ids
stringlengths 6
10
| seqs
stringlengths 11
1.02k
| texts
stringlengths 108
11.1k
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Q7XTB2 | MASIRRPHSPAKQQHLLRHGHLGPFASSSPPSSPLRHSSSSSSPRSAAHHHHHLLAAAGHTSFRRPLPRFAAFFLLGSFLGLLHFLSHLPRPLGPIPNPNSHHRHRDPFPILQHPHPPSTPHSNHKLLIVVTPTRARPSQAYYLTRMAHTLRLLHDSPLLWIVVQAGNPTPEAAAALRRTAVLHRYVGCCHNINASAPDFRPHQINAALDIVDNHRLDGVLYFADEEGVYSLHLFHHLRQIRRFATWPVPEISQHTNEVVLQGPVCKQGQVVGWHTTHDGNKLRRFHLAMSGFAFNSTMLWDPKLRSHLAWNSIRHPEMVKESLQGSAFVEQLVEDESQMEGIPADCSQIMNWHVPFGSESVVYPKGWRVATDLDVIIPLK | 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 | MKLPLLRPLWPMLSPAAGSPDSPPEPSKPSLPAAWLLLHALFCATSMAVGFRFSRLIVYLLFLPTPINPTAHLVSLVSPPVMLAAANATTTITTTTTTTTTTVTTTTVAAEVGAHPQHHHHGPVFVGRHPIRVRPWPHPDPNELLKAHHILAAVQNAQRSSRRRGAGPPRPVIAVTPTTTSALQVPSLTSMAHTLRLVDGPLTWIVVEPEHHTDAVAAVLSRSNLNFLHITGPDSSTSRLRMHALREIRKRKMDGVVVFADENSILRTELFDEAQKVKSVGAVPVGVLGEDEGTSETFLQAPSCDAEGKLVGYHVSEETMLPANRGDMLLSSRLEWAGFVVNAQALWEGGGAASRPEWVSDIDAIDDGAAASPLSLVTDAARVEPLASCGQAALAWSHRSDALHEVKFPHEWKIDPPLVTIASRQQDAKPETPLKRTTLLNTEGQH | 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 | MDNGSNQLHVLFLPYFATGHIIPLVNAARLFVFHAGVKVTILTTHHNASLFRSTIDNDVEDGHSVISIHTLRFPSTEVGLPEGIENFSSASSPELAGKVFYAIYLLQKPMEDKIREIHPDCIFSDMYLPWTVNIALELKIPRLLFNQSSYMYNSILYNLRLYKPHKSKTITSTDSISVPGLPDKIEFKLSQLTDDLIKPEDEKNAFDELLDRTRESEDRSYGIVHDTFYELEPAYADYYQKVKKTKCWQIGPISHFSSKLFRRKELINAVDESNSCAIVEWLNEQEHKSVLYVSFGSVVRFPEAQLTEIAKALEASSIPFIWVVKKDQSAETTCLLEEEKLKNKGLIIRGWAPQLTILDHSAVGGFMTHCGWNSILEAIIAGVPLVTWPVFAEQFYNEKLVEVMGLGVKVGAEVHESNGGVEISSLVIESEKIKEAIEKLMDDSKESQKIREKVIGMSEMAKNAVEEGGSSWNNLTALIDDIKNFTSTTNV | 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(+) + nuatigenin 3-beta-D-glucopyranoside + UDP
Sequence Mass (Da): 55328
Sequence Length: 491
EC: 2.4.1.192
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C7J0P3 | MMEKHGGKVTSDRRAGRRQHGQRCSASDAAPLVVVVILIVAALFLILGPTGSSSFTVPRIRVVFNEPVHVAVAAPPPPPPPAQMQAGANASSEEDSGLPPPRQLTDPPYSLGRTILGYDARRSAWLAAHPEFPARVAPAGRPRVLVVTGSAPARCPDPDGDHLLLRAFKNKVDYCRIHGLDVFYNTAFLDAEMSGFWAKLPLLRMLMVAHPEAELIWWVDSDAVFTDMLFEIPWERYAVHNLVLHGWEAKVFDEKSWIGVNTGSFLIRNCQWSLDLLDAWAPMGPRGPVRDRYGELFAEELSGRPPFEADDQSALIYLLVTQRQRWGDKVFIESSYDLNGFWEGIVDKYEELRRAGRDDGRWPFVTHFVGCKPCRRYADSYPAERCRRGMERAFNFADDQILKLYGFAHESLNTTAVRRVRNETGEPLDAGDEELGRLLHPTFRAARPT | 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 | MGVKSVRFSIWFLFVVTDLVFCRTLSGDPDPCDATNQREFQKLRSDQITVLINGYSEYRIPLLQTIVASYSSSSIVSSILVLWGNPSTPDQLLDQLYQNLTQYSPGSASISLIQQSSSSLNARFLPRSSVDTRAVLICDDDVEIDQRSLEFAFSVWKSNPDRLVGTFVRSHGFDLQGKEWIYTVHPDKYSIVLTKFMMMKQDYLFEYSCKGGVEMEEMRMIVDQMRNCEDILMNFVAADRLRAGPIMVGAERVRDWGDARNEEVEERVRDVGLSSRRVEHRKRRGNCIREFHRVMGKMPLMYSYGKVVNSVGEQGLCRKAGKLVFCDRD | Function: Probable glycosyltransferase.
Sequence Mass (Da): 37703
Sequence Length: 329
Pathway: Protein modification; protein glycosylation.
EC: 2.4.1.-
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Q9SZG1 | MGKPGGAKTRTAVCLSDGVFFLAGAFMSLTLVWSYFSIFSPSFTSLRHDGKPVQCSGLDMQFDPSEPGFYDDPDLSYSIEKPITKWDEKRNQWFESHPSFKPGSENRIVMVTGSQSSPCKNPIGDHLLLRCFKNKVDYARIHGHDIFYSNSLLHPKMNSYWAKLPVVKAAMLAHPEAEWIWWVDSDAIFTDMEFKPPLHRYRQHNLVVHGWPNIIYEKQSWTALNAGVFLIRNCQWSMDLIDTWKSMGPVSPDYKKWGPIQRSIFKDKLFPESDDQTALIYLLYKHKELYYPKIYLEAEYYLQGYWIGVFGDFANVTERYLEMEREDDTLRRRHAEKVSERYGAFREERFLKGEFGGRGSRRRAFITHFTGCQPCSGDHNPSYDGDTCWNEMIRALNFADNQVMRVYGYVHSDLSKTSPLQPLPFDYPNEAW | 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 | MGHSPPVLPLCASVSLLGGLTFGYELAVISGALLPLQLDFGLSCLEQEFLVGSLLLGALLASLVGGFLIDCYGRKQAILGSNLVLLAGSLTLGLAGSLAWLVLGRAVVGFAISLSSMACCIYVSELVGPRQRGVLVSLYEAGITVGILLSYALNYALAGTPWGWRHMFGWATAPAVLQSLSLLFLPAGTDETATHKDLIPLQGGEAPKLGPGRPRYSFLDLFRARDNMRGRTTVGLGLVLFQQLTGQPNVLCYASTIFSSVGFHGGSSAVLASVGLGAVKVAATLTAMGLVDRAGRRALLLAGCALMALSVSGIGLVSFAVPMDSGPSCLAVPNATGQTGLPGDSGLLQDSSLPPIPRTNEDQREPILSTAKKTKPHPRSGDPSAPPRLALSSALPGPPLPARGHALLRWTALLCLMVFVSAFSFGFGPVTWLVLSEIYPVEIRGRAFAFCNSFNWAANLFISLSFLDLIGTIGLSWTFLLYGLTAVLGLGFIYLFVPETKGQSLAEIDQQFQKRRFTLSFGHRQNSTGIPYSRIEISAAS | 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 | MGLRPAVLLLCASVSLLGGLTFGYELAVISGALLPLQLNFGLSCLEQELLVGSLLLGALLASLVGGFLIDCYGRRRAILGSNAVLLAGSLILGLASSLPWLLLGRLSVGFAISLSSMACCIYVSELVGPRQRGVLVSLYEVGITVGILFSYGLNYVLAGSPWGWRHMFGWAAAPALLQSLSLFLLPAGAEGTAAPKDLIPLQGRETSKPGLVKPQYSFLDLFRAQDGMWSRTVVGLGLVLFQQLTGQPNVLYYASTIFRSVGFHGGSSAVLASVGLGTVKVAATLVATGLVDRAGRRVLLLFGCALMALSVSGIGLVSFAVSLDSGPSCLATSNASQQVDLPGSSGLLVRSSLPPVLHTNGDQGQLVLSVTERPIHPVITASLGPVLNTASPVPTSPILEHTLLCWSALVCMMVYVSAFSVGFGPVTWLVLSEIYPAEIRGRAFAFCSSFNWAANLFISLSFLDLIGAIGLAWTFLLYGLTAVLGLAFIYLLVPETKGQSLAEIEQQFQTSRFPLNFGHRQRIGIQYHRLDVSSAS | 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 | MRALRRLIQGRILLLTICAAGIGGTFQFGYNLSIINAPTLHIQEFTNETWQARTGEPLPDHLVLLMWSLIVSLYPLGGLFGALLAGPLAITLGRKKSLLVNNIFVVSAAILFGFSRKAGSFEMIMLGRLLVGVNAGVSMNIQPMYLGESAPKELRGAVAMSSAIFTALGIVMGQVVGLRELLGGPQAWPLLLASCLVPGALQLASLPLLPESPRYLLIDCGDTEACLAALRRLRGSGDLAGELEELEEERAACQGCRARRPWELFQHRALRRQVTSLVVLGSAMELCGNDSVYAYASSVFRKAGVPEAKIQYAIIGTGSCELLTAVVSCVVIERVGRRVLLIGGYSLMTCWGSIFTVALCLQSSFPWTLYLAMACIFAFILSFGIGPAGVTGILATELFDQMARPAACMVCGALMWIMLILVGLGFPFIMEALSHFLYVPFLGVCVCGAIYTGLFLPETKGKTFQEISKELHRLNFPRRAQGPTWRSLEVIQSTEL | 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 | MDAPEESIRMTSDPQSKIYVQNPDTHIHLEQGPSAKSGNGRALVLCSVSVACLSGLLMGYEMSLISGALLQLRDVLTLSCPEQEQVVGSLLLGAFLLSLGGGTILDHYGRRFTIILTALLCVLGTLLSVCVVSFWALVVGRMLVGMSVALSGTASCLYAAEVAPAAWRGRCVCVYELMVVLGMLLGFGLSWAFAGVPDGWRFTFGGALLPALLQAGVMPLLPDSPRFLLAQQREKEAHATLLRLRAGIKEVEPVEDELRAIRLAMGAERLHGFLDLFQSRDNMLQRLLVGAALVFLQQATGQPNILAYASTVLSSVGFHGNEAATLASTGFGVVKVGGTIPAIFLVDKVGPKALLCVGVVVMMLSTATLGAITMQSRTHVSSLCRGPGNTANFTLFETGDETDIQTNTPLGLYQPQNKLKTNTFLTSINDTREHWILNHTYNHRTALMETAELSKKDSAKIALQSLHEVSPSLKWISLVSLLVYVAGFSISLGPMVHVVLSAIFPTGIRGKAVSVISAFNWATNLLISMTFLTLTERIGLPTVIFSYSAMSFLLVVFVIVFVPETKGRSLEQISKELAMKNHLRGTLLCHRRKHKATAQPSQEEKALATV | 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 | MVPVENTEGPSLLNQKGTAVETEGSGSRHPPWARGCGMFTFLSSVTAAVSGLLVGYELGIISGALLQIKTLLALSCHEQEMVVSSLVIGALLASLTGGVLIDRYGRRTAIILSSCLLGLGSLVLILSLSYTVLIVGRIAIGVSISLSSIATCVYIAEIAPQHRRGLLVSLNELMIVIGILSAYISNYAFANVFHGWKYMFGLVIPLGVLQAIAMYFLPPSPRFLVMKGQEGAASKVLGRLRALSDTTEELTVIKSSLKDEYQYSFWDLFRSKDNMRTRIMIGLTLVFFVQITGQPNILFYASTVLKSVGFQSNEAASLASTGVGVVKVISTIPATLLVDHVGSKTFLCIGSSVMAASLVTMGIVNLNIHMNFTHICRSHNSINQSLDESVIYGPGNLSTNNNTLRDHFKGISSHSRSSLMPLRNDVDKRGETTSASLLNAGLSHTEYQIVTDPGDVPAFLKWLSLASLLVYVAAFSIGLGPMPWLVLSEIFPGGIRGRAMALTSSMNWGINLLISLTFLTVTDLIGLPWVCFIYTIMSLASLLFVVMFIPETKGCSLEQISMELAKVNYVKNNICFMSHHQEELVPKQPQKRKPQEQLLECNKLCGRGQSRQLSPET | 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 | MVPVENTEGPNLLNQKGREAETEGSCGASGGGHPACAGGPSMFTFLTSVTAAISGLLVGYELGLISGALLQIRTLLALTCHEQEMVVSSLLIGAFLASLTGGVLIDRYGRRLAIILSSCLLGLGSLVLIMSLSYTLLIMGRVAIGVSISLSSIATCVYIAEIAPQHRRGLLVSLNELMIVTGILFAYISNYAFANISNGWKYMFGLVIPLGVLQAIAMYFLPPSPRFLVMKGQEESAGKVLRKLRVISDTTEELTLIKSSLKDEYQYSFWDLFRSKDNMRTRILIGLTLVFFVQTTGQPNILFYASTVLKSVGFQSNEAASLASTGVGVVKVVSTIPATLLVDHIGSKTFLCIGSSVMSASLLTMGIVNLNINMNFTNICRSHSLLNQSLEEFVFYATGNLSISNSSLREHFKRITPYSKGSFMPMGNGMEPKGEMTFTSSLPNAGLSRTEHQGVTDTAVVPAAYKWLSLASLLVYVAAFSIGLGPMPWLVLSEIFPGGIRGRAMALTSSMNWGVNLLISLTFLTVTDLIGLSWVCFIYTIMSLASLAFVVLFIPETKGCSLEQISVELAKANYVKNNICFMSHHQEELVPTQLQKRKPQEQLPECNHLCGRGQSQRPSPDT | 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 | MEPSSKKLTGRLMLAVGGAVLGSLQFGYNTGVINAPQKVIEEFYNQTWVHRYGESILPTTLTTLWSLSVAIFSVGGMIGSFSVGLFVNRFGRRNSMLMMNLLAFVSAVLMGFSKLGKSFEMLILGRFIIGVYCGLTTGFVPMYVGEVSPTALRGALGTLHQLGIVVGILIAQVFGLDSIMGNKDLWPLLLSIIFIPALLQCIVLPFCPESPRFLLINRNEENRAKSVLKKLRGTADVTHDLQEMKEESRQMMREKKVTILELFRSPAYRQPILIAVVLQLSQQLSGINAVFYYSTSIFEKAGVQQPVYATIGSGIVNTAFTVVSLFVVERAGRRTLHLIGLAGMAGCAILMTIALALLEQLPWMSYLSIVAIFGFVAFFEVGPGPIPWFIVAELFSQGPRPAAIAVAGFSNWTSNFIVGMCFQYVEQLCGPYVFIIFTVLLVLFFIFTYFKVPETKGRTFDEIASGFRQGGASQSDKTPEELFHPLGADSQV | 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 energy-independent, facilitative transport of glucose into the brain . In association with BSG and NXNL1, promotes retinal cone survival by increasing glucose uptake into photoreceptors (By similarity).
PTM: Phosphorylation at Ser-226 by PKC promotes glucose uptake by increasing cell membrane localization.
Location Topology: Multi-pass membrane protein
Catalytic Activity: D-glucose(out) = D-glucose(in)
Sequence Mass (Da): 54084
Sequence Length: 492
Pathway: Carbohydrate degradation.
Subcellular Location: Cell membrane
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Q83BZ6 | MLKDIHQHRILILDFGSQYAQLIARRVREIGVYCELMPCDIDEETIRDFNPHGIILSGGPETVTLSHTLRAPAFIFEIGCPVLGICYGMQTMAYQLGGKVNRTAKAEFGHAQLRVLNPAFLFDGIEDQVSPQGEPLLDVWMSHGDIVSELPPGFEATACTDNSPLAAMADFKRRFFGLQFHPEVTHTPQGHRILAHFVIHICQCIPNWTTKHIIEDSIRDIQEKVGKEQVIVGLSGGVDSAVTATLVHKAIGDQLVCVLVDTGLLRLNEVDEVLNVFQKHLGAKVICVDAKDRFMKALKGISDPEEKRKIAGEQFIRVFEEQAKKLNVKWLGQGTIYPDVIESAKTKTGKGHIIKTHHNVGGLPLNMELKLIEPLRELFKDEVRKLGLELGLPADLIYRHPFPGPGLAIRILGEVSAEYINILKQADAIFIEELKKSDYYHQVSQAFAVFMPLKSVGVKGDARHYGYIIALRAVKTVDFMTAQWADLPHEFLSKVSHRIVNEIKEVSRVVYDMTNKPPATIEWE | 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 | MAPGGVVGHRLAFMEQLHDVVLVVDFGAQYAQLIARRVREANVYSEIVPHNMPVRDMLAKEPAAIILSGGPASVYVEGAPSVDPALFNAGVPVLGICYGFQAMAQALGGQVAHTGASEYGRTSLCITSAGQLLSRIPHTISVWMSHGDSVSRAPEGFSTLARTAGAPVAAFEDVERRLVGVQWHPEVHHTESGQTVLEHFLFDIAGCRPDWNASSIVGDQIAQIRGQVGDRRVICGLSGGVDSAVAAALVQRAVGDQLTCVFVDHGLLRQGEAEQVKNDFVAATGADLVVADESQRFLDALAGVTDPETKRKIIGREFIRTFEDVAKRLNADQPIDFLVQGTLYPDVVESGGGEGAANIKSHHNVGGLPDDFQFSLVEPLRTLFKDEVRAVGLELGLPEDIVWRQPFPGPGLAIRIIGEVTAERLEVLRTADAITREEMGAAGLDRKVWQCPVVLLSDVHSVGVQGDGRTYGSPIVLRPVTSEDAMTADWARIPYDVLEKISTRITNACPQINRVVLDITSKPPATIEWE | 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 | MEIAKEKSGAKPEFIDNEDESLRESIVIFDFGSQYSLLIARRIREMHVYCELVSHDTPWEKIAHLNPRGFILSGGPSSVYEAGAPLAPAYIFESKLPVLGICYGMQAITHQLGGVVEHSEKREYGHALLHSSVANSDLLSDMPEPSPVWMSHGDRIEKMPAGFTALAYTENCPVAVMGNEADIYGLQFHPEVVHSPNGKIILKNFVFNICKCHANWTMGNYIQESIHNIREQVGDGQVICALSGGVDSAVVASLIHKAIGDQLTCIYVNNGLLRREEADRTLHVFKNHMGMKIIYVDAVDRFLDSLSGVTDPEQKRKVIGSEFIKVFEDEACKLGKIDFLAQGTLYPDVIESVSSVSKASAKIKSHHNVGGLPAHMKLKLIEPLRYLFKDEVRLLGKELGLPDEMIWRQPFPGPGLAIRIIGEVTREKLEILRAADWIVMSEIKKAKMYHQVWQSFAILTDVKSVGVMGDFRTYGYLVAIRAVTSEDAMTADWAKLPYDLLSVISNRIVNEVKEVNRVVYDISSKPPSTIEWE | 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 | MSIVILDFGSQFTRLITRRFRELGAYSVILPGTASLERIQQENPQGIVLSGGPSSVYDEGAPRPAPGVLDLNVPILGVCYGMQYLAHEAGGDVKRAGKREYGKADLTEYGGRLFEGIQGEFVAWMSHSDSVTQLPQGYQVVARTEHTPVTAIENNDTRRYGVQFHPEVVHTPKGGQMLANFLDICGVTRDWNAEHIVDELIEGVRAQVGDTGRVLLGISGGVDSSTLALLLAKAVGERLTAVFIDHGLLRLGEREQVEAALTPLGVNLVTVDAKDEFLGQLAGVSDPEQKRKIIGREFIRAFERETAKLGDFEFLAQGTLYPDVIESAGGEGAANIKSHHNVGGLPDDVQFKLVEPFRTLFKDEVREIARLLGLPDHIRMRHPFPGPGLAIRCLGEVTAEKVDILQRVDDIFISGLREFGLYDGCSQALAVLTPIQSVGVMGDERTYSYTAALRAVTTDDFMTAEWARLPYDFLATMSNRIVNQVHEINRVVYDITGKPPATIEWE | 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 | MRFLDGHTPAYDLTYNDVFVVPGRSDVASRFDVDLSTVDGSGTTIPVVVANMTAVAGRRMAETVARRGGIVVLPQDLPITAVSETVDFVKSRDLVVDTPVTLSPEDSVSDANALLHKRAHGAAVVVFEGRPIGLVTEANCAGVDRFARVRDIALSDFVTAPVGTDPREVFDLLEHAPIDVAVMTAPDGTLAGVLTRTGAIRAGIYTPAVDAKGRLRIAAAVGINGDVGAKAQALAEAGADLLVIDTAHGHQAKMLDAIKAVASLDLGLPLVAGNVVSAEGTRDLIEAGASIVKVGVGPGAMCTTRMMTGVGRPQFSAVVECAAAARQLGGHVWADGGVRHPRDVALALAAGASNVMIGSWFAGTYESPGDLLFDRDDRPYKESYGMASKRAVAARTAGDSSFDRARKGLFEEGISTSRMSLDPARGGVEDLLDHITSGVRSTCTYVGAANLPELHEKVVLGVQSAAGFAEGHPLPAGW | 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 Activity: IMP + NADP(+) + NH4(+) = GMP + 2 H(+) + NADPH
Sequence Mass (Da): 49593
Sequence Length: 478
Pathway: Purine metabolism; IMP biosynthesis via salvage pathway.
EC: 1.7.1.7
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Q9Y2T3 | MCAAQMPPLAHIFRGTFVHSTWTCPMEVLRDHLLGVSDSGKIVFLEEASQQEKLAKEWCFKPCEIRELSHHEFFMPGLVDTHIHASQYSFAGSSIDLPLLEWLTKYTFPAEHRFQNIDFAEEVYTRVVRRTLKNGTTTACYFATIHTDSSLLLADITDKFGQRAFVGKVCMDLNDTFPEYKETTEESIKETERFVSEMLQKNYSRVKPIVTPRFSLSCSETLMGELGNIAKTRDLHIQSHISENRDEVEAVKNLYPSYKNYTSVYDKNNLLTNKTVMAHGCYLSAEELNVFHERGASIAHCPNSNLSLSSGFLNVLEVLKHEVKIGLGTDVAGGYSYSMLDAIRRAVMVSNILLINKVNEKSLTLKEVFRLATLGGSQALGLDGEIGNFEVGKEFDAILINPKASDSPIDLFYGDFFGDISEAVIQKFLYLGDDRNIEEVYVGGKQVVPFSSSV | 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.
EC: 3.5.4.3
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Q9R111 | MCAARTPPLALVFRGTFVHSTWTCPMEVLRDHLLGVSDSGKIVFLEESSQQEKLAKEWCFKPCEIRELSHHEFFMPGLVDTHIHAPQYAFAGSNVDLPLLEWLNKYTFPTEQRFRSTDVAEEVYTRVVRRTLKNGTTTACYFGTIHTDSSLILAEITDKFGQRAFVGKVCMDLNDTVPEYKETTEESVKETERFVSEMLQKNYPRVKPIVTPRFTLSCTETLMSELGNIAKTHDLYIQSHISENREEIEAVKSLYPSYKNYTDVYDKNNLLTNKTVMAHGCYLSEEELNIFSERGASIAHCPNSNLSLSSGLLNVLEVLKHKVKIGLGTDVAGGYSYSMLDAIRRAVMVSNVLLINKVNEKNLTLKEVFRLATLGGSQALGLDSEIGNFEVGKEFDALLINPRASDSPIDLFYGDFVGDISEAVIQKFLYLGDDRNIEEVYVGGKQVVPFSSSV | 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.
EC: 3.5.4.3
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O14057 | MDGHTCDVFVGKLIHTPSLGELEITDATVGVYNGKIVFLEKSMTPKTLEEAKSHHLLKEATIHKLKPLQFMFPGLIDTHIHAPQYPNSGIGIDVPLLQWLEKYTFPLESSLADLEEARQVYKRVVERTLSNGTTFASYFSTLHTPTSALLAEICYSYGQRAYIGKCNMNNLSPDHYCEKSAESSLEATRQLISYMSILDPKREMVTPIITPRFAPSCTEDLLSGCGELAEKHNLPIQTHISENTSEIELVKELFPERKSYADVYDYYKLLTPQTILAHAIHLEDEEIELLTKRSSGISHCPTSNSILASGLANVRKLLDSGINVGLGTDVSGGYAPSILIALRHAAMTSRSLSYVLGDPKVMLDLSELLYLATQGGAEVVSRGDQVGSFAVGKYWDALIVDLSAETHSCVDIFERDTWPVMLSKWVFTSDDRNLAQVWVNGRLVSGFEMKANLKNSTPLTNGVTSSGHQVFKELTQAHLLPRTQCVDTPPSCCGGHCCKEESCRTENCKGAYPANATVTVEEDSGMS | 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.
EC: 3.5.4.3
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Q07729 | MTKSDLLFDKFNDKHGKFLVFFGTFVDTPKLGELRIREKTSVGVLNGIIRFVNRNSLDPVKDCLDHDSSLSPEDVTVVDIIGKDKTRNNSFYFPGFVDTHNHVSQYPNVGVFGNSTLLDWLEKYTFPIEAALANENIAREVYNKVISKTLSHGTTTVAYYNTIDLKSTKLLAQLSSLLGQRVLVGKVCMDTNGPEYYIEDTKTSFESTVKVVKYIRETICDPLVNPIVTPRFAPSCSRELMQQLSKLVKDENIHVQTHLSENKEEIQWVQDLFPECESYTDVYDKYGLLTEKTVLAHCIHLTDAEARVIKQRRCGISHCPISNSSLTSGECRVRWLLDQGIKVGLGTDVSAGHSCSILTTGRQAFAVSRHLAMRETDHAKLSVSECLFLATMGGAQVLRMDETLGTFDVGKQFDAQMIDTNAPGSNVDMFHWQLKEKDQMQEQEQEQGQDPYKNPPLLTNEDIIAKWFFNGDDRNTTKVWVAGQQVYQI | 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.
Subcellular Location: Cytoplasm
EC: 3.5.4.3
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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: 312
Pathway: Glycan metabolism; beta-D-glucan degradation.
EC: 3.2.1.73
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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 | QKPGETKEVHPQLTTFRCTKRGGCKPATNFIVLDSLSHPIHRAEGLGPGGCGDWGNPPPKDVCPDVESCAKNCIMEGIPDYSQYGVTTNGTSLRLQHILPDGRVPSPRVYLLDKTKRRYEMLHLTGFEFTFDVDATKLPCGMNSALYLSEMHPTGAKSKYNPGGAYYGTGYCDAQCFVTPFINGLGNIEGKGSCCNEMDIWEANSRASHVAPHTCNKKGLYLCEGEECAFEGVCDKNGCGWNNYRVNVTDYYGRGEEFKVNTLKPFTVVTQFLANRRGKLEKIHRFYVQDGKVIESFYTNKEGVPYTNMIDDEFCEATGSRKYMELGATQGMGEALTRGMVLAMSIWWDQGGNMEWLDHGEAGPCAKGEGAPSNIVQVEPFPEVTYTNLRWGEIGSTYQELQ | 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-glucosidases which hydrolyze the cellobiose and other short cello-oligosaccharides to glucose.
Catalytic Activity: Endohydrolysis of (1->4)-beta-D-glucosidic linkages in cellulose, lichenin and cereal beta-D-glucans.
Sequence Mass (Da): 44577
Sequence Length: 402
Subcellular Location: Secreted
EC: 3.2.1.4
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A0A024SNB7 | MAPSVTLPLTTAILAIARLVAAQQPGTSTPEVHPKLTTYKCTKSGGCVAQDTSVVLDWNYRWMHDANYNSCTVNGGVNTTLCPDEATCGKNCFIEGVDYAASGVTTSGSSLTMNQYMPSSSGGYSSVSPRLYLLDSDGEYVMLKLNGQELSFDVDLSALPCGENGSLYLSQMDENGGANQYNTAGANYGSGYCDAQCPVQTWRNGTLNTSHQGFCCNEMDILEGNSRANALTPHSCTATACDSAGCGFNPYGSGYKSYYGPGDTVDTSKTFTIITQFNTDNGSPSGNLVSITRKYQQNGVDIPSAQPGGDTISSCPSASAYGGLATMGKALSSGMVLVFSIWNDNSQYMNWLDSGNAGPCSSTEGNPSNILANNPNTHVVFSNIRWGDIGSTTNSTAPPPPPASSTTFSTTRRSSTTSSSPSCTQTHWGQCGGIGYSGCKTCTSGTTCQYSNDYYSQCL | 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 new chain ends for exocellobiohydrolases (CBHs). The CBH release the disaccharide cellobiose from the non-reducing end of the cellulose polymer chain. Finally, beta-1,4-glucosidases hydrolyze the cellobiose and other short cello-oligosaccharides into glucose units.
PTM: Asn-204 contains mainly a high-mannose-type glycan (Hex(7-9)GlcNAc(2)), with a small fraction (8%) bearing a single GlcNAc at this site.
Catalytic Activity: Endohydrolysis of (1->4)-beta-D-glucosidic linkages in cellulose, lichenin and cereal beta-D-glucans.
Sequence Mass (Da): 48208
Sequence Length: 459
Domain: The enzyme consists of two functional domains, a catalytic core joined to a carbohydrate-binding domain (CBM) by a serine-, threonine-, and proline-rich, highly glycosylated linker sequence.
Subcellular Location: Secreted
EC: 3.2.1.4
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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 Length: 25
EC: 3.2.1.4
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P33682 | MSRKLRTLMAALCALPLAFAAAPPAHAADPTTMTNGFYADPDSSASRWAAANPGDGRAAAINASIANTPMARWFGSWSGAIGTAAGAYAGAADGRDKLPILVAYNIYNRDYCGGHSAGGAASPSAYADWIARFAGGIAARPAVVILEPDSLGDYGCMNPAQIDEREAMLTNALVQFNRQAPNTWVYMDAGNPRWADAATMARRLHEAGLRQAHGFSLNVSNYITTAENTAYGNAVNNELAARYGYTKPFVVDTSRNGNGSNGEWCNPSGRRIGTPTRTGGGAEMLLWIKTPGESDGNCGVGSGSTAGQFLPEVAYKMIYGY | 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 | MKRRTTAVLTLTALLGTALTALPVQQAGAEEVEQVRNGTFDTTTDPWWTSNVTAGLSDGRLCADVPGGTTNRWDSAIGQNDITLVKGETYRFSFHASGIPEGHVVRAVVGLAVSPYDTWQEASPVLTEADGSYSYTFTAPVDTTQGQVAFQVGGSTDAWRFCVDDVSLLGGVPPEVYEPDTGPRVRVNQVAYLPAGPKNATLVTDATARLPWQLRNAQGTTVARGLTVPRGVDASSGQNVHSIDFGSYRGRGTGYTLVADGETSHPFDIDAAAYRPLRLDSVKYYYTQRSGIAIRDDLRPGYGRAAGHLNVAPNQGDANVPCQPGVCDYTLDVTGGWYDAGDHGKYVVNGGIATWELLSTYERSLTARTGHPAALGDGTLALPESGNKVPDVLDEARWELEFLLKMQVPAGQPLAGMAHHKLHDEQWTGLPLLPDQDPQKRELHPPTTAATLNLAATAAQAARLYRPFDKAFAARALTAARTAWQAALAHPDLLADPNDGTGGGAYNDDDVTDEFYWAAAELYLTTGERQFADHVLDSPVHTADIFGPTGFDWGHTAAAGRLDLALVPSRLPGRDQVRRSVIKAADTYLATLTAHPYGMPYAPAGNRYDWGSSHQVLNNGVVLASAYDLTGAAKYRDGALQGMDYVLGRNALNMSYVTGYGEVSSHNQHSRWYAHQLDPTLPNPPSGTLAGGPNSSIQDPYAQSKLTGCVGQFCYIDDIQSWSTNETAINWNAALARMASFAADQG | 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 | MENPRTTPTPTPLRRRRSERRARGGRVLTALTGVTLLAGLAIAPAATGASPSPAPPASPAPSADSGTADAGTTALPSMELYRAEAGVHAWLDANPGDHRAPLIAERIGSQPQAVWFAGAYNPGTITQQVAEVTSAAAAAGQLPVVVPYMIPFRDCGNHSGGGAPSFAAYAEWSGLFAAGLGSEPVVVVLEPDAIPLIDCLDNQQRAERLAALAGLAEAVTDANPEARVYYDVGHSAWHAPAAIAPTLVEAGILEHGAGIATNISNYRTTTDETAYASAVIAELGGGLGAVVDTSRNGNGPLGSEWCDPPGRLVGNNPTVNPGVPGVDAFLWIKLPGELDGCDGPVGSFSPAKAYELAGG | 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
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P54424 | MAFKLNIGLLALSLSLSLVHLDGVRAGMATRYWDCCLASASWEGKAPVYAPVDACKADGVTLIDSKKDPSGQSGCNGGNKFMCSCMQPFDDETDPTLAFGFGAFTTGQESDTDCACFYAEFEHDAQGKAMKRNKLIFQVTNVGGDVQSQNFDFQIPGGGLGAFPKGCPAQWGVEASLWGDQYGGVKSATECSKLPKPLQEGCKWRFSEWGDNPVLKGSPKRVKCPKSLIDRSGCQRKDDNTISPYSGKVDSANTAAPAQYKRDRSVCLAGGKKGKSAAGGVDGSGDASGGADASGAGGAAEGSQGQPEGYGQPSGGNDQGSSNGDATTGAGSGSGSDSGSTANGSGSGAPTSGSDGSAVAPPSGGSNPGAAQGGQGGAQPGPSGGHKKCHKKH | 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
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P37651 | MNVLRSGIVTMLLLAAFSVQAACTWPAWEQFKKDYISQEGRVIDPSDARKITTSEGQSYGMFSALAANDRAAFDNILDWTQNNLAQGSLKERLPAWLWGKKENSKWEVLDSNSASDGDVWMAWSLLEAGRLWKEQRYTDIGSALLKRIAREEVVTVPGLGSMLLPGKVGFAEDNSWRFNPSYLPPTLAQYFTRFGAPWTTLRETNQRLLLETAPKGFSPDWVRYEKDKGWQLKAEKTLISSYDAIRVYMWVGMMPDSDPQKARMLNRFKPMATFTEKNGYPPEKVDVATGKAQGKGPVGFSAAMLPFLQNRDAQAVQRQRVADNFPGSDAYYNYVLTLFGQGWDQHRFRFSTKGELLPDWGQECANSH | 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
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A0A023VXA2 | MPRMLAASAAIIATTLAPLSAQAAGCEMTLHGINLSGAEFGQPGDPYGQGYIYPSESTIKAFADDGFNAVRLPFLWERLQPTLNGTLDATELSRIKDTVETLRDNGMVVILDVHNYARYHGEMIGTPNVPVAAFADFWKRLSAVFANDDDVIFGLMNEPHDISAPAWLAAANAAIDAIRTIGAGNLVLVPGTAWTGAHSWSQTFYGPSNASVMAQVVDSSNNFAYEVHQYTDDDFSGKNADCSKIDDAVSALNDFTSWLNANDVQGFLGEFGTTEQIQCLRGLKQMVDVVQQNPRAWLGWAYWAGGDWWPKDSPMIIHSNPRDGGTQQLRTLQPVLGSNTTRASCNTKS | 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
EC: 3.2.1.4
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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
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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
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Q8RSY9 | MSPLKCMALAALGAVMFVGSAQAQTCDWPLWQNYAKRFVQDDGRVLNSSMKPTESSSEGQSYAMFFALVGNDRASFDKLWTWTKANMSGADIGQNLPGWLWGKKADNTWGVIDPNSASDADLWMAYALLEAARVWNAPQYRADAQLLLANVERNLIVRVPGLGKMLLPGPVGYVHAGGLWRFNPSYQVLAQLRRFHKERPNAGWNEVADSNAKMLADTASNPHGLAANWVGYRATSANTGLFVVDPFSDDLGSYDAIRTYMWAGMTAKGDPLAAPMLKSLGGMTRATAASATGYPPEKIHVLTGEVEKNNGYTPMGFSASTVAFFQARGETALAQLQKAKVDDALAKALAPSAPDTAQPIYYDYMLSLFSQGFADQKYRFEQDGTVKLSWEAACAVTR | 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
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P17974 | MRRCMPLVAASVAALMLAGCGGGDGDPSLSTASVSATDTTTLKPAATSTTSSVWLTLAKDSAAFTVSGTRTVRYGAGSAWVEKSVSGSGRCTSTFFGKDPAAGVAKVCQLLQGTGTLLWRGVSLAGAEFGEGSLPGTYGSNYIYPSADSVTYYKNKGMNLVRLPFRWERLQPTLNQVFDANELSRLTGFVNAVTATGQTVLLDPHNYARYYGNVIGSSAVPNSAYADFWRRLATQFKSNPRVILGLMNEPNSMPTEQWLSGANAELAAIRSANASNVVFVPGNAWTGAHSWNQNWYGTPNGTVMKGINDPGHNLVFEVHQYLDGDSSGQSANCVSATIGAQRLQDFTTWLRSNGYRGFLGEFGAASNDTCNQAVSNMLTFVKNNADVWTGWAWWAGGPWWGGYMYSIEPSNGVDKPQMSVLAPYLK | 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
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P23044 | MKLVFSALASLLSGASATIYYAGVAESSGEFGVWSATQTPGTGLPGRFGVDYAFISEAAVDVHVDQNHLNLFRVAFLLERMCPPATGLGAAFNETHFDYFKEAVDYITVTKGAYAILDPHNYMRYNDPSYQPFSGSVIGNTSDSTAATTEQFGEFWGELASRFNDNERVIFGLMNEPHDMATSLVLANNQAAIDAIRAANASNLIIMPGNSWTGGHSWTEGSDPSSALLNQFKDPLNNTAIDIHEYLDYDFSGGHLECVSDPETNLAALTAWLKENNLKAFITEFGGSNSTSCQEMLPDLINYMADNAEYIGWTAWAAGPFWGPNSPCCTNSTQLGSLEPGSTAVDGSPGLYDTVWLPVIQPLVPTELQWSGPASISGGELTSRA | 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
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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
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P58935 | MTRRRLLHAGTLAGVAALLPAAALAAPSQCGPWPLWSAFVDKHIQRDGRVVDFLNPDQRSTSEGQSYALFFALVNNDQVLFDKVLSWTRHNLCGGRPDLNLPAWLWGRDGSGAWRVLDANTASDGELWIAYALLEAGRLWSRPGFLKAGQQMLQLIRTQEVATLPGLGPMLLPGRTGFVDNGRWTLNPSYLPIQVLRRCANADPKGPWAAIAANSARVLRDSAPVGFAPDWTVWDGKTFNADPKRGNVGSYDAIRVYLWAGMLDAGEPLRARLLQDLSGPADLLAAQQTPAEKIDTARGVGTGALPVGFSAALLPYLSALGKPALLKAQAQRVPAATQPAAAALPYFERTLALFGQGWLENRYRFAADGRLLPAWRTPACAATT | 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
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Q5AKZ2 | MNYLSQLGKLFSLETLDTRLNPTTNPIKRQSIIKKANPTSRWSTLEFKIYLTILIIVVPLMIKAAMESSNETNPNYPRFQHLLSDGWILGRKVDNSDQQYRFFRNNFPLLCGLIFIHVTLRKLINTFIIIPNGRYNNNFKRTYFDLIFGIIFLIGAHGINVFKISFHLFINYLIGKYIKNYKLAIWCTWIYGIFSLFFNEWFGDSSFGLSIFVNGSGYYTGIIPRWDVFYNFTLLRMLSFNLDYIERERKLGNNDGQLNLNKQENINGADNPPTLLNLDDRQRLSAPLPLDDYNVSNYIAYISYTPLFIAGPIITFNDYVYQSNYQQSSTTQNYQRIFMYAIRFLFCLLVMEFLLHFMYVVAVSKTKAWDGDTPFQISMLGMFNLNLIWLKLLIPWRLFRLWALLDGIDPPENMIRCMDNNFSALAFWRAWHRSYNRWVIRYIYIPMGGSGTGKYRIINSLLVFSFVAIWHDIELKLLMWGWLVVIFLIPEISATLIFSKYNKNWWYRYLCGIGAVINIWMMMIANLVGFCLGTDGMWKLLHDLFQTFEGGRFFIISSICLFVGAQIMFELRESELRRAIDVRC | 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 integrity and apoptosis (By similarity). Plays a role in virulence and antifungal resistance .
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 68733
Sequence Length: 584
Subcellular Location: Cell membrane
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Q7Z888 | MFKAAMDASNETNPNYPKFAHLLSQGWMFGRKVDNSDQQYRFFRDNFPLLCGLVLLHTSLRRGVNLIAGNHKRTGFDFVFGXDIHLCSTRDEFLPYFDSLGYXIFPFLKYIKRNDVATXTYVDXTAILSLFLNDNYXSCTIWNRFYRSWISEVSFQDGMCFSISHCXRMLSYNLDYIEKRKSASEESNLELKNSSSSLSELDDRERLVAPIPLTDYNFVNYMAYITYAPLFIAGPIITFNDYIYQSDYKAMSSVKDYKRTFIYFLRFAFCILVMEFLLHFMYVVAVSKTKAWEGDTPFQLSMLGLFNLNIIWLKLLIPWRLFRLWSLIDGIDPPENMIRCMDNNFSTLAFWRAWHRSYNRWIIRYIYIPLGGGGKYRILNSLCVFSFVAIWHDIELKLLMWGWLVVIFIIPELAATAIFKNYQHEPWYRHVCALGAVINIWMMMLANLFGFCMGKDGTMSLIKTLFTTAVGLRFLFLSLGALFVGSQVMFELREAEKRRGVNVKC | 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 integrity and apoptosis.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 59111
Sequence Length: 505
Subcellular Location: Cell membrane
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Q09758 | MLRLFRFDVLETSTKDTERPNSKSSRLSSTSGSSHPSSSSRLTVRSAVPEKSAFGSIEFIFYFSVILSILTIACFKIHYVSSPKHPNYKNIEKYLKPGWLFGQKVDSADFQYSAFRENMPILLLVIIVYNFLWRLVKLVFTKNTNDELAIKNNYRLCFSLLFALLVYGTGVIYVLTIALINYLISKSLKNSIFNPLLTWTLDISVVFFKEYFAYCKFSSLHPGLGFLDQYTGILERWYVLFNITMLRLVSFNMDYYWSLKHNSEKLNTLIFDKDREPTTLTFRERVDYSCLDEDYNLKNFLTYIFYAPLYLAGPIISFNNFMSQMKYPTVSTLKYRNLLYAIRFLVCVLTMEFLLHYAYVTAISKDGNWNQYSAVESAMISFIVLFMTWLKLLIPWRLFRLWSLIDDIEPPENIVRCMCNNYSAVGFWRAWHRSFNRWLIRYIYVPLGGSNHSILNLFIIFTFVALWHDISWELFAWGWLIVLFILPERLCCFMSRRTGLTKHPYYRYISGFGAALNIYFMIICNLIGFAVGIDGIKNVLVSFFLTLKGAMSAIAAFIMFFSAVQIMFQIRVNEEEEGINLRC | 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 integrity and apoptosis.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 68234
Sequence Length: 583
Subcellular Location: Cell membrane
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P53154 | MSLISILSPLITSEGLDSRIKPSPKKDASTTTKPSLWKTTEFKFYYIAFLVVVPLMFYAGLQASSPENPNYARYERLLSQGWLFGRKVDNSDSQYRFFRDNFALLSVLMLVHTSIKRIVLYSTNITKLRFDLIFGLIFLVAAHGVNSIRILAHMLILYAIAHVLKNFRRIATISIWIYGISTLFINDNFRAYPFGNICSFLSPLDHWYRGIIPRWDVFFNFTLLRVLSYNLDFLERWENLQKKKSPSYESKEAKSAILLNERARLTAAHPIQDYSLMNYIAYVTYTPLFIAGPIITFNDYVYQSKHTLPSINFKFIFYYAVRFVIALLSMEFILHFLHVVAISKTKAWENDTPFQISMIGLFNLNIIWLKLLIPWRLFRLWALLDGIDTPENMIRCVDNNYSSLAFWRAWHRSYNKWVVRYIYIPLGGSKNRVLTSLAVFSFVAIWHDIELKLLLWGWLIVLFLLPEIFATQIFSHYTDAVWYRHVCAVGAVFNIWVMMIANLFGFCLGSDGTKKLLSDMFCTVSGFKFVILASVSLFIAVQIMFEIREEEKRHGIYLKC | 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 deacylates, GUP1 subsequently reacylates the anchor lipid, thus replacing a shorter fatty acid (C16:0 or C18:0) by C26:0 . Also involved in lipid metabolism, having profound effects on sphingolipid-sterol-ordered domains integrity and assembly . Together with GUP2, has an influence on the chemical composition of the yeast extracellular matrix (yECM) in yeast multicellular aggregates, such as biofilms and colonies . Involved in cell integrity and apoptosis .
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 65340
Sequence Length: 560
Subcellular Location: Cell membrane
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E2RJI4 | MEATAGSETESGGDTVTAECANRIPVPRPPSIEEFTIVKPISRGAFGKVYLGQKGGKLYAVKVVKKADMINKNMTHQVQAERDALALSKSPFIVHLYYSLQSANNVYLVMEYLIGGDVKSLLHIYGYFDEEMAVKYISEVALALDYLHRHGIIHRDLKPDNMLISNEGHIKLTDFGLSKITLNRDIDINMMDILTTPSMAKPRQDYSRTPGQVLSLISSLRFYTPAAEKDKDSANILSTHVFETSQLSQGLICPMSVDHRDTTPYSSKLLHSCLETVTSDPGMPVKCLTSNLLQSRRRLATSSASSQSHTFLSSVESECHSSPRWEKDCQESDDALGSTVMSWNIIEKSSCTKSTDAIETKGFNKKDFELTLSPIHNSSIIPATGSSCVNLAKKCFPGEVSWEARELDINNVNVATDTTRCVFHQSDQWVVDPSDGTEEYCGKRGFKRNSELVDSSPCQNIIQNKKNCIEHKSRNEKSNGYINQRTSLTNEVQDLKLSVCESQQSDCANKENMVNSSIDKQQTPEKSPIPMIAKNLMCELDEDCNKNNKKFLSSSFLGSDDERASKSICMDSDSSFPGISIMESSLERQSLDPDKSIRESSFEESNIEDLLAVSPSWQENPLPKDDENLAVQASSQKMLASSSDVLKTLTLSKRNAVAFRSFNSHINASNNSEPSKMSVTSLDAMDISCVYSGSYPMAITPSQKGISYVPYQQTPNQVKSETPYRTPKSVRRGAAPVDDARILGTPDYLAPELLLGRAHGPAVDWWALGVCLFEFLTGIPPFNDETSQQVFQNILKRDIPWPEGEEKLSDNAQNAVEILLTIDNAKRAGIKELKCHPLFSDVDWENLQHQTMPFIPQPDDETDTSYFEARNNAQHLTVSGFSL | 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 ENSA at 'Ser-62' and 'Ser-67', respectively. ARPP19 and ENSA are phosphatase inhibitors that specifically inhibit the PPP2R2D (PR55-delta) subunit of PP2A. Inactivation of PP2A during M phase is essential to keep cyclin-B1-CDK1 activity high. Following DNA damage, it is also involved in checkpoint recovery by being inhibited (By similarity).
PTM: Phosphorylation at Thr-745 by CDK1 during M phase activates its kinase activity. Maximum phosphorylation occurs in prometaphase (By similarity).
Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Sequence Mass (Da): 98069
Sequence Length: 883
Subcellular Location: Cytoplasm
EC: 2.7.11.1
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Q96GX5 | MDPTAGSKKEPGGGAATEEGVNRIAVPKPPSIEEFSIVKPISRGAFGKVYLGQKGGKLYAVKVVKKADMINKNMTHQVQAERDALALSKSPFIVHLYYSLQSANNVYLVMEYLIGGDVKSLLHIYGYFDEEMAVKYISEVALALDYLHRHGIIHRDLKPDNMLISNEGHIKLTDFGLSKVTLNRDINMMDILTTPSMAKPRQDYSRTPGQVLSLISSLGFNTPIAEKNQDPANILSACLSETSQLSQGLVCPMSVDQKDTTPYSSKLLKSCLETVASNPGMPVKCLTSNLLQSRKRLATSSASSQSHTFISSVESECHSSPKWEKDCQESDEALGPTMMSWNAVEKLCAKSANAIETKGFNKKDLELALSPIHNSSALPTTGRSCVNLAKKCFSGEVSWEAVELDVNNINMDTDTSQLGFHQSNQWAVDSGGISEEHLGKRSLKRNFELVDSSPCKKIIQNKKTCVEYKHNEMTNCYTNQNTGLTVEVQDLKLSVHKSQQNDCANKENIVNSFTDKQQTPEKLPIPMIAKNLMCELDEDCEKNSKRDYLSSSFLCSDDDRASKNISMNSDSSFPGISIMESPLESQPLDSDRSIKESSFEESNIEDPLIVTPDCQEKTSPKGVENPAVQESNQKMLGPPLEVLKTLASKRNAVAFRSFNSHINASNNSEPSRMNMTSLDAMDISCAYSGSYPMAITPTQKRRSCMPHQQTPNQIKSGTPYRTPKSVRRGVAPVDDGRILGTPDYLAPELLLGRAHGPAVDWWALGVCLFEFLTGIPPFNDETPQQVFQNILKRDIPWPEGEEKLSDNAQSAVEILLTIDDTKRAGMKELKRHPLFSDVDWENLQHQTMPFIPQPDDETDTSYFEARNTAQHLTVSGFSL | 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 ENSA at 'Ser-62' and 'Ser-67', respectively. ARPP19 and ENSA are phosphatase inhibitors that specifically inhibit the PPP2R2D (PR55-delta) subunit of PP2A. Inactivation of PP2A during M phase is essential to keep cyclin-B1-CDK1 activity high. Following DNA damage, it is also involved in checkpoint recovery by being inhibited. Phosphorylates histone protein in vitro; however such activity is unsure in vivo. May be involved in megakaryocyte differentiation.
PTM: Phosphorylation at Thr-741 by CDK1 during M phase activates its kinase activity (By similarity). Maximum phosphorylation occurs in prometaphase.
Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Sequence Mass (Da): 97319
Sequence Length: 879
Subcellular Location: Cytoplasm
EC: 2.7.11.1
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Q6NTJ3 | MGIVAETSQNGDTSLCSEKKFTVPQPPSIEEFGIVKPISRGAFGKVYLARRKNNSKLFAVKVVKKADMINKNMVQQVQAERDALALSKSPFIVHLYYSLQSANNIYLVMEYLIGGDVKSLLHIYGYFDEEMAVKYISEVAMALDYLHRHGIIHRDLKPDNMLISNKGHIKLTDFGLSKVTLKRELCMMDILTTPSMAKPKRDYSRTPGQVLSLISSLGFNTPAGGRTQGSLNQQTEGMRGNASTPLLMKKRESLVKGNKLMISCPEASLSSPSIPVKCLTPNLLKCRTQFATSSTSSQSRICLSSLESECGSPRWENCSQDAEAPPYFNSSRVKDSSSEQARSKKPTGSSASQNLKRLEFAFSPIVDRRTGKKAGFQDETGELSDTPLATLNAKGVIRKCLYENKAQEKPKDFDKTGQGELGKFTSSPDSPPWLANGSVAPIQFNDEEKTEKMGVKRNYDLVEKSPEQELLQDKKTNTDYKRGCAITDYPVSQSTGLTMEINSLFLSELRNSANKYASDRKSEDKYISAPRTLEKLDSGNPVAKNLLCELDDNCERDGEVSSTSEGEDRKERLNQDSSSTGMSVTENQIDRDLSHVDKSIKELSFEESQSENSEEITPDNKGIPFMAENDERVQSKYEPNTSILPDSLQNVLASPAPASAMTNPRRKPMVAFRSYNSPINVSNVSEPSKISMNSADKIHFSLECTGSFPMAVTPAQNKVQGLIETPYRTPKSVRRGGIQVDHERILGTPDYLAPELLLRKSHGPAVDWWALGVCLFEFLTGIPPFNDETPSQVFQNILNRDIPWPEEEEEVLSVNAQSAIEILLTIDPTKRAGLKDLKAHPLFHGMEWEELQYQPMSFIPQPDDETDTTYFEARNNAQHLKVSGFSL | 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 ensa at 'Ser-67', 2 phosphatase inhibitors that specifically inhibit the ppp2r2d (PR55-delta) subunit of PP2A. Inactivation of PP2A during M phase is essential to keep cyclin-B1-CDK1 activity high. Following DNA damage, it is also involved in checkpoint recovery by being inhibited.
PTM: Phosphorylation at Thr-748 by CDK1 during M phase activates its kinase activity. Not active during other phases of the cell cycle. Has the ability to autophosphorylate.
Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Sequence Mass (Da): 98683
Sequence Length: 887
Subcellular Location: Cytoplasm
EC: 2.7.11.1
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Q873N1 | MDPDYKARKEAFVSGLAGGSILEINAVTLVASVSVFLWSILQSRLSFFTPYSAAALLVDFLLNVLAILFATTLYSSAPLLLNLLLISPALLILLSTKRPRTPVKAKPPRQSARAGKDDSKHATALPESLPIHPFLTTYRAAMMVITCIAILAVDFRIFPRRFAKVENWGTSLMDLGVGSFVFSGGVVSARSLLKSRINGSKRLPLAKRLIASTRHSIPLLVLGLIRLYSVKGLDYAEHVTEYGVHWNFFFTLGLLPPFVEVFDALATIIPSYEVLSVGIAVLYQVALESTDLKSYILVSPRGPSLLSKNREGVFSFSGYLAIFLAGRAIGIRIIPRGTSFSRSPEQARRRVLISLGVQALVWTTLFVLNSTYAMGYGANIPVSRRLANMPYVLWVSAFNTAQLFVFCLIETLCFPAVHRTTTQESESERVDFATSRIMSAFNKNSLAIFLLANLLTGAVNLSISTIDANTAQAIAVLIGYSSIITGVALALHHANIKVLPF | 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.
Subcellular Location: Endoplasmic reticulum membrane
EC: 2.3.-.-
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Q873N2 | MSSSLKQLKEQFVSDLTGGTIEEIYAVTSIALSSYLSFRLLKKSLGDLALIYDYILNVLTILASITVYSNSPSYLHYFIVIPSLVIYLVNYHVEKPSSPHRQNDTKEDKSDELLPRKQFITAYRSQMLIITNLAILAVDFPIFPRRFAKVETWGTSMMDLGVGSFVFSMGLANSRQLIKNHTDNYKFSWKSYLKTIKQNFIKSVPILVLGAIRFVSVKQLDYQEHETEYGIHWNFFFTLGFLPIVLGILDPVLNLVPRFIIGIGISIAYEVALNKTGLLKFILSSENRLESLITMNKEGIFSFIGYLCIFIIGQSFGSFVLTGYKTKNNLITISKIRISKKQHKKESSSFFSVATTQGLYLACIFYHLAFSLFISNLSFLQPISRRLANFPYVMWVVSYNATFLLCYDLIEKFIPGNLTSTVLDSINNNGLFIFLVSNLLTGFINMSINTLETSNKMAVIILIGYSLTWTLLALYLDKRKIYIKL | 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.
Subcellular Location: Endoplasmic reticulum membrane
EC: 2.3.-.-
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P0CP65 | MGDYKLAKEAFVSGNPGASIWSINAVSLVALATYALWIALSPYIRHGLLNNYLICVLPLLLGVTIFSTSPLVFASFLSIISLFFIAKSQKRFNFPRSPEKPKGQWLDESDSDEEPAEPASAAGSAAVSPAKLLPSQVAFASGSLLSTDPTISPMSPSSSSSSGHEDPLGIMGVNRRRSPLEGVSLDVPSHIDSKVRISPVPSLRLKKSRATKVQGVEEKGRLPFLTVYRAHMMLMTVICILAVDFEVFPRWQGKCEDFGTSLMDVGVGSFVFSLGLVSTKSLSPPPPPPTPTSPALNSHIIPLTPSPLSFILISLRKSVPVLVLGFIRLIMVKGSDYPEHVTEYGVHWNFFFTLALVPVLAVGVRPLTQWLRWSVLGVIISLLHQLCLTYYLQPIIFSFGRSGIFLANKEGFSSLPGYLSIFLIGLSIGDHVLRLSLPPRRERVVSETIEEHEQSHFERKKLDLIMELIGYSLGWWALLGGWIWAGGEVSRRLANAPYVFWVAAYNTTFLLGYLLLTHIIPSSISSQTSPSILVPRLLDAMNKNGLAVFLAANLLTGLVNVSMETMYAPAWLSMGVLMLYSLAVSCVGWVLKGRSIKI | 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.
Subcellular Location: Endoplasmic reticulum membrane
EC: 2.3.-.-
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P13364 | MSENQTYDSSSIKVLKGLDAVRKRPGMYIGDTDDGSGLHHMVFEVVDNSIDEALAGHCDDITVIIHTDESISVRDNGRGIPVDVHKEEGVSAAEVIMTVLHAGGKFDDNSYKVSGGLHGVGVSVVNALSEKLVLTVRRSGKIWEQTYVHGVPQAPMAVVGESETTGTHIHFKPSAETFKNIHFSWDILAKRIRELSFLNSGVGILLKDERSGKEEFFKYEGGLRAFVEYLNTNKTPVNSQVFHFSVQREDGVGVEVALQWNDSFNENLLCFTNNIPQRDGGTHLVGFRSSLTRSLNSYIEQEGLAKKNKVATTGDDAREGLTAIISVKVPDPKFSSQTKDKLVSSEVKTAVEQEMNKYFSDFLLENPNEAKAVVGKMIDAARAREAARKAREMTRRKGALDIAGLPGKLADCQEKDPALSELYLVEGDSAGGSAKQGRNRRTQAILPLKGKILNVEKARFDKMISSQEVGTLITALGCGIGREEYNIDKLRYHNIIIMTDADVDGSHIRTLLLTFFFRQLPELVERGYIYIAQPPLYKVKKGKQEQYIKDDEAMEEYMTQSALEDASLHLDESAPAVSGVQLESLVNEFRSVMKTLKRLSRLYPEELTEHFVYLPEVTLEQLGDHAVMQAWLAKLQERLNSSQKSGLAYNASLREDKERNVWLPEVEITSHGLASYITFNRDFFGSNDYRTVVNIGAKLSSLLGEGAYVQRGERRKAIVEFKEGLDWLMNETTKRHTIQRYKGLGEMNPDQLWETTMDPTVRRMLKVTIEDAIAADQIFNTLMGDAVEPRREFIESNALSVSNLDF | 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 modulate DNA topology and maintain chromosomes in an underwound state. Negative supercoiling favors strand separation, and DNA replication, transcription, recombination and repair, all of which involve strand separation. Also able to catalyze the interconversion of other topological isomers of dsDNA rings, including catenanes and knotted rings. Type II topoisomerases break and join 2 DNA strands simultaneously in an ATP-dependent manner.
Catalytic Activity: ATP-dependent breakage, passage and rejoining of double-stranded DNA.
Sequence Mass (Da): 90078
Sequence Length: 806
Subcellular Location: Cytoplasm
EC: 5.6.2.2
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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 which involve strand separation. Also able to catalyze the interconversion of other topological isomers of dsDNA rings, including catenanes and knotted rings. Type II topoisomerases break and join 2 DNA strands simultaneously in an ATP-dependent manner.
Catalytic Activity: ATP-dependent breakage, passage and rejoining of double-stranded DNA.
Sequence Mass (Da): 14961
Sequence Length: 134
Subcellular Location: Cytoplasm
EC: 5.6.2.2
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Q9ZCX2 | MSVIEEKCNESSYSADSIKVLKGLEAVRKRPGMYIGDVGDGSGLHHMIYEVVDNSIDEALAGYCDLVQVTLNKNGSVTVSDNGRGIPVEIHEEEGISAAEVIMTQLHAGGKFDQQSYKISGGLHGVGVSVVNALSEWLELRIWRNNKEYFIRFNNGITEAPLSIVKENIDKKGTEVTFFPSVGTFTNIEFDFVTIEHRLRELAFLNSGVKILLVDNRFEEVKKVEFYYTGGIEAYVQYIDRAKHAIHPCIVVNTVHVESGISLELALHWNDSYHENILCFTNNIRQRDGGTHLSAFKSAITRVITSYLDTTGLNKKTKHDFSGEDTREGICCVLSVKVPDPKFSSQTKDKLVSSEVRPVVENAVYTKVLEWFEEHPTEAKAIIAKIMEAANAREAARKARELTRRKSALEVSNLPGKLADCHAKDPAISELFIVEGDSAGGTAKQGRDSKIQAILPLRGKILNVERARFDKMLGSDQIGTLITALGISVEREFSLEKLRYHKVIIMTDADVDGSHIRALLLTFFYRHMPELINKGYLYIAQPPLYKVKSGASELYLKNEKALQNYLIKSTINDTYLILDGQEQLVGENLEDLINKVVKFNNLLDHVSKKFNRSITEILAINDLFNKKIFEPESSARLQKALDILNNLEESPDKTNLQVLKHENKIEFFHFSRGLKETKILLKEQLELFEFVEISQFALSIFDIFSKRLKLIVKSKAFDILTPSQLLNTIIECGKKGITIQRFKGLGEMNSDQLWETTLDPTKRTLLQVRVAEVDEAEGIFSTLMGDVVEPRRLFIQANALNVMNLDV | 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 modulate DNA topology and maintain chromosomes in an underwound state. Negative supercoiling favors strand separation, and DNA replication, transcription, recombination and repair, all of which involve strand separation. Also able to catalyze the interconversion of other topological isomers of dsDNA rings, including catenanes and knotted rings. Type II topoisomerases break and join 2 DNA strands simultaneously in an ATP-dependent manner.
Catalytic Activity: ATP-dependent breakage, passage and rejoining of double-stranded DNA.
Sequence Mass (Da): 90823
Sequence Length: 807
Subcellular Location: Cytoplasm
EC: 5.6.2.2
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P34031 | MGDNYNSESIQILEGLEAIRKRPGMYIGATNARGLHHLVWEIVDNSIDEVLANFANKIKIILNKDESITVIDNGRGIPIEIHPKTKVSTLETVFTILHAGGKFDSNTYKISGGLHGVGASVVNALSKYLKVEVRKNNKKYVMEFHNGGQILTPIKEVGSTSETGTTVTFLPDEKIFKETTIFSFSTIQNRIKQLVFLNKGLEISLVDLREEDEEKTVLYQFNNGIKDYVLELNKTIGTPLNDVFYVEGIEDNIVVEFGLQYNDNYSENIFSFCNNINTHEGGTHEEGARLAIVREINNYFKNQINKNNKGNEDKFTWDDIKEGMTIIISIRHPEPQYEGQTNQKLLNSEVKKIVSNIVGKGLSSYLLENPEDAKKIIEKISLSLKATIVAQRAKEITRRKIVMDSFSLPGKLSDCETKDAKIAELYIVEGDSAGGSAKSGRNRKFQAILPLRGKILNVEKAKQIKIFENNEINSIITALGAGIKDNFNDKKLRYQKVIIMTDADVDGAHIRILLLTFFYRYMKDLIENGNIYIAQPPLYKVENSNQIRYVYSDNELELYKEELLKQNKNYTIQRYKGLGEMNPEQLWETTMDPERRLLLKVSVNNAFEANLICNELMGENVEPRKKFIRENAKYVKNLDV | 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 modulate DNA topology and maintain chromosomes in an underwound state. Negative supercoiling favors strand separation, and DNA replication, transcription, recombination and repair, all of which involve strand separation. Also able to catalyze the interconversion of other topological isomers of dsDNA rings, including catenanes and knotted rings. Type II topoisomerases break and join 2 DNA strands simultaneously in an ATP-dependent manner.
Catalytic Activity: ATP-dependent breakage, passage and rejoining of double-stranded DNA.
Sequence Mass (Da): 72763
Sequence Length: 640
Subcellular Location: Cytoplasm
EC: 5.6.2.2
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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 regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling.
Sequence Mass (Da): 15704
Sequence Length: 149
Domain: Contains one SPKK motif which may interact with the minor groove of A/T-rich DNA sites. Phosphorylation of this motif may regulate DNA binding. This motif is reiterated in both termini of histone H1 and in the N-terminus of sea urchin histones H2B, but its presence in the C-terminus seems to be unique to plant H2A.
Subcellular Location: Nucleus
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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, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling.
PTM: Phosphorylated to form H2AS128ph (gamma-H2A) in response to DNA double-strand breaks (DSBs) generated by exogenous genotoxic agents and by stalled replication forks. Phosphorylation is dependent on the DNA damage checkpoint kinases MEC1/ATR and TEL1/ATM, spreads on either side of a detected DSB site and may mark the surrounding chromatin for recruitment of proteins required for DNA damage signaling and repair. Gamma-H2A is removed from the DNA prior to the strand invasion-primer extension step of the repair process and subsequently dephosphorylated. Dephosphorylation is necessary for efficient recovery from the DNA damage checkpoint (By similarity).
Sequence Mass (Da): 13897
Sequence Length: 130
Domain: The [ST]-Q motif constitutes a recognition sequence for kinases from the PI3/PI4-kinase family.
Subcellular Location: Nucleus
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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, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling.
PTM: Phosphorylated to form H2AS128ph (gamma-H2A) in response to DNA double-strand breaks (DSBs) generated by exogenous genotoxic agents and by stalled replication forks. Phosphorylation is dependent on the DNA damage checkpoint kinases rad3/ATR and tel1/ATM, spreads on either side of a detected DSB site and may mark the surrounding chromatin for recruitment of proteins required for DNA damage signaling and repair. Gamma-H2A is required for recruiting crb2, a modulator of DNA damage checkpoint signaling, to DSB sites. Gamma-H2A is removed from the DNA prior to the strand invasion-primer extension step of the repair process and subsequently dephosphorylated. Dephosphorylation is necessary for efficient recovery from the DNA damage checkpoint.
Sequence Mass (Da): 13776
Sequence Length: 131
Domain: The [ST]-Q motif constitutes a recognition sequence for kinases from the PI3/PI4-kinase family.
Subcellular Location: Nucleus
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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 regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling.
PTM: Phosphorylated within its C-terminal part, probably at the SPKK motifs.
Sequence Mass (Da): 16013
Sequence Length: 151
Domain: Contains 2 SPKK motifs which may interact with the minor groove of A/T-rich DNA sites. Phosphorylation of this motif may regulate DNA binding. This motif is reiterated in both termini of histone H1 and in the N-terminus of sea urchin histones H2B, but its presence in the C-terminus seems to be unique to plant H2A.
Subcellular Location: Nucleus
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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 regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling.
PTM: Monoubiquitination of Lys-120 (H2AK119Ub) gives a specific tag for epigenetic transcriptional repression. Following DNA double-strand breaks (DSBs), it is ubiquitinated through 'Lys-63' linkage of ubiquitin moieties, leading to the recruitment of repair proteins to sites of DNA damage. H2AK119Ub and ionizing radiation-induced 'Lys-63'-linked ubiquitination are distinct events (By similarity).
Sequence Mass (Da): 14000
Sequence Length: 130
Subcellular Location: Nucleus
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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 regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling.
PTM: Not ubiquitinated.
Sequence Mass (Da): 13833
Sequence Length: 131
Subcellular Location: Nucleus
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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 regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling.
PTM: Monoubiquitination of Lys-120 (H2AK119Ub) gives a specific tag for epigenetic transcriptional repression. Following DNA double-strand breaks (DSBs), it is ubiquitinated through 'Lys-63' linkage of ubiquitin moieties, leading to the recruitment of repair proteins to sites of DNA damage. H2AK119Ub and ionizing radiation-induced 'Lys-63'-linked ubiquitination are distinct events (By similarity).
Sequence Mass (Da): 13966
Sequence Length: 129
Subcellular Location: Nucleus
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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 regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling.
PTM: Deiminated on Arg-4 in granulocytes upon calcium entry.
Sequence Mass (Da): 14121
Sequence Length: 130
Subcellular Location: Nucleus
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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 regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling.
PTM: Monoubiquitination of Lys-119 gives a specific tag for epigenetic transcriptional repression.
Sequence Mass (Da): 13411
Sequence Length: 126
Subcellular Location: Nucleus
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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 regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling.
PTM: Not ubiquitinated.
Sequence Mass (Da): 15966
Sequence Length: 150
Domain: Contains one SPKK motif which may interact with the minor groove of A/T-rich DNA sites. Phosphorylation of this motif may regulate DNA binding. This motif is reiterated in both termini of histone H1 and in the N-terminus of sea urchin histones H2B, but its presence in the C-terminus seems to be unique to plant H2A.
Subcellular Location: Nucleus
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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 regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling.
PTM: Not ubiquitinated.
Sequence Mass (Da): 13200
Sequence Length: 118
Subcellular Location: Nucleus
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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 role in transcription regulation, DNA repair, DNA replication and chromosomal stability. Nucleosomes containing this histone are less rigid and organize less DNA than canonical nucleosomes in vivo. They are enriched in actively transcribed genes and associate with the elongating form of RNA polymerase. They associate with spliceosome components and are required for mRNA splicing. May participate in spermatogenesis.
Sequence Mass (Da): 12713
Sequence Length: 115
Domain: The docking domain is responsible for the weaker heterodimerization with H2B.
Subcellular Location: Nucleus
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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 regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling.
PTM: Monoubiquitination of Lys-120 (H2AXK119ub) gives a specific tag for epigenetic transcriptional repression. Following DNA double-strand breaks (DSBs), it is ubiquitinated through 'Lys-63' linkage of ubiquitin moieties (By similarity).
Sequence Mass (Da): 14016
Sequence Length: 129
Subcellular Location: Nucleus
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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 regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling.
PTM: Monoubiquitination of Lys-120 (H2AXK119ub) gives a specific tag for epigenetic transcriptional repression. Following DNA double-strand breaks (DSBs), it is ubiquitinated through 'Lys-63' linkage of ubiquitin moieties (By similarity).
Sequence Mass (Da): 14019
Sequence Length: 129
Subcellular Location: Nucleus
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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 regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling.
PTM: Monoubiquitination of Lys-120 (H2AXK119ub) gives a specific tag for epigenetic transcriptional repression. Following DNA double-strand breaks (DSBs), it is ubiquitinated through 'Lys-63' linkage of ubiquitin moieties (By similarity).
Sequence Mass (Da): 13989
Sequence Length: 129
Subcellular Location: Nucleus
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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 regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling.
PTM: Monoubiquitination of Lys-120 (H2AXK119ub) gives a specific tag for epigenetic transcriptional repression. Following DNA double-strand breaks (DSBs), it is ubiquitinated through 'Lys-63' linkage of ubiquitin moieties (By similarity).
Sequence Mass (Da): 14045
Sequence Length: 129
Subcellular Location: Nucleus
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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 stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling. This variant is enriched at promoters, it may keep them in a repressed state until the appropriate activation signal is received. Near telomeres, it may counteract gene silencing caused by the spread of heterochromatin proteins. Required for the RNA polymerase II and SPT15/TBP recruitment to the target genes. Involved in chromosome stability (By similarity).
PTM: Acetylated once deposited into chromatin.
Sequence Mass (Da): 14888
Sequence Length: 138
Subcellular Location: Nucleus
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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 and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling. May be involved in the formation of constitutive heterochromatin. May be required for chromosome segregation during cell division.
PTM: Monoubiquitination of Lys-122 gives a specific tag for epigenetic transcriptional repression.
Sequence Mass (Da): 13553
Sequence Length: 128
Subcellular Location: Nucleus
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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 stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling. This variant is enriched at promoters, it may keep them in a repressed state until the appropriate activation signal is received. Near telomeres, it may counteract gene silencing caused by the spread of heterochromatin proteins. Required for the RNA polymerase II and SPT15/TBP recruitment to the target genes. Involved in chromosome stability (By similarity).
PTM: Acetylated once deposited into chromatin.
Sequence Mass (Da): 14342
Sequence Length: 132
Subcellular Location: Nucleus
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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 regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling.
PTM: Monoubiquitination at Lys-35 (H2BK34Ub) by the MSL1/MSL2 dimer is required for histone H3 'Lys-4' (H3K4me) and 'Lys-79' (H3K79me) methylation and transcription activation at specific gene loci, such as HOXA9 and MEIS1 loci. Similarly, monoubiquitination at Lys-121 (H2BK120Ub) by the RNF20/40 complex gives a specific tag for epigenetic transcriptional activation and is also prerequisite for histone H3 'Lys-4' and 'Lys-79' methylation. It also functions cooperatively with the FACT dimer to stimulate elongation by RNA polymerase II. H2BK120Ub also acts as a regulator of mRNA splicing: deubiquitination by USP49 is required for efficient cotranscriptional splicing of a large set of exons.
Sequence Mass (Da): 13906
Sequence Length: 126
Subcellular Location: Nucleus
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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 regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling.
PTM: Monoubiquitination at Lys-35 (H2BK34Ub) by the MSL1/MSL2 dimer is required for histone H3 'Lys-4' (H3K4me) and 'Lys-79' (H3K79me) methylation and transcription activation at specific gene loci, such as HOXA9 and MEIS1 loci. Similarly, monoubiquitination at Lys-121 (H2BK120Ub) by the RNF20/40 complex gives a specific tag for epigenetic transcriptional activation and is also prerequisite for histone H3 'Lys-4' and 'Lys-79' methylation. It also functions cooperatively with the FACT dimer to stimulate elongation by RNA polymerase II. H2BK120Ub also acts as a regulator of mRNA splicing: deubiquitination by USP49 is required for efficient cotranscriptional splicing of a large set of exons (By similarity).
Sequence Mass (Da): 13992
Sequence Length: 126
Subcellular Location: Nucleus
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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 regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling.
PTM: Can be acetylated to form H2BK6ac, H2BK33ac and H2BK34ac.
Sequence Mass (Da): 16402
Sequence Length: 148
Subcellular Location: Nucleus
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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 regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling.
PTM: Monoubiquitination of Lys-117 gives a specific tag for epigenetic transcriptional activation and is also prerequisite for histone H3 'Lys-4' and 'Lys-79' methylation.
Sequence Mass (Da): 13501
Sequence Length: 122
Subcellular Location: Nucleus
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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 regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling.
PTM: Monoubiquitination of Lys-121 by the BRE1 gives a specific tag for epigenetic transcriptional activation and is also prerequisite for histone H3 'Lys-4' and 'Lys-79' methylation.
Sequence Mass (Da): 13922
Sequence Length: 126
Subcellular Location: Nucleus
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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 regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling.
PTM: Monoubiquitination of Lys-119 by the BRE1 gives a specific tag for epigenetic transcriptional activation and is also prerequisite for histone H3 'Lys-4' and 'Lys-79' methylation.
Sequence Mass (Da): 13578
Sequence Length: 124
Subcellular Location: Nucleus
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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 regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling.
PTM: Monoubiquitination at the C-terminal Lys gives a specific tag for epigenetic transcriptional activation and is also prerequisite for histone H3 'Lys-4' and 'Lys-79' methylation.
Sequence Mass (Da): 2166
Sequence Length: 21
Subcellular Location: Nucleus
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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 regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling.
PTM: Can be acetylated to form H2BK6ac and H2BK33ac.
Sequence Mass (Da): 17249
Sequence Length: 158
Subcellular Location: Nucleus
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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 regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling.
PTM: Monoubiquitination of Lys-110 gives a specific tag for epigenetic transcriptional activation and is also prerequisite for histone H3 'Lys-4' and 'Lys-79' methylation.
Sequence Mass (Da): 12662
Sequence Length: 114
Subcellular Location: Nucleus
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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 regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling.
PTM: Monoubiquitination of Lys-119 by BRE1 gives a specific tag for epigenetic transcriptional activation and is also prerequisite for histone H3 'Lys-4' and 'Lys-79' methylation.
Sequence Mass (Da): 13596
Sequence Length: 124
Subcellular Location: Nucleus
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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 regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling.
PTM: Monoubiquitination of Lys-117 gives a specific tag for epigenetic transcriptional activation and is also prerequisite for histone H3 'Lys-4' and 'Lys-79' methylation.
Sequence Mass (Da): 13466
Sequence Length: 122
Subcellular Location: Nucleus
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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 regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling.
PTM: Can be acetylated to form H2BK6ac, H2BK33ac and H2BK34ac.
Sequence Mass (Da): 13471
Sequence Length: 120
Subcellular Location: Nucleus
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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 regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling.
PTM: Monoubiquitination gives a specific tag for epigenetic transcriptional activation and is also prerequisite for histone H3 'Lys-4' and 'Lys-79' methylation.
Sequence Mass (Da): 12775
Sequence Length: 116
Subcellular Location: Nucleus
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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 regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling.
PTM: Monoubiquitinated by BRE1 to form H2BK123ub1. H2BK123ub1 gives a specific tag for epigenetic transcriptional activation and is also prerequisite for H3K4me and H3K79me formation. H2BK123ub1 also modulates the formation of double-strand breaks during meiosis and is a prerequisite for DNA-damage checkpoint activation (By similarity).
Sequence Mass (Da): 15151
Sequence Length: 140
Subcellular Location: Nucleus
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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 regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling.
PTM: Monoubiquitination of Lys-118 gives a specific tag for epigenetic transcriptional activation and is also prerequisite for histone H3 'Lys-4' and 'Lys-79' methylation.
Sequence Mass (Da): 13638
Sequence Length: 123
Subcellular Location: Nucleus
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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 regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling.
PTM: Monoubiquitinated to form H2BK123ub1. H2BK123ub1 gives a specific tag for epigenetic transcriptional activation and is also prerequisite for H3K4me and H3K79me formation. H2BK123ub1 also modulates the formation of double-strand breaks during meiosis and is a prerequisite for DNA-damage checkpoint activation (By similarity).
Sequence Mass (Da): 14798
Sequence Length: 136
Subcellular Location: Nucleus
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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 regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling.
PTM: Phosphorylated to form H3S10ph. H3S10ph promotes subsequent H3K14ac formation and is required for transcriptional activation through TBP recruitment to the promoters (By similarity).
Sequence Mass (Da): 15342
Sequence Length: 136
Subcellular Location: Nucleus
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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 regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling.
PTM: Acetylation is generally linked to gene activation. Can be acetylated to form H3K9ac, H3K14ac, H3K18ac and H3K23ac. H3K9ac could compete with H3K9me and prevent gene silencing. H3K9ac is restricted to euchromatin (By similarity).
Sequence Mass (Da): 15284
Sequence Length: 136
Subcellular Location: Nucleus
|
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, suggesting that it represents an epigenetic imprint of transcriptionally active chromatin. 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 regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling.
PTM: Acetylation is generally linked to gene activation.
Sequence Mass (Da): 15360
Sequence Length: 136
Subcellular Location: Nucleus
|
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, suggesting that it represents an epigenetic imprint of transcriptionally active chromatin. 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 regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling.
PTM: Acetylation is generally linked to gene activation. Can be acetylated to form H3K9ac, H3K14ac, H3K18ac and H3K23ac. H3K9ac could compete with H3K9me and prevent gene silencing. H3K9ac is restricted to euchromatin (By similarity).
Sequence Mass (Da): 15378
Sequence Length: 136
Subcellular Location: Nucleus
|
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 regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling.
PTM: Acetylation is generally linked to gene activation.
Sequence Mass (Da): 15560
Sequence Length: 136
Subcellular Location: Nucleus
|
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, suggesting that it represents an epigenetic imprint of transcriptionally active chromatin. 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 regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling.
PTM: Acetylation is generally linked to gene activation. Can be acetylated to form H3K9ac, H3K14ac, H3K18ac and H3K23ac. H3K9ac could compete with H3K9me and prevent gene silencing. H3K9ac is restricted to euchromatin (By similarity).
Sequence Mass (Da): 15616
Sequence Length: 137
Subcellular Location: Nucleus
|
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