ids stringlengths 6 10 | seqs stringlengths 11 1.02k | texts stringlengths 108 11.1k |
|---|---|---|
O43761 | MEGASFGAGRAGAALDPVSFARRPQTLLRVASWVFSIAVFGPIVNEGYVNTDSGPELRCVFNGNAGACRFGVALGLGAFLACAAFLLLDVRFQQISSVRDRRRAVLLDLGFSGLWSFLWFVGFCFLTNQWQRTAPGPATTQAGDAARAAIAFSFFSILSWVALTVKALQRFRLGTDMSLFATEQLSTGASQAYPGYPVGSGVEGTETYQSPPFTETLDTSPKGYQVPAY | Function: May play a role in regulated exocytosis. May indirectly regulate the activity of the plasma membrane dopamine transporter SLC6A3 and thereby regulate dopamine transport back from the synaptic cleft into the presynaptic terminal.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 24555
Sequence... |
Q8R191 | MEGASFGAGRAGAAFDPVSFARRPQTLLRVVSWVFSIAVFGPIVNEGYVNSDSGPELRCVFNGNAGACRFGVVLGLGAFIACVAFLLLDVRFQQISSVRDRRRAVLLDLGFSGVWSFLWFVGFCFLTNQWQRTTPGPGTAQAGDAARAAIAFSFFSILSWVALTVKALQRFRLGTDMSLFATDQLGTGAAQAYPGYPVGSGVEGTETYQSPPFTETLDTSSKGYQVPAY | Function: May play a role in regulated exocytosis . May indirectly regulate the activity of the plasma membrane dopamine transporter SLC6A3 and thereby regulate dopamine transport back from the synaptic cleft into the presynaptic terminal .
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 24561
Sequen... |
Q7JYV2 | MDMLNQILSINNGGAYGGGKAGGAFDPLTFAMKPQVVIRALCWLFSVVVFGCISSEGWTEKDGKEYCLYNGDGMACKYGNMVGVFGFLASMGFMGGEFLFERMSSVKSRKRYVMADMGFSALWTFMYFVAFLYLWSQWSSSAPPPLGIGAGSMKTAIWFCLFSIVSWALCALMAYKRFLIGAGDEFTSAFETDPANVVHQQAYGYSMDNDNDQYSASPFGQPQQGGMEQQQSGMEYQQPTY | Function: Required for the correct formation of synaptic vesicles at nerve terminals and has a role in the regulation of the synaptic vesicle exo-endocytic cycle.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 26610
Sequence Length: 241
Subcellular Location: Cytoplasmic vesicle membrane
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Q08826 | MPREFKSFGSTEKSLLSKGHGEPSYSEIYAEPENFLEIEVHNPKTHIPNGMDSKGMFTDYEIICRTNLPSFHKRVSKVRRRYSDFEFFRKCLIKEISMLNHPKVMVPHLPGKILLSNRFSNEVIEERRQGLNTWMQSVAGHPLLQSGSKVLVRFIEAEKFVG | Function: Required for retention of late Golgi membrane proteins. Component of the retrieval machinery that functions by direct interaction with the cytosolic tails of certain TGN membrane proteins during the sorting/budding process at the prevacuolar compartment. Binds phosphatidylinositol 3-phosphate (PtdIns(P3)).
Lo... |
Q759T1 | MNSFRESDEEDNNPFSGTNHLYASGIGAVPEGDDDFLSAEVDTADETVQETREQMMSRLFGECEGPRESSAGGWTSGSMGSIGAPDGHSDEVTEFGIDTVLVEGEVRTPGRARVPASYPDAEGSLGALRIVDAGQYKDTFGNYAIGYTIAYEGRQVTRRYSEFDSLRQALARLLPTVIIPPIPSKHPLIRYFLNPLNAENDIRIIEKRRRLLSRFLNNCHDITDIREHTVFQKFLNPEYIWSEVLLTPPVSILPTNNLLAPPLNPTKPSPLHLLLPTPPRRTTSYGSPKTNNPEYDIRFTELESLLLRYHKCLQPVLASS... | Function: May be required for cytoplasm to vacuole transport (Cvt) and pexophagy.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 68638
Sequence Length: 603
Domain: The PX domain binds phosphatidylinositol 3-phosphate which is necessary for peripheral membrane localization to the perivacuolar punctat... |
Q5AD73 | MSTDNLFEDIEQDNNPSFYGNPSILNDPYRPIQPPPPQQQQQQHQENESKQSHTKSPKPPLQSIHSGTSNAHPQSQPQHKHKHKHNTSLNNGYPNELVNSTIGLSNRILELLNDSQLQVDIINSEKLVNSSVIVYTIELSSPTTKIVVKRRYSEFKSLRDNLLKLFPTLIIPPIPEKHSILSYLLNTINHSHEISIIEMRKRYFKMFLDDLIFQSDYKLKNCPLLHKFFDPNYELCWYNALNEPPVSLIPDNLLLANPINPADQNGLYSLLPIVNGFDFNSHIDNLSNLKKINEDLYKLNDQVKLYELKGFEQDLEFSIP... | Function: May be required for cytoplasm to vacuole transport (Cvt) and pexophagy.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 78368
Sequence Length: 681
Domain: The PX domain binds phosphatidylinositol 3-phosphate which is necessary for peripheral membrane localization to the perivacuolar punctat... |
P0CR64 | MDSDTSPNPFASSPPSSPSPRPSLPPPVPRKPSSLVSAASGSPPPTHRASFPDPARHPKMGATVPGPKPKTGYCCSIDKDISAGEQVHIVDALKTTEGGTASYITYVIRLGTHTVRRRYSAFLSLHQSLTGLYPVLIIPPIPSKQSLTDYAVKGQSKAREDATIIARRKRLLEDFLQRLIRHPILGGEHVLHRFLEEDVSWSEVLHSPPISLLSKNPLHAPSHNPTFQPTTPTSPSEAPATTSYIAHHLLPTPSPSHPLRQPDQRFMDSEAFTEKFQSHFSGTMEKVNRRVTKRWGERAHDMSELGGIWNGFSLVEQGKL... | Function: May be required for cytoplasm to vacuole transport (Cvt) and pexophagy.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 70714
Sequence Length: 638
Domain: The PX domain binds phosphatidylinositol 3-phosphate which is necessary for peripheral membrane localization to the perivacuolar punctat... |
Q6CWX3 | MNVFDGSDEEDNNPFSGTTHLYASGIAAVTDGPDDYDFTEPSINGSSDENAQSNAVAEPIEETDEPAEEIDDDTLQTWRFASAELSRSSAFETSYTNLLGQGKNPEVIRIVDAGQYRDIYGKYAIGYKIEFGGIVVTRRYSEFDSLRQSLCRLLPTIIIPPIPSKHPIIKYLFNPLHAKKDIKIIERRQRLLSRFLNNCHKVREIRNHIVFQKFLNPEYFWKEVLNTPPISILPMNNLLAPPLNPTKPSPIHLLLPTPTVLTMRKHEQLIGRNDVMEIKFADYDSDLIRYKAILQPLNKTVRSIRSNIQTYSAVLSELGA... | Function: May be required for cytoplasm to vacuole transport (Cvt) and pexophagy.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 65900
Sequence Length: 575
Domain: The PX domain binds phosphatidylinositol 3-phosphate which is necessary for peripheral membrane localization to the perivacuolar punctat... |
O60107 | MDFFEDNNPFSGSDNRSASSAVNVEPKVEPSQHQGSSSVKENAISQPNESFQSRNMFFQKDVDSVVDSALDPNGIVITGAMKAESGSHIVYIIKLQDSEIHHRYSEFASLRVQLSRLYPTCLVPPLPDKHKIMDYLINVTKNQRMSRMLEERKRLLQLFLRRVAQHPILGLSEVFRKFLSRHVSWKEVLHSPPISCLPKDLLKAPPADPSSKENAELYKELPIPSKTLVPRDNYDDVGKNFLMLEDTLQQYSIVAQEESNLFNQIVLSNSKYCLAHSTLGAMFNALSLSESGKLLTALEKVGQANDHTCLASIDFMHNFV... | Function: May be required for cytoplasm to vacuole transport (Cvt) and pexophagy (By similarity). Has a role in meiosis.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 67002
Sequence Length: 586
Domain: The PX domain binds phosphatidylinositol 3-phosphate which is necessary for peripheral membrane l... |
Q6C9X0 | MSDFEDNNPFAGADRRDSVSSDATDDGPSASFLATNTTNDFGGASFMAGGGSFYGAASQIGGLGGMGMSAYDPESALANPFDDGSNSFSATPTASITNQNDTAHEATNERTTTASQSNIPPIEIIEANKNHEGTSRGFITYTIRVGDVSVRRRYSEFESLRTTLTRMFPTLIVPPIPEKHSITDYAVAPTKAREDKDMIEHRQRMLQVFLNRCRNLPQISNCIVFQRFLDPHASWSEVLNSPPVSTLPRYSLRAPPVDPSNNVTEAHSYLPIPSANGVVRNRGGDEEGKQEAFFAEAEKTAKEYEAVIGGGLEKVARRIL... | Function: May be required for cytoplasm to vacuole transport (Cvt) and pexophagy.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 62244
Sequence Length: 570
Domain: The PX domain binds phosphatidylinositol 3-phosphate which is necessary for peripheral membrane localization to the perivacuolar punctat... |
Q04053 | MDYNIFEAVHEQQSSTSDMDLSEEDNNPFVGTHHLYASGIGTTIGEARPENENSPPSSSSLPSSPAHSSSAGSSRASTSSSTSSHAVVEADAETEPFVSLSMSTTATISKFTPHDMNGTQQIQIIDAGDFKDPWGKHAIGYVILYENNKIIRRYSEFHSLRQSLTRLLPTIIIPPIPSKHSLLKYIWSPINAANDSKIISTRKKMLNSFLSNCLNIQEISNDIVFQKFLNPEFNWKDVLSSSPIIILPLNNLLAPPLSPTKPSPLHSILPIPSNSSLRNYNSIWQQHITVKSHNEISNLPTEILQNESQFTHIENLFQNY... | Function: Involved in proper sorting of the v-SNARE protein SNC1.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 70741
Sequence Length: 625
Domain: The PX domain binds to phosphatidylinositol 3-phosphate which is necessary for peripheral membrane localization to the punctate structures.
Subcellular ... |
Q4WQI6 | MDQHDDFDSVSWRQDPESDISRPTTSGTDADESLEYNRDTNGKRRMSSVHEDPPQAGPLADAVDLAGIGDGVLECRVDSPLKENDGTKDAYISYLVTTHTDFKSFQKPDFAVRRRFTDFYFLYKTLYREYPACAVPPLPEKHKMEYVTGDRFGPEFTSRRAWSLHRFLKRLTLHPVLRRAPLLAIFLESPDWNAHMRLHSTRTSTGNSDGSGTGIFDNFTDTFVNAFTKVHKPDRRFIEVKEKADKLDEDLNHVEKIVARVARRESDLEADYNDLATQFRKLVPLEPDVEVPLQIFAASVEETARGFKMLKDHTDQNYLG... | Function: Sorting nexin, involved in the separation or division of vacuoles throughout the entire life cycle of the cells. Involved in retrieval of late-Golgi SNAREs from post-Golgi endosomes to the trans-Golgi network, for cytoplasm to vacuole transport (Cvt), autophagy, mitophagy, and pexophagy.
Location Topology: Pe... |
Q5AD77 | MSSEDQFTSIQWDRDDGENTNNTPTDTTIKSKSSKSKKSKKSSSKKKNGNKISPSSTTETSDADDTMKEVTDQLESTQINDDNHEVDDGNKEQNVDANQIGNSDEDPTNSLLLPVNPQPKEPQEEKEDLQQQLQQPQQQLASIQQEPAPIQPPFNAVVNDESLSIQQQQQQQQPTGYVDISYYEKYSIKTTVTHPNRDLDTASKPFISYLVTTTTDNPSILKLTKEKKPKQGEEYLTFSVRRRYGDFRYLYESLSNDFPTVMIPPLPSKSNFKYLTGDTFSSEFVHKRLHSLDRFIRFILQHKILSQSSIFHLFISNSND... | Function: Sorting nexin, involved in the separation or division of vacuoles throughout the entire life cycle of the cells. Involved in retrieval of late-Golgi SNAREs from post-Golgi endosomes to the trans-Golgi network, for cytoplasm to vacuole transport (Cvt), autophagy, mitophagy, and pexophagy.
Location Topology: Pe... |
Q6FPT9 | MDSASADASVTGSGNAKGSSAERVNGGGKFYKLEILVSDPQKRAGEAGLGPYVSYQISTRTDNPSYHGNQKASFDDIIVVHRRYNDVVLLHDILQNDHPTCIIPPLPDKKVLQYIAGDRFGRRFTQRRCHSLQNFLRRVSQHPILSTSKVLEIFLVGNEWDTYRKNIAGTLQNAQKEDVTDAVMNAFKKVHNQNEEFTEIRDRSDKLDNSVNRINKVFHRVVKKNEAIIEDYSKLGLTLQELQELVSSDNDKLADSLKVFIEGVTQFSYGLQDLNMFIDYEYLIDLKDLSHYIGSMKQTMRLKDQKQIDYEELSDYLTKS... | Function: Sorting nexin, involved in the separation or division of vacuoles throughout the entire life cycle of the cells. Involved in retrieval of late-Golgi SNAREs from post-Golgi endosomes to the trans-Golgi network, for cytoplasm to vacuole transport (Cvt), autophagy, mitophagy, and pexophagy.
Location Topology: Pe... |
P0CR63 | MDQDGFHSIAWDDAPSSNPPLSAPSPSQSPFEEGFESISPSSAQPPASDQYEGYDNSKAGEAGDVGVTLDRRERLGGHEVDGSVWNGKWMDVQVREPAKEHEGSKDMYVSYAVKTETSLPTFRKPLTVVRRRFQDFVFLREHLVKNFPACVVPPIPDKHRLEYIKGDRFSPEFVERRRLDLQRFADRIARHPVLQRSQLVNDFLQSTEWSVAKHHHISHPPPESHASLIDSLSDTFINAFSRVRKPDARFVEMTEELERFEEGLTGVERVVGRGKSRVDDLAADYQDMAAAYQGLGYLESGITEPLNRFAEKMLDFSTLL... | Function: Sorting nexin, involved in the separation or division of vacuoles throughout the entire life cycle of the cells. Involved in retrieval of late-Golgi SNAREs from post-Golgi endosomes to the trans-Golgi network, for cytoplasm to vacuole transport (Cvt), autophagy, mitophagy, and pexophagy.
Location Topology: Pe... |
Q6BZE9 | MSSDDQFTSIQWDRDELGPNKETKVNKQETITEDDEHHNNDNEDKDNDTTKSNEPENIQEDDETKDDNEPTDSLILSKTGDENISNIESQNEGDHIVGEPDVNQEPSSDSQTEAYEINVVVTSPLRDLDSSSKPYISYLLTTATNHPSVMKLSTVKKEQGKEVVEITARRRYGDFRFLFDCLSNDHPEVMMPPLPSKSNFKYLTGDTFSTEFVHKRLHSLDRFVRFITCHKVLSQSSIFHLFVSDSADWSTFQKNLKISKVGVQESDADKGNSSMTSNVVNKVVNEDLLTETIMNFLTPSKHKRETNKEILEISDKLKKL... | Function: Sorting nexin, involved in the separation or division of vacuoles throughout the entire life cycle of the cells. Involved in retrieval of late-Golgi SNAREs from post-Golgi endosomes to the trans-Golgi network, for cytoplasm to vacuole transport (Cvt), autophagy, mitophagy, and pexophagy.
Location Topology: Pe... |
O75908 | MEPGGARLRLQRTEGLGGERERQPCGDGNTETHRAPDLVQWTRHMEAVKAQLLEQAQGQLRELLDRAMREAIQSYPSQDKPLPPPPPGSLSRTQEPSLGKQKVFIIRKSLLDELMEVQHFRTIYHMFIAGLCVFIISTLAIDFIDEGRLLLEFDLLIFSFGQLPLALVTWVPMFLSTLLAPYQALRLWARGTWTQATGLGCALLAAHAVVLCALPVHVAVEHQLPPASRCVLVFEQVRFLMKSYSFLREAVPGTLRARRGEGIQAPSFSSYLYFLFCPTLIYRETYPRTPYVRWNYVAKNFAQALGCVLYACFILGRLCV... | Function: Catalyzes the formation of fatty acid-cholesterol esters, which are less soluble in membranes than cholesterol . Plays a role in lipoprotein assembly and dietary cholesterol absorption . Utilizes oleoyl-CoA ((9Z)-octadecenoyl-CoA) and linolenoyl-CoA ((9Z,12Z,15Z)-octadecatrienoyl-CoA) as substrates . May prov... |
O88908 | MQPKVPQLRRREGLGEEQEKGARGGEGNARTHGTPDLVQWTRHMEAVKTQFLEQAQRELAELLDRALWEAMQAYPKQDRPLPSAAPDSTSKTQELHPGKRKVFITRKSLIDELMEVQHFRTIYHMFIAGLCVLIISTLAIDFIDEGRLMLEFDLLLFSFGQLPLALMTWVPMFLSTLLVPYQTLWLWARPRAGGAWMLGASLGCVLLAAHAVVLCVLPVHVSVRHELPPASRCVLVFEQVRLLMKSYSFLRETVPGIFCVRGGKGISPPSFSSYLYFLFCPTLIYRETYPRTPSIRWNYVAKNFAQVLGCLLYACFILGR... | Function: Catalyzes the formation of fatty acid-cholesterol esters, which are less soluble in membranes than cholesterol. Plays a role in lipoprotein assembly and dietary cholesterol absorption. Utilizes oleoyl-CoA ((9Z)-octadecenoyl-CoA) and linolenoyl-CoA ((9Z,12Z,15Z)-octadecatrienoyl-CoA) as substrates. May provide... |
A6QP84 | MRANCSSGLACPANSSEEELPEGLKAFGNLDLVFTVVSALMIGLLMFSLGCSVEVQKLWGHIRRPWGIAVGMLCQFGLMPLIAYLLIISFSLKPLQAIAVLIMGCCPGGTVSNIFTFWVDGDMDLSISMTTCSTMAALGMMPLCLYLYTLSWNLEQNLTIPYQNIGITLVCLIIPVAFGIYVNYRWPKQSKIILKIGAIAGGLLFLVVTGAGMVLMKEFWSSDIILLMISFIFPLIGHATGFLLALLTHQSWQRCRTISLETGTQNVQMCFTMLQLSFTAEQLVQIFGFVLAYGLFQMLNGFFMVAAYKMYKRRLKNKHG... | Function: Transports sulfoconjugated steroid hormones from the extracellular compartment into the cytosol in a sodium-dependent manner without hydrolysis. Steroid sulfate hormones are commonly considered to be biologically inactive metabolites, that may be activated by steroid sulfatases into free steroids (By similari... |
Q3KNW5 | MRANCSSSSACPANSSEEELPVGLEVHGNLELVFTVVSTVMMGLLMFSLGCSVEIRKLWSHIRRPWGIAVGLLCQFGLMPFTAYLLAISFSLKPVQAIAVLIMGCCPGGTISNIFTFWVDGDMDLSISMTTCSTVAALGMMPLCIYLYTWSWSLQQNLTIPYQNIGITLVCLTIPVAFGVYVNYRWPKQSKIILKIGAVVGGVLLLVVAVAGVVLAKGSWNSDITLLTISFIFPLIGHVTGFLLALFTHQSWQRCRTISLETGAQNIQMCITMLQLSFTAEHLVQMLSFPLAYGLFQLIDGFLIVAAYQTYKRRLKNKHG... | Function: Transports sulfoconjugated steroid hormones from the extracellular compartment into the cytosol in a sodium-dependent manner without hydrolysis . Steroid sulfate hormones are commonly considered to be biologically inactive metabolites, that may be activated by steroid sulfatases into free steroids . May play ... |
Q9CXB2 | MSTDCAGNSTCPVNSTEEDPPVGMEGHANLKLLFTVLSAVMVGLVMFSFGCSVESQKLWLHLRRPWGIAVGLLSQFGLMPLTAYLLAIGFGLKPFQAIAVLMMGSCPGGTISNVLTFWVDGDMDLSISMTTCSTVAALGMMPLCLYIYTRSWTLTQNLVIPYQSIGITLVSLVVPVASGVYVNYRWPKQATVILKVGAILGGMLLLVVAVTGMVLAKGWNTDVTLLVISCIFPLVGHVTGFLLAFLTHQSWQRCRTISIETGAQNIQLCIAMLQLSFSAEYLVQLLNFALAYGLFQVLHGLLIVAAYQAYKRRQKSKCRR... | Function: Transports sulfoconjugated steroid hormones from the extracellular compartment into the cytosol in a sodium-dependent manner without hydrolysis . Steroid sulfate hormones are commonly considered to be biologically inactive metabolites, that may be activated by steroid sulfatases into free steroids (By similar... |
Q9LEZ1 | MESANIFGSDEDCRSCESGWTMYLASQSHDRDDDCYYGDDDEEEEDSDGGDSMDSDASSGPMEATSYLKLAQEIEEQNSIKKKKKKTNEEMVLVETTRVHNNINHDDDDDDDEDDGDNHDYDDGNDSYSVVHSYVGSVRQKGLV | Function: Involved in cytokinin-mediated development . Promotes the expression of cytokinin synthases (e.g. IPT3 and IPT7), thus triggering the accumulation of trans-zeatin riboside, trans-zeatin riboside monophosphate and isopentenyladenine 9-glucoside .
Location Topology: Peripheral membrane protein
Sequence Mass (Da... |
Q95088 | INGDAKGTVFFEQETSEAPVKVTGEGLGLAKGLHGFHVHEFGDNTNGCMSSGPHFNPRNKEHGAPTDENRHLGDLGNIQAAGDSPTAVSITDSKITLFGADSIIGRTVVVHADA | Cofactor: Binds 1 copper ion per subunit.
Function: Destroys radicals which are normally produced within the cells and which are toxic to biological systems.
Catalytic Activity: 2 H(+) + 2 superoxide = H2O2 + O2
Sequence Mass (Da): 11864
Sequence Length: 114
Subcellular Location: Cytoplasm
EC: 1.15.1.1
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P0AGD2 | MKRFSLAILALVVATGAQAASEKVEMNLVTSQGVGQSIGSVTITETDKGLEFSPDLKALPPGEHGFHIHAKGSCQPATKDGKASAAESAGGHLDPQNTGKHEGPEGAGHLGDLPALVVNNDGKATDAVIAPRLKSLDEIKDKALMVHVGGDNMSDQPKPLGGGGERYACGVIK | Cofactor: Binds 1 copper ion per subunit.
Function: Destroys radicals which are normally produced within the cells and which are toxic to biological systems.
Catalytic Activity: 2 H(+) + 2 superoxide = H2O2 + O2
Sequence Mass (Da): 17681
Sequence Length: 173
Subcellular Location: Periplasm
EC: 1.15.1.1
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Q59448 | MTAFYKLCGMSMLSLVLADCTFLSANKPYDRDHDGELIVHMKDVNTHKEVGTITISPYIHDGNQEGMLITPHLYNLPANTTHGMHIHINPSCEDNGIAAGGHWDPDNTQKHLGPYNDNGHKGDLPVLVVNADGTATEPVVAPKLNSLEELAGHSLMLHAGGDNYSDKPQPLGGGGARMWCGVIAD | Cofactor: Binds 1 copper ion per subunit.
Function: Destroys radicals which are normally produced within the cells and which are toxic to biological systems.
Catalytic Activity: 2 H(+) + 2 superoxide = H2O2 + O2
Sequence Mass (Da): 19887
Sequence Length: 185
Subcellular Location: Periplasm
EC: 1.15.1.1
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P81926 | MSIKAVCVLVGSVKGTLNFKQDAIGSCTVTGEVSGLIPGKHGFHIHEYGDLTNGCTSSGGHFNPFKQIHGAPEDDIRHVGDLGNITADSSGVATVNITDRMISLTGEHSIIGRAVVVHAGEDDLGKGGHEDSKTTGHAGGRLSCGVIGINHL | Cofactor: Binds 1 copper ion per subunit.
Function: Destroys radicals which are normally produced within the cells and which are toxic to biological systems. The plasma superoxide dismutase has phagocytosis-stimulating activity and may play an important role in the biological defenses of the organism.
Catalytic Activit... |
P34936 | MXKAVAVLTGSEGVXGTIFFTQ | Cofactor: Binds 1 copper ion per subunit.
Function: Destroys radicals which are normally produced within the cells and which are toxic to biological systems.
Catalytic Activity: 2 H(+) + 2 superoxide = H2O2 + O2
Sequence Mass (Da): 2279
Sequence Length: 22
Subcellular Location: Cytoplasm
EC: 1.15.1.1
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P28759 | MASLGGLQNVSGINFLIKEGPKVNAKFELKPPPYPLNGLEPVMSQQTLEFHWGKHHKTYVENLKKQVVGTELDGKSLEEIIVTSYNKGDILPAFNNAAQVWNHDFFWECMKPGGGGKPSGELLELIERDFGSFVKFLDEFKAAAATQFGSGWAWLAYRARKFDGENVANPPSPDEDNKLVVLKSPNAVNPLVWGGYYPLLTIDVWEHAYYLDFQNRRPDYISVFMDKLVSWDAVSSRLEQAKALITSA | Cofactor: Binds 1 Fe cation per subunit.
Function: Destroys superoxide anion radicals which are normally produced within the cells and which are toxic to biological systems.
Catalytic Activity: 2 H(+) + 2 superoxide = H2O2 + O2
Sequence Mass (Da): 27842
Sequence Length: 248
Subcellular Location: Plastid
EC: 1.15.1.1
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O51917 | MSVYTLPELPYDYSALAPVISPEIIELHHDKHHAAYVKGANDTLEQLAEARDKETWGSINGLEKNLAFHLSGHILHSIYWHNMTGDGGGEPLDKDGVGELADAIAESFGSFAGFRAQLTKAAATTQGSGWGVLAYEPLSGRLIVEQIYDHQGNVGQGSTPILVFDAWEHAFYLQYKNQKVDFIDAMWAVVNWQDVARRYEAAKSRTNTLLLAP | Cofactor: Binds 1 Fe(3+) or Zn(2+) ion per subunit.
Function: Destroys superoxide anion radicals which are normally produced within the cells and which are toxic to biological systems.
Catalytic Activity: 2 H(+) + 2 superoxide = H2O2 + O2
Sequence Mass (Da): 23527
Sequence Length: 213
Subcellular Location: Cytoplasm
EC... |
Q08713 | MTQVIQLKRYEFPQLPYKVDALEPYISKDIIDVHYNGHHKGYVNGANSLLDRLEKLIKGDLPQGQYDLQGILRGLTFNINGHKLHAIYWNNMAPAGKGGGKPGGALADLINKQYGSFDRFKQVFSESANSLPGSGWTVLYYDNESGNLQIMTVENHFMNHIAELPVILIVDEFEHAYYLQYKNKRGDYLNAWWNVVNWDDAEKRLQKYLNK | Cofactor: Binds 1 Fe cation per subunit.
Function: Destroys superoxide anion radicals which are normally produced within the cells and which are toxic to biological systems.
Catalytic Activity: 2 H(+) + 2 superoxide = H2O2 + O2
Sequence Mass (Da): 24266
Sequence Length: 211
Subcellular Location: Cytoplasm
EC: 1.15.1.1
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P19666 | LNYEYSDLEPVLSAHLLSFHHGKHHQAYVNNLNATYEQIAAATKENDAHKIATLQSALRFNLGGHVNHWIYWDNLAPVKSGGGVLPDEHSPLTKAIKEKWGSYENFITLFNTRTAAIQGSGWGWLGYDTVSKSLRLFELGNQDMPEWSSIVPLLTIDVWEHAYYLDYQNLRPKYLTEVWKIVNWREVEKRYLQAIE | Cofactor: Binds 1 Fe cation per subunit.
Function: Destroys superoxide anion radicals which are normally produced within the cells and which are toxic to biological systems.
Catalytic Activity: 2 H(+) + 2 superoxide = H2O2 + O2
Sequence Mass (Da): 22657
Sequence Length: 196
EC: 1.15.1.1
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P53647 | MAEYTLPDLDWDYAALEPHISGQINEIHHTKHHATYVKGVNDALAKLEEARANEDHAAIFLNEKNLAFHLGGHVNHSIWWKNLSPDGGDKPTGELAAAIDDAFGSFDKFRAQFSAAANGLQGSGWAVLGYDTVGSRLLTFQLYDQQANVPLGIIPLLQVDMWEHAFYLQYKNVKADYVKAFWNVVNWADVQKRYAAATSKAQGLIFG | Cofactor: Binds 1 Mn(2+) ion per subunit.
Function: Destroys superoxide anion radicals which are normally produced within the cells and which are toxic to biological systems.
Catalytic Activity: 2 H(+) + 2 superoxide = H2O2 + O2
Sequence Mass (Da): 23030
Sequence Length: 207
Subcellular Location: Secreted
EC: 1.15.1.1
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P80582 | AEYTLPDLGWDYAASGPG | Cofactor: Binds 1 Mn(2+) ion per subunit.
Function: Destroys superoxide anion radicals which are normally produced within the cells and which are toxic to biological systems.
Catalytic Activity: 2 H(+) + 2 superoxide = H2O2 + O2
Sequence Mass (Da): 1883
Sequence Length: 18
Subcellular Location: Cytoplasm
EC: 1.15.1.1
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Q9Y783 | MVNLGSIWQNLLASQAPLQSMTGNATTMAGLATYSLPQLPYAYNALEPYISAQIMELHHSKHHQTYVTNLNNALKVHVAAIASSDIPAQIAQQPAIKFNGGGHINHSLFWKNLAPAETPETNYSKAAPSLAAEIEKTWGSFDEFKKAFSAALLGIQGSGWGWLVKESTAEKGRLRIITTKDQDPVVGGEVPVFGVDMWEHAYYLQYLNGKAAYVENIWKVINWKTAEERFQGSREDAFADLKALL | Cofactor: Binds 1 Mn(2+) ion per subunit.
Function: Destroys superoxide anion radicals which are normally produced within the cells and which are toxic to biological systems.
Catalytic Activity: 2 H(+) + 2 superoxide = H2O2 + O2
Sequence Mass (Da): 27020
Sequence Length: 245
Subcellular Location: Mitochondrion matrix
E... |
Q43008 | MALRTLASRKTLAAAALPLAAAAAARGVTTVALPDLPYDYGALEPAISGEIMRLHHQKHHATYVANYNKALEQLDAAVAKGDAPAIVHLQSAIKFNGGGHVNHSIFWNNLKPISEGGGDPPHAKLGWAIDEDFGSFEALVKKMSAEGAALQGSGWVWLALDKEAKKLSVETTANQDPLVTKGANLVPLLGIDVWEHAYYLQYKNVRPDYLSNIWKVMNWKYAGEVYENATA | Cofactor: Binds 1 Mn(2+) ion per subunit.
Function: Destroys superoxide anion radicals which are normally produced within the cells and which are toxic to biological systems.
Catalytic Activity: 2 H(+) + 2 superoxide = H2O2 + O2
Sequence Mass (Da): 24997
Sequence Length: 231
Subcellular Location: Mitochondrion matrix
E... |
P28765 | HISEMIMQIHHTKHHQAYINNLKACTEKLKQAEQANDVAAMNALLPAIKFNGGGHINHTIFWTNMAPSAGGEPAGPVADAITKEFGSFQAFKDKFSTASVGVKGSGWGWLGYCPKNDKLAVATCQNQDPLQLTHGLIPLLGLDV | Cofactor: Binds 1 Mn(2+) ion per subunit.
Function: Destroys superoxide anion radicals which are normally produced within the cells and which are toxic to biological systems.
Catalytic Activity: 2 H(+) + 2 superoxide = H2O2 + O2
Sequence Mass (Da): 15505
Sequence Length: 144
Subcellular Location: Mitochondrion matrix
E... |
Q9CPN6 | MAYTLPELGYAYDALEPHFDAMTMEIHHSKHHQAYVNNANAALENLPELAQGCPGQLLTKLAEVPADKLTAIRNNVGGHLNHSLFWKSLKKGTTLQGALKDAIVRDFGSVEAFQAEFEKAAATRFGSGWAWLVLQENGKLAVVSTANQDSPVMGKAIAGCEGYPLLGLDVWEHAYYLKFQNRRPDYIKEFWHVVNWDFVAERFEKKVEHCNCTK | Cofactor: Binds 1 Mn(2+) ion per subunit.
Function: Destroys superoxide anion radicals which are normally produced within the cells and which are toxic to biological systems.
Catalytic Activity: 2 H(+) + 2 superoxide = H2O2 + O2
Sequence Mass (Da): 24020
Sequence Length: 214
EC: 1.15.1.1
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O75007 | MTSQTHTLPPLPYAYDALEPVISKQIMELHHQKHHQTYINNLNAALSAQASATASNDVPTLISLQQKLRFNGGGHINHSLFWKNLTPPGTPANDIAGAPALREAIVSRWGSHEAFVKAFGAELLGLQGSGWGWLVSKGGAKGRLEIVTTKDQDPVNAPDVPVFGVDMWEHAYYLQYLNNKAGYVEGIWKIIHWAEAEKRYTAGVENPLKL | Cofactor: Binds 1 Mn(2+) ion per subunit.
Function: Destroys superoxide anion radicals which are normally produced within the cells and which are toxic to biological systems.
PTM: The N-terminus is blocked.
Catalytic Activity: 2 H(+) + 2 superoxide = H2O2 + O2
Sequence Mass (Da): 23128
Sequence Length: 210
Subcellular ... |
I3V6A7 | MATNGEIFNTYGHNRQTATVTKITASNESSNGVCYLSETANLGKLICIPMALRAAMELNVFQLISKFGTDAKVSASEIASKMPNAKNNPEAAMYLDRILRLLGASSILSVSTTKKSINRGGDDVVVHEKLYGLTNSSCCLVPRQEDGVSLVEELLFTSDKVVVDSFFKLKCVVEEKDSVPFEVAHGAKIFEYAATEPRMNQVFNDGMAVFSIVVFEAVFRFYDGFLDMKELLDVGGGIGTSVSKIVAKYPLIRGVNFDLPHVISVAPQYPGVEHVAGDMFEEVPKGQNMLLKWVLHDWGDERCVKLLKNCWNSLPVGGKV... | Function: Methyltransferase involved in the biosynthesis of the benzylisoquinoline alkaloid noscapine . Catalyzes the conversion of (S)-scoulerine to (S)-tetrahydrocolumbamine . Can convert (S)-tetrahydrocolumbamine to tetrahydropalmatine . Can convert (S)-norreticuline to (S)-norcodamine . Can convert (S)-reticuline t... |
I3PLQ6 | MEIHLESQEQEMKYQSQIWNQICGTVDTSVLRCAIQLGIFDAIHNSGKPMITLTELSSIVSSPSSSSIEPCNLYRLVRYLSQMDLISIGECLNEATVSLTGTSKLLLRNQEKSLIDWVLAISCEMMVVVWHELSSSVSTPADEPPIFQKVHGKNALELAGEFPEWNDLINNAMTSDTSVTKPALIQGCGKILNGVTSLIDVGGGHGATMAYIVEAFPHIKGAVIDLPHVVEAAPERPGVEFISGDIFKSISNADAVLLKYVLHNWEDTECVNLLKRCKEAVPADKGKVIIMDLVIDDDDNSILTQAKLSLDLTVMNHGGG... | Function: Methyltransferase involved in the biosynthesis of the benzylisoquinoline alkaloid noscapine . Catalyzes the conversion of (S)-scoulerine to (S)-tetrahydrocolumbamine . The heterodimers SOMT2-SOMT3 and SOMT2-6OMT convert 3-O-acetyl-4'-O-demethylpapaveroxine to 3-O-acetylpapaveroxine, where SOMT2 is the catalyt... |
C6TAY1 | MASPLNNGRKASEIFQGQALLYKHLLGFIDSKCLKWMVELDIPDIIHSHSHGQPITFSELVSILQVPPTKTRQVQSLMRYLAHNGFFEIVRIHDNIEAYALTAASELLVKSSELSLAPMVEYFLEPNCQGAWNQLKRWVHEEDLTVFGVSLGTPFWDFINKDPAYNKSFNEAMACDSQMLNLAFRDCNWVFEGLESIVDVGGGTGITAKIICEAFPKLKCMVLERPNVVENLSGSNNLTFVGGDMFKCIPKADAVLLKLVLHNWNDNDCMKILENCKEAISGESKTGKVVVIDTVINENKDERQVTELKLLMDVHMACII... | Function: S-adenosyl-L-methionine-dependent methyltransferase that catalyzes the 4'-methylation of naringenin (4',5,7-trihydroxyflavanone) into ponciretin (4'-methoxy-5,7-dihydroxyflavanone). In vitro, also able to convert apigenin, daidzein, genistein and quercetin into the 4'-O-methylated compounds acacetin, formonon... |
P48434 | MNLLDPFMKMTEEQDKCISDAPSPTMSDDSAGSPCPSGSGSDTENTRPQENTFPKGDPDLKKESDEDKFPVCIREAVSQVLKGYDWTLVPMPVRVNGSSKNKPHVKRPMNAFMVWAQAARRKLADQYPHLHNAELSKTLGKLWRLLNESEKRPFVEEAERLRVQHKKDHPDYKYQPRRRKSVKNGQSEQEEGSEQTHISPNAIFKALQADSPQSSSSISEVHSPGEHSGQSQGPPTPPTTPKTDAQQPGKQDLKREGRPLAEGGRQPPHIDFRDVDIGELSSDVISNIETFDVNEFDQYLPPNGHPGVPATHGQVTTYSG... | Function: Transcription factor that plays a key role in chondrocytes differentiation and skeletal development . Specifically binds the 5'-ACAAAG-3' DNA motif present in enhancers and super-enhancers and promotes expression of genes important for chondrogenesis, including COL2A1 . Plays a central role in successive step... |
Q04887 | MNLLDPFMKMTDEQEKGLSGAPSPTMSEDSAGSPCPSGSGSDTENTRPQENTFPKGEPDLKKESEEDKFPVCIREAVSQVLKGYDWTLVPMPVRVNGSSKNKPHVKRPMNAFMVWAQAARRKLADQYPHLHNAELSKTLGKLWRLLNESEKRPFVEEAERLRVQHKKDHPDYKYQPRRRKSVKNGQAEAEEATEQTHISPNAIFKALQADSPHSSSGMSEVHSPGEHSGQSQGPPTPPTTPKTDVQAGKVDLKREGRPLAEGGRQPPIDFRDVDIGELSSDVISNIETFDVNEFDQYLPPNGHPGVPATHGQVTYTGSYG... | Function: Transcription factor that plays a key role in chondrocytes differentiation and skeletal development . Specifically binds the 5'-ACAAAG-3' DNA motif present in enhancers and super-enhancers and promotes expression of genes important for chondrogenesis, including cartilage matrix protein-coding genes COL2A1, CO... |
D3DJG4 | MGKWVTIIFVLFLYAIAQQENPAEEVKKQKELLLKEMGILPGDVYAEQGRDMFNKPMGNAGKSCSSCHGQDGRYLRGAYAHMPRYYKDMDAVADLDTRIKYCMEKYMGVGNVKHDLNFKSIATYVATLSNGMKMDVKLTHPKEREMYEKGRELWYARVGKMDFSCAICHDSEAGKRVFLQTVVAVKEDKVATHWPAYRFSNDQLWTMEDRIRGCFGDMRVAPPEHFHWAVVALNLYLSYKAKGGVVRVPGFIY | Cofactor: Binds 2 heme c groups covalently per subunit.
Function: C-type diheme cytochrome, which is part of the SoxAX cytochrome complex involved in sulfur oxidation. The SoxAX complex catalyzes the formation of a heterodisulfide bond between the conserved cysteine residue on a sulfur carrier SoxYZ complex subunit Sox... |
D3DJG5 | MRKLWFLPILLGAVGGVSLYAIAQQENPAEEVKKQKELLLKEMGILPGDVYAEQGRDMFNKPMGNAGKSCSSCHGQDGRYLRGAYAHMPRYYKDMDAVADLDTRIKYCMEKYMGVGNVKHDLNFKSIATYVATLSNGMKMDVKLTHPKEREMYEKGRELWYARVGKMDFSCAICHDTFGGQRIRLQTLAKVKEDKVATHWPAYRFSNDQLWTMEDRIRGCYNQIRVTPPPHFSWPQIALSLYMAYESKGGTIETPGFVR | Cofactor: Binds 2 heme c groups covalently per subunit.
Function: C-type diheme cytochrome, which is part of the SoxAX cytochrome complex involved in sulfur oxidation. The SoxAX complex catalyzes the formation of a heterodisulfide bond between the conserved cysteine residue on a sulfur carrier SoxYZ complex subunit Sox... |
Q1W3E4 | MTKHGFLLATLVLAGATLPIGPVTAATPEEEQAAFQAYFKQRFPNVPEDEFKNGTYAIDPVTRENWEAIEEFPPYENAISQGETLWNTPFADGQGYADCFPDGPAIMNHYPRWDRERGQVMTLPLALNACRTAHGETPLKYKKGPIADLLAYIAFESRGQITRVEIPQDDPRALAAYEQGKRFYFARRGQLNFACAHCHLATSGTKLRTETLSPAYGHTTHWPVYRSEWGEMGTLHRRFAGCNEQVRAKAFEPQGEEYRNLEYFLTYMNNGLELNGPGARK | Cofactor: Binds 1 heme group per subunit.
Function: C-type monoheme cytochrome, which is part of the SoxAX cytochrome complex involved in sulfur oxidation. The SoxAX complex catalyzes the formation of a heterodisulfide bond between the conserved cysteine residue on a sulfur carrier SoxYZ complex subunit SoxY and thiosu... |
Q8RLX0 | MKKTIQRGLFTGALVLLTAMTSKPAHAAVNYQALVDADVKKFQGYFLKEFPGVKLEDFGDGVYALDEDSRKQWKEMEEFPPYELDVEAGKALFNKPFANGKSLGSCFSNGGAVRGMYPYFDEKRKEVITLEMAINECRVANGEKPYAPKKGDIARVSAYIASISRGQKIDVKVKSKAAYDAYMKGKEMFYAKRGQLNMSCSGCHMEYSGRHLRAEIISPALGHTTHFPVFRSKWGEIGTLHRRYAGCNENIGAKPFPAQSKEYRDLEFFQTVMSNGLKFNGPASRK | Cofactor: Binds 1 heme group per subunit.
Function: C-type monoheme cytochrome, which is part of the SoxAX cytochrome complex involved in sulfur oxidation. The SoxAX complex catalyzes the formation of a heterodisulfide bond between the conserved cysteine residue on a sulfur carrier SoxYZ complex subunit SoxY and thiosu... |
Q46337 | MSQNTSYRLPAEQSPAARIDRGEALVLTVDGKQLEAFRGDTVASAMLANGQRACGNSMYLDRPRGIFSAGVEEPNALVTVEARHEQDINESMLAATTVPVTANLSATLLRGLGVLDPSTDPAYYDHVHVHTDVLVVGAGPAGLAAAREASRSGARVLLLDERAEAGGSLRDAAGEQIDGQDAAAWIDATVAELAAAEETTHLQRTTVLGSYDANYVVAVQRRTVHLDGPSGAGVSRERIWHIRANQVVLATGAHERPIVFENNDRPGIMLAGAVRSYLNCYGVRAGSQIVVATTNDSAYPLVADLAASGGVVAVIDARTT... | Function: Catalyzes the oxidative demethylation of sarcosine to yield glycine, hydrogen peroxide and 5,10-methylenetetrahydrofolate.
Catalytic Activity: H2O + O2 + sarcosine = formaldehyde + glycine + H2O2
Sequence Mass (Da): 102767
Sequence Length: 967
Subcellular Location: Cytoplasm
EC: 1.5.3.1
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Q08IS0 | MKKTVTAVALLCALSSTAIAPTFAADDDEAARLKAIEEYRKQIADGNPSDLLAMEGEELWRTPYGPKNQSLEQCDLGLGPGVVKGAAAKLPRYFPDTGKVEDLESRLMTCMERLQGVERQKVIDSPWRKGEKLRMDKIVAYIVTESNGEKIDVDMSHPKMKEMYELGKRMFFYRTGPFDFSCATCHGKDGQRIRLQELPNLTKHEGAAAGWGSWPAYRVSNSQFWTMQMRLNDCFRQQRTAEPIYGSDATIALSVYMAANGNGGVMLTPGIKR | Cofactor: Binds 1 heme group per subunit.
Function: C-type monoheme cytochrome, which is part of the SoxAX cytochrome complex involved in sulfur oxidation. The SoxAX complex catalyzes the formation of a heterodisulfide bond between the conserved cysteine residue on a sulfur carrier SoxYZ complex subunit SoxY and thiosu... |
O33434 | MPRFTKTKGTLAATALGLALAGAAFADPVEDGLVIETDSGPVEIVTKTAPPAFLADTFDTIYSGWHFRDDSTRDLERDDFDNPAMVFVDRGLDKWNAAMGVNGESCASCHQGPESMAGLRAVMPRVDEHTGKLMIMEDYVNACVTERMGLEKWGVTSDNMKDMLSLISLQSRGMAVNVKIDGPAAPYWEHGKEIYYTRYGQLEMSCANCHEDNAGNMIRADHLSQGQINGFPTYRLKDSGMVTAQHRFVGCVRDTRAETFKAGSDDFKALELYVASRGNGLSVEGVSVRH | Cofactor: Binds 2 heme c groups covalently per subunit.
Function: C-type diheme cytochrome, which is part of the SoxAX cytochrome complex involved in sulfur oxidation. The SoxAX complex catalyzes the formation of a heterodisulfide bond between the conserved cysteine residue on a sulfur carrier SoxYZ complex subunit Sox... |
Q94BM7 | MKGSSESSSRGLNNTSGVSEFCTDGSKSLSHIDYVRSLLGSHKEANLGGLDDDSIVRALECEDVSLRQWLDNPDRSVDAFECFHVFRQIVEIVNAAHSQGIVVHNVRPSCFVMSSFNNVSFIESASCSDSGSDEDATTKSREIGSSRQEEILSERRSKQQEEVKKQPFPMKQILAMEMSWYTSHEEDNGSLCNCASDIYRLGVLLFELFCPVSSREEKSRTMSSLRHRVLPPQILLNWPKEASFCLWLLHPEPSCRPSMSELLQSEFINEPRENLEEREAAMELRDRIEEQELLLEFLFLIQQRKQEAADKLQDTISLLS... | Function: Repressor of photomorphogenesis in the light. Probably part of the COP1/SPA E3 ubiquitin-protein ligase complex.
Sequence Mass (Da): 89071
Sequence Length: 794
Domain: The protein kinase domain is predicted to be catalytically inactive. The DWD box is required for interaction with DDB1A (By similarity).
Subce... |
Q86WD7 | MASYLYGVLFAVGLCAPIYCVSPANAPSAYPRPSSTKSTPASQVYSLNTDFAFRLYRRLVLETPSQNIFFSPVSVSTSLAMLSLGAHSVTKTQILQGLGFNLTHTPESAIHQGFQHLVHSLTVPSKDLTLKMGSALFVKKELQLQANFLGNVKRLYEAEVFSTDFSNPSIAQARINSHVKKKTQGKVVDIIQGLDLLTAMVLVNHIFFKAKWEKPFHPEYTRKNFPFLVGEQVTVHVPMMHQKEQFAFGVDTELNCFVLQMDYKGDAVAFFVLPSKGKMRQLEQALSARTLRKWSHSLQKRWIEVFIPRFSISASYNLET... | Function: Protease inhibitor that inhibits trypsin and trypsin-like serine proteases (in vitro). Inhibits plasmin and thrombin with lower efficiency (in vitro).
Location Topology: Single-pass type II membrane protein
Sequence Mass (Da): 46557
Sequence Length: 417
Subcellular Location: Secreted
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Q96EA4 | MEADIITNLRCRLKEAEEERLKAAQYGLQLVESQNELQNQLDKCRNEMMTMTESYEQEKYTLQREVELKSRMLESLSCECEAIKQQQKMHLEKLEEQLSRSHGQEVNELKTKIEKLKVELDEARLSEKQLKHQVDHQKELLSCKSEELRVMSERVQESMSSEMLALQIELTEMESMKTTLKEEVNELQYRQEQLELLITNLMRQVDRLKEEKEEREKEAVSYYNALEKARVANQDLQVQLDQALQQALDPNSKGNSLFAEVEDRRAAMERQLISMKVKYQSLKKQNVFNREQMQRMKLQIATLLQMKGSQTEFEQQERLL... | Function: Required for the localization of dynein and dynactin to the mitotic kintochore. Dynein is believed to control the initial lateral interaction between the kinetochore and spindle microtubules and to facilitate the subsequent formation of end-on kinetochore-microtubule attachments mediated by the NDC80 complex.... |
O48661 | MSSTQEASVTDLPVKRPREAEEDNNGGAMETENGGGEIKEPSCMSSIIPGWFSEISPMWPGEAHSLKVEKILFQGKSDYQDVIVFQSATYGKVLVLDGVIQLTERDECAYQEMITHLPLCSISNPKKVLVIGGGDGGVLREVARHSSVEQIDICEIDKMVVDVAKQYFPNVAVGYEDPRVNLIIGDGVAFLKNAAEGTYDAVIVDSSDPIGPAKELFEKPFFESVNRALRPGGVVCTQAESLWLHMDIIEDIVSNCRDIFKGSVNYAWTSVPTYPSGVIGFMLCSSEGPQVDFKKPVSLIDTDESSIKSHCPLKYYNAEI... | Catalytic Activity: putrescine + S-adenosyl 3-(methylsulfanyl)propylamine = H(+) + S-methyl-5'-thioadenosine + spermidine
Sequence Mass (Da): 37140
Sequence Length: 340
Pathway: Amine and polyamine biosynthesis; spermidine biosynthesis; spermidine from putrescine: step 1/1.
EC: 2.5.1.16
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O48659 | MEEQGNNESAYISSILPGWFSEISPLWPGEAHSLKVEKILFQGKSDYQNVVVFQSSTYGKVLVLDGVIQLTERDECAYQEMITHLPLCSIPNPKKVLVIGGGDGGVLREVSRHSSVEQIDICEIDKMVIDVSKQFFPNVAIGYEDPRVKLHVGDGVAFLKNVPEGTYDAVIVDSSDPIGPAQELFEKPFFESVARALCPGGVVCTQAESIWLHMHIIEDIVSNCRQIFKGSVNYAWTTVPTYPSGVIGFMLCSTEGPAVDFKNPINPIDADDSHTKTRGPLKFYNSEIHSASFCLPSFAKRVIESNAK | Catalytic Activity: putrescine + S-adenosyl 3-(methylsulfanyl)propylamine = H(+) + S-methyl-5'-thioadenosine + spermidine
Sequence Mass (Da): 33917
Sequence Length: 308
Pathway: Amine and polyamine biosynthesis; spermidine biosynthesis; spermidine from putrescine: step 1/1.
EC: 2.5.1.16
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Q9ZTR0 | MAAESTVELESSMKEHRDDDEKSNGFSVSAVSMDVEGGDKDPSGNGVSSVIPGWFSEISPMWPGEAHSLKIEKILFQGKSEYQKVMVFQSSTYGKVLVLDGVIQLTERDECAYQEMITHLPLCSIPNPKKVLVIGGGDGGVLREVARHSSIEKIDICEIDNMVVEVSKQFFPEVAVGFNDPRVTLRIGDGVAFLKAAPEGTYDAVIVDSSDPIGPAQELFEKPFFQSVARALRPGGVMCTQAESIWLHMDIIEDIVSNCRHIFKGSVNYAWTTVPTYPSGMIGFMLCSTEGPLVDFKHPVNPIDQKDCQKSVRPLKFYNS... | Catalytic Activity: putrescine + S-adenosyl 3-(methylsulfanyl)propylamine = H(+) + S-methyl-5'-thioadenosine + spermidine
Sequence Mass (Da): 37590
Sequence Length: 342
Pathway: Amine and polyamine biosynthesis; spermidine biosynthesis; spermidine from putrescine: step 1/1.
EC: 2.5.1.16
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Q5MJ70 | MRHNQMCCETPPTVTVYVKSGSNRSHQPKKPITLKRPICKDNWQAFEKNTHNNNKSKRPKGPCLVIQRQDMTAFFKLFDDDLIQDFLWMDCCCKIADKYLLAMTFVYFKRAKFTISEHTRINFFIALYLANTVEEDEEETKYEIFPWALGKNWRKLFPNFLKLRDQLWDRIDYRAIVSRRCCEEVMAIAPTHYIWQRERSVHHSGAVRNYNRDEVQLPRGPSATPVDCSLCGKKRRYVRLGLSSSSSLSSHTAGVTEKHSQDSYNSLSMDIIGDPSQAYTGSEVVNDHQSNKGKKTNFLKKDKSMEWFTGSEE | Function: Regulates the G1/S phase transition of the cell cycle by binding and activating CDK1 and CDK2 . Contributes to CDK2 activation without promoting CDK2 phosphorylation, by inducing a conformation change of the CDK2 T-loop that obstructs the substrate-binding cleft prior to kinase activation . Mediates cell surv... |
Q5IBH7 | MRHNQMYCETPPTVTIHVKSGSNRSHQTRKPISLKRPILKDSWEASENNAQNNKSKRPRGPCLIIQRQEMTAFFKLFDDDLIQDFLWMDCCCKIADKYLLAMTFVYFKRAKFTINEHTRINFFIALYLANTVEEDEEEAKYEIFPWALGKNWRKLFPNFLKLRDQLWDRIDYRAIVSRRCCEEVMAIAPTHYIWQRERSVHHSGAVRNYNRDEVHLPRGPSATPVDCSLCGKKGRYVRLGLSSSSSSSSDTGELMEKDSQELHSAFSVDTAGDPPHTYSQVANDHQSNKENETNFVKKNKSVEWFAESEE | Function: Regulates the G1/S phase transition of the cell cycle by binding and activating CDK1 and CDK2 . Contributes to CDK2 activation without promoting CDK2 phosphorylation, by inducing a conformation change of the CDK2 T-loop that obstructs the substrate-binding cleft prior to kinase activation. Interferes with CDK... |
P0C0J1 | MNKKKLGVRLLSLLALGGFVLANPVFADQNFARNEKEAKDSAITFIQKSAAIKAGARSAEDIKLDKVNLGGELSGSNMYVYNISTGGFVIVSGDKRSPEILGYSTSGSFDANGKENIASFMESYVEQIKENKKLDTTYAGTAEIKQPVVKSLLDSKGIHYNQGNPYNLLTPVIEKVKPGEQSFVGQHAATGCVATATAQIMKYHNYPNKGLKDYTYTLSSNNPYFNHPKNLFAAISTRQYNWNNILPTYSGRESNVQKMAISELMADVGISVDMDYGPSSGSAGSSRVQRALKENFGYNQSVHQINRGDFSKQDWEAQID... | Function: Cysteine protease that acts as a key streptococcal virulence factor by cleaving host proteins involved in immune response . Triggers inflammation by mediating cleavage of host proteins, which can both promote host pathogenesis by triggering sterile inflammation and/or restrict streptococcal infection, dependi... |
A6TS03 | MDIKSFEKIQLYGFNNLTKTLSFNIYDICYAKAPEQSKAYIAYIDEQYNAERLTKILSNVADITGANILSISKQDYDPQGASVTMLVAEEMTVPTLTPESLTGESPGPLPGNKPSPGSIVTHLDKSHVTVHTYPETHPLDGISTFRADIDVSTCGHISPIKALNYLIHSFESDIVTIDYRVRGFTRDINGQKYFIDHDINSIQNYIAKDILNLYHAIDVNVYQENIFHTKMTLKDFKLNNYLFGVSEEELSDHESASIKDQLRDEMQEIFYGRNVTKV | Cofactor: Binds 1 pyruvoyl group covalently per subunit.
Function: Catalyzes the decarboxylation of S-adenosylmethionine to S-adenosylmethioninamine (dcAdoMet), the propylamine donor required for the synthesis of the polyamines spermine and spermidine from the diamine putrescine.
PTM: Is synthesized initially as an ina... |
A3PFH4 | MTNIQTWIDEYHKGSRFGLNGDVLIKQKSQYQEIIVIENEYYGRALMLDGCWMTSLKDEKYYHECLVHPALSSIDEKSNVLIIGGGDGGTVRECVKYAQISKIDLVEIDEEVIKISKKFLKEIGGEAWHDKRLEIHVDDGVKWVKKTRDNYYDVIFIDCSDPSEFSNLLFSDSFYKECKRILTPKGILATQSESPESFKNIHINILKTLKNIFKVSETMYSFVPIYPSGIWSWTFASSEDLNLSKQNYDEILKIEKGCEIWNLNFQNAAFKMMPNKIIKELDS | Function: Catalyzes the irreversible transfer of a propylamine group from the amino donor S-adenosylmethioninamine (decarboxy-AdoMet) to putrescine (1,4-diaminobutane) to yield spermidine.
Catalytic Activity: putrescine + S-adenosyl 3-(methylsulfanyl)propylamine = H(+) + S-methyl-5'-thioadenosine + spermidine
Sequence ... |
Q8ZXM4 | MSKVPGPIVLMEPLSGKTSLIIKINAIHVSKRSKYQGILIVDTDDYGRTLVLDDYIQSSYYDEIYYHESLVHPAVTTHPRPSDVLILGGGEGATLREVLKHNTVKRAVMVDIDGDVVELSKKYLPQMHQGAFDDPRSEVRIEDGFVYVENALKRGEKFDVVIMDLTDPYSSDIAKQLYTPEFFGKVKRLLREDGIVVTQAGNSFYFPEAYDYVLQGVKGNFPIIAEYSVWIPSFGYAVNFVLGSLKHDPHSLSAEEVDKRLSERGVRAEFYSGKTHIALMNMPVIKKILRV | Function: Involved in the biosynthesis of polyamines which are thought to support the growth of thermophilic microorganisms under high-temperature conditions. It seems that long-chain and branched-chain of polyamines effectively stabilize DNA and RNA, respectively. Catalyzes the irreversible transfer of a propylamine g... |
O66615 | MAKTLGLHILADLYGVDADKIDRVEDIRELLEGAVKYANLTKISSHYYQFQPHGATGVVLLAESHISIHTWPEHGLATVDVYTCGDPSKAYRAMDYIITQLNPKRIDKQVHERGIVEEESNQSEAEKLRSILLQV | Cofactor: Binds 1 pyruvoyl group covalently per subunit.
Function: Catalyzes the decarboxylation of S-adenosylmethionine to S-adenosylmethioninamine (dcAdoMet), the propylamine donor required for the synthesis of the polyamines spermine and spermidine from the diamine putrescine.
PTM: Is synthesized initially as an ina... |
O28663 | MIVGRHIIAELYGVKEELIAKEEVVRSIVEEVVDKAELTKVGSVYKQFNPHGVTGIVLIAESHVSIHTWPEYGLVNLDIFTCGDTSKVEKAFKLFLEKFKPESYRHYVLDRG | Cofactor: Binds 1 pyruvoyl group covalently per subunit.
Function: Catalyzes the decarboxylation of S-adenosylmethionine to S-adenosylmethioninamine (dcAdoMet), the propylamine donor required for the synthesis of the polyamines spermine and spermidine from the diamine putrescine.
PTM: Is synthesized initially as an ina... |
O34426 | METMGRHVISELWGCDFDKLNDMDFIEKTFVNAALKSGAEVREVAFHKFAPQGVSGVVIISESHLTIHSFPEHGYASIDVYTCGDLDPNVAADYIAEALHADTRENIEIPRGMGPVQIKQAQAKVL | Cofactor: Binds 1 pyruvoyl group covalently per subunit.
Function: Catalyzes the decarboxylation of S-adenosylmethionine to S-adenosylmethioninamine (dcAdoMet), the propylamine donor required for the synthesis of the polyamines spermine and spermidine from the diamine putrescine.
PTM: Is synthesized initially as an ina... |
C0ZGF5 | MEYSTFGRHVAVDTWGVQFDLLNDAEFLKKEMIEAAEACGATVLSVQAKQFSPQGATVLVLLSESHLSIHTYPERGFAALDCYTCGETVDPQIAIDYLVSVLKPEKTYAKKLVRGLGELQVVEPEMKLVEAAK | Cofactor: Binds 1 pyruvoyl group covalently per subunit.
Function: Catalyzes the decarboxylation of S-adenosylmethionine to S-adenosylmethioninamine (dcAdoMet), the propylamine donor required for the synthesis of the polyamines spermine and spermidine from the diamine putrescine.
PTM: Is synthesized initially as an ina... |
Q8RA74 | MNALGRHILAEVYGCDSRILDDVEMIEDIMVQAAIATGAEVREVAFHKFNPQGVSGVVVISESHLTIHTWPELGYAAVDVFTCGDHVNPWDGVNYIARMLKAENMTATEVKRGVFEKPVKVANF | Cofactor: Binds 1 pyruvoyl group covalently per subunit.
Function: Catalyzes the decarboxylation of S-adenosylmethionine to S-adenosylmethioninamine (dcAdoMet), the propylamine donor required for the synthesis of the polyamines spermine and spermidine from the diamine putrescine.
PTM: Is synthesized initially as an ina... |
Q3AB53 | MNALGRHVIAELYGCGFDVLNDVKRVEEIMVRSALEAGAEIREVAFHKFSPQGVSGVVVISESHLAIHTWPELGYAAVDVFTCGDTVDPWDATNYLAKEFGAKYMTAKETKRGVMVEEFAESQAVNL | Cofactor: Binds 1 pyruvoyl group covalently per subunit.
Function: Catalyzes the decarboxylation of S-adenosylmethionine to S-adenosylmethioninamine (dcAdoMet), the propylamine donor required for the synthesis of the polyamines spermine and spermidine from the diamine putrescine.
PTM: Is synthesized initially as an ina... |
Q8L7L1 | MDRQPERENDELPSPAIISDRVLVNGVVTPLTLTAEGELRSTESGRRKSTLAKEILSFVVEGNKVRVKTLVEKGGGICCRGSAGDYARNDFVFEPLSDESRKLWSDKFHQHLVSLGRPKKLLVFVNPFGGKKTARKIFQEEVKPLFEDANIQLEIQETKYQLHAKEIVRSMDVSKYDGIVCVSGDGILVEVVNGLLEREDWKTAIKLPIGMVPAGSGNGMIKSLLEPVGLPCSATSATISIIRGRTRSLDVATISQGTTKFFSVLMLAWGLVADIDIESEKFRWMGSARFDIYGLQRIICLRQYHGRILFVPAPGFESYG... | Function: Involved in the production of sphingolipid metabolites. Phosphorylates sphingosine and various sphingoid long-chain base (LCB) products, such as phytosphingosine (PHS, 4-hydroxysphinganine), 4-hydroxy-8-sphingenine, 4,8-sphingadienine, D-erythro-dihydrosphingosine and D,L-threo-dihydrosphingosine. Is required... |
Q9Y657 | MKTPFGKTPGQRSRADAGHAGVSANMMKKRTSHKKHRSSVGPSKPVSQPRRNIVGCRIQHGWKEGNGPVTQWKGTVLDQVPVNPSLYLIKYDGFDCVYGLELNKDERVSALEVLPDRVATSRISDAHLADTMIGKAVEHMFETEDGSKDEWRGMVLARAPVMNTWFYITYEKDPVLYMYQLLDDYKEGDLRIMPDSNDSPPAEREPGEVVDSLVGKQVEYAKEDGSKRTGMVIHQVEAKPSVYFIKFDDDFHIYVYDLVKTS | Function: Chromatin reader that specifically recognizes and binds histone H3 both trimethylated at 'Lys-4' and asymmetrically dimethylated at 'Arg-8' (H3K4me3 and H3R8me2a) and acts as an activator of Wnt signaling pathway downstream of PRMT2. In case of cancer, promotes cell cancer proliferation via activation of the ... |
Q75GR5 | MSGLYSPGFSPARNLSPQIRSNPTDVDSQYLAELLAEHQKLGPFMQVLPICSKLLSQEIMRVSSIVHNHGFGDFDRHRFRSPSPMSSPNPRSNRSGNGFSPWNGLHQERLGFPQGTSMDWQGAPPSPSSHVVKKILRLDVPVDSYPNFNFVGRILGPRGNSLKRVEASTGCRVFIRGKGSIKDPGKEDKLRGKPGYEHLSDPLHILIEAEFPASIIDARLRHAQEVIEELLKPVDESQDFYKRQQLRELAMLNSTLREDSPHPGSVSPFSNGGMKRAKTGQ | Function: Involved in flowering time control. Binds DNA and RNA in vitro.
PTM: Ubiquitinated by SPL11. Ubiquitination probably leads to its subsequent degradation, thus negatively regulating flowering time control.
Sequence Mass (Da): 31285
Sequence Length: 281
Subcellular Location: Nucleus
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F6UH96 | MQLSVVDPTWELLDPNPDIRALFLEFNDTFFWGQLSGIEVKWSARMTLCAGVCSYEGRGGLCSIRLSEPLLKLRPRKDLVQTLLHEMIHALLFVTHNNKDHDSHGPEFCKHMERINKRTGANISVYHNFHDEVDEYRKHWWLCNGPCQKRKPYFGYVKRAMNRAPSSLDPWWADHQRTCGGEFVKIKEPENYSQKRKRNNDPTKSELGNSSHVKINKGKSNGVDIRTVIPFSGTGYKLFEPSKSDAQLKIQNDNPTKDKAVMHHTPPSTNQTDSTFLSRKIVSAKKISVANTKVFINLNGSPIKLPSSSNNKSHQDSSKQ... | Function: DNA-dependent metalloendopeptidase that mediates the proteolytic cleavage of covalent DNA-protein cross-links (DPCs) during DNA synthesis, thereby playing a key role in maintaining genomic integrity (By similarity). DPCs are highly toxic DNA lesions that interfere with essential chromatin transactions, such a... |
Q59072 | MDKYKNLTRSLTREFINLNPIQRGGILPKEAKKAVYEYWDGYSVCDYCHGRLDEVTCPPIKDFLEDIAKFLNMDCARPTHGAREGKFIVMHAICKEGDYVVLDKNAHYTSYVAAERAKLNVAEVGYEEEYPTYKINLEGYKEVIDNLEDKGKNVGLILLTHVDGEYGNLNDAKKVGKIAKEKGIPFLLNCAYTVGRMPVNGKEVKADFIVASGHKSMAASAPCGILAFSEEFSDKITKTSEKFPVKEIEMLGCTSRGLPIVTLMASFPHVVERVKKWDEELKKTRYVVDELEKIGFKQLGIKPKEHDLIKFETPVLDEIA... | Function: Converts O-phospho-L-seryl-tRNA(Cys) (Sep-tRNA(Cys)) to L-cysteinyl-tRNA(Cys) (Cys-tRNA(Cys)).
Catalytic Activity: H(+) + hydrogen sulfide + O-phospho-L-seryl-tRNA(Cys) = L-cysteinyl-tRNA(Cys) + phosphate
Sequence Mass (Da): 42764
Sequence Length: 377
EC: 2.5.1.73
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Q8TYR3 | MNLDRYRNIVRETERKYINVNPIQRGGVLTPEARKALLEFGDGYSVCDFCEGLLHEIEKPPIRQFHEDLAEFLGMDVVRITAGARYAKEAVMSALCEEGDVVVADSLAHYTTFVAAEKAGATVREVPNTGHPEYKVKVDEYARVIDEVEDERGDPPALALLTHVDSEYGNLADAEKFVKICRKKGVPALLNCAYTMGRMDLSNLSPKPDFMVGSGHKGMAACAPCGVLAMREEWEEEVLRGSSLRGDVSGREWPHKEVEMLGCTVMGAPIVTMMASFPHVVERVKRWKEEVRKTRWFVKEMERIEGVRQLGERPKRHDLV... | Function: Converts O-phospho-L-seryl-tRNA(Cys) (Sep-tRNA(Cys)) to L-cysteinyl-tRNA(Cys) (Cys-tRNA(Cys)).
Catalytic Activity: H(+) + hydrogen sulfide + O-phospho-L-seryl-tRNA(Cys) = L-cysteinyl-tRNA(Cys) + phosphate
Sequence Mass (Da): 44252
Sequence Length: 392
EC: 2.5.1.73
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Q94BN2 | MEGDVGIGLVCQNTMDGKASNGNGLEKTVPSCCLKAMACVPEDDAKCHSTVVSGWFSEPHPRSGKKGGKAVYFNNPMWPGEAHSLKVEKVLFKDKSDFQEVLVFESATYGKVLVLDGIVQLTEKDECAYQEMIAHLPLCSISSPKNVLVVGGGDGGVLREISRHSSVEVIDICEIDKMVIDVSKKFFPELAVGFDDPRVQLHIGDAAEFLRKSPEGKYDAIIVDSSDPVGPALALVEKPFFETLARALKPGGVLCNMAESMWLHTHLIEDMISICRQTFKSVHYAWSSVPTYPSGVIGFVLCSTEGPAVDFKNPINPIEK... | Catalytic Activity: S-adenosyl 3-(methylsulfanyl)propylamine + spermidine = H(+) + S-methyl-5'-thioadenosine + spermine
Sequence Mass (Da): 39239
Sequence Length: 359
Pathway: Amine and polyamine biosynthesis; spermine biosynthesis; spermine from spermidine: step 1/1.
EC: 2.5.1.22
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Q3SZA5 | MAAARHSTLDFMLGAKADGETILKGLQSIFQEQGMTESVHTWQDHGYLATYINKNGSFANLRIYPHGLVLLDLQSYDGDAQGKEVDSLLNKVEERMKELSQDSTERVKRLPPIVRGGAIDRYWPTADGRLVEYDIDKVVYDEDSPYQNIKILHSKQFGNILILSGDVNLAESDLAYTRAIMGSGKEDYSGKDVLILGGGDGGILCEIVKLKPKMVTMVEIDQMVIDGCKKYMRKTCGDVLDNLKGDCYQVLIEDCIPVLKRYAKEGREFDYVINDLTAVPISTSPEEDSTWEFLRLILDLSMKVLKQDGKYFTQGNCVNL... | Function: Catalyzes the production of spermine from spermidine and decarboxylated S-adenosylmethionine (dcSAM).
Catalytic Activity: S-adenosyl 3-(methylsulfanyl)propylamine + spermidine = H(+) + S-methyl-5'-thioadenosine + spermine
Sequence Mass (Da): 41224
Sequence Length: 365
Domain: Composed of 3 domains: the N-term... |
P52788 | MAAARHSTLDFMLGAKADGETILKGLQSIFQEQGMAESVHTWQDHGYLATYTNKNGSFANLRIYPHGLVLLDLQSYDGDAQGKEEIDSILNKVEERMKELSQDSTGRVKRLPPIVRGGAIDRYWPTADGRLVEYDIDEVVYDEDSPYQNIKILHSKQFGNILILSGDVNLAESDLAYTRAIMGSGKEDYTGKDVLILGGGDGGILCEIVKLKPKMVTMVEIDQMVIDGCKKYMRKTCGDVLDNLKGDCYQVLIEDCIPVLKRYAKEGREFDYVINDLTAVPISTSPEEDSTWEFLRLILDLSMKVLKQDGKYFTQGNCVN... | Function: Catalyzes the production of spermine from spermidine and decarboxylated S-adenosylmethionine (dcSAM).
Catalytic Activity: S-adenosyl 3-(methylsulfanyl)propylamine + spermidine = H(+) + S-methyl-5'-thioadenosine + spermine
Sequence Mass (Da): 41268
Sequence Length: 366
Domain: Composed of 3 domains: the N-term... |
P97355 | MAAARHSTLDFKLGAKADGEAILKGLQSIFQEQGMTESVHTWQDHGYLATYTNKNGSFANLRIYPHGLVLLDLQSYDSDVQGKQETDSLLNKIEEKMKELSQDSTGRVKRLPPIVRGGAIDRYWPTADGRLVEYDIDEVVYDEDSPYQNIKILHSKQFGNILILSGDVNLAESDLAYTRAIMGSGKEDYTGKDVLILGGGDGGILCEIVKLKPKMVTMVEIDQMVIDGCKKYMRRTCGDVLDNLRGDCYQVLIEDCIPVLKMYAKEGREFDYVINDLTAVPISTSPEEDSTWDFLRLILDLSMKVLKQDGKYFTQGNCVN... | Function: Catalyzes the production of spermine from spermidine and decarboxylated S-adenosylmethionine (dcSAM) . Required for normal viability, growth and fertility .
Catalytic Activity: S-adenosyl 3-(methylsulfanyl)propylamine + spermidine = H(+) + S-methyl-5'-thioadenosine + spermine
Sequence Mass (Da): 41313
Sequenc... |
Q12455 | MVNNSQHPYIKDGWFREINDKSFPGQAFTMTVDSILYEARSEFQDILIFRNKVYGTVLVLDGIVQCTEFDEFAYQEMITHIAMFAHSNPKRVLIIGGGDGGVLREVAKHSCVEDITMVEIDSSVIELSRKFLPTLSNGAFDDERLDLKLCDGFKFLQDIGASDVHKKFDVIITDSSDPEGPAEAFFQERYFELLKDALNPNGVVIMQSSENFWLNLKYLHDLKNTAKKVFPNTEYCYTMVPTYTSGQLGLIVCSNNANIPLNIPQRKISEQEQGKLKYYNPQIHSSAFVLPTWADKVINE | Catalytic Activity: S-adenosyl 3-(methylsulfanyl)propylamine + spermidine = H(+) + S-methyl-5'-thioadenosine + spermine
Sequence Mass (Da): 34091
Sequence Length: 300
Pathway: Amine and polyamine biosynthesis; spermine biosynthesis; spermine from spermidine: step 1/1.
EC: 2.5.1.22
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Q9PTL1 | NPCSCSQSHCCSRYLCMGAMSLFLPCLLCYPPAKGCLKLCRGCYDRVNRPGCRCKNSNTVYCKLESCPSRGQGKPS | Function: Inhibits fibroblast growth factor (FGF)-induced retinal lens fiber differentiation (By similarity). Inhibits TGFB-induced epithelial-to-mesenchymal transition in lens epithelial cells (By similarity).
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 8349
Sequence Length: 76
Domain: The Cys-r... |
Q9Y6N5 | MVPLVAVVSGPRAQLFACLLRLGTQQVGPLQLHTGASHAARNHYEVLVLGGGSGGITMAARMKRKVGAENVAIVEPSERHFYQPIWTLVGAGAKQLSSSGRPTASVIPSGVEWIKARVTELNPDKNCIHTDDDEKISYRYLIIALGIQLDYEKIKGLPEGFAHPKIGSNYSVKTVEKTWKALQDFKEGNAIFTFPNTPVKCAGAPQKIMYLSEAYFRKTGKRSKANIIFNTSLGAIFGVKKYADALQEIIQERNLTVNYKKNLIEVRADKQEAVFENLDKPGETQVISYEMLHVTPPMSPPDVLKTSPVADAAGWVDVDK... | Cofactor: Binds 1 FAD per subunit.
Function: Catalyzes the oxidation of hydrogen sulfide with the help of a quinone, such as ubiquinone-10, giving rise to thiosulfate and ultimately to sulfane (molecular sulfur) atoms. Requires an additional electron acceptor; can use sulfite, sulfide or cyanide (in vitro) . It is beli... |
Q9R112 | MAPLVTVVSSPRARLFACFLRLGTQQAGPLQLHTGACCTAKNHYEVLVLGGGAGGITMATRMKRRVGAENVAIVEPSERHFYQPIWTLVGAGAKELSLSVRSTLSVIPSGVQWIQDRVAELNPDENCIRTDSGKEISYRYLIIALGIQLDYEKIKGLPEGFAYPKIGSNYSVKTVEKTWKALQGFKEGNALFTFPNTPVKCAGAPQKIMYLSEAYFRKTGKRPKANIIFNTALGTIFGVKKYADALQEIIRERDVSVNYKHNLIEVRPDKQEAVFEILDKPGETHVIPYEMLHVTPPMSAPDVLKRSPVADSAGWVDVDK... | Cofactor: Binds 1 FAD per subunit.
Function: Catalyzes the oxidation of hydrogen sulfide with the help of a quinone, such as ubiquinone-10, giving rise to thiosulfate and ultimately to sulfane (molecular sulfur) atoms. Requires an additional electron acceptor; can use sulfite, sulfide or cyanide (in vitro). It is belie... |
Q7ZAG8 | MTKVLVLGGRFGALTAAYTLKRLVGSKADVKVINKSRFSYFRPALPHVAIGVRDVDELKVDLSEALPEKGIQFQEGTVEKIDAKSSMVYYTKPDGSMAEEEYDYVIVGIGAHLATELVKGWDKYGYSVCEPEFATKLREKLESFQGGNIAIGSGPFYQGHNPKPKVPENFVPNADSACEGPVFEMSLMLHGYFKKKGMLDKVHVTVFSPGEYLSDLSPNSRKAVASIYNQLGIKLVHNFKIKEIREHEIVDEKGNTIPADITILLPPYTGNPALKNSTPDLVDDGGFIPTDLNMVSIKYDNVYAVGDANSMTVPKLGYLA... | Cofactor: Binds 1 FAD per subunit.
Function: Catalyzes the oxidation of sulfides, such as hydrogen sulfide, with the help of a quinone. Has the highest activity with caldariella quinone and decylubiquinone, and lower activity with naphtoquinones. Consecutive reaction cycles lead to the accumulation of a polysulfide pro... |
B7JBP8 | MAHVVILGAGTGGMPAAYEMKEALGSGHEVTLISANDYFQFVPSNPWVGVGWKERDDIAFPIRHYVERKGIHFIAQSAEQIDAEAQNITLADGNTVHYDYLMIATGPKLAFENVPGSDPHEGPVQSICTVDHAERAFAEYQALLREPGPIVIGAMAGASCFGPAYEYAMIVASDLKKRGMRDKIPSFTFITSEPYIGHLGIQGVGDSKGILTKGLKEEGIEAYTNCKVTKVEDNKMYVTQVDEKGETIKEMVLPVKFGMMIPAFKGVPAVAGVEGLCNPGGFVLVDEHQRSKKYANIFAAGIAIAIPPVETTPVPTGAPK... | Cofactor: Binds 1 FAD per subunit.
Function: Catalyzes the oxidation of hydrogen sulfide, with the help of a quinone. Consecutive reaction cycles lead to the accumulation of a polysulfide product on the active site Cys residues; these products are released when they exceed a critical length, typically as cyclooctasulfu... |
O67931 | MAKHVVVIGGGVGGIATAYNLRNLMPDLKITLISDRPYFGFTPAFPHLAMGWRKFEDISVPLAPLLPKFNIEFINEKAESIDPDANTVTTQSGKKIEYDYLVIATGPKLVFGAEGQEENSTSICTAEHALETQKKLQELYANPGPVVIGAIPGVSCFGPAYEFALMLHYELKKRGIRYKVPMTFITSEPYLGHFGVGGIGASKRLVEDLFAERNIDWIANVAVKAIEPDKVIYEDLNGNTHEVPAKFTMFMPSFQGPEVVASAGDKVANPANKMVIVNRCFQNPTYKNIFGVGVVTAIPPIEKTPIPTGVPKTGMMIEQM... | Cofactor: Binds 1 FAD per subunit.
Function: Catalyzes the oxidation of hydrogen sulfide, with the help of a quinone. Consecutive reaction cycles lead to the accumulation of a polysulfide product on the active site Cys residues; these products are released when they exceed a critical length, typically as cyclooctasulfu... |
O48666 | MGSLGAILKHPEDFYPLLKLKFAARHAEKQIPPEPHWAFCYSMLHKVSRSFGLVIQQLGPQLRDAVCIFYLVLRALDTVEDDTSIPTEVKVPILMAFHRHIYDKDWHFSCGTKEYKVLMDEFHHVSNAFLELGSGYQEAIEDITMRMGAGMAKFICKEVETINDYDEYCHYVAGLVGLGLSKLFHASGAEDLATDSLSNSMGLFLQKTNIIRDYLEDINEIPKSRMFWPRQIWSKYVDKLEDLKYEENSAKAVQCLNDMVTDALVHAEDCLKYMSDLRGPAIFRFCAIPQIMAIGTLALCFNNTQVFRGVVKMRRGLTAK... | Function: Component of the triterpene saponins (e.g. ginsenosides or panaxosides) and phytosterols biosynthetic pathways . Catalyzes the biosynthesis of squalene .
Catalytic Activity: 2 (2E,6E)-farnesyl diphosphate + H(+) + NADH = 2 diphosphate + NAD(+) + squalene
Location Topology: Multi-pass membrane protein
Sequence... |
P84109 | LNRDDDSDLHSPRYSFSEDTKCDDGWFVGTSRRTK | Function: Plays a role in tyrosine phosphorylation of CBL by linking CBL to the insulin receptor. Required for insulin-stimulated glucose transport. Involved in formation of actin stress fibers and focal adhesions (By similarity).
PTM: O-glycosylated.
Sequence Mass (Da): 4107
Sequence Length: 35
Subcellular Location: C... |
G5EE56 | MGCLFSKERRSGGSDMGVSERIDVSRFQTPQQQTVFHVNNGGNEGTISQLNGTSDGMMGNGRGGGGGGGAQERETLVALYPYDSRADGDLSFQKGDAMYLLDHSNCDWWYVRHQRTGQTGYVPRNFVAKQQTIESEEWYAGKIPRNRAERLVLSSHLPKGTFLIREREADTREFALTIRDTDDQRNGGTVKHYKIKRLDHDQGYFITTRRTFRSLQELVRYYSDVPDGLCCQLTFPAPRLAPTRPDLSHDTQQNWEIPRNQLHLKRKLGDGNFGEVWYGKWRGIVEVAIKTMKPGTMSPEAFLQEAQIMKQCDHPNLVKL... | Function: Non-receptor tyrosine-protein kinase which plays a role in endoderm development by controlling spindle orientation in EMS blastomere, probably downstream of receptor mes-1. Also involved in embryonic body morphogenesis, especially in the formation of the pharynx and the intestine . May be dispensable for phar... |
Q03707 | MNSDLEYLEDGFDPNSMKVATLRRILVENNVDFPSNARKNALVGLFDEKVKPQIPQLRKMYLNVRPSDEGIVKMDRPSSSPSIASPRRSRRARREKSASPMAKQFKKNRILDDVSNDDDDDDDDDDDNDKKDDPLIVPSGTDTDEVDDEEDDVITSSSNKSDTNDFQQNSDTRKKRKDPDSDDWSESNSKENKIDNKHLNLLSSDSEIEQDYQKAKKRKTSDLNQEHGNGSAILGKLSVKTPIKNTNRKPVSMDNFNDSLTSSGTENDPFVPNIRHNPKELGTANGTGHSTPLSKLKVSASFADKLPQKEVPSTILVPEV... | Function: Plays a role in sister chromatid separation.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 95498
Sequence Length: 834
Subcellular Location: Nucleus inner membrane
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O04023 | MECRSLDLTIISAEDLKDVQLIGKQDLYAVVSINGDARTKQKTKVDKDCGTKPKWKHQMKLTVDDAAARDNRLTLVFEIVADRPIAGDKPVGEVSVPVKELLDQNKGDEEKTVTYAVRLPNGKAKGSLKFSFKFGEKYTYGSSSGPHAPVPSAMDHKTMDQPVTAYPPGHGAPSAYPAPPAGPSSGYPPQGHDDKHDGVYGYPQQAGYPAGTGGYPPPGAYPQQGGYPGYPPQQQGGYPGYPPQGPYGYPQQGYPPQGPYGYPQQQAHGKPQKPKKHGKAGAGMGLGLGLGAGLLGGLLVGEAVSDIADMGDMGDMGDMG... | Function: May act as an activator of the calcium-dependent activation of RBOHF that mediates reactive oxygen species (ROS) production and may play a role in cold responses.
Location Topology: Single-pass type II membrane protein
Sequence Mass (Da): 34189
Sequence Length: 324
Subcellular Location: Endoplasmic reticulum ... |
O04133 | MTMEYRTLELNIISAKDIKNVNLFSKMDVYAAVSLSGDPLHPQGATTHVHKDAGSNPTWNYPVKFSVNESLAKENRLSLEIKLISDRTLGDTVIGTVHVPLRELLDNPGDDSSFRQVSYQVMKQSRKSKGSLNFSYKFGEHVPAPAAKTPKAAKAGQEPVMAYPPAGAGSSSMPYGTPHPPPPQQYAATGYGYPPQQVHGGYPPQAAYGYPPQTGYGYPQQSGYGYPQQSGYGYPPQAQKPKKNKFGMGLGAGLLGGALGGMLIGDMVSDAAEYDAGYDAGFDDAGGFDF | Function: May play a role in cold responses.
Location Topology: Single-pass type II membrane protein
Sequence Mass (Da): 31011
Sequence Length: 290
Subcellular Location: Endoplasmic reticulum membrane
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Q8L3X8 | MRRYSPPYYSPPRRGYGGRGRSPPPPPPRRGYGGGGGGGGRRGSSHGSLLVRNIPLDCRPEELREPFERFGPVRDVYIPRDYYSGQPRGFAFVEFVDAYDAGEAQRSMNRRSFAGREITVVVASESRKRPEEMRVKTRTRSREPSGSRDRSHGRSRSRSISRSRSPRRPSDSRSRYRSRSYSPAPRRRGGPPRGEEDENYSRRSYSPGYEGAAAAAPDRDRNGDNEIREKPGYEAEDRRRGGRAVSRSPSGSRSRSVEVSPR | Function: Involved in intron recognition and spliceosome assembly (Probable). Probably active at the 5' splice sites.
PTM: Phosphorylated.
Sequence Mass (Da): 29567
Sequence Length: 262
Subcellular Location: Nucleus speckle
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Q9SEU4 | MRGRSYTPSPPRGYGRRGRSPSPRGRYGGRSRDLPTSLLVRNLRHDCRQEDLRKSFEQFGPVKDIYLPRDYYTGDPRGFGFVQFMDPADAADAKHHMDGYLLLGRELTVVFAEENRKKPTEMRARERGGGRFRDRRRTPPRYYSRSRSPPPRRGRSRSRSGDYYSPPPRRHHPRSISPREERYDGRRSYSRSPASDGSRGRSLTPVRGKSRSLSPSPRRSISRSPRRSRSPSPKRNRSVSPRRSISRSPRRSRSPRRSRRSYTPEPARSRSQSPHGGQYDEDRSPSQ | Function: Involved in intron recognition and spliceosome assembly. Binds to multiple 5'-GAAG-3' repeats found in its third intron, suggesting autoregulation of alternative splicing . May be necessary for accurate splicing of the 3' region of introns.
PTM: Phosphorylated by AFC2.
Sequence Mass (Da): 33337
Sequence Lengt... |
Q9V9J3 | MGNCLTTQKGEPDKPADRIKLDDPPTIGVGVGVPQIPMPSHAGQPPEQIRPVPQIPESETAGANAKIFVALYDYDARTDEDLSFRKGEHLEILNDTQGDWWLARSKKTRSEGYIPSNYVAKLKSIEAEPWYFRKIKRIEAEKKLLLPENEHGAFLIRDSESRHNDYSLSVRDGDTVKHYRIRQLDEGGFFIARRTTFRTLQELVEHYSKDSDGLCVNLCKPCVQIEKPVTEGLSHRTRDQWEIDRTSLKFVRKLGSGQFGDVWEGLWNNTTPVAIKTLKSGTMDPKDFLAEAQIMKKLRHTKLIQLYAVCTVEEPIYIIT... | Function: Required directly or indirectly for the phosphorylation of drpr which is necessary for the interaction of drpr with shark and subsequent glial phagocytic activity . Together with drpr and shark, promotes the migration of macrophages to sites of wounding as part of a signaling cascade where Scr42a detects prod... |
P00528 | MGNKCCSKRQDQELALAYPTGGYKKSDYTFGQTHINSSGGGNMGGVLGQKHNNGGSLDSRYTPDPNHRGPLKIGGKGGVDIIRPRTTPTGVPGVVLKRVVVALYDYKSRDESDLSFMKGDRMEVIDDTESDWWRVVNLTTRQEGLIPLNFVAEERSVNSEDWFFENVLRKEADKLLLAEENPRGTFLVRPSEHNPNGYSLSVKDWEDGRGYHVKHYRIKPLDNGGYYIATNQTFPSLQALVMAYSKNALGLCHILSRPCPKPQPQMWDLGPELRDKYEIPRSEIQLLRKLGRGNFGEVFYGKWRNSIDVAVKTLREGTMS... | Function: May play a role in the development of neural tissue and smooth muscle.
PTM: Phosphorylated.
Catalytic Activity: ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-[protein]
Sequence Mass (Da): 63003
Sequence Length: 552
EC: 2.7.10.2
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Q01406 | MTVLLLVVLQMWKATAGHSIAVSQDDGADDWETDPDFVNDVSEKEQRWGAKTVKGSGHQEHINIHQLRENVFQEHQTIKEKELETGPKASHGYGGKFGVEQDRMDKSAVGHEYQSKLSKHCSQVDSVKGFGGKFGVQTDRVDQSAVGFEYQGKTEKHASQKDYSSGFGGKYGVQADRVDKSAVGFDYQGKTEKHESQKDYSKGFGGKYGVDKDKVDKSAVGFEYQGKTEKHESQKDYVKGFGGKFGVQTDRQDKCALGWDHQEKVQLHESQKDYKSGFGGKFGVQTERQDPSAVGFDYKEKLAKHESQQDYSKGFGGKYG... | Function: Contributes to the organization of the actin cytoskeleton and cell shape (By similarity). Plays a role in the formation of lamellipodia and in cell migration (By similarity). Plays a role in the regulation of neuron morphology, axon growth and formation of neuronal growth cones, and may play a role in the reg... |
Q75K18 | MVLADLGNQLSSALRSLNETTIVNEDTINQLLKEVGNALSKSDVSMSLIIQMRKNIKDKIKLDQMAAGLNKRKIIKQVVFDELIRLLDPGVPLWKPTKGKSNIVMFVGLQGAGKTTSVTKLAYFYKKKGFSTAIVCADTFRAGAFDQVRHNAAKAKIHYYGSETEKDPVVVARTGVDIFKKDGTEIIIVDTSGRHKQDSELFEEMKQIETAVKPDNCIFVMDSSIGQAAYEQATAFRSSVKVGSIIITKMDGNSMGGGAISAVAATNTPIIFIGTGEHLTDLELFDPSTFVSKLLGYGDMKGMLEKIKEVIPEDSTSLKE... | Function: Component of the signal recognition particle (SRP) complex, a ribonucleoprotein complex that mediates the cotranslational targeting of secretory and membrane proteins to the endoplasmic reticulum (ER). As part of the SRP complex, associates with the SRP receptor (SR) component srpra to target secretory protei... |
O15821 | MVLSQLGSSLVTALRKMTSSTVVDEEVINTLLKEIETSLLGEDVNPIFIRQMVNNIKKKINSEDIPDGIDKRKLIKDSVFEELINLVDPKTEAFKPKKGKTCVLMMVGLQGAGKTTTITKLALYYKNRGYKPAVVGADTFRAGAYEQLQMNAKRAGVPFFGIKEESDPVKVASEGVRTFRKEKNDIILVDTSGRHKQDKELFKEMQSVRDAIKPDSIIFVMDGAIGQAAFGQAKAFKDAVEVGSVIITKLDGHSNGGGALSAVAATKSPIIFIGTGEKVNEIEEFDAESFVRKLLGMGDLKGIAKLAKDFAENAEYKTMV... | Function: Component of the signal recognition particle (SRP) complex, a ribonucleoprotein complex that mediates the cotranslational targeting of secretory and membrane proteins to the endoplasmic reticulum (ER). As part of the SRP complex, associates with the SRP receptor (SR) component SRPRA to target secretory protei... |
Q8MZJ6 | MVLADLGRKITTALLPRQRTVINEEVLQAMLKEICTALLEADVNVKLVGKLRQNVRAAIDFEDMGAGLSKRRIIQTSVFNELCKLLDPGVPVWHPTKGHSNVIMFVGLQGSGKTTTCTKLAYHYQKKGWKTCLVCADTFRAGAFDQLKQNATKARVPFYGSYTEMDPVVIAQEGVEKFKEDSFEVIIVDTSGRHKQEESLFEEMLQVSQAIDPDNIIFVMDGTIGQACESQARAFKEKVDVASVIVTKLDGHAKGGGALSAVAATRSPIIFIGTGEHIDEMEPFKTKPFVSKLLGMGDLEGLMEKVSDLKLDENEELMDK... | Function: Component of the signal recognition particle (SRP) complex, a ribonucleoprotein complex that mediates the cotranslational targeting of secretory and membrane proteins to the endoplasmic reticulum (ER) (By similarity). As part of the SRP complex, associates with the SRP receptor (SR) component SRPRA to target ... |
P44518 | MFENLSDRLSKTLRNITGKGRLTEDNIKETLREVRMALLEADVALPVVREFIAKVKESALGEEVNKSLTPGQEFLKIVQRELEKAMGEANESLNLATQPPAVILMAGLQGAGKTTSVGKLAKFLRERHKKKVLVVSADVYRPAAIKQLETLAQSVGVDFFPSDVKQNPVDIAKSALADAKLKFYDVLIVDTAGRLHVDTEMMDEIKQVHAALNPIETLFTVDAMTGQDAANTAKAFNEALPLTGVILTKVDGDARGGAALSIRQITGKPIKFLGVGEKTEALEPFHPDRVASRILGMGDVLSLIEDLERSVDREKAEKMA... | Function: Involved in targeting and insertion of nascent membrane proteins into the cytoplasmic membrane. Binds to the hydrophobic signal sequence of the ribosome-nascent chain (RNC) as it emerges from the ribosomes. The SRP-RNC complex is then targeted to the cytoplasmic membrane where it interacts with the SRP recept... |
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