ids stringlengths 6 10 | seqs stringlengths 11 1.02k | texts stringlengths 108 11.1k |
|---|---|---|
Q9PLV4 | MRYGEKEIKEFDVENMEIWPNDAKNDYIIKITLPEFMCCCPRSGYPDFATIYLEYMPDKFVVELKAIKLYINTFMYRNVSHEASINEIYNTLKDKLKPKWIKVVGDFNPRGNVHTVIECRSDMVVPK | Function: Catalyzes the NADPH-dependent reduction of 7-cyano-7-deazaguanine (preQ0) to 7-aminomethyl-7-deazaguanine (preQ1).
Catalytic Activity: 7-aminomethyl-7-carbaguanine + 2 NADP(+) = 7-cyano-7-deazaguanine + 3 H(+) + 2 NADPH
Sequence Mass (Da): 15040
Sequence Length: 127
Pathway: tRNA modification; tRNA-queuosine ... |
B9KE89 | MRYGEKEIKEFDVENMEVWPNDAKNDYVIKITLPEFMCCCPRSGYPDFATIYLEYIPNKLVVELKAIKLYINTFMYRNVSHEASINEIYNTLKEKLDPKWIKVVGDFNPRGNVHTVIECRSDLVVPQ | Function: Catalyzes the NADPH-dependent reduction of 7-cyano-7-deazaguanine (preQ0) to 7-aminomethyl-7-deazaguanine (preQ1).
Catalytic Activity: 7-aminomethyl-7-carbaguanine + 2 NADP(+) = 7-cyano-7-deazaguanine + 3 H(+) + 2 NADPH
Sequence Mass (Da): 14941
Sequence Length: 127
Pathway: tRNA modification; tRNA-queuosine ... |
Q9ZE74 | MPLSTSLLGKKNTYKDSYDATLLFKIPRINNRNVLGIDSNHLPFYGVDIWNTYEISCLNKNGKPLVGIGTFYIPADSENIVESKSFKLYLNSFNNFIIESIEELERIILQDLSNVTYAKVTGRIFPINTKIEFGIPSGKNIDNLDIVCNNYGPPDNSLIEYEDVLVEEEIYSNLFKSNCLVTGQPDWGTIVIKYKGKKLKYDSFLRYLISFRNFNEFAEQCAERIFIDIKNSINLDFLSIYIVYTRRGGIDICPYRSTDKSYTLPNDKRLIRQ | Function: Catalyzes the NADPH-dependent reduction of 7-cyano-7-deazaguanine (preQ0) to 7-aminomethyl-7-deazaguanine (preQ1).
Catalytic Activity: 7-aminomethyl-7-carbaguanine + 2 NADP(+) = 7-cyano-7-deazaguanine + 3 H(+) + 2 NADPH
Sequence Mass (Da): 31481
Sequence Length: 273
Pathway: tRNA modification; tRNA-queuosine ... |
B5A5T4 | MWTQRNAVGNWLLVLTAVIGFLTFIWIPQTSAECQTRSIYCYECDSWTDARCKDPFNYTALPRDQPPLMTCNGCCVKMVRHQRSPYEVVRRMCTSQLQINLFMVDHVCMMESSGNGHMCFCEEDMCNSSKNLHTNGCQLHLIPIAVAVSWLMGQLLSR | Function: Required for homeostatic regulation of sleep under normal conditions and after sleep deprivation. Important regulator of the Sh K(+) channel, acting as a signaling molecule that connects sleep drive to lowered membrane excitability, possibly by enhancing K(+) channel activity and thus reducing neuronal excita... |
B4MQJ1 | MSLPAGNAVGNWLLILTAIFGFLTLIWIPQASAECQTRSIYCYECDSWTDARCKDPFNYTALPRDQPPLMTCNGCCVKMVRHQRSRYEVVRRMCTSQLQINLFMVDHVCMMESSGNGHMCFCEEDMCNSSKNLYTKNGYQHLINIMIIWLIGILLNQLSNR | Function: Required for homeostatic regulation of sleep under normal conditions and after sleep deprivation. Important regulator of the Sh K(+) channel, acting as a signaling molecule that connects sleep drive to lowered membrane excitability, possibly by enhancing K(+) channel activity and thus reducing neuronal excita... |
P34140 | MNPEYDYLFKLLLIGDSGVGKSCLLLRFADDTYTESYISTIGVDFKIRTINLDGKIIKLQIWDTAGQERFRTITSSYYRGAHGIIVVYDVTDHVSFNNVKQWMQEIQRYACDSVTRLLVGNKCDLIEKKIVDTSTAREYADSVGIPFLETSAKSSANVEQAFMIMASEIKKLQGGIQPNNNSTYNAHVVKPTGFTPIGKKKKCSII | Function: The small GTPases Rab are key regulators of intracellular membrane trafficking, from the formation of transport vesicles to their fusion with membranes. Rabs cycle between an inactive GDP-bound form and an active GTP-bound form that is able to recruit to membranes different set of downstream effectors directl... |
Q9H0U4 | MNPEYDYLFKLLLIGDSGVGKSCLLLRFADDTYTESYISTIGVDFKIRTIELDGKTIKLQIWDTAGQERFRTITSSYYRGAHGIIVVYDVTDQESYANVKQWLQEIDRYASENVNKLLVGNKSDLTTKKVVDNTTAKEFADSLGIPFLETSAKNATNVEQAFMTMAAEIKKRMGPGAASGGERPNLKIDSTPVKPAGGGCC | Function: The small GTPases Rab are key regulators of intracellular membrane trafficking, from the formation of transport vesicles to their fusion with membranes . Rabs cycle between an inactive GDP-bound form and an active GTP-bound form that is able to recruit to membranes different set of downstream effectors direct... |
P10536 | MNPEYDYLFKLLLIGDSGVGKSCLLLRFADDTYTESYISTIGVDFKIRTIELDGKTIKLQIWDTAGQERFRTVTSSYYRGAHGIIVVYDVTDQESYANVKQWLQEIDRYASENVNKLLVGNKSDLTTKKVVDNTTAKEFADSLGVPFLETSAKNATNVEQAFMTMAAEIKKRMGPGAASGGERPNLKIDSTPVKSASGGCC | Function: The small GTPases Rab are key regulators of intracellular membrane trafficking, from the formation of transport vesicles to their fusion with membranes. Rabs cycle between an inactive GDP-bound form and an active GTP-bound form that is able to recruit to membranes different set of downstream effectors directl... |
Q92928 | MNPGYDCLFKLLLIGDSGVGKSCLLLRFADDPYTESYISTIGVDFKIQTIELDGKTIKLQIWDTAGQERFWTITSSYYRGAHGFLVVYDVTDQESYANVKQWLQEIDRHASENVNKLLVGNKSDLTTKKVVDNTTAKEFADSLGIPFLETSAKNATNVEQAFMTMAAEIKKQMGPGAASGGERPNLKIDSTPVKPAGGGCC | Function: Protein transport. Probably involved in vesicular traffic (By similarity).
PTM: (Microbial infection) Phosphocholinated at Ser-76 by L.pneumophila AnkX, leading to displace GDP dissociation inhibitors (GDI) . Both GDP-bound and GTP-bound forms can be phosphocholinated. Dephosphocholinated by L.pneumophila Lem... |
Q9TVU5 | MKEYDYLFKIIVIGDSGTGKSSLLLRFADNTYSESYMSTIGVDFKIKTVKIDNTTIKLQIWDTAGQERFRTITSTYYRGAHGIICVYDVTNKLSFDHITETWLQDIDKYATSNVCKLLIGNKIDLAESRVVSADEAKHVAEQNNMNYIEASAKTDSNVEKAFTTIAKALKDKVTQYPSNAPASTVSLNTASKVPTNRGLTDSCQESSVFKKMNFSSGKCT | Function: Protein transport. Probably involved in vesicular traffic from ER to Golgi (By similarity).
Location Topology: Lipid-anchor
Sequence Mass (Da): 24470
Sequence Length: 220
Subcellular Location: Cell membrane
|
Q9NX57 | MRKPDSKIVLLGDMNVGKTSLLQRYMERRFPDTVSTVGGAFYLKQWRSYNISIWDTAGREQFHGLGSMYCRGAAAIILTYDVNHRQSLVELEDRFLGLTDTASKDCLFAIVGNKVDLTEEGALAGQEKEECSPNMDAGDRVSPRAPKQVQLEDAVALYKKILKYKMLDEQDVPAAEQMCFETSAKTGYNVDLLFETLFDLVVPMILQQRAERPSHTVDISSHKPPKRTRSGCCA | Function: Plays a role in apical endocytosis/recycling. Plays a role in the maturation and acidification of phagosomes that engulf pathogens, such as S.aureus and M.tuberculosis. Plays a role in the fusion of phagosomes with lysosomes.
Location Topology: Lipid-anchor
Sequence Mass (Da): 26277
Sequence Length: 234
Subce... |
P35295 | MRKPDGKIVLLGDMNVGKTSLLQRYMERRFPDTVSTVGGAFYLKQWRSFNISIWDTAGREQFHGLGSLYCRGAAAIILTYDVNHPQSLFELEDRFLGLTETANNDCLFAIVGNKVDLTSERDTEGGEKEGPASGKVGSCVSTKVPKQVQPEDAVALYKKILKYKMLDEREMPAAEQMCFETSAKTGYNVDLLFETLFDLVVPMIMRQRAEESDQTVDIASCKTPKQTRSGCCA | Function: Plays a role in apical endocytosis/recycling. Plays a role in the maturation and acidification of phagosomes that engulf pathogens, such as S.aureus and Mycobacterium. Plays a role in the fusion of phagosomes with lysosomes (By similarity).
Location Topology: Lipid-anchor
Sequence Mass (Da): 25989
Sequence Le... |
Q17R06 | MAAAGGGGAAAGRTYSFKVVLLGEGCVGKTSLVLRYCENKFNDKHITTLQASFLTKKLNIGGKRVNLAIWDTAGQERFHALGPIYYRDSNGAILVYDITDEDSFQKVKNWVKELRKMLGNEICLCIVGNKVDLEKERHVSIQEAESYAESVGAKHYHTSAKQNKGIEELFLDLCKRMIETAQVDERAKGNGSSQPGAARRGVQIIDDEPQAQSVGGGCCSSG | Function: Small GTPase involved in membrane trafficking control (By similarity). Regulates integrin internalization and recycling, but does not influence the traffic of endosomally translocated receptors in general (By similarity). As a result, may regulate cell adhesion and migration (By similarity). During the mitosi... |
Q00578 | MTDVEGYQPKSKGKIFPDMGESFFSSDEDSPATDAEIDENYDDNRETSEGRGERDTGAMVTGLKKPRKKTKSSRHTAADSSMNQMDAKDKALLQDTNSDIPADFVPDSVSGMFRSHDFSYLRLRPDHASRPLWISPSDGRIILESFSPLAEQAQDFLVTIAEPISRPSHIHEYKITAYSLYAAVSVGLETDDIISVLDRLSKVPVAESIINFIKGATISYGKVKLVIKHNRYFVETTQADILQMLLNDSVIGPLRIDSDHQVQPPEDVLQQQLQQTAGKPATNVNPNDVEAVFSAVIGGDNEREEEDDDIDAVHSFEIAN... | Function: ATP-dependent 3'-5' DNA helicase, component of the general transcription and DNA repair factor IIH (TFIIH) core complex, which is involved in general and transcription-coupled nucleotide excision repair (NER) of damaged DNA and, when complexed to TFIIK, in RNA transcription by RNA polymerase II. In NER, TFIIH... |
P28188 | MNPEYDYLFKLLLIGDSGVGKSCLLLRFSDDSYVESYISTIGVDFKIRTVEQDGKTIKLQIWDTAGQERFRTITSSYYRGAHGIIIVYDVTDEESFNNVKQWLSEIDRYASDNVNKLLVGNKSDLTENRAIPYETAKAFADEIGIPFMETSAKDATNVEQAFMAMSASIKERMASQPAGNNARPPTVQIRGQPVAQKNGCCST | Function: Protein transport. Regulator of membrane traffic from the Golgi apparatus towards the endoplasmic reticulum (ER).
Location Topology: Lipid-anchor
Sequence Mass (Da): 22648
Sequence Length: 203
Subcellular Location: Golgi apparatus
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Q9SEH3 | MNPEYDYLFKLLLIGDSGVGKSCLLLRFADDSYLDSYISTIGVDFKIRTVEQDGKTIKLQIWDTAGQERFRTITSSYYRGAHGIIVTYDVTDLESFNNVKQWLNEIDRYASENVNKLLVGNKCDLTSQKVVSTETAKAFADELGIPFLETSAKNATNVEEAFMAMTAAIKTRMASQPAGGSKPPTVQIRGQPVNQQSGCCSS | Function: Protein transport. Regulator of membrane traffic from the Golgi apparatus towards the endoplasmic reticulum (ER) (By similarity).
Location Topology: Lipid-anchor
Sequence Mass (Da): 22318
Sequence Length: 202
Subcellular Location: Cell membrane
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P06839 | MKFYIDDLPVLFPYPKIYPEQYNYMCDIKKTLDVGGNSILEMPSGTGKTVSLLSLTIAYQMHYPEHRKIIYCSRTMSEIEKALVELENLMDYRTKELGYQEDFRGLGLTSRKNLCLHPEVSKERKGTVVDEKCRRMTNGQAKRKLEEDPEANVELCEYHENLYNIEVEDYLPKGVFSFEKLLKYCEEKTLCPYFIVRRMISLCNIIIYSYHYLLDPKIAERVSNEVSKDSIVIFDEAHNIDNVCIESLSLDLTTDALRRATRGANALDERISEVRKVDSQKLQDEYEKLVQGLHSADILTDQEEPFVETPVLPQDLLTEA... | Cofactor: Binds 1 [4Fe-4S] cluster.
Function: ATP-dependent 5'-3' DNA helicase, component of the general transcription and DNA repair factor IIH (TFIIH) core complex, which is involved in general and transcription-coupled nucleotide excision repair (NER) of damaged DNA and, when complexed to TFIIK, in RNA transcription... |
O12944 | LAKRKAGGEEEDGEWRPPATQKRQKAGSEAESADCYRSPFRKPLTQLTNRPLCLDSSQHEAFIRSILSKPFKVPIPNYKGPTGLRALGIKRAGLRSPLHDPFEEGALVLYEPPLLSAHEQLKIDKDKVPVHVVVDPVLSRVLRPHQREGVKFLWDCVTSRRIPGSHGCIMADEMGLGKTLQCITLMWTLLRQSPDCKPEIEKAMVVSPSSLVRNWYNEVEKWLGGRIQPLAIDGGSKEEIDRKLVGSMNQRGLRVPSPILIISYETFRLHAEALQKGSVGLVICDEGHRLKNSENQTYQALNSLNTPRRVLISGTPIQND... | Function: Plays an essential role in homologous recombination (HR) which is a major pathway for repairing DNA double-strand breaks (DSBs), single-stranded DNA (ssDNA) gaps, and stalled or collapsed replication forks. Acts as a molecular motor during the homology search and guides RAD51 ssDNA along a donor dsDNA thereby... |
F1Q8K0 | MRRSLAPSQVAKRKQGPDSDDEEDWEPDMEPQCKRDCREKYISPYRKPLTPLTNRPFCADGNEHEAFIRKILSKPFKIPIPNYTGVLGLRALGLRRAGVRKALHDPFEDGALVLYEPPVISAHDLIKADKEKLPVHVVVDPVLSKVLRPHQREGVKFLWDCVTGRRIENSYGCIMADEMGLGKTLQCITLIWTLLKQSPDCKPEIDKVIVVSPSSLVRNWYNEVGKWLGGRVQPVAIDGGSKDEIDSKLVNFISQQGMRIPTPILIISYETFRLHAEVLHKGKVGLVICDEGHRLKNSDNQTYLALNSMNAQRRVLISGT... | Function: Plays an essential role in homologous recombination (HR) which is a major pathway for repairing DNA double-strand breaks (DSBs), single-stranded DNA (ssDNA) gaps, and stalled or collapsed replication forks . Acts as a molecular motor during the homology search and guides RAD51 ssDNA along a donor dsDNA thereb... |
O76460 | MRRSLAPSQRGPLRPESRHSFTPPLLKKNKRSCQQELEREQELDRRRLGALRDASNTSELPLPIRFTANSEYELAIAKVLARKFKVPMDNYVPDYGGKRVLGVRRCISRRPLHDPMACNALVLFHPPAYTEHERMGMDPTKVLVHVVVDPLLSNILRPHQREGVRFMYECVEGKRGNFNGCIMADEMGLGKTLQCVTLVWTLLRQGPECKPTINKAIVVSPSSLVKNWEKEFTKWLHGRLLCLPMEGGTKENTIRALEQFSMTSARLGTPVLLISYETFRIYAEILCKYEVGMVICDEGHRLKNSDNLTYQALMGLKTKR... | Function: Involved in mitotic DNA repair and meiotic recombination. Functions in the recombinational DNA repair pathway. Essential for interhomolog gene conversion (GC), but may have a less important role in intersister GC than spn-A/Rad51. In the presence of DNA, spn-A/Rad51 enhances the ATPase activity of okr/Rad54.
... |
Q92698 | MRRSLAPSQLAKRKPEGRSCDDEDWQPGLVTPRKRKSSSETQIQECFLSPFRKPLSQLTNQPPCLDSSQHEAFIRSILSKPFKVPIPNYQGPLGSRALGLKRAGVRRALHDPLEKDALVLYEPPPLSAHDQLKLDKEKLPVHVVVDPILSKVLRPHQREGVKFLWECVTSRRIPGSHGCIMADEMGLGKTLQCITLMWTLLRQSPECKPEIDKAVVVSPSSLVKNWYNEVGKWLGGRIQPLAIDGGSKDEIDQKLEGFMNQRGARVSSPILIISYETFRLHVGVLQKGSVGLVICDEGHRLKNSENQTYQALDSLNTSRR... | Function: Plays an essential role in homologous recombination (HR) which is a major pathway for repairing DNA double-strand breaks (DSBs), single-stranded DNA (ssDNA) gaps, and stalled or collapsed replication forks . Acts as a molecular motor during the homology search and guides RAD51 ssDNA along a donor dsDNA thereb... |
P41410 | MIQQPTTAKPRISTSSKLNTVLSKNKENVPGKLFKKFKCPSLVISEKRKELPLRKKPRVNYSEYGSVDGKYDSAYVSENVSGLATIKEANRLILNHERRDPSTVIKKQFSVPKPIKGHEDISKLCAHRPPPTLGMKRKVDFIPRPLYDPADEFAIVLYDPTTDADEIIPDIKEVLAEKRKKDELLKNRKGKKEISDSEPESDHDSCVSTDTVASCSTEQSLITSNTSKHRRPNKSLKDLLGIQKEKPPPPPVAVVIDPKLARILRPHQIEGVKFLYKCVTGRIDRCANGCIMADEMGLGKTLQCIALLWTLLKQSPQAGK... | Function: Plays an essential role in homologous recombination (HR) which is a major pathway for repairing DNA double-strand breaks (DSBs), single-stranded DNA (ssDNA) gaps, and stalled or collapsed replication forks. Acts as a molecular motor during the homology search and guides RAD51 ssDNA along a donor dsDNA thereby... |
P32863 | MARRRLPDRPPNGIGAGERPRLVPRPINVQDSVNRLTKPFRVPYKNTHIPPAAGRIATGSDNIVGGRSLRKRSATVCYSGLDINADEAEYNSQDISFSQLTKRRKDALSAQRLAKDPTRLSHIQYTLRRSFTVPIKGYVQRHSLPLTLGMKKKITPEPRPLHDPTDEFAIVLYDPSVDGEMIVHDTSMDNKEEESKKMIKSTQEKDNINKEKNSQEERPTQRIGRHPALMTNGVRNKPLRELLGDSENSAENKKKFASVPVVIDPKLAKILRPHQVEGVRFLYRCVTGLVMKDYLEAEAFNTSSEDPLKSDEKALTESQK... | Function: Plays an essential role in homologous recombination (HR) which is a major pathway for repairing DNA double-strand breaks (DSBs), single-stranded DNA (ssDNA) gaps, and stalled or collapsed replication forks . Acts as a molecular motor during the homology search and guides RAD51 ssDNA along a donor dsDNA thereb... |
Q2YMH5 | MAKTRVQFICQNCGAVHSRWAGKCDSCGEWNTLIEEGTNSGIGSGPAAMLSKRKGRAVALTSLSGEIEDAPRIVSGISELDRVTGGGFVRGSALLIGGDPGIGKSTLLTQAAAALSNRGHRIVYVSGEEAVAQIRLRAQRLGVAASAVELAAETNVEDIIATISSDNSGSKRPDLVIIDSIQTLWTDMADSAPGTVTQVRSSAQAMIRYAKQTGAAVVLVGHVTKDGQIAGPRVVEHMVDGVLYFEGEGGHHYRILRTVKNRFGPTDEIGVFEMSDGGLREVSNPSELFLGERNEKSPGAAVFAGMEGTRPVLVEIQALV... | Function: DNA-dependent ATPase involved in processing of recombination intermediates, plays a role in repairing DNA breaks. Stimulates the branch migration of RecA-mediated strand transfer reactions, allowing the 3' invading strand to extend heteroduplex DNA faster. Binds ssDNA in the presence of ADP but not other nucl... |
Q9PK96 | MTTTKIKTQWACSECGSYSPKWLGQCPGCFQWNTLVEEIHSSKLKTSSYPLSSTTPVPLNTVKFQEEIRISTRSKGWNRLLGGGTVCGSLTLLGGEPGIGKSTLLLQISSQFAEQGYKVLYVCGEESVSQTSLRAQRLQISSSNIFLFPETNLEDIKQQISDLAPDILIIDSIQIIFSPSLSSAPGSVAQVRETTAELMHIAKQKQITTFIIGHVTKSGEIAGPRILEHLVDTVLYFEGNAHTNYRMIRSVKNRFGPTNELLILSMQTDGLHEVENPSGFFLQEKVVETTGSTIIPIVEGSETLLVEVQALVSSSPFSNP... | Function: DNA-dependent ATPase involved in processing of recombination intermediates, plays a role in repairing DNA breaks. Stimulates the branch migration of RecA-mediated strand transfer reactions, allowing the 3' invading strand to extend heteroduplex DNA faster. Binds ssDNA in the presence of ADP but not other nucl... |
Q9RVC4 | MERVAVLFRRTCNSENCSKGRRPLRERPLAGLFFCSLPAPLSIPCLSLPGSNPGDFVPKVKTNYICNSCGYQSAKPLGRCPNCQAWNSFEEEVPTASTSGKSGRGGLGGYGGVKGGKLTPLSTVGRREEPRTPSGIPELDRVLGGGLVAGGVTLIGGEPGIGKSTLLLQVADKVASRGGTVLYVAGEESLEQIRLRADRLGVAADLQMTRDTRAEHIAALLEEHKPALCIVDSIQTVTVEGEGAPGGVAQVRDGTAMLTRAAKETGTATVLVGHVTKDGTVAGPKVMEHIVDTTVFLETVGAFRLLRSVKNRFGQAGELG... | Function: DNA-dependent ATPase involved in processing of recombination intermediates, plays a role in repairing DNA breaks. Stimulates the branch migration of RecA-mediated strand transfer reactions, allowing the 3' invading strand to extend heteroduplex DNA faster. Binds ssDNA in the presence of ADP but not other nucl... |
P24554 | MAKAPKRAFVCNECGADYPRWQGQCSACHAWNTITEVRLAASPMVARNERLSGYAGSAGVAKVQKLSDISLEELPRFSTGFKEFDRVLGGGVVPGSAILIGGNPGAGKSTLLLQTLCKLAQQMKTLYVTGEESLQQVAMRAHRLGLPTDNLNMLSETSIEQICLIAEEEQPKLMVIDSIQVMHMADVQSSPGSVAQVRETAAYLTRFAKTRGVAIVMVGHVTKDGSLAGPKVLEHCIDCSVLLDGDADSRFRTLRSHKNRFGAVNELGVFAMTEQGLREVSNPSAIFLSRGDEVTSGSSVMVVWEGTRPLLVEIQALVDH... | Function: DNA-dependent ATPase involved in processing of recombination intermediates, plays a role in repairing DNA breaks. Stimulates the branch migration of RecA-mediated strand transfer reactions, allowing the 3' invading strand to extend heteroduplex DNA faster. Binds ssDNA in the presence of ADP but not other nucl... |
P56148 | MAKKTSLFECQHCGFTSPKWLGKCVQCNAWESFIELNQAQKEVLNTLKKPIPQAQKSVSIAAIEHEEVIKFSSTQSELDIVLGGGIAKGGLYLVGGSPGVGKSTLLLKVASGLAKNQQKVLYVSGEESLSQIKMRAIRLDCIEKELYLLNEINWPVIKANIESENYFACVIDSIQTLYSPEISSAPGSISQVREITFELMRLAKTRDIAIFIIGHITKEGSIAGPRVLEHMVDSVLYFEGDPSRELRILRSFKNRFGPTSEIGLFEMKEQGLVSAKEASSLFFSKEEPMEGSAITITLEGSRALILEIQALVSECSFGSP... | Function: DNA-dependent ATPase involved in processing of recombination intermediates, plays a role in repairing DNA breaks. Stimulates the branch migration of RecA-mediated strand transfer reactions, allowing the 3' invading strand to extend heteroduplex DNA faster. Binds ssDNA in the presence of ADP but not other nucl... |
O13034 | MSLQPLTAVNCGSLVQPGFSLLDLEGDVYLFGQKGWPKRSCPTGIFGVRIKKGELKLRAISFSNNSSYLPPLRCPAIAHFEAQDGKPECYLIHGGRTPNNELSSSLYMLSVDSRGCNRKVTLRCEEKELVGDVPSARYGHTLSVINSRGKTACVLFGGRSYMPPTERTTQNWNSVGDCPPQVYLIDLEFGCCTAHTLPELTDGQSFHVALARQDCVYFLGGHILSSDCRPSRLIRLHVELLLGSPVLTCTILHEGLTITSAIASPIGYHEYIIFGGYQSETQKRMECTYVGLDDVGVHMESREPPQWTSEISHSRTWFGG... | Function: Core component of the RAG complex, a multiprotein complex that mediates the DNA cleavage phase during V(D)J recombination. V(D)J recombination assembles a diverse repertoire of immunoglobulin and T-cell receptor genes in developing B and T lymphocytes through rearrangement of different V (variable), in some c... |
P21784 | MSLQMVTVGHNIALIQPGFSLMNFDGQVFFFGQKGWPKRSCPTGVFHFDIKQNHLKLKPAIFSKDSCYLPPLRYPATCSYKGSIDSDKHQYIIHGGKTPNNELSDKIYIMSVACKNNKKVTFRCTEKDLVGDVPEPRYGHSIDVVYSRGKSMGVLFGGRSYMPSTQRTTEKWNSVADCLPHVFLIDFEFGCATSYILPELQDGLSFHVSIARNDTVYILGGHSLASNIRPANLYRIRVDLPLGTPAVNCTVLPGGISVSSAILTQTNNDEFVIVGGYQLENQKRMVCSLVSLGDNTIEISEMETPDWTSDIKHSKIWFGS... | Function: Core component of the RAG complex, a multiprotein complex that mediates the DNA cleavage phase during V(D)J recombination. V(D)J recombination assembles a diverse repertoire of immunoglobulin and T-cell receptor genes in developing B and T-lymphocytes through rearrangement of different V (variable), in some c... |
O04157 | MSTRRRTLLKVIILGDSGVGKTSLMNQYVNNKFSQQYKATIGADFVTKELQIDDRLVTLQIWDTAGQERFQSLGVAFYRGADCCVLVYDVNHLKSFESLDNWHNEFLTRASPRDPMAFPFILLGNKVDIDGGNSRVVSEKKAREWCAEKGNIVYFETSAKEDYNVDDSFLCITKLALANERDQDIYFQPDTGSVPEQRGGCAC | Function: Intracellular vesicle trafficking and protein transport. Functions in autophagy. Involved in xylem and tracheary element differentiation.
Location Topology: Lipid-anchor
Sequence Mass (Da): 22945
Sequence Length: 203
Subcellular Location: Cell membrane
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Q9LW76 | MASRRRVLLKVIILGDSGVGKTSLMNQFVNRKFSNQYKATIGADFLTKEVQIDDRIFTLQIWDTAGQERFQSLGVAFYRGADCCVLVNDVNVMKSFENLNNWREEFLIQASPSDPENFPFVVLGNKTDVDGGKSRVVTEKKAKSWCASKGNIPYFETSAKDGVNVDAAFECIAKNALKNEPEEEVYLPDTIDVAGARQQRSTGCEC | Function: Intracellular vesicle trafficking and protein transport.
Location Topology: Lipid-anchor
Sequence Mass (Da): 22966
Sequence Length: 206
Subcellular Location: Cell membrane
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Q9XI98 | MPSRRRTLLKVIILGDSGVGKTSLMNQYVNKKFSNQYKATIGADFLTKEVQFEDRLFTLQIWDTAGQERFQSLGVAFYRGADCCVLVYDVNSAKSFEDLNNWREEFLIQASPSDPENFPFVVIGNKIDVDGGSSRVVSEKKARAWCASKGNIPYYETSAKVGTNVEDAFLCITTNAMKSGEEEEMYLPDTIDVGTSNPQRSTGCEC | Function: Intracellular vesicle trafficking and protein transport. May play a role in adaptation to stress by recylcing macromolecules in specific cellular compartments.
Location Topology: Lipid-anchor
Sequence Mass (Da): 22980
Sequence Length: 206
Subcellular Location: Cell membrane
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Q9LS94 | MPSRRRTLLKVIILGDSGVGKTSLMNQYVNKKFSNQYKATIGADFLTKEVQFEDRLFTLQIWDTAGQERFQSLGVAFYRGADCCVLVYDVNSMKSFENLNNWREEFLIQASPSDPENFPFVLIGNKVDVDDGNSRVVSEKKAKAWCASKGNIPYFETSAKVGTNVEEAFQCIAKDALKSGEEEELYLPDTIDVGTSNQQRSTGCEC | Function: Essential for trafficking from prevacuolar compartments to vacuoles. Involved in the trafficking of newly synthesized protein to vacuoles. Essential for plant growth . Participates in the recruitment of the core retromer components to the endosomal membrane by interacting with VPS35A .
Location Topology: Lipi... |
O74824 | MRKKVLLMGRSGSGKSSMRSIVFSNYVAKDTRRLGATIDIEHSHVRFLGNLVLNLWDCGGQEAFMENYLSAQRDHIFRNVQVLIYVFDVESREFERDLVTFRNCLEATVANSPQARVFCLIHKMDLVQEDLRDLVFEERKAILLETSKDLETTCLATSIWDETLFKAWSAIVYTLIPNTPTLESHLREFAKAAEAAEVILFERTTFLVISSYSSESNPATDAHRFEKISNIVKQFKLSCSKMQAQFTTFELRGGNFSAFIVPYTEDTYILVVIADPEIESAVTLMNIQSARRFIEASKSASDGIQLQP | Function: GTPase involved in activation of the TORC1 signaling pathway, which promotes growth and represses autophagy in nutrient-rich conditions (By similarity). Also required for TORC1 inactivation during nitrogen starvation (By similarity).
Catalytic Activity: GTP + H2O = GDP + H(+) + phosphate
Location Topology: Pe... |
Q00582 | MSSNNRKKLLLMGRSGSGKSSMRSIIFSNYSAFDTRRLGATIDVEHSHLRFLGNMTLNLWDCGGQDVFMENYFTKQKDHIFQMVQVLIHVFDVESTEVLKDIEIFAKALKQLRKYSPDAKIFVLLHKMDLVQLDKREELFQIMMKNLSETSSEFGFPNLIGFPTSIWDESLYKAWSQIVCSLIPNMSNHQSNLKKFKEIMNALEIILFERTTFLVICSSNGENSNENHDSSDNNNVLLDPKRFEKISNIMKNFKQSCTKLKSGFKTLILNNNIYVSELSSNMVCFIVLKDMNIPQELVLENIKKAKEFFQ | Function: GTPase involved in activation of the TORC1 signaling pathway, which promotes growth and represses autophagy in nutrient-rich conditions . Also required for TORC1 inactivation during nitrogen starvation . Required for intracellular sorting of GAP1 out of the endosome . Functionally associated with the inorgani... |
O74544 | MKPRKIILMGLRRSGKSSIQKVVFYKMPPNETLFLESTSKLTQDHISSFIDFSVWDFPGQVDVFDAAFDFESIFTQVGALIFVIDAQDDYLDALARLHVTVARVVTINPNICIEVFIHKVDGLSDEFKIDTQRDIQQRTQDELADIGLENVPISFHLTSIFDHSIFEAFSRVIQKLIPQLPTLENLLNIFCSNSLVEKAYLFDVLSKIYVATDSSPVDVQSYEICSDFIDVILDIGSIYGRSSQLKPGHSPEILDETSSVIRLSNDLVLFLREMNQYLALICIVRADNFEKSGLIEYNVQCLQTAIQSIFSPRT | Function: GTPase involved in activation of the TORC1 signaling pathway, which promotes growth and represses autophagy in nutrient-rich conditions (By similarity). Also required for TORC1 inactivation during nitrogen starvation (By similarity).
Catalytic Activity: GTP + H2O = GDP + H(+) + phosphate
Location Topology: Pe... |
Q9VZ23 | MAQEGQDIPTFKCVLVGDGGTGKTTFVKRHMTGEFEKKYVATLGVEVHPLIFHTNRGAIRFNVWDTAGQEKFGGLRDGYYIQGQCAVIMFDVTSRVTYKNVPNWHRDLVRVCENIPIVLCGNKVDIKDRKVKAKSIVFHRKKNLQYYDISAKSNYNFEKPFLWLARKLVGDPNLEFVAMPALLPPEVKMDKDWQAQIERDLQEAQATALPDEDEEL | Cofactor: Mg(2+) interacts primarily with the phosphate groups of the bound guanine nucleotide.
Function: GTPase involved in nucleocytoplasmic transport, participating both to the import and the export from the nucleus of proteins and RNAs. Switches between a cytoplasmic GDP- and a nuclear GTP-bound state by nucleotide... |
P62826 | MAAQGEPQVQFKLVLVGDGGTGKTTFVKRHLTGEFEKKYVATLGVEVHPLVFHTNRGPIKFNVWDTAGQEKFGGLRDGYYIQAQCAIIMFDVTSRVTYKNVPNWHRDLVRVCENIPIVLCGNKVDIKDRKVKAKSIVFHRKKNLQYYDISAKSNYNFEKPFLWLARKLIGDPNLEFVAMPALAPPEVVMDPALAAQYEHDLEVAQTTALPDEDDDL | Cofactor: Mg(2+) interacts primarily with the phosphate groups of the bound guanine nucleotide.
Function: GTPase involved in nucleocytoplasmic transport, participating both to the import and the export from the nucleus of proteins and RNAs . Switches between a cytoplasmic GDP- and a nuclear GTP-bound state by nucleotid... |
P62834 | MREYKLVVLGSGGVGKSALTVQFVQGIFVEKYDPTIEDSYRKQVEVDCQQCMLEILDTAGTEQFTAMRDLYMKNGQGFALVYSITAQSTFNDLQDLREQILRVKDTEDVPMILVGNKCDLEDERVVGKEQGQNLARQWCNCAFLESSAKSKINVNEIFYDLVRQINRKTPVEKKKPKKKSCLLL | Function: Induces morphological reversion of a cell line transformed by a Ras oncogene. Counteracts the mitogenic function of Ras, at least partly because it can interact with Ras GAPs and RAF in a competitive manner. Together with ITGB1BP1, regulates KRIT1 localization to microtubules and membranes. Plays a role in ne... |
P32253 | MSKLLKLVIVGDGGVGKSALTIQLTQNQFIAEYDPTIENSYRKQVNIDEEVYMLDILDTAGQEEYSAMRDQYIRSGRGFLIVYSIISRASFEAVTTFREQILRVKDLSTYPIVIIGNKADLPDKDRKVPPMEGKELAKSFGAPFLETSAKSRVNVEEAFFTLVREIKRWNQNPQNEEMLPPKKRGCIIL | Function: Ras proteins bind GDP/GTP and possess intrinsic GTPase activity.
Catalytic Activity: GTP + H2O = GDP + H(+) + phosphate
Location Topology: Lipid-anchor
Sequence Mass (Da): 21496
Sequence Length: 189
Subcellular Location: Cell membrane
EC: 3.6.5.2
|
Q9Y272 | MKLAAMIKKMCPSDSELSIPAKNCYRMVILGSSKVGKTAIVSRFLTGRFEDAYTPTIEDFHRKFYSIRGEVYQLDILDTSGNHPFPAMRRLSILTGDVFILVFSLDNRDSFEEVQRLRQQILDTKSCLKNKTKENVDVPLVICGNKGDRDFYREVDQREIEQLVGDDPQRCAYFEISAKKNSSLDQMFRALFAMAKLPSEMSPDLHRKVSVQYCDVLHKKALRNKKLLRAGSGGGGGDPGDAFGIVAPFARRPSVHSDLMYIREKASAGSQAKDKERCVIS | Function: Small GTPase. Negatively regulates the transcription regulation activity of the APBB1/FE65-APP complex via its interaction with APBB1/FE65 (By similarity).
PTM: S-nitrosylation stimulates guanine-nucleotide exchange activity.
Location Topology: Lipid-anchor
Sequence Mass (Da): 31642
Sequence Length: 281
Subce... |
P03967 | MTEYKLVIVGGGGVGKSALTIQLIQNHFIDEYDPTIEDSYRKQVSIDDETCLLDILDTAGQEEYSAMRDQYMRTGQGFLCVYSITSRSSYDEIASFREQILRVKDKDRVPLILVGNKADLDHERQVSVNEGQELAKGFNCPFMESSAKSRINVEEAFYSLVREIRKELKGDQSSGKAQKKKKQCLIL | Function: Ras proteins bind GDP/GTP and possess intrinsic GTPase activity.
Catalytic Activity: GTP + H2O = GDP + H(+) + phosphate
Location Topology: Lipid-anchor
Sequence Mass (Da): 21202
Sequence Length: 187
Subcellular Location: Cell membrane
EC: 3.6.5.2
|
Q8THK1 | MSLNKAVLEIRQRIKVKPSPTNEPAASWTGTDLVNGVQTKTLTVIFKSAGCRWGKAGGCTMCGYVYDCASEPPSLEDYMAQLEKAMRKAEKFPEFMVKIFTSGSFLDEQEVLPEARDAILKNLTEDPRVTKVLVETRPNYVTEENVQACLSILKNKPFELAFGLETSSDKIRRDSINKGFTFQDFVHAAETAKKYGVTVKVYLMLKPLFLSERQAMEDIIRSIDDAAPYADTISINLCNVQKGTLVEALWEKGQYRPPWLWSIIEILRQAKAAHPELPLMSDPVGAGSKRGPHNCKICSSEVADSLRTFSLTQNPADLST... | Cofactor: Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine.
Function: Radical SAM enzyme involved in the synthesis of archaeosine, a modified nucleoside present in the dihydrouridine loop (D-loop) of archaeal tRNAs. Catalyzes the cleavage of the C(epsilon... |
Q5JE80 | MTYWTSEDNVAGKPGTALFIILPTIGCYRYRIGQACYMCSYPTAAPKVKWTQEAIVNYVKEALEKIEGTEGPFAVRMFTSGSFLDNGELKPETRRKIFEILAEMDNVEEIVIESRSELVRYEAVKELAEIVPDKHFEVAIGLETANDDVADVSINKGNTFADFVKAAEITHKAGAKVKTYLLLKPIFLSERDGVEDAKESIIKAEPYTDTFSINITDIQKGTLYERLWEKKEYRPPWLWSAVEVLIWAKRKFPNKRILSDPVGAGSKRGPHNCLTDYDRVIGKAIKKFSATQDLSYIENLKPECRDRWEYIVENGLLDWQ... | Cofactor: Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine.
Function: Radical SAM enzyme involved in the synthesis of archaeosine, a modified nucleoside present in the dihydrouridine loop (D-loop) of archaeal tRNAs. Catalyzes the cleavage of the C(epsilon... |
Q7Z444 | MELPTKPGTFDLGLATWSPSFQGETHRAQARRRDVGRQLPEYKAVVVGASGVGKSALTIQLNHQCFVEDHDPTIQDSYWKELTLDSGDCILNVLDTAGQAIHRALRDQCLAVCDGVLGVFALDDPSSLIQLQQIWATWGPHPAQPLVLVGNKCDLVTTAGDAHAAAAALAHSWGAHFVETSAKTRQGVEEAFSLLVHEIQRVQEAMAKEPMARSCREKTRHQKATCHCGCSVA | Function: Ras proteins bind GDP/GTP and possess intrinsic GTPase activity. Plays an important role in the tumor-like growth properties of embryonic stem cells (By similarity).
Catalytic Activity: GTP + H2O = GDP + H(+) + phosphate
Location Topology: Lipid-anchor
Sequence Mass (Da): 25287
Sequence Length: 233
Subcellula... |
Q7TN89 | MALPTKSSILDLSSGTPCTRSPEESHEAWAQCKDAGRQLPEYKAVVVGASGVGKSALTIQMTHQCFVKDHDPTIQDSYWKEVARDNGGYILNVLDTSGQDIHRALRDQCLASGDGVLGVFALDDPSSLDQLQQIWSTWTPHHKQPLVLVGNKCDLVTTAGDAHAAAALLAHKLGAPLVKTSAKTRQGVEEAFALLVHEIQRAQEAVAESSKKTRHQKAVCSCGCSVA | Function: Ras proteins bind GDP/GTP and possess intrinsic GTPase activity. Plays an important role in the tumor-like growth properties of embryonic stem cells.
Catalytic Activity: GTP + H2O = GDP + H(+) + phosphate
Location Topology: Lipid-anchor
Sequence Mass (Da): 24321
Sequence Length: 227
Subcellular Location: Cell... |
Q15907 | MGTRDDEYDYLFKVVLIGDSGVGKSNLLSRFTRNEFNLESKSTIGVEFATRSIQVDGKTIKAQIWDTAGQERYRAITSAYYRGAVGALLVYDIAKHLTYENVERWLKELRDHADSNIVIMLVGNKSDLRHLRAVPTDEARAFAEKNNLSFIETSALDSTNVEEAFKNILTEIYRIVSQKQIADRAAHDESPGNNVVDISVPPTTDGQKPNKLQCCQNL | Function: The small GTPases Rab are key regulators of intracellular membrane trafficking, from the formation of transport vesicles to their fusion with membranes. Rabs cycle between an inactive GDP-bound form and an active GTP-bound form that is able to recruit to membranes different set of downstream effectors directl... |
P46638 | MGTRDDEYDYLFKVVLIGDSGVGKSNLLSRFTRNEFNLESKSTIGVEFATRSIQVDGKTIKAQIWDTAGQERYRAITSAYYRGAVGALLVYDIAKHLTYENVERWLKELRDHADSNIVIMLVGNKSDLRHLRAVPTDEARAFAEKNNLSFIETSALDSTNVEEAFKNILTEIYRIVSQKQIADRAAHDESPGNNVVDISVPPTTDGQRPNKLQCCQSL | Function: The small GTPases Rab are key regulators of intracellular membrane trafficking, from the formation of transport vesicles to their fusion with membranes. Rabs cycle between an inactive GDP-bound form and an active GTP-bound form that is able to recruit to membranes different set of downstream effectors directl... |
Q9LET3 | MNGGPSGFHNAPVTKAFVITSALFTVFFGIQGRSSKLGLSYQDIFEKFRIWKLIMSTFAFSSTPELMFGLYLLYYFRVFERQIGSNKYSVFILFSGTVSLLLEVILLSLLKDTTANLLTSGPYGLIFASFIPFYLDIPVSTRFRVFGVNFSDKSFIYLAGVQLLLSSWKRSIFPGICGIIAGSLYRLNILGIRKAKFPEFVASFFSRLSFPSFGNSPPPAPSRNIVGTISPNTGRRAERSQPAPLPSSVEPSEEAITTLVSMGFDRNAARQALVHARNDVNAATNILLEAQSH | Function: Probable rhomboid-type serine protease that catalyzes intramembrane proteolysis.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 32378
Sequence Length: 293
Subcellular Location: Membrane
|
Q9CAN1 | MANRDVERVGKKNRGANNNYFYEESSGETHWTSWLIPAIVVANLAVFIAVMFVNDCPKKITGPNKECVARFLGRFSFQPLKENPLFGPSSSTLEKMGALEWRKVVHEHQGWRLLSCMWLHAGIIHLLTNMLSLIFIGIRLEQQFGFIRVGLIYLISGLGGSILSSLFLQESISVGASGALFGLLGAMLSELLTNWTIYANKAAALITLLFIIAINLALGMLPRVDNFAHIGGFLTGFCLGFVLLVRPQYGWEASRTNTSRTKRKYSMYQYVLFVVSVVLLVVGLTVALVMLFKGENGNKHCKWCHYLSCFPTSKWTC | Function: Rhomboid-type serine protease that catalyzes intramembrane proteolysis. Can cleave the Drosophila proteins Spitz and Keren . May function in pollen elongation .
Catalytic Activity: Cleaves type-1 transmembrane domains using a catalytic dyad composed of serine and histidine that are contributed by different tr... |
O58677 | MMVLRMKVEWYLDFVDLNYEPGRDELIVEYYFEPNGVSPEEAAGRIASESSIGTWTTLWKLPEMAKRSMAKVFYLEKHGEGYIAKIAYPLTLFEEGSLVQLFSAVAGNVFGMKALKNLRLLDFHPPYEYLRHFKGPQFGVQGIREFMGVKDRPLTATVPKPKMGWSVEEYAEIAYELWSGGIDLLKDDENFTSFPFNRFEERVRKLYRVRDRVEAETGETKEYLINITGPVNIMEKRAEMVANEGGQYVMIDIVVAGWSALQYMREVTEDLGLAIHAHRAMHAAFTRNPRHGITMLALAKAARMIGVDQIHTGTAVGKMA... | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Catalyzes the addition of molecular CO(2) and H(2)O to ribulose 1,5-bisphosphate (RuBP), generating two molecules of 3-phosphoglycerate (3-PGA). Functions in an archaeal AMP degradation pathway, together with AMP phosphorylase and R15P isomerase.
Catalytic Activity: 2... |
P31200 | MSPQTETKASVGFKAGVKDYKLTYYTPEYETKDTDILAAFRVTPQPGVPPEEAGQAVA | Function: RuBisCO catalyzes two reactions: the carboxylation of D-ribulose 1,5-bisphosphate, the primary event in carbon dioxide fixation, as well as the oxidative fragmentation of the pentose substrate in the photorespiration process. Both reactions occur simultaneously and in competition at the same active site (By s... |
Q96T37 | MRTAGRDPVPRRSPRWRRAVPLCETSAGRRVTQLRGDDLRRPATMKGKERSPVKAKRSRGGEDSTSRGERSKKLGGSGGSNGSSSGKTDSGGGSRRSLHLDKSSSRGGSREYDTGGGSSSSRLHSYSSPSTKNSSGGGESRSSSRGGGGESRSSGAASSAPGGGDGAEYKTLKISELGSQLSDEAVEDGLFHEFKRFGDVSVKISHLSGSGSGDERVAFVNFRRPEDARAAKHARGRLVLYDRPLKIEAVYVSRRRSRSPLDKDTYPPSASVVGASVGGHRHPPGGGGGQRSLSPGGAALGYRDYRLQQLALGRLPPPPP... | Function: RNA-binding protein that acts as a key regulator of N6-methyladenosine (m6A) methylation of RNAs, thereby regulating different processes, such as hematopoietic cell homeostasis, alternative splicing of mRNAs and X chromosome inactivation mediated by Xist RNA . Associated component of the WMM complex, a comple... |
Q0VBL3 | MRSAGREPLPRRSPRWRRASPLCETSAGWRVSQLRRDDLRRPSTMKGKERSPVKPKRSRGGEDSSSRGERSKKLGGSGGSNGSSSGKTDSGGSRRSLHLDKSSSRGGSREYETGGGSSSSRLHSYSSPSTKNSSGGGESRSSSRGGGGESRSSGAASSAPGGGDGVEYKTLKISELGSQLSDEAVEDGLFHEFKRFGDVSVKISHLSGSGSGDERVAFVNFRRPEDARAAKHARGRLVLYDRPLKIEAVYVSRRRSRSPLDKDAYAPSSSVVGTSVGSHRHAPGGGGGQRSLSPGGAALGYRDYRLQQLALGRLPPPPPP... | Function: RNA-binding protein that acts as a key regulator of N6-methyladenosine (m6A) methylation of RNAs, thereby regulating different processes, such as hematopoietic cell homeostasis, alternative splicing of mRNAs and X chromosome inactivation mediated by Xist RNA . Associated component of the WMM complex, a comple... |
A7GLA2 | MKKHGVLNSEIAAILAALGHTDTIVIADCGLPIPDSVKRIDLAVELGKPSFLDVLQVVIEDMAIEKVTVAEEITTNNREIYKEIETRLKEANFEYVLHEEFKEKTKQAKAIIRTGEATPYANIILHAGVIF | Function: Catalyzes the interconversion of beta-pyran and beta-furan forms of D-ribose.
Catalytic Activity: beta-D-ribopyranose = beta-D-ribofuranose
Sequence Mass (Da): 14542
Sequence Length: 131
Pathway: Carbohydrate metabolism; D-ribose degradation; D-ribose 5-phosphate from beta-D-ribopyranose: step 1/2.
Subcellula... |
P36946 | MKKHGILNSHLAKILADLGHTDKIVIADAGLPVPDGVLKIDLSLKPGLPAFQDTAAVLAEEMAVEKVIAAAEIKASNQENAKFLENLFSEQEIEYLSHEEFKLLTKDAKAVIRTGEFTPYANCILQAGVLF | Function: Catalyzes the interconversion of beta-pyran and beta-furan forms of D-ribose.
Catalytic Activity: beta-D-ribopyranose = beta-D-ribofuranose
Sequence Mass (Da): 14227
Sequence Length: 131
Pathway: Carbohydrate metabolism; D-ribose degradation; D-ribose 5-phosphate from beta-D-ribopyranose: step 1/2.
Subcellula... |
Q7NTN5 | MKKHGHLNRDIARILASMGHTDSLVIADCGLPIPPGVECVDLSLKLGQPGFIETLDSILADFQCERAVFAIECRQHNPAVQDKAERMAQAGAALDFVSHEEFKQRCQAARAVIRTGECTPYANVILHSGVIF | Function: Catalyzes the interconversion of beta-pyran and beta-furan forms of D-ribose.
Catalytic Activity: beta-D-ribopyranose = beta-D-ribofuranose
Sequence Mass (Da): 14412
Sequence Length: 132
Pathway: Carbohydrate metabolism; D-ribose degradation; D-ribose 5-phosphate from beta-D-ribopyranose: step 1/2.
Subcellula... |
Q88RZ3 | MNTTALLIGLGPLLGWGLYPTIASKIGGRPVNQILGSTIGTLIFALIYAWVQGIAFPSGMNLWFSILSGIGWASAQIVTFKVFTMVGSSRAMPITTAFQLLGASLWGVFALGDWPGAMDKVLGGLALVGIIIGAWLTVWSEHKDAGNARTLRQAVIWLAVGEIGYWAYSAAPQATNIGGEEAFVPQAIGMVIVSIVYALFLASRGEKLALVEGVSYTHIISGFFFAFAALTYLISAQPNMNGLATGFILSQTSVVLATLTGIWFLGQKKTTKEMWVTIGGLILIIAAAAVTVTI | Function: Could be involved in the uptake of ribose.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 31049
Sequence Length: 294
Subcellular Location: Cell membrane
|
Q9X4M3 | MNAVNILIGLMPMIGWGIFPVIVGKIGGKPASQILGTTFGTLILAIVVAIFRGTPIPETKTFIFCLISGACWALAQIITFHVFETMGVSRTMPITTGFQLVGASLWGVFVLGNWSSSQSKLIGFTAIALIIIGVYLTAWSEDKSSASKSGAVKGILLLLVGELGYLGYSAFPQAVSADGFQGFLPQAIGMTIVGIIFGLTQTKKDYKPFKEATSYKNIFSGFFFAFAALTYLISAQPSVNGLATGFVLSQTSVIFATIGGIYILKEKKSKKEMIAVMVGLLLVLVAGSVTAFIK | Function: Could be involved in the uptake of ribose.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 31169
Sequence Length: 294
Subcellular Location: Cell membrane
|
O00559 | MAITQFRLFKFCTCLATVFSFLKRLICRSGRGRKLSGDQITLPTTVDYSSVPKQTDVEEWTSWDEDAPTSVKIEGGNGNVATQQNSLEQLEPDYFKDMTPTIRKTQKIVIKKREPLNFGIPDGSTGFSSRLAATQDLPFIHQSSELGDLDTWQENTNAWEEEEDAAWQAEEVLRQQKLADREKRAAEQQRKKMEKEAQRLMKKEQNKIGVKLS | Function: May participate in suppression of cell proliferation and induces apoptotic cell death through activation of interleukin-1-beta converting enzyme (ICE)-like proteases.
Location Topology: Single-pass type III membrane protein
Sequence Mass (Da): 24377
Sequence Length: 213
Domain: The coiled coil domain is neces... |
Q5PQP2 | MAITQFRLFKVCTCLATVLSFLKRLICRSGRGRKLSGDQITLPTTVDYSSVPKQTDVEEWTSWDEDAPTSVKIEGGTGNAAAQQNSLEQLEPDYFKDMTPTIRKTQKIVIKKREPLSFGVPDGSTGFSSRLAATQDMPFIHQSSELGDLDTWQENSNAWEEEEDAAWQAEEVLRQQKIADREKRAAEQQRKKMEKEAQRLLKKEQNKMGVKLS | Function: May participate in suppression of cell proliferation and induces apoptotic cell death through activation of interleukin-1-beta converting enzyme (ICE)-like proteases.
Location Topology: Single-pass type III membrane protein
Sequence Mass (Da): 24187
Sequence Length: 213
Domain: The coiled coil domain is neces... |
P10896 | MAAAVSTVGAINRAPLSLNGSGSGAVSAPASTFLGKKVVTVSRFAQSNKKSNGSFKVLAVKEDKQTDGDRWRGLAYDTSDDQQDITRGKGMVDSVFQAPMGTGTHHAVLSSYEYVSQGLRQYNLDNMMDGFYIAPAFMDKLVVHITKNFLTLPNIKVPLILGIWGGKGQGKSFQCELVMAKMGINPIMMSAGELESGNAGEPAKLIRQRYREAADLIKKGKMCCLFINDLDAGAGRMGGTTQYTVNNQMVNATLMNIADNPTNVQLPGMYNKEENARVPIICTGNDFSTLYAPLIRDGRMEKFYWAPTREDRIGVCKGIF... | Function: Activation of RuBisCO (ribulose-1,5-bisphosphate carboxylase/oxygenase; EC 4.1.1.39) involves the ATP-dependent carboxylation of the epsilon-amino group of lysine leading to a carbamate structure.
PTM: Phosphorylated at Thr-78 by CK2.
Sequence Mass (Da): 51981
Sequence Length: 474
Subcellular Location: Plasti... |
P38623 | MLKIKALFSKKKPDQADLSQESKKPFKGKTRSSGTNNKDVSQITSSPKKSFQDKNIVQYPSVVADDHHMKSLTDELVTTIDSDSSPSDNITTENVETVTSVPAIDVHESSEGQLSSDPLISDESLSEQSEIISDIQDDSTDDDNMEDEIPEKSFLEQKELIGYKLINKIGEGAFSKVFRAIPAKNSSNEFLTKNYKAVAIKVIKKADLSSINGDHRKKDKGKDSTKTSSRDQVLKEVALHKTVSAGCSQIVAFIDFQETDSYYYIIQELLTGGEIFGEIVRLTYFSEDLSRHVIKQLALAVKHMHSLGVVHRDIKPENLL... | Function: Serine/threonine-protein kinase involved in a signal transduction pathway that is activated by changes in the osmolarity of the extracellular environment.
PTM: Autophosphorylated. Phosphorylated by HOG1 at Ser-520 after osmotic stress.
Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-ser... |
P75685 | MEKYLHLLSRGDKIGLTLIRLSIAIVFMWIGLLKFVPYEADSITPFVANSPLMSFFYEHPEDYKQYLTHEGEYKPEARAWQTANNTYGFSNGLGVVEVIIALLVLANPVNRWLGLLGGLMAFTTPLVTLSFLITTPEAWVPALGDAHHGFPYLSGAGRLVLKDTLMLAGAVMIMADSAREILKQRSNESSSTLKTEY | Function: Probably involved in reactive chlorine species (RCS) stress resistance.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 21899
Sequence Length: 197
Subcellular Location: Cell inner membrane
|
O14039 | MDFYNHAANILSDLSKKKGSIKQLAFNSKKHDPKRTYALVCETLKYKPVLDEIIARSELLVLEKKLKENLARVLVHDLLMSKRGLSISNGPIKECILRHKTRLNAEFVKLKVKKGVKSHEELALKNPVSLPRWLRINTIKSTKDEVLQGLGLDKVSSIEELGPDKFYIDDCVENLIAIDPSFPIVENSLYKEGKVIIQDKASCFPAAVLAGLTGHVGDIIDGCAAPGNKTTHLAACFPKSHIFAFERDAKRVQTLRKMVGISGANNVTIEHQDFTLTDPKSDLYRNVTHILLDPSCSGSGIVSRQDYLLGNEQDVTEDTE... | Function: S-adenosyl-L-methionine-dependent methyltransferase that specifically methylates the C(5) position of a cytosine in 25S rRNA.
Catalytic Activity: a cytidine in 25S rRNA + S-adenosyl-L-methionine = a 5-methylcytidine in 25S rRNA + H(+) + S-adenosyl-L-homocysteine
Sequence Mass (Da): 51877
Sequence Length: 460
... |
P53972 | MNFYRDATWVLEDIEKEAAKERISGSMQTLVLKSCKRYKLKSNPKHIYAVLDSCWKYKPYLEKVMKKAHILEDIPKKKGKPLFSRLTLLLLCHDLLLSKQKRIQMGKHPIKDYVLKFKSPLHSEMVKLKLKLKVRELSELVLSEDISNDLPPVRWIRINPLKCHPNGETEPVLAELRKKFTLKVDKWSELVPGSIYYDEFIPNLFGIHPSDKITAHELYKHGKIIIQDRASCFPAHILNPGPSDIVIDSCSAPGNKTTHTASYIYPEPPKDNNTRIYAFEKDPERAKVLQKMIKIAGCSPNISVNVGDFTKLATPEKYKD... | Function: S-adenosyl-L-methionine-dependent methyltransferase that specifically methylates the C(5) position of cytosine 2278 (m5C2278) in 25S rRNA . Loss of m5C2278 in 25S rRNA results in anisomycin hypersensitivity .
Catalytic Activity: cytidine(2278) in 25S rRNA + S-adenosyl-L-methionine = 5-methylcytidine(2278) in ... |
Q92781 | MWLPLLLGALLWAVLWLLRDRQSLPASNAFVFITGCDSGFGRLLALQLDQRGFRVLASCLTPSGAEDLQRVASSRLHTTLLDITDPQSVQQAAKWVEMHVKEAGLFGLVNNAGVAGIIGPTPWLTRDDFQRVLNVNTMGPIGVTLALLPLLQQARGRVINITSVLGRLAANGGGYCVSKFGLEAFSDSLRRDVAHFGIRVSIVEPGFFRTPVTNLESLEKTLQACWARLPPATQAHYGGAFLTKYLKMQQRIMNLICDPDLTKVSRCLEHALTARHPRTRYSPGWDAKLLWLPASYLPASLVDAVLTWVLPKPAQAVY | Function: Catalyzes the oxidation of cis-isomers of retinol, including 11-cis-, 9-cis-, and 13-cis-retinol in an NAD-dependent manner . Has no activity towards all-trans retinal (By similarity). Plays a significant role in 11-cis retinol oxidation in the retinal pigment epithelium cells (RPE). Also recognizes steroids ... |
O55240 | MWLPLLLGALLWAVLWLLRDRQSLPASDAFIFITGCDSGFGRLLALQLDQKGFQVLAGCLTPSGAEDLQQMASSRLHTTLLDITDPQNVQQVAKWVKTRVGETGLFGLVNNAGVAGIIGPTPWLTQDDFQRVLSVNTLGPIGVTLALLPLLQQARGRVVNITSVLGRIAANGGGYCVSKFGLEAFSDSLRRDMAPFGVQVSIVEPGFFRTPVTNLESLESTLKACWARLPPAIQAHYGEAFLDTYLRVQRRIMNLICDPELTKVTSCLEHALTARHPRTRYSPGWDAKLLWLPASYLPARVVDAVLTWILPRPAQSVS | Function: Catalyzes the oxidation of cis-isomers of retinol, including 11-cis-, 9-cis-, and 13-cis-retinol in an NAD-dependent manner . Has no activity towards all-trans retinal (By similarity). Plays a significant role in 11-cis retinol oxidation in the retinal pigment epithelium cells (RPE). Also recognizes steroids ... |
Q9N126 | MADAPRTVLISGCSSGIGLELAVQLAHDPRQRYQVVATMRDLGKKGTLETAAGEALGQTLTVAQLDVCSDESVAQCLNCIQGGEVDVLVNNAGVGLVGPLEGLSLAAMQNVFDTNFFGAVRLVKAVLPSMKRRRQGHIVVVSSVMGLQGVVFNEVYAASKFAMEGFFESLAVQLLQFNIFISLVEPGPVVTEFEGKLLEQVSTAEFPGTDPDTLSYFRDLYLPASRELFHNVGQSPQDVAKVIVKVIGSARPPLRRRTNTRYTPLIALKAMDPSGSLYVRTSHCLLFRWPRLLNLGLRCLACSCFRTPVWPR | Function: Retinol dehydrogenase with a clear preference for NADP. Converts all-trans-retinal to all-trans-retinol. May play a role in the regeneration of visual pigment at high light intensity.
Catalytic Activity: all-trans-retinol + NADP(+) = all-trans-retinal + H(+) + NADPH
Location Topology: Multi-pass membrane prot... |
Q9NYR8 | MAAAPRTVLISGCSSGIGLELAVQLAHDPKKRYQVVATMRDLGKKETLEAAAGEALGQTLTVAQLDVCSDESVAQCLSCIQGEVDVLVNNAGMGLVGPLEGLSLAAMQNVFDTNFFGAVRLVKAVLPGMKRRRQGHIVVISSVMGLQGVIFNDVYAASKFALEGFFESLAIQLLQFNIFISLVEPGPVVTEFEGKLLAQVSMAEFPGTDPETLHYFRDLYLPASRKLFCSVGQNPQDVVQAIVNVISSTRPPLRRQTNIRYSPLTTLKTVDSSGSLYVRTTHRLLFRCPRLLNLGLQCLSCGCLPTRVRPR | Function: Retinol dehydrogenase with a clear preference for NADP. Converts all-trans-retinal to all-trans-retinol. May play a role in the regeneration of visual pigment at high light intensity (By similarity).
Catalytic Activity: all-trans-retinol + NADP(+) = all-trans-retinal + H(+) + NADPH
Location Topology: Multi-pa... |
Q8N3Y7 | MSFNLQSSKKLFIFLGKSLFSLLEAMIFALLPKPRKNVAGEIVLITGAGSGLGRLLALQFARLGSVLVLWDINKEGNEETCKMAREAGATRVHAYTCDCSQKEGVYRVADQVKKEVGDVSILINNAGIVTGKKFLDCPDELMEKSFDVNFKAHLWTYKAFLPAMIANDHGHLVCISSSAGLSGVNGLADYCASKFAAFGFAESVFVETFVQKQKGIKTTIVCPFFIKTGMFEGCTTGCPSLLPILEPKYAVEKIVEAILQEKMYLYMPKLLYFMMFLKSFLPLKTGLLIADYLGILHAMDGFVDQKKKL | Function: Oxidoreductase with strong preference for NAD . Active in both the oxidative and reductive directions . Oxidizes all-trans-retinol in all-trans-retinaldehyde . No activity was detected with 11-cis-retinol or 11-cis-retinaldehyde as substrates with either NAD(+)/NADH or NADP(+)/NADPH .
Catalytic Activity: all-... |
Q12305 | MWKAVMNAWNGTESQSKNVSNIQSYSFEDMKRIVGKHDPNVVLVDVREPSEYSIVHIPASINVPYRSHPDAFALDPLEFEKQIGIPKPDSAKELIFYCASGKRGGEAQKVASSHGYSNTSLYPGSMNDWVSHGGDKLDL | Function: Thiosulfate:glutathione sulfurtransferase (TST) required to produce S-sulfanylglutathione (GSS(-)), a central intermediate in hydrogen sulfide metabolism . Provides the link between the first step in H(2)S metabolism performed by the sulfide:quinone oxidoreductase (SQOR) which catalyzes the conversion of H(2)... |
Q08742 | MFKHSTGILSRTVSARSPTLVLRTFTTKAPKIYTFDQVRNLVEHPNDKKLLVDVREPKEVKDYKMPTTINIPVNSAPGALGLPEKEFHKVFQFAKPPHDKELIFLCAKGVRAKTAEELARSYGYENTGIYPGSITEWLAKGGADVKPKK | Function: Thiosulfate sulfurtransferase which catalyzes the transfer of sulfane sulfur from thiosulfate to cyanide.
Catalytic Activity: hydrogen cyanide + thiosulfate = 2 H(+) + sulfite + thiocyanate
Sequence Mass (Da): 16697
Sequence Length: 149
Subcellular Location: Mitochondrion
EC: 2.8.1.1
|
Q934F8 | MIKKVVAYAAIAASVMGASAAAAPQAMAIGDDSGPVSANGNGASQYFGNSMTTGNMSPQMALIQGSFNKPCIAVSDIPVSVIGLVPIQDLNVLGDDMNQQCAENSTQAKRDGALAHLLEDVSILSSNGEGGKG | Function: Forms part of the rodlet layer on the spore surface; despite their high similarity both RdlA and RdlB are required for rodlet formation . Plays a role in cell adhesion to polystyrene plates . Forms amyloid-like fibrils in vitro composed of stacked beta-sheets .
Sequence Mass (Da): 13355
Sequence Length: 133
D... |
Q10215 | MFSKTLSVSRLLMTRSFYSSTVVKNVSIFDFEKVYNLSKRPTGDKSTVLIDVREPDEFKQGAIETSYNLPVGKIEEAMKLSDEEFSKTYGFSKPVFEDNVVVYCRSGRRSTTASDILTKLGYKNIGNYTGSWLEWSDKIKSK | Function: Thiosulfate sulfurtransferase which catalyzes the transfer of sulfane sulfur from thiosulfate to cyanide.
Catalytic Activity: hydrogen cyanide + thiosulfate = 2 H(+) + sulfite + thiocyanate
Sequence Mass (Da): 16185
Sequence Length: 142
Subcellular Location: Mitochondrion
EC: 2.8.1.1
|
P34057 | MGNSKSGALSKEILEELQLNTKFTEEELSAWYQSFLKECPSGRITRQEFESIYSKFFPDSDPKAYAQHVFRSFDANSDGTLDFKEYVIALHMTTAGKPTQKLEWAFSLYDVDGNGTISKNEVLEIVMAIFKMIKPEDVKLLPDDENTPEKRAEKIWAFFGKKEDDKLTEEEFIEGTLANKEILRLIQFEPQKVKERIKEKKQ | Function: Acts as a calcium sensor and regulates phototransduction of cone and rod photoreceptor cells (By similarity). Modulates light sensitivity of cone photoreceptor in dark and dim conditions . In response to high Ca(2+) levels induced by low light levels, prolongs RHO/rhodopsin activation in rod photoreceptor cel... |
P0AG22 | MVAVRSAHINKAGEFDPEKWIASLGITSQKSCECLAETWAYCLQQTQGHPDASLLLWRGVEMVEILSTLSMDIDTLRAALLFPLADANVVSEDVLRESVGKSVVNLIHGVRDMAAIRQLKATHTDSVSSEQVDNVRRMLLAMVDDFRCVVIKLAERIAHLREVKDAPEDERVLAAKECTNIYAPLANRLGIGQLKWELEDYCFRYLHPTEYKRIAKLLHERRLDREHYIEEFVGHLRAEMKAEGVKAEVYGRPKHIYSIWRKMQKKNLAFDELFDVRAVRIVAERLQDCYAALGIVHTHYRHLPDEFDDYVANPKPNGYQ... | 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 formation of pppGpp which is then hydrolyzed to form ppGpp (By similarity).
Catalyt... |
P9WHG8 | MTAQRSTTNPVLEPLVAVHREIYPKADLSILQRAYEVADQRHASQLRQSGDPYITHPLAVANILAELGMDTTTLVAALLHDTVEDTGYTLEALTEEFGEEVGHLVDGVTKLDRVVLGSAAEGETIRKMITAMARDPRVLVIKVADRLHNMRTMRFLPPEKQARKARETLEVIAPLAHRLGMASVKWELEDLSFAILHPKKYEEIVRLVAGRAPSRDTYLAKVRAEIVNTLTASKIKATVEGRPKHYWSIYQKMIVKGRDFDDIHDLVGVRILCDEIRDCYAAVGVVHSLWQPMAGRFKDYIAQPRYGVYQSLHTTVVGPE... | Cofactor: Binds 1 Mg(2+) ion per subunit.
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 both the formation of pppGpp, which is then h... |
O52177 | MWGNVAPPLVQSYDCSSFDDSPERHPPTVSQYHPDPDLDIIKKAYVYSAKVHQGQLRKSGEPYLVHPLEVAGILGELKLDEASIVTGLLHDTIEDTLATEEELTELFGSEVAHLVDGVTKLSKFSASASLSQEEKQAENFRKMIIAMAQDIRVILVKLADRTHNMRTLDHMSEEKQARIAQETLDIYAPLANRLGISWIKTELEDLSFRYVKPQEFFALQAKLNKRKKEREKYIEDTCDLIRSKLAERGLKGEVSGRFKHVYSIYKKIKSQGIDFDQIHDIIAFRIIAPTAPSCYEALGLVHEMWKPVPGRFKDFIAIPK... | 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 formation of pppGpp which is then hydrolyzed to form ppGpp (By similarity).
Catalyt... |
P55133 | MVAVRGAHLKENTTFELVSWVESLRQDAKVSSRIEGTYQRCIELAAEQENGPLLLWRGRELVEILVTLSMDADTLIAALLYPLVEGGCYSTDALKEEYSGTILHLVQGVEQMCAISQLKSTAEETAQAAQVDNIRRMLLSMVDDFRCVVIKLAERICNLREVKDQPDEVRRAAAQECANIYAPLANRLGIGQLKWEIEDYAFRYQHPDTYKQIAKQLSERRIDREDYITHFVDDLSDAMKASNIRAEVQGRPKHIYSIWRKMQKKSLEFDELFDVRAVRIVAEELQDCYAALGVVHTKYRHLPKEFDDYVANPKPNGYQS... | 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 formation of pppGpp which is then hydrolyzed to form ppGpp. Also plays a role in th... |
Q9TSZ1 | MDAWRGMPRWGLLLLLWGSCTFGLPTETTTFKRISLKRMPSIRESLKERGVDMARLGPERMALVNITSSVILTNYMDTQYYGEIGIGTPPQTFKVVFDTGSSNVWVPSSKCSRLYTACVYHKLFDASDSSSYKHNGTELTLRYSTGTVSGFLSQDVITVGGITVTQTFGEVTEMPALPFMLAEFDGVVGMGFSEQAIGKVTPLFDNIISQGLLKEDVFSFYYNRDSENSQSLGGQIVLGGSDPQHYEGNFHYINLIRTGLWQIPMKGVSVGSSTLLCEDGCLALVDTGASYISGSTSSIEKLMEALGAKKRLFDYVVKCN... | Function: Renin is a highly specific endopeptidase, whose only known function is to generate angiotensin I from angiotensinogen in the plasma, initiating a cascade of reactions that produce an elevation of blood pressure and increased sodium retention by the kidney.
Catalytic Activity: Cleavage of Leu-|-Xaa bond in ang... |
Q6DYE7 | MARCRMPRWGLLLVLWGSCTFGLPADTGAFRRIFLKKMPSIRESLKERGVDVAGLGAEWNQFTKRLSSGNSTSPVVLTNYLDTQYYGEIGIGTPPQTFKVVFDTGSANLWVPSTRCSPLYTACEIHCLYDSSESSSYMENGTTFTIRYGSGKVKGFLSQDMVTVGGITVTQTFGEVTELPLIPFMLAKFDGVLGMGFPAQAVGGVTPVFDHILSQGVLKEEVFSVYYSRNSHLLGGEVVLGGSDPQYYQGNFHYVSISKTGSWQIKMKGVSVRSATLVCEEGCMVVVDTGASYISGPTSSLRLLMDTLGAQELSTNEYVV... | Function: Renin is a highly specific endopeptidase, whose only known function is to generate angiotensin I from angiotensinogen in the plasma, initiating a cascade of reactions that produce an elevation of blood pressure and increased sodium retention by the kidney.
Catalytic Activity: Cleavage of Leu-|-Xaa bond in ang... |
P00797 | MDGWRRMPRWGLLLLLWGSCTFGLPTDTTTFKRIFLKRMPSIRESLKERGVDMARLGPEWSQPMKRLTLGNTTSSVILTNYMDTQYYGEIGIGTPPQTFKVVFDTGSSNVWVPSSKCSRLYTACVYHKLFDASDSSSYKHNGTELTLRYSTGTVSGFLSQDIITVGGITVTQMFGEVTEMPALPFMLAEFDGVVGMGFIEQAIGRVTPIFDNIISQGVLKEDVFSFYYNRDSENSQSLGGQIVLGGSDPQHYEGNFHYINLIKTGVWQIQMKGVSVGSSTLLCEDGCLALVDTGASYISGSTSSIEKLMEALGAKKRLFD... | Function: Renin is a highly specific endopeptidase, whose only known function is to generate angiotensin I from angiotensinogen in the plasma, initiating a cascade of reactions that produce an elevation of blood pressure and increased sodium retention by the kidney.
Catalytic Activity: Cleavage of Leu-|-Xaa bond in ang... |
P08424 | MGGRRMPLWALLLLWTSCSFSLPTDTASFGRILLKKMPSVREILEERGVDMTRISAEWGEFIKKSSFTNVTSPVVLTNYLDTQYYGEIGIGTPSQTFKVIFDTGSANLWVPSTKCGPLYTACEIHNLYDSSESSSYMENGTEFTIHYGSGKVKGFLSQDVVTVGGIIVTQTFGEVTELPLIPFMLAKFDGVLGMGFPAQAVDGVIPVFDHILSQRVLKEEVFSVYYSRESHLLGGEVVLGGSDPQHYQGNFHYVSISKAGSWQITMKGVSVGPATLLCEEGCMAVVDTGTSYISGPTSSLQLIMQALGVKEKRANNYVVN... | Function: Renin is a highly specific endopeptidase, whose only known function is to generate angiotensin I from angiotensinogen in the plasma, initiating a cascade of reactions that produce an elevation of blood pressure and increased sodium retention by the kidney.
Catalytic Activity: Cleavage of Leu-|-Xaa bond in ang... |
P81134 | MAVLVVFLSFLVADVFGNEFSILRSPGSVVFRNGNWPIPGERIPDVAALSMGFSVKEDLSWPGLAVGNLFHRPRATVMVMVKGVDKLALPPGSVISYPLENAVPFSLDSVANSIHSLFSEETPVVLQLAPSEERVYMVGKANSVFEDLSVTLRQLRNRLFQENSVLTSLPLNSLSRNNEVDLLFLSELQVLRDISSLLSRHKHLAKDHSPDLYSLELAGLDEIGKHYGEDSEQFRDASKILIDALQKFADDMYNLYGGNAVVELVTVRSFDTSLVRKTRNILETKQVKDPSTTYNLAYKYNFEYPVVFNLVLWIMIGLAL... | Function: Multifunctional protein which functions as a renin, prorenin cellular receptor and is involved in the assembly of the lysosomal proton-transporting V-type ATPase (V-ATPase) and the acidification of the endo-lysosomal system (By similarity). May mediate renin-dependent cellular responses by activating ERK1 and... |
Q9VHG4 | MLRVFVIFSLFIAAINASGEFTVLNRPKAISFKGNDALESHYVGDVLYASMGNAVSGDTNWNGLTINDPFNLAKGVILVHVQGIGHVTTAGNVKTYELTGSGTDASLNALAAELEAANEPVCDINFEQFDDGVQAWKSCFGDFEAPAAKPTKHLNPSLHTADKQFLQEVGFINSAADHLAEMAKPSNVLMLRVSVDGVAKAHGEKSVAVEEANKLLSAAISRLLAASQKSSDSVLFVQTTEKDVAASRAKRDTIAASTTNPYNLAVYYGSDYPVIFNIILWFMVVFGLSLLAICYAIAAMDPGRDSIIYRMTSTRIKKDN | Function: Multifunctional protein which functions as transmembrane receptor in the planar cell polarity (PCP) and is involved in the assembly of the proton-transporting vacuolar (V)-ATPase protein pump . As transmembrane receptor mediates fz/PCP signaling through interaction with fz and stabilizes asymmetric PCP domain... |
O75787 | MAVFVVLLALVAGVLGNEFSILKSPGSVVFRNGNWPIPGERIPDVAALSMGFSVKEDLSWPGLAVGNLFHRPRATVMVMVKGVNKLALPPGSVISYPLENAVPFSLDSVANSIHSLFSEETPVVLQLAPSEERVYMVGKANSVFEDLSVTLRQLRNRLFQENSVLSSLPLNSLSRNNEVDLLFLSELQVLHDISSLLSRHKHLAKDHSPDLYSLELAGLDEIGKRYGEDSEQFRDASKILVDALQKFADDMYSLYGGNAVVELVTVKSFDTSLIRKTRTILEAKQAKNPASPYNLAYKYNFEYSVVFNMVLWIMIALALA... | Function: Multifunctional protein which functions as a renin, prorenin cellular receptor and is involved in the assembly of the lysosomal proton-transporting V-type ATPase (V-ATPase) and the acidification of the endo-lysosomal system . May mediate renin-dependent cellular responses by activating ERK1 and ERK2 . By incr... |
Q9CYN9 | MAVLVVLLFFLVAGALGNEFSILRSPGSVVFRNGNWPIPGDRIPDVAALSMGFSVKEDLSWPGLAVGNLFHRPRATIMVMVKGVDKLALPAGSVISYPLENAVPFSLDSVANSIHSLFSEETPVVLQLAPSEERVYMVGKANSVFEDLSVTLRQLRNRLFQENSLLNSLPLNSLSRNNEVDLLFLSELQVLHDISSLLSRHKHLAKDHSPDLYSLELAGLDELGKRYGEDSEQFRDASKILVDALQKFADDMYSLYGGNAVVELVTVKSFDTSLVRKSRTILEAKQENTQSPYNLAYKYNLEYSVVFNLVLWIMIGLALA... | Function: Multifunctional protein which functions as a renin, prorenin cellular receptor and is involved in the assembly of the lysosomal proton-transporting V-type ATPase (V-ATPase) and the acidification of the endo-lysosomal system (By similarity). May mediate renin-dependent cellular responses by activating ERK1 and... |
Q6AXS4 | MAVLVVLLSSLVSSALANEFSILRSPGSVVFRNGNWPIPGDRIPDVAALSMGFSVKEDLSWPGLAVGNLFHRPRATIMVTVKGVDKLALPTGSVISYPLENAVPFSLDSVANSIHSLFSEETPVVLQLAPSEERVYMVGKANSVFEDLSVTLRQLRNRLFQENSVLNSLPLNSLSRNNEVDLLFLSELQVLHDISSLLSRHKHLAKDHSPDLYSLELAGLDELGKRYGEDSEQFRDASRILVDALQKFADDMYSLYGGNAVVELVTVKSFDTSLVRKSRTILETKQENTQSPYNLAYKYNLEYSVVFNLVLWIMTGLALA... | Function: Multifunctional protein which functions as a renin, prorenin cellular receptor and is involved in the assembly of the lysosomal proton-transporting V-type ATPase (V-ATPase) and the acidification of the endo-lysosomal system (By similarity). May mediate renin-dependent cellular responses by activating ERK1 and... |
P82708 | MPPNLTGYYRFVSQKNLEDYLQALNVNMALRKIALLLKPDKEIDQRGNHMTVKTLSTFRNYVLEFEVGVEFEEDLRTVDGRKCQTIVTWEEEQLVCVQKGEVPNRGWRLWLEEEMLYQEVTARDAVCQCVFRKVK | Function: Intracellular transport of retinol.
Sequence Mass (Da): 15962
Sequence Length: 135
Domain: Forms a beta-barrel structure that accommodates hydrophobic ligands in its interior.
Subcellular Location: Cytoplasm
|
P82980 | MPPNLTGYYRFVSQKNMEDYLQALNISLAVRKIALLLKPDKEIEHQGNHMTVRTLSTFRNYTVQFDVGVEFEEDLRSVDGRKCQTIVTWEEEHLVCVQKGEVPNRGWRHWLEGEMLYLELTARDAVCEQVFRKVR | Function: Intracellular transport of retinol.
Sequence Mass (Da): 15931
Sequence Length: 135
Domain: Forms a beta-barrel structure that accommodates hydrophobic ligands in its interior.
Subcellular Location: Cytoplasm
|
Q96R05 | MPADLSGTWTLLSSDNFEGYMLALGIDFATRKIAKLLKPQKVIEQNGDSFTIHTNSSLRNYFVKFKVGEEFDEDNRGLDNRKCKSLVIWDNDRLTCIQKGEKKNRGWTHWIEGDKLHLEMFCEGQVCKQTFQRA | Function: Intracellular transport of retinol.
Sequence Mass (Da): 15536
Sequence Length: 134
Domain: Forms a beta-barrel structure that accommodates hydrophobic ligands in its interior.
Subcellular Location: Cytoplasm
|
Q9EPC5 | MPADLSGTWNLLSSDNFEGYMLALGIDFATRKIAKLLKPQKVIEQNGDSFTIQTCSSLRNYLVKFKVGEEFEEDNKGLDNRKCTSLVTWENDKLTCVQRGEKKNRGWSHWIEGDQLHLEMFCEGQVCKQTFQRA | Function: Intracellular transport of retinol.
Sequence Mass (Da): 15428
Sequence Length: 134
Domain: Forms a beta-barrel structure that accommodates hydrophobic ligands in its interior.
Subcellular Location: Cytoplasm
|
B9DFK5 | MAGCAMNLQFSSVVKVRNEISSFGICNRDFVFRDLAKAMKVPVLRIRGGSGRQRSRLFVVNMSQSPIEPQSGGFAATEQIKGEGDNSILGKDNVRNLGTDQLENLDIDGNVGDGFNGSDGNGGGGGGGNGGEGDGEGEDYEEKEFGPILKFEEVMKETEARGATLPSDMLEAAKNYGIRKVLLLRYLDLQSSAGLLGFAIRSWAMLRNRMLADPSFLFKIGAEIVIDSCCATVAEVQKRGKDFWAEFELYVADLLVGTVVNIALVGMLAPYVRFGQPSASPGFLGRMVFAYNALPSSVFEAERPGCRFSAQQRLATYFYK... | Function: May play a role in leaf development. Required for leaf mesophyll cell division in the early stages of leaf organogenesis . Acts in a developmental pathway that involves PPT1/CUE1 but does not include ASE2/DOV1 .
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 46629
Sequence Length: 432
Subc... |
B2UL99 | MDYTPLIEKRRQRLEELETVIAEPDFFNDQKKASEIMREHRRLKELMETWDSLNATEQQLADNQELAKTDDPELAELAALEIPELEAALEKLRSDVQYSLLPRDTTEDRDAIIEIRAGTGGDEASLFAGDLLRMYQRFAEERGWRFEHLESSPSDVGGFKEVVCRIAGEEVFRFLKYEGGVHRVQRVPATETQGRIHTSTATVAVMPEAEEVDIEIRPEDLRIEVCRSGGAGGQHVNKTESAVQIWHIPTGVYVRCEEERSQMKNREKGMKILRAKLFEAKKREEAEKYSAARRNLIGSGGREEKIRTYNFPQNRLTDHR... | Function: Peptide chain release factor 1 directs the termination of translation in response to the peptide chain termination codons UAG and UAA.
PTM: Methylated by PrmC. Methylation increases the termination efficiency of RF1.
Sequence Mass (Da): 40973
Sequence Length: 358
Subcellular Location: Cytoplasm
|
P56905 | MANMSRLNELVSEFGLVERRLGDPQALADGREYARLTRRHRELLPLVTLVREREQAEADLSGARELLQDPDMRDPDMKELAQLEVGGLQARLAEIEAELEVLLLPTDPDDGKDVILELRAGAGGAEAGLFVMDLLRMYERYAAGLNLKLNVLDAAESDLGGASKVVAEVTGDFAFRALKWERGVHRVQRVPATESQGRIHTSTATVAVLPEAEPGEVNLDLSEVRIDVFRSQGAGGQGVNTTDSAVRAVYRAGTPDEIMVICQDGRSQIKNREKALQVLTARLAERERAAREAQERQERASQVGSGDRSEKIRTYNYPQN... | Function: Peptide chain release factor 1 directs the termination of translation in response to the peptide chain termination codons UAG and UAA.
PTM: Methylated by PrmC. Methylation increases the termination efficiency of RF1 (By similarity).
Sequence Mass (Da): 41126
Sequence Length: 375
Subcellular Location: Cytoplas... |
B8E003 | MLQKLVIDKLEEIEKRFEEIEGLLAKEDVISDFNKYQSLLKERAKIEEIVDKFREYKRLLKEKEDLEEMVKEEQDEDLRSLAETELEDIQEKLEKVEFELKALLLPKDPNDEKNIIMEIRAGTGGEEAALFAADLFRMYLGYAQKKGWKVEIVSSNPTGLGGFKEIIFIVEGKGAYSRLKFESGVHRVQRVPITESSGRIHTSTATVAVLPEMEEIEVEIDPKDLRIETFRSGGAGGQHVNKTESGVRITHIPSGIVVQCQDERSQHQNREKAMKVLRARLYEYYQREKENEIASQRRQQVGTGERSEKIRTYNFPQRRV... | Function: Peptide chain release factor 1 directs the termination of translation in response to the peptide chain termination codons UAG and UAA.
PTM: Methylated by PrmC. Methylation increases the termination efficiency of RF1.
Sequence Mass (Da): 42486
Sequence Length: 367
Subcellular Location: Cytoplasm
|
B1MLV1 | MSETPLIDAMLAEHAELEKQLADPALHADAAAARKAGRRFAMLSPIVATHRKLATARDDLATARELSADDPSFADEVTELESSIAELETQLSDMLAPRDPHDGDDILLEVKSGEGGEESALFAADLARMYIRYAERHGWKVTVLDETESDLGGYKDATLAIASKGDSADGVWSRLKFEGGVHRVQRVPVTESQGRVHTSAAGVLVYPEPEEVEEIQIDESDLRIDVYRSSGKGGQGVNTTDSAVRITHLPTGIVVTCQNERSQLQNKARAMQVLAARLQALAEEQAQADASAGRASQIRTVDRSERIRTYNFPENRITDH... | Function: Peptide chain release factor 1 directs the termination of translation in response to the peptide chain termination codons UAG and UAA.
PTM: Methylated by PrmC. Methylation increases the termination efficiency of RF1.
Sequence Mass (Da): 38804
Sequence Length: 356
Subcellular Location: Cytoplasm
|
A5IZH6 | MEKTMFKSLSEIKQSYLELLKKIDDPEVISNIKEYSAINKEIAKIREISEKFITYENILKDVEQAKIMLESKNEEEVEFAKMIIDENSLKLDELEEKLKILILPQDENDDKNIIVEIRGAAGGDEANIFAGDLFRMYSKFADELGFRLKILSTNSASAGGFSQIVFSIKGEKAYSKFKFESGVHRVQRVPVTESQGRIHTSTTTVTVMPEIDDSVEIEIKPSDLKIDVFRSSGAGGQSVNTTDSAVRITHLPTNIVVTSQDERSQIANRETALTILKSKLYDLEMQKKAEEESGYRKLAGHGDRSEKIRTYNYPQDRVTD... | Function: Peptide chain release factor 1 directs the termination of translation in response to the peptide chain termination codons UAG and UAA.
PTM: Methylated by PrmC. Methylation increases the termination efficiency of RF1.
Sequence Mass (Da): 40472
Sequence Length: 358
Subcellular Location: Cytoplasm
|
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