ids stringlengths 6 10 | seqs stringlengths 11 1.02k | texts stringlengths 108 11.1k |
|---|---|---|
Q0VCI1 | MPAVLGFEGSANKIGVGVVRDGKVLANPRRTYVTPPGTGFLPGDTARHHRAVILDLLQEALTEAGLTSEDIDCIAYTKGPGMGAPLVSVAVVARTVAQLWNKPLLGVNHCIGHIEMGRLITGATNPTVLYVSGGNTQVIAYSEHRYRIFGETIDIAVGNCLDRFARVLKISNDPSPGYNIEQMAKRGKKLVELPYTVKGMDVSFSGILSFIEDVAQRMLATGECTPEDLCFSLQETVFAMLVEITERAMAHCGSQEALIVGGVGCNVRLQEMMETMCQERGARLFATDERFCIDNGAMIAQAGWEMFQAGHRTPLSESGI... | Cofactor: Binds 1 divalent metal cation per subunit.
Function: Component of the EKC/KEOPS complex that is required for the formation of a threonylcarbamoyl group on adenosine at position 37 (t(6)A37) in tRNAs that read codons beginning with adenine. The complex is probably involved in the transfer of the threonylcarbam... |
P45971 | MRWLPGLLLIASIGFHQSLADRVLVLGETAAVKDTHSVFLNSVKERGHELTVRAADDSQLALFKHGQLIFDHLFILAPGVQVFGGSLSPSEISKFVDAGGNVLVAAGSNIGDALREIAAEHGFEFEEAGTSVIDHHNYDQTLDSGDHTTLVVGKDQLISAELIVGNSAKLHPVLFKGIGLVAGKTNNLALSIVRASGTAYSYDPKAVRATNPSIAGSRTLLVGGLQSRNNARIVFTGSSELFSNTFFSAKTNSVNPSVQGAQSGNADFATAITRWVMKESGVLRVKTVNHHKKGETVPPVEGYFITEDVVYTIEIEELKN... | Function: Subunit of the oligosaccharyl transferase (OST) complex that catalyzes the initial transfer of a defined glycan (Glc(3)Man(9)GlcNAc(2) in eukaryotes) from the lipid carrier dolichol-pyrophosphate to an asparagine residue within an Asn-X-Ser/Thr consensus motif in nascent polypeptide chains, the first step in ... |
Q54E62 | MMMKSILITFIIASALLSSVFADIGGKRTLVVLDDLSIKKTHSTFFKNLENKGYKLQFEQSNTKVVLEKYGDFNFDNLILFSPTSESLSFSSADVTRFIDGGNNVLFAGSNVISENIRDIAAECGMEIEEDKTLIFDHFNYDKSQSDHSVLVADQFIDDSPIILQGLNKPILFKGIGHKIRNNPLNYAILTGSSTAFSAKAISGVSTKLMGKSCGLVSSLQARNNARVTFSGSLDLFSDKSFYSKIDNKESGNKEFVERLVSWTFQERGILRASELELVKISTESNSTVAPDVFTIKDEVKYSLKVEEFDGIKGKWVPYV... | Function: Subunit of the oligosaccharyl transferase (OST) complex that catalyzes the initial transfer of a defined glycan (Glc(3)Man(9)GlcNAc(2) in eukaryotes) from the lipid carrier dolichol-pyrophosphate to an asparagine residue within an Asn-X-Ser/Thr consensus motif in nascent polypeptide chains, the first step in ... |
P39656 | MGYFRCARAGSFGRRRKMEPSTAARAWALFWLLLPLLGAVCASGPRTLVLLDNLNVRETHSLFFRSLKDRGFELTFKTADDPSLSLIKYGEFLYDNLIIFSPSVEDFGGNINVETISAFIDGGGSVLVAASSDIGDPLRELGSECGIEFDEEKTAVIDHHNYDISDLGQHTLIVADTENLLKAPTIVGKSSLNPILFRGVGMVADPDNPLVLDILTGSSTSYSFFPDKPITQYPHAVGKNTLLIAGLQARNNARVIFSGSLDFFSDSFFNSAVQKAAPGSQRYSQTGNYELAVALSRWVFKEEGVLRVGPVSHHRVGETA... | Function: Subunit of the oligosaccharyl transferase (OST) complex that catalyzes the initial transfer of a defined glycan (Glc(3)Man(9)GlcNAc(2) in eukaryotes) from the lipid carrier dolichol-pyrophosphate to an asparagine residue within an Asn-X-Ser/Thr consensus motif in nascent polypeptide chains, the first step in ... |
Q6ZLK0 | MAAPRHHHLALAVALALLVVTAAAADEGGPRGRRVLVLVDDLAVRSSHSAFFASLQGRGFDLDFRLADDPKLSLHRYGQYLYDGLVLFAPSTPRFGGSVDQNSILEFIDAGHDMILAADSSASDLIRGIATECGVDFDEDPEAMVIDHINYAATDAEGDHTLIAGDDLIQSDVILGSKKIEAPVLFRGIGHAVNPSNSLVLKVLSASPSAYSANPKSKLASPPSLTGSAISLVSVMQARNNARVLISGSLDLFSNRFLKSGVQKAGSKIRHEKAGNEQFVTETSKWVFHERGHLKAVNVKHNKVGETNEPGMYRINDDLE... | Function: Subunit of the oligosaccharyl transferase (OST) complex that catalyzes the initial transfer of a defined glycan (Glc(3)Man(9)GlcNAc(2) in eukaryotes) from the lipid carrier dolichol-pyrophosphate to an asparagine residue within an Asn-X-Ser/Thr consensus motif in nascent polypeptide chains, the first step in ... |
Q6GNR9 | MASLRLSVLLVSVSWLLLLVSGLRAGPRTLVLMENINLRETHSLFFRSLSDRGFDLSFKTADDPSLSLIKYGEFLYDNLIIFSPSVEDFGGNINIETISSFIDGGGSVLVAASSDIGDPLRELGSECGIEFDEEKTAVIDHHNYDISDPGQHTLIVADSENLLKAPTIVGKTPLNPILFRGVGMVADPDNPLVLDILTGSSTSYSFFPDKPITQYPHAVGKNTLLIAGLQARNNARVVFSGSLDFFSDSFFNSAVQKAASGSNRYAKTGNYELAMALSRWVFKEEGVLRVGEVSHHRVGESSPPSAYTVTDLVEYSIVIE... | Function: Subunit of the oligosaccharyl transferase (OST) complex that catalyzes the initial transfer of a defined glycan (Glc(3)Man(9)GlcNAc(2) in eukaryotes) from the lipid carrier dolichol-pyrophosphate to an asparagine residue within an Asn-X-Ser/Thr consensus motif in nascent polypeptide chains, the first step in ... |
Q9LHK3 | MIDDQDLGFIANFLGIFIFALVIAYHYVTADPKYEAT | Function: Subunit of the oligosaccharyl transferase (OST) complex that catalyzes the initial transfer of a defined glycan (Glc(3)Man(9)GlcNAc(2) in eukaryotes) from the lipid carrier dolichol-pyrophosphate to an asparagine residue within an Asn-X-Ser/Thr consensus motif in nascent polypeptide chains, the first step in ... |
C7J4U3 | MFDDQDLGFFANFLGIFIFVLVIAYHFVMADPKYEGN | Function: Subunit of the oligosaccharyl transferase (OST) complex that catalyzes the initial transfer of a defined glycan (Glc(3)Man(9)GlcNAc(2) in eukaryotes) from the lipid carrier dolichol-pyrophosphate to an asparagine residue within an Asn-X-Ser/Thr consensus motif in nascent polypeptide chains, the first step in ... |
Q8L986 | MFDDQDLGFFANFLGIFIFIMVIAYHFVVAEPKFE | Function: Subunit of the oligosaccharyl transferase (OST) complex that catalyzes the initial transfer of a defined glycan (Glc(3)Man(9)GlcNAc(2) in eukaryotes) from the lipid carrier dolichol-pyrophosphate to an asparagine residue within an Asn-X-Ser/Thr consensus motif in nascent polypeptide chains, the first step in ... |
C7J0R5 | MFDDQDLGFFANFLGIFIFVLVMAYHFVMADVKYEGN | Function: Subunit of the oligosaccharyl transferase (OST) complex that catalyzes the initial transfer of a defined glycan (Glc(3)Man(9)GlcNAc(2) in eukaryotes) from the lipid carrier dolichol-pyrophosphate to an asparagine residue within an Asn-X-Ser/Thr consensus motif in nascent polypeptide chains, the first step in ... |
Q9P838 | MITDEQLNTIALTFGFASIILIIIYHAISTNVHKLEDETPSSSFTRTNTTETTVASKKKK | Function: Subunit of the oligosaccharyl transferase (OST) complex that catalyzes the initial transfer of a defined glycan (Glc(3)Man(9)GlcNAc(2) in eukaryotes) from the lipid carrier dolichol-pyrophosphate to an asparagine residue within an Asn-X-Ser/Thr consensus motif in nascent polypeptide chains, the first step in ... |
Q86WC4 | MEPGPTAAQRRCSLPPWLPLGLLLWSGLALGALPFGSSPHRVFHDLLSEQQLLEVEDLSLSLLQGGGLGPLSLPPDLPDLDPECRELLLDFANSSAELTGCLVRSARPVRLCQTCYPLFQQVVSKMDNISRAAGNTSESQSCARSLLMADRMQIVVILSEFFNTTWQEANCANCLTNNSEELSNSTVYFLNLFNHTLTCFEHNLQGNAHSLLQTKNYSEVCKNCREAYKTLSSLYSEMQKMNELENKAEPGTHLCIDVEDAMNITRKLWSRTFNCSVPCSDTVPVIAVSVFILFLPVVFYLSSFLHSEQKKRKLILPKRL... | Function: Required for osteoclast and melanocyte maturation and function.
PTM: Undergoes proteolytic cleavage in the luminal domain, the cleaved fragments might be linked by disulfide bonds with the remnant of the protein.
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 37257
Sequence Length:... |
Q8BGT0 | MARDAELARSSGWPWRWLPALLLLQLLRWRCALCALPFTSSRHPGFADLLSEQQLLEVQDLTLSLLQGGGLGPLSLLPPDLPDLEPECRELLMDFANSSAELTACMVRSARPVRLCQTCYPLFQQVAIKMDNISRNIGNTSEGPRCGGSLLTADRMQIVLMVSEFFNSTWQEANCANCLTNNGEDLSNNTEDFLSLFNKTLACFEHNLQGHTYSLLPPKNYSEVCRNCKEAYKNLSLLYSQMQKLNGLENKAEPETHLCIDVEDAMNITRKLWSRTFNCSVTCSDTVSVVAVSVFILFLPVVFYLSSFLHSEQKKRKLIL... | Function: Required for osteoclast and melanocyte maturation and function.
PTM: Undergoes proteolytic cleavage in the luminal domain, the cleaved fragments might be linked by disulfide bonds with the remnant of the protein.
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 38000
Sequence Length:... |
P31096 | MRIAVICFCLLGIASALPVKPTSSGSSEEKQLNNKYPDAVATWLKPDPSQKQTFLAPQNSVSSEETDDNKQNTLPSKSNESPEQTDDLDDDDDNSQDVNSNDSDDAETTDDPDHSDESHHSDESDEVDFPTDIPTIAVFTPFIPTESANDGRGDSVAYGLKSRSKKFRRSNVQSPDATEEDFTSHIESEEMHDAPKKTSQLTDHSKETNSSELSKELTPKAKDKNKHSNLIESQENSKLSQEFHSLEDKLDLDHKSEEDKHLKIRISHELDSASSEVN | Function: Major non-collagenous bone protein that binds tightly to hydroxyapatite (Probable). Appears to form an integral part of the mineralized matrix (Probable). Probably important to cell-matrix interaction (Probable).
PTM: Extensively phosphorylated by FAM20C in the extracellular medium at multiple sites within th... |
P23498 | MKLAFLCLCFISIAAAWPVSKSRQHAISASSEEKYDPRSHHTHRYHQDHVDSQSQEHLQQTQNDLASLQQTHYSSEENADVPEQPDFPDIPSKSQEAVDDDDDDDNDSNDTDESDEVVTDFPTEAPVTPFNRGDNAGRGDSVAYGFRAKAHVVKASKLRKAARKLIEDDATAEVGDSQLAGLWLPKESREQDSRELAQHQSVENDSRPRFDSPEVGGGDSKASAGVDSRESLASRSAVDTSNQTLESAEDAEDRHSIENNEVTR | Function: Major non-collagenous bone protein that binds tightly to hydroxyapatite. Appears to form an integral part of the mineralized matrix. Probably important to cell-matrix interaction.
PTM: Extensively phosphorylated on serine residues.
Sequence Mass (Da): 29162
Sequence Length: 264
Subcellular Location: Secreted
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P10451 | MRIAVICFCLLGITCAIPVKQADSGSSEEKQLYNKYPDAVATWLNPDPSQKQNLLAPQNAVSSEETNDFKQETLPSKSNESHDHMDDMDDEDDDDHVDSQDSIDSNDSDDVDDTDDSHQSDESHHSDESDELVTDFPTDLPATEVFTPVVPTVDTYDGRGDSVVYGLRSKSKKFRRPDIQYPDATDEDITSHMESEELNGAYKAIPVAQDLNAPSDWDSRGKDSYETSQLDDQSAETHSHKQSRLYKRKANDESNEHSDVIDSQELSKVSREFHSHEFHSHEDMLVVDPKSKEEDKHLKFRISHELDSASSEVN | Function: Major non-collagenous bone protein that binds tightly to hydroxyapatite. Appears to form an integral part of the mineralized matrix. Probably important to cell-matrix interaction.
PTM: Forms covalent cross-links mediated by transglutaminase TGM2, between a glutamine and the epsilon-amino group of a lysine res... |
P10923 | MRLAVICFCLFGIASSLPVKVTDSGSSEEKLYSLHPDPIATWLVPDPSQKQNLLAPQNAVSSEEKDDFKQETLPSNSNESHDHMDDDDDDDDDDGDHAESEDSVDSDESDESHHSDESDETVTASTQADTFTPIVPTVDVPNGRGDSLAYGLRSKSRSFQVSDEQYPDATDEDLTSHMKSGESKESLDVIPVAQLLSMPSDQDNNGKGSHESSQLDEPSLETHRLEHSKESQESADQSDVIDSQASSKASLEHQSHKFHSHKDKLVLDPKSKEDDRYLKFRISHELESSSSEVN | Function: Major non-collagenous bone protein that binds tightly to hydroxyapatite. Appears to form an integral part of the mineralized matrix. Probably important to cell-matrix interaction.
PTM: Extensively phosphorylated by FAM20C in the extracellular medium at multiple sites within the S-x-E/pS motif (By similarity).... |
A5VIM0 | MAFNLRNRSFLTLADFNTREMEYMLDLAEDLKKAKYAGYEGKNLKGKNIALIFEKSSTRTRCSFEVGAKDEGAHVTYLGPSGSHIGHKESVKDTARVLGGMFDGIEYRGFSQRNVEILAKYSGVPVWNGLTDEDHPTQVLADFLTAHEVLKKPYKDIKFAFVGDGQDNVSNALMLGAAVMGMEYHVVTPKELEPTKETLDKANEIAAKTGAKIVVTNDIKEGVKGMDVIYADVWVSMGESDDMWEKRINLLKPYQVTMDVMKATENPNVLFEHCLPAFHNLDTEVGKEIEKKFGLKEMEVTDEVFESEHSVVFREAENRM... | Function: Reversibly catalyzes the transfer of the carbamoyl group from carbamoyl phosphate (CP) to the N(epsilon) atom of ornithine (ORN) to produce L-citrulline.
Catalytic Activity: carbamoyl phosphate + L-ornithine = H(+) + L-citrulline + phosphate
Sequence Mass (Da): 37560
Sequence Length: 335
Pathway: Amino-acid d... |
Q8Y6U5 | MTMYAKNNTSGKDMLSLLEWNKEELTDIIKLAVAMKTNPAHYSHILSGKILGMIFDKPSTRTRVSFEAGILQLGGQAIVMSSKELQIGRGEPIKDTAHVMSEYIDAIMIRTFSHEKVEELAYHAEIPIINGLTDLHHPCQALADLMTIYEWKDQLEGIKLAYIGDGNNVCHSLLLAGAMVGIDIRLAMPKGYEVDETILAKAENLAKQSGGKIFVTEDSKLAVTDADFIYTDVWTSMGQEDENAKRLADFGEKYQVNAELVSGAKPDYHFLHCLPAHREEEVTTEIIDGIHSVIYQQAGNRLHAQKALLAAILEAK | Function: Reversibly catalyzes the transfer of the carbamoyl group from carbamoyl phosphate (CP) to the N(epsilon) atom of ornithine (ORN) to produce L-citrulline.
Catalytic Activity: carbamoyl phosphate + L-ornithine = H(+) + L-citrulline + phosphate
Sequence Mass (Da): 35041
Sequence Length: 316
Pathway: Amino-acid b... |
Q8TWG4 | MRLKRLSTNHLLSIADLDREDVETVLRVAERFKERYLAGERVIPILEGKTLGLIFEKPSTRTRVSFEVAMHQLGGQAFTYTKQELQLGRGEAIKDTAAVLSRYLDGVMIRARRHEDIEEFARYSEVPVINGLSDLEHPCQALTDAFTIREKLGRGPHTVAFVGDGNNVCSSLALVCATLGWDFVHAVPEGYECPDRVWREVERRAEESGSETRVVRDPKEAVREADVVYTDVWVSMGDEAEREERLRVFRPYQVNEELMSHAPEHAIVMHCMPIQRGYELTDDVADSERSVIYDQAENRLHVQKAILALLMG | Function: Reversibly catalyzes the transfer of the carbamoyl group from carbamoyl phosphate (CP) to the N(epsilon) atom of ornithine (ORN) to produce L-citrulline.
Catalytic Activity: carbamoyl phosphate + L-ornithine = H(+) + L-citrulline + phosphate
Sequence Mass (Da): 35494
Sequence Length: 312
Pathway: Amino-acid b... |
A3DL27 | MVTSLKGRDFLTLADYSREELLFVLETAKHLKQRYLAGERVIPLLPGRHLAMIFEKSSTRTRISFETAMRELGGDALYLGWKELQLGRGETIEDTARVVSRYVDGIMARVYEHEKLEKLAQYSRVPVINGLSDLLHPAQALTDIYTIMEKKGSDLSKLKIVFIGDGGDNVLHSLMLGIGILGGKIIISSPKGYDPDPRIIKLFEEKAVPNGGEYEIIRDPYEAVRDADVVYTDVWVSMGQEAEKEKRIKDLEPYRVTVELMKHAKSDAVFMHCLPAHRGQEVVDEVIDGKWSIVWDQAENRKHVQKAILALIIP | Function: Reversibly catalyzes the transfer of the carbamoyl group from carbamoyl phosphate (CP) to the N(epsilon) atom of ornithine (ORN) to produce L-citrulline.
Catalytic Activity: carbamoyl phosphate + L-ornithine = H(+) + L-citrulline + phosphate
Sequence Mass (Da): 35514
Sequence Length: 314
Pathway: Amino-acid d... |
Q9XIP2 | MTRILVQRGSSGSSSNSSRPSSSSSSSSGSETQINNNIPVPPVTIDEEITDEKQEEVTVVEKAECSDAKDVAVDSDEPADREDDEGLVVAENVHVQSEGIDCDSPVSGGSNSDSPPVPAPPPKPSSTVNPGSNRSVLGSFGALRIGPTRRAAGPRSLVSSRSSPTGSHPSSPRSHSENEGYNSSDEHMPCYVPSHPGSGLEREHQFEAEIRYSKGFEIRRMLEDGNCLFRAVADQVYGDSEAYDLARQMCMDYMEQERDHFSQFITEGFTSYLKRKRRDKVYGNNVEIQALAEMYNRPIHIYSYSTEPINIFQGNYSTDT... | Function: Hydrolase that can remove conjugated ubiquitin from proteins in vitro and may therefore play an important regulatory role at the level of protein turnover by preventing degradation . Binds chromatin (e.g. nucleosomes and histones) and has enzymatic histone deubiquitinase activity, specific for the H2B histone... |
Q8TE49 | MVSSVLPNPTSAECWAALLHDPMTLDMDAVLSDFVRSTGAEPGLARDLLEGKNWDLTAALSDYEQLRQVHTANLPHVFNEGRGPKQPEREPQPGHKVERPCLQRQDDIAQEKRLSRGISHASSAIVSLARSHVASECNNEQFPLEMPIYTFQLPDLSVYSEDFRSFIERDLIEQATMVALEQAGRLNWWSTVCTSCKRLLPLATTGDGNCLLHAASLGMWGFHDRDLVLRKALYTMMRTGAEREALKRRWRWQQTQQNKEEEWEREWTELLKLASSEPRTHFSKNGGTGGGVDNSEDPVYESLEEFHVFVLAHILRRPIV... | Function: Has deubiquitinating activity towards 'Lys-11'-linked polyubiquitin chains.
Catalytic Activity: Thiol-dependent hydrolysis of ester, thioester, amide, peptide and isopeptide bonds formed by the C-terminal Gly of ubiquitin (a 76-residue protein attached to proteins as an intracellular targeting signal).
Sequen... |
Q6GQQ9 | MTLDMDAVLSDFVRSTGAEPGLARDLLEGKNWDVNAALSDFEQLRQVHAGNLPPSFSEGSGGSRTPEKGFSDREPTRPPRPILQRQDDIVQEKRLSRGISHASSSIVSLARSHVSSNGGGGGSNEHPLEMPICAFQLPDLTVYNEDFRSFIERDLIEQSMLVALEQAGRLNWWVSVDPTSQRLLPLATTGDGNCLLHAASLGMWGFHDRDLMLRKALYALMEKGVEKEALKRRWRWQQTQQNKESGLVYTEDEWQKEWNELIKLASSEPRMHLGTNGANCGGVESSEEPVYESLEEFHVFVLAHVLRRPIVVVADTMLRD... | Function: Negative regulator of the non-canonical NF-kappa-B pathway that acts by mediating deubiquitination of TRAF3, an inhibitor of the NF-kappa-B pathway, thereby acting as a negative regulator of B-cell responses. In response to non-canonical NF-kappa-B stimuli, deubiquitinates 'Lys-48'-linked polyubiquitin chains... |
F4K3M6 | MAKTKQQKSKPKKQPHQKQGKDCDLSQFRAQLDALGLKIIQVTADGNCFFRAIADQLEGNEDEHNKYRNMIVLYIVKNREMFEPFIEDDVPFEDYCKTMDDDGTWAGNMELQAASLVTRSNICIHRNMSPRWYIRNFEDTRTRMIHLSYHDGEHYNSVRSKEDACGGPARPVVIEADAKVSAASKQAKATESKSKNKADKCHVNAGAIKVVMSGSCCDNTEKAEQVLLQVNGDVDAAIEFLIADQGMESLTENDTETASASDTINPKHASDSPMENTEQAREELIEEESASGNNSETVQAKCTTQTDDKKIPRNKTCPCG... | Function: Hydrolase that can remove conjugated ubiquitin from proteins in vitro and may therefore play an important regulatory role at the level of protein turnover by preventing degradation . Cysteine protease with a preference for 'Lys-63' over 'Lys-48' over 'Met-1' -linked ubiquitin (UB) tetramers as substrates . Cl... |
O80949 | MMKSDGNCQFRALADQLYQNSDCHELVRQEIVKQNMSLSTNSQWGDEVTLRVAADVYQVKIILITSIKLIPFMEFLPKSQKEPDKVIHMSYLAGIHFNSIYKKNKEKGSRSSSSSSSAVWMKLQRKKENEAKKKEEEEKERKDMEKEEKKKDKEDKKKDKEDKKKAKVQKEKKEKKEKKNRNHHFHYSE | Function: Hydrolase that can remove conjugated ubiquitin from proteins in vitro and may therefore play an important regulatory role at the level of protein turnover by preventing degradation.
Catalytic Activity: Thiol-dependent hydrolysis of ester, thioester, amide, peptide and isopeptide bonds formed by the C-terminal... |
Q8LBW2 | MGYEPDPDALRWGLHDLEVCTLTNAGSCSSVTRYESGGGGTQGYVREGYNQPVTGYVDNDAVIAQFYQDELSRVARAEASGINSLSPTSVVAQDWPHPHQGQENQGEAIDITQESDILHNHNGNMEDKNVARIRFEGGQSSPSRDDDSVCSVEIEEESWSEVGKRLNQMIPIAHVPKINGELPSEDEQISDHERLFQRLQLYGLVENKIEGDGNCQFRSLSDQLYRSPEHHNFVREQVVNQLAYNREIYEGYVPMAYNDYLKAMKRNGEWGDHVTLQAAADLFGVRMFVITSFKDTCYIEILPHFQKSNRLICLSFWAEV... | Function: Hydrolase that can remove conjugated ubiquitin from proteins in vitro and may therefore play an important regulatory role at the level of protein turnover by preventing degradation (Probable). Cysteine protease with a preference for 'Lys-63' and 'Lys-48' -linked ubiquitin (UB) tetramers as substrates . Cleave... |
Q96FW1 | MAAEEPQQQKQEPLGSDSEGVNCLAYDEAIMAQQDRIQQEIAVQNPLVSERLELSVLYKEYAEDDNIYQQKIKDLHKKYSYIRKTRPDGNCFYRAFGFSHLEALLDDSKELQRFKAVSAKSKEDLVSQGFTEFTIEDFHNTFMDLIEQVEKQTSVADLLASFNDQSTSDYLVVYLRLLTSGYLQRESKFFEHFIEGGRTVKEFCQQEVEPMCKESDHIHIIALAQALSVSIQVEYMDRGEGGTTNPHIFPEGSEPKVYLLYRPGHYDILYK | Function: Hydrolase that can specifically remove 'Lys-48'-linked conjugated ubiquitin from proteins and plays an important regulatory role at the level of protein turnover by preventing degradation . Regulator of T-cell anergy, a phenomenon that occurs when T-cells are rendered unresponsive to antigen rechallenge and n... |
Q96DC9 | MSETSFNLISEKCDILSILRDHPENRIYRRKIEELSKRFTAIRKTKGDGNCFYRALGYSYLESLLGKSREIFKFKERVLQTPNDLLAAGFEEHKFRNFFNAFYSVVELVEKDGSVSSLLKVFNDQSASDHIVQFLRLLTSAFIRNRADFFRHFIDEEMDIKDFCTHEVEPMATECDHIQITALSQALSIALQVEYVDEMDTALNHHVFPEAATPSVYLLYKTSHYNILYAADKH | Function: Hydrolase that can remove conjugated ubiquitin from proteins in vitro and may therefore play an important regulatory role at the level of protein turnover by preventing degradation. Mediates deubiquitination of 'Lys-11'-,'Lys-48'- and 'Lys-63'-linked polyubiquitin chains, with a preference for 'Lys-63'-linked... |
Q9CQX0 | MSETSFNLISEKCDILSILRDHPENRIYQRKIQELSKRFTSIRKTKGDGNCFYRALGYSYLESLLGKSREILKFKERVLQTPNDLLAAGFEEHKFRNFFNAFYSVVELVEKDSSVSSLLKVFNDQSSSDRIVQFLRLLTSAFIRNRADFFRHFIDEEMDIKDFCTHEVEPMAMECDHVQITALSQALNIALQVEYVDEMDTALNHHVFPEAAIPSVYLLYKTSHYNILYAAEKH | Function: Hydrolase that can remove conjugated ubiquitin from proteins in vitro and may therefore play an important regulatory role at the level of protein turnover by preventing degradation. Mediates deubiquitination of 'Lys-11'-,'Lys-48'- and 'Lys-63'-linked polyubiquitin chains, with a preference for 'Lys-63'-linked... |
Q9XVR6 | MANEPQKSDDNGQAAEAVVTDDEIVLQDQQLKTIEDEQKSVPLVATLAPFSILCAEYDNETSAAFLSKATELSEVYGEIRYIRGDGNCFYRAILVGLIEIMLKDRARLEKFIASSRDWTRTLVELGFPDWTCTDFCDFFIEFLEKIHSGVHTEEAVYTILNDDGSANYILMFFRLITSAFLKQNSEEYAPFIDEGMTVAQYCEQEIEPMWKDADHLAINSLIKAAGTRVRIEYMDRTAAPNGGWHYDIPSDDQQIAPEITLLYRPGHYDVIYKKDSTEASEIEN | Function: Hydrolase that can remove conjugated ubiquitin from proteins and plays an important regulatory role at the level of protein turnover by preventing degradation. Specifically cleaves 'Lys-48'-linked polyubiquitin.
Catalytic Activity: Thiol-dependent hydrolysis of ester, thioester, amide, peptide and isopeptide ... |
Q9VL00 | MEPFTHNDGNRDELIIQQKRDIEKEISDTTPLVSEQLPLTCLYAEYSGDEIFTAKIQDLSKKYKFIRRTRPDGNCFFRAFAYSYLEYLISNTSAYQEFKKLAEESKEKLVQLGFPSFTLEDFHETFMEVIQRVSPDNAGGHSTVQDELHKIFNEQGYSDYVVVYLRLITSGKLQEEADFYQNFIEGDLTIEAFRHLEVEPMYKESDHIHIIALCTALGAGVRVEYLDRGEGGTVKAHDFPEGSEPRIYLIYRPGHYDILYPN | Function: Possible hydrolase that can remove conjugated ubiquitin from proteins in vitro and may therefore play an important regulatory role at the level of protein turnover by preventing degradation.
Catalytic Activity: Thiol-dependent hydrolysis of ester, thioester, amide, peptide and isopeptide bonds formed by the C... |
Q5VV17 | MQLYSSVCTHYPAGAPGPTAAAPAPPAAATPFKVSLQPPGAAGAAPEPETGECQPAAAAEHREAAAVPAAKMPAFSSCFEVVSGAAAPASAAAGPPGASCKPPLPPHYTSTAQITVRALGADRLLLHGPDPVPGAAGSAAAPRGRCLLLAPAPAAPVPPRRGSSAWLLEELLRPDCPEPAGLDATREGPDRNFRLSEHRQALAAAKHRGPAATPGSPDPGPGPWGEEHLAERGPRGWERGGDRCDAPGGDAARRPDPEAEAPPAGSIEAAPSSAAEPVIVSRSDPRDEKLALYLAEVEKQDKYLRQRNKYRFHIIPDGNC... | Function: Deubiquitinating enzyme that specifically hydrolyzes 'Lys-63'-linked polyubiquitin to monoubiquitin . Required for the stability and translation of a subset mRNAs with a high abundance of rare codons by mediating deubiquitination of 40S ribosomal protein RPS10/eS10, thereby antagonizing ZNF598-mediated 40S ub... |
Q5T2D3 | MSRKQAAKSRPGSGSRKAEAERKRDERAARRALAKERRNRPESGGGGGCEEEFVSFANQLQALGLKLREVPGDGNCLFRALGDQLEGHSRNHLKHRQETVDYMIKQREDFEPFVEDDIPFEKHVASLAKPGTFAGNDAIVAFARNHQLNVVIHQLNAPLWQIRGTEKSSVRELHIAYRYGEHYDSVRRINDNSEAPAHLQTDFQMLHQDESNKREKIKTKGMDSEDDLRDEVEDAVQKVCNATGCSDFNLIVQNLEAENYNIESAIIAVLRMNQGKRNNAEENLEPSGRVLKQCGPLWEEGGSGARIFGNQGLNEGRTEN... | Function: Deubiquitinating enzyme that hydrolyzes 'Lys-6'- and 'Lys-11'-linked polyubiquitin. Also hydrolyzes heterotypic (mixed and branched) and homotypic chains . Important regulator of energy metabolism . Glucose and fatty acids trigger its nuclear translocation by CBP-dependent acetylation . In the nucleus, deubiq... |
G4MVZ5 | MSVPSFITAPEFEGGPPQGLSIPFRLRWSKTHPPKEPIVTFKGRTVLVTGANTGLGFEAAVKYAAFGADKIILAVRSIEKGEEAKKRIVERTGRDATDISVLKLDLGEYSSVKDFVSALHEVTPTLDVALLNAGLGNPTYEKSSAGWEMAVQVNVLSTALLAMLLLPLLRSSAAASGAKSHLTFVNSFAHTLVPRDFPLIEGSILKTATDESSWNASSSYNIVKLLAMASVQGFARMEAGEDQQRVIVNSVCPDLCETDLGRKFTGFISSIGKAIFYYLFALSAEEGARCLIGATALGPESHGRFWHHDFLYPFGELAQD... | Function: Short-chain dehydrogenase/reductase; part of the gene cluster that mediates the biosynthesis of a tyrosine-derived cytochalasan acting as a fungal signal recognized by resistant rice plants and leads to avirulence in Pi33 resistant rice cultivars . The first step in the pathway is catalyzed by the hybrid PKS-... |
B2KWH9 | MLSLFYQRISTYIKLSASSLLSILPLYRPFQRRRLTMPSNEGSISSSSTTRPKDVLVVGGSYSGLAAALNLLDLCQGRSCRFAGALDPEISEPAEMRERVPVQITIVDERDGYFHLIGTPLAFASEEYALSAWRKFADIPALQTPAIKFIQGSVTRVDCERKISTIKEAGTNNEISQKYDYLVASSGLRRTWPSAPQSLNKDKYLEEVGEHIAKIKMANGGVVVIGGGAVGIEMASELKEMHPDLRVTLIHSRAKLLSSEPLPDEFRDRALELLHETGVETILGSRVIRTTQTELNGAATPSYTLSLTDGRTIKAGYVIN... | Cofactor: Binds 6-hydroxy-FAD non-covalently.
Function: Oxidoreductase; part of the gene cluster that mediates the biosynthesis of hydroxamate-containing siderophores that play a critical role in virulence via intracellular iron acquisition during macrophage infection .
Sequence Mass (Da): 50819
Sequence Length: 463
Pa... |
G4N285 | MTIKFASLILAGLGLGSGALGSVTFRREESSWTNDSLTSVFAQQAKGLFLPRTVISFQGQEWFENVTERWDIYAPPTFKVSVSPSTEKDVESAVKLAAKFKIPFLATGGRHGYGTTLGKLKNGLSIDLSLLNQFSIDSKAATITVGPGVRFRDIFTPLYEAGFQVPTGTCSCVGMIGATLGGGIGRLNGLDGLMIDALESARVVTADGRTLTVSEKENKDLFWGMRGAGQNFGVVVSATYKLKPLYAAGVWTNVDLIFSPDKNATYFDVVTSMEVPPQLTIASVVTYNATLDEPQLIATLTWTGPRDEALAAMKPILDVG... | Function: FAD-linked oxidoreductase; part of the gene cluster that mediates the biosynthesis of pyriculol and pyriculariol, two heptaketides that induce lesion formation upon application on rice leaves but are dispensable for pathogenicity . The highly reducing polyketide synthase synthesizes the heptaketide backbone o... |
Q7XTC7 | MAAAAAAATVEAVGVAGGRRRRSGSVALGDLLRREASAERASASASAGAGGRERERRPSVAAGQACRAKKGEDFALLKPACERLPAGGAPFSAFALFDGHNGSGAAVYAKENILSNVMCCVPADLSGDEWLAALPRALVAGFVKTDKDFQTRAHSSGTTVTFVIIDGYVVTVASVGDSRCVLEAEGTIYHLSADHRFDASEEEVGRVTECGGEVGRLNVVGGAEIGPLRCWPGGLCLSRSIGDQDVGEFIIPVPYVKQIKLSSAGGRIIISSDGVWDALTVDTAFSCARGLPPEAAADQIVKEAIASKGLRDDTTCIVID... | Cofactor: Binds 2 magnesium or manganese ions per subunit.
Function: Mediates the negative regulation of osmotic and salt stress tolerance through regulation of the jasmonate and abscisic acid signaling pathways and modulation of the raffinose family oligosaccharide metabolism pathway.
Catalytic Activity: H2O + O-phosp... |
Q9LRZ4 | MVLLPAFLDGLARTVSTKKGKKLSEDEDGGREIAKSMIKDSKKNSTLLGTSGFVSSESSKRFTSICSNRGEKGINQDRAIVWEGFGCQEDITFCGMFDGHGPWGHVIAKRVKKSFPSSLLCQWQQTLASLSSSPECSSPFDLWKQACLKTFSIIDLDLKISPSIDSYCSGCTALTAVLQGDHLVIANAGDSRAVIATTSDDGNGLVPVQLSVDFKPNIPEEAERIKQSDGRLFCLDDEPGVYRVGMPNGGSLGLAVSRAFGDYCLKDFGLVSEPEVTYRKITDKDQFLILATDGMWDVMTNNEAVEIVRGVKERRKSAKR... | Cofactor: Binds 2 magnesium or manganese ions per subunit.
Catalytic Activity: H2O + O-phospho-L-seryl-[protein] = L-seryl-[protein] + phosphate
Sequence Mass (Da): 38601
Sequence Length: 351
EC: 3.1.3.16
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Q0V7V2 | MSGSLMNLFSLCFKPFGHVCDNSEAGSGGGGGVSGGTGGEGKDGLLWFRDLGKYCGGDFSMAVIQANQVLEDQSQVESGNFGTFVGVYDGHGGPEAARYVCDHLFNHFREISAETQGVVTRETIERAFHATEEGFASIVSELWQEIPNLATVGTCCLVGVIYQNTLFVASLGDSRVVLGKKGNCGGLSAIQLSTEHNANNEDIRWELKDLHPDDPQIVVFRHGVWRVKGIIQVSRSIGDMYMKRPEFNKEPISQKFRIAEPMKRPLMSATPTILSHPLHPNDSFLIFASDGLWEHLTNEKAVEIVHNHPRAGSAKRLIKA... | Cofactor: Binds 2 magnesium or manganese ions per subunit.
Function: Dephosphorylates and represses plasma membrane H(+)-ATPases (PM H(+)-ATPases, e.g. AHA1 and AHA2), thus influencing negatively plant growth and fitness . Promotes the apical hook maintenance of etiolated seedlings .
Catalytic Activity: H2O + O-phospho... |
Q7XU84 | MAQPQRPLQVPDITKSTHSGGNTVLAYASSAMQGYRSTMEDAHATIENLDALTNTSFFGVYDGHGGSAVARYCANHLHNKVLEQEDFSSNLANALRQSFFRMDEMLRNQAASKELTEYGSGNEYWRTAGRSWLRCAPCVLGPVYCGPLAEGCTACVVLIRNTQIVVGNAGDARCVISRNGQAIALSNDHKPNFPEETQRIVAAGGSVSFSRGSHRVNNGIAVSRAIGDLSYKNNKKLRPEQQLLTCSPEIRADQLTDDTEFLVIACDGVWDVLANQAVVDFVRLHLNNGVELSVICESLLQEAITRDPPSTDNMSVILVR... | Cofactor: Binds 2 magnesium or manganese ions per subunit.
Catalytic Activity: H2O + O-phospho-L-seryl-[protein] = L-seryl-[protein] + phosphate
Sequence Mass (Da): 38170
Sequence Length: 352
EC: 3.1.3.16
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Q0JAA0 | MVGRMERQSASSSASCSPSSSAAGTSSSSSACGGKKRPDILNMIRSATCLNSSSTDTGKGRSKQSSNKVTHGFHLVEGKSGHDMEDYHVAEYKYDKSHELGLFAIFDGHLGDSVPSYLKANLFCNILKEPIFWTNPQEAIKNAYRSTNKYILENAKQLGPGGSTAVTAIVVDGKDMWVANVGDSRAVVCERGAANQLTVDHEPHTTNERQRIEKQGGFVTTFPGDVPRVNGQLAVARAFGDQSLKAHLSSEPDVRHVPINSSIEFVILASDGLWKVMKNQEAVDLVKSIKDPQAAAKRLTTEALARKSKDDISCIVIRFR... | Cofactor: Binds 2 magnesium or manganese ions per subunit.
Catalytic Activity: H2O + O-phospho-L-seryl-[protein] = L-seryl-[protein] + phosphate
Sequence Mass (Da): 34773
Sequence Length: 321
EC: 3.1.3.16
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Q7XR06 | MGYLSSVIPTDGSPVSGGGLSQNGKFSYGYASSPGKRASMEDFYETRIDSVDGQIIGLFGVFDGHGGAKVAEYVKQNLFSHLLRHPKFISDTKVAIDDAYKSTDSEFLESDSSQNQCGSTASTAVLVGDRLFVANVGDSRAIICRGGNAIAVSKDHKPDQTDERQRIEDAGGFVMWAGTWRVGGVLAVSRAFGDKLLKQYVVVDPEIREEVIDHSLEFLILASDGLWDVVTNEEAVDMTRSIHDPEEAAKKLLQEAYKRESSDNITCVVVRFLHGQGSSGYA | Cofactor: Binds 2 magnesium or manganese ions per subunit.
Catalytic Activity: H2O + O-phospho-L-seryl-[protein] = L-seryl-[protein] + phosphate
Sequence Mass (Da): 30584
Sequence Length: 282
EC: 3.1.3.16
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Q9SD12 | MLSTLMKLLSACLWPSSSSGKSSDSTGKQDGLLWYKDFGQHLVGEFSMAVVQANNLLEDQSQVESGPLSTLDSGPYGTFIGIYDGHGGPETSRFVNDHLFQHLKRFAAEQASMSVDVIKKAYEATEEGFLGVVTKQWPTKPQIAAVGSCCLVGVICGGMLYIANVGDSRAVLGRAMKATGEVIALQLSAEHNVSIESVRQEMHSLHPDDSHIVMLKHNVWRVKGLIQISRSIGDVYLKKAEFNKEPLYTKYRIREPFKRPILSGEPTITEHEIQPQDKFLIFASDGLWEQMSNQEAVDIVQNHPRNGIARRLVKMALQEA... | Cofactor: Binds 2 magnesium or manganese ions per subunit.
Function: May dephosphorylate and repress plasma membrane H(+)-ATPases (PM H(+)-ATPases, e.g. AHA1 and AHA2), thus influencing negatively plant growth and fitness.
Catalytic Activity: H2O + O-phospho-L-seryl-[protein] = L-seryl-[protein] + phosphate
Sequence Ma... |
A3AZ89 | MGNSLASLATPCFADAAAGGGRGRGHHAAGDDAVAFDDDDAAGGCNSIGHILSFDGRDAPAFAIHGVLLPSNPSTMASTGGGGGGGASVLNDGALSIGSSSFDSSNSFSFRTLQPRQYSGPLEYCTTSPSTSGASSSRQLGPRTDKQILNDIYANRQRRRCQGSKGPPLLGRLRKAVASLLRAGPCGFPEQEEPAAMINGVGVVRNGEESISRNVDAAAADDGAERVQWARGKAGEDRVHVVVSEEHGWMFVGIYDGFNGPDATDYLADNLYAAVCRELNGVLSEDEPDPPEAAAAAGRCNGCGGAARHREVLDAMARAL... | Cofactor: Binds 2 magnesium or manganese ions per subunit.
Catalytic Activity: H2O + O-phospho-L-seryl-[protein] = L-seryl-[protein] + phosphate
Sequence Mass (Da): 63480
Sequence Length: 593
EC: 3.1.3.16
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Q9SD02 | MAPVTEVSPMINTLEVADDKMTNLSSSGKPPRNISAMRHCNSTAWLTDYEGDERFGAKSPEGVNSTFQPVFRSGSWSDKGPKQSMEDEFICVDDLTEYIGSSTGAFYGVFDGHGGVDAASFTKKNIMKLVMEDKHFPTSTKKATRSAFVKTDHALADASSLDRSSGTTALTALILDKTMLIANAGDSRAVLGKRGRAIELSKDHKPNCTSERLRIEKLGGVIYDGYLNGQLSVARALGDWHIKGTKGSLCPLSCEPELEEIVLTEEDEYLIMGCDGLWDVMSSQCAVTMVRRELMQHNDPERCSQALVKEALQRNSCDNL... | Cofactor: Binds 2 magnesium or manganese ions per subunit.
Catalytic Activity: H2O + O-phospho-L-seryl-[protein] = L-seryl-[protein] + phosphate
Sequence Mass (Da): 39486
Sequence Length: 361
EC: 3.1.3.16
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Q6AUQ4 | MVAEAEVMHQPVPVLEVPYHRCVAKGVEEVAAAAAVAPPPVVEVEVAVQVPHMGLESAAGAPSISVDALQFVPSIRSGSFADIGPRRYMEDEHIRIDDLSAHLGSLLVCPLPSAFYGVFDGHGGLDAAAYMKRHAMRFLFEDSEFPQASQVDETYVQSVENSVRRAFLQADLALADDLDISRSSGTTALTALVFGRQLLVANAGDCRAVLCRRGVAMEMSRDHRANYAEECERVAASGGYIEDGYLNGVLSVTRALGDWDMKMPDGSISPLIAEPEFRQTMLTEDDEFLIMGCDGIWDVMTSQHAVSIVRRGLRQHDDPE... | Cofactor: Binds 2 magnesium or manganese ions per subunit.
Catalytic Activity: H2O + O-phospho-L-seryl-[protein] = L-seryl-[protein] + phosphate
Sequence Mass (Da): 42379
Sequence Length: 389
EC: 3.1.3.16
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Q6L482 | MRHISSLLQGLARSLSVGKERKGGDGDDGKAAAATATAVLRTSGTLWGEGSETFAAVCSRRGEKGINQDCSIVCEGFGCEEGSVLCGIFDGHGQWGHYVAKAVRESLPPALLRRWREAVTLAALIDGGEKRLCECRPDLWRQSYLAACAAVDAELRASRRLDAVHSGCTALSLVKHGDLLVVANVGDSRAVLATASPDDGGGARLAAVQLTVDFKPNLPQERERIMECNGRVQCLADEPGVHRVWRPDREGPGLAMSRAFGDYCVKDYGVISAPEVTHRRITAQDHFVILATDGVWDVVSNEEAVQIVASAPEREKAAKR... | Cofactor: Binds 2 magnesium or manganese ions per subunit.
Catalytic Activity: H2O + O-phospho-L-seryl-[protein] = L-seryl-[protein] + phosphate
Sequence Mass (Da): 38101
Sequence Length: 353
EC: 3.1.3.16
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Q3EAF9 | MVAEAEVVFQQSLPAVLEIELFDGVSSAVKSPVSSPKLGFTQSTASVSGSLTTSPVQADIFPEGDCDPSVLDYIPTIRSGSFADIGPKRNMEDEHIRIDDLSSQVGSLFELPKPSAFYAVFDGHGGPEAAAYVRENAIRFFFEDEQFPQTSEVSSVYVEEVETSLRNAFLQADLALAEDCSISDSCGTTALTALICGRLLMVANAGDCRAVLCRKGRAIDMSEDHKPINLLERRRVEESGGFITNDGYLNEVLAVTRALGDWDLKLPHGSQSPLISEPEIKQITLTEDDEFLVIGCDGIWDVLTSQEAVSIVRRGLNRHN... | Cofactor: Binds 2 magnesium or manganese ions per subunit.
Catalytic Activity: H2O + O-phospho-L-seryl-[protein] = L-seryl-[protein] + phosphate
Sequence Mass (Da): 41968
Sequence Length: 384
EC: 3.1.3.16
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Q65XG6 | MAAEICREEAAKSMPAAAAGATAIARRRRRVEGFRFAAGSLEPPQEDADAGVARCGKRQRVAGARAGAGAATAGPCRPSAGAEFGSRWWPRYGVTSVFGRRREMEDAVSIRPDFLRGSTSSGKHHFFGVFDGHGCSHVARMCQDRMHELVVDAYKKAVSGKEAAAAAPAWKDVMEKGFARMDDEATIWAKSRTGGEPACRCELQTPARCDHVGSTAVVAVVGPNRVVVANSGDSRAVLCRAGVPVPLSVDHKPDRPDELERIKAAGGRVIYWDGARVLGVLAMSRAIGDGYLKPYVTSEPEVTVTERADDDECLILASDG... | Cofactor: Binds 2 magnesium or manganese ions per subunit.
Catalytic Activity: H2O + O-phospho-L-seryl-[protein] = L-seryl-[protein] + phosphate
Sequence Mass (Da): 43783
Sequence Length: 416
EC: 3.1.3.16
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Q9M1V8 | MVELRQFSDLPIALSGISRIADPSPPPPVVAIRRRFKGGGNTRRIVFSVPLIFAFPFPTGTPKDVLVGIAAVFDGHSGSEASEMASQLLLDYFALHIYFLLDATFSKELTGKLPNSLMHLYDLDSQRFQDSLPLNFHLDILKEALLRAIYDIDATFTKEASTRKLDSGSTATIALIADGQLLVASIGDSKALLCSERYETPEEAKATLIKLYRERKRNQDSSPSRFSDLKLEHRTGLMRFIAKELTKDHHPDREDEMLRVKAAGGYVTKWAGVPRVNGQLAVSRSIGDLTYRSYGVISAPEVMDWQPLVANDSYLVVSSD... | Cofactor: Binds 2 magnesium or manganese ions per subunit.
Catalytic Activity: H2O + O-phospho-L-seryl-[protein] = L-seryl-[protein] + phosphate
Sequence Mass (Da): 46803
Sequence Length: 423
EC: 3.1.3.16
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Q49378 | MFSLKKLKSKLVGVSFVFSGVIALGTGVGLTSEHKYEHSPTLVLHEGETNSVGPRKITSEPWFYPVVGAGAGLIVVSLLLGLGIGIPIAKKKERMMIQEREEHQKMVESLGIIEEQNKTEAIEPTEEVNTQEPTQPAGVNVANNPQMGINQPQINPQFGPNPQQRINPQCFGGPMQPNQMGMRPGFNQMPPQMGGMPPNQMGMRPGFNQMPPQMGGMPPRPNFPNQMPNMNQPRPGFRPQPGGGVPMGNKAGGGFNHPGTPMGPNRMNFPNQGMNQPPHMAGPRAGFPPQNGPR | Function: Adhesin necessary for successful cytadherence and virulence.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 31784
Sequence Length: 294
Subcellular Location: Cell projection
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Q49417 | MELNGFLRYKKLFIVLALLFTTILIVSLSLLAFALVVKTNGSELGVVFHQTEDNTTVIQGRSIVEQPWFIPTVAGSFGFSALAIILGLAIGLPIVKRKEKRLLEEKERQEQIAEQLQRISDQQEQQTVEIDPQQSQAQPSQPQVQQPLQPQFQQRVPLLRPAFNPNMQQRPGFNQPNQQFQPHNNFNPRMNPNMQRPGFNPNMQQRPGFNQPNQQFQPHNNFNPRMNPNMQRPGFNQPHPNQFAQPNNFNPNMQQRPGFNPNMQQRPNPSQLMPKGGLKP | Function: Adhesin necessary for successful cytadherence and virulence.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 32150
Sequence Length: 280
Subcellular Location: Cell projection
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Q3T044 | MASRQPEVPALEPSGPLGKMSLPIGMYRRAFSYDDALEDPTPMTPPPSDMGSIPWKPVIPERKYQDLAKVEEGEPSVSPPAPAPPPATDSAEKAPVVKAKATHVIMSSLITKQTQESIQRFEQQAGLRDAGYTPHKGLTTEETKYLRVAEALHKLKLQSGETAREERQPASTQSTPSSSPQASPKQKSRGWFTSGSATALPGPSLSTMDSGSGDKDRSSADKWSLFGPRSLQKSESGGFAIQAYKGAQKPSPMEVMRAQATRRAEEPATFKPPKMDIPVMEGTKQLPRAHSLKPRDLNVLTPTGF | Function: Potential NADPH-dependent oxidoreductase. May be involved in the regulation of neuronal survival, differentiation and axonal outgrowth (By similarity).
Sequence Mass (Da): 32987
Sequence Length: 305
Subcellular Location: Cytoplasm
EC: 1.-.-.-
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A4QNZ7 | MVSRPGDLPALEAGPGSSEGLLGGMSIPAGMTRRALSYDDNLERPMSPPPSDINISNLWKRPVIPERKFARLAEEDESEGGVKQSASFESTKPIPVVKAKASSVMNSLIIKQTQESMQKFEKQAGLTDTGYTPHKGLNAEETRYHRLAESMHKLQMQSTDAKEERQPSSNQSTPAGTPQSSPKQKRRGWFNSQGSTASLTGSEMSTSSSSSVDLASAEGPIERWGVFGPRPQVSKSTTDPGTHPDTSGGFALQSYKGAQKPTPMEVMKAQATRLAEDPTNFKAPPKMEIPTMDGKRQVTRPHKLKHRDMNVLTPSGF | Function: Potential NADPH-dependent oxidoreductase.
Sequence Mass (Da): 34422
Sequence Length: 317
Subcellular Location: Cytoplasm
EC: 1.-.-.-
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Q96A73 | MASRQPEVPALEASAPLGKMSLPIGIYRRAVSYDDTLEDPAPMTPPPSDMGSVPWKPVIPERKYQHLAKVEEGEASLPSPAMTLSSAIDSVDKVPVVKAKATHVIMNSLITKQTQESIQHFERQAGLRDAGYTPHKGLTTEETKYLRVAEALHKLKLQSGEVTKEERQPASAQSTPSTTPHSSPKQRPRGWFTSGSSTALPGPNPSTMDSGSGDKDRNLSDKWSLFGPRSLQKYDSGSFATQAYRGAQKPSPLELIRAQANRMAEDPAALKPPKMDIPVMEGKKQPPRAHNLKPRDLNVLTPTGF | Function: Potential NADPH-dependent oxidoreductase. May be involved in the regulation of neuronal survival, differentiation and axonal outgrowth.
Sequence Mass (Da): 33247
Sequence Length: 305
Subcellular Location: Cytoplasm
EC: 1.-.-.-
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Q32NP7 | MASRQPDVPAIEHGSSGLLGKMSLPVGMHRRAFSYDDALDDTAPMTPPPSDMCSNTMWRKPIIPERKYQLLSKIEDGDSNIPPPSLPPSSSTEKVPVVKAKATSIIMNSLMTKHTQESIQRFEQQAGLRDAGYTPHKGLTSEETKYHRVAEALHKLNMHIGESTEEKQSSSAQSTPCSTPSSSPKQMRRSWFSQGSTSSLPAGDLSNSDGGVDKWSMFGPRAVQKSTTDPGGFTVQPYKGAQKPTPMELMRAQASRISDDPAALKPPKMEMPSLVSGTKNIPRGHNLKPRDMNILTPTGF | Function: Potential NADPH-dependent oxidoreductase.
Sequence Mass (Da): 32686
Sequence Length: 300
Subcellular Location: Cytoplasm
EC: 1.-.-.-
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Q83046 | MIMMSPLYALTKQCVIDTAYRLAVPTQHCAIYTVACRILFLSVGFMTIVKLCGFKMDTSSFIASIEKDNLMDCLISLVEMRDRLRLCNDFPILNYGVNILELLIGKRLNKINNLKNCYVIRELITINISKEWVGKQALKVGLHCFLNLSQADSRHVKYLLSDKESLNKMNFSRYYVPKVVTDLYLDLIGVLYVNTGYNIDLVEKFIFDKLEFLVYDGEEGFKSPQVEYNDICTVNNLKPIIKYNRWHTDGSIVIECGDVIGKGINKTKKKFAINDAKAEFVKNFKAKNKNNE | Function: Acts as a ssRNA-binding protein that may be involved in targeting RNA2 to replication sites or facilitating RNA2 replication.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 33523
Sequence Length: 292
Subcellular Location: Host endoplasmic reticulum membrane
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Q20065 | MRAVLLVCLLAGLAHADLFTAIADLQHMLGAEKDVTTIIDQYIEAERARLDDLRRYAHEYVHRNAHAESVGPEFVTNPINAYLLIKRLTTEWKKVENIMLNNKASTFLKNITDNRVRSEVKFPGEEDLSGAATALLRLQDTYSLDTLDLSNGIIGGEKVSNKLSGHDTFEVGRSAYNQKDYYHCLMWMQVALVKIENENPPTIEEWEILEYLAYSLYQQGNVRRALSLTKRLAKIAPNHPRAKGNVKWYEDMLQGKDMVGDLPPIVNKRVEYDGIVERDAYEALCRGEIPPVEPKWKNKLRCYLKRDKPFLKLAPIKVEI... | Cofactor: Binds 1 Fe(2+) ion per subunit.
Function: Catalyzes the post-translational formation of 4-hydroxyproline in -Xaa-Pro-Gly- sequences in collagens and other proteins.
Catalytic Activity: 2-oxoglutarate + L-prolyl-[collagen] + O2 = CO2 + succinate + trans-4-hydroxy-L-prolyl-[collagen]
Sequence Mass (Da): 61527
S... |
Q5ZLK5 | MKPWLCLVFFTSAFLIWHAEAEFFTSIGQMTDLIYAEKDLVQSLKEYIRAEETKLSQIKSWAEKMDVLTSKSTSDPEGYLAHPVNAYKLVKRLNTDWLELENLVLQDTTNGFITNLTIQRQFFPTEEDETGAAKALMRLQDTYKLDPETLSRGNLPGTKYRSSLTVSDCFGMGKTAYNDGDYYHTVLWMEQALKQHDEGEDTTVSKVEILDYLSYAVFQFGDLHRAMELTRRLISLDSTHERAGSNLRYFEKLLEKEREKPSNKTVATTEPVVQSGAYERPLDYLPERDIYEALCRGEGVKMTPRRQKRLFCRYHDGNRN... | Cofactor: Binds 1 Fe(2+) ion per subunit.
Function: Catalyzes the post-translational formation of 4-hydroxyproline in -Xaa-Pro-Gly- sequences in collagens and other proteins.
Catalytic Activity: 2-oxoglutarate + L-prolyl-[collagen] + O2 = CO2 + succinate + trans-4-hydroxy-L-prolyl-[collagen]
Sequence Mass (Da): 61435
S... |
O15460 | MKLWVSALLMAWFGVLSCVQAEFFTSIGHMTDLIYAEKELVQSLKEYILVEEAKLSKIKSWANKMEALTSKSAADAEGYLAHPVNAYKLVKRLNTDWPALEDLVLQDSAAGFIANLSVQRQFFPTDEDEIGAAKALMRLQDTYRLDPGTISRGELPGTKYQAMLSVDDCFGMGRSAYNEGDYYHTVLWMEQVLKQLDAGEEATTTKSQVLDYLSYAVFQLGDLHRALELTRRLLSLDPSHERAGGNLRYFEQLLEEEREKTLTNQTEAELATPEGIYERPVDYLPERDVYESLCRGEGVKLTPRRQKRLFCRYHHGNRAP... | Cofactor: Binds 1 Fe(2+) ion per subunit.
Function: Catalyzes the post-translational formation of 4-hydroxyproline in -Xaa-Pro-Gly- sequences in collagens and other proteins.
Catalytic Activity: 2-oxoglutarate + L-prolyl-[collagen] + O2 = CO2 + succinate + trans-4-hydroxy-L-prolyl-[collagen]
Sequence Mass (Da): 60902
S... |
Q7Z4N8 | MGPGARLAALLAVLALGTGDPERAAARGDTFSALTSVARALAPERRLLGLLRRYLRGEEARLRDLTRFYDKVLSLHEDSTTPVANPLLAFTLIKRLQSDWRNVVHSLEASENIRALKDGYEKVEQDLPAFEDLEGAARALMRLQDVYMLNVKGLARGVFQRVTGSAITDLYSPKRLFSLTGDDCFQVGKVAYDMGDYYHAIPWLEEAVSLFRGSYGEWKTEDEASLEDALDHLAFAYFRAGNVSCALSLSREFLLYSPDNKRMARNVLKYERLLAESPNHVVAEAVIQRPNIPHLQTRDTYEGLCQTLGSQPTLYQIPSL... | Cofactor: Binds 1 Fe(2+) ion per subunit.
Function: Catalyzes the post-translational formation of 4-hydroxyproline in -Xaa-Pro-Gly- sequences in collagens and other proteins.
PTM: N-glycosylation plays no role in the catalytic activity.
Catalytic Activity: 2-oxoglutarate + L-prolyl-[collagen] + O2 = CO2 + succinate + t... |
Q6W3F0 | MGPGARLALLALLALGGDPAAATGREDTFSALTSVARALAPERRLLGTLRRYLRGEEARLRDLTRFYDKVLSLHEDLKIPVVNPLLAFTVIKRLQSDWRNVVHSLEATENIRALKDGYEKVEQDLPAFEDLEGAARALMRLQDVYMLNVKGLARGVFQRVTGSSITDLYSPRQLFSLTADDCFQVGKVAYDTGDYYHAIPWLEEAVSLFRRAHGEWKTEDEASLEDALDYLAFACFQVGNVSCALSLSREFLVYSPDNKRMARNVLKYERLLAENGHQMAAETAIQRPNVPHLQTRDTYEGLCQTLGSQPTHYQIPSLYC... | Cofactor: Binds 1 Fe(2+) ion per subunit.
Function: Catalyzes the post-translational formation of 4-hydroxyproline in -Xaa-Pro-Gly- sequences in collagens and other proteins.
PTM: N-glycosylation plays no role in the catalytic activity.
Catalytic Activity: 2-oxoglutarate + L-prolyl-[collagen] + O2 = CO2 + succinate + t... |
Q86KR9 | MDISNLPPHIRQQILGLISKPQQNNDESSSSNNKNNLINNEKVSNVLIDLTSNLKIENFKIFNKESLNQLEKKGYLIIDNFLNDLNKINLIYDESYNQFKENKLIEAGMNKGTDKWKDKSIRGDYIQWIHRDSNSRIQDKDLSSTIRNINYLLDKLDLIKNEFDNVIPNFNSIKTQTQLAVYLNGGRYIKHRDSFYSSESLTISRRITMIYYVNKDWKKGDGGELRLYTNNPNNTNQKELKQTEEFIDIEPIADRLLIFLSPFLEHEVLQCNFEPRIAITTWIY | Cofactor: Binds 1 Fe(2+) ion per subunit.
Function: Catalyzes the post-translational formation of 4-hydroxyproline. Probably hydroxylates skp1 on Pro-143.
Catalytic Activity: 2-oxoglutarate + L-prolyl-[Skp1 protein] + O2 = CO2 + succinate + trans-4-hydroxy-L-prolyl-[Skp1 protein]
Sequence Mass (Da): 33348
Sequence Leng... |
Q9NXG6 | MAAAAVTGQRPETAAAEEASRPQWAPPDHCQAQAAAGLGDGEDAPVRPLCKPRGICSRAYFLVLMVFVHLYLGNVLALLLFVHYSNGDESSDPGPQHRAQGPGPEPTLGPLTRLEGIKVGHERKVQLVTDRDHFIRTLSLKPLLFEIPGFLTDEECRLIIHLAQMKGLQRSQILPTEEYEEAMSTMQVSQLDLFRLLDQNRDGHLQLREVLAQTRLGNGWWMTPESIQEMYAAIKADPDGDGVLSLQEFSNMDLRDFHKYMRSHKAESSELVRNSHHTWLYQGEGAHHIMRAIRQRVLRLTRLSPEIVELSEPLQVVRYG... | Cofactor: Binds 1 Fe(2+) ion per subunit.
Function: Catalyzes the post-translational formation of 4-hydroxyproline in hypoxia-inducible factor (HIF) alpha proteins. Hydroxylates HIF1A at 'Pro-402' and 'Pro-564'. May function as a cellular oxygen sensor and, under normoxic conditions, may target HIF through the hydroxyl... |
Q5UP57 | MKTVTIITIIVVIIVVILIIMVLSKSCVSHFRNVGSLNSRDVNLKDDFSYANIDDPYNKPFVLNNLINPTKCQEIMQFANGKLFDSQVLSGTDKNIRNSQQMWISKNNPMVKPIFENICRQFNVPFDNAEDLQVVRYLPNQYYNEHHDSCCDSSKQCSEFIERGGQRILTVLIYLNNEFSDGHTYFPNLNQKFKPKTGDALVFYPLANNSNKCHPYSLHAGMPVTSGEKWIANLWFRERKFS | Function: May catalyze the post-translational formation of 4-hydroxyproline in -Xaa-Pro-Gly- sequences in the 6 collagen-like proteins of Mimivirus.
Catalytic Activity: 2-oxoglutarate + L-prolyl-[collagen] + O2 = CO2 + succinate + trans-4-hydroxy-L-prolyl-[collagen]
Sequence Mass (Da): 27901
Sequence Length: 242
Subcel... |
Q989T9 | MTTRILGVVQLDQRRLTDDLAVLAKSNFSSEYSDFACGRWEFCMLRNQSGKQEEQRVVVHETPALATPLGQSLPYLNELLDNHFDRDSIRYARIIRISENACIIPHRDYLELEGKFIRVHLVLDTNEKCSNTEENNIFHMGRGEIWFLDASLPHSAGCFSPTPRLHLVVDIEGTRSLEEVAINVEQPSARNATVDTRKEWTDETLESVLGFSEIISEANYREIVAILAKLHFFHKVHCVDMYGWLKEICRRRGEPALIEKANSLERFYLIDRAAGEVMTY | Cofactor: Binds 1 Fe(2+) ion.
Function: Dioxygenase that catalyzes the 2-oxoglutarate-dependent selective hydroxylation of free L-proline to cis-4-hydroxy-L-proline (cis-4-Hyp).
Catalytic Activity: 2-oxoglutarate + L-proline + O2 = cis-4-hydroxy-L-proline + CO2 + succinate
Sequence Mass (Da): 32217
Sequence Length: 280... |
Q6PE18 | MDETSPLVSPLRDSNDFNYGPAEPTSPRGGFGSTPGSVVRLPAGSPGRSRERQPLLDRDRGASPRDPHRNEFPEDPEFREIIRKAERAIEEGIYPERIYQGSSGSYFVKDSAGKIIGVFKPKNEEPYGQLNPKWTKWLQKLCCPCCFGRDCLVLNQGYLSEAGASLVDQKLELNIVPRTKVVYLASETFNYSAIDRVKSRGKRLALEKVPKVGQRFHRIGLPPKVGSFQIFVEGYKDADFWLRRFEAEPLPENTNRQLQLQFERLVVLDYIIRNTDRGNDNWLIKYDYPMDTSSNRDSDWVLVKDPIIKLAAIDNGLAFP... | Function: Membrane-bound phosphatidylinositol-4 kinase (PI4-kinase) that catalyzes the phosphorylation of phosphatidylinositol (PI) to phosphatidylinositol 4-phosphate (PI4P), a lipid that plays important roles in endocytosis, Golgi function, protein sorting and membrane trafficking. Besides, phosphorylation of phospha... |
Q9BTU6 | MDETSPLVSPERAQPPDYTFPSGSGAHFPQVPGGAVRVAAAAGSGPSPPGSPGHDRERQPLLDRARGAAAQGQTQTVAAQAQALAAQAAAAAHAAQAHRERNEFPEDPEFEAVVRQAELAIERCIFPERIYQGSSGSYFVKDPQGRIIAVFKPKNEEPYGHLNPKWTKWLQKLCCPCCFGRDCLVLNQGYLSEAGASLVDQKLELNIVPRTKVVYLASETFNYSAIDRVKSRGKRLALEKVPKVGQRFNRIGLPPKVGSFQLFVEGYKDADYWLRRFEAEPLPENTNRQLLLQFERLVVLDYIIRNTDRGNDNWLIKYDC... | Function: Membrane-bound phosphatidylinositol-4 kinase (PI4-kinase) that catalyzes the phosphorylation of phosphatidylinositol (PI) to phosphatidylinositol 4-phosphate (PI4P), a lipid that plays important roles in endocytosis, Golgi function, protein sorting and membrane trafficking and is required for prolonged surviv... |
Q99M64 | MDETSPLVSPERAQPPEYTFPSVSGAHFPQVPGGAVRVAAAGSGPSPPCSPGHDRERQPLLDRARGAAAQGQTHTVAAQAQALAAQAAVAVHAVQTHRERNDFPEDPEFEVVVRQAEIAIECSIYPERIYQGSSGSYFVKDSQGRIIAVFKPKNEEPYGNLNPKWTKWLQKLCCPCCFGRDCLVLNQGYLSEAGASLVDQKLELNIVPRTKVVYLASETFNYSAIDRVKSRGKRLALEKVPKVGQRFNRIGLPPKVGSFQLFVEGYKDADYWLRRFEAEPLPENTNRQLLLQFERLVVLDYIIRNTDRGNDNWLIKYDYP... | Function: Membrane-bound phosphatidylinositol-4 kinase (PI4-kinase) that catalyzes the phosphorylation of phosphatidylinositol (PI) to phosphatidylinositol 4-phosphate (PI4P), a lipid that plays important roles in endocytosis, Golgi function, protein sorting and membrane trafficking and is required for prolonged surviv... |
O15350 | MAQSTATSPDGGTTFEHLWSSLEPDSTYFDLPQSSRGNNEVVGGTDSSMDVFHLEGMTTSVMAQFNLLSSTMDQMSSRAASASPYTPEHAASVPTHSPYAQPSSTFDTMSPAPVIPSNTDYPGPHHFEVTFQQSSTAKSATWTYSPLLKKLYCQIAKTCPIQIKVSTPPPPGTAIRAMPVYKKAEHVTDVVKRCPNHELGRDFNEGQSAPASHLIRVEGNNLSQYVDDPVTGRQSVVVPYEPPQVGTEFTTILYNFMCNSSCVGGMNRRPILIIITLEMRDGQVLGRRSFEGRICACPGRDRKADEDHYREQQALNESSA... | Cofactor: Binds 1 zinc ion per subunit.
Function: Participates in the apoptotic response to DNA damage. Isoforms containing the transactivation domain are pro-apoptotic, isoforms lacking the domain are anti-apoptotic and block the function of p53 and transactivating p73 isoforms. May be a tumor suppressor protein. Is a... |
Q7YXD4 | MKVISGLLFFILISCSLFLVQGQVDCVTNSSDASCTNFQYPLANITADINNLCGSMPYMPVCTIQQSCNQESSTSGICDPFSILGDSCLHDMPGMSGCNNFKKLCASGSVVEQCSTVDSVTDLPTTMKMWANIKSICNEMTMTGCEKCTILNATCDVLTVYSTLCLAMPEMGQCANWTQMCASSGNMASSPISSGICTDEPTPATDCFTNPSDPSCADYVYTAANANADILNLCKSMPYMTVCSIQKSCNQESSTSGICAPFSILGDSCLHDMPGMNGCSNFKKLCASGSVVEQCSSVDSISNLPTTMQLFAGIKSICTE... | Location Topology: Single-pass membrane protein
Sequence Mass (Da): 57633
Sequence Length: 530
Domain: The cytoplasmic domain (residues 431-481) is responsible for the endocytosis and localization of the protein to endocytic compartments.
Subcellular Location: Late endosome membrane
|
P27986 | MSAEGYQYRALYDYKKEREEDIDLHLGDILTVNKGSLVALGFSDGQEARPEEIGWLNGYNETTGERGDFPGTYVEYIGRKKISPPTPKPRPPRPLPVAPGSSKTEADVEQQALTLPDLAEQFAPPDIAPPLLIKLVEAIEKKGLECSTLYRTQSSSNLAELRQLLDCDTPSVDLEMIDVHVLADAFKRYLLDLPNPVIPAAVYSEMISLAPEVQSSEEYIQLLKKLIRSPSIPHQYWLTLQYLLKHFFKLSQTSSKNLLNARVLSEIFSPMLFRFSAASSDNTENLIKVIEILISTEWNERQPAPALPPKPPKPTTVANN... | Function: Binds to activated (phosphorylated) protein-Tyr kinases, through its SH2 domain, and acts as an adapter, mediating the association of the p110 catalytic unit to the plasma membrane. Necessary for the insulin-stimulated increase in glucose uptake and glycogen synthesis in insulin-sensitive tissues. Plays an im... |
P86523 | NLLQFGFMIRCANKRRRPVWPYEESGC | Cofactor: Binds 1 Ca(2+) ion.
Function: Heterotrimer: presynaptic neurotoxin. Inhibits nerve-evoked twitch contractions but not responses to cholinergic agonists acetylcholine and carbachol and to depolarizing agonist KCl. Causes a fade in tetanic contractions. Displays a triphasic mode of action with depression, enhan... |
G9I930 | MDKMNPAHLLVLAAVCVSLLGASSIPPQALNLNQFRLMIKCTNDRVWADFVDYGCYCVARDSNTPVDDLDRCCQAQKQCYDEAVKVHGCKPLVMFYSFECRYLASDLDCSGNNTKCRNFVCNCDRTATLCILTATYNRNNHKIDPSRCQ | Function: Heterodimer: MitTx, a heteromeric complex between Kunitz- and phospholipase-A2-like proteins, potently, persistently and selectively activates rat and chicken acid-sensing ion channel ASIC1 . Both alternatively spliced rat isoforms ASIC1a and ASIC1b are activated, with a higher potency for ASIC1a (EC(50)=9.4 ... |
P86374 | RGSXLTILPLRNIRDIFYVG | PTM: N-glycosylated.
Sequence Mass (Da): 2315
Sequence Length: 20
Subcellular Location: Secreted
EC: 3.4.23.-
|
P86370 | RGSXLTILPLRNISD | PTM: N-glycosylated.
Sequence Mass (Da): 1666
Sequence Length: 15
Subcellular Location: Secreted
EC: 3.4.23.-
|
Q9T0H9 | MKLTSLSKNANSTATAVTVSSIQKLPFLSLSETLPCPKSSRKPTFLPLRCRRRPKLDLLWGKFRVRASDAGVGSGSYSGGEEDGSQSSSLDQSPATSSESLKPRGPFPYSLSIALVLLSCGLVFSLITFVKGGPSSVLAAVAKSGFTAAFSLIFVSEIGDKTFFIAALLAMQYEKTLVLLGSMGALSLMTILSVVIGKIFQSVPAQFQTTLPIGEYAAIALLMFFGLKSIKDAWDLPPVEAKNGEETGIELGEYSEAEELVKEKASKKLTNPLEILWKSFSLVFFAEWGDRSMLATVALGAAQSPLGVASGAIAGHLVAT... | Function: Probable chloroplast-localized Mn(2+)/H(+) and/or Ca(2+)/H(+) antiporter regulating Ca(2+), Mn(2+) and pH homeostasis.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 37929
Sequence Length: 359
Subcellular Location: Plastid
|
P86373 | RGSXLTILPLRNKIDLFYVG | PTM: N-glycosylated.
Sequence Mass (Da): 2287
Sequence Length: 20
Subcellular Location: Secreted
EC: 3.4.23.-
|
Q9HUG6 | MFAATRLSRLRHDTSRILSHWILPLGWLALLTGMFWVGDRSDYHRLFYILLAAPTLLYVILQPRLLRPLTGSPLFIAFLAFSSYMMLSLSWSTPENSTGSLLKRPLYIALLFFCAAILALEAPLRLKTATWLAALGAVISAAATLLRYYWDANPLRLTGYGALYNPLLSAHVYGAFTALWLAYWMQSRPILAPLPLISLALLGGLLIATGSRTPLVGLTAALMWLVLAGDRKKALIALALALAGALLGYILYPEVITQRGASFRPEIWADALRQISEHPWLGHGYDHPMRIVLSNGMLLADPHNIELGVLFAGGIIGLLL... | Function: Potential O-antigen polymerase, which may be involved in the synthesis of LPS.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 44399
Sequence Length: 401
Pathway: Bacterial outer membrane biogenesis; LPS core biosynthesis.
Subcellular Location: Cell membrane
|
Q12447 | MASSSSTLPLHMYIRPLIIEDLKQILNLESQGFPPNERASEEIISFRLINCPELCSGLFIREIEGKEVKKETLIGHIMGTKIPHEYITIESMGKLQVESSNHIGIHSVVIKPEYQKKNLATLLLTDYIQKLSNQEIGNKIVLIAHEPLIPFYERVGFKIIAENTNVAKDKNFAEQKWIDMERELIKEEYDN | Function: Acetylates spermine and probably also other polyamines such as putrescine or spermidine. May regulate the levels of polyamines on chromosomal DNA, which would modify chromatin structure and affect transcription or replication. Also able to acetylate arylalkylamines such as tryptamine and serotonin in vitro.
S... |
P76077 | MTQEERFEQRIAQETAIEPQDWMPDAYRKTLIRQIGQHAHSEIVGMLPEGNWITRAPTLRRKAILLAKVQDEAGHGLYLYSAAETLGCAREDIYQKMLDGRMKYSSIFNYPTLSWADIGVIGWLVDGAAIVNQVALCRTSYGPYARAMVKICKEESFHQRQGFEACMALAQGSEAQKQMLQDAINRFWWPALMMFGPNDDNSPNSARSLTWKIKRFTNDELRQRFVDNTVPQVEMLGMTVPDPDLHFDTESGHYRFGEIDWQEFNEVINGRGICNQERLDAKRKAWEEGTWVREAALAHAQKQHARKVA | Function: Component of 1,2-phenylacetyl-CoA epoxidase multicomponent enzyme system which catalyzes the reduction of phenylacetyl-CoA (PA-CoA) to form 1,2-epoxyphenylacetyl-CoA. The subunit A is the catalytic subunit involved in the incorporation of one atom of molecular oxygen into phenylacetyl-CoA.
Catalytic Activity:... |
P76081 | MTTFHSLTVAKVESETRDAVTITFAVPQPLQEAYRFRPGQHLTLKASFDGEELRRCYSICRSYLPGEISVAVKAIEGGRFSRYAREHIRQGMTLEVMVPQGHFGYQPQAERQGRYLAIAAGSGITPMLAIIATTLQTEPESQFTLIYGNRTSQSMMFRQALADLKDKYPQRLQLLCIFSQETLDSDLLHGRIDGEKLQSLGASLINFRLYDEAFICGPAAMMDDAETALKALGMPDKTIHLERFNTPGTRVKRSVNVQSDGQKVTVRQDGRDREIVLNADDESILDAALRQGADLPYACKGGVCATCKCKVLRGKVAMET... | Cofactor: Binds 1 [2Fe-2S] cluster.
Function: Component of 1,2-phenylacetyl-CoA epoxidase multicomponent enzyme system which catalyzes the reduction of phenylacetyl-CoA (PA-CoA) to form 1,2-epoxyphenylacetyl-CoA. The subunit E is a reductase with a preference for NADPH and FAD, capable of reducing cytochrome c.
Sequenc... |
Q6FAW0 | MLISKRRMIHALSYEVILLVIIAIALSFIFDVPLEVTGTLGIVMAVTSVFWNMIFNHFFEKFERKHQLERTVKIRILHAIGFEGGLMLVTIPMVAYAMNMSLWQAIVLDFGLTMCILVYTFIFQWCYDTIEKRLGYTPRHS | Function: Mediates the efflux of short-chain diamines when energized by an electrochemical gradient (By similarity). Involved in resistance to the synthetic biocide chlorhexidine, a widely used antiseptic and disinfectant in both hospital and community settings . Interacts directly with chlorhexidine and mediates its e... |
P0DUT9 | MLISKRRLIHAISYEGILLVIIAIALSFIFNMPMEVTGTLGVFMAVVSVFWNMIFNHYFEKVEHKYNWERTIPVRILHAIGFEGGLLIATVPMIAYMMQMTVIDAFILDIGLTLCILVYTFIFQWCYDHIEDKFFPNAKAASLH | Function: Mediates the efflux of short-chain diamines when energized by an electrochemical gradient . Recognizes specifically the short-chain diamines cadaverine and putrescine as substrates, and promotes the active transport of these substrates in exchange for a cation . Protons are probably the primary source of ener... |
Q87QJ4 | MTRNERIFHAVLFELMALAIIVPAAALITGKGSSDLALVGIGLSLYTVVWNYIYNLYFDKWFGSNRADRSLAMRLGHTVGFEGGLIFISIPVIAWFLEITFLRALMLEAGFLVFFLFYATGFNWLYDKVQPFGKMRKLLV | Function: Mediates the efflux of short-chain diamines when energized by an electrochemical gradient (By similarity). Confers resistance to chlorhexidine, benzalkonium, proflavine and acriflavine. Mediates efflux of both proflavine and acriflavine via an energy-dependent mechanism .
Location Topology: Multi-pass membran... |
Q4V920 | MSGAYDESAMSDETTDSFWEVGNYKRTVKRIEDGHRLCNDMMSCIQERAKIEKAYSQQLTDWSKRWRQLVERGPQYGTLERAWLAVMTEAEKVSELHQEVKNNLLNEDLEKVKNWQKDAYHKQMMGGFKETKEADEGFRKAQKPWAKKLKELETAKKTYHMACKEEKIASAREANSKGEASVTTDQQKKLQEKVDKCKNDVQKAKEKYEKSLDELNKCTPQYMENMEVVFDQCQQFEEKRLNFLREVLLDTKRHLNLTESQSYATVYRELERTIVSASAQEDLKWFSSVHGPGMHMNWPQFEEFNPDLSHAISKKEKVKR... | Function: Binds to membranes via its F-BAR domain and mediates membrane tubulation. Plays a role in cellular transport processes by recruiting dynamins to membranes. Plays a role in the reorganization of the actin cytoskeleton and in neuron morphogenesis via its interaction with cobl, and by recruiting cobl to the cell... |
Q9Z0W5 | MSGPYDEASEEITDSFWEVGNYKRTVKRIDDGHRLCNDLMSCVQERAKIEKAYAQQLTDWAKRWRQLIEKGPQYGSLERAWGAMMTEADKVSELHQEVKNSLLNEDLEKVKNWQKDAYHKQIMGGFKETKEAEDGFRKAQKPWAKKMKELEAAKKAYHLACKEEKLAMTREMNSKTEQSVTPEQQKKLVDKVDKCRQDVQKTQEKYEKVLEDVGKTTPQYMEGMEQVFEQCQQFEEKRLVFLKEVLLDIKRHLNLAENSSYIHVYRELEQAIRGADAQEDLRWFRSTSGPGMPMNWPQFEEWNPDLPHTAAKKEKQPKKA... | Function: Binds to membranes via its F-BAR domain and mediates membrane tubulation. Plays a role in the reorganization of the microtubule cytoskeleton via its interaction with MAPT; this decreases microtubule stability and inhibits MAPT-induced microtubule polymerization. Plays a role in cellular transport processes by... |
O13154 | MSGSYDDSVGVEVSSDSFWEVGNYKRTVKRIDDGHRLCNDLMNCIHERARIEKVYAQQLTEWAKRWKQLVEKGPQYGTVERAWCAFMSEAEKVSELHLEVKGSLMNEDFEKIKNWQKEAFHKQMMGGFKETKEAEDGFRKAQKPWAKKLKEVEAAKKAYHAACKEEKLAISRETNSKADPALNPEQLKKLQDKVERSKQDVLKTKAKYEKSLKELDNATPQYMENMEQVFEQCQQFEEKRLRFFREVLLEVQKHLDLSNVASYKNIYRELEQNIKTADAVEDLRWFRANQGPGMSMNWPQFEDDEWSADLNRTLSRREKK... | Function: Regulates the morphogenesis and endocytosis of caveolae (By similarity). Lipid-binding protein that is able to promote the tubulation of the phosphatidic acid-containing membranes it preferentially binds. Plays a role in intracellular vesicle-mediated transport. Involved in the endocytosis of cell-surface rec... |
Q9UNF0 | MSVTYDDSVGVEVSSDSFWEVGNYKRTVKRIDDGHRLCSDLMNCLHERARIEKAYAQQLTEWARRWRQLVEKGPQYGTVEKAWMAFMSEAERVSELHLEVKASLMNDDFEKIKNWQKEAFHKQMMGGFKETKEAEDGFRKAQKPWAKKLKEVEAAKKAHHAACKEEKLAISREANSKADPSLNPEQLKKLQDKIEKCKQDVLKTKEKYEKSLKELDQGTPQYMENMEQVFEQCQQFEEKRLRFFREVLLEVQKHLDLSNVAGYKAIYHDLEQSIRAADAVEDLRWFRANHGPGMAMNWPQFEEWSADLNRTLSRREKKKA... | Function: Regulates the morphogenesis and endocytosis of caveolae (By similarity). Lipid-binding protein that is able to promote the tubulation of the phosphatidic acid-containing membranes it preferentially binds. Plays a role in intracellular vesicle-mediated transport. Involved in the endocytosis of cell-surface rec... |
Q9UKS6 | MAPEEDAGGEALGGSFWEAGNYRRTVQRVEDGHRLCGDLVSCFQERARIEKAYAQQLADWARKWRGTVEKGPQYGTLEKAWHAFFTAAERLSALHLEVREKLQGQDSERVRAWQRGAFHRPVLGGFRESRAAEDGFRKAQKPWLKRLKEVEASKKSYHAARKDEKTAQTRESHAKADSAVSQEQLRKLQERVERCAKEAEKTKAQYEQTLAELHRYTPRYMEDMEQAFETCQAAERQRLLFFKDMLLTLHQHLDLSSSEKFHELHRDLHQGIEAASDEEDLRWWRSTHGPGMAMNWPQFEEWSLDTQRTISRKEKGGRSP... | Function: Plays a role in endocytosis and regulates internalization of plasma membrane proteins. Overexpression impairs internalization of SLC2A1/GLUT1 and TRPV4 and increases the levels of SLC2A1/GLUT1 and TRPV4 at the cell membrane. Inhibits the TRPV4 calcium channel activity (By similarity).
PTM: Phosphorylated by c... |
Q28057 | MKWLVLLGLVALSECIVILPLKKMKTLRETLREKNLLNNFLEEQAYRLSKNDSKITIHPLRNYLDTAYVGNITIGTPPQEFRVVFDTGSANLWVPCITCTSPACYTHKTFNPQNSSSFREVGSPITIFYGSGIIQGFLGSDTVRIGNLVSPEQSFGLSLEEYGFDSLPFDGILGLAFPAMGIEDTIPIFDNLWSHGAFSEPVFAFYLNTNKPEGSVVMFGGVDHRYYKGELNWIPVSQTSHWQISMNNISMNGTVTACSCGCEALLDTGTSMIYGPTKLVTNIHKLMNARLENSEYVVSCDAVKTLPPVIFNINGIDYPL... | Function: PAG2 or a processed derivative of this molecule might represent a factor that binds the LH receptor.
PTM: N-Glycosylated; the glycans terminate in either N-acetyl-galactosamine (GalNAc) or N-acetyllactosamine . Terminal GalNAc on Asn-linked glycans is greatly reduced prior to parturition while lactosamine-typ... |
P83202 | RGSXLTILPLRNMRDIVY | PTM: Glycosylated.
Sequence Mass (Da): 2129
Sequence Length: 18
Subcellular Location: Secreted
EC: 3.4.23.-
|
P83203 | ISSRVSXLTIHPLRNIMDML | PTM: Glycosylated.
Sequence Mass (Da): 2308
Sequence Length: 20
Subcellular Location: Secreted
EC: 3.4.23.-
|
P86371 | RGSXLTHLPLRNISD | PTM: N-glycosylated.
Sequence Mass (Da): 1690
Sequence Length: 15
Subcellular Location: Secreted
EC: 3.4.23.-
|
P85049 | RGSXLTILPLRNIID | PTM: N-glycosylated.
Sequence Mass (Da): 1692
Sequence Length: 15
Subcellular Location: Secreted
EC: 3.4.23.-
|
P84916 | RGSNLTSLPLQNVIDLFYVGNITIG | PTM: N-glycosylated.
Sequence Mass (Da): 2705
Sequence Length: 25
Subcellular Location: Secreted
EC: 3.4.23.-
|
P85048 | RGSXLTIHPLRNIRDFFYVG | PTM: N-glycosylated.
Sequence Mass (Da): 2373
Sequence Length: 20
Subcellular Location: Secreted
EC: 3.4.23.-
|
P0DPA0 | MEEILKSFKISIDNEGYSKSFSLEDLDNFNNNNNNNNNNNNNEENNPYEFFERYGFLVIRNVISEEDCNKTVGEIFDIIESKVKTFDRNDQSTWDQTFSEDGSSIPQYGSPSKPPIFKKQFLMNRTNPNVYKVFSKLLKNQDLMVNHDRACFFRPTLVNPKWKTNDNVHLDMNPYNWMGNGDICREELSKLTYARLGEFIVENNQPTQNDGLQLQGVINLLDNQELDGGYCVTPGFHTIFNEYFTSKKPQYTSPSWNFDKKDIAFKYAKRISMRKGSIVVWNQQMPHGSMSNKSFNPRMAQFIKIFPTSTVNSVRYQHRK... | Function: Converts phytanoyl-CoA to 2-hydroxyphytanoyl-CoA.
Catalytic Activity: 2-oxoglutarate + O2 + phytanoyl-CoA = 2-hydroxyphytanoyl-CoA + CO2 + succinate
Sequence Mass (Da): 40645
Sequence Length: 349
Pathway: Lipid metabolism; fatty acid metabolism.
EC: 1.14.11.18
|
O14832 | MEQLRAAARLQIVLGHLGRPSAGAVVAHPTSGTISSASFHPQQFQYTLDNNVLTLEQRKFYEENGFLVIKNLVPDADIQRFRNEFEKICRKEVKPLGLTVMRDVTISKSEYAPSEKMITKVQDFQEDKELFRYCTLPEILKYVECFTGPNIMAMHTMLINKPPDSGKKTSRHPLHQDLHYFPFRPSDLIVCAWTAMEHISRNNGCLVVLPGTHKGSLKPHDYPKWEGGVNKMFHGIQDYEENKARVHLVMEKGDTVFFHPLLIHGSGQNKTQGFRKAISCHFASADCHYIDVKGTSQENIEKEVVGIAHKFFGAENSVNL... | Function: Catalyzes the 2-hydroxylation of not only racemic phytanoyl-CoA and the isomers of 3-methylhexadecanoyl-CoA, but also a variety of other mono-branched 3-methylacyl-CoA esters (with a chain length of at least seven carbon atoms) and straight-chain acyl-CoA esters (with a chain length longer than four carbon at... |
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