ids stringlengths 6 10 | seqs stringlengths 11 1.02k | texts stringlengths 108 11.1k |
|---|---|---|
Q2Y8V8 | MSQSNLQRSMPIVTLPDLFDARFDNRFVRQLPGDPETRNVPRQVRNAGYTQVSPTPVRSPRLLAWADEVGEMLGIARPASPVSPAVEVLAGNRILPSMQPYAARYGGHQFGHWAGQLGDGRAITLGELISPNDKRYELQLKGAGKTPYSRTADGRAVLRSSVREFLCSEAMHSLGVPTTRALSLVATGEAVIRDMFYDGHPGAEPGAIVCRVSPSFLRFGNFEILAAQKEPELLRQLADFVIGEHFPELASSHRPPEVYAKWFEEVCRRTGILVAHWMRVGFVHGVMNTDNMSILGLTIDYGPYGWLEGFDLHWTPNTTD... | Function: Catalyzes the transfer of adenosine 5'-monophosphate (AMP) to Ser, Thr or Tyr residues of target proteins (AMPylation).
Catalytic Activity: ATP + L-tyrosyl-[protein] = diphosphate + O-(5'-adenylyl)-L-tyrosyl-[protein]
Sequence Mass (Da): 63264
Sequence Length: 565
EC: 2.7.7.108
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Q3JD89 | MPSSTAMKHQDIGWHFDNTYAQLPGHFYTKLHPVPVHEPRLVIVNNALAEELGLNFKASSEDELAQLFSGNQLPEGAEPLAQAYAGHQFGHFTYLGDGRAHLIGEHLTPDGKRVDIQFKGSGQTPYARRGDGRAALGPMLREYIISEAMHALGIPTTRSLAIATTGESVYRETVLQGAILTRVASSHLRVGTFEYLAAQEDKAGLKQLTDYAIQRHYPEIIDSDTPYLELLKAVMACQIKLITEWLRVGFIHGVMNTDNMAVSCQTIDYGPCAFMDNYDPNTVFSSIDHMGRYAYANQPRIAQWNLARFAEAILPLLHEN... | Function: Catalyzes the transfer of adenosine 5'-monophosphate (AMP) to Ser, Thr or Tyr residues of target proteins (AMPylation).
Catalytic Activity: ATP + L-tyrosyl-[protein] = diphosphate + O-(5'-adenylyl)-L-tyrosyl-[protein]
Sequence Mass (Da): 56033
Sequence Length: 493
EC: 2.7.7.108
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Q88PM7 | MRPDCTDFRQLFLDDVPMMDMRAPVEFAKGAFPGVVNLPLMNDQERQKVGTCYKQQGQAAAIALGHQLVSGATKQARLEAWAAFAKAHPDGYLYCFRGGLRSQIVQGWLRDEAGIQYPRVKGGYKAMRTFLLETTQQAVEQCDFVLVGGLTGTGKTDVLHQLDNVLDLEGHANHRGSSFGKRATAQPAQIDFENQLAIDVLKKRARGIGQFVLEDEGRIVGSCTVPLELYQGMQHYPLVWLEDSFTNRVERILRDYVVNLSAEFKAVHGEEDGPRLFAERMLQSMANIYKRLGGERHQRLSEMLREALQEQQRSGAVDLH... | Function: Involved in the post-transcriptional modification of the uridine at the wobble position (U34) of tRNA(Lys), tRNA(Glu) and tRNA(Gln). Catalyzes the conversion of 2-thiouridine (S2U-RNA) to 2-selenouridine (Se2U-RNA). Acts in a two-step process involving geranylation of 2-thiouridine (S2U) to S-geranyl-2-thiour... |
A1SRN6 | MQQSDLQEQQLYRSLFLLKTPLIDLRAPVEFAQGAFPESCNLPLMTDNEREQVGTCYKKEGQAAAITLGHQLVASDIQNRIRKWAQFKEENPTAWLYCFRGGLRSRLSAQFLKDHGVDINIVPGGYKALRRYLINVIDQASEKKLMIVGGNTGCGKTLLIQALDNGLDIEGRANHRGSSFGKQVTEQPRQISYENQLAVDILHISQHASSLVIEDESKAVGALYVPERLFAGMTRAPMVVVNDPLEIRLQRLCYEYCTLMTEKFNLALGAEQGWQAYEKYLQNGLYGIRKRLGTEKFKVMNTVLEAALKQQKNTGSVEGH... | Function: Involved in the post-transcriptional modification of the uridine at the wobble position (U34) of tRNA(Lys), tRNA(Glu) and tRNA(Gln). Catalyzes the conversion of 2-thiouridine (S2U-RNA) to 2-selenouridine (Se2U-RNA). Acts in a two-step process involving geranylation of 2-thiouridine (S2U) to S-geranyl-2-thiour... |
Q9H4L4 | MKETIQGTGSWGPEPPGPGIPPAYSSPRRERLRWPPPPKPRLKSGGGFGPDPGSGTTVPARRLPVPRPSFDASASEEEEEEEEEEDEDEEEEVAAWRLPPRWSQLGTSQRPRPSRPTHRKTCSQRRRRAMRAFRMLLYSKSTSLTFHWKLWGRHRGRRRGLAHPKNHLSPQQGGATPQVPSPCCRFDSPRGPPPPRLGLLGALMAEDGVRGSPPVPSGPPMEEDGLRWTPKSPLDPDSGLLSCTLPNGFGGQSGPEGERSLAPPDASILISNVCSIGDHVAQELFQGSDLGMAEEAERPGEKAGQHSPLREEHVTCVQSI... | Function: Protease that releases SUMO2 and SUMO3 monomers from sumoylated substrates, but has only weak activity against SUMO1 conjugates . Deconjugates SUMO2 from MEF2D, which increases its transcriptional activation capability . Deconjugates SUMO2 and SUMO3 from CDCA8 . Redox sensor that, when redistributed into nucl... |
Q9EP97 | MKETIQGTGSWGPEPPGPGTTYSNPRRERLRWPLPPKPRLKSGGGFGPDPGSGTTVPTRRLPAPRPSFDASASEEEEEEEEEDEEEVAAWRLPPRWGQLGASQRSRALRPSHRKTCSQRRRRAMRAFQMLLYSKSTSLTFHWKLWGRHRGRRRNLAHPKNHLSPQEGGATPQVPSPCCRFDSPRGLPPPRLGLLGALMAEDGMRGSPPVPSGPPMEEDGLRWTPKSPLDPDSGLLSCTLPNGFGGLSGPEGERSLAPPDASILISNVCSIGDHVAQELFQSSDLGIAEEADRTGEKAGQHSPLREEHVTCVQSILDEFLQ... | Function: Protease that releases SUMO2 and SUMO3 monomers from sumoylated substrates, but has only weak activity against SUMO1 conjugates . Deconjugates SUMO2 from MEF2D, which increases its transcriptional activation capability (By similarity). Deconjugates SUMO2 and SUMO3 from CDCA8 (By similarity). Redox sensor that... |
Q96HI0 | MKKQRKILWRKGIHLAFSEKWNTGFGGFKKFYFHQHLCILKAKLGRPVTWNRQLRHFQGRKKALQIQKTWIKDEPLCAKTKFNVATQNVSTLSSKVKRKDAKHFISSSKTLLRLQAEKLLSSAKNSDHEYCREKNLLKAVTDFPSNSALGQANGHRPRTDPQPSDFPMKFNGESQSPGESGTIVVTLNNHKRKGFCYGCCQGPEHHRNGGPLIPKKFQLNQHRRIKLSPLMMYEKLSMIRFRYRILRSQHFRTKSKVCKLRKAQRSWVQKVTGDHQETRRENGEGGSCSPFPSPEPKDPSCRHQPYFPDMDSSAVVKGTN... | Function: Protease that catalyzes two essential functions in the SUMO pathway: processing of full-length SUMO3 to its mature form and deconjugation of SUMO2 and SUMO3 from targeted proteins. Has weak proteolytic activity against full-length SUMO1 or SUMO1 conjugates. Required for cell division.
Sequence Mass (Da): 8669... |
Q09353 | MSRRSDLSDKDSQSRKRHWLTDQAVTNEEKEQSPTKRTRKTKSQGLGGLFNTFFGMFVSSNSGEKEKTEVSGEVQVQEDDEIIVEGTTRRVAENKKYMIFLNEDAPVRANAGSEENEVIIEKHVQKNVEIRNDEEKQEVQGDLVLTLSSSPKSPKNLEKSFEVQQDDEEPDVLFEKVVKTPNKQLQEARRFQNELIFLNDNPDTPDDVSVISDSRSKEFISPTPDDSVSRPITPSLSSLSNYTSNNVRDYWRRNSAKKPEVLRRVPVRHQFKHSTSVRKMNTIIDLKKIKNHLSSRDRLLQGVVASGQYEAKAISGIVEK... | Function: Protease that deconjugates smo-1 from targeted proteins and may catalyze the processing of smo-1 to its mature form.
Sequence Mass (Da): 79647
Sequence Length: 697
Subcellular Location: Nucleus envelope
EC: 3.4.22.-
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P0A601 | MTVFSALLLAGVLSALALAVGGAVGMRLTSRVVEQRQRVATEWSGITVSQMLQCIVTLMPLGAAVVDTHRDVVYLNERAKELGLVRDRQLDDQAWRAARQALGGEDVEFDLSPRKRSATGRSGLSVHGHARLLSEEDRRFAVVFVHDQSDYARMEAARRDFVANVSHELKTPVGAMALLAEALLASADDSETVRRFAEKVLIEANRLGDMVAELIELSRLQGAERLPNMTDVDVDTIVSEAISRHKVAADNADIEVRTDAPSNLRVLGDQTLLVTALANLVSNAIAYSPRGSLVSISRRRRGANIEIAVTDRGIGIAPED... | Function: Member of the two-component regulatory system SenX3/RegX3 . Autophosphorylates, and then transfers the phosphate group to RegX3 .
PTM: Autophosphorylated.
Location Topology: Multi-pass membrane protein
Catalytic Activity: ATP + protein L-histidine = ADP + protein N-phospho-L-histidine.
Sequence Mass (Da): 448... |
Q63175 | MSARCCAGQLACCCGSAGCALCCGCCPKFRQSRSTRFMYLFYFTLVIIPCCVMMSPSVMKQMTEHIPFFEDFCKGIKAGDTCENLVGYSAVYRVCFGMACFFFVFCVLTFKVNNSKSCRASIHNGFWFFKLLLLGAMCSGAFFIPDQETFLNVWRYVGAVGSFFFICIQLLLIVEFAHKWNKNWTAGTVRNKLWYASLSLALIMYSIAVGGLALMAVFYTQWDDCMDNKILLGVHGGLCVLISLAAISPCVQNRQPHSGLLQPGLISCYVTYLTFSALTSKPEKVVKDEHGKNVTICVPDFGQDFRRDESMVTWLGTLLL... | Function: Restriction factor required to restrict infectivity of gammaretroviruses: acts by inhibiting early step of viral infection and impairing the ability of the viral particle to translocate its content to the cytoplasm (By similarity). Enhances the incorporation of serine into phosphatidylserine and sphingolipids... |
F4KI56 | MGHEWIDAEREFKWSEDVKVESEVTEIVLVRHGETTWNAAGRIQGQIESDLNEVGLKQAVAIAERLGKEERPVAVYSSDLKRAKDTALMIAKTCFCPEVIEVPDLKERHVGSLQGLYWKEGAEKEPEAYSAFFSSQNDLEIPGGGESFDQLADRSMDALEQIAKKHKGERVIVVTHGGVLRAIYLRITQASSAGKLLNASVNVVHLRDQKWIIDSWSDVSHLSSVGFLQRGFDGDAKP | Function: Phosphoglycerate mutase-like protein lacking PGM activity, but having a low metal-independent phosphoserine phosphatase activity in vitro. May be involved in serine biosynthesis.
Catalytic Activity: H2O + O-phospho-L-serine = L-serine + phosphate
Sequence Mass (Da): 26474
Sequence Length: 238
EC: 3.1.3.3
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B7J6V1 | MNQTIFNFSAGPAVLPHVVLEQVQAELLDWHGSGMSVMEMSHRGPEFMKIAAEAEQDLRDLLDIPANYKILFLQGGATLQFAMVPLNLMRGHGKASYVQTGIWSKKAIAEARRFTAVEIAASNEDRHASYVPMQADWQVSPDTAYVHITGNETIGGVEFDFIPDLGDIPLVSDASSHILSKPTDVSRFGLIYAGAQKNIGPAGLTLVIVRDDLLGHAPANTATMLDYAVYAKEESMHNTPPTFAIYVAGLVFKWLKQLGGLERMAEINARKARLLYDAIDESRGFYANPVETRNRSRMNVPFTLADAAMDEAFLKGARSH... | Cofactor: Binds 1 pyridoxal phosphate per subunit.
Function: Catalyzes the reversible conversion of 3-phosphohydroxypyruvate to phosphoserine and of 3-hydroxy-2-oxo-4-phosphonooxybutanoate to phosphohydroxythreonine.
Catalytic Activity: 2-oxoglutarate + O-phospho-L-serine = 3-phosphooxypyruvate + L-glutamate
Sequence M... |
Q21Y51 | MNRPYNFSAGPAAMPQEVLTEAAAEMLDWHGSGMSVMEMSHRGREFVSIYEQAHLDLRELLAVPDSFKILFMQGGGLAENAIVPLNLSARVSPAGAAGSADFVVTGGWSLKSQQEARKYCTVNIAASNESDGHTTLPGPASWQLSHGASYVHICSNETIHGVEYHTLPDLQALGSEAALVVDCSSHVASRPIDWSRVGLAFAGAQKNLGPAGLTLVVVREDLLGHALAVCPSAFNYKTVADNQSMFNTPPTYAIYIAGLVFQWLKRQGGIAAMEARNQAKAALLYDAIDNSQLYYNKVAPNCRSRMNVPFFLRDESLNDA... | Cofactor: Binds 1 pyridoxal phosphate per subunit.
Function: Catalyzes the reversible conversion of 3-phosphohydroxypyruvate to phosphoserine and of 3-hydroxy-2-oxo-4-phosphonooxybutanoate to phosphohydroxythreonine.
Catalytic Activity: 2-oxoglutarate + O-phospho-L-serine = 3-phosphooxypyruvate + L-glutamate
Sequence M... |
Q9RME2 | MVKQVFNFNAGPSALPKPALERAQKELLNFNDTQMSVMELSHRSQSYEEVHEQAQNLLRELLQIPNDYQILFLQGGASLQFTMLPMNLLTKGTIGNYVLTGSWSEKALKEAKLLGETHIAASTKANSYQSIPDFSEFQLNENDAYLHITSNNTIYGTQYQNFPEINHAPLIADMSSDILSRPLKVNQFGMIYAGAQKNLGPSGVTVVIVKKDLLNTKVEQVPTMLQYATHIKSDSLYNTPPTFSIYMLRNVLDWIKDLGGAEAIAKQNEEKAKIIYDTIDESNGFYVGHAEKGSRSLMNVTFNLRNEELNQQFLAKAKEQ... | Cofactor: Binds 1 pyridoxal phosphate per subunit.
Function: Catalyzes the reversible conversion of 3-phosphohydroxypyruvate to phosphoserine and of 3-hydroxy-2-oxo-4-phosphonooxybutanoate to phosphohydroxythreonine.
Catalytic Activity: 2-oxoglutarate + O-phospho-L-serine = 3-phosphooxypyruvate + L-glutamate
Sequence M... |
O82796 | MEALTTSRVVPVQVPCRKLSSLFANFSCLELRRYPCRGLVSIMNHPKLLRPVTASVQPHELSTLGHEGNIVPSKEILDLWRSVEAVCFDVDSTVCVDEGIDELAEFCGAGKAVAEWTARAMGGSVPFEEALAARLSLFKPSLSKVEEYLDKRPPRLSPGIEELVKKLRANNIDVYLISGGFRQMINPVASILGIPRENIFANNLLFGNSGEFLGFDENEPTSRSGGKAKAVQQIRKGRLYKTMAMIGDGATDLEARKPGGADLFICYAGVQLREAVAANADWLIFKFESLINSLD | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Catalyzes the last step in the plastidial phosphorylated pathway of serine biosynthesis (PPSB). The reaction mechanism proceeds via the formation of a phosphoryl-enzyme intermediates. Required for embryo, pollen and root development. May be required preferentially for... |
Q820S0 | MRKIYNFSAGPAVLPEEVLEQAREEMLDWHGSGMSVMEMSHRGKEFMSIADETESALRELAGIPDHYKVLFLQGGASSQFAMVPMNLLGKKGKADYVNTGQWSAKAISEAKNYGSVQIAASSESDGFNSVPPLAQWHISPDAAYVHYASNETIGGVEFQWTPDLSAVAGDNKNIPLVADMSSNFLSRPFDVSKFGLIYAGAQKNVGPAGLVVVIVREDLLDIPPLAGTPAMFRYKTHADNASMYNTPPTYAIYIMGLVMEWLKKQGGLTAIEQRNIAKAKLIYDLIDVSSFYHCPVNQADRSRMNVPFTLSDPGLDDAFL... | Cofactor: Binds 1 pyridoxal phosphate per subunit.
Function: Catalyzes the reversible conversion of 3-phosphohydroxypyruvate to phosphoserine and of 3-hydroxy-2-oxo-4-phosphonooxybutanoate to phosphohydroxythreonine.
Catalytic Activity: 2-oxoglutarate + O-phospho-L-serine = 3-phosphooxypyruvate + L-glutamate
Sequence M... |
A1SEM0 | MTDALQIPRDLLPADGRFGAGPSKIQTAHLDALAATGSTLMGTSHRQAPVRDLVGRVRSGLAELFSLPDGYQVVLGNGGATAFWDIATYGLIQERSQHLTFGEFSSKFAKAAKAAPWLADPSVIASEPGSRPAPVAEDGVDAYAWAHNETSTAVMAPVVRPAGTSSDSSLVLVDATSGAGGLPVDLREVDVYYFAPQKCFASDGGLWIALFSPAALERAATVAASGRHIPAFFDLPTAIDNSAKNQTYNTPAVATLFLMAEQLDWMNASGGLDGMVARTTESSDTLYTWAEKSPYAFPYVTDPDHRSLVIGTIDFEDGID... | Cofactor: Binds 1 pyridoxal phosphate per subunit.
Function: Catalyzes the reversible conversion of 3-phosphohydroxypyruvate to phosphoserine and of 3-hydroxy-2-oxo-4-phosphonooxybutanoate to phosphohydroxythreonine.
Catalytic Activity: 2-oxoglutarate + O-phospho-L-serine = 3-phosphooxypyruvate + L-glutamate
Sequence M... |
B2RID6 | MKKHNFTAGPCILNDLVLKDAASACLNFAGTGLSVLEVSHRDKEFDAVMLEARNLFKELLDVPEGYEVLFLGGGASLQFYQVPLNLLKKKAAFINTGTWATNAIKQAKIMTQVYGGEVEVLASSEDKNFSYIPKDFVIPEDVDYFHFTTNNTIYGTEIRKDFDTKTRLVADMSSDIFSRPIDVSKYDLIYGGAQKNIGPAGATFVLVKTDVLGQVDRPLPDMLNYQIHIKKDSMFNTPPVFPVYVALQTMKWYKELGGVKVLEKMNLDKAALIYDAIDSSKIFRGTVNPEDRSIMNACFVMKDEYKELEKEFATFAASRG... | Cofactor: Binds 1 pyridoxal phosphate per subunit.
Function: Catalyzes the reversible conversion of 3-phosphohydroxypyruvate to phosphoserine and of 3-hydroxy-2-oxo-4-phosphonooxybutanoate to phosphohydroxythreonine.
Catalytic Activity: 2-oxoglutarate + O-phospho-L-serine = 3-phosphooxypyruvate + L-glutamate
Sequence M... |
Q6CIT4 | MSGYYNRQYSHFHGNNDRYQTGRYAYQENGNRYKGFQRNGSGNRRYSREGFGSQLRNNENESRPIRSQSRGISEIPRNPFATRPVVSAKYDRDEFNTKYHYYDIVSKRLRNESSFKKWKSEKIPEHGYVTTTELIASDKQKPILMARQPEQTSVDPRIRPMNGDAVSGSISAKKRYRKLRSALVRNSRIPYDSFYIGPEPPKEIIVYPSASNQQPIAAALSEAIIKNYFKSFGEIAHFEQFMDPNSALPLYVYLIKFTGPVSQPDAPYKAAYKASEKFKDAPYTVSGIKFNVILNQNTVLNSIKDKLIKQNAARVTEVNK... | Function: Catalytic component of the COMPASS (Set1C) complex that specifically mono-, di- and trimethylates histone H3 to form H3K4me1/2/3, which subsequently plays a role in telomere length maintenance and transcription elongation regulation.
Catalytic Activity: L-lysyl(4)-[histone H3] + 3 S-adenosyl-L-methionine = 3 ... |
Q9Y7R4 | MDFNTSTRSKSQPVQRNNYKVLYDPELGIKENLGRKIIYRFNGVSKPPLVVRDPRLKNPIYARGIPKSGRPFLKSLQTINYDYNENSLGPEPPTQVFVSNISPLVTSEQLRYHFKSFGEVFDLDLKLNPYTGTSLGLCCISFDKRSSISVAAHSAKIAVQQANGLRFSGKPLSVVLDRDGSLCEEAFKKALNAVEKQFQEETLQKQRFEREDESSRQKLSAAMNEDIPPWRQPSKNSQTLSNGDLQHSKVQNVDQKSGFLTSSETDVPKNINDYIYLLIDDRFVPPDRVYYTDIKHHFRKFLYEKIYMNKDGFYITFNNY... | Function: Catalytic component of the Set1 complex that specifically mono-, di- and trimethylates histone H3 to form H3K4me1/2/3. Methylation promotes maintenance of active chromatin states at euchromatic chromosomal domains and is present throughout the cell cycle. Plays a role in telomere maintenance and DNA repair in... |
Q95Y12 | MNYEKIDSTIPGPGISETDWNDVFEGCNCEAECSSAAGCSCLINKIDNYTVDGKINKSSELLIECSDQCACILLPTSCRNRVVQCGPQKKLEIFSTCEMAKGFGVRAGEQIAAGEFVCEYAGECIGEQEVERRCREFRGDDNYTLTLKEFFGGKPVKTFVDPRLRGNIGRFLNHSCEPNCEIILARLGRMIPAAGIFAKRDIVRGEELCYDYGHSAIEGENRKLCLCKSEKCRKYLPMSATPIE | Function: Probable histone methyltransferase (By similarity). Required for embryonic development.
Catalytic Activity: L-lysyl-[histone] + S-adenosyl-L-methionine = H(+) + N(6)-methyl-L-lysyl-[histone] + S-adenosyl-L-homocysteine
Sequence Mass (Da): 27108
Sequence Length: 244
Domain: In the pre-SET domain, Cys residues ... |
G5EEU2 | MLPAWGTSTEATASHAGWDGDDEGDIRAAYTEDEKKENIPPISLTSVSTNGAYPGQKRRRSESVRTLKPECPPEETQRLRQRRRISATDATQSSRTMNVIEDRKPRVNRARKSQDAPSTSTCGFETPVGTKRKSKAADSQKPPKQSKLRKIDEASTSKAVDNSSKDGKKTTKPAVTQSNRRRSGLSLRPVPIETIFSESSGRESSTEDEADVSHQQRVEKIAKNPIMVVVLPLGPGNYPNNERITVVSTYKSRVNKNCNEARRAQRHGSWSRKGIAFPGIPTKKFTKSDLAKYGAHASNWPAQAAFRSEEGKILIYYEGW... | Function: Histone methyltransferase that specifically trimethylates 'Lys-9' of histone H3 using mono- and dimethylated H3 'Lys-9' as substrate . Acts redundantly with the methyltransferase met-2 to position chromosome arms at the nuclear lamina . Required for small-RNA-induced H3K9 methylation . Together with met-2, pr... |
Q4WTT2 | MSSHDNADSPSSSVANAVTAMKIEQHDGAADMLLSNGGDAVLKRDSNGLSEHAVTAKDYPGMNDLASSTVKSRTSSLTPIKTENGDSTAKEEKVGGDITVKMEPGQPPKLSRSSSQKVVAQPPQLFLHLPDSTAEAQSTFEVMETCTYANKYMGYTEHAMECDCAEEWEPSLSRNLACGEDSDCINRATKIECVGDCSCGAECQNQRFQRKEYANVAVIKTEKKGFGLRAETDLRPHQFIFEYVGEVINEAQFRRRMRQYDEEGIKHFYFMSLSRGEFVDATKKGNLGRFCNHSCNPNCYVDKWVVGEKLRMGIFAERAI... | Function: Histone methyltransferase that trimethylates histone H3 'Lys-36' forming H3K36me3. Involved in transcription elongation as well as in transcription repression.
Catalytic Activity: L-lysyl(36)-[histone H3] + 3 S-adenosyl-L-methionine = 3 H(+) + N(6),N(6),N(6)-trimethyl-L-lysyl(36)-[histone H3] + 3 S-adenosyl-L... |
Q59XV0 | MSNNNFQESSNNTSSPSKRSTPMLFLDAENKTQEALTTFELLNACTYQNKYVGSANVTTTATTSTKTSNSTSTKSHQQQHRRKLEYMTCDCEEEWDSELQMNLACGPDSNCINRITCVECVNRNCLCGDDCQNQRFQNRQYSKVKVIQTELKGYGLIAEQDIEENQFIYEYIGEVIDEISFRQRMIEYDLRHLKHFYFMMLSNDSFIDATEKGSLGRFINHSCNPNAFVDKWHVGDRLRMGIFAKRKISRGEEITFDYNVDRYGAQSQPCYCGEPNCIKFMGGKTQTDAALLLPQMIAEALGVTPRQEKAWLKENKSIRN... | Function: Histone methyltransferase that trimethylates histone H3 'Lys-36' forming H3K36me3. Involved in transcription elongation as well as in transcription repression.
Catalytic Activity: L-lysyl(36)-[histone H3] + 3 S-adenosyl-L-methionine = 3 H(+) + N(6),N(6),N(6)-trimethyl-L-lysyl(36)-[histone H3] + 3 S-adenosyl-L... |
Q1DU03 | MAGHDDEEARIETVKDAVTDMKLERQSSTESVAPNGILDTITPKDEPNGHLSSKPSTPSLKPPKSRSRSSNSLAKDEVPEEKVGGDITIKQEPGQPPKLARSASQKLPPRAAPLFTDLPDKTTEATSTFQLMEVCTYANKYLGYTEHAMDCDCAEEWDAATCRNTACGEDSDCINRATKMECFGDCGCGDSCQNQRFQRREYAKVSVIKTEKKGYGLRADCDLRPNEFIFEYIGEVINEPQFRRRMIQYDEEGIKHFYFMSLNKGEFVDATKKGNLGRFCNHSCNPNCYVDKWVVGEKLRMGIFAERYIKAGEELVFNYN... | Function: Histone methyltransferase that trimethylates histone H3 'Lys-36' forming H3K36me3. Involved in transcription elongation as well as in transcription repression.
Catalytic Activity: L-lysyl(36)-[histone H3] + 3 S-adenosyl-L-methionine = 3 H(+) + N(6),N(6),N(6)-trimethyl-L-lysyl(36)-[histone H3] + 3 S-adenosyl-L... |
Q13435 | MATEHPEPPKAELQLPPPPPPGHYGAWAAQELQAKLAEIGAPIQGNREELVERLQSYTRQTGIVLNRPVLRGEDGDKAAPPPMSAQLPGIPMPPPPLGLPPLQPPPPPPPPPPGLGLGFPMAHPPNLGPPPPLRVGEPVALSEEERLKLAQQQAALLMQQEERAKQQGDHSLKEHELLEQQKRAAVLLEQERQQEIAKMGTPVPRPPQDMGQIGVRTPLGPRVAAPVGPVGPTPTVLPMGAPVPRPRGPPPPPGDENREMDDPSVGPKIPQALEKILQLKESRQEEMNSQQEEEEMETDARSSLGQSASETEEDTVSVSK... | Function: Involved in pre-mRNA splicing as a component of the splicing factor SF3B complex . SF3B complex is required for 'A' complex assembly formed by the stable binding of U2 snRNP to the branchpoint sequence (BPS) in pre-mRNA. Sequence independent binding of SF3A/SF3B complex upstream of the branch site is essentia... |
Q9BWM7 | MGELPLDINIQEPRWDQSTFLGRARHFFTVTDPRNLLLSGAQLEASRNIVQNYRAGVVTPGITEDQLWRAKYVYDSAFHPDTGEKVVLIGRMSAQVPMNMTITGCMLTFYRKTPTVVFWQWVNQSFNAIVNYSNRSGDTPITVRQLGTAYVSATTGAVATALGLKSLTKHLPPLVGRFVPFAAVAAANCINIPLMRQRELQVGIPVADEAGQRLGYSVTAAKQGIFQVVISRICMAIPAMAIPPLIMDTLEKKDFLKRRPWLGAPLQVGLVGFCLVFATPLCCALFPQKSSIHISNLEPELRAQIHEQNPSVEVVYYNKG... | Function: Mitochondrial serine transporter that mediates transport of serine into mitochondria, an important step of the one-carbon metabolism pathway . Mitochondrial serine is converted to glycine and formate, which then exits to the cytosol where it is used to generate the charged folates that serve as one-carbon don... |
Q91V61 | MGDLPLNINIQEPRWDQSTFLGRARHFFTVTDPRNLLLSGEQLEASRNIVQNYRAGVATPGLTEDQLWRAKYVYDSAFHPDTGEKVVLIGRMSAQVPMNMTITGCMLTFYRKTPTVVFWQWVNQSFNAIVNYSNRSGDAPITVQQLGTAYVSATTGAVATALGLKSLTKHLPPLVGRFVPFAAVAAANCINIPLMRQRELQVGIPVTDEAGQRLGHSVTAAKQGIFQVVISRIGMAIPAMAIPPVIMNTLEKKDFLKRRPWLGAPLQVGLVGFCLVFATPLCCALFPQRSSIHVTRLEPELRAQIQAQNPSIDVVYYNKG... | Function: Mitochondrial serine transporter that mediates transport of serine into mitochondria, an important step of the one-carbon metabolism pathway. Mitochondrial serine is converted to glycine and formate, which then exits to the cytosol where it is used to generate the charged folates that serve as one-carbon dono... |
A8E7G5 | MDPNLQYWQNNGQSFLSRLGLWSKILDPTLLLSQAEIEEARTLIQNEENTPGKNDKVSNAWLLSLSSVHSDTGAVISPAYRPQVFLPISAPLVVGSLIAHKGIKSAMFWQFVLHTYCAGFNHANRNATATKDNKTTMKQSLLILGAVSYSTVTGALPQIILQRLRLISSLTQTICRSFLPVPLAAGLAAFNILVVRSEEAENGISLFDANGNAVGVSKEAGFKAVKETAISRATLFGTTAALPTFLMALLERAKFVQRNPRLIAPIGSMCTVITFGLMIPVSFSLFPQLGKIKKENLEKEFQSLDGNEELFYHRGL | Function: Mitochondrial amino-acid transporter (By similarity). Does not act as a serine transporter: not able to mediate transport of serine into mitochondria (By similarity).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 34567
Sequence Length: 316
Subcellular Location: Mitochondrion inner membran... |
Q6P4A7 | MSLEQEEETQPGRLLGRRDAVPAFIEPNVRFWITERQSFIRRFLQWTELLDPTNVFISVESIENSRQLLCTNEDVSSPASADQRIQEAWKRSLATVHPDSSNLIPKLFRPAAFLPFMAPTVFLSMTPLKGIKSVILPQVFLCAYMAAFNSINGNRSYTCKPLERSLLMAGAVASSTFLGVIPQFVQMKYGLTGPWIKRLLPVIFLVQASGMNVYMSRSLESIKGIAVMDKEGNVLGHSRIAGTKAVRETLASRIVLFGTSALIPEVFTYFFKRTQYFRKNPGSLWILKLSCTVLAMGLMVPFSFSIFPQIGQIQYCSLEE... | Function: Mitochondrial amino-acid transporter (By similarity). Does not act as a serine transporter: not able to mediate transport of serine into mitochondria .
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 37998
Sequence Length: 337
Subcellular Location: Mitochondrion inner membrane
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Q925N1 | MEPNLQFWISERQAFFRRFCQWMDLLDPVNMFISIGSIEKSRQLLFTTEDAPKHYLDNQVIKDAWNKSLSTVHPDSSKLIPHLFRPAAFLPVTAPMVFLLMMPDTGIKSIILTQGCLYGYTTAFNITNGNASYSHGPVERTLLGAGVSVSSTFIGLIPHLFQMKYPPNNFWLKRTLPIVFLAQVSGMNVFASRSFENHRGIEVMDKEGHVVGHSRKAGRKAIKDTAKSRAVLFGTSALAPELFIHIFKRTRFYPQTLLSLVILRMSSTFFMMGLMVPVSFSMFPQIGQIQCSQLEEKIQSSTEEKELFYYRGV | Function: Mitochondrial amino-acid transporter (By similarity). Does not act as a serine transporter: not able to mediate transport of serine into mitochondria (By similarity).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 35580
Sequence Length: 313
Subcellular Location: Mitochondrion inner membran... |
Q5FC79 | MALDETLFGYPIYPKFKLGEPRFPQDTFLGRYLHCLDVIDPRTLFASNKKLEESLELLNSFKAGTATNVPDKSLWEAQKLKSAILHPDTGEKVLPPFRMSGFVPFGWITVTGMLLPNPSWPTLLFWQWMNQSHNACVNYANRNATQPQPLSKYIGAYGAAVTAACSISGGLTYFIKKASSLPPTTRIIIQRFVPLPATSLASSLNVICMRWNELETGIQVYEKDTGKVVGVSKVAAKQAVTDTTMVRAFLPVPLLLMPPCIMPYLERFKWVTKTQVRHIFVNAIVCTLSFAVSLPVALALFPQESAISREQLEPELQQKT... | Function: Mitochondrial amino-acid transporter.
Catalytic Activity: citrate(in) = citrate(out)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 36992
Sequence Length: 331
Subcellular Location: Mitochondrion inner membrane
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Q8TD22 | MADTATTASAAAASAASASSDAPPFQLGKPRFQQTSFYGRFRHFLDIIDPRTLFVTERRLREAVQLLEDYKHGTLRPGVTNEQLWSAQKIKQAILHPDTNEKIFMPFRMSGYIPFGTPIVVGLLLPNQTLASTVFWQWLNQSHNACVNYANRNATKPSPASKFIQGYLGAVISAVSIAVGLNVLVQKANKFTPATRLLIQRFVPFPAVASANICNVVLMRYGELEEGIDVLDSDGNLVGSSKIAARHALLETALTRVVLPMPILVLPPIVMSMLEKTALLQARPRLLLPVQSLVCLAAFGLALPLAISLFPQMSEIETSQ... | Function: Mitochondrial amino-acid transporter (By similarity). Transports citrate (By similarity). Does not act as a serine transporter: not able to mediate transport of serine into mitochondria (By similarity). In brown adipose tissue, plays a role in the regulation of UCP1-dependent thermogenesis probably by suppor... |
Q54NQ9 | MTSNSFPVFDGVSNKYDNNTFYGRYQNFRDITDPSTLFATEKDLSQSKTLLDNFKKGLVDPVKHSDELWKAKKILDSTIHPDTGKPIFLPFRVSAFLPINVIICAGLILPNASIGTTIFWQWINQSYNIALNHANRNASNTMSNKQILEAYASAVGISCSLAVGLGWGVNKLNIQNKTISSALRMMVPFTAVTSAGIANVLIMRGNEMVNGIDIKDKDGVIHGKSKEAGKSAVYKVAFSRAATSFPALLLPPIVMGLFERTSFVKKYPKVRMPLNLAVIAAIFNTSLPAAIALFPQESTISADSLEPQFRNIKDKNGNII... | Function: Mitochondrial amino-acid transporter that mediates transport of serine into mitochondria.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 36158
Sequence Length: 329
Subcellular Location: Mitochondrion membrane
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Q4F883 | MESSSSLKGSALGKLVVTSGLLHSSWSKILEIHNPPYSNHDPGLQVSKKKKDSGLEFQIHREEKFTLVVFSAPPICRSSSSDSTLLHVKDKENPFPFLCSENNPSFSLHTPAFNLFTSASTSLTYLKSELLQTLKSEKPVIITGAALGGSVASLYTLWLLETIEPTLKRPLCITFGSPLIGDASLQQILENSVRNSCFLHVVSAQTRIKMDFFKPFGTFLICFDSGCVCIEDHVAVTELLNGVHDSGLVDYSQVLNRLDQSMLSLADSRLIPEDVIKGIEKRAEMKNLRFDMMFKKLNDMKISMAYIEWYKKKCKEVKIG... | Function: Acyl hydrolase that triggers the leaf senescence onset. Can use triolein as substrate to produce oleic acids.
Catalytic Activity: a carboxylic ester + H2O = a carboxylate + an alcohol + H(+)
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 62066
Sequence Length: 537
Subcellular Location: Me... |
B4MVH6 | MSRTIVVKNPRTSGKDEDKAQIPSQDELPSGSSGAKTTNQIISEFRALIKDPIKLDEAVNYLYETLVDDAAVGIFIETRQLQKTGSLTALEGTVEETNDMCDLPDCDIFGMSTAEKTAKCCCPNCERMVAAVRFAPHLQTCLGLGRSSSRAALRRLTVSSRSSSTSTGGGQANEKSTDDEDWSLDSRPGKSTKNSRNKGSKKNQKNKLK | Function: Component of the transcription regulatory histone acetylation (HAT) complex SAGA, a multiprotein complex that activates transcription by remodeling chromatin and mediating histone acetylation and deubiquitination. Within the SAGA complex, participates in a subcomplex that specifically deubiquitinates histone ... |
B4N4E1 | MSTTAAATTTTPSTMSNNQGQGQTTIPGTGTGTGAAKTTNRIINNFRALLKDPNNLDEAVNYLYRTLIDDATAGIFIETHHLRKTGNLAALDGLAEESAYRICEMPNLDIFGISTAKKPMDCTCPNCDRLVAAARFAPHLEKCMGMGRISSRIASRRLATKEGTSASSSSSSTYMHSGGDRGGGGGHHAGAGGTDDEDDVDWSSDKRKKKSTQSSRNNGSKKNNGKTF | Function: Component of the transcription regulatory histone acetylation (HAT) complex SAGA, a multiprotein complex that activates transcription by remodeling chromatin and mediating histone acetylation and deubiquitination. Within the SAGA complex, participates in a subcomplex that specifically deubiquitinates histone ... |
Q8TEC5 | MDDLTLLDLLECPVCFEKLDVTAKVLPCQHTFCKPCLQRVFKAHKELRCPECRTPVFSNIEALPANLLLVRLLDGVRSGQSSGRGGSFRRPGTMTLQDGRKSRTNPRRLQASPFRLVPNVRIHMDGVPRAKALCNYRGQNPGDLRFNKGDIILLRRQLDENWYQGEINGISGNFPASSVEVIKQLPQPPPLCRALYNFDLRGKDKSENQDCLTFLKDDIITVISRVDENWAEGKLGDKVGIFPILFVEPNLTARHLLEKNKGRQSSRTKNLSLVSSSSRGNTSTLRRGPGSRRKVPGQFSITTALNTLNRMVHSPSGRHM... | Function: Has E3 ubiquitin-protein ligase activity . Acts as an anti-apoptotic regulator of the JNK pathway by ubiquitinating and promoting the degradation of SH3RF1, a scaffold protein that is required for pro-apoptotic JNK activation . Facilitates TNF-alpha-mediated recruitment of adapter proteins TRADD and RIPK1 to ... |
Q8TEJ3 | MLLGASWLCASKAAAAAAQSEGDEDRPGERRRRRAAATAAGAGEDMDESSLLDLLECSVCLERLDTTAKVLPCQHTFCRRCLESIVCSRHELRCPECRILVGCGVDELPANILLVRLLDGIRQRPRAGTSPGGSPPARPIPGQSAAPTLAGGGGGAAGSTPGSPVFLSAAAGSTAGSLRELATSRTAPAAKNPCLLPYGKALYSYEGKEPGDLKFNKGDIIVLRRKVDEQWYHGELHGTQGFLPASYIQCIQPLPHAPPQGKALYDFEMKDKDQDKDCLTFTKDEILTVLRRVDENWAEGMLGDKIGIFPLLYVELNDSA... | Function: Has E3 ubiquitin-protein ligase activity.
PTM: Autoubiquitinated.
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): 92776
Sequence Lengt... |
Q8C120 | MLLGASWLCASKAAATAARGEGEDRQGEQQRGAQARTEEDMDESSLLDLLECSVCLERLDTTAKVLPCQHTFCRRCLESIVCSRHELRCPECRILVGCGVDELPANILLVRLLDGIRQRPRTGASPGSSPPARPGPGTFSALAGGAGGATGSPPCSPVFLSAAAGSSTSSLCDVATNRSVPVAKTLSQLPYAKALYSYEGKEPGDLKFNKGDIIILRRKVDENWYHGELQGMHGFLPASYIQCVRPLPQALPQGKALYDFEMKDRDQDKDCLTFTKDEVLTVIRRVDDNWAEGMLGDKIGIFPLLYVELNDSAKQLIEMD... | Function: Has E3 ubiquitin-protein ligase activity.
PTM: Autoubiquitinated.
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): 93130
Sequence Lengt... |
Q5BLC7 | MKWTVLLLEYFLVKVLVLLYSADGEAQQLEGFIMLSGSNGSRDEESVSEPPHTEDKCRGYYDVMGQWDPPFVCQTGNYLYCCGTCGFRFCCAYKNSRLDQSTCKNYDTPVWLTGQTPYKKTLDPRHDPTKDKTNLIVYIICGVVAIMALVGIFTKLGLEKAHRPHRESMSRAVASVMQGARQGQHEEAIGMHTQHYDTVQARANNMQAGQINNMMQTHPYPALSQLSHVYEQQQSAKDLNKYASLKAVAAKANGDFLNKQHRHLVELAAKGNLPLHPIRMEHVEPTATYVTEVPCIKQNGQKPKSIKANVSHPAMAYSSN... | Function: Regulator of short-term neuronal synaptic plasticity in the dentate gyrus. Associates with AMPA receptors (ionotropic glutamate receptors) in synaptic spines and promotes AMPA receptor desensitization at excitatory synapses (By similarity).
Location Topology: Single-pass type I membrane protein
Sequence Mass ... |
B3DHW5 | MKSTGLLLGYFLMKVLVCDAEGEPGKSLDGAVTASGSNDSRDGENGLSETPHTEDRCRGYYDVMGQWDPPFVCRTGSYLYCCGTCGFRFCCEFKNSRLDQTTCKNYDTPPWSMTGRPPPKMMDQHDPTKDKTNLIVYIICGVVAIMALVGIFTKLGLEKAHRPHRENMSRALAQVMRQTAPGEHVEREESLAVHGQPYENLQARATGNNLQSAQMNSVGPSSSMMQAMTPYPALGQVPVAHPYEPSPAAKELNKYASLKAVAEKANENFYTNRRHLADLAAKGTLPMHSVSLEQEPTNPYSPELPCQKQNGHKSKSTKVH... | Function: Regulator of short-term neuronal synaptic plasticity in the dentate gyrus. Associates with AMPA receptors (ionotropic glutamate receptors) in synaptic spines and promotes AMPA receptor desensitization at excitatory synapses (By similarity).
Location Topology: Single-pass type I membrane protein
Sequence Mass ... |
Q7PXN1 | MLDIFRGLKSLVKISHVNTDSPVFRLHYSITVIILMSFSLIVTTRQYVGNPIDCVHTKDIPADVLNTYCWIHSTFALKSLFLKEVGKDVPYPGVGNSAEATAADKKIYKYYQWVCFCLFFQAILFYTPRWLWKSWEGGKIHALMMDLDIGICSEIEKKQKKKLLLDYLWDNLRYHNWWAYRYYVCEFLSLCNVIGQMFLMNRFFDGEFMTFGLDVITHMEADQEDRMDPMIYIFPRMTKCTFYKYGVSGEVERHDAICILPLNVVNEKIYIFLWFWFIILTILTTLTIFYRIIIIFSPRMRVYLLRLRFRLVRRDAIEII... | Function: Structural component of the gap junctions at electrical synapses in distal and mid-depth levels in the lamina.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 44426
Sequence Length: 373
Subcellular Location: Cell membrane
|
P33085 | MLDIFRGLKNLVKVSHVKTDSIVFRLHYSITVMILMSFSLIITTRQYVGNPIDCVHTKDIPEDVLNTYCWIQSTYTLKSLFLKKQGVSVPYPGIGNSDGDPADKKHYKYYQWVCFCLFFQAILFYTPRWLWKSWEGGKIHALIMDLDIGICSEAEKKQKKKLLLDYLWENLRYHNWWAYRYYVCELLALINVIGQMFLMNRFFDGEFITFGLKVIDYMETDQEDRMDPMIYIFPRMTKCTFFKYGSSGEVEKHDAICILPLNVVNEKIYIFLWFWFILLTFLTLLTLIYRVVIIFSPRMRVYLFRMRFRLVRRDAIEIIV... | Function: Structural component of the gap junctions at electrical synapses in distal and mid-depth levels in the lamina. Isoform Lethal forms voltage sensitive intercellular channels through homotypic interactions.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 44355
Sequence Length: 372
Subcellular... |
Q9Y371 | MNIMDFNVKKLAADAGTFLSRAVQFTEEKLGQAEKTELDAHLENLLSKAECTKIWTEKIMKQTEVLLQPNPNARIEEFVYEKLDRKAPSRINNPELLGQYMIDAGTEFGPGTAYGNALIKCGETQKRIGTADRELIQTSALNFLTPLRNFIEGDYKTIAKERKLLQNKRLDLDAAKTRLKKAKAAETRNSSEQELRITQSEFDRQAEITRLLLEGISSTHAHHLRCLNDFVEAQMTYYAQCYQYMLDLQKQLGSFPSNYLSNNNQTSVTPVPSVLPNAIGSSAMASTSGLVITSPSNLSDLKECSGSRKARVLYDYDAAN... | Function: May be required for normal outer mitochondrial membrane dynamics . Required for coatomer-mediated retrograde transport in certain cells (By similarity). May recruit other proteins to membranes with high curvature. May promote membrane fusion . Involved in activation of caspase-dependent apoptosis by promoting... |
P68966 | MSEEPVSGTTVEIEEDTHTPPNSPVLETFSLSPEPEAEACPNTDRYLSANLLCKHLQRQSAIVLDSIKDQLQVPTSVSELSCAYERSLLCPNIPPKQQSNGTCEANPKLNFYPTFLVPETLATYHIFFVNQKIPVSCKANRAKADKALTLQEGDCLPDYETMDTVSRVFEGLGGEVVAENALQNNDSVLVELKEDNPRLAVLKRNLSVSHFAYPAVHLPPKIITTVMNNLLVKRANPSADVSELDPDGGQEVVSDTELSRWLNTSDPETLEKQRKLVMGSVLVTVVLECMQRLFTSKDMVKKIGETLHYTFRHGYVSLAC... | Function: Protein that inhibits host translation while promoting late viral translation by ribosome shunting. Blocks host cap-dependent translation by binding to eIF4G, displacing MKNK1 from cap initiation complexes and preventing EIF4E phosphorylation. Binds to the tripartite leader sequence of viral late mRNAs and re... |
Q64760 | MADKITREEKTIATLDLVLRVVVDAGNWDVFSKRLVRYTREQYGIELPEDIGDLPDTSEVSKVLLSHLGEDKAVLSAYRIAELTQPSEMDRAKVTEGGLAVLNASRDESEAQNPSNPEPESIESDAVEDLGVAAESDPSDDEPDPEPEYDHREADHDSDADSGYYSADGGRPGTPVDEEPQDDSPSSEETASTVIEEAQTSASNDSHDDDTHRDDGSASEEDLERDALVAPADPFPNLRKCFERQAMMLTGALKDAADTADPPETLSVDSVQRQLERFVFNPDRRVPAEHLEVRYNFYPPFLTPKAIASYHIFAVTASIP... | Function: Protein that inhibits host translation while promoting late viral translation by ribosome shunting. Blocks host cap-dependent translation by binding to eIF4G, displacing MKNK1 from cap initiation complexes and preventing EIF4E phosphorylation. Binds to the tripartite leader sequence of viral late mRNAs and re... |
P36856 | MESTADGDKARGEEPVAEGEASDIRRGDGEFPAPEDEHPDDGEPDEPADRDDRSGESDADSGYYSADGGRDAECDGEAARPDTPTDESSAPTTPSTAVRRSSGESSPDRGGCFSHSSDSELGCATETRDPFAAGLRKCIERQAMILTGALKDAHVDPPLDSMPLTVDAVQRQLERFLFNPDPKVPREHVELATTFMPPFMTPKAIANYHIFCGNRPIPPSCKANRSGSEVLRAAENARFFKRLPRWKQGVTVDDGLGDEVSPITELKDAKLVPLRDDTSRLEWAKMRGEHVRYFCYPSLHMPPKISRMLMEVLLQPFAQE... | Function: Protein that inhibits host translation while promoting late viral translation by ribosome shunting. Blocks host cap-dependent translation by binding to eIF4G, displacing MKNK1 from cap initiation complexes and preventing EIF4E phosphorylation. Binds to the tripartite leader sequence of viral late mRNAs and re... |
Q9YTR7 | MEDQHSAASELGSSAAPTLPPPPPPPPPPTSPPPSLQQRQQEPTETDDAEDTCSSSSSSSASSECFVSPLEDTSSEDSADTVLPSEPRRDEEEQEEDSPDRYMDADVLQRHLLRQSTILRQVLQEAAPGAAAEAAEAPSVAELSRRLEAALFSPATPPRRQENGTCAPDPRLNFYPVFMLPEALATYLLFFHNQKIPVSCRANRPRADAHWRLPSGTPLPDYPTTDEVYKIFEGLGDEEPACANQDLKERDSVLVELKLDNPRLAVVKQCIAVTHFAYPALALPPKVMSTLMQTLLVRRASPLPDEGETPLEDLLVVSDE... | Function: Protein that inhibits host translation while promoting late viral translation by ribosome shunting. Blocks host cap-dependent translation by binding to eIF4G, displacing MKNK1 from cap initiation complexes and preventing EIF4E phosphorylation. Binds to the tripartite leader sequence of viral late mRNAs and re... |
A9CB91 | MAAEGERQNLLSKHLERQVKILQSICKNDSEACNLLDLGYILEKNLFAPADSRKADSGPDPQLNFFPPFLTPECLALHYPFFLTTSIPPSCKGNRSGTDTYSQFCSRSSCLEDIPDPSEWDDSLGNVSLMAELKENQKLAPLEEDSPRTTAVDESKCSSKQSYSYPALTFPPQVQKILFDYLIGESQDPNDLDSEYKLAFTDEDLPQEGQAEKTKQRETLGAVATFGAVLLSIQRLFTHPVVIKNTQESLHYTFLHGFVRMVHLLTEVNLSEFVTFHGLTHRNRLNNPVQHRQLEGADRFDYILDTIYLYLVFAWQTAMD... | Function: Protein that inhibits host translation while promoting late viral translation by ribosome shunting. Blocks host cap-dependent translation by binding to eIF4G, displacing MKNK1 from cap initiation complexes and preventing EIF4E phosphorylation. Binds to the tripartite leader sequence of viral late mRNAs and re... |
P28957 | MGLFGLLKYAYSNRLVKHDAITTPPGIMTPIAIDLWNVMYTLMEKFDQERNFPLDGAAVTARCFFSLLRLLLKRSYYPIFVSDRGIYGDGRVKQGAKAIVSQTMSSYGGSGRLSSACFTGDEHDTEFQEDPEENDVSVPPQDTCPPTEISAGYVEPERKCEHSSTRWSALDGAPRLSYRLCVNLIRHLGYPYVNACNLEADDVCANLYHTNTVAQIYTTDTDLILMGCDIILDIMPLFPPTLRCCDVLMDLGVTYDEFLTEFVRCHTDLHEPQTLASVQSVISSLHSPPDEDEGADMPQTPSGHSWRCPNERRVISWRRQ... | Function: Minor structural protein that acts as an endoribonuclease during lytic infection. Degrades host mRNAs in the cytoplasm by cutting them at preferred sites, including some in regions of translation initiation (By similarity).
Sequence Mass (Da): 56543
Sequence Length: 497
Subcellular Location: Virion
EC: 3.1.27... |
Q9E6N0 | MGVYGCMNFAYANGLVRSHISGFISGGDMTPIAVDLWNVMYGLLEKLYPGKIDGVDDSIITLRCLYCLLRLLHQRSYYPVFVADRGFYGNGKTLYGAKAIAATCIATRGGSGRLHARLFDECGSTDVGEARCKRKHPGKKVCRWSERFETPKILYQLCMSIIRYMGYPYVDAGTMEADDICANLFHTKTVAYVLSSDTDLILMGCDIIIDLTRIFPPTIYCRDVLAALQMDYFTFLLNFVRCHTDLHREPTLKSMQEIINLSSAKRCLHDTDCATDDDVPRCIRPLYEEQDRRTGENSYHSEGFDLHIRKDQSKTSCWDN... | Function: Minor structural protein that acts as an endoribonuclease during lytic infection. Degrades host mRNAs in the cytoplasm by cutting them at preferred sites, including some in regions of translation initiation (By similarity).
Sequence Mass (Da): 50398
Sequence Length: 441
Subcellular Location: Virion
EC: 3.1.27... |
Q82171 | MGLFGMMKFAHTHHLVKRQGLGAPAGYFTPIAVDLWNVMYTLVVKYQRRYPSYDREAITLHCLCRLLKVFTQKSLFPIFVTDRGVNCMEPVVFGAKAILARTTAQCRTDEEASDVDASPPPSPITDSRPSSAFSNMRRRGTSLASGTRGTAGSGAALPSAAPSKPALRLAHLFCIRVLRALGYAYINSGQLEADDACANLYHTNTVAYVYTTDTDLLLMGCDIVLDISACYIPTINCRDILKYFKMSYPQFLALFVRCHTDLHPNNTYASVEDVLRECHWTPPSRSQTRRAIRREHTSSRSTETRPPLPPAAGGTEMRVS... | Function: Minor structural protein that acts as an endoribonuclease during lytic infection. Degrades host mRNAs in the cytoplasm by cutting them at preferred sites, including some in regions of translation initiation. Together with inhibition of host splicing by ICP27, contributes to an overall decrease in host protein... |
Q6UDJ0 | MGILGMRRFIREHELSVHLSIQMERGLYIPIAVDTWNVLTPIMRRLDPGNMMDPVERTLRGIMQVFSLLNKKSCFPIFVLDGGRKRAFKGPVKHDYHNIDHRAPTDGDDLEASANENQPHSLAGNAPRLASGARGAHQSSRRKTALRATPHYKLCWDLITASGFPTVYVKGMEADYGCANLFHTKTVMYVWSSDSDMVFMGCDVITDLTPAFPVAVFSKHVLEYLNMTQREFANTFVDCHTNLHSPETIYSFAAKLLEHRCGSAIDEPPAASEESSASDQQSADEDEHGAWSRYTRRPPRRADAAAWGAGPGGNGQLKGV... | Function: Minor structural protein that acts as an endoribonuclease during lytic infection. Degrades host mRNAs in the cytoplasm by cutting them at preferred sites, including some in regions of translation initiation (By similarity).
Sequence Mass (Da): 49502
Sequence Length: 440
Subcellular Location: Virion
EC: 3.1.27... |
P36314 | MGLFGLLKYAHRHRLVRSEAISTPPGVLTPIAIDLWNVMYTLMEKHYQETTEDNATTTARCLLRLLRMLHKRTYFPIFVSDRGIFGNGRIARGAKAIMAAAVRADGDGAADAPPRPRWSTMLHAPRIVHRLCVNLIRHMGYAYVDVSDMEADDVCANLYHTNTVAQVHTTDTDMILTGCDMILDIAPVFPLVLRCRDVLASLGVDYSEFLAAFVRCHTDLHRAPDVDSVQQVAESLEGREVAPEDVKLKYASRCPDIMRDAGKALALLPAAGDARSPRAEREFIQHVVAMLTPARHGHLSVLRRVPIVQEPSDVNKVFGS... | Function: Minor structural protein that acts as an endoribonuclease during lytic infection. Degrades host mRNAs in the cytoplasm by cutting them at preferred sites, including some in regions of translation initiation (By similarity).
Sequence Mass (Da): 40910
Sequence Length: 365
Subcellular Location: Virion
EC: 3.1.27... |
P09275 | MGLFGLTRFIHEHKLVKPSIISTPPGVLTPVAVDVWNVMYTLLERLYPVGKRENLHGPSVTIHCLGVLLRLLTQRSYYPIFVLERCTDGPLSRGAKAIMSRAMNHDERGTSDLTRVLLSSNTSCSIKYNKTSETYDSVFRNSSTSCIPSEENKSQDMFLDGCPRQTDKTICLRDQNVCSLTSTMPSRGHPNHRLYHKLCASLIRWMGYAYVEAVDIEADEACANLFHTRTVALVYTTDTDLLFMGCDILLDAIPMFAPVVRCRDLLQYLGITYPEFLVAFVRCQTDLHTSDNLKSVQQVIQDTGLKVPHQMDTSTRSPTY... | Function: Minor structural protein that acts as an endoribonuclease during lytic infection. Degrades host mRNAs in the cytoplasm by cutting them at preferred sites, including some in regions of translation initiation (By similarity).
Sequence Mass (Da): 51368
Sequence Length: 455
Subcellular Location: Virion
EC: 3.1.27... |
Q701R1 | MKPNLKQWKQFMLFGICAWGLLFLVIFVYFTDSNSVEPVPSAFSYVESKKHFPLQGKQRAIMGAHQDQLFSYAIDDQDLLKEGILDSFIVGPGSMKKMAGADNYFESEQEFIMSKKTQKSTSNNHEDDDDEIYLHKNIDSVSGKKAPAYGKRYYHDTQRQHKKIRRNMQRKKQHMIEDSYDWNGFSSSMSKSFLQKLWKGNVSSKMLTPRLQKARREYLRANKLGVNFNGKQNSRKLNPQELLCVLKDRAQVKTLDGKDAPFSSLGWEKYFPKIALNKLYPHGFSTCAVVSSAGAILNSSLGAEIDSHDAVLRFNSAPTR... | Function: Transfers sialic acid from the donor of substrate CMP-sialic acid to galactose containing acceptor substrates.
Catalytic Activity: a beta-D-galactoside + CMP-N-acetyl-beta-neuraminate = an N-acetyl-alpha-neuraminyl-(2->6)-beta-D-galactosyl derivative + CMP + H(+)
Location Topology: Single-pass type II membran... |
Q11203 | MGLLVFVRNLLLALCLFLVLGFLYYSAWKLHLLQWEEDSNSVVLSFDSAGQTLGSEYDRLGFLLNLDSKLPAELATKYANFSEGACKPGYASALMTAIFPRFSKPAPMFLDDSFRKWARIREFVPPFGIKGQDNLIKAILSVTKEYRLTPALDSLRCRRCIIVGNGGVLANKSLGSRIDDYDIVVRLNSAPVKGFEKDVGSKTTLRITYPEGAMQRPEQYERDSLFVLAGFKWQDFKWLKYIVYKERVSASDGFWKSVATRVPKEPPEIRILNPYFIQEAAFTLIGLPFNNGLMGRGNIPTLGSVAVTMALHGCDEVAVA... | Function: Catalyzes the formation of the NeuAc-alpha-2,3-Gal-beta-1,4-GlcNAc-, NeuAc-alpha-2,3-Gal-beta-1,3-GlcNAc- and NeuAc-alpha-2,3-Gal-beta-1,3-GalNAc- sequences found in terminal carbohydrate groups of glycoproteins and glycolipids. The highest activity is toward Gal-beta-1,3-GlcNAc and the lowest toward Gal-beta... |
Q70D51 | MRKKAAGGAERRPLKPRTEAAAAAPAGRAMPSDHSRMKLRRDCSRPSLQWYTRAQNKMRRPNLLLKDILKCTLLLFGVWILFYILKLNHTTEECDMKRMPYMDPDRIKRAQQYAQQVLQKECRPQFAKRSMAQLFGSRYSLDLPPFVTKVPAESEAEYKYDPPFGFRKFSGKVQTLLELLPEHDFPEHLRAKSCKHCVVIGSGGILHGLEMGHALNQFDVVIRLNNAPVEGYSEHVGNKTTIRMTYPEGAPLSDLEYYSSDLFVTVLFKSVDFNWLQAMVKNETLPFWVRLFFWKQVAEKIPLQPKQFRILNPVIIKETA... | Function: Transfers the sialyl group (N-acetyl-alpha-neuraminyl or NeuAc) from CMP-NeuAc to the non-reducing terminal galactose (Gal) of glycosphingolipids forming gangliosides (important molecules involved in the regulation of multiple cellular processes, including cell proliferation and differentiation, apoptosis, em... |
Q9UNP4 | MRTKAAGCAERRPLQPRTEAAAAPAGRAMPSEYTYVKLRSDCSRPSLQWYTRAQSKMRRPSLLLKDILKCTLLVFGVWILYILKLNYTTEECDMKKMHYVDPDHVKRAQKYAQQVLQKECRPKFAKTSMALLFEHRYSVDLLPFVQKAPKDSEAESKYDPPFGFRKFSSKVQTLLELLPEHDLPEHLKAKTCRRCVVIGSGGILHGLELGHTLNQFDVVIRLNSAPVEGYSEHVGNKTTIRMTYPEGAPLSDLEYYSNDLFVAVLFKSVDFNWLQAMVKKETLPFWVRLFFWKQVAEKIPLQPKHFRILNPVIIKETAFD... | Function: Transfers the sialyl group (N-acetyl-alpha-neuraminyl or NeuAc) from CMP-NeuAc to the non-reducing terminal galactose (Gal) of glycosphingolipids forming gangliosides (important molecules involved in the regulation of multiple cellular processes, including cell proliferation and differentiation, apoptosis, em... |
O88829 | MHTEAVGGAARRPQKLRSQAAAPACRAMPSEFTSAKLRSDCSRTSLQWYTRTQHKMRRPSLLIKDICKCTLVAFGVWLLYILILNYTAEECDMKRMHYVDPDRIKRAQSYAQEVLQKECRPRYAKTAMALLFEDRYSINLEPFVQKVPTASEAELKYDPPFGFRKFSSKVQSLLDMLPEHDFPEHLRAKACKRCVVVGNGGILHGLELGHALNQFDVVIRLNSAPVEGYSEHVGNKTTIRMTYPEGAPLSDVEYYANDLFVTVLFKSVDFKWLQAMVKNESLPFWVRLFFWKQVAEKVPLQPKHFRILNPVIIKETAFDI... | Function: (Microbial infection) Gangliosides GD1b and GT1b (derived from GM3) may serve as receptors for some C.botulinum neurotoxins (minimally types BoNT/A, B, C) .
Catalytic Activity: a beta-D-Gal-(1->4)-beta-D-Glc-(1<->1)-Cer(d18:1(4E)) + CMP-N-acetyl-beta-neuraminate = CMP + ganglioside GM3 (d18:1(4E)) + H(+)
Loca... |
Q6KB55 | MRRPSLLLKDILKCTLLVFGVWILYILKLNYTTEECDMKKMHYVDPDRVKRAQTYAQQVLQKECRPKFAKTSMALLFEHRYSVDLLPFVQKAPKDSEAESKYDPPFGFRKFSSKVQTLLELLPEHDLPEHLKAKTCRRCVVIGSGGILHGLELGHTLNQFDVVIRLNSAPVEGYSEHVGNKTTIRMTYPEGAPLSDLEYYSNDLFVAVLFKSVDFNWLQAMVKNETLPFWVRLFFWKQVAEKIPLQPKHFRILNPVIIKETAFDILQYSEPQSRFWGRDKNVPTIGVIAVVLATHLCDEVSLAGFGYDLSQPRTPLHYFD... | Function: Transfers the sialyl group (N-acetyl-alpha-neuraminyl or NeuAc) from CMP-NeuAc to the non-reducing terminal galactose (Gal) of glycosphingolipids forming gangliosides (important molecules involved in the regulation of multiple cellular processes, including cell proliferation and differentiation, apoptosis, em... |
D4B4P1 | MGIKQWLLSLVVVAISATATQARVDDPAGKAAQYHKEYALFRSANMPSPDKLASGVGFHSFRIPAVVRTNTGRILAFAEGRRHNNRDYGDINLVYKRTKSPTNNGENPTDWESLREVVGTGPHTWGNPTPVVDGNTIYLFLSMNDGAYSQNGGNTLPDGTKTKTIDSTWVGRRHLYLTTSTDDGDTWTKPVDMTKTLTPDGQAWDAVGPGNGIKLSTGELVIPAQGRNIIGHGPSGNRTWSMQVLKGAGSEGTICQTPDGKLMRNDRPGPMGHRSVARGTLAGFGPFATDNGLPDPACQGSILSYNSDEPARTIFMNSAS... | Function: Sialidase is able to release sialic acid from a wide variety of natural substrates.
Catalytic Activity: Hydrolysis of alpha-(2->3)-, alpha-(2->6)-, alpha-(2->8)- glycosidic linkages of terminal sialic acid residues in oligosaccharides, glycoproteins, glycolipids, colominic acid and synthetic substrates.
Seque... |
Q4WQS0 | MQSMRFMILALLVQFLPAWAINDPAKSAAPYHDEFPLFRSANMASPDKLSTGIGFHSFRIPAVVRTTTGRILAFAEGRRHTNQDFGDINLVYKRTKTTANNGASPSDWEPLREVVGSGAGTWGNPTPVVDDDNTIYLFLSWNGATYSQNGKDVLPDGTVTKKIDSTWEGRRHLYLTESRDDGNTWSKPVDLTKELTPDGWAWDAVGPGNGIRLTTGELVIPAMGRNIIGRGAPGNRTWSVQRLSGAGAEGTIVQTPDGKLYRNDRPSQKGYRMVARGTLEGFGAFAPDAGLPDPACQGSVLRYNSDAPARTIFLNSASGT... | Function: Sialidase is able to release sialic acid from a wide variety of natural substrates including bovine salivary mucin, colominic acid, bovine fetuin, a serum glycoprotein containing both alpha-2-6 and alpha-2-3-linkages in a ratio of about 3:2, and glycoproteins and glycolipids from thermally denatured human lun... |
Q6IA17 | MPGVCDRAPDFLSPSEDQVLRPALGSSVALNCTAWVVSGPHCSLPSVQWLKDGLPLGIGGHYSLHEYSWVKANLSEVLVSSVLGVNVTSTEVYGAFTCSIQNISFSSFTLQRAGPTSHVAAVLASLLVLLALLLAALLYVKCRLNVLLWYQDAYGEVEINDGKLYDAYVSYSDCPEDRKFVNFILKPQLERRRGYKLFLDDRDLLPRAEPSADLLVNLSRCRRLIVVLSDAFLSRAWCSHSFREGLCRLLELTRRPIFITFEGQRRDPAHPALRLLRQHRHLVTLLLWRPGSVTPSSDFWKEVQLALPRKVQYRPVEGDP... | Function: Acts as a negative regulator of the Toll-like and IL-1R receptor signaling pathways. Attenuates the recruitment of receptor-proximal signaling components to the TLR4 receptor, probably through an TIR-TIR domain interaction with TLR4. Through its extracellular domain interferes with the heterodimerization of I... |
Q9JLZ8 | MAGVCDMAPNFLSPSEDQALGLALGREVALNCTAWVFSRPQCPQPSVQWLKDGLALGNGSHFSLHEDFWVSANFSEIVSSVLVLNLTNAEDYGTFTCSVWNVSSHSFTLWRAGPAGHVAAVLASLLVLVVLLLVALLYVKCRLNMLLWYQDTYGEVEMNDGKLYDAYVSYSDCPEDRKFVNFILKPQLERRRGYKLFLEDRDLLPRAEPSADLLVNLSRCRRLIVVLSDAFLSRPWCSQSFREGLCRLLELTRRPIFITFEGQRREPIHPALRLLRQHRHLVTLVLWKPGSVTPSSDFWKELQLALPRKVQYRPVEGDPQ... | Function: Acts as a negative regulator of the Toll-like and IL-1R receptor signaling pathways. Attenuates the recruitment of receptor-proximal signaling components to the TLR4 receptor, probably through an TIR-TIR domain interaction with TLR4. Through its extracellular domain interferes with the heterodimerization of I... |
Q86MW9 | MNNSITEVNMSVPSRATNSNNTILSEERTCHRSQMASSDAVGRTMALLPINHNHALHHGIKLMPHINMPHREVGATTPLVTNSGTASTCSMSLPGSMSSASDTVCNILPHNTSDSSSIDLASLFECPVCMDYALPPIMQCQSGHIVCASCRSKLSSCPTCRGNLDNIRNLAMEKLASSVLFPCKYSTSGCPETFHYTSKSEHEAACEYRPYDCPCPGASCKWLGELEQVMPHLVHHHKSITTLQGEDIVFLATDISLPGAVDWVMMQSCFGHSFMLVLEKQERVPDQIFFALVQLIGTRKQADQFVYRLELNGHRRRLTW... | Function: E3 ubiquitin-protein ligase that mediates ubiquitination and subsequent proteasomal degradation of target proteins. E3 ubiquitin ligases accept ubiquitin from an E2 ubiquitin-conjugating enzyme in the form of a thioester and then directly transfers the ubiquitin to targeted substrates. Mediates the ubiquitin-... |
Q5XVI1 | MGLNLNPILRQELANLDKDTESRKSAMKALKSYVKDLDSKAIPGFLAQVFETKETNSLSGEYTISLYEILARVHGPNIVPQIDTIMSTIVKTLASSAGSFPLQQACSKVIPAIARYGIDPTTTEDKKRVIIHSLCKPLTDSLLASQESLTSGAALCLKALVDSDNWRFASDEMVNRVCQNVVVALDSNSNQTHLQMGLVMSLAKHNPLIVEAYARLLIHTGLRILGFGVSEGNSQKRLSAVQMLNFLMKCLDPRSIYSEVELIIKEMERCQSDQMAYVRGAAYEAMMTSKRIAAELESKMEKGCRSVTGSNFSRRNCSSI... | Function: Plays a role in nucleus positioning in guard cells.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 62153
Sequence Length: 560
Domain: The KASH domain, which contains a transmembrane domain, mediates the nuclear envelope targeting and is involved in the binding to the SUN proteins.
Subcell... |
Q9SQR5 | MGRNLGSAFRQELANLDKDPDSHKTAMSNLRSIVKDLDAKVVHVFVAQLSDVKEIGLESGGYTVSLFEDLARAHGVKIAPHIDIIMPAIIRTLSSSEGSLRVQQACSRAVAAMARYGIDPTTPEDKKTNVIHSLCKPLSDSLIDSQHQQHLALGSALCLKSLVDCDNWRSASSEMVNNVCQSLAVALEATSSEAKSHMALVMALSKHNPFTVEAYARLFVKSGLRILDLGVVEGDSQKRLLAIQMLNFLMKNLNPKSISSELELIYQEMEKYQKDQHYVKMAAHETMRQAERLICEADPMFDAENCKPRNSLSGSVKSTS... | Function: Plays a role in innate immunity against the oomycete pathogen A.arabidopsidis (Hpa).
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 61442
Sequence Length: 554
Domain: The KASH domain, which contains a transmembrane domain, mediates the nuclear envelope targeting and is involved in the bin... |
Q9C900 | MKEIQIPRKSFARSSELGAKRLKDPEMKNRKVTTEKRQIATFSDVSFESTKDPMDFSPISQISGAISDSEAESVIQGSSLDLMSTPEICLPADDSPVSTITSVEARIDTSSTDRIQSIVDLPASVQSLRGEINELKKLICSVDNSAEINWVDRVVTVKFRIVLLSFILWAILAAIVVFFSSGEERAYRGPLPT | Location Topology: Single-pass membrane protein
Sequence Mass (Da): 21284
Sequence Length: 193
Domain: The KASH domain, which contains a transmembrane domain, mediates the nuclear envelope targeting and is involved in the binding to the SUN proteins.
Subcellular Location: Nucleus membrane
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Q9SW31 | MEEREESSSHEHLKEKLRELEEEWTAMKTGKNSSAVSWITVEDALEYVENSPRNLMLSLQHKPKAEMIQEISPLRRKLFHDSDDDDQTKKTTLLSHSSCWSSNVTSSSDTTKAKKKTTIRRFVSVTMVLLLSWVLVVLMNHFDHLSMNTQIITLVPT | Location Topology: Single-pass membrane protein
Sequence Mass (Da): 18116
Sequence Length: 157
Domain: The KASH domain, which contains a transmembrane domain, mediates the nuclear envelope targeting and is involved in the binding to the SUN proteins.
Subcellular Location: Nucleus membrane
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Q9VXD1 | MASFGVRGMGQPLGIRICCCRVCTCINFGFVLSRIGLLKLMQLGLAMLCEGLLIRYGVPYADSIGQALTSFLATTGHCFTTTGILLLCYAFSDKSYSLIRQSLFETLFNGLASCMYFSSSSYMGFACVVWLHPQFLVRPGFWAYPAMTACYYMGYAAGILHALDAYLAFRHFRGAR | Function: Essential for myoblast fusion in developing embryos and pupae, and consequently is essential for muscle formation in adults . Required for progression past the pre-fusion complex stage of myoblast fusion .
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 19460
Sequence Length: 176
Subcellula... |
Q9C6H4 | MVKGTNAEQALAREEASSSRPKRQRVPSIVEEEGENGGGDVVVRSGTLFELDLLDCPICCNALTIPIFQCDKGHIACSSCCTNVSNKCPYCSLAIGNYRSRIMERVVEAFIVRCPIVAGEASSSRQKRLRVPSIDEENGENGGRDVVVPSGTLSQLDLLDCPVCSKALKISIFQQSLFLAKRQNGCTETFSYGNELVHEKKCSFALCYCPAPNCNYAGVYKDLYSHYAANHKKLWTRFSCGYSMHVCMDFESKSLVLQQYSDGPLVVLQCFKEPPQGLFWTVNCIAPSAPGVGKFSYELSYSTAGNTLTFRSSEMNRIQK... | Function: E3 ubiquitin-protein ligase that mediates ubiquitination and subsequent proteasomal degradation of target proteins. E3 ubiquitin ligases accept ubiquitin from an E2 ubiquitin-conjugating enzyme in the form of a thioester and then directly transfers the ubiquitin to targeted substrates. It probably triggers th... |
Q9C6H3 | MSGEASTSRRKRQRVPSSVESVENGGGDAVARSGTLFELDLLDCPICCHALTSPIFQCDNGHIACSSCCTKLRNKCPSCALPIGNFRSRIMERVVEAVMVTCPNVKHGCTEKFSYGKELIHEKDCRFALCYCPAPNCNYSGVYKDLYSHFYVNHYDTWNQIGCGNFAGAWLRISEKILVLQYGQGPLIAVQCFKETQGMYVTVNCIAPCAPGVGELSFELSYKMPMGGNSTMMFKSEEMNRIQKVSFQTPEKDFMLVPYYFLGDFSTLKMEICIRKLKKDEEEADEDEESEEEEDDDDDDDDDDEEEDADEEE | Function: E3 ubiquitin-protein ligase that mediates ubiquitination and subsequent proteasomal degradation of target proteins. E3 ubiquitin ligases accept ubiquitin from an E2 ubiquitin-conjugating enzyme in the form of a thioester and then directly transfers the ubiquitin to targeted substrates. It probably triggers th... |
Q9C6H2 | MENITNNSERSLDRPKRQRPVSMENVGGTASGSEVARSATLLELDLLDCPICYHKLGAPIYQCDNGHIACSSCCKKVKYKCPYCSLRIGFFRSRILEKIVEAVVVSCPNAKYGCTEKIPYDNESESAHERVCEFTLCYCPEPECKYTGVYTDLYRHYHAEHKTDHSWFKCGEYNNAWLHVTGEKLSFLVLQEYEDGPLVVVQCSMESHGICVTVNCIAPCAPGVGEFSCHLIYRNGSEKITFESKKMNKIQKVSPENHVANYKPIPYYLRGEASNFMSIPYYLLDEASILKMQICIRRSGEEV | Function: E3 ubiquitin-protein ligase that mediates ubiquitination and subsequent proteasomal degradation of target proteins. E3 ubiquitin ligases accept ubiquitin from an E2 ubiquitin-conjugating enzyme in the form of a thioester and then directly transfers the ubiquitin to targeted substrates. It probably triggers th... |
Q9C9M0 | MTKLGRRNDGGGKSHRSSTKRQRRTSVSVDDPSPGEEEEKTLVVLTDDSDSEEDDKPLGDVLRTCRKRRVSSPKSVTLPNSNVLECPNCFDPLKKPIFQCNNGHLACFLCCIKLKKRCSFCKLPIGDVRCRAMEKVIKAGLVSCSNAIYGCKQSTTYGNQLQSHEKVCVFAPCSCPIKDCNYIGFYKDLINHFRATHKVSPGDINSFVFDRPVIFGLDLDSSDKMVIFVEEKQGNLFVVQGFIGSHGVYATVSHIAPMVPEVRKFSCSLARLRPYSTLRLGLEVKNIQKLRSQEEQPQEDFLLIPSYMVNGDHMKMEISI... | Function: E3 ubiquitin-protein ligase that mediates ubiquitination and subsequent proteasomal degradation of target proteins. E3 ubiquitin ligases accept ubiquitin from an E2 ubiquitin-conjugating enzyme in the form of a thioester and then directly transfers the ubiquitin to targeted substrates. It probably triggers th... |
Q7XA77 | MARSGGNDGHEEELDPELFEEPSNLEGYEDGEFEEDEEEFEEEEEELEEEEDEEEEEEENVTTDEQSGSPKSSQPVKLQSSDVLDCPTCCEPLKRPIYQCSNGHLACSSCCQKLNKKCSFCRCNIGDIRCRAMEKVIEASIVPCPNAKHGCKETTTYCNQSSHEKVCKFVRCSCPVSNCNYVSSYSNLKSHACSTAHVWGEDDIHFQLVIDRPRIFNMNLGRKKTVVFKEEKEGDLIVVQAFKGLEGVYVTVNRIAHMAPGIRDLSCSLAKLNEYSTLRSGSLVKKIQKVREKMHLEDDLMWIPPKMLSGDHWKMQICIA... | Function: E3 ubiquitin-protein ligase that mediates ubiquitination and subsequent proteasomal degradation of target proteins. E3 ubiquitin ligases accept ubiquitin from an E2 ubiquitin-conjugating enzyme in the form of a thioester and then directly transfers the ubiquitin to targeted substrates. It probably triggers th... |
Q9FKD7 | MVGAAILESPGEGIGSNSILSQKRQLSSSDAAKRDAKKRSTMLMDLEILDCPICYEAFTIPIFQCDNGHLACSSCCPKLNNKCPACTSPVGHNRCRAMESVLESILIPCPNAKLGCKKNVSYGKELTHEKECMFSHCACPALDCNYTSSYKDLYTHYRITHMEINQINTFICDIPLSVRMNISKKILIRTEHLTNHLFAVQCFREPYGVYVTVSCIAPSSPELSQYSYALSYTVDGHTVIYQSPEVKRVLKLSFQTPQENFMLIPNSLLRGDVLEMRISVKKLNKE | Function: E3 ubiquitin-protein ligase that mediates ubiquitination and subsequent proteasomal degradation of target proteins. E3 ubiquitin ligases accept ubiquitin from an E2 ubiquitin-conjugating enzyme in the form of a thioester and then directly transfers the ubiquitin to targeted substrates. It probably triggers th... |
Q9FKD6 | MVGALEALISQGHGGERVAKRQRSATLLDLDILDCPICCEGLTCPIFQCENGHLACSSCCPKLRNKCPACPMENILESILVTCPNDMFGCTESFLYGKKSTHEEECIFSLCSCPSLDCEYSGRYEDLYDHYKLTHISNSYWTTNCFRSSIPYKAPMLISDKIQITRVYEKKILFAVQCFRESCGVYVTVSCIAPSAPEVGQFSYQISYTVDEHTMVYRSPQMKRVRKVSFETPQENFMLIPHNLLRSELLDIKLSIVETSNQE | Function: E3 ubiquitin-protein ligase that mediates ubiquitination and subsequent proteasomal degradation of target proteins. E3 ubiquitin ligases accept ubiquitin from an E2 ubiquitin-conjugating enzyme in the form of a thioester and then directly transfers the ubiquitin to targeted substrates. It probably triggers th... |
Q9FKD5 | MVLASISEALISQGDGGERVAKRQRSAIVLLDLDILDCPICCEALTSPIFQCDNGHLACGSCCPKLSNKCPACTLPVGHSRSRAMESVLESILIPCPNVRFGCTKSFFYGKESAHEKECIFSQCSCPSSVCDYTGSYKDLYAHYKLTHSTNIFWNIKRFRCANFFTTSMLISDKILIKRVHEKKLLLAVQCFREPCGVYVTVSFIAPSAPEVGEFSYQLSYNVDGHTVTYESPEVKRVCKVSIETPQENFMLIPHSLLRGDLLEMQVFIIENVDQE | Function: E3 ubiquitin-protein ligase that mediates ubiquitination and subsequent proteasomal degradation of target proteins. E3 ubiquitin ligases accept ubiquitin from an E2 ubiquitin-conjugating enzyme in the form of a thioester and then directly transfers the ubiquitin to targeted substrates. It probably triggers th... |
O34632 | MKQAILYVGHGSRVKKAQQEAAAFLEGCKAHISVPVQEISFLELQEPTIETGFEACVKQGATHIAVVPLLLLTAAHAKHDIPEEIVRVASRYPSVRISYGKPIGIDEEVVKAVYHRMKDIGVPYENARVVLIGRGSSDPDVKRDVTGIANLLQEMVPVKEVIPCFLTACGPNYKEVFSELEKDDGITTFIVPYLLFTGMLMNEIEREVQKLKAHNPNVYLSSYIGFHPHVKNAFLNRVRETAANSEGQFDFDGGSYASAAH | Function: Chelates iron to the siroheme precursor.
Catalytic Activity: 2 H(+) + siroheme = Fe(2+) + sirohydrochlorin
Sequence Mass (Da): 28835
Sequence Length: 261
Pathway: Porphyrin-containing compound metabolism; siroheme biosynthesis; siroheme from sirohydrochlorin: step 1/1.
EC: 4.99.1.4
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Q6Q884 | MSTLQDFQIAPAILHRVTVRDASAILFCTLLTVFLFISQGTVRGVKRVGKSRLRTLVTGETPLRFDLEKYGYLGYQQFSKKANKPFLVKIYGLDHYVLPVKYLDSLKTVDHHRLSFAQSLNDFLNVDASLGDLVTHSDMEIAVVTKHLNPRLTTLTPVLVDEANFAFEKELGKLETWKTVNALFLSAFLTNRTSGRVLVGDLCRDDNYLHAMMKYTESVFSSGVAFNGIPLGPFRKIVYYLGARQHRRDLDNAAALVLPEIKRRMAAQAEDPNCRKENDAIQWNLDLPLASPKEGLPLRHAHRVLHLSFAATGTVAILIT... | Function: Cytochrome P450 monooxygenase; part of the gene cluster that mediates the biosynthesis of sirodesmin PL, an epipolythiodioxopiperazine (ETP) characterized by a disulfide bridged cyclic dipeptide and that acts as a phytotoxin which is involved in the blackleg didease of canola . SirD catalyzes the O-prenylatio... |
P61817 | MHKKLTKEVDYMDAVLYVCHGSRVKEGADQAVAFIERCKKNLDVPIQEVCFLELASPTIEQGFEACIEQGATRIAIVPLLLLTAAHAKHDIPEEIQKVYERYPQVEVLYGEPFGVDERIVDILVERINETNVDKHEDSMVLLVGRGSSDPAVKRDLNEIAQLLKGKGAFKEVSTCYLAAASPNLKEGLHLAKRTSYKQVFVLPYLLFTGILMNEIKEELEQLSTDAQQFILANYLGYHDGLAHILSHQVKTLLSSKGNQYDVYRYA | Function: Chelates iron to the siroheme precursor.
Catalytic Activity: 2 H(+) + siroheme = Fe(2+) + sirohydrochlorin
Sequence Mass (Da): 29938
Sequence Length: 266
Pathway: Porphyrin-containing compound metabolism; siroheme biosynthesis; siroheme from sirohydrochlorin: step 1/1.
EC: 4.99.1.4
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O34813 | MLPLHISLEKKKVVIAGGGSIALRRLKTVISEGADITLVSPDVEPEIKQMAEERRIKWEKRTIEKEDYLNAFFIIAATDNAAVNKEIAQSASPFQLVNCVSDAELGNVYMPKIVKRGHVTVSVSTSGASPKHTKELAENVDKLIDGDFVAEVNRLYQMRRKK | Function: Catalyzes the dehydrogenation of precorrin-2 to form sirohydrochlorin which is used as a precursor in both siroheme biosynthesis and in the anaerobic branch of adenosylcobalamin biosynthesis.
Catalytic Activity: NAD(+) + precorrin-2 = 2 H(+) + NADH + sirohydrochlorin
Sequence Mass (Da): 18004
Sequence Length:... |
Q6Q881 | MESIVYETQPLLRGMVVGTIMLLCYRYGLALSILQLYLNFMYRITNEKGKPLRGPEFSWPDGQTVEKFLQGGQKSFSWQAYGPLYRIWTVFRPEVVITRPEDVKAFFFDSHTHQKAASSNAGWLFSQILGDCLGLINGERWSRVRHAFDPFFTRKISAQRLPHIMAAGEGYVNEVHQYDLGGKQAASTINLNAVDAFQRFPFFYVAEIIYGPLGITERVELWKLAETHTNIFRRLVQGGIHRYKATKFLSTSAYKETAHFVAAWRQFTLELAQKQLREGRTSPLTDLMAEVEDGKVTLNEVLHTIDESLFANLDVTTHVL... | Function: Cytochrome P450 monooxygenase; part of the gene cluster that mediates the biosynthesis of sirodesmin PL, an epipolythiodioxopiperazine (ETP) characterized by a disulfide bridged cyclic dipeptide and that acts as a phytotoxin which is involved in the blackleg didease of canola . SirD catalyzes the O-prenylatio... |
P61818 | MYTVMLDLKGRSVLVVGGGTIATRRIKGFLQEGAAITVVAPTVSAEINEWEAKGQLRVKRKKVGEEDLLNVFFIVVATNDQAVNKFVKQHIKNDQLVNMASSFSDGNIQIPAQFSRGRLSLAISTDGASPLLTKRIKEDLSSNYDESYTQYTQFLYECRVLIHRLNVSKSRKHELLTEIIDDQYRLSLVKQREFLQQIEKYK | Function: Catalyzes the dehydrogenation of precorrin-2 to form sirohydrochlorin which is used as a precursor in both siroheme biosynthesis and in the anaerobic branch of adenosylcobalamin biosynthesis. It is unable to oxidize precorrin-3.
Catalytic Activity: NAD(+) + precorrin-2 = 2 H(+) + NADH + sirohydrochlorin
Seque... |
Q6Q874 | MQTARLFQGNLNLAAANIRDYEKKEQRNLGVWLSLNQWLRLYDEDTRFWWTTTAPMLGRMMELIGYDQDAQQKHLLFYYIYVLPSLGRRPSPEGYPTGWNSFMTDDYSPLELSWDWGVAEGESSVRFSIEPIGKYAGTQADPLNQKMVYQLVDGLRPAFHHTLDLTLFDVFSEALTTSREKFGTRKLSLEGRSQYFVAFDLDVGHPRLKAYFMPGLKSIESNTPVSELVVKAMDACELHFGSLFMQAFRRLNSDLEAFSATSYHRPEIEIVGIDCVSPVKSRAKIYIRHRGTSFDSVCRMLSMGAKAPLDAASVASLREL... | Function: 4-O-dimethylallyl-L-tyrosine synthase; part of the gene cluster that mediates the biosynthesis of sirodesmin PL, an epipolythiodioxopiperazine (ETP) characterized by a disulfide bridged cyclic dipeptide and that acts as a phytotoxin which is involved in the blackleg didease of canola . SirD catalyzes the O-pr... |
Q6Q879 | MFFRYTVTLVANETDHHATVVQALLRRHIGDITPGTTQEIENALETVCGQSKEWSSTSLAAIIIAVVARSTSRLLVGPSLCRNNDYINLCIEYATEMESSAAKIRALVPFLRPLIAPYYCRRLAELRKLAHAHIAPLLAGPDSAPKEKNASSQYTAVQWLAQKLRGVPEETEERQVARIMFLNVISIFTVMMASLNVLYDILARPDVKRALLEEIAEVSGGKGDLGLGDVEFERLRRLDSCIRESQRLNPTNWIILEGQAQKDLTFSTGLCVEKGSYLSICGGAILKSNGPPLSTSSNPPPIDEFHAFRYVTPDSGISTD... | Function: Cytochrome P450 monooxygenase; part of the gene cluster that mediates the biosynthesis of sirodesmin PL, an epipolythiodioxopiperazine (ETP) characterized by a disulfide bridged cyclic dipeptide and that acts as a phytotoxin which is involved in the blackleg didease of canola . SirD catalyzes the O-prenylatio... |
Q6Q889 | MVSAKLPSIFIEAQLPLIYANIILAFALGPQAHTFRVCLTLPILLFLVCQSLYREQNGPWEDLLSNNSLVMFTVFVYIDWILLQSPDREQWHKLNNAKTESNGPTKAKESGPPHGFFQRIWFGCRIATAWRYIGWSCQVKNVPMEHSAGYPRRYFIARKSLRALAFYLMKETLEVYTASTPHGGWWDTQNTKPALSIKNVPLWHQFKYTWVHIFLAYATLEMANSILGVVSVILHLATPQECPSAFGDLEDFFTVRKAWSTVWHQHMRRLTSTMGLFVARDLMQLRKGSFQSKYVQLFVGFGVSAGLHAGVALLCSKALN... | Function: Acetyltransferase; part of the gene cluster that mediates the biosynthesis of sirodesmin PL, an epipolythiodioxopiperazine (ETP) characterized by a disulfide bridged cyclic dipeptide and that acts as a phytotoxin which is involved in the blackleg didease of canola . SirD catalyzes the O-prenylation of L-tyros... |
Q6Q887 | MLSQRSQRNTSEIIPRLLREYHQPQAGNIDILDLSQAENSVLRDETLDEIRSAIGKHLNGSNLSYPTGVGGELAARKSLAMFFNDRFNPARSVSPDHIVMTPGASEALETLIFHICDPGEGVLIAAPYWSGLDLALETRSLARIVQVNIPLHEFFEMSSIQYYERALATSPIPIKAILMCNPHNPLGQCYNADVLEGLLGFCQRNKLHYISDEVYGMSVFSDSDKGVTPAFTSILSHATAPGLTSWVHMVYSLSKDFGCSGLRLGAIVTQGNTDLLLGSALITNNKVSSLTSVIVPSLLEPRTTQKLLNQNLRSRLNLNY... | Function: Probable aminotransferase; part of the gene cluster that mediates the biosynthesis of sirodesmin PL, an epipolythiodioxopiperazine (ETP) characterized by a disulfide bridged cyclic dipeptide and that acts as a phytotoxin which is involved in the blackleg didease of canola . SirD catalyzes the O-prenylation of... |
Q6Q886 | MKSEPGNEFLERAANLLSRVPLIDGHNDWANIIRGYYSNKIHVRNFSREESLVGHVDIKKLRKGLVGGTFWSAYVDCPAQDKINVFNDDSYLETIRETLQQIDLILRLIKKYPDDLELATTSSGILSSFQNGKIASLLGIEGLHQIGNSPSVLRMFYNLGVRYATLTHNHNNAYADSATAKTPVHNGLSIKGRAIIQEMNRLGMIIDLSHTSEQTAEDVLRQTRAPIIFSHSSAFGVHPHPRNVKDNILHMLKSNKGLIMISFVPEFSSADPGLSSLMDVVKHIIYVGELIGYDHVGIGSDFDGMARAVLGLSDTSTFPR... | Function: Dipeptidase; part of the gene cluster that mediates the biosynthesis of sirodesmin PL, an epipolythiodioxopiperazine (ETP) characterized by a disulfide bridged cyclic dipeptide and that acts as a phytotoxin which is involved in the blackleg didease of canola . SirD catalyzes the O-prenylation of L-tyrosine (L... |
O64483 | MAMLKSLSSILFTSFALLFFLVHAQDQSGFISIDCGIPDDSSYNDETTGIKYVSDSAFVDSGTTKRIAAQFQSSGFDRHLLNVRSFPQSKRSCYDVPTPRGKGFKYLIRTRFMYGNYDDLGRVPEFDLYLGVNFWDSVKLDDATTILNKEIITIPLLDNVQVCVVDKNAGTPFLSVLEIRLLLNTTYETPYDALTLLRRLDYSKTGKLPSRYKDDIYDRIWTPRIVSSEYKILNTSLTVDQFLNNGYQPASTVMSTAETARNESLYLTLSFRPPDPNAKFYVYMHFAEIEVLKSNQTREFSIWLNEDVISPSFKLRYLLT... | Function: Involved in innate immune response of plants.
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 98712
Sequence Length: 876
Subcellular Location: Membrane
|
Q6Q880 | MDNELDNLISLLQKSKASLKEKHGDRIRSIFAAHHSGSILPKEDKSLYDKCLATVDLLDEVQQMLTPPLHTLIDGFFGFINSKTLLCAVEFGIPDALSQGPKSIEQLASSSPQGELSPHRLTQVLRTLTGIGIFNYDKTSKLYSNNATSDLITTAHWSKWVYWTKFYPTEFYDMMRFLPDHIKANASRTAAQSNYNTDMEFYEYLSNSGLAKEFHRVLGAGATAQLPGMISDFPWDTLGDETVLDLGTGSGEFLFQLLENYPRMRGAFMDIPSTISRIQAECEQPGGRFSGVRDRVAGFHAGNFLDEVPASVVYTIKWCL... | Function: O-methyltransferase; part of the gene cluster that mediates the biosynthesis of sirodesmin PL, an epipolythiodioxopiperazine (ETP) characterized by a disulfide bridged cyclic dipeptide and that acts as a phytotoxin which is involved in the blackleg didease of canola . SirD catalyzes the O-prenylation of L-tyr... |
Q6Q875 | MSPSAHPDAPIIIFGTANFGSPEDSKGKLFGPVTVEQGREYLDVLQEFNVDVLDTARIYSGGESEKLLGALDASREFKMCTKASGTLDGCGTRDAVLSAFKASSEALGVKEVDTYYLHTPDRTTSLEETMDTINELHKAGSFKTFGISNLRADEVQHLHTYARSKNYILPTIYQGTYNLLSRQCETKLLPLLRTLGIRFYAYSPLCCGLLINAEAKLQASTGRWDTSHFGGKFMNALYNKPSYIAASNAFQDMCGKYGVRPAGAAYRWVRYHSELEGGLGDGMVVGASSARQLEESLGEIEKGPLEEGLVGELEGLWDLV... | Function: Oxidoreductase; part of the gene cluster that mediates the biosynthesis of sirodesmin PL, an epipolythiodioxopiperazine (ETP) characterized by a disulfide bridged cyclic dipeptide and that acts as a phytotoxin which is involved in the blackleg didease of canola . SirD catalyzes the O-prenylation of L-tyrosine... |
Q6AVN2 | MAEAAITRYWCHECEQAIEEAMVDEIKCPSCGGGFVEEMTDEEIERLTNRQPEPGFSQWNPIEHPGETMDSDDEDNDLGREFEGFIRRHRRASTLRRVLDSIHDDLADDQERDSSILINAFNQALALQGSVLDPDEGQGDQGGSTNDDGLLEEYVLGAGLSLLLQHLAESDPSRNGTPPAKKEAVEALPTVKIEEVVSCSVCLDDLEVGSQAKQMPCEHKFHSSCILPWLELHSSCPVCRFELPSEETKDLNEPSNIGRVEDSHEEVRADGPGNVSESSNRPWAIVPWLNELFSTREAQNAGGVSTDQQSPHTSGTNPNA... | Function: Possesses E3 ubiqutin-protein ligase activity in vitro. Acts as negative regulator of salinity stress tolerance mediated by the ubiquitin-proteasome degradation pathway.
Catalytic Activity: S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enz... |
A7TZF0 | MGSIQIIFAAYCVVLCVLQMLVLSSEQFTITGLERPVLAPLGGILELSCQLSPPQNAQQMEIRWFRNRYTEPVYLYRNGKDLHGETISKYVERTELLKHDIGKGKVTLRVFKVTVDDDGSYHCVFKDGIFYEEHITEVKVTATSSDIKIIMHPPNIKGVMLECHSRGWFPQPHMEWRDSNGQVIPATSKSQSQDENKLFNMTMNLFADVGLHQIVTCYIQNLLTHQEESISIVLTGDLFSWKIDWILILSIIACVMIPYSMTSYLQQHLIHGSCSQRSHHWRKNAMVCMSSVIAIIGSMLILHLKQRVPISDQHFELDTL... | Function: May act by engaging a cell surface molecule on immature T-cells in the embryonic thymus.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 53068
Sequence Length: 458
Subcellular Location: Membrane
|
A7TZF3 | MGATEVLTSYCVVLCLLQMVALSSGHFTVIGSQRPILATLGGNVELNCQLSPPQQAQHMEIRWFRNRYTQPVHLYRNGKNLHGETMSKYVERTELLTDAFNEGKVILRILNVTVDDGGAYHCVFKDGEFYEEHITEVKVTATSSDIQILMHTPNIKGVMLECHSGGWFPQPHMEWRNSKGEVIQATSKFHSQDKNKLFNMSMVLFIEASSHRNVICYFQNLVTHQEQSINIVLSGELFSWKIVWIMILSTISFVMIDFCMTYCVQQQLIHEESLSTVDNDQCESDQSEGTCYKRNYPWIIIAVVPIISVFAIIGVMLFLH... | Function: May act by engaging a cell surface molecule on immature T-cells in the embryonic thymus.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 54166
Sequence Length: 474
Subcellular Location: Membrane
|
A7XV04 | MMKPEFFCFSGFCVYFLFLQVVVSSEKLRVTTPTRHLLARVGGQAELSCQVIPPHSVMHMEVRWFRSGHSQPVYLYRGGHKMSEEAAPEYANRTEFVKEAIGEGKVSLRIHNINILDDGPYQCSFNGSGFIDAAIMNLNVTAVGLETEIHVQAPDADGVMVECNSGGWFPRPQMEWRDSKGATLPHSLKSYSQDEARFFYMKMTLLLTNMSHGSIICCIFNPVTGEEKQTSIILANELFNRDRIWMESLASIVWIMLSVYILYIICFYWRTGCASGCLSKCFCVVTSWPVQIVHLLFCTGTFFAIYLPHRSRVSLSDPQF... | Function: May act by engaging a cell surface molecule on immature T-cells in the embryonic thymus.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 45215
Sequence Length: 395
Subcellular Location: Membrane
|
P12755 | MEAAAGGRGCFQPHPGLQKTLEQFHLSSMSSLGGPAAFSARWAQEAYKKESAKEAGAAAVPAPVPAATEPPPVLHLPAIQPPPPVLPGPFFMPSDRSTERCETVLEGETISCFVVGGEKRLCLPQILNSVLRDFSLQQINAVCDELHIYCSRCTADQLEILKVMGILPFSAPSCGLITKTDAERLCNALLYGGAYPPPCKKELAASLALGLELSERSVRVYHECFGKCKGLLVPELYSSPSAACIQCLDCRLMYPPHKFVVHSHKALENRTCHWGFDSANWRAYILLSQDYTGKEEQARLGRCLDDVKEKFDYGNKYKRR... | Function: May play a role in terminal differentiation of skeletal muscle cells but not in the determination of cells to the myogenic lineage. Functions as a repressor of TGF-beta signaling.
PTM: Ubiquitinated by ARK2C, promoting proteasomal degradation, leading to enhance the BMP-Smad signaling.
Sequence Mass (Da): 800... |
Q60698 | MEAAAAGRGGFQQPGLQKTLEQFHLSSMSSLGGPAVSRRAGQEAYKKESAKEAGAATVPAPVPTAAEPPPVLHLPAIQPPPPVLPGPFFMPSDRSTERCETVLEGETISCFVVGGEKRLCLPQILNSVLRDFSLQQINSVCDELHIYCSRCTADQLEILKVMGILPFSAPSCGLITKTDAERLCNALLYGGAYPPPCKKELAASLALGLELSERSVRVYHECFGKCKGLLVPELYSSPSAACIQCLDCRLMYPPHKFVVHSHKALENRTCHWGFDSANWRAYILLSQDYTGKEEQARLGRCLDDVKEKFDYANKYKRRVP... | Function: May play a role in terminal differentiation of skeletal muscle cells but not in the determination of cells to the myogenic lineage. Functions as a repressor of TGF-beta signaling.
PTM: Ubiquitinated by ARK2C, promoting proteasomal degradation, leading to enhance the BMP-Smad signaling.
Sequence Mass (Da): 801... |
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