ids stringlengths 6 10 | seqs stringlengths 11 1.02k | texts stringlengths 108 11.1k |
|---|---|---|
Q7XT42 | MEGNGCGGSGATPRGVVGMHWAPVVTSPPSPQPPFLPPAPCRPDVQMQQQGGLTCLKLGKRPCFWGGDGAGQVAQGSGGGGGGGGGGSADQGKRKEKAATAVPVVPRCQVEGCDITLQGVKEYHRRHKVCEVHAKAPRVVVHGTEQRFCQQCSRFHVLAEFDDAKKSCRRRLAGHNERRRRSNASEAMARGSAHPHGMPVLGHGFPPYGLPTSSAGALSLLSSARATGPWLMPTPDISARSSAALDELIAENRAALLSWQFFSDRQPPPAGRPTGRSPGSETAGGWHAHLQARPPPPGAGGQHENQSGHVTLDLMQATTA... | Function: Trans-acting factor that binds specifically to the consensus nucleotide sequence 5'-TNCGTACAA-3' (By similarity). May be involved in panicle development.
Sequence Mass (Da): 37387
Sequence Length: 360
Domain: The SBP-type zinc finger is required for the binding to DNA.
Subcellular Location: Nucleus
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Q8GXL3 | MLDYEWDNPSSIVLSGDERNPDSDPTRSSFSFFDPISHYNNDHRHITISPPLLSSFSNQQQQHHLTLYGQTNSNNQFLHHHHHHHSLYGSTTTTTPYGASDPIYHPHSSAPPASLFSYDQTGPGSGSGSSYNFLIPKTEVDFTSNRIGLNLGGRTYFSAADDDFVSRLYRRSRPGESGMANSLSTPRCQAEGCNADLSHAKHYHRRHKVCEFHSKASTVVAAGLSQRFCQQCSRFHLLSEFDNGKRSCRKRLADHNRRRRKCHQSASATQDTGTGKTTPKSPNDSGVKASSSPSSNAPPTISLECFRQRQFQTTASSSTS... | Cofactor: Binds 2 Zn(2+) ions per subunit.
Function: Trans-acting factor that binds specifically to the consensus nucleotide sequence 5'-TNCGTACAA-3'. Binds specifically to the 5'-GTAC-3' core sequence. Involved in development and floral organogenesis. Required for ovule differentiation, pollen production, filament elo... |
Q7XPY1 | MMNVPSAAAASSCDDFGYNATPPPPPSLLPIMDQDGGGGSIQRDHHQHHNHQQLGYNLEPSSLALLPPSNAAAAAAHHATIAHASPHDLLQFYPTSHYLAAAGGAGGGGNPYSHFTAAAAAGSTFQSYYQQPPQDAPEYYFPTLVSSAEENMASFAATQLGLNLGYRTYFPPRGGYTYGHHPPRCQAEGCKADLSSAKRYHRRHKVCEHHSKAPVVVTAGGLHQRFCQQCSRFHLLDEFDDAKKSCRKRLADHNRRRRKSKPSDGEHSGEKRRAQANKSAATKDKAGSSSKNAGIGDGFETQLLGGAHMSKDQDQAMDLG... | Function: Probable transcription factor that plays an important role in building the laminar joint between leaf blade and leaf sheath boundary, thereby controlling ligule and auricle development.
Sequence Mass (Da): 45030
Sequence Length: 416
Domain: The SBP-type zinc finger is required for the binding to DNA.
Subcellu... |
Q700W2 | MEMGSNSGPGHGPGQAESGGSSTESSSFSGGLMFGQKIYFEDGGGGSGSSSSGGRSNRRVRGGGSGQSGQIPRCQVEGCGMDLTNAKGYYSRHRVCGVHSKTPKVTVAGIEQRFCQQCSRFHQLPEFDLEKRSCRRRLAGHNERRRKPQPASLSVLASRYGRIAPSLYENGDAGMNGSFLGNQEIGWPSSRTLDTRVMRRPVSSPSWQINPMNVFSQGSVGGGGTSFSSPEIMDTKLESYKGIGDSNCALSLLSNPHQPHDNNNNNNNNNNNNNNTWRASSGFGPMTVTMAQPPPAPSQHQYLNPPWVFKDNDNDMSPVL... | Cofactor: Binds 2 Zn(2+) ions per subunit.
Function: Trans-acting factor that binds specifically to the consensus nucleotide sequence 5'-TNCGTACAA-3'.
Sequence Mass (Da): 40847
Sequence Length: 375
Domain: The SBP-type zinc finger is required for the binding to DNA.
Subcellular Location: Nucleus
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P74007 | MNAVAALPTPTIHTTCAQDIHDIELPQWLEDCLQQWQREIEQGQDETTAPHCLICRAFCFAYDLHAQQRRKSGEPYIAHPVAVAGLLRDLGGDEAMIAAGFLHDVVEDTDISIEQIEALFGEETASLVEGVTKLSKFNFSSTTEHQAENFRRMFLAMAKDIRVIVVKLADRLHNMRTLDALSPEKQRRIARETKDIFAPLANRLGIWRFKWELEDLSFKYLEPDSYRKIQSLVVEKRGDRESRLETVKDMLRFRLRDEGIEHFELQGRPKHLYGIYYKMTSQDKAFEEIYDIAALRIIVESKGECYRALSVVHDVFKPIP... | Function: In eubacteria ppGpp (guanosine 3'-diphosphate 5'-diphosphate) is a mediator of the stringent response that coordinates a variety of cellular activities in response to changes in nutritional abundance. This enzyme catalyzes the degradation of ppGpp into GDP. It may also be capable of catalyzing the synthesis o... |
Q9KNM2 | MYLFDSLKDVAQEYLTEPQIEALRQSYVVARDAHEGQTRSSGEPYIIHPVAVARILAEMRLDLETLQAALLHDVIEDCDVTKEDLDAHFGSSVAELVDGVSKLDKLKFRDRKEAQAENFRKMVLAMVQDIRVILIKLADRTPNMRTLGALRPDKKRRIARETLEIYAPLAHRLGIHNIKTELEELGFEALYPNRYRVLKEVVKAARGNRKEMIQRIHSEIEGRLQEVGLPARVVGREKNLFSIYNKMKTKEQRFHTIMDIYAFRIVVDTADTCYRVLGQVHSLYKPRPARMKDYIAVPKANGYQSLHTSMVGPHGVPVEV... | Function: In eubacteria ppGpp (guanosine 3'-diphosphate 5'-diphosphate) is a mediator of the stringent response that coordinates a variety of cellular activities in response to changes in nutritional abundance.
Catalytic Activity: guanosine 3',5'-bis(diphosphate) + H2O = diphosphate + GDP + H(+)
Sequence Mass (Da): 794... |
P37817 | MKFYTIKLPKFLGGIVRAMLGSFRKD | Function: Coordinates cortex and coat assembly during sporulation . Associates with the spore coat protein SpoIVA and with the outer forespore membrane, thereby serving as a membrane anchor that tethers SpoIVA and the entire spore coat to the forespore surface . May also serve as a competitive inhibitor of FtsH activit... |
Q710A0 | MGKTPEDFERHTMRSLIFVLALSVFTCSGFPVYDYELPVTEEALNASIARINSQTWGPNLYGVVRSHVRHVDMWNSNDYRLELQLSIRETECTKASGRDPFTCGFKVGPFVPTAVCKSVVEVSSEQIVNVIVRCHQSTFSSESMSSEEMTYMLMTDPRKRGSSRSEAFSSRGRGHSNGDWRKPDYTSPGKVE | Function: Could coordinate an aspect of bone turnover.
PTM: Multiply phosphorylated at serine residues.
Sequence Mass (Da): 21648
Sequence Length: 192
Subcellular Location: Secreted
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Q13103 | MISRMEKMTMMMKILIMFALGMNYWSCSGFPVYDYDPSSLRDALSASVVKVNSQSLSPYLFRAFRSSLKRVEVLDENNLVMNLEFSIRETTCRKDSGEDPATCAFQRDYYVSTAVCRSTVKVSAQQVQGVHARCSWSSSTSESYSSEEMIFGDMLGSHKWRNNYLFGLISDESISEQFYDRSLGIMRRVLPPGNRRYPNHRHRARINTDFE | Function: Could coordinate an aspect of bone turnover.
PTM: Phosphorylation sites are present in the extracellular medium.
Sequence Mass (Da): 24338
Sequence Length: 211
Subcellular Location: Secreted
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Q711S8 | MEKRAMRMLAMFVLGTSFWSCAGFPVYDYDPSSLREAVGASVAKVNSQSLSPYLFRAFRSSLKRVNVLGEDSLSMDIEFGIRETTCKRDSGEDPATCDFQRGYFTPSAICRSTVQISAEKVQDVWVRCRWSSSSESNSSEEMIFGDILGSSTSRNNYLRGLIPDVSRTEPLYERSLETMRRFPPPGNRSFPNQWPRARTNTGFE | Function: Could coordinate an aspect of bone turnover.
PTM: Multiply phosphorylated at serine residues.
Sequence Mass (Da): 23097
Sequence Length: 204
Subcellular Location: Secreted
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Q710A1 | MKWCGVLMVALLQSLCCSGLPLYQSELASTADKALVVTMTQVNNLYAGLRLYRVSRGSIKRVVPLGLNTYDLIMNFGIKETDCLKSSGEDPQRCAFRVGFFVPAASCTARVRVTAEFTQVVSLNCGQDSSSSESSSEENFTRKRQQLNVQPFGNRGPVLPVPGFSEATRFPSHSFSRQEVEPQPIPRGDSFGNHLE | Function: Could coordinate an aspect of bone turnover.
PTM: Multiply phosphorylated at serine residues.
Sequence Mass (Da): 21560
Sequence Length: 196
Subcellular Location: Secreted
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Q69XJ0 | MKFGKSLSSQIVETLPEWRDKFLSYKDLKKRLKLIGGGGGGEERQAKRARVAADGGEEEAAAAAMTPEEAGFMRLLEAELDKFNSFFVEKEEEYIIRQKELQDRVARAAGRESKEELMRVRKEIVDFHGEMVLLENYSALNYTGLVKILKKYDKRTGALIRLPFIQKVLQQPFFTTDLLYKLVKQCEAMLDQLLPSNELSVSSEDGRGDSTNEDKPSNPSSSLVNGGTIPELDEIEYMESMYMKGTVAALRSLKEIRSGSSTVSAFSLPPLQGDSSPEEQQELWNKIPVIEQAAK | Function: Involved in plant adaptation to phosphate (Pi) starvation . Inhibits PHR2 DNA-binding activity via a Pi-dependent protein interaction . Suppresses the regulation on expression of PT2 by PHR2 and accumulation of shoot Pi . Optimizes growth under phosphate-limited conditions through a negative feedback loop of ... |
A2X254 | MKFGKSLSSQIVEMQPEWRDNFLSYKDLKKRLNLISGGAAGERASKRRRVGGATAVTVTAAAAGGMTLEQAGFVGLLDAELDKFNFFFLEKEEEYVIKQKELRERKMASAEEVMRVRKEIVDLHGEMVLLENYSALNYTGLVKILKKYDKRTGSMIRLPFVQKVLQQPFFTTDLLYKLVKECEEMLDQLMPTNEHSVASEDGKDDSEGEEKGSKPSSSSSANGGAVPGEAEDERSTDMKSTVTAALRALREIRSGSSTVSVFSLPPLHGSNGQDEPGR | Function: Inhibits PHR2 DNA-binding activity via a phosphate (Pi)-dependent protein interaction (By similarity). Together with SPX1, plays a negative role in the regulation of leaf inclination by preventing RLI1 transcription factor activity in Pi depleted conditions (By similarity).
Sequence Mass (Da): 30755
Sequence ... |
Q6Z784 | MKFGKSLSSQIVEMQPEWRDNFLSYKDLKKRLNLISGGAAGERASKRRRVGGATAVTVTAAAAGGMTLEQAGFVGLLDAELDKFNFFFLEKEEEYVIKQKELRERKMASAEEVMRVRKEIVDLHGEMVLLENYSALNYTGLVKILKKYDKRTGSMIRLPFVQKVLQQPFFTTDLLYKLVKECEEMLDQLMPTNEHSVASEDGKDDSEGEEKGSKPSSSSSANGGAVPGEAEAEDERSTDMKSTVTAALRALREIRSGSSTVSVFSLPPLHGSNGQDEPGR | Function: Inhibits PHR2 DNA-binding activity via a phosphate (Pi)-dependent protein interaction . Together with SPX1, plays a negative role in the regulation of leaf inclination by preventing RLI1 transcription factor activity in Pi depleted conditions .
Sequence Mass (Da): 30955
Sequence Length: 280
Domain: The SPX do... |
Q5F3N0 | MAVPGSSRRQPSNRGLVSHCTHHHIVVFLLTFFSYSLLHASRKTFSNVKVSISSQWTPSCLNSTTFELRPNELWNSNHLFPNAEEATLFLGTLDTIFLFSYAVGLFVSGIVGDRLNLRWVLSFGMCSSALVVFFFGTLTEWLHFYNKWFYCCLWVVNGLLQSTGWPCVVAVMGNWFGKAGRGFVFGLWSACASVGNILGAFLASCVLKYGYEYAFLVTASVQFAGGVIVFCGLLTSPKEVGLPELGADEEGSVEEDANRPLMGDDDADDDEGNYSIQAADTDSQPKAIGFFQACCLPGVVLYSLAYACLKLVNYSFFFWL... | Function: Unlike the other SLC37 members, seems to lack glucose-6-phosphate antiporter activity.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 54911
Sequence Length: 501
Subcellular Location: Endoplasmic reticulum membrane
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Q8NCC5 | MAWPNVFQRGSLLSQFSHHHVVVFLLTFFSYSLLHASRKTFSNVKVSISEQWTPSAFNTSVELPVEIWSSNHLFPSAEKATLFLGTLDTIFLFSYAVGLFISGIVGDRLNLRWVLSFGMCSSALVVFVFGALTEWLRFYNKWLYCCLWIVNGLLQSTGWPCVVAVMGNWFGKAGRGVVFGLWSACASVGNILGACLASSVLQYGYEYAFLVTASVQFAGGIVIFFGLLVSPEEIGLSGIEAEENFEEDSHRPLINGGENEDEYEPNYSIQDDSSVAQVKAISFYQACCLPGVIPYSLAYACLKLVNYSFFFWLPFYLSNN... | Function: Unlike the other SLC37 members, lacks glucose-6-phosphate antiporter activity . In osteoclasts, forms a transporter complex with ATRAID for nitrogen-containing-bisphophonates (N-BPs) required for releasing N-BP molecules that have trafficked to lysosomes through fluid-phase endocytosis into the cytosol .
PTM:... |
P48607 | MMTPMWISLFKVLLLLFAFFATYEAKEYERIIKELFTITNDEGVVLFNTSADSAPFMPIPTQHDDPTQKQKQNQNQSPIPETNRHYHQYHSLIQPDQYFKVQRSPNGKLNLVFNDTFVSLQRTDTEVQSEQPIPPRHPSDTFVFPDSPIAKYRPPQSPARPLRNDTKEHNPCAKDESQHLRNFCTNVDDYPDLSGLTHKLKNNFAKFFSNDLQPTDVSSRVGGSDERFLCRSIRKLVYPKKGLRADDTWQLIVNNDEYKQAIQIEECEGADQPCDFAANFPQSYNPICKQHYTQQTLASIKSDGELDVVQNSFKIPSCCK... | Function: The activated form, spaetzle C-106, acts as a ligand for the Toll receptor . Binding to Toll activates the Toll signaling pathway and induces expression of the antifungal peptide drosomycin . Component of the extracellular signaling pathway that establishes dorsal-ventral polarity in the embryo .
PTM: During ... |
P32138 | MDTPRPQLLDFQFHQNNDSFTLHFQQRLILTHSKDNPCLWIGSGIADIDMFRGNFSIKDKLQEKIALTDAIVSQSPDGWLIHFSRGSDISATLNISADDQGRLLLELQNDNLNHNRIWLRLAAQPEDHIYGCGEQFSYFDLRGKPFPLWTSEQGVGRNKQTYVTWQADCKENAGGDYYWTFFPQPTFVSTQKYYCHVDNSCYMNFDFSAPEYHELALWEDKATLRFECADTYISLLEKLTALLGRQPELPDWIYDGVTLGIQGGTEVCQKKLDTMRNAGVKVNGIWAQDWSGIRMTSFGKRVMWNWKWNSENYPQLDSRI... | Function: Catalyzes the hydrolysis of sulfoquinovosyl diacylglycerides (SQDG) to sulfoquinovose (SQ), which is then degraded by E.coli through the SQ Embden-Meyerhof-Parnas (SQ-EMP) sulfoglycolysis pathway as a source of carbon and sulfur. Therefore, is likely involved in the utilization of the sulfoquinovose headgroup... |
O48917 | MAHLLSASCPSVISLSSSSSKNSVKPFVSGQTFFNAQLLSRSSLKGLLFQEKKPRKSCVFRATAVPITQQAPPETSTNNSSSKPKRVMVIGGDGYCGWATALHLSKKNYEVCIVDNLVRRLFDHQLGLESLTPIASIHDRISRWKALTGKSIELYVGDICDFEFLAESFKSFEPDSVVHFGEQRSAPYSMIDRSRAVYTQHNNVIGTLNVLFAIKEFGEECHLVKLGTMGEYGTPNIDIEEGYITITHNGRTDTLPYPKQASSFYHLSKVHDSHNIAFTCKAWGIRATDLNQGVVYGVKTDETEMHEELRNRLDYDAVFG... | Function: Involved in the biosynthesis of sulfolipids found in thylakoid membranes. Converts UDP-glucose and sulfite to the sulfolipid head group precursor UDP-sulfoquinovose.
Catalytic Activity: H(+) + sulfite + UDP-alpha-D-glucose = H2O + UDP-alpha-D-6-sulfoquinovose
Sequence Mass (Da): 53114
Sequence Length: 477
Sub... |
Q84KI6 | MAHLLSTSCSMKVSPSEKLSSKCWNIGSTKYPMSFTQQTSKSAFKSLVHQRNNTQKLTVVRATTVPLNQETKAESGTSSFENNGNTSGRKRVMVIGGDGYCGWATALHLSKKNYDVCIVDNLVRRLFDHQLGLDSLTPIASIQNRIRRWQGLTGKTIDLHVGDICDFEFLAETFKSFEPDTVVHFGEQRSAPYSMIDRSRAVYTQQNNVIGTINVLFAIKEFSEECHLVKLGTMGEYGTPNIDIEEGFITITHNGRTDTLPYPKQASSFYHLSKVHDSHNIAFTCKAWGIRATDLNQGVVYGVMTEETAMHEELCNRFDY... | Function: Involved in the biosynthesis of sulfolipids found in thylakoid membranes. Converts UDP-glucose and sulfite to the sulfolipid head group precursor UDP-sulfoquinovose. The sulfite is delivered to the reaction center by the FMN-binding domain of FdGOGAT.
PTM: The N-terminus is blocked.
Catalytic Activity: H(+) +... |
Q8S4F6 | MTTLSSINLSIPPHLLPSTTNTCSSSSATSCSPPRSSSFVLHSPLSFGHRRLPISKKSKLRFCGVITKEAVSGSNDMTITQVREDDESEIDAPLLDPESLSKPRRIALFVEPSPFAYVSGYKNRFQNFIRYLREMGDEVIVVTTHEGVPEEFYGARVIGSRSFPCPYYQKVPLSLALSPRIISEIARFKPDIIHASSPGVMVFGALAIAKMLSVPIVMSYHTHVPVYIPRYTFSWLVKPMWSIIRFLHRAADLTLVPSAAIGKDLIAAGATAANQLRLWNKGVDSESFNPRFRSQEMRIRLSNGEPEKPLVIHVGRIGVE... | Function: Catalyzes the transfer of the sulfoquinovose moiety from UDP-sulfoquinovose to diacylglycerol during sulfolipid biosynthesis . Sulfolipid contributes to maintaining a negatively charged lipid-water interface, a requirement for proper function of photosynthetic membranes . Sulfolipid may also function as a sub... |
P0DOV5 | MNRHTDTHYPSLADKVVLISGGASGIGRAFVEAFVAQGSRVAFLDLDAEAGQGLAHALGANSLFLPCDVRDIERLKACVAEVERTWGAVDVLINNAARDDRHALADVSVEYWDERMQTNLRHAFFAAQAVAPGMARRGSGAIINMGSISWMRGRPGMVCYTTAKAALNGMTRTLARELGGQGIRINSLVPGAIRTERQDAMWAADPAGLEAASQAFIDQQMLKFRLDASDCARLALFLASDDSRGCTGQNFVVDAGLSIQ | Function: Catalyzes the oxidation of sulfoquinovose to 6-deoxy-6-sulfo-D-glucono-1,5-lactone, with a strong preference for NAD(+) as the electron acceptor. Is involved in a degradation pathway of sulfoquinovose (SQ) that allows P.putida SQ1 to use SQ as the sole carbon and energy source for growth.
Catalytic Activity: ... |
O48651 | MNSSSSTTTTDTLHSFMEASALLIDQYFLGWIFAFLFGFLLLLNFKRKREKNNSTEFGTDDSNGYYTPENIAGSTDVIIVGAGVAGSALAYTLANDGRRVHVIERDLTEQDRIVGELLQPGGYLKLIELGLEDCVNEIDAQRVFGYALYMDGKNTRLSYPLEKFHSDVAGRSFHNGRFVQRMREKAASLPNVRMEQGTVTSLVEKKGSVKGVQYKTKDGQELSAFAPLTIVCDGCFSNLRRSLCNPKVEVPSCFVGLILENIDLPHINHGHVILADPSPILFYKISSTEIRCLVDVPGQKVPCISNGELANYLKTVVAPQ... | Function: Component of the triterpene saponins (e.g. ginsenosides or panaxosides) and phytosterols biosynthetic pathways . Catalyzes the first oxygenation step in sterol biosynthesis and is suggested to be one of the rate-limiting enzymes in this pathway (By similarity).
Catalytic Activity: O2 + reduced [NADPH--hemopro... |
P33247 | MAEQLVEAPAYARTLDRAVEYLLSCQKDEGYWWGPLLSNVTMEAEYVLLCHILDRVDRDRMEKIRRYLLHEQREDGTWALYPGGPPDLDTTIEAYVALKYIGMSRDEEPMQKALRFIQSQGGIESSRVFTRMWLALVGEYPWEKVPMVPPEIMFLGKRMPLNIYEFGSWARATVVALSIVMSRQPVFPLPERARVPELYETDVPPRRRGAKGGGGWIFDALDRALHGYQKLSVHPFRRAAEIRALDWLLERQAGDGSWGGIQPPWFYALIALKILDMTQHPAFIKGWEGLELYGVELDYGGWMFQASISPVWDTGLAVLA... | Function: Catalyzes the cyclization of squalene into hopene.
Catalytic Activity: squalene = hop-22(29)-ene
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 71570
Sequence Length: 631
Pathway: Secondary metabolite biosynthesis; hopanoid biosynthesis.
Subcellular Location: Cell membrane
EC: 4.2.1.129
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Q796C3 | MGTLQEKVRRFQKKTITELRDRQNADGSWTFCFEGPIMTNSFFILLLTSLDEGENEKELISSLAAGIHAKQQPDGTFINYPDETRGNLTATVQGYVGMLASGCFHRTEPHMKKAEQFIISHGGLRHVHFMTKWMLAANGLYPWPALYLPLSLMALPPTLPIHFYQFSSYARIHFAPMAVTLNQRFVLINRNISSLHHLDPHMTKNPFTWLRSDAFEERDLTSILLHWKRVFHAPFAFQQLGLQTAKTYMLDRIEKDGTLYSYASATIYMVYSLLSLGVSRYSPIIRRAITGIKSLVTKCNGIPYLENSTSTVWDTALISY... | Function: Catalyzes the cyclization of tetraprenyl beta-curcumene into sporulenol.
Catalytic Activity: sporulenol = (R)-tetraprenyl-beta-curcumene + H2O
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 71224
Sequence Length: 632
Pathway: Secondary metabolite biosynthesis; hopanoid biosynthesis.
Subcel... |
P54924 | MDSVNATAREAKESKISESEILESSIASATQGVLGFQQSDGHWVFELEADCTIPAEYVLLRHYLAEPVDTVLEAKIGNYLRRVQGAHGGWPLVHDGEFDMSASVKAYFALKMIGDSIDAPHMVRAREAIHARGGAIHSNVFTRFMLAMFGIVTWRAVPVLPIEIMLLPFWSPFHINKISYWARTTMVPLMVIAALKPRAKNPKGVGIDELFLQDPRSIGMTAKAPHQSMAWFLLFRSLDAILRVIEPLFPKSLRKRAIDTALAFSEERLNGEDGMGAIYPPMANLVMMYDALGKDENYPPRAVTRRGIDKLLVIGDDEAY... | Function: Catalyzes the cyclization of squalene into hopene.
Catalytic Activity: squalene = hop-22(29)-ene
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 73702
Sequence Length: 660
Pathway: Secondary metabolite biosynthesis; hopanoid biosynthesis.
Subcellular Location: Cell membrane
EC: 4.2.1.129
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P55348 | MNKHSGNRTAIDPAALEMSIASATEALLAYRHADGHWAFELEADSTIPSEYILLRHYLAEPIDVVLEAKIGNYLRRTQGAHGGWPLVHDGPFDMSASVKSYFALKMIGDSVDAAHMVKAREAIRARGGAANSNVLTRFLLALYGVVSWRAVPVLPIEIVLLPIWSPFHLYKISYWARTTIVPLMVLAVLKPRAKNPKGVGIEELFLQDTKSVGMNPKAPHQSWGWFLLFRGIDGILRVIEPHLPKKLRERAIASALAFTEERLNGEDGMGAIYPSMANIVMMYDALGKDDHFPPRAIARRAIDKLLVIGEEEAYCQPCLS... | Function: Catalyzes the cyclization of squalene into hopene. Probably part of an operon y4aABCD involved in the synthesis of an isoprenoid compound.
Catalytic Activity: squalene = hop-22(29)-ene
Sequence Mass (Da): 72130
Sequence Length: 647
Pathway: Secondary metabolite biosynthesis; hopanoid biosynthesis.
EC: 4.2.1.1... |
B7FXW1 | MLVDRVENNEKQQQQMASSSDAMSDSSLSDDEIIEHVVHGKEPKSTYELSWVSNAIAWSGALVWPLMLTVPLLLSSMYSPISYRQVFPESWYVYDTLSNCAPKPLGLVLGILAVAVGQVFVWIFFYLFKFGYLGTDPRSIQSKGAREYIFREGLLTHIGQPEGFVLLIGYLAITWMLKLMPQSYYSFEGTIQYKELFMCLVLQDGIQYTMHVLEHIVSPAFYQMSHKPHHRFTNPRLFDAFNGSLMDTFCMIIIPLFVTANLVRHCNVWTYMAFGSSYACWLTLIHSEYVFPWDGIFRKLGLGTPADHHVHHKFFKFNYG... | Function: Catalyzes the stereospecific epoxidation of squalene at the terminal double bond to form (S)-2,3-epoxysqualene, the first oxygenation step in sterol biosynthesis.
Catalytic Activity: 2 Fe(II)-[cytochrome b5] + 2 H(+) + O2 + squalene = (S)-2,3-epoxysqualene + 2 Fe(III)-[cytochrome b5] + H2O
Location Topology: ... |
Q54DK1 | MFKSIMYALAVAPAVTSSSDKLPNGVVSASQLGSEKEKRKLKNVTKIVIVGGGAGGLSVASQLEHKFKNKGDIVIVEPSEKHYYQPLWTLVGGGIFSRKDSEKDEKDFIPKGATWVKDSVTVFKPEENIVLTKDGKEIDYDYLVVSTGLELYWDRVKGLKENLGKNGVTSNYSYDSCEKTFEFIKSLKPGNVAIFTVPTTGVKCGGAPQKILWLCDDYLRKHGIRDKVRLDFNSAGASMFPVKKYSEVLDKMAKERGVNQNFAHNLVEIKGDSKEAVFETPQGNKTVKYDMIHVVPPMGPHSVIKNSPLADPATGFVNVD... | Cofactor: Binds 1 FAD per subunit.
Function: Catalyzes the oxidation of hydrogen sulfide, with the help of a quinone.
Catalytic Activity: 2 H(+) + hydrogen sulfide + sulfite + ubiquinone-10 = thiosulfate + ubiquinol-10
Sequence Mass (Da): 50145
Sequence Length: 452
Subcellular Location: Mitochondrion
EC: 1.8.5.8
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A0A0A0LLY1 | MASSSVEFRCFVGGLAWATDSNSLEKAFSVYGEIVEAKIVSDRETGRSRGFGFVTFLEEEAMRSAIEAMNGHILDGRNITVNEAQQRGGGGGGGYNRGGGYGGRRDGGGFSRGGGGGYGGGGGGGYGGGRDRGYGGGGGYGGGRDSRGSGGGGSEGGWRN | Function: Possibly has a role in RNA transcription or processing during stress (By similarity). Binds sequence non-specifically to RNAs and DNAs (By similarity). Mediates cell-to-cell trafficking of RNA interference (RNAi) signals (small RNAs (sRNA), e.g. small interfering RNA (siRNA) and microRNA (miRNA)) which regula... |
G5EC32 | MMHHPHPFGSNLANSSEPQQPSGQYLNPAADAYNFDTFEDSDKFSPKGNVAALRNVIHGQLDMKTPTGNSSRYQKPAPPPVDSTPSWAKNVKVYEPNGYVDPHLNKHNMGRVLDGPVNPNKYFQGVPPASYSQVKHNESKPPVPPSTKPPHSAAQALQAQVLQSSKAPSQPQQSQKTSYRIPYDVALDPRHHLGEFDIDDSASIISSCISTFGESSEIAGFSAAAEQRHLYEQYRKKLMEEKNELKEGSETPCVSLSEKVMTSSTENLKNGNNQQNQQPEPQPPSSSIFNSELTPFGHVAPVAKQFEPTNFPPFSPEKES... | Function: Required for organization of sarcomeres in body wall muscles and for maintaining normal mitochondrial position in myocytes.
Sequence Mass (Da): 112832
Sequence Length: 1005
Domain: SH3 domains 1 and 2 are required for its localization to the cell membrane of dense bodies.
Subcellular Location: Cell junction
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Q4UKH4 | MFKTLTQNLTKIFDKLVSSGILTEAQIDAAMRDIRVALLESDVALPVIKDFIAEVKQKALGQEVIKSVSPGQMIIKIIHEEMINLLASSESETKLNLNSKPPVNFLMVGLQGSGKTTASSKLALRLKNQNKKVLLVSLDTYRPAAQEQLAILANSVQINSLPIVQGEKPLDIVKRAIAEAKISAYGVVIYDTAGRTQIDKEMMEEALAIKKIVEPTETLLVIDSMTGQDAVVTANSFNEKLEISGLILSRIDGDSKGGAALSVKYITKKPIKFLSSGEKLTDLEEFDAERLASRILDMGDIISFVEKAASIVDREEAEKT... | Function: Involved in targeting and insertion of nascent membrane proteins into the cytoplasmic membrane. Binds to the hydrophobic signal sequence of the ribosome-nascent chain (RNC) as it emerges from the ribosomes. The SRP-RNC complex is then targeted to the cytoplasmic membrane where it interacts with the SRP recept... |
P21565 | MVFADLGRRLNSALGDFSKATSVNEELVDTLLKNICTALLETDVNVRLVQELRSNIKKKINVSTLPQGINGKRIVQKAVFDELCSLVDPKVDAFTPKKGRPSVIMMVGLQGSGKTTTCSKLALHYQRRGLKSCLVAADTFRAGAFDQLKQNAIKARVPYFGSYTETDPVVIAKEGVDKFKNDRFDVIIVDTSGRHQQEQELFAEMVEISDAIRPDQTIMILDASIGQAAESQSKAFKETADFGAVIITKLDGHAKGGGALSAVAATKTPIVFIGTGEHINDLERFSPRSFISKLLGLGDLEGLMEHVQSLDFDKKNMVKN... | Function: Signal-recognition-particle (SRP) assembly has a crucial role in targeting secretory proteins to the rough endoplasmic reticulum (ER) membrane. SRP is required for the cotranslational protein translocation for ER import and preferentially recognizes strongly hydrophobic signal sequences. It is involved in tar... |
Q54431 | MAFESLTERLQGVFKNLRGKRKLSEKDVQEVTKEIRLALLEADVALPVVKEFIKRVRKRAVGHEVIDTLDPSQQIIKIVNEELTAVLGSETAEIEKSSKIPTIIMMVGLQGAGKTTFAGKLANKLVKEENARPLMIAADIYRPAAIDQLKTLGQQINVPVFDMGTEHSAVEIVSQGLAQAKENRNDYVLIDTAGRLQIDEKLMTELRDIKALANPNEILLVVDSMIGQEAANVAREFNQQLEVTGVILTKIDGDTRGGAALSVRQITGKPIKFTGTGEKITDIETFHPDRMSSRILGMGDLLTLIEKASQDYDEQKSAEL... | Function: Involved in targeting and insertion of nascent membrane proteins into the cytoplasmic membrane. Binds to the hydrophobic signal sequence of the ribosome-nascent chain (RNC) as it emerges from the ribosomes. The SRP-RNC complex is then targeted to the cytoplasmic membrane where it interacts with the SRP recept... |
O07853 | MLDGLRDAVRKFLGSSDYEKAVNEFIKELQIILIKADVNVRLVKDLTDRIKKRITEEKPPSAIEKREWFISIVYDELSRLFGGDKEPEVMPKKLPYIIMLVGVQGSGKTTTSGKLALFYKKKGYKVGLVAADIYRPAAYEQLIQIGQQINIPVYGEPGNKNPIEIATNGLEKFLKEKMNIVIIDTAGRHGYGEEASLLEEMKSMYDKIHPDEVILVIDASIGQKAYDLASRFHQASPIGSLIVSKMDGTAKGGGALSAVIATGAQIKFIGTGEKLDELEVFNPRRFVSRLLGLGDIESIIEKIKSVEDYENLEKRMEDVI... | Function: Involved in targeting and insertion of nascent membrane proteins into the cytoplasmic membrane. Binds to the hydrophobic signal sequence of the ribosome-nascent chain (RNC) as it emerges from the ribosomes. The SRP-RNC complex is then targeted to the cytoplasmic membrane where it interacts with the SRP recept... |
Q55311 | MFDALAERLEQAWTKLRGQDKISESNVQEALKEVRRALLEADVNLGVVKEFIAQVQEKAVGTQVISGIRPDQQFIKVVYDELVQVMGETHVPLAQAAKAPTVILMAGLQGAGKTTATAKLALHLRKEGRSTLLVATDVYRPAAIDQLITLGKQIDVPVFELGSDANPVEIARQGVEKARQEGIDTVIVDTAGRLQIDTEMMEELAQVKEAIAPHEVLLVVDSMIGQEAASLTRSFHERIGITGAILTKLDGDSRGGAALSIRRVSGQPIKFVGLGEKVEALQPFHPERMASRILGMGDVLTLVEKAQEEIDLADVEKMQE... | Function: Involved in targeting and insertion of nascent membrane proteins into the cytoplasmic membrane. Binds to the hydrophobic signal sequence of the ribosome-nascent chain (RNC) as it emerges from the ribosomes. The SRP-RNC complex is then targeted to the cytoplasmic membrane where it interacts with the SRP recept... |
P74214 | MFDALADRLEDAWKKLRGQDKISESNIKEALQEVRRALLAADVNLQVVKGFIKDVEQKALGADVISGVNPGQQFIKIVYDELVNLMGESNVPLAQAEQAPTVILMAGLQGTGKTTATAKLALYLRKQKRSALMVATDVYRPAAIDQLKTLGQQIDVPVFDLGSDANPVEIARQGVEKAKELGVDTVLIDTAGRLQIDPQMMAELAEIKQVVKPDDTLLVVDAMTGQEAANLTHTFHEQIGITGAILTKLDGDTRGGAALSVRQISGQPIKFVGVGEKVEALQPFYPDRLASRILNMGDVLTLVEKAQEAIDVGDVEKLQN... | Function: Involved in targeting and insertion of nascent membrane proteins into the cytoplasmic membrane. Binds to the hydrophobic signal sequence of the ribosome-nascent chain (RNC) as it emerges from the ribosomes. The SRP-RNC complex is then targeted to the cytoplasmic membrane where it interacts with the SRP recept... |
Q9HKT0 | MVLESFSASLRETIRKITGSSYIDKETVKEISKDLQRILLKADVNVKTVLQVTKEMERRALEEKPPAGMAHQDYMVRIIYEELLKILGEPSNVKLKPQTIMLVGLYGNGKTTTAGKLARFFAKKGLNSGLIAADVHRYAAYDQLKQIASEVNAKFYGDQSEKDPVRLIKHGLEQLKDVAVKIIDTSGRDSMDAELFDEIRRIKEAVAPDEVLMIIDATMGQQAGPEAKAFNDAIGVTGIIITKMDGTAKGGGALSAVAEIHVPIYFIGTGEHMDDLEVFDPKKFLSRLLGLGDLESLFETVQEADITEEEAQESFEKLMT... | Function: Involved in targeting and insertion of nascent membrane proteins into the cytoplasmic membrane. Binds to the hydrophobic signal sequence of the ribosome-nascent chain (RNC) as it emerges from the ribosomes. The SRP-RNC complex is then targeted to the cytoplasmic membrane where it interacts with the SRP recept... |
O07347 | MFQQLSARLQEAIGRLRGRGRITEEDLKATLREIRRALMDADVNLEVARDFVERVREEALGKQVLESLTPAEVILATVYEALKEALGGEARLPVLKDRNLWFLVGLQGSGKTTTAAKLALYYKGKGRRPLLVAADTQRPAAREQLRLLGEKVGVPVLEVMDGESPESIRRRVEEKARLEARDLILVDTAGRLQIDEPLMGELARLKEVLGPDEVLLVLDAMTGQEALSVARAFDEKVGVTGLVLTKLDGDARGGAALSARHVTGKPIYFAGVSEKPEGLEPFYPERLAGRILGMGDVASLAEKVRAAGLEAEAPKSAKEL... | Function: Involved in targeting and insertion of nascent membrane proteins into the cytoplasmic membrane. Binds to the hydrophobic signal sequence of the ribosome-nascent chain (RNC) as it emerges from the ribosomes. The SRP-RNC complex is then targeted to the cytoplasmic membrane where it interacts with the SRP recept... |
Q10213 | METKSSYLKFLNEEQRISVQSPHKYTQILAGPGSGKTRVLTARVAYLLQKNHIAAEDLIIATFTNKAANEIKLRIEAILGNSEASKLISGTFHSIAYKYLVKYGKHIGLSSNWLIADRNDTQAIMKRLLDSLKKAKNPIASGIRGQELTPQNALNRITKLKSNGLLVKPGMDQLSLINGLEEPPKELQSHQSVELYRLYQTSLWKNNLADFDDLLLNFILLLQKQPDCVRNIKHILIDEFQDTSKIQYFLVKLLALQNSDITIVGDPDQSIYGFRSAEIRNLNQMSEDFEGTQVLHLERNYRSAKPILELALSIISQDKS... | Function: ATP-dependent DNA helicase involved in DNA repair at least for UV-induced lesions. Also aids the recombinational repair of camptothecin-induced collapsed replication forks.
Catalytic Activity: Couples ATP hydrolysis with the unwinding of duplex DNA by translocating in the 3'-5' direction.
Sequence Mass (Da): ... |
B0G168 | MIAKVFKSITPESYILLVNAGLISAYGVRIIFQSVKNDEGKVDEKAHIGIGHFFKKRGAQLVDGKNLTDILKEKKKKKKKKKKINISNKLIIFKISRQLYSKLKLK | Function: Involved in starvation response and aggregation stage of the life cycle. May be involved in fruiting body morphogenesis and spore formation.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 12100
Sequence Length: 106
Subcellular Location: Cell membrane
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P36394 | MEGHVKRPMNAFMVWSRGERRKLAQQNPSMQNSEISKHLGYQWKSLTEAEKRPFFQEAQRLKTLHREKYPNYKYQPHRRVKVPQRSYTLQREVASTKLYNLLQWDNNLHTIIYGQDWARAAHQSSKNQKSIYLQPVDIPTGYPLQQKQQHQQQQHVHLQQQQQQQHQFH | Function: Transcriptional regulator that controls a genetic switch in male development . It is necessary and sufficient for initiating male sex determination by directing the development of supporting cell precursors (pre-Sertoli cells) as Sertoli rather than granulosa cells . Involved in different aspects of gene regu... |
P36395 | MCSFLDVEVKDRFVEGDFGMSEMVKSNLANCSSRVKRPMNAFMVWSQTQRRKVALQNPKMHNSEISKQLGVTWKLLSDSEKRPFIDEAKRLRDKHKQVSDYKYQPRRKTKSFLKNVYNHKDHLTKATDQLIKTQHLKEDSTTIYENTMKCPEISSFYCAQESTYLDNWMNLPPEQENTEFWQGLFTNETETCRSLPHGQMDCNECRSI | Function: Transcriptional regulator that controls a genetic switch in male development. It is necessary and sufficient for initiating male sex determination by directing the development of supporting cell precursors (pre-Sertoli cells) as Sertoli rather than granulosa cells. Involved in different aspects of gene regula... |
P32343 | MYVTFNEALDSSFGNLESPNHDFKVGDPNMVPTPPMDSDSAAISLAFLISLSITFAILMLILVVIAAYVTFCGDDESEYDEENALGTRTSGTLHSLFGKKHSGILLDSSFASPGGFDDEIVLQERELEELPKMSAYEVELYIRAKEFQMMSPPMVKDFGTYLDSDDQQFIKDRGIQSYFLLPSINDNIDEYGNFLPSFIVQDKLDIQFSKFNKSSSTVMNYPLPHNRKDAVYFEVKIFRHIQKSNSIFSIGLTTVPYPYFRVPGMAKYSIAYESTGKLRINNPFTASTLLPKLEEGDTVGFGYRYKTGTIFITHNGKKLM... | Function: Components of the endosome-vacuole trafficking pathway that regulates nutrient transport. May be involved in processes which determine whether plasma membrane proteins are degraded or routed to the plasma membrane. Confers leflunomide resistance when overexpressed.
Location Topology: Single-pass type II membr... |
Q6IVY4 | MALVTLQVSSLDVGSNITPVQDDEKSRRKRMQRRQSFVMVKGAALLLQDEGEPIDTREPLSSSGPNEQQIHLQSMLRLLREEDTLTLAVRLEPVRSCLTRYLLVVSSTGKSNVEETLLLGVDFPHDGSLCCTIGTVLPIWSNTQVFLDGDGGFTVTSGMDIRTFKPISVQTMWSLLQMLHKACESALSNNVISSSLYSGLIYYQSNRSSPQVCLNAWTASPDIESARRDPATPEREETERIIKLKLRDILRESDLENITSKEVRSALEQHTLCALQDYKEFIDNEMIIILAQMDRPSEIFPYLYLGSEWNASNLEELQKN... | Function: Protein phosphatase which regulates actin filament dynamics. Dephosphorylates and activates the actin binding/depolymerizing factor cofilin, which subsequently binds to actin filaments and stimulates their disassembly. Required for completion of the gastrulation movement and for cytokinesis.
Catalytic Activit... |
Q55A00 | MEKIKKQNNIGSYSSDKDGEYKKFRFSKTSIRGFLLKEYEREVPIIVKIQSYRNKFLDFYFKMASILGEEVFFILALPISTWCVATQLGVELCVVLALTIGGGNILKNTFTLPRPPPNIVWTNTAHQKDHGLPSTHTASAFGLTFYFLIYTYFLFPTIGESFNISLLSMFFIVLFWSTSVMFSRLYNGHHTPMDVIAGLIVAITSILATTYQLRYFIEGMVLSETFLFGPMLYIAILSAILFFHPQANTGPTPAYPETGLVCGASLGSLISLWLHAQHPCPLMNQELLLLEANYDSIVSTIHSIPLLLHGSRILIGLVLV... | Function: Has enzymatic activity against both sphingosine 1 phosphate (S1P) and dihydro-S1P. Regulates intracellular and extracellular S1P levels (By similarity).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 45887
Sequence Length: 406
Subcellular Location: Endoplasmic reticulum membrane
EC: 3.1.3.... |
Q2FZL2 | MKGKFLKVSSLFVATLTTATLVSSPAANALSSKAMDNHPQQTQSSKQQTPKIQKGGNLKPLEQREHANVILPNNDRHQITDTTNGHYAPVTYIQVEAPTGTFIASGVVVGKDTLLTNKHVVDATHGDPHALKAFPSAINQDNYPNGGFTAEQITKYSGEGDLAIVKFSPNEQNKHIGEVVKPATMSNNAETQVNQNITVTGYPGDKPVATMWESKGKITYLKGEAMQYDLSTTGGNSGSPVFNEKNEVIGIHWGGVPNEFNGAVFINENVRNFLKQNIEDIHFANDDQPNNPDNPDNPNNPDNPNNPDEPNNPDNPNNPD... | Function: Preferentially cleaves peptide bonds on the carboxyl-terminal side of aspartate and glutamate. Along with other extracellular proteases it is involved in colonization and infection of human tissues. Required for proteolytic maturation of thiol protease SspB and inactivation of SspC, an inhibitor of SspB. It i... |
P30873 | MFPNGTASSPSSSPSPSPGSCGEGACSRGPGSGAADGMEEPGRNASQNGTLSEGQGSAILISFIYSVVCLVGLCGNSMVIYVILRYAKMKTATNIYILNLAIADELLMLSVPFLVTSTLLRHWPFGALLCRLVLSVDAVNMFTSIYCLTVLSVDRYVAVVHPIKAARYRRPTVAKVVNLGVWVLSLLVILPIVVFSRTAANSDGTVACNMLMPEPAQRWLVGFVLYTFLMGFLLPVGAICLCYVLIIAKMRMVALKAGWQQRKRSERKITLMVMMVVMVFVICWMPFYVVQLVNVFAEQDDATVSQLSVILGYANSCANP... | Function: Receptor for somatostatin with higher affinity for somatostatin-14 than -28. This receptor is coupled via pertussis toxin sensitive G proteins to inhibition of adenylyl cyclase. In addition it stimulates phosphotyrosine phosphatase and Na(+)/H(+) exchanger via pertussis toxin insensitive G proteins.
Location ... |
P30874 | MDMADEPLNGSHTWLSIPFDLNGSVVSTNTSNQTEPYYDLTSNAVLTFIYFVVCIIGLCGNTLVIYVILRYAKMKTITNIYILNLAIADELFMLGLPFLAMQVALVHWPFGKAICRVVMTVDGINQFTSIFCLTVMSIDRYLAVVHPIKSAKWRRPRTAKMITMAVWGVSLLVILPIMIYAGLRSNQWGRSSCTINWPGESGAWYTGFIIYTFILGFLVPLTIICLCYLFIIIKVKSSGIRVGSSKRKKSEKKVTRMVSIVVAVFIFCWLPFYIFNVSSVSMAISPTPALKGMFDFVVVLTYANSCANPILYAFLSDNFK... | Function: Receptor for somatostatin-14 and -28. This receptor is coupled via pertussis toxin sensitive G proteins to inhibition of adenylyl cyclase. In addition it stimulates phosphotyrosine phosphatase and PLC via pertussis toxin insensitive as well as sensitive G proteins. Inhibits calcium entry by suppressing voltag... |
P32745 | MDMLHPSSVSTTSEPENASSAWPPDATLGNVSAGPSPAGLAVSGVLIPLVYLVVCVVGLLGNSLVIYVVLRHTASPSVTNVYILNLALADELFMLGLPFLAAQNALSYWPFGSLMCRLVMAVDGINQFTSIFCLTVMSVDRYLAVVHPTRSARWRTAPVARTVSAAVWVASAVVVLPVVVFSGVPRGMSTCHMQWPEPAAAWRAGFIIYTAALGFFGPLLVICLCYLLIVVKVRSAGRRVWAPSCQRRRRSERRVTRMVVAVVALFVLCWMPFYVLNIVNVVCPLPEEPAFFGLYFLVVALPYANSCANPILYGFLSYRF... | Function: Receptor for somatostatin-14 and -28. This receptor is coupled via pertussis toxin sensitive G proteins to inhibition of adenylyl cyclase.
PTM: Phosphorylated. Phosphorylation increases upon somatostatin binding (By similarity).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 45847
Sequence... |
P31391 | MSAPSTLPPGGEEGLGTAWPSAANASSAPAEAEEAVAGPGDARAAGMVAIQCIYALVCLVGLVGNALVIFVILRYAKMKTATNIYLLNLAVADELFMLSVPFVASSAALRHWPFGSVLCRAVLSVDGLNMFTSVFCLTVLSVDRYVAVVHPLRAATYRRPSVAKLINLGVWLASLLVTLPIAIFADTRPARGGQAVACNLQWPHPAWSAVFVVYTFLLGFLLPVLAIGLCYLLIVGKMRAVALRAGWQQRRRSEKKITRLVLMVVVVFVLCWMPFYVVQLLNLFVTSLDATVNHVSLILSYANSCANPILYGFLSDNFRR... | Function: Receptor for somatostatin-14. The activity of this receptor is mediated by G proteins which inhibits adenylyl cyclase. It is functionally coupled not only to inhibition of adenylate cyclase, but also to activation of both arachidonate release and mitogen-activated protein (MAP) kinase cascade. Mediates antipr... |
Q881U6 | MDIRVDRKAFAGHTVLHDINLSLQTGEIVSLLGPSGCGKSTLLRIVAGLEQDFRGSVERIQGQVAFVFQEPRLMPWLTVEQNIGFSDDNGYDRKWVSQLIEEVGLSGFANALPKALSGGMAQRVAIARGLYSHPTILLLDEPFSAVDAFTRMKLQDLLLQLAERHAITLLLVTHDVDEALYLSDRVLVMGSRPGTITHELPVGLQTPRDRRDPLLARLKAEALTELHQAQVI | Function: Part of the ABC transporter complex SsuABC involved in aliphatic sulfonates import. Responsible for energy coupling to the transport system.
Catalytic Activity: ATP + H2O + aliphatic sulfonate-[sulfonate-binding protein]Side 1 = ADP + phosphate + aliphatic sulfonateSide 2 + [sulfonate-binding protein]Side 1.
... |
Q1M7A6 | MAPHPGKLKPATKAVHVRDLARRFATKTILDGVDLDIEEGEFVALLGRSGSGKSTFLRALAGLDHGVEGTGTLETPESLSVVFQDARLLPWRTVIQNVTLGLTGASGQEAGRKALAEVGLAGRETAWPNQLSGGEQQRVALARSLVREPALLLADEPFGALDALTRLKMHDLLRELCARHRPAVLLVTHDVDEAISLADRILVLDEGRLIEDLKIDLPTPRDHGDPRFAQFRIQLLSRLGVELPGRKAA | Function: Part of the ABC transporter complex SsuABC involved in aliphatic sulfonates import. Responsible for energy coupling to the transport system.
Catalytic Activity: ATP + H2O + aliphatic sulfonate-[sulfonate-binding protein]Side 1 = ADP + phosphate + aliphatic sulfonateSide 2 + [sulfonate-binding protein]Side 1.
... |
Q981Y8 | MASHLGGLRDAPVVRVESLVRSFGPRTILDGLSLDIEKGEFVALLGRSGSGKSTLLRALADLDDKVSGSGRLETPDKKSVVFQDARLLPWKRVLENVVLGLDLPDAAERGRAALEEVGLNGRETAWPVELSGGEQQRVALARSLVRDPDLLLADEPFGALDALTRLRMHDLLRQLCARHQPAVLLVTHDVDEAVTLADRVLVLDKGAIAADIAIDIPKPRDHGHRRFGEIRSELLRHLGVETRPVLPV | Function: Part of the ABC transporter complex SsuABC involved in aliphatic sulfonates import. Responsible for energy coupling to the transport system.
Catalytic Activity: ATP + H2O + aliphatic sulfonate-[sulfonate-binding protein]Side 1 = ADP + phosphate + aliphatic sulfonateSide 2 + [sulfonate-binding protein]Side 1.
... |
Q0S6U9 | MAQDARRLEPAAVQVRSLVRGFGDKTVLDRLDLDIPEGQFVALLGKSGSGKSTLLRALAGLDYDVEGRGGTLTVPEEVSVAFQDSRLLPWLKVLDNVTLGLGRTGTSRGAAALAEVGLAGREKAWPSELSGGEQQRVALARALVREPRLFLADEPFGALDALTRIKMHALLQELIRRHRPTVLLVTHDVDEAIALADRVLVLDRGQIVVDEIIDIPKPRALGDSKFHEFRTTLLGALGVEVAAQ | Function: Part of the ABC transporter complex SsuABC involved in aliphatic sulfonates import. Responsible for energy coupling to the transport system.
Catalytic Activity: ATP + H2O + aliphatic sulfonate-[sulfonate-binding protein]Side 1 = ADP + phosphate + aliphatic sulfonateSide 2 + [sulfonate-binding protein]Side 1.
... |
Q82CD3 | MATHTEQLTRPAVRLQGLTRSFADRTVLDGIDLDLPAGQFTALLGHSGSGKSTLLRAVAGLDHEVTGSGQLTAPERVSVVFQDSRLLPWRRVLDNVLLGTDGKEAAERGRAALAEVGLAGRERAWPGELSGGEAQRAALARSLVREPELLLADEPFGALDALTRIRMHTLLRELWERHRPSVLLVTHDVDEAIVLADRVLVLERGRIGLDLTIDRPHPRSYRDPLLGEYRERLLTALGVTEHQGAQEDHQ | Function: Part of the ABC transporter complex SsuABC involved in aliphatic sulfonates import. Responsible for energy coupling to the transport system.
Catalytic Activity: ATP + H2O + aliphatic sulfonate-[sulfonate-binding protein]Side 1 = ADP + phosphate + aliphatic sulfonateSide 2 + [sulfonate-binding protein]Side 1.
... |
Q8PHQ3 | MAGLASGATTACRATPMSAATTGLPLRVRGIAKRYGDSDVLRGIDLEIAPSACVAIVGRSGCGKSTLLRVIAGLETADVGTVDSGRAPLAAQRDAVRLMFQDARLLPWKRVIDNVALGLGRAGRAQAQQALDAVGLGTRGNAWPSALSGGQRQRVALARALVHRPRLLLLDEPLGALDALTRIEMQQLIVQLWRQHGFTLVLVTHDVAEASALADRIVVLEHGKVGLDVAVPVPHPRAPGLPALASIQAQVLSRLLGTTQVPEPAAPKAQTRHGPPRGATAQDTSPLQRIL | Function: Part of the ABC transporter complex SsuABC involved in aliphatic sulfonates import. Responsible for energy coupling to the transport system.
Catalytic Activity: ATP + H2O + aliphatic sulfonate-[sulfonate-binding protein]Side 1 = ADP + phosphate + aliphatic sulfonateSide 2 + [sulfonate-binding protein]Side 1.
... |
Q5YRK2 | MMAGSTTTTTAAVRVRGAGRAFAGRQVLRGVDLDIAPGEFVALLGASGSGKSTLLRAIGGLDRGFTGTLEAPRSKAIVFQEHRLIPWISVWRNVVLGVRGRDLAARARTALDEVGLSAEADAWPATLSGGEAQRVALARALVRHPDLLLLDEPFGALDALTRLKAQALVARLWQQHRPAVLLVTHDVEEALLLADRALVLRDGRIAESFDITVTRPRSVVDPEFSALRRRLLLALGVDPDAPTGAQS | Function: Part of the ABC transporter complex SsuABC involved in aliphatic sulfonates import. Responsible for energy coupling to the transport system.
Catalytic Activity: ATP + H2O + aliphatic sulfonate-[sulfonate-binding protein]Side 1 = ADP + phosphate + aliphatic sulfonateSide 2 + [sulfonate-binding protein]Side 1.
... |
Q48CA0 | MTSLKQQPPHLLRGIPLAVRNLKKAFGTREVLKDIDLHIPAGQFVAIVGRSGCGKSTLLRLLAGLDKPTEGQLLAGSAPLDDAREDTRLMFQEARLLPWKKIIDNVGLGLSGDWRAQALEALEAVGLAERANEWPAALSGGQKQRVALARALIHKPRLLLLDEPLGALDALTRIEMQQLIEKLWHQYGFTVLLVTHDVSEAVAIADRVILIEEGQIGLDLLVDLPRPRVRGSHRLAALEAEVLNRVLALPGSPPDPEPFSPLPTQLRWAN | Function: Part of the ABC transporter complex SsuABC involved in aliphatic sulfonates import. Responsible for energy coupling to the transport system.
Catalytic Activity: ATP + H2O + aliphatic sulfonate-[sulfonate-binding protein]Side 1 = ADP + phosphate + aliphatic sulfonateSide 2 + [sulfonate-binding protein]Side 1.
... |
Q0S0X2 | MTAAEAPLPPLAPRERTATTAAERRTGSPLAVSLSGVRKSFGDKTVLSGIDLEITRGEFVVLLGPSGTGKTTLLRLLSGLEPPDGGDVLVPRQRTVVYQEPRLIPSKRVLANVSVGQKRAQLTRDNARRALAEVNLADKERAWPATLSGGEAQRVALARALVREPELLLLDEPFAALDALTRLQMQDLVGDLVARHRPAVLLVTHDVDEAVRLADRVLILDNGGFAVDVDIDLPRPRDRNDPEALRYRATFLAQLGVGRPSSTRQDIS | Function: Part of the ABC transporter complex SsuABC involved in aliphatic sulfonates import. Responsible for energy coupling to the transport system.
Catalytic Activity: ATP + H2O + aliphatic sulfonate-[sulfonate-binding protein]Side 1 = ADP + phosphate + aliphatic sulfonateSide 2 + [sulfonate-binding protein]Side 1.
... |
Q6FFZ1 | MTIMSNLNIPLFPDQEKDLSSSASQPETAPIGAEILIEQLHKFYGQIKVLEDLDLHIQAGEFIAIVGRSGCGKSTLLRLIAGLEHTSYGEIKFKSARHFREGITSDDIRVMFQDPRLLPWKSILHNVQLGLNKQQLPIAEQLLEKVGLKDKAGQWPSQLSGGQRQRTALARALSHSPRILLLDEPLGALDALTRLEMQSLIERLWKEQGFTAILVTHDVSEAVQLADRIILLDKGHIAQSFEVNLPRPRHKSLEFAQLEQQVLEAVLAT | Function: Part of the ABC transporter complex SsuABC involved in aliphatic sulfonates import. Responsible for energy coupling to the transport system.
Catalytic Activity: ATP + H2O + aliphatic sulfonate-[sulfonate-binding protein]Side 1 = ADP + phosphate + aliphatic sulfonateSide 2 + [sulfonate-binding protein]Side 1.
... |
Q91XS8 | MSRRRFDCRSISGLLTTTPQTPMKTENFNNFYTLTPKELGRGKFAVVRQCISKSTGQEYAAKFLKKRRRGQDCRAEILHEIAVLELARSCPHVINLHEVYETATEIILVLEYAAGGEIFNLCLPELAEMVSENDVIRLIKQILEGVHYLHQNNIVHLDLKPQNILLSSIYPLGDIKIVDFGMSRKIGNASELREIMGTPEYLAPEILNYDPITTATDMWNIGIIAYMLLTHTSPFVGEDNQETYLNISQVNVDYSEEMFSSVSQLATDFIQSLLVKNPEKRPTAESCLSHSWLQQWDFGSLFHPEETSESSQTQDLSLRS... | Function: Acts as a positive regulator of apoptosis. Phosphorylates myosin light chains.
PTM: Autophosphorylated.
Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Sequence Mass (Da): 42133
Sequence Length: 371
Subcellular Location: Nucleus
EC: 2.7.11.1
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P50227 | MELIQDTSRPPAKYVKGIPLIKYFAEALGPLESFEAWPDDLLISTYPKSGTTWVSEILDLIYQEGDLEKCQRAPVFLRVPFLEFSAPGVPTGVELLKDTPAPRLLKTHLPLALLPKTLLDQKVKVIYIARNAKDVAVSYYHFYRMAKVHPDPGTWDSFLEKFMAGEVCYGSWYQHVQEWWELSHTHPVLYLFYEDIKEDPKREIQKILEFIGRSLPEETVDHIVQRTSFKEMKKNPMTNYSTIPTAVMDHSISAFMRKGITGDWKSTFTVAQNELFEAHYAKKMAGCKLRFRWEL | Function: Sulfotransferase that utilizes 3'-phospho-5'-adenylyl sulfate (PAPS) as sulfonate donor to catalyze the sulfate conjugation of a wide variety of acceptor molecules bearing a hydroxyl or an amine groupe. Sulfonation increases the water solubility of most compounds, and therefore their renal excretion, but it c... |
Q29476 | MEDIPDTSRPPLKYVKGIPLIKYFAEALESLQDFQAQPDDLLISTYPKSGTTWVSEILDMIYQDGDVEKCRRAPVFIRVPFLEFKAPGIPTGLEVLKDTPAPRLIKTHLPLALLPQTLLDQKVKVVYVARNAKDVAVSYYHFYRMAKVHPDPDTWDSFLEKFMAGEVSYGSWYQHVQEWWELSHTHPVLYLFYEDMKENPKREIQKILKFVGRSLPEETVDLIVQHTSFKEMKNNSMANYTTLSPDIMDHSISAFMRKGISGDWKTTFTVAQNERFDADYAKKMEGCGLSFRTQL | Function: Sulfotransferase that utilizes 3'-phospho-5'-adenylyl sulfate (PAPS) as sulfonate donor to catalyze the sulfate conjugation of a wide variety of acceptor molecules bearing a hydroxyl or an amine groupe . Sulfonation increases the water solubility of most compounds, and therefore their renal excretion, but it ... |
P50225 | MELIQDTSRPPLEYVKGVPLIKYFAEALGPLQSFQARPDDLLISTYPKSGTTWVSQILDMIYQGGDLEKCHRAPIFMRVPFLEFKAPGIPSGMETLKDTPAPRLLKTHLPLALLPQTLLDQKVKVVYVARNAKDVAVSYYHFYHMAKVHPEPGTWDSFLEKFMVGEVSYGSWYQHVQEWWELSRTHPVLYLFYEDMKENPKREIQKILEFVGRSLPEETVDFVVQHTSFKEMKKNPMTNYTTVPQEFMDHSISPFMRKGMAGDWKTTFTVAQNERFDADYAEKMAGCSLSFRSEL | Function: Sulfotransferase that utilizes 3'-phospho-5'-adenylyl sulfate (PAPS) as sulfonate donor to catalyze the sulfate conjugation of a wide variety of acceptor molecules bearing a hydroxyl or an amine groupe. Sulfonation increases the water solubility of most compounds, and therefore their renal excretion, but it c... |
P50226 | MELIQDISRPPLEYVKGVPLIKYFAEALGPLQSFQARPDDLLISTYPKSGTTWVSQILDMIYQGGDLEKCHRAPIFMRVPFLEFKVPGIPSGMETLKNTPAPRLLKTHLPLALLPQTLLDQKVKVVYVARNAKDVAVSYYHFYHMAKVYPHPGTWESFLEKFMAGEVSYGSWYQHVQEWWELSRTHPVLYLFYEDMKENPKREIQKILEFVGRSLPEETVDLMVEHTSFKEMKKNPMTNYTTVRREFMDHSISPFMRKGMAGDWKTTFTVAQNERFDADYAKKMAGCSLSFRSEL | Function: Sulfotransferase that utilizes 3'-phospho-5'-adenylyl sulfate (PAPS) as sulfonate donor to catalyze the sulfate conjugation of catecholamines, phenolic drugs and neurotransmitters. Is also responsible for the sulfonation and activation of minoxidil. Mediates the metabolic activation of carcinogenic N-hydroxya... |
Q3T0Y3 | MTSPKDVLRKNLKLIHGCPITYAFANNWEKIEQFQSRPDDIMIVTYPKSGTTWISEIVDMVLHDGDVEKCKRDVITAKVPMLELALPGLRTSGLEQLEKNPSPRVVKTHLPIDLIPKSFWENNCKIIYLARNAKDVAVSFYHFDLMNNLQPLPGTWGEYLEKFLTGNVAYGSWFNHVKSWWKKKEGHPILFLFYEDMKENPKQEIKKVVRFLEKNLDDEILDKIIYHTSFEMMKDNPLVNYTHLPSEVMDHSKSSFMRKGIAGDWKNYFTVAQNEKFDAIYKKEMSETELQFRTEI | Function: Sulfotransferase that utilizes 3'-phospho-5'-adenylyl sulfate (PAPS) as sulfonate donor to catalyze the sulfate conjugation of dopamine small phenols such as 1-naphthol and 4-nitrophenol . Catalyzes also the sulfate conjugation of dopamine and thyroid hormones, including 3,3'-diiodothyronine, triidothyronine ... |
Q8JG30 | MGTVDAYLRQPWSTVHAIPMVSAFAQNWERVDNFQSRPDDIVVATFPKSGTTWISEIVDMILQGGDPKKCKRDAIVNRVPMLEFAAPGQMPAGTEQLENMPSPRIIKTHIPADILPKSFWDKSCKMIYVGRNAKDVAVSYYHFDLMNKLHPHPGTWDQYLEAFMAGKVAYGSWFDHVRGYWERRQEHPILYLFYEDMKEDLRREVAKVAQFLGRELTEVALDAIAHHTSFEAMRDNPSTNYSVVPSQLMDHGISPFMRKGITGDWKNHFTVAQSAHFDQYYAQKMAGTDLRFRTHI | Function: Sulfotransferase that utilizes 3'-phospho-5'-adenylyl sulfate (PAPS) as sulfonate donor to catalyze the sulfate conjugation of dopamine, small phenols such as 1-naphthol and p-nitrophenol and thyroid hormones, including 3,3'-diiodothyronine, triidothyronine (T3) and reverse triiodothyronine (rT3).
Catalytic A... |
O43704 | MLSPKDILRKDLKLVHGYPMTCAFASNWEKIEQFHSRPDDIVIATYPKSGTTWVSEIIDMILNDGDIEKCKRGFITEKVPMLEMTLPGLRTSGIEQLEKNPSPRIVKTHLPTDLLPKSFWENNCKMIYLARNAKDVSVSYYHFDLMNNLQPFPGTWEEYLEKFLTGKVAYGSWFTHVKNWWKKKEEHPILFLYYEDMKENPKEEIKKIIRFLEKNLNDEILDRIIHHTSFEVMKDNPLVNYTHLPTTVMDHSKSPFMRKGTAGDWKNYFTVAQNEKFDAIYETEMSKTALQFRTEI | Function: Sulfotransferase that utilizes 3'-phospho-5'-adenylyl sulfate (PAPS) as sulfonate donor to catalyze the sulfate conjugation of dopamine, small phenols such as 1-naphthol and p-nitrophenol and thyroid hormones, including 3,3'-diiodothyronine, triidothyronine (T3) and reverse triiodothyronine (rT3) . May play a... |
Q80VR3 | MPLEKLKDLHLDEQNMQPETREVNGILMSKMMSENWDKIWNFQAKPDDLLIATYAKAGTTWTQEIVDMIQNDGDVQKCQRANTYDRHPFIEWTLPPPLNSGLDLANKMPSPRTLKTHLPVQMLPPSFWKENSKIIYVARNAKDCLVSYYYFSRMNKMLPDPGTLGEYIETFKAGKVLWGSWYDHVKGWWDVKDKHRILYLFYEDMKEDPKREIKKIVKFLEKDISEEVLNKIIHHTSFDVMKQNPMANYTTLPSSIMDHSISPFMRKGMPGDWKNYFTVAQSEDFDEDYRKKMAGSTITFRTEI | Function: Sulfotransferase that utilizes 3'-phospho-5'-adenylyl sulfate (PAPS) as sulfonate donor to catalyze the sulfate conjugation of drugs, xenobiotic compounds, hormones, and neurotransmitters. May be involved in the activation of carcinogenic hydroxylamines. Shows activity towards p-nitrophenol and N-hydroxy-2-ac... |
Q54BD4 | MSNNNPKKRPLDAISNTFEVKQEEPEFSSDGFNTTNDDLMSLMTFLDNGTGQQNQQNQQNQQPQPQPQPQPQLPQPQSQQPIYNSNTTTVTVKTEGIATSPLSNASSPISTNNNINNNTNNNNNNNNNNNNNNNNNNNNNNNINTATPPAIGVQQNSNIPYSYPIYTDVTGQQTQHQQNIGQNSVNIDPYFQTIDGAQIQQQQLLQQQLQPIQQVNNPQIDQAQIQQQQAQQIQQQQAQIQAQQAQIQQQQLEQQHLQQQQFQFQQQQQQQQQQQQQQQQQQQQQQQQQQQQQQQQHHQQQQQQQQHQQQQQHQQQQQHQ... | Function: Transcription factor that regulates gene expression during development. May play a role in regulating gene expression in response to osmotic stress.
PTM: Tyrosine phosphorylated in response to the chlorinated hexaphenone DIF. Minimally phosphorylated in the absence of DIF. Phosphorylation increases during dev... |
Q24151 | MSLWKRISSHVDCEQRMAAYYEEKGMLELRLCLAPWIEDRIMSEQITPNTTDQLERVALKFNEDLQQKLLSTRTASDQALKFRVVELCALIQRISAVELYTHLRSGLQKELQLVTEKSVAATAGQSMPLNPYNMNNTPMVTGYMVDPSDLLAVSNSCNPPVVQGIGPIHNVQNTGIASPALGMVTPKVELYEVQHQIMQSLNEFGNCANALKLLAQNYSYMLNSTSSPNAEAAYRSLIDEKAAIVLTMRRSFMYYESLHEMVIHELKNWRHQQAQAGNGAPFNEGSLDDIQRCFEMLESFIAHMLAAVKELMRVRLVTEE... | Function: Might play a role in signal transduction and activation of transcription. Plays an important role in the segmental pattern formation in the early embryo by activating specific stripes of pair rule gene expression in early development as part of the Janus kinase-STAT pathway . Might play a role in male germlin... |
P02808 | MKFLVFAFILALMVSMIGADSSEEKFLRRIGRFGYGYGPYQPVPEQPLYPQPYQPQYQQYTF | Function: Salivary protein that stabilizes saliva supersaturated with calcium salts by inhibiting the precipitation of calcium phosphate salts. It also modulates hydroxyapatite crystal formation on the tooth surface.
PTM: Substrate for transglutaminase-2. More than 95% of the cyclized peptide is cyclo-statherin Q-37, a... |
O95793 | MSQVQVQVQNPSAALSGSQILNKNQSLLSQPLMSIPSTTSSLPSENAGRPIQNSALPSASITSTSAAAESITPTVELNALCMKLGKKPMYKPVDPYSRMQSTYNYNMRGGAYPPRYFYPFPVPPLLYQVELSVGGQQFNGKGKTRQAAKHDAAAKALRILQNEPLPERLEVNGRESEEENLNKSEISQVFEIALKRNLPVNFEVARESGPPHMKNFVTKVSVGEFVGEGEGKSKKISKKNAAIAVLEELKKLPPLPAVERVKPRIKKKTKPIVKPQTSPEYGQGINPISRLAQIQQAKKEKEPEYTLLTERGLPRRREFV... | Function: Binds double-stranded RNA (regardless of the sequence) and tubulin. May play a role in specific positioning of mRNAs at given sites in the cell by cross-linking cytoskeletal and RNA components, and in stimulating their translation at the site.
Sequence Mass (Da): 63182
Sequence Length: 577
Domain: One of the ... |
Q9Z108 | MYKPVDPHSRMQSTYSYGMRGGAYPPRYFYPFPVPPLLYQVELSVGGQQFNGKGKMRPPVKHDAPARALRTLQSEPLPERLEVNGREAEEENLNKSEISQVFEIALKRNLPVNFEVARESGPPHMKNFVTRVSVGEFVGEGEGKSKKISKKNAARAVLEQLRRLPPLPAVERVKPRIKKKSQPTCKTAPDYGQGMNPISRLAQIQQAKKEKEPEYMLLTERGLPRRREFVMQVKVGHHTAEGVGTNKKVAKRNAAENMLEILGFKVPQAQPAKPALKSEEKTPVKKPGDGRKVTFFEPSPGDENGTSNKDEEFRMPYLSH... | Function: Binds double-stranded RNA (regardless of the sequence) and tubulin. May play a role in specific positioning of mRNAs at given sites in the cell by cross-linking cytoskeletal and RNA components, and in stimulating their translation at the site.
Sequence Mass (Da): 53925
Sequence Length: 487
Domain: One of the ... |
Q9NUL3 | MANPKEKTAMCLVNELARFNRVQPQYKLLNERGPAHSKMFSVQLSLGEQTWESEGSSIKKAQQAVANKALTESTLPKPVQKPPKSNVNNNPGSITPTVELNGLAMKRGEPAIYRPLDPKPFPNYRANYNFRGMYNQRYHCPVPKIFYVQLTVGNNEFFGEGKTRQAARHNAAMKALQALQNEPIPERSPQNGESGKDVDDDKDANKSEISLVFEIALKRNMPVSFEVIKESGPPHMKSFVTRVSVGEFSAEGEGNSKKLSKKRAATTVLQELKKLPPLPVVEKPKLFFKKRPKTIVKAGPEYGQGMNPISRLAQIQQAKK... | Function: RNA-binding protein required for the microtubule-dependent transport of neuronal RNA from the cell body to the dendrite. As protein synthesis occurs within the dendrite, the localization of specific mRNAs to dendrites may be a prerequisite for neurite outgrowth and plasticity at sites distant from the cell bo... |
Q68SB1 | MANPKEKTPMCLVNELARFHSIQPQYKLLNESGPAHSKMFSVQLSLGEQTWESEGSSIKKAQQAVANKALTESTLPKPVQKPPKSNVNNNPGSITPTVELNGLAMKRGEPAIYRPLDPKPFPNYRANYNFRGMYNQRYHCPMPKIFYVQLTVGNNEFFGEGKTRQAARHNAAMKALQALQNEPIPEKSPQNGESGKEMDDDKDANKSEISLVFEIALKRNMPVSFEVIKESGPPHMKSFVTRVSVGEFSAEGEGNSKKLSKKRAATTVLQELKKLPPLPVIEKPKLFFKKRPKTIIKAGPEYGQGMNPISRLAQIQQARK... | Function: RNA-binding protein required for the microtubule-dependent transport of neuronal RNA from the cell body to the dendrite. As protein synthesis occurs within the dendrite, the localization of specific mRNAs to dendrites may be a prerequisite for neurite outgrowth and plasticity at sites distant from the cell bo... |
P37506 | MIMKMTHLNMKDFNKPNEPFVVFGRMIPAFENGVWTYTEERFSKPYFKQYEDDDMDVSYVEEEGKAAFLYYLENNCIGRIKIRSNWNGYALIEDIAVAKDYRKKGVGTALLHKAIEWAKENHFCGLMLETQDINISACHFYAKHHFIIGAVDTMLYSNFPTANEIAIFWYYKF | Function: Involved in resistance to streptothricin, a broad-spectrum antibiotic produced by streptomycetes. Detoxifies streptothricin via acetylation of the beta amino group of the first beta-lysyl moiety of streptothricin.
Catalytic Activity: acetyl-CoA + streptothricin D = CoA + H(+) + N(beta)-acetylstreptothricin D
... |
O05139 | MAVYNYDVVVLGSGPAGEGAAMNAAKAGRKVAMVDSRRQVGGNCTHLGTIPSKALRHSVRQIMQFNTNPMFRAIGEPRWFSFPDVLKSAEKVISKQVASRTGYYARNRVDLFFGTGSFADEQTVEVVCANGVVEKLVAKHIIIATGSRPYRPADIDFHHPRIYDSDTILSLGHTPRKLIIYGAGVIGCEYASIFSGLGVLVELVDNRDQLLSFLDSEISQALSYHFSNNNITVRHNEEYDRVEGLDNGVILHLKSGKKIKADALLWCNGRTGNTDKLGMENIGVKVNSRGQIEVDENYRTCVTNIYGAGDVIGWPSLASA... | Cofactor: Binds 1 FAD per subunit.
Function: Conversion of NADPH, generated by peripheral catabolic pathways, to NADH, which can enter the respiratory chain for energy generation.
Catalytic Activity: NAD(+) + NADPH = NADH + NADP(+)
Sequence Mass (Da): 51008
Sequence Length: 464
Subcellular Location: Cytoplasm
EC: 1.6.1... |
Q15208 | MAMTGSTPCSSMSNHTKERVTMTKVTLENFYSNLIAQHEEREMRQKKLEKVMEEEGLKDEEKRLRRSAHARKETEFLRLKRTRLGLEDFESLKVIGRGAFGEVRLVQKKDTGHVYAMKILRKADMLEKEQVGHIRAERDILVEADSLWVVKMFYSFQDKLNLYLIMEFLPGGDMMTLLMKKDTLTEEETQFYIAETVLAIDSIHQLGFIHRDIKPDNLLLDSKGHVKLSDFGLCTGLKKAHRTEFYRNLNHSLPSDFTFQNMNSKRKAETWKRNRRQLAFSTVGTPDYIAPEVFMQTGYNKLCDWWSLGVIMYEMLIGYP... | Function: Negative regulator of MAP3K1/2 signaling. Converts MAP3K2 from its phosphorylated form to its non-phosphorylated form and inhibits autophosphorylation of MAP3K2.
PTM: ISGylated.
Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Sequence Mass (Da): 54190
Sequence Length: 46... |
Q9UEW8 | MAEPSGSPVHVQLPQQAAPVTAAAAAAPAAATAAPAPAAPAAPAPAPAPAAQAVGWPICRDAYELQEVIGSGATAVVQAALCKPRQERVAIKRINLEKCQTSMDELLKEIQAMSQCSHPNVVTYYTSFVVKDELWLVMKLLSGGSMLDIIKYIVNRGEHKNGVLEEAIIATILKEVLEGLDYLHRNGQIHRDLKAGNILLGEDGSVQIADFGVSAFLATGGDVTRNKVRKTFVGTPCWMAPEVMEQVRGYDFKADMWSFGITAIELATGAAPYHKYPPMKVLMLTLQNDPPTLETGVEDKEMMKKYGKSFRKLLSLCLQK... | Function: Effector serine/threonine-protein kinase component of the WNK-SPAK/OSR1 kinase cascade, which is involved in various processes, such as ion transport, response to hypertonic stress and blood pressure . Specifically recognizes and binds proteins with a RFXV motif . Acts downstream of WNK kinases (WNK1, WNK2, W... |
Q9Z1W9 | MAEPSGSPVHVQLSQQAAPVTAAAATAPAAATSAPAPAPAPAPAASAAPAPAPAAAPAPAPAAQAVGWPICRDAYELQEVIGSGATAVVQAALCKPRQERVAIKRINLEKCQTSMDELLKEIQAMSQCSHPNVVTYYTSFVVKDELWLVMKLLSGGSMLDIIKYIVNRGEHKNGVLEEAIIATILKEVLEGLDYLHRNGQIHRDLKAGNILLGEDGSVQIADFGVSAFLATGGDVTRNKVRKTFVGTPCWMAPEVMEQVRGYDFKADMWSFGITAIELATGAAPYHKYPPMKVLMLTLQNDPPTLETGVEDKEMMKKYGK... | Function: Effector serine/threonine-protein kinase component of the WNK-SPAK/OSR1 kinase cascade, which is involved in various processes, such as ion transport, response to hypertonic stress and blood pressure . Specifically recognizes and binds proteins with a RFXV motif . Acts downstream of WNK kinases (WNK1, WNK2, W... |
Q7ZUQ3 | MEHSVPKNKLKKLSEDSLTKQPEEVFDVLEKLGEGSYGSVFKAIHKESGQVVAIKQVPVESDLQEIIKEISIMQQCDSPYVVKYYGSYFKNTDLWIVMEYCGAGSVSDIIRLRNKTLTEDEIATVLKSTLKGLEYLHFMRKIHRDIKAGNILLNTEGHAKLADFGVAGQLTDTMAKRNTVIGTPFWMAPEVIQEIGYNCVADIWSLGITSIEMAEGKPPYADIHPMRAIFMIPTNPPPTFRKPEHWSDDFTDFVKKCLVKNPEQRATATQLLQHPFIVGAKPVSILRDLITEAMDMKAKRQQEQQRELEEDDENSEEEVE... | Function: Stress-activated, pro-apoptotic kinase which, following caspase-cleavage, enters the nucleus and induces chromatin condensation followed by internucleosomal DNA fragmentation. Key component of the Hippo signaling pathway which plays a pivotal role in organ size control and tumor suppression by restricting pro... |
Q13188 | MEQPPAPKSKLKKLSEDSLTKQPEEVFDVLEKLGEGSYGSVFKAIHKESGQVVAIKQVPVESDLQEIIKEISIMQQCDSPYVVKYYGSYFKNTDLWIVMEYCGAGSVSDIIRLRNKTLIEDEIATILKSTLKGLEYLHFMRKIHRDIKAGNILLNTEGHAKLADFGVAGQLTDTMAKRNTVIGTPFWMAPEVIQEIGYNCVADIWSLGITSIEMAEGKPPYADIHPMRAIFMIPTNPPPTFRKPELWSDDFTDFVKKCLVKNPEQRATATQLLQHPFIKNAKPVSILRDLITEAMEIKAKRHEEQQRELEEEEENSDEDE... | Function: Stress-activated, pro-apoptotic kinase which, following caspase-cleavage, enters the nucleus and induces chromatin condensation followed by internucleosomal DNA fragmentation. Key component of the Hippo signaling pathway which plays a pivotal role in organ size control and tumor suppression by restricting pro... |
Q9JI10 | MEQPPASKSKLKKLSEDSLTKQPEEVFDVLEKLGEGSYGSVFKAIHKESGQVVAIKQVPVESDLQEIIKEISIMQQCDSPYVVKYYGSYFKNTDLWIVMEYCGAGSVSDIIRLRNKTLTEDEIATILKSTLKGLEYLHFMRKIHRDIKAGNILLNTEGHAKLADFGVAGQLTDTMAKRNTVIGTPFWMAPEVIQEIGYNCVADIWSLGITSIEMAEGKPPYADIHPMRAIFMIPTNPPPTFRKPELWSDDFTDFVKKCLVKSPEQRATATQLLQHPFIKNAKPVSILRDLIAEAMEIKAKRHEEQQRELEEEEENSDEDE... | Function: Stress-activated, pro-apoptotic kinase which, following caspase-cleavage, enters the nucleus and induces chromatin condensation followed by internucleosomal DNA fragmentation. Key component of the Hippo signaling pathway which plays a pivotal role in organ size control and tumor suppression by restricting pro... |
Q8N2I9 | MKRRASDRGAGETSARAKALGSGISGNNAKRAGPFILGPRLGNSPVPSIVQCLARKDGTDDFYQLKILTLEERGDQGIESQEERQGKMLLHTEYSLLSLLHTQDGVVHHHGLFQDRTCEIVEDTESSRMVKKMKKRICLVLDCLCAHDFSDKTADLINLQHYVIKEKRLSERETVVIFYDVVRVVEALHQKNIVHRDLKLGNMVLNKRTHRITITNFCLGKHLVSEGDLLKDQRGSPAYISPDVLSGRPYRGKPSDMWALGVVLFTMLYGQFPFYDSIPQELFRKIKAAEYTIPEDGRVSENTVCLIRKLLVLDPQQRLA... | Function: May be a negative regulator of NF-kappa-B and p53-mediated gene transcription.
Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Sequence Mass (Da): 49001
Sequence Length: 435
Subcellular Location: Nucleus
EC: 2.7.11.1
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O64530 | MASTLFSRTFLAASHRLITPSLPQKIFNPATFLSRSLHSQLGSASTAYKSTTWARRAMASTGVETKAGYSTSSVSTSEPVVSVDWLHANLREPDLKILDASWYMPDEQRNPIQEYQVAHIPRALFFDLDGISDRKTSLPHMLPTEEAFAAGCSALGIDNKDEVVVYDGKGIFSAARVWWMFRVFGHEKVWVLDGGLPRWRASGYDVESSASGDAILKASAASEAIEKIYQGQTVSPITFQTKFQPHLVWTLDQVKNNMEDPTYQHIDARSKARFDGTAPEPRKGIRSGHIPGSKCIPFPQMFDSCNTLLPAEELKKRFDQ... | Function: Catalyzes the transfer of a sulfur ion from a donor to cyanide or to other thiol compounds. Substrate preference is 3-mercaptopyruvate > thiosulfate. Involved in embryo and seed development.
Catalytic Activity: hydrogen cyanide + thiosulfate = 2 H(+) + sulfite + thiocyanate
Sequence Mass (Da): 41893
Sequence ... |
D3GE74 | MARLERDGTNKSLESLMDSHKPGGTTTNLNQLRTQKSIPGYGLEFTNLSYSIIKKQKKDGVWINKETYLLHDISGQAIKGEIMAIMGPSGAGKSTFLDALAGRIAKGSLQGSVRIDGKPVTTSYMKMVSSYVMQDDQLFPMLTVFETFMFAAEVRLPPSISRDEKKKRVHELLNKLGLQSATHTYIGDEGRRGVSGGERRRVSIGIEIIHKPSLLFLDEPTSGLDSTSAYSVVEKIKDIAQGGSIVLMTIHQPSFRIQMLLDKITILARGRLIYMGRPDALHTHLSGFGRPVPDGENNIEYLLDVITEYDQATVGLDPLV... | Function: Together with STR2, required for arbuscule development in arbuscular mycorrhizal (AM) symbiosis.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 91885
Sequence Length: 817
Subcellular Location: Cell membrane
EC: 7.6.2.-
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O74395 | MRLKSFSTTLDTLRRRFNDSSSEEDKLEKNIQDETSIKEVSLQDAKQSDEKGVEEKVFNDESFSIDVAPKPEDELSGIVKARYLTEHSSRISFYICYFSIFLLFFAISFQAECYYSLTAYATSAFAGHSLLSTIAVANNIISAAIKPPLARLSDVFGRLEAFLFSLLLYLVGLILMAASTNVQTYAGGSVLYNAGYTGVELIMTIFMADTSSMANRSLVLGISYLPFVVTIWIGPRVAQEFYMHSTWRWGIAVWTILIPACSIPFLAVYSYYQFRAWREGALKGTLTINPVELFKKLDIIGLILMTAGLALVLLSISLAS... | Function: Involved in the transport of siderophore iron and so has a role in iron homeostasis.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 68156
Sequence Length: 612
Subcellular Location: Membrane
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A0A384XG60 | MAQVVADPIVDKSAILKSELSKQPETLIAYAKWYGKVAGPITGVDLSAIDAKSLTLICTLSDGSKQQVRIELSPPLARYEDAKPRLLEMKTRALEGLGLTKTPVITNFIFPSLALKTTIWSVAGLLYLTFVPNPYLTGANIPRAWAAVGLIHGPQAIYTATLARKHVGNLTTGVSYVLGTLVFGFPFWIDLRQRITAARVESVAKIQ | Function: Part of the gene cluster that mediates the biosynthesis of strobilurin A, an antifungal polyketide that contains a key beta-methoxyacrylate toxophore that targets the complex III of the mitochondrial electron transport chain . Strobilurin biosynthesis begins with construction of benzoyl CoA by step-wise elimi... |
Q24JL3 | MKRAFSSQLRSAYPASKSTHFGRVMASSGSEAKANYAPISTNEPVVSVDWLHSNLGDADIKVLDASWYMAHEQRNPIQEYQVAHIPGALFFDLNGIADRKTNLRHMLPSEEAFAAGCSALGIENNDGVVVYDGMGLFSAARVWWMFRVFGHDKVWVLDGGLPKWRASGYDVESSVSNDAILKASAATEAIEKIYQGQTISPITFQTKFRPHLVLALDQVKENIEDKTYQHIDARSKARFDGIAPEPWKGLPSGHIPGSKCVPFPLMFDSSQTLLPAEELKKQFEQEDISLDSPIAASCGTGVTACILALGLYRLGKTNVA... | Function: Catalyzes the transfer of a sulfur ion from a donor to cyanide or to other thiol compounds. Substrate preference is 3-mercaptopyruvate > thiosulfate. Involved in embryo and seed development.
Catalytic Activity: hydrogen cyanide + thiosulfate = 2 H(+) + sulfite + thiocyanate
Sequence Mass (Da): 37412
Sequence ... |
A9YWR6 | MKTQGLELETVIDIKHKPVSFTGGLEFESLTYTVTKKKKVDGKWSNEDVDLLHDITGYAPKGCITAVMGPSGAGKSTLLDGLAGRIASGSLKGKVSLDGNSVNASLIKRTSAYIMQEDRLFPMLTVYETLMFAADFRLGPLSAVDKRQRVEKLIEQLGLSSSRNTYIGDEGTRGVSGGERRRVSIGVDIIHGPSLLFLDEPTSGLDSTSALSVIEKLHDIARNGSTVILTIHQPSSRIQLLLDHLIILARGQLMFQGSLKDVGHHLNRMGRKIPKGENPIENLIDVIQEYDQCDFVGVEVLAEFARTGMKPPLLSDMEEI... | Function: Together with STR, required for arbuscule development in arbuscular mycorrhizal symbiosis.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 81603
Sequence Length: 727
Subcellular Location: Cell membrane
EC: 7.6.2.-
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A0A0M4FLW6 | MRHANGRRGDTTIDIGKPVNFTGGLEFSNLTYTVIKKIKDSDGKWLNQEVDLLHQITGYAPKGCVTAVMGPSGAGKSTFLDGLAGRISSLRGRVSVDGMDMTPSFIKRTSAYIMQDDRLFPMLTVYETLLFAADLRLGPISMTDKRQRVEKLIEQLGLSSARNTYIGDEGTRGVSGGERRRVSIGVDIIHGPSLLFLDEPTSGLDSTSAHSVIDKVHAIARAGSTVILTIHQPSSRIQLLLDHLIILARGQLMYQGSPKDVSLHLGRMGRKVPKGESSIENLIDVIQEYDQSELGVEALAAFALTGMKPPPLGAHEMSIV... | Function: Together with STR, required for arbuscule development in arbuscular mycorrhizal (AM) symbiosis.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 80854
Sequence Length: 720
Subcellular Location: Cell membrane
EC: 7.6.2.-
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O94607 | MTENYGSMEHRKKSFRNNENLEQQFHPLREELDNAGPINDRTSELSLEGVSKAEAIASTWSKRSIIVAYLGLYLLSFASSLEQQTTYSLQRYATSNFSAHSNLATINLVGNILLAVVRAPMVKAADVFGRSESLSLALGMTVLGYLSLAFSRNIQMFTVAYILYICGQTGLGLLSQLIIADTSSLLNRGILSAIPELPYLATVWIGPVLAQAFHPEKNYGWRLGYGIWAFILPTVSLPLLASLFLNQRKAKAAGLYREHHNLINHSTPEKLRLFYLFWQELDGLGIVLFVSGFTLLLLPFSHSSQVVSPDSTILTLFTIT... | Function: Involved in the transport of siderophore iron and so has a role in iron homeostasis.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 66122
Sequence Length: 597
Subcellular Location: Membrane
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A0A384XC21 | MAAESAKQTPYVLVADEVEWARLDAMHNGIAKFLGNELTPVDLGQPKKILEIGAGSGAWAIQAAKLYPDADVLAIDMNPIPARPLPPNVRYQNINVLEPFPFEAASFDVIHIRLVLCHLPDGHSVLKRIIDLVAPGGWLLIDDIDWAEAFEGLDKAPGIKRGLTALVRSMEAEAGDPHYGKTLKPYLEASKELSEVHVREVELPVNPIPEDPALAGLSQMMRKALVGALGAAKQSSATVGLTKEVQEGFLSEMAREDMDWSYSCYLYFAAVKKSA | Function: Methyltransferase; part of the gene cluster that mediates the biosynthesis of strobilurin A, an antifungal polyketide that contains a key beta-methoxyacrylate toxophore that targets the complex III of the mitochondrial electron transport chain . Strobilurin biosynthesis begins with construction of benzoyl CoA... |
O95772 | MNHLPEDMENALTGSQSSHASLRNIHSINPTQLMARIESYEGREKKGISDVRRTFCLFVTFDLLFVTLLWIIELNVNGGIENTLEKEVMQYDYYSSYFDIFLLAVFRFKVLILAYAVCRLRHWWAIALTTAVTSAFLLAKVILSKLFSQGAFGYVLPIISFILAWIETWFLDFKVLPQEAEEENRLLIVQDASERAALIPGGLSDGQFYSPPESEAGSEEAEEKQDSEKPLLEL | Function: Tethering protein that creates contact site between the endoplasmic reticulum and late endosomes: localizes to late endosome membranes and contacts the endoplasmic reticulum via interaction with VAPA and VAPB .
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 26655
Sequence Length: 234
Domai... |
Q9DCI3 | MNHLPEHMENTLTGSQSSHASLRDIHSINPAQLMARIESYEGREKKGISDVRRTFCLFVTFDLLFVTLLWIIELNVNGGIENTLKKEVIHYDYYSSYFDIFLLAVFRFKVLILGYAVCRLRHWWAIALTTAVTSAFLLAKVILSKLFSQGAFGYVLPIISFILAWIETWFLDFKVLPQEAEEENRLLLVQDASERAALIPAGLSDGQFYSPPESEAGSEEEAEEKQESEKPLLEL | Function: Tethering protein that creates contact site between the endoplasmic reticulum and late endosomes: localizes to late endosome membranes and contacts the endoplasmic reticulum via interaction with VAPA and VAPB.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 26811
Sequence Length: 235
Domain... |
Q92341 | MEAKETHSISDHEVELQDAKPEEKSENGNFVFEKAFSSDEEKGSGYNTNETYSKMDNSLQHRGVSKIEAVRDSIYQNKRGMYLAYAFGIAILACSWASAIQSSTTYSYQVYATASFNRTSMISTLEIATAIISSVCKPILGKFSDITSRPMTYTLVLLFYVIGFIVVASSSTISAYVIGSVFISIGSSGLDYLNTLVVGDLTSLKWRGFMTALLSTPYIATVWFTGFIVQGIIDSNWRWGYGMFAIIMPAVMTPAVIILMYLERQANKDENIKKIINYQTEEKNKNKQSKWQKLWKAVLEVDLFGLILLGVGWSILLLPF... | Function: Low affinity heme transporter involved in the assimilation of exogenous heme during conditions of low cellular iron.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 70558
Sequence Length: 630
Subcellular Location: Cell membrane
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P53101 | MPIKRLDTVVVNTGSQNDQHSASVPPVYLSTTFKVDLNNEDAQNYDYSRSGNPTRSVLQHQIGKLYRVPQENVLAVSSGMTALDVILRGLVLLNGTDNHTPTIIAGDDLYGGTQRLLNFFKQQSHAVSVHVDTSDFEKFKTVFQSLDKVDCVLLESPTNPLCKVVDIPRILRFVKCISPDTTVVVDNTMMSGLNCNPLQLNPGCDVVYESATKYLNGHHDLMGGVIISKTPEIASKLYFVINSTGAGLSPMDSWLLVRGLKTLGVRLYQQQRNAMILAHWLENSCGFKPTRTNKATKTRFVGLRSNPDFKLHKSFNNGPG... | Catalytic Activity: H2O + L,L-cystathionine = L-homocysteine + NH4(+) + pyruvate
Sequence Mass (Da): 51828
Sequence Length: 465
Pathway: Amino-acid biosynthesis; L-methionine biosynthesis via de novo pathway; L-homocysteine from L-cystathionine: step 1/1.
Subcellular Location: Cytoplasm
EC: 4.4.1.13
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Q9M158 | MEALKTATFSPMSVLSEKRSEPRKPFSLPNLFPPKSQRPISQESFLKRFNGGLALLTSVLSSATAPAKSLTYEEALQQSMTTSSSFDSDGLIEGISNFVTDNPLVIAGGVAALAVPFVLSQVLNKKPKSWGVESAKNAYTKLGTDDNAQLLDIRATADFRQVGSPNIKGLGKKAVSTVYNGEDKPGFLKKLSLKFKDPENTTLYILDKFDGNSELVAELVALNGFKSAYAIKDGAEGPRGWLNSSLPWIEPKKTLSLDLSSLTDSISGVFGESSDGVSVALGVAAAAGLSVFAFTEIETILQLLGSAALVQLAGKKLLFA... | Function: Rhodanese domain-containing protein required for anchoring ferredoxin--NADP reductase to the thylakoid membranes and sustaining efficient linear electron flow (LEF).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 49387
Sequence Length: 466
Subcellular Location: Plastid
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