ids
stringlengths 6
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stringlengths 11
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stringlengths 108
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A8HAL1 | MGKKKVKDRSAGTDSSSETAGPSCTHIRKGTENSVLKKACLNEHWSSCQDCEQDKPEEKQILEDQTDGESPAVWMCLKCGHRGCGRSGNQHAIKHYETPRSEPHCLVLSLDVWSVWCYICDDEVQYSSTGQLAQLITNIRKQVLTAPDKRNASKKSWKEDISVMNSAEQTQDEEKGKKGKQKSSSKQEDSPKSHQSAAAGSSAVVSVRGLSNLGNTCFFNAVVQSLSQTQYLRELLKQIAEEKSSFSITPALSSELDPLQIQLERPGSLTLAMCQLMNEIQETKKGVVTPKELFTQVCKKAPRFKGFQQQDSQELLRYLLDGMRAEEAKRVNSGILEALKSSGKNFEAEQTKKIVKEYEKDGAPKNFVDRVFGGAMSSTVMCKECKTVSLVTEMFLDLSLPVADEAYRKKNQKKAVQHRHSVSDDGDQDTSSLANGNEDMPTGTGSKYQQKKAKKQAKKQAKNQRRQQKQGGKVTLDAITNQSSTDPADSSMQTQTVSVNGSADAQPADTNQEDLSLEKHNEDQDDEEPEQEQAASVNNRFTALSEDQTTEDIAEQVNEDEDEIEQNCAEEEELVEELNTMSLTTPSEGDVENGEDTLEDVKEYTVVNRDPELAFRALASRTAPVKQECSVESCLYQFTEVEHLTENNRLMCVTCTKQQPGYKDGCKKAVYRDALKQMLISDPPVVLTLHLKRFQQVAYSVCKVNRHVQFPQILDLAPFCSLNCTGVKEGETQVLYSLYGIVEHSGTMRSGHYTAYVKSRPSTHNCVQNGTAAASGDAEASKGSWFHISDSSVHPVPEAKVQSSQAYLLFYEKIS | 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 segregation when cells enter into mitosis. Regulates Hox gene expression via histone H2A deubiquitination. Prefers nucleosomal substrates. Does not deubiquitinate histone H2B.
Catalytic Activity: Thiol-dependent hydrolysis of ester, thioester, amide, peptide and isopeptide bonds formed by the C-terminal Gly of ubiquitin (a 76-residue protein attached to proteins as an intracellular targeting signal).
Sequence Mass (Da): 90450
Sequence Length: 815
Domain: The UBP-type zinc finger binds 3 zinc ions that form a pair of cross-braced ring fingers encapsulated within a third zinc finger in the primary structure. It recognizes the C-terminal tail of free ubiquitin.
Subcellular Location: Nucleus
EC: 3.4.19.12
|
Q9Y5T5 | MGKKRTKGKTVPIDDSSETLEPVCRHIRKGLEQGNLKKALVNVEWNICQDCKTDNKVKDKAEEETEEKPSVWLCLKCGHQGCGRNSQEQHALKHYLTPRSEPHCLVLSLDNWSVWCYVCDNEVQYCSSNQLGQVVDYVRKQASITTPKPAEKDNGNIELENKKLEKESKNEQEREKKENMAKENPPMNSPCQITVKGLSNLGNTCFFNAVMQNLSQTPVLRELLKEVKMSGTIVKIEPPDLALTEPLEINLEPPGPLTLAMSQFLNEMQETKKGVVTPKELFSQVCKKAVRFKGYQQQDSQELLRYLLDGMRAEEHQRVSKGILKAFGNSTEKLDEELKNKVKDYEKKKSMPSFVDRIFGGELTSMIMCDQCRTVSLVHESFLDLSLPVLDDQSGKKSVNDKNLKKTVEDEDQDSEEEKDNDSYIKERSDIPSGTSKHLQKKAKKQAKKQAKNQRRQQKIQGKVLHLNDICTIDHPEDSEYEAEMSLQGEVNIKSNHISQEGVMHKEYCVNQKDLNGQAKMIESVTDNQKSTEEVDMKNINMDNDLEVLTSSPTRNLNGAYLTEGSNGEVDISNGFKNLNLNAALHPDEINIEILNDSHTPGTKVYEVVNEDPETAFCTLANREVFNTDECSIQHCLYQFTRNEKLRDANKLLCEVCTRRQCNGPKANIKGERKHVYTNAKKQMLISLAPPVLTLHLKRFQQAGFNLRKVNKHIKFPEILDLAPFCTLKCKNVAEENTRVLYSLYGVVEHSGTMRSGHYTAYAKARTANSHLSNLVLHGDIPQDFEMESKGQWFHISDTHVQAVPTTKVLNSQAYLLFYERIL | 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 segregation when cells enter into mitosis . In resting B- and T-lymphocytes, phosphorylation by AURKB leads to enhance its activity, thereby maintaining transcription in resting lymphocytes. Regulates Hox gene expression via histone H2A deubiquitination . Prefers nucleosomal substrates . Does not deubiquitinate histone H2B . Also deubiquitinates non-histone proteins, such as ribosomal protein RPS27A: deubiquitination of monoubiquitinated RPS27A promotes maturation of the 40S ribosomal subunit .
PTM: Phosphorylated at the onset of mitosis and dephosphorylated during the metaphase/anaphase transition. Phosphorylation by AURKB enhances the deubiquitinase activity.
Catalytic Activity: Thiol-dependent hydrolysis of ester, thioester, amide, peptide and isopeptide bonds formed by the C-terminal Gly of ubiquitin (a 76-residue protein attached to proteins as an intracellular targeting signal).
Sequence Mass (Da): 93570
Sequence Length: 823
Domain: The UBP-type zinc finger binds 3 zinc ions that form a pair of cross-braced ring fingers encapsulated within a third zinc finger in the primary structure. It recognizes the C-terminal tail of free ubiquitin.
Subcellular Location: Nucleus
EC: 3.4.19.12
|
Q0VA64 | MVKKRGKNLPAQDSLDAEPVCKHLRKALDEGSVKKALVNVEWTVCQECQADNKEKNNSDDELVEDPSVWLCLKCGHRGCGRNSASQHALNHYNTPRSEPHCLVLSVDMWSAWCYLCDNEVPYNRSSRLGQLVDYLQRKAKAKSKSTDSAALDEEVKAEIVAENEVKIEDQEEKPKGQAKWDKASSTQNNSTEPTVKGLSNLGNTCFFNAVMQNLSQTPAVRELLNEAKTLKKPVTVPLPDSSSPTNVEVHLEQQPGPLTLAMWQFLTEMQETKKGVVTPKEVFSQVCKKAIRFKGYQQQDSQELLRYLLDGMRGEEIQRVSLAMSKSLQNTLDEEEIKKIVKDSEKRRTIPNFVDHLFGGELTSTIMCEECHTVSLVHEPFLDLSLPVLDDVIVKKNSQKSSAPAPERKEEEENDDGYIKERDEASPGASKHLQKKAKKAAKKQAKNQRRQLKMQGKTVLLTDVAKQECSEDEEEIAPNNTESEANTRPDDEVPIADGLNTMKSDLSALENGSETIESAMERVTEDTDLDTSGHNTESVEMNAMELVRNMENNNNNNTDVNKTLERTEGSGVDSMEATAAVDNGNADTVCVDDTEAANGLLDCSAASMDNELTNSLNRLKLSSDIEPTQVEIEILPDQQQPHTQIYEVINEDPKTAFSTLSERKDLPLDGYSVLSCLYQFTHKETLTGNNKLLCNVCTRKQASRLNNSNKGEKTFVYTNAKKQMLVSDPSPILTLHLKRFQQNGFNLRKINRHIKFPEVLDLAPFCTSKCKNIPAGESRLLYSLYGVIEHSGSMRSGHYTAFVKLRRPNQQLCEMVLKGVIPEVSGSEPGQGSWYHISDSHVQAVSLSRVLSSQAYLLFYERML | 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 segregation when cells enter into mitosis. Regulates Hox gene expression via histone H2A deubiquitination. Prefers nucleosomal substrates. Does not deubiquitinate histone H2B.
Catalytic Activity: Thiol-dependent hydrolysis of ester, thioester, amide, peptide and isopeptide bonds formed by the C-terminal Gly of ubiquitin (a 76-residue protein attached to proteins as an intracellular targeting signal).
Sequence Mass (Da): 96666
Sequence Length: 864
Domain: The UBP-type zinc finger binds 3 zinc ions that form a pair of cross-braced ring fingers encapsulated within a third zinc finger in the primary structure. It recognizes the C-terminal tail of free ubiquitin.
Subcellular Location: Nucleus
EC: 3.4.19.12
|
Q9FKP5 | MMLVFLLIRRQWRSASVRREEVIRLIALATEESYLAEEVRPATVDYGGDSVSDVYRCAVCLYPTTTRCSQCKSVRYCSSKCQILHWRRGHKEECRSPDYDEEKEEYVQSDYDAKESNVDFPSRGTAYESSSNVSVDVACDMSTSRPSIHKVQPRSEAVDFTTSLNIKDNLYETRPLSRKKSRNRTDKVESASNYSKGKTDAKLRKLGNQNSRRSGDSANMSISDQFLSVGFEEEMNALKHERITSEPSSASAAMSSSSTLLLPSKANSKPKVSQASSSGLKTSVQKVVQHFRPPQSSKKSQPSSSIDEMSFSYELFVKLYCDRVELQPFGLVNLGNSCYANAVLQCLAFTRPLISYLIRGLHSKTCRKKSWCFVCEFEHLILKARGGESPLSPIKILSKLQKIGKHLGPGKEEDAHEFLRCAVDTMQSVFLKEAPAAGPFAEETTLVGLTFGGYLHSKIKCMACLHKSERPELMMDLTVEIDGDIGSLEEALAQFTAYEVLDGENRYFCGRCKSYQKAKKKLMILEGPNILTVVLKRFQSDNFGKLSKPIHFPELLDISPYMSDPNHGDHPVYSLYAVVVHLDAMSTLFSGHYVCYIKTLDGDWFKIDDSNVFPVQLETVLLEGAYMLLYARDSPRPVSKNGGRKSKQRRNLAAIPSRKGNKKQRDGDNNSLLPRVDWSSGSLSSMFSSSDTTSSCSTKDSSGIENLSDYLFGGVEPVWKWDRHNKSQTFD | 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 the C-terminal Gly of ubiquitin (a 76-residue protein attached to proteins as an intracellular targeting signal).
Sequence Mass (Da): 81999
Sequence Length: 731
EC: 3.4.19.12
|
Q67XW5 | MHEVGFPLDLSVFTRLIATLFFLAVGVFYFLKNTAAKYFDIGAAAAGGFDRDFMAVDAEDCSVCGNFSTKKCSRCKSVRYCSAECQRSDWSSGHQRNCRDYGITTLTPSAKNGLRFRASPFGDSSASSIALISERGQNKSSLKPREVLFPYEEFVEYFNWDNPELAPCGLMNCGNSCFANVILQCLSWTRPLVAYLLEKGHKRECMRNDWCFLCEFQTHVERASQSRFPFSPMNIISRLTNIGGTLGYGRQEDAHEFMRYAIDMMQSVCLDEFGGEKIVPPRSQETTLIQYIFGGLLQSQVQCTVCNHVSDQYENMMDLIVEMHGDAGSLEECLDQFTAEEWLHGDNMYKCDRCSDYVKACKRLTIRRAPNILTIALKRYQGGRYGKLNKRISFPETLDLNPYMSEGGDGSDVYKLYAVIVHLDMLNASFFGHYICYIKDFCGNWYRIDDSEIESVELEDVLSQRAYMLLYSRIQARSSSSCLRSEVKDEKKTDTLDTESCVKELVESSMVGAIESRSSTHATIEDPVCEQSPSPSPSPSPSPSPSPSPSVLASECCSEVERIDTLDSESNSSIDDSATDHQEDVANGNKDPEVKYQAADSWSDPTTSTPLVCTKSKPPVRDMDTKMIDAQ | 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 the C-terminal Gly of ubiquitin (a 76-residue protein attached to proteins as an intracellular targeting signal).
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 70753
Sequence Length: 631
Subcellular Location: Membrane
EC: 3.4.19.12
|
Q9UMW8 | MSKAFGLLRQICQSILAESSQSPADLEEKKEEDSNMKREQPRERPRAWDYPHGLVGLHNIGQTCCLNSLIQVFVMNVDFTRILKRITVPRGADEQRRSVPFQMLLLLEKMQDSRQKAVRPLELAYCLQKCNVPLFVQHDAAQLYLKLWNLIKDQITDVHLVERLQALYTIRVKDSLICVDCAMESSRNSSMLTLPLSLFDVDSKPLKTLEDALHCFFQPRELSSKSKCFCENCGKKTRGKQVLKLTHLPQTLTIHLMRFSIRNSQTRKICHSLYFPQSLDFSQILPMKRESCDAEEQSGGQYELFAVIAHVGMADSGHYCVYIRNAVDGKWFCFNDSNICLVSWEDIQCTYGNPNYHWQETAYLLVYMKMEC | 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 differentiation by deubiquitinating TAK1, likely to keep TAK1-TAB complexes in steady conditions . In turn, restricts activation of NF-kappa-B, NFAT, and JNK as well as expression of IL2 in T-cells after TCR activation . Acts as a molecular adapter with USP20 to promote innate antiviral response through deubiquitinating STING1 . Involved also in the negative regulation of the inflammatory response triggered by type I interferon . Upon recruitment by STAT2 to the type I interferon receptor subunit IFNAR2 interferes with the assembly of the ternary interferon-IFNAR1-IFNAR2 complex and acts as a negative regulator of the type I interferon signaling pathway .
Catalytic Activity: Thiol-dependent hydrolysis of ester, thioester, amide, peptide and isopeptide bonds formed by the C-terminal Gly of ubiquitin (a 76-residue protein attached to proteins as an intracellular targeting signal).
Sequence Mass (Da): 43011
Sequence Length: 372
Subcellular Location: Cytoplasm
EC: 3.4.19.12
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Q9SJA1 | MHEVGLFVDLNSFTQLILTLFFVSIGLLYFVKRTAAKYFEVGGGSGGFDRDHRRDFMVSDTAECSVCGKATTKKCSRCKSVRYCSAACQTSDWKSGHKLKCKGFRSTDSSPVRRDDIDFEASLFGNRSASKKTRIALVPQQSQSKATLKPTDVLFPYESFVRYYNWDRPIMAPCGLTNCGNSCFANVVLQCLSWTRPLVAYLLERGHKRECRRNDWCFLCEFENHLDRANYSRFPFSPMNIISRLPNIGGNLGYGRQEDAHELMRFAIDMMQSVCLDEFGGEKVVPPRAQETTLIQYIFGGLLQSQVQCTACSNVSDQYENMMDLTVEIHGDAVSLEECLDQFTAKEWLQGDNLYKCDRCDDYVKACKRLSIRCAPNILTIALKRFQGGRFGKLNKRISFPETFDLGPYMSGGGEGSDVYKLYAVIVHLDMLNASFFGHYICYVKDFRGNWYRIDDSEVEKVELEDVLSQRAYMLLYSRVQPRPSNLRSEESQDEKKTDTLNTESNQDGSVESSGVGTNDTSVSSLCNGIISHSEDPEYEKESSLSASVPVSEEGKEVDVKVDTVDSESNRSIDMEHDSGTDHQEEEANGKEDPTVENLAVDSSCLDITTPSPSAATEFIPQENERSDTESKPLEKEHSDTESNKPLEKEHLDSESKPLEKEHSDTEMIDAQ | 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 the C-terminal Gly of ubiquitin (a 76-residue protein attached to proteins as an intracellular targeting signal).
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 75720
Sequence Length: 672
Subcellular Location: Membrane
EC: 3.4.19.12
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Q70CQ1 | MDRCKHVGRLRLAQDHSILNPQKWCCLECATTESVWACLKCSHVACGRYIEDHALKHFEETGHPLAMEVRDLYVFCYLCKDYVLNDNPEGDLKLLRSSLLAVRGQKQDTPVRRGRTLRSMASGEDVVLPQRAPQGQPQMLTALWYRRQRLLARTLRLWFEKSSRGQAKLEQRRQEEALERKKEEARRRRREVKRRLLEELASTPPRKSARLLLHTPRDAGPAASRPAALPTSRRVPAATLKLRRQPAMAPGVTGLRNLGNTCYMNSILQVLSHLQKFRECFLNLDPSKTEHLFPKATNGKTQLSGKPTNSSATELSLRNDRAEACEREGFCWNGRASISRSLELIQNKEPSSKHISLCRELHTLFRVMWSGKWALVSPFAMLHSVWSLIPAFRGYDQQDAQEFLCELLHKVQQELESEGTTRRILIPFSQRKLTKQVLKVVNTIFHGQLLSQVTCISCNYKSNTIEPFWDLSLEFPERYHCIEKGFVPLNQTECLLTEMLAKFTETEALEGRIYACDQCNSKRRKSNPKPLVLSEARKQLMIYRLPQVLRLHLKRFRWSGRNHREKIGVHVVFDQVLTMEPYCCRDMLSSLDKETFAYDLSAVVMHHGKGFGSGHYTAYCYNTEGGFWVHCNDSKLNVCSVEEVCKTQAYILFYTQRTVQGNARISETHLQAQVQSSNNDEGRPQTFS | 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 hydrolysis of ester, thioester, amide, peptide and isopeptide bonds formed by the C-terminal Gly of ubiquitin (a 76-residue protein attached to proteins as an intracellular targeting signal).
Sequence Mass (Da): 79198
Sequence Length: 688
Subcellular Location: Nucleus
EC: 3.4.19.12
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Q8LAM0 | MGAAGSKLEKALGDQFPEGERYFGFENFGNTCYCNSVLQALYFCAPFREQLLEHYANNKADAEENLLTCLADLFSQISSQKKKTGVIAPKRFVQRLKKQNELFRSYMHQDAHEFLNYLLNELVEILEKETQATKADNETSSSPEKIANVLKAPLANGVHKEPIVTWVHKIFQGILTNETRCLRCETVTARDETFLDLSLDIEQNSSITSCLKNFSSTETLHAEDKFFCDKCCSLQEAQKRMKIKKPPHILVIHLKRFKYMEQLGRYKKLSYRVVFPLELKLSNTVDEYVDIEYSLFAVVVHVGSGPNHGHYVSLVKSHNHWLFFDDESVEIIEESAVQTFFGSSQEYSSNTDHGYILLYESLGTR | 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 and isopeptide bonds formed by the C-terminal Gly of ubiquitin (a 76-residue protein attached to proteins as an intracellular targeting signal).
Sequence Mass (Da): 41846
Sequence Length: 365
Subcellular Location: Nucleus
EC: 3.4.19.12
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Q6FQF0 | MPGIEQPVSRKNETLVKLSSLADEFVFNDEVQLNLQDVLQECVDTYQNYQDEVKKIKNMDHTESEKVSELCKSAYIYYKIVHNFITKVIPHLPEFEVATGPKASKLQAELIKIYYSLFSRLESDKKISYIKNIIIKHMDTQENNHSVESHEQVKLSNKKLPVNRDAIEIDKDSILQDIRYINGKRSGSGISCSELLSLMKMKEDSLLLIDVRPKLEYDAHHIKTKNIICIEPISFKESYSDQQIEKTSMIPSPKHEIQLFQRRSEFQYIILYTDLEEKSNFYFQQLKSLLEILLQRSFLRPIDDRKTKVLFLSDSLQNWIKNGGEIDKSQEVSKIRNRSISGSGPLLNSLSERKTIGAFPDINRNSTKQMPISPLPSLPGSERTVATPPNGSSTLGRINSPVTHYPKAPLINDSEFHLNINNNHSPPTHLPSKDNNPLASSMPIGSDHKPFMSPQNSLPLAPKPPTLESKNYNFISDRSNIIDQKQNRSRSLEPQLPPIPSTLIRKNSPEKTLSCNQMMDTSFTVGLENMGNSCYINCIIQCIFATTELIKIFLNGTYAKHINKQSKLGSKGVLSHNFAKLLKDMYEENSSKKIGKKHGAVKTLQFKMACASVNSLFKDASQQDCLEFCQFLLDGLHEDLNQCGANPPLKELSPEAEKMRENLSLRVASSIEWERYLTTDFSIIVDLFQGQYASQLRCKVCNRTSTTYQAFSVLSVPVPSGKSCGLLDCFIEFTKTENLEVDEQWFCPSCKKKQPSTKKLTITRLPRNLIIHLKRFDNMMNKNNIFVRYPQILDLTPFWANDSDGKLPPGITDEIPARGQVPPFNYRLYGAACHFGTLYGGHYTSYVDKGPEKGWIYFDDTVYRPVRFQNEFISPSAYVLFYHRITS | 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 promoting coordination of DNA replication and avoids DNA overreplication (By similarity).
Catalytic Activity: Thiol-dependent hydrolysis of ester, thioester, amide, peptide and isopeptide bonds formed by the C-terminal Gly of ubiquitin (a 76-residue protein attached to proteins as an intracellular targeting signal).
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 101165
Sequence Length: 887
Subcellular Location: Cytoplasm
EC: 3.4.19.12
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Q13107 | MAEGGGCRERPDAETQKSELGPLMRTTLQRGAQWYLIDSRWFKQWKKYVGFDSWDMYNVGEHNLFPGPIDNSGLFSDPESQTLKEHLIDELDYVLVPTEAWNKLLNWYGCVEGQQPIVRKVVEHGLFVKHCKVEVYLLELKLCENSDPTNVLSCHFSKADTIATIEKEMRKLFNIPAERETRLWNKYMSNTYEQLSKLDNTVQDAGLYQGQVLVIEPQNEDGTWPRQTLQSKSSTAPSRNFTTSPKSSASPYSSVSASLIANGDSTSTCGMHSSGVSRGGSGFSASYNCQEPPSSHIQPGLCGLGNLGNTCFMNSALQCLSNTAPLTDYFLKDEYEAEINRDNPLGMKGEIAEAYAELIKQMWSGRDAHVAPRMFKTQVGRFAPQFSGYQQQDSQELLAFLLDGLHEDLNRVKKKPYLELKDANGRPDAVVAKEAWENHRLRNDSVIVDTFHGLFKSTLVCPECAKVSVTFDPFCYLTLPLPLKKDRVMEVFLVPADPHCRPTQYRVTVPLMGAVSDLCEALSRLSGIAAENMVVADVYNHRFHKIFQMDEGLNHIMPRDDIFVYEVCSTSVDGSECVTLPVYFRERKSRPSSTSSASALYGQPLLLSVPKHKLTLESLYQAVCDRISRYVKQPLPDEFGSSPLEPGACNGSRNSCEGEDEEEMEHQEEGKEQLSETEGSGEDEPGNDPSETTQKKIKGQPCPKRLFTFSLVNSYGTADINSLAADGKLLKLNSRSTLAMDWDSETRRLYYDEQESEAYEKHVSMLQPQKKKKTTVALRDCIELFTTMETLGEHDPWYCPNCKKHQQATKKFDLWSLPKILVVHLKRFSYNRYWRDKLDTVVEFPIRGLNMSEFVCNLSARPYVYDLIAVSNHYGAMGVGHYTAYAKNKLNGKWYYFDDSNVSLASEDQIVTKAAYVLFYQRRDDEFYKTPSLSSSGSSDGGTRPSSSQQGFGDDEACSMDTN | 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 of the U4 spliceosomal protein PRPF3 . This may prevent its recognition by the U5 component PRPF8 thereby destabilizing interactions within the U4/U6.U5 snRNP . May also play a role in the regulation of quality control in the ER .
PTM: Monoubiquitinated by TRIM21. Ubiquitination does not lead to its proteasomal degradation. Autodeubiquitinated.
Catalytic Activity: Thiol-dependent hydrolysis of ester, thioester, amide, peptide and isopeptide bonds formed by the C-terminal Gly of ubiquitin (a 76-residue protein attached to proteins as an intracellular targeting signal).
Sequence Mass (Da): 108565
Sequence Length: 963
Domain: The DUSP and ubiquitin-like 1 domains promote ubiquitin release and thus enhance USB4 catalytic activity. However, these domains do not bind ubiquitin.
Subcellular Location: Cytoplasm
EC: 3.4.19.12
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O60139 | MSDDYFDRLFELAFVYINEDETIQSCSFRGQRWLEEAQTLEQKNSLLKAYYYYLKALKLAYEIPCRFEISVKSTHYGEFKQFQKLAIQAVSKAFTIKSKLAVKHYLPVIQISDALSLSKKSSLKVLFLNFYSQESSKGYVFSKHTIAIPISCLQSMDSSKIYDFLKSAPFHPSMVICYSLERYFEDVSLAYKLYSMLRSLKLDPHFMELANPKKVDSSLSYENYQPIGLTNLGNTCYMNCVLQCLFACKDLTIPMLQGRGLLQNINTKNPLGTGGKITSAFFSLLQSVLLNHGQRSISPRNFLEIVQSLNRDFSIDGQCDAQEFLNFFLDKLHEDLNSNASRSPIAPLTEDQLSAREELPLSHFSHIEWNLHLRSNKSIVVNNFVGQLCSRTQCMTCGRTSTTFAPFTSLAIPIDDVSHVVSLQECLLKFSAPELLQGHDGWHCPVCKVQRSAKKVIMISKLPEYLIIQIQRFKISVMGRKKIDTPLGLSLQIPSKMLVPPSFQSGIGYIPSNYNLFAFICHYGQLENGHYISDVLFNNEWCHIDDSIVRTVGGITDLREDFSSSYILFYKRSSLLEEFEDKCPKMTLKRNVK | 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, peptide and isopeptide bonds formed by the C-terminal Gly of ubiquitin (a 76-residue protein attached to proteins as an intracellular targeting signal).
Sequence Mass (Da): 67747
Sequence Length: 593
Subcellular Location: Cytoplasm
EC: 3.4.19.12
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A7TGY3 | MVEVDSRKQLLYDPIVRLSGIADKFVMQDATSSNMKVSLQECIDTLANYQDECKKLKRNEPTLSPSERYSIYESAYIYYKIIHIMVLTRIPSLPQFSSAKSSDATNEDKELMQIYNMLVKTLLSDEKIAQIKSYLRANYPDKNSKGKESIVNKQLLNNEVFMLPLSGSPISAVQLNHLIQMYDSSLLLIDVRPRAEFDSKHIKAKSVICVEPVSFKNSFTDLEVEKKSLITSPQKEIALFQARDKYNYIVIYTQQSEKTQFYMHQQLVLLDILMNKSFAKPLNEKNIKVFTLDKGFSGWVSKKGACETTTQNGDAIYISGNTSSLNLQNLPQLSPNIGSSMDKSMRDMMSTSADFEGRTYQLPQQQQPVFARTPSFKNLFNKAKSSSTSSVTSSSPAPSQLVRPQTSSMPPLEQNFTQYPETPKLLTQINTNTMPLSQISPISSRAMSPMTKNMLTQSPQLPMKISRTTIGNGAMLDLKPHPDSKPPGQPVPALPQLPHHMTGTYQNLNQPKLDLDFTVGLENMGNSCYMNCIIQCLLSTHELSQIFLNNSYEKHINLNSKLGSKGVLAKYFARLVHTMYREGSFKRPLEKNKPIQPIQFKMACGSINSLFKDNTQQDSQEFCQFLLDGLHEDLNQCGANPPLKELSEDAEKMREKLSMRIASSIEWERFLTTDFSVIVDLFQGQYASQLKCKVCGCTSTTYQTFSVLSVPVPHVSSCHILDCFNEFTKVEKLGTDELWSCPTCKKKQPSTKKLTITRLPRNLIIHLKRFDNMMNKNNVFVKYPFLLDLTPYWANDFDGRLPPGVTDELPTRGQVPPFRYKLNAVASHVGSLYGGHYTAYVNKGINRGWHYFDDTSYRPIKNETECITPNAYVLFYHRVYGV | 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 promoting coordination of DNA replication and avoids DNA overreplication (By similarity).
Catalytic Activity: Thiol-dependent hydrolysis of ester, thioester, amide, peptide and isopeptide bonds formed by the C-terminal Gly of ubiquitin (a 76-residue protein attached to proteins as an intracellular targeting signal).
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 100061
Sequence Length: 882
Subcellular Location: Cytoplasm
EC: 3.4.19.12
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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 systems (By similarity).
Sequence Mass (Da): 33436
Sequence Length: 294
Domain: The UBA domain specifically recognizes and binds 'Lys-6'-linked polyubiquitin chains.
Subcellular Location: Cytoplasm
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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/TRAF3/TRAF6 signalosome. This function probably serves as a brake to prevent excessive RLR signaling . Interferes with the TNFalpha-triggered NF-kappa-B pathway by interacting with cellular inhibitors of apoptosis proteins (cIAPs) and thereby inhibiting their recruitment to TNFR1 . Prevents also the activation of NF-kappa-B by associating with CUL1 and thus inhibiting NF-kappa-B inhibitor alpha/NFKBIA degradation that remains bound to NF-kappa-B . Interacts with the BRCA1-BARD1 heterodimer and regulates its activity. Specifically binds 'Lys-6'-linked polyubiquitin chains. Interaction with autoubiquitinated BRCA1 leads to the inhibition of the E3 ubiquitin-protein ligase activity of the BRCA1-BARD1 heterodimer . 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.
Sequence Mass (Da): 33325
Sequence Length: 297
Domain: The UBA domain specifically recognizes and binds 'Lys-6'-linked polyubiquitin chains.
Subcellular Location: Cytoplasm
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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 complex required to couple deglycosylation and proteasome-mediated degradation of misfolded proteins in the endoplasmic reticulum that are retrotranslocated in the cytosol (By similarity).
Sequence Mass (Da): 33582
Sequence Length: 297
Domain: The UBA domain specifically recognizes and binds 'Lys-6'-linked polyubiquitin chains.
Subcellular Location: Cytoplasm
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P34631 | MQWFGGNVATAIQISRKNKALLIVYITTDSEDGQIFDGFWQHIDSSNLLCAVVGIKLKAGETSAQQFADIYPTPILPAAYLIDQNGKPLEVITPLVGKTYDQFRAKFDKATAQFVNGMPTAAANQLSTPSPSPAPVQVPASTDAPIPAPTPVTAPIQSSSTSQEMTRELAEKVARAKALLEQKKQKDAEKKREADKHVKEEMTKAREAKQERDAEALVKAAKQRKMEKLAAESDKKRILAQIKADREAAQKKFGKLVNTENASENTEKKQETTVGKAVPSDRCRLQVRLPDGSTFVEEFPSNDVLNSLVEIIRQKPSIAGTTFEIQQPYPRRIFTNDDYSKTFLENQLTPSTALVVIQKSSGSSSNYGSFSLSTQTVSFVTWVLYPLTAFWNIFCGMIGWNSTGKQQDSKSKKNDGPSTSGQSGSQPQRRGMPRSAEVRRRGNVAGLENPNEDDPEERASFNGNSTQFM | 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 membrane protein
Sequence Mass (Da): 51631
Sequence Length: 469
Domain: The intramembrane domain also contains the signal for ER targeting.
Subcellular Location: Endoplasmic reticulum membrane
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Q92575 | MLWFQGAIPAAIATAKRSGAVFVVFVAGDDEQSTQMAASWEDDKVTEASSNSFVAIKIDTKSEACLQFSQIYPVVCVPSSFFIGDSGIPLEVIAGSVSADELVTRIHKVRQMHLLKSETSVANGSQSESSVSTPSASFEPNNTCENSQSRNAELCEIPPTSDTKSDTATGGESAGHATSSQEPSGCSDQRPAEDLNIRVERLTKKLEERREEKRKEEEQREIKKEIERRKTGKEMLDYKRKQEEELTKRMLEERNREKAEDRAARERIKQQIALDRAERAARFAKTKEEVEAAKAAALLAKQAEMEVKRESYARERSTVARIQFRLPDGSSFTNQFPSDAPLEEARQFAAQTVGNTYGNFSLATMFPRREFTKEDYKKKLLDLELAPSASVVLLPAGRPTASIVHSSSGDIWTLLGTVLYPFLAIWRLISNFLFSNPPPTQTSVRVTSSEPPNPASSSKSEKREPVRKRVLEKRGDDFKKEGKIYRLRTQDDGEDENNTWNGNSTQQM | 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.
Subcellular Location: Endoplasmic reticulum membrane
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Q2KIJ6 | MKKFFQEIKADIKFKSAGPGQKLTESVGEKAPKEKPSQPPVRQPRQGPTNEAQMAAAAALARLEQKQPRARGPTSQDSIRNQVRKELRAEAAVSGDPEAPGSNTAPEPKEEGSAHLAVPGVYFTCPLTGAILRKDQRDARIREAILMHFSTDPVAASIMKIHTFNKDRDRVKLGVDTIAKYLDNIHLHPEEEKYRKIKVQNKVFQERIHCLEGTHEFFEAIGFQKVLLPIPDQEGPEEFYVLSEAALAQPQSLEWHKEQLLSAEPVRATLARQRRVFRPSTLASQFDLPADFFNLTAEEIKREQRLRSEAVERLSVLRTKAMREREEQREMRKYTYTLLRVRLPDGCLLQGTFYARERVAALYGFVREALQNDWLPFELLASGGQKLSEDENLAFNECGLVPSALLTFSLDAAVLEDIRAAGTQPDTSILKPELLSAIEKL | 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-associated degradation (ERAD) of misfolded proteins. Together with VCP and other cofactors, it may play a role in macroautophagy, regulating for instance the clearance of damaged lysosomes.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 49733
Sequence Length: 441
Domain: The UBX domain lacks key residues critical for VCP binding.
Subcellular Location: Cytoplasm
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Q9BZV1 | MKKFFQEFKADIKFKSAGPGQKLKESVGEKAHKEKPNQPAPRPPRQGPTNEAQMAAAAALARLEQKQSRAWGPTSQDTIRNQVRKELQAEATVSGSPEAPGTNVVSEPREEGSAHLAVPGVYFTCPLTGATLRKDQRDACIKEAILLHFSTDPVAASIMKIYTFNKDQDRVKLGVDTIAKYLDNIHLHPEEEKYRKIKLQNKVFQERINCLEGTHEFFEAIGFQKVLLPAQDQEDPEEFYVLSETTLAQPQSLERHKEQLLAAEPVRAKLDRQRRVFQPSPLASQFELPGDFFNLTAEEIKREQRLRSEAVERLSVLRTKAMREKEEQRGLRKYNYTLLRVRLPDGCLLQGTFYARERLGAVYGFVREALQSDWLPFELLASGGQKLSEDENLALNECGLVPSALLTFSWDMAVLEDIKAAGAEPDSILKPELLSAIEKLL | 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-associated degradation (ERAD) of misfolded proteins . Together with VCP and other cofactors, it may play a role in macroautophagy, regulating for instance the clearance of damaged lysosomes .
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 49754
Sequence Length: 441
Domain: The UBX domain lacks key residues critical for VCP binding.
Subcellular Location: Cytoplasm
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O94888 | MAAHGGSAASSALKGLIQQFTTITGASESVGKHMLEACNNNLEMAVTMFLDGGGIAEEPSTSSASVSTVRPHTEEEVRAPIPQKQEILVEPEPLFGAPKRRRPARSIFDGFRDFQTETIRQEQELRNGGAIDKKLTTLADLFRPPIDLMHKGSFETAKECGQMQNKWLMINIQNVQDFACQCLNRDVWSNEAVKNIIREHFIFWQVYHDSEEGQRYIQFYKLGDFPYVSILDPRTGQKLVEWHQLDVSSFLDQVTGFLGEHGQLDGLSSSPPKKCARSESLIDASEDSQLEAAIRASLQETHFDSTQTKQDSRSDEESESELFSGSEEFISVCGSDEEEEVENLAKSRKSPHKDLGHRKEENRRPLTEPPVRTDPGTATNHQGLPAVDSEILEMPPEKADGVVEGIDVNGPKAQLMLRYPDGKREQITLPEQAKLLALVKHVQSKGYPNERFELLTNFPRRKLSHLDYDITLQEAGLCPQETVFVQERN | 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 modification on cullins.
Subcellular Location: Nucleus
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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] = a plastoquinone + 4 H(+)(out) + 2 reduced [plastocyanin]
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 24325
Sequence Length: 230
Subcellular Location: Plastid
EC: 7.1.1.6
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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] = a plastoquinone + 4 H(+)(out) + 2 reduced [plastocyanin]
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 18685
Sequence Length: 178
Subcellular Location: Cellular thylakoid membrane
EC: 7.1.1.6
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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] = a plastoquinone + 4 H(+)(out) + 2 reduced [plastocyanin]
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 23726
Sequence Length: 222
Subcellular Location: Plastid
EC: 7.1.1.6
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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] = a plastoquinone + 4 H(+)(out) + 2 reduced [plastocyanin]
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 24837
Sequence Length: 241
Subcellular Location: Plastid
EC: 7.1.1.6
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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) = a quinone + 2 Fe(II)-[cytochrome c](out) + 2 H(+)(out)
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 22190
Sequence Length: 207
Subcellular Location: Cell membrane
EC: 7.1.1.8
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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) = a quinone + 2 Fe(II)-[cytochrome c](out) + 2 H(+)(out)
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 19011
Sequence Length: 179
Subcellular Location: Cell membrane
EC: 7.1.1.8
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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 transmembrane complex that is part of the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII) and cytochrome c oxidase (complex IV, CIV), that cooperate to transfer electrons derived from NADH and succinate to molecular oxygen, creating an electrochemical gradient over the inner membrane that drives transmembrane transport and the ATP synthase. The cytochrome b-c1 complex catalyzes electron transfer from ubiquinol to cytochrome c, linking this redox reaction to translocation of protons across the mitochondrial inner membrane, with protons being carried across the membrane as hydrogens on the quinol. In the process called Q cycle, 2 protons are consumed from the matrix, 4 protons are released into the intermembrane space and 2 electrons are passed to cytochrome c. The Rieske protein is a catalytic core subunit containing a [2Fe-2S] iron-sulfur cluster. It cycles between 2 conformational states during catalysis to transfer electrons from the quinol bound in the Q(0) site in cytochrome b to cytochrome c1 (By similarity). Incorporation of UQCRFS1 is the penultimate step in complex III assembly (By similarity).
Catalytic Activity: a quinol + 2 Fe(III)-[cytochrome c](out) = a quinone + 2 Fe(II)-[cytochrome c](out) + 2 H(+)(out)
PTM: Proteolytic processing is necessary for the correct insertion of UQCRFS1 in the complex III dimer. Several fragments are generated during UQCRFS1 insertion, most probably due to the endogenous matrix-processing peptidase (MPP) activity of the 2 core protein subunits UQCRC1/QCR1 and UQCRC2/QCR2, which are homologous to the 2 mitochondrial-processing peptidase (MPP) subunits beta-MPP and alpha-MPP respectively. The action of the protease is also necessary for the clearance of the UQCRFS1 fragments.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 29547
Sequence Length: 274
Subcellular Location: Mitochondrion inner membrane
EC: 7.1.1.8
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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) = a quinone + 2 Fe(II)-[cytochrome c](out) + 2 H(+)(out)
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 18823
Sequence Length: 176
Subcellular Location: Cell membrane
EC: 7.1.1.8
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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
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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 mismatched double-stranded DNA and polynucleotides, releasing free uracil.
Sequence Mass (Da): 22718
Sequence Length: 199
Domain: Contains a pseudo-FCL region, a large solvent-exposed peptide region containing an alpha helix and loop anchored on each end via ligation of two cysteine thiolates to a [4Fe-4S](2+) cluster. This region is involved in DNA binding and catalysis, particularly in duplex DNA contexts.
EC: 3.2.2.27
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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 mismatched double-stranded DNA and polynucleotides, releasing free uracil.
Sequence Mass (Da): 21563
Sequence Length: 196
EC: 3.2.2.27
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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 mismatched double-stranded DNA and polynucleotides, releasing free uracil.
Sequence Mass (Da): 24498
Sequence Length: 216
EC: 3.2.2.27
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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: 220
EC: 3.2.2.27
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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 mismatched double-stranded DNA and polynucleotides, releasing free uracil.
Sequence Mass (Da): 21501
Sequence Length: 192
Domain: The seven N-terminal amino acids are important for maintaining proper protein folding and increase temperature stability of the protein.
EC: 3.2.2.27
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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 flipped out from double-stranded DNA .
Catalytic Activity: Hydrolyzes single-stranded DNA or mismatched double-stranded DNA and polynucleotides, releasing free uracil.
Sequence Mass (Da): 22966
Sequence Length: 205
EC: 3.2.2.27
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Q0P8H3 | MKIVIVGIGYVGLANAILFSKNNENEVVLLDIDENKIQSINNHKSPIKDKLIEKFFVQNISKLHATSNIKEAYFNADFAVIATPTDYDEQLNFFDTRSIENVLKDIKNINSKINVIIKSTVPIGYTKTIKQKFNMSNIVFSPEFLREGSALYDSLYPSRIIIGDKSVLGKTIGDLFLKNIEKKNVDIFYMDSDEAESVKLFSNTYLAMRVGFFNEVDSYARKHNLNSADIIKGISADDRIGKYYNNPSFGYGGYCLPKDTKQLLANFYNIPNSLIKAIVETNEIRKKFITQLILEKKPNILGIYRLIMKQNSDNFRNSVIIDIIKYLQEYNSNIELIIYEPLVKEKKFLNIKVENDFNVFGAKVDLIIANRFDDKLKEIKDKVFSADVFYTDI | 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): 45093
Sequence Length: 393
Pathway: Nucleotide-sugar biosynthesis; UDP-alpha-D-glucuronate biosynthesis; UDP-alpha-D-glucuronate from UDP-alpha-D-glucose: step 1/1.
EC: 1.1.1.22
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O94874 | MADAWEEIRRLAADFQRAQFAEATQRLSERNCIEIVNKLIAQKQLEVVHTLDGKEYITPAQISKEMRDELHVRGGRVNIVDLQQVINVDLIHIENRIGDIIKSEKHVQLVLGQLIDENYLDRLAEEVNDKLQESGQVTISELCKTYDLPGNFLTQALTQRLGRIISGHIDLDNRGVIFTEAFVARHKARIRGLFSAITRPTAVNSLISKYGFQEQLLYSVLEELVNSGRLRGTVVGGRQDKAVFVPDIYSRTQSTWVDSFFRQNGYLEFDALSRLGIPDAVSYIKKRYKTTQLLFLKAACVGQGLVDQVEASVEEAISSGTWVDIAPLLPTSLSVEDAAILLQQVMRAFSKQASTVVFSDTVVVSEKFINDCTELFRELMHQKAEKEMKNNPVHLITEEDLKQISTLESVSTSKKDKKDERRRKATEGSGSMRGGGGGNAREYKIKKVKKKGRKDDDSDDESQSSHTGKKKPEISFMFQDEIEDFLRKHIQDAPEEFISELAEYLIKPLNKTYLEVVRSVFMSSTTSASGTGRKRTIKDLQEEVSNLYNNIRLFEKGMKFFADDTQAALTKHLLKSVCTDITNLIFNFLASDLMMAVDDPAAITSEIRKKILSKLSEETKVALTKLHNSLNEKSIEDFISCLDSAAEACDIMVKRGDKKRERQILFQHRQALAEQLKVTEDPALILHLTSVLLFQFSTHSMLHAPGRCVPQIIAFLNSKIPEDQHALLVKYQGLVVKQLVSQSKKTGQGDYPLNNELDKEQEDVASTTRKELQELSSSIKDLVLKSRKSSVTEE | 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, recruited to the endoplasmic reticulum membrane by DDRGK1, and mediates ufmylation of proteins such as RPN1 and RPL26/uL24, thereby promoting reticulophagy of endoplasmic reticulum sheets . Ufmylation-dependent reticulophagy inhibits the unfolded protein response (UPR) via ERN1/IRE1-alpha . Ufmylation in response to endoplasmic reticulum stress is essential for processes such as hematopoiesis, blood vessel morphogenesis or inflammatory response . Regulates inflammation in response to endoplasmic reticulum stress by promoting reticulophagy, leading to inhibit the activity of the NF-kappa-B transcription factor (By similarity). Mediates ufmylation of DDRGK1 and CDK5RAP3; the role of these modifications is however unclear: as both DDRGK1 and CDK5RAP3 act as substrate adapters for ufmylation, it is uncertain whether ufmylation of these proteins is a collateral effect or is required for ufmylation . Catalyzes ufmylation of various subunits of the ribosomal complex or associated components, such as RPS3/uS3, RPS20/uS10, RPL10/uL16, RPL26/uL24 and EIF6 (By similarity). Anchors CDK5RAP3 in the cytoplasm, preventing its translocation to the nucleus which allows expression of the CCND1 cyclin and progression of cells through the G1/S transition . Also involved in the response to DNA damage: recruited to double-strand break sites following DNA damage and mediates monoufmylation of histone H4 . Catalyzes ufmylation of TRIP4, thereby playing a role in nuclear receptor-mediated transcription . Required for hematopoietic stem cell function and hematopoiesis (By similarity). Required for cardiac homeostasis (By similarity).
PTM: Ubiquitinated, leading to its degradation by the proteasome . Interaction with CDK5RAP3 protects both proteins against ubiquitination and degradation via the proteasome .
Sequence Mass (Da): 89595
Sequence Length: 794
Subcellular Location: Endoplasmic reticulum membrane
EC: 2.3.2.-
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Q2K1C8 | MAPINIVDVKKNYGSVPAVKGINLAVADGEFIVLVGPSGCGKSTLLRMIAGLESITGGRVEIGGRNVNKAEPAERDIAMVFQNYALYPHMTVRGNLEYGLKNRGTARAEIDRRVKEAADILEIGPMLDRKPRELSGGQRQRVAMGRAIVREPAAFLFDEPLSNLDAKLRVQMRVEIRRLQRRLKTTSIYVTHDQLEAMTLADRLVVMNGGLVEQVGTPVEVYDRPASLFVAGFIGSPPMNLVPIEVFHATESGGTLALPEGTDMVGLRPDALLLEKPAEPSIRLNAIVELLEPIGGESHLHVRLGEGQQTIVLTVQGRPDFAESARIDVFARIDQMHPFNSRTGRRTD | 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 protein
Sequence Mass (Da): 38097
Sequence Length: 348
Subcellular Location: Cell inner membrane
EC: 7.6.2.10
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A0A067YBQ3 | MKGTIVLYPAMGRGHIVPMVELGKFLSTHHHATLSVKILLPSPPNSTTLRYITAVSAATPSITFLHLSPSQHLLRVLQTLISQSSKPKAFILDFFNHSAADVTQTLNIPTYYYFPNAASCVALMLYTPTIHHNTKNGNSSYNDTLRRIPGLPPLSPEDMPAPLLDRRSFESFANMSIQMRKSDGIIVNTFEKLENKAFLALKNGTCVSETSRSHSSTPETRKPRIFCVGPLVSNGGGEHDNDDSGCMSWLDLQPSRTVVFLSFGSYGRFSKSQIREIALGLERSGQRFLWVVRDPYERSELSLEELLPKGFLERTKERGMVVKNWAPQVKVLSHDSVGGFVTHCGWNSVLEAVSWGVPMVAWPLYAEQRLNRVVMVEEMKVALPLKEVDEDGFVRASELEERVRELMDSERGRGKEVRKRVLGATNDAVAALSDGGSSRIELNDLVGLWMQ | 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 Activity: a 7-hydroxyisoflavone + UDP-alpha-D-glucose = a 7-hydroxyisoflavone 7-O-beta-D-glucoside + H(+) + UDP
Sequence Mass (Da): 50258
Sequence Length: 451
EC: 2.4.1.170
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F8WKW0 | MVQQRHVLLITYPAQGHINPALQFAQRLLRMGIQVTLATSVYALSRMKKSSGSTPKGLTFATFSDGYDDGFRPKGVDHTEYMSSLAKQGSNTLRNVINTSADQGCPVTCLVYTLLLPWAATVARECHIPSALLWIQPVAVMDIYYYYFRGYEDDVKNNSNDPTWSIQFPGLPSMKAKDLPSFILPSSDNIYSFALPTFKKQLETLDEEERPKVLVNTFDALEPQALKAIESYNLIAIGPLTPSAFLDGKDPSETSFSGDLFQKSKDYKEWLNSRPAGSVVYVSFGSLLTLPKQQMEEIARGLLKSGRPFLWVIRAKENGEEEKEEDRLICMEELEEQGMIVPWCSQIEVLTHPSLGCFVTHCGWNSTLETLVCGVPVVAFPHWTDQGTNAKLIEDVWETGVRVVPNEDGTVESDEIKRCIETVMDDGEKGVELKRNAKKWKELAREAMQEDGSSDKNLKAFVEDAGKGYQAESN | 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-gentiobiosyl) crocetin).
Catalytic Activity: crocetin + UDP-alpha-D-glucose = beta-D-glucosyl crocetin + UDP
Sequence Mass (Da): 53008
Sequence Length: 474
Subcellular Location: Plastid
EC: 2.4.1.271
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A0A068J840 | MKSELIFLPAPAIGHLVGMVEMAKLFISRHENLSVTVLIAKFYMDTGVDNYNKSLLTNPTPRLTIVNLPETDPQNYMLKPRHAIFPSVIETQKTHVRDIISGMTQSESTQVVGLLADLLFINIMDIANEFNVPTYVYSPAGAGHLGLAFHLQTLNDKKQDVTEFRNSDTELLVPSFANPVPAEVLPSMYVDKEGGYDYLFSLFRRCRESKAIIINTFEELEPYAINSLRMDSMIPPIYPVGPILNLNGDGQNSDEAAVILGWLDDQPPSSVVFLCFGSYGSFQENQVKEIAMGLERSGHRFLWSLRPSIPKGETKLQLKYSNLKEILPVGFLDRTSCVGKVIGWAPQVAVLGHESVGGFLSHCGWNSTLESVWCGVPVATWPMYGEQQLNAFEMVKELGIAVEIEVDYKKDYFNMKNDFIVRAEEIETKIKKLMMDENNSEIRKKVKEMKEKSRAAMSENGSSYNSLAKLFEEIM | 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 of protopanaxadiol (PPD) to the ginsenoside compound K . catalyzes the production of 20S-O-beta-(D-glucosyl)-dammarenediol II form dammarenediol II (DM) .
Catalytic Activity: (20S)-protopanaxadiol + UDP-alpha-D-glucose = (20S)-ginsenoside C-K + H(+) + UDP
Sequence Mass (Da): 53374
Sequence Length: 475
Pathway: Secondary metabolite biosynthesis; terpenoid biosynthesis.
EC: 2.4.1.363
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A0A0D1CFF0 | MATEHILLVCWPAVGHARPMLDYAAAQLKQNPGLIITFICSKMQIALLEGLAISEHLADKKFGDRLRLLGTGRPAQEVLKEFGDREDAKNAANSASKAPNTTANGPEPEVILTMQAATLIQKRFAEIFPTILANDDLFDEQDNSLLLPACVAGKPTTIVVNWMLPGMVETVRKHSSDLKMVTFFDNSCTFVTRMLGPRSIGGFGGIERLWSQYCNSNPEVDPNDSTLKEKLLGRRWTGKFYIPGSRMGAIEEQEMAALAKDWLLSVPLTPSLIEIQKLVDASHTILINTHLAVEERELDYLRMVYPFKKIGILGPAMFSGFVEKGEKLAAKLLDKHINVKPAASRPLTPPETPPPGSPDTDSHGEEEDPKQKSVKQVEKFLAESATGSVVYISFGTMFRPQPTHLIKMLEIIIYEMSLSSQFRLLFTFGGSKDLASSCPPSFAPQISALESQLFKSGNTLFVNWVDQHYVLQHPSVGWFLSHGGWNSCQESMLAGTPLLILPFFGDQLFNAYFLESIQIAYRFNTAANMSVADFVASFREGITCTRPESERGSQLTKNAKELQLRLKGERALAEVRLF | 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-trihydroxypalmitic acid, which is O-glycosidically linked to cellobiose at its terminal hydroxyl group . In addition, the cellobiose moiety is acetylated and acylated with a short-chain hydroxy fatty acid . UA biosynthesis starts with omega-hydroxylation of palmitic acid catalyzed by the cytochrome P450 monooxygenase cyp1 . Terminal hydroxylation of palmitic acid precedes subterminal hydroxylation catalyzed by the cytochrome P450 monooxygenase cyp2 . Sequential glucosylation of the hydroxy fatty acid is probably catalyzed by the glycosyltransferase ugt1 (Probable). The cellobiose lipid is further decorated by acetylation of the proximal glucose residue and by acylation with a short-chain beta-hydroxy fatty acid at the distal glucose residue (Probable). The acyltransferase uat1 may be a good candidate for catalyzing either acetylation or acylation of the cellobiose lipid (Probable). The fatty acid synthase fas2 may be involved in synthesis of the carbon backbone of the short-chain beta-hydroxy fatty acid esterified to the cellobiose disaccharide (Probable). The secreted UA consists of a mixture of both alpha-hydroxylated and non-hydroxylated glycolipids; therefore, alpha-hydroxylation of the long-chain fatty, catalyzed by the fatty acid hydroxylase ahd1, occurs late in UA biosynthesis and may be the last step before secretion .
Sequence Mass (Da): 64072
Sequence Length: 578
Pathway: Secondary metabolite biosynthesis.
EC: 2.4.1.-
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A0A0A6ZFY4 | MDNQNGRISIALLPFLAHGHISPFFELAKQLAKRNCNVFLCSTPINLSSIKDKDSSASIKLVELHLPSSPDLPPHYHTTNGLPSHLMLPLRNAFETAGPTFSEILKTLNPDLLIYDFNPSWAPEIASSHNIPAVYFLTTAAASSSIGLHAFKNPGEKYPFPDFYDNSNITPEPPSADNMKLLHDFIACFERSCDIILIKSFRELEGKYIDLLSTLSDKTLVPVGPLVQDPMGHNEDPKTEQIINWLDKRAESTVVFVCFGSEYFLSNEELEEVAIGLEISTVNFIWAVRLIEGEKKGILPEGFVQRVGDRGLVVEGWAPQARILGHSSTGGFVSHCGWSSIAESMKFGVPVIAMARHLDQPLNGKLAAEVGVGMEVVRDENGKYKREGIAEVIRKVVVEKSGEVIRRKARELSEKMKEKGEQEIDRALEELVQICKKKKDEQ | 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)-ginsenoside F2 + UDP-alpha-D-glucose = (20S)-ginsenoside Rd + H(+) + UDP
Sequence Mass (Da): 49133
Sequence Length: 442
Pathway: Secondary metabolite biosynthesis; terpenoid biosynthesis.
EC: 2.4.1.365
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A0A291PQH4 | MEFRLLILALFSVLMSTSNGAEILALFPIHGISNYNVAEALLKTLANRGHNVTVVTSFPQKKPVPNLYEIDVSGAKGLATNSIHFERLQTIIQDVKSNFKNMVRLSRTYCEIMFSDPRVLNIRDKKFDLVINAVFGSDCDAGFAWKSQAPLISILNARHTPWALHRMGNPSNPAYMPVIHSRFPVKMNFFQRMINTGWHLYFLYMYFYYGNGEDANKMARKFFGNDMPDINEMVFNTSLLFVNTHFSVDMPYPLVPNCIEIGGIHVKEPQPLPLEIQKFMDEAEHGVIFFTLGSMVRTSTFPNQTIQAFKEAFAELPQRVLWKFENENEDMPSNVLIRKWFPQNDIFGHKNIKAFISHGGNSGALEAVHFGVPIIGIPLFYDQYRNILSFVKEGVAVLLDVNDLTKDNILSSVRTVVNDKSYSERMKALSQLFRDRPMSPLDTAVYWTEYVIRHRGAHHLKTAGAFLHWYQYLLLDVITFLLVTFCAFCFIVKYICKALIHHYWSSSKSEKLKKN | 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 I membrane protein
Catalytic Activity: kermesate + UDP-alpha-D-glucose = carminate + 2 H(+) + UDP
Sequence Mass (Da): 59115
Sequence Length: 515
Subcellular Location: Endoplasmic reticulum membrane
EC: 2.4.1.-
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F8WKW1 | MGSISLPEKHHAVCIPYPAQGHINPMLKLAKILHHKGFHITFVNTEFNHKRLLKSRGPDALNGLPDFQFKTIPDGLPPSDVDATQDIPSLCESTTTRCLDPFRNLLAELNGPSSSQVPPVSCIVSDGVMSFTLEAAAELGVPEILFWTTSACGFLGYMHYAKLIEKGLTPLKDASYLSNGYLEQSLDWIPGMKDIRLKDLPSFLRTTNPDDYMVKFVLQETERAKKASAIILNTFQELEDDVINALSAILPPIYTIGPLQFLQKEVKDERLSVLGSNLWKEEPECLDWLDSKDPNSVVYVNFGSITVMTPGQLVEFAWGLANSKQTFLWIIRPDLVSGDSAILPPEFLEETKDRGLLASWCPQEQVLSHPAIGGFLTHSGWNSTLESICSGVPMICWPFFAEQQTNCWFCCTKWYNGLEIDNNVKRDEVESLVTELMVGEKGMDMKKKALEWKNKAEEAAKSSGGSSYSNLEKVVQVLLSK | 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 | LVPESSLFMHQSEDYETEVYPVSFTTEEMDATHKQLKDGLFLKQPDWTEYYVNIMRFVNFTSIHLRGCENLLENQPLMSRMRGMGFDIVLTDPFFPCGALVGNIFSIPVVNFLRGLPCGLDMKVNKCPSPPSYIPVPYSGNTNIMTFPQRVINMAMTVVESYQCSLLYGHYDEMVSKYVGNNMDYRTLLSHGALWLIRNEFTLDWPRPLLPNMVLIGGINCAEKKKNASLPADLEEFVQGSGDDGFIIFTLGSMLPDMPQEKAQHFLDAFRQIPQRVVWRYAGDPPKGLPKNVRLMKWLPQKELLAHPKAKLFLTHGGSHSVYEGICNAVPMLMFPLFAEQGDNGLRMVTRGAAETLNIYDVTSDNLLAALNKILKNKSYKEKITEMSQIHHDRPVAPLDLAIFWTEFVIRHKGASHLRVAAHELNWIQYHSLDVFGFILLILLTVLWVTLKCCLFCTRRCCRRGTAKTKSE | 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 (Da): 53781
Sequence Length: 472
Subcellular Location: Microsome membrane
EC: 2.4.1.17
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Q10941 | MRLIFVLLATFVNAAFSYKILVFSPATSKSHLISNGRLADELARAGHDVTVLELDFLGISQTTNSVKVAKKRIIDGFQESTNFKNVLHGFSETVMEEPSFTDEIKGWWAYQNVYNDLCAEFLKMDDIFNELKNAKFDGFFAEQINLCGFGYAHALEIPRHFLISSCPFAAPVYDFTGLPMPTSTVAFAADLSISPTYTERARNLFVAVLTKLEFTLLNNRLQAHFQHKFGEHFPSLYSVTSDVDVIFVATDEIIDISTTTLQNIVHVGGLGVDDDVAEMDNVFASEMSKGKEGVIYFSLGTIANTTKIDSKVMRTVLDIVKKFPDYHFVIRADKYDLSTREYAKSVSNAFVSDWLPQPAILHHPRLKLFITHSGYNSIVEAARAGVPLINIPFMFDQNLNSRAVEKKGWGIRRHKKQLLTEPEEIEKAISEIIHNKKYSLKAQRIRDLIKSKPLSSSQLLIKTTEWAIKNHGLDEIKFESRGQTTWTYYNLDVIIPVFWLSISLVIPTIFGWYKFSCFGHVEEKKGKSKRD | 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 | MNQQLSWRTIVGYSLGDVANNFAFAMGALFLLSYYTDVAGVGAAAAGTMLLLVRVFDAFADVFAGRVVDSVNTRWGKFRPFLLFGTAPLMIFSVLVFWVPTDWSHGSKVVYAYLTYMGLGLCYSLVNIPYGSLATAMTQQPQSRARLGAARGIAASLTFVCLAFLIGPSIKNSSPEEMVSVYHFWTIVLAIAGMVLYFICFKSTRENVVRIVAQPSLNISLQTLKRNRPLFMLCIGALCVLISTFAVSASSLFYVRYVLNDTGLFTVLVLVQNLVGTVASAPLVPGMVARIGKKNTFLIGALLGTCGYLLFFWVSVWSLPVALVALAIASIGQGVTMTVMWALEADTVEYGEYLTGVRIEGLTYSLFSFTRKCGQAIGGSIPAFILGLSGYIANQVQTPEVIMGIRTSIALVPCGFMLLAFVIIWFYPLTDKKFKEIVVEIDNRKKVQQQLISDITN | 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 | MPRRKKKVKEVSESRNLEKKDVETTSSVSVKRKRRLEDAFIVISDSDGEEPKEENGLQKTKTKQSNRAKCLAKRKIAQMTEEEQFALALKMSEQEAREVNSQEEEEEELLRKAIAESLNSCRPSDASATRSRPLATGPSSQSHQEKTTDSGLTEGIWQLVPPSLFKGSHISQGNEAEEREEPWDHTEKTEEEPVSGSSGSWDQSSQPVFENVNVKSFDRCTGHSAEHTQCGKPQESTGRGSAFLKAVQGSGDTSRHCLPTLADAKGLQDTGGTVNYFWGIPFCPDGVDPNQYTKVILCQLEVYQKSLKMAQRQLLNKKGFGEPVLPRPPSLIQNECGQGEQASEKNECISEDMGDEDKEERQESRASDWHSKTKDFQESSIKSLKEKLLLEEEPTTSHGQSSQGIVEETSEEGNSVPASQSVAALTSKRSLVLMPESSAEEITVCPETQLSSSETFDLEREVSPGSRDILDGVRIIMADKEVGNKEDAEKEVAISTFSSSNQVSCPLCDQCFPPTKIERHAMYCNGLMEEDTVLTRRQKEAKTKSDSGTAAQTSLDIDKNEKCYLCKSLVPFREYQCHVDSCLQLAKADQGDGPEGSGRACSTVEGKWQQRLKNPKEKGHSEGRLLSFLEQSEHKTSDADIKSSETGAFRVPSPGMEEAGCSREMQSSFTRRDLNESPVKSFVSISEATDCLVDFKKQVTVQPGSRTRTKAGRGRRRKF | 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-strand breaks (DSBs). The BRCA1-A complex also possesses deubiquitinase activity that specifically removes 'Lys-63'-linked ubiquitin on histones H2A and H2AX. Also weakly binds monoubiquitin but with much less affinity than 'Lys-63'-linked ubiquitin. May interact with monoubiquitinated histones H2A and H2B; the relevance of such results is however unclear in vivo. Does not bind Lys-48'-linked ubiquitin. May indirectly act as a transcriptional repressor by inhibiting the interaction of NR6A1 with the corepressor NCOR1.
PTM: Sumoylated.
Sequence Mass (Da): 79727
Sequence Length: 719
Domain: The tandem UIM domains form a continuous 60 Angstrom-long alpha-helix and mediate binding to 'Lys-63'-linked ubiquitins. UIM1 and UIM2 bind to the proximal and distal ubiquitin moieties and recognize an 'Ile-44'-centered hydrophobic patch. Since UIMs don't interact with the 'Lys-63' isopeptide bond the UIM-linker region between the 2 UIM domains determines the selectivity for 'Lys-63'-linkage, and its length is very important for specificity.
Subcellular Location: Nucleus
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P16788 | MSSALRSRARSASLGTTTQGWDPPPLRRPSRARRRQWMREAAQAAAQAAVQAAQAAAAQVAQAHVDENEVVDLMADEAGGGVTTLTTLSSVSTTTVLGHATFSACVRSDVMRDGEKEDAASDKENLRRPVVPSTSSRGSAASGDGYHGLRCRETSAMWSFEYDRDGDVTSVRRALFTGGSDPSDSVSGVRGGRKRPLRPPLVSLARTPLCRRRVGGVDAVLEENDVELRAESQDSAVASGPGRIPQPLSGSSGEESATAVEADSTSHDDVHCTCSNDQIITTSIRGLTCDPRMFLRLTHPELCELSISYLLVYVPKEDDFCHKICYAVDMSDESYRLGQGSFGEVWPLDRYRVVKVARKHSETVLTVWMSGLIRTRAAGEQQQPPSLVGTGVHRGLLTATGCCLLHNVTVHRRFHTDMFHHDQWKLACIDSYRRAFCTLADAIKFLNHQCRVCHFDITPMNVLIDVNPHNPSEIVRAALCDYSLSEPYPDYNERCVAVFQETGTARRIPNCSHRLRECYHPAFRPMPLQKLLICDPHARFPVAGLRRYCMSELSALGNVLGFCLMRLLDRRGLDEVRMGTEALLFKHAGAACRALENGKLTHCSDACLLILAAQMSYGACLLGEHGAALVSHTLRFVEAKMSSCRVRAFRRFYHECSQTMLHEYVRKNVERLLATSDGLYLYNAFRRTTSIICEEDLDGDCRQLFPE | 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 complex (NEC) subunits UL50 and UL53 . Redistributes the host nuclear lamina by phosphorylating cellular Lamins-A/C. Plays a role in viral DNA synthesis by phosphorylating the DNA polymerase processivity factor UL44. Stimulates host cell cycle to support viral DNA synthesis by phosphorylating host retinoblastoma/RB1 protein. Additional substrates have been identified including host EF1D or H2B. Phosphorylates also host SAMHD1 and thereby counteracts its antiviral effect by reducing its dNTP hydrolase activity .
PTM: Autophosphorylates on serine and threonine residues.
Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Sequence Mass (Da): 78233
Sequence Length: 707
Subcellular Location: Virion
EC: 2.7.11.1
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D3XDS2 | MSVELTPPRSDGSVGFAPVVVPPAPRKPLRRRAVSDLEKLYKVKRRLVFGADDGAVDNDTSNNNSGSSSTTSRSRRKTAADVVSDSPKRTDDSSTAGEDGYTHCVHSCACTPGERHLLCCELVSIGDSVSVARCPLCSLGISTTYLSRGCCRGRSKVTGGDEDEEDEDEEENSQDEDRDEEEAASASSSGGLEWSDDSNSALSWSDENIIISPFPGLKCYVTTFEDIRQPVLLETGSAYLPVYVPYDESFCRNRCLERGGDDDDERDATLIGKGSFGQVWRLSDKKTALKAAASESINETLLTVWISGVVRSRAQDAGYRGELDDSVYCNILVATGSCLRHNLVSFASFDRDLYNYRGWHYAGLASYRRAFSGIADALRFLNLRCGVGHFDVTPMNVLINYDRADDRQIARAVICDFSLSQCHTEGTTGHCVVVFQQTKTVRALPKSAYYLTDIYHPAFKPLMLQKLCAIEPRKQFPKPSANRFCVSDLCALGHVAAFCLVRVLDERGQLKVRSTSEDALFGVARKTCDALARHSVDEVANFCSLLITRQLAYTATLLGSDDMREPMARLCDYFETVSDKDAPDRFRSVYKRARREIDGSYMVRLLLAASETEDGRYLLDNIRATCLMVDSEDLDVDPYKIFP | 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). Phosphorylates host SAMHD1 and thereby counteracts its antiviral effect by reducing its dNTP hydrolase activity . Inhibits host DNA synthesis by cyclin A/CDKN2A sequestration to the cytoplasm .
Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Sequence Mass (Da): 71158
Sequence Length: 643
Subcellular Location: Virion
EC: 2.7.11.1
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Q13564 | MAQLGKLLKEQKYDRQLRLWGDHGQEALESAHVCLINATATGTEILKNLVLPGIGSFTIIDGNQVSGEDAGNNFFLQRSSIGKNRAEAAMEFLQELNSDVSGSFVEESPENLLDNDPSFFCRFTVVVATQLPESTSLRLADVLWNSQIPLLICRTYGLVGYMRIIIKEHPVIESHPDNALEDLRLDKPFPELREHFQSYDLDHMEKKDHSHTPWIVIIAKYLAQWYSETNGRIPKTYKEKEDFRDLIRQGILKNENGAPEDEENFEEAIKNVNTALNTTQIPSSIEDIFNDDRCINITKQTPSFWILARALKEFVAKEGQGNLPVRGTIPDMIADSGKYIKLQNVYREKAKKDAAAVGNHVAKLLQSIGQAPESISEKELKLLCSNSAFLRVVRCRSLAEEYGLDTINKDEIISSMDNPDNEIVLYLMLRAVDRFHKQQGRYPGVSNYQVEEDIGKLKSCLTGFLQEYGLSVMVKDDYVHEFCRYGAAEPHTIAAFLGGAAAQEVIKIITKQFVIFNNTYIYSGMSQTSATFQL | 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 cysteine of UBE2M. Necessary for cell cycle progression through the S-M checkpoint. Overexpression of NAE1 causes apoptosis through deregulation of NEDD8 conjugation. The covalent attachment of NEDD8 to target proteins is known as 'neddylation' and the process is involved in the regulation of cell growth, viability and development.
PTM: Ubiquitinated by TRIP12, leading to its degradation by the proteasome.
Sequence Mass (Da): 60246
Sequence Length: 534
Pathway: Protein modification; protein neddylation.
Subcellular Location: Cell membrane
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Q9UT93 | MGTSAKMQKYDRQVRLWKAEGQNAIEKSHVCLLYANTVGCEALKNLILPGIGSFAVVDDTSVDFSMDGMNFFIQYDQEGKSRARCTASLLQQLNPNVEMEYLEMSPEALIDKNIEYFSKFSVVLSSNLKEKPLFRLEEYLRSHKIPLLHFNSVGFAGILRISTHEYTTTQSQPELPQDLRLKNPWPELINYVKSMDLDNMDSSSLSEIPYIVLIIHVLLKVSPAHAQNSQEADDCAMFRKIMEEYKGKCDSENIEEASSNSWKAFKEYKLPSNVYEVLHDTRCVKIQEDSESFWIMAHCLKMFYDETEFLPLSGLLPDMNCSTQQYVKLQVIYKEKSENDILKFKKYVQQTLKRLNRSVEEITDLEIKHFSRNCLNIKVMDFKTMKEEYQPTSNSVLESSSIDSNSLLPWYLAFRIYDTILEKHGKNYKEAFSDTTKTISVAQSFLSQIGLEKFFDVVYTAIQELERADGHELHSISSFIGGIVAQETIKLLAQQYLPLNNTFVFDGVHSRTETFKL | 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 cysteine of ubc12 (By similarity).
Sequence Mass (Da): 59569
Sequence Length: 517
Pathway: Protein modification; protein neddylation.
Subcellular Location: Cytoplasm
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Q83IJ0 | MSKVKSITRESWILSTFPEWGSWLNEEIEQEQVAPGTFAMWWLGCTGIWLKSEGGTNVCVDFWCGTGKQSHGNPLMKQGHQMQRMAGVKKLQPNLRTTPFVLDPFAIRQIDAVLATHDHNDHIDVNVAAAVMQNCADDVPFIGPKTCVDLWIGWGVPKERCIVVKPGDVVKVKDIEIHALDAFDRTALITLPADQKAAGVLPDGMDDRAVNYLFKTPGGSLYHSGDSHYSNYYAKHGNEHQIDVALGSYGENPRGITDKMTSADMLRMGEALNAKVVIPFHHDIWSNFQADPQEIRVLWEIKKDRLKYGFKPFIWQVGGKFTWPLDKDNFEYHYPRGFDDCFTIEPDLPFKSFL | 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 degradation; L-ascorbate degradation; D-xylulose 5-phosphate from L-ascorbate: step 1/4.
Subcellular Location: Cytoplasm
EC: 3.1.1.-
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P34579 | MASNRFQNLQNWTNKHVFSNSLDYWNQELNEVPSYQNQPQTGESGSNPPPHDRLEPIQESVVSEQPQKDDINKQEEAKDDGHGEASEPISALQAAWNVTNAIQGMFIVGLPIAVKVGGWWSIGAMVGVAYVCYWTGVLLIECLYENGVKKRKTYREIADFYKPGFGKWVLAAQLTELLSTCIIYLVLAADLLQSCFPSVDKAGWMMITSASLLTCSFLDDLQIVSRLSFFNAISHLIVNLIMVLYCLSFVSQWSFSTITFSLNINTLPTIVGMVVFGYTSHIFLPNLEGNMKNPAQFNVMLKWSHIAAAVFKVVFGMLGFLTFGELTQEEISNSLPNQSFKILVNLILVVKALLSYPLPFYAAVQLLKNNLFLGYPQTPFTSCYSPDKSLREWAVTLRIILVLFTLFVALSVPYLVELMGLVGNITGTMLSFIWPALFHLYIKEKTLNNFEKRFDQGIIIMGCSVCISGVYFSSMELLRAINSADS | 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 | MEQFDGFEYSKRDLLGHGAFAIVYRGRYVDRTDVPVAIKAIAKKNISKSKNLLTKEIKILKELSSLKHENLVGLLKCTETPTHVYLVMEFCNGGDLADYLQQKTTLNEDTIQHFVVQIAHALEAINKKGIVHRDLKPQNILLCNNSRTQNPHFTDIVIKLADFGFARFLNDGVMAATLCGSPMYMAPEVIMSMQYDAKADLWSIGTILFQCLTGKAPFVAQTPPQLKAYYEKTRELRPNIPEWCSPNLRDLLLRLLKRNAKDRISFEDFFNHPFLTSPLLPSPSKRILESARSPLLANRRIITPQSSLPVPKRAGSTKLDSPTPVRRIGESPRVQRRVITPGMPSPVPGAPMQESTDFTFLPPRQESSPVKQVQVHTNVSPSLTTCKPVPVPSQRLTYQKMEERLAAARKTAVPSSSSPTGSAVSAQHQHQHQQQQEPASSPVVQRIERPDQLPRRTTLQDPNAHDIERMTMPNPTFVVCGSSTKPSPNNANRVRRSTITSPADTQDMVAADQMLSNLDPTTTTTTIPKSATTANIQGIPRGARDRSVTSPPQPTIHENEPLDNAKYQQTDVNNSPTAPTEPFIIKNQTTCSTSSTSSSVVEEEEAMSLPFASGSHLAAGFKKTPAEVPMDHGALPPALDQEIVLGEEHKQILAKLRFVAELVDTLIHVAEQKDNPLASAMASRRQLLTTGTSTTNTSSPYRRAEQLVVYVRALHMLSSALLLAQTNVANRVLHPSVAVQQVLNQLNDKYHQCLVRSQELASLGLPGQDPAMAVISAERIMYRHAIELCQAAALDELFGNPQLCSQRYQTAYMMLHTLAEQVNCDQDKTVLTRYKVAVEKRLRILERQGFVAAVNT | 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 autophagosome formation . Interaction with autophagy related proteins such as atg-13 links it to the autophagy machinery to in turn promote P-granule degradation in somatic cells . Plays a role in mitophagy during limited food availability . Regulates cell size . Plays a role in male tail ray pattern formation . May be required for normal dauer morphogenesis .
Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Sequence Mass (Da): 94893
Sequence Length: 856
Domain: The LIR motif (LC3-interacting region) is required for its interaction with lgg-1.
EC: 2.7.11.1
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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
Sequence Length: 224
Subcellular Location: Cytoplasm
EC: 3.2.2.27
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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
Sequence Length: 238
Subcellular Location: Cytoplasm
EC: 3.2.2.27
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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
Sequence Length: 254
Subcellular Location: Cytoplasm
EC: 3.2.2.27
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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
Sequence Length: 229
Subcellular Location: Cytoplasm
EC: 3.2.2.27
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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
Sequence Length: 248
Subcellular Location: Cytoplasm
EC: 3.2.2.27
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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
Sequence Length: 247
Subcellular Location: Cytoplasm
EC: 3.2.2.27
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P53766 | MSGKITDFFEKKTTTTIDEAENKDNDKELTSTTTTTTTTSTTSKKKVAAAPKKKAAVASKKRKHESSDEETDKEEQQNDDDDDGEEKVENNNNNKKLKNEEKSEEINSTITDNNYYDDIENYFTDKQWKEALSGEFGKAYFKKMITQLNKRYSSKEKPIYPPKNEIFSAFNYAHLEDVKVVIIGQDPYHGKGQAHGLSFSVKKGVSPPPSLINIYKELETDIEGFKRPLKNGFLEPWARQGVFLLNAVLTVEEATPNSHKDFGWADFTDAVLKILSKQDQPIVFILWGGFAQKKEKLFTNKNHLVLKSGHPSPLSIKHFIGCKHFSKSNEFLKSKGIEEIDWKITE | 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
Sequence Length: 346
Subcellular Location: Mitochondrion
EC: 3.2.2.27
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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.
Catalytic Activity: Hydrolyzes single-stranded DNA or mismatched double-stranded DNA and polynucleotides, releasing free uracil.
Sequence Mass (Da): 28605
Sequence Length: 255
Subcellular Location: Host nucleus
EC: 3.2.2.27
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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
Sequence Length: 234
Subcellular Location: Cytoplasm
EC: 3.2.2.27
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O74834 | MTVLNTTDKRKADDTVNKLDGKLKQPRLDNFFKTNTSSPALKDTQVLDNKENNSVSKFNKEKWAENLTPAQRKLLQLEIDTLESSWFDALKDEFLKPYFLNLKEFLMKEWQSQRVFPPKEDIYSWSHHTPLHKTKVILLGQDPYHNIGQAHGLCFSVRPGIPCPPSLVNIYKAIKIDYPDFVIPKTGYLVPWADQGILMLNASLTVRAHQAASHSGKGWETFTSAVLQVALNRNRKGLVILAWGTPAAKRLQGLPLKAHYVLRSVHPSPLSAHRGFFECHHFKKTNEWLEEQYGPEKCINWSAVSEQKAKIKSSELESSSTE | 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
Sequence Length: 322
Subcellular Location: Mitochondrion
EC: 3.2.2.27
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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 apical membrane through AUM/cytoskeletal interactions.
PTM: The N-terminus is blocked.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 28902
Sequence Length: 258
Subcellular Location: Membrane
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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 apical membrane through AUM/cytoskeletal interactions (By similarity).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 28879
Sequence Length: 258
Subcellular Location: Membrane
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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 apical membrane through AUM/cytoskeletal interactions.
PTM: N-glycosylated with high-mannose oligosaccharides.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 29730
Sequence Length: 260
Subcellular Location: Membrane
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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 apical membrane through AUM/cytoskeletal interactions (By similarity).
PTM: N-glycosylated with high-mannose oligosaccharides.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 29643
Sequence Length: 260
Subcellular Location: Membrane
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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
Sequence Length: 263
Subcellular Location: Cell inner membrane
EC: 3.6.1.27
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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
Sequence Length: 294
Subcellular Location: Cell membrane
EC: 3.6.1.27
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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
Sequence Length: 294
Subcellular Location: Cell inner membrane
EC: 3.6.1.27
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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
Sequence Length: 282
Subcellular Location: Cell inner membrane
EC: 3.6.1.27
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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
Sequence Length: 266
Subcellular Location: Cell inner membrane
EC: 3.6.1.27
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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
Sequence Length: 277
Subcellular Location: Cell inner membrane
EC: 3.6.1.27
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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
Sequence Length: 281
Subcellular Location: Cell membrane
EC: 3.6.1.27
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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
Sequence Length: 270
Subcellular Location: Cell inner membrane
EC: 3.6.1.27
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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
Sequence Length: 268
Subcellular Location: Cell inner membrane
EC: 3.6.1.27
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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 Location: Cell membrane
EC: 3.6.1.27
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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
Sequence Length: 268
Subcellular Location: Cell inner membrane
EC: 3.6.1.27
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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 Location: Cell membrane
EC: 3.6.1.27
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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
Sequence Length: 281
Subcellular Location: Cell membrane
EC: 3.6.1.27
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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 Length: 209
Pathway: Pyrimidine metabolism; UMP biosynthesis via salvage pathway; UMP from uracil: step 1/1.
EC: 2.4.2.9
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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 Length: 216
Pathway: Pyrimidine metabolism; UMP biosynthesis via salvage pathway; UMP from uracil: step 1/1.
EC: 2.4.2.9
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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 Length: 214
Pathway: Pyrimidine metabolism; UMP biosynthesis via salvage pathway; UMP from uracil: step 1/1.
EC: 2.4.2.9
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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 Length: 209
Pathway: Pyrimidine metabolism; UMP biosynthesis via salvage pathway; UMP from uracil: step 1/1.
EC: 2.4.2.9
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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 Length: 210
Pathway: Pyrimidine metabolism; UMP biosynthesis via salvage pathway; UMP from uracil: step 1/1.
EC: 2.4.2.9
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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 Length: 209
Pathway: Pyrimidine metabolism; UMP biosynthesis via salvage pathway; UMP from uracil: step 1/1.
EC: 2.4.2.9
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A8L7B0 | MSELERSRYATLYGPTVGDRIRLADTDLFIEVTDDLSRGPGGTATGDEAVFGGGKVIRESMGQARATRAQGAPDLVITGAVVLDHWGVVKADVGIRDGRISALGKAGNPDTMDGVHPDLVIGPGTEIIAGNGKILTAGAVDTHVHFICPQQVPEALGTGVTTLIGGGTGPAEGTKATTVTASPWNLHRMMSAMDGWPVNVALLGKGNTVSEDAMWEQLRAGAAGFKLHEDWGTTPAAIDACLRVADASGVQVALHSDTLNEAGFVEDTLAAIAGRAIHAYHTEGAGGGHAPDIITVASFANILPSSTNPTRPHTVNTLDEHLDMLMVCHHLNPSVPEDLAFAESRIRPSTIAAEDILHDLGAISMIGSDSQAMGRVGEVVTRTWQTAHVMKRRRGALPGDTVADNNRARRYVAKYTICPAVAHGLDAEIGSVEAGKLADLVLYEPAFFGVRPSLVLKGGFIAWAAMGDANASIPTPQPVLPRPMFGAAPGPAAASSLMFVAPAALQDGLDERLGLAKPMVATADVRRRGKADLPENTATPDIRVDPDTFTVRIDGEAVEAAPAAELPMAQRYFLF | 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.
Subcellular Location: Cytoplasm
EC: 3.5.1.5
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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
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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
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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
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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
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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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Subsets and Splits