ids stringlengths 6 10 | seqs stringlengths 11 1.02k | texts stringlengths 108 11.1k |
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Q9JKU1 | MMEGHILFFFLVVMVQFVTGVLANGLIVVVHAIDLIMWKKMAPLDLLLFCLATSRIILQLCILFAQLCLFSLVRHTLFEDNITFVFIINELSLWFATWLGVFYCAKIATIPHPLFLWLKMRISRLVPWLILGSVLYVIITTFIHSRETSAILKPIFISLFPKNATQVGTGHATLLSVLVLGLTLPLFIFTVAVLLLIYSLWNYSRQMRTMVGTREYSGHAHISAMLSILSFLILYLSHYMVAVLISTQVLYLGSRTFVFCLLVIGMYPSIHSIVLILGNPKLKRNAKMFIVHCKCCHCTRAWVTSRSPRLSDLPVPPTHPSANKTSCSEACIMPS | Function: Gustducin-coupled receptor implicated in the perception of bitter compounds in the oral cavity and the gastrointestinal tract. Signals through PLCB2 and the calcium-regulated cation channel TRPM5.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 37852
Sequence Length: 335
Subcellular Location: Membrane
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O00300 | MNNLLCCALVFLDISIKWTTQETFPPKYLHYDEETSHQLLCDKCPPGTYLKQHCTAKWKTVCAPCPDHYYTDSWHTSDECLYCSPVCKELQYVKQECNRTHNRVCECKEGRYLEIEFCLKHRSCPPGFGVVQAGTPERNTVCKRCPDGFFSNETSSKAPCRKHTNCSVFGLLLTQKGNATHDNICSGNSESTQKCGIDVTLCEEAFFRFAVPTKFTPNWLSVLVDNLPGTKVNAESVERIKRQHSSQEQTFQLLKLWKHQNKDQDIVKKIIQDIDLCENSVQRHIGHANLTFEQLRSLMESLPGKKVGAEDIEKTIKACKPSDQILKLLSLWRIKNGDQDTLKGLMHALKHSKTYHFPKTVTQSLKKTIRFLHSFTMYKLYQKLFLEMIGNQVQSVKISCL | Function: Acts as decoy receptor for TNFSF11/RANKL and thereby neutralizes its function in osteoclastogenesis. Inhibits the activation of osteoclasts and promotes osteoclast apoptosis in vitro. Bone homeostasis seems to depend on the local ratio between TNFSF11 and TNFRSF11B. May also play a role in preventing arterial calcification. May act as decoy receptor for TNFSF10/TRAIL and protect against apoptosis. TNFSF10/TRAIL binding blocks the inhibition of osteoclastogenesis.
PTM: N-glycosylated. Contains sialic acid residues.
Sequence Mass (Da): 46026
Sequence Length: 401
Subcellular Location: Secreted
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Q7M721 | MNLVEWIVTIIMMTEFLLGNCANVFITIVNFIDCVKRRKISSADRIITAIAIFRIGLLWAMLTNWHSHVFTPDTDNLQMRVFGGITWAITNHFTTWLGTILSMFYLFKIANFSNSLFLHLKRKLDNVLLVIFLGSSLFLVAYLGMVNIKKIAWMSIHEGNVTTKSKLKHVTSITNMLLFSLINIVPFGISLNCVLLLIYSLSKHLKNMKFYGKGCQDQSTMVHIKALQTVVSFLLLYATYSSCVIISGWSLQNAPVFLFCVTIGSFYPAGHSCILIWGNQKLKQVFLLLLRQMRC | Function: Putative taste receptor which may play a role in the perception of bitterness.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 33594
Sequence Length: 295
Subcellular Location: Membrane
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Q61382 | MPGFDYKFLEKPKRRLLCPLCGKPMREPVQVSTCGHRFCDTCLQEFLSEGVFKCPEDQLPLDYAKIYPDPELEVQVLGLAIRCIHSEEGCRWSGPLRHLQGHLNTCSFNVVPCPNRCPAKLSRRDLPAHLQHDCPKRRLKCEFCGCDFSGEAYESHEGVCPQESVYCENKCGARMMRRLLAQHATSECPKRTQPCAYCTKEFVYDTIQSHQYQCPRLPVPCPNQCGVGTVAREDLPTHLKDSCSTAFVLCPFKESGCKHRCPKLAMGRHVEESVKPHLAMMCALVSRQRQELQELRRELEELSIGSDGVLIWKIGSYGRRLQEAKAKPNLECFSPAFYTHKYGYKLQVSAFLNGNGSGEGTHLSIYIRVLPGAFDNLLEWPFARRVTFSLLDQSDPGLAKPQHVTETFHPDPNWKNFQKPGTWRGSLDESSLGFGYPKFISHQDIRKRNYVRDDAVFIRASVELPRKILS | Function: Adapter protein with E3 ligase activity that is involved in many diverse biological processes including cell proliferation, migration, differentiation, DNA repair, platelet activation or apoptosis. Promotes EGFR-mediated signaling by facilitating the dimerization of EGFR and downstream AKT activation thereby promoting cell proliferation. Ubiquitinates SMURF2 through 'Lys-48'-linked ubiquitin chain leading to SMURF2 degradation through the proteasome and subsequently osteogenic differentiation. Promotes 'Lys-63'-mediated ubiquitination of CHK1 which in turn activates cell cycle arrest and activation of DNA repair. In addition, promotes an atypical 'Lys-29'-linked ubiquitination at the C-terminal end of IRS1 which is crucial for insulin-like growth factor (IGF) signal transduction (By similarity). Regulates activation of NF-kappa-B in response to signaling through Toll-like receptors. Required for normal skeleton development, and for normal development of the respiratory tract. Required for activation of RPS6KB1 in response to TNF signaling. Modulates TRAF6 functions. Inhibits adipogenic differentiation by activating pyruvate kinase PKM activity and subsequently the beta-catenin signaling pathway (By similarity).
PTM: Polyubiquitinated, leading to its proteasomal degradation (By similarity). Ubiquitinated at Lys-263 by the SCF(FBXL2) complex, leading to its degradation by the proteasome .
Location Topology: Peripheral membrane protein
Catalytic Activity: S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.
Sequence Mass (Da): 53504
Sequence Length: 470
Domain: The coiled coil domain mediates homo- and hetero-oligomerization.
Pathway: Protein degradation; proteasomal ubiquitin-dependent pathway.
Subcellular Location: Cytoplasm
EC: 2.3.2.27
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O00463 | MAYSEEHKGMPCGFIRQNSGNSISLDFEPSIEYQFVERLEERYKCAFCHSVLHNPHQTGCGHRFCQHCILSLRELNTVPICPVDKEVIKSQEVFKDNCCKREVLNLYVYCSNAPGCNAKVILGRYQDHLQQCLFQPVQCSNEKCREPVLRKDLKEHLSASCQFRKEKCLYCKKDVVVINLQNHEENLCPEYPVFCPNNCAKIILKTEVDEHLAVCPEAEQDCPFKHYGCAVTDKRRNLQQHEHSALREHMRLVLEKNVQLEEQISDLHKSLEQKESKIQQLAETIKKLEKEFKQFAQLFGKNGSFLPNIQVFASHIDKSAWLEAQVHQLLQMVNQQQNKFDLRPLMEAVDTVKQKITLLENNDQRLAVLEEETNKHDTHINIHKAQLSKNEERFKLLEGTCYNGKLIWKVTDYKMKKREAVDGHTVSIFSQSFYTSRCGYRLCARAYLNGDGSGRGSHLSLYFVVMRGEFDSLLQWPFRQRVTLMLLDQSGKKNIMETFKPDPNSSSFKRPDGEMNIASGCPRFVAHSVLENAKNAYIKDDTLFLKVAVDLTDLEDL | Function: Adapter protein and signal transducer that links members of the tumor necrosis factor receptor family to different signaling pathways by association with the receptor cytoplasmic domain and kinases. Mediates activation of NF-kappa-B and probably JNK. Seems to be involved in apoptosis. Plays a role in mediating activation of NF-kappa-B by EIF2AK2/PKR.
PTM: Ubiquitinated at Lys-318 by the SCF(FBXL2) complex, leading to its degradation by the proteasome.
Sequence Mass (Da): 64406
Sequence Length: 557
Domain: The MATH/TRAF domain binds to receptor cytoplasmic domains.
Subcellular Location: Cytoplasm
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P70191 | MAHSEEQAAVPCAFIRQNSGNSISLDFEPDTEYQFVEQLEERYKCAFCHSVLHNPHQTGCGHRFCQQCIRSLRELNSVPICPVDKEVIKPQEVFKDNCCKREVLNLHVYCKNAPGCNARIILGRFQDHLQHCSFQAVPCPNESCREAMLRKDVKEHLSAYCRFREEKCLYCKRDIVVTNLQDHEENSCPAYPVSCPNRCVQTIPRARVNEHLTVCPEAEQDCPFKHYGCTVKGKRGNLLEHERAALQDHMLLVLEKNYQLEQRISDLYQSLEQKESKIQQLAETVKKFEKELKQFTQMFGRNGTFLSNVQALTSHTDKSAWLEAQVRQLLQIVNQQPSRLDLRSLVDAVDSVKQRITQLEASDQRLVLLEGETSKHDAHINIHKAQLNKNEERFKQLEGACYSGKLIWKVTDYRVKKREAVEGHTVSVFSQPFYTSRCGYRLCARAYLNGDGSGKGTHLSLYFVVMRGEFDSLLQWPFRQRVTLMLLDQSGKKNHIVETFKADPNSSSFKRPDGEMNIASGCPRFVSHSTLENSKNTYIKDDTLFLKVAVDLTDLEDL | Function: Adapter protein and signal transducer that links members of the tumor necrosis factor receptor family to different signaling pathways by association with the receptor cytoplasmic domain and kinases. Mediates activation of NF-kappa-B and probably JNK. Seems to be involved in apoptosis. Plays a role in mediating activation of NF-kappa-B by EIF2AK2/PKR.
PTM: Ubiquitinated at Lys-318 by the SCF(FBXL2) complex, leading to its degradation by the proteasome.
Sequence Mass (Da): 64145
Sequence Length: 558
Domain: The MATH/TRAF domain binds to receptor cytoplasmic domains.
Subcellular Location: Cytoplasm
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Q6IWL4 | MACNDVDKSSFDDVCCDSGHSSCAAAMEKERESFLSPTENPSTISVSSSMPPDQQGYDVEFDPPLESKYECPICLMGLRSAVQTPCGHRFCDSCIRKSIRDTGQKCPVDNEVLLEEQLFPDNFAKREILSLTVKCSNFGCSEKMELRQLEKHLSQCRFATAPCPQCQESVPISHLDEHKSQHCLQRIMTCPDCAGSFVYAVKQNHEQFCPFANTVCEYCEMELIRDQLALHCDTDCLKAPVACTFSTFGCREKMTRNELAQHMQEFTQMHMRYMAEFLRSQTLNNCTMPSAAAHLSSDDRGASARSPDSCQCKQELLNLRETVLELEGRLVRQDQQIRELCIHNDTQKNQVTELRRKLVSLEESTRELEAQQYQGIYVWRVENFSHHLRNQEAGQPIVLHSPPFYTGRPGYKLCLRLHLQTPSAPRCSNFISLFVHTMQGEFDSQLSWPLQGTIRLAVLDQVEGQHHIEVMETKPDLQAFQRPTVMRNPKGFGYVTFLHLQALRQRGFVKEDVLLVRCEVTPRFDASLRREGVQPRGPEPSI | Function: E3 ubiquitin ligase that, together with UBE2N and UBE2V1, mediates the synthesis of 'Lys-63'-linked-polyubiquitin chains conjugated to proteins, such as IKBKG, IRAK1, AKT1 and AKT2. Also mediates ubiquitination of free/unanchored polyubiquitin chain that leads to MAP3K7 activation.
Catalytic Activity: S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.
Sequence Mass (Da): 61806
Sequence Length: 542
Domain: The coiled coil domain mediates homo- and hetero-oligomerization.
Pathway: Protein modification; protein ubiquitination.
Subcellular Location: Cytoplasm
EC: 2.3.2.27
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Q9Y4K3 | MSLLNCENSCGSSQSESDCCVAMASSCSAVTKDDSVGGTASTGNLSSSFMEEIQGYDVEFDPPLESKYECPICLMALREAVQTPCGHRFCKACIIKSIRDAGHKCPVDNEILLENQLFPDNFAKREILSLMVKCPNEGCLHKMELRHLEDHQAHCEFALMDCPQCQRPFQKFHINIHILKDCPRRQVSCDNCAASMAFEDKEIHDQNCPLANVICEYCNTILIREQMPNHYDLDCPTAPIPCTFSTFGCHEKMQRNHLARHLQENTQSHMRMLAQAVHSLSVIPDSGYISEVRNFQETIHQLEGRLVRQDHQIRELTAKMETQSMYVSELKRTIRTLEDKVAEIEAQQCNGIYIWKIGNFGMHLKCQEEEKPVVIHSPGFYTGKPGYKLCMRLHLQLPTAQRCANYISLFVHTMQGEYDSHLPWPFQGTIRLTILDQSEAPVRQNHEEIMDAKPELLAFQRPTIPRNPKGFGYVTFMHLEALRQRTFIKDDTLLVRCEVSTRFDMGSLRREGFQPRSTDAGV | Function: E3 ubiquitin ligase that, together with UBE2N and UBE2V1, mediates the synthesis of 'Lys-63'-linked-polyubiquitin chains conjugated to proteins, such as ECSIT, IKBKG, IRAK1, AKT1 and AKT2 . Also mediates ubiquitination of free/unanchored polyubiquitin chain that leads to MAP3K7 activation . Leads to the activation of NF-kappa-B and JUN . Seems to also play a role in dendritic cells (DCs) maturation and/or activation (By similarity). Represses c-Myb-mediated transactivation, in B-lymphocytes . Adapter protein that seems to play a role in signal transduction initiated via TNF receptor, IL-1 receptor and IL-17 receptor . Regulates osteoclast differentiation by mediating the activation of adapter protein complex 1 (AP-1) and NF-kappa-B, in response to RANK-L stimulation (By similarity). Together with MAP3K8, mediates CD40 signals that activate ERK in B-cells and macrophages, and thus may play a role in the regulation of immunoglobulin production (By similarity). Participates also in the TCR signaling by ubiquitinating LAT .
PTM: Sumoylated on Lys-124, Lys-142 and Lys-453 with SUMO1.
Catalytic Activity: S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.
Sequence Mass (Da): 59573
Sequence Length: 522
Domain: The coiled coil domain mediates homo- and hetero-oligomerization.
Pathway: Protein modification; protein ubiquitination.
Subcellular Location: Cytoplasm
EC: 2.3.2.27
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Q6Q0C0 | MSSGKSARYNRFSGGPSNLPTPDVTTGTRMETTFGPAFSAVTTITKADGTSTYKQHCRTPSSSSTLAYSPRDEEDSMPPISTPRRSDSAISVRSLHSESSMSLRSTFSLPEEEEEPEPLVFAEQPSVKLCCQLCCSVFKDPVITTCGHTFCRRCALKSEKCPVDNVKLTVVVNNIAVAEQIGELFIHCRHGCRVAGSGKPPIFEVDPRGCPFTIKLSARKDHEGSCDYRPVRCPNNPSCPPLLRMNLEAHLKECEHIKCPHSKYGCTFIGNQDTYETHLETCRFEGLKEFLQQTDDRFHEMHVALAQKDQEIAFLRSMLGKLSEKIDQLEKSLELKFDVLDENQSKLSEDLMEFRRDASMLNDELSHINARLNMGILGSYDPQQIFKCKGTFVGHQGPVWCLCVYSMGDLLFSGSSDKTIKVWDTCTTYKCQKTLEGHDGIVLALCIQGCKLYSGSADCTIIVWDIQNLQKVNTIRAHDNPVCTLVSSHNVLFSGSLKAIKVWDIVGTELKLKKELTGLNHWVRALVAAQSYLYSGSYQTIKIWDIRTLDCIHVLQTSGGSVYSIAVTNHHIVCGTYENLIHVWDIESKEQVRTLTGHVGTVYALAVISTPDQTKVFSASYDRSLRVWSMDNMICTQTLLRHQGSVTALAVSRGRLFSGAVDSTVKVWTC | Function: E3 ubiquitin ligase capable of auto-ubiquitination, following phosphorylation by MAP3K3. Potentiates MAP3K3-mediated activation of the NF-kappa-B, JUN/AP1 and DDIT3 transcriptional regulators . Induces apoptosis when overexpressed . Plays a role in the phosphorylation of MAPK1 and/or MAPK3, probably via its interaction with MAP3K3.
PTM: Phosphorylated by MAP3K3.
Catalytic Activity: S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.
Sequence Mass (Da): 74609
Sequence Length: 670
Pathway: Protein modification; protein ubiquitination.
Subcellular Location: Cytoplasmic vesicle
EC: 2.3.2.27
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A0A481WQD3 | MTSGTEQATLNTEENGSDSDHLSKEPIAMPALDWDGPTDSNNPRNFSTPKKVFITACLASLVCISTFGSSVMSPASGQLIHEFGISKELSILATALYVLGFAVGPLLFGPASEVLGRKYPLSVGVFLFAIFSIPIAVAKNVATIFVCRFLCGTFAAAPLAIAGGGLADLWEPLSRGIAVAGFASATFLGPVLGPLVGGFVTKSHLGWRWTQWLSIIFSLVFLAIYFVFCPETYSPIVLARLAKKRGQMPPGGKVDFKQLAKVYMLRPFIMLVQEPILALLTLYMGFIYGFLYLCFEAFPIAFEEHRGWDIGIGSLPFLSITVGVLIGVVIIIVHTMTRMRRKLETVGDAPEERLVPMMIGSILMPAGIFWFAWTSNTSLPWAPQVVSGVFIGCGILLIFLQGMNYIIDVYKVMANSAISINAMFRGLLGAGFPLFASYMFDNLGVPWAMSLLGFLCVALVPVPFLFFIYGERIRKWSKFTAH | Function: MFS-type transporter; part of the tra gene cluster that produces terrestric acid . The clavatol biosynthesis cluster cla and the terrestric acid cluster tra are both involved in the production of peniphenones and penilactones .
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 52532
Sequence Length: 482
Subcellular Location: Membrane
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P02788 | MKLVFLVLLFLGALGLCLAGRRRSVQWCAVSQPEATKCFQWQRNMRKVRGPPVSCIKRDSPIQCIQAIAENRADAVTLDGGFIYEAGLAPYKLRPVAAEVYGTERQPRTHYYAVAVVKKGGSFQLNELQGLKSCHTGLRRTAGWNVPIGTLRPFLNWTGPPEPIEAAVARFFSASCVPGADKGQFPNLCRLCAGTGENKCAFSSQEPYFSYSGAFKCLRDGAGDVAFIRESTVFEDLSDEAERDEYELLCPDNTRKPVDKFKDCHLARVPSHAVVARSVNGKEDAIWNLLRQAQEKFGKDKSPKFQLFGSPSGQKDLLFKDSAIGFSRVPPRIDSGLYLGSGYFTAIQNLRKSEEEVAARRARVVWCAVGEQELRKCNQWSGLSEGSVTCSSASTTEDCIALVLKGEADAMSLDGGYVYTAGKCGLVPVLAENYKSQQSSDPDPNCVDRPVEGYLAVAVVRRSDTSLTWNSVKGKKSCHTAVDRTAGWNIPMGLLFNQTGSCKFDEYFSQSCAPGSDPRSNLCALCIGDEQGENKCVPNSNERYYGYTGAFRCLAENAGDVAFVKDVTVLQNTDGNNNEAWAKDLKLADFALLCLDGKRKPVTEARSCHLAMAPNHAVVSRMDKVERLKQVLLHQQAKFGRNGSDCPDKFCLFQSETKNLLFNDNTECLARLHGKTTYEKYLGPQYVAGITNLKKCSTSPLLEACEFLRK | Function: Transferrins are iron binding transport proteins which can bind two Fe(3+) ions in association with the binding of an anion, usually bicarbonate.
PTM: Phosphorylation at Ser-10 activates the transcriptional activity . Phosphorylation at Ser-10 also promotes proteasomal degradation . Alternatively can undergo O-GlcNAcylation at Ser-10 .
Sequence Mass (Da): 78182
Sequence Length: 710
Subcellular Location: Secreted
EC: 3.4.21.-
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Q9VTZ5 | MASSLVFVALVGALCFTLANAQHHYDEHKTTRMVWCTKSQAEQYKCQNLTVAIERDRALFDEVFLNLTCFMAYSADECIHHIDREKAHITTLDAGDVFTAGRYNSLIPIMQEKLEGGFADYQSVAVIKKGSLPDLNNLRDMRNKRVCFPWVGSLAGWIVPIHTLQREGGMEVVDCNNQVKTAASYFNNSCAVYSLSDKHNPIGDNSDKLCTLCTGKIPGGRCSSADPYFGYEGAFKCLLEKGDVAFLRHSTVNEMLQTTEFKNIAPDTFELLCRDGRRASINDYRQCNWGQVPADAIVTSSARSFSDRKQYQQFLKRIAELYSDGTRDDQSRQGGQSFNSRNNINDQNAYGQFDNNDPYRTQNQYDQYRSERLDSSFAEERNQQDGTNTSILYEKFRIFESKRYGKPNLLFQDSSRALTVIPEDDQSFTKYLGPAINFIYGIRECPVPAMTLCVTSENELDKCIKMRTALKAHLLKPELICKKMHSHINCMQFIEAGKADISVFDAGDVYTGGLNYDLVPFMSEVYNLGEPEYYVVAVAKEDDPDTELTYLKGKNTCHTGINTAAGWTYPMALFISNGWIRPYGCDSVRAAAEYFTKSCVPGAISNEYNTGVPYDSMCDLCHGTSYRYCRRDASEEYYGHTGAFRCLVEGGGHVAFMKHTTVMESTGGKRKEWWARNALNDDFELLCTDGTRAEIQDYKRCNLGKVKANAVVTRGGVNYNETQMNAYINLLTYAQQLYGRKEVDAFSFSMFSSPIGHYDLIFQDATRQLQVIPPNKRRYDAYLGSDFMRARRITDCYAGASQLALSVGLLLVGSLVAML | Function: Iron-binding protein and component of septate junctions that form the paracellular permeability barrier in epithelial tissues . In an iron-dependent manner, required for septate junction assembly during epithelial maturation in embryos and mature septa junctions stability .
Location Topology: Lipid-anchor
Sequence Mass (Da): 92325
Sequence Length: 819
Subcellular Location: Apicolateral cell membrane
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P08582 | MRGPSGALWLLLALRTVLGGMEVRWCATSDPEQHKCGNMSEAFREAGIQPSLLCVRGTSADHCVQLIAAQEADAITLDGGAIYEAGKEHGLKPVVGEVYDQEVGTSYYAVAVVRRSSHVTIDTLKGVKSCHTGINRTVGWNVPVGYLVESGRLSVMGCDVLKAVSDYFGGSCVPGAGETSYSESLCRLCRGDSSGEGVCDKSPLERYYDYSGAFRCLAEGAGDVAFVKHSTVLENTDGKTLPSWGQALLSQDFELLCRDGSRADVTEWRQCHLARVPAHAVVVRADTDGGLIFRLLNEGQRLFSHEGSSFQMFSSEAYGQKDLLFKDSTSELVPIATQTYEAWLGHEYLHAMKGLLCDPNRLPPYLRWCVLSTPEIQKCGDMAVAFRRQRLKPEIQCVSAKSPQHCMERIQAEQVDAVTLSGEDIYTAGKTYGLVPAAGEHYAPEDSSNSYYVVAVVRRDSSHAFTLDELRGKRSCHAGFGSPAGWDVPVGALIQRGFIRPKDCDVLTAVSEFFNASCVPVNNPKNYPSSLCALCVGDEQGRNKCVGNSQERYYGYRGAFRCLVENAGDVAFVRHTTVFDNTNGHNSEPWAAELRSEDYELLCPNGARAEVSQFAACNLAQIPPHAVMVRPDTNIFTVYGLLDKAQDLFGDDHNKNGFKMFDSSNYHGQDLLFKDATVRAVPVGEKTTYRGWLGLDYVAALEGMSSQQCSGAAAPAPGAPLLPLLLPALAARLLPPAL | Function: Involved in iron cellular uptake. Seems to be internalized and then recycled back to the cell membrane. Binds a single atom of iron per subunit. Could also bind zinc.
Location Topology: Lipid-anchor
Sequence Mass (Da): 80215
Sequence Length: 738
Subcellular Location: Cell membrane
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Q9R0R1 | MRLLSVTFWLLLSLRTVVCVMEVQWCTISDAEQQKCKDMSEAFQGAGIRPSLLCVQGNSADHCVQLIKEQKADAITLDGGAIYEAGKEHGLKPVVGEVYDQDIGTSYYAVAVVRRNSNVTINTLKGVKSCHTGINRTVGWNVPVGYLVESGHLSVMGCDVLKAVGDYFGGSCVPGTGETSHSESLCRLCRGDSSGHNVCDKSPLERYYDYSGAFRCLAEGAGDVAFVKHSTVLENTDGNTLPSWGKSLMSEDFQLLCRDGSRADITEWRRCHLAKVPAHAVVVRGDMDGGLIFQLLNEGQLLFSHEDSSFQMFSSKAYSQKNLLFKDSTLELVPIATQNYEAWLGQEYLQAMKGLLCDPNRLPHYLRWCVLSAPEIQKCGDMAVAFSRQNLKPEIQCVSAESPEHCMEQIQAGHTDAVTLRGEDIYRAGKVYGLVPAAGELYAEEDRSNSYFVVAVARRDSSYSFTLDELRGKRSCHPYLGSPAGWEVPIGSLIQRGFIRPKDCDVLTAVSQFFNASCVPVNNPKNYPSALCALCVGDEKGRNKCVGSSQERYYGYSGAFRCLVEHAGDVAFVKHTTVFENTNGHNPEPWASHLRWQDYELLCPNGARAEVDQFQACNLAQMPSHAVMVRPDTNIFTVYGLLDKAQDLFGDDHNKNGFQMFDSSKYHSQDLLFKDATVRAVPVREKTTYLDWLGPDYVVALEGMLSQQCSGAGAAVQRVPLLALLLLTLAAGLLPRVL | Function: Involved in iron cellular uptake. Seems to be internalized and then recycled back to the cell membrane. Binds a single atom of iron per subunit. Could also bind zinc.
Location Topology: Lipid-anchor
Sequence Mass (Da): 81293
Sequence Length: 738
Subcellular Location: Cell membrane
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O97490 | MRCRSAAMWIFLALRTALGSVEVRWCTASEPEQQKCEDMSQAFREAGLQPALLCVQGTSADHCVQLIAAHEADAITLDGGAIYEAGKEHGLKPVVGEVYDQEVGTSYYAVAVVKRSSNVTINTLRGVKSCHTGINRTVGWNVPVGYLVDSGRLSVMGCDVLKAVSEYFGGSCVPGAGETRYSESLCRLCRGDTSGEGVCDKSPLERYYDYSGAFRCLAEGAGDVAFVKHSTVLENTDGRTLPSWGHMLMSRDFELLCRDGSRASVTEWQHCHLARVPAHAVVVRADTDAGLIFRLLNEGQRLFSHEGSSFQMFSSEAYGQKNLLFKDSTLELVPIATQTYEAWLGPEYLHAMKGLLCDPNRLPPYLRWCVLSTPEIQKCGDMAVAFSRQRLKPEIQCVSAESPQHCMEQIQAGHIDAVTLNGEDIHTAGKTYGLIPAAGELYAADDRSNSYFVVAVVKRDSAYAFTVDELRGKRSCHPGFGSPAGWDVPVGALIHWGYIRPRNCDVLTAVGQFFNASCVPVNNPKKYPSSLCALCVGDEQGRNKCTGNSQERYYGDSGAFRCLVEGAGDVAFVKHTTIFDNTNGHNPEPWAAHLRSQDYELLCPNGARAEAHQFAACNLAQIPSHAVMVRPDTNIFTVYGLLDKAQDLFGDDHNKNGFKMFDSSSYHGRDLLFKDATVRAVPVGERTTYQDWLGPDYVAALEGMQSQRCSGAAVGAPGASLLPLLPLAVGLLLSSL | Function: Involved in iron cellular uptake. Seems to be internalized and then recycled back to the cell membrane. Binds a single atom of iron per subunit. Could also bind zinc (By similarity).
Location Topology: Lipid-anchor
Sequence Mass (Da): 80170
Sequence Length: 736
Subcellular Location: Cell membrane
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P34981 | MENETVSELNQTQLQPRAVVALEYQVVTILLVLIICGLGIVGNIMVVLVVMRTKHMRTPTNCYLVSLAVADLMVLVAAGLPNITDSIYGSWVYGYVGCLCITYLQYLGINASSCSITAFTIERYIAICHPIKAQFLCTFSRAKKIIIFVWAFTSLYCMLWFFLLDLNISTYKDAIVISCGYKISRNYYSPIYLMDFGVFYVVPMILATVLYGFIARILFLNPIPSDPKENSKTWKNDSTHQNTNLNVNTSNRCFNSTVSSRKQVTKMLAVVVILFALLWMPYRTLVVVNSFLSSPFQENWFLLFCRICIYLNSAINPVIYNLMSQKFRAAFRKLCNCKQKPTEKPANYSVALNYSVIKESDHFSTELDDITVTDTYLSATKVSFDDTCLASEVSFSQS | Function: Receptor for thyrotropin-releasing hormone (TRH). Upon ligand binding, this G-protein-coupled receptor triggers activation of the phosphatidylinositol (IP3)-calcium-protein kinase C (PKC) pathway.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 45085
Sequence Length: 398
Subcellular Location: Cell membrane
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Q9BVG3 | MACSLKDELLCSICLSIYQDPVSLGCEHYFCRRCITEHWVRQEAQGARDCPECRRTFAEPALAPSLKLANIVERYSSFPLDAILNARRAARPCQAHDKVKLFCLTDRALLCFFCDEPALHEQHQVTGIDDAFDELQRELKDQLQALQDSEREHTEALQLLKRQLAETKSSTKSLRTTIGEAFERLHRLLRERQKAMLEELEADTARTLTDIEQKVQRYSQQLRKVQEGAQILQERLAETDRHTFLAGVASLSERLKGKIHETNLTYEDFPTSKYTGPLQYTIWKSLFQDIHPVPAALTLDPGTAHQRLILSDDCTIVAYGNLHPQPLQDSPKRFDVEVSVLGSEAFSSGVHYWEVVVAEKTQWVIGLAHEAASRKGSIQIQPSRGFYCIVMHDGNQYSACTEPWTRLNVRDKLDKVGVFLDYDQGLLIFYNADDMSWLYTFREKFPGKLCSYFSPGQSHANGKNVQPLRINTVRI | Function: E3 ubiquitin ligase that plays a role in antifungal immunity by mediating 'Lys-27'-linked ubiquitination of CARD9 downstream of C-type lectin receptors; leading to CARD9 activation, followed by activation of NF-kappa-B and MAP kinase p38 pathways . E3 ubiquitin ligase activity is dependent on E2 ubiquitin-conjugating enzyme UBE2D2 .
PTM: Polyubiquitinated, autoubiquitinated in the presence of UBE2D2.
Catalytic Activity: S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.
Sequence Mass (Da): 54268
Sequence Length: 475
Domain: The RING finger is required for ubiquitin ligase activity.
Pathway: Protein modification; protein ubiquitination.
Subcellular Location: Cytoplasm
EC: 2.3.2.27
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Q80V85 | MACSLKDELLCSICLSIYQDPVSLGCEHYFCRRCITEHWVRQEAQGARDCPECRRTFAEPALAPSLKLANIVERYSAFPLDAILNARRAARPCQAHDKVKLFCLTDRALLCFFCDEPALHEQHQVTGIDDAFEELQRELKEQLQALQDSEREHTEALQLLKRQLAETKSSTKSLRTTIGEAFERLHRLLRERQKAMLEELEADTARTLTDIEQKVQRYSQQLRKVQEGAQILQERLAETDRHTFLAGVASLSERLKGKIHETNLTYEDFPTSKYTGPLQYTIWKSLFQDIHPVPAALTMDPGTAHQRLILSDDCTIVAYGNLHPQPLQDSPKRFDVEVSVLGSEAFSSGVHYWEVVVAEKTQWVIGLAHEAASRKGSIQIQPSRGFYCIVMHDGNQYSACTEPWTRLNVRDKLDKVGVFLDYDQGLLIFYNADDMSWLYTFREKFPGKLCSYFSPGQSHANGKNVQPLRINTVRI | Function: E3 ubiquitin ligase that plays a role in antifungal immunity by mediating 'Lys-27'-linked ubiquitination of CARD9 downstream of C-type lectin receptors; leading to CARD9 activation, followed by activation of NF-kappa-B and MAP kinase p38 pathways (By similarity). E3 ubiquitin ligase activity is dependent on E2 ubiquitin-conjugating enzyme UBE2D2 (By similarity).
PTM: Polyubiquitinated, autoubiquitinated in the presence of UBE2D2.
Catalytic Activity: S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.
Sequence Mass (Da): 54298
Sequence Length: 475
Domain: The RING finger is required for ubiquitin ligase activity.
Pathway: Protein modification; protein ubiquitination.
Subcellular Location: Cytoplasm
EC: 2.3.2.27
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Q969Q1 | MDYKSSLIQDGNPMENLEKQLICPICLEMFTKPVVILPCQHNLCRKCANDIFQAANPYWTSRGSSVSMSGGRFRCPTCRHEVIMDRHGVYGLQRNLLVENIIDIYKQECSSRPLQKGSHPMCKEHEDEKINIYCLTCEVPTCSMCKVFGIHKACEVAPLQSVFQGQKTELNNCISMLVAGNDRVQTIITQLEDSRRVTKENSHQVKEELSQKFDTLYAILDEKKSELLQRITQEQEKKLSFIEALIQQYQEQLDKSTKLVETAIQSLDEPGGATFLLTAKQLIKSIVEASKGCQLGKTEQGFENMDFFTLDLEHIADALRAIDFGTDEEEEEFIEEEDQEEEESTEGKEEGHQ | Function: E3 ubiquitin ligase. Mediates the ubiquitination and subsequent proteasomal degradation of CKM, GMEB1 and HIBADH. Regulates the proteasomal degradation of muscle proteins under amino acid starvation, where muscle protein is catabolized to provide other organs with amino acids. Inhibits de novo skeletal muscle protein synthesis under amino acid starvation. Regulates proteasomal degradation of cardiac troponin I/TNNI3 and probably of other sarcomeric-associated proteins. May play a role in striated muscle atrophy and hypertrophy by regulating an anti-hypertrophic PKC-mediated signaling pathway. May regulate the organization of myofibrils through TTN in muscle cells.
Catalytic Activity: S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.
Sequence Mass (Da): 40248
Sequence Length: 353
Domain: The RING-type zinc finger mediates interaction with SUMO2 and localization to the nucleus. Also required for the E3 ubiquitin ligase activity (By similarity).
Pathway: Protein modification; protein ubiquitination.
Subcellular Location: Cytoplasm
EC: 2.3.2.27
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Q38HM4 | MDYKSGLIPDGNAMENLEKQLICPICLEMFTKPVVILPCQHNLCRKCANDIFQAANPYWTNRGGSVSMSGGRFRCPSCRHEVIMDRHGVYGLQRNLLVENIIDIYKQECSSRPLQKGSHPMCKEHEDEKINIYCLTCEVPTCSLCKVFGAHQACEVAPLQSIFQGQKTELSNCISMLVAGNDRVQTIISQLVDSCRVTKENSHQVKEELSQKFDTLYAILDEKKSELLQRITQEQEEKLGFIEALILQYREQLEKSTKLVETAIQSLDEPGGATFLSSAKQLIKSNVEASKGCQLGKTEQGFENMDYFTLDLEHIAEALRAIDFGTDEEEEEFTEEEADEEEGVTTEGHQ | Function: E3 ubiquitin ligase. Mediates the ubiquitination and subsequent proteasomal degradation of CKM, GMEB1 and HIBADH. Regulates the proteasomal degradation of muscle proteins under amino acid starvation, where muscle protein is catabolized to provide other organs with amino acids. Inhibits de novo skeletal muscle protein synthesis under amino acid starvation. Regulates proteasomal degradation of cardiac troponin I/TNNI3 and probably of other sarcomeric-associated proteins. May play a role in striated muscle atrophy and hypertrophy by regulating an anti-hypertrophic PKC-mediated signaling pathway. May regulate the organization of myofibrils through TTN in muscle cells.
Catalytic Activity: S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.
Sequence Mass (Da): 39491
Sequence Length: 350
Domain: The RING-type zinc finger mediates interaction with SUMO2 and localization to the nucleus (By similarity). Also required for the E3 ubiquitin ligase activity.
Pathway: Protein modification; protein ubiquitination.
Subcellular Location: Cytoplasm
EC: 2.3.2.27
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Q6PJ69 | MAAQLLEEKLTCAICLGLYQDPVTLPCGHNFCGACIRDWWDRCGKACPECREPFPDGAELRRNVALSGVLEVVRAGPARDPGPDPGPGPDPAARCPRHGRPLELFCRTEGRCVCSVCTVRECRLHERALLDAERLKREAQLRASLEVTQQQATQAEGQLLELRKQSSQIQNSACILASWVSGKFSSLLQALEIQHTTALRSIEVAKTQALAQARDEEQRLRVHLEAVARHGCRIRELLEQVDEQTFLQESQLLQPPGPLGPLTPLQWDEDQQLGDLKQLLSRLCGLLLEEGSHPGAPAKPVDLAPVEAPGPLAPVPSTVCPLRRKLWQNYRNLTFDPVSANRHFYLSRQDQQVKHCRQSRGPGGPGSFELWQVQCAQSFQAGHHYWEVRASDHSVTLGVSYPQLPRCRLGPHTDNIGRGPCSWGLCVQEDSLQAWHNGEAQRLPGVSGRLLGMDLDLASGCLTFYSLEPQTQPLYTFHALFNQPLTPVFWLLEGRTLTLCHQPGAVFPLGPQEEVLS | Function: E3 ubiquitin ligase that plays a role in several processes including innate immnity, autophagy or inflammation . Negatively regulates miRNAs by modulating the ubiquitination and stability of TNRC6A, a protein involved in RNA-mediated gene silencing by both micro-RNAs (miRNAs) and short interfering RNAs . This ubiquitination results in the suppressed expression of miR-138-5p leading to increased autophagy . Upon enteroviral infection, promotes 'Lys-63'-mediated ubiquitination activation of IFIH1/MDA5 leading to innate signaling cascade . Mechanistically, selectively recognizes MDA5 filaments that occur on dsRNAs . Plays also a role in limitation of inflammation through different mechanisms. First, promotes 'Lys-48'-mediated ubiquitination of VCAM1 leading to its degradation and limitation of LPS-induced lung inflammation . In addition, negatively regulates inflammasome activation by promoting 'lys48'-linked ubiquitination of NLRP3 which is critical for the inhibition of NLRP3 inflammasome activation in resting macrophages .
Catalytic Activity: S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.
Sequence Mass (Da): 57353
Sequence Length: 517
Pathway: Protein modification; protein ubiquitination.
Subcellular Location: Cytoplasm
EC: 2.3.2.27
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Q8BFW4 | MAAQLLEEDVVTCSICLGRYRDPVTLPCGHSFCGNCIQDSWRSCEKSCPECRQPFPEGAKLSRNVKMSTLLQALPVLPAPPAVTPRRDSATSHSARCLRHGRPLEFFCRTEGLCVCSACTVHDCSHHERALLDVERRVREDQLRARVLVTQQQVAQAETQLQELQEQRSRIESSACTLASVVSRRFSSLLQALEKQQASTLSDIEVAKKQALGQVLNEKQRLTDHLRALSQYDQSVQDLLAQADDCIFFQELQQLPEPTESLGPLTSPQWNEEQQLSNVNQLLSPLCELLLEEKSLPKVAAKAADAGPLETLGPLAPVPSAVCPLRKKLWQNYRNLTFDPETANQYLHLSHKDQRVTHHFQAQGPAKSGSFELWQVQCTQSFQTGQHYWEVRVSDHSVTLGVTYPKLSRQKLGTHTDNIGRGPCSWGLCIQEDSMQAWHNGKSQRLRGLPGQLLGVDLNLTSGCLTFYSLEPRTQPLHTFYAVFSQPLFPVFWLLEGRTLTLCHQPEATLPARPQEEATAPS | Function: E3 ubiquitin ligase that plays a role in several processes including innate immnity, autophagy or inflammation . Negatively regulates miRNAs by modulating the ubiquitination and stability of TNRC6A, a protein involved in RNA-mediated gene silencing by both micro-RNAs (miRNAs) and short interfering RNAs. This ubiquitination results in the suppressed expression of miR-138-5p leading to increased autophagy (By similarity). Upon enteroviral infection, promotes 'Lys-63'-mediated ubiquitination activation of IFIH1/MDA5 leading to innate signaling cascade. Mechanistically, selectively recognizes MDA5 filaments that occur on dsRNAs (By similarity). Plays also a role in limitation of inflammation through different mechanisms. First, promotes 'Lys-48'-mediated ubiquitination of VCAM1 leading to its degradation and limitation of LPS-induced lung inflammation . In addition, negatively regulates inflammasome activation by promoting 'lys48'-linked ubiquitination of NLRP3 which is critical for the inhibition of NLRP3 inflammasome activation in resting macrophages .
Catalytic Activity: S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.
Sequence Mass (Da): 58458
Sequence Length: 522
Pathway: Protein modification; protein ubiquitination.
Subcellular Location: Cytoplasm
EC: 2.3.2.27
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Q6AZZ1 | MDPTALVEAIVEEVACPICMTFLREPMSIDCGHSFCHSCLSGLWEIPGESQNWGYTCPLCRAPVQPRNLRPNWQLANVVEKVRLLRLHPGMGLKGDLCERHGEKLKMFCKEDVLIMCEACSQSPEHEAHSVVPMEDVAWEYKWELHEALEHLKKEQEEAWKLEVGERKRTATWKIQVETRKQSIVWEFEKYQRLLEKKQPPHRQLGAEVAAALASLQREAAETMQKLELNHSELIQQSQVLWRMIAELKERSQRPVRWMLQDIQEVLNRSKSWSLQQPEPISLELKTDCRVLGLREILKTYAADVRLDPDTAYSRLIVSEDRKRVHYGDTNQKLPDNPERFYRYNIVLGSQCISSGRHYWEVEVGDRSEWGLGVCKQNVDRKEVVYLSPHYGFWVIRLRKGNEYRAGTDEYPILSLPVPPRRVGIFVDYEAHDISFYNVTDCGSHIFTFPRYPFPGRLLPYFSPCYSIGTNNTAPLAICSLDGED | Function: Functions as a ubiquitin E3 ligase. Acts as a coactivator of androgen receptor (AR) depending on its ubiquitin ligase activity.
PTM: Auto-ubiquitinated.
Catalytic Activity: S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.
Sequence Mass (Da): 56259
Sequence Length: 485
Domain: The RING domain is essential for ubiquitin E3 ligase activity.
Pathway: Protein modification; protein ubiquitination.
Subcellular Location: Cytoplasm
EC: 2.3.2.27
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Q86WT6 | MEVSTNPSSNIDPGDYVEMNDSITHLPSKVVIQDITMELHCPLCNDWFRDPLMLSCGHNFCEACIQDFWRLQAKETFCPECKMLCQYNNCTFNPVLDKLVEKIKKLPLLKGHPQCPEHGENLKLFSKPDGKLICFQCKDARLSVGQSKEFLQISDAVHFFTEELAIQQGQLETTLKELQTLRNMQKEAIAAHKENKLHLQQHVSMEFLKLHQFLHSKEKDILTELREEGKALNEEMELNLSQLQEQCLLAKDMLVSIQAKTEQQNSFDFLKDITTLLHSLEQGMKVLATRELISRKLNLGQYKGPIQYMVWREMQDTLCPGLSPLTLDPKTAHPNLVLSKSQTSVWHGDIKKIMPDDPERFDSSVAVLGSRGFTSGKWYWEVEVAKKTKWTVGVVRESIIRKGSCPLTPEQGFWLLRLRNQTDLKALDLPSFSLTLTNNLDKVGIYLDYEGGQLSFYNAKTMTHIYTFSNTFMEKLYPYFCPCLNDGGENKEPLHILHPQ | Function: E3 ubiquitin ligase that plays an important role in antiviral immunity by restricting different viral infections including dengue virus or vesicular stomatitis indiana virus . Ubiquitinates viral proteins such as dengue virus NS3 thereby limiting infection . In addition, acts as a key mediator of type I interferon induced microtubule stabilization by directly associating to microtubules independently of its E3 ligase activity . Plays also a role in cataract formation together with TP53 . Mechanistically, inhibits UVB-induced cell apoptosis and reactive oxygen species (ROS) production by inducing TP53 ubiquitination .
PTM: Phosphorylated. Phosphorylation is necessary for nuclear localization.
Catalytic Activity: S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.
Sequence Mass (Da): 57419
Sequence Length: 500
Domain: The RING-type zinc finger domain is responsible for E3 ubiquitin ligase activity and for nuclear localization and aggregation.
Pathway: Protein modification; protein ubiquitination.
Subcellular Location: Cytoplasm
EC: 2.3.2.27
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Q6ZMU5 | MSAAPGLLHQELSCPLCLQLFDAPVTAECGHSFCRACLGRVAGEPAADGTVLCPCCQAPTRPQALSTNLQLARLVEGLAQVPQGHCEEHLDPLSIYCEQDRALVCGVCASLGSHRGHRLLPAAEAHARLKTQLPQQKLQLQEACMRKEKSVAVLEHQLVEVEETVRQFRGAVGEQLGKMRVFLAALEGSLDREAERVRGEAGVALRRELGSLNSYLEQLRQMEKVLEEVADKPQTEFLMKYCLVTSRLQKILAESPPPARLDIQLPIISDDFKFQVWRKMFRALMPALEELTFDPSSAHPSLVVSSSGRRVECSEQKAPPAGEDPRQFDKAVAVVAHQQLSEGEHYWEVDVGDKPRWALGVIAAEAPRRGRLHAVPSQGLWLLGLREGKILEAHVEAKEPRALRSPERRPTRIGLYLSFGDGVLSFYDASDADALVPLFAFHERLPRPVYPFFDVCWHDKGKNAQPLLLVGPEGAEA | Function: Muscle-specific protein that plays a central role in cell membrane repair by nucleating the assembly of the repair machinery at injury sites. Specifically binds phosphatidylserine. Acts as a sensor of oxidation: upon membrane damage, entry of extracellular oxidative environment results in disulfide bond formation and homooligomerization at the injury site. This oligomerization acts as a nucleation site for recruitment of TRIM72-containing vesicles to the injury site, leading to membrane patch formation. Probably acts upstream of the Ca(2+)-dependent membrane resealing process. Required for transport of DYSF to sites of cell injury during repair patch formation. Regulates membrane budding and exocytosis. May be involved in the regulation of the mobility of KCNB1-containing endocytic vesicles (By similarity).
PTM: Disulfide bond formation at Cys-242 occurs in case of membrane damage that cause the entry of the oxidized milieu of the extracellular space, resulting in homooligomerization.
Sequence Mass (Da): 52731
Sequence Length: 477
Subcellular Location: Cell membrane
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K9IMD0 | MKLLFLALLSLLALGPSLAARRRGVRWCTISKPEAAKCSKLQQNLKRVRGPSLSCISRKSYLECIQAIAAKRADAMSLDAGLVYEAGQDPYRLRPVAAEVYGTEGAPRTHYYAVALVKKDSNLQLNQLQGVRSCHTGLNRSAGWKIPVGTLRPYLGWAGPPAPLQEAVANFFSASCVPCADGNQYPNLCRLCAGTGADKCACSSKEPYFGYSGAFKCLKDGAGDVAFVKDSTVFENLPNKAERDQYELLCPDNTRKPVDEFEQCHLARVPSHAVVARSVGGKEDSIWRLLSKAQEKFGKGTSGSFQLFSSPPGQKDLLFKDGAQGFLRIPSRVDAELYLGPSYLTVIKNLKESAAEVEARGARVVWCAVGPEELRKCQQWSGQSNGTVTCTTAADTEDCIALVLKGEADAMSLDGGVIYIAGKCGLAPVLAESQRSEGGSNLDCVNRPLEGDRAVAVVRKSSAGLTWNSRRGTKSCHTAVGRTAGWNIPMGLLFNQTRSCNFDEFFSQSCAPGADPNSNLCALCVGNEQGQDKCAPNSNERYFSYAGSFRCLVENAGDVAFVKASTVLENPDGRGTEAWAKDLKLEDFELLCLDGTRKPVSEFETCHLARAPSHGVVSRKDRVQYLEQVLLDQQGKFGRNGPLCPGKFCLFQSETKNLLFNDNTECLAKLQGKTTYEKYLGPEYVTAVANLRQCSTSPLLEACTFLRN | Function: Transferrins are iron binding transport proteins which can bind two Fe(3+) ions in association with the binding of an anion, usually bicarbonate.
PTM: N-glycosylated . Glycosylation is important for draculin anticoagulant activity . Probably also O-glycosylated .
Sequence Mass (Da): 76856
Sequence Length: 708
Subcellular Location: Secreted
EC: 3.4.21.-
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Q4WXA1 | MEDDDRPRKYPKLNHDEVQEGSEPVMTGAVGAVHDDDAESADSDNRASPSNDRIDNDVKQACDEEGQDAHGKDGPPTLSKNQLKKLKRKEHWEAMREQRKVKRKEKLVAKRERRRAALEQAKQEGAEATEETRKAFESTQKKFQRSTLLPVTLVLDCSYDDLMLDKERVSLGAQITRSYSDNSRAPFRSHLVVSSFNKLLKERFDTVLGKTHENWKGVRFLQEDFAEAAEMAKEWMQGPKGGQLAGVFADKADAKPEDGEIVYLSSDSPNILTELKPYSTYIIGGLVDKNRHKGICYKSAVAKGIKTAKLPIGEYIQMAHRQVLATNHVVEIMIRWLELGDWGKAFIQVIPQRKGGKLKSADHESEDQTPRESVEAVEAEPDGEGAAAEAGEGGKE | Function: S-adenosyl-L-methionine-dependent guanine N(1)-methyltransferase that catalyzes the formation of N(1)-methylguanine at position 9 (m1G9) in cytoplasmic tRNA.
Catalytic Activity: guanosine(9) in tRNA + S-adenosyl-L-methionine = H(+) + N(1)-methylguanosine(9) in tRNA + S-adenosyl-L-homocysteine
Sequence Mass (Da): 44284
Sequence Length: 396
Subcellular Location: Cytoplasm
EC: 2.1.1.221
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Q59Q39 | MTEQTSEATVVNNSPAPTIPKIKREKPTPEEIEERRKLKQLEVVPEGFSRKQWKRELKKQRWQDTKQEYLEVQREKKRLARQRKRERLKDLDENDELRKAQPIPSRQISTNNVSVIIDCDFDELMHEKEIVSLSNQIKACYSAMRHCTYKLPIQITSFNKRLKQRFEAQLHDYHLWQGNISFTDRSLTEYVTGAPNSESKDNDGNSNSNTTNSTDTINTENLVYLTADTDEEITKLEPNHTYIIGGIVDKNRHKQLCYNKAKELGIKVARLPIGKYIEMNGRHVLVTSHVYELLCKWFENDGDWETAFNKVLPPRKIKSKSPS | Function: S-adenosyl-L-methionine-dependent guanine N(1)-methyltransferase that catalyzes the formation of N(1)-methylguanine at position 9 (m1G9) in cytoplasmic tRNA.
Catalytic Activity: guanosine(9) in tRNA + S-adenosyl-L-methionine = H(+) + N(1)-methylguanosine(9) in tRNA + S-adenosyl-L-homocysteine
Sequence Mass (Da): 37760
Sequence Length: 323
Subcellular Location: Cytoplasm
EC: 2.1.1.221
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P0CS10 | MKFHLGLTEALQEREPNINASSKDLSPLHFELYRRSEPIMDIDEESYLNAGPSAPSKIPQGGEGDRLQGMSKKAMKRAAKQARLEEIKPLKRAAERERRRQRTAQLAEGYAAGTLSEADKELVERRRRVEKERKEAQRRIESGDQANDWLGGVVIDLGFDDLMTDQEIASMAQQLGYLYSSNRTAEKPVRTVIHTTFSPAASPRLWQRMENFNWHKWSRCHWWEQGLETLKSQLDPSTSILSVQSVVSKETQDKAGIDTKSLLSRLTGPQVPVDLQAGKHKLVYLSADAEDELLSLSEDEIYIIGGIVDRNRHKNLCQGKAEQLGIRTARLPIGTFLEMLPTRKVLTVNQVFDILVKYLHLGDWAAAFEAVIPIRKYAPGRKTKRAKTETKRNEKEEEEVECTSAEGEEDIGVIEESAEVDPEDVFSNQ | Function: S-adenosyl-L-methionine-dependent guanine N(1)-methyltransferase that catalyzes the formation of N(1)-methylguanine at position 9 (m1G9) in cytoplasmic tRNA.
Catalytic Activity: guanosine(9) in tRNA + S-adenosyl-L-methionine = H(+) + N(1)-methylguanosine(9) in tRNA + S-adenosyl-L-homocysteine
Sequence Mass (Da): 48581
Sequence Length: 429
Subcellular Location: Cytoplasm
EC: 2.1.1.221
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Q6BWG3 | MENQDTEQSQKRSGSEVEKDDFKRQKVVVPEGMTKREYKRQLKQQRWEETKDEYKQKKREKKKAARERRKERIKEAEANGETNEELYNYHQMKRAKVAPQEQIDTDVKIIMDCEFDSLMNDKEIVSLSNQITRSYSAKKHSTYDVQLDITSFNKNLKKRFEKAIPQYDKWTNVTFVENDKLEDILPMDDKQALSKYVYLTADTDEVIDTLEPHHTYIIGGIVDKNRYKNLCLNKAQSLGLKIGRLPIDKFIKMNGRQVLATSHVFELCCKWFENDKDWGKAFNEVLPPRKVKGKLTHGSDPEKSIEPSEVSEQPVSSEQSEQPVLSEQPVSSEQPVLSEQPVLSESSDEPSDEPSKGADH | Function: S-adenosyl-L-methionine-dependent guanine N(1)-methyltransferase that catalyzes the formation of N(1)-methylguanine at position 9 (m1G9) in cytoplasmic tRNA.
Catalytic Activity: guanosine(9) in tRNA + S-adenosyl-L-methionine = H(+) + N(1)-methylguanosine(9) in tRNA + S-adenosyl-L-homocysteine
Sequence Mass (Da): 41793
Sequence Length: 360
Subcellular Location: Cytoplasm
EC: 2.1.1.221
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Q5B8X0 | MEEEERPRKIQKLGSSEAHESEPLITGAIKGSQDDTSPAEQTNSQKAIPGATTDNSKESEEPASSTATDGPETTEQKISKRQLRRQAKLEQWEAKREERKIIRKQKTAARKERRRELWEEAKREGKDPNEELNKLFPMTTRTRHRKSTRLPLTLIIDCGFDDLMQDKERVSLGQQLTRSYSENNKSAFNGHLIISSFNKKLKERFETVLHKTHEGWKGVRFTGEDWLQAAKEASEVMQGPNGGKLVGPFEDKTDAKPEDGEIVYLTSDSSETLTELKPYSTYIIGGLVDKNRHKGICHKRATELGIRTAKLPIGQYIQMNSRPVLATNHVVEIMVRWLQLRDWAEAFMQTLPPRKGGALKDSVKGQRDSTPRDDVESNTEKGTVSETVEDTEATEPAEAVTPKDIDAVQENKQDE | Function: S-adenosyl-L-methionine-dependent guanine N(1)-methyltransferase that catalyzes the formation of N(1)-methylguanine at position 9 (m1G9) in cytoplasmic tRNA.
Catalytic Activity: guanosine(9) in tRNA + S-adenosyl-L-methionine = H(+) + N(1)-methylguanosine(9) in tRNA + S-adenosyl-L-homocysteine
Sequence Mass (Da): 46963
Sequence Length: 415
Subcellular Location: Cytoplasm
EC: 2.1.1.221
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Q4I8X0 | MDLDPAHKPSQAEETKEQGNEQGQVEQNQAQQDPTTGPQAETEKAIIPSQGSTIPQKRSAEDEPAQPMSKNALKRLRKQQQWEAGKEDRKLKRKDSRIARKVRKREERDALIAQGINPYANKQKPPSVNVPISLIFDCEFEQYMREKEIISLGSQITRSYSENKNAKYRTNIYVSNWNGKLAERFHQILDDKHQNWKGIDFVEGDFIECAEKAREKMKHENMIEPLQRSLTEKSPWARDEKDPLPLPDPEPEPRPEYSDIVYLSSDSPYTLERLEPNTSYVIGGLVDKNREKGLCYKRARERGIRTARLPIGQYMVMQSRTVLTTNHVVEIMLKWLEYENWGEAFMSVIPKRKGGKLKEQQGASGETQETEEAEAEDPEEENEETKDPDAEASASKQNTPKVEVTSK | Function: S-adenosyl-L-methionine-dependent guanine N(1)-methyltransferase that catalyzes the formation of N(1)-methylguanine at position 9 (m1G9) in cytoplasmic tRNA.
Catalytic Activity: guanosine(9) in tRNA + S-adenosyl-L-methionine = H(+) + N(1)-methylguanosine(9) in tRNA + S-adenosyl-L-homocysteine
Sequence Mass (Da): 46769
Sequence Length: 407
Subcellular Location: Cytoplasm
EC: 2.1.1.221
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Q6CUM6 | MSDTSENSNAEIPADTSDVKDKPKPIVRAPQFPPPPEGISKSQWKKICRKKRFEETRAEYAQIRKEKRNRAKLARREKLKEYTDRGEEIPEELKRPPKVNLNQSDSGISIILDCSFDDLMNDREIVSLSTQVTRAYSSNKRENNYAKIKVTSFDKRLKQRFDNDLSNSNYTKWKNFEFTADPTLPTENAVYLTADTEEKLDTLEPGTTYIVGGIVDKNRHKNLCYNKAKELNIPTKRLPIGEFINLAGRKVLTTSHMVQLMLRYFDNKDWKEAFESVLPPRKLEVDSTKEDSETASAE | Function: S-adenosyl-L-methionine-dependent guanine N(1)-methyltransferase that catalyzes the formation of N(1)-methylguanine at position 9 (m1G9) in cytoplasmic tRNA.
Catalytic Activity: guanosine(9) in tRNA + S-adenosyl-L-methionine = H(+) + N(1)-methylguanosine(9) in tRNA + S-adenosyl-L-homocysteine
Sequence Mass (Da): 34387
Sequence Length: 298
Subcellular Location: Cytoplasm
EC: 2.1.1.221
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O14214 | MENKDALDIGKDDTNTSEADVSKNETQEQPVLSKSALKRLKRQQEWDAGREKRAEMRREKKRLRKEERKRKIEAGEVVKSQKKRIRLGKVVPSSIRIVLDCAFDDLMNDKEINSLCQQVTRCHSANRTALHPVELFATNFGGRLKTRQDFVLKGQQNNWKRYNPTTKSYLEEFESQKEKLVYLSADSDNTITELDEDKIYIIGAIVDKNRYKNLCQNKASEQGIKTAKLPIDEYIKITDRKILTVNQVFEILSLWLEYRDWEKAFMEVIPKRKGILLKSDESFDVSEDTRSQSNQSDSELEKEN | Function: S-adenosyl-L-methionine-dependent guanine N(1)-methyltransferase that catalyzes the formation of N(1)-methylguanine at position 9 (m1G9) in cytoplasmic tRNA.
Catalytic Activity: guanosine(9) in tRNA + S-adenosyl-L-methionine = H(+) + N(1)-methylguanosine(9) in tRNA + S-adenosyl-L-homocysteine
Sequence Mass (Da): 35470
Sequence Length: 304
Subcellular Location: Cytoplasm
EC: 2.1.1.221
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Q4J894 | MTLAKVFSQKLRELGISSIYIGHERPSLQSLAIKMLLKNYGLVEERREGMLITQDHGIKLISGKGTETSRYTFRKGGKKVSIHLPEYPKMVIDLGLFEFLNEEEKEKTLLQVDLCLSVIRKFLWDGNLTVVGKADYVLGRANIVQSLSLSDEDNPVILDPYGDVVATDQILRDHNVFVIGGIVDKGRRLDRATERLALSRGYSFPRVKIQLRGSIIGVPDEINKILEIILRVKELDQSLEEAIISLQSKSDKISRLLHDVQLYGMEVLEEEARWLRADDKVIEIVRSRLGKN | Function: Catalyzes the S-adenosyl-L-methionine-dependent formation of N(1)-methyladenine at position 9 (m1A9) in tRNA.
Catalytic Activity: adenosine(9) in tRNA + S-adenosyl-L-methionine = H(+) + N(1)-methyladenosine(9) in tRNA + S-adenosyl-L-homocysteine
Sequence Mass (Da): 33153
Sequence Length: 292
Subcellular Location: Cytoplasm
EC: 2.1.1.218
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Q5JD38 | MKTLADVFREALKEKGISSIGTLSKRFRKSKNKLQDIAIEIVHGKGAVFRVPEKTAVAWDLNGNRVDGSYYAYAPLCMREKFEPVLTPEELREKLPDWPYFIIDLYHWDKHTQKEKGKICLQVNQSYGLLRDYFTGSELAVTWANEEFREMFHGPLDRITTYGGPTSEFLKENGINEVVLLDPWAEEVLSEKDFDVKAFIIGGIVDTGGNKKKTTPKIGEELESAGIKVRRRKIVLRGDVVGVPDRINRILGIILKMMVEGKSMDEAVYEMQEPLHARWRLRKELPKRATRYMVEGKVYRVVEKELFDEYSKWLKIRWEDFVKVLRELDLVALERKRIHHLNKISNARIINGKLHRVILLKRAAMLCYNC | Function: Catalyzes the S-adenosyl-L-methionine-dependent formation of either N(1)-methyladenine or N(1)-methylguanine at position 9 (m1A9 or m1G9) in tRNA.
Catalytic Activity: adenosine(9) in tRNA + S-adenosyl-L-methionine = H(+) + N(1)-methyladenosine(9) in tRNA + S-adenosyl-L-homocysteine
Sequence Mass (Da): 42996
Sequence Length: 370
Subcellular Location: Cytoplasm
EC: 2.1.1.218
|
Q6C1W9 | MVDVTEPVAPVEAVKETAGASSATPEVDRTSEPHPKNPQNVPAPYNTKTAVIPEGMSKNEWKKAQKKAIWESKKDEIAAVKKEKKKAARKRKQLAISRGEIPAPIPQDERPPQTQLPISIVLDCGFDEMMTQKEKVSLSAQVGRCYSANRKADARFDLTVNSFNKGLKDRFNNEMNKVHELWTNIKFVEDDYTVPEDETAKSKLVYLSSDSDNVINELEDGKTYIIGGIVDKGRYKNLCQDKASKQGLQTGRLPIADFIKLSGRKVLTTNHVFEILLKWTELKDWKAAFEAVLPMRKLDPANYGRAHRRARKKARLAEGAEGNDEEDDEDDDDEEEEEEESVSAEPEVVETKAEVETDTETKAETEAETKA | Function: S-adenosyl-L-methionine-dependent guanine N(1)-methyltransferase that catalyzes the formation of N(1)-methylguanine at position 9 (m1G9) in cytoplasmic tRNA.
Catalytic Activity: guanosine(9) in tRNA + S-adenosyl-L-methionine = H(+) + N(1)-methylguanosine(9) in tRNA + S-adenosyl-L-homocysteine
Sequence Mass (Da): 41649
Sequence Length: 371
Subcellular Location: Cytoplasm
EC: 2.1.1.221
|
Q12400 | MSNDEINQNEEKVKRTPPLPPVPEGMSKKQWKKMCKRQRWEENKAKYNAERRVKKKRLRHERSAKIQEYIDRGEEVPQELIREPRINVNQTDSGIEIILDCSFDELMNDKEIVSLSNQVTRAYSANRRANHFAEIKVAPFDKRLKQRFETTLKNTNYENWNHFKFLPDDKIMFGDEHISKDKIVYLTADTEEKLEKLEPGMRYIVGGIVDKNRYKELCLKKAQKMGIPTRRLPIDEYINLEGRRVLTTTHVVQLMLKYFDDHNWKNAFESVLPPRKLDAEAKSASSSPAPKDT | Function: S-adenosyl-L-methionine-dependent guanine N(1)-methyltransferase that catalyzes the formation of N(1)-methylguanine at position 9 (m1G9) in cytoplasmic tRNAs.
Catalytic Activity: guanosine(9) in tRNA + S-adenosyl-L-methionine = H(+) + N(1)-methylguanosine(9) in tRNA + S-adenosyl-L-homocysteine
Sequence Mass (Da): 34520
Sequence Length: 293
Subcellular Location: Cytoplasm
EC: 2.1.1.221
|
Q58780 | MVVEVLRLGHRGDRDKRISTHVALTARALGADKIIFTTEDEHVENSVKKVVESWGGNFEFVVEKHWRKYIREFKKRGIVVHLTMYGANINEIMPEIREISRDKDILVIVGAEKVPKEVYELADYNVSVGNQPHSEVAALAIFLDRLFEGKTLYRDFEDAKIKIVPSKDGKVVIREKQNK | Function: Specifically catalyzes the AdoMet-dependent 2'-O-ribose methylation of cytidine at position 56 in tRNAs.
Catalytic Activity: cytidine(56) in tRNA + S-adenosyl-L-methionine = 2'-O-methylcytidine(56) in tRNA + H(+) + S-adenosyl-L-homocysteine
Sequence Mass (Da): 20573
Sequence Length: 179
Subcellular Location: Cytoplasm
EC: 2.1.1.206
|
O27185 | MDVKVLRLGHRPSRDARITTHVCLTARAFGASEVILSGEEDPKLMEGVEDVVRRWGGPFSVVYRRNWQGVIDSWKKDGGEVIHLTMYGLPARDVVPGIMDNGKDKLIVVGGARVPGKVYSLADYNVGVTNQPHSEVSSLAVFMHMLLDGAEFDLKFEDARIEVIPQARGKMLREIDDGD | Function: Specifically catalyzes the AdoMet-dependent 2'-O-ribose methylation of cytidine at position 56 in tRNAs.
Catalytic Activity: cytidine(56) in tRNA + S-adenosyl-L-methionine = 2'-O-methylcytidine(56) in tRNA + H(+) + S-adenosyl-L-homocysteine
Sequence Mass (Da): 19831
Sequence Length: 179
Subcellular Location: Cytoplasm
EC: 2.1.1.206
|
A9A624 | MVIEVVRIGQRLVRDDRVTTHVALVSRAFGAERIFMTEINPEIKDTLGKINDTWGGNFEIEFIDSWKPIVKKKKEEGFKIVHLSMYGEKINDAQEEIRKEENLLIVVGAEKVPREIYELADFNVGVGSQPHSEISALAILLDRIQGGQQFEKEFPNAKRKIIPTKTGKNVQVKETRD | Function: Specifically catalyzes the AdoMet-dependent 2'-O-ribose methylation of cytidine at position 56 in tRNAs.
Catalytic Activity: cytidine(56) in tRNA + S-adenosyl-L-methionine = 2'-O-methylcytidine(56) in tRNA + H(+) + S-adenosyl-L-homocysteine
Sequence Mass (Da): 20187
Sequence Length: 177
Subcellular Location: Cytoplasm
EC: 2.1.1.206
|
Q5P8D0 | MPLPAIDPAEYASQLADKVTQFKHAFTPFAVPEPTVFPSAPLHYRLRAEFRMWHDGERIDYAMFDPAEPKQPIAIEQFDIAAEPICAAMPRLRERLRASETLKRRLFQVEFLATLSGELMISLIYHRPLDESWEAAARELAAELNVQLIGRSRKQKIVLDRDWVLERFALDGRPLQYKQIEGSFTQPNGGVNRQMLGWACEQVRGVGGDLLELYCGNGNFTVALAPLFDRVLATEVSKTSVEAAHYNLAANDIGNVAMVRMSSDEISAALARTREFRRMKDVDLDRYRFSTLFVDPPRSGLDAPTVELARGFDRILYISCNPQTLQENVAALQATHGIAGAAVFDQFPYTRHLECGLLLTRRGGPRAP | Function: Dual-specificity methyltransferase that catalyzes the formation of 5-methyluridine at position 54 (m5U54) in all tRNAs, and that of position 341 (m5U341) in tmRNA (transfer-mRNA).
Catalytic Activity: S-adenosyl-L-methionine + uridine(54) in tRNA = 5-methyluridine(54) in tRNA + H(+) + S-adenosyl-L-homocysteine
Sequence Mass (Da): 41362
Sequence Length: 368
EC: 2.1.1.-
|
Q0ACP5 | MERRADAATGKRPIRSFVRREGRLTAGQQRALELLWPAFGLERPPAGQPLDLDRAFGRRAPRILEIGFGNGESLAEQAATHPERDYLGIEVHRPGVGHLLMEVEKRHLGNVRVMMADAAEVLAHHIPDGSLHGVQLFFPDPWPKKRHHKRRLVQPQWVRAVAAKLAPGGFLHLATDWADYAEHMLDVLEAEPDLENTCGPRQFSPRGERPETKFERRGLRKGHQVFDLYYRKREHPG | Function: Catalyzes the formation of N(7)-methylguanine at position 46 (m7G46) in tRNA.
Catalytic Activity: guanosine(46) in tRNA + S-adenosyl-L-methionine = N(7)-methylguanosine(46) in tRNA + S-adenosyl-L-homocysteine
Sequence Mass (Da): 27016
Sequence Length: 237
Pathway: tRNA modification; N(7)-methylguanine-tRNA biosynthesis.
EC: 2.1.1.33
|
A6TMJ6 | MRVRHIPGAKEQLKEYEFYIQDPSQYQNQWHLYFQNQHPIHLEVGLGKGQFLTTLAKVHKNINYLGLEKSQEVLLQALKKLDRQVSRQELSNMGLFHYNALDLNEVFGEGNIEKIYLNFSDPWPKERHKKRRLTHQGFLKIYRGLLSEQGEIQIKTDNKALFEFSLQQLKEENFHFVQVIYNLHNDGIKDPFMTEYEEKFVKAGKTIYKCIATV | Function: Catalyzes the formation of N(7)-methylguanine at position 46 (m7G46) in tRNA.
Catalytic Activity: guanosine(46) in tRNA + S-adenosyl-L-methionine = N(7)-methylguanosine(46) in tRNA + S-adenosyl-L-homocysteine
Sequence Mass (Da): 25387
Sequence Length: 214
Pathway: tRNA modification; N(7)-methylguanine-tRNA biosynthesis.
EC: 2.1.1.33
|
Q2IG43 | MIFSIEDDAPIVRDLLPDWRARFGEAGGRLELEIGCGHGGFALGFARAFPERALVGIEQRRKFAAELAAKGARHGLSNLLVLNGDARLLAPRLFAAGSLAAIHVHFPDPWWKRRHHRRRLVDDRMSALLLGLLAPGGVLDFRTDVERYAREAVVRLEEVGFRNAAGPGRFAEAAPDEIPSTRERRYLASGEPVWRLRLVKA | Function: Catalyzes the formation of N(7)-methylguanine at position 46 (m7G46) in tRNA.
Catalytic Activity: guanosine(46) in tRNA + S-adenosyl-L-methionine = N(7)-methylguanosine(46) in tRNA + S-adenosyl-L-homocysteine
Sequence Mass (Da): 22375
Sequence Length: 201
Pathway: tRNA modification; N(7)-methylguanine-tRNA biosynthesis.
EC: 2.1.1.33
|
Q7Q2P7 | MEEAIDDHVKLPQKRFYRQRAHSNPIADHSFDYPLLPELSNWNELYPNIGNRQVVFADIGCGYGGFLVTLGETFPDKLAIGMEIRVKVSDYVMDRIKALRQRHKGKYENIACIRTNAMKYLPNYFRKHQLEKLFFLYPDPHFKKAKHKWRIINPTLLSEYAYVLRPGGKIYTVTDVRELHEWMCKHIEEHPCFKRLPDTEAQEDILAPKLLDSSEEGQKVTRMSGEKFMAIFTRL | Function: Catalyzes the formation of N(7)-methylguanine at position 46 (m7G46) in tRNA.
Catalytic Activity: guanosine(46) in tRNA + S-adenosyl-L-methionine = N(7)-methylguanosine(46) in tRNA + S-adenosyl-L-homocysteine
Sequence Mass (Da): 27662
Sequence Length: 235
Pathway: tRNA modification; N(7)-methylguanine-tRNA biosynthesis.
Subcellular Location: Nucleus
EC: 2.1.1.33
|
O66479 | MLCYVNYKRVKRPVEIPNLEVEIGFGRGDFIVKLAKENPDKNFFGIEISQISIEKLMKRVGKKGLKNVYCTNVDAYWGFYFLFRDNYVENIYMNYPDPWFKKRHHKRRLTKPERLYMFAKKLKLGGEIRIRTDNYEFLEFTKESAKVLDCFEVEEGTLNVKEPLTKYEQKWLSMGKTLYKLILRKVKEPKFVEHPEVEEVRELFPVKVKVESVDPKKIESREIKLDEEVYFKTFKVWQRDKDFLVECLLSEKGYLQKFFIQIKRKEDGYVIDVSPYSEVLRTRNLQRSIQTVAQLLS | Function: Catalyzes the formation of N(7)-methylguanine at position 46 (m7G46) in tRNA.
Catalytic Activity: guanosine(46) in tRNA + S-adenosyl-L-methionine = N(7)-methylguanosine(46) in tRNA + S-adenosyl-L-homocysteine
Sequence Mass (Da): 35639
Sequence Length: 297
Domain: The C-terminal region is probably involved in protein stability.
Pathway: tRNA modification; N(7)-methylguanine-tRNA biosynthesis.
EC: 2.1.1.33
|
Q8GXB7 | MDNETKATTFSKSTGLPRKRFYRARAHSNPLSDSHFPIPISPAHVDYSLHFPKFVEADNKFIKKVEFADIGCGFGGLLISLATLFPDTLMIGMELRDKVTEYVKERILALRRTSSEGQYENISVVRTNSMKYIPNYFEKGQLSKMFFLFPDPHFKEKNHRRRVISTHLLDEYAYVLRAGGIIYTITDVEELGEWMKSCLEKHPMFESLTQEELVSDPVVELLCSATEEGQKVARNGGQTFRAVFRRIAYVS | Function: Catalyzes the formation of N(7)-methylguanine at position 46 (m7G46) in tRNA.
Catalytic Activity: guanosine(46) in tRNA + S-adenosyl-L-methionine = N(7)-methylguanosine(46) in tRNA + S-adenosyl-L-homocysteine
Sequence Mass (Da): 28818
Sequence Length: 251
Pathway: tRNA modification; N(7)-methylguanine-tRNA biosynthesis.
Subcellular Location: Nucleus
EC: 2.1.1.33
|
Q8G9C6 | MTFPSHNPPETGHPSAAPDEALPAAEAPVPGDPEARFSSRSIRSFVLRQGRMSVAQQRHLDETLPKVGIPYRVAPLDLDAAFGRAAPKIVEIGFGMGETTAKIAAALPDKDFLTIEVHGPGVGSLCKLIAEGVLDNVRIVQHDAVEVLRDMIPERALAGVHVFFPDPWHKKRHHKRRIIQPDFVALIASRLAPGAYLHCATDWEEYAQWMLEVLAAEPALENTADGYAPRPAYRPLTKFENRGLKLGHGVWDLVFRRRG | Function: Catalyzes the formation of N(7)-methylguanine at position 46 (m7G46) in tRNA.
Catalytic Activity: guanosine(46) in tRNA + S-adenosyl-L-methionine = N(7)-methylguanosine(46) in tRNA + S-adenosyl-L-homocysteine
Sequence Mass (Da): 28575
Sequence Length: 259
Pathway: tRNA modification; N(7)-methylguanine-tRNA biosynthesis.
EC: 2.1.1.33
|
A0K1I7 | MSESPETPEPSPAQSPEAAPEQPQAARPVTPGSQASFGTYGGRPVSFVRRGTRLQGRRQQAWEEHSDRWAVDVPRHIANTSVHPDYVFDAEAEFGRSAPLIVEIGSGLGDAVCHAAEENPDWDFLAVEVYTPGLANTVIKINSRKLSNVRVVEANAPEVLATMLPAGSVSEVWVFFPDPWHKSRHHKRRLIQPEFAALVAAALKPGGLFRVATDWSNYAVHVRDVMAGSADFVNLHDGERRGPESPLTQVWQSGVESLVGGAPVKEGRAPVSTEHTGPNEGVDETGGWAPRFEGRIRTSFENKAHEAGRLIFDLCYRRL | Function: Catalyzes the formation of N(7)-methylguanine at position 46 (m7G46) in tRNA.
Catalytic Activity: guanosine(46) in tRNA + S-adenosyl-L-methionine = N(7)-methylguanosine(46) in tRNA + S-adenosyl-L-homocysteine
Sequence Mass (Da): 34907
Sequence Length: 319
Pathway: tRNA modification; N(7)-methylguanine-tRNA biosynthesis.
EC: 2.1.1.33
|
Q4WQB9 | MTPPPPKRQKRDEYRKATAEATSQSGASDVAEIKLPKKKYYRQRAHANPFSDHHLKYPLSPAHMDWSSHYPAFVNPDPSHINLAGARRLLKDVEVVDIGCGFGGLLIGLAPLLPESLIVGMEIRVSVLEYVTTRIQALRAQQQKLRAATATATAASETPSQQQAQIDGKQANANAAADAASPAPSTDTEHMPTTLVPGSYENISAIRSNTMKFFPNFFARHQLSKIFICFPDPHFKARKHKARIISETLNAEYAYALRPGGLLYTITDVEEYHHWILRHFGVELGAEEESEEKSTSPNANANAGVRELFERVSEEELEKDECVRVMKEATEEGKKVARNKGNKYVAVFRRKTDPEWPA | Function: Catalyzes the formation of N(7)-methylguanine at position 46 (m7G46) in tRNA.
Catalytic Activity: guanosine(46) in tRNA + S-adenosyl-L-methionine = N(7)-methylguanosine(46) in tRNA + S-adenosyl-L-homocysteine
Sequence Mass (Da): 39946
Sequence Length: 358
Pathway: tRNA modification; N(7)-methylguanine-tRNA biosynthesis.
Subcellular Location: Nucleus
EC: 2.1.1.33
|
A8IG13 | MTALSETEHKGAFYGRRVGKTLRQGQQQALARTLPRYLIDLPTVAEPAALFPCPVDEIRLEIGFGGGEHLLSEAKRFPRAGYIGIEPFLNGMAKAVLELDLAPQENVRLFNLDAALLLARLPEGSVSQVELLYPDPWPKRRHWKRRFVRPDNLDLLARALKPGGVFRFASDVPDYVDWTLREVRAHPAFRWTQTRADDWRTPYEGWPGTRYEAKAIAAGRVPTYLSFARV | Function: Catalyzes the formation of N(7)-methylguanine at position 46 (m7G46) in tRNA.
Catalytic Activity: guanosine(46) in tRNA + S-adenosyl-L-methionine = N(7)-methylguanosine(46) in tRNA + S-adenosyl-L-homocysteine
Sequence Mass (Da): 26108
Sequence Length: 230
Pathway: tRNA modification; N(7)-methylguanine-tRNA biosynthesis.
EC: 2.1.1.33
|
B0TXQ5 | MSDNSKENLRQIKSYVQRAGRVTKKQQQALDDYASKYMIEYDQNKSLDFSEIFKNSNDVVLEIGFGMGGSLVQMALENPTKNYLGIEVHKAGVGNILYEIEHQNISNLLVMSHDAVEILENMISDNSLSGMQIYFPDPWHKKKHNKRRLVNQSNVDLFAKKLKVGGVFHYASDWLPYAEEVLELLENDNKYKNLYDGFAPRPEWRPLTKFEKRGQNLDHPISDILFEKI | Function: Catalyzes the formation of N(7)-methylguanine at position 46 (m7G46) in tRNA.
Catalytic Activity: guanosine(46) in tRNA + S-adenosyl-L-methionine = N(7)-methylguanosine(46) in tRNA + S-adenosyl-L-homocysteine
Sequence Mass (Da): 26515
Sequence Length: 229
Pathway: tRNA modification; N(7)-methylguanine-tRNA biosynthesis.
EC: 2.1.1.33
|
Q8Y1I7 | MQPNEQPGTGPADTTLEQQDTAAAEVGHPRRIRSFVRRAGRTSTGQQRAIDELGPRFLLPYAAAPLDWEAAFGRTGARRIFEIGFGMGETSAHIAQLRPDDDFLGVEVHEPGVGALLKLIGERGIGNVRIVSHDAVEVLAQMIPEGTLDGIHVFFPDPWHKKRHNKRRLIQGPFVARLAAHLRPGGYLHCATDWEEYAHQMLEVLSAEPLLENTADGFAPRPDYRPVTKFEKRGLRLGHGVWDVVFRKRAA | Function: Catalyzes the formation of N(7)-methylguanine at position 46 (m7G46) in tRNA.
Catalytic Activity: guanosine(46) in tRNA + S-adenosyl-L-methionine = N(7)-methylguanosine(46) in tRNA + S-adenosyl-L-homocysteine
Sequence Mass (Da): 27913
Sequence Length: 251
Pathway: tRNA modification; N(7)-methylguanine-tRNA biosynthesis.
EC: 2.1.1.33
|
B2U7E2 | MQPIEQPGTGPDDITPESQDTNTAESAESGAETGHPRRIRSFVRRAGRTSTGQQRAINELGPRFQLPYTTEPLDWDAAFGRAGAKRIFEIGFGMGETTAHIAQLRPDDDFLGVEVHEPGVGALLKLIGEREIGNIRIVSHDAVEVLAQMIPEGTLDGIHVFFPDPWHKKRHNKRRLIQSPFVARLAAHLKPGGYLHCATDWEEYAHQMLEVLSSEPTLENTADGFAPRPDYRPVTKFEKRGLRLGHGVWDVVFRKRG | Function: Catalyzes the formation of N(7)-methylguanine at position 46 (m7G46) in tRNA.
Catalytic Activity: guanosine(46) in tRNA + S-adenosyl-L-methionine = N(7)-methylguanosine(46) in tRNA + S-adenosyl-L-homocysteine
Sequence Mass (Da): 28698
Sequence Length: 257
Pathway: tRNA modification; N(7)-methylguanine-tRNA biosynthesis.
EC: 2.1.1.33
|
Q98BJ3 | MSPQDRPSRTTEAFFGRRRGKPVRPQQAAALESGLDAYRLDLTADAPSDLRTLFETEVSAVRLEIGFGGGEHLLHRAIEAPTTGFIGVEPFVNGMAKMMMAVRARPLANLRVHDDDATRLLDWLPPASLGGIDLLYPDPWPKKKHWKRRFVSPVNLERFARVLKPGAKFRFASDIDTYVNWTLLHCRAHGAFAWQAAEAADWHRPYEGWPGTRYEAKAIREGRRPAYLTFVRK | Function: Catalyzes the formation of N(7)-methylguanine at position 46 (m7G46) in tRNA.
Catalytic Activity: guanosine(46) in tRNA + S-adenosyl-L-methionine = N(7)-methylguanosine(46) in tRNA + S-adenosyl-L-homocysteine
Sequence Mass (Da): 26434
Sequence Length: 233
Pathway: tRNA modification; N(7)-methylguanine-tRNA biosynthesis.
EC: 2.1.1.33
|
Q92SI3 | MTETRGARATEAFFGRRKGKPLRERQAAHLEHLLPLLKLDLEEPAPADLTALFPEPVERIRLEIGFGGGEHLIHRAAEDPATGFIGVEPFVNSMAKLLGQIEAKAIRNIRLYDDDATQVLDWLPAASVDQIDLLYPDPWPKRKHWKRRFVSQINLDRFARILKPGGLFCFASDIDSYINWTLIHCREHAAFEWTAERAADWLTPFAGWPSTRYEAKARREGRSSAYLAFRRA | Function: Catalyzes the formation of N(7)-methylguanine at position 46 (m7G46) in tRNA.
Catalytic Activity: guanosine(46) in tRNA + S-adenosyl-L-methionine = N(7)-methylguanosine(46) in tRNA + S-adenosyl-L-homocysteine
Sequence Mass (Da): 26532
Sequence Length: 232
Pathway: tRNA modification; N(7)-methylguanine-tRNA biosynthesis.
EC: 2.1.1.33
|
Q7UN36 | MLVVAAMRVWNPEEGWANRVGRKREGKIVEILRRVTMTAHGLSHFPRQLLRMPRAALRKPNPALDLDSWLKTPEDLPATINSQTLFGNDQPLEIEVGSGKGLFIQTESDRRPEHNYFGIEIARKYAAHAAARLAKRERANAKMLAGDATPLFAVTDEGKRIEDGSLDGVHVYFPDPWWKKRHRKRRVLSHDNILNFSRCLRVGGRLHFWTDVLDYFELTVELIAEIAPELGVPLPETQRESTHDLDFHTHFERRSRKMGIPVYRVCYRKRS | Function: Catalyzes the formation of N(7)-methylguanine at position 46 (m7G46) in tRNA.
Catalytic Activity: guanosine(46) in tRNA + S-adenosyl-L-methionine = N(7)-methylguanosine(46) in tRNA + S-adenosyl-L-homocysteine
Sequence Mass (Da): 31306
Sequence Length: 271
Pathway: tRNA modification; N(7)-methylguanine-tRNA biosynthesis.
EC: 2.1.1.33
|
Q0S679 | MPETPLMRDNGPVNHADQDAPAVPEEGQTKDSKGSRLHPRVTSFRSRRGALTVAQQESWDRQWPRIGADVSDHRLDAPSWFGRDAPLILEIGSGTGTATAAMAKAEPHVNLMAVEVYRPGLAQLLQQIERDEIPNIRVLRGDAMDVLENMIEPESLTGVRVFFPDPWPKARHHKRRLLQSPTFALIASRLKAGGVLHVATDHAEYAEAIAEAGNAEPLLTSLDWESPMTHERPVTKFEDKAHQVGSAITELIWGKIRS | Function: Catalyzes the formation of N(7)-methylguanine at position 46 (m7G46) in tRNA.
Catalytic Activity: guanosine(46) in tRNA + S-adenosyl-L-methionine = N(7)-methylguanosine(46) in tRNA + S-adenosyl-L-homocysteine
Sequence Mass (Da): 28586
Sequence Length: 258
Pathway: tRNA modification; N(7)-methylguanine-tRNA biosynthesis.
EC: 2.1.1.33
|
Q2RMS4 | MPEKPTEDARFYGRRKGKPLRATRQRLLDTMLPALTLPLAGLGEGERLDPRGLFPRPVDQLWLEIGFGGGEHLVAQAAAHPEVGLIGSEVFAYGVGKALSQIDETGVDNIRLWPEDVRQVLPALPDGCLQRLFVLFPDPWPKRRHARRRMIQPARLDDFARLLADGGELRVASDDMGYVRWTLMHVTAHPAFRWTAQGPTDWRERPADWVETRYEAKALQAGRKPAYLIFRRRPRAADPGTLAEAPAGEGADNNP | Function: Catalyzes the formation of N(7)-methylguanine at position 46 (m7G46) in tRNA.
Catalytic Activity: guanosine(46) in tRNA + S-adenosyl-L-methionine = N(7)-methylguanosine(46) in tRNA + S-adenosyl-L-homocysteine
Sequence Mass (Da): 28578
Sequence Length: 255
Pathway: tRNA modification; N(7)-methylguanine-tRNA biosynthesis.
EC: 2.1.1.33
|
Q161H1 | MSKQTRPHRNFYGRLKGKSLKAAQKRYLDEDLAALSPGAVGWEENPDRRPLDLPGLFEGKPVWLEIGFGGGEHLVHQAAQNPDIGIIGAEPYINGVAMLLGKIRRAGVENLAVHAGDARDLMDVLPAASIDRAFLLYPDPWPKARHHRRRFVTAEHLDPLARALKPGSVFRVATDIEDYVRQTLQEVPKHGFKWLANAPQDWRRPWPDWISTRYEQKALREGRTPHYLTFVRE | Function: Catalyzes the formation of N(7)-methylguanine at position 46 (m7G46) in tRNA.
Catalytic Activity: guanosine(46) in tRNA + S-adenosyl-L-methionine = N(7)-methylguanosine(46) in tRNA + S-adenosyl-L-homocysteine
Sequence Mass (Da): 26531
Sequence Length: 233
Pathway: tRNA modification; N(7)-methylguanine-tRNA biosynthesis.
EC: 2.1.1.33
|
Q1AUF5 | MTRRKLGRMKVRPPDPETAQRYLLRFTGRQLYHEAERLPGLSSPELFGDQRPLELDVGCGTGEYICHLARSDPEANFVGVDLHLKSLHKAIRRAEEANLQNIKFICADFRQMYPLLRPSALRAVYLHFPDPGIKPRYRKRRLFNERFLEEMHRAVVPGGRMSLVTDDEDYFRQMLELIERDGRWRRAHEEPYLTGFDPPVKSRFQKMWERRGRTIYRFELVRP | Function: Catalyzes the formation of N(7)-methylguanine at position 46 (m7G46) in tRNA.
Catalytic Activity: guanosine(46) in tRNA + S-adenosyl-L-methionine = N(7)-methylguanosine(46) in tRNA + S-adenosyl-L-homocysteine
Sequence Mass (Da): 26541
Sequence Length: 223
Pathway: tRNA modification; N(7)-methylguanine-tRNA biosynthesis.
EC: 2.1.1.33
|
B8I005 | MRLRRKPWARPELAACDFYVDDPPSYKGRWREFFDNSNPIHLELGCGKGGFISELAADNQNINYIAVDIKSEVLALAKRKIEKEYKERGIQEIKNIRLMSHNIELIDNMLDTVDFIEKIYINFCNPWPKTPYKKKRLTHGKQLIKYKQFLASGAEIWFKTDDDGLFEDSVKYFEENGFIIKYKTWNLHESGFGENVPTEHEIMFSEEGIPIKFLIAEYKQKIHQAVCIGINIKEEN | Function: Catalyzes the formation of N(7)-methylguanine at position 46 (m7G46) in tRNA.
Catalytic Activity: guanosine(46) in tRNA + S-adenosyl-L-methionine = N(7)-methylguanosine(46) in tRNA + S-adenosyl-L-homocysteine
Sequence Mass (Da): 27703
Sequence Length: 236
Pathway: tRNA modification; N(7)-methylguanine-tRNA biosynthesis.
EC: 2.1.1.33
|
O31741 | MKIDFLTLFPEMFEGVLGSSILQKAQEKDAVQFQVVNFREYSDNKHNTVDDYPYGGGAGMVLKPQPVFDAVEDLTSKAAAAPRIILVCPQGERFTQKKAEQLAKEEHLLFICGHYEGYDERIREHLVTDEISIGDFVLTGGELPAMMIADSVVRLLPGVLGKEASHIEDSFSTGLLEHPHYTRPADYKGLKVPETLLSGNHAKIEEWRNKESIRRTYLRRPDLLKDHPLTEQQRKWISEWEKE | Function: Specifically methylates guanosine-37 in various tRNAs.
Catalytic Activity: guanosine(37) in tRNA + S-adenosyl-L-methionine = H(+) + N(1)-methylguanosine(37) in tRNA + S-adenosyl-L-homocysteine
Sequence Mass (Da): 27709
Sequence Length: 243
Subcellular Location: Cytoplasm
EC: 2.1.1.228
|
Q8A9C2 | MRIDIITVLPEMIEGFFNCSIMKRAQNKGLAEIHIHNLRDYTEDKYRRVDDYPFGGFAGMVMKIEPIERCINALKAERDYDEVIFTTPDGEQFNQPMANSLSLAQNLIILCGHFKGIDYRIREHLITKEISIGDYVLTGGELAAAVMADAIVRIIPGVISDEQSALSDSFQDNLLAAPVYTRPADYKGWKVPDILLSGHEAKIKEWELQQSLERTKKLRPDLLED | Function: Specifically methylates guanosine-37 in various tRNAs.
Catalytic Activity: guanosine(37) in tRNA + S-adenosyl-L-methionine = H(+) + N(1)-methylguanosine(37) in tRNA + S-adenosyl-L-homocysteine
Sequence Mass (Da): 25558
Sequence Length: 225
Subcellular Location: Cytoplasm
EC: 2.1.1.228
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Q6G1R9 | MKFQARVLTLYPEMFPGFLGCSLAGQALKQGIWSLETVQIRDFALDKHHSVDDTPAGGGAGMVMRADVLAAALDSCPNDSPRLLMSPRGRLLNQAYARSLARSSGVTLVCGRFEGVDERIIEARELEEVSIGDYILSGGETAALVLLDAIVRLLPGVMGNEISAKCESFENGLLEHPQYTRPAVFEGRGIPPVLTSGHHKAIANWRQQQAESLTRQRRPDLYALYNKNRQKT | Function: Specifically methylates guanosine-37 in various tRNAs.
Catalytic Activity: guanosine(37) in tRNA + S-adenosyl-L-methionine = H(+) + N(1)-methylguanosine(37) in tRNA + S-adenosyl-L-homocysteine
Sequence Mass (Da): 25463
Sequence Length: 232
Subcellular Location: Cytoplasm
EC: 2.1.1.228
|
Q5ZYH6 | MALHLGVITLLPEIIQGIHYGVTGRAIEQGLVKIDCWNPRDWSSRPYKQVDDKPYGGGPGMVMMYEPLHAAIKHARSEMKENCKTIYLSPQGKVVRQNDLKQIAAQKQSLLFVAGRYEGIDERIISHHVDEEWSLGDFVLSGGELAAMVFIDAIIRLIPGSLGHLGSAEQDSFMNGLLDCPHYTRPATINGLDVPDVLLGGNHKEIERWRRKQSLGKTWLKRPDLLEKVQLSETDKQLLAEFKCEHGDSC | Function: Specifically methylates guanosine-37 in various tRNAs.
Catalytic Activity: guanosine(37) in tRNA + S-adenosyl-L-methionine = H(+) + N(1)-methylguanosine(37) in tRNA + S-adenosyl-L-homocysteine
Sequence Mass (Da): 28022
Sequence Length: 250
Subcellular Location: Cytoplasm
EC: 2.1.1.228
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Q72S28 | MKFNFITLFPDKIQSYFSEGLQQKAIESGVFSVNIIQLRNFSGNKHNRVDDTIYGGGPGMLLRVEPIHKAILSLGEEKGIVILTSPSGIPFNQSIAMDLKKGGKPLTFISGYYEGVDHRVTEHLVDMEMSLGNYVLSAGDLASICIADAVSRLLPGFLGADESLLDESHNHPDILEYPQFTKPSEYNGWKVPDVLLSGNHASILAWREQNRKKIERGNYESTFKRSADSGC | Function: Specifically methylates guanosine-37 in various tRNAs.
Catalytic Activity: guanosine(37) in tRNA + S-adenosyl-L-methionine = H(+) + N(1)-methylguanosine(37) in tRNA + S-adenosyl-L-homocysteine
Sequence Mass (Da): 25594
Sequence Length: 231
Subcellular Location: Cytoplasm
EC: 2.1.1.228
|
Q8CX44 | MWLGVITLFPEMFRAVTDFGVTGRAVKNGLLELHTWNPRDFTHDRHSTVDDRPYGGGPGMLMMVQPLRDAIHAARAAAGEDAKVIYLSPQGRKLDQQGVTELAKSSRLILVCGRYEGIDERIIQTEVDEEWSVGDYVLSGGELPAMTMIDAVSRLVPGVLGKQASAEQDSFSDGLLDCPHYTRPESLDGLDVPAVLLSGNHEQIRLWRLQQSLGRTLLRRPELLQNLALTDEQSTLLAQFVEAMDKNA | Function: Specifically methylates guanosine-37 in various tRNAs.
Catalytic Activity: guanosine(37) in tRNA + S-adenosyl-L-methionine = H(+) + N(1)-methylguanosine(37) in tRNA + S-adenosyl-L-homocysteine
Sequence Mass (Da): 27451
Sequence Length: 248
Subcellular Location: Cytoplasm
EC: 2.1.1.228
|
Q7NFC3 | MIEPVRVIGGGIAGAEAAWQCARAGVPVVLSEMRPVRPSPAHHTDHLGELVCSNSFGAMATDRAPGLLKEELRRLGSLVIAVADAHAVPAGGALAVDRAVYTRELTERVANHPLIELRREEVTEIPAAGLVVFATGPLTSEPLAHGLQALTGLGYLSFFDAASPIVAGESLDTEKVFLASRYDRGEAAYYNCPMSEPEYRAFWEALASAEQAELKEFEHEERKFFEACLPVEELARRGYETLRYGPLKPVGLTDPRTGRWPFACVQLRQEDRAGRLWNLVGFQTNLKWGEQKRVFQMIPGLEQAEFVRLGVMHRNTFLCSPHLLAPTLQFHAHPRLLACGQLTGTEGYTAAVAGGWLAGTNAARLAQSRDPLVLPVETMAGALVDYVSHGDPKTFQPMPPNFALLPEITPRIRHKQQRYWAYRDRALAAIDTFGRTHGLGAAPALARAN | Function: Catalyzes the folate-dependent formation of 5-methyl-uridine at position 54 (M-5-U54) in all tRNAs.
Catalytic Activity: (6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + H(+) + NADH + uridine(54) in tRNA = (6S)-5,6,7,8-tetrahydrofolate + 5-methyluridine(54) in tRNA + NAD(+)
Sequence Mass (Da): 49166
Sequence Length: 449
Subcellular Location: Cytoplasm
EC: 2.1.1.74
|
B4U7L4 | MKVNVIGAGLAGSEAAYFLANKGIKVRMFEMRPITSHFTSRQDEKTGTHDVRNATQTRPITTTEAHKTDKFGELVCSNTLGSFEITTGAGLLKKEMELLNSLVIKAAKHSYVKAGSALAVDRNEFSDFITKTILSHPNIEVVREEVESLNENELNIVATGPLTSEKFSKYLKNLITDDYLYFYDAIAPIVEASSVDFSKGFWGSRYDKGDDYFNCTMTKEEYDIFYNELLKAEKVPTKDFERVVHFEGCLPIEEIASRGYETLVFGPMSPKGLKHHISKDVYAIVQLRKETKEGEALSLVGFQTKLTYKEQVRVFRLIPCLRNAVFSRLGSMHRNTFLQSNKLLKPTLELRKNPNILFAGQITGVEGYSASAATGIIAGINAWLKLEGKEPTTPPKTTMLGALLDYISSKEGELQPMNPVFGLLPDIEVHKKHKKLLKAYRALFDMKKFIEHHKIYD | Function: Catalyzes the folate-dependent formation of 5-methyl-uridine at position 54 (M-5-U54) in all tRNAs.
Catalytic Activity: (6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + H(+) + NADH + uridine(54) in tRNA = (6S)-5,6,7,8-tetrahydrofolate + 5-methyluridine(54) in tRNA + NAD(+)
Sequence Mass (Da): 51415
Sequence Length: 457
Subcellular Location: Cytoplasm
EC: 2.1.1.74
|
Q1IHM1 | MNLKIRIIGAGLAGCEAAWQCARRGLDVELYEMRPVKSTPAHQTSDFAELVCSNSLKSAGENSAPWLLKEEMRRGGSLLLEIAQKTSVPAGHALAVDRGAFAAEVTRVIEAEPRIRVVRGEVTKIDENDALTVIATGPLTSDALSQEIARLSGNTHLYFYDSISPIVEADSIDMSRVYMAARYDKGTADYINCPMNKEEYDRFLDALIEAHSVDAKEWENLNYFEGCLPIEEIARRGRDTLRFGPMKPVGLTDPKTGRYPYAVVQLRQENLRADSYNLVGFQNHLKYGDQARVMRLIPGLENAKFLRYGQIHRNTYINSPTLLTETLRMKEHPNVFFAGQISGVEGYVESIATGQMAGMHVSTVAMGHEPVAPPRATAFGSLVNYICHAEAKHFQPANITFDLLPQLDEAARRKVRDKKERHRMVCEAALKEFDGWLATSQIFQ | Function: Catalyzes the folate-dependent formation of 5-methyl-uridine at position 54 (M-5-U54) in all tRNAs.
Catalytic Activity: (6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + H(+) + NADH + uridine(54) in tRNA = (6S)-5,6,7,8-tetrahydrofolate + 5-methyluridine(54) in tRNA + NAD(+)
Sequence Mass (Da): 49565
Sequence Length: 444
Subcellular Location: Cytoplasm
EC: 2.1.1.74
|
Q88W23 | MASIPTVNVIGAGLAGSEAAWHIANMGVNVRLYEMRPNKMTPAHHTAQFAELVCTNSLRANQLANAAGLLKAEMRQMDSIVMQAAEHHAVPAGGALAVDRDTFSAEITAAITALPNVEIINEEITSLPDGITVVATGPLTAASLAKSIQAFNDEDDLHFFDAAAPILTKDSIDMDKVYLKSRYDRGEAAYLNCPMTEAEFDVFYDALIHAEMAEAHDFENSDVFEGCMPIEVMAQRGRQTMLFGPLKPVGLEDPKTGKQPFAVVQLRQDDAAGDLYNIVGFQTHLKWGEQKRVFSLIPGLENVEFVRYGVMHRNTFMKSPKLLTPTYQTQQRPDLFFAGQMTGVEGYIESAASGIVAGTNAARLALGLEPVVFPTDTMMGAMAHYITHTSASNFQPMNANFGIMPKLKQRIRDKRERNTAISERALADLTTFKDETLTVNN | Function: Catalyzes the folate-dependent formation of 5-methyl-uridine at position 54 (M-5-U54) in all tRNAs.
Catalytic Activity: (6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + H(+) + NADH + uridine(54) in tRNA = (6S)-5,6,7,8-tetrahydrofolate + 5-methyluridine(54) in tRNA + NAD(+)
Sequence Mass (Da): 48261
Sequence Length: 441
Subcellular Location: Cytoplasm
EC: 2.1.1.74
|
Q58871 | MIIMISVILVNPKYSGNVGSIARVMMNFGFEELRIVGDKSIINNEAYMMAVHAREILDNAKFYNTFDEAIGDLDFVIATSGARGGDRNLKRVPITPKELADKILEVKGNIGIVFGREDDGLRNEEIDKCDLLVSIPTSEKYPIMNLSHAVAVILYEIYTKKVRNKFLDINMREASKEDKELLIRKFNEFIDKNEKIPEHKKELCKIIFKRLVNRAFISGKEAWTLMSAFK | Function: Catalyzes the formation of 2'O-methylated cytidine (Cm32) at position 32 in tRNA.
Catalytic Activity: cytidine(32) in tRNA + S-adenosyl-L-methionine = 2'-O-methylcytidine(32) in tRNA + H(+) + S-adenosyl-L-homocysteine
Sequence Mass (Da): 26280
Sequence Length: 230
Subcellular Location: Cytoplasm
EC: 2.1.1.-
|
Q6D257 | MLDNIRIVLVETSHTGNMGSVARAMKTMGLSKLYLVNPLVKPDSQAIALAAGASDVIGNATLVDSLDQALEGCNLVVGTSARSRTLPWPMLEPRECGVRSAQEAEHAPVALVFGRERVGLTNDELQKCHYHVAIPANPEYSSLNLAMAVQIIAYEVRIAHLDRLQAGQPEHEESPYPLVDDLERFYQHLEQTLLQTGFIRPAHQGQVMNKLRRLFTRARPEAQELNILRGILSSVQKTHDE | Function: Catalyzes the formation of 2'O-methylated cytidine (Cm32) or 2'O-methylated uridine (Um32) at position 32 in tRNA.
Catalytic Activity: cytidine(32) in tRNA + S-adenosyl-L-methionine = 2'-O-methylcytidine(32) in tRNA + H(+) + S-adenosyl-L-homocysteine
Sequence Mass (Da): 26690
Sequence Length: 241
Subcellular Location: Cytoplasm
EC: 2.1.1.200
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A0A0H2ZF87 | MLDRIRVVLVNTSHPGNIGGAARAMKNMGLSQLVLVQPESFPHGDAVARASGATDILDAARVVDTLEEALSGCSVVLGTSARDRRIPWPLLDPRECATTCLEHLEANGEVALVFGREYAGLTNEELQRCQFHVHIPSDPEFGSLNLAAAVQVLTYEVRMAWLAAQGKPTKMEKFESTSMLNTELVTADELELYYAHLERTLIDIGFLDPEKPRHLMSRLRRLYGRSAISKLEMNILRGILTETQKVARGLSYKRSDD | Function: Catalyzes the formation of 2'O-methylated cytidine (Cm32), 2'O-methylated uridine (Um32) or 2'O-methylated adenosine (Am32) at position 32 in tRNA. Confers resistance to oxidative stress.
Catalytic Activity: cytidine(32) in tRNA + S-adenosyl-L-methionine = 2'-O-methylcytidine(32) in tRNA + H(+) + S-adenosyl-L-homocysteine
Sequence Mass (Da): 28486
Sequence Length: 257
Subcellular Location: Cytoplasm
EC: 2.1.1.-
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Q2NS29 | MLHNIRIVLVETSHTGNIGSTARAMKTMGLSNLYLVNPLHKPDAQAIALSAGASDIIGNASVVDNLDQALAGCSLVVGTSARSRTLPWPMLEPRECGVKSIQEAAQAPVALLFGRERVGLTNDELQKCHFHVQIPANHEYSSLNLAMAVQILAYEVRVAWLDSQRQDATVQEASVYPVAEDLERFYQHLEQVLSGTGFIRRAHPGLVMNKLRRLFNRARPESQELNILRGMLTSIEHTQKPETPAPDTGHGRPQA | Function: Catalyzes the formation of 2'O-methylated cytidine (Cm32) or 2'O-methylated uridine (Um32) at position 32 in tRNA.
Catalytic Activity: cytidine(32) in tRNA + S-adenosyl-L-methionine = 2'-O-methylcytidine(32) in tRNA + H(+) + S-adenosyl-L-homocysteine
Sequence Mass (Da): 28024
Sequence Length: 255
Subcellular Location: Cytoplasm
EC: 2.1.1.200
|
Q4JB16 | MTIRLVIVEPEGAYNLGFIARLVKNFLIDEFYVVNPKCDINEAIKFSAKGSEVIEKMMKITNNFDDAIRDVDLKIATSSIADIKGDLLRKSIRPIDLERLIKDKKVAFIFGRESVGLTREEIAKSDFLLFIPANPEYPVLNLSHAVGIVLYELWRNRDNKVPTVSSEPIKLIDDYSKKITDILVNKEATKSMYLVLKRVLIKGIEDNEEAMTIVRILRKIYVRLAKKENESDKLL | Function: Catalyzes the formation of 2'O-methylated cytidine (Cm32) at position 32 in tRNA. Is specific for cytidine.
Catalytic Activity: cytidine(32) in tRNA + S-adenosyl-L-methionine = 2'-O-methylcytidine(32) in tRNA + H(+) + S-adenosyl-L-homocysteine
Sequence Mass (Da): 26902
Sequence Length: 235
Subcellular Location: Cytoplasm
EC: 2.1.1.-
|
Q1C5G8 | MLHNIRIVLVETSHTGNMGSTARAMKTMGLTNLYLVNPLVKPDSQAIALSAGASDVIGKATIVDTLDEALAGCSLVVGTSARSRTLPWPMLEPRECGVRSAREAEHAPVALVFGRERVGLTNDELQKCHYHVAIPANPEYSSLNLAMAVQILAYEVRVAYLDRQQANAPVEEEEEAPYPLVDDLERFYQHLEQVLSHSGFIRQAHPGQIMSKLRRLFTRARPEAQELNILRGMLTSIEKQDKYPQRGTGDTAGKSKD | Function: Catalyzes the formation of 2'O-methylated cytidine (Cm32) or 2'O-methylated uridine (Um32) at position 32 in tRNA.
Catalytic Activity: cytidine(32) in tRNA + S-adenosyl-L-methionine = 2'-O-methylcytidine(32) in tRNA + H(+) + S-adenosyl-L-homocysteine
Sequence Mass (Da): 28385
Sequence Length: 257
Subcellular Location: Cytoplasm
EC: 2.1.1.200
|
Q72IH5 | MWLEATTHPGLEDLLLEELSALYPGEGAEVDARKGRVRIPRAWVGEEALGLRLAHHLVLFRARLLLSREDPLGALERAALALPWPELEGAGSFRVEARREGEHPFTSPEVERRVGEALHRAYGVPVDLKRPAVRVRVDVRGEEAFLGVQLTERPLSRRFPKAALRGSLTPVLAQALLRLADARPGMRVLDPFTGSGTIALEAASTLGPTSPVYAGDLDEKRLGLAREAALASGLSWIRFLRADARHLPRFFPEVDRILANPPHGLRLGRKEGLFHLYWDFLRGALALLPPGGRVALLTLRPALLKRALPPGFALRHARVVEQGGVYPRVFVLEKL | Function: S-adenosyl-L-methionine-dependent methyltransferase that catalyzes the methylation of the guanosine nucleotide at position 6 (m2G6) in tRNA(Phe).
Catalytic Activity: guanosine(6) in tRNA + S-adenosyl-L-methionine = H(+) + N(2)-methylguanosine(6) in tRNA + S-adenosyl-L-homocysteine
Sequence Mass (Da): 36980
Sequence Length: 335
Domain: Consists of an N-terminal THUMP domain fused to a catalytic Rossmann-fold MTase (RFM) domain.
Subcellular Location: Cytoplasm
EC: 2.1.1.256
|
P28634 | MSSFQFEQIGVIRSPYKEKFAVPRQPGLVKSANGELHLIAPYNQADAVRGLEAFSHLWILFVFHQTMEGGWRPTVRPPRLGGNARMGVFATRSTFRPNPIGMSLVELKEVVCHKDSVILKLGSLDLVDGTPVVDIKPYLPFAESLPDASASYAQSAPAAEMAVSFTAEVEKQLLTLEKRYPQLTLFIREVLAQDPRPAYRKGEETGKTYAVWLHDFNVRWRVTDAGFEVFALEPR | Function: S-adenosyl-L-methionine-dependent methyltransferase responsible for the addition of the methyl group in the formation of N6-methyl-N6-threonylcarbamoyladenosine at position 37 (m(6)t(6)A37) of the tRNA anticodon loop of tRNA(Thr)(GGU) that read codons starting with adenosine . The methyl group of m(6)t(6)A37 appears to slightly improve the efficiency of the tRNA decoding ability .
Catalytic Activity: N(6)-L-threonylcarbamoyladenosine(37) in tRNA + S-adenosyl-L-methionine = H(+) + N(6)-methyl,N(6)-L-threonylcarbamoyladenosine(37) in tRNA + S-adenosyl-L-homocysteine
Sequence Mass (Da): 26362
Sequence Length: 235
EC: 2.1.1.-
|
P37752 | SFSHIWVQFVFHGVAGAGWQPLVRPPRLGGNRKMGVFATRSPFRPNPLGLSLLKLERIETEGGVRLWCGGADLLDGTPVLDIKPYLPFVEAQPDAAPGFAAVPPVPLEVAWADEISAASLPPPNRLLIEQSIAQDPRPAYQDTPQRVYKMAVDDWEVAFRIEKGMALIEAVMAVEG | Function: S-adenosyl-L-methionine-dependent methyltransferase responsible for the addition of the methyl group in the formation of N6-methyl-N6-threonylcarbamoyladenosine at position 37 (m(6)t(6)A37) of the tRNA anticodon loop of tRNA(Thr)(GGU). The methyl group of m(6)t(6)A37 appears to slightly improve the efficiency of the tRNA decoding ability. Binds to tRNA.
Catalytic Activity: N(6)-L-threonylcarbamoyladenosine(37) in tRNA + S-adenosyl-L-methionine = H(+) + N(6)-methyl,N(6)-L-threonylcarbamoyladenosine(37) in tRNA + S-adenosyl-L-homocysteine
Sequence Mass (Da): 19221
Sequence Length: 176
EC: 2.1.1.-
|
P44740 | MNDLTLSPIAIIHTPYKEKFSVPRQPNLVEDGVGIVELLPPYNSPEAVRGLEQFSHLWLIFQFDQIQQGKWQPTVRPPRLGGNQRVGVFASRATHRPNPLGLSKVELRQVECINGNIFLHLGAVDLVDGTPIFDIKPYIAYADSEPNAQSSFAQEKLPVKLTVEFTEQAKSAVKKREEKRPHLSRFIRQVLEQDPRPAYQQGKPSDRIYGMSLYEFNVKWRIKAGTVNCVEVIEIEKDK | Function: S-adenosyl-L-methionine-dependent methyltransferase responsible for the addition of the methyl group in the formation of N6-methyl-N6-threonylcarbamoyladenosine at position 37 (m(6)t(6)A37) of the tRNA anticodon loop of tRNA(Thr)(GGU). The methyl group of m(6)t(6)A37 appears to slightly improve the efficiency of the tRNA decoding ability. Binds to tRNA.
Catalytic Activity: N(6)-L-threonylcarbamoyladenosine(37) in tRNA + S-adenosyl-L-methionine = H(+) + N(6)-methyl,N(6)-L-threonylcarbamoyladenosine(37) in tRNA + S-adenosyl-L-homocysteine
Sequence Mass (Da): 27214
Sequence Length: 239
EC: 2.1.1.-
|
Q9BU70 | MRGLEESGPRPTATPCGCVKPALETGNLLTEPVGYLESCFSAKNGTPRQPSICSYSRACLRIRKRIFNNPEHSLMGLEQFSHVWILFVFHKNGHLSCKAKVQPPRLNGAKTGVFSTRSPHRPNAIGLTLAKLEKVEGGAIYLSGIDMIHGTPVLDIKPYIAEYDSPQNVMEPLADFNLQNNQHTPNTVSQSDSKTDSCDQRQLSGCDEPQPHHSTKRKPKCPEDRTSEENYLTHSDTARIQQAFPMHREIAVDFGLESRRDQSSSVAEEQIGPYCPEKSFSEKGTDKKLERVEGAAVLQGSRAETQPMAPHCPAGRADGAPRSVVPAWVTEAPVATLEVRFTPHAEMDLGQLSSQDVGQASFKYFQSAEEAKRAIEAVLSADPRSVYRRKLCQDRLFYFTVDIAHVTCWFGDGFAEVLRIKPASEPVHMTGPVGSLVSLGS | Function: S-adenosyl-L-methionine-dependent methyltransferase responsible for the addition of the methyl group in the formation of N6-methyl-N6-threonylcarbamoyladenosine at position 37 (m(6)t(6)A37) of the tRNA anticodon loop of tRNA(Ser)(GCU) . The methyl group of m(6)t(6)A37 may improve the efficiency of the tRNA decoding ability (By similarity).
Catalytic Activity: N(6)-L-threonylcarbamoyladenosine(37) in tRNA + S-adenosyl-L-methionine = H(+) + N(6)-methyl,N(6)-L-threonylcarbamoyladenosine(37) in tRNA + S-adenosyl-L-homocysteine
Sequence Mass (Da): 48587
Sequence Length: 441
EC: 2.1.1.-
|
O32036 | MTDRYEQINDYIEALLKPRPDNVKRLEAYAEEHHVPIMEKAGMEVLLQILSVKQPKKILEIGTAIGYSAIRMALELPSAEIYTIERNEKRHEEAVNNIKEFQLDDRIHVFYGDALELADAVHVTAPYDVIFIDAAKGQYQNFFHLYEPMLSPDGVIITDNVLFKGLVAEDYSKIEPKRRRRLVAKIDEYNHWLMNHPDYQTAIIPVGDGLAISKKKR | Function: Catalyzes the methylation of 5-hydroxyuridine (ho5U) to form 5-methoxyuridine (mo5U) at position 34 in tRNAs.
Catalytic Activity: 5-hydroxyuridine(34) in tRNA + S-adenosyl-L-methionine = 5-methoxyuridine(34) in tRNA + H(+) + S-adenosyl-L-homocysteine
Sequence Mass (Da): 25063
Sequence Length: 217
EC: 2.1.1.-
|
B6YR34 | MNKITTLFQNRQRNIVSIYFTAGFPQLNDTIEIIKELQINGIDMIEVGVPFSDPIADGKVIQASSYKAIQNGMNLKILFKQLEAIKSKIQIPLIIMSYLNPIIQYGFENFCEDCHKIDISGIIIPDLPFEEYINEYKFITDAYDLKMIMLISPKTSEERIRLIDSNVEGFIYMVSSAATTGIQESFDEQKQEYFRRINSMKLRNPRLIGFGISNKETLTVALENASGVIIGSKFVSLLAEENNPKKAVQKLLAELK | Function: The alpha subunit is responsible for the aldol cleavage of indoleglycerol phosphate to indole and glyceraldehyde 3-phosphate.
Catalytic Activity: (1S,2R)-1-C-(indol-3-yl)glycerol 3-phosphate + L-serine = D-glyceraldehyde 3-phosphate + H2O + L-tryptophan
Sequence Mass (Da): 29090
Sequence Length: 256
Pathway: Amino-acid biosynthesis; L-tryptophan biosynthesis; L-tryptophan from chorismate: step 5/5.
EC: 4.2.1.20
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A1K4B0 | MSKIQTTFQRLQAQGRKALIPFITAGDPDPTLTVPLMHALVAGGADIIELGVPFSDPMADGPTIQRASERALAQGMTLRKVLQAVREFRSGDADTPVVLMGYANPIEAMGQQAFVAAAREAGVDGALVVDYPPEECVEFAAASKAAGLDPIFLLAPTSSEQRFADVARAGSGYIYYVSLKGVTGAGTLDLDEVARRIPQIRAAVGMPVGVGFGIRDAESARRIGAVADAVVIGSRIIEEIERSPREQACSNVTHFVKGIREALDTLPGVKQ | Function: The alpha subunit is responsible for the aldol cleavage of indoleglycerol phosphate to indole and glyceraldehyde 3-phosphate.
Catalytic Activity: (1S,2R)-1-C-(indol-3-yl)glycerol 3-phosphate + L-serine = D-glyceraldehyde 3-phosphate + H2O + L-tryptophan
Sequence Mass (Da): 28616
Sequence Length: 271
Pathway: Amino-acid biosynthesis; L-tryptophan biosynthesis; L-tryptophan from chorismate: step 5/5.
EC: 4.2.1.20
|
Q81GG4 | MGVEKIKAAFENGKKAFIPYVMGGDGGLEKLKERIRFLDEAGASIVEIGIPFSDPVADGPTIQRAGKRALDSGVTLKGIFQALAEVRKEVQMPFVLMTYLNPVLAFGKERFIENCIEAGVDGIIVPDLPYEEQNIIAPLLREVNIALIPLVTVTSPIERIEKITSESEGFVYAVTVAGVTGVRQNFKEEIHSYLEKVKSHVNLPVVAGFGISTKEHVEEMVTICDGVVVGSKVIELLENEKREEICELIYATKQKEEA | Function: The alpha subunit is responsible for the aldol cleavage of indoleglycerol phosphate to indole and glyceraldehyde 3-phosphate.
Catalytic Activity: (1S,2R)-1-C-(indol-3-yl)glycerol 3-phosphate + L-serine = D-glyceraldehyde 3-phosphate + H2O + L-tryptophan
Sequence Mass (Da): 28332
Sequence Length: 258
Pathway: Amino-acid biosynthesis; L-tryptophan biosynthesis; L-tryptophan from chorismate: step 5/5.
EC: 4.2.1.20
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Q2S1Z2 | MSRLDETFDALGPDEKAMGLFLTDGFPNPDATVPLLHAIDRGGADFIELGMPFSDPLAEGRPIQRASARALSHGVTLPDTLRTVEAFREDSDTPLLLMGYVNPVFKYGVDAFCRDAAEAGVDGLILPDLPPQESDALCDAAAAHGLELVFLIAPNTSDERIRVVDERATGFVYAVSVTGLTGSDLAETPSVDEYLMHARDFVAQNPLLVGFGIKTHDDAMELSRHTDGFIVGSALINRVEALWEDPERSTTDRLDTVEGFARHLKSGTPVPTPQPNPA | Function: The alpha subunit is responsible for the aldol cleavage of indoleglycerol phosphate to indole and glyceraldehyde 3-phosphate.
Catalytic Activity: (1S,2R)-1-C-(indol-3-yl)glycerol 3-phosphate + L-serine = D-glyceraldehyde 3-phosphate + H2O + L-tryptophan
Sequence Mass (Da): 29956
Sequence Length: 278
Pathway: Amino-acid biosynthesis; L-tryptophan biosynthesis; L-tryptophan from chorismate: step 5/5.
EC: 4.2.1.20
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Q8ECU9 | MNSISNQTIPHQASRYQAAFSRLKAEGRGAFVPFVTLGDPSPELSLKIIDTLVQNGADALELGFPFSDPLADGPVIQGANLRALAAGTTPTACFELLAKIRAKYPELPIGLLLYANLVFANGIDAFYAKAQQAGVDSVLIADVPVEEAAPFIQAAKAHGIAPIFIAPPNADSDTLAKVSQSGEGYTYLLSRAGVTGADTKAGTPVEEILAKLQEFNAPPPLLGFGIAEPAQVSAAIKAGAAGAISGSAVVKIIETHQQDEVKLLAALGEFTRTMKAAT | Function: The alpha subunit is responsible for the aldol cleavage of indoleglycerol phosphate to indole and glyceraldehyde 3-phosphate.
Catalytic Activity: (1S,2R)-1-C-(indol-3-yl)glycerol 3-phosphate + L-serine = D-glyceraldehyde 3-phosphate + H2O + L-tryptophan
Sequence Mass (Da): 28808
Sequence Length: 278
Pathway: Amino-acid biosynthesis; L-tryptophan biosynthesis; L-tryptophan from chorismate: step 5/5.
EC: 4.2.1.20
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Q59169 | MTLLNSYFGSFGGMYVPQILMPALYQLESEFVLSLKNLQFKKKLANLLKNYAGRPTPLTLCRNLTKGTNTRIYLKREDLLHGGAHKTNQVLGQALLAKQMKKKEIIAETGAGQHGVAAALSCALLNLKCRIYMGIKDIERQKQNVFRMKLMGAQVIPVKSGNGTLKDACNEALRDWSENYINAHYMLGTAAGPHPYPTIVKQFQSVIGKETKQQIFEKEHCLPNSVIACVGGGSNAIGIFSSFIEDTSVNLIGVEPGGIGIHTEKHGASLICGETGIFFGMKSKVMQTHEGQIKESWSISAGLDFPAVGPEHAWLDSIKRVTYVSITDSEAVHAFQHLSKLEGIIPALESSHALAYAIKLMNNYPNKNQTLIVNISGRGDKDLKTVEKFLNK | Function: The beta subunit is responsible for the synthesis of L-tryptophan from indole and L-serine.
Catalytic Activity: (1S,2R)-1-C-(indol-3-yl)glycerol 3-phosphate + L-serine = D-glyceraldehyde 3-phosphate + H2O + L-tryptophan
Sequence Mass (Da): 43033
Sequence Length: 392
Pathway: Amino-acid biosynthesis; L-tryptophan biosynthesis; L-tryptophan from chorismate: step 5/5.
EC: 4.2.1.20
|
Q8ZV44 | MVDRWYNIAADLPSVLAPPRDPDEGESRIGLLSKILPSALIDQEFTAERWVSIPEEVREAYRRVGRPTPLFRAEGLEKALGTGVRIYYKYEGVLPVGSHKLNTALAQAYYAKADGAVEVATETGAGQWGMAVSLAAALFGLRAVVFMTRSSYNSKRQRLTFMRAYGAVVYPSPSDVTEAGRRHYRPDHPGSLGIAISEAVEYVLSGERRKYLPGSVMEFVLLHQTVIGLEAVRQLPEEPDVAVACVGGGSNFAGFTYPMIGMKLRGEGFGRTRFVAVESEAAPKLTRGEYKYDFPDAVGVLPMLKMYTLGHDYVPPAIHAAGLRYHGAAPSLSLLRKLGIVEAVAYPQEEVMRAALLFARTEGIVPAPESAHAIKAAVDLAKKLPRGSVIAFNLSGHGLLDSDAYEKFLG | Function: The beta subunit is responsible for the synthesis of L-tryptophan from indole and L-serine.
Catalytic Activity: (1S,2R)-1-C-(indol-3-yl)glycerol 3-phosphate + L-serine = D-glyceraldehyde 3-phosphate + H2O + L-tryptophan
Sequence Mass (Da): 44572
Sequence Length: 410
Pathway: Amino-acid biosynthesis; L-tryptophan biosynthesis; L-tryptophan from chorismate: step 5/5.
EC: 4.2.1.20
|
Q2KE82 | MNETPKPNSFRSGPDEDGRFGIYGGRFVAETLMPLILDLQDEWNKAKSDPAFQAELKHLGAHYIGRPSPLYFAERLTAELGGAKIYFKREELNHTGSHKINNCIGQILLAKRMGKTRIIAETGAGQHGVASATVAARFGLPCVVYMGATDVERQAPNVFRMKLLGAEVKPVTAGSGTLKDAMNEALRDWVTNVEDTYYLIGTAAGPHPYPEMVRDFQSVIGAEAKEQMLAAEGRLPDLVVAAVGGGSNAIGIFHPFLDDSSVKIVGVEAGGKGLQGDEHCASITAGSPGVLHGNRTYLLQDGDGQIKEGHSISAGLDYPGIGPEHSWLSDIGRVDYVPIMDHEALEAFQTLTRLEGIIPALEAAHAIAEVIKRAPKMGKDEIILMNLSGRGDKDIFTVGKILGMGL | Function: The beta subunit is responsible for the synthesis of L-tryptophan from indole and L-serine. Essential for production of nod factors and establishment of symbiosis.
Catalytic Activity: (1S,2R)-1-C-(indol-3-yl)glycerol 3-phosphate + L-serine = D-glyceraldehyde 3-phosphate + H2O + L-tryptophan
Sequence Mass (Da): 43538
Sequence Length: 406
Pathway: Amino-acid biosynthesis; L-tryptophan biosynthesis; L-tryptophan from chorismate: step 5/5.
EC: 4.2.1.20
|
Q7UKG9 | MSTAPSQQHASAQVPDPRGRFGDFGGRFVPETLTRALDELSEEYEKAKRDPEFQRELDGLLKTFVGRPSPLYHAKRLSSAVGGAQIWLKREDLNHTGAHKINNTIGQALLTLRMGKTRVIAETGAGQHGVASATACAHFGLPCTVYMGAEDIRRQKPNVFSMKLLGANISAVESGSRTLRDAVNEAMRDWMSSVEDTHYIIGSVIGPHPFPMMVRDFQSVIGRETREQCRDTFGRLPDCVVACVGGGSNAAGMFYPFVEDEGVRMVGVEAGGRSATPGDHASPLSYGNPGVLHGSYSYVMQDEDGQTCDVHSMSAGLDYPGVGPEHSYWKDTKRVDYIDCRDDEALTAFERLASSEGILAALETSHAVAKAIEIAGKMSDQEHLVICLSGRGDKDSMEIARLRGEEW | Function: The beta subunit is responsible for the synthesis of L-tryptophan from indole and L-serine.
Catalytic Activity: (1S,2R)-1-C-(indol-3-yl)glycerol 3-phosphate + L-serine = D-glyceraldehyde 3-phosphate + H2O + L-tryptophan
Sequence Mass (Da): 44283
Sequence Length: 407
Pathway: Amino-acid biosynthesis; L-tryptophan biosynthesis; L-tryptophan from chorismate: step 5/5.
EC: 4.2.1.20
|
Q9Y210 | MSQSPAFGPRRGSSPRGAAGAAARRNESQDYLLMDSELGEDGCPQAPLPCYGYYPCFRGSDNRLAHRRQTVLREKGRRLANRGPAYMFSDRSTSLSIEEERFLDAAEYGNIPVVRKMLEECHSLNVNCVDYMGQNALQLAVANEHLEITELLLKKENLSRVGDALLLAISKGYVRIVEAILSHPAFAEGKRLATSPSQSELQQDDFYAYDEDGTRFSHDVTPIILAAHCQEYEIVHTLLRKGARIERPHDYFCKCNDCNQKQKHDSFSHSRSRINAYKGLASPAYLSLSSEDPVMTALELSNELAVLANIEKEFKNDYKKLSMQCKDFVVGLLDLCRNTEEVEAILNGDVETLQSGDHGRPNLSRLKLAIKYEVKKFVAHPNCQQQLLSIWYENLSGLRQQTMAVKFLVVLAVAIGLPFLALIYWFAPCSKMGKIMRGPFMKFVAHAASFTIFLGLLVMNAADRFEGTKLLPNETSTDNAKQLFRMKTSCFSWMEMLIISWVIGMIWAECKEIWTQGPKEYLFELWNMLDFGMLAIFAASFIARFMAFWHASKAQSIIDANDTLKDLTKVTLGDNVKYYNLARIKWDPSDPQIISEGLYAIAVVLSFSRIAYILPANESFGPLQISLGRTVKDIFKFMVIFIMVFVAFMIGMFNLYSYYIGAKQNEAFTTVEESFKTLFWAIFGLSEVKSVVINYNHKFIENIGYVLYGVYNVTMVIVLLNMLIAMINSSFQEIEDDADVEWKFARAKLWFSYFEEGRTLPVPFNLVPSPKSLFYLLLKLKKWISELFQGHKKGFQEDAEMNKINEEKKLGILGSHEDLSKLSLDKKQVGHNKQPSIRSSEDFHLNSFNNPPRQYQKIMKRLIKRYVLQAQIDKESDEVNEGELKEIKQDISSLRYELLEEKSQNTEDLAELIRELGEKLSMEPNQEETNR | Function: Thought to form a receptor-activated non-selective calcium permeant cation channel . Probably is operated by a phosphatidylinositol second messenger system activated by receptor tyrosine kinases or G-protein coupled receptors. Activated by diacylglycerol (DAG) in a membrane-delimited fashion, independently of protein kinase C . Seems not to be activated by intracellular calcium store depletion.
PTM: Phosphorylated by FYN, leading to an increase of TRPC6 channel activity.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 106326
Sequence Length: 931
Subcellular Location: Cell membrane
|
Q9WVC5 | MLGSNTFKNMQRRHTTLREKGRRQAIRGPAYMFNEKGTSLTPEEERFLDSAEYGNIPVVRKMLEESKTLNFNCVDYMGQNALQLAVGNEHLEVTELLLKKENLARVGDALLLAISKGYVRIVEAILSHPAFAQGQRLTLSPLEQELRDDDFYAYDEDGTRFSHDITPIILAAHCQEYEIVHILLLKGARIERPHDYFCKCNECTEKQRKDSFSHSRSRMNAYKGLASAAYLSLSSEDPVLTALELSNELARLANIETEFKNDYRKLSMQCKDFVVGVLDLCRDTEEVEAILNGDVNLQVWSDHHRPSLSRIKLAIKYEVKKFVAHPNCQQQLLTMWYENLSGLRQQSIAVKFLAVFGVSIGLPFLAIAYWIAPCSKLGQTLRSPFMKFVAHAVSFTIFLGLLVVNASDRFEGVKTLPNETFTDYPKQIFRVKTTQFSWTEMLIMKWVLGMIWSECKEIWEEGPREYVLHLWNLLDFGMLSIFVASFTARFMAFLKASEAQLYVDQYVQDVTLHNVSLPPEVAYFTYARDKWWPSDPQIISEGLYAIAVVLSFSRIAYILPANESFGPLQISLGRTVKDIFKFMVIFIMVFVAFMIGMFNLYSYYRGAKYNPAFTTVEESFKTLFWSIFGLSEVISVVLKYDHKFIENIGYVLYGVYNVTMVVVLLNMLIAMINNSYQEIEEDADVEWKFARAKLWLSYFDEGRTLPAPFNLVPSPKSFYYLIMRIKMCLIELCQSKAKRCENDLEMGMLNSKFRKTRYQAGMRNSENLTANSTFSKPTRYQKIMKRLIKRYVLKAQVDRENDEVNEGELKEIKQDISSLRYELLEEKSQATGELADLIQQLSEKFGKNLNKDHLRVNQGKDI | Function: Thought to form a receptor-activated non-selective calcium permeant cation channel. Probably is operated by a phosphatidylinositol second messenger system activated by receptor tyrosine kinases or G-protein coupled receptors. Activated by diacylglycerol (DAG). May also be activated by intracellular calcium store depletion.
PTM: Phosphorylation by PRKG1 at Thr-15 negatively regulates TRPC7 activity.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 99475
Sequence Length: 862
Subcellular Location: Cell membrane
|
O28668 | MMDFGFVDSLKGASKRGKNAVIAEVKVRSPIHGDLLRGRRIEDILRAYEKAGAAAISYITAEQFSGNFETLKKIVGLTDLPVLRKDFIRGRKEVERTAEVEAAALLLIARHLKERTAEMVDFCFEHGIEPLVEVHHAEDLVYAENARAVLINNRDIDRMERDGGSIDVTAKIAEKIRAFKVSGSGIGSVEDLLFVLQYVDAALIGTAFMMAENTEEFVQTVCGGEKMIEDVLRGLDFDKAYELAKTLPELDEIKIAAVLAALEAKGYGAEVIAGFAKGVAEKSKIEIGKVMDTCGTGGDKTSSINVSTAVAIALSTVHPVAKHGNRAVSSKSGSADVLEALGVRIEMDEERARKMIAETNFAFLFAPLYHKSFARVAAVRRNLGIRTIFNVTGPLTNPARPEVQIVGVASEILLVEVAKAMSLLGRRAVVVYGSGMDEVNPNSSTDIAVVNGGVERLKLEPEDFGIERCRVLPCSSSGESAERIRAVFSGKGLKEDRRLIAINFATALFALGYEDLKENVEIFEEKVQSGELARKLEEIACKSTSM | Cofactor: Binds 2 magnesium ions per monomer.
Function: Bifunctional enzyme that catalyzes the second and fourth steps of tryptophan biosynthetic pathway. The second step is catalyzed by the anthranilate phosphoribosyltransferase, coded by the TrpD domain and the fourth step is catalyzed by indole-3-glycerol phosphate synthase, coded by the TrpC domain (By similarity).
Catalytic Activity: 1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate + H(+) = (1S,2R)-1-C-(indol-3-yl)glycerol 3-phosphate + CO2 + H2O
Sequence Mass (Da): 59328
Sequence Length: 546
Pathway: Amino-acid biosynthesis; L-tryptophan biosynthesis; L-tryptophan from chorismate: step 2/5.
|
A3DDS7 | MILDEIVAQKKIQLKKDMSRITIEGWKQKIKRPGIHKPLDFYGALKNNGDISIIAEVKKASPSKGIIKEDFDPLKIAKEYVESDIQAISVLTERNFFKGDEDYLVKIRQFCPLPILRKDFIIDLWQIYESRYIGADAILLIVSLLSDEELKKFQIVANILGMQCLVEVHDERELERALESGARIIGINNRDLRTFEVDLKNTEKLMNRIPNDRVVVSESGIKDTEDLKYLKELGVDAVLIGETFMRARSISEKIREFKAV | Catalytic Activity: 1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate + H(+) = (1S,2R)-1-C-(indol-3-yl)glycerol 3-phosphate + CO2 + H2O
Sequence Mass (Da): 29895
Sequence Length: 260
Pathway: Amino-acid biosynthesis; L-tryptophan biosynthesis; L-tryptophan from chorismate: step 4/5.
EC: 4.1.1.48
|
P00911 | MIQIQNTILGKIVDRKHEELADRLKQRNLKDVEQWVKEAPPVRGFAQSLRSKRPGVIAEIKKASPSKGVIRADFNPAEIAQQYEQAGAACLSVLTDVDFFQGADENIAIARQHCSLPALRKDFLIDPYNVVEARALQADCILLIVACLSDQQLEEMSKTAFEYDLDVLVEVHDEQELERALKLSEQCLLGVNNRNLKTFDVDLNTSLRLKKLLDPSRLLVTESGIATPQDVQLMQEHDIHSFLVGESFMKQPRPDQAFTELFGVPKLV | Catalytic Activity: 1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate + H(+) = (1S,2R)-1-C-(indol-3-yl)glycerol 3-phosphate + CO2 + H2O
Sequence Mass (Da): 30189
Sequence Length: 268
Pathway: Amino-acid biosynthesis; L-tryptophan biosynthesis; L-tryptophan from chorismate: step 4/5.
EC: 4.1.1.48
|
Q8CPB2 | MTILNEIIEYKKTLLERKYYDKKLEILQDNGNVKRRKLIDSLNYDRTLSVIAEIKSKSPSVPQLPQRDLVQQVKDYQKYGANAISILTDEKYFGGSFERLNQLSKITSLPVLCKDFIIDKIQIDVAKRAGASIILLIVNILSDDQLKELYSYAINHNLEVLVEVHTIRELERAHQINPKIIGVNNRDLKRFETDVLHTNKLLKFKKSNCCYISESGIHTKEDVEKIVDSNIDGLLVGEALMKTNDLSQFLPSLKLKKNLYDS | Catalytic Activity: 1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate + H(+) = (1S,2R)-1-C-(indol-3-yl)glycerol 3-phosphate + CO2 + H2O
Sequence Mass (Da): 30123
Sequence Length: 262
Pathway: Amino-acid biosynthesis; L-tryptophan biosynthesis; L-tryptophan from chorismate: step 4/5.
EC: 4.1.1.48
|
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