ids stringlengths 6 10 | seqs stringlengths 11 1.02k | texts stringlengths 108 11.1k |
|---|---|---|
A8HAL1 | MGKKKVKDRSAGTDSSSETAGPSCTHIRKGTENSVLKKACLNEHWSSCQDCEQDKPEEKQILEDQTDGESPAVWMCLKCGHRGCGRSGNQHAIKHYETPRSEPHCLVLSLDVWSVWCYICDDEVQYSSTGQLAQLITNIRKQVLTAPDKRNASKKSWKEDISVMNSAEQTQDEEKGKKGKQKSSSKQEDSPKSHQSAAAGSSAVVSVRGLSNLGNTCFFNAVVQSLSQTQYLRELLKQIAEEKSSFSITPALSSELDPLQIQLERPGSLTLAMCQLMNEIQETKKGVVTPKELFTQVCKKAPRFKGFQQQDSQELLRYLL... | Function: Specifically deubiquitinates 'Lys-120' of histone H2A (H2AK119Ub), a specific tag for epigenetic transcriptional repression, thereby acting as a coactivator. Deubiquitination of histone H2A is a prerequisite for subsequent phosphorylation at 'Ser-11' of histone H3 (H3S10ph), and is required for chromosome seg... |
Q9Y5T5 | MGKKRTKGKTVPIDDSSETLEPVCRHIRKGLEQGNLKKALVNVEWNICQDCKTDNKVKDKAEEETEEKPSVWLCLKCGHQGCGRNSQEQHALKHYLTPRSEPHCLVLSLDNWSVWCYVCDNEVQYCSSNQLGQVVDYVRKQASITTPKPAEKDNGNIELENKKLEKESKNEQEREKKENMAKENPPMNSPCQITVKGLSNLGNTCFFNAVMQNLSQTPVLRELLKEVKMSGTIVKIEPPDLALTEPLEINLEPPGPLTLAMSQFLNEMQETKKGVVTPKELFSQVCKKAVRFKGYQQQDSQELLRYLLDGMRAEEHQRVS... | Function: Specifically deubiquitinates 'Lys-120' of histone H2A (H2AK119Ub), a specific tag for epigenetic transcriptional repression, thereby acting as a coactivator . Deubiquitination of histone H2A is a prerequisite for subsequent phosphorylation at 'Ser-11' of histone H3 (H3S10ph), and is required for chromosome se... |
Q0VA64 | MVKKRGKNLPAQDSLDAEPVCKHLRKALDEGSVKKALVNVEWTVCQECQADNKEKNNSDDELVEDPSVWLCLKCGHRGCGRNSASQHALNHYNTPRSEPHCLVLSVDMWSAWCYLCDNEVPYNRSSRLGQLVDYLQRKAKAKSKSTDSAALDEEVKAEIVAENEVKIEDQEEKPKGQAKWDKASSTQNNSTEPTVKGLSNLGNTCFFNAVMQNLSQTPAVRELLNEAKTLKKPVTVPLPDSSSPTNVEVHLEQQPGPLTLAMWQFLTEMQETKKGVVTPKEVFSQVCKKAIRFKGYQQQDSQELLRYLLDGMRGEEIQRV... | Function: Specifically deubiquitinates 'Lys-120' of histone H2A (H2AK119Ub), a specific tag for epigenetic transcriptional repression, thereby acting as a coactivator. Deubiquitination of histone H2A is a prerequisite for subsequent phosphorylation at 'Ser-11' of histone H3 (H3S10ph), and is required for chromosome seg... |
Q9FKP5 | MMLVFLLIRRQWRSASVRREEVIRLIALATEESYLAEEVRPATVDYGGDSVSDVYRCAVCLYPTTTRCSQCKSVRYCSSKCQILHWRRGHKEECRSPDYDEEKEEYVQSDYDAKESNVDFPSRGTAYESSSNVSVDVACDMSTSRPSIHKVQPRSEAVDFTTSLNIKDNLYETRPLSRKKSRNRTDKVESASNYSKGKTDAKLRKLGNQNSRRSGDSANMSISDQFLSVGFEEEMNALKHERITSEPSSASAAMSSSSTLLLPSKANSKPKVSQASSSGLKTSVQKVVQHFRPPQSSKKSQPSSSIDEMSFSYELFVKLY... | Function: Recognizes and hydrolyzes the peptide bond at the C-terminal Gly of ubiquitin. Involved in the processing of poly-ubiquitin precursors as well as that of ubiquitinated proteins (By similarity).
Catalytic Activity: Thiol-dependent hydrolysis of ester, thioester, amide, peptide and isopeptide bonds formed by th... |
Q67XW5 | MHEVGFPLDLSVFTRLIATLFFLAVGVFYFLKNTAAKYFDIGAAAAGGFDRDFMAVDAEDCSVCGNFSTKKCSRCKSVRYCSAECQRSDWSSGHQRNCRDYGITTLTPSAKNGLRFRASPFGDSSASSIALISERGQNKSSLKPREVLFPYEEFVEYFNWDNPELAPCGLMNCGNSCFANVILQCLSWTRPLVAYLLEKGHKRECMRNDWCFLCEFQTHVERASQSRFPFSPMNIISRLTNIGGTLGYGRQEDAHEFMRYAIDMMQSVCLDEFGGEKIVPPRSQETTLIQYIFGGLLQSQVQCTVCNHVSDQYENMMDLI... | Function: Recognizes and hydrolyzes the peptide bond at the C-terminal Gly of ubiquitin. Involved in the processing of poly-ubiquitin precursors as well as that of ubiquitinated proteins (By similarity).
Catalytic Activity: Thiol-dependent hydrolysis of ester, thioester, amide, peptide and isopeptide bonds formed by th... |
Q9UMW8 | MSKAFGLLRQICQSILAESSQSPADLEEKKEEDSNMKREQPRERPRAWDYPHGLVGLHNIGQTCCLNSLIQVFVMNVDFTRILKRITVPRGADEQRRSVPFQMLLLLEKMQDSRQKAVRPLELAYCLQKCNVPLFVQHDAAQLYLKLWNLIKDQITDVHLVERLQALYTIRVKDSLICVDCAMESSRNSSMLTLPLSLFDVDSKPLKTLEDALHCFFQPRELSSKSKCFCENCGKKTRGKQVLKLTHLPQTLTIHLMRFSIRNSQTRKICHSLYFPQSLDFSQILPMKRESCDAEEQSGGQYELFAVIAHVGMADSGHYC... | Function: Interferon-induced ISG15-specific protease that plays a crucial role for maintaining a proper balance of ISG15-conjugated proteins in cells . Regulates protein ISGylation by efficiently cleaving ISG15 conjugates linked via isopeptide bonds. Regulates T-cell activation and T-helper 17 (Th17) cell differentiati... |
Q9SJA1 | MHEVGLFVDLNSFTQLILTLFFVSIGLLYFVKRTAAKYFEVGGGSGGFDRDHRRDFMVSDTAECSVCGKATTKKCSRCKSVRYCSAACQTSDWKSGHKLKCKGFRSTDSSPVRRDDIDFEASLFGNRSASKKTRIALVPQQSQSKATLKPTDVLFPYESFVRYYNWDRPIMAPCGLTNCGNSCFANVVLQCLSWTRPLVAYLLERGHKRECRRNDWCFLCEFENHLDRANYSRFPFSPMNIISRLPNIGGNLGYGRQEDAHELMRFAIDMMQSVCLDEFGGEKVVPPRAQETTLIQYIFGGLLQSQVQCTACSNVSDQYE... | Function: Recognizes and hydrolyzes the peptide bond at the C-terminal Gly of ubiquitin. Involved in the processing of poly-ubiquitin precursors as well as that of ubiquitinated proteins (By similarity).
Catalytic Activity: Thiol-dependent hydrolysis of ester, thioester, amide, peptide and isopeptide bonds formed by th... |
Q70CQ1 | MDRCKHVGRLRLAQDHSILNPQKWCCLECATTESVWACLKCSHVACGRYIEDHALKHFEETGHPLAMEVRDLYVFCYLCKDYVLNDNPEGDLKLLRSSLLAVRGQKQDTPVRRGRTLRSMASGEDVVLPQRAPQGQPQMLTALWYRRQRLLARTLRLWFEKSSRGQAKLEQRRQEEALERKKEEARRRRREVKRRLLEELASTPPRKSARLLLHTPRDAGPAASRPAALPTSRRVPAATLKLRRQPAMAPGVTGLRNLGNTCYMNSILQVLSHLQKFRECFLNLDPSKTEHLFPKATNGKTQLSGKPTNSSATELSLRND... | Function: Specifically deubiquitinates histone H2B at 'Lys-120' (H2BK120Ub). H2BK120Ub is a specific tag for epigenetic transcriptional activation and acts as a regulator of mRNA splicing. Deubiquitination is required for efficient cotranscriptional splicing of a large set of exons.
Catalytic Activity: Thiol-dependent ... |
Q8LAM0 | MGAAGSKLEKALGDQFPEGERYFGFENFGNTCYCNSVLQALYFCAPFREQLLEHYANNKADAEENLLTCLADLFSQISSQKKKTGVIAPKRFVQRLKKQNELFRSYMHQDAHEFLNYLLNELVEILEKETQATKADNETSSSPEKIANVLKAPLANGVHKEPIVTWVHKIFQGILTNETRCLRCETVTARDETFLDLSLDIEQNSSITSCLKNFSSTETLHAEDKFFCDKCCSLQEAQKRMKIKKPPHILVIHLKRFKYMEQLGRYKKLSYRVVFPLELKLSNTVDEYVDIEYSLFAVVVHVGSGPNHGHYVSLVKSHNH... | Function: Recognizes and hydrolyzes the peptide bond at the C-terminal Gly of ubiquitin. Involved in the processing of poly-ubiquitin precursors as well as that of ubiquitinated proteins. Required for the correct development of pollen.
Catalytic Activity: Thiol-dependent hydrolysis of ester, thioester, amide, peptide a... |
Q6FQF0 | MPGIEQPVSRKNETLVKLSSLADEFVFNDEVQLNLQDVLQECVDTYQNYQDEVKKIKNMDHTESEKVSELCKSAYIYYKIVHNFITKVIPHLPEFEVATGPKASKLQAELIKIYYSLFSRLESDKKISYIKNIIIKHMDTQENNHSVESHEQVKLSNKKLPVNRDAIEIDKDSILQDIRYINGKRSGSGISCSELLSLMKMKEDSLLLIDVRPKLEYDAHHIKTKNIICIEPISFKESYSDQQIEKTSMIPSPKHEIQLFQRRSEFQYIILYTDLEEKSNFYFQQLKSLLEILLQRSFLRPIDDRKTKVLFLSDSLQNWI... | Function: Ubiquitin thioesterase that acts at the late endosome/prevacuolar compartment to recover ubiquitin from ubiquitinated membrane proteins en route to the vacuole. Removes also ubiquitin from soluble proteins targeted to proteasomes. Is essential to maintain a normal level of free ubiquitin. Required for promoti... |
Q13107 | MAEGGGCRERPDAETQKSELGPLMRTTLQRGAQWYLIDSRWFKQWKKYVGFDSWDMYNVGEHNLFPGPIDNSGLFSDPESQTLKEHLIDELDYVLVPTEAWNKLLNWYGCVEGQQPIVRKVVEHGLFVKHCKVEVYLLELKLCENSDPTNVLSCHFSKADTIATIEKEMRKLFNIPAERETRLWNKYMSNTYEQLSKLDNTVQDAGLYQGQVLVIEPQNEDGTWPRQTLQSKSSTAPSRNFTTSPKSSASPYSSVSASLIANGDSTSTCGMHSSGVSRGGSGFSASYNCQEPPSSHIQPGLCGLGNLGNTCFMNSALQCL... | Function: Deubiquitinating enzyme that removes conjugated ubiquitin from target proteins . Deubiquitinates PDPK1 . Deubiquitinates TRIM21 . Deubiquitinates receptor ADORA2A which increases the amount of functional receptor at the cell surface . Deubiquitinates HAS2 . May regulate mRNA splicing through deubiquitination ... |
O60139 | MSDDYFDRLFELAFVYINEDETIQSCSFRGQRWLEEAQTLEQKNSLLKAYYYYLKALKLAYEIPCRFEISVKSTHYGEFKQFQKLAIQAVSKAFTIKSKLAVKHYLPVIQISDALSLSKKSSLKVLFLNFYSQESSKGYVFSKHTIAIPISCLQSMDSSKIYDFLKSAPFHPSMVICYSLERYFEDVSLAYKLYSMLRSLKLDPHFMELANPKKVDSSLSYENYQPIGLTNLGNTCYMNCVLQCLFACKDLTIPMLQGRGLLQNINTKNPLGTGGKITSAFFSLLQSVLLNHGQRSISPRNFLEIVQSLNRDFSIDGQCD... | Function: Has an ATP-independent isopeptidase activity, cleaving at the C-terminus of the ubiquitin moiety. Acts late in the proteolytic pathway in conjunction with the 26S proteasome. Plays a role in avoiding DNA overreplication (By similarity).
Catalytic Activity: Thiol-dependent hydrolysis of ester, thioester, amide... |
A7TGY3 | MVEVDSRKQLLYDPIVRLSGIADKFVMQDATSSNMKVSLQECIDTLANYQDECKKLKRNEPTLSPSERYSIYESAYIYYKIIHIMVLTRIPSLPQFSSAKSSDATNEDKELMQIYNMLVKTLLSDEKIAQIKSYLRANYPDKNSKGKESIVNKQLLNNEVFMLPLSGSPISAVQLNHLIQMYDSSLLLIDVRPRAEFDSKHIKAKSVICVEPVSFKNSFTDLEVEKKSLITSPQKEIALFQARDKYNYIVIYTQQSEKTQFYMHQQLVLLDILMNKSFAKPLNEKNIKVFTLDKGFSGWVSKKGACETTTQNGDAIYISG... | Function: Ubiquitin thioesterase that acts at the late endosome/prevacuolar compartment to recover ubiquitin from ubiquitinated membrane proteins en route to the vacuole. Removes also ubiquitin from soluble proteins targeted to proteasomes. Is essential to maintain a normal level of free ubiquitin. Required for promoti... |
Q6NXA9 | MADCTTLDSLLEMGFGRNRAEKAVAHTGNQGIERAMDWLMEHENDPDIDEPYVPPAGNTLGPAEEQSQSPTEIPESIEDTEEGNARQPMTEEERKEQVKRLEDLMKARQEERRERERQEGIEREKQRRKQGQELLQVRQKLQEDEMKKLADQRRKEKMEDRLAKQRVKDKIARDREERAQKFGGGSSSTGLSSPPAEAPALSPPENQGAPPAKKDYDDCRIQVRLLDGTTLSTVFKAQEPLAAVRVYVQMNGANGQDFNLITPYPRRVYTDLDMEKPLRELGLVPSAVLVVTKK | Function: Ubiquitin-binding protein that specifically binds 'Lys-6'-linked polyubiquitin chains. Component of a complex required to couple deglycosylation and proteasome-mediated degradation of misfolded proteins in the endoplasmic reticulum that are retrotranslocated in the cytosol. Involved in ubiquitin-proteasome sy... |
Q04323 | MAELTALESLIEMGFPRGRAEKALALTGNQGIEAAMDWLMEHEDDPDVDEPLETPLGHILGREPTSSEQGGLEGSGSAAGEGKPALSEEERQEQTKRMLELVAQKQREREEREEREALERERQRRRQGQELSAARQRLQEDEMRRAAEERRREKAEELAARQRVREKIERDKAERAKKYGGSVGSQPPPVAPEPGPVPSSPSQEPPTKREYDQCRIQVRLPDGTSLTQTFRAREQLAAVRLYVELHRGEELGGGQDPVQLLSGFPRRAFSEADMERPLQELGLVPSAVLIVAKKCPS | Function: Ubiquitin-binding protein that plays a role in the modulation of innate immune response. Blocks both the RIG-I-like receptors (RLR) and NF-kappa-B pathways. Following viral infection, UBXN1 is induced and recruited to the RLR component MAVS. In turn, interferes with MAVS oligomerization, and disrupts the MAVS... |
Q499N6 | MAELTALESLIEMGFPRGRAEKALALTGNQGIEAAMDWLMEHEDDPDVDEPLETPLSHILGREPTPSEQVGPEGSGSAAGESKPVLTEEERQEQTKRMLELVAQKQREREEREEREALEREKQRRRQGQELSAARQKLQEDEIRRAAEERRREKAEELAARQRVREKIERDKAERAQKYGGTVGSRSSPPATDPGPVPSSPRQEPPTKREYDQCRIQVRLPDGTSLTQTFRAREQLAAVRLYVELHRGEEPGQDQDPVQLLSGFPRRAFSEADMERPLQELGLVPSAVLIVAKKCPS | Function: Ubiquitin-binding protein that interacts with the BRCA1-BARD1 heterodimer, and regulates its activity. Specifically binds 'Lys-6'-linked polyubiquitin chains. Interaction with autoubiquitinated BRCA1, leads to inhibit the E3 ubiquitin-protein ligase activity of the BRCA1-BARD1 heterodimer. Component of a comp... |
P34631 | MQWFGGNVATAIQISRKNKALLIVYITTDSEDGQIFDGFWQHIDSSNLLCAVVGIKLKAGETSAQQFADIYPTPILPAAYLIDQNGKPLEVITPLVGKTYDQFRAKFDKATAQFVNGMPTAAANQLSTPSPSPAPVQVPASTDAPIPAPTPVTAPIQSSSTSQEMTRELAEKVARAKALLEQKKQKDAEKKREADKHVKEEMTKAREAKQERDAEALVKAAKQRKMEKLAAESDKKRILAQIKADREAAQKKFGKLVNTENASENTEKKQETTVGKAVPSDRCRLQVRLPDGSTFVEEFPSNDVLNSLVEIIRQKPSIAG... | Function: Probably acts as an adapter for ATPase cdc-48.1 and/or cdc-48.2, conferring substrate specificity. May play a role in the ER-associated protein degradation pathway (ERAD) possibly acting as a platform to recruit both ubql-1 and cdc-48.1 and/or cdc-48.2 to the ER during ERAD.
Location Topology: Peripheral memb... |
Q92575 | MLWFQGAIPAAIATAKRSGAVFVVFVAGDDEQSTQMAASWEDDKVTEASSNSFVAIKIDTKSEACLQFSQIYPVVCVPSSFFIGDSGIPLEVIAGSVSADELVTRIHKVRQMHLLKSETSVANGSQSESSVSTPSASFEPNNTCENSQSRNAELCEIPPTSDTKSDTATGGESAGHATSSQEPSGCSDQRPAEDLNIRVERLTKKLEERREEKRKEEEQREIKKEIERRKTGKEMLDYKRKQEEELTKRMLEERNREKAEDRAARERIKQQIALDRAERAARFAKTKEEVEAAKAAALLAKQAEMEVKRESYARERSTVA... | Function: Involved in endoplasmic reticulum-associated protein degradation (ERAD). Acts as a platform to recruit both UBQLN1 and VCP to the ER during ERAD .
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 56778
Sequence Length: 508
Domain: The UBX domain is required for interaction with VCP.
Subcellu... |
Q2KIJ6 | MKKFFQEIKADIKFKSAGPGQKLTESVGEKAPKEKPSQPPVRQPRQGPTNEAQMAAAAALARLEQKQPRARGPTSQDSIRNQVRKELRAEAAVSGDPEAPGSNTAPEPKEEGSAHLAVPGVYFTCPLTGAILRKDQRDARIREAILMHFSTDPVAASIMKIHTFNKDRDRVKLGVDTIAKYLDNIHLHPEEEKYRKIKVQNKVFQERIHCLEGTHEFFEAIGFQKVLLPIPDQEGPEEFYVLSEAALAQPQSLEWHKEQLLSAEPVRATLARQRRVFRPSTLASQFDLPADFFNLTAEEIKREQRLRSEAVERLSVLRTK... | Function: May negatively regulate the ATPase activity of VCP, an ATP-driven segregase that associates with different cofactors to control a wide variety of cellular processes. As a cofactor of VCP, it may play a role in the transport of CAV1 to lysosomes for degradation. It may also play a role in endoplasmic reticulum... |
Q9BZV1 | MKKFFQEFKADIKFKSAGPGQKLKESVGEKAHKEKPNQPAPRPPRQGPTNEAQMAAAAALARLEQKQSRAWGPTSQDTIRNQVRKELQAEATVSGSPEAPGTNVVSEPREEGSAHLAVPGVYFTCPLTGATLRKDQRDACIKEAILLHFSTDPVAASIMKIYTFNKDQDRVKLGVDTIAKYLDNIHLHPEEEKYRKIKLQNKVFQERINCLEGTHEFFEAIGFQKVLLPAQDQEDPEEFYVLSETTLAQPQSLERHKEQLLAAEPVRAKLDRQRRVFQPSPLASQFELPGDFFNLTAEEIKREQRLRSEAVERLSVLRTK... | Function: May negatively regulate the ATPase activity of VCP, an ATP-driven segregase that associates with different cofactors to control a wide variety of cellular processes . As a cofactor of VCP, it may play a role in the transport of CAV1 to lysosomes for degradation . It may also play a role in endoplasmic reticul... |
O94888 | MAAHGGSAASSALKGLIQQFTTITGASESVGKHMLEACNNNLEMAVTMFLDGGGIAEEPSTSSASVSTVRPHTEEEVRAPIPQKQEILVEPEPLFGAPKRRRPARSIFDGFRDFQTETIRQEQELRNGGAIDKKLTTLADLFRPPIDLMHKGSFETAKECGQMQNKWLMINIQNVQDFACQCLNRDVWSNEAVKNIIREHFIFWQVYHDSEEGQRYIQFYKLGDFPYVSILDPRTGQKLVEWHQLDVSSFLDQVTGFLGEHGQLDGLSSSPPKKCARSESLIDASEDSQLEAAIRASLQETHFDSTQTKQDSRSDEESES... | Function: Ubiquitin-binding adapter that links a subset of NEDD8-associated cullin ring ligases (CRLs) to the segregase VCP/p97, to regulate turnover of their ubiquitination substrates.
Sequence Mass (Da): 54862
Sequence Length: 489
Domain: The UIM (ubiquitin-interacting motif) is required to engage the NEDD8 modificat... |
P08980 | MASFTLSSATPSQLCSSKNGMFAPSLALAKAGRVNVLISKERIRGMKLTCQATSIPADNVPDMQKRETLNLLLLGALSLPTGYMLLPYASFFVPPGGGAGTGGTIAKDALGNDVIAAEWLKTHAPGDRTLTQGLKGDPTYLVVESDKTLATFGINAVCTHLGCVVPFNAAENKFICPCHGSQYNNQGRVVRGPAPLSLALAHCDVDDGKVVFVPWTETDFRTGEAPWWSA | Cofactor: Binds 1 [2Fe-2S] cluster per subunit.
Function: Component of the cytochrome b6-f complex, which mediates electron transfer between photosystem II (PSII) and photosystem I (PSI), cyclic electron flow around PSI, and state transitions.
Catalytic Activity: a plastoquinol + 2 H(+)(in) + 2 oxidized [plastocyanin] ... |
P74714 | MDNTQAIAPPSYSRRQLLNFLAGTTVAVTASAGAYAMGKFFVPPAEKGGAGGGIIAKDVLGNPIPASQILAEAPGTRALVAGLAGDPTYLIVKEDGSLDSIGIVDSCTHLGCTFPWNGNDQEFQCPCHGSRYHPDGSVARGPAPLPLKIVQVAVVDDQIFISPWTDLDPRTGEKPWWV | Cofactor: Binds 1 [2Fe-2S] cluster per subunit.
Function: Component of the cytochrome b6-f complex, which mediates electron transfer between photosystem II (PSII) and photosystem I (PSI), cyclic electron flow around PSI, and state transitions.
Catalytic Activity: a plastoquinol + 2 H(+)(in) + 2 oxidized [plastocyanin] ... |
Q7X9A6 | MASTALSTASNPTQLCRTRASSLCKPVKGLGFGRERIPRNITCMAGSISADRVPDMSKRELMNLLLLGAISLPTFGMLVPYGSFLVPAGSGSNAGGVAAKDKLGNDILVEDWLKTHGPNDRTLAQGLKGDPTYLVVESDKTLATYGINAVCTHLGCVVPWNAAENKFLCPCHGSQYNNQGKVVRGPAPLSLALVHADVDDGKVVFVPWVETDFRTGDNPWWK | Cofactor: Binds 1 [2Fe-2S] cluster per subunit.
Function: Component of the cytochrome b6-f complex, which mediates electron transfer between photosystem II (PSII) and photosystem I (PSI), cyclic electron flow around PSI, and state transitions.
Catalytic Activity: a plastoquinol + 2 H(+)(in) + 2 oxidized [plastocyanin] ... |
Q5CC92 | MSAFACSAVAAPARGAIKANSSSVCAIENGKAVAVGTSKQVGAFKPVFAAAKAAKATTFSISCSAASDEVPDMGKRKLMNLLLLGAIAGPTIGAGGPFVSFLVPPKSGGGAGAGQAAKDAAGNDIKVEKWLETXKPGDRSLAQGLKGDATYLIVKEDGTLEKYGLNAVCTHLGCVVPWNQSEGKFMCPCHGSQYDRTGKVVRGPAPLSLALAHVNVLEDGVVAFEPWTETDFRTNTAPWWK | Cofactor: Binds 1 [2Fe-2S] cluster per subunit.
Function: Component of the cytochrome b6-f complex, which mediates electron transfer between photosystem II (PSII) and photosystem I (PSI), cyclic electron flow around PSI, and state transitions.
Catalytic Activity: a plastoquinol + 2 H(+)(in) + 2 oxidized [plastocyanin] ... |
O31214 | MLASAGGYWPMSAQGVNKMRRRVLVAATSVVGAVGAGYALVPFVASMNPSARARAAGAPVEADISKLEPGALLRVKWRGKPVWVVHRSPEMLAALSSNDPKLVDPTSEVPQQPDYCKNPTRSIKPEYLVAIGICTHLGCSPTYRPEFGPDDLGSDWKGGFHCPCHGSRFDLAARVFKNVPAPTNLVIPKHVYLNDTTILIGEDRGSA | Cofactor: Binds 1 [2Fe-2S] cluster per subunit.
Function: Component of the ubiquinol-cytochrome c reductase complex (complex III or cytochrome b-c1 complex), which is a respiratory chain that generates an electrochemical potential coupled to ATP synthesis.
Catalytic Activity: a quinol + 2 Fe(III)-[cytochrome c](out) = ... |
P81380 | MASSDTAEATRRDFLYVATAAVGAAGVAAVAWPFITQMNPDAATIAAGAPIDIDISPVTEGQIVRVFWRGKPIFIRHRTAKEIQSEEAADVGALIDPQPDSARVKPGKAEWLVVYASCTHLGCIPLGHQGDWGGWFCPCHGSQYDASGRVRKGPAPTNLPVPPYEFVDNTKIRIGAGVA | Cofactor: Binds 1 [2Fe-2S] cluster per subunit.
Function: Component of the ubiquinol-cytochrome c reductase complex (complex III or cytochrome b-c1 complex), which is a respiratory chain that generates an electrochemical potential coupled to ATP synthesis.
Catalytic Activity: a quinol + 2 Fe(III)-[cytochrome c](out) = ... |
P13272 | MLSVAARSGPFAPVLSATSRGVAGALRPLVQAAVPATSESPVLDLKRSVLCRESLRGQAAGRPLVASVSLNVPASVRYSHTDIKVPDFSDYRRPEVLDSTKSSKESSEARKGFSYLVTATTTVGVAYAAKNVVSQFVSSMSASADVLAMSKIEIKLSDIPEGKNMAFKWRGKPLFVRHRTKKEIDQEAAVEVSQLRDPQHDLERVKKPEWVILIGVCTHLGCVPIANAGDFGGYYCPCHGSHYDASGRIRKGPAPLNLEVPSYEFTSDDMVIVG | Cofactor: Binds 1 [2Fe-2S] cluster per subunit. Fe-S cluster delivery to the Rieske protein is mediated by components of the iron sulfur (Fe-S) cluster assembly machinery that reside in the mitochondrial matrix (including HSC20 and LYRM7).
Function: Component of the ubiquinol-cytochrome c oxidoreductase, a multisubunit... |
P51130 | MTTASSADHPTRRDFLFVATGAAAAVGGAAALWPFISQMNPDASTIAAGAPIEVDLSPIAEGQDIKVFWRGKPIYISHRTKKQIDEARAVNVASLPDPQSDEARVKSGHEQWLVVIGICTHLGCIPIAHEGNYDGFFCPCHGSQYDSSGRIRQGPAPANLPVPPYQFVSDTKIQIG | Cofactor: Binds 1 [2Fe-2S] cluster per subunit.
Function: Component of the ubiquinol-cytochrome c reductase complex (complex III or cytochrome b-c1 complex), which is a respiratory chain that generates an electrochemical potential coupled to ATP synthesis.
Catalytic Activity: a quinol + 2 Fe(III)-[cytochrome c](out) = ... |
P80143 | MRKYYYWILLLLFLILSIYIKLIGGEQNIGFNVELFKLINYNQIATLNGLMVFLSKYGREYVWIPVTALLLIFKRTRKIGITLVISFVIAIVLGEVSKYVMAQLRPFNFVNPTYLLEPKPTDYSYPSGHALIVSTGAVTLLLTSPKWMWILGIIEAVLVSYSRVYVGVHWPLDVIAGWLLGSWISFLSVQIESTGPIKKIEQMLKA | Catalytic Activity: di-trans,octa-cis-undecaprenyl diphosphate + H2O = di-trans,octa-cis-undecaprenyl phosphate + H(+) + phosphate
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 23525
Sequence Length: 206
Subcellular Location: Cell membrane
EC: 3.6.1.27
|
O28007 | MESLDDIVREIMSCRKCDLHKTKTNYVPGVGNEKAEIVFVGEAPGRDEDLKGEPFVGAAGKLLTEMLASIGLRREDVYITNVLKCRPPNNRDPTPEEVEKCGDYLVRQLEAIRPNVIVCLGRFAAQFIFNLFDLEFTTISRVKGKVYEVERWGKKVKVIAIYHPAAVLYRPQLREEYESDFKKIGELCGKKQPTLFDYL | Function: Removes uracil bases that are present in DNA as a result of either deamination of cytosine or misincorporation of dUMP instead of dTMP. Can remove uracil from double-stranded DNA containing either a U/G or U/A base pair as well as from single-stranded DNA.
Catalytic Activity: Hydrolyzes single-stranded DNA or... |
Q8ZYS2 | MDLQKLHELIKNCDKCPLHKYRKNAVPGEGEMKLGVMIVGEAPGASEDEAGRPFVGAAGQLLTEALSRLGVRRGDVFITNVVKCRPPNNRTPNREEVEACLPYLIQQIGILKPRRIIALGLISAKALMELMGRRAEKLGDVKGKCYQGRIAGVQVELCITYHPAAVLRKPALRGEFQKDLAMFFGGGLDRFLDPSK | Function: Removes uracil bases that are present in DNA as a result of either deamination of cytosine or misincorporation of dUMP instead of dTMP. Can remove uracil from double-stranded DNA containing either a U/G or U/A base pair as well as from single-stranded DNA.
Catalytic Activity: Hydrolyzes single-stranded DNA or... |
Q97WF1 | MDNLDLIADEVRKCQKCKLWKFRKNAVPGEGNSKAEIMFIGEAPGENEDIEGKPFVGVAGKLLTRLINEILGLSREDVFITNLVKCRPPNNRDPEEDEILACSPYLTRQIESIRPHIIITLGRHSTSYLFKKMNMKMESIGKVRGKFYTWNIYGYKILVFPTYHPAAALYNPPIRKVLEEDFRKVKEALSSKPITLDNFLYGSGDKGEKGNSNSGK | Function: Removes uracil bases that are present in DNA as a result of either deamination of cytosine or misincorporation of dUMP instead of dTMP. Can remove uracil from double-stranded DNA containing either a U/G or U/A base pair as well as from single-stranded DNA.
Catalytic Activity: Hydrolyzes single-stranded DNA or... |
Q96YD0 | MDSLEKIKEEVISCKKCKLWQFRTNAVPGEGYPKAEIMFVGEAPGENEDKEGRPFVGAAGKLLTQMIKEILGLERDQVFITNVVKCRPPNNRDPEEDEITACSPYLDRQIDIIMPKIIVTLGRHSTKYIFSKMGENFSSITKVRGKSYVWKYKEKEIIVFPTYHPAAALYNPNLRKILEEDFKKIRELAITPKRYTIDYFLGGKNRSWDKREKSDSNSGK | Function: Removes uracil bases that are present in DNA as a result of either deamination of cytosine or misincorporation of dUMP instead of dTMP.
Catalytic Activity: Hydrolyzes single-stranded DNA or mismatched double-stranded DNA and polynucleotides, releasing free uracil.
Sequence Mass (Da): 25359
Sequence Length: 22... |
Q9WYY1 | MYTREELMEIVSERVKKCTACPLHLNRTNVVVGEGNLDTRIVFVGEGPGEEEDKTGRPFVGRAGMLLTELLRESGIRREDVYICNVVKCRPPNNRTPTPEEQAACGHFLLAQIEIINPDVIVALGATALSFFVDGKKVSITKVRGNPIDWLGGKKVIPTFHPSYLLRNRSNELRRIVLEDIEKAKSFIKKEG | Function: Removes uracil bases that are present in DNA as a result of either deamination of cytosine or misincorporation of dUMP instead of dTMP. Can remove uracil from double-stranded DNA containing either a U/G or U/A base pair as well as from single-stranded DNA.
Catalytic Activity: Hydrolyzes single-stranded DNA or... |
Q5SKC5 | MTLELLQAQAQNCTACRLMEGRTRVVFGEGNPDAKLMIVGEGPGEEEDKTGRPFVGKAGQLLNRILEAAGIPREEVYITNIVKCRPPQNRAPLPDEAKICTDKWLLKQIELIAPQIIVPLGAVAAEFFLGEKVSITKVRGKWYEWHGIKVFPMFHPAYLLRNPSRAPGSPKHLTWLDIQEVKRALDALPPKERRPVKAVSQEPLF | Function: Removes uracil bases that are present in DNA as a result of either deamination of cytosine or misincorporation of dUMP instead of dTMP. Can remove uracil from double-stranded DNA containing either a U/G, U/A, U/C or U/T base pair as well as from single-stranded DNA . Specifically recognizes uracil that is fli... |
Q0P8H3 | MKIVIVGIGYVGLANAILFSKNNENEVVLLDIDENKIQSINNHKSPIKDKLIEKFFVQNISKLHATSNIKEAYFNADFAVIATPTDYDEQLNFFDTRSIENVLKDIKNINSKINVIIKSTVPIGYTKTIKQKFNMSNIVFSPEFLREGSALYDSLYPSRIIIGDKSVLGKTIGDLFLKNIEKKNVDIFYMDSDEAESVKLFSNTYLAMRVGFFNEVDSYARKHNLNSADIIKGISADDRIGKYYNNPSFGYGGYCLPKDTKQLLANFYNIPNSLIKAIVETNEIRKKFITQLILEKKPNILGIYRLIMKQNSDNFRNSVI... | Function: Catalyzes the formation of UDP-glucuronic acid which is required for capsular polysaccharide synthesis. Does not catalyze the formation of glucuronamide moiety of the capsular polysaccharide.
Catalytic Activity: H2O + 2 NAD(+) + UDP-alpha-D-glucose = 3 H(+) + 2 NADH + UDP-alpha-D-glucuronate
Sequence Mass (Da... |
O94874 | MADAWEEIRRLAADFQRAQFAEATQRLSERNCIEIVNKLIAQKQLEVVHTLDGKEYITPAQISKEMRDELHVRGGRVNIVDLQQVINVDLIHIENRIGDIIKSEKHVQLVLGQLIDENYLDRLAEEVNDKLQESGQVTISELCKTYDLPGNFLTQALTQRLGRIISGHIDLDNRGVIFTEAFVARHKARIRGLFSAITRPTAVNSLISKYGFQEQLLYSVLEELVNSGRLRGTVVGGRQDKAVFVPDIYSRTQSTWVDSFFRQNGYLEFDALSRLGIPDAVSYIKKRYKTTQLLFLKAACVGQGLVDQVEASVEEAISSG... | Function: E3 protein ligase that mediates ufmylation, the covalent attachment of the ubiquitin-like modifier UFM1 to lysine residues on target proteins, and which plays a key role in reticulophagy (also called ER-phagy) induced in response to endoplasmic reticulum stress . In response to endoplasmic reticulum stress, r... |
Q2K1C8 | MAPINIVDVKKNYGSVPAVKGINLAVADGEFIVLVGPSGCGKSTLLRMIAGLESITGGRVEIGGRNVNKAEPAERDIAMVFQNYALYPHMTVRGNLEYGLKNRGTARAEIDRRVKEAADILEIGPMLDRKPRELSGGQRQRVAMGRAIVREPAAFLFDEPLSNLDAKLRVQMRVEIRRLQRRLKTTSIYVTHDQLEAMTLADRLVVMNGGLVEQVGTPVEVYDRPASLFVAGFIGSPPMNLVPIEVFHATESGGTLALPEGTDMVGLRPDALLLEKPAEPSIRLNAIVELLEPIGGESHLHVRLGEGQQTIVLTVQGRPD... | Function: Part of the ABC transporter complex UgpBAEC involved in sn-glycerol-3-phosphate (G3P) import. Responsible for energy coupling to the transport system.
Catalytic Activity: ATP + H2O + sn-glycerol 3-phosphate(out) = ADP + H(+) + phosphate + sn-glycerol 3-phosphate(in)
Location Topology: Peripheral membrane prot... |
A0A067YBQ3 | MKGTIVLYPAMGRGHIVPMVELGKFLSTHHHATLSVKILLPSPPNSTTLRYITAVSAATPSITFLHLSPSQHLLRVLQTLISQSSKPKAFILDFFNHSAADVTQTLNIPTYYYFPNAASCVALMLYTPTIHHNTKNGNSSYNDTLRRIPGLPPLSPEDMPAPLLDRRSFESFANMSIQMRKSDGIIVNTFEKLENKAFLALKNGTCVSETSRSHSSTPETRKPRIFCVGPLVSNGGGEHDNDDSGCMSWLDLQPSRTVVFLSFGSYGRFSKSQIREIALGLERSGQRFLWVVRDPYERSELSLEELLPKGFLERTKERGM... | Function: Isoflavone 7-O-glucosyltransferase converting daidzein to daidzin, genistein to genistin and formononetin to ononin . Shows some activity toward the flavanones liquiritigenin and naringenin, but not toward cyanidin, isoliquiritigenin, apigenin, luteolin, kaempferol, quercetin, daidzin and puerarin .
Catalytic... |
F8WKW0 | MVQQRHVLLITYPAQGHINPALQFAQRLLRMGIQVTLATSVYALSRMKKSSGSTPKGLTFATFSDGYDDGFRPKGVDHTEYMSSLAKQGSNTLRNVINTSADQGCPVTCLVYTLLLPWAATVARECHIPSALLWIQPVAVMDIYYYYFRGYEDDVKNNSNDPTWSIQFPGLPSMKAKDLPSFILPSSDNIYSFALPTFKKQLETLDEEERPKVLVNTFDALEPQALKAIESYNLIAIGPLTPSAFLDGKDPSETSFSGDLFQKSKDYKEWLNSRPAGSVVYVSFGSLLTLPKQQMEEIARGLLKSGRPFLWVIRAKENGE... | Function: Glucosyltransferase acting on a broad range of substrates, including crocetin, 4-coumaric acid, caffeic acid and ferulic acid. No activity with indol-3-acetic acid, bixin and norbixin, and no formation of O-glucosides. Involved with UGT94E5 in sequential glycosylation of crocetin to crocin (bis(beta-D-gentiob... |
A0A068J840 | MKSELIFLPAPAIGHLVGMVEMAKLFISRHENLSVTVLIAKFYMDTGVDNYNKSLLTNPTPRLTIVNLPETDPQNYMLKPRHAIFPSVIETQKTHVRDIISGMTQSESTQVVGLLADLLFINIMDIANEFNVPTYVYSPAGAGHLGLAFHLQTLNDKKQDVTEFRNSDTELLVPSFANPVPAEVLPSMYVDKEGGYDYLFSLFRRCRESKAIIINTFEELEPYAINSLRMDSMIPPIYPVGPILNLNGDGQNSDEAAVILGWLDDQPPSSVVFLCFGSYGSFQENQVKEIAMGLERSGHRFLWSLRPSIPKGETKLQLKY... | Function: Component of the dammarane-type triterpene saponins (e.g. ginsenosides or panaxosides) biosynthetic pathway . Glycosyltransferase that catalyzes the biosynthesis of ginsenoside F1 from protopanaxatriol (PPT) . Triggers C20-OH glycosylation of ginsenoside Rg3 to produce ginsenoside Rd . Mediates the conversion... |
A0A0D1CFF0 | MATEHILLVCWPAVGHARPMLDYAAAQLKQNPGLIITFICSKMQIALLEGLAISEHLADKKFGDRLRLLGTGRPAQEVLKEFGDREDAKNAANSASKAPNTTANGPEPEVILTMQAATLIQKRFAEIFPTILANDDLFDEQDNSLLLPACVAGKPTTIVVNWMLPGMVETVRKHSSDLKMVTFFDNSCTFVTRMLGPRSIGGFGGIERLWSQYCNSNPEVDPNDSTLKEKLLGRRWTGKFYIPGSRMGAIEEQEMAALAKDWLLSVPLTPSLIEIQKLVDASHTILINTHLAVEERELDYLRMVYPFKKIGILGPAMFSG... | Function: Glycosyltransferase; part of the gene cluster that mediates the biosynthesis of the glycolipid biosurfactant ustilagic acid (UA) . UA is a secreted cellobiose glycolipid that is toxic for many microorganisms and confers biocontrol activity to U.maydis . UA consists of 15,16-dihydroxypalmitic or 2,15,16-trihyd... |
A0A0A6ZFY4 | MDNQNGRISIALLPFLAHGHISPFFELAKQLAKRNCNVFLCSTPINLSSIKDKDSSASIKLVELHLPSSPDLPPHYHTTNGLPSHLMLPLRNAFETAGPTFSEILKTLNPDLLIYDFNPSWAPEIASSHNIPAVYFLTTAAASSSIGLHAFKNPGEKYPFPDFYDNSNITPEPPSADNMKLLHDFIACFERSCDIILIKSFRELEGKYIDLLSTLSDKTLVPVGPLVQDPMGHNEDPKTEQIINWLDKRAESTVVFVCFGSEYFLSNEELEEVAIGLEISTVNFIWAVRLIEGEKKGILPEGFVQRVGDRGLVVEGWAPQ... | Function: Component of the dammarane-type triterpene saponins (e.g. PPD-type ginsenosides or panaxosides) biosynthetic pathway . Glycosyltransferase that catalyzes the conversion of ginsenoside Rh2 to ginsenoside Rg3 . Triggers the biosynthesis of ginsenoside Rd from ginsenoside F2 .
Catalytic Activity: (20S)-ginsenosi... |
A0A291PQH4 | MEFRLLILALFSVLMSTSNGAEILALFPIHGISNYNVAEALLKTLANRGHNVTVVTSFPQKKPVPNLYEIDVSGAKGLATNSIHFERLQTIIQDVKSNFKNMVRLSRTYCEIMFSDPRVLNIRDKKFDLVINAVFGSDCDAGFAWKSQAPLISILNARHTPWALHRMGNPSNPAYMPVIHSRFPVKMNFFQRMINTGWHLYFLYMYFYYGNGEDANKMARKFFGNDMPDINEMVFNTSLLFVNTHFSVDMPYPLVPNCIEIGGIHVKEPQPLPLEIQKFMDEAEHGVIFFTLGSMVRTSTFPNQTIQAFKEAFAELPQRV... | Function: Membrane-bound UDP-glucosyltransferase (UGT) which catalyzes the C-glucosylation of kermesate and flavokermesate to produce carminate and flavokermesate 7-C-beta-D-glucoside (dcll) respectively . Carminate is used as a deterrent against insect predators .
PTM: Glycosylated.
Location Topology: Single-pass type... |
F8WKW1 | MGSISLPEKHHAVCIPYPAQGHINPMLKLAKILHHKGFHITFVNTEFNHKRLLKSRGPDALNGLPDFQFKTIPDGLPPSDVDATQDIPSLCESTTTRCLDPFRNLLAELNGPSSSQVPPVSCIVSDGVMSFTLEAAAELGVPEILFWTTSACGFLGYMHYAKLIEKGLTPLKDASYLSNGYLEQSLDWIPGMKDIRLKDLPSFLRTTNPDDYMVKFVLQETERAKKASAIILNTFQELEDDVINALSAILPPIYTIGPLQFLQKEVKDERLSVLGSNLWKEEPECLDWLDSKDPNSVVYVNFGSITVMTPGQLVEFAWGL... | Function: Iridoid glucosyltransferase acting on genipin and 7-deoxyloganetin. No activity with 7-deoxyloganetic acid. Involved in geniposide biosynthesis.
Catalytic Activity: 7-deoxyloganetin + UDP-alpha-D-glucose = 7-deoxyloganin + H(+) + UDP
Sequence Mass (Da): 53592
Sequence Length: 481
EC: 2.4.1.324
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Q91280 | LVPESSLFMHQSEDYETEVYPVSFTTEEMDATHKQLKDGLFLKQPDWTEYYVNIMRFVNFTSIHLRGCENLLENQPLMSRMRGMGFDIVLTDPFFPCGALVGNIFSIPVVNFLRGLPCGLDMKVNKCPSPPSYIPVPYSGNTNIMTFPQRVINMAMTVVESYQCSLLYGHYDEMVSKYVGNNMDYRTLLSHGALWLIRNEFTLDWPRPLLPNMVLIGGINCAEKKKNASLPADLEEFVQGSGDDGFIIFTLGSMLPDMPQEKAQHFLDAFRQIPQRVVWRYAGDPPKGLPKNVRLMKWLPQKELLAHPKAKLFLTHGGSH... | Function: UDPGT is of major importance in the conjugation and subsequent elimination of potentially toxic xenobiotics and endogenous compounds.
Catalytic Activity: glucuronate acceptor + UDP-alpha-D-glucuronate = acceptor beta-D-glucuronoside + H(+) + UDP
Location Topology: Single-pass membrane protein
Sequence Mass (D... |
Q10941 | MRLIFVLLATFVNAAFSYKILVFSPATSKSHLISNGRLADELARAGHDVTVLELDFLGISQTTNSVKVAKKRIIDGFQESTNFKNVLHGFSETVMEEPSFTDEIKGWWAYQNVYNDLCAEFLKMDDIFNELKNAKFDGFFAEQINLCGFGYAHALEIPRHFLISSCPFAAPVYDFTGLPMPTSTVAFAADLSISPTYTERARNLFVAVLTKLEFTLLNNRLQAHFQHKFGEHFPSLYSVTSDVDVIFVATDEIIDISTTTLQNIVHVGGLGVDDDVAEMDNVFASEMSKGKEGVIYFSLGTIANTTKIDSKVMRTVLDIV... | Catalytic Activity: glucuronate acceptor + UDP-alpha-D-glucuronate = acceptor beta-D-glucuronoside + H(+) + UDP
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 60204
Sequence Length: 531
Subcellular Location: Membrane
EC: 2.4.1.17
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P0CE45 | MNQQLSWRTIVGYSLGDVANNFAFAMGALFLLSYYTDVAGVGAAAAGTMLLLVRVFDAFADVFAGRVVDSVNTRWGKFRPFLLFGTAPLMIFSVLVFWVPTDWSHGSKVVYAYLTYMGLGLCYSLVNIPYGSLATAMTQQPQSRARLGAARGIAASLTFVCLAFLIGPSIKNSSPEEMVSVYHFWTIVLAIAGMVLYFICFKSTRENVVRIVAQPSLNISLQTLKRNRPLFMLCIGALCVLISTFAVSASSLFYVRYVLNDTGLFTVLVLVQNLVGTVASAPLVPGMVARIGKKNTFLIGALLGTCGYLLFFWVSVWSLP... | Function: Responsible for the transport of glucuronide into the cell energized by the proton motive force (probably by symport). Import is enhanced by UidC (GusC, AC Q47706).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 49892
Sequence Length: 457
Subcellular Location: Cell inner membrane
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Q96RL1 | MPRRKKKVKEVSESRNLEKKDVETTSSVSVKRKRRLEDAFIVISDSDGEEPKEENGLQKTKTKQSNRAKCLAKRKIAQMTEEEQFALALKMSEQEAREVNSQEEEEEELLRKAIAESLNSCRPSDASATRSRPLATGPSSQSHQEKTTDSGLTEGIWQLVPPSLFKGSHISQGNEAEEREEPWDHTEKTEEEPVSGSSGSWDQSSQPVFENVNVKSFDRCTGHSAEHTQCGKPQESTGRGSAFLKAVQGSGDTSRHCLPTLADAKGLQDTGGTVNYFWGIPFCPDGVDPNQYTKVILCQLEVYQKSLKMAQRQLLNKKGF... | Function: Ubiquitin-binding protein . Specifically recognizes and binds 'Lys-63'-linked ubiquitin . Plays a central role in the BRCA1-A complex by specifically binding 'Lys-63'-linked ubiquitinated histones H2A and H2AX at DNA lesions sites, leading to target the BRCA1-BARD1 heterodimer to sites of DNA damage at double... |
P16788 | MSSALRSRARSASLGTTTQGWDPPPLRRPSRARRRQWMREAAQAAAQAAVQAAQAAAAQVAQAHVDENEVVDLMADEAGGGVTTLTTLSSVSTTTVLGHATFSACVRSDVMRDGEKEDAASDKENLRRPVVPSTSSRGSAASGDGYHGLRCRETSAMWSFEYDRDGDVTSVRRALFTGGSDPSDSVSGVRGGRKRPLRPPLVSLARTPLCRRRVGGVDAVLEENDVELRAESQDSAVASGPGRIPQPLSGSSGEESATAVEADSTSHDDVHCTCSNDQIITTSIRGLTCDPRMFLRLTHPELCELSISYLLVYVPKEDDF... | Function: Serine/threonine protein kinase that plays important roles in several processes including nuclear viral egress, viral replication or regulation of host cell cycle progression . Participates in the acquisition of tegument during virion morphogenesis in the nucleus. Phosphorylates the viral nuclear egress compl... |
D3XDS2 | MSVELTPPRSDGSVGFAPVVVPPAPRKPLRRRAVSDLEKLYKVKRRLVFGADDGAVDNDTSNNNSGSSSTTSRSRRKTAADVVSDSPKRTDDSSTAGEDGYTHCVHSCACTPGERHLLCCELVSIGDSVSVARCPLCSLGISTTYLSRGCCRGRSKVTGGDEDEEDEDEEENSQDEDRDEEEAASASSSGGLEWSDDSNSALSWSDENIIISPFPGLKCYVTTFEDIRQPVLLETGSAYLPVYVPYDESFCRNRCLERGGDDDDERDATLIGKGSFGQVWRLSDKKTALKAAASESINETLLTVWISGVVRSRAQDAGYR... | Function: Serine/threonine protein kinase that plays important roles in several processes including viral morphogenesis, nuclear viral egress, viral replication or regulation of host cell cycle progression . Participates in the acquisition of tegument during virion morphogenesis in the nucleus (By similarity). Phosphor... |
Q13564 | MAQLGKLLKEQKYDRQLRLWGDHGQEALESAHVCLINATATGTEILKNLVLPGIGSFTIIDGNQVSGEDAGNNFFLQRSSIGKNRAEAAMEFLQELNSDVSGSFVEESPENLLDNDPSFFCRFTVVVATQLPESTSLRLADVLWNSQIPLLICRTYGLVGYMRIIIKEHPVIESHPDNALEDLRLDKPFPELREHFQSYDLDHMEKKDHSHTPWIVIIAKYLAQWYSETNGRIPKTYKEKEDFRDLIRQGILKNENGAPEDEENFEEAIKNVNTALNTTQIPSSIEDIFNDDRCINITKQTPSFWILARALKEFVAKEGQ... | Function: Regulatory subunit of the dimeric UBA3-NAE1 E1 enzyme. E1 activates NEDD8 by first adenylating its C-terminal glycine residue with ATP, thereafter linking this residue to the side chain of the catalytic cysteine, yielding a NEDD8-UBA3 thioester and free AMP. E1 finally transfers NEDD8 to the catalytic cystein... |
Q9UT93 | MGTSAKMQKYDRQVRLWKAEGQNAIEKSHVCLLYANTVGCEALKNLILPGIGSFAVVDDTSVDFSMDGMNFFIQYDQEGKSRARCTASLLQQLNPNVEMEYLEMSPEALIDKNIEYFSKFSVVLSSNLKEKPLFRLEEYLRSHKIPLLHFNSVGFAGILRISTHEYTTTQSQPELPQDLRLKNPWPELINYVKSMDLDNMDSSSLSEIPYIVLIIHVLLKVSPAHAQNSQEADDCAMFRKIMEEYKGKCDSENIEEASSNSWKAFKEYKLPSNVYEVLHDTRCVKIQEDSESFWIMAHCLKMFYDETEFLPLSGLLPDMN... | Function: Regulatory subunit of the dimeric uba3-ula1 E1 enzyme. E1 activates NEDD8/ubl1 by first adenylating its C-terminal glycine residue with ATP, thereafter linking this residue to the side chain of the catalytic cysteine, yielding a NEDD8-UBA3 thioester and free AMP. E1 finally transfers NEDD8 to the catalytic cy... |
Q83IJ0 | MSKVKSITRESWILSTFPEWGSWLNEEIEQEQVAPGTFAMWWLGCTGIWLKSEGGTNVCVDFWCGTGKQSHGNPLMKQGHQMQRMAGVKKLQPNLRTTPFVLDPFAIRQIDAVLATHDHNDHIDVNVAAAVMQNCADDVPFIGPKTCVDLWIGWGVPKERCIVVKPGDVVKVKDIEIHALDAFDRTALITLPADQKAAGVLPDGMDDRAVNYLFKTPGGSLYHSGDSHYSNYYAKHGNEHQIDVALGSYGENPRGITDKMTSADMLRMGEALNAKVVIPFHHDIWSNFQADPQEIRVLWEIKKDRLKYGFKPFIWQVGGK... | Function: Probably catalyzes the hydrolysis of L-ascorbate-6-P into 3-keto-L-gulonate-6-P. Is essential for L-ascorbate utilization under anaerobic conditions.
Catalytic Activity: H2O + L-ascorbate 6-phosphate = 3-dehydro-L-gulonate 6-phosphate
Sequence Mass (Da): 40043
Sequence Length: 354
Pathway: Cofactor degradatio... |
P34579 | MASNRFQNLQNWTNKHVFSNSLDYWNQELNEVPSYQNQPQTGESGSNPPPHDRLEPIQESVVSEQPQKDDINKQEEAKDDGHGEASEPISALQAAWNVTNAIQGMFIVGLPIAVKVGGWWSIGAMVGVAYVCYWTGVLLIECLYENGVKKRKTYREIADFYKPGFGKWVLAAQLTELLSTCIIYLVLAADLLQSCFPSVDKAGWMMITSASLLTCSFLDDLQIVSRLSFFNAISHLIVNLIMVLYCLSFVSQWSFSTITFSLNINTLPTIVGMVVFGYTSHIFLPNLEGNMKNPAQFNVMLKWSHIAAAVFKVVFGMLGF... | Function: Involved in the uptake of GABA into the synaptic vesicles.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 54439
Sequence Length: 486
Subcellular Location: Cytoplasmic vesicle membrane
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Q10045 | MSSQPRGSGTQPGPSQSPISQRNFRYEPARSGYTSPGQYSTYSTSTADRVGCLTAVRMSAFAKLSRFTRRLVHIRQMDFEFALWQMLYLLIQPSKVYKNFIYRKRTKDQFARDDPAFLVLLALSLLFSSIFYAYALGLEKIGFFTFFLWSVFVDCIGVGVVIATVLWWVSNRFLRKVRDQDVEWGYCFDVHLNAFFPMLILLHVIVPILYPTLIDSPAFLSILLGNTFWFLAACYYVYITFLGYTALPILHKTQYFLYPISFIFMFFVATLTGGWNISRTALNFYHSRAEPHKFAPQHGGL | Function: Required for cell surface expression of acetylcholine receptors in body-wall muscles.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 34739
Sequence Length: 301
Subcellular Location: Golgi apparatus membrane
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Q7ZUU1 | MLPTSSPQIHRNGSLSERDAARHTAGAKRYKYLRRLLHFRQMDFEFAVWQMLYLFTSPQKVYRNFHYRKQTKDQWARDDPAFLVLLSIWLCVSTVGFGLVLDMGFVETLTLLLWVVFIDCIGVGLLISTLMWFVTNKYLMKHPNRDYDVEWGYAFDVHLNAFYPLLVILHFLQLFFINHVVVISSDWFLGYFVGNTMWLIAIGYYVYITFLGYSALPFLKNTVVLLYPFALLGLLYVLSISLGWNFTKGLCWFYKHRVQ | Function: Involved in the cell surface expression of neuronal nicotinic receptors (By similarity). Binds RNA (By similarity).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 30554
Sequence Length: 259
Subcellular Location: Nucleus inner membrane
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Q9VHN5 | MTQYSHVKYTQSPTPSVVSGYSSASRLHSPLPPPANHRRDCLSATTKSYKYLRRLLKFNQMDFEFALWQMLYLFVAPQKVYRNFNYRKQTKSQFARDDPAFLVLLVVCLCVTSLGFAYVLGLSFWQSISFIFYVVFVDCIFVGIIIASFFWAVTNRYLRTNSLEPDIEWGYAFDVHLNAFFPPLMLLHFIQLFFYNWLISQTWFISRFLGNTFWLMGMGYYVYITFLGYNCIPHLKNTRIILIALPIIFLLFLVVTIIGWNATISFVNFYKYRVY | Function: Required for cell surface expression of acetylcholine receptors.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 32472
Sequence Length: 275
Subcellular Location: Golgi apparatus membrane
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Q53HI1 | MLPSTSVNSLVQGNGVLNSRDAARHTAGAKRYKYLRRLFRFRQMDFEFAAWQMLYLFTSPQRVYRNFHYRKQTKDQWARDDPAFLVLLSIWLCVSTIGFGFVLDMGFFETIKLLLWVVLIDCVGVGLLIATLMWFISNKYLVKRQSRDYDVEWGYAFDVHLNAFYPLLVILHFIQLFFINHVILTDTFIGYLVGNTLWLVAVGYYIYVTFLGYSALPFLKNTVILLYPFAPLILLYGLSLALGWNFTHTLCSFYKYRVK | Function: Involved in the cell surface expression of neuronal nicotinic receptors (By similarity). Binds RNA (By similarity).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 30373
Sequence Length: 259
Subcellular Location: Nucleus inner membrane
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Q23023 | MEQFDGFEYSKRDLLGHGAFAIVYRGRYVDRTDVPVAIKAIAKKNISKSKNLLTKEIKILKELSSLKHENLVGLLKCTETPTHVYLVMEFCNGGDLADYLQQKTTLNEDTIQHFVVQIAHALEAINKKGIVHRDLKPQNILLCNNSRTQNPHFTDIVIKLADFGFARFLNDGVMAATLCGSPMYMAPEVIMSMQYDAKADLWSIGTILFQCLTGKAPFVAQTPPQLKAYYEKTRELRPNIPEWCSPNLRDLLLRLLKRNAKDRISFEDFFNHPFLTSPLLPSPSKRILESARSPLLANRRIITPQSSLPVPKRAGSTKLD... | Function: Protein kinase important for axonal elongation and axonal guidance . Functions in the CAN axons to direct both anterior and posterior migrations . Phosphorylates both unc-14 and vab-8 . Component of the unc-51/atg-13 complex that is probably recruited by lgg-1 to preautophagosomes and is required for autophag... |
Q182G9 | MVNLGNDWDELLKEEFEKDYYLNLRKFLIEEYKTRQIFPNMHNIYEALKHTSYKDTKVLILGQDPYHGDNQAHGLAFSVQPQVKTPPSLLNMYKELKDDLGCFIPNNGYLMPWADQGVLLLNTALTVRAHEANSHKNKGWEIFTDRVISILSEREDPVIFVLWGSNARKKVELIDTSKHYILEAPHPSPLSASKGFFGCKHFSKINEILKKLGKEPINWQIENI | Function: Excises uracil residues from the DNA which can arise as a result of misincorporation of dUMP residues by DNA polymerase or due to deamination of cytosine.
Catalytic Activity: Hydrolyzes single-stranded DNA or mismatched double-stranded DNA and polynucleotides, releasing free uracil.
Sequence Mass (Da): 25941
... |
Q8FPQ4 | MPVDEQPTTPEAVQWRTIEDLPIHPSWRKVLEPVMDQIRDLGQFLTAETQAGRGFLPPEPDIFRAFSYPFEEVKVLILGQDPYPTPGHSMGLCFSTQPGVRPLPRSLVNIFKEMATDLGVSINATDGDLRPWSRQGVMLLNRVLTVQPGNSNSHKGRGWEAVTEAAITALGQRDQPLVAILWGRQAQAVQKFLGDTPCITSAHPSPLSASRGFFGSRPFSTTNRMLDDLGATPVDWRL | Function: Excises uracil residues from the DNA which can arise as a result of misincorporation of dUMP residues by DNA polymerase or due to deamination of cytosine.
Catalytic Activity: Hydrolyzes single-stranded DNA or mismatched double-stranded DNA and polynucleotides, releasing free uracil.
Sequence Mass (Da): 26326
... |
Q8NQU9 | MEKLLMTNTLWNSVDELPIHDSWKPVLKPVEDAIRKLGVFLAEEEFLPPVDDVFRAFSYPFDAVKVLIMGQDPYPTPGHAMGLSFSTQPDVRPLPRSLNNIFKELVSDVGSLGDSASEQGALDLGINAPGSVAGTQVALPADGDLRAWSNQGVALFNRVLTVHPGQAGSHKGKGWEAVTEQAIKALAERDQPLVAILWGKQAQEVQKFLGDTPCICSVHPSPLSASRGFFGSKPFSRANEILSSLGATEIDWSL | Function: Excises uracil residues from the DNA which can arise as a result of misincorporation of dUMP residues by DNA polymerase or due to deamination of cytosine.
Catalytic Activity: Hydrolyzes single-stranded DNA or mismatched double-stranded DNA and polynucleotides, releasing free uracil.
Sequence Mass (Da): 27443
... |
Q83CW4 | MTTMAETQTWQTVLGEEKQEPYFQEILDFVKKERKAGKIIYPPQKDIFNALKLTPYEAIKVVILGQDPYHGPNQAHGLAFSVRPGVPAPPSLQNIFKELHADLGVSIPSHGFLEKWAKQGVLLLNAALTVEAGKPQSHANIGWHRFTDKVIESLNDHPEGIVFLLWGSYAQKKSQLITNLRHRILKAPHPSPLSAARGFLGCRHFSKANQLLHEMGRGEIDWALDEKVS | Function: Excises uracil residues from the DNA which can arise as a result of misincorporation of dUMP residues by DNA polymerase or due to deamination of cytosine.
Catalytic Activity: Hydrolyzes single-stranded DNA or mismatched double-stranded DNA and polynucleotides, releasing free uracil.
Sequence Mass (Da): 25667
... |
C1CXS7 | MSDQPDLFGTPTGAKAPHAIMPAGLPASWKEALAEEFAAPYFHALKDFLVEERRTHTVYPPAADVFNALRYTPLENVKVMILGQDPYHGPGQAHGLSFSVRPGVRIPPSLKNIYKELQSDIPGFTPPRHGYLKAWAEQGVLLLNAVLTVRAGEANSHAGKGWESFTDAVIRAVNNRPQRVVFVLWGAYARKKARLITAPHHVIIESAHPSPLSVTRFMGTRPFSRVNAALEEAGEAPIDWQLPAQVEE | Function: Excises uracil residues from the DNA which can arise as a result of misincorporation of dUMP residues by DNA polymerase or due to deamination of cytosine.
Catalytic Activity: Hydrolyzes single-stranded DNA or mismatched double-stranded DNA and polynucleotides, releasing free uracil.
Sequence Mass (Da): 27279
... |
Q9RWH9 | MTDQPDLFGLAPDAPRPIIPANLPEDWQEALLPEFSAPYFHELTDFLRQERKEYTIYPPAPDVFNALRYTPLGEVKVLILGQDPYHGPNQAHGLSFSVRPGVRVPPSLRNIYKELTEDIPGFVAPKHGYLRSWAEQGVLLLNAVLTVRAGQANSHQGKGWEHFTDAVIKAVNAKEERVVFILWGSYARKKKKLITGKNHVVIESGHPSPLSEQYFFGTRPFSKTNEALEKAGRGPVEWQLPATVTEE | Function: Excises uracil residues from the DNA which can arise as a result of misincorporation of dUMP residues by DNA polymerase or due to deamination of cytosine.
Catalytic Activity: Hydrolyzes single-stranded DNA or mismatched double-stranded DNA and polynucleotides, releasing free uracil.
Sequence Mass (Da): 27746
... |
P53766 | MSGKITDFFEKKTTTTIDEAENKDNDKELTSTTTTTTTTSTTSKKKVAAAPKKKAAVASKKRKHESSDEETDKEEQQNDDDDDGEEKVENNNNNKKLKNEEKSEEINSTITDNNYYDDIENYFTDKQWKEALSGEFGKAYFKKMITQLNKRYSSKEKPIYPPKNEIFSAFNYAHLEDVKVVIIGQDPYHGKGQAHGLSFSVKKGVSPPPSLINIYKELETDIEGFKRPLKNGFLEPWARQGVFLLNAVLTVEEATPNSHKDFGWADFTDAVLKILSKQDQPIVFILWGGFAQKKEKLFTNKNHLVLKSGHPSPLSIKHFI... | Function: Excises uracil residues from the DNA which can arise as a result of misincorporation of dUMP residues by DNA polymerase or due to deamination of cytosine.
Catalytic Activity: Hydrolyzes single-stranded DNA or mismatched double-stranded DNA and polynucleotides, releasing free uracil.
Sequence Mass (Da): 39374
... |
P12888 | MASRGLDLWLDEHVWKRKQEIGVKGENLLLPDLWLDFLQLSPIFQRKLAAVIACVRRLRTQATVYPEEDMCMAWARFCDPSDIKVVILGQDPYHGGQANGLAFSVAYGFPVPPSLRNIYAELHRSLPEFSPPDHGCLDAWASQGVLLLNTILTVQKGKPGSHADIGWAWFTDHVISLLSERLKACVFMLWGAKAGDKASLINSKKHLVLTSQHPSPLAQNSTRKSAQQKFLGNNHFVLANNFLREKGLGEIDWRL | Function: Excises uracil residues from the DNA which can arise as a result of misincorporation of dUMP residues by DNA polymerase or deamination of cytosines. Therefore may reduce deleterious uracil incorporation into the viral genome, particularly in terminally differentiated cells which lack DNA repair enzymes.
Catal... |
Q1GHJ4 | MAPQDHASALRPAVGGWAELPFFETHWPRIEAALAQETRQILPPAHQRFAALERTPPESTRVVILGQDPYPTPGHAHGLSFSVEPDVTPLPRSLRNIYQEMRDDLGTCPETGDLRPWAAQGVLLLNTVLSVPAGEANGHKSLGWQELAHQVLDLSSRRPTAYVLWGNQAQKLESHIRPGDHLIVKTAHPSPLSARRGFFGSRVFSAINDWLTARGEPPITWADPRPAQGSIFDV | Function: Excises uracil residues from the DNA which can arise as a result of misincorporation of dUMP residues by DNA polymerase or due to deamination of cytosine.
Catalytic Activity: Hydrolyzes single-stranded DNA or mismatched double-stranded DNA and polynucleotides, releasing free uracil.
Sequence Mass (Da): 25792
... |
O74834 | MTVLNTTDKRKADDTVNKLDGKLKQPRLDNFFKTNTSSPALKDTQVLDNKENNSVSKFNKEKWAENLTPAQRKLLQLEIDTLESSWFDALKDEFLKPYFLNLKEFLMKEWQSQRVFPPKEDIYSWSHHTPLHKTKVILLGQDPYHNIGQAHGLCFSVRPGIPCPPSLVNIYKAIKIDYPDFVIPKTGYLVPWADQGILMLNASLTVRAHQAASHSGKGWETFTSAVLQVALNRNRKGLVILAWGTPAAKRLQGLPLKAHYVLRSVHPSPLSAHRGFFECHHFKKTNEWLEEQYGPEKCINWSAVSEQKAKIKSSELESSS... | Function: Excises uracil residues from the DNA which can arise as a result of misincorporation of dUMP residues by DNA polymerase or due to deamination of cytosine.
Catalytic Activity: Hydrolyzes single-stranded DNA or mismatched double-stranded DNA and polynucleotides, releasing free uracil.
Sequence Mass (Da): 36705
... |
P38572 | MASAAAATTEKGSPVVVGLLVMGNIIILLSGLALFAETVWVTADQYRIYPLMGVSGKDDVFAGAWIAIFCGFSFFVVASFGVGAALCRRRSMILTYLILMLIIYIFECASCITSYTHRDYMVSNPSLITKQMLTFYSADSNQGRELTRLWDRIMIEQECCGTSGPMDWVNFTSAFRATTPEVVFPWPPLCCRRTGNFIPVNEEGCRLGHLDYLFTKGCFEHIGHAIDSYTWGISWFGFAILMWTLPVMLIAMYFYTTL | Function: Component of the asymmetric unit membrane (AUM); a highly specialized biomembrane elaborated by terminally differentiated urothelial cells. May play an important role in normal bladder epithelial physiology, possibly in regulating membrane permeability of superficial umbrella cells or in stabilizing the apica... |
O00322 | MASAAAAEAEKGSPVVVGLLVVGNIIILLSGLSLFAETIWVTADQYRVYPLMGVSGKDDVFAGAWIAIFCGFSFFMVASFGVGAALCRRRSMVLTYLVLMLIVYIFECASCITSYTHRDYMVSNPSLITKQMLTFYSADTDQGQELTRLWDRVMIEQECCGTSGPMDWVNFTSAFRAATPEVVFPWPPLCCRRTGNFIPLNEEGCRLGHMDYLFTKGCFEHIGHAIDSYTWGISWFGFAILMWTLPVMLIAMYFYTML | Function: Component of the asymmetric unit membrane (AUM); a highly specialized biomembrane elaborated by terminally differentiated urothelial cells. May play an important role in normal bladder epithelial physiology, possibly in regulating membrane permeability of superficial umbrella cells or in stabilizing the apica... |
P38573 | MAKDDSTVRCFQGLLIFGNVIIGMCSIALMAECIFFVSDQNSLYPLLEATNNDDIYAAAWIGMFVGICLFCLSVLGIVGIMKSNRKILLVYFILMFIVYAFEVASCITAATQRDFFTPNLFLKQMLERYQNNSPPNNDDQWKNNGVTKTWDRLMLQDNCCGVNGPSDWQKYTSAFRTENSDADYPWPRQCCVMNSLKEPLNLDACKLGVPGYYHSQGCYELISGPMNRHAWGVAWFGFAILCWTFWVLLGTMFYWSRIDY | Function: Component of the asymmetric unit membrane (AUM); a highly specialized biomembrane elaborated by terminally differentiated urothelial cells. May play an important role in normal bladder epithelial physiology, possibly in regulating membrane permeability of superficial umbrella cells or in stabilizing the apica... |
O75841 | MAKDNSTVRCFQGLLIFGNVIIGCCGIALTAECIFFVSDQHSLYPLLEATDNDDIYGAAWIGIFVGICLFCLSVLGIVGIMKSSRKILLAYFILMFIVYAFEVASCITAATQQDFFTPNLFLKQMLERYQNNSPPNNDDQWKNNGVTKTWDRLMLQDNCCGVNGPSDWQKYTSAFRTENNDADYPWPRQCCVMNNLKEPLNLEACKLGVPGFYHNQGCYELISGPMNRHAWGVAWFGFAILCWTFWVLLGTMFYWSRIEY | Function: Component of the asymmetric unit membrane (AUM); a highly specialized biomembrane elaborated by terminally differentiated urothelial cells. May play an important role in normal bladder epithelial physiology, possibly in regulating membrane permeability of superficial umbrella cells or in stabilizing the apica... |
P60936 | MSYLHAIILGIVEGITEFLPISSTGHMIIASSMMGIEDSSFTKAFEVIIQFGAIMSVLVLYWKRFLPHWGFYRKLFVAFLPTAIIGFVVKDVVEHLMGSVQVVAWSLIIGGVILIWADKAFAHLTMMGRKTDDLTYKDSVKLGLFQAIAMIPGVSRSGATIMGGLTLGMNKKEAAEFSFFLAVPTMAAATLYKLLKIYKTIEPAQINLLLVGCAVAFVVAMIAIKFFIGIVSRYGFRGFGYYRIVLGLVILILLYTGHDLQMV | Function: Catalyzes the dephosphorylation of undecaprenyl diphosphate (UPP). Confers resistance to bacitracin.
Catalytic Activity: di-trans,octa-cis-undecaprenyl diphosphate + H2O = di-trans,octa-cis-undecaprenyl phosphate + H(+) + phosphate
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 28996
Seque... |
A1A1M3 | MNFFQAIFLGLVQALTEYLPVSSSAHIRIIGDLMLGSDPGAAFTAIIQIGTELAVILYFRHDIIRILGAWFGSLFGKEGKDFKSRMGAHNRDTQMGWFIIIGTLPILIAGLLFKDAIESTLRNLWITVTVLIIFGILLWVVDARAKQVKTMDEMTWKDALIFGIGQMLALIPGVSRSGGTITFGRAMGYTREAAVRVSFLMAIPAVFGAGILEAVSAVKDVAAGNAGMFPGWGATIAATIVAFVVGYVVIIGFLKFVSTFSYKAFAIYRIALAVVVALLLICGVLHPTEVVAAA | Function: Catalyzes the dephosphorylation of undecaprenyl diphosphate (UPP). Confers resistance to bacitracin.
Catalytic Activity: di-trans,octa-cis-undecaprenyl diphosphate + H2O = di-trans,octa-cis-undecaprenyl phosphate + H(+) + phosphate
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 31596
Seque... |
Q493X5 | MSMIYITLNIIAYVIDVRSLILDVRRLVFSLILGIVEGLTEFLPISSTGHMILVENILNCMDDSVIAFTVIIQLGAILSITKIFWSQLYGMSMICIKKIFFKQHDDHNHLCIRHIFLGTFPGIMLGMIFYEKIGLIFELTYIMYGLIIGGIFLLVGELCASKEPRVSRINNITYLQAFLIGCFQCLAFWPGFSRAGATIGGGLVVGLDRRISSEFSFFLAVPIIFGSAVLTLYHYRSCIGLMDVLLLIAGSATAFFIALFTVRYFLKIVKNVSLIPFAIYRFLLAGGIYWGLMT | Function: Catalyzes the dephosphorylation of undecaprenyl diphosphate (UPP). Confers resistance to bacitracin.
Catalytic Activity: di-trans,octa-cis-undecaprenyl diphosphate + H2O = di-trans,octa-cis-undecaprenyl phosphate + H(+) + phosphate
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 32957
Seque... |
Q2KX31 | MTDSTLYFVKAFFLGIIEGLTEFIPVSSTGHLILFGDWINFESGSGKVFEVVIQLGAILAVMWIFRARLWQLIRGTLSGQRQEMLFTRNLLLAFFPAAIIGAIFIKAIKQTFYHPGVVAVTLVLGGLIMLWVERRAPRSDGSASETATEERATAHSLEEISWKQALGVGVAQCLAMIPGTSRSGATIIGGMVAGIQRKTATEFSFFLAMPTMLGAAVYDMYRNIDLLTSHDLGAIAVGFVAAFLSALLVVRAVLRFVANHTYRGFAWYRIALGVVVAAWLAF | Function: Catalyzes the dephosphorylation of undecaprenyl diphosphate (UPP). Confers resistance to bacitracin.
Catalytic Activity: di-trans,octa-cis-undecaprenyl diphosphate + H2O = di-trans,octa-cis-undecaprenyl phosphate + H(+) + phosphate
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 30791
Seque... |
O51273 | MTNILSAIILGIIQGITEFLPISSSGHLLLFRHFINLKLSIIFDIYLHLATVLVIIIYYRKRILELFLTFIRFSLRKTVKSDLTNLKLILLILIITIVTGVVGTFISKYESMFTLSFVLINFIITGILILMLEFNFLKVDFKGNILLAGIFMGLMQGLGALPGISRSGITIFSASVIGFNRKSAFEISFLSLIPIVFGAILLKHKEFYDIFMVLNFFEINLGALVAFVVGIFSINFFFKMLNNKKLYYFSIYLFALSIIVCYFVRI | Function: Catalyzes the dephosphorylation of undecaprenyl diphosphate (UPP). Confers resistance to bacitracin.
Catalytic Activity: di-trans,octa-cis-undecaprenyl diphosphate + H2O = di-trans,octa-cis-undecaprenyl phosphate + H(+) + phosphate
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 30271
Seque... |
P62465 | MNPYLNAFLRSIIEAITEFLPVSSTGHLFLFSSFFPFYGENVEFDDLFDIFIQSGAILSVLFLYREKFKSQIVSSFRYILKQNSDSEGFHFLIQICIGAFPILIAGFIAKKFLDTIKARPDLLEILSGAWIFGGVLILVAEWYFHQRPEEKKSIGFKDSILIGIFQCMALIPGMSRSAATIITARFLGKDTKSSAEFSFFLAVPVLLAAGIYKLIKYRSILNGNTIPVLMFGFLVSFLLCTLVIRWFLRYIQKHSFSVFGVYRILLGVGVLVLTKLI | Function: Catalyzes the dephosphorylation of undecaprenyl diphosphate (UPP). Confers resistance to bacitracin.
Catalytic Activity: di-trans,octa-cis-undecaprenyl diphosphate + H2O = di-trans,octa-cis-undecaprenyl phosphate + H(+) + phosphate
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 31374
Seque... |
Q03ZT9 | MFDLIKAIIIGIIEGLTEFLPVSSTGHIILAEALMKIPSGNVWTKAFSSVFDYSIQLGAIFAVIQLYFDKLNPFSSKKTDHEKFQTWRLWIRVIVGVLPAIVFGFALNDFMDAHLMNFWVVSATLIIYGIAFIVIENRQKSIVPVITNVNQITFKLALYIGLFQVLSIVPGTSRSGATILGAIILGASRFVAAEFSFFLSIPVMFGVTFLKMGSFFRDGGSFTGMQSIVMLVGFIVSWIVAWFAIKFMMNYIKNNDFKVFGYYRIIIGAIFLVFGILGIVG | Function: Catalyzes the dephosphorylation of undecaprenyl diphosphate (UPP). Confers resistance to bacitracin.
Catalytic Activity: di-trans,octa-cis-undecaprenyl diphosphate + H2O = di-trans,octa-cis-undecaprenyl phosphate + H(+) + phosphate
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 31301
Seque... |
A0L9F4 | MDLFNAAILALIQGITEFLPISSSGHLILTPYLLGWQDQGLVFDIAANSGSLAAVMLYFRREVGQMLRGGWRLLCAPRAWRQANAESHLVLQLALATIPVGLVGLACKDWVATVARDPMIIATTSILFGLLLWWADRQGRCNNDGSALSWRQVGIIGIAQAFALIPGTSRSGVTMTAGLMLGLTREAAARFSFLMAIPVGILAALLDLKDLFAHPMQGDELYFLGVGFCVSGLSAYMVIHGLLAWLKRQTMTPFVVYRVVLGVVIFATLG | Function: Catalyzes the dephosphorylation of undecaprenyl diphosphate (UPP). Confers resistance to bacitracin.
Catalytic Activity: di-trans,octa-cis-undecaprenyl diphosphate + H2O = di-trans,octa-cis-undecaprenyl phosphate + H(+) + phosphate
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 29193
Seque... |
Q0ATH6 | MSLIYLVVLALVQGITEFLPISSSAHLILAPQVLGQADQGPLIDVMAHAGSLLAVLVYFRSDIVSVAMGKLALLQGRVTPGGRLALLVAASMPPIIIVAGALVAFDLVDALRSPRVIAIATLAFALPLWLADRYGRQTITIETMSFKHAALIGIAQLFALIPGASRSGVTMTAARGLGLTRTDSARFSMLMAIPVIAAFGLVSLIELVRADGMAAGASLSDGLIVAGLSFVTAWAAIAVLMRLVERIGFLPFALYRVGLGLALLVFFV | Function: Catalyzes the dephosphorylation of undecaprenyl diphosphate (UPP). Confers resistance to bacitracin.
Catalytic Activity: di-trans,octa-cis-undecaprenyl diphosphate + H2O = di-trans,octa-cis-undecaprenyl phosphate + H(+) + phosphate
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 28004
Seque... |
Q12UC1 | MLSLSEAIILGIVQGLAEWLPISSEGMTSLVMVTFFGRSLSEAIPISIWLHLGTLLAAIVYFREDVKVLLYGVPDYVRSFSRKQPHDPVISFLLISTALTGIVGLPLLLFVTDNVEISGGSATAVIGIMLIVTGILQRTVSRDESLSRVPGMSDSLVSGVAQGFAAIPGISRSGITMSALLLRKFDAADAIRLSFLMSIPAVLVAEIGVGLMGMVELDINSIVGLFFAFAFGLVTIDLFLKVAKKVDFSYFCIGLGVLSVLTMFL | Function: Catalyzes the dephosphorylation of undecaprenyl diphosphate (UPP).
Catalytic Activity: di-trans,octa-cis-undecaprenyl diphosphate + H2O = di-trans,octa-cis-undecaprenyl phosphate + H(+) + phosphate
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 28295
Sequence Length: 265
Subcellular Locati... |
B3E171 | MHDLWPTILLGIIEGLSEFLPISSTGHLLVAEHWLGERSETFNIFIQLGAVLAVCLIYKERLSSFLFLWKDREKLPYFLKLSVAFIITSILGLWVKKMGWELPKDLGPVIIAIFGGAFWIYFTEKVSSQRQSFVEEISWPTAIAVGASQVVAGVLPGFSRSAATILMAVLLGVSRPAATEFAFLLGIPTMFAASLFAWIEETHFLKNPSLDSPLTLATGFCVSAVVAFISVKWLLSYIQTHTFIPFVWYRVGLGFFLIALVALGWKTQ | Function: Catalyzes the dephosphorylation of undecaprenyl diphosphate (UPP). Confers resistance to bacitracin.
Catalytic Activity: di-trans,octa-cis-undecaprenyl diphosphate + H2O = di-trans,octa-cis-undecaprenyl phosphate + H(+) + phosphate
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 29824
Seque... |
Q8TW25 | MREIELWTAVLAGVVQGITEWLPISSEGQATMTMMKVLGIPPSTAMDLALWLHAGTLLAVLLRFGVPYWLTVRDLLMGGPWRRLGLFAIVATVCTAVVGLPVYKVLKGIFSAATGDAVQMAIGGALIVTGLLLRISPEGLRDRREVNVVDAVIVGLGQGFSVIPGISRSGTTMALLLWRRFDGGEAVWLSFYLAGPAMLGATALELKEGLSAATKMGTSWMVTAIGVSFVVSLICMEVLLRVARRLDFSKVCLLLGGIALLVPLAAKML | Function: Catalyzes the dephosphorylation of undecaprenyl diphosphate (UPP).
Catalytic Activity: di-trans,octa-cis-undecaprenyl diphosphate + H2O = di-trans,octa-cis-undecaprenyl phosphate + H(+) + phosphate
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 28622
Sequence Length: 269
Subcellular Locati... |
Q8CWZ1 | MLFFEIIKAIIFGIVEGITEWLPISSTGHLILVEEFIHFNNANAAFTNMFNVVIQLGAILAVVVIYFDRLNPFKSGKTAREVQITWQLWAKVILSALPAAVIGLIFDDWLDAHFQNFFSVALMLILYGIAFIYVERRHQGVEPQVTHLVSLPYKTAFFIGLFQVLSLIPGTSRSGATILGGILLGTSRQVATEFTFFLGIPIMFGASLVKVLKFIVSGTILTGSQLFILLVAMLVAFAVSLYVIRFLTDYVKNHDFTFFGKYRIGLGILLLFYGLMKVLFG | Function: Catalyzes the dephosphorylation of undecaprenyl diphosphate (UPP). Confers resistance to bacitracin.
Catalytic Activity: di-trans,octa-cis-undecaprenyl diphosphate + H2O = di-trans,octa-cis-undecaprenyl phosphate + H(+) + phosphate
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 31363
Seque... |
Q89E48 | MEGVTIVDHPLVQHKLTLVRDKSISTKSFRELIKEIGMLLCYEVTRDLPLADTVIETPLATMHSAKIAGKKLVFVPMLRAGTTFVDGMMDLVPTARVAHIGLYREPHSFAAVEYFFKSPSDLGERLAIVVTPVVATANTAVAAIDRLKERGAKDIRLACLIAAPEGLERLRGLHPDVPIWTAAVDEGLDENGFILPGLGDAGDRAYGTR | Cofactor: Binds 1 Mg(2+) ion per subunit. The magnesium is bound as Mg-PRPP.
Function: Catalyzes the conversion of uracil and 5-phospho-alpha-D-ribose 1-diphosphate (PRPP) to UMP and diphosphate.
Catalytic Activity: diphosphate + UMP = 5-phospho-alpha-D-ribose 1-diphosphate + uracil
Sequence Mass (Da): 22727
Sequence L... |
B4E5R5 | MKQDSRFPNLFITDHPLIQHKLTHMRDKDTSTRTFRELLREITLLMGYEITRNLPITTKRVETPLVAVDAPVIAGKKLAIVPVLRAGIGMSDGLLDLVPSARVGHIGVYRADDHRPVEYLVRLPDLEDRIFILCDPMVATGYSAVHAVDVLKRRNVPAANIMFVALVAAPEGVQVFQDAHPDVKLFVASLDSHLNEHAYIVPGLGDAGDRLFGTKN | Cofactor: Binds 1 Mg(2+) ion per subunit. The magnesium is bound as Mg-PRPP.
Function: Catalyzes the conversion of uracil and 5-phospho-alpha-D-ribose 1-diphosphate (PRPP) to UMP and diphosphate.
Catalytic Activity: diphosphate + UMP = 5-phospho-alpha-D-ribose 1-diphosphate + uracil
Sequence Mass (Da): 23945
Sequence L... |
A5IE48 | MDFNQVKVINHPLIQHKLTIMRKKETSTVKFRTLMHEVSMLLAYEVTRDLEIEYEEIETPLATMQSPVLKGKKLVFVSILRAGNGLLDGMLQLVPTARIGHIGLYRDPKTLEAVEYYFKLPEHTQDRDVIVVDPMLATGNSAIAAVKEVKALHPKSIKFLCLLASPEGISNFHGEHPDVPIFTAAIDEQLNDHGYIVPGLGDAGDRLYGTKLAH | Cofactor: Binds 1 Mg(2+) ion per subunit. The magnesium is bound as Mg-PRPP.
Function: Catalyzes the conversion of uracil and 5-phospho-alpha-D-ribose 1-diphosphate (PRPP) to UMP and diphosphate.
Catalytic Activity: diphosphate + UMP = 5-phospho-alpha-D-ribose 1-diphosphate + uracil
Sequence Mass (Da): 23893
Sequence L... |
Q03QY1 | MGKFQVLDHPLIQHKLTIIRNKDCGTRSFREVVNEISTLMAYEVSRDMPLQDKTIETPVAKMTAKELAGKKVAIVPILRAGIGMVDGILELIPAAKVGHIGMYRDEETLQPHEYFVKLPSDIGQRQVFVVDPMLATGGSAIMAIDALKKRGASNIKFVCLVSAPEGVKALREKHPDIDIYTAALDDRLNEDGYIVPGLGDAGDRLFGTK | Cofactor: Binds 1 Mg(2+) ion per subunit. The magnesium is bound as Mg-PRPP.
Function: Catalyzes the conversion of uracil and 5-phospho-alpha-D-ribose 1-diphosphate (PRPP) to UMP and diphosphate.
Catalytic Activity: diphosphate + UMP = 5-phospho-alpha-D-ribose 1-diphosphate + uracil
Sequence Mass (Da): 22911
Sequence L... |
B2FLX2 | MKIVEVRHPLVQHKIGLMRNAALSTKDFRELANELGTLLAYEATADLDTEPHTLAGWAGPVTVQRIAGAKITVVPILRAGLGMLSGVLSLIPAARVSVVGLQRDEETLQPVPYFERLTGRLEERDALILDPMLATGGTLIATIDMLKRAGARRIKGIFLVAAPEGIEAVKAVHPDVEIYTAAIDAQLNDKGYILPGLGDAGDRIFGTRVG | Cofactor: Binds 1 Mg(2+) ion per subunit. The magnesium is bound as Mg-PRPP.
Function: Catalyzes the conversion of uracil and 5-phospho-alpha-D-ribose 1-diphosphate (PRPP) to UMP and diphosphate.
Catalytic Activity: diphosphate + UMP = 5-phospho-alpha-D-ribose 1-diphosphate + uracil
Sequence Mass (Da): 22490
Sequence L... |
Q8DQI3 | MGKIEVINHPLIQHKLSILRRTDTSTKAFRELVDEIAMLMGYEVLRDLPLEDVEIETPITKTVQKQLAGKKLAIVPILRAGIGMVDGLLSLVPAAKVGHIGMYRDEETLQPVEYLVKLPEDIDQRQIFVVDPMLATGGSAILAVDSLKKRGASNIKFVCLVSAPEGVKALQEAHPDVEIFTAALDERLNEHGYIVPGLGDAGDRLFGTK | Cofactor: Binds 1 Mg(2+) ion per subunit. The magnesium is bound as Mg-PRPP.
Function: Catalyzes the conversion of uracil and 5-phospho-alpha-D-ribose 1-diphosphate (PRPP) to UMP and diphosphate.
Catalytic Activity: diphosphate + UMP = 5-phospho-alpha-D-ribose 1-diphosphate + uracil
Sequence Mass (Da): 22872
Sequence L... |
A8L7B0 | MSELERSRYATLYGPTVGDRIRLADTDLFIEVTDDLSRGPGGTATGDEAVFGGGKVIRESMGQARATRAQGAPDLVITGAVVLDHWGVVKADVGIRDGRISALGKAGNPDTMDGVHPDLVIGPGTEIIAGNGKILTAGAVDTHVHFICPQQVPEALGTGVTTLIGGGTGPAEGTKATTVTASPWNLHRMMSAMDGWPVNVALLGKGNTVSEDAMWEQLRAGAAGFKLHEDWGTTPAAIDACLRVADASGVQVALHSDTLNEAGFVEDTLAAIAGRAIHAYHTEGAGGGHAPDIITVASFANILPSSTNPTRPHTVNTLDE... | Cofactor: Binds 2 nickel ions per subunit.
PTM: Carboxylation allows a single lysine to coordinate two nickel ions.
Catalytic Activity: 2 H(+) + H2O + urea = CO2 + 2 NH4(+)
Sequence Mass (Da): 60164
Sequence Length: 575
Pathway: Nitrogen metabolism; urea degradation; CO(2) and NH(3) from urea (urease route): step 1/1.
... |
Q93PJ5 | MRLTPKELDKLMLHYAGALAKSRKERGIKLNYVESIALISMEIMELAREGNKSVAELMQQGREILKADEVMEGVASMVNEVQVEVSFPDGTKLVTIHNPIEDNGKLTPGEYILKDEDITLNANKESISIKVTHKGDRPIQVGSHFHFFEVNALLEFDRAQAFGKRLDIASGTSVRFEPGEEKNVNLIDFGGKQKIIGFNDLTNAHINKENKEQCLANAAQKHFIH | Catalytic Activity: 2 H(+) + H2O + urea = CO2 + 2 NH4(+)
Sequence Mass (Da): 25198
Sequence Length: 225
Pathway: Nitrogen metabolism; urea degradation; CO(2) and NH(3) from urea (urease route): step 1/1.
Subcellular Location: Cytoplasm
EC: 3.5.1.5
|
Q9ZMZ4 | MKLTPKELDKLMLHYAGELARKRKEKGIKLNYVEAVALISAHIMEEARAGKKTAAELMQEGRTLLKPDDVMDGVASMIHEVGIEAMFPDGTKLVTVHTPIEANGKLVPGELFLKNEDITINEGKKAVSVKVKNVGDRPVQIGSHFHFFEVNRCLDFDREKTFGKRLDIASGTAVRFEPGEEKSVELIDIGGNRRIFGFNALVDRQADNESKKIALHRAKERGFHGAKSDDNYVKTIKE | Catalytic Activity: 2 H(+) + H2O + urea = CO2 + 2 NH4(+)
Sequence Mass (Da): 26568
Sequence Length: 238
Pathway: Nitrogen metabolism; urea degradation; CO(2) and NH(3) from urea (urease route): step 1/1.
EC: 3.5.1.5
|
O86507 | MRLTPTERDRLLLFGAAELARARRARGLRLNVPEATALIADTVCEAARDGARLAQAIERARSVLGPDDVLPGVADVVTEVHVEAVFDDGSRLAVVADPVGGGGLGDDAPGALLPGHDRPEPEAALRLPVTNTATVPVSVTSHFHFFEANPRLDFDRGRAYGMRLAVPAGSSVRFGPGERVEVGLVPIGGARVAIGFAGLVDGPLDAPGAREEALRRAAACGYLGADR | Catalytic Activity: 2 H(+) + H2O + urea = CO2 + 2 NH4(+)
Sequence Mass (Da): 23636
Sequence Length: 227
Pathway: Nitrogen metabolism; urea degradation; CO(2) and NH(3) from urea (urease route): step 1/1.
Subcellular Location: Cytoplasm
EC: 3.5.1.5
|
A3DGF9 | MIPGEYIIKNEFITLNDGRRTLNIKVSNTGDRPVQVGSHYHFFEVNRYLEFDRKSAFGMRLDIPSGTAVRFEPGEEKTVQLVEIGGSREIYGLNDLTCGPLDREDLSNVFKKAKELGFKGVE | Catalytic Activity: 2 H(+) + H2O + urea = CO2 + 2 NH4(+)
Sequence Mass (Da): 13828
Sequence Length: 122
Pathway: Nitrogen metabolism; urea degradation; CO(2) and NH(3) from urea (urease route): step 1/1.
Subcellular Location: Cytoplasm
EC: 3.5.1.5
|
A1TSZ5 | MVPGELLVDDGEHPLIPCRRTVTLVVRNSADRPIQVGSHYHFAETNGALDFDRAAARGMRLNITSGTAVRFEPGQQRTVELVDFAGSRTVYGFRGDIQGPLDAGTAETAPGLPQQP | Catalytic Activity: 2 H(+) + H2O + urea = CO2 + 2 NH4(+)
Sequence Mass (Da): 12500
Sequence Length: 116
Pathway: Nitrogen metabolism; urea degradation; CO(2) and NH(3) from urea (urease route): step 1/1.
Subcellular Location: Cytoplasm
EC: 3.5.1.5
|
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