetaldehyde = acetaldehyde + H(+) + phosphate
Sequence Mass (Da): 28574
Sequence Length: 269
EC: 3.11.1.1
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A0LMC1 | MEIFVRNKPYTGPVKAVVLDWAGTTVDFGCMAPVTAFIEAFALRGVEISASEVRGPMGLMKMDHVRALCGLPSVSERWRELFGRIPNEDDVRLVYGDTVPLMVLSVADHAELIPGLLPAIGYFRGNGIKIGTSTGYTTPMMEVLLPRAEKRGYRPDSVVCSSDVPRGRPFPFMCYRNAIDLEVYPLEAVVKIGDTVSDIREGLNAGMWTIGVSKSGSDLGLTEAELDALPADDLRNRLALVESRFLEAGAHFVVEHIGRCPEIIEEINDLLSQGEVP | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Involved in phosphonate degradation.
Catalytic Activity: H2O + phosphonoacetaldehyde = acetaldehyde + H(+) + phosphate
Sequence Mass (Da): 30294
Sequence Length: 277
EC: 3.11.1.1
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Q87JL6 | MSNSPIQAVIFDWAGTIVDFGSFAPTSIFVEAFKQGFDFDIDLEEAREPMGLGKWDHIQAVGRIPAVDKRWNEKFGRSMTNEDIDAIYAAFMPLQKAKVADHAEPILNAVEVVNGLKDKGIKIGSCSGYPREVMDVLIPVAADYGYQPDYVVATDDLPQGGRPAPFMALKNVIELDVTDVKACVKVDDSAPGIFEGHNAGMWTVGLLLSGNEAGLTFEEYQAADEATLEKAREKARAKFIKSAPHYLIDTISDLPEVIVDIEQRLAAGERP | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Involved in phosphonate degradation.
Catalytic Activity: H2O + phosphonoacetaldehyde = acetaldehyde + H(+) + phosphate
Sequence Mass (Da): 29649
Sequence Length: 271
EC: 3.11.1.1
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Q6E0X0 | MNRYSRRSRHPNPPVPNQEEPERDPNHIDQDLADLAQPLVLKERHAVMAPTQPSLSDVINEERQAPITFGNPPEVMANARLSALGYDNLTEREKRILAVGVRCGEAAKDYHSLTTTKKWIEDELKSQMVALASSTRTLTEAASLHTTFAMLHSPSIKRKAEAMSHISQGEESIDISKLNKTGMEDIWVAMESESKEDAVDTYLRNILEVDPTQFYAIDGWGLYLDFIPTWHYIAAGKNSAQFKTSYADEIVEQRAAFERVLSKRPRVEI | Function: Non catalytic polymerase cofactor and regulatory protein that plays a role in viral transcription and replication. Stabilizes the RNA polymerase L to the N-RNA template and binds the soluble protein N, preventing it from encapsidating non-genomic RNA (By similarity).
PTM: Phosphorylated by host kinases.
Seque... |
Q5MKM7 | MEKFAPEFVGEDANKKAEEFLKHRSFPSEKPLAGIPNTATHVTKYNMPPILRSSFKLPSPRVAANLTEPSAPPTTPPPTPPQNKEEQPKESDVDIETMHVCKVPDNPEHSKKPCCSDDTDTKKTRKPMVTFVEPEEKFVGLGASLYRETMQTFAADGYDEESNLSFEETNQEPGSSSVEQRLDRIEEKLSYIIGLLNTIMVATAGPTTARDEIRDALIGTREELIEMIKSDILTVNDRIVAMEKLRDEECSRADTDDGSACYLTDRARILDKIVSSNAEEAKEDLDVDDIMGINF | Function: Plays critical roles in regulating RNA replication and transcription through its interactions with multiple proteins. Tethers the RNA-directed RNA polymerase L to the nucleoprotein-RNA complex. Recruits the M2-1 protein, a processivity factor that is required for efficient transcription of viral RNA. Acts as ... |
Q9JGU0 | MDKKASGISGENALFGDVPNDVVGTTYEMGLDGIFDDGETDVIESPADAEEHVTTDIVADEGDNLITKVDDMIGYLKRECQDHGIAVRKEWVNVLTRKFHMSKKIYASHLDFFLLGVMGERHVAVEKDFKDTAVRLSDEVNKMSGISKKVADNETRMIKELDAKMKEMGSLIGKFNGVLNEFKGSMAVSSRPASVASWALDQTTETSREKNYNEFLKKLGFQDHHIKSPLMKKCTVMITDEMYDEVMLENTSEDTLGIYKEQIITYGQSIQKKVEKPIKKDPYADF | Function: Non catalytic polymerase cofactor and regulatory protein that plays a role in viral transcription and replication. Stabilizes the RNA polymerase L to the N-RNA template and binds the soluble protein N, preventing it from encapsidating non-genomic RNA (By similarity).
PTM: Phosphorylated by host kinases.
Seque... |
A9CJC9 | MSLKTAPVIVWFRKDLRLSDNLALLAAVEHGGPVIPVYIREKSAGPLGGAQEWWLHHSLAALSSSLEKAGGRLVLASGDAERILRDLISETGADTVVWNRRYDPTGMATDKALKQKLRDDGLTVRSFSGQLLHEPSRLQTKSGGPYRVYTPFWRALEGSDEPHAPADPPKSLTAPKVWPKSEKLSNWKLLPTKPDWAKDFSDIWTPGETGALDKLDDFIDGALKGYEEGRDFPAKPATSLLSPHLAAGEISPAAVWHATKGLSRHIASNDISRFRKEIVWREFCYHLLFHFPELGEKNWNDSFDAFSWRDDEKSFKAWTR... | Cofactor: Binds 1 FAD per subunit.
Function: Photolyase involved in the repair of UV radiation-induced DNA damage. By using blue-light energy, catalyzes the photoreactivation of cyclobutane pyrimidine dimers (CPDs), which are formed between adjacent bases on the same DNA strand upon exposure to ultraviolet radiation. C... |
Q00829 | MKSKWMSGLLLVAVGFSFTQVMVHAGETANTEGKTFHIAARNQT | Function: Signaling molecule involved in the regulation of sporulation . Secreted during production, but the mature peptide acts intracellularly, indicating that it needs to be imported into the cell to function . Inhibitor of the RapA phosphatase activity . Does not act on RapB .
PTM: Secreted with a propeptide domain... |
P11394 | MKTPLTEAVAAADSQGRFLSNTEVQAASGRFNRAKASLEAAKALTSKADSLVNGAAQAVYSKFPYTTQMEGSNYSATPEGKAKCSRDVGYYLRMITYCLVAGGTGPMDDYLIAGLDEINRTFELSPSWYVEALKHIKANHGLSGDAATEANSYIDYAINALI | Function: Light-harvesting photosynthetic bile pigment-protein from the phycobiliprotein complex.
PTM: Contains one covalently linked bilin chromophore.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 17335
Sequence Length: 162
Subcellular Location: Cellular thylakoid membrane
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A9CH39 | MSQLVLILGDQLSPSIAALDGVDKKQDTIVLCEVMAEASYVGHHKKKIAFIFSAMRHFAEELRGEGYRVRYTRIDDADNAGSFTGEVKRAIDDLTPSRICVTEPGEWRVRSEMDGFAGAFGIQVDIRSDRRFLSSHGEFRNWAAGRKSLTMEYFYREMRRKTGLLMNGEQPVGGRWNFDAENRQPARPDLLRPKHPVFAPDKITKEVIDTVERLFPDNFGKLENFGFAVTRTDAERALSAFIDDFLCNFGATQDAMLQDDPNLNHSLLSFYINCGLLDALDVCKAAERAYHEGGAPLNAVEGFIRQIIGWREYMRGIYWL... | Cofactor: Binds 1 FAD per subunit.
Function: Photolyase involved in the repair of UV-induced (6-4) lesions in DNA. Catalyzes the photoreactivation of (6-4) pyrimidine-pyrimidone photoproducts by using blue-light energy. Can repair (6-4) photoproducts in ssDNA as well as in dsDNA.
Catalytic Activity: (6-4) photoproduct ... |
P94416 | MKLKSKLFVICLAAAAIFTAAGVSANAEALDFHVTERGMT | Function: Signaling molecule that serves as a cell density signal for both genetic competence development and sporulation . Secreted during production, but the mature peptide acts intracellularly, indicating that it needs to be imported into the cell to function . At low concentrations, CSF stimulates expression of the... |
O32025 | MKSKLFISLSAVLIGLAFFGSMYNGEMKEASRNVTLAPTHEFLV | Function: Signaling molecule involved in the regulation of sporulation . Secreted during production, but the mature peptide acts intracellularly, indicating that it needs to be imported into the cell to function (Probable). Inhibitor of the RapE phosphatase activity . Does not inhibit the phosphatase activity of RapA a... |
P71001 | MKLKSKLLLSCLALSTVFVATTIANAPTHQIEVAQRGMI | Function: Signaling molecule involved in the regulation of genetic competence development . Secreted during production, but the mature peptide acts intracellularly, indicating that it needs to be imported into the cell to function (By similarity). Stimulates expression of the genes controlled by ComA, a transcriptional... |
O32295 | MKRFLIGAGVAAVILSGWFIADHQTHSQEMKVAEKMIG | Function: Signaling molecule involved in the regulation of expression of DegU-controlled genes . Secreted during production, but the mature peptide acts intracellularly, indicating that it needs to be imported into the cell to function (By similarity). Stimulates the DegU-dependent expression of aprE, an extracellular ... |
Q59HN7 | MPIKKKVMMCLAVTLVFGSMSFPTLTNSGGFKESTDRNTTYIDHSPYKLSDQKKALS | Function: Signaling molecule involved the regulation of both sporulation and competence . Secreted during production, but the mature peptide acts intracellularly, indicating that it needs to be imported into the cell to function . Acts by inhibiting RapH activity . Can inhibit both RapH activities, the dephosphorylatio... |
Q8MZS4 | MRLLSLLFLLGLATLSFAVRSQWAQQGRATHEALITIRFALTQQNLDVLERTLLDISDTTSKNYGKWKTAEEVTELVAPAREISERVASFLERQGATKVENFRDMVKVTAPVSWIEETLHTNLFFFQHKTRTSKVIIRADGGYKIPAEIAEHVDFVAGLFEFPSIKNARTQVGAGVDGYIVPYVIFDLYGIPTTFPVHPNSSICLVEFQDDQSYNKDDLKKFAKENEITETVVSHTVGPYSGSSADTESTLDVQYGGAIALNTTVWFWTVEDWMYDFATDFLNTKNPPLVVSMSWGWPEPEQCQVGNCTGDETSLEYVVR... | Cofactor: Binds 1 Ca(2+) ion per subunit.
PTM: Autocatalytically processed.
Catalytic Activity: Milk clotting activity. Preferential cleavage of 8-Gly-|-Ser-9 in B chain of insulin most rapidly, followed by 11-Leu-|-Val-12, 19-Cys(SO(3)H)-|-Gly and 24-Phe-|-Phe-25. No action on Ac-Phe-Tyr(I)2.
Sequence Mass (Da): 62709... |
Q715L4 | MEEDFNMSTPGVKVGVXEEEKKLSYYKYYEQDLAPVPAEKIAILQGGPIAPEKCIPFDERNKFLKGEDDEYANIGFGVAADGTALVCNTTYMPGVTGEMLDWWFPWHSVGSDLRYKIWDPEDHYFARAYPASYVVDPNVPMNQKTWGVDHYIMEDVGPGPEFLKLCFKRPADFGYDESIIGTEKCESLVCAIGESSCAAAMTHKWHPYKDGVLFESRFWIGYRIDEEGNIVKAIPEGVSIPPFVPQGLFAHNIKEFTNLAAILPTLYAEEKDTF | Function: Catalyzes the hydrolytic C-C cleavage of phloretin to phloroglucinol and 3-(4-hydroxyphenyl)propionic acid during flavonoid degradation. Also hydrolyzes other C-acylated phenols.
Catalytic Activity: H2O + phloretin = 1,3,5-trihydroxybenzene + H(+) + phloretate
Sequence Mass (Da): 30923
Sequence Length: 274
Su... |
B1MK49 | MHPITYYPVDTQRLVRSNAERIRHKPYAHYFNPDVAVPEEVFAALKAPLEPEQVLGTSSTELNRLLEPGYLEGETGYCGLPDGAGYTSSLVRFPGATPEMFRWWFWWHSFEPERYSLWHPWCHADIWRTDPETETAPNLTDEQRYVGSTHHINEYIGQDPLDIEITFIDPARWGFDADGFAAAGIGAHACGSVLMKGSHMRLATMVHLARITDDGFELRSRYWIADRAEPRHDPVAGIAQLTTVPGFSGERQAYEQLVHDQTEFNHLATFLPDIYQEFGPR | Function: Catalyzes the hydrolytic C-C cleavage of phloretin to phloroglucinol and 3-(4-hydroxyphenyl)propionic acid. Can also hydrolyze monoacetylphloroglucinol (MAPG) but not 2,4-diacetylphloroglucinol (DAPG).
Catalytic Activity: H2O + phloretin = 1,3,5-trihydroxybenzene + H(+) + phloretate
Sequence Mass (Da): 32091
... |
Q9UBF8 | MGDTVVEPAPLKPTSEPTSGPPGNNGGSLLSVITEGVGELSVIDPEVAQKACQEVLEKVKLLHGGVAVSSRGTPLELVNGDGVDSEIRCLDDPPAQIREEEDEMGAAVASGTAKGARRRRQNNSAKQSWLLRLFESKLFDISMAISYLYNSKEPGVQAYIGNRLFCFRNEDVDFYLPQLLNMYIHMDEDVGDAIKPYIVHRCRQSINFSLQCALLLGAYSSDMHISTQRHSRGTKLRKLILSDELKPAHRKRELPSLSPAPDTGLSPSKRTHQRSKSDATASISLSSNLKRTASNPKVENEDEELSSSTESIDNSFSSPV... | Function: Phosphorylates phosphatidylinositol (PI) in the first committed step in the production of the second messenger inositol-1,4,5,-trisphosphate (PIP). May regulate Golgi disintegration/reorganization during mitosis, possibly via its phosphorylation. Involved in Golgi-to-plasma membrane trafficking (By similarity... |
B3EX61 | MGDTAVEPAPLKPASEPAPGPPGNNGGSLLSVITEGVGELSVIDPEVAQKACQEVLEKVRLLHGAVAVSKRGTALELVNGDGVDTEIRCLDDPPAQIREEEDEMGATVTSGTAKGARRRRQNNSAKQSWLLRLFESKLFDISMAISYLYNSKEPGVQAYIGNRLFCFRNEDVDFYLPQLLNMYIHMDEDVGDAIKPYIVHRCRQSINFSLQCALLLGAYSSDMHISTQRHSRGTKLRKLILSDELKPAHRKRELPSLSPALNTGLSPSKRTHQRSKSDATASISLSSSLKRTASNPKVENEDEPIRLAPEREFIKSLMAI... | Function: Phosphorylates phosphatidylinositol (PI) in the first committed step in the production of the second messenger inositol-1,4,5,-trisphosphate (PIP). May regulate Golgi disintegration/reorganization during mitosis, possibly via its phosphorylation (By similarity). Involved in Golgi-to-plasma membrane traffickin... |
A4IID4 | MGDTMVEPVPAKLSDPTLVLRGNGGSPLCVITEGVGEAQMVIDPDVAEKACQDVLDKVKLIRGSSAESLDKIDGSDTGDGGSLANGDAGPRHSESCGPPVSASRITEEEESLIDINSVKSARRRQKNNSAKQSWLLRLFECKLFDVSMAISYLYNSKEPGVQAYIGNRLFCFRYEDVDFYLPQLLNMYIHMDEDVGDAIKPYVVHRCRQSINFSLQCAWLLGAYSSDMHISTQRHSRGTKLRKLILSDELKPAHKKREIPPLSLAPDTGLSPSKRTHQRSKSDATVSISLSSNLKRTSSNPKVENDDEPVRLAPEREFIK... | Function: Phosphorylates phosphatidylinositol (PI) in the first committed step in the production of the second messenger inositol-1,4,5,-trisphosphate (PIP). May play an important role in the inner ear development.
Catalytic Activity: a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol) + ATP = a 1,2-diacyl-sn-glycero-3... |
Q99755 | MASASSGPSSSVGFSSFDPAVPSCTLSSAASGIKRPMASEVLEARQDSYISLVPYASGMPIKKIGHRSVDSSGETTYKKTTSSALKGAIQLGITHTVGSLSTKPERDVLMQDFYVVESIFFPSEGSNLTPAHHYNDFRFKTYAPVAFRYFRELFGIRPDDYLYSLCSEPLIELCSSGASGSLFYVSSDDEFIIKTVQHKEAEFLQKLLPGYYMNLNQNPRTLLPKFYGLYCVQAGGKNIRIVVMNNLLPRSVKMHIKYDLKGSTYKRRASQKEREKPLPTFKDLDFLQDIPDGLFLDADMYNALCKTLQRDCLVLQSFKI... | Function: Catalyzes the phosphorylation of phosphatidylinositol 4-phosphate (PtdIns(4)P/PI4P) to form phosphatidylinositol 4,5-bisphosphate (PtdIns(4,5)P2/PIP2), a lipid second messenger that regulates several cellular processes such as signal transduction, vesicle trafficking, actin cytoskeleton dynamics, cell adhesio... |
D3ZSI8 | MASASSGPAAAGFSPLDSGVPAGTAASGIKRGTVSEGPYASLMPVKKIGHRSVDSSGETTYKKTTSSALKGAIQLGITHTVGSLSTKPERDVLMQDFYVVESIFFPSEGSNLTPAHHYNDFRFKTYAPVAFRYFRELFGIRPDDYLYSLCSEPLIELSNSGASGSLFYVSSDDEFIIKTVQHKEAEFLQKLLPGYYMNLNQNPRTLLPKFYGLYCVQAGGKNIRIVVMNNLLPRSVKMHMKYDLKGSTYKRRASQKEREKTLPTFKDLDFLQDIPDGLFLDADMYSALCKTLQRDCLVLQSFKIMDYSLLMSIHNMDHAQ... | Function: Catalyzes the phosphorylation of phosphatidylinositol 4-phosphate (PtdIns(4)P/PI4P) to form phosphatidylinositol 4,5-bisphosphate (PtdIns(4,5)P2/PIP2), a lipid second messenger that regulates several cellular processes such as signal transduction, vesicle trafficking, actin cytoskeleton dynamics, cell adhesio... |
O14986 | MSSAAENGEAAPGKQNEEKTYKKTASSAIKGAIQLGIGYTVGNLTSKPERDVLMQDFYVVESVFLPSEGSNLTPAHHYPDFRFKTYAPLAFRYFRELFGIKPDDYLYSICSEPLIELSNPGASGSLFFVTSDDEFIIKTVQHKEAEFLQKLLPGYYMNLNQNPRTLLPKFYGLYCMQSGGINIRIVVMNNVLPRSMRMHFTYDLKGSTYKRRASRKEREKSNPTFKDLDFLQDMHEGLYFDTETYNALMKTLQRDCRVLESFKIMDYSLLLGIHFLDHSLKEKEEETPQNVPDAKRTGMQKVLYSTAMESIQGPGKSGDG... | Function: Catalyzes the phosphorylation of phosphatidylinositol 4-phosphate (PtdIns(4)P/PI4P) to form phosphatidylinositol 4,5-bisphosphate (PtdIns(4,5)P2/PIP2), a lipid second messenger that regulates several cellular processes such as signal transduction, vesicle trafficking, actin cytoskeleton dynamics, cell adhesio... |
P70181 | MSSTAENGDAVPGKQNEEKTYKKTASSAIKGAIQLGIGYTVGNLTSKPERDVLMQDFYVVESVFLPSEGSNLTPAHHYPDFRFKTYAPLAFRYFRELFGIKPDDYLYSICSEPLIELSNPGASGSLFFLTSDDEFIIKTVQHKEAEFLQKLLPGYYMNLNQNPRTLLPKFYGLYCMQSGGINIRIVVMNNVLPRAMRMHLTYDLKGSTYKRRASRKEREKPNPTFKDLDFLQDMHEGLYFDTETYNALMKTLQRDCRVLESFKIMDYSLLLGIHILDHSLKDKEEEPLQNVPDAKRPGMQKVLYSTAMESIQGPGKSADG... | Function: Catalyzes the phosphorylation of phosphatidylinositol 4-phosphate (PtdIns(4)P/PI4P) to form phosphatidylinositol 4,5-bisphosphate (PtdIns(4,5)P2/PIP2), a lipid second messenger that regulates several cellular processes such as signal transduction, vesicle trafficking, actin cytoskeleton dynamics, cell adhesio... |
Q9Y2B2 | MEAMWLLCVALAVLAWGFLWVWDSSERMKSREQGGRLGAESRTLLVIAHPDDEAMFFAPTVLGLARLRHWVYLLCFSAGNYYNQGETRKKELLQSCDVLGIPLSSVMIIDNRDFPDDPGMQWDTEHVARVLLQHIEVNGINLVVTFDAGGVSGHSNHIALYAAVRALHSEGKLPKGCSVLTLQSVNVLRKYISLLDLPLSLLHTQDVLFVLNSKEVAQAKKAMSCHRSQLLWFRRLYIIFSRYMRINSLSFL | Function: Involved in the second step of GPI biosynthesis. De-N-acetylation of N-acetylglucosaminyl-phosphatidylinositol.
Catalytic Activity: a 6-(N-acetyl-alpha-D-glucosaminyl)-1-phosphatidyl-1D-myo-inositol + H2O = acetate + an alpha-D-GlcN-(1->6)-(1,2-diacyl-sn-glycero-3-phospho)-1D-myo-inositol
Location Topology: S... |
O35790 | MEVVGLLCVAVAVLTWGFLRVWNSAERMRSPEQAGLPGAGSRALVVIAHPDDEAMFFAPTILGLARLKQQVSLLCFSSGNYYNQGEIRKKELLQSCAVLGIPPSRVMIIDKREFPDDPEVQWDTEHVASTILQHIHANATDLVVTFDAEGVSGHSNHIALYKAVRALHSGGKLPEGCSVLTLQSVNVLRKYVFLLDLPWTLLSPQGVLFVLTSKEVAQAKKAMSCHRSQLLWFRHLYTVFSRYMSVNSLQLL | Function: Involved in the second step of GPI biosynthesis. De-N-acetylation of N-acetylglucosaminyl-phosphatidylinositol.
Catalytic Activity: a 6-(N-acetyl-alpha-D-glucosaminyl)-1-phosphatidyl-1D-myo-inositol + H2O = acetate + an alpha-D-GlcN-(1->6)-(1,2-diacyl-sn-glycero-3-phospho)-1D-myo-inositol
Location Topology: S... |
Q500W7 | MSRESENTDDEPSKWMKFRSLLVFSMLLRVFLIVYGEWQDAHMEVRYTDVDYIVFSDAASLMASGESPYKRTTYRYSPLLALLLTPNSFFHRSWGKFLFSASDLLVGWFIHKILKQRKVPEKICTYSVMVWLFNPFTFTIGTRGNCEPIVCAMILWIILCLMQGNLLQAAFWYGLVVHFRVYPIIYALPIILVLDTQVFRSGQKPALLYWNTGQAKTPASNMERKTFLFNLLTTLKSLFSRERIMFALISGGVFLACNAVSFYFYGQEFLHEALLYHLTRTDPRHNFSIYFYHIYLHYERQFSAVEKLISFLPQFTVQFA... | Function: Mannosyltransferase involved in glycosylphosphatidylinositol-anchor biosynthesis. Transfers the first alpha-1,4-mannose to GlcN-acyl-PI during GPI precursor assembly.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 52946
Sequence Length: 450
Pathway: Glycolipid biosynthesis; glycosylphospha... |
Q5F380 | MAGGRPGLRAALGAGLLARLSLVLYGLYQDAVMRVRYTDVDYRVFTDAARLVTQGRSPYRRATFRYTPLLAWLLTPNVHLGELFGKLLFVAGDLAAAGVAYRALRRRGASPGRACGCCAAAWLLNPLPMAVSSRGNAEALVAVLVLAALHLVEAGSVGRAALCYGLAVHLKIYPLTYALPIALRLQGSGEGAAGAGRDGTAEFTLVGGIWRRVVRVLNRNVLLFGAVAGSVLAALTVLFYHLYGWEFLEHAYLYHLTRRDIRHNFSPYFYMLYLTAESKWSFALGLAAFLPQLLLLLVVSVAFYKDLFFCCFLHTAIFVS... | Function: Mannosyltransferase involved in glycosylphosphatidylinositol-anchor biosynthesis. Transfers the first alpha-1,4-mannose to GlcN-acyl-PI during GPI precursor assembly (By similarity).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 46577
Sequence Length: 418
Pathway: Glycolipid biosynthesis;... |
Q54IA4 | MTRVKTVMTNENNKYDFIFKGINLTKSIFIVGLVIRLVLIVFAEWQDANMLVKYTDIDYVVYTDASRAVVNGLSPYDRSTYRYTPLLAYLLVPNILIHPAFGKLLFVICDMIIAYLLKGILLERFPKITSRTLLICLASWLLNPFSINVSTRGNAESVIGAMVLASFYFLTKKNLTLASIFYGLSVHFKIYPIIYSIPMYLYIDENFFSRKPSEYTSLNNNFKNIFKNFFNKNRLKFFLISAFTFISLTFIMYLIYGYIFLFETYLYHVIRADNRHNFSVYFYQIYLNTPIVETVGDLVGKVNGSNMIVALASFLPQVIL... | Function: Mannosyltransferase involved in glycosylphosphatidylinositol-anchor biosynthesis. Transfers the first alpha-1,4-mannose to GlcN-acyl-PI during GPI precursor assembly (By similarity).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 51328
Sequence Length: 442
Pathway: Glycolipid biosynthesis;... |
Q9H3S5 | MGSTKHWGEWLLNLKVAPAGVFGVAFLARVALVFYGVFQDRTLHVRYTDIDYQVFTDAARFVTEGRSPYLRATYRYTPLLGWLLTPNIYLSELFGKFLFISCDLLTAFLLYRLLLLKGLGRRQACGYCVFWLLNPLPMAVSSRGNADSIVASLVLMVLYLIKKRLVACAAVFYGFAVHMKIYPVTYILPITLHLLPDRDNDKSLRQFRYTFQACLYELLKRLCNRAVLLFVAVAGLTFFALSFGFYYEYGWEFLEHTYFYHLTRRDIRHNFSPYFYMLYLTAESKWSFSLGIAAFLPQLILLSAVSFAYYRDLVFCCFLH... | Function: Mannosyltransferase involved in glycosylphosphatidylinositol-anchor biosynthesis. Transfers the first alpha-1,4-mannose to GlcN-acyl-PI during GPI precursor assembly.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 49460
Sequence Length: 423
Pathway: Glycolipid biosynthesis; glycosylphospha... |
Q4R4E1 | MGSTKHWGEWLLNLKLAPAGVFGVAFLARVALVFYGVFQDRTLHVRYTDIDYQVFTDAARFVAEGRSPYLRATYRYTPLLGWLLTPNIYLSELFGKFLFISCDLLTAFLLYRLLLLKGLARRQACGYCVFWLLNPLPMAVSSRGNADSIVASLVLMVLYLIRKRVVACAAVFYGFAVHMKIYPVTYILPITLHLLPDRDNDKSLRQSRYTFQAHLYELLKRLCDRAVLLFVAVAGLTFFALSFGFYYEYGWEFLEHTYFYHLTRRDIRHNFSPYFYMLYLTAESKWSFSLGIAAFLPQFILLSAVSFAYYRDLVFCCFLH... | Function: Mannosyltransferase involved in glycosylphosphatidylinositol-anchor biosynthesis. Transfers the first alpha-1,4-mannose to GlcN-acyl-PI during GPI precursor assembly (By similarity).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 49451
Sequence Length: 423
Pathway: Glycolipid biosynthesis;... |
Q5W259 | MVNDTFEQALQNAINIARLAPSSHNCQPWSVHYDAATRCGEVSIDRQRALKGLPSLEREMLMSCGIFFEYLSTLLKHSGYPLDWQWVGARQNGSSGMLISFAPSAPCVADLVAYQQWVQRISDRHTVRTAYQPTQVNEQQQAQLYALFDRSPVTCDIKYGEATRHDVAFLTANYASLDFADQQAWRETYHYIRFNEQQAAEDGFYLHHLFGPVSCGFRWFFRIAFHPRLSWLAKRLRLPASMAKGLAELVVEGPQYLALSLEHESDENLFIAGMKLGQLWLMLQSWGWSLHPLSVLVQHATARCALADTVRLTGLPVFFA... | Function: Involved in the biosynthesis of 4-methoxy-2,2'-bipyrrole-5-carbaldehyde (MBC), one of the terminal products involved in the biosynthesis of the red antibiotic prodigiosin (Pig). Catalyzes the oxidation of the hydroxy group of 4-hydroxy-2,2'-bipyrrole-5-methanol (HBM) to yield 4-methoxy-2,2'-bipyrrole-5-carbal... |
Q9BPQ5 | MELQSLIDTVSLQKLLLLGALLRLILIAYAFFHDQWFRVKYTDIDYMIVVDGARHMWNGGSPFDRTTFRYTPLLAALVMPSIWIANPMGKLIFASSDLGAAWYCYGVLKSFAKERSAKWMVSLFILFNPIVLSVSTRGNSDMLVTFMSLMVLSKFARRKCYQAAAVLGFAVHFKIYPIIYALPLTLGVWEQSVAASTNTWRRVVKTAVVVSICALMAAISFAVPTVLCYMKYGQQYLNEAFIYHVYREDHRHNFSPYWLLMYLNMARRHLGQGVDFSPRLVAFAPQAVVLSFVSYKLRRNTAHACCVQTVLFVAFNKVCT... | Function: Mannosyltransferase involved in glycosylphosphatidylinositol-anchor biosynthesis. Transfers the first alpha-1,4-mannose to GlcN-PI during GPI precursor assembly (By similarity).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 48849
Sequence Length: 430
Pathway: Glycolipid biosynthesis; glyc... |
Q66IJ4 | MMKQAGILKIFLQHQFMFPTAFFLRSALVLFGVYQDQTMLVKYTDVDYHVFTDAAEYLTQGVSPYKRATYRYTPLLAWILTPNIYVTELYGKMLFVCCDLLAAYLIHRILVDRGIKDSASLYCAIWLFNPLPMVVSSRGNAESVLAVLVLSVLYYVQKRRLIKGALIYGLSVHMKIYPITYILPIALFFQKEDFYGSQEGKRVVSNLKYIRIFRNLLQRLLSRDILLFVTVSGVTFALLTLFFYYRYGWEFLENTYLYHLTRRDIRHNFSPYFYMLYLTAENNNSFILGLAAFFPQLVLLFVVSLAYFKDLPFCCFLHTA... | Function: Mannosyltransferase involved in glycosylphosphatidylinositol-anchor biosynthesis. Transfers the first alpha-1,4-mannose to GlcN-acyl-PI during GPI precursor assembly (By similarity).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 49036
Sequence Length: 419
Pathway: Glycolipid biosynthesis;... |
O95427 | MLLFFTLGLLIHFVFFASIFDIYFTSPLVHGMTPQFTPLPPPARRLVLFVADGLRADALYELDENGNSRAPFIRNIIMHEGSWGISHTRVPTESRPGHVALIAGFYEDVSAVAKGWKENPVEFDSLFNESKYTWSWGSPDILPMFAKGASGDHVYTYSYDAKREDFGAQDATKLDTWVFDNVKDFFHHARNNQSLFSKINEEKIVFFLHLLGIDTNGHAHRPSSRDYKHNIKKVDDGVKEIVSMFNHFYGNDGKTTFIFTSDHGMTDWGSHGAGHPSETLTPLVTWGAGIKYPQRVSAQQFDDAFLKEWRLENWKRLDVN... | Function: Ethanolamine phosphate transferase involved in glycosylphosphatidylinositol-anchor biosynthesis. Transfers ethanolamine phosphate to the first alpha-1,4-linked mannose of the glycosylphosphatidylinositol precursor of GPI-anchor (By similarity). May act as suppressor of replication stress and chromosome misseg... |
Q9R1S3 | MLLFFALGLLIHFVFFASIFDIYFTSPLVHGMTPQFTPLPPPAKRLVLFVADGLRADTLYELDEDGNSRAPFIRNVIIHEGSWGVSHTRVPTESRPGHVALIAGFYEDVSAVAKGWKENPVEFDSLFNESKYTWSWGSPDILPMFAKGASGDHVYTYSYDAQREDFGAHDATKLDTWVFDKVKDFFDAARNNQSLFTKVNEEKVVFFLHLLGIDTNGHAHRPSSREYKDNIKKVDDGVKEIVSIFKHFYGDDGKTAFIFTSDHGMTDWGSHGAGHPSETLTPFVTWGAGIKFPQNVSAQQYDDEFLKEWRLENWKRRDVN... | Function: Ethanolamine phosphate transferase involved in glycosylphosphatidylinositol-anchor biosynthesis. Transfers ethanolamine phosphate to the first alpha-1,4-linked mannose of the glycosylphosphatidylinositol precursor of GPI-anchor. May act as suppressor of replication stress and chromosome missegregation.
Locati... |
Q9C999 | MSGFSSGNVNSRVVDILSGVVPLLKLICLTVIGLLLAHPKTQLVPRATFRLLSKLVFALFLPCLIFTELGESITLDNIVQWWFIPVNVLLSAVVGSLIGYLVVLICRPPPEFNRFTIVMTAFGNTGNLLLAIVSSVCHTKTNPFGPNCNSRGVSYVSFAQWVAVILVYTVVYHMMEPPLEYYEVVEEEGVEIEEINVENHDASRPLLVEAEWPGIEDKETEHCKTPFIARVFNSISSFSQTSFPEVDLGGEYGGESSSPRSIQCLAEPRVMRRIRVVAEQTPVKHILQPPTIASLLAIIIGSVPQLKSVVFGYDAPLSFI... | Function: Involved in cellular auxin homeostasis by regulating auxin metabolism. Regulates intracellular auxin accumulation at the endoplasmic reticulum and thus auxin availability for nuclear auxin signaling.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 49880
Sequence Length: 457
Subcellular Loca... |
Q9C9K5 | MVKLLELFITSSKPVVEILLITSVGFYMALDGVNLLGHDARKYLNNIVFYVFSPSLIGSRLADSVTYESLVKMWFMPVNVLLTFIIGSLLGWIVIVITKPPSHLRGLILGCCAAGNLGNMPLIIIPAVCKEKGGPFGDPESCQKYGMGYVALSMAMGSIYIWTYVYNLMRVLSNSPVETPPSVESNYDSYKVPLISSKEEENNQKAGRWEKVKRRLVSLSQKVNLKTIFAPSTIAAMIALVIGLITPLRKLIIGTEAPLRVLQDSVTLVGDGAVPAMTMIIGGNLLKGLRSSGMKMSSIIGVLVARYVLLPMSGVLIVRG... | Function: Involved in cellular auxin homeostasis by regulating auxin metabolism. Regulates intracellular auxin accumulation at the endoplasmic reticulum and thus auxin availability for nuclear auxin signaling.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 42632
Sequence Length: 390
Subcellular Loca... |
Q9C9K4 | MKLLELFIASSKPVVETLLITSVGFYLALDTVNLLGHDARKHLNNIVFYVFSPSLIGSRLADSVTYESLVKMWFMPVNVLLTFMIGSLLGWIVIVITKPPSQLRGLIISCCASGNLGTMPLIIIPAICKEKGGPFGDSESCEKYGMGYVTLSMTAFFISVYKHDTNWYVSGGNGLLMDLYINLMRVLSNSPVETHTHSIESNYDDSCKVQLISSKEEEKEEDNHQVGRWEEVKQRVVSLSKKVNLGSIFAPATIAAIIALVIGLITPLRNLIIGTVAPFRVIQDSLTLLGDGAIPAMTLILGGNLLKGMRRSEVRSSEMK... | Function: Involved in cellular auxin homeostasis by regulating auxin metabolism. Regulates intracellular auxin accumulation at the endoplasmic reticulum and thus auxin availability for nuclear auxin signaling.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 45586
Sequence Length: 415
Subcellular Loca... |
Q9SHL8 | MGFWSLLEVASMPVIQVLFMSLVGAFMASDRCKLFPVEARNSMNKVVFVLFAPALMFANLAQTVTLEDIISWWFMPVNMGLTFLIGGLLGWLVVKILKPPPYLEGLIVATCSAGNMGNLPIILVPAICDEDKSPFGNRSVCRTVGLSYASFSMALGGFYIWTYTFRLIKGSAMKVQAIEESEKIAIKSSNSDLEADHKTHLLGAPEDKENKVVKEKTGFWRKGVDFLHEILEELLAPPTLGAIIGFIFGAVRWLRNLIIGDDAPLRIVQSTAKLLGDGTIPCMTIILGGNLIQGLRSSAVKPMVVLGIVCVRYIAMPIIG... | Function: Involved in cellular auxin homeostasis by regulating auxin metabolism. Regulates intracellular auxin accumulation at the endoplasmic reticulum and thus auxin availability for nuclear auxin signaling.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 43394
Sequence Length: 396
Subcellular Loca... |
Q9LZN2 | MIARILAALADSMEMPVAAGGGSVLGTIKIAVMPIAKVFTMCFLGLLMASKYVNILPPSGRKLLNGLVFSLLLPCLIFSQLGQAVTLQKMLQWWFIPVNVVLGTISGSIIGFIVASIVRPPYPYFKFTIIQIGVGNIGNVPLVLLAALCRDTSNPFGDSEKCSIDGTAYISFGQWVGAIILYTYVYQMFAPPPEGFDAEEENLALKTLPVDAAPEQVPLLTQNFPKDFSPTQDLLPVQSTEPRGRGVSRKGKIAQIFVFLYEKLKLKQIVQPAIVASILAMILGAIPFTKKLIFTNGAPLFFFTDSCMILGDAMIPCILL... | Function: Involved in cellular auxin homeostasis by regulating auxin metabolism. Regulates intracellular auxin accumulation at the endoplasmic reticulum and thus auxin availability for nuclear auxin signaling.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 46465
Sequence Length: 431
Subcellular Loca... |
Q9FKY4 | MGFLELLEVASMPIVQVLLISVLGAFLATDYCSLLSADTRRSVNKLVFVVFTPCIMFANLAETVTLQDIISWWFMPINVGITFLVGGILGWLVVKLLNPKPQLHGLIIATCASGNMGNLMLILVPAICDEEGSPFGNRSVCRSIGLSYASFSMALGGFYIWTYSYQLVRSSATQFRALEAAGLVKSPNKDIDSDPHALLLKPHQNQDLEIQGKQKVSTRTYIKDLLHQILEELFAPPTIGAILGFVFGATNWLRNLIIGENAPLRVIQDSVKLLGEGTIPCITLILGGNLIQGLRSSAVKKSVIVGVIIVRYILLPVVGV... | Function: Involved in cellular auxin homeostasis by regulating auxin metabolism. Regulates intracellular auxin accumulation at the endoplasmic reticulum and thus auxin availability for nuclear auxin signaling.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 43074
Sequence Length: 395
Subcellular Loca... |
P33639 | MRAERLRLSEEQGQRILRLYHLYRLTIGLVLVLLISSELEDQVLKLVHPELFHVGSWCYLVFNILVALFLPPSRQLLPIFILALTDVLMLCGLFYAGGGVPSGIGSLLVVAVAIANILLRGRIGLVIAAAASLGLLYLTFFLSLSSPDATNHYVQAGGLGTLCFAAALVIQALVRRQEQTETLAEERAETVANLEELNALILQRMRTGILVVDSRQAILLANQAALGLLRQDDVQGASLGRHSPMLMHCMKQWRLNPSLRPPTLKVVPDGPTVQPSFISLNREDDQHVLIFLEDISQIAQQAQQMKLAGLGRLTAGIAHE... | Function: Member of the two-component regulatory system PilS/PilR that regulates the expression of multiple genes including the type IV pilus (T4P) major subunit PilA . Thereby, plays a major role in the regulation of multiple motility pathways . Functions as a membrane-associated protein kinase that phosphorylates Pil... |
P24559 | MDITELLAFSAKQGASDLHLSAGLPPMIRVDGDVRRINLPPLEHKQVHALIYDIMNDKQRKDFEEFLETDFSFEVPGVARFRVNAFNQNRGAGAVFRTIPSKVLTMEELGMGEVFKRVSDVPRGLVLVTGPTGSGKSTTLAAMLDYLNNTKYHHILTIEDPIEFVHESKKCLVNQREVHRDTLGFSEALRSALREDPDIILVGEMRDLETIRLALTAAETGHLVFGTLHTTSAAKTIDRVVDVFPAEEKAMVRSMLSESLQSVISQTLIKKIGGGRVAAHEIMIGTPAIRNLIREDKVAQMYSAIQTGGSLGMQTLDMCL... | Function: ATPase component of the type IV pilus (T4P) that plays a role in surface and host cell adhesion, colonization, biofilm maturation, virulence, and twitching, a form of surface-associated motility facilitated by cycles of extension, adhesion, and retraction of T4P fibers . Acts as a molecular motor to provide t... |
G3XCX3 | MEFEKLLRLMVEKGGSDLFITAGVPPSMKVNGRVMPVTKTPLSPEQTRETVLGVMNEQQRRDFAENHECNFAISARGIGRFRVSAFYQRNLVGMVLRRIETNIPTLEELKLPEILKKLALTKRGLVIFVGATGTGKSTSLAAMIGYRNKNSTGHIISIEDPIEYIHQHQGCIVTQREVGLDTDSFEVALKNTLRQAPDVIMIGEVRSRETMDHAVAFAETGHLCLATLHANNANQALERIIHFFPADRHGQVWMDLSLNLKAIVAQQLVPTPDGKGRRAVIEVLLNTPLAADLIRKGEVHELKPLMKRSTEQGMQTFDQA... | Function: ATPase component of the type IV pilus (T4P) that plays a role in surface and host cell adhesion, colonization, biofilm maturation, virulence, and twitching, a form of surface-associated motility facilitated by cycles of extension, adhesion, and retraction of T4P fibers . Functions as a PilT-dependent retracti... |
P11309 | MLLSKINSLAHLRAAPCNDLHATKLAPGKEKEPLESQYQVGPLLGSGGFGSVYSGIRVSDNLPVAIKHVEKDRISDWGELPNGTRVPMEVVLLKKVSSGFSGVIRLLDWFERPDSFVLILERPEPVQDLFDFITERGALQEELARSFFWQVLEAVRHCHNCGVLHRDIKDENILIDLNRGELKLIDFGSGALLKDTVYTDFDGTRVYSPPEWIRYHRYHGRSAAVWSLGILLYDMVCGDIPFEHDEEIIRGQVFFRQRVSSECQHLIRWCLALRPSDRPTFEEIQNHPWMQDVLLPQETAEIHLHSLSPGPSK | Function: Proto-oncogene with serine/threonine kinase activity involved in cell survival and cell proliferation and thus providing a selective advantage in tumorigenesis . Exerts its oncogenic activity through: the regulation of MYC transcriptional activity, the regulation of cell cycle progression and by phosphorylati... |
P06803 | MLLSKINSLAHLRAAPCNDLHATKLAPGKEKEPLESQYQVGPLLGSGGFGSVYSGIRVADNLPVAIKHVEKDRISDWGELPNGTRVPMEVVLLKKVSSDFSGVIRLLDWFERPDSFVLILERPEPVQDLFDFITERGALQEDLARGFFWQVLEAVRHCHNCGVLHRDIKDENILIDLSRGEIKLIDFGSGALLKDTVYTDFDGTRVYSPPEWIRYHRYHGRSAAVWSLGILLYDMVCGDIPFEHDEEIIKGQVFFRQTVSSECQHLIKWCLSLRPSDRPSFEEIRNHPWMQGDLLPQAASEIHLHSLSPGSSK | Function: Proto-oncogene with serine/threonine kinase activity involved in cell survival and cell proliferation and thus providing a selective advantage in tumorigenesis . Exerts its oncogenic activity through: the regulation of MYC transcriptional activity, the regulation of cell cycle progression and by phosphorylati... |
P26794 | MLLSKINSLAHLRAAPCNDLHANKLAPGKEKEPLESQYQVGPLLGSGGFGSVYSGIRVADNLPVAIKHVEKDRISDWGELPNGTRVPMEVVLLKKVSSGFSGVIRLLDWFERPDSFVLILERPEPVQDLFDFITERGALQEELARSFFWQVLEAVRHCHNCGVLHRDIKDENILIDLNRGELKLIDFGSGALLKDTVYTDFDGTRVYSPPEWIRYHRYHGRSAAVWSLGILLYDMVCGDIPFEHDEEIVKGQVYFRQRVSSECQHLIRWCLSLRPSDRPSFEEIQNHPWMQDVLLPQATAEIHLHSLSPSPSK | Function: Proto-oncogene with serine/threonine kinase activity involved in cell survival and cell proliferation and thus providing a selective advantage in tumorigenesis. Exerts its oncogenic activity through: the regulation of MYC transcriptional activity, the regulation of cell cycle progression and by phosphorylatio... |
Q9YHZ5 | MLDKRIVDVRLDQLEILKAKNGKEHFEKQYTMGNLLGSGGFGSVYSGHRISDGQKVAIKQISRDRIQQWSKMPGEVNPVPNEIALLQSLGGGSGSVPGHRGIIRMLDWFEIPGQEYLIVFEKPQHCQDLFDFITERGALDESLARRFLKQVIEAVQFCHSKGIVHRDIKDENILVDTRTGDIKVIDFGSGATLKDSMYTDFEGTRVYSPPEWILYHKYHALPLTVWSLGVLLYDMVCGDIPFEQDTDIVKAKPSFNKRISNDCRSLICSCLSYNPGDRPSLEQILQHPWMMESSVDNGDLQEESKIKPSL | Function: Proto-oncogene with serine/threonine kinase activity involved in cell survival and cell proliferation.
PTM: Autophosphorylated.
Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Sequence Mass (Da): 35102
Sequence Length: 310
EC: 2.7.11.1
|
Q9P1W9 | MLTKPLQGPPAPPGTPTPPPGGKDREAFEAEYRLGPLLGKGGFGTVFAGHRLTDRLQVAIKVIPRNRVLGWSPLSDSVTCPLEVALLWKVGAGGGHPGVIRLLDWFETQEGFMLVLERPLPAQDLFDYITEKGPLGEGPSRCFFGQVVAAIQHCHSRGVVHRDIKDENILIDLRRGCAKLIDFGSGALLHDEPYTDFDGTRVYSPPEWISRHQYHALPATVWSLGILLYDMVCGDIPFERDQEILEAELHFPAHVSPDCCALIRRCLAPKPSSRPSLEEILLDPWMQTPAEDVPLNPSKGGPAPLAWSLLP | Function: Proto-oncogene with serine/threonine kinase activity involved in cell survival and cell proliferation. Exerts its oncogenic activity through: the regulation of MYC transcriptional activity, the regulation of cell cycle progression, the regulation of cap-dependent protein translation and through survival signa... |
Q07N42 | MPLAPPPEKMMFQLSLRRRGISDQAVLRAMDAVPRDLFVTPDLRDEAWRDTALPIACGQTISQPFVVAYMTEQLQLKPEHRVLEIGTGSGYQAAVLSRLCQQVLTLERFKTLADSARARLESLECHNVEVQLGDGFDVPAKAGLFDRILVTAAMEEVPGALIARLDLDGILIAPVGPHQATQTLVRIRNAKGGIERKELVAVRFVPALPGIAREL | Function: Catalyzes the methyl esterification of L-isoaspartyl residues in peptides and proteins that result from spontaneous decomposition of normal L-aspartyl and L-asparaginyl residues. It plays a role in the repair and/or degradation of damaged proteins.
Catalytic Activity: [protein]-L-isoaspartate + S-adenosyl-L-m... |
Q6NCU3 | MVERQIAARGVHDPRVLAAMRKVPREAFLPEPMRDLAYEDAPVPIAAEQTMSQPYIVALMVEALLLQGSDNVLEIGAGSGYAAAVLGEIAGHVTTVERIATLADAAAAKLAELGYGDVDVHRSDGTRGWPAAAPYDAIVVAAGGPQVPESLKAQLKIGGRLVMPVGADQQAQELVRLTRLGEADFKREHLGDVRFVPLLGAEGWQQPEPAGRTAREKG | Function: Catalyzes the methyl esterification of L-isoaspartyl residues in peptides and proteins that result from spontaneous decomposition of normal L-aspartyl and L-asparaginyl residues. It plays a role in the repair and/or degradation of damaged proteins.
Catalytic Activity: [protein]-L-isoaspartate + S-adenosyl-L-m... |
Q136H9 | MVSSVAPPPEKMMFQLSLRRRGISDRAVLQAMEAVPRDRFVDPVHRDGAWRDTALPIACGQTISQPFVVAYMTEQLRLEAGHRLLEIGTGSGYHAAVLSRLVRDVVSVERFKTLADRARARLKELNYANVEVLLGDGFAIPEGAGTFDRIIVTAAMTELSQPLLDLLDPGGILIAPIGPANGRQTLIRVERKDDDFIRKALVDVRFVPALTGIAREL | Function: Catalyzes the methyl esterification of L-isoaspartyl residues in peptides and proteins that result from spontaneous decomposition of normal L-aspartyl and L-asparaginyl residues. It plays a role in the repair and/or degradation of damaged proteins.
Catalytic Activity: [protein]-L-isoaspartate + S-adenosyl-L-m... |
Q2RTH7 | MSVPSRKIRLIMELRQNGVSATPVLAAIERVPRDAFVSAPFSDQAYENTALPIGCGQTISQPLVVGLMTQALDLNDRHKVLEIGTGSGYQTAVLARLCRRVYTIERHGALLREAEARLTALGLHRTVVTREGDGGRGWPEQAPFERILVTAAALDIPKVLVAQLAIGGVMVLPVGKESGAQEVVRVRRTAEDALVTERLFPVRFVPLVDGLPPRDAPGA | Function: Catalyzes the methyl esterification of L-isoaspartyl residues in peptides and proteins that result from spontaneous decomposition of normal L-aspartyl and L-asparaginyl residues. It plays a role in the repair and/or degradation of damaged proteins.
Catalytic Activity: [protein]-L-isoaspartate + S-adenosyl-L-m... |
Q08733 | MEGKEEDVRVGANKFPERQPIGTSAQTDKDYKEPPPAPFFEPGELSSWSFYRAGIAEFIATFLFLYITVLTVMGVKRAPNMCASVGIQGIAWAFGGMIFALVYCTAGISGGHINPAVTFGLFLARKLSLTRAVFYIVMQCLGAICGAGVVKGFQPNPYQTLGGGANTVAHGYTKGSGLGAEIIGTFVLVYTVFSATDAKRSARDSHVPILAPLPIGFAVFLVHLATIPITGTGINPARSLGAAIIYNKDHAWDDHWIFWVGPFIGAALAALYHQLVIRAIPFKSRS | Function: Water channel required to facilitate the transport of water across cell membrane. Its function is impaired by Hg(2+).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 30633
Sequence Length: 286
Domain: The Asn-Pro-Ala (NPA) motifs may contribute to the formation of two hemipores that could g... |
Q9AR14 | MEGKEEDVRLGANRYSERQPIGTAAQGTEEKDYKEPPPAPLFEAEELTSWSFYRAGIAEFVATFLFLYISILTVMGVSKSSSKCATVGIQGIAWSFGGMIFALVYCTAGISGGHINPAVTFGLFLARKLSLTRALFYMVMQCLGAICGAGVVKGFQEGLYMGAGGGANAVNPGYTKGDGLGAEIVGTFVLVYTVFSATDAKRSARDSHVPILAPLPIGFAVFLVHLATIPITGTGINPARSLGAAIVYNRSHAWNDHWIFWVGPFIGAALAAIYHVVIIRALPFKSRD | Function: Water channel required to facilitate the transport of water across cell membrane.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 30725
Sequence Length: 288
Domain: Aquaporins contain two tandem repeats each containing three membrane-spanning domains and a pore-forming loop with the signatu... |
Q1PE40 | MRRVSWSTVLIVVVMVSLFFVEHVVVPAAAGRVLTEKSGDGSATMTVEKMKSTVDSWFQRLASGPSPRGRGH | Function: Endogenous secreted peptide that acts as elicitor of immune response and positive regulator of defense response. Amplifies the immune response triggered by flg22, the active epitope of bacterial flagellin. Acts as negative regulator of root growth.
PTM: Contains 4-hydroxyproline; hydroxylated on Pro-65 and Pr... |
P43286 | MAKDVEAVPGEGFQTRDYQDPPPAPFIDGAELKKWSFYRAVIAEFVATLLFLYITVLTVIGYKIQSDTDAGGVDCGGVGILGIAWAFGGMIFILVYCTAGISGGHINPAVTFGLFLARKVSLPRALLYIIAQCLGAICGVGFVKAFQSSYYTRYGGGANSLADGYSTGTGLAAEIIGTFVLVYTVFSATDPKRSARDSHVPVLAPLPIGFAVFMVHLATIPITGTGINPARSFGAAVIYNKSKPWDDHWIFWVGPFIGAAIAAFYHQFVLRASGSKSLGSFRSAANV | Function: Water channel required to facilitate the transport of water across cell membrane. Probably involved in root water uptake. Its function is impaired by Hg(2+).
PTM: Ubiquitinated by RMA1, leading to proteasomal degradation.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 30474
Sequence Length... |
Q6K215 | MAKDIEASAPEGGEFSAKDYTDPPPAPLIDVEELTKWSLYRAVIAEFIATLLFLYITVATVIGYKHQSDATVNTTDAACSGVGILGIAWAFGGMIFILVYCTAGISGGHINPAVTFGLFLARKVSLIRAVLYIIAQCLGAICGVGLVKGFQSSYYARYGGGANELSDGYSKGTGLGAEIIGTFVLVYTVFSATDPKRNARDSHIPVLAPLPIGFAVFMVHLATIPITGTGINPARSLGTAVIYNKDKAWDDQWIFWVGPLIGAAIAAAYHQYVLRASAAKLGSYRSNA | Function: Aquaporins facilitate the transport of water and small neutral solutes across cell membranes.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 30498
Sequence Length: 288
Domain: Aquaporins contain two tandem repeats each containing three membrane-spanning domains and a pore-forming loop with... |
Q9UG56 | MATSVGHRCLGLLHGVAPWRSSLHPCEITALSQSLQPLRKLPFRAFRTDARKIHTAPARTMFLLRPLPILLVTGGGYAGYRQYEKYRERELEKLGLEIPPKLAGHWEVALYKSVPTRLLSRAWGRLNQVELPHWLRRPVYSLYIWTFGVNMKEAAVEDLHHYRNLSEFFRRKLKPQARPVCGLHSVISPSDGRILNFGQVKNCEVEQVKGVTYSLESFLGPRMCTEDLPFPPAASCDSFKNQLVTREGNELYHCVIYLAPGDYHCFHSPTDWTVSHRRHFPGSLMSVNPGMARWIKELFCHNERVVLTGDWKHGFFSLTA... | Cofactor: Binds 1 pyruvoyl group covalently per subunit.
Function: Catalyzes the formation of phosphatidylethanolamine (PtdEtn) from phosphatidylserine (PtdSer) . Plays a central role in phospholipid metabolism and in the interorganelle trafficking of phosphatidylserine. May be involved in lipid droplet biogenesis at t... |
Q8BSF4 | MAASGGRACVRSLRGGVLWRSSPCHYESTATRHFLGTLQKLPLQAGVRNFHTAPVRSLFLLRPVPILLATGGGYAGYRQYEKYRERKLEKLGLEIPPKLASHWEVSLYKSVPTRLLSRACGRLNQVELPYWLRRPVYSLYIWTFGVNMTEAAVEDLHHYRNLSEFFRRKLKPQARPVCGLHCVTSPSDGKILTFGQVKNSEVEQVKGVTYSLESFLGPRANTEDLPFPPASSSDSFRNQLVTREGNELYHCVIYLAPGDYHCFHSPTDWTISHRRHFPGSLMSVNPGMARWIKELFCHNERVVLTGDWKHGFFSLTAVGA... | Cofactor: Binds 1 pyruvoyl group covalently per subunit.
Function: Catalyzes the formation of phosphatidylethanolamine (PtdEtn) from phosphatidylserine (PtdSer). Plays a central role in phospholipid metabolism and in the interorganelle trafficking of phosphatidylserine. May be involved in lipid droplet biogenesis at th... |
D3ZAW2 | MAVAGGRGCVRSLREGVLWRSSPCHCDYTATRHFLGALQKLPLQAWVRKVHTAPLRTLFLLRPVPILLAAGGGYAGYRQYEKYRERQLEKLGLEIPPKLASHWEVSLYKSVPTRLLSRACGRLNQVELPSWLRRPVYSLYIWTFGVNMTEAAVEDLQHYRNLSEFFRRKLKPQARPVCGLHSVISPSDGKILTFGQVKNSEVEQVKGVTYSLESFLGPRACTEDLPFPPASSCDSFRNQLVTREGNELYHCVIYLAPGDYHCFHSPTDWTVSHRRHFPGSLMSVNPGMARWIKELFCHNERVVLTGDWKHGFFSLTAVGA... | Cofactor: Binds 1 pyruvoyl group covalently per subunit.
Function: Catalyzes the formation of phosphatidylethanolamine (PtdEtn) from phosphatidylserine (PtdSer). Plays a central role in phospholipid metabolism and in the interorganelle trafficking of phosphatidylserine. May be involved in lipid droplet biogenesis at th... |
Q59RA2 | MPSAKSSDLSPTKTNLESTTKQKVSVQDIFLYIPNLIGYLRIITAIISFLCMANHPVATLIFYGISGFLDAFDGYAARKFNQGTRFGAVLDMVTDRCATSSLIVYLGVLYPQYTVFWQILVSLDLSSHYMHMYAMLSAGSTSHKNVDETQSKLLSLYYNNRLVLFFVCLINELFYMAVYLHYYKFFWLGTVMLVASTPIWLFKQIANIIQLKNASLILARMDAHDHSKRD | Cofactor: Catalytic activity is higher with Mg(2+).
Function: Catalyzes the synthesis of phosphatidylinositol (PtdIns) . Required for proper membrane dynamics and cell wall integrity .
Catalytic Activity: a CDP-1,2-diacyl-sn-glycerol + myo-inositol = a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol) + CMP + H(+)
Loca... |
Q10153 | MGKNEQKDPNVYFFVPNLIGFTRVFLVLISLYFMSWHPNYCTIVYLYSSLLDAFDGWAARKLHQATNFGAILDMVTDRCATSCLLCFLCAAYPKYAIIFQLLVSLDLASHYMHMYSTLHQGASSHKTVTKKHNWMLRLYYGNNKVLFIFCAANEMFFVALYLLSFTPRTPPKLGYLPVPSFIYSTGELPLSYPTLLAVLCGPICLAKQIINVVQLVNAANALVKMDVEQRRAAKKLQ | Cofactor: Divalent metal cations; Mn(2+) or Mg(2+).
Function: Catalyzes the synthesis of phosphatidylinositol (PtdIns).
Catalytic Activity: a CDP-1,2-diacyl-sn-glycerol + myo-inositol = a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol) + CMP + H(+)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 26... |
P06197 | MSSNSTPEKVTAEHVLWYIPNKIGYVRVITAALSFFVMKNHPTAFTWLYSTSCLLDALDGTMARKYNQVSSLGAVLDMVTDRSSTAGLMCFLCVQYPQWCVFFQLMLGLDITSHYMHMYASLSAGKTSHKSVGEGESRLLHLYYTRRDVLFTICAFNELFYAGLYLQLFSNSATFGKWTTIISFPGYVFKQTANVVQLKRAALILADNDAKNANEKNKTY | Cofactor: Divalent metal cations; Mn(2+) or Mg(2+).
Function: Catalyzes the synthesis of phosphatidylinositol (PtdIns).
Catalytic Activity: a CDP-1,2-diacyl-sn-glycerol + myo-inositol = a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol) + CMP + H(+)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 24... |
P28069 | MSCQAFTSADTFIPLNSDASATLPLIMHHSAAECLPVSNHATNVMSTATGLHYSVPSCHYGNQPSTYGVMAGSLTPCLYKFPDHTLSHGFPPIHQPLLAEDPTAADFKQELRRKSKLVEEPIDMDSPEIRELEKFANEFKVRRIKLGYTQTNVGEALAAVHGSEFSQTTICRFENLQLSFKNACKLKAILSKWLEEAEQVGALYNEKVGANERKRKRRTTISIAAKDALERHFGEQNKPSSQEIMRMAEELNLEKEVVRVWFCNRRQREKRVKTSLNQSLFSISKEHLECR | Function: Transcription factor involved in the specification of the lactotrope, somatotrope, and thyrotrope phenotypes in the developing anterior pituitary. Specifically binds to the consensus sequence 5'-TAAAT-3'. Activates growth hormone and prolactin genes .
Sequence Mass (Da): 32912
Sequence Length: 291
Domain: The... |
Q05749 | MTCQAFASSDNFVPLNSDSSPSLPLIMHHSAAECLPVSNHATSVVSTVPSVLSLIQTPKCSHLHFAMMTSGNVSAGLHYSVPSCHYGNQTSTYGVMTGIKPATPEMLSASLSQSRILQTCSMPHPNVVNGVSTLQSKSFSFSCSLTPCLYKFPEHALSASSCALGHSFTPMHQTLLSDDPTAADFKQEFRRKSKSVEEPVDMDSPEIRELEKFANEFKLRRIKLGYTQTNVGEALAAVHGSEFSQTTICRFENSQLSFKNACKLKSILSKWLEEAEQVGALYNEKVGVNERKRKRRTTISIAAKEALERHFGEQSKPSSQ... | Function: Transcription factor that activates growth hormone and prolactin genes. Specifically binds to the consensus sequence 5'-TAAAT-3'.
Sequence Mass (Da): 41191
Sequence Length: 370
Domain: The 9aaTAD motif is a transactivation domain present in a large number of yeast and animal transcription factors.
Subcellular... |
Q9HYF1 | MFESAEVGHSIDKDTYEKAVIELREALLEAQFELKQQARFPVIILINGIEGAGKGETVKLLNEWMDPRLIEVQSFLRPSDEELERPPQWRFWRRLPPKGRTGIFFGNWYSQMLYARVEGHIKEAKLDQAIDAAERFERMLCDEGALLFKFWFHLSKKQLKERLKALEKDPQHSWKLSPLDWKQSEVYDRFVHYGERVLRRTSRDYAPWYVVEGADERYRALTVGRILLEGLQAALATKERAKRQPHAAPLVSSLDNRGLLDSLDLGQYLDKDAYKEQLAAEQARLAGLIRDKRFRQHSLVAVFEGNDAAGKGGAIRRVTD... | Cofactor: Has low activity with Co(2+) or Ni(2+).
Function: Uses inorganic polyphosphate (polyP) as a donor to convert AMP to ADP. Can also convert GMP to GDP, with lower efficiency. Cannot dephosphorylate ADP in the presence of polyP.
Catalytic Activity: [phosphate](n) + ADP = [phosphate](n+1) + AMP
Sequence Mass (Da)... |
Q886D9 | MFESAEIGHAIDDDTYEAALPSLREALLEAQIDLHEQAKRQIIVLINGIEGAGKGETVKLLSEWMDPRLIEVRTFDQQTDEELAHPPVWRYWRQLPAKGRMGIFFGNWYSQMLQGRVHGQYKDAVLDQAISGAERLEKMLCDEGALIFKFWFHLSKKQMKLRLKTLKDDPLHSWRISPLDWQQSKTYDKFVRFGERVLRRTSRDYAPWHVIEGVDANYRSLTVGRLLLEGMQAALNKVEPESSALTIGPLAIHNNERTLLDSLDLSLHLSKEDYQHELIAEQARLSGNLRDKRMKSHALVAVFEGNDAAGKGGAIRRVAA... | Function: Uses inorganic polyphosphate (polyP) as a donor to convert AMP to ADP. Can also convert GMP to GDP, with lower efficiency.
Catalytic Activity: [phosphate](n) + ADP = [phosphate](n+1) + AMP
Sequence Mass (Da): 57955
Sequence Length: 498
EC: 2.7.4.33
|
M9XB82 | MKKYRVQPDGRFELKRFDPDDTSAFEGGKQAALEALAVLNRRLEKLQELLYAEGQHKVLVVLQAMDAGGKDGTIRVVFDGVNPSGVRVASFGVPTEQELARDYLWRVHQQVPRKGELVIFNRSHYEDVLVVRVKNLVPQQVWQKRYRHIREFERMLADEGTTILKFFLHISKDEQRQRLQERLDNPEKRWKFRMGDLEDRRLWDRYQEAYEAAIRETSTEYAPWYVIPANKNWYRNWLVSHILVETLEGLAMQYPQPETASEKIVIE | Function: Uses inorganic polyphosphate (polyP) as a donor to convert both AMP to ADP and ADP to ATP. Can also use GMP, CMP, UMP, GDP, CDP and UDP.
Catalytic Activity: [phosphate](n) + ADP = [phosphate](n+1) + AMP
Sequence Mass (Da): 31559
Sequence Length: 267
EC: 2.7.4.-
|
Q9P0L9 | MNAVGSPEGQELQKLGSGAWDNPAYSGPPSPHGTLRVCTISSTGPLQPQPKKPEDEPQETAYRTQVSSCCLHICQGIRGLWGTTLTENTAENRELYIKTTLRELLVYIVFLVDICLLTYGMTSSSAYYYTKVMSELFLHTPSDTGVSFQAISSMADFWDFAQGPLLDSLYWTKWYNNQSLGHGSHSFIYYENMLLGVPRLRQLKVRNDSCVVHEDFREDILSCYDVYSPDKEEQLPFGPFNGTAWTYHSQDELGGFSHWGRLTSYSGGGYYLDLPGSRQGSAEALRALQEGLWLDRGTRVVFIDFSVYNANINLFCVLRL... | Function: Pore-forming subunit of a heterotetrameric, non-selective cation channel that is permeable to Ca(2+) . Pore-forming subunit of a calcium-permeant ion channel formed by PKD1L2 and PKD1L1 in primary cilia, where it controls cilium calcium concentration, but does not affect cytoplasmic calcium concentration . Th... |
Q9NZM6 | MAEASRWHRGGASKHKLHYRKEVEITTTLQELLLYFIFLINLCILTFGMVNPHMYYLNKVMSSLFLDTSVPGEERTNFKSIRSITDFWKFMEGPLLEGLYWDSWYNNQQLYNLKNSSRIYYENILLGVPRVRQLKVRNNTCKVYSSFQSLMSECYGKYTSANEDLSNFGLQINTEWRYSTSNTNSPWHWGFLGVYRNGGYIFTLSKSKSETKNKFIDLRLNSWITRGTRVIFIDFSLYNANVNLFCIIRLVAEFPATGGILTSWQFYSVKLLRYVSYYDYFIASCEITFCIFLFVFTTQEVKKIKEFKSAYFKSIWNWLE... | Function: May function as a subunit of a cation channel and play a role in fertilization.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 73790
Sequence Length: 624
Subcellular Location: Membrane
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G5EFU0 | MNRTFSLRRKVKKSEISTPSNFEHRIHAGFDARSGTYTGLPKQWQALLGPPRSISRPKPMVDPSCITPVDVAELKTVIRGPSSSFRYNSPLPFGMTNSPMPSVARSNSLRISATASPVVNVSSARHSFRPTLPPVSQRGYPFNDPSYAPLPLRNQKPPMSTTFGVEKPHQYQQIITIVAPSRTTTPQLQPKSPSTPQAMRQQPKCTEGVSDEEFRNALKFVVDGTDPRSDLTDYKQIGEGSTGVVEAAYKISTKQIVAVKRMNLRKQQRRELLFNEVSILRQYQHPNIVRFFSSHLVDDELWVVMEFMEGGSLTDIVTAT... | Cofactor: Divalent cations such as magnesium or manganese.
Function: Serine/threonine-protein kinase which plays a redundant role with pak-1 in embryogenesis but, in contrast to pak-1, is not involved in commissural axon guidance of ventral cord motoneurons or in distal tip cell (DTC) migration.
Catalytic Activity: ATP... |
P28178 | MGKGQSKIKNGGSGKPAKAGKPKKGNKNDETTPTSTPTPTPTPTQQNLDNSAQQQQQQQQTTTAAVSLDNKEQQQQQNIPAPATQTPITQTGTPTIEESQKNTDNNNINGASNEASSSPDSPNGSGNGNDDEDEGPEEVIFSKNKQSATKDDFELLNVIGKGSFGKVMQVKKKGEDKIFAMKVLRKDAIIARKQVNHTKSEKTILQCISHPFIVNLHYAFQTKDKLYMVLDFVNGGELFFHLKREGRFSEPRVKIYAAEIVSALDHLHKQDIVYRDLKPENILLDSEGHICITDFGLSKKIETTDGTFTFCGTPEYLAPE... | Function: Required for morphogenesis during multicellular development. Phosphorylates talB, gefN, gefS, PI4P 5-kinase and gacQ.
PTM: Seems to be myristoylated.
Location Topology: Lipid-anchor
Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Sequence Mass (Da): 52994
Sequence Length... |
P41676 | MKPEQLVYLNPRQHRIYIASPLNEYMLSDYLKQRNLQTFAKTNIKVPADFGFYISKFVDLVSAVKAIHSVNIVHHNINPEDIFMTGPDFDLYVGGMFGSLYKTFIKNNPQNITLYAAPEQIKKVYTPKNDMYSLGIVLFELIMPFKTALERETTLTNFRNNVQQMPASLSQGHPKLTEIVCKLIQHDYSQRPDAEWLLKEMEQLLLEYTTCSKKL | Function: Plays a role in the inhibition of host eIF2alpha/EIF2S1 phosphorylation, thereby increasing viral fitness. In the insect host, targets the endogenous insect heme-regulated inhibitor (HRI)-like eIF2alpha kinase.
Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Sequence Mas... |
Q9TXI7 | MIPGMRATPTESFSFVYSCDLQTNVQVKVAEFEGIFRDVLNPVRRLNQLFAEITVYCNNQQIGYPVCTSFHTPPDSSQLARQKLIQKWNEWLTLPIRYSDLSRDAFLHITIWEHEDDEIVNNSTFSRRLVAQSKLSMFSKRGILKSGVIDVQMNVSTTPDPFVKQPETWKYSDAWGDEIDLLFKQVTRQSRGLVEDVPWLDPFASRRIEMIRAKYKYSSPDRHVFLVLEMAAIRLGPTFYKVVYYEDETKNMRVSTSVNGGVGIVSACTRYCVADPELLLESLAEVKHSAMTRRIRDVEDERHRQVKPNKQAKDRLETIV... | Function: Catalytic subunit of the PI3K complex that mediates formation of phosphatidylinositol 3-phosphate . Together with bec-1, mediates the production of phosphatidylinositol 3-phosphate on intracellular vesicles and thereby regulates membrane trafficking . Plays a role in endosome-to-Golgi retrograde transport of ... |
Q8NEB9 | MGEAEKFHYIYSCDLDINVQLKIGSLEGKREQKSYKAVLEDPMLKFSGLYQETCSDLYVTCQVFAEGKPLALPVRTSYKAFSTRWNWNEWLKLPVKYPDLPRNAQVALTIWDVYGPGKAVPVGGTTVSLFGKYGMFRQGMHDLKVWPNVEADGSEPTKTPGRTSSTLSEDQMSRLAKLTKAHRQGHMVKVDWLDRLTFREIEMINESEKRSSNFMYLMVEFRCVKCDDKEYGIVYYEKDGDESSPILTSFELVKVPDPQMSMENLVESKHHKLARSLRSGPSDHDLKPNAATRDQLNIIVSYPPTKQLTYEEQDLVWKFR... | Function: Catalytic subunit of the PI3K complex that mediates formation of phosphatidylinositol 3-phosphate; different complex forms are believed to play a role in multiple membrane trafficking pathways: PI3KC3-C1 is involved in initiation of autophagosomes and PI3KC3-C2 in maturation of autophagosomes and endocytosis ... |
Q6PF93 | MGEAEKFHYIYSCDLDINVQLKIGSLEGKREQKSYKAVLEDPMLKFSGLYQETCSDLYVTCQVFAEGKPLALPVRTSYKAFSTRWNWNEWLKLPVKYPDLPRNAQVALTIWDVYGPGSAVPVGGTTVSLFGKYGMFRQGMHDLKVWPNVEADGSEPTRTPGRTSSTLSEDQMSRLAKLTKAHRQGHMVKVDWLDRLTFREIEMINESEKRSSNFMYLMVEFRCVKCDDKEYGIVYYEKDGDESSPILTSFELVKVPDPQMSMENLVESKHHKLARSLRSGPSDHDLKPNATTRDQLNIIVSYPPTKQLTYEEQDLVWKFR... | Function: Catalytic subunit of the PI3K complex that mediates formation of phosphatidylinositol 3-phosphate; different complex forms are believed to play a role in multiple membrane trafficking pathways: PI3KC3-C1 is involved in initiation of autophagosomes and PI3KC3-C2 in maturation of autophagosomes and endocytosis.... |
O88763 | MGEAEKFHYIYSCDLDINVQLKIGSLEGKREQKSYKAVLEDPMLKFSGLYQETCSDLYVTCQVFAEGKPLALPVRTSYKPFSTRWNWNEWLKLPVKYPDLPRNAQVALTIWDVYGPGRAVPVGGTTVSLFGKYGMFRQGMHDLKVWPNVEADGSEPTRTPGRTSSTLSEDQMSRLAKLTKAHRQGHMVKVDWLDRLTFREIEMINESEKRSSNFMYLMVEFRCVKCDDKEYGIVYYEKDGDESSPILTSFELVKVPDPQMSMENLVESKHHKLARSLRSGPSDHDLKPNATTRDQLNIIVSYPPTKQLTYEEQDLVWKFR... | Function: Catalytic subunit of the PI3K complex that mediates formation of phosphatidylinositol 3-phosphate; different complex forms are believed to play a role in multiple membrane trafficking pathways: PI3KC3-C1 is involved in initiation of autophagosomes and PI3KC3-C2 in maturation of autophagosomes and endocytosis.... |
Q9P7Y3 | MSYWVELWESIFTPGVTPVLAKSAHVACGALVAVFLGLYIGTKSIHCLILFFLAICLWLSLTWFLVELAHARVNNDLQMSSQSANKNDDNSNNQNPSNNKEMSDKESDSATTTQTFSVPEELLRARTTANNS | Function: Functions together with the other V-type ATPase assembly factors in the endoplasmic reticulum to efficiently assemble the V-type ATPase membrane sector V(0).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 14613
Sequence Length: 132
Subcellular Location: Endoplasmic reticulum membrane
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Q03880 | MANFFVRLWESVFEPGTSPQLIIATHVSFVALLLTLIWLIYATNGNIHFYALFCISLLLWITVIWFINELSHVKLKDNDELDKDANKKDDSAIKEDSEDKQESGKSTSTARRTQAQSRSRKA | Function: Functions together with the other V-type ATPase assembly factors in the endoplasmic reticulum to efficiently assemble the V-type ATPase membrane sector V(0).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 13962
Sequence Length: 122
Subcellular Location: Endoplasmic reticulum membrane
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Q8NFJ6 | MAAQNGNTSFTPNFNPPQDHASSLSFNFSYGDYDLPMDEDEDMTKTRTFFAAKIVIGIALAGIMLVCGIGNFVFIAALTRYKKLRNLTNLLIANLAISDFLVAIICCPFEMDYYVVRQLSWEHGHVLCASVNYLRTVSLYVSTNALLAIAIDRYLAIVHPLKPRMNYQTASFLIALVWMVSILIAIPSAYFATETVLFIVKSQEKIFCGQIWPVDQQLYYKSYFLFIFGVEFVGPVVTMTLCYARISRELWFKAVPGFQTEQIRKRLRCRRKTVLVLMCILTAYVLCWAPFYGFTIVRDFFPTVFVKEKHYLTAFYVVEC... | Function: Receptor for prokineticin 2. Exclusively coupled to the G(q) subclass of heteromeric G proteins. Activation leads to mobilization of calcium, stimulation of phosphoinositide turnover and activation of p44/p42 mitogen-activated protein kinase.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): ... |
Q8K458 | MGPQNRNTSFAPDLNPPQDHVSLNYSYGDYDLPLGEDEDVTKTQTFFAAKIVIGVALAGIMLVCGIGNFVFIAALARYKKLRNLTNLLIANLAISDFLVAIVCCPFEMDYYVVRQLSWAHGHVLCASVNYLRTVSLYVSTNALLAIAIDRYLAIVHPLKPRMNYQTASFLIALVWMVSILIAVPSAYFTTETILVIVKNQEKIFCGQIWSVDQQLYYKSYFLFVFGLEFVGPVVTMTLCYARISQELWFKAVPGFQTEQIRKRLRCRRKTVLLLMGILTAYVLCWAPFYGFTIVRDFFPTVVVKEKHYLTAFYVVECIAM... | Function: Receptor for prokineticin 2. Exclusively coupled to the G(q) subclass of heteromeric G proteins. Activation leads to mobilization of calcium, stimulation of phosphoinositide turnover and activation of p44/p42 mitogen-activated protein kinase (By similarity).
Location Topology: Multi-pass membrane protein
Sequ... |
Q7VEV2 | MSVIAGVFGALPPYRYSQRELTDSFVSIPDFEGYEDIVRQLHASAKVNSRHLVLPLEKYPKLTDFGEANKIFIEKAVDLGVQALAGALDESGLRPEDLDVLITATVTGLAVPSLDARIAGRLGLRADVRRVPLFGLGCVAGAAGVARLHDYLRGAPDGVAALVSVELCSLTYPGYKPTLPGLVGSALFADGAAAVVAAGVKRAQDIGADGPDILDSRSHLYPDSLRTMGYDVGSAGFELVLSRDLAAVVEQYLGNDVTTFLASHGLSTTDVGAWVTHPGGPKIINAITETLDLSPQALELTWRSLGEIGNLSSASVLHVL... | Function: Could catalyze the elongation of hydroxybenzoyl-CoA as well as elongation of the aliphatic precursor involved in the synthesis of phthiocerol dimycocerosate (DIM).
Sequence Mass (Da): 37146
Sequence Length: 353
Pathway: Lipid metabolism; fatty acid biosynthesis.
EC: 2.3.1.-
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Q948R1 | MRFSLSPVRPHSVVVPSLPKQDVVSYISGTTSNRQCRCVLTLPSPSVSTSRPPVLPKPETWESLLLNHDQIPGEFSPTGSSIPVKLGRRWMEYQGLQNWDGLLDPLDDNLRREILRYGQFVESAYQAFDFDPSSPTYGTCRFPRSTLLERSGLPNSGYRLTKNLRATSGINLPRWIEKAPSWMATQSSWIGYVAVCQDKEEISRLGRRDVVISFRGTATCLEWLENLRATLTHLPNGPTGANLNGSNSGPMVESGFLSLYTSGVHSLRDMVREEIARLLQSYGDEPLSVTITGHSLGAAIATLAAYDIKTTFKRAPMVTV... | Function: Sn-1-specific phospholipase that releases free fatty acids from phospholipids. Low activity on galactolipids and triacylglycerols. Catalyzes the initial step of jasmonic acid biosynthesis. Not essential for jasmonate biosynthesis after wounding or upon pathogen infection.
Catalytic Activity: a 1,2-diacyl-sn-g... |
Q9MA46 | MAAKVFTQNPIYSQSLVRDKTPQQKHNLDHFSISQHTSKRLVVSSSTMSPPISSSPLSLPSSSSSQAIPPSRAPAVTLPLSRVWREIQGSNNWENLIEPLSPILQQEITRYGNLLSASYKGFDLNPNSKRYLSCKYGKKNLLKESGIHDPDGYQVTKYIYATPDINLNPIKNEPNRARWIGYVAVSSDESVKRLGRRDILVTFRGTVTNHEWLANLKSSLTPARLDPHNPRPDVKVESGFLGLYTSGESESKFGLESCREQLLSEISRLMNKHKGEEISITLAGHSMGSSLAQLLAYDIAELGMNQRRDEKPVPVTVFSF... | Function: Sn-1-specific phospholipase that releases free fatty acids from phosphatidylcholine. Has a higher galactolipase activity than phospholipase A1 activity when digalactosyldiacylglycerol (DGDG) is used as substrate. Catalyzes the initial step of jasmonic acid biosynthesis. Required for the biosynthesis of basal-... |
O23522 | MQTLTPNADIFHAKRRRFTCNTHTSTLIPTKPLSVSPARKTNKEHLRNLENVLRTSSNSIDHIENVTSRQEKTTKNTSTSSLLGGLNLARIWPQMKAAVDEMSPKNLKRLQRLLSKSSEERSPKSKLGSKWRELHGLNNWAGLLDPLDENLRRELVRYGEFVQAAYHAFHSDPEGSPRHVALPDGSFKVTKSLYATSSVRLPKWIDDVAPDLRWMTKQTSWVGYVAVCDDPREIRRMGRREIVIALRGTATLLEWSENFRPNLVSMPEPKPDQSDPTRPKVECGFNSLYTTGDQHAPSLAESLVGEISRLVELYAGEELS... | Function: Acylhydrolase that catalyzes the hydrolysis of phosphatidylcholine at the sn-1 position. Has a strong galactolipase activity toward digalactosyldiacylglycerol (DGDG). Hydrolyzes triacylglycerol (TAG), but has a low activity toward phosphatidylcholine (PC) and monogalactosyldiacylglycerol (MGDG).
Sequence Mass... |
Q941F1 | MATIPSHNLRPHTTNQRTQYSLSFRPHFSRSTLITFPARSSPARAMSRTDEEASISTRLEQESYGLTTAEDIRRRDGEAKESKRLRDTWRKIQGEDDWAGLMDPMDPVLRSELIRYGEMAQACYDAFDFDPFSRYCGSCRFTRRHLFDSLGIIDSGYEVARYLYATSNINLPNFFSKSRWSKVWSKNANWMGYVAVSDDNEATRCRLGRRDIAIAWRGTVTRLEWIADLKDFLKPVSGNGFRCPDPAVKAESGFLDLYTDKDTSCNFSKFSAREQVLTEVKRLVERYGDEEGEELSITVTGHSLGGALAVLSAYDVAEMG... | Function: Acylhydrolase with a broad specificity. Catalyzes the hydrolysis of phosphatidylcholine at the sn-1 position. Moderate activity toward phosphatidylcholine (PC), monogalactosyldiacylglycerol (MGDG), digalactosyldiacylglycerol (DGDG) and triacylglycerol (TAG). May display dual sn-1/sn-2 substrate specificity. C... |
Q3EBR6 | MAAIPSHNNLLTINHKNSITGSSSLNTNFSEINFPAKFRVATRALSRTDESSLSAVISRLERERRERQGLLIEEAEGAGELWMTAEDIRRRDKKTEEERRLRDTWRKIQGEDDWAGLMDPMDPILRSELIRYGEMAQACYDAFDFDPASKYCGTSRFTRLEFFDSLGMIDSGYEVARYLYATSNINLPNFFSKSRWSKVWSKNANWMGYVAVSDDETSRNRLGRRDIAIAWRGTVTKLEWIADLKDYLKPVTENKIRCPDPAVKVESGFLDLYTDKDTTCKFARFSAREQILTEVKRLVEEHGDDDDSDLSITVTGHSLG... | Function: Acylhydrolase with broad specificity . Catalyzes the hydrolysis of phosphatidylcholine at the sn-1 position . Possesses moderate activity toward phosphatidylcholine (PC), monogalactosyldiacylglycerol (MGDG), digalactosyldiacylglycerol (DGDG) and triacylglycerol (TAG) .
Catalytic Activity: 1,2-dihexadecanoyl-s... |
Q9C8J6 | MASLSLPITLKNPRFFSSSPQNIFKTQPQTLVLTTKFKTCSIICSSSCTSISSSTTQQKQSNKQTHVSDNKREEKAEEEEEEKEVSLREIWREVQGCNNWEGQLDPMNNHLRREIIRYGEFAQACYDSFDFDPHSKYCGSCKYHPSDFFLNLDLHLHKGYTITRYLYATSNINLPNFFQKSKLSSIWSQHANWMGFVAVATDEEEVSRLGRRDIVIAWRGTVTYLEWIYDLKDILCSANFGDDPSIKIELGFHDLYTKKEDSCKFSSFSAREQVLAEVKRLIEYYGTEEEGHKTSITVTGHSLGASLALVSAYDIAELNL... | Function: Acylhydrolase that catalyzes the hydrolysis of phosphatidylcholine at the sn-1 position. Moderate activity toward phosphatidylcholine (PC), monogalactosyldiacylglycerol (MGDG), digalactosyldiacylglycerol (DGDG) and triacylglycerol (TAG).
Catalytic Activity: 1,2-dihexadecanoyl-sn-glycero-3-phosphocholine + H2O... |
O82274 | MVGDIATRWKELSGSSKWKDLLDPLDLDLRRYILHYGDMAEVGYLAFNSDRRSKYVGDSCYTKEELFARTGYLKANPFRYEVTKYIYGTSSIRLPECFIIKSLSREAWNKESNWLGYIAVATDEGKKLLGRRGIVVAWRGTIQLYEWANDFDFPLESAVMVFPGANPNDEPRVANGWLSLYTSTDPRSRFDKTSAQEQVQEELKRLLELYKNEDVTITLTGHSLGAVMSILSAADFLHNEWPKITPSLQHSLCVTVFAFGSPQIGDRSFKRLVESLEHLHILRVTNVPDLIPRYPVFRFTDIGEELQINTLKSEYLKRSL... | Function: Acylhydrolase that catalyzes the hydrolysis of phospholipids at the sn-1 position.
Sequence Mass (Da): 47581
Sequence Length: 414
Subcellular Location: Cytoplasm
EC: 3.1.1.-
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Q6NYZ4 | MAWKWIKAFVYLSVCVTSALGDDEEASASKCADFNNTTWLEYRQATKLQVQYLLLTRKNANCASLFTQDCLNHTQKHTAYFNSSLPTKVIVHGYRALGSKPSWVSGLAQALLREEDVNVLVVDWVYGASFAYNLVVENYKEVAVQISVLINQLTKYGSTLESFHFIGVSLGAHVSGFVGTLFHGKLGRITGLDPAGPMFKSADPFDRLDSSDALFVEAIHTDSDYFGISIPVGHVDFFLNGGMDQAGCARSRFASMYGYVICDHMRALHVYMSALNGSCPLIGFPCSGYEEFLAGKCITCDDPFNGTCPQIGLLKNSGIT... | Function: Hydrolyzes the ester bond at the sn-1 position of glycerophospholipids and produces 2-acyl lysophospholipids. Hydrolyzes phosphatidylserine (PS) in the form of liposomes and 1-acyl-2 lysophosphatidylserine (lyso-PS), but not triolein, phosphatidylcholine (PC), phosphatidylethanolamine (PE), phosphatidic acid ... |
A0A0R4IY06 | MDNQQRRTDNMASGETDHLQCVEEPQPGDLIEIFRPAYQHWALYLGDGYIINLTPVDEGQATAVSSVKSVFSRKAVVRMQLLKEVVGADSYRINNKYDDDHTPLPVSEIIQRAQMLIGQEVSYDLLGSNCEHFVTLLRYGEGVSEQASRAIGAISLVTAAASAFSVLGLINTRSRNRPF | Function: Exhibits both phospholipase A1/2 and acyltransferase activities. Shows phospholipase A1 (PLA1) and A2 (PLA2) activity, catalyzing the calcium-independent release of fatty acids from the sn-1 or sn-2 position of glycerophospholipids. Shows O-acyltransferase activity, catalyzing the transfer of a fatty acyl gro... |
Q9HDD0 | MAFNDCFSLNYPGNPCPGDLIEVFRPGYQHWALYLGDGYVINIAPVDGIPASFTSAKSVFSSKALVKMQLLKDVVGNDTYRINNKYDETYPPLPVEEIIKRSEFVIGQEVAYNLLVNNCEHFVTLLRYGEGVSEQANRAISTVEFVTAAVGVFSFLGLFPKGQRAKYY | Function: Exhibits both phospholipase A1/2 and acyltransferase activities . Shows phospholipase A1 (PLA1) and A2 (PLA2) activity, catalyzing the calcium-independent release of fatty acids from the sn-1 or sn-2 position of glycerophospholipids . Shows O-acyltransferase activity, catalyzing the transfer of a fatty acyl g... |
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