ids stringlengths 6 10 | seqs stringlengths 11 1.02k | texts stringlengths 108 11.1k |
|---|---|---|
Q7XTB2 | MASIRRPHSPAKQQHLLRHGHLGPFASSSPPSSPLRHSSSSSSPRSAAHHHHHLLAAAGHTSFRRPLPRFAAFFLLGSFLGLLHFLSHLPRPLGPIPNPNSHHRHRDPFPILQHPHPPSTPHSNHKLLIVVTPTRARPSQAYYLTRMAHTLRLLHDSPLLWIVVQAGNPTPEAAAALRRTAVLHRYVGCCHNINASAPDFRPHQINAALDIVDNHRLDGVLYFADEEGVYSLHLFHHLRQIRRFATWPVPEISQHTNEVVLQGPVCKQGQVVGWHTTHDGNKLRRFHLAMSGFAFNSTMLWDPKLRSHLAWNSIRHPEMV... | Function: Involved in the synthesis of glucuronoxylan hemicellulose in secondary cell walls.
Location Topology: Single-pass type II membrane protein
Sequence Mass (Da): 42897
Sequence Length: 381
Subcellular Location: Golgi apparatus membrane
EC: 2.4.-.-
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B9FCV3 | MKLPLLRPLWPMLSPAAGSPDSPPEPSKPSLPAAWLLLHALFCATSMAVGFRFSRLIVYLLFLPTPINPTAHLVSLVSPPVMLAAANATTTITTTTTTTTTTVTTTTVAAEVGAHPQHHHHGPVFVGRHPIRVRPWPHPDPNELLKAHHILAAVQNAQRSSRRRGAGPPRPVIAVTPTTTSALQVPSLTSMAHTLRLVDGPLTWIVVEPEHHTDAVAAVLSRSNLNFLHITGPDSSTSRLRMHALREIRKRKMDGVVVFADENSILRTELFDEAQKVKSVGAVPVGVLGEDEGTSETFLQAPSCDAEGKLVGYHVSEETM... | Function: Involved in the synthesis of glucuronoxylan hemicellulose in secondary cell walls.
Location Topology: Single-pass type II membrane protein
Sequence Mass (Da): 48093
Sequence Length: 446
Subcellular Location: Golgi apparatus membrane
EC: 2.4.-.-
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Q5H861 | MDNGSNQLHVLFLPYFATGHIIPLVNAARLFVFHAGVKVTILTTHHNASLFRSTIDNDVEDGHSVISIHTLRFPSTEVGLPEGIENFSSASSPELAGKVFYAIYLLQKPMEDKIREIHPDCIFSDMYLPWTVNIALELKIPRLLFNQSSYMYNSILYNLRLYKPHKSKTITSTDSISVPGLPDKIEFKLSQLTDDLIKPEDEKNAFDELLDRTRESEDRSYGIVHDTFYELEPAYADYYQKVKKTKCWQIGPISHFSSKLFRRKELINAVDESNSCAIVEWLNEQEHKSVLYVSFGSVVRFPEAQLTEIAKALEASSIPF... | Function: Glucosyltransferase involved in steroid saponin biosynthesis . Catalyzes the 3-O-glucosylation of steroidal sapogenins, such as diosgenin, nuatigenin and tigogenin . Can glucosylate steroidal alkaloids, such as solanidine, solasodine and tomatidine .
Catalytic Activity: nuatigenin + UDP-alpha-D-glucose = H(+)... |
C7J0P3 | MMEKHGGKVTSDRRAGRRQHGQRCSASDAAPLVVVVILIVAALFLILGPTGSSSFTVPRIRVVFNEPVHVAVAAPPPPPPPAQMQAGANASSEEDSGLPPPRQLTDPPYSLGRTILGYDARRSAWLAAHPEFPARVAPAGRPRVLVVTGSAPARCPDPDGDHLLLRAFKNKVDYCRIHGLDVFYNTAFLDAEMSGFWAKLPLLRMLMVAHPEAELIWWVDSDAVFTDMLFEIPWERYAVHNLVLHGWEAKVFDEKSWIGVNTGSFLIRNCQWSLDLLDAWAPMGPRGPVRDRYGELFAEELSGRPPFEADDQSALIYLLV... | Function: Probable glycosyltransferase that may be involved in the biosynthesis of xyloglucan.
Location Topology: Single-pass type II membrane protein
Sequence Mass (Da): 50416
Sequence Length: 449
Subcellular Location: Golgi apparatus membrane
EC: 2.4.-.-
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Q9C975 | MGVKSVRFSIWFLFVVTDLVFCRTLSGDPDPCDATNQREFQKLRSDQITVLINGYSEYRIPLLQTIVASYSSSSIVSSILVLWGNPSTPDQLLDQLYQNLTQYSPGSASISLIQQSSSSLNARFLPRSSVDTRAVLICDDDVEIDQRSLEFAFSVWKSNPDRLVGTFVRSHGFDLQGKEWIYTVHPDKYSIVLTKFMMMKQDYLFEYSCKGGVEMEEMRMIVDQMRNCEDILMNFVAADRLRAGPIMVGAERVRDWGDARNEEVEERVRDVGLSSRRVEHRKRRGNCIREFHRVMGKMPLMYSYGKVVNSVGEQGLCRKA... | Function: Probable glycosyltransferase.
Sequence Mass (Da): 37703
Sequence Length: 329
Pathway: Protein modification; protein glycosylation.
EC: 2.4.1.-
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Q9SZG1 | MGKPGGAKTRTAVCLSDGVFFLAGAFMSLTLVWSYFSIFSPSFTSLRHDGKPVQCSGLDMQFDPSEPGFYDDPDLSYSIEKPITKWDEKRNQWFESHPSFKPGSENRIVMVTGSQSSPCKNPIGDHLLLRCFKNKVDYARIHGHDIFYSNSLLHPKMNSYWAKLPVVKAAMLAHPEAEWIWWVDSDAIFTDMEFKPPLHRYRQHNLVVHGWPNIIYEKQSWTALNAGVFLIRNCQWSMDLIDTWKSMGPVSPDYKKWGPIQRSIFKDKLFPESDDQTALIYLLYKHKELYYPKIYLEAEYYLQGYWIGVFGDFANVTERY... | Function: Probable glycosyltransferase that may be involved in the biosynthesis of xyloglucan.
Location Topology: Single-pass type II membrane protein
Sequence Mass (Da): 50295
Sequence Length: 432
Subcellular Location: Golgi apparatus membrane
EC: 2.4.-.-
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O95528 | MGHSPPVLPLCASVSLLGGLTFGYELAVISGALLPLQLDFGLSCLEQEFLVGSLLLGALLASLVGGFLIDCYGRKQAILGSNLVLLAGSLTLGLAGSLAWLVLGRAVVGFAISLSSMACCIYVSELVGPRQRGVLVSLYEAGITVGILLSYALNYALAGTPWGWRHMFGWATAPAVLQSLSLLFLPAGTDETATHKDLIPLQGGEAPKLGPGRPRYSFLDLFRARDNMRGRTTVGLGLVLFQQLTGQPNVLCYASTIFSSVGFHGGSSAVLASVGLGAVKVAATLTAMGLVDRAGRRALLLAGCALMALSVSGIGLVSFA... | Function: Facilitative glucose transporter required for the development of the cardiovascular system.
Catalytic Activity: D-glucose(out) = D-glucose(in)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 56911
Sequence Length: 541
Subcellular Location: Endomembrane system
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Q8VHD6 | MGLRPAVLLLCASVSLLGGLTFGYELAVISGALLPLQLNFGLSCLEQELLVGSLLLGALLASLVGGFLIDCYGRRRAILGSNAVLLAGSLILGLASSLPWLLLGRLSVGFAISLSSMACCIYVSELVGPRQRGVLVSLYEVGITVGILFSYGLNYVLAGSPWGWRHMFGWAAAPALLQSLSLFLLPAGAEGTAAPKDLIPLQGRETSKPGLVKPQYSFLDLFRAQDGMWSRTVVGLGLVLFQQLTGQPNVLYYASTIFRSVGFHGGSSAVLASVGLGTVKVAATLVATGLVDRAGRRVLLLFGCALMALSVSGIGLVSFA... | Function: Facilitative glucose transporter required for the development of the cardiovascular system.
Catalytic Activity: D-glucose(out) = D-glucose(in)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 56579
Sequence Length: 536
Subcellular Location: Endomembrane system
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Q9BYW1 | MRALRRLIQGRILLLTICAAGIGGTFQFGYNLSIINAPTLHIQEFTNETWQARTGEPLPDHLVLLMWSLIVSLYPLGGLFGALLAGPLAITLGRKKSLLVNNIFVVSAAILFGFSRKAGSFEMIMLGRLLVGVNAGVSMNIQPMYLGESAPKELRGAVAMSSAIFTALGIVMGQVVGLRELLGGPQAWPLLLASCLVPGALQLASLPLLPESPRYLLIDCGDTEACLAALRRLRGSGDLAGELEELEEERAACQGCRARRPWELFQHRALRRQVTSLVVLGSAMELCGNDSVYAYASSVFRKAGVPEAKIQYAIIGTGSC... | Function: Facilitative glucose transporter.
Catalytic Activity: D-glucose(out) = D-glucose(in)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 53703
Sequence Length: 496
Subcellular Location: Cell membrane
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Q6NWF1 | MDAPEESIRMTSDPQSKIYVQNPDTHIHLEQGPSAKSGNGRALVLCSVSVACLSGLLMGYEMSLISGALLQLRDVLTLSCPEQEQVVGSLLLGAFLLSLGGGTILDHYGRRFTIILTALLCVLGTLLSVCVVSFWALVVGRMLVGMSVALSGTASCLYAAEVAPAAWRGRCVCVYELMVVLGMLLGFGLSWAFAGVPDGWRFTFGGALLPALLQAGVMPLLPDSPRFLLAQQREKEAHATLLRLRAGIKEVEPVEDELRAIRLAMGAERLHGFLDLFQSRDNMLQRLLVGAALVFLQQATGQPNILAYASTVLSSVGFHG... | Function: Insulin-regulated facilitative glucose transporter.
Catalytic Activity: D-glucose(out) = D-glucose(in)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 65778
Sequence Length: 610
Subcellular Location: Cell membrane
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Q8TD20 | MVPVENTEGPSLLNQKGTAVETEGSGSRHPPWARGCGMFTFLSSVTAAVSGLLVGYELGIISGALLQIKTLLALSCHEQEMVVSSLVIGALLASLTGGVLIDRYGRRTAIILSSCLLGLGSLVLILSLSYTVLIVGRIAIGVSISLSSIATCVYIAEIAPQHRRGLLVSLNELMIVIGILSAYISNYAFANVFHGWKYMFGLVIPLGVLQAIAMYFLPPSPRFLVMKGQEGAASKVLGRLRALSDTTEELTVIKSSLKDEYQYSFWDLFRSKDNMRTRIMIGLTLVFFVQITGQPNILFYASTVLKSVGFQSNEAASLAS... | Function: Insulin-independent facilitative glucose transporter.
Catalytic Activity: D-glucose(out) = D-glucose(in)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 66966
Sequence Length: 617
Subcellular Location: Cell membrane
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Q8BFW9 | MVPVENTEGPNLLNQKGREAETEGSCGASGGGHPACAGGPSMFTFLTSVTAAISGLLVGYELGLISGALLQIRTLLALTCHEQEMVVSSLLIGAFLASLTGGVLIDRYGRRLAIILSSCLLGLGSLVLIMSLSYTLLIMGRVAIGVSISLSSIATCVYIAEIAPQHRRGLLVSLNELMIVTGILFAYISNYAFANISNGWKYMFGLVIPLGVLQAIAMYFLPPSPRFLVMKGQEESAGKVLRKLRVISDTTEELTLIKSSLKDEYQYSFWDLFRSKDNMRTRILIGLTLVFFVQTTGQPNILFYASTVLKSVGFQSNEAA... | Function: Insulin-independent facilitative glucose transporter.
Catalytic Activity: D-glucose(out) = D-glucose(in)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 67336
Sequence Length: 622
Subcellular Location: Cell membrane
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P11166 | MEPSSKKLTGRLMLAVGGAVLGSLQFGYNTGVINAPQKVIEEFYNQTWVHRYGESILPTTLTTLWSLSVAIFSVGGMIGSFSVGLFVNRFGRRNSMLMMNLLAFVSAVLMGFSKLGKSFEMLILGRFIIGVYCGLTTGFVPMYVGEVSPTALRGALGTLHQLGIVVGILIAQVFGLDSIMGNKDLWPLLLSIIFIPALLQCIVLPFCPESPRFLLINRNEENRAKSVLKKLRGTADVTHDLQEMKEESRQMMREKKVTILELFRSPAYRQPILIAVVLQLSQQLSGINAVFYYSTSIFEKAGVQQPVYATIGSGIVNTAF... | Function: Facilitative glucose transporter, which is responsible for constitutive or basal glucose uptake . Has a very broad substrate specificity; can transport a wide range of aldoses including both pentoses and hexoses . Most important energy carrier of the brain: present at the blood-brain barrier and assures the e... |
Q83BZ6 | MLKDIHQHRILILDFGSQYAQLIARRVREIGVYCELMPCDIDEETIRDFNPHGIILSGGPETVTLSHTLRAPAFIFEIGCPVLGICYGMQTMAYQLGGKVNRTAKAEFGHAQLRVLNPAFLFDGIEDQVSPQGEPLLDVWMSHGDIVSELPPGFEATACTDNSPLAAMADFKRRFFGLQFHPEVTHTPQGHRILAHFVIHICQCIPNWTTKHIIEDSIRDIQEKVGKEQVIVGLSGGVDSAVTATLVHKAIGDQLVCVLVDTGLLRLNEVDEVLNVFQKHLGAKVICVDAKDRFMKALKGISDPEEKRKIAGEQFIRVFE... | Function: Catalyzes the synthesis of GMP from XMP.
Catalytic Activity: ATP + H2O + L-glutamine + XMP = AMP + diphosphate + GMP + 2 H(+) + L-glutamate
Sequence Mass (Da): 58682
Sequence Length: 524
Pathway: Purine metabolism; GMP biosynthesis; GMP from XMP (L-Gln route): step 1/1.
EC: 6.3.5.2
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Q6A6X1 | MAPGGVVGHRLAFMEQLHDVVLVVDFGAQYAQLIARRVREANVYSEIVPHNMPVRDMLAKEPAAIILSGGPASVYVEGAPSVDPALFNAGVPVLGICYGFQAMAQALGGQVAHTGASEYGRTSLCITSAGQLLSRIPHTISVWMSHGDSVSRAPEGFSTLARTAGAPVAAFEDVERRLVGVQWHPEVHHTESGQTVLEHFLFDIAGCRPDWNASSIVGDQIAQIRGQVGDRRVICGLSGGVDSAVAAALVQRAVGDQLTCVFVDHGLLRQGEAEQVKNDFVAATGADLVVADESQRFLDALAGVTDPETKRKIIGREFIR... | Function: Catalyzes the synthesis of GMP from XMP.
Catalytic Activity: ATP + H2O + L-glutamine + XMP = AMP + diphosphate + GMP + 2 H(+) + L-glutamate
Sequence Mass (Da): 56987
Sequence Length: 530
Pathway: Purine metabolism; GMP biosynthesis; GMP from XMP (L-Gln route): step 1/1.
EC: 6.3.5.2
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Q3Z886 | MEIAKEKSGAKPEFIDNEDESLRESIVIFDFGSQYSLLIARRIREMHVYCELVSHDTPWEKIAHLNPRGFILSGGPSSVYEAGAPLAPAYIFESKLPVLGICYGMQAITHQLGGVVEHSEKREYGHALLHSSVANSDLLSDMPEPSPVWMSHGDRIEKMPAGFTALAYTENCPVAVMGNEADIYGLQFHPEVVHSPNGKIILKNFVFNICKCHANWTMGNYIQESIHNIREQVGDGQVICALSGGVDSAVVASLIHKAIGDQLTCIYVNNGLLRREEADRTLHVFKNHMGMKIIYVDAVDRFLDSLSGVTDPEQKRKVIG... | Function: Catalyzes the synthesis of GMP from XMP.
Catalytic Activity: ATP + H2O + L-glutamine + XMP = AMP + diphosphate + GMP + 2 H(+) + L-glutamate
Sequence Mass (Da): 59511
Sequence Length: 533
Pathway: Purine metabolism; GMP biosynthesis; GMP from XMP (L-Gln route): step 1/1.
EC: 6.3.5.2
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Q9RT91 | MSIVILDFGSQFTRLITRRFRELGAYSVILPGTASLERIQQENPQGIVLSGGPSSVYDEGAPRPAPGVLDLNVPILGVCYGMQYLAHEAGGDVKRAGKREYGKADLTEYGGRLFEGIQGEFVAWMSHSDSVTQLPQGYQVVARTEHTPVTAIENNDTRRYGVQFHPEVVHTPKGGQMLANFLDICGVTRDWNAEHIVDELIEGVRAQVGDTGRVLLGISGGVDSSTLALLLAKAVGERLTAVFIDHGLLRLGEREQVEAALTPLGVNLVTVDAKDEFLGQLAGVSDPEQKRKIIGREFIRAFERETAKLGDFEFLAQGTL... | Function: Catalyzes the synthesis of GMP from XMP.
Catalytic Activity: ATP + H2O + L-glutamine + XMP = AMP + diphosphate + GMP + 2 H(+) + L-glutamate
Sequence Mass (Da): 55513
Sequence Length: 506
Pathway: Purine metabolism; GMP biosynthesis; GMP from XMP (L-Gln route): step 1/1.
EC: 6.3.5.2
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A0QYE8 | MRFLDGHTPAYDLTYNDVFVVPGRSDVASRFDVDLSTVDGSGTTIPVVVANMTAVAGRRMAETVARRGGIVVLPQDLPITAVSETVDFVKSRDLVVDTPVTLSPEDSVSDANALLHKRAHGAAVVVFEGRPIGLVTEANCAGVDRFARVRDIALSDFVTAPVGTDPREVFDLLEHAPIDVAVMTAPDGTLAGVLTRTGAIRAGIYTPAVDAKGRLRIAAAVGINGDVGAKAQALAEAGADLLVIDTAHGHQAKMLDAIKAVASLDLGLPLVAGNVVSAEGTRDLIEAGASIVKVGVGPGAMCTTRMMTGVGRPQFSAVVE... | Cofactor: Activity is highest with Rb(+), followed by K(+), NH4(+) and Cs(+).
Function: Involved in the purine-salvage pathway . Catalyzes the NADPH-dependent conversion of GMP to IMP . Is not essential for viability, but may contribute to the regulation of the purine nucleotide pool by recycling GMP to IMP .
Catalytic... |
Q9Y2T3 | MCAAQMPPLAHIFRGTFVHSTWTCPMEVLRDHLLGVSDSGKIVFLEEASQQEKLAKEWCFKPCEIRELSHHEFFMPGLVDTHIHASQYSFAGSSIDLPLLEWLTKYTFPAEHRFQNIDFAEEVYTRVVRRTLKNGTTTACYFATIHTDSSLLLADITDKFGQRAFVGKVCMDLNDTFPEYKETTEESIKETERFVSEMLQKNYSRVKPIVTPRFSLSCSETLMGELGNIAKTRDLHIQSHISENRDEVEAVKNLYPSYKNYTSVYDKNNLLTNKTVMAHGCYLSAEELNVFHERGASIAHCPNSNLSLSSGFLNVLEVLK... | Cofactor: Binds 1 zinc ion per subunit.
Function: Catalyzes the hydrolytic deamination of guanine, producing xanthine and ammonia.
Catalytic Activity: guanine + H(+) + H2O = NH4(+) + xanthine
Sequence Mass (Da): 51003
Sequence Length: 454
Pathway: Purine metabolism; guanine degradation; xanthine from guanine: step 1/1.... |
Q9R111 | MCAARTPPLALVFRGTFVHSTWTCPMEVLRDHLLGVSDSGKIVFLEESSQQEKLAKEWCFKPCEIRELSHHEFFMPGLVDTHIHAPQYAFAGSNVDLPLLEWLNKYTFPTEQRFRSTDVAEEVYTRVVRRTLKNGTTTACYFGTIHTDSSLILAEITDKFGQRAFVGKVCMDLNDTVPEYKETTEESVKETERFVSEMLQKNYPRVKPIVTPRFTLSCTETLMSELGNIAKTHDLYIQSHISENREEIEAVKSLYPSYKNYTDVYDKNNLLTNKTVMAHGCYLSEEELNIFSERGASIAHCPNSNLSLSSGLLNVLEVLK... | Cofactor: Binds 1 zinc ion per subunit.
Function: Catalyzes the hydrolytic deamination of guanine, producing xanthine and ammonia.
Catalytic Activity: guanine + H(+) + H2O = NH4(+) + xanthine
Sequence Mass (Da): 51013
Sequence Length: 454
Pathway: Purine metabolism; guanine degradation; xanthine from guanine: step 1/1.... |
O14057 | MDGHTCDVFVGKLIHTPSLGELEITDATVGVYNGKIVFLEKSMTPKTLEEAKSHHLLKEATIHKLKPLQFMFPGLIDTHIHAPQYPNSGIGIDVPLLQWLEKYTFPLESSLADLEEARQVYKRVVERTLSNGTTFASYFSTLHTPTSALLAEICYSYGQRAYIGKCNMNNLSPDHYCEKSAESSLEATRQLISYMSILDPKREMVTPIITPRFAPSCTEDLLSGCGELAEKHNLPIQTHISENTSEIELVKELFPERKSYADVYDYYKLLTPQTILAHAIHLEDEEIELLTKRSSGISHCPTSNSILASGLANVRKLLDS... | Cofactor: Binds 1 zinc ion per subunit.
Function: Catalyzes the hydrolytic deamination of guanine, producing xanthine and ammonia.
Catalytic Activity: guanine + H(+) + H2O = NH4(+) + xanthine
Sequence Mass (Da): 58047
Sequence Length: 527
Pathway: Purine metabolism; guanine degradation; xanthine from guanine: step 1/1.... |
Q07729 | MTKSDLLFDKFNDKHGKFLVFFGTFVDTPKLGELRIREKTSVGVLNGIIRFVNRNSLDPVKDCLDHDSSLSPEDVTVVDIIGKDKTRNNSFYFPGFVDTHNHVSQYPNVGVFGNSTLLDWLEKYTFPIEAALANENIAREVYNKVISKTLSHGTTTVAYYNTIDLKSTKLLAQLSSLLGQRVLVGKVCMDTNGPEYYIEDTKTSFESTVKVVKYIRETICDPLVNPIVTPRFAPSCSRELMQQLSKLVKDENIHVQTHLSENKEEIQWVQDLFPECESYTDVYDKYGLLTEKTVLAHCIHLTDAEARVIKQRRCGISHCP... | Cofactor: Binds 1 zinc ion per subunit.
Function: Catalyzes the hydrolytic deamination of guanine, producing xanthine and ammonia.
Catalytic Activity: guanine + H(+) + H2O = NH4(+) + xanthine
Sequence Mass (Da): 55204
Sequence Length: 489
Pathway: Purine metabolism; guanine degradation; xanthine from guanine: step 1/1.... |
P12257 | PPSVESIGVCYGMSANNLPAASTVVSMFKFNGIKSMRLYAPNQAALQAVGGTGINVVVGAPNDVLSNLAASPAAAASWVKSNIQAYPKVSFRYVCVGNEVAGGATRNLVPAMKNVHGALVAAGLGHIKVTTSVSQAILGVFSPPSAGSFTGEAAAFMGPVVQFLARTNAPLMANIYPYLAWAYNPSAMDMGYALFNASGTVVRDGAYGYQNLFDTTVDAFYTAMGKHGGSSVKLVVSESGWPSGGGTAATPANARFYNQHLINHVGRGTPRHPGAIETYIFAMFNENQKDSGVEQNWGLFYPNMQHVYPINF | Function: Functions in plant cell wall hydrolysis during mobilization of the endosperm in germinating grain or during the growth of vegetative tissues.
Catalytic Activity: Hydrolysis of (1->4)-beta-D-glucosidic linkages in beta-D-glucans containing (1->3)- and (1->4)-bonds.
Sequence Mass (Da): 32774
Sequence Length: 31... |
P37073 | MVKSKYLVFISVFSLLFGVFVVGFSHQGVKAEEERPMGTAFYESFDAFDDERWSKAGVWTNGQMFNATWYPEQVTADGLMRLTIAKKTTSARNYKAGELRTNDFYHYGLFEVSMKPAKVEGTVSSFFTYTGEWDWDGDPWDEIDIEFLGKDTTRIQFNYFTNGVGGNEFYYDLGFDASESFNTYAFEWREDSITWYVNGEAVHTATENIPQTPQKIMMNLWPGVGVDGWTGVFDGDNTPVYSYYDWVRYTPLQNYQIHQ | Function: Hydrolyzes B-glucans containing mixed beta-1,3 and beta-1,4 linkages.
Catalytic Activity: Hydrolysis of (1->4)-beta-D-glucosidic linkages in beta-D-glucans containing (1->3)- and (1->4)-bonds.
Sequence Mass (Da): 29960
Sequence Length: 259
EC: 3.2.1.73
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O14412 | MKSIISIAALSVLGLISKTMAAPAPAPVPGTAWNGSHDVMDFNYHESNRFEMSNWPNGEMFNCRWTPNNDKFENGKLKLTIDRDGSGYTCGEYRTKNYYGYGMFQVNMKPIKNPGVVSSFFTYTGPSDGTKWDEIDIEFLGYDTTKVQFNYYTNGQGHHEHIHYLGFDASQGFHTYGFFWARNSITWYVDGTAVYTAYDNIPDTPGKIMMNAWNGIGVDDWLRPFNGRTNISAYYDWVSYDAPRN | Catalytic Activity: Hydrolysis of (1->4)-beta-D-glucosidic linkages in beta-D-glucans containing (1->3)- and (1->4)-bonds.
Sequence Mass (Da): 27929
Sequence Length: 245
Subcellular Location: Secreted
EC: 3.2.1.73
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C0HLV0 | QAVLSETGGGDTASCDEYLYQELAYVK | Function: Endoglucanase (EG) that cleaves the internal beta-1,4-glucosidic bonds in cellulose.
Catalytic Activity: Endohydrolysis of (1->4)-beta-D-glucosidic linkages in cellulose, lichenin and cereal beta-D-glucans.
Sequence Mass (Da): 2911
Sequence Length: 27
EC: 3.2.1.4
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P56680 | QKPGETKEVHPQLTTFRCTKRGGCKPATNFIVLDSLSHPIHRAEGLGPGGCGDWGNPPPKDVCPDVESCAKNCIMEGIPDYSQYGVTTNGTSLRLQHILPDGRVPSPRVYLLDKTKRRYEMLHLTGFEFTFDVDATKLPCGMNSALYLSEMHPTGAKSKYNPGGAYYGTGYCDAQCFVTPFINGLGNIEGKGSCCNEMDIWEANSRASHVAPHTCNKKGLYLCEGEECAFEGVCDKNGCGWNNYRVNVTDYYGRGEEFKVNTLKPFTVVTQFLANRRGKLEKIHRFYVQDGKVIESFYTNKEGVPYTNMIDDEFCEATGS... | Function: The biological conversion of cellulose to glucose generally requires three types of hydrolytic enzymes: (1) Endoglucanases which cut internal beta-1,4-glucosidic bonds; (2) Exocellobiohydrolases that cut the disaccharide cellobiose from the non-reducing end of the cellulose polymer chain; (3) Beta-1,4-glucosi... |
A0A024SNB7 | MAPSVTLPLTTAILAIARLVAAQQPGTSTPEVHPKLTTYKCTKSGGCVAQDTSVVLDWNYRWMHDANYNSCTVNGGVNTTLCPDEATCGKNCFIEGVDYAASGVTTSGSSLTMNQYMPSSSGGYSSVSPRLYLLDSDGEYVMLKLNGQELSFDVDLSALPCGENGSLYLSQMDENGGANQYNTAGANYGSGYCDAQCPVQTWRNGTLNTSHQGFCCNEMDILEGNSRANALTPHSCTATACDSAGCGFNPYGSGYKSYYGPGDTVDTSKTFTIITQFNTDNGSPSGNLVSITRKYQQNGVDIPSAQPGGDTISSCPSASA... | Function: Endoglucanase (EG) that cleaves the internal beta-1,4-glucosidic bonds in cellulose. The degradation of cellulose involves an interplay between different cellulolytic enzymes. Hydrolysis starts with EGs, which cut internal glycosidic linkages to reduce the polymerization degree of the substrate and creates ne... |
P85218 | SYPNKQPYGPSGFWM | Function: Has endoglucanase activity on carboxymethylcellulose (CMC).
Catalytic Activity: Endohydrolysis of (1->4)-beta-D-glucosidic linkages in cellulose, lichenin and cereal beta-D-glucans.
Sequence Mass (Da): 1759
Sequence Length: 15
Subcellular Location: Secreted
EC: 3.2.1.4
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P17877 | YDASLKPNLQIPQKNIPNNDAVNIK | Function: This enzyme hydrolyzes cellotetraose, cellopentaose, and cellohexaose to cellobiose and cellotriose but does not hydrolyze cellobiose or cellotriose.
Catalytic Activity: Endohydrolysis of (1->4)-beta-D-glucosidic linkages in cellulose, lichenin and cereal beta-D-glucans.
Sequence Mass (Da): 2808
Sequence Leng... |
P33682 | MSRKLRTLMAALCALPLAFAAAPPAHAADPTTMTNGFYADPDSSASRWAAANPGDGRAAAINASIANTPMARWFGSWSGAIGTAAGAYAGAADGRDKLPILVAYNIYNRDYCGGHSAGGAASPSAYADWIARFAGGIAARPAVVILEPDSLGDYGCMNPAQIDEREAMLTNALVQFNRQAPNTWVYMDAGNPRWADAATMARRLHEAGLRQAHGFSLNVSNYITTAENTAYGNAVNNELAARYGYTKPFVVDTSRNGNGSNGEWCNPSGRRIGTPTRTGGGAEMLLWIKTPGESDGNCGVGSGSTAGQFLPEVAYKMIYG... | Function: Implicated in the mechanism of induction exerted by cellobiose.
Catalytic Activity: Endohydrolysis of (1->4)-beta-D-glucosidic linkages in cellulose, lichenin and cereal beta-D-glucans.
Sequence Mass (Da): 33695
Sequence Length: 321
EC: 3.2.1.4
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Q05156 | MKRRTTAVLTLTALLGTALTALPVQQAGAEEVEQVRNGTFDTTTDPWWTSNVTAGLSDGRLCADVPGGTTNRWDSAIGQNDITLVKGETYRFSFHASGIPEGHVVRAVVGLAVSPYDTWQEASPVLTEADGSYSYTFTAPVDTTQGQVAFQVGGSTDAWRFCVDDVSLLGGVPPEVYEPDTGPRVRVNQVAYLPAGPKNATLVTDATARLPWQLRNAQGTTVARGLTVPRGVDASSGQNVHSIDFGSYRGRGTGYTLVADGETSHPFDIDAAAYRPLRLDSVKYYYTQRSGIAIRDDLRPGYGRAAGHLNVAPNQGDANV... | Function: This endoglucanase acts only on crystalline cellulose.
Catalytic Activity: Endohydrolysis of (1->4)-beta-D-glucosidic linkages in cellulose, lichenin and cereal beta-D-glucans.
Sequence Mass (Da): 80000
Sequence Length: 746
EC: 3.2.1.4
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P13933 | MENPRTTPTPTPLRRRRSERRARGGRVLTALTGVTLLAGLAIAPAATGASPSPAPPASPAPSADSGTADAGTTALPSMELYRAEAGVHAWLDANPGDHRAPLIAERIGSQPQAVWFAGAYNPGTITQQVAEVTSAAAAAGQLPVVVPYMIPFRDCGNHSGGGAPSFAAYAEWSGLFAAGLGSEPVVVVLEPDAIPLIDCLDNQQRAERLAALAGLAEAVTDANPEARVYYDVGHSAWHAPAAIAPTLVEAGILEHGAGIATNISNYRTTTDETAYASAVIAELGGGLGAVVDTSRNGNGPLGSEWCDPPGRLVGNNPTVN... | Function: CMCase I preferentially hydrolyzes carboxymethyl cellulose (CMC).
Catalytic Activity: Endohydrolysis of (1->4)-beta-D-glucosidic linkages in cellulose, lichenin and cereal beta-D-glucans.
Sequence Mass (Da): 36515
Sequence Length: 359
EC: 3.2.1.4
|
P54424 | MAFKLNIGLLALSLSLSLVHLDGVRAGMATRYWDCCLASASWEGKAPVYAPVDACKADGVTLIDSKKDPSGQSGCNGGNKFMCSCMQPFDDETDPTLAFGFGAFTTGQESDTDCACFYAEFEHDAQGKAMKRNKLIFQVTNVGGDVQSQNFDFQIPGGGLGAFPKGCPAQWGVEASLWGDQYGGVKSATECSKLPKPLQEGCKWRFSEWGDNPVLKGSPKRVKCPKSLIDRSGCQRKDDNTISPYSGKVDSANTAAPAQYKRDRSVCLAGGKKGKSAAGGVDGSGDASGGADASGAGGAAEGSQGQPEGYGQPSGGNDQG... | PTM: May also be O-glycosylated.
Catalytic Activity: Endohydrolysis of (1->4)-beta-D-glucosidic linkages in cellulose, lichenin and cereal beta-D-glucans.
Sequence Mass (Da): 39594
Sequence Length: 393
Subcellular Location: Secreted
EC: 3.2.1.4
|
P37651 | MNVLRSGIVTMLLLAAFSVQAACTWPAWEQFKKDYISQEGRVIDPSDARKITTSEGQSYGMFSALAANDRAAFDNILDWTQNNLAQGSLKERLPAWLWGKKENSKWEVLDSNSASDGDVWMAWSLLEAGRLWKEQRYTDIGSALLKRIAREEVVTVPGLGSMLLPGKVGFAEDNSWRFNPSYLPPTLAQYFTRFGAPWTTLRETNQRLLLETAPKGFSPDWVRYEKDKGWQLKAEKTLISSYDAIRVYMWVGMMPDSDPQKARMLNRFKPMATFTEKNGYPPEKVDVATGKAQGKGPVGFSAAMLPFLQNRDAQAVQRQR... | Function: Hydrolyzes carboxymethylcellulose.
Catalytic Activity: Endohydrolysis of (1->4)-beta-D-glucosidic linkages in cellulose, lichenin and cereal beta-D-glucans.
Sequence Mass (Da): 41700
Sequence Length: 368
Pathway: Glycan metabolism; bacterial cellulose biosynthesis.
Subcellular Location: Secreted
EC: 3.2.1.4
|
A0A023VXA2 | MPRMLAASAAIIATTLAPLSAQAAGCEMTLHGINLSGAEFGQPGDPYGQGYIYPSESTIKAFADDGFNAVRLPFLWERLQPTLNGTLDATELSRIKDTVETLRDNGMVVILDVHNYARYHGEMIGTPNVPVAAFADFWKRLSAVFANDDDVIFGLMNEPHDISAPAWLAAANAAIDAIRTIGAGNLVLVPGTAWTGAHSWSQTFYGPSNASVMAQVVDSSNNFAYEVHQYTDDDFSGKNADCSKIDDAVSALNDFTSWLNANDVQGFLGEFGTTEQIQCLRGLKQMVDVVQQNPRAWLGWAYWAGGDWWPKDSPMIIHSN... | Function: Shows highest activity on carboxymethyl cellulose (CMC). Shows weak activity on xylan, and no activity against avicel, laminarin and chitin.
Catalytic Activity: Endohydrolysis of (1->4)-beta-D-glucosidic linkages in cellulose, lichenin and cereal beta-D-glucans.
Sequence Mass (Da): 37840
Sequence Length: 349
... |
P82186 | NQKCSGNPRRYNGKSCASTTNYHDSHKGACGCGPASGDAQFGWNAGSFVAAASQMYFDSGNKGWCGQHCGQCIKLTTTGGYVPGQGGPVREGLSKTFMITNLCPNIYPNQDWCNQGSQYGGHNKYGYELHLDLENGRSQVTGMGWNNPETTWEVVNCDSEHNHDHRTPSNSMYGQCQCAHQ | Function: Active towards the soluble carboxymethylcellulose (CMC). Possesses expansin activity too.
Catalytic Activity: Endohydrolysis of (1->4)-beta-D-glucosidic linkages in cellulose, lichenin and cereal beta-D-glucans.
Sequence Mass (Da): 19711
Sequence Length: 181
EC: 3.2.1.4
|
O97401 | MQVIVLPLVFLATFATSGSLAAPDASPEIVPVDGGLSGYGTTTRYWDCCKPSCAWKENINTPTMTPVQTCAIDGNTVVNASVQSGCIGGSSYMCSNQQAFVVNSTLAFGFAAGSFTGGVDNNLCCSCMLLTFQGQLAGKQFLVQITNTGGDLGSTSSIWPFPGGGVGIFTQGCHDQWTPRGAAGGDQYGGVYSVEQCSDLPEVLQPGCRFRFEFLENVSNPQVSFQQVQCPAEIVAISNCAL | Catalytic Activity: Endohydrolysis of (1->4)-beta-D-glucosidic linkages in cellulose, lichenin and cereal beta-D-glucans.
Sequence Mass (Da): 25336
Sequence Length: 242
Subcellular Location: Secreted
EC: 3.2.1.4
|
Q8RSY9 | MSPLKCMALAALGAVMFVGSAQAQTCDWPLWQNYAKRFVQDDGRVLNSSMKPTESSSEGQSYAMFFALVGNDRASFDKLWTWTKANMSGADIGQNLPGWLWGKKADNTWGVIDPNSASDADLWMAYALLEAARVWNAPQYRADAQLLLANVERNLIVRVPGLGKMLLPGPVGYVHAGGLWRFNPSYQVLAQLRRFHKERPNAGWNEVADSNAKMLADTASNPHGLAANWVGYRATSANTGLFVVDPFSDDLGSYDAIRTYMWAGMTAKGDPLAAPMLKSLGGMTRATAASATGYPPEKIHVLTGEVEKNNGYTPMGFSAS... | Function: Hydrolyzes carboxymethylcellulose.
Catalytic Activity: Endohydrolysis of (1->4)-beta-D-glucosidic linkages in cellulose, lichenin and cereal beta-D-glucans.
Sequence Mass (Da): 43345
Sequence Length: 398
Pathway: Glycan metabolism; bacterial cellulose biosynthesis.
Subcellular Location: Secreted
EC: 3.2.1.4
|
P17974 | MRRCMPLVAASVAALMLAGCGGGDGDPSLSTASVSATDTTTLKPAATSTTSSVWLTLAKDSAAFTVSGTRTVRYGAGSAWVEKSVSGSGRCTSTFFGKDPAAGVAKVCQLLQGTGTLLWRGVSLAGAEFGEGSLPGTYGSNYIYPSADSVTYYKNKGMNLVRLPFRWERLQPTLNQVFDANELSRLTGFVNAVTATGQTVLLDPHNYARYYGNVIGSSAVPNSAYADFWRRLATQFKSNPRVILGLMNEPNSMPTEQWLSGANAELAAIRSANASNVVFVPGNAWTGAHSWNQNWYGTPNGTVMKGINDPGHNLVFEVHQ... | Catalytic Activity: Endohydrolysis of (1->4)-beta-D-glucosidic linkages in cellulose, lichenin and cereal beta-D-glucans.
Location Topology: Lipid-anchor
Sequence Mass (Da): 45578
Sequence Length: 426
Subcellular Location: Cell membrane
EC: 3.2.1.4
|
P23044 | MKLVFSALASLLSGASATIYYAGVAESSGEFGVWSATQTPGTGLPGRFGVDYAFISEAAVDVHVDQNHLNLFRVAFLLERMCPPATGLGAAFNETHFDYFKEAVDYITVTKGAYAILDPHNYMRYNDPSYQPFSGSVIGNTSDSTAATTEQFGEFWGELASRFNDNERVIFGLMNEPHDMATSLVLANNQAAIDAIRAANASNLIIMPGNSWTGGHSWTEGSDPSSALLNQFKDPLNNTAIDIHEYLDYDFSGGHLECVSDPETNLAALTAWLKENNLKAFITEFGGSNSTSCQEMLPDLINYMADNAEYIGWTAWAAGP... | Function: Active towards carboxymethyl cellulose.
Catalytic Activity: Endohydrolysis of (1->4)-beta-D-glucosidic linkages in cellulose, lichenin and cereal beta-D-glucans.
Sequence Mass (Da): 41428
Sequence Length: 385
Pathway: Glycan metabolism; cellulose degradation.
EC: 3.2.1.4
|
P81190 | SLQAATEWLKANNQRGFLGEMGAGSNAD | Catalytic Activity: Endohydrolysis of (1->4)-beta-D-glucosidic linkages in cellulose, lichenin and cereal beta-D-glucans.
Location Topology: Lipid-anchor
Sequence Mass (Da): 2937
Sequence Length: 28
Subcellular Location: Cell membrane
EC: 3.2.1.4
|
P58935 | MTRRRLLHAGTLAGVAALLPAAALAAPSQCGPWPLWSAFVDKHIQRDGRVVDFLNPDQRSTSEGQSYALFFALVNNDQVLFDKVLSWTRHNLCGGRPDLNLPAWLWGRDGSGAWRVLDANTASDGELWIAYALLEAGRLWSRPGFLKAGQQMLQLIRTQEVATLPGLGPMLLPGRTGFVDNGRWTLNPSYLPIQVLRRCANADPKGPWAAIAANSARVLRDSAPVGFAPDWTVWDGKTFNADPKRGNVGSYDAIRVYLWAGMLDAGEPLRARLLQDLSGPADLLAAQQTPAEKIDTARGVGTGALPVGFSAALLPYLSAL... | Function: Hydrolyzes carboxymethylcellulose.
Catalytic Activity: Endohydrolysis of (1->4)-beta-D-glucosidic linkages in cellulose, lichenin and cereal beta-D-glucans.
Sequence Mass (Da): 41510
Sequence Length: 384
Pathway: Glycan metabolism; bacterial cellulose biosynthesis.
Subcellular Location: Secreted
EC: 3.2.1.4
|
Q5AKZ2 | MNYLSQLGKLFSLETLDTRLNPTTNPIKRQSIIKKANPTSRWSTLEFKIYLTILIIVVPLMIKAAMESSNETNPNYPRFQHLLSDGWILGRKVDNSDQQYRFFRNNFPLLCGLIFIHVTLRKLINTFIIIPNGRYNNNFKRTYFDLIFGIIFLIGAHGINVFKISFHLFINYLIGKYIKNYKLAIWCTWIYGIFSLFFNEWFGDSSFGLSIFVNGSGYYTGIIPRWDVFYNFTLLRMLSFNLDYIERERKLGNNDGQLNLNKQENINGADNPPTLLNLDDRQRLSAPLPLDDYNVSNYIAYISYTPLFIAGPIITFNDYV... | Function: Membrane-bound O-acyltransferase involved in the remodeling of glycosylphosphatidylinositol (GPI) anchors. Acts only on GPI-anchored proteins, but not on free GPI lipids. Also involved in lipid metabolism, having profound effects on sphingolipid-sterol-ordered domains integrity and assembly. Involved in cell ... |
Q7Z888 | MFKAAMDASNETNPNYPKFAHLLSQGWMFGRKVDNSDQQYRFFRDNFPLLCGLVLLHTSLRRGVNLIAGNHKRTGFDFVFGXDIHLCSTRDEFLPYFDSLGYXIFPFLKYIKRNDVATXTYVDXTAILSLFLNDNYXSCTIWNRFYRSWISEVSFQDGMCFSISHCXRMLSYNLDYIEKRKSASEESNLELKNSSSSLSELDDRERLVAPIPLTDYNFVNYMAYITYAPLFIAGPIITFNDYIYQSDYKAMSSVKDYKRTFIYFLRFAFCILVMEFLLHFMYVVAVSKTKAWEGDTPFQLSMLGLFNLNIIWLKLLIPWR... | Function: Membrane-bound O-acyltransferase involved in the remodeling of glycosylphosphatidylinositol (GPI) anchors. Acts only on GPI-anchored proteins, but not on free GPI lipids. Also involved in lipid metabolism, having profound effects on sphingolipid-sterol-ordered domains integrity and assembly. Involved in cell ... |
Q09758 | MLRLFRFDVLETSTKDTERPNSKSSRLSSTSGSSHPSSSSRLTVRSAVPEKSAFGSIEFIFYFSVILSILTIACFKIHYVSSPKHPNYKNIEKYLKPGWLFGQKVDSADFQYSAFRENMPILLLVIIVYNFLWRLVKLVFTKNTNDELAIKNNYRLCFSLLFALLVYGTGVIYVLTIALINYLISKSLKNSIFNPLLTWTLDISVVFFKEYFAYCKFSSLHPGLGFLDQYTGILERWYVLFNITMLRLVSFNMDYYWSLKHNSEKLNTLIFDKDREPTTLTFRERVDYSCLDEDYNLKNFLTYIFYAPLYLAGPIISFNN... | Function: Membrane-bound O-acyltransferase involved in the remodeling of glycosylphosphatidylinositol (GPI) anchors. Acts only on GPI-anchored proteins, but not on free GPI lipids. Also involved in lipid metabolism, having profound effects on sphingolipid-sterol-ordered domains integrity and assembly. Involved in cell ... |
P53154 | MSLISILSPLITSEGLDSRIKPSPKKDASTTTKPSLWKTTEFKFYYIAFLVVVPLMFYAGLQASSPENPNYARYERLLSQGWLFGRKVDNSDSQYRFFRDNFALLSVLMLVHTSIKRIVLYSTNITKLRFDLIFGLIFLVAAHGVNSIRILAHMLILYAIAHVLKNFRRIATISIWIYGISTLFINDNFRAYPFGNICSFLSPLDHWYRGIIPRWDVFFNFTLLRVLSYNLDFLERWENLQKKKSPSYESKEAKSAILLNERARLTAAHPIQDYSLMNYIAYVTYTPLFIAGPIITFNDYVYQSKHTLPSINFKFIFYYA... | Function: Membrane-bound O-acyltransferase involved in the remodeling of glycosylphosphatidylinositol (GPI) anchors. Acts only on GPI-anchored proteins, but not on free GPI lipids. Acts as an acyltransferase for GPI anchors that adds C26 fatty acids to the sn2 position of lyso-PI-containing GPI anchors. PER1 first deac... |
E2RJI4 | MEATAGSETESGGDTVTAECANRIPVPRPPSIEEFTIVKPISRGAFGKVYLGQKGGKLYAVKVVKKADMINKNMTHQVQAERDALALSKSPFIVHLYYSLQSANNVYLVMEYLIGGDVKSLLHIYGYFDEEMAVKYISEVALALDYLHRHGIIHRDLKPDNMLISNEGHIKLTDFGLSKITLNRDIDINMMDILTTPSMAKPRQDYSRTPGQVLSLISSLRFYTPAAEKDKDSANILSTHVFETSQLSQGLICPMSVDHRDTTPYSSKLLHSCLETVTSDPGMPVKCLTSNLLQSRRRLATSSASSQSHTFLSSVESECH... | Function: Serine/threonine kinase that plays a key role in M phase by acting as a regulator of mitosis entry and maintenance. Acts by promoting the inactivation of protein phosphatase 2A (PP2A) during M phase: does not directly inhibit PP2A but acts by mediating phosphorylation and subsequent activation of ARPP19 and E... |
Q96GX5 | MDPTAGSKKEPGGGAATEEGVNRIAVPKPPSIEEFSIVKPISRGAFGKVYLGQKGGKLYAVKVVKKADMINKNMTHQVQAERDALALSKSPFIVHLYYSLQSANNVYLVMEYLIGGDVKSLLHIYGYFDEEMAVKYISEVALALDYLHRHGIIHRDLKPDNMLISNEGHIKLTDFGLSKVTLNRDINMMDILTTPSMAKPRQDYSRTPGQVLSLISSLGFNTPIAEKNQDPANILSACLSETSQLSQGLVCPMSVDQKDTTPYSSKLLKSCLETVASNPGMPVKCLTSNLLQSRKRLATSSASSQSHTFISSVESECHSS... | Function: Serine/threonine kinase that plays a key role in M phase by acting as a regulator of mitosis entry and maintenance. Acts by promoting the inactivation of protein phosphatase 2A (PP2A) during M phase: does not directly inhibit PP2A but acts by mediating phosphorylation and subsequent activation of ARPP19 and E... |
Q6NTJ3 | MGIVAETSQNGDTSLCSEKKFTVPQPPSIEEFGIVKPISRGAFGKVYLARRKNNSKLFAVKVVKKADMINKNMVQQVQAERDALALSKSPFIVHLYYSLQSANNIYLVMEYLIGGDVKSLLHIYGYFDEEMAVKYISEVAMALDYLHRHGIIHRDLKPDNMLISNKGHIKLTDFGLSKVTLKRELCMMDILTTPSMAKPKRDYSRTPGQVLSLISSLGFNTPAGGRTQGSLNQQTEGMRGNASTPLLMKKRESLVKGNKLMISCPEASLSSPSIPVKCLTPNLLKCRTQFATSSTSSQSRICLSSLESECGSPRWENCSQ... | Function: Serine/threonine kinase that plays a key role in M phase by acting as a regulator of mitosis entry and maintenance. Acts by promoting the inactivation of protein phosphatase 2A (PP2A) during M phase: does not directly inhibit PP2A but acts by mediating phosphorylation and subsequent activation of arpp19 and e... |
Q873N1 | MDPDYKARKEAFVSGLAGGSILEINAVTLVASVSVFLWSILQSRLSFFTPYSAAALLVDFLLNVLAILFATTLYSSAPLLLNLLLISPALLILLSTKRPRTPVKAKPPRQSARAGKDDSKHATALPESLPIHPFLTTYRAAMMVITCIAILAVDFRIFPRRFAKVENWGTSLMDLGVGSFVFSGGVVSARSLLKSRINGSKRLPLAKRLIASTRHSIPLLVLGLIRLYSVKGLDYAEHVTEYGVHWNFFFTLGLLPPFVEVFDALATIIPSYEVLSVGIAVLYQVALESTDLKSYILVSPRGPSLLSKNREGVFSFSGYL... | Function: Probable acetyltransferase, which acetylates the inositol ring of phosphatidylinositol during biosynthesis of GPI-anchor.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 54677
Sequence Length: 501
Pathway: Glycolipid biosynthesis; glycosylphosphatidylinositol-anchor biosynthesis.
Subcellula... |
Q873N2 | MSSSLKQLKEQFVSDLTGGTIEEIYAVTSIALSSYLSFRLLKKSLGDLALIYDYILNVLTILASITVYSNSPSYLHYFIVIPSLVIYLVNYHVEKPSSPHRQNDTKEDKSDELLPRKQFITAYRSQMLIITNLAILAVDFPIFPRRFAKVETWGTSMMDLGVGSFVFSMGLANSRQLIKNHTDNYKFSWKSYLKTIKQNFIKSVPILVLGAIRFVSVKQLDYQEHETEYGIHWNFFFTLGFLPIVLGILDPVLNLVPRFIIGIGISIAYEVALNKTGLLKFILSSENRLESLITMNKEGIFSFIGYLCIFIIGQSFGSFV... | Function: Probable acetyltransferase, which acetylates the inositol ring of phosphatidylinositol during biosynthesis of GPI-anchor.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 55200
Sequence Length: 485
Pathway: Glycolipid biosynthesis; glycosylphosphatidylinositol-anchor biosynthesis.
Subcellula... |
P0CP65 | MGDYKLAKEAFVSGNPGASIWSINAVSLVALATYALWIALSPYIRHGLLNNYLICVLPLLLGVTIFSTSPLVFASFLSIISLFFIAKSQKRFNFPRSPEKPKGQWLDESDSDEEPAEPASAAGSAAVSPAKLLPSQVAFASGSLLSTDPTISPMSPSSSSSSGHEDPLGIMGVNRRRSPLEGVSLDVPSHIDSKVRISPVPSLRLKKSRATKVQGVEEKGRLPFLTVYRAHMMLMTVICILAVDFEVFPRWQGKCEDFGTSLMDVGVGSFVFSLGLVSTKSLSPPPPPPTPTSPALNSHIIPLTPSPLSFILISLRKSVP... | Function: Probable acetyltransferase, which acetylates the inositol ring of phosphatidylinositol during biosynthesis of GPI-anchor.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 65412
Sequence Length: 598
Pathway: Glycolipid biosynthesis; glycosylphosphatidylinositol-anchor biosynthesis.
Subcellula... |
P13364 | MSENQTYDSSSIKVLKGLDAVRKRPGMYIGDTDDGSGLHHMVFEVVDNSIDEALAGHCDDITVIIHTDESISVRDNGRGIPVDVHKEEGVSAAEVIMTVLHAGGKFDDNSYKVSGGLHGVGVSVVNALSEKLVLTVRRSGKIWEQTYVHGVPQAPMAVVGESETTGTHIHFKPSAETFKNIHFSWDILAKRIRELSFLNSGVGILLKDERSGKEEFFKYEGGLRAFVEYLNTNKTPVNSQVFHFSVQREDGVGVEVALQWNDSFNENLLCFTNNIPQRDGGTHLVGFRSSLTRSLNSYIEQEGLAKKNKVATTGDDAREG... | Cofactor: Binds two Mg(2+) per subunit. The magnesium ions form salt bridges with both the protein and the DNA. Can also accept other divalent metal cations, such as Mn(2+) or Ca(2+).
Function: A type II topoisomerase that negatively supercoils closed circular double-stranded (ds) DNA in an ATP-dependent manner to modu... |
P31860 | EFVKYLDRSKTAVMPDPIYMVGEVRGIGVEVAMWWNDSYHETVLPFTNNIPQRDGGTHLAGFRGALTRTITKYAQDSGIAKREKIDFTGDDAREGLTCVLSVKVPDPKFSSQTKDKLVSSEVRPAVENLVNEKL | Function: A type II topoisomerase that negatively supercoils closed circular double-stranded (ds) DNA in an ATP-dependent manner to modulate DNA topology and maintain chromosomes in an underwound state. Negative supercoiling favors strand separation, and DNA replication, transcription, recombination and repair, all of ... |
Q9ZCX2 | MSVIEEKCNESSYSADSIKVLKGLEAVRKRPGMYIGDVGDGSGLHHMIYEVVDNSIDEALAGYCDLVQVTLNKNGSVTVSDNGRGIPVEIHEEEGISAAEVIMTQLHAGGKFDQQSYKISGGLHGVGVSVVNALSEWLELRIWRNNKEYFIRFNNGITEAPLSIVKENIDKKGTEVTFFPSVGTFTNIEFDFVTIEHRLRELAFLNSGVKILLVDNRFEEVKKVEFYYTGGIEAYVQYIDRAKHAIHPCIVVNTVHVESGISLELALHWNDSYHENILCFTNNIRQRDGGTHLSAFKSAITRVITSYLDTTGLNKKTKHD... | Cofactor: Binds two Mg(2+) per subunit. The magnesium ions form salt bridges with both the protein and the DNA. Can also accept other divalent metal cations, such as Mn(2+) or Ca(2+).
Function: A type II topoisomerase that negatively supercoils closed circular double-stranded (ds) DNA in an ATP-dependent manner to modu... |
P34031 | MGDNYNSESIQILEGLEAIRKRPGMYIGATNARGLHHLVWEIVDNSIDEVLANFANKIKIILNKDESITVIDNGRGIPIEIHPKTKVSTLETVFTILHAGGKFDSNTYKISGGLHGVGASVVNALSKYLKVEVRKNNKKYVMEFHNGGQILTPIKEVGSTSETGTTVTFLPDEKIFKETTIFSFSTIQNRIKQLVFLNKGLEISLVDLREEDEEKTVLYQFNNGIKDYVLELNKTIGTPLNDVFYVEGIEDNIVVEFGLQYNDNYSENIFSFCNNINTHEGGTHEEGARLAIVREINNYFKNQINKNNKGNEDKFTWDDI... | Cofactor: Binds two Mg(2+) per subunit. The magnesium ions form salt bridges with both the protein and the DNA. Can also accept other divalent metal cations, such as Mn(2+) or Ca(2+).
Function: A type II topoisomerase that negatively supercoils closed circular double-stranded (ds) DNA in an ATP-dependent manner to modu... |
D2Y296 | MNTVRVTFLLVFVLAVSLGQADKDESRMEMQEKTEQGKSYLDFAENLLPQKLEELEAKLLEEDSEESRNSRQKRCIGEGVPCDENDPRCCSGLVCLKPTLHGIWYKSYYCYKK | Function: Probable ion channel inhibitor.
Sequence Mass (Da): 13046
Sequence Length: 113
Domain: The presence of a 'disulfide through disulfide knot' structurally defines this protein as a knottin.
Subcellular Location: Secreted
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D2Y251 | MKLSIIIIATSLVIAVVAFPSKDSKAIENDKTEQRMEIVVQETARACSKQIGDKCKRNCECCGKTVVCGTIYVGGKEVNQCMDKTSDNAILNGLGKGMNFIENTFSFCV | Function: Putative ion channel inhibitor.
Sequence Mass (Da): 11846
Sequence Length: 109
Domain: The presence of a 'disulfide through disulfide knot' structurally defines this protein as a knottin.
Subcellular Location: Secreted
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P40281 | MDASTKVKKGAGGRKGGGPRKKAVTRSVRAGLQFPVGRIGRFLKKGRYAQRVGTGAPVYLAAVLEYLAAEVLELAGNAARDNKKNRISPRHLLLAVRNDVELGKLLAGVTIAYGGVLPNINPVLLPKRTESAASAPKSPSKAKKTPKKA | Function: Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is r... |
A5DJJ2 | MSGKGKSAGADKASTSRSAKAGLTFPVGRIHRLLRKGNYAQRVGSGAPVYLTSVLEYLTAEILELAGNAARDNKKSRIIPRHLQLAIRNDEELNKLLGDVTIAQGGVLPNIHQNLLPKKSGKGDKASQEL | Function: Core component of nucleosome which plays a central role in DNA double strand break (DSB) repair. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair... |
P04910 | MSGGKSGGKAAVAKSAQSRSAKAGLAFPVGRVHRLLRKGNYAQRVGAGAPVYLAAVLEYLAAEILELAGNAARDNKKTRIIPRHLQLAIRNDEELNKLLGHVTIAQGGVVPNINAHLLPKQSGKGKPSQEL | Function: Core component of nucleosome which plays a central role in DNA double strand break (DSB) repair. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair... |
P02276 | MDGSKAKKVAAKKFGGPRKKSVTKSIKAGLQFPVGRIGRYLKKGRYAQRVGSGAPVYLAAVLEYLAAEVLELAGNAAKDNKKTRIVPRHLLLAIRNDQELGRLLSGVTIAHGGVIPNINPVLLPKKAAEKAEKAGAAPKSPKKTTKSPKKA | Function: Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is r... |
P06898 | MSGRGKQGGKTRAKSKTRSSRAGLQFPVGRVHRLLRKGNYAERVGAGAPVYLAAVLEYLTAEILELAWERLPEITKRPVLSPGTCNSLCNDEELNKLLGGVTIAQGGVLPNIQSVLLPKKTESSKSTKSK | Function: Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is r... |
O81826 | MAGRGKQLGSGAAKKSTSRSSKAGLQFPVGRIARFLKAGKYAERVGAGAPVYLAAVLEYLAAEVLELAGNAARDNKKTRIVPRHIQLAVRNDEELSKLLGDVTIANGGVMPNIHNLLLPKKAGSSKPTEED | Function: Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is r... |
P35062 | MSGRGKQGGKARAKAKSRSSRAGLQFPVGRVHRLLRKGNYAERVGAGAPVYLAAVLEYLTAEILELAGNPARDNKKTRIIPRHLQLAIRNDEELNKLLGKVTIAQGGVLPNIQAVLLPKKTDSHKAKAK | Function: Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is r... |
Q7L7L0 | MSGRGKQGGKARAKAKSRSSRAGLQFPVGRVHRLLRKGNYSERVGAGAPVYLAAVLEYLTAEILELAGNAARDNKKTRIIPRHLQLAIRNDEELNKLLGRVTIAQGGVLPNIQAVLLPKKTESHHKAKGK | Function: Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is r... |
P69139 | MSGRGKGAKAKGKAKSRSSRAGLQFPVGRVHRFLRKGNYANRVGAGAPVYLAAVLEYLAAEILELAGNAARDNKKTRIIPRHLQLAIRNDEELNKLLGGVTIAQGGVLPNIQAVLLPKKTGSKSSK | Function: Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is r... |
Q9FJE8 | MESTGKVKKAFGGRKPPGAPKTKSVSKSMKAGLQFPVGRITRFLKKGRYAQRLGGGAPVYMAAVLEYLAAEVLELAGNAARDNKKSRIIPRHLLLAIRNDEELGKLLSGVTIAHGGVLPNINSVLLPKKSATKPAEEKATKSPVKSPKKA | Function: Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is r... |
Q9T0H7 | MVCNTNILKDVSTKISAFENVRMIMVEGEMFQVARIHKQLKNRVSAHSSVGATDVVYMTSILEYLTTEVLQLAENTSKDLKVKRITPRHLQLAIRGDEELDTLIKGTIIGGSVIPHIH | Function: Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is r... |
P0C5Z0 | MPRRRRRRGSSGAGGRGRTCSRTVRAELSFSVSQVERSLREGHYAQRLSRTAPVYLAAVIEYLTAKVLELAGNEAQNSGERNITPLLLDMVVHNDRLLSTLFNTTTISQVAPGED | Function: Atypical histone H2A which can replace conventional H2A in some nucleosomes and is associated with active transcription and mRNA processing. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central ... |
P70082 | MSGRGKQGGKVRAKAKSRSSRAGLQFPVGRVHRLLRKGNYAERVGAGAPVYMAAVLEYLTAEILELAGNAARDNKKTRIIPRHLQLAIRNDEELNKLLGKVTIAQGGVLPNIQAVLLPKKTESHKAKSK | Function: Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is r... |
Q9BTM1 | MSGRGKQGGKVRAKAKSRSSRAGLQFPVGRVHRLLRKGNYAERVGAGAPVYLAAVLEYLTAEILELAGNAARDNKKTRIIPRHLQLAIRNDEELNKLLGKVTIAQGGVLPNIQAVLLPKKTESQKTKSK | Function: Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is r... |
Q4R3X5 | MSGRGKQGGKVRAKAKSRSSRAGLQFPVGRVHRLLRKGNYAERVGAGAPVYLAAVLEYLTAEILELAGNAARDNKKTRIIPRHLQLAIRNDEELNKLLGKVTIAQGGVLPNIQAVLLPKKTESQKAKSK | Function: Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is r... |
Q8R1M2 | MSGRGKQGGKVRAKAKSRSSRAGLQFPVGRVHRLLRKGNYAERVGAGAPVYLAAVLEYLTAEILELAGNAARDNKKTRIIPRHLQLAIRNDEELNKLLGRVTIAQGGVLPNIQAVLLPKKTESQKVKSK | Function: Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is r... |
Q1DTG2 | MPGGKGKSVGGKGAPKDASGKTQRSHSAKAGLQFPCGRIKRFLKNNTQNKMRVGAKAAVYVTAVLEYLTAEVLELAGNAAKDLKVKRITPRHLQLAIRGDEELDTLIRATIAFGGVLPRINRALLLKVEQKKKSKIEA | Function: Variant histone H2A which can replace H2A in some nucleosomes. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal ... |
P0C0S5 | MAGGKAGKDSGKAKTKAVSRSQRAGLQFPVGRIHRHLKSRTTSHGRVGATAAVYSAAILEYLTAEVLELAGNASKDLKVKRITPRHLQLAIRGDEELDSLIKATIAGGGVIPHIHKSLIGKKGQQKTV | Function: Variant histone H2A which replaces conventional H2A in a subset of nucleosomes. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication... |
A3GHC1 | MSGKGKVHGGKGKSSEAAKSSTSHSARAGLQFPVGRIKRYLKRTAQNKIRVGSKSAIYLTAVLEYLTAEVLELAGNAAKDLKVKRITPRHLQLAIRGDEELDNLIKATIAYGGVLPHINKALLLKVEKKKQK | Function: Variant histone H2A which can replace H2A in some nucleosomes. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal ... |
P23527 | MPDPAKSAPAPKKGSKKAVTKAQKKDGKKRKRSRKESYSIYVYKVLKQVHPDTGISSKAMGIMNSFVNDIFERIAGEASRLAHYNKRSTITSREIQTAVRLLLPGELAKHAVSEGTKAVTKYTSSK | Function: Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is r... |
Q8CGP2 | MPEPVKSVPAPKKGSKKAVTKAQKKDGKKRKRSRKESYSVYVYKVLKQVHPDTGISSKAMGIMNSFVNDIFERIASEASRLAHYNKRSTITSREIQTAVRLLLPGELAKHAVSEGTKAVTKYTSSK | Function: Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is r... |
Q9LQQ4 | MAPRAEKKPAEKKTAAERPVEENKAAEKAPAEKKPKAGKKLPPKEAGDKKKKRSKKNVETYKIYIFKVLKQVHPDIGISSKAMGIMNSFINDIFEKLAQESSKLARYNKKPTITSREIQTAVRLVLPGELAKHAVSEGTKAVTKFTSS | Function: Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is r... |
P04255 | MPPKPSAKGAKKAAKTVTKPKDGKKRRHARKESYSVYIYRVLKQVHPDTGVSSKAMSIMNSFVNDVFERIAAEASRLAHYNKRSTISSREIQTAVRLILPGELAKHAVSEGTKAVTKYTSSK | Function: Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is r... |
P0C1H3 | MPEPAKSAPAPKKGSKKAVTKTQKKGDKKRKKSRKESYSIYVYKVLKQVHPDTGISSKAMGIMNSFVNDIFERIAGEASRLAHYNKRSTITSREIQTAVRLLLPGELAKHAVSEGTKAVTKYTSSK | Function: Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is r... |
Q5BJA5 | MPEPAKAAPKKGSKKAVTKTAGKGGKKRKRTRKESYAIYVYKVLKQVHPDTGISSKAMGIMNSFVNDIFERIAGEASRLAHYNKRSTITSREIQTAVRLLLPGELAKHAVSEGTKAVTKYTSSK | Function: Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is r... |
P81903 | MPDPAKTAPKKGSKKAVTKXA | Function: Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is r... |
Q9MBF7 | MPPRRKKKAAAAAAAAAAAAAAAGKAAAGKDGKAGIMTPKKPKKGKKKIPLMKYRVYIRRVLTQVRPELGISSKSMLIMNNFVVHNFQNIAKEASILAQYSKKKTITVKELKAAVKLVLPHQLLEYADRDGDRAVHNFESETSKKNSQGRKRGRGQQT | Function: Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is r... |
P82887 | MAKTPSKKAAKAPKKAGSKRNKRVETYSSYIYKVLKQVHPDTGISKRGMSIMNSFINDIFERLAGEASRLARYNKRSTLSSREIQTAVRLMLPGELAKHAVSEGTKAVTKFTSN | Function: Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is r... |
P69069 | MPEPAKSAPKKGSKKAVTKTAGKGGKKRKRSRKESYAIYVYKVLKQVHPDTGISSKAMGIMNSFVNDIFERIAGESSRLAHYNKRSTITSREIQTAVRLLLPGELAKHAVSEGTKAVTKYTSSK | Function: Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is r... |
Q7M4G7 | MPPKPSGKGQKKAGKAKGAPSTNKKRKRKRKESYGIYIYKVMKQVHPDTGISSKAMSIMNSFVNDIFERIAAEASRLAHYNKKSTITSREVQTAVRLLLPGELAKHAVSEGTKAVTKYTTSK | Function: Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is r... |
Q99285 | MAEPAKKKPKKLPKKDKGQKDIKRKKKESYTVKIYIFKVLKQVHPDIGISSKAMGIMNSFINDIFEKLASEASRLARYNKKSTITPREIQTAVRLLLPGEVAKHKVSEATKAVTKFTSGA | Function: Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is r... |
P83863 | TSGKAAKKAGKAQKSITKGDKKKRKESYSIYIYKVLKQVHPDTGISSKAMSIMNSFVNDIFERIAAEASRLAHYNKRSTITSREIQTAVRLLLPGELAKHAVSEGTKAVTKYTSSK | Function: Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is r... |
Q0U1A0 | MPPKAQKTPTTGGKAPAGKAPVEKKEAGKKTAAPSGEKKKRTKTRKETYSSYIYKVLKQVHPDTGISNRAMSILNSFVTTTHIFERVATEASKLAAYNKKSTISSREIQTSVRLILPGELAKHAVSEGTKAVTKYSSSTK | Function: Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is r... |
P19374 | MPPKVASKGAKKAASKAKAARSGEKKKKRRRRESYSIYIYKVLKQVHPDTGISSKAMSIMNSFVNDIFERIAAEASRLAHYNKRSTITSREIQTAVRLLLPGELAKHAVSEGTKAVTKYTSSK | Function: Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is r... |
Q8J1K2 | MPPKAADKKPAAKAPVASKAPEKKDAGKKTASTGEKKKRTKARRETYSSYIYKVLKQVHPDTGISNRAMSILNSFVNDIFERVATEASKLAAYNKKSTISSREIQTSVRLILPGELAKHAVSEGTKAVTKYSSSTK | Function: Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is r... |
Q4PB04 | MARTKQTARKSTGGKAPRKQLATKAARKSAPSAGGVKKPHRYRPGTVALREIRRYQKSTELLIRKLPFQRLVREIAQDFKTDLRFQSSAVMALQESAEAYLVSLFEDTNLAAIHAKRVTIQPKDIALARRLRGERT | Function: Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is r... |
P68428 | MARTKQTARKSTGGKAPRKQLATKAARKSAPATGGVKKPHRFRPGTVALREIRKYQKSTELLIRKLPFQRLVREIAQDFKTDLRFQSSAVSALQEAAEAYLVGLFEDTNLCAIHAKRVTIMPKDIQLARRIRGERA | Function: Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is r... |
Q9U281 | MARTKQTARKSTGGKAPRKQLATKAARKSAPTTGGVKKPHRYRPGTVALREIRRYQKSTELLIRKLPFQRLVREIAQDFKTDLRFQSAAIGALQEASEAYLVGLFEDTNLCAIHAKRVTIMPKDMQLARRIRGERA | Function: Variant histone H3 which replaces conventional H3 in a wide range of nucleosomes in active genes. Constitutes the predominant form of histone H3 in non-dividing cells and is incorporated into chromatin independently of DNA synthesis. Deposited at sites of nucleosomal displacement throughout transcribed genes,... |
Q402E2 | MARTKQTARKSTGGKAPRKQLATKAARKSAPTTGGVKKPHRYRPGTVALREIRKYQKSTDLLIRKLPFQRLVREIAQDYKADLRFQSHAVLALQEAAEAYLVGLFEDTNLCAIHAKRVTIMPKDIQLARRIRGERA | Function: Variant histone H3 which replaces conventional H3 in a wide range of nucleosomes in active genes. Constitutes the predominant form of histone H3 in non-dividing cells and is incorporated into chromatin independently of DNA synthesis. Deposited at sites of nucleosomal displacement throughout transcribed genes,... |
Q55BN9 | MARTKQTARKSTGAKVPRKHLGNKSSQKSFPSTQGLKKTHRFRPGTVALREIRRYQKSSELLIKKLPFQRLVREIAQEFKTDLRFQAAAIQALQEASEAYLVGLFEDTNLCAIHAKRVTIMVKDIQLARRIRGERA | Function: Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is r... |
Q2Z2F4 | MARTKQTARKSTGGKAPRKQLATKAARKSIPTGMGGMKRPRRYRPGTVALREIRKYQKSTELLIRKLPFQRLVREIAQDYKTDLRFQSHAVLALQEGAEAYLVGIFEDTNLCAIHAKRVTIMPKDIQLARRIRGERA | Function: Variant histone H3 which replaces conventional H3 in a wide range of nucleosomes in active genes. Constitutes the predominant form of histone H3 in non-dividing cells and is incorporated into chromatin independently of DNA synthesis. Deposited at sites of nucleosomal displacement throughout transcribed genes,... |
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