ids stringlengths 6 10 | seqs stringlengths 11 1.02k | texts stringlengths 108 11.1k |
|---|---|---|
P27274 | MRARRGFILLLLLAVLCSTGVSLRCYNCLDPVSSCKTNSTCSPNLDACLVAVSGKQVYQQCWRFSDCNAKFILSRLEIANVQYRCCQADLCNKSFEDKPNNGAISLLGKTALLVTSVLAAILKPCF | Function: Potent inhibitor of the complement membrane attack complex (MAC) action. Acts at or after the C5b-8 stage of MAC assembly.
PTM: N-glycosylated.
Location Topology: Lipid-anchor
Sequence Mass (Da): 13790
Sequence Length: 126
Subcellular Location: Cell membrane
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P58020 | LQCYSCINQVDCTSVINCTXNQDACLY | Function: Potent inhibitor of the complement membrane attack complex (MAC) action. Acts by binding, in a species specific manner, to the C8 and/or C9 complements of the assembling MAC, thereby preventing incorporation of the multiple copies of C9 required for complete formation of the osmolytic pore.
Location Topology:... |
O43866 | MALLFSLILAICTRPGFLASPSGVRLVGGLHRCEGRVEVEQKGQWGTVCDDGWDIKDVAVLCRELGCGAASGTPSGILYEPPAEKEQKVLIQSVSCTGTEDTLAQCEQEEVYDCSHDEDAGASCENPESSFSPVPEGVRLADGPGHCKGRVEVKHQNQWYTVCQTGWSLRAAKVVCRQLGCGRAVLTQKRCNKHAYGRKPIWLSQMSCSGREATLQDCPSGPWGKNTCNHDEDTWVECEDPFDLRLVGGDNLCSGRLEVLHKGVWGSVCDDNWGEKEDQVVCKQLGCGKSLSPSFRDRKCYGPGVGRIWLDNVRCSGEEQ... | Function: Secreted protein that acts as a key regulator of lipid synthesis: mainly expressed by macrophages in lymphoid and inflamed tissues and regulates mechanisms in inflammatory responses, such as infection or atherosclerosis. Able to inhibit lipid droplet size in adipocytes. Following incorporation into mature adi... |
P26309 | MPESSRDKGNAAISGNRSVLSIASPTKLNILSSDWSRNQGKVSKNSLKRSSSLNIRNSKRPSLQASANSIYSRPKITIGAPPLIRRDSSFFKDEFDAKKDKATFSAYSSRSYPTIGSESVVSQTSLSQPTTSREVDEQFTVAADRYIPILQGASQNKVDPETLHEALPPPNASPISHLRAQTKIVFKQNVAEACGLDMNKRILQYMPEPPKCSSLRQKSYIMKKRTHYSYQQEQKIPDLIKLRKINTNPERILDAPGFQDDFYLNLLSWSKKNVLAIALDTALYLWNATTGDVSLLTDFENTTICSVTWSDDDCHISIGK... | Function: Activator protein that regulates the ubiquitin ligase activity and substrate specificity of the anaphase promoting complex/cyclosome (APC/C). At the metaphase-to-anaphase transition, recognizes and binds proteins containing a D-box including the B-type cyclins CLB2 and CLB5, HSL1 and securin PDS1, and recruit... |
Q9SZA4 | MDAGMNNTSSHYKTQARCPLQEHFLPRKPSKENLDRFIPNRSAMNFDYAHFALTEGRKGKDQTAAVSSPSKEAYRKQLAETMNLNHTRILAFRNKPQAPVELLPSNHSASLHQQPKSVKPRRYIPQTSERTLDAPDIVDDFYLNLLDWGSANVLAIALDHTVYLWDASTGSTSELVTIDEEKGPVTSINWAPDGRHVAVGLNNSEVQLWDSASNRQLRTLKGGHQSRVGSLAWNNHILTTGGMDGLIINNDVRIRSPIVETYRGHTQEVCGLKWSGSGQQLASGGNDNVVHIWDRSVASSNSTTQWLHRLEEHTSAVKAL... | Function: Component of the anaphase promoting complex/cyclosome (APC/C), a cell cycle-regulated E3 ubiquitin-protein ligase complex that controls progression through mitosis and the G1 phase of the cell cycle.
Sequence Mass (Da): 50551
Sequence Length: 457
Pathway: Protein modification; protein ubiquitination.
Subcellu... |
P19026 | VVYKARDRVTNETIALKKIRLEQEDEGVPSTAIREISLLKEMQHRNIVRLQDVVHSEKRLYLVFEYLDLDLKKHMDSSPEFVKDPRQVKMFLYQMLCGIAYCHSHRVLHRDLKPQNLLIDRRTNCVKLADFGLARAFGIPVRTFTHEV | Function: Plays a key role in the control of the eukaryotic cell cycle. It is required in higher cells for entry into S-phase and mitosis. Component of the kinase complex that phosphorylates the repetitive C-terminus of RNA polymerase II.
Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[pro... |
Q9STS3 | MVSKECCRNEIRAAIRQLSDRCLYSAAKWAGEQLVGIEQDPSNFTPANTRFQRGSSSIRRRFSTNESISTPLPSVGFSQAATPLPEEDEAIDGDIYLLAKSYFDCREYRRASHMLRDQVSKKSLFLRYYALYLAGEKRKEEEMIELEGPLGKSDAINRELVSLERDLSALRRTGAIDSFGLYLYGVVLKEKGNESLARASLVESVNSYPWNWSAWSELQSLCTSIEILNSLNLNNHWMKEFFLGNAYQELRMHTESLAKYEYLQGIFSFSNYIQAQTAKAQYSLREFDQVEIMFEELLRNDPYRVEDMDLYSNVLYAKEA... | Function: Component of the anaphase promoting complex/cyclosome (APC/C), a cell cycle-regulated E3 ubiquitin-protein ligase complex that controls progression through mitosis and the G1 phase of the cell cycle. The APC/C complex controls several key steps in the cell cycle by mediating ubiquitination and subsequent degr... |
Q86B11 | MSQIKIELIKSINDLNSRGLLLSSKWSSEQLNGLSPTILATPLTNEEQLSIISQPSISSPPIGSNEYYKYILAKNYFDLKEYRRCSDVLIDCNKYQLPIFLRSYATYLAIEKRREEDIIEQQAQQQQQQQQAQQQAQQAQQESQQNDKNNDTNNNNKTDQQQQQQQQQKIEQCQEFKQLFQFYKKLYIENKKDMDGFLLYFYSMLLKKQRDFTMARKVLIESVHKYPCNWSAWSDLSSLCSDSADIIMQLSLPDHFMKDFFLAHFKLELQQNNESLVIYQQLSRTLFTQSTYILAQTAIGNYNLRAYDIGEELFERLIEL... | Function: Component of the anaphase promoting complex/cyclosome (APC/C), a cell cycle-regulated E3 ubiquitin-protein ligase complex that controls progression through mitosis and the G1 phase of the cell cycle.
Sequence Mass (Da): 69874
Sequence Length: 592
Pathway: Protein modification; protein ubiquitination.
Subcellu... |
Q9UJX2 | MAASTSMVPVAVTAAVAPVLSINSDFSDLREIKKQLLLIAGLTRERGLLHSSKWSAELAFSLPALPLAELQPPPPITEEDAQDMDAYTLAKAYFDVKEYDRAAHFLHGCNSKKAYFLYMYSRYLSGEKKKDDETVDSLGPLEKGQVKNEALRELRVELSKKHQARELDGFGLYLYGVVLRKLDLVKEAIDVFVEATHVLPLHWGAWLELCNLITDKEMLKFLSLPDTWMKEFFLAHIYTELQLIEEALQKYQNLIDVGFSKSSYIVSQIAVAYHNIRDIDKALSIFNELRKQDPYRIENMDTFSNLLYVRSMKSELSYLA... | Function: Component of the anaphase promoting complex/cyclosome (APC/C), a cell cycle-regulated E3 ubiquitin ligase that controls progression through mitosis and the G1 phase of the cell cycle. The APC/C complex acts by mediating ubiquitination and subsequent degradation of target proteins: it mainly mediates the forma... |
P16522 | MNDDSQDKIIHDIRIQLRKAATELSRWKLYGSSKWAAEALAGLAEAIDVDQTHSLADESPLRNKQGVPKQMFEIPQNGFGLSETEYDLYLLGSTLFDAKEFDRCVFFLKDVTNPYLKFLKLYSKFLSWDKKSQESMENILTTGKFTDEMYRANKDGDGSGNEDINQSGHQRANLKMVSNEHESQSNISSILKEINTFLESYEIKIDDDEADLGLALLYYLRGVILKQEKNISKAMSSFLKSLSCYSFNWSCWLELMDCLQKVDDALLLNNYLYQNFQFKFSENLGSQRTIEFNIMIKFFKLKVFEELNGQLEDYFEDLEF... | Function: Component of the anaphase promoting complex/cyclosome (APC/C), a cell cycle-regulated E3 ubiquitin-protein ligase complex that controls progression through mitosis and the G1 phase of the cell cycle. The APC/C is thought to confer substrate specificity and, in the presence of ubiquitin-conjugating E2 enzymes,... |
Q8GY31 | MGRSIFSFFTKKKKMAMARSISYITSTQLLPLHRRPNIAIIDVRDEERNYDGHIAGSLHYASGSFDDKISHLVQNVKDKDTLVFHCALSQVRGPTCARRLVNYLDEKKEDTGIKNIMILERGFNGWEASGKPVCRCAEVPCKGDCA | Function: Tyrosine protein phosphatase that dephosphorylates CDK complex and activate its kinase activity in vitro.
Catalytic Activity: H2O + O-phospho-L-tyrosyl-[protein] = L-tyrosyl-[protein] + phosphate
Sequence Mass (Da): 16450
Sequence Length: 146
Subcellular Location: Nucleus
EC: 3.1.3.48
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P32320 | MAQKRPACTLKPECVQQLLVCSQEAKKSAYCPYSHFPVGAALLTQEGRIFKGCNIENACYPLGICAERTAIQKAVSEGYKDFRAIAIASDMQDDFISPCGACRQVMREFGTNWPVYMTKPDGTYIVMTVQELLPSSFGPEDLQKTQ | Function: This enzyme scavenges exogenous and endogenous cytidine and 2'-deoxycytidine for UMP synthesis.
Catalytic Activity: cytidine + H(+) + H2O = NH4(+) + uridine
Sequence Mass (Da): 16185
Sequence Length: 146
EC: 3.5.4.5
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A6TBN1 | MHSRFQAALTTLAADLQAAIAPMLADPHFPALLEADQVATLQHATGLDEDALAFALLPLAAACARPDLSHFNVGAIARGVSGRWYFGGNMEFLGATMQQTVHAEQSAISHAWLRGETSLRAITVNYTPCGHCRQFMNELNSGLALRIHLPGREAHALEHYLPDAFGPKDLEIKTLLMDEQDHGFPVSGDALTQAAIQAANRCHAPYSHSPSGVALELKDGTIFSGSYAENAAFNPTLPPLQGALNLLSLNGYDYPAIQRAILAEKADAALIQWDATVATLKALGCHNIERVLLG | Cofactor: Binds 1 zinc ion.
Function: This enzyme scavenges exogenous and endogenous cytidine and 2'-deoxycytidine for UMP synthesis.
Catalytic Activity: cytidine + H(+) + H2O = NH4(+) + uridine
Sequence Mass (Da): 31477
Sequence Length: 294
EC: 3.5.4.5
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Q65RG8 | MKNTIIKGLTDLVEQKRDNLIRQVVVQLEAQGYKAVLEQATVQQFCRQFALSPVEFALRCLPVAACYALTPISQFNVGAIAIGQSGSFYFGANQEFVAASMQQTVHAEQSAISHAWLAGEKAIAHMVVNYTPCGHCRQFMNELNSAERLKIHLPHSQNNLLHNYLPDAFGPKDLNIQNVFFDGQSHPFNYQGHDPLIRAAVEAASQSYAPYSQAFSGVALQLGELIICGRYAENAAFNPTFLPLQSALNYQRLQGLIDVKVSRVVMAEAKADLTSLPMTQSLAGAHLGLDIEYISL | Cofactor: Binds 1 zinc ion.
Function: This enzyme scavenges exogenous and endogenous cytidine and 2'-deoxycytidine for UMP synthesis.
Catalytic Activity: cytidine + H(+) + H2O = NH4(+) + uridine
Sequence Mass (Da): 32541
Sequence Length: 296
EC: 3.5.4.5
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P56389 | MAQERPSCAVEPEHVQRLLLSSREAKKSAYCPYSRFPVGAALLTGDGRIFSGCNIENACYPLGVCAERTAIQKAISEGYKDFRAIAISSDLQEEFISPCGACRQVMREFGTDWAVYMTKPDGTFVVRTVQELLPASFGPEDLQKIQ | Function: This enzyme scavenges exogenous and endogenous cytidine and 2'-deoxycytidine for UMP synthesis.
Catalytic Activity: cytidine + H(+) + H2O = NH4(+) + uridine
Sequence Mass (Da): 16131
Sequence Length: 146
EC: 3.5.4.5
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P47298 | MKVNLEWIIKQLQMIVKRAYTPFSNFKVACMIIANNQTFFGVNIENSSFPVTLCAERSAIASMVTSGHRKIDYVFVYFNTKNKSNSPCGMCRQNLLEFSHQKTKLFCIDNDSSYKQFSIDELLMNGFKKS | Cofactor: Binds 1 zinc ion.
Function: This enzyme scavenges exogenous and endogenous cytidine and 2'-deoxycytidine for UMP synthesis.
Catalytic Activity: cytidine + H(+) + H2O = NH4(+) + uridine
Sequence Mass (Da): 14974
Sequence Length: 130
EC: 3.5.4.5
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P47718 | MKEKDIYFQKLNELISNAYVPYSNFRVSCLLLTDGGWFAGVNIENSAYSPTICAERSAVSSMITSGFKQIFKVYILTDTIVKDIGTPCGVCRQVLSEFAKPETPIITYNLKGEKFFYTLEQLLPFAFNKDALK | Cofactor: Binds 1 zinc ion.
Function: This enzyme scavenges exogenous and endogenous cytidine and 2'-deoxycytidine for UMP synthesis.
Catalytic Activity: cytidine + H(+) + H2O = NH4(+) + uridine
Sequence Mass (Da): 15018
Sequence Length: 133
EC: 3.5.4.5
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P9WPH2 | MPDVDWNMLRGNATQAAAGAYVPYSRFAVGAAALVDDGRVVTGCNVENVSYGLTLCAECAVVCALHSTGGGRLLALACVDGHGSVLMPCGRCRQVLLEHGGSELLIDHPVRPRRLGDLLPDAFGLDDLPRERR | Cofactor: Binds 1 Zn(2+) ion per subunit.
Function: Recycles cytidine and 2-deoxycytidine for uridine and 2-deoxyuridine synthesis, respectively. Catalyzes the hydrolytic deamination of cytidine and 2-deoxycytidine to form, respectively, uridine and 2-deoxyuridine (By similarity).
Catalytic Activity: cytidine + H(+) + ... |
Q3IBX5 | MASATFLVQANTALSNTHISLSVAQTQALRSQLKTQRGILNANNINQLCAQLNVTNDALLQGLVPLASEFAVAPVSNFHVGAIVKALDESGEVNFYFGANAEFNRQALSLVVHAEQSAINNAWLNGAKKILKIAISDAPCGYCRQFMNELADAREFDILLPEQQFKLADLLPHSFGPTDLGNQYSLFNPAPQARSFNNTEVEQQLAAYALAAYVPYSQNYSAVKITTFNNGDFYGSYAENAAYSPSLSPLQSALSQLFLAGLSFDQHTVKGITLLETAGHENQAGVAQAVLASFVNLPPLELISAPLSE | Cofactor: Binds 1 zinc ion.
Function: This enzyme scavenges exogenous and endogenous cytidine and 2'-deoxycytidine for UMP synthesis.
Catalytic Activity: cytidine + H(+) + H2O = NH4(+) + uridine
Sequence Mass (Da): 33242
Sequence Length: 309
EC: 3.5.4.5
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Q01738 | MLGRSLLALLPFVGLAFSQSASQFTDPTTGFQFTGITDPVHDVTYGFVFPPLATSGAQSTEFIGEVVAPIASKWIGIALGGAMNNDLLLVAWANGNQIVSSTRWATGYVQPTAYTGTATLTTLPETTINSTHWKWVFRCQGCTEWNNGGGIDVTSQGVLAWAFSNVAVDDPSDPQSTFSEHTDFGFFGIDYSTAHSANYQNYLNGDSGNPTTTSTKPTSTSSSVTTGPTVSATPYDYIIVGAGPGGIIAADRLSEAGKKVLLLERGGPSTKQTGGTYVAPWATSSGLTKFDIPGLFESLFTDSNPFWWCKDITVFAGCLV... | Cofactor: Binds 1 FAD per subunit.
Function: Degrades both lignin and cellulose. Oxidizes cellobiose to cellobionolactone.
Catalytic Activity: A + D-cellobiose = AH2 + D-cellobiono-1,5-lactone
Sequence Mass (Da): 82007
Sequence Length: 773
Subcellular Location: Secreted
EC: 1.1.99.18
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Q8ZA34 | MSRSIKWRRYLLTLLILIILAAGLIYKLRFSNADALWKIISQQCIPHMTTEDDPRPCAEVNIPAGFAVLKDRNGPLQYLLIPTVPISGIESPQLLTATSPNYFADAWQARYFMAEKYGAPIDDTDISLAINSQYGRTQDQLHIHISCLKPQVKTALAAHSADFQQQWQPLPGGLLGHDYWVRRITATELQQPGPFHLLADEMPGAKEQMGRYGLAITALPSGDFLLLANKASLITQDRASAEELQDHTCQVLPHLPVQ | Catalytic Activity: a CDP-1,2-diacyl-sn-glycerol + H2O = a 1,2-diacyl-sn-glycero-3-phosphate + CMP + 2 H(+)
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 28779
Sequence Length: 258
Pathway: Phospholipid metabolism; CDP-diacylglycerol degradation; phosphatidate from CDP-diacylglycerol: step 1/1.
Su... |
B3BM80 | MVNATLSVVQKNSAFVGSATGELAARAIGMLYPGVKQSDLSEEQKQTISTLATVSAGLAGGLTGSSTASAAVGAQSGKNAVENNYLSTNQSLTFDKELSDCRKSGGNCQDIIDKWEKISDEQSAEIDQKLKDNPLEAQVIDKEVAKGGYDMTQRPGWLGNIGVEVMTSDEAKAYVQKWNGRDLTKIDVNSPEWTKFAVFASDPENQAMLVSGGLLVKDITKAAISFMSRNTATATVNASEVGMQWGQGNMKQGMPWEDYVGKSLPADARLPKNFKIFDYYDGATKTATSVKSIDTQTMAKLANPNQVYSSIKGNIDAAAK... | Cofactor: Bind 1 Zn(2+) per subunit.
Function: Toxic component of a toxin-immunity protein module, which functions as a cellular contact-dependent growth inhibition (CDI) system. CDI modules allow bacteria to communicate with and inhibit the growth of closely related neighboring bacteria in a contact-dependent fashion ... |
Q27032 | MRRYHKMEKIGEGTYGVVYKAQNNHGEICALKKIRVEEEDEGIPSTAIREISLLKELHHPNIVWLRDVIHSEKCLTLVFEYLDQDLKKLLDACDGGLEPTTAKSFLYQILRGISYCHDHRILHRDLKPQNLLINREGVLKLADFGLARAFAIPVRSYTHEVVTLWYRAPDVLMGSKKYSTAVDIWSVGCIFAEMINGVPLFPGISEQDQLKRIFKILGTPSVDSWPQVVNLPAYNPDFSYYEKQSWSSIVPKLNESGIDLISRMLQLDPVQRISAKEALKHDYFKDLHRPPEFLNGVH | Function: Serine/threonine-protein kinase (By similarity). Involved in the control of the cell cycle. Required for entry into S-phase and mitosis (By similarity). Probable component of the kinase complex that phosphorylates the repetitive C-terminus of RNA polymerase II (By similarity).
Catalytic Activity: ATP + L-sery... |
O61847 | MSREIRSLESIISDARENTHEKMLIRKQRDMTTDIAPERDLQGRFCSLRRIGEGTYGVVFKAIHVRDNVKCALKMIRTDRDEEGIPSTCLREISCIKDLQHDNIVTLFDIIYANSKLYMVFEFIDRDLKNLLEMLEPTNSVLPPNYVKSFMWQLLSALSYCHLRRIVHRDLKPQNILVSDSGVIKIADFGLARNFSFPSRNYTHEVVTLWYRPPEILLGSQRYSTSLDMWSLGCIFSEIASNKPLFPGECEISQLFKIFEIVGTPNIKSWPGVDSFPHYKAVFPQWPVNLKKLEETSCLTGNGLDVLREILRYPPERRLT... | Cofactor: Binds 2 Mg(2+) ions.
Function: Serine/threonine-protein kinase which, in association with cye-1, regulates proliferation, quiescent state and cell fate during the development of several cell lineages . In the embryo, initiates the establishment of cell polarity through the recruitment of the centrosomal prote... |
P43450 | MESFQKVEKIGEGTYGVVYKAKNKVTGETVALKKIRLDTETEGVPSTAIREISLLKELNHPNIVKLHDVIHTENKLYLVFEFLHQDLKRFMDSSTVTGISLPLVKSYLFQLLQGLAFCHSHRVLHRDLKPQNLLINAQGEIKLADFGLARAFGVPVRTYTHEVVTLWYRAPEILLGCKYYSTAVDIWSLGCIFAEMITRKALFPGDSEIDQLFRIFRTLGTPDESIWPGVTSMPDYKPSFPKWARQDLSKVVPPLDEDGRDLLGQMLIYDPNKRISAKNALVHRFFRDVTMPVPPLRL | Function: Involved in the control of the cell cycle. Interacts with cyclins A, B1, B3, D, or E. Activity of CDK2 is maximal during S phase and G2 (By similarity).
Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Sequence Mass (Da): 33999
Sequence Length: 298
EC: 2.7.11.22
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O55076 | MENFQKVEKIGEGTYGVVYKAKNKLTGEVVALKKIRLDTETEGVPSTAIREISLLKELNHPNIVKLLDVIHTENKLYLVFEFLHQDLKKFMDASAVTGIPLPLIKSYLFQLLQGLAFCHSHRVLHRDLKPQNLLINAEGSIKLADFGLARAFGVPVRTYTHEVVTLWYRAPEILLGCKYYSTAVDIWSLGCIFAEMVTRRALFPGDSEIDQLFRIFRTLGTPDEVVWPGVTSMPDYKPSFPKWARQDFSKVVPPLDEDGRSLLSQMLHYDPNKRISAKAALAHPFFQDVTKPVPHLRL | Cofactor: Binds 2 Mg(2+) ions.
Function: Serine/threonine-protein kinase involved in the control of the cell cycle; essential for meiosis, but dispensable for mitosis. Phosphorylates CTNNB1, USP37, p53/TP53, NPM1, CDK7, RB1, BRCA2, MYC, NPAT, EZH2. Triggers duplication of centrosomes and DNA. Acts at the G1-S transitio... |
P23573 | MTTILDNFQRAEKIGEGTYGIVYKARSNSTGQDVALKKIRLEGETEGVPSTAIREISLLKNLKHPNVVQLFDVVISGNNLYMIFEYLNMDLKKLMDKKKDVFTPQLIKSYMHQILDAVGFCHTNRILHRDLKPQNLLVDTAGKIKLADFGLARAFNVPMRAYTHEVVTLWYRAPEILLGTKFYSTGVDIWSLGCIFSEMIMRRSLFPGDSEIDQLYRIFRTLSTPDETNWPGVTQLPDFKTKFPRWEGTNMPQPITEHEAHELIMSMLCYDPNLRISAKDALQHAYFRNVQHVDHVALPVDPNAGSASRLTRLV | Function: Like Cdk1, could play a key role in the control of the eukaryotic cell cycle.
Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Sequence Mass (Da): 35888
Sequence Length: 314
EC: 2.7.11.22
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P24941 | MENFQKVEKIGEGTYGVVYKARNKLTGEVVALKKIRLDTETEGVPSTAIREISLLKELNHPNIVKLLDVIHTENKLYLVFEFLHQDLKKFMDASALTGIPLPLIKSYLFQLLQGLAFCHSHRVLHRDLKPQNLLINTEGAIKLADFGLARAFGVPVRTYTHEVVTLWYRAPEILLGCKYYSTAVDIWSLGCIFAEMVTRRALFPGDSEIDQLFRIFRTLGTPDEVVWPGVTSMPDYKPSFPKWARQDFSKVVPPLDEDGRSLLSQMLHYDPNKRISAKAALAHPFFQDVTKPVPHLRL | Cofactor: Binds 2 Mg(2+) ions.
Function: Serine/threonine-protein kinase involved in the control of the cell cycle; essential for meiosis, but dispensable for mitosis. Phosphorylates CTNNB1, USP37, p53/TP53, NPM1, CDK7, RB1, BRCA2, MYC, NPAT, EZH2. Triggers duplication of centrosomes and DNA. Acts at the G1-S transitio... |
P97377 | MENFQKVEKIGEGTYGVVYKAKNKLTGEVVALKKIRLDTETEGVPSTAIREISLLKELNHPNIVKLLDVIHTENKLYLVFEFLHQDLKKFMDASALTGIPLPLIKSYLFQLLQGLAFCHSHRVLHRDLKPQNLLINAEGSIKLADFGLARAFGVPVRTYTHEVVTLWYRAPEILLGCKYYSTAVDIWSLGCIFAEMHLVCTQHHAKCCGEHRRNGRHSLCPLCSYLEVAASQGGGMTAVSAPHPVTRRALFPGDSEIDQLFRIFRTLGTPDEVVWPGVTSMPDYKPSFPKWARQDFSKVVPPLDEDGRSLLSQMLHYDPN... | Cofactor: Binds 2 Mg(2+) ions.
Function: Serine/threonine-protein kinase involved in the control of the cell cycle; essential for meiosis, but dispensable for mitosis. Phosphorylates CTNNB1, USP37, p53/TP53, NPM1, CDK7, RB1, BRCA2, MYC, NPAT, EZH2. Triggers duplication of centrosomes and DNA. Acts at the G1-S transitio... |
P23437 | MENFQKVEKIGEGTYGVVYKARNRETGEIVALKKIRLDTETEGVPSTAIREISLLKELNHPNIVKLLDVIHTENKLYLVFEFLNQDLKKFMDGSNISGISLALVKSYLFQLLQGLAFCHSHRVLHRDLKPQNLLINSDGAIKLADFGLARAFGVPVRTFTHEVVTLWYRAPEILLGCKFYSTAVDIWSLGCIFAEMITRRALFPGDSEIDQLFRIFRTLGTPDEVSWPGVTTMPDYKSTFPKWIRQDFSKVVPPLDEDGRDLLAQMLQYDSNKRISAKVALTHPFFRDVSRPTPHLI | Function: Involved in the control of the cell cycle. Interacts with cyclins A, B, D, or E. Activity of CDK2 is maximal during S phase and G2.
Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Sequence Mass (Da): 33870
Sequence Length: 297
EC: 2.7.11.22
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Q9UY86 | MNPIFEAFWYILPAYFANSSPVVLGGGTPIDFGKKWRDGRRIFGDGKTWRGFFGGITVGTVVGTIQHLMFPGYYGSLKLAVGVAFLLSLGALVGDLIGSFIKRRLNMPRGYPAVGLDQWGFLISALCFAYPLRTIPTGEVLFLLVVTPVIHWLANVFAYRMKWKNVPW | Function: Catalyzes the formation of CDP-2,3-bis-(O-geranylgeranyl)-sn-glycerol (CDP-archaeol) from 2,3-bis-(O-geranylgeranyl)-sn-glycerol 1-phosphate (DGGGP) and CTP. This reaction is the third ether-bond-formation step in the biosynthesis of archaeal membrane lipids.
Catalytic Activity: 2,3-bis-O-(geranylgeranyl)-sn-... |
O58081 | MKMNQLLEAFWYILPAYFANSSPVVLGGGTPIDFGKKWRDGRRILGDGKTWRGFFGGLIVGTIIGIVQYFLLPEYYGSLGIAIELAFLLSLGTLVGDLIGSFIKRRLNMPRGYPAVGLDQWGFLIAALCFAYPVKTIPTGEVLFLLVITPLIHWGANIFAYKMGWKKVPW | Function: Catalyzes the formation of CDP-2,3-bis-(O-geranylgeranyl)-sn-glycerol (CDP-archaeol) from 2,3-bis-(O-geranylgeranyl)-sn-glycerol 1-phosphate (DGGGP) and CTP. This reaction is the third ether-bond-formation step in the biosynthesis of archaeal membrane lipids.
Catalytic Activity: 2,3-bis-O-(geranylgeranyl)-sn-... |
A1RSF4 | MDLLYFFLLIWPPYVANGSAVLANKFKIRHPIDFGKTFVDGRRIFGDGKTYEGFLIGLSTGTFIGYAPNLLYKHLSLLDAFVLSIAALLGDLFGAFIKRRLCMPRGYPAFPLDQLDFLLTSLAVYTLYKDISVEYIIAAVIITPLIHRITNYIAYYLRLKKEPW | Function: Catalyzes the formation of CDP-2,3-bis-(O-geranylgeranyl)-sn-glycerol (CDP-archaeol) from 2,3-bis-(O-geranylgeranyl)-sn-glycerol 1-phosphate (DGGGP) and CTP. This reaction is the third ether-bond-formation step in the biosynthesis of archaeal membrane lipids.
Catalytic Activity: 2,3-bis-O-(geranylgeranyl)-sn-... |
Q9UXG3 | MSIAYDLLLSILIYLPAFVANGSGPFIKRGTPIDFGKNFVDGRRLFGDGKTFEGLIVALTFGTTVGVIISKFFTAEWTLISFLESLFAMIGDMIGAFIKRRLGIPRGGRVLGLDQLDFVLGASLILVLMRVNITWYQFLFICGLAFFLHQGTNYVAYLLKIKNVPW | Function: Catalyzes the formation of CDP-2,3-bis-(O-geranylgeranyl)-sn-glycerol (CDP-archaeol) from 2,3-bis-(O-geranylgeranyl)-sn-glycerol 1-phosphate (DGGGP) and CTP. This reaction is the third ether-bond-formation step in the biosynthesis of archaeal membrane lipids.
Catalytic Activity: 2,3-bis-O-(geranylgeranyl)-sn-... |
A3DM64 | MSGYMISPEYYFIYWFLKYYLSPMIANASPVLVKGIHRIDFSHIFIDGKPLFGKNKTWEGFYVGVLMGFLTSIGIGIILCEEEYILIGLGSSIFALIGDLLGSFIKRRMNIASGEPLPIIDQLDFALMATLYYYFLGIEEFISYPLYILYSLIIILALHIITNNIAYYLGVKDKRW | Function: Catalyzes the formation of CDP-2,3-bis-(O-geranylgeranyl)-sn-glycerol (CDP-archaeol) from 2,3-bis-(O-geranylgeranyl)-sn-glycerol 1-phosphate (DGGGP) and CTP. This reaction is the third ether-bond-formation step in the biosynthesis of archaeal membrane lipids.
Catalytic Activity: 2,3-bis-O-(geranylgeranyl)-sn-... |
Q9HLW7 | MQSIILFIPALIANSGAVITGGHFIIDRGKKFIDGRRILGNGKTLSGYAGGIAIGTVTGFIIYLISTLFNYALGTYGTLAEAIIIPFIMATGSLTGDIAGSFVKRRIGIDRGGKGGLLDQWPFALMAFLFLYIFERPFFMYHYFYVTMIVILVIVPPIHRAVNIIGYKMHKKDVPW | Function: Catalyzes the formation of CDP-2,3-bis-(O-geranylgeranyl)-sn-glycerol (CDP-archaeol) from 2,3-bis-(O-geranylgeranyl)-sn-glycerol 1-phosphate (DGGGP) and CTP. This reaction is the third ether-bond-formation step in the biosynthesis of archaeal membrane lipids.
Catalytic Activity: 2,3-bis-O-(geranylgeranyl)-sn-... |
Q5JEX0 | MGWLSSIFWAFWYILPAYFANASPVLVGGGRPIDGGRVWRDGRRLLGDGKTWRGFIGGVLIGTLVGIVQYFITPDFYGSLETAVKLAFLLSFGALIGDLVGSFIKRRANLPRGYPAIGLDQLGFLISALAFAYPVKTLSSGQIIFLLVVSPFIHWGANYFAYRMGWKSVPW | Function: Catalyzes the formation of CDP-2,3-bis-(O-geranylgeranyl)-sn-glycerol (CDP-archaeol) from 2,3-bis-(O-geranylgeranyl)-sn-glycerol 1-phosphate (DGGGP) and CTP. This reaction is the third ether-bond-formation step in the biosynthesis of archaeal membrane lipids.
Catalytic Activity: 2,3-bis-O-(geranylgeranyl)-sn-... |
O52582 | MPKIVVVGAVAGGATCASQIRRLDKESDIIIFEKDRDMSFANCALPYVIGEVVEDRRYALAYTPEKFYDRKQITVKTYHEVIAINDERQTVSVLNRKTNEQFEESYDKLILSPGASANSLGFESDITFTLRNLEDTDAIDQFIKANQVDKVLVVGAGYVSLEVLENLNERGLHPTLIHRSDKINKLMDADMNQPILDELDKREIPYRLNEEINAINGNEITFKSGKVEHYDMIIEGVGTHPNSKFIESSNIKLDRKGFIPVNDKFETNVPNIYAIGDIATSHYRHVDLPASVPLAWGAHRAASIVAEQIAGNDTIEFKGF... | Cofactor: Binds 1 FAD per subunit.
Function: Catalyzes specifically the NADPH-dependent reduction of coenzyme A disulfide. Is also active with other disulfide substrates containing at least one 4'-phosphopantethienyl moiety such as 4,4'-diphosphopantethine, but is not able to reduce oxidized glutathione, cystine, pante... |
Q49X46 | MKVRTLTAIIALIVFLPVLLKGGLILMLFSYLLAFIALKELLNMNMIKFLSIPGIISALGILIIMLPQDAGSWVNDLQLKSLIAMSFILLSYTVLSKNRFSFMDAAFCLMSIAYVGIGFMYLYETRSEGLHYILFAFLVVWLTDTGAYIFGRLMGKHKLWPVISPNKTVEGFVGGLICSLIVPLVMMIFVDFNIALWLLLIITIILSMFGQLGDLVESGFKRHFGVKDSGRILPGHGGILDRFDSFMFVLPLLNILLIQI | Catalytic Activity: a 1,2-diacyl-sn-glycero-3-phosphate + CTP + H(+) = a CDP-1,2-diacyl-sn-glycerol + diphosphate
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 29066
Sequence Length: 260
Pathway: Phospholipid metabolism; CDP-diacylglycerol biosynthesis; CDP-diacylglycerol from sn-glycerol 3-phospha... |
P73548 | MPTQRIISAVIGIALAFSLLILGGWYFSAAIALVIYLGLREYFQMVRAKGIAPAAKTTMVLSLMLLLSATVTPHLTDAFFPLTGALICFYLLFQPKMATIADISTSLLGLFYGGYLPSYWVRLRLGDGAVNPMGLHLPLNGFWPESWAHPENFPTGLLVTILAFACIWAADIGAYIMGKWLGRTRLSDISPKKTVEGSLWGVGGSLLVGVLGAWYLQWPYWEITGALLGLLIGIVSLLGDLTESMMKRDAGVKDSGQLIPGHGGILDRTDSYVFTAPLVYYFVVLLLPVLNNL | Catalytic Activity: a 1,2-diacyl-sn-glycero-3-phosphate + CTP + H(+) = a CDP-1,2-diacyl-sn-glycerol + diphosphate
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 31876
Sequence Length: 293
Pathway: Phospholipid metabolism; CDP-diacylglycerol biosynthesis; CDP-diacylglycerol from sn-glycerol 3-phospha... |
Q9X1B7 | MDDLKTRVITASVVAPFVVLCFVSYESLIGLVSAILILAGYELITLEMKERDARFFYVILLALYPVLYGLVFEEPTQPLSILFITGVVFSLITDKDPSQVFKTVAAFSIALIYVTFFLSFFLPIYRDFGAANALLVLTSTWVFDSFAYFTGLKFGRTRISPRYSPRKSLEGVIGGFLGVVIYTFLYRLVVNDLLSVNVISFRTFLPFAATVAIMDTFGDIFESALKRHYGVKDSGKTLPGHGGMLDRIDGLLFVAPVSYIVFKILEGVVR | Catalytic Activity: a 1,2-diacyl-sn-glycero-3-phosphate + CTP + H(+) = a CDP-1,2-diacyl-sn-glycerol + diphosphate
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 30099
Sequence Length: 270
Pathway: Phospholipid metabolism; CDP-diacylglycerol biosynthesis; CDP-diacylglycerol from sn-glycerol 3-phospha... |
Q9P381 | MARKRTNKRNNSDKENGNVGVVQNKDSASSKTTEPARLTKHKSLARKPSQNFITRTIWTFLLLGIFFTALAMGHFWVVLLVTIVQIGVYKEVIAIASVPSREKDLPWTRFINWYFLMTTLYYAYGESIYAYFHHLFIMDSFMLPLVLHHRFISFMLYIIGFVLFVASLKKGNYKFQFSQFCWTHMTLLLVVGQSHFMINNLFEGLFWFFVPVCYVVCNDVFAYLCGKMFGKHPLIQVSPKKTVEGFLGGWICTVVIGSLISYVLMHFKYFICPTRDLSTSAFSGLNCTPNSVFLPHTYTIPAVFVDTFRLPETITLAPIY... | Function: Supplies CDP-diacylglycerol, which may play an important role as both a precursor to phosphoinositide biosynthesis in the plasma membrane and as a negative effector of phosphatidylinositol 4-kinase activity, thereby exerting an effect on cell proliferation via a lipid-dependent signal transduction cascade.
Ca... |
P56079 | MAEVRRRKGEDEPLEDTAISGSDAANKRNSAADSSDHVDSEEEKIPEEKFVDELAKNLPQGTDKTPEILDSALKDLPDRWKNWVIRGIFTWIMICGFALIIYGGPLALMITTLLVQVKCFQEIISIGYQVYRIHGLPWFRSLSWYFLLTSNYFFYGENLVDYFGVVINRVEYLKFLVTYHRFLSFALYIIGFVWFVLSLVKKYYIKQFSLFAWTHVSLLIVVTQSYLIIQNIFEGLIWFIVPVSMIVCNDVMAYVFGFFFGRTPLIKLSPKKTWEGFIGGGFATVLFGILFSYVLCNYQYFICPIQYSEEQGRMTMSCVP... | Function: Catalyzes the conversion of phosphatidic acid (PA) to CDP-diacylglycerol (CDP-DAG), an important precursor for the synthesis of phosphatidylinositol (PtdIns) and phosphatidylglycerol (PG) . Required for the regeneration of the signaling molecule phosphatidylinositol 4,5-bisphosphate (PtdInsP2) from PA and mai... |
Q9SJW9 | MSTPGSSRSIPFKSKKRLVMDSPSSKSQTGNPNPSSVALPTPEKPLENMLSRSRNRSVALSVKEIRQAAGSRRRSEDPVASSAKSRLFFDSSSSSPSKRKSSNKNAEKEKLPEKYENLGKFFEALDNSMLLSKLRGSKPTFSNISKQIEHLTERRFCYSHLAQIKHILPEAIEIKRVLIHDETTCCMKPDLHVTLNADAVEYNDKSKSESKKIALRKVFRARLADFVKAHPQGDEVPEEPLPEPFNRRKPVENSNVEVKRVSSLMEEMASIPASKLFSSPITSTPVKTTSSLAKPTSSQINIAPTPTKPTSTPAKQTLSE... | Function: Member of the pre-replication complex. Component of the plastid division machinery. Promotes polyloidization and regulates endoreduplication. Involved in the coordination of cell and plastid division.
PTM: Phosphorylated by cyclin D- and cyclin A-containing CDKA-1, and thus targeted to proteasome-mediated pro... |
P49715 | MESADFYEAEPRPPMSSHLQSPPHAPSSAAFGFPRGAGPAQPPAPPAAPEPLGGICEHETSIDISAYIDPAAFNDEFLADLFQHSRQQEKAKAAVGPTGGGGGGDFDYPGAPAGPGGAVMPGGAHGPPPGYGCAAAGYLDGRLEPLYERVGAPALRPLVIKQEPREEDEAKQLALAGLFPYQPPPPPPPSHPHPHPPPAHLAAPHLQFQIAHCGQTTMHLQPGHPTPPPTPVPSPHPAPALGAAGLPGPGSALKGLGAAHPDLRASGGSGAGKAKKSVDKNSNEYRVRRERNNIAVRKSRDKAKQRNVETQQKVLELTSD... | Function: Transcription factor that coordinates proliferation arrest and the differentiation of myeloid progenitors, adipocytes, hepatocytes, and cells of the lung and the placenta. Binds directly to the consensus DNA sequence 5'-T[TG]NNGNAA[TG]-3' acting as an activator on distinct target genes . During early embryoge... |
P53566 | MESADFYEVEPRPPMSSHLQSPPHAPSNAAFGFPRGAGPAPPPAPPAAPEPLGGICEHETSIDISAYIDPAAFNDEFLADLFQHSRQQEKAKAAAGPAGGGGDFDYPGAPAGPGGAVMSAGAHGPPPGYGCAAAGYLDGRLEPLYERVGAPALRPLVIKQEPREEDEAKQLALAGLFPYQPPPPPPPPHPHASPAHLAAPHLQFQIAHCGQTTMHLQPGHPTPPPTPVPSPHAAPALGAAGLPGPGSALKGLAGAHPDLRTGGGGGGSGAGAGKAKKSVDKNSNEYRVRRERNNIAVRKSRDKAKQRNVETQQKVLELTS... | Function: Transcription factor that coordinates proliferation arrest and the differentiation of myeloid progenitors, adipocytes, hepatocytes, and cells of the lung and the placenta . Binds directly to the consensus DNA sequence 5'-T[TG]NNGNAA[TG]-3' acting as an activator on distinct target genes. During early embryoge... |
Q05826 | MQRLVAWDAACLPIQPPAFKSMEVANFYYEADCLAALNKLHPRAAGGRSMTELTVGDHERAIDFSPYLDPLAASQQPAQPPPPAAAAGGNFEPACSSGGQDFLSDLFAEDYKGSGGGKKPDYTYISLTRHGHPCGSQSHKPGVLPGCFPPQIVETKVEPVFETLDSCKGPRKEEGGAGPGPGGMSSPYGSTVRSYLGYQSVPSGSSGNLSTSSSSSPPGTPNPSESSKSAAGAGGYSGPPAGKNKPKKCVDKHSDEYKLRRERNNIAVRKSRDKAKMRNLETQHKVLELTAENERLQKKVEQLSRELSTLRNLFKQLPEP... | Function: Important transcriptional activator regulating the expression of genes involved in immune and inflammatory responses. Binds to regulatory regions of several acute-phase and cytokines genes and probably plays a role in the regulation of acute-phase reaction, inflammation and hemopoiesis. The consensus recognit... |
P17676 | MQRLVAWDPACLPLPPPPPAFKSMEVANFYYEADCLAAAYGGKAAPAAPPAARPGPRPPAGELGSIGDHERAIDFSPYLEPLGAPQAPAPATATDTFEAAPPAPAPAPASSGQHHDFLSDLFSDDYGGKNCKKPAEYGYVSLGRLGAAKGALHPGCFAPLHPPPPPPPPPAELKAEPGFEPADCKRKEEAGAPGGGAGMAAGFPYALRAYLGYQAVPSGSSGSLSTSSSSSPPGTPSPADAKAPPTACYAGAAPAPSQVKSKAKKTVDKHSDEYKIRRERNNIAVRKSRDKAKMRNLETQHKVLELTAENERLQKKVEQL... | Function: Important transcription factor regulating the expression of genes involved in immune and inflammatory responses . Also plays a significant role in adipogenesis, as well as in the gluconeogenic pathway, liver regeneration, and hematopoiesis. The consensus recognition site is 5'-T[TG]NNGNAA[TG]-3'. Its function... |
P28033 | MHRLLAWDAACLPPPPAAFRPMEVANFYYEPDCLAYGAKAARAAPRAPAAEPAIGEHERAIDFSPYLEPLAPAADFAAPAPAHHDFLSDLFADDYGAKPSKKPADYGYVSLGRAGAKAAPPACFPPPPPAALKAEPGFEPADCKRADDAPAMAAGFPFALRAYLGYQATPSGSSGSLSTSSSSSPPGTPSPADAKAAPAACFAGPPAAPAKAKAKKTVDKLSDEYKMRRERNNIAVRKSRDKAKMRNLETQHKVLELTAENERLQKKVEQLSRELSTLRNLFKQLPEPLLASAGHC | Function: Important transcription factor regulating the expression of genes involved in immune and inflammatory responses . Also plays a significant role in adipogenesis, as well as in the gluconeogenic pathway, liver regeneration, and hematopoiesis . The consensus recognition site is 5'-T[TG]NNGNAA[TG]-3'. Its functio... |
Q15744 | MSHGTYYECEPRGGQQPLEFSGGRAGPGELGDMCEHEASIDLSAYIESGEEQLLSDLFAVKPAPEARGLKGPGTPAFPHYLPPDPRPFAYPPHTFGPDRKALGPGIYSSPGSYDPRAVAVKEEPRGPEGSRAASRGSYNPLQYQVAHCGQTAMHLPPTLAAPGQPLRVLKAPLATAAPPCSPLLKAPSPAGPLHKGKKAVNKDSLEYRLRRERNNIAVRKSRDKAKRRILETQQKVLEYMAENERLRSRVEQLTQELDTLRNLFRQIPEAANLIKGVGGCS | Function: Transcriptional activator . C/EBP are DNA-binding proteins that recognize two different motifs: the CCAAT homology common to many promoters and the enhanced core homology common to many enhancers. Required for the promyelocyte-myelocyte transition in myeloid differentiation .
PTM: Phosphorylated.
Sequence Mas... |
Q37050 | MYTFIYFKNPKHFNLSQPSRCTAQPFISTRNRPLSCPIPTVQPIYVTHGIILPILKGTLISQRGVNIVPFVSKRDSSYYTDKDKVVSITYEEIGLFPRSFSRVLDRFLKQLFSDVDNLVIQEYRFYRYLFLTTIKTIFILFFVPFLVNFAAKNYIVKPITEYFWNTSHPEIFLNSYEQKRAFVELAKFEEKIYFETLVESHSHHQTHRDSKPLRENGIYFPDGEFLDNANLLSTPRSINSNTFLKQNIDISLREEKPLTLVQGVNLLEEKKELNIPLAQENIAYNNQSIPQTSFGQGNFSSLFTGDREGEETAKQNLLSQ... | Function: May be involved in proton extrusion. Indirectly promotes efficient inorganic carbon uptake into chloroplasts.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 57855
Sequence Length: 500
Subcellular Location: Plastid
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P56349 | MKKRTREQTGLIPRSILRTFERFRKQLLPGAEMLVIQEFRISRYQVIVSVRCLITLIFVPLFINILSKSFLIRPGIEYLWNQNHNEIFLNSYQENRALHDLHQFEEKVYFDSFVTDFAPSSNVLLQKQSVEIAKNYNLESIEAISNLFADFLSFLSLSVVFLLLKPQIIILKAFLSESLYSLSDTTKSFLLILGTDLLVGFHSPRGWEVFLEWLLRHFGLPENSDFMSLFVATFPVFLDTVFKYWIFRSLNKISPSTVATYHNIIE | Function: May be involved in proton extrusion. Indirectly promotes efficient inorganic carbon uptake into chloroplasts.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 31121
Sequence Length: 266
Subcellular Location: Plastid
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A8W3D2 | MTKKKAFTPILYLSFIVFLPWWIYFSFNKCLGSWITNWWNTRESEIFLNDLQEKSILEKLIELEEFLFVDEILKKNSETHPQEFHTGIHKEAIQFIKIQNESYIHMILRLSTNLICVVIISGFYIWRNETLVILNSWSREFLYNLSDTVKVFSILLLTDLCIGFHSPHGWELMIGSIYQDFGFVQNDRIISGLVSTFPVILDTILKYWIFRYLNRVSPSLVVIYHSIND | Function: May be involved in proton extrusion. Indirectly promotes efficient inorganic carbon uptake into plastids (By similarity).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 27204
Sequence Length: 229
Subcellular Location: Plastid membrane
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Q9TM16 | MKNWKFNKINYPTFEKSGAIPRSITKTFEKLKKELNPHSESEIIEEFTISRYQTIASLRYLIVLVVFPVVVHQVSKNFIIGPAVDYFWKYNQIDVFLNSSQEERAFAELQRFEEKIHFEMLIGTKQSVSQQSLEASIKQKAVEIADHYTYESLHAIKNILADSISISVFILLIVLGKRQTFVLKSFLNEIVYGLSDTAKAFLIILFTDMFIGFHSPHGWEVVIESLLRHFGLPENRDFIFLFIATFPVSLDTVFKYWIFRYLNQVSPSAVATYHNMNE | Function: May be involved in proton extrusion. Indirectly promotes efficient inorganic carbon uptake into chloroplasts.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 32355
Sequence Length: 278
Subcellular Location: Plastid
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P49450 | MGPRRRSRKPEAPRRRSPSPTPTPGPSRRGPSLGASSHQHSRRRQGWLKEIRKLQKSTHLLIRKLPFSRLAREICVKFTRGVDFNWQAQALLALQEAAEAFLVHLFEDAYLLTLHAGRVTLFPKDVQLARRIRGLEEGLG | Function: Histone H3-like nucleosomal protein that is specifically found in centromeric nucleosomes . Replaces conventional H3 in the nucleosome core of centromeric chromatin that serves as an assembly site for the inner kinetochore . The presence of CENPA subtly modifies the nucleosome structure and the way DNA is wra... |
Q0MXD0 | MQSQQYSTPNLSLFNDGSAIIGEIRPIHGANQDVINDRALQLLQRTREHRNFLHRAHDDIRRYEPPTTQIDALENDEDENFYLNDMNTNEEYQSDRESVKSGLNSIANRYKNAVQSSPSDLDDIDFVGEEEQDLSYDESDYSDPLQEIDSNYRESPRRTTDKILKSSSKNYRRRENLGGEIRKIRQEKANKTATRYRPSDLALYEIRKYQQSTDLLISKIPFARLVKEVTDNFILENQHLQWHSMAILALQEASEAYLVGLLEHANLLALHAKRITLMKKDVQLARRIRGQFI | Function: Histone H3-like nucleosomal protein that is specifically found in centromeric nucleosomes. Replaces conventional H3 in the nucleosome core of centromeric chromatin that serves as an assembly site for the inner kinetochore. Required for recruitment and assembly of kinetochore proteins, mitotic progression and ... |
Q6CTI2 | MEQSIRSIDGSRSLSNVGASLIDRESINQRALQLLQRNRRRRLLLNRSEDKARYIQPERSASSQQIHPPEHHISAHERITKARGTRYKPTDLALAEIRKYQRSTDLLISRMPFARLVKEVTDQFTTESEPLRWQSMAIMALQEASEAYLVGLLEHTNLLALHAKRITIMRKDMQLARRIRGQFI | Function: Histone H3-like nucleosomal protein that is specifically found in centromeric nucleosomes. Replaces conventional H3 in the nucleosome core of centromeric chromatin that serves as an assembly site for the inner kinetochore. Required for recruitment and assembly of kinetochore proteins, mitotic progression and ... |
Q0MXD1 | MARISTSSNRPVPTSSALRRQRERDDGGRSTRAPGHNTGLYGNQPGDPPTIRSTNTTVKRRYRPGTKALREIRRYQRSSELLIRKLPFARLVKEVAENYIGADYGIRWQSNAVLALQEACEAFLVHLLEDTNLCAIHAKRVTIMQKDIQLARRIRGNI | Function: Histone H3-like nucleosomal protein that is specifically found in centromeric nucleosomes. Replaces conventional H3 in the nucleosome core of centromeric chromatin that serves as an assembly site for the inner kinetochore. Required for recruitment and assembly of kinetochore proteins, mitotic progression and ... |
Q7RXR3 | MPPKKGGVTKSKAVSKKAAAVPTPKATPPGRRKSRASSVQPGDPVPQGKKRRYRPGTLALKEIRNYQRTTDLLVAKLPFARLVREIAMQFRPMDEEMRWQSQAILALQEAAEAFLVHLFEDTNLCAIHAKRVTIMQKDIQLARRIRGVWGGAGWV | Function: Histone H3-like nucleosomal protein that is specifically found in centromeric nucleosomes. Replaces conventional H3 in the nucleosome core of centromeric chromatin that serves as an assembly site for the inner kinetochore. Required for recruitment and assembly of kinetochore proteins, mitotic progression and ... |
Q9Y812 | MAKKSLMAEPGDPIPRPRKKRYRPGTTALREIRKYQRSTDLLIQRLPFSRIVREISSEFVANFSTDVGLRWQSTALQCLQEAAEAFLVHLFEDTNLCAIHAKRVTIMQRDMQLARRIRGA | Function: Histone H3-like nucleosomal protein that is specifically found in centromeric nucleosomes. Replaces conventional H3 in the nucleosome core of centromeric chromatin that serves as an assembly site for the inner kinetochore. Required for recruitment and assembly of kinetochore proteins, mitotic progression and ... |
Q6CER9 | MARISLASSSAGVAGKPRGGGGLHPLGQTRKTLPGERRDTTQKITKPRYKPGQKALKEIRRYQRGTELLIAKLPFARVVREVALNYLGSEYGNLQWQSMALLALQEAAEAFLVHLFEDVNLCAIHAKRVTIMQKDMQLARRIRGAWGGAG | Function: Histone H3-like nucleosomal protein that is specifically found in centromeric nucleosomes. Replaces conventional H3 in the nucleosome core of centromeric chromatin that serves as an assembly site for the inner kinetochore. Required for recruitment and assembly of kinetochore proteins, mitotic progression and ... |
P36012 | MSSKQQWVSSAIQSDSSGRSLSNVNRLAGDQQSINDRALSLLQRTRATKNLFPRREERRRYESSKSDLDIETDYEDQAGNLEIETENEEEAEMETEVPAPVRTHSYALDRYVRQKRREKQRKQSLKRVEKKYTPSELALYEIRKYQRSTDLLISKIPFARLVKEVTDEFTTKDQDLRWQSMAIMALQEASEAYLVGLLEHTNLLALHAKRITIMKKDMQLARRIRGQFI | Function: Histone H3-like nucleosomal protein that is specifically found in centromeric nucleosomes. Replaces conventional H3 in the nucleosome core of centromeric chromatin that serves as an assembly site for the inner kinetochore. Required for recruitment and assembly of kinetochore proteins, mitotic progression and ... |
P07199 | MGPKRRQLTFREKSRIIQEVEENPDLRKGEIARRFNIPPSTLSTILKNKRAILASERKYGVASTCRKTNKLSPYDKLEGLLIAWFQQIRAAGLPVKGIILKEKALRIAEELGMDDFTASNGWLDRFRRRHGVVSCSGVARARARNAAPRTPAAPASPAAVPSEGSGGSTTGWRAREEQPPSVAEGYASQDVFSATETSLWYDFLPDQAAGLCGGDGRPRQATQRLSVLLCANADGSEKLPPLVAGKSAKPRAGQAGLPCDYTANSKGGVTTQALAKYLKALDTRMAAESRRVLLLAGRLAAQSLDTSGLRHVQLAFFPPG... | Function: Interacts with centromeric heterochromatin in chromosomes and binds to a specific 17 bp subset of alphoid satellite DNA, called the CENP-B box . May organize arrays of centromere satellite DNA into a higher-order structure which then directs centromere formation and kinetochore assembly in mammalian chromosom... |
P49451 | LGLMEVHFVAAAWQAVEPSDIAVCFREAGFGGGPNATITTALKSEGEEEEEEEEEEEEEEGEGEEEEEEDGEEEEEAGEGEELGEEEEVEEEGDVDTVEEEEEEEEESSSEGLEAEDWAQGVVEAGGSFGGYGAQEEAQCPTLHFLEGEEDSESDSEEEEEDDDEDEDDEDDEEEDDEVPVPSFGEAMAYFAMVKRYLTSSPIDDRVQSHILHLEHDLVHVTRKNHARQAGARGLGHQS | Function: Interacts with centromeric heterochromatin in chromosomes and binds to a specific 17 bp subset of alphoid satellite DNA, called the CENP-B box. May organize arrays of centromere satellite DNA into a higher-order structure which then directs centromere formation and kinetochore assembly in mammalian chromosome... |
Q66LG9 | MADVSRSSSLYTEEDPLQAYSGLSLFPRTLKSLSNPLPPSYQSEDLQQTHTLLQSMPFEIQSEHQEQAKAILEDVDVDVQLNPIPNKRERRPGLDRKRKSFSLHLTTSQPPPVAPSFDPSKYPRSEDFFAAYDKFELANREWQKQTGSSVIDIQENPPSRRPRRPGIPGRKRRPFKESFTDSYFTDVINLEASEKEIPIASEQSLESATAAHVTTVDREVDDSTVDTDKDLNNVLKDLLACSREELEGDGAIKLLEERLQIKSFNIEKFSIPEFQDVRKMNLKASGSNPPNRKSLSDIQNILKGTNRVAVRKNSHSPSPQ... | Function: Component of the CENPA-NAC (nucleosome-associated) complex, a complex that plays a central role in assembly of kinetochore proteins, mitotic progression and chromosome segregation.
Sequence Mass (Da): 78935
Sequence Length: 705
Domain: The MIF2 homology domain II targets centromeres and binds the alpha satell... |
Q03188 | MAASGLDHLKNGYRRRFCRPSRARDINTEQGQNVLEILQDCFEEKSLANDFSTNSTKSVPNSTRKIKDTCIQSPSKECQKSHPKSVPVSSKKKEASLQFVVEPSEATNRSVQAHEVHQKILATDVSSKNTPDSKKISSRNINDHHSEADEEFYLSVGSPSVLLDAKTSVSQNVIPSSAQKRETYTFENSVNMLPSSTEVSVKTKKRLNFDDKVMLKKIEIDNKVSDEEDKTSEGQERKPSGSSQNRIRDSEYEIQRQAKKSFSTLFLETVKRKSESSPIVRHAATAPPHSCPPDDTKLIEDEFIIDESDQSFASRSWITI... | Function: Component of the CENPA-NAC (nucleosome-associated) complex, a complex that plays a central role in assembly of kinetochore proteins, mitotic progression and chromosome segregation. The CENPA-NAC complex recruits the CENPA-CAD (nucleosome distal) complex and may be involved in incorporation of newly synthesize... |
P49452 | MASFHLDHLKNYHRRYCRSSRAPNIHTKKGQNMLEILQDCFEDQSKASFLDDFTESLTSSTQKKKANYSQSSSKKCPESHSKPVPVSSRTGEASLQASAEPSEAAGGSVQANEVHHGASDELDLCVGSPVVLLDANVNTLQKAASPAGQKRVASVSRSPVDRQASNKNISFKTRKRLNFEDKVTLSTAETENSVLQVEDNLSKGQEGTSSEITQKRDDLSSDVQSRSKKNFSELFLETVKRKSKSSSVVRHTAAVPFSPPPPSDMKLLEDEFIIDRSDRSFSSRLWVMIPSKDRHLSAHKPSPENTALLQGKKSREKSHS... | Function: Component of the CENPA-NAC (nucleosome-associated) complex, a complex that plays a central role in assembly of kinetochore proteins, mitotic progression and chromosome segregation. The CENPA-NAC complex recruits the CENPA-CAD (nucleosome distal) complex and may be involved in incorporation of newly synthesize... |
A8R7E6 | MKLKISLIAPILLLFSFFFAVESKCRTSCPLALASYYLENGTTLSVINQNLNSSIAPYDQINFDPILRYNSNIKDKDRIQMGSRVLVPFPCECQPGDFLGHNFSYSVRQEDTYERVAISNYANLTTMESLQARNPFPATNIPLSATLNVLVNCSCGDESVSKDFGLFVTYPLRPEDSLSSIARSSGVSADILQRYNPGVNFNSGNGIVYVPGRDPNGAFPPFKSSKQDGVGAGVIAGIVIGVIVALLLILFIVYYAYRKNKSKGDSFSSSIPLSTKADHASSTSLQSGGLGGAGVSPGIAAISVDKSVEFSLEELAKATD... | Function: Lysin motif (LysM) receptor kinase that functions as a cell surface receptor in chitin elicitor (chitooligosaccharides) signaling leading to innate immunity toward both biotic and abiotic stresses (e.g. tolerance to salinity, heavy-metal stresses, and Botrytis cinerea infection). Recognizes microbe-derived N-... |
Q8TCT0 | MGATGAAEPLQSVLWVKQQRCAVSLEPARALLRWWRSPGPGAGAPGADACSVPVSEIIAVEETDVHGKHQGSGKWQKMEKPYAFTVHCVKRARRHRWKWAQVTFWCPEEQLCHLWLQTLREMLEKLTSRPKHLLVFINPFGGKGQGKRIYERKVAPLFTLASITTDIIVTEHANQAKETLYEINIDKYDGIVCVGGDGMFSEVLHGLIGRTQRSAGVDQNHPRAVLVPSSLRIGIIPAGSTDCVCYSTVGTSDAETSALHIVVGDSLAMDVSSVHHNSTLLRYSVSLLGYGFYGDIIKDSEKKRWLGLARYDFSGLKTFL... | Function: Catalyzes specifically the phosphorylation of ceramide to form ceramide 1-phosphate . Acts efficiently on natural and analog ceramides (C6, C8, C16 ceramides, and C8-dihydroceramide), to a lesser extent on C2-ceramide and C6-dihydroceramide, but not on other lipids, such as various sphingosines . Shows a grea... |
A0A0P0XII1 | MEASTSLLVLVLAAAAFAAGTVTEAAGDGCSAGCDLALASFYVTPNQNVTNMADLFGIGAANYRSLAPYNPNIPNLDFINVGGRVNVYFTCGCRSLPGSPGATYLAGAFPFQMSRGQIYTSVAANYNNLTTAEWLQATNSYPANNIPDTAVINATVNCSCGDASISPDYGLFLTYPLRAEDTLASVAATYGLSSQLDVVRRYNPGMESATGSGIVYIPVKDPNGSYLPLKSPGKGASAGAIAGGVVAGVVVLAAIFLYIIFYRRRKAKQATLLQSSEDSTQLGTISMDKVTPSTIVGPSPVAGITVDKSVEFSYEELSNA... | Function: Lysin motif (LysM) receptor kinase required as a cell surface receptor for chitin elicitor (chitooligosaccharides) signaling leading to innate immunity in response to biotic stresses. Involved in the resistance to pathogenic fungi, probably by sensing microbe-associated molecular patterns (MAMP) and pathogen-... |
A9TXT1 | MKFQMKMKSELCRTYKYWLILLVLWLSGVTQRETGVLIVDADCIPPNGCKALAYYRLKQGDDLEKLQGRFQTNNSEVLAYNPQLVDANSIQAGTNIYLPFDCLCLNGELVHRFSYTVTTNDTAEKVVDVTYQKLTTVGAVRSASNSGDLSSIYSGQSLTIPVRCYCGDPNVDPKYGLFSTYVVQADDQLTSLSTNFSVDADVISKFNSDTRNLSPDSIIFIPSKAANGSFPPFSGYVLGTVHWRSNVGIIVGVVVGGIVLAVLLLFALIFGFKHFRRRKLAKEPTMQQSGLLSSSSMAGSKPSRSGSTMLPVPKSVEFTY... | Function: Lysin motif (LysM) receptor kinase required as a cell surface receptor for chitin elicitor (chitooligosaccharides) signaling leading to innate immunity in response to biotic stresses (By similarity). The CERK1, MEKK1a/b, MKK1a/b/c and MPK4a/b proteins are involved in pathogen defense. The pathway induces rapi... |
Q49MI3 | MPWRRRRNRVSALEGGREEEAPPEAAAVPPALLTSPQQTEAAAERILLRGIFEIGRDSCDVVLSERALRWRPIQPERPAGDSKYDLLCKEEFIELKDIFSVKLKRRCSVKQQRSGTLLGITLFICLKKEQNKLKNSTLDLINLSEDHCDIWFRQFKKILAGFPNRPKSLKILLNPQSHKKEATQVYYEKVEPLLKLAGIKTDVTIMEYEGHALSLLKECELQGFDGGHRKPLFAIHWSVQRLFTGMQTLEPSVVCVGGDGSASEVAHALLLRAQKNAGMETDRILTPVRAQLPLGLIPAGSTNVLAHSLHGVPHVITATL... | Function: Has no detectable ceramide-kinase activity. Overexpression of CERKL protects cells from apoptosis in oxidative stress conditions.
PTM: Phosphorylated on serine residues.
Sequence Mass (Da): 62622
Sequence Length: 558
Subcellular Location: Cytoplasm
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Q6USK2 | MEEGRDDEYCSFSNSGDRDGGLSGCFFLDHVGQVLLSRNHDGLSWKCLDSSDCEGTTCLGIIICENSETEIKFSDIYAVEFVSYGLVHSPKLGLRHAKECFRERLLNTQEMYRFTVHGFQSSPKEPCLWNLAAFTFGHMDLQTCQSWMDQLNYSLIKEVERPRNLLVFVHPKSGKGNGSKVWETVSKIFIRAKVNTKVIVTERAGHAFDVMASIQNKELHTYDGIIAVGGDGFFNEILNGYLLSRLKVPLPPSPSDSFNSVQSRGSSSVPEPGDEVHETDQKEHYPLLPDSVQEVMNFRTVNGSCEGIEDPDHPFSSERP... | Function: Catalyzes specifically the phosphorylation of ceramide to form ceramide 1-phosphate. Possesses high activity on ceramide analogs (C6, C8 synthetic ceramides) and lower activity on C6 and C8 dihydroceramides. Has weak activity on natural ceramides (a mixture of ceramides from bovine brain) and the synthetic su... |
Q9TZI1 | MPNSKKSKKGGDQQHVTIVPVEPVKGENVDTVAYSSRSRISGESGHLIADVQSPHAKKHRIIFDRDHNVFEFRLLDGSAKHIIVYRLDELLSTTCYPFKIKNGVPIIPTKPTTSDKTLYFNFVYKKDKQKWRLKQIPVIFYTTSERDYWHSLIDTTLRRVKNRPKNIIIFINPFGGNGKAQKIFKDNVDAFFWLTPGLRYKVVLTERANHARDYIVEMPPEQWSAIDGLVSVGGDGLFNELLSGALLRTQTDAGRNIDNPSSHLVTPHIRFGIIGAGSANSIVSTVHETNDHATSAVHIAIGSECNVDVCTVHQHQKLIR... | Function: Catalyzes the phosphorylation of ceramide to form ceramide 1-phosphate.
Catalytic Activity: an N-acylsphing-4-enine + ATP = ADP + an N-acylsphing-4-enine 1-phosphate + H(+)
Sequence Mass (Da): 62425
Sequence Length: 549
Pathway: Lipid metabolism; sphingolipid metabolism.
EC: 2.7.1.138
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C0LT23 | MEGGGEALFLDGVGEVTVAVGDDGLSFQPLHQEVSSSCWSSIIMQPKLESKLKFSDVYAVELLEVGPVCEPWNARATVQGKINTEMNRFVIHTVTRPRKRPSPWVPCEYIFGHKDQQTCKTWVEHIKTCINKEQDRPKSLMVFVHPLCGKGRGCKNWETVAPLFERAKVKTKVIVTQRAGHAYDTLASLSDKDLKKFDGVIAVGGDGLFNEILNGLLSTRHTNSYPPTPEGFGYFRNNMKCQEHRNNDLSNSELTGDDANAISGSSNTPDDHEPLLSTTRSTGLDISSSDSSDEPCNGDQVPLVSFPNNWFRLGIIPSGS... | Function: Catalyzes specifically the phosphorylation of ceramide to form ceramide 1-phosphate. Possesses activity on ceramide analog (C6 synthetic ceramide) in vitro. Ceramide is a critical sphingolipid metabolite that induces programmed cell death (PCD) in plants and ceramide-1-phosphate has a PCD suppressive effect. ... |
A0A0H3C8X7 | MATDARGVVAITGATGFLGRHLVRALAQDGWRPRVLVRRDPVHPFWRDLEVEVVTGDLGTPRALDRLAKGAEVFIHVAGLIKARTLEGFNRVNQDGARAAAEAARAAGARFILVSSLAAREPSLSNYAASKRAGEDAVRAADPSALIVRPPAIYGPGDTETLGLFQLAARSPVLPVLSQTSRVAMIHVEDAAAKLVAFCRTPVLGLVELSDVRRDGYTWTEIMRGAAHVMGAKPRLIRLPDPGILTAGALVDAWSSLTNTPSVFGLGKARELLHTDWTPSSAPMAEGVPSKFGLIDGFTHTVDWYRAAGWLPKNIVA | Function: Involved in de novo bacterial ceramide synthesis . Catalyzes the reduction of bacterial oxidized ceramides to bacterial dihydroceramides .
Catalytic Activity: H(+) + N-acyl-3-oxosphinganine + NADH = an N-acylsphinganine + NAD(+)
Sequence Mass (Da): 33857
Sequence Length: 317
Pathway: Lipid metabolism; sphingo... |
P27544 | MAAAGPAAGPTGPEPMPSYAQLVQRGWGSALAAARGCTDCGWGLARRGLAEHAHLAPPELLLLALGALGWTALRSAATARLFRPLAKRCCLQPRDAAKMPESAWKFLFYLGSWSYSAYLLFGTDYPFFHDPPSVFYDWTPGMAVPRDIAAAYLLQGSFYGHSIYATLYMDTWRKDSVVMLLHHVVTLILIVSSYAFRYHNVGILVLFLHDISDVQLEFTKLNIYFKSRGGSYHRLHALAADLGCLSFGFSWFWFRLYWFPLKVLYATSHCSLRTVPDIPFYFFFNALLLLLTLMNLYWFLYIVAFAAKVLTGQVHELKDL... | Function: Ceramide synthase that catalyzes the transfer of the acyl chain from acyl-CoA to a sphingoid base, with high selectivity toward stearoyl-CoA (octadecanoyl-CoA; C18:0-CoA) . N-acylates sphinganine and sphingosine bases to form dihydroceramides and ceramides in de novo synthesis and salvage pathways, respective... |
P27545 | MAAAAATPRLEAPEPMPSYAQMLQRSWASALAAAQGCGDCGWGLARRGLAEHAHLAAPELLLAVLCALGWTALRWAATTHIFRPLAKRCRLQPRDAARLPESAWKLLFYLACWSYCAYLLLGTSYPFFHDPPSVFYDWRSGMAVPWDIAVAYLLQGSFYCHSIYATVYMDSWRKDSVVMLVHHVVTLLLIASSYAFRYHNVGLLVFFLHDVSDVQLEFTKLNIYFKARGGAYHRLHGLVANLGCLSFCFCWFWFRLYWFPLKVLYATCHCSLQSVPDIPYYFFFNILLLLLMVMNIYWFLYIVAFAAKVLTGQMRELEDL... | Function: Ceramide synthase that catalyzes the transfer of the acyl chain from acyl-CoA to a sphingoid base, with high selectivity toward stearoyl-CoA (octadecanoyl-CoA; C18:0-CoA). N-acylates sphinganine and sphingosine bases to form dihydroceramides and ceramides in de novo synthesis and salvage pathways, respectivel... |
Q96G23 | MLQTLYDYFWWERLWLPVNLTWADLEDRDGRVYAKASDLYITLPLALLFLIVRYFFELYVATPLAALLNIKEKTRLRAPPNATLEHFYLTSGKQPKQVEVELLSRQSGLSGRQVERWFRRRRNQDRPSLLKKFREASWRFTFYLIAFIAGMAVIVDKPWFYDMKKVWEGYPIQSTIPSQYWYYMIELSFYWSLLFSIASDVKRKDFKEQIIHHVATIILISFSWFANYIRAGTLIMALHDSSDYLLESAKMFNYAGWKNTCNNIFIVFAIVFIITRLVILPFWILHCTLVYPLELYPAFFGYYFFNSMMGVLQLLHIFWA... | Function: Ceramide synthase that catalyzes the transfer of the acyl chain from acyl-CoA to a sphingoid base, with high selectivity toward very-long-chain fatty acyl-CoA (chain length C22-C27) . N-acylates sphinganine and sphingosine bases to form dihydroceramides and ceramides in de novo synthesis and salvage pathways,... |
Q924Z4 | MLQTLYDYFWWERLWLPVNLTWADLEDKDGRVYAKASDLYITLPLALLFLVIRYFFELYVATPLAALLNVKEKTRLRAPPNATLEHFYQTSGKQPKQVEVDLLSRQSGLSGRQVERWFRRRRNQDRPSLLKKFREASWRFTYYLIAFVAGMAVTVDKPWFYDLRKVWEGYPIQSIIPSQYWYYMIELSFYWSLLFSIASDVKRKDFKEQIIHHVATIILLCFSWFANYVRAGTLIMALHDASDYLLESAKMFNYAGWKNTCNNLFIVFAIVFIITRLVIMPFWILHCTMIYPLELYPAFFGYYFFNFMMAVLQMLHIFWA... | Function: Ceramide synthase that catalyzes the transfer of the acyl chain from acyl-CoA to a sphingoid base, with high selectivity toward very-long-chain fatty acyl-CoA (chain length C22-C27) . N-acylates sphinganine and sphingosine bases to form dihydroceramides and ceramides in de novo synthesis and salvage pathways,... |
Q8IU89 | MFWTFKEWFWLERFWLPPTIKWSDLEDHDGLVFVKPSHLYVTIPYAFLLLIIRRVFEKFVASPLAKSFGIKETVRKVTPNTVLENFFKHSTRQPLQTDIYGLAKKCNLTERQVERWFRSRRNQERPSRLKKFQEACWRFAFYLMITVAGIAFLYDKPWLYDLWEVWNGYPKQPLLPSQYWYYILEMSFYWSLLFRLGFDVKRKDFLAHIIHHLAAISLMSFSWCANYIRSGTLVMIVHDVADIWLESAKMFSYAGWTQTCNTLFFIFSTIFFISRLIVFPFWILYCTLILPMYHLEPFFSYIFLNLQLMILQVLHLYWGY... | Function: Ceramide synthase that catalyzes the transfer of the acyl chain from acyl-CoA to a sphingoid base, with high selectivity toward very- and ultra-long-chain fatty acyl-CoA (chain length greater than C22) . N-acylates sphinganine and sphingosine bases to form dihydroceramides and ceramides in de novo synthesis a... |
Q1A3B0 | MFQTFRKWFWSERYWLPPTIKWSDLEDHDGLVFVKASHLYITIPYAFLLMVVRYFFEKFVATPLANALGIKKTQHKIKPNAILENFFKHSTSKPSHTDIYGLAKKCNLTERQVERWLRIRQKQNKPCRLQKFQESCWRFTFYLLITMAGAVFLYDKPWAYDLWEVWNDYPRQPLLPSQYWYYILEMSFYWSLVFSLSTDIKRKDFLAHVIHHLAAISLMSFSWCANYIRSGTLVMFIHDISDIWLESAKMFSYAGWKQTCNTLFFIFTVVFFISRFIIFPFWILYCTLILPLHYLEPFFSYIFLNLQLMILQGLHVYWGY... | Function: Ceramide synthase that catalyzes the transfer of the acyl chain from acyl-CoA to a sphingoid base, with high selectivity toward very- and ultra-long-chain fatty acyl-CoA (chain length greater than C22) . N-acylates sphinganine and sphingosine bases to form dihydroceramides and ceramides in de novo synthesis a... |
Q5E9R6 | MWSSLNDWLWNERLWLPANISWAQLEDHDGLVFPHPQDTLMAVPLALALVVVRFTFERFVALPLSRWLGVRNQIRRPADPNATLEKHYLMKGREPTESQMNLLATQCGLTLRQTQCWFRRRRNQDRPCLTKKFCESSWKFVFYLCCFVCGTMVLYHESWLWTPVKCWENYPHQPLKPGLYHWYLLELSFYISLLMTLPFDTKRKDFKEQVIHHFVTIILISFSYSLNLLRIGSLVLLLHDSADYLLEASKLFNYMHWRRMCDTLFIIFSLVFFYTRLVLFPTRILYTTFFESIGNFSPFFGYYFLNILLVILQLLHVFWS... | Function: Ceramide synthase that catalyzes formation of ceramide from sphinganine and acyl-CoA substrates, with high selectivity toward long and very-long chains (C18:0-C22:0) as acyl donor.
PTM: Phosphorylated at the C-terminus by CK2.
Location Topology: Multi-pass membrane protein
Catalytic Activity: octadecanoyl-CoA... |
O15519 | MSAEVIHQVEEALDTDEKEMLLFLCRDVAIDVVPPNVRDLLDILRERGKLSVGDLAELLYRVRRFDLLKRILKMDRKAVETHLLRNPHLVSDYRVLMAEIGEDLDKSDVSSLIFLMKDYMGRGKISKEKSFLDLVVELEKLNLVAPDQLDLLEKCLKNIHRIDLKTKIQKYKQSVQGAGTSYRNVLQAAIQKSLKDPSNNFRLHNGRSKEQRLKEQLGAQQEPVKKSIQESEAFLPQSIPEERYKMKSKPLGICLIIDCIGNETELLRDTFTSLGYEVQKFLHLSMHGISQILGQFACMPEHRDYDSFVCVLVSRGGSQS... | Function: Apoptosis regulator protein which may function as a crucial link between cell survival and cell death pathways in mammalian cells. Acts as an inhibitor of TNFRSF6 mediated apoptosis. A proteolytic fragment (p43) is likely retained in the death-inducing signaling complex (DISC) thereby blocking further recruit... |
O35732 | MAQSPVSAEVIHQVEECLDEDEKEMMLFLCRDVTENLAAPNVRDLLDSLSERGQLSFATLAELLYRVRRFDLLKRILKTDKATVEDHLRRNPHLVSDYRVLLMEIGESLDQNDVSSLVFLTRDYTGRGKIAKDKSFLDLVIELEKLNLIASDQLNLLEKCLKNIHRIDLNTKIQKYTQSSQGARSNMNTLQASLPKLSIKYNSRLQNGRSKEPRFVEYRDSQRTLVKTSIQESGAFLPPHIREETYRMQSKPLGICLIIDCIGNDTKYLQETFTSLGYHIQLFLFPKSHDITQIVRRYASMAQHQDYDSFACVLVSLGGS... | Function: Apoptosis regulator protein which may function as a crucial link between cell survival and cell death pathways in mammalian cells. Acts as an inhibitor of TNFRSF6 mediated apoptosis. A proteolytic fragment (p43) is likely retained in the death-inducing signaling complex (DISC) thereby blocking further recruit... |
I1REI8 | MKYSVAFVALAAVAAQAQSLADVPKCAIPCLDKAIASETSCDKTDLACVCKGFSAVRSKATSCVIDECGTDVAINEVLPATENLCKNPPKESEAKSTAEEEKPTTTAAATSTLVVVTTSAEVVETTAAATTTVAPIIPTTAAEEPATSTPAAATPTKGPEQANGAAGLKGLGALAMAAFAALAL | Function: Suppresses host programmed cell death during infection by binding to Z.mays WAK17 isoform 2 and Z.mays LRR5, to prevent activation of Z.mays WAK17 isoform 1 and the downstream hypersensitive response.
Location Topology: Lipid-anchor
Sequence Mass (Da): 18289
Sequence Length: 184
Domain: The CFEM domain mediat... |
K1XVG1 | MKFSAPVLAIFLASASAQSTAELAAQIPSCAQTCLATAITGAGCTAGDYACQCGTSQNTITASATPCVISACTSEEALNTQRTTSQICALVAAGSASSPSASSSASASASSSASSTSGAASASASASSSASSASAAASALTLAHPIPNPSHPPSPTIQTNLRKKVRNSNRLTPASLSSVSSALVSSASSVRASASSAVSAATTAANPAATTAAGVKEEASFFIPAAVALFAVFAV | Function: Appears to function during host infection, and may play a role in suppressing the host immune response.
Location Topology: Lipid-anchor
Sequence Mass (Da): 22460
Sequence Length: 235
Domain: The CFEM domain is involved in heme-binding and contains 8 cysteines and is found in proteins from several pathogenic f... |
I1RET0 | MFSLTKSVLFTSIVAIAAQATTAVSSPTQTSLPGLASQVPNCVAVCLRNLHESIGCDVGDIVCLCKSKASLISKVGLCVVGSQCDFEDASSSTDIVRDMCDLVAEDPGTAVIASASKVLDAVVASATTSDIEAPTSTNAAGLVAYDVVKVVVVGAAAAIAI | Function: Suppresses host programmed cell death during infection by binding to Z.mays WAK17 isoform 2 and Z.mays LRR5, to prevent activation of Z.mays WAK17 isoform 1 and the downstream hypersensitive response.
Location Topology: Lipid-anchor
Sequence Mass (Da): 16109
Sequence Length: 161
Domain: The CFEM domain mediat... |
K1WG73 | MKYSMITLGAFAMMAVAQLSSLPACGQTCISNMLALAPTFGCTANDASCLCSDVNFAYGIRDCSNAACGAEAAGPVIAYGVEYCSSAGVGLSGSATGIDPGLGPATAVVASTPIATDGASAGSLSAITTSEFTSYVISGDSTVSTIVGSTTIYGPAAGSSSAITTSPIVSTVTSGDTSYPTTVGSTTIFGVAGVISTPTASASSALDSLSSSIASEASVITSSASAAVSSLSSRLSSAASPVSTTTSSAGGARQTAFAGLAAAAGFAAIIL | Function: Appears to function during host infection, and may play a role in suppressing the host immune response.
Location Topology: Lipid-anchor
Sequence Mass (Da): 25819
Sequence Length: 271
Domain: The CFEM domain is involved in heme-binding and contains 8 cysteines and is found in proteins from several pathogenic f... |
D6WI29 | MENILNDINKRFISLPEEDVRGNKQILESVLRTFVEQMKTQDPLFKALFRRVFYGGSFYDGLKVGKPEEFDLDILLHIPIYAQPVLNESNVPGFVWLKLNNLDGWLRQPEGRVYKDFRKKFLADNDFLDTGKTLRWMESLVQKTLNTLPWVNNATCELTNEFGTFHINWWKGGPAMTLGISHSSGEKIMDVDLVACFVFSGDKWPINGYRSNPFPSTKPEFFIVPKKPQGPVNPQGRYWSLSFQEQERVLIDNKNRLKPAVKLIKKLKEKTHPNIASYYIKTVFLHIIEQKDQSFWNKSLREVFMTTLREYNEFIADQSI... | Function: Nucleotidyltransferase that catalyzes the formation of cyclic GMP-AMP (2',3'-cGAMP) from ATP and GTP and plays a key role in innate immunity . Acts as a key sensor of double-stranded RNA (dsRNA), the presence of dsRNA in the cytoplasm being a danger signal that triggers the immune responses . Directly binds d... |
F4K5T2 | MEDRVLIKNDVTELIGNTPMVYLNKIVDGCVARIAAKLEMMEPCSSIKDRIAYSMIKDAEDKGLITPGKSTLIEATGGNTGIGLASIGASRGYKVILLMPSTMSLERRIILRALGAEVHLTDISIGIKGQLEKAKEILSKTPGGYIPHQFINPENPEIHYRTTGPEIWRDSAGKVDILVAGVGTGGTVTGTGKFLKEKNKDIKVCVVEPSESAVLSGGKPGPHLIQGIGSGEIPANLDLSIVDEIIQVTGEEAIETTKLLAIKEGLLVGISSGASAAAALKVAKRPENVGKLIVVIFPSGGERYLSTELFESVRYEAENL... | Function: Involved in maintaining Cys homeostasis through the desulfuration of L-cysteine. Modulates the generation of the signaling molecule sulfide in plant cytosol. Probably unable to interact with SAT and to form the decameric Cys synthase complex (CSC) and is therefore not an enzymatically true OASTL protein.
Cata... |
Q55DV9 | MTQPNNYKIGTNVIHAGQSADKNTGAVIVPISLSTTFLQPSPGVLHSEYDYSRSGNPTRKAFEECIAACENAKYALSFASGLATLTTITHLLKSGDEVISIDDVYGGTRRYFTRVAANFDLKFSFVDLSTLDDLKNAFTDKTRLVWIETPTNPLLKVADIKAVADYVHSRGATLVVDNTFMSPYFQNPLDLGADIVMHSVTKYINGHSDCVMGVLATNNDELYAKLKFLQNSIGAVPSPFDCFLALRGLKTLHVRMEAHQKNAFAICNFLEKHPKVERVIYPGLPSHPQHEICKRQMKGYGGMVVFFVKGSIDQSRSFLE... | Function: Catalyzes the last step in the trans-sulfuration pathway from L-methionine to L-cysteine in a pyridoxal-5'-phosphate (PLP)-dependent manner, which consists on cleaving the L,L-cystathionine molecule into L-cysteine, ammonia and 2-oxobutanoate. Part of the L-cysteine derived from the trans-sulfuration pathway ... |
P32929 | MQEKDASSQGFLPHFQHFATQAIHVGQDPEQWTSRAVVPPISLSTTFKQGAPGQHSGFEYSRSGNPTRNCLEKAVAALDGAKYCLAFASGLAATVTITHLLKAGDQIICMDDVYGGTNRYFRQVASEFGLKISFVDCSKIKLLEAAITPETKLVWIETPTNPTQKVIDIEGCAHIVHKHGDIILVVDNTFMSPYFQRPLALGADISMYSATKYMNGHSDVVMGLVSVNCESLHNRLRFLQNSLGAVPSPIDCYLCNRGLKTLHVRMEKHFKNGMAVAQFLESNPWVEKVIYPGLPSHPQHELVKRQCTGCTGMVTFYIKG... | Function: Catalyzes the last step in the trans-sulfuration pathway from L-methionine to L-cysteine in a pyridoxal-5'-phosphate (PLP)-dependent manner, which consists on cleaving the L,L-cystathionine molecule into L-cysteine, ammonia and 2-oxobutanoate . Part of the L-cysteine derived from the trans-sulfuration pathway... |
Q19QT7 | MQEKDVSSHGFLPRFQHFATQAIHAGQEPEQWASKAVVPPISLSTTFKQEAPGQHSGFEYSRSGNPTXNCLEKAVAVLDGAKYSLAFASGLAATVTITHLLKAGXQIISMDDVYGGTNRYFRQVAAEFGLKISFVDCSKSKLLEAAITPETKLVWIETPTNPILKMIDIEACAQIVHKHGDIILVVDNTFMSAYFQRPLALGADICMYSATKYMNGHSDVVMGLVSLNSETLHSRLRFLQNSLGAVPSPIDCYLCNRGLKTLQVRMEKHFENGMAVAQFLESHPLVEKVIYPGLPSHPQHELAKRQCTGCPGMISFYIKG... | Function: Catalyzes the last step in the trans-sulfuration pathway from L-methionine to L-cysteine in a pyridoxal-5'-phosphate (PLP)-dependent manner, which consists on cleaving the L,L-cystathionine molecule into L-cysteine, ammonia and 2-oxobutanoate. Part of the L-cysteine derived from the trans-sulfuration pathway ... |
P32397 | MSDGKKHVVIIGGGITGLAAAFYMEKEIKEKNLPLELTLVEASPRVGGKIQTVKKDGYIIERGPDSFLERKKSAPQLVKDLGLEHLLVNNATGQSYVLVNRTLHPMPKGAVMGIPTKIAPFVSTGLFSLSGKARAAMDFILPASKTKDDQSLGEFFRRRVGDEVVENLIEPLLSGIYAGDIDKLSLMSTFPQFYQTEQKHRSLILGMKKTRPQGSGQQLTAKKQGQFQTLSTGLQTLVEEIEKQLKLTKVYKGTKVTKLSHSGSCYSLELDNGVTLDADSVIVTAPHKAAAGMLSELPAISHLKNMHSTSVANVALGFPE... | Cofactor: Binds 1 FAD per subunit.
Function: Involved in coproporphyrin-dependent heme b biosynthesis . Catalyzes the oxidation of coproporphyrinogen III to coproporphyrin III . Can also oxidize protoporphyrinogen IX to protoporphyrin-IX . The specific activity for the oxidation of coproporphyrinogen III is much higher... |
P0A5A8 | MTPRSYCVVGGGISGLTSAYRLRQAVGDDATITLFEPADRLGGVLRTEHIGGQPMDLGAEAFVLRRPEMPALLAELGLSDRQLASTGARPLIYSQQRLHPLPPQTVVGIPSSAGSMAGLVDDATLARIDAEAARPFTWQVGSDPAVADLVADRFGDQVVARSVDPLLSGVYAGSAATIGLRAAAPSVAAALDRGATSVTDAVRQALPPGSGGPVFGALDGGYQVLLDGLVRRSRVHWVRARVVQLERGWVLRDETGGRWQADAVILAVPAPRLARLVDGIAPRTHAAARQIVSASSAVVALAVPGGTAFPHCSGVLVAGD... | Cofactor: Binds 1 FAD per subunit.
Function: Involved in coproporphyrin-dependent heme b biosynthesis. Catalyzes the oxidation of coproporphyrinogen III to coproporphyrin III.
Catalytic Activity: coproporphyrinogen III + 3 O2 = coproporphyrin III + 3 H2O2
Sequence Mass (Da): 46846
Sequence Length: 452
Pathway: Porphyri... |
Q50008 | MTSRSYCVVGGGISGLTAAYRLRVATGDDVAITLFDPGDRLGGVLRTECVGGQPMDLGAEAFLLRRPEVPALLAELGLSERQRATTDARPLIYSQQRLHSLPPDTVAGIPSSATSVAGLVDDATVARIGAEAVRPLSWEPGSDPAMAELVADRFGEQAVARLVDPLLGGVYAGSAATIGLRAGAPSVAAALDCGATSLMEAVRQGLPPVAAGPVFGALDGGYQVLIDELVRRSRLQWVAATVVGLDRGTCGWTLVDDTGACWSADGVILAVPAPRLVRLLQQIAPRTVAAASRIVSASSAVVALSVPRDTTFPQNSGVLV... | Cofactor: Binds 1 FAD per subunit.
Function: Involved in coproporphyrin-dependent heme b biosynthesis. Catalyzes the oxidation of coproporphyrinogen III to coproporphyrin III.
Catalytic Activity: coproporphyrinogen III + 3 O2 = coproporphyrin III + 3 H2O2
Sequence Mass (Da): 46580
Sequence Length: 451
Pathway: Porphyri... |
O32434 | MSTTDRVTTPTPTVSGTDAPGPDASHCHLVVVGGGITGLAAAWQGMARGARVSVVESDDHFGGKVVTDRRDGFLVEQGPDSFVAYRPAALKLIEELGLSDQVIAPGGGRRVSLLSRGKLRPMPAGMGMVLPTRMWPFVTTTVLSWPDKIRAGLDLVIPRRLPDHDVAIGAFLRQRLGDGIVRRFADPMVGGIYGAGIDELSLDAVLPSLRDNERDHRSLMVASLAGGRASRRAARQRAAQNNAQQNSSHQNSTGQNNSAGTRGPAASPFRTLRGGLGQLIDALVDQLRAGGVELLVNTSVDLLGRDGVHLSDGRVLPADA... | Cofactor: Binds 1 FAD per subunit.
Function: Involved in coproporphyrin-dependent heme b biosynthesis. Catalyzes the oxidation of coproporphyrinogen III to coproporphyrin III.
Catalytic Activity: coproporphyrinogen III + 3 O2 = coproporphyrin III + 3 H2O2
Sequence Mass (Da): 55268
Sequence Length: 527
Pathway: Porphyri... |
Q2FXA5 | MTKSVAIIGAGITGLSSAYFLKQQDPNIDVTIFEASNRPGGKIQSYRKDGYMIELGPESYLGRKTIMTELAKDIGLEQDIVTNTTGQSYIFAKNKLYPIPGGSIMGIPTDIKPFVTTKLISPLGKLRAGFDLLKKPTQMQDGDISVGAFFRARLGNEVLENLIEPLMGGIYGTDIDKLSLMSTFPNFKEKEEAFGSLIKGMKDEKNKRLKQRQLYPGAPKGQFKQFKHGLSSFIEALEQDVKNKGVTIRYNTSVDDIITSQKQYKIVYNDQLEEVYDGVLVTTPHQVFLNWFGQDPAFDYFKTMDSTTVATVVLAFDEKD... | Cofactor: Binds 1 FAD per subunit.
Function: Involved in coproporphyrin-dependent heme b biosynthesis . Catalyzes the oxidation of coproporphyrinogen III to coproporphyrin III . Can also oxidize protoporphyrinogen IX .
Catalytic Activity: coproporphyrinogen III + 3 O2 = coproporphyrin III + 3 H2O2
Sequence Mass (Da): 5... |
Q1MKX4 | MASKEIKFGRTAREKMLRGVDILADAVKVTLGPKGRNVIIDKSFGAPRITKDGVSVAKEIELEDKFENMGAQMVREVASKTNDIAGDGTTTATVLAQAIVREGNKAVAAGMNPMDLKRGIDLAVADVVKDLQAKAKKISTSEEVAQVGTISANGDKQVGLDIAEAMQKVGNEGVITVEEAKTAETELEVVEGMQFDRGYLSPYFVTNPEKMIADLEDVFILLHEKKLSNLQSMLPVLEAVVQTGKPLLIVAEDVEGEALATLVVNKLRGGLKIAAVKAPGFGDRRKAMLEDIAILTGGTVISEDLGIKLESVTLDMLGRA... | Function: Together with its co-chaperonin GroES, plays an essential role in assisting protein folding. The GroEL-GroES system forms a nano-cage that allows encapsulation of the non-native substrate proteins and provides a physical environment optimized to promote and accelerate protein folding.
Catalytic Activity: ATP ... |
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