ids stringlengths 6 10 | seqs stringlengths 11 1.02k | texts stringlengths 108 11.1k |
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B6YRV8 | MKIRIGFGYDVHPLVMNYNLWLGGIKIPYEKGLKGHSDADVLIHALCDALLGAADIGNIGTNFPNTNKKLRNIDSKILLKQTMSFIYSKNYELNNADITVCIEQPKLNPFIPQMKTCLAEIMQTDKGNISIKATTSEKMGFIGREEGIAVFATVLITPINEIGISCQ | Cofactor: Binds 1 divalent metal cation per subunit.
Function: Involved in the biosynthesis of isopentenyl diphosphate (IPP) and dimethylallyl diphosphate (DMAPP), two major building blocks of isoprenoid compounds. Catalyzes the conversion of 4-diphosphocytidyl-2-C-methyl-D-erythritol 2-phosphate (CDP-ME2P) to 2-C-meth... |
Q1IVA8 | MIRVGLGFDSHEFREGIPLRIGGLTIPHTHGLSGHSDGDVLLHAITDALLGAVAAGDIGAFFPPSDPKWKGANSVVFIEEAMRHIETAGYRVGNVDCSLVLNAPKIGPHAKAIQESVAKLLKIEPTAVGIKAKTPEGLNLDGTALAHVVVLLEKR | Cofactor: Binds 1 divalent metal cation per subunit.
Function: Involved in the biosynthesis of isopentenyl diphosphate (IPP) and dimethylallyl diphosphate (DMAPP), two major building blocks of isoprenoid compounds. Catalyzes the conversion of 4-diphosphocytidyl-2-C-methyl-D-erythritol 2-phosphate (CDP-ME2P) to 2-C-meth... |
C5CGG7 | MYRVGIGFDAHPLEANKKGLYLGGVKVSEEYSSIGHSDGDALIHAIVDAILGATNAGNIGIWFPENEENRGRRSTEFLEIIRKKILAGKYEILNIDSVIIIDKVRMNPHIENIRLKLARILGISKGNINVKPKSGNTLYGNSVSVYAVCMLKKVGT | Cofactor: Binds 1 divalent metal cation per subunit.
Function: Involved in the biosynthesis of isopentenyl diphosphate (IPP) and dimethylallyl diphosphate (DMAPP), two major building blocks of isoprenoid compounds. Catalyzes the conversion of 4-diphosphocytidyl-2-C-methyl-D-erythritol 2-phosphate (CDP-ME2P) to 2-C-meth... |
Q8F0A5 | MYRIGNGIDFHKLEINLNRPLILGGIECESEFALVGHSDADIILHAISDAILGALALGDIGQYFPDTDPSLKNIDSKIILVKCLELMKEKNFDLVNIDCTVIGERPKITPLKDRITKSLSNLLNLPLDCISVKATTTEKMGALGRQEGIGTFCSILLEKRS | Cofactor: Binds 1 divalent metal cation per subunit.
Function: Involved in the biosynthesis of isopentenyl diphosphate (IPP) and dimethylallyl diphosphate (DMAPP), two major building blocks of isoprenoid compounds. Catalyzes the conversion of 4-diphosphocytidyl-2-C-methyl-D-erythritol 2-phosphate (CDP-ME2P) to 2-C-meth... |
Q8YAB4 | MIRIGQGYDVHKLAYDRDLIIGGVKIPYEKGLLGHSDADVLLHAITDAIIGAIGAGDIGHFFPDTDMVFKDADSAELLAEIWQKVEADGFRLGNLDATIIAEKPKMAPYVEQMKLRIAELLHADSAQVNVKATTTEKLGFTGREEGIASLAVVLLEK | Cofactor: Binds 1 divalent metal cation per subunit.
Function: Involved in the biosynthesis of isopentenyl diphosphate (IPP) and dimethylallyl diphosphate (DMAPP), two major building blocks of isoprenoid compounds. Catalyzes the conversion of 4-diphosphocytidyl-2-C-methyl-D-erythritol 2-phosphate (CDP-ME2P) to 2-C-meth... |
Q8RG40 | MERNTRVVKVANLKIGGNNPIIIQSMTNTNSADVEATVKQINNLEKVGCQLVRMTINNIKAAEAIKEIKKKVSLPLVADIHFDYRLALLAIKNGIDKLRINPGNIGSDENVKKVVEAAKEKNIPIRIGVNSGSIEKEILEKYGKPCVDALVESAMYHIRLLEKFDFFDIIVSLKSSNVKMMVEAYRKISSLVDYPLHLGVTEAGTKFQGTVKSAIGIGALLVDGIGDTLRVSLTENPVEEIKVAKEILKVLDLSDEGVEIISCPTCGRTEIDLIGLAKQVEEEFRTKKNKFKIAVMGCVVNGPGEAREADYGIAAGRGIG... | Cofactor: Binds 1 [4Fe-4S] cluster.
Function: Converts 2C-methyl-D-erythritol 2,4-cyclodiphosphate (ME-2,4cPP) into 1-hydroxy-2-methyl-2-(E)-butenyl 4-diphosphate.
Catalytic Activity: (2E)-4-hydroxy-3-methylbut-2-enyl diphosphate + 2 H(+) + H2O + oxidized [flavodoxin] = 2-C-methyl-D-erythritol 2,4-cyclic diphosphate + ... |
Q7NS59 | MTKTIMLANPRGFCAGVDRAIAIVERAIELYGAPIYVRHEVVHNRFVVDDLRGKGAVFIEELKDVPPGSTLIYSAHGVPLSVRAEAEALGLTVFDATCPLVTKVHVEVKRMNKAGMEIIMIGHAGHPEVEGTMGQVDAGIYLVQTVDDVATLRVVNEDQLSYVSQTTLSVDETRDIIAALKARFPNIHSPKKDDICYATQNRQDAVKLLADQCDIVVVVGSPNSSNSNRLREVAALKGVDAYMVDNASLLEPEWFAGKRRVGVTAGASAPEVLVQAVIDRIKAFDVTQVTELPGVEESTVFALPPALRPLF | Cofactor: Binds 1 [4Fe-4S] cluster per subunit.
Function: Catalyzes the conversion of 1-hydroxy-2-methyl-2-(E)-butenyl 4-diphosphate (HMBPP) into a mixture of isopentenyl diphosphate (IPP) and dimethylallyl diphosphate (DMAPP). Acts in the terminal step of the DOXP/MEP pathway for isoprenoid precursor biosynthesis.
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B5E9S9 | MQVILAKHAGFCFGVKRATQLAFQAANIGSETYTLGPIIHSPQVVQRLEEMGVIPVDNVSEVETGGTIIIRSHGVAAEELEAAVRANLEVVDATCPFVKKAQEHVATLSKEGYDIVVVGDAVHPEVQGIVSYAAGRVYVVSSHKDVERLPRMSKIGVVAQTTQSFEHLHEVVAACLARGGEARVYNTICDATAVRQEEAKKLAGAVDCMVVIGGFNSANTMRLAQICLELLPRTHHVETASQIDEQWFKGVKKVGVTAGASTPKWIIDEVIDRISAIDKDKIS | Cofactor: Binds 1 [4Fe-4S] cluster per subunit.
Function: Catalyzes the conversion of 1-hydroxy-2-methyl-2-(E)-butenyl 4-diphosphate (HMBPP) into a mixture of isopentenyl diphosphate (IPP) and dimethylallyl diphosphate (DMAPP). Acts in the terminal step of the DOXP/MEP pathway for isoprenoid precursor biosynthesis.
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Q97I09 | MRKVMLAEKAGFCFGVKRAVDMALLTQKEYNKKIYTLGELIHNNDVVDKLKDNNVYPIGIEDIDNLKENDVILIRSHGISEEIYKILLSKGLTVINATCPFVTKIQEKVKKYNELGYDIVIVGDKYHPEVIGINGWCDNKAIISKQGENLENITSESKVCIVSQTTEKLENWEKVLKEVKNRAIEVISFNTICNATSERQKIAKDLSNKVDFMVVIGGKQSSNTTKLYEICKSNCNETIHVENSGEIPENILKNKNCVIGVTAGASTPDWIIEEAISKMSENQISNETNNEMADAMKFIAENEGKIYVGASVTGEIIQVS... | Cofactor: Binds 1 [4Fe-4S] cluster per subunit.
Function: Catalyzes the conversion of 1-hydroxy-2-methyl-2-(E)-butenyl 4-diphosphate (HMBPP) into a mixture of isopentenyl diphosphate (IPP) and dimethylallyl diphosphate (DMAPP). Acts in the terminal step of the DOXP/MEP pathway for isoprenoid precursor biosynthesis.
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Q187C6 | MNIKIAKNAGFCFGVKRAMKMAWDEVEKNDSGIYALGPLIHNKQAVAKYEEKGLKTVNEIDTIPNHENMIIRSHGVPENIYKEAKDKKLKIVDTTCPFVKKIHTVVSEYHNKGYEIIVIGDMKHPEVIGINGWCENSAIIIKTLEQMENMEFDNSKRYCLVAQTTINPELYISIVNKLSDKLEEIVFNDTICSATKTRQESAKELAKEVDCMIVIGGKHSSNTQKLVKVCEDLVPTFAIETKDELDVNTLKKYKNLGITAGASTPNWIIEEVVTFLENL | Cofactor: Binds 1 [4Fe-4S] cluster per subunit.
Function: Catalyzes the conversion of 1-hydroxy-2-methyl-2-(E)-butenyl 4-diphosphate (HMBPP) into a mixture of isopentenyl diphosphate (IPP) and dimethylallyl diphosphate (DMAPP). Acts in the terminal step of the DOXP/MEP pathway for isoprenoid precursor biosynthesis.
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P58675 | MERNVILAKNAGFCFGVKRAVDEAIKYQKEFGKKIYTLGPLIHNNDVVNYLEDNNIFAIELSDADSLKKGDVVLIRSHGVKESVIKDLTDKGLIVKNATCPYVTNIQLKVKKCYEQGYKIIIVGDKNHPEVIGINGWCNDSAIITNGKTELENIPAKVCVVSQTTEKKETWNKVLNEIVRASKEIVAFNTICSATDVRQKSVQELSKEADLVFVIGGKNSSNTTKLYEICKKECPKSYHIENVKELDESLLEDESVKTIGITAGASTPDWIINEVISKIKEL | Cofactor: Binds 1 [4Fe-4S] cluster per subunit.
Function: Catalyzes the conversion of 1-hydroxy-2-methyl-2-(E)-butenyl 4-diphosphate (HMBPP) into a mixture of isopentenyl diphosphate (IPP) and dimethylallyl diphosphate (DMAPP). Acts in the terminal step of the DOXP/MEP pathway for isoprenoid precursor biosynthesis.
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Q11YY5 | MDVIIDKNSGYCFGVEFAIQMAEDEMATGEPLFCLGDIVHNSMEVERLAKKGLKIIDREELKKLSDCKVLIRAHGEPPETYQLALENNIELVDASCPVVLKLQNRVKASFDAIDSKDGQIVIYGQEGHAEVIGIAGQTGDKAIVITTEKDLDKIDFEKPVTLYSQTTKSTQGFYKMKDLIEARVAEAGKNVDENFEYNDSICRQVSNREPQLRKFSKEFDVVIFVSGKKSSNGKALYGVCKQENERSYFVENETEIEPSWIRATDNVGICGATSTPMWLMEKVQNYIQAHSWN | Cofactor: Binds 1 [4Fe-4S] cluster per subunit.
Function: Catalyzes the conversion of 1-hydroxy-2-methyl-2-(E)-butenyl 4-diphosphate (HMBPP) into a mixture of isopentenyl diphosphate (IPP) and dimethylallyl diphosphate (DMAPP). Acts in the terminal step of the DOXP/MEP pathway for isoprenoid precursor biosynthesis.
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Q7ULU1 | MTPMKIILAAPRGFCAGVNMAIDSLDLTLQKFGPPVYVYHEIVHNQFVVKTFREKGAVFVDTIDEVPEGGVLLFSAHGVSPEIRKAAQARKLHALDATCPLVTKVHLEAIKYAKAGYTIILIGHEGHDEVLGTMGEAPEAIVLVEDEADVDRLEFEPGTQLAYLTQTTLSVDDAGRVIRRLRERFPEIHSPPKDDICYATQNRQEAVKLLREDADVIVVLGSQNSSNSQRLKELAAEQGKRAMLVDGPQDLAVDQFSDDDRVLITAGASAPESVVQSTIDWLKENFDASVDTQVVREEDVQFPLPKPLRAFAAEQAAAK | Cofactor: Binds 1 [4Fe-4S] cluster per subunit.
Function: Catalyzes the conversion of 1-hydroxy-2-methyl-2-(E)-butenyl 4-diphosphate (HMBPP) into a mixture of isopentenyl diphosphate (IPP) and dimethylallyl diphosphate (DMAPP). Acts in the terminal step of the DOXP/MEP pathway for isoprenoid precursor biosynthesis.
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Q5LNJ7 | MTKSPLTLYLAAPRGFCAGVDRAIKIVEMAIEKWGAPVYVRHEIVHNKFVVDGLRAKGAVFVEELDECPDDRPVIFSAHGVPKAIPAEAERRQMVYVDATCPLVSKVHIEAERHAEHGLQIIMIGHRGHPETIGTMGQLPEGEVLLVETVADVARIAVRDPARLAFVTQTTLSVDDTRDIVAALQARFPQIVGPHKEDICYATTNRQEAVKAVAPKSDALLVVGAPNSSNSRRLVEVAAKAGCSYAQLVQRADDIDWRALDGIATIAVSAGASAPELLVNEVIDAFRARFDVTVEVVETAVEHVEFKVPRVLRQPA | Cofactor: Binds 1 [4Fe-4S] cluster per subunit.
Function: Catalyzes the conversion of 1-hydroxy-2-methyl-2-(E)-butenyl 4-diphosphate (HMBPP) into a mixture of isopentenyl diphosphate (IPP) and dimethylallyl diphosphate (DMAPP). Acts in the terminal step of the DOXP/MEP pathway for isoprenoid precursor biosynthesis.
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Q97SR4 | MFGFFKKDKAVEVEVPTQVPAHIGIIMDGNGRWAKKRMQPRVFGHKAGMEALQTVTKAANKLGVKVITVYAFSTENWTRPDQEVKFIMNLPVEFYDNYVPELHANNVKIQMIGETDRLPKQTFEALTKAEELTKNNTGLILNFALNYGGRAEITQALKLISQDVLDAKINPGDITEELIGNYLFTQHLPKDLRDPDLIIRTSGELRLSNFLPWQGAYSELYFTDTLWPDFDEAALQEAILAYNRRHRRFGGV | Cofactor: Binds 2 magnesium ions per subunit.
Function: Catalyzes the condensation of isopentenyl diphosphate (IPP) with allylic pyrophosphates generating different type of terpenoids.
Sequence Mass (Da): 28705
Sequence Length: 252
EC: 2.5.1.-
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Q9X1B8 | MRIPQHVAIIMDGNGRWAKKRGLPRIKGHQRGAEVLHNTVKWSLELGIKYLTAFSFSTENWKRPKEEVEFLMDLFVQMIDREMELLRRERVRVRILGRKEGLPEKVLKKWQEVEEKTKEFDRMTLIIAFNYGGRREILDAVEFILKDVSHGKKIELTEETFRQYLYLPDVPDPDLIIRTSGEMRLSNFLLWQSAYSELYFFKKLWPDFTKRDFLRAIESYSKRERRFGGLING | Cofactor: Binds 2 magnesium ions per subunit.
Function: Catalyzes the condensation of isopentenyl diphosphate (IPP) with allylic pyrophosphates generating different type of terpenoids.
Sequence Mass (Da): 27859
Sequence Length: 233
EC: 2.5.1.-
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Q5SH15 | MVRRLLALSRPLYWLYEKRLLREVKRGPMPRHLGLILDGNRRYARALGLSPTKGHEFGVQKAYEVLEWCLEMGIKTVTVWVFSTDNFKRPPEEVETLMNLFLREAERMAEDHRILEHQVRVRFIGRREGFSPEVVRAIERLERRTEGHRGMFLNIAMGYGGREEIVDAVKRLLLEAEARGLSPKEVAEGLTPEDIARHLYTAGLPDPDFIIRTSGEIRLSGFLLWQSAYSEFYFADVLWPEFRKIDFLRALRSYQARERRFGR | Cofactor: Binds 2 magnesium ions per subunit.
Function: Catalyzes the condensation of isopentenyl diphosphate (IPP) with allylic pyrophosphates generating different type of terpenoids.
Sequence Mass (Da): 30893
Sequence Length: 263
EC: 2.5.1.-
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Q73K76 | MSDELKHIAIVMDGNGRWAKKRGLPRSMGHKEGLNTVKRITKAVSDLGIPYITLYIFSTENWKRTEAEVGFLMGLIKQHLKAELKFYADNNIRIEHIGNLSGLPQDIQDEINSVRDKTSAYTGTAIVLGINYGAHDEILRAIKKLNSDELASINEESFSLKLDTGKIPPVDLLIRTGGEKRLSNFLLWQSAYAELYFTDTLWPDWTVENLYEAIEDYKKRNRRYGNA | Cofactor: Binds 2 magnesium ions per subunit.
Function: Catalyzes the condensation of isopentenyl diphosphate (IPP) with allylic pyrophosphates generating different type of terpenoids.
Sequence Mass (Da): 25879
Sequence Length: 227
EC: 2.5.1.-
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O83612 | MQHVAIIMDGNGRWAERRGLRRSAGHRRGLQTAREIVAALCAIRVPFVTLYVFSTENWKRSAHEVHFLMNLIRWYLKKEMSFYVEHAIRVVHLGCAQTLPPDVRSQIEYVVERTRSHRGTTVALAINYGGKDEILRAVKKVLCSTSCPDGELLTEEAFGACLDAPQLPSVDFLIRTGGQQRMSNFLLWQSAYAEFYFTDILWPDFRVEDMLRALDEYRLRTRTFGGLE | Cofactor: Binds 2 magnesium ions per subunit.
Function: Catalyzes the condensation of isopentenyl diphosphate (IPP) with allylic pyrophosphates generating different type of terpenoids.
Sequence Mass (Da): 26270
Sequence Length: 228
EC: 2.5.1.-
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Q9X5F1 | MIAPLANSAVKPHKSASFVPRHVAIIMDGNGRWASARHLPRIAGHKKGADAVKTTVRAAAEMGIEVLTLYAFSSENWRRPASEVADLMGLLRLCLRQEMHNIKERGICLKVIGDYTRLDQDLVALLNQAIEITANNTRLTLVFALNYGAQDELVHVTKRIAEKAKEGQLDPENIDVGTIESLLYTHDLPPLDLVIRTSGEKRLSNFLLWQAAYAELLFIDTLWPDFGSETLKAAVEEYARRERRYGGL | Cofactor: Binds 2 magnesium ions per subunit.
Function: Catalyzes the condensation of isopentenyl diphosphate (IPP) with allylic pyrophosphates generating different type of terpenoids.
Sequence Mass (Da): 27715
Sequence Length: 248
EC: 2.5.1.-
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Q863C4 | MGIELLCLFFLFLGRNDHVQGGCAMGGAETCEDCLLIGPQCAWCSQENFTHLSGVGERCDTPANLLAKGCQLTFIENPVSQVEILTNKPLSIGRQKNSSNIVQISPQSLALKLRPGLEQTLQVQVRQTEDYPVDLYYLMDLSASMDDDLNTIKELGSLLSKEMSKLTSNFRLGFGSFVEKPISPFMKTTPEEIANPCSSIPYFCLPTFGFKHILPLTNDAERFNEIVKNQKISANIDTPEGGFDAIMQAAVCKEKIGWRNDSLHLLVFVSDADSHFGMDSKLAGIVIPNDGLCHLDSKNEYSMSTILEYPTIGQLIDKLV... | Function: Integrin alpha-V:beta-6 (ITGAV:ITGB6) is a receptor for fibronectin and cytotactin (By similarity). It recognizes the sequence R-G-D in its ligands (By similarity). ITGAV:ITGB6 acts as a receptor for fibrillin-1 (FBN1) and mediates R-G-D-dependent cell adhesion to FBN1 (By similarity). Integrin alpha-V:beta-6... |
P26010 | MVALPMVLVLLLVLSRGESELDAKIPSTGDATEWRNPHLSMLGSCQPAPSCQKCILSHPSCAWCKQLNFTASGEAEARRCARREELLARGCPLEELEEPRGQQEVLQDQPLSQGARGEGATQLAPQRVRVTLRPGEPQQLQVRFLRAEGYPVDLYYLMDLSYSMKDDLERVRQLGHALLVRLQEVTHSVRIGFGSFVDKTVLPFVSTVPSKLRHPCPTRLERCQSPFSFHHVLSLTGDAQAFEREVGRQSVSGNLDSPEGGFDAILQAALCQEQIGWRNVSRLLVFTSDDTFHTAGDGKLGGIFMPSDGHCHLDSNGLYS... | Function: Integrin ITGA4/ITGB7 (alpha-4/beta-7) (Peyer patches-specific homing receptor LPAM-1) is an adhesion molecule that mediates lymphocyte migration and homing to gut-associated lymphoid tissue (GALT) (Probable). Integrin ITGA4/ITGB7 interacts with the cell surface adhesion molecules MADCAM1 which is normally exp... |
P26012 | MCGSALAFFTAAFVCLQNDRRGPASFLWAAWVFSLVLGLGQGEDNRCASSNAASCARCLALGPECGWCVQEDFISGGSRSERCDIVSNLISKGCSVDSIEYPSVHVIIPTENEINTQVTPGEVSIQLRPGAEANFMLKVHPLKKYPVDLYYLVDVSASMHNNIEKLNSVGNDLSRKMAFFSRDFRLGFGSYVDKTVSPYISIHPERIHNQCSDYNLDCMPPHGYIHVLSLTENITEFEKAVHRQKISGNIDTPEGGFDAMLQAAVCESHIGWRKEAKRLLLVMTDQTSHLALDSKLAGIVVPNDGNCHLKNNVYVKSTTM... | Function: Integrin alpha-V:beta-8 (ITGAV:ITGB8) is a receptor for fibronectin . It recognizes the sequence R-G-D in its ligands . Integrin alpha-V:beta-6 (ITGAV:ITGB6) mediates R-G-D-dependent release of transforming growth factor beta-1 (TGF-beta-1) from regulatory Latency-associated peptide (LAP), thereby playing a k... |
Q27591 | MTSLGGRAFLWIYLVFLIAEISHSDADSIDDQCRHADSCERCLSAHLECAWCTDKEYQVGYRCLSRRQLLNYNCSETDIYENQPVLDVLQDKPLKDYETSDQAVQVTPQRAYLKLVKGNTQRMKLSYRTARNNPLDLYVLMDLTWTMRDDKKTLEELGAQLSQTLKNLTGNYRLGFGSFADKPTLPMILPQHRENPCAAERATCEPTYGYRHQLSLTDDIPAFTSAVANSKITGNLDNLEGGLDALMQVIVCTKEIGWKEQARKVVILVTDGFMHLAGDGLLAGIIQRNDKQCHLNKAGEYTGSLNYDYPSLEEIYRELL... | Function: Contributes to endodermal integrity and adhesion between the midgut epithelium and the surrounding visceral muscle. Essential for migration of the primordial midgut cells and for maintaining, but not establishing, cell polarity in the midgut epithelium. Can only partially compensate for the loss of beta-PS in... |
Q3ZBM4 | MFRKGKKRHSSSSSQSSEISTKSKSVDSSLGGLSRSSTVASLDTDSTKSSGQSNNNSDTCAEFRIKYVGAIEKLKLSEGKSLEGPLDLINYIDVAQQDGKLPFVPLEEEFIMGVSKYGIKVSTSDQYDVLHRHALYLIIRMVCYDDGLGSGKSLLALKTTDANNQEYSLWVYQCNSLEQAQAICKVLSTAFDSVLTSEKP | Function: Key regulator of the integrin-mediated cell-matrix interaction signaling by binding to the ITGB1 cytoplasmic tail and preventing the activation of integrin alpha-5/beta-1 (heterodimer of ITGA5 and ITGB1) by talin or FERMT1. Plays a role in cell proliferation, differentiation, spreading, adhesion and migration... |
O14713 | MFRKGKKRHSSSSSQSSEISTKSKSVDSSLGGLSRSSTVASLDTDSTKSSGQSNNNSDTCAEFRIKYVGAIEKLKLSEGKGLEGPLDLINYIDVAQQDGKLPFVPPEEEFIMGVSKYGIKVSTSDQYDVLHRHALYLIIRMVCYDDGLGAGKSLLALKTTDASNEEYSLWVYQCNSLEQAQAICKVLSTAFDSVLTSEKP | Function: Key regulator of the integrin-mediated cell-matrix interaction signaling by binding to the ITGB1 cytoplasmic tail and preventing the activation of integrin alpha-5/beta-1 (heterodimer of ITGA5 and ITGB1) by talin or FERMT1. Plays a role in cell proliferation, differentiation, spreading, adhesion and migration... |
Q5R5S7 | MFRKGKKRHSSSSSQSSEISTKSKSVDSSLGGLSRSSTVASLDTDSTKSSGQSNSNSDTCAEFRIKYVGAIEKLKLSEGKDLEGPLDLINYIDVAQQDGKLPFVPPEEEFIMGVSKYGIKVSTSDQYDVLHRHALYLIIRMVCYDDGLGAGKSLLALKTTDASNEEYSLWVYQCNSLEQAQAICKVLSTAFDSVLTSEKP | Function: Key regulator of the integrin-mediated cell-matrix interaction signaling by binding to the ITGB1 cytoplasmic tail and preventing the activation of integrin alpha-5/beta-1 (heterodimer of ITGA5 and ITGB1) by talin or FERMT1. Plays a role in cell proliferation, differentiation, spreading, adhesion and migration... |
P11584 | MILERNRRCQLALLMIAILAAIAGQTDAQKAAKLTAVSTCASKEKCHTCIQTEGCAWCMQPDFKGQSRCYQNTSSLCPEEFAYSPITVEQILVNNKLTNQYKAELAAGGGGSAMSGSSSSSYSSSSSSSSFYSQSSSGSSSASGYEEYSAGEIVQIQPQSMRLALRVNEKHNIKISYSQAEGYPVDLYYLMDLSKSMEDDKAKLSTLGDKLSETMKRITNNFHLGFGSFVDKVLMPYVSTIPKKLEHPCENCKAPYGYQNHMPLNNNTESFSNEVKNATVSGNLDAPEGGFDAIMQAIACRSQIGWREQARRLLVFSTDA... | Function: Integrin alpha-PS1/beta-PS is a receptor for laminin . Integrin alpha-PS2/beta-PS is a receptor for Tig, wb and Ten-m . Contributes to endodermal integrity and adhesion between the midgut epithelium and the surrounding visceral muscle . Essential for migration of the primordial midgut cells and for maintainin... |
Q96J02 | MSDSGSQLGSMGSLTMKSQLQITVISAKLKENKKNWFGPSPYVEVTVDGQSKKTEKCNNTNSPKWKQPLTVIVTPVSKLHFRVWSHQTLKSDVLLGTAALDIYETLKSNNMKLEEVVVTLQLGGDKEPTETIGDLSICLDGLQLESEVVTNGETTCSENGVSLCLPRLECNSAISAHCNLCLPGLSDSPISASRVAGFTGASQNDDGSRSKDETRVSTNGSDDPEDAGAGENRRVSGNNSPSLSNGGFKPSRPPRPSRPPPPTPRRPASVNGSPSATSESDGSSTGSLPPTNTNTNTSEGATSGLIIPLTISGGSGPRPL... | Function: Acts as an E3 ubiquitin-protein ligase which accepts ubiquitin from an E2 ubiquitin-conjugating enzyme in the form of a thioester and then directly transfers the ubiquitin to targeted substrates . Catalyzes 'Lys-29'-, 'Lys-48'- and 'Lys-63'-linked ubiquitin conjugation . Involved in the control of inflammator... |
Q8C863 | MSDSGPQLDSMGSLTMKSQLQITVISAKLKENKKNWFGPSPYVEVTVDGQSKKTEKCNNTNSPKWKQPLTVIVTPTSKLCFRVWSHQTLKSDVLLGTAGLDIYETLKSNNMKLEEVVMTLQLVGDKEPTETMGDLSVCLDGLQVEAEVVTNGETSCSESTTQNDDGCRTRDDTRVSTNGSEDPEVAASGENKRANGNNSPSLSNGGFKPSRPPRPSRPPPPTPRRPASVNGSPSTNSDSDGSSTGSLPPTNTNVNTSTSEGATSGLIIPLTISGGSGPRPLNTVSQAPLPPGWEQRVDQHGRVYYVDHVEKRTTWDRPEP... | Function: Acts as an E3 ubiquitin-protein ligase which accepts ubiquitin from an E2 ubiquitin-conjugating enzyme in the form of a thioester and then directly transfers the ubiquitin to targeted substrates . It catalyzes 'Lys-29'-, 'Lys-48'- and 'Lys-63'-linked ubiquitin conjugation (By similarity). Involved in the cont... |
J9VTS6 | MSDEKNYGISLAAPARPDLGSRTASQLEKATASHVEFATPKDPGALHDATLMAGERTEKLTKFVVGLALFASVSGFCFGFDTGVISAALVSIKDDFGHILDDTEKEWISAATSCGALVGALSSGALADRVGRKWTLAVGDVWFTLGAIIICSSFSVVQMIVGRAVLGLGVGTAAAIAPLYIAEVAPTRFRGALVTVQSIAITGGQFFSYCIGIPLTGHNGWRIQFAIGIVPAVVQAAVVHFLPESPRYDLLRGQREAALATIHRSYKGMSEDYIAVKFAALEEVVGISADFNRGHTLGQKMRLVLTEGKYRKPAITALGI... | Function: Major transporter for myo-inositol . Plays a role in the traversal of the host blood-brain barrier .
Catalytic Activity: H(+)(out) + myo-inositol(out) = H(+)(in) + myo-inositol(in)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 60694
Sequence Length: 566
Subcellular Location: Cell membrane... |
A0A1D8PH98 | MGSSTNNTQSKATPSVLENEVNSSKSSVVSSTSSAKGLLRETTNHGTMETSSVQISESESRPSKMVLVLTLASSISGFMFGYDTGYISSALVQIGTDLSNKILTSGEKEFITSATSLGALLGAVVGGVLANLIGRRRVLLGSNIIFVVGTIIQLAARTVWTMIAGRFVLGWGVGIASLIAPLMISELAPAKYRGRLIVTNVIFITGGQLIAYFINWGLTRVSHGWRVSVGLCMVPPVLQFVLFWFLPDTPRFYVMNGNFEKARQVLRKVHVDPSDEFVNATIDEMIASDSTVPGNGPLQKAWKSIKIIHTTPGNFRALIL... | Function: Major transporter for myo-inositol.
Catalytic Activity: H(+)(out) + myo-inositol(out) = H(+)(in) + myo-inositol(in)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 59703
Sequence Length: 554
Subcellular Location: Cell membrane
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J9VHZ4 | MSARPAQPNIYAPIRTSLSGYPSPTHSGSSTPASLEFSDGRLPENNVERDMSKVVERVALLGEADEGAVIVEGEDKVTKFVWMLVSAAAISGLLFGYDTAAISGMLVIIKDDLGTILSSWQKEVITSATTLGALLGGLAAGCVSDFTGRRLVIVFANVAFIGGSICQAACHTVAAMIAGRFIVGLGVGLASCIVPLYIGELAPTMIRGRLVTINCVAVTLGQVVAYAIGASFQNVHNGWRWIVGLGAMPSFVQLAAIGFLPESPRILLLRSDVAGARAITAKIYPLATIEQVDRKIEIMKAAVDQSIEYNANSTWFERLK... | Function: May function as a transporter or as a sensor for myo-inositol.
Catalytic Activity: H(+)(out) + myo-inositol(out) = H(+)(in) + myo-inositol(in)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 60983
Sequence Length: 567
Subcellular Location: Cell membrane
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Q10286 | MSISSKDFQNVTSAGFADDTFAADTFAADKKSPFESSVFENKTQVLPVDSVSRLSNGARSRSNSNISLSEPHALNDTVEDQPVSKWVWVLAFAAGIGGLLFGYDTGVISGALVVIGTSLGGHELTNGGKEFITSATSLGALLGGIIAGALADFFGRKPVIAIASIIIIVGSIVQVTAHHLWHMIVGRFVIGWGVGIASLIIPLYLSEIAPSKIRGRLVIIYVLLITAGQVIAYGIDTAFEHVHNGWRWMVGLAMVPAAFQLFILIWLPESPRLLVKKERSQEAYNTLARIYPTAHPYEIKTKLYLIQEGVRDPFSGSRWQ... | Function: Transporter for myo-inositol.
Catalytic Activity: H(+)(out) + myo-inositol(out) = H(+)(in) + myo-inositol(in)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 62758
Sequence Length: 575
Subcellular Location: Golgi apparatus membrane
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Q43667 | MAAFVESARAGAGADEVIQLVSDGVNEYSEKMMEGVVACPRILMPCKVNDDCLRGCKCLSNGYCG | Function: Inhibits trypsin.
Sequence Mass (Da): 6877
Sequence Length: 65
Domain: The presence of a 'disulfide through disulfide knot' structurally defines this protein as a knottin.
Subcellular Location: Secreted
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Q9US46 | MLEVEVESDNKHLVADELIALQSIYPEIHLDGNNYGRLNIPVNTESDYFLSFKSPDESTLTDTIVVRHFPDLVMEFFLPEAYPFNSPPTFFLKSSWLPLKQKRVLTSSLIKLWNEIHDCVLFDAIEHVRSIATIAFHLPTEMVFPGGFDDLKKEILAFDKNAKLLEFQIRKFQCNVCFDEFNGTDCFQLTRCGHVSCQSCLRDYYTMCIQEGMFSQIKCIDLDCGKDAPVLTLKELESIVGVQLTNRYKELEEKRRYENDSNIIFCPRSFCQGPSKRDPGQKLAICQKCDFAFCSFCQATWHGDLSPCKLEGDSKKLVEM... | Catalytic Activity: [E2 ubiquitin-conjugating enzyme]-S-ubiquitinyl-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-N(6)-ubiquitinyl-L-lysine.
Sequence Mass (Da): 50297
Sequence Length: 435
Domain: Members of the RBR family are atypical E3 ligases. They inter... |
Q04638 | MALTQFENDLEILRDMYPELEMKSVKVEEEGEFPQRINGKLLFKISLLADVNIEFGEQHMLLSNLSNECVEFTIYSCHYPDIRRCVVMDIKSLWISTDEKKMLIDKALRLVEETVDMSIEFADSFTSILILIFGFLIDDTAILLFPNGIRKCLTQDQYDLFKQISEEATLQKVSRSNYHCCICMEMEKGVRMIKLPCENANVEHYLCRGCAKSYFTAMIQENRISSVRCPQCEYKELKLEDFKSYKKMLKALFTPLIPVSFLKEVIDTELCERYEKMFYNQAATRLSKYCPYACVTCRRCDSWCTKEDLDDAMIQCQKCH... | Function: Modulates the efficiency of translation termination, resulting in the readthrough of all three types of nonsense codons UAA, UAG and UGA.
Catalytic Activity: [E2 ubiquitin-conjugating enzyme]-S-ubiquitinyl-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor prot... |
Q47316 | MILPSEKSATDVAAQCFLNALIRETKDWQLAEYPPDELIIPLDEQKSLHFRVAYFSPTQHHRFAFPAHLVTASGSYPVDFTTLSRLIIDKLRHQLFLPVPLCETFHQRVLESYAHTQQTIDARHDWAILREKALNFGEAEQALLTGHAFHPAPKSHEPFNRQEAERYLPDMAPHFPLRWFSVDKTQIAGESLHLNLQQRLTRFAAENAPQLLNELSDNQWLFPLRPWQGEYLFQQVWCQALFAKGLIRDLGEAGTSWLPTTSSRSLYCATSRDMIKFSLSVRLTNSVRTLSVKEVERGMRLARLAQTDGWQMLQARFPTF... | Function: Catalyzes the attachment of a first N-acetyl-N-hydroxylysine to a carboxylic group of citric acid to yield N-citryl-N-acetyl-N-hydroxylysine. Involved in the biosynthesis of the siderophore aerobactin which is a chelator that mediates the high-affinity iron transport systems induced under iron-stressed condit... |
Q76BS7 | MHRNNERINLEKSNDWANTNEPSIACFLNSLARESQSVQLLWGEDGKRVYRLPLANSDSINIPLSYFSSLGSHEYCLPALLHTQDSIKTLSVEQLIEHIVNEPALVGIVSEAKKAIFTKRVLESHRNTEQAIEHSPYQEQLFTEQLDFKTAEQGLLIGHSFHPAPKSREQFSLSDAKLYSPELGGQFKLFWLSVEQSLLTSGSSADIHFNQRFEALVAHDPKLVEALQNAQQQGHELLPVHPWQWHVMVENPSIKGYIATKQIQNLGQLGATWYPTSSTRSLYAPGLPYMLKFSLSVKLTNSIRNLSLKECDSWNDLNDL... | Function: Catalyzes the attachment of a first N-acetyl-N-hydroxylysine to a carboxylic group of citric acid to yield N-citryl-N-acetyl-N-hydroxylysine. Involved in the biosynthesis of the siderophore aerobactin which is a chelator that mediates the high-affinity iron transport systems induced under iron-stressed condit... |
Q47317 | MSGPNIVHSGYGLRCEKLDKPLNLGWGLDNSAVLHWPGELPTGWLCDALDQIFIAAPQLSAVVLPWSEWCEEPQALTLFGQVQSDIIHRSAFWQLPLWLSSPANRASGEMVFDAEREIYFPQRPPRPQGEVYRRYDPRIRRMLSFRIADPVSDAERFTRWMNDPRVEYFWEQSGSLEVQIAYLERQLTSKHAFPLIGCFDDRPVSNIEIYWAAEDRIGRHYSWQPFDRGLHLLVGEQQWRGAHYVQSWLRGVTHYLLLNEPRTQRTVLEPRTDNQRLFRHLEPAGYRTIKEFDFPHKRSRMVMADRHHFFTEVGL | Function: Catalyzes the transfer of acetyl from acetyl-CoA to the N-hydroxylysine. Involved in the biosynthesis of the siderophore aerobactin which is a chelator that mediates the high-affinity iron transport systems induced under iron-stressed conditions.
Catalytic Activity: acetyl-CoA + N(6)-hydroxy-L-lysine = CoA + ... |
Q47318 | MNHKDWDLVNRRLVAKMLSELEYEQVFHAESQGDDRYCINLPGAQWRFIAERGIWGWLWIDAQTLRCADEPVLAQTLLMQLKQVLSMSDATVAEHMQDLYATLLGDLQLLKARRGLSASDLINLNADRLQCLLSGHPKFVFNKGRRGWGKEALERYAPEYANTFRLHWLAVKREHMIWRCDNEMDIHQLLTAAMDPQEFARFSQVWQENGLDHNWLPLPVHPWQWQEKIATDFIADFGEGRMVSLGEFGDQWLAQQSLRTLTNASRRGGLDIKLPLTIYNTSCYRGIPGRYIAAGPLASRWLQQVFATDATLVQSGAVIL... | Function: Catalyzes the attachment of the second N-acetyl-N-hydroxylysine to the carboxylic group of N-citryl-N-acetyl-N-hydroxylysine to yield aerobactin. Involved in the biosynthesis of the siderophore aerobactin which is a chelator that mediates the high-affinity iron transport systems induced under iron-stressed co... |
Q76BS5 | MVMDQLALHRYWAVANQKMVGKILSEFAYEQAFQFEPTAQGYQLNLENGTRYCFAGEENIWGQVMIDPTSITRHAEIEADEPISAALLMRDLQPLLKMPDDAFAEHLEDLNATLLGDCKLMQRNEAITARDLAMLPCEQQQTYFDGHPKFVFNKGRRGWGSDDLKRYAPEAERVSNWVGSRFITRFCSSPPTMKSHGKPCCKAPSRPMKSSRWTVCWLPISLDSTIIVMFRFILWQWSNKLALLFVREIATKQLVYLGEFGDHFLPQLSLRTLSNVTRPAGYDIKLPLTVMNTSCYRGIPGRYILAGPTASDWIDQVFKS... | Function: Catalyzes the attachment of the second N-acetyl-N-hydroxylysine to the carboxylic group of N-citryl-N-acetyl-N-hydroxylysine to yield aerobactin. Involved in the biosynthesis of the siderophore aerobactin which is a chelator that mediates the high-affinity iron transport systems induced under iron-stressed co... |
P11295 | MKKSVDFIGVGTGPFNLSIAALSHQIEELDCLFFDEHPHFSWHPGMLVPDCHMQTVFLKDLVSAVAPTNPYSFVNYLVKHKKFYRFLTSRLRTVSREEFSDYLRWAAEDMNNLYFSHTVENIDFDKKRRLFLVQTSQGEYFARNICLGTGKQPYLPPCVKHMTQSCFHASEMNLRRPDLSGKRITVVGGGQSGADLFLNALRGEWGEAAEINWVSRRNNFNALDEAAFADEYFTPEYISGFSGLEEDIRHQLLDEQKMTSDGITADSLLTIYRELYHRFEVLRKPRNIRLLPSRSVTTLESSGPGWKLLMEHHLDQGRES... | Function: Flavoprotein monooxygenase required for N-hydroxylation of lysine. Involved in the biosynthesis of the siderophore aerobactin which is a chelator that mediates the high-affinity iron transport systems induced by the organism under iron-stressed conditions.
Catalytic Activity: L-lysine + NADPH + O2 = H2O + N(6... |
Q27546 | MPKKIILDCDPGLDDAVAILLAHGNPEIELLAITTVVGNQTLAKVTRNAQLVADIAGITGVPIAAGCDKPLVRKIMTAGHIHGESGMGTVAYPAEFKNKVDERHAVNLIIDLVMSHEPKTITLVPTGGLTNIAMAARLEPRIVDRVKEVVLMGGGYHEGNATSVAEFNIIIDPEAAHIVFNESWQVTMVGLDLTHQALATPPILQRVKEVDTNPARFMLEIMDYYTKIYQSNRYMAAAAVHDPCAVAYVIDPSVMTTERVPVDIELTGKLTLGMTVADFRNPRPEHCHTQVAVKLDFEKFWGLVLDALERIGDPQ | Function: Catalyzes the hydrolysis of the N-glycosidic bond of commonly occurring purine and pyrimidine nucleosides into ribose and the base, but has a preference for inosine and uridine as substrates. Is not active on thymidine and 2'-deoxynucleosides. Functions in purine salvage from the blood of the host, a fundamen... |
P83851 | MPRKIILDCDPGIDDAVAIFLAHGNPEIELLAITTVVGNQSLEKVTQNARLVADVAGIVGVPVAAGCTKPLVRGVRNASHIHGETGMGNVSYPPEFKTKLDGRHAVQLIIDLIMSHEPKTITLVPTGGLTNIAMAVRLEPRIVDRVKEVVLMGGGYHTGNASPVAEFNVFIDPEAAHIVFNESWNVTMVGLDLTHQALATPAVQKRVREVGTKPAAFMLQILDFYTKVYEKEHDTYGKVHDPCAVAYVIDPTVMTTERVPVDIELNGALTTGMTVVDFRYPRPKNCRTQVAVKLDFDKFWCLVIDALERIGDPQ | Function: Catalyzes the hydrolysis of the N-glycosidic bond of all of the commonly occurring purine and pyrimidine nucleosides into ribose and the associated base, but has a preference for inosine and uridine as substrates. Likely functions in purine salvage from the host, a fundamental pathway since protozoan parasite... |
P14542 | MMISKKYTLWALNPLLLTMMAPAVAQQTDDETFVVSANRSNRTVAEMAQTTWVIENAELEQQIQGGKELKDALAQLIPGLDVSSRSRTNYGMNVRGRPLVVLVDGVRLNSSRTDSRQLDSIDPFNMHHIEVIFGATSLYGGGSTGGLINIVTKKGQPETMMEFEAGTKSGFSSSKDHDERIAGAVSGGNEHISGRLSVAYQKFGGWFDGNGDATLLDNTQTGLQYSDRLDIMGTGTLNIDESRQLQLITQYYKSQGDDDYGLNLGKGFSAIRGTSTPFVSNGLNSDRIPGTDGHLISLQYSDSAFLGQELVGQVYYRDES... | Function: Receptor for cloacin DF13/aerobactin.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 81014
Sequence Length: 732
Subcellular Location: Cell outer membrane
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A0A1W7HCY1 | MSGHSFFEHLFEHSQHVTPYLHGAIKPRPERCAEHGFIHIEHASSDHIRALYESLKLAHPEAGAAYWLTRTWTLLCWQPLYVAFIAIYSCQGLPKLSSMGQHVQPRFVSGYQFDDDEYRQGSEQELIAHAGKELCALFDYFRQEMSLWTRIRPGFTQHLFADGVFGCLVKLSQFYPTLSGDYFLEQARLWLAACQLPEKLIQSLRYDETSRQLSLVRTSCCLVYKCQGRELCRDCPRHPDNKRE | Cofactor: Binds 1 [2Fe-2S] cluster.
Function: Ferric-siderophore reductase involved in iron removal from the siderophores after their transport into the cell (Probable). Acts as a major ferric-aerobactin reductase catalyzing the reduction of Fe(3+)-aerobactin, a citrate-hydroxamate siderophore produced by other bacteri... |
Q7NN81 | MMRFLILATNNQGKLQELRRLLAGTGWVVQAAPPDFAVEETGTTFAENARLKALAAAERTGEWSVGDDSGLAVDALGGAPGVYSARYGRNDGERISRLLAALAGQADRGARFICAIALAEPGRVLKEVEAECRGVILHAPRGNGGFGYDPIFLVPELDKTFAELDIVEKERHSHRGRAVRKLLSGCSRGTFIVDH | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Pyrophosphatase that catalyzes the hydrolysis of nucleoside triphosphates to their monophosphate derivatives, with a high preference for the non-canonical purine nucleotides XTP (xanthosine triphosphate), dITP (deoxyinosine triphosphate) and ITP. Seems to function as ... |
Q7VLS3 | MNRTKIVLATSNKGKVKEMADVLSAFGFEVIAQSEFGLVSPPETGLTFVENALLKARYASKMTGLPAIADDSGLAVDALAGAPGLYSARYAGIEDDDTANRRKLLAEMQNVPDGQRAAKFVSCIVMLKHETDPTPKIAFGECFGEILREERGQNGFGYDALFFYPAKQCTFAELDSTEKKQISHRALALVALQKQL | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Pyrophosphatase that catalyzes the hydrolysis of nucleoside triphosphates to their monophosphate derivatives, with a high preference for the non-canonical purine nucleotides XTP (xanthosine triphosphate), dITP (deoxyinosine triphosphate) and ITP. Seems to function as ... |
P44598 | MKQKIVLATGNKGKVKEMADVLSDFGFEVIAQTDLGIESPEETGLTFVENALLKARYASEKSGLPAIADDSGLVVSALNGAPGLYSARYAGEEGNDAKNREKLLAELAHIAQEQRQAKFVSCIVFLQHPTDPSPIIAEGECCGVIGFEEKGENGFGYDSLFFSPEQGCTFAELETAEKKKISHRAKALSVLKSKL | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Pyrophosphatase that catalyzes the hydrolysis of nucleoside triphosphates to their monophosphate derivatives, with a high preference for the non-canonical purine nucleotides XTP (xanthosine triphosphate), dITP (deoxyinosine triphosphate) and ITP. Seems to function as ... |
Q7VF43 | MVIVLASANQHKICEFQAMLKNVKEKVKVYAYGELLETFEIAENGNSFKENATLKVKAIYQALYTLSQSTMQENIRNLFAQPLAIIAEDSGLCVPVLNGEPGIYSARYAHHKQFASMQYKNTDEANLYCLLNALTHCAPTPAFFVAHIALIFIKPYFCTYTLPPLEQCVIEHFEGILNGEVINEMRGNEGFGYDPLFIPAEHNPQSLTLAEFDMSAKNTISHRKKALSQCINRLFDKS | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Pyrophosphatase that catalyzes the hydrolysis of nucleoside triphosphates to their monophosphate derivatives, with a high preference for the non-canonical purine nucleotides XTP (xanthosine triphosphate), dITP (deoxyinosine triphosphate) and ITP. Seems to function as ... |
B4U8R9 | MKLMICTSNKKKFEEISSILESLKKDENLDLEFVKPPKEIEVEEYANTFLSNAYLKAKAYYNAFGIPALADDSGLVVEAFSDNLERPGVYSARFYKDSFGSHVLKEEDFKLSKDELNNLKVLRLLEKEENRKAKFVSVVAIVLSNNYGIFGEGELKGHIAKEPFGNFGFGYDPIFIPEGYNTTLANIENKDKISHRRQALEAVFFMLKKML | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Pyrophosphatase that catalyzes the hydrolysis of nucleoside triphosphates to their monophosphate derivatives, with a high preference for the non-canonical purine nucleotides XTP (xanthosine triphosphate), dITP (deoxyinosine triphosphate) and ITP. Seems to function as ... |
A2BJY7 | MEARVILIATTNKHKIEEINEVLQSCGYRVEPAAASKLEVQSNRLEDVAAYAAIQAYLALQRPVIVEDAGLFVEALGGFPGPYSSYVFKTIGIRGLLKLLEDVENRRAYFKSVIALAHSGGVEVFTGTVHGVIAEKPRGDRGFGYDPVFIPEGSSKTFAEMETQEKNKFSHRGKAARELCRWLRQYGPPR | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Pyrophosphatase that catalyzes the hydrolysis of nucleoside triphosphates to their monophosphate derivatives, with a high preference for the non-canonical purine nucleotides XTP (xanthosine triphosphate), dITP (deoxyinosine triphosphate) and ITP. Seems to function as ... |
A8A8W1 | MVSKKVYFLTSNPHKAKEVSDVLSQFSIEVVPLKGEKLEIQADSVEEVARFAAEEAKKRFKERPLLLEDSGLFVDALKGFPGPYSNYVYRTLGLEGLLKLMEGVEDRRARFVCAAALVKEDDKIVIEVGEVEGEIAYEPRGDKGFGFDPIFVPLGYEKTFAELGEEVKKRISHRARAFMKIAKHLSGE | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Pyrophosphatase that catalyzes the hydrolysis of nucleoside triphosphates to their monophosphate derivatives, with a high preference for the non-canonical purine nucleotides XTP (xanthosine triphosphate), dITP (deoxyinosine triphosphate) and ITP. Seems to function as ... |
B1L6T7 | MIFASSNRHKYEEFRRMLSDLIDLKFLEVDYLEPQGEDTREIVVTSAKWLSNYIREPFFIEDSGLFIEALNGFPGPYSSYVFKKIGNEGVLKLMNGVENRRAFFISVIALSYGRGIEVFEGRVQGTIAREVRGGGWGFDPIFIPNGSNKTYGELGDEKDRFSHRGASCRKLREFLMRFGSDRLP | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Pyrophosphatase that catalyzes the hydrolysis of nucleoside triphosphates to their monophosphate derivatives, with a high preference for the non-canonical purine nucleotides XTP (xanthosine triphosphate), dITP (deoxyinosine triphosphate) and ITP. Seems to function as ... |
Q5FLV7 | MSQKILFATGNKGKARELKEAFKTAGVDVEIITNSDLDNPPHPIESGRTFEANAKIKAHELADYSKLPTIADDSGLMVDALNGEPGVRSARYAGEAHNDAKNNAKLLANLGGIPDEKRTAKFWTTIVVSMPGEFEKDLVVSGTCSGRILAAPRGDDGFGYDPLFFVPKKDKTFAQMTTDEKNEISHRGNVVRELLKVLPALA | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Pyrophosphatase that catalyzes the hydrolysis of nucleoside triphosphates to their monophosphate derivatives, with a high preference for the non-canonical purine nucleotides XTP (xanthosine triphosphate), dITP (deoxyinosine triphosphate) and ITP. Seems to function as ... |
Q9CG29 | MEKTLIIATRNSGKTKEFKKLFADFGYEIKDLTDYPELSEIEETGTTFEENARLKAEQIAEITGQVVIGDDSGLCVDVLGGLPGIWSHRFSAPDPTDEKNIAKLLHELAPTAITPERRSAHFHTTLVAAKPGRESLVVEADWDGYIALAPKGENGFGYDPIFMVDAFRTAAELSEKEKNQVSHRGQALRKLMAELPEWLYK | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Pyrophosphatase that catalyzes the hydrolysis of nucleoside triphosphates to their monophosphate derivatives, with a high preference for the non-canonical purine nucleotides XTP (xanthosine triphosphate), dITP (deoxyinosine triphosphate) and ITP. Seems to function as ... |
Q88V20 | MTKPQTLIIATNNANKAREFSAMLAPYDITIKTLADFPNIPEIKENGITFEENATKKATVVVEATGLPAIADDSGLMVKALHGDPGVFSARYAGDHDDAANNAKLLANLGGVPEAERTATFHTTLVALKPSGEKLVVNGELAGRILIAPRGDNGFGYDPLFWSSKFQKSLAELTPAQKNQISHRGAALRQLMTKFDEWWAKA | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Pyrophosphatase that catalyzes the hydrolysis of nucleoside triphosphates to their monophosphate derivatives, with a high preference for the non-canonical purine nucleotides XTP (xanthosine triphosphate), dITP (deoxyinosine triphosphate) and ITP. Seems to function as ... |
E9FR69 | MENYVPFLVSHWRTVGLISVSIAAGVALGQLNQTHERAANKSQRVHTNSSIKAKQVKRESAIEQINEIEDDDEQSLEDQDVLPILFQYEKPSEADSIRRSEEFYRRMNQRRSVREISSDPVALEVIENIIKTGGTSPSGAHTEPWTFVVVSNLEMKQQIRQIIEAEEEINYKQRMGDVWVQDLQPVGTTWVKEYLTEAPWLILIFKQVHGFKRNGQKKIHYYNEISVSIATGFLLAAIQEAGLVTVTTTPLNCGPSIRVLLGRPVNEKLLLLLPVGYPKVGATVPDFKRKPLHDIMVHYQ | Function: Catalyzes the dehalogenation of halotyrosines such as 3,5-diiodo-L-tyrosine . Likely to also catalyze the dehalogenation of other halotyrosines such as 3-bromo-L-tyrosine, 3-chloro-L-tyrosine and 3-iodo-L-tyrosine (By similarity).
PTM: May be cleaved at Gln-55 . The cleaved form retains catalytic activity .
L... |
E1JIB2 | MDVDELISSSKLLKHWPSLFITLALIWIVKRLFFKGNRVLKTYNLDEQVEEEVEHFADLGDELQPALEDKPHVPFVPGQNLNPNGAKRLYELMRGRRSIRSFNSHPKPDLSVIEDCIRAAGTAPSGAHTEPWTYCVVQEPELKRSIREIVEQEELVNYSQRMHPQWVTDLRPLQTNHVKEYLTEAPYLILIFKQTYGLSENGKRMRRHYYNEISTSIAAGILLCALQAAGLASLVTTPLNCGPALRNLLGRPVNEKLLILLPVGYPKDGCTVPDLARKNLSNIMVTF | Function: Catalyzes the dehalogenation of halotyrosines such as 3-bromo-L-tyrosine, 3-chloro-L-tyrosine, 3-iodo-L-tyrosine and 3,5-diiodo-L-tyrosine . Activity towards 3-fluoro-L-tyrosine is weak . Important for male and female fertility . May be involved in maintaining the viability of sperm, both during development i... |
F4KU78 | MKQKPAFIPYAGAQFEPEEMLSKSAEYYQFMDHRRTVREFSNRAIPLEVIENIVMTASTAPSGAHKQPWTFVVVSDPQIKAKIRQAAEKEEFESYNGRMSNEWLEDLQPFGTDWHKPFLEIAPYLIVVFRKAYDVLPDGTQRKNYYVQESVGIACGFLLAAIHQAGLVALTHTPSPMNFLQKILQRPENERPFLLVPVGYPAEGAMVPDLQRKDKAAVMVVY | Function: Catalyzes the dehalogenation of halotyrosines such as 3-iodo-L-tyrosine and 3,5-diiodo-L-tyrosine . Likely to also catalyze the dehalogenation of other halotyrosines such as 3-bromo-L-tyrosine, 3-chloro-L-tyrosine and 3-iodo-L-tyrosine (By similarity). Activity towards 3-iodo-L-tyrosine is much stronger than ... |
T2MBC4 | MFDNLSGVSYGLLAGILAMLIHLVYQKITELKRRKDELKERESHPTDDLFPKEDFIPYHPSRYSEEEMIKRSNDFYLSMNARRSVRFFSNEDVPDEVIDNIIRTAGTSPSGAHTEPWTFVVIKNKLLKAKVREIIEEEEELNYKQRMGQKWVDDLKPLKTNWIKEYLTEAPYLILVFKQTYGITEDGQKKTHYYNEISASISCGFLLAAIQNAGLVALTSTPLNAGSKLRNLVGRGPNEKIVILLPVGYPSKNCQVPNLKRKPLNEIMIKFD | Function: Catalyzes the dehalogenation of halotyrosines such as 3,5-diiodo-L-tyrosine . Likely to also catalyze the dehalogenation of other halotyrosines such as 3-bromo-L-tyrosine, 3-chloro-L-tyrosine and 3-iodo-L-tyrosine (By similarity).
Catalytic Activity: 2 iodide + L-tyrosine + 2 NADP(+) = 3,5-diiodo-L-tyrosine +... |
A7S5D9 | MEVFKALFKSKEAYTVDVDPMKDSDEHDLPRDPLSIRVTGEEEVNHIPYPYFDEIPTEEEMKKKSAEFYKSMKKRRTVRKISSEPVPLEVIENIVRVAGTSPSGAHTEPWTYVVIRDPDLKKQIKEVVEEEEQLNYARRMGEKWVQDLSILKTTWSKPYIETAPYLILIFKQVYGIKPDGDKKVHYYNEISVCISCGLLLAAIQNAGLVTVTSTPMNAGPRLRVLLNRPQNEKLIMLLPVGYPAKDAEVPNLTRKPLEEIMVLK | Function: Catalyzes the dehalogenation of halotyrosines such as 3,5-diiodo-L-tyrosine . Likely to also catalyze the dehalogenation of other halotyrosines such as 3-bromo-L-tyrosine, 3-chloro-L-tyrosine and 3-iodo-L-tyrosine (By similarity).
Catalytic Activity: 2 iodide + L-tyrosine + 2 NADP(+) = 3,5-diiodo-L-tyrosine +... |
B9K712 | MKMLYDLAKKRKTVRRFKKEKPPLEDLIYSLKVANEAPSGMNAQPWRFLIVEDEKLKGQIRRVCERSEKTFYENVRGRLKEWLDEKRFTWRKPFLKEAPYLLLVFSEKSAPYSRESVWLAVGYLLLALEEKGLGSVPYTPPDFREVEKLVNTPSELRLEVILPVGYPDDPKPKYPRNEVIVRYNTF | Function: Catalyzes the dehalogenation of halotyrosines such as 3-bromo-L-tyrosine, 3-chloro-L-tyrosine, 3-iodo-L-tyrosine and 3,5-diiodo-L-tyrosine . Activity towards 2-iodophenol is weak .
Catalytic Activity: 2 iodide + L-tyrosine + 2 NADP(+) = 3,5-diiodo-L-tyrosine + H(+) + 2 NADPH
Sequence Mass (Da): 22028
Sequence... |
Q753H5 | MSEERGMKEQTISEMAQEMAHTTSEGLKKRIRKLYTFDELPAWQKDNELILSGYVRETNSVKECLRAMTYFNNESINIYTHLIPGVAYLVLFLIFADLVLAQLLPGLDAGEHRMLRFYLLGAFTCLACSSCFHCLKQHSEPHSRLWSKVDYLGILAQITCSTISLLYYGYHSYPSHFVFFSTLTVALCSACAVLVLNDSFNTVAFRPLRAFLFMAFGLSGVIPVLAGSYQFGFAEWAARIQLKYVLYEAVFYITGALVYGFRIPERFAPGKFDMVGHSHQIFHLLVVLGTLCHFRAVTGSYIFICTGKHYSSLLMFI | Function: ADIPOR-like receptor involved in zinc metabolism either by altering membrane sterol content or by directly altering cellular zinc levels.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 35981
Sequence Length: 317
Subcellular Location: Endoplasmic reticulum membrane
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Q03419 | MSITTTRRRNQDSVCCKATRASIKVEAVSGQTVFEKQKLLHNFDELPEWQKDNDKILTGYVRETLSWKKCLYSLFYWNNETVNIYTHLVPAIVYFVFAITLTNYFLIPVFPSTSWSDYTVINIFLMGAFSCLMCSSCFHCMKQHSEKQSNFWSKLDYLGIISLISCSMIPIIYFGYFDHISYFSLFTIVTLVLATFCTVCVLHDKFNTSTFRPFRAMFFILFGFSGLLPLTTGFFKFGIQGVLNRIKVSFVFWEALFYISGAVIYGFRIPETLAPGKFDFFGSSHQIFHIMVVLGSVCHLKAIIDSYKLMHSHIHP | Function: ADIPOR-like receptor involved in zinc metabolism either by altering membrane sterol content or by directly altering cellular zinc levels.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 36492
Sequence Length: 316
Subcellular Location: Endoplasmic reticulum membrane
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Q12442 | MSTLLERTKSVQELKKRAAGKTSANPAEVAKAKKVLRRLYSWDEIPEWQRDNDFILHGYVKETSSFIETFKSLFYLHNESVNIYSHLIPALGFFTVLLLDKSTIKVFATTTWLDHMVIDLFYSGAFACLILSSSFHCLKSHSLRIATLGNKLDYLGICILIVTSMVSILYYGYFEKFSLFCLFALITVSFGIACSIVSLKDKFRKREWRPYRAGLFVCFGLSSIIPIFSGLYCYSFSEIWTQIQLFWVLLGGVLYIIGAVLYGMRFPEKICPGKFDIWGHSHQLFHFLVVIAALCHLRGLLNSYELVHIKMENGIVS | Function: Probable receptor, which is involved in metabolic pathways that regulate lipid metabolism such as fatty acid oxidation.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 36279
Sequence Length: 317
Subcellular Location: Membrane
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Q75F81 | MSHPNTHMPRTHAVHGRAAPQRRGCRTSVEKTDQSGHSRSSLAESAMEQAQLRSRGEAGGGRSVLCASGEPGSAHKWAGAVTCSGAEEQPLHWAESRARGLARHLHYWELPYAWRENRYIIYGHRFYHSHRKSLLSVLNAYGWHNETINIWSHLVGAAVLAYLLCWGWPRSDVYRAAQVPRLAKWAIGAFLACGVKCMASSVAWHTFNGTCHLKLRSRFVCVDYTGITLLVTASVVTTVAVTLYGLSRPLMYAYMVASIGLGTAAGVMNWSPHFDRPEARPLRIAVYVGLAALGLVSFVHVWMQVRWASAHLMAPLVYKS... | Function: ADIPOR-like receptor involved in zinc metabolism either by altering membrane sterol content or by directly altering cellular zinc levels.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 47153
Sequence Length: 419
Subcellular Location: Endoplasmic reticulum membrane
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Q07959 | MMDSSSKSLTQYIPSPMGSLSRLKQKGVDNFQKVKKSGKSIYNYNYSKFVPHPFSTIDESVKHSESGRYDDLEIIRPTKEKEVTSSVYKRNSGKSLNTESQFSLGDSDAATLVNSVATFKLNNASTSTSLVSSSSTVCSQAKSSLRSPTSRLNDTKIKEENNYISSVKDYCGPMRKSMVKTEILIEEPLNPTTDIKSFINSYNHGKAYSLGETQHLHYYQLPFPWRENRYIIHGYRFYNTHSKSLLSIFNWYGWHNETSNIWSHLLGAIYIIYLAIYDFPQSEVWRNSQVPPQARWIVFMFLAAALKCMLSSVFWHTFNG... | Function: ADIPOR-like receptor involved in zinc metabolism either by altering membrane sterol content or by directly altering cellular zinc levels.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 62571
Sequence Length: 543
Subcellular Location: Endoplasmic reticulum membrane
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Q99393 | MVSLTTIEQSPVKCETTTEKESNDTRGTDSNENAETKETKKGFPFHDLAKLQKQYKNKSSRNESLVALIYLLGSMLSFCLLIFFTDFYLIPLFPTTTTMTDYIVFNFYLLNVFVFCMVHFIYHFVKNISLQQHLEHWQKFSYLSNINLLISSQITILYYLFYDYVFFFKIFTLLMNFIGLVAYFFILTDKLISSKRFNKTVFFISVSVVCCSLPLLTAIITFDGLENLKERIKVNAITWELVALVAASIIYVTRFPESLFRRNKKEEGWNHSEYLFHLLISGTAFYHFFILIQSYILMHSSLNQPELINFKS | Function: ADIPOR-like receptor involved in zinc metabolism either by altering membrane sterol content or by directly altering cellular zinc levels.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 36608
Sequence Length: 312
Subcellular Location: Endoplasmic reticulum membrane
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Q8IYV9 | MGPHFTLLCAALAGCLLPAEGCVICDPSVVLALKSLEKDYLPGHLDAKHHKAMMERVENAVKDFQELSLNEDAYMGVVDEATLQKGSWSLLKDLKRITDSDVKGDLFVKELFWMLHLQKETFATYVARFQKEAYCPNKCGVMLQTLIWCKNCKKEVHACRKSYDCGERNVEVPQMEDMILDCELNWHQASEGLTDYSFYRVWGNNTETLVSKGKEATLTKPMVGPEDAGSYRCELGSVNSSPATIINFHVTVLPKMIKEEKPSPNIVTPGEATTESSISLQPLQPEKMLASRLLGLLICGSLALITGLTFAIFRRRKVID... | Function: Essential sperm cell-surface protein required for fertilization by acting as a ligand for IZUMO1R/JUNO receptor on egg. The IZUMO1:IZUMO1R/JUNO interaction is a necessary adhesion event between sperm and egg that is required for fertilization but is not sufficient for cell fusion. The ligand-receptor interact... |
Q9D9J7 | MGPHFTLLLAALANCLCPGRPCIKCDQFVTDALKTFENTYLNDHLPHDIHKNVMRMVNHEVSSFGVVTSAEDSYLGAVDENTLEQATWSFLKDLKRITDSDLKGELFIKELLWMLRHQKDIFNNLARQFQKEVLCPNKCGVMSQTLIWCLKCEKQLHICRKSLDCGERHIEVHRSEDLVLDCLLSWHRASKGLTDYSFYRVWENSSETLIAKGKEPYLTKSMVGPEDAGNYRCVLDTINQGHATVIRYDVTVLPPKHSEENQPPNIITQEEHETPVHVTPQTPPGQEPESELYPELHPELYPELIPTVAQNPEKKMKTRL... | Function: Essential sperm cell-surface protein required for fertilization by acting as a ligand for IZUMO1R/JUNO receptor on egg . The IZUMO1:IZUMO1R/JUNO interaction is a necessary adhesion event between sperm and egg that is required for fertilization but is not sufficient for cell fusion . The ligand-receptor intera... |
Q8WYK2 | MMPGQIPDPSVTTGSLPGLGPLTGLPSSALTVEELKYADIRNLGAMIAPLHFLEVKLGKRPQPVKSELDEEEERRKRRREKNKVAAARCRNKKKERTEFLQRESERLELMNAELKTQIEELKQERQQLILMLNRHRPTCIVRTDSVKTPESEGNPLLEQLEKK | Function: Component of the AP-1 transcription factor that represses transactivation mediated by the Jun family of proteins. Involved in a variety of transcriptional responses associated with AP-1 such as UV-induced apoptosis, cell differentiation, tumorigenesis and antitumogeneris. Can also function as a repressor by r... |
P97875 | MMPGQIPDPSVTAGSLPGLGPLTGLPSSALTTEELKYADIRNIGAMIAPLHFLEVKLGKRPQPVKSELDEEEERRKRRREKNKVAAARCRNKKKERTEFLQRESERLELMNAELKTQIEELKLERQQLILMLNRHRPTCIVRTDSVRTPESEGNPLLEQLDKK | Function: Component of the AP-1 transcription factor that represses transactivation mediated by the Jun family of proteins. Involved in a variety of transcriptional responses associated with AP-1, such as UV-induced apoptosis, cell differentiation, tumorigenesis and antitumogeneris. Can also function as a repressor by ... |
P9WJW8 | MTPRQRLTVLATGLGIFMVFVDVNIVNVALPSIQKVFHTGEQGLQWAVAGYSLGMAAVLMSCALLGDRYGRRRSFVFGVTLFVVSSIVCVLPVSLAVFTVARVIQGLGAAFISVLSLALLSHSFPNPRMKARAISNWMAIGMVGAASAPALGGLMVDGLGWRSVFLVNVPLGAIVWLLTLVGVDESQDPEPTQLDWVGQLTLIPAVALIAYTIIEAPRFDRQSAGFVAALLLAAGVLLWLFVRHEHRAAFPLVDLKLFAEPLYRSVLIVYFVVMSCFFGTLMVITQHFQNVRDLSPLHAGLMMLPVPAGFGVASLLAGRA... | Function: Involved in resistance to ethambutol and isoniazid.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 53479
Sequence Length: 508
Subcellular Location: Cell inner membrane
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Q9PTT2 | MKGLVIFFCLFYGCHVAGATGKTIMLFPQKTDTDYVTLKPTERVLNQITVCLKSYTELIKEHSLFSLAMQGSGKDNTLLIYPYPPNNISISIHNEDIYFKVDPEVLQWKRTCVTWDSKTGLLQLWINGKLYPRRITKSRSPIGPQISVILGQEQDSYGGSFDINQAFVGEMSDVNVWDYVLPPENIKAYFSDDYTLDGNFYSWDGGNYTINGLIVVLRNQFIPKL | Cofactor: Binds 2 calcium ions per subunit.
Function: Calcium-dependent beta-galactose specific lectin.
PTM: Glycosylated.
Sequence Mass (Da): 25618
Sequence Length: 225
Subcellular Location: Secreted
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P40358 | MILISGYCLLVYSVILPVLISASKLCDLAELQRLNKNLKVDTESLPKYQWIAGQLEQNCMTADPASENMSDVIQLANQIYYKIGLIQLSNDQHLRAINTFEKIVFNETYKGSFGKLAEKRLQELYVDFGMWDKVHQKDDQYAKYLSLNETIRNKISSKDVSVEEDISELLRITPYDVNVLSTHIDVLFHKLAEEIDVSLAAAIILDYETILDKHLASLSIDTRLSIHYVISVLQTFVLNSDASFNIRKCLSIDMDYDKCKKLSLTISKLNKVNPSKRQILDPATYAFENKKFRSWDRIIEFYLKDKKPFITPMKILNKDT... | Function: Acts as a DnaJ-like chaperone required for nuclear membrane fusion during mating.
Location Topology: Single-pass type IV membrane protein
Sequence Mass (Da): 75144
Sequence Length: 645
Subcellular Location: Endoplasmic reticulum membrane
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P36035 | MSSSITDEKISGEQQQPAGRKLYYNTSTFAEPPLVDGEGNPINYEPEVYNPDHEKLYHNPSLPAQSIQDTRDDELLERVYSQDQGVEYEEDEEDKPNLSAASIKSYALTRFTSLLHIHEFSWENVNPIPELRKMTWQNWNYFFMGYFAWLSAAWAFFCVSVSVAPLAELYDRPTKDITWGLGLVLFVRSAGAVIFGLWTDKSSRKWPYITCLFLFVIAQLCTPWCDTYEKFLGVRWITGIAMGGIYGCASATAIEDAPVKARSFLSGLFFSAYAMGFIFAIIFYRAFGYFRDDGWKILFWFSIFLPILLIFWRLLWPETK... | Function: Essential to lactate transport.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 69376
Sequence Length: 616
Subcellular Location: Membrane
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Q9GYI4 | MSLGRDRYSLPRTYKRVSHAKDKARPELRKFGWETLGYSESFNLPPFRDSIQRVDGNNLTVEEFRRDFERPRIPVIITGLTDNWAAKDKWTVERLSKKYRNQNFKCGEDDNGNSVRMKMKYYHDYMLNNKDDSPLYIFDSSFAERRKTKKLSEDYSVPKFFEDDLFHYADDKKRPPHRWFVMGPARSGTAIHIDPLGTSAWNSLLQGHKRWVLIPPIAPRDLVKPMAHEKGKHPDEGITWFQTVYKRVRSPSWPKEYAPIECRQGPGETMFVPSGWWHVVINEEYTIAVTHNYCSVENLHLVWPKTVKGRPKLSKHWVKR... | Cofactor: Binds 1 Fe(2+) ion per subunit.
Function: Dioxygenase that can both act as a histone arginine demethylase and a lysyl-hydroxylase.
Sequence Mass (Da): 46618
Sequence Length: 400
Subcellular Location: Nucleus
EC: 1.14.11.-
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Q6PFM0 | MNHKSKKRIKEAKRSARPELKDSSDWTKHEYCKSFDLSHRSVKDNVERADVQRLSPEEFIQRFEKPYKPVVLLNVEDSWPAREKWTLERLKRKYRNQKFKCGEDNDGYSVKMKMKYYVEYLESTHDDSPLYIFDSSFGEHAKRRKLLEDYQVPLFFRDDLFQFAGEKRRPPYRWFVMGPARSGTGIHIDPLGTSAWNALVQGHKRWCLFPTHTPRELIKVTRDEGGNQQDEAITWFNVIYPRTQQSTWPDEFRPLEILQRPGETVFVPGGWWHVVLNLDTTIAVTQNFASTTNFPIVWHKTVRGRPKLSRKWYRILKQER... | Cofactor: Binds 1 Fe(2+) ion per subunit.
Function: Dioxygenase that can both act as a arginine demethylase and a lysyl-hydroxylase. Acts as a lysyl-hydroxylase that catalyzes 5-hydroxylation on specific lysine residues of target proteins such as u2af2/u2af65 and LUC7L2. Regulates RNA splicing by mediating 5-hydroxylat... |
Q6NYC1 | MNHKSKKRIREAKRSARPELKDSLDWTRHNYYESFSLSPAAVADNVERADALQLSVEEFVERYERPYKPVVLLNAQEGWSAQEKWTLERLKRKYRNQKFKCGEDNDGYSVKMKMKYYIEYMESTRDDSPLYIFDSSYGEHPKRRKLLEDYKVPKFFTDDLFQYAGEKRRPPYRWFVMGPPRSGTGIHIDPLGTSAWNALVQGHKRWCLFPTSTPRELIKVTRDEGGNQQDEAITWFNVIYPRTQLPTWPPEFKPLEILQKPGETVFVPGGWWHVVLNLDTTIAITQNFASSTNFPVVWHKTVRGRPKLSRKWYRILKQEH... | Cofactor: Binds 1 Fe(2+) ion per subunit.
Function: Dioxygenase that can both act as a arginine demethylase and a lysyl-hydroxylase . Acts as a lysyl-hydroxylase that catalyzes 5-hydroxylation on specific lysine residues of target proteins such as U2AF2/U2AF65 and LUC7L2. Regulates RNA splicing by mediating 5-hydroxyla... |
Q6Q4H1 | MDKRTDDAVRETKLKARPELKGDEGWTRLGYANNFDLSYQHIKDTLPRIHCKSISHDEFIARYEKPRIPVILTGCTDSWLANQKWKLSSLAKKYRNQKFKVGEDNDGFSVKMKMKYYIEYLKHQKDDSPLYIFDGSYGEHPKKRKLLDDYHPPSFFQDDLFKYAGEKRRPPYRWIVIGPARSGTGIHIDPLGTSAWNALISGHKRWMMFPTETPKHLLEVSKQDGQHQSGEGIQWFVKVYPKVKSPTWPKEYAPLEIIQHPGETVFVPGGWWHVVLNLDQTVAVTQNFSSPTNFHVVWHKTVRGRPKLSQKWLRALKIYR... | Cofactor: Binds 1 Fe(2+) ion per subunit.
Function: Dioxygenase that can both act as a histone arginine demethylase and a lysyl-hydroxylase.
Sequence Mass (Da): 44240
Sequence Length: 385
Subcellular Location: Nucleus
EC: 1.14.11.-
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Q9ERI5 | MNHKSKKRIREAKRSARPELKDSLDWTRHNYYESYPLNPAAVPDNVERADALQLSVKEFVERYERPYKPVVLLNAQEGWSAQEKWTLERLKRKYRNQKFKCGEDNDGYSVKMKMKYYIEYMESTRDDSPLYIFDSSYGEHPKRRKLLEDYKVPKFFTDDLFQYAGEKRRPPYRWFVMGPPRSGTGIHIDPLGTSAWNALVQGHKRWCLFPTNTPRELIKVTREEGGNQQDEAITWFNVIYPRTQLPTWPPEFKPLEILQKPGETVFVPGGWWHVVLNLDTTIAITQNFASSTNFPVVWHKTVRGRPKLSRKWYRILKQEH... | Cofactor: Binds 1 Fe(2+) ion per subunit.
Function: Dioxygenase that can both act as a arginine demethylase and a lysyl-hydroxylase. Acts as a lysyl-hydroxylase that catalyzes 5-hydroxylation on specific lysine residues of target proteins such as U2AF2/U2AF65 and LUC7L2. Regulates RNA splicing by mediating 5-hydroxylat... |
Q6AYK2 | MNHKSKKRIREAKRSARPELKDSLDWTRHNYYESYPLSPAAVPDNVERADALQLSVKEFVERYERPYKPVVLLNAQEGWSAQEKWTLERLKRKYRNQKFKCGEDNDGYSVKMKMKYYIEYMESTRDDSPLYIFDSSYGEHPKRRKLLEDYKVPKFFTDDLFQYAGEKRRPPYRWFVMGPPRSGTGIHIDPLGTSAWNALVQGHKRWCLFPTNTPRELIKVTREEGGNQQDEAITWFNVIYPRTQLPTWPPEFKPLEILQKPGETVFVPGGWWHVVLNLDTTIAITQNFASSTNFPVVWHKTVRGRPKLSRKWYRILKQEH... | Cofactor: Binds 1 Fe(2+) ion per subunit.
Function: Dioxygenase that can both act as a arginine demethylase and a lysyl-hydroxylase. Acts as a lysyl-hydroxylase that catalyzes 5-hydroxylation on specific lysine residues of target proteins such as U2AF2/U2AF65 and LUC7L2. Regulates RNA splicing by mediating 5-hydroxylat... |
P0C870 | MAEAALEAVRSELREFPAAARELCVPLAVPYLDKPPTPLHFYRDWVCPNRPCIIRNALQHWPALQKWSLPYFRATVGSTEVSVAVTPDGYADAVRGDRFMMPAERRLPLSFVLDVLEGRAQHPGVLYVQKQCSNLPSELPQLLPDLESHVPWASEALGKMPDAVNFWLGEAAAVTSLHKDHYENLYCVVSGEKHFLFHPPSDRPFIPYELYTPATYQLTEEGTFKVVDEEAMEKVPWIPLDPLAPDLARYPSYSQAQALRCTVRAGEMLYLPALWFHHVQQSQGCIAVNFWYDMEYDLKYSYFQLLDSLTKASGLD | Function: Bifunctional enzyme that acts both as an endopeptidase and 2-oxoglutarate-dependent monooxygenase . Endopeptidase that cleaves histones N-terminal tails at the carboxyl side of methylated arginine or lysine residues, to generate 'tailless nucleosomes', which may trigger transcription elongation . Preferential... |
P0C872 | MAEAALEAVRRALQEFPAAARDLNVPRVVPYLDEPPSPLCFYRDWVCPNRPCIIRNALQHWPALQKWSLSYLRATVGSTEVSVAVTPDGYADAVRGDRFVMPAERRLPISHVLDVLEGRAQHPGVLYVQKQCSNLPTELPQLLSDIESHVPWASESLGKMPDAVNFWLGDASAVTSLHKDHYENLYCVVSGEKHFLLHPPSDRPFIPYNLYTPATYQLTEEGTFRVVDEEAMEKVPWIPLDPLAPDLTQYPSYSQAQALHCTVRAGEMLYLPALWFHHVQQSHGCIAVNFWYDMEYDLKYSYFQLMDTLTRATGLD | Function: Bifunctional enzyme that acts both as an endopeptidase and 2-oxoglutarate-dependent monooxygenase (By similarity). Endopeptidase that cleaves histones N-terminal tails at the carboxyl side of methylated arginine or lysine residues, to generate 'tailless nucleosomes', which may trigger transcription elongatio... |
Q96S16 | MAPASRLLALWALAAVALPGSGAEGDGGWRPGGPGAVAEEERCTVERRADLTYAEFVQQYAFVRPVILQGLTDNSRFRALCSRDRLLASFGDRVVRLSTANTYSYHKVDLPFQEYVEQLLHPQDPTSLGNDTLYFFGDNNFTEWASLFRHYSPPPFGLLGTAPAYSFGIAGAGSGVPFHWHGPGYSEVIYGRKRWFLYPPEKTPEFHPNKTTLAWLRDTYPALPPSARPLECTIRAGEVLYFPDRWWHATLNLDTSVFISTFLG | Function: Functions as a positive regulator of TNF-induced NF-kappa-B signaling . Regulates angiogenesis and cellular metabolism through interaction with PKM .
PTM: N-glycosylated.
Sequence Mass (Da): 29509
Sequence Length: 264
Subcellular Location: Endoplasmic reticulum lumen
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A0A061FBW2 | MEVMQVLHMNKGNGETSYAKNSTVQSKIISVGKPIIEEAVHEISCNNLLESMGIADLGCSSGPNTLSVISEIMDMVQTTSRRLGRPVPEFRVYLNDLYSNDFNYIFMSLPAFYHRLKEEKGIGCGSCYISGVAGSFYGRLFPSKSLHFVHSSSSLHWLSQVPPGLESKALAPLNKGKVYISKSSPQSVLNAYSLQFQNDFSMFIESRSQELVPGGRMVLSFMGRRSTDPTTEESCHHWELLAQAIMSLVREGLIEEAKVDSFNAPYYAPCAEEIKVEIQKVGSFVIDRLEGFEIDWDGGAVSDVQTAQGKLLIGQRVAKT... | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Catalyzes the methylation of jasmonate into methyljasmonate, a plant volatile that acts as an important cellular regulator mediating diverse developmental processes and defense responses.
Catalytic Activity: jasmonate + S-adenosyl-L-methionine = methyl (-)-jasmonate +... |
Q9AR07 | MEVMRVLHMNKGNGETSYAKNSTAQSNIISLGRRVMDEALKKLMMSNSEISSIGIADLGCSSGPNSLLSISNIVDTIHNLCPDLDRPVPELRVSLNDLPSNDFNYICASLPEFYDRVNNNKEGLGFGRGGGESCFVSAVPGSFYGRLFPRRSLHFVHSSSSLHWLSQVPCREAEKEDRTITADLENMGKIYISKTSPKSAHKAYALQFQTDFWVFLRSRSEELVPGGRMVLSFLGRRSLDPTTEESCYQWELLAQALMSMAKEGIIEEEKIDAFNAPYYAASSEELKMVIEKEGSFSIDRLEISPIDWEGGSISEESYDL... | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Catalyzes the methylation of jasmonate into methyljasmonate, a plant volatile that acts as an important cellular regulator mediating diverse developmental processes and defense responses.
Catalytic Activity: jasmonate + S-adenosyl-L-methionine = methyl (-)-jasmonate +... |
Q8N9B5 | MSFALEETLESDWVAVRPHVFDEREKHKFVFIVAWNEIEGKFAITCHNRTAQRQRSGSREQAGARGGAEAGGAASDGSRGPGSPAGRGRPEATASATLVRSPGPRRSSAWAEGGSPRSTRSLLGDPRLRSPGSKGAESRLRSPVRAKPIPGQKTSEADDAAGAAAAAARPAPREAQVSSVRIVSASGTVSEEIEVLEMVKEDEAPLALSDAEQPPPATELESPAEECSWAGLFSFQDLRAVHQQLCSVNSQLEPCLPVFPEEPSGMWTVLFGGAPEMTEQEIDTLCYQLQVYLGHGLDTCGWKILSQVLFTETDDPEEYY... | Function: Acts both as a nuclear p53/TP53-cofactor and a cytoplasmic regulator of actin dynamics depending on conditions . In nucleus, acts as a cofactor that increases p53/TP53 response via its interaction with p300/EP300. Increases p53/TP53-dependent transcription and apoptosis, suggesting an important role in p53/TP... |
Q9HCI6 | MGDPGSEIIESVPPAGPEASESTTDENEDDIQFVSEGPSRPVLEYIDLVCGDDENPSAYYSDILFPKMPKRQGDFLHFLNVKKVKTDTENNEVSKNHCRLSKAKEPHFEYIEQPIIEEKPSLSSKKEIDNLVLPDCWNEKQAFMFTEQYKWLEIKEGKLGCKDCSAVRHLGSKAEKHVHVSKEWIAYLVTPNGSNKTTRQASLRKKIREHDVSKAHGKIQDLLKESTNDSICNLVHKQNNKNIDATVKVFNTVYSLVKHNRPLSDIEGARELQEKNGEVNCLNTRYSATRIAEHIAKEMKMKIFKNIIEENAKICIIIDE... | Function: E3 SUMO-protein ligase; facilitates UBE2I/UBC9-mediated SUMO2 modification of target proteins .
Sequence Mass (Da): 89673
Sequence Length: 787
Domain: Binds UBE2I/UBC9 and two SUMO2 molecules via its N-terminus. The most N-terminal region interacts with the SUMO2 chain that is covalently bound to the UBE2I/UB... |
Q9QR69 | MKTLIFFWNLWLWALLVCFWCITLVCVTTNSIDTMASLLVMCILFVSAINKYTQAISSNNPKWPSSWHLGIIACIVLKLWNLSTTNSVTYACLITTAILSLVTAFLTLIKHCTACKLQLEHGILFTSTFAVLMTNMLVHMSNTWQSSWIFFPISFTLSLPFLYAFATVKTGNIKLVSSVSFICAGLVMGYPVSCCKTHTCTATAAGLSLSSIYLGFTGIISTLHKSWAPPKRGILTFLLLQGGVLTTQTLTTELLAITSTTGNIKGHEILLLVCLIFLWCLYVWQSFNKASLVTGMLHLIAAWSHTGGCVQLVMLLPSGL... | Function: Plays a crucial role for reactivation of the virus from latency, early viral gene expression and virus production. Modulates host signaling pathways including activation of MAP kinases c-JUN-N-terminal kinase (JNK), ERK2, and NF-kappa-B resulting in the activation of AP-1 and NFAT-dependent gene expression in... |
P04264 | MSRQFSSRSGYRSGGGFSSGSAGIINYQRRTTSSSTRRSGGGGGRFSSCGGGGGSFGAGGGFGSRSLVNLGGSKSISISVARGGGRGSGFGGGYGGGGFGGGGFGGGGFGGGGIGGGGFGGFGSGGGGFGGGGFGGGGYGGGYGPVCPPGGIQEVTINQSLLQPLNVEIDPEIQKVKSREREQIKSLNNQFASFIDKVRFLEQQNQVLQTKWELLQQVDTSTRTHNLEPYFESFINNLRRRVDQLKSDQSRLDSELKNMQDMVEDYRNKYEDEINKRTNAENEFVTIKKDVDGAYMTKVDLQAKLDNLQQEIDFLTALYQ... | Function: May regulate the activity of kinases such as PKC and SRC via binding to integrin beta-1 (ITB1) and the receptor of activated protein C kinase 1 (RACK1). In complex with C1QBP is a high affinity receptor for kininogen-1/HMWK.
PTM: Undergoes deimination of some arginine residues (citrullination).
Sequence Mass ... |
P13647 | MSRQSSVSFRSGGSRSFSTASAITPSVSRTSFTSVSRSGGGGGGGFGRVSLAGACGVGGYGSRSLYNLGGSKRISISTSGGSFRNRFGAGAGGGYGFGGGAGSGFGFGGGAGGGFGLGGGAGFGGGFGGPGFPVCPPGGIQEVTVNQSLLTPLNLQIDPSIQRVRTEEREQIKTLNNKFASFIDKVRFLEQQNKVLDTKWTLLQEQGTKTVRQNLEPLFEQYINNLRRQLDSIVGERGRLDSELRNMQDLVEDFKNKYEDEINKRTTAENEFVMLKKDVDAAYMNKVELEAKVDALMDEINFMKMFFDAELSQMQTHVSD... | Function: Required for the formation of keratin intermediate filaments in the basal epidermis and maintenance of the skin barrier in response to mechanical stress (By similarity). Regulates the recruitment of Langerhans cells to the epidermis, potentially by modulation of the abundance of macrophage chemotactic cytokin... |
Q922U2 | MSRQSSVSFRSGGSRSFSAASAITPSVSRTSFSSVSRSGGGGGGRISLGGACGAGGYGSRSLYNVGGSKRISYSSGGGSFRNQFGAGGFGFGGGAGSGFGFGGGAGSGFGFGGGAGFGGGYGGAGFPVCPPGGIQEVTVNQNLLTPLNLQIDPTIQRVRTEEREQIKTLNNKFASFIDKVRFLEQQNKVLDTKWALLQEQGTKTIKQNLDPLFEQYINNLRRQLDGVLGERGRLDSELRNMQDLVEDYKNKYEDEINKRTTAENEFVMLKKDVDAAYMNKVELEARVDALMDEINFMKMFFDAELSQMQTHVSDTSVVLS... | Function: Required for the formation of keratin intermediate filaments in the basal epidermis and maintenance of the skin barrier in response to mechanical stress . Regulates the recruitment of Langerhans cells to the epidermis, potentially by modulation of the abundance of macrophage chemotactic cytokines, macrophage ... |
P35028 | MKIGIVTGIPGVGKSTVLAKVKEILDNQGINNKIINYGDFMLATALKLGYAKDRDEMRKLSVEKQKKLQIDAAKGIAEEARAGGEGYLFIDTHAVIRTPSGYLPGLPSYVITEINPSVIFLLEADPKIILSRQKRDTTRNRNDYSDESVILETINFARYAATASAVLAGSTVKVIVNVEGDPSIAANEIIRSMK | Catalytic Activity: AMP + ATP = 2 ADP
Sequence Mass (Da): 21110
Sequence Length: 194
Subcellular Location: Cytoplasm
EC: 2.7.4.3
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Q975K4 | MKIGIVTGIPGVGKTTVLSKVKEILEEKKINNKIVNYGDYMLMTAMKLGYVNNRDEMRKLPVEKQKQLQIEAARGIANEAKEGGDGLLFIDTHAVIRTPSGYLPGLPKYVIEEINPRVIFLLEADPKVILDRQKRDTSRSRSDYSDERIISETINFARYAAMASAVLVGATVKIVINVEGDPAVAANEIINSML | Catalytic Activity: AMP + ATP = 2 ADP
Sequence Mass (Da): 21447
Sequence Length: 194
Subcellular Location: Cytoplasm
EC: 2.7.4.3
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Q9HIT1 | MRSVITGVAGVGKTTVLDIVSKETGIKIVNYGTLMFDLAKKRGLVENRDQMRKLSRDIQIDLQKNAATEIGRMEDVIVDTHMSIKTPFGYLPGLPEWVLREINASAFIIIEADPELILRRRQNDPTRARDEDSVESIREHQEINRAFAAAYSIFSGATVKIITNEEGKPDKAAHDIIKVIAVD | Catalytic Activity: AMP + ATP = 2 ADP
Sequence Mass (Da): 20445
Sequence Length: 183
Subcellular Location: Cytoplasm
EC: 2.7.4.3
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Q5JJH2 | MPFVVVITGIPGVGKSTITKLALKKTRAKFRLVNFGDLMFEEAVNMGLVKHRDEMRKLDPLTQKELQLKVAQRIVEIARKEPVLLDTHATIRTPAGYLLGFPREVIEILNPNFIVIIEAAPSEILGRRLRDLKRDRDVETEEQIARHQDLNRAAAIAYAMHSNALIKIIENHEDKGLEEAVNELVKVLDLAVSEYA | Catalytic Activity: AMP + ATP = 2 ADP
Sequence Mass (Da): 22138
Sequence Length: 196
Subcellular Location: Cytoplasm
EC: 2.7.4.3
|
Q54CT8 | MALNLLRNYSTKIRMDHLRMTIIGAPGSGKGTQSEKLKKDYNLPIISTGQILREVSEQNTKSGIEIKSKLAAGELISDAIMSDIITEHLTKTGNSWLLDGYPRNTEQAKGLDKYLNVKMALNVVLHLDVPEKVLAERVQDRWVHPGSGRVYNSVFSPPKVKGIDDVTGEPLVRRSDDKDEEVFRNRIQTFKNNTLPLLKYYEDRGVLYTIDSPNSDEGYVKIKQILDSILTK | Function: Catalyzes the reversible transfer of the terminal phosphate group between ATP and AMP. Plays an important role in cellular energy homeostasis and in adenine nucleotide metabolism.
Catalytic Activity: AMP + ATP = 2 ADP
Sequence Mass (Da): 26172
Sequence Length: 232
Subcellular Location: Cytoplasm
EC: 2.7.4.3
|
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