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Q0VCI1 | MPAVLGFEGSANKIGVGVVRDGKVLANPRRTYVTPPGTGFLPGDTARHHRAVILDLLQEALTEAGLTSEDIDCIAYTKGPGMGAPLVSVAVVARTVAQLWNKPLLGVNHCIGHIEMGRLITGATNPTVLYVSGGNTQVIAYSEHRYRIFGETIDIAVGNCLDRFARVLKISNDPSPGYNIEQMAKRGKKLVELPYTVKGMDVSFSGILSFIEDVAQRMLATGECTPEDLCFSLQETVFAMLVEITERAMAHCGSQEALIVGGVGCNVRLQEMMETMCQERGARLFATDERFCIDNGAMIAQAGWEMFQAGHRTPLSESGITQRYRTDEVEVTWRD | 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 threonylcarbamoyl moiety of threonylcarbamoyl-AMP (TC-AMP) to the N6 group of A37. OSGEP likely plays a direct catalytic role in this reaction, but requires other protein(s) of the complex to fulfill this activity.
Catalytic Activity: adenosine(37) in tRNA + L-threonylcarbamoyladenylate = AMP + H(+) + N(6)-L-threonylcarbamoyladenosine(37) in tRNA
Sequence Mass (Da): 36502
Sequence Length: 335
Subcellular Location: Cytoplasm
EC: 2.3.1.234
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P45971 | MRWLPGLLLIASIGFHQSLADRVLVLGETAAVKDTHSVFLNSVKERGHELTVRAADDSQLALFKHGQLIFDHLFILAPGVQVFGGSLSPSEISKFVDAGGNVLVAAGSNIGDALREIAAEHGFEFEEAGTSVIDHHNYDQTLDSGDHTTLVVGKDQLISAELIVGNSAKLHPVLFKGIGLVAGKTNNLALSIVRASGTAYSYDPKAVRATNPSIAGSRTLLVGGLQSRNNARIVFTGSSELFSNTFFSAKTNSVNPSVQGAQSGNADFATAITRWVMKESGVLRVKTVNHHKKGETVPPVEGYFITEDVVYTIEIEELKNGKWVPFQGKDVQLEFVRIDPFVRATLKNSNGRLSVAFKLPDVLGVFKFLVDYRRVGYTHLYDVQQVSVRPLWHTQYERFIRSAYPYYASSFSMMAGLVLFSIVYLYHKDTPVKGAKVLDSEKKKN | 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 protein N-glycosylation. N-glycosylation occurs cotranslationally and the complex associates with the Sec61 complex at the channel-forming translocon complex that mediates protein translocation across the endoplasmic reticulum (ER). All subunits are required for a maximal enzyme activity (By similarity). Required for the assembly of both SST3A- and SS3B-containing OST complexes (By similarity). Required for normal lifespan .
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 48760
Sequence Length: 445
Pathway: Protein modification; protein glycosylation.
Subcellular Location: Endoplasmic reticulum membrane
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Q54E62 | MMMKSILITFIIASALLSSVFADIGGKRTLVVLDDLSIKKTHSTFFKNLENKGYKLQFEQSNTKVVLEKYGDFNFDNLILFSPTSESLSFSSADVTRFIDGGNNVLFAGSNVISENIRDIAAECGMEIEEDKTLIFDHFNYDKSQSDHSVLVADQFIDDSPIILQGLNKPILFKGIGHKIRNNPLNYAILTGSSTAFSAKAISGVSTKLMGKSCGLVSSLQARNNARVTFSGSLDLFSDKSFYSKIDNKESGNKEFVERLVSWTFQERGILRASELELVKISTESNSTVAPDVFTIKDEVKYSLKVEEFDGIKGKWVPYVGSLQLEVIMLDPYIRTFIKGDANGLYKIHFKLPDVYGVFTFEASIHKSGYSTLDHIYRKPILPFRHDSYERFIPAAFPYYATCFSMLIGTFIFSIIFLFNKDQLNK | 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 protein N-glycosylation. N-glycosylation occurs cotranslationally and the complex associates with the Sec61 complex at the channel-forming translocon complex that mediates protein translocation across the endoplasmic reticulum (ER). All subunits are required for a maximal enzyme activity.
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 47889
Sequence Length: 426
Pathway: Protein modification; protein glycosylation.
Subcellular Location: Endoplasmic reticulum membrane
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P39656 | MGYFRCARAGSFGRRRKMEPSTAARAWALFWLLLPLLGAVCASGPRTLVLLDNLNVRETHSLFFRSLKDRGFELTFKTADDPSLSLIKYGEFLYDNLIIFSPSVEDFGGNINVETISAFIDGGGSVLVAASSDIGDPLRELGSECGIEFDEEKTAVIDHHNYDISDLGQHTLIVADTENLLKAPTIVGKSSLNPILFRGVGMVADPDNPLVLDILTGSSTSYSFFPDKPITQYPHAVGKNTLLIAGLQARNNARVIFSGSLDFFSDSFFNSAVQKAAPGSQRYSQTGNYELAVALSRWVFKEEGVLRVGPVSHHRVGETAPPNAYTVTDLVEYSIVIQQLSNGKWVPFDGDDIQLEFVRIDPFVRTFLKKKGGKYSVQFKLPDVYGVFQFKVDYNRLGYTHLYSSTQVSVRPLQHTQYERFIPSAYPYYASAFSMMLGLFIFSIVFLHMKEKEKSD | 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 protein N-glycosylation . N-glycosylation occurs cotranslationally and the complex associates with the Sec61 complex at the channel-forming translocon complex that mediates protein translocation across the endoplasmic reticulum (ER). All subunits are required for a maximal enzyme activity (By similarity). Required for the assembly of both SST3A- and SS3B-containing OST complexes .
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 50801
Sequence Length: 456
Pathway: Protein modification; protein glycosylation.
Subcellular Location: Endoplasmic reticulum membrane
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Q6ZLK0 | MAAPRHHHLALAVALALLVVTAAAADEGGPRGRRVLVLVDDLAVRSSHSAFFASLQGRGFDLDFRLADDPKLSLHRYGQYLYDGLVLFAPSTPRFGGSVDQNSILEFIDAGHDMILAADSSASDLIRGIATECGVDFDEDPEAMVIDHINYAATDAEGDHTLIAGDDLIQSDVILGSKKIEAPVLFRGIGHAVNPSNSLVLKVLSASPSAYSANPKSKLASPPSLTGSAISLVSVMQARNNARVLISGSLDLFSNRFLKSGVQKAGSKIRHEKAGNEQFVTETSKWVFHERGHLKAVNVKHNKVGETNEPGMYRINDDLEYSVEIYEWSGTSWKPYVADDVQVQFYMMSPYVLKTLSTDKKGVFSTSFKVPDVYGVFQFKVEYQRLGYTGLSLSKQIPVRPYRHNEYERFITSAYPYYAASFSTMGAFFIFSFVYLYHK | 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 protein N-glycosylation. N-glycosylation occurs cotranslationally and the complex associates with the Sec61 complex at the channel-forming translocon complex that mediates protein translocation across the endoplasmic reticulum (ER). All subunits are required for a maximal enzyme activity.
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 48390
Sequence Length: 439
Pathway: Protein modification; protein glycosylation.
Subcellular Location: Endoplasmic reticulum membrane
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Q6GNR9 | MASLRLSVLLVSVSWLLLLVSGLRAGPRTLVLMENINLRETHSLFFRSLSDRGFDLSFKTADDPSLSLIKYGEFLYDNLIIFSPSVEDFGGNINIETISSFIDGGGSVLVAASSDIGDPLRELGSECGIEFDEEKTAVIDHHNYDISDPGQHTLIVADSENLLKAPTIVGKTPLNPILFRGVGMVADPDNPLVLDILTGSSTSYSFFPDKPITQYPHAVGKNTLLIAGLQARNNARVVFSGSLDFFSDSFFNSAVQKAASGSNRYAKTGNYELAMALSRWVFKEEGVLRVGEVSHHRVGESSPPSAYTVTDLVEYSIVIEKLSDGKWVPFDGDDIQLEFVRIDPFVRTFLKKNGGKYSVQFKLPDVYGVFQFKVDYNRLGYTHLYSTTQISVRPLQHTQYERFIPSAYPYYASAFSVMFGLFIFSIVFLHMKEKEKSD | 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 protein N-glycosylation (By similarity). N-glycosylation occurs cotranslationally and the complex associates with the Sec61 complex at the channel-forming translocon complex that mediates protein translocation across the endoplasmic reticulum (ER). All subunits are required for a maximal enzyme activity (By similarity). Required for the assembly of both SST3A- and SS3B-containing OST complexes (By similarity).
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 48712
Sequence Length: 438
Pathway: Protein modification; protein glycosylation.
Subcellular Location: Endoplasmic reticulum membrane
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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 protein N-glycosylation. N-glycosylation occurs cotranslationally and the complex associates with the Sec61 complex at the channel-forming translocon complex that mediates protein translocation across the endoplasmic reticulum (ER). All subunits are required for a maximal enzyme activity.
Location Topology: Single-pass type III membrane protein
Sequence Mass (Da): 4197
Sequence Length: 37
Subcellular Location: Endoplasmic reticulum membrane
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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 protein N-glycosylation. N-glycosylation occurs cotranslationally and the complex associates with the Sec61 complex at the channel-forming translocon complex that mediates protein translocation across the endoplasmic reticulum (ER). All subunits are required for a maximal enzyme activity.
Location Topology: Single-pass type III membrane protein
Sequence Mass (Da): 4306
Sequence Length: 37
Subcellular Location: Endoplasmic reticulum membrane
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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 protein N-glycosylation. N-glycosylation occurs cotranslationally and the complex associates with the Sec61 complex at the channel-forming translocon complex that mediates protein translocation across the endoplasmic reticulum (ER). All subunits are required for a maximal enzyme activity.
Location Topology: Single-pass type III membrane protein
Sequence Mass (Da): 4133
Sequence Length: 35
Subcellular Location: Endoplasmic reticulum membrane
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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 protein N-glycosylation. N-glycosylation occurs cotranslationally and the complex associates with the Sec61 complex at the channel-forming translocon complex that mediates protein translocation across the endoplasmic reticulum (ER). All subunits are required for a maximal enzyme activity.
Location Topology: Single-pass type III membrane protein
Sequence Mass (Da): 4326
Sequence Length: 37
Subcellular Location: Endoplasmic reticulum membrane
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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 protein N-glycosylation. N-glycosylation occurs cotranslationally and the complex associates with the Sec61 complex at the channel-forming translocon complex that mediates protein translocation across the endoplasmic reticulum (ER). All subunits are required for a maximal enzyme activity.
Location Topology: Single-pass type III membrane protein
Sequence Mass (Da): 6672
Sequence Length: 60
Pathway: Protein modification; protein glycosylation.
Subcellular Location: Endoplasmic reticulum membrane
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Q86WC4 | MEPGPTAAQRRCSLPPWLPLGLLLWSGLALGALPFGSSPHRVFHDLLSEQQLLEVEDLSLSLLQGGGLGPLSLPPDLPDLDPECRELLLDFANSSAELTGCLVRSARPVRLCQTCYPLFQQVVSKMDNISRAAGNTSESQSCARSLLMADRMQIVVILSEFFNTTWQEANCANCLTNNSEELSNSTVYFLNLFNHTLTCFEHNLQGNAHSLLQTKNYSEVCKNCREAYKTLSSLYSEMQKMNELENKAEPGTHLCIDVEDAMNITRKLWSRTFNCSVPCSDTVPVIAVSVFILFLPVVFYLSSFLHSEQKKRKLILPKRLKSSTSFANIQENSN | 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: 334
Subcellular Location: Lysosome membrane
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Q8BGT0 | MARDAELARSSGWPWRWLPALLLLQLLRWRCALCALPFTSSRHPGFADLLSEQQLLEVQDLTLSLLQGGGLGPLSLLPPDLPDLEPECRELLMDFANSSAELTACMVRSARPVRLCQTCYPLFQQVAIKMDNISRNIGNTSEGPRCGGSLLTADRMQIVLMVSEFFNSTWQEANCANCLTNNGEDLSNNTEDFLSLFNKTLACFEHNLQGHTYSLLPPKNYSEVCRNCKEAYKNLSLLYSQMQKLNGLENKAEPETHLCIDVEDAMNITRKLWSRTFNCSVTCSDTVSVVAVSVFILFLPVVFYLSSFLHSEQKKRKLILPKRLKSSTSFANIQENAT | 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: 338
Subcellular Location: Lysosome membrane
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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 the S-x-E/pS motif (By similarity). The phosphorylated form inhibits hydroxyapatite crystallization. Dephosphorylation via a mechanism involving ALPL/TNAP promotes hydroxyapatite crystallization (By similarity).
Sequence Mass (Da): 30904
Sequence Length: 278
Subcellular Location: Secreted
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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 residue, forming homopolymers and heteropolymers, increasing its collagen binding properties.
Sequence Mass (Da): 35423
Sequence Length: 314
Subcellular Location: Secreted
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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). The phosphorylated form inhibits hydroxyapatite crystallization . Dephosphorylation via a mechanism involving ALPL/TNAP promotes hydroxyapatite crystallization .
Sequence Mass (Da): 32459
Sequence Length: 294
Subcellular Location: Secreted
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A5VIM0 | MAFNLRNRSFLTLADFNTREMEYMLDLAEDLKKAKYAGYEGKNLKGKNIALIFEKSSTRTRCSFEVGAKDEGAHVTYLGPSGSHIGHKESVKDTARVLGGMFDGIEYRGFSQRNVEILAKYSGVPVWNGLTDEDHPTQVLADFLTAHEVLKKPYKDIKFAFVGDGQDNVSNALMLGAAVMGMEYHVVTPKELEPTKETLDKANEIAAKTGAKIVVTNDIKEGVKGMDVIYADVWVSMGESDDMWEKRINLLKPYQVTMDVMKATENPNVLFEHCLPAFHNLDTEVGKEIEKKFGLKEMEVTDEVFESEHSVVFREAENRMHTIKAVMVATLGEQN | 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 degradation; L-arginine degradation via ADI pathway; carbamoyl phosphate from L-arginine: step 2/2.
Subcellular Location: Cytoplasm
EC: 2.1.3.3
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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 biosynthesis; L-arginine biosynthesis; L-arginine from L-ornithine and carbamoyl phosphate: step 1/3.
Subcellular Location: Cytoplasm
EC: 2.1.3.3
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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 biosynthesis; L-arginine biosynthesis; L-arginine from L-ornithine and carbamoyl phosphate: step 1/3.
Subcellular Location: Cytoplasm
EC: 2.1.3.3
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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 degradation; L-arginine degradation via ADI pathway; carbamoyl phosphate from L-arginine: step 2/2.
Subcellular Location: Cytoplasm
EC: 2.1.3.3
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Q9XIP2 | MTRILVQRGSSGSSSNSSRPSSSSSSSSGSETQINNNIPVPPVTIDEEITDEKQEEVTVVEKAECSDAKDVAVDSDEPADREDDEGLVVAENVHVQSEGIDCDSPVSGGSNSDSPPVPAPPPKPSSTVNPGSNRSVLGSFGALRIGPTRRAAGPRSLVSSRSSPTGSHPSSPRSHSENEGYNSSDEHMPCYVPSHPGSGLEREHQFEAEIRYSKGFEIRRMLEDGNCLFRAVADQVYGDSEAYDLARQMCMDYMEQERDHFSQFITEGFTSYLKRKRRDKVYGNNVEIQALAEMYNRPIHIYSYSTEPINIFQGNYSTDTPPIRLSYHHGNHYNSLVDPHRLTVGAGLGFSSLSGRHVDKEQVKAAIKAQQEHQIDNALLAEGRFYSDLELTEKEIERSVMEASRAEYLMEWSKPRIGPKESSTSNAETSSSGARPSGSDSKPAEAVKEKTVLSSSIEMVLSMGFSYAQAMEAYSIFGDDVDSMVCYVLETSCGGNNRRKGKATE | 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 . Can both repress (e.g. OSR2) and promote (e.g. AN3) the expression of target genes by associating with chromatin, deubiquitinating H2B and regulating its euchromatic histone marks (e.g. H3ac and H3K4me) . In association with LDL1/KDM1C, involved in transcriptional gene repression via histone deubiquitination and demethylation . Promotes the concerted epigenetic regulation and repression (e.g. the removal of euchromatic histone acetylation, ubiquitination, and methylation marks) of a set of genes (e.g. GA20OX, WUS, OSR2, ARL and ABI5) that collectively limit plant growth thus stimulating plant growth and increasing cell size .
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).
Sequence Mass (Da): 55274
Sequence Length: 505
Subcellular Location: Nucleus
EC: 3.4.19.12
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Q8TE49 | MVSSVLPNPTSAECWAALLHDPMTLDMDAVLSDFVRSTGAEPGLARDLLEGKNWDLTAALSDYEQLRQVHTANLPHVFNEGRGPKQPEREPQPGHKVERPCLQRQDDIAQEKRLSRGISHASSAIVSLARSHVASECNNEQFPLEMPIYTFQLPDLSVYSEDFRSFIERDLIEQATMVALEQAGRLNWWSTVCTSCKRLLPLATTGDGNCLLHAASLGMWGFHDRDLVLRKALYTMMRTGAEREALKRRWRWQQTQQNKEEEWEREWTELLKLASSEPRTHFSKNGGTGGGVDNSEDPVYESLEEFHVFVLAHILRRPIVVVADTMLRDSGGEAFAPIPFGGIYLPLEVPPNRCHCSPLVLAYDQAHFSALVSMEQRDQQREQAVIPLTDSEHKLLPLHFAVDPGKDWEWGKDDNDNARLAHLILSLEAKLNLLHSYMNVTWIRIPSETRAPLAQPESPTASAGEDVQSLADSLDSDRDSVCSNSNSNNGKNGKDKEKEKQRKEKDKTRADSVANKLGSFSKTLGIKLKKNMGGLGGLVHGKMGRANSANGKNGDSAERGKEKKAKSRKGSKEESGASASTSPSEKTTPSPTDKAAGASPAEKGGGPRGDAWKYSTDVKLSLNILRAAMQGERKFIFAGLLLTSHRHQFHEEMIGYYLTSAQERFSAEQEQRRRDAATAAAAAAAAAAATAKRPPRRPETEGVPVPERASPGPPTQLVLKLKERPSPGPAAGRAARAAAGGTASPGGGARRASASGPVPGRSPPAPARQSVIHVQASGARDEACAPAVGALRPCATYPQQNRSLSSQSYSPARAAALRTVNTVESLARAVPGALPGAAGTAGAAEHKSQTYTNGFGALRDGLEFADADAPTARSNGECGRGGPGPVQRRCQRENCAFYGRAETEHYCSYCYREELRRRREARGARP | 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).
Sequence Mass (Da): 100677
Sequence Length: 926
Subcellular Location: Cytoplasm
EC: 3.4.19.12
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Q6GQQ9 | MTLDMDAVLSDFVRSTGAEPGLARDLLEGKNWDVNAALSDFEQLRQVHAGNLPPSFSEGSGGSRTPEKGFSDREPTRPPRPILQRQDDIVQEKRLSRGISHASSSIVSLARSHVSSNGGGGGSNEHPLEMPICAFQLPDLTVYNEDFRSFIERDLIEQSMLVALEQAGRLNWWVSVDPTSQRLLPLATTGDGNCLLHAASLGMWGFHDRDLMLRKALYALMEKGVEKEALKRRWRWQQTQQNKESGLVYTEDEWQKEWNELIKLASSEPRMHLGTNGANCGGVESSEEPVYESLEEFHVFVLAHVLRRPIVVVADTMLRDSGGEAFAPIPFGGIYLPLEVPASQCHRSPLVLAYDQAHFSALVSMEQKENTKEQAVIPLTDSEYKLLPLHFAVDPGKGWEWGKDDSDNVRLASVILSLEVKLHLLHSYMNVKWIPLSSDAQAPLAQPESPTASAGDEPRSTPESGDSDKESVGSSSTSNEGGRRKEKSKRDREKDKKRADSVANKLGSFGKTLGSKLKKNMGGLMHSKGSKPGGVGTGLGGSSGTETLEKKKKNSLKSWKGGKEEAAGDGPVSEKPPAESVGNGGSKYSQEVMQSLSILRTAMQGEGKFIFVGTLKMGHRHQYQEEMIQRYLSDAEERFLAEQKQKEAERKIMNGGIGGGPPPAKKPEPDAREEQPTGPPAESRAMAFSTGYPGDFTIPRPSGGGVHCQEPRRQLAGGPCVGGLPPYATFPRQCPPGRPYPHQDSIPSLEPGSHSKDGLHRGALLPPPYRVADSYSNGYREPPEPDGWAGGLRGLPPTQTKCKQPNCSFYGHPETNNFCSCCYREELRRREREPDGELLVHRF | 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 of TRAF3, preventing TRAF3 proteolysis and over-activation of non-canonical NF-kappa-B. Negatively regulates mucosal immunity against infections (By similarity). Deubiquitinates ZAP70, and thereby regulates T cell receptor (TCR) signaling that leads to the activation of NF-kappa-B . Plays a role in T cell homeostasis and is required for normal T cell responses, including production of IFNG and IL2 (By similarity). Mediates deubiquitination of EGFR . Has deubiquitinating activity toward 'Lys-11', 'Lys-48' and 'Lys-63'-linked polyubiquitin chains . Has a much higher catalytic rate with 'Lys-11'-linked polyubiquitin chains (in vitro); however the physiological significance of these data are unsure . Hydrolyzes both linear and branched forms of polyubiquitin.
PTM: Phosphorylated by EGFR.
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).
Sequence Mass (Da): 92526
Sequence Length: 843
Domain: The protein undergoes a significant conformation change upon binding to ubiquitinated substrates. The loop that precedes the active site is in an autoinhibitory conformation in the apoprotein. Ubiquitin binding leads to a conformation change; the loop is stabilized in a catalytically competent conformation with the result that the active site Cys can form the reaction state intermediate.
Subcellular Location: Cytoplasm
EC: 3.4.19.12
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F4K3M6 | MAKTKQQKSKPKKQPHQKQGKDCDLSQFRAQLDALGLKIIQVTADGNCFFRAIADQLEGNEDEHNKYRNMIVLYIVKNREMFEPFIEDDVPFEDYCKTMDDDGTWAGNMELQAASLVTRSNICIHRNMSPRWYIRNFEDTRTRMIHLSYHDGEHYNSVRSKEDACGGPARPVVIEADAKVSAASKQAKATESKSKNKADKCHVNAGAIKVVMSGSCCDNTEKAEQVLLQVNGDVDAAIEFLIADQGMESLTENDTETASASDTINPKHASDSPMENTEQAREELIEEESASGNNSETVQAKCTTQTDDKKIPRNKTCPCGSKKKYKSCCGTATGRSSVKLLVSQTMESKKGRKNLRRGTSNEVEANAPDVGALCI | 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 . Cleaves also RUB-GST fusion .
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).
Sequence Mass (Da): 41534
Sequence Length: 375
Subcellular Location: Nucleus
EC: 3.4.19.12
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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 Gly of ubiquitin (a 76-residue protein attached to proteins as an intracellular targeting signal).
Sequence Mass (Da): 22398
Sequence Length: 189
Subcellular Location: Nucleus
EC: 3.4.19.12
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Q8LBW2 | MGYEPDPDALRWGLHDLEVCTLTNAGSCSSVTRYESGGGGTQGYVREGYNQPVTGYVDNDAVIAQFYQDELSRVARAEASGINSLSPTSVVAQDWPHPHQGQENQGEAIDITQESDILHNHNGNMEDKNVARIRFEGGQSSPSRDDDSVCSVEIEEESWSEVGKRLNQMIPIAHVPKINGELPSEDEQISDHERLFQRLQLYGLVENKIEGDGNCQFRSLSDQLYRSPEHHNFVREQVVNQLAYNREIYEGYVPMAYNDYLKAMKRNGEWGDHVTLQAAADLFGVRMFVITSFKDTCYIEILPHFQKSNRLICLSFWAEVHYNSIYPEGELPIPEGKKKKKYWVF | 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 . Cleaves also RUB-GST fusion .
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).
Sequence Mass (Da): 39231
Sequence Length: 345
EC: 3.4.19.12
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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 no longer respond to their cognate antigen . Acts via its interaction with RNF128/GRAIL, a crucial inductor of CD4 T-cell anergy . Isoform 1 destabilizes RNF128, leading to prevent anergy . In contrast, isoform 2 stabilizes RNF128 and promotes anergy . Surprisingly, it regulates RNF128-mediated ubiquitination, but does not deubiquitinate polyubiquitinated RNF128 . Deubiquitinates estrogen receptor alpha (ESR1) . Mediates deubiquitination of 'Lys-48'-linked polyubiquitin chains, but not 'Lys-63'-linked polyubiquitin chains . Not able to cleave di-ubiquitin . Also capable of removing NEDD8 from NEDD8 conjugates, but with a much lower preference compared to 'Lys-48'-linked ubiquitin .
PTM: Phosphorylation at Tyr-26 by SRC and SRMS promotes deubiquitination of RPTOR via a non-catalytic process.
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).
Sequence Mass (Da): 31284
Sequence Length: 271
Domain: In addition to ubiquitin-binding at the Cys-91 active site, a proximal ubiquitin-binding site is also present at Cys-23 Occupancy of the active site is needed to enable tight binding to the second site. Distinct binding sites for the ubiquitins may allow to discriminate among different isopeptide linkages (i.e. 'Lys-48'-, 'Lys-63'-linked polyubiquitin) in polyubiquitin substrates and achieve linkage-specific deubiquitination.
Subcellular Location: Cytoplasm
EC: 3.4.19.12
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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 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).
Sequence Mass (Da): 27213
Sequence Length: 234
EC: 3.4.19.12
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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 polyubiquitin chains (By similarity).
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).
Sequence Mass (Da): 27300
Sequence Length: 234
EC: 3.4.19.12
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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 bonds formed by the C-terminal Gly of ubiquitin (a 76-residue protein attached to proteins as an intracellular targeting signal).
Sequence Mass (Da): 32293
Sequence Length: 284
EC: 3.4.19.12
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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-terminal Gly of ubiquitin (a 76-residue protein attached to proteins as an intracellular targeting signal).
Sequence Mass (Da): 30372
Sequence Length: 262
EC: 3.4.19.12
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Q5VV17 | MQLYSSVCTHYPAGAPGPTAAAPAPPAAATPFKVSLQPPGAAGAAPEPETGECQPAAAAEHREAAAVPAAKMPAFSSCFEVVSGAAAPASAAAGPPGASCKPPLPPHYTSTAQITVRALGADRLLLHGPDPVPGAAGSAAAPRGRCLLLAPAPAAPVPPRRGSSAWLLEELLRPDCPEPAGLDATREGPDRNFRLSEHRQALAAAKHRGPAATPGSPDPGPGPWGEEHLAERGPRGWERGGDRCDAPGGDAARRPDPEAEAPPAGSIEAAPSSAAEPVIVSRSDPRDEKLALYLAEVEKQDKYLRQRNKYRFHIIPDGNCLYRAVSKTVYGDQSLHRELREQTVHYIADHLDHFSPLIEGDVGEFIIAAAQDGAWAGYPELLAMGQMLNVNIHLTTGGRLESPTVSTMIHYLGPEDSLRPSIWLSWLSNGHYDAVFDHSYPNPEYDNWCKQTQVQRKRDEELAKSMAISLSKMYIEQNACS | 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 ubiquitination . The abundance of rare codons in mRNAs can limit the translation rate and can lead to ribosome collisions that trigger activation of ribosome quality control (RQC) pathway by ZNF598 . OTUD1-mediated deubiquitination prevents activation of the RQC and subsequent dissociation of ribosomes and stimulates formation of polysomes and translation .
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).
Sequence Mass (Da): 51063
Sequence Length: 481
Domain: The UIM repeat increases the specificity and efficiency of the enzyme toward 'Lys-63'-linked polyubiquitin.
EC: 3.4.19.12
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Q5T2D3 | MSRKQAAKSRPGSGSRKAEAERKRDERAARRALAKERRNRPESGGGGGCEEEFVSFANQLQALGLKLREVPGDGNCLFRALGDQLEGHSRNHLKHRQETVDYMIKQREDFEPFVEDDIPFEKHVASLAKPGTFAGNDAIVAFARNHQLNVVIHQLNAPLWQIRGTEKSSVRELHIAYRYGEHYDSVRRINDNSEAPAHLQTDFQMLHQDESNKREKIKTKGMDSEDDLRDEVEDAVQKVCNATGCSDFNLIVQNLEAENYNIESAIIAVLRMNQGKRNNAEENLEPSGRVLKQCGPLWEEGGSGARIFGNQGLNEGRTENNKAQASPSEENKANKNQLAKVTNKQRREQQWMEKKKRQEERHRHKALESRGSHRDNNRSEAEANTQVTLVKTFAALNI | 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, deubiquitinates and stabilizes the nuclear receptor PPARD regulating the expression of various genes involved in glucose and lipid metabolism and oxidative phosphorylation . Also acts as a negative regulator of the ribosome quality control (RQC) by mediating deubiquitination of 40S ribosomal proteins RPS10/eS10 and RPS20/uS10, thereby antagonizing ZNF598-mediated 40S ubiquitination .
PTM: Glucose and fatty acids stimulate CREBBP-dependent acetylation, promoting its nuclear translocation.
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).
Sequence Mass (Da): 45124
Sequence Length: 398
Domain: The UBA-like domain has no influence on ubiquitin hydrolysis.
Subcellular Location: Cytoplasm
EC: 3.4.19.12
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G4MVZ5 | MSVPSFITAPEFEGGPPQGLSIPFRLRWSKTHPPKEPIVTFKGRTVLVTGANTGLGFEAAVKYAAFGADKIILAVRSIEKGEEAKKRIVERTGRDATDISVLKLDLGEYSSVKDFVSALHEVTPTLDVALLNAGLGNPTYEKSSAGWEMAVQVNVLSTALLAMLLLPLLRSSAAASGAKSHLTFVNSFAHTLVPRDFPLIEGSILKTATDESSWNASSSYNIVKLLAMASVQGFARMEAGEDQQRVIVNSVCPDLCETDLGRKFTGFISSIGKAIFYYLFALSAEEGARCLIGATALGPESHGRFWHHDFLYPFGELAQDQALMKKTWNEIIEAVGRDEPEILQLCRTT | 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-NRPS ACE1, assisted by the enoyl reductase RAP1, that are responsible for fusion of the tyrosine precursor and the polyketide backbone . The polyketide synthase module (PKS) of ACE1 is responsible for the synthesis of the polyketide backbone and the downstream nonribosomal peptide synthetase (NRPS) amidates the carboxyl end of the polyketide with the tyrosine precursor . Because ACE1 lacks a designated enoylreductase (ER) domain, the required activity is provided the enoyl reductase RAP1 . Reduction by the hydrolyase ORFZ, followed by dehydration and intra-molecular Diels-Alder cyclization by the Diels-Alderase ORF3 then yield the required isoindolone-fused macrocycle (Probable). A number of oxidative steps catalyzed by the tailoring enzymes identified within the cluster, including cytochrome P450 monooxygenases CYP1 to CYP4, the FAD-linked oxidoreductase OXR2 and the short-chain dehydrogenase/reductase OXR1, are further required to afford the final cytochalasans that confer avirulence and which have still to be identified (Probable). The monooxygenase CYP1 has been shown to be a site-selective C-18 hydroxylase whereas the function of CYP3 is the site-selective epoxidation of the C-6/C-7 olefin that is present in some intermediate compounds . Finally, SYN2 and RAP2 are not required for avirulence in Pi33 resistant rice cultivars .
Sequence Mass (Da): 37898
Sequence Length: 349
Pathway: Secondary metabolite biosynthesis.
EC: 1.1.1.-
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B2KWH9 | MLSLFYQRISTYIKLSASSLLSILPLYRPFQRRRLTMPSNEGSISSSSTTRPKDVLVVGGSYSGLAAALNLLDLCQGRSCRFAGALDPEISEPAEMRERVPVQITIVDERDGYFHLIGTPLAFASEEYALSAWRKFADIPALQTPAIKFIQGSVTRVDCERKISTIKEAGTNNEISQKYDYLVASSGLRRTWPSAPQSLNKDKYLEEVGEHIAKIKMANGGVVVIGGGAVGIEMASELKEMHPDLRVTLIHSRAKLLSSEPLPDEFRDRALELLHETGVETILGSRVIRTTQTELNGAATPSYTLSLTDGRTIKAGYVINAISKYSPTTAYLPSSVLDKEGYVKVNSALNFTDEVPNAKYHFAAGDLALWSGIKRAGRAMHHGHYVGMNIYQQLLNERFGTKPKFSEMAHAPPSMAVAVGKNTVAYGTEQGVVSGEEIAKIFFEDDLGFGICWRYLKLGEAPK | 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
Pathway: Siderophore biosynthesis.
EC: 1.-.-.-
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G4N285 | MTIKFASLILAGLGLGSGALGSVTFRREESSWTNDSLTSVFAQQAKGLFLPRTVISFQGQEWFENVTERWDIYAPPTFKVSVSPSTEKDVESAVKLAAKFKIPFLATGGRHGYGTTLGKLKNGLSIDLSLLNQFSIDSKAATITVGPGVRFRDIFTPLYEAGFQVPTGTCSCVGMIGATLGGGIGRLNGLDGLMIDALESARVVTADGRTLTVSEKENKDLFWGMRGAGQNFGVVVSATYKLKPLYAAGVWTNVDLIFSPDKNATYFDVVTSMEVPPQLTIASVVTYNATLDEPQLIATLTWTGPRDEALAAMKPILDVGPRHSEVTEATYATLPRVATFGTTDAVCAPGQIYDIYGVGLRRLDSAAWRSTFSKMARFYAAEPAGRASSILYETWPVQATVAVPDDATAYPWRDASTYVLIQMRWDRPGSPLERAADRLGAELRSDLSATGGYQGAGPAVYVNYAHGDERLEDIYGARKLPRLAKLKKQYDPGNVFRFHHALPTKYP | 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 of pyriculol and pyriculariol . Pyriculol and pyriculariol contain several hydroxyl moieties and double bonds, so it can be assumed that several reduction steps occur during biosynthesis. These reactions could be executed by PKS19 itself or partly by the tailoring enzymes OXR1, OXR2, RED1, RED2 or RED3, identified within the cluster (Probable). The FAD-linked oxidoreductase OXR1 is the only tailoring enzyme for which the function has been determined yet, and is involved in the oxidation of dihydropyriculol and dihydropyriculariol into pyriculol and pyriculariol, respectively .
Catalytic Activity: A + dihydropyriculol = AH2 + pyriculol
Sequence Mass (Da): 54993
Sequence Length: 507
Pathway: Polyketide biosynthesis.
EC: 1.-.-.-
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Q7XTC7 | MAAAAAAATVEAVGVAGGRRRRSGSVALGDLLRREASAERASASASAGAGGRERERRPSVAAGQACRAKKGEDFALLKPACERLPAGGAPFSAFALFDGHNGSGAAVYAKENILSNVMCCVPADLSGDEWLAALPRALVAGFVKTDKDFQTRAHSSGTTVTFVIIDGYVVTVASVGDSRCVLEAEGTIYHLSADHRFDASEEEVGRVTECGGEVGRLNVVGGAEIGPLRCWPGGLCLSRSIGDQDVGEFIIPVPYVKQIKLSSAGGRIIISSDGVWDALTVDTAFSCARGLPPEAAADQIVKEAIASKGLRDDTTCIVIDIIPPEKISPTVQPAKKAGKGLFKNIFYKKATSDSPCHADKDQCTQPDLVEEVFEDGCPSLSRRLDSEYPVRNMFKLFICAICQVELESGQGISIHEGLSKSGKLRPWDGPFLCHSCQEKKEAMEGKRHSRDSSSRNSGSSE | 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-phospho-L-seryl-[protein] = L-seryl-[protein] + phosphate
Sequence Mass (Da): 48707
Sequence Length: 461
Subcellular Location: Nucleus
EC: 3.1.3.16
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Q9LRZ4 | MVLLPAFLDGLARTVSTKKGKKLSEDEDGGREIAKSMIKDSKKNSTLLGTSGFVSSESSKRFTSICSNRGEKGINQDRAIVWEGFGCQEDITFCGMFDGHGPWGHVIAKRVKKSFPSSLLCQWQQTLASLSSSPECSSPFDLWKQACLKTFSIIDLDLKISPSIDSYCSGCTALTAVLQGDHLVIANAGDSRAVIATTSDDGNGLVPVQLSVDFKPNIPEEAERIKQSDGRLFCLDDEPGVYRVGMPNGGSLGLAVSRAFGDYCLKDFGLVSEPEVTYRKITDKDQFLILATDGMWDVMTNNEAVEIVRGVKERRKSAKRLVERAVTLWRRKRRSIAMDDISVLCLFFRPS | 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 | MSGSLMNLFSLCFKPFGHVCDNSEAGSGGGGGVSGGTGGEGKDGLLWFRDLGKYCGGDFSMAVIQANQVLEDQSQVESGNFGTFVGVYDGHGGPEAARYVCDHLFNHFREISAETQGVVTRETIERAFHATEEGFASIVSELWQEIPNLATVGTCCLVGVIYQNTLFVASLGDSRVVLGKKGNCGGLSAIQLSTEHNANNEDIRWELKDLHPDDPQIVVFRHGVWRVKGIIQVSRSIGDMYMKRPEFNKEPISQKFRIAEPMKRPLMSATPTILSHPLHPNDSFLIFASDGLWEHLTNEKAVEIVHNHPRAGSAKRLIKAALHEAARKREMRYSDLRKIDKKVRRHFHDDITVIVVFLNHDLISRGHINSTQDTTVSIRSALEH | 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-L-seryl-[protein] = L-seryl-[protein] + phosphate
Sequence Mass (Da): 42489
Sequence Length: 384
EC: 3.1.3.16
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Q7XU84 | MAQPQRPLQVPDITKSTHSGGNTVLAYASSAMQGYRSTMEDAHATIENLDALTNTSFFGVYDGHGGSAVARYCANHLHNKVLEQEDFSSNLANALRQSFFRMDEMLRNQAASKELTEYGSGNEYWRTAGRSWLRCAPCVLGPVYCGPLAEGCTACVVLIRNTQIVVGNAGDARCVISRNGQAIALSNDHKPNFPEETQRIVAAGGSVSFSRGSHRVNNGIAVSRAIGDLSYKNNKKLRPEQQLLTCSPEIRADQLTDDTEFLVIACDGVWDVLANQAVVDFVRLHLNNGVELSVICESLLQEAITRDPPSTDNMSVILVRFLHPEGNRGARAATSSTSTGTVPSRHSKSISL | 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 | MVGRMERQSASSSASCSPSSSAAGTSSSSSACGGKKRPDILNMIRSATCLNSSSTDTGKGRSKQSSNKVTHGFHLVEGKSGHDMEDYHVAEYKYDKSHELGLFAIFDGHLGDSVPSYLKANLFCNILKEPIFWTNPQEAIKNAYRSTNKYILENAKQLGPGGSTAVTAIVVDGKDMWVANVGDSRAVVCERGAANQLTVDHEPHTTNERQRIEKQGGFVTTFPGDVPRVNGQLAVARAFGDQSLKAHLSSEPDVRHVPINSSIEFVILASDGLWKVMKNQEAVDLVKSIKDPQAAAKRLTTEALARKSKDDISCIVIRFRC | 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
|
Q9SD12 | MLSTLMKLLSACLWPSSSSGKSSDSTGKQDGLLWYKDFGQHLVGEFSMAVVQANNLLEDQSQVESGPLSTLDSGPYGTFIGIYDGHGGPETSRFVNDHLFQHLKRFAAEQASMSVDVIKKAYEATEEGFLGVVTKQWPTKPQIAAVGSCCLVGVICGGMLYIANVGDSRAVLGRAMKATGEVIALQLSAEHNVSIESVRQEMHSLHPDDSHIVMLKHNVWRVKGLIQISRSIGDVYLKKAEFNKEPLYTKYRIREPFKRPILSGEPTITEHEIQPQDKFLIFASDGLWEQMSNQEAVDIVQNHPRNGIARRLVKMALQEAAKKREMRYSDLKKIERGVRRHFHDDITVVIIFLDTNQVSSVKGPPLSIRGGGMTFPKKI | 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 Mass (Da): 42179
Sequence Length: 379
EC: 3.1.3.16
|
A3AZ89 | MGNSLASLATPCFADAAAGGGRGRGHHAAGDDAVAFDDDDAAGGCNSIGHILSFDGRDAPAFAIHGVLLPSNPSTMASTGGGGGGGASVLNDGALSIGSSSFDSSNSFSFRTLQPRQYSGPLEYCTTSPSTSGASSSRQLGPRTDKQILNDIYANRQRRRCQGSKGPPLLGRLRKAVASLLRAGPCGFPEQEEPAAMINGVGVVRNGEESISRNVDAAAADDGAERVQWARGKAGEDRVHVVVSEEHGWMFVGIYDGFNGPDATDYLADNLYAAVCRELNGVLSEDEPDPPEAAAAAGRCNGCGGAARHREVLDAMARALRRTEEGYFAEAEARAAECPELAMMGSCVLVVLMKGADVYAMNVGDSRAVLAHQAEPDLSHVVLPRGSHHDGDGDLAGVKEAIKRQFDECEMGELAALQLTMDHSTNVYKEVRRIRSEHLDDPGCITNGRVKGCLKVTRAFGAGYLKEPRWNKALLEVFQVDYVGSSPYISCRPYIRHHRLGAQDKFLILSSDGLYDYFTKEEVVAQVEAFTAGYPDEDPAKYLSHQILLRAANQAGMGFHELLEIQQGDRRQYHDDVSIIIISLEGKIWRSSQ | 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
|
Q9SD02 | MAPVTEVSPMINTLEVADDKMTNLSSSGKPPRNISAMRHCNSTAWLTDYEGDERFGAKSPEGVNSTFQPVFRSGSWSDKGPKQSMEDEFICVDDLTEYIGSSTGAFYGVFDGHGGVDAASFTKKNIMKLVMEDKHFPTSTKKATRSAFVKTDHALADASSLDRSSGTTALTALILDKTMLIANAGDSRAVLGKRGRAIELSKDHKPNCTSERLRIEKLGGVIYDGYLNGQLSVARALGDWHIKGTKGSLCPLSCEPELEEIVLTEEDEYLIMGCDGLWDVMSSQCAVTMVRRELMQHNDPERCSQALVKEALQRNSCDNLTVVVVCFSPEAPPRIEIPKSHKRRSISAEGLDLLKGVLNEL | 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
|
Q6AUQ4 | MVAEAEVMHQPVPVLEVPYHRCVAKGVEEVAAAAAVAPPPVVEVEVAVQVPHMGLESAAGAPSISVDALQFVPSIRSGSFADIGPRRYMEDEHIRIDDLSAHLGSLLVCPLPSAFYGVFDGHGGLDAAAYMKRHAMRFLFEDSEFPQASQVDETYVQSVENSVRRAFLQADLALADDLDISRSSGTTALTALVFGRQLLVANAGDCRAVLCRRGVAMEMSRDHRANYAEECERVAASGGYIEDGYLNGVLSVTRALGDWDMKMPDGSISPLIAEPEFRQTMLTEDDEFLIMGCDGIWDVMTSQHAVSIVRRGLRQHDDPERCARELVMEAKRLETADNLTVIVVCFVSELGSPRQEQVGGQAGVARPRSCKSLSAEALCNLRSWLETDR | 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
|
Q6L482 | MRHISSLLQGLARSLSVGKERKGGDGDDGKAAAATATAVLRTSGTLWGEGSETFAAVCSRRGEKGINQDCSIVCEGFGCEEGSVLCGIFDGHGQWGHYVAKAVRESLPPALLRRWREAVTLAALIDGGEKRLCECRPDLWRQSYLAACAAVDAELRASRRLDAVHSGCTALSLVKHGDLLVVANVGDSRAVLATASPDDGGGARLAAVQLTVDFKPNLPQERERIMECNGRVQCLADEPGVHRVWRPDREGPGLAMSRAFGDYCVKDYGVISAPEVTHRRITAQDHFVILATDGVWDVVSNEEAVQIVASAPEREKAAKRLVEFAVRAWRRKRRGIAVDDCSAICLFFHSPPS | 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
|
Q3EAF9 | MVAEAEVVFQQSLPAVLEIELFDGVSSAVKSPVSSPKLGFTQSTASVSGSLTTSPVQADIFPEGDCDPSVLDYIPTIRSGSFADIGPKRNMEDEHIRIDDLSSQVGSLFELPKPSAFYAVFDGHGGPEAAAYVRENAIRFFFEDEQFPQTSEVSSVYVEEVETSLRNAFLQADLALAEDCSISDSCGTTALTALICGRLLMVANAGDCRAVLCRKGRAIDMSEDHKPINLLERRRVEESGGFITNDGYLNEVLAVTRALGDWDLKLPHGSQSPLISEPEIKQITLTEDDEFLVIGCDGIWDVLTSQEAVSIVRRGLNRHNDPTRCARELVMEALGRNSFDNLTAVVVCFMTMDRGDKPVVPLEKRRCFSLSPEAFCSLRNLLDG | 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
|
Q65XG6 | MAAEICREEAAKSMPAAAAGATAIARRRRRVEGFRFAAGSLEPPQEDADAGVARCGKRQRVAGARAGAGAATAGPCRPSAGAEFGSRWWPRYGVTSVFGRRREMEDAVSIRPDFLRGSTSSGKHHFFGVFDGHGCSHVARMCQDRMHELVVDAYKKAVSGKEAAAAAPAWKDVMEKGFARMDDEATIWAKSRTGGEPACRCELQTPARCDHVGSTAVVAVVGPNRVVVANSGDSRAVLCRAGVPVPLSVDHKPDRPDELERIKAAGGRVIYWDGARVLGVLAMSRAIGDGYLKPYVTSEPEVTVTERADDDECLILASDGLWDVVTNEMACEVVRACFRSNGPPSPPGCSRPKAVLPPPAGASGGGGGDAVVKGVDKAESDKACADAALLLAKLAIARRSADNVSVVVVDLRRPVP | 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
|
Q9M1V8 | MVELRQFSDLPIALSGISRIADPSPPPPVVAIRRRFKGGGNTRRIVFSVPLIFAFPFPTGTPKDVLVGIAAVFDGHSGSEASEMASQLLLDYFALHIYFLLDATFSKELTGKLPNSLMHLYDLDSQRFQDSLPLNFHLDILKEALLRAIYDIDATFTKEASTRKLDSGSTATIALIADGQLLVASIGDSKALLCSERYETPEEAKATLIKLYRERKRNQDSSPSRFSDLKLEHRTGLMRFIAKELTKDHHPDREDEMLRVKAAGGYVTKWAGVPRVNGQLAVSRSIGDLTYRSYGVISAPEVMDWQPLVANDSYLVVSSDGIFEKLEVQDACDRLWEVKNQTSFGAGVPSYCSISLADCLVNTAFEKGSMDNMAAVVVPLKSNLDWESQPKEQSVGPSGFKMKNTYALPCEFLSSQPNLFRMG | 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
|
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.-.-.-
|
A4QNZ7 | MVSRPGDLPALEAGPGSSEGLLGGMSIPAGMTRRALSYDDNLERPMSPPPSDINISNLWKRPVIPERKFARLAEEDESEGGVKQSASFESTKPIPVVKAKASSVMNSLIIKQTQESMQKFEKQAGLTDTGYTPHKGLNAEETRYHRLAESMHKLQMQSTDAKEERQPSSNQSTPAGTPQSSPKQKRRGWFNSQGSTASLTGSEMSTSSSSSVDLASAEGPIERWGVFGPRPQVSKSTTDPGTHPDTSGGFALQSYKGAQKPTPMEVMKAQATRLAEDPTNFKAPPKMEIPTMDGKRQVTRPHKLKHRDMNVLTPSGF | Function: Potential NADPH-dependent oxidoreductase.
Sequence Mass (Da): 34422
Sequence Length: 317
Subcellular Location: Cytoplasm
EC: 1.-.-.-
|
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.-.-.-
|
Q32NP7 | MASRQPDVPAIEHGSSGLLGKMSLPVGMHRRAFSYDDALDDTAPMTPPPSDMCSNTMWRKPIIPERKYQLLSKIEDGDSNIPPPSLPPSSSTEKVPVVKAKATSIIMNSLMTKHTQESIQRFEQQAGLRDAGYTPHKGLTSEETKYHRVAEALHKLNMHIGESTEEKQSSSAQSTPCSTPSSSPKQMRRSWFSQGSTSSLPAGDLSNSDGGVDKWSMFGPRAVQKSTTDPGGFTVQPYKGAQKPTPMELMRAQASRISDDPAALKPPKMEMPSLVSGTKNIPRGHNLKPRDMNILTPTGF | Function: Potential NADPH-dependent oxidoreductase.
Sequence Mass (Da): 32686
Sequence Length: 300
Subcellular Location: Cytoplasm
EC: 1.-.-.-
|
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 | MRAVLLVCLLAGLAHADLFTAIADLQHMLGAEKDVTTIIDQYIEAERARLDDLRRYAHEYVHRNAHAESVGPEFVTNPINAYLLIKRLTTEWKKVENIMLNNKASTFLKNITDNRVRSEVKFPGEEDLSGAATALLRLQDTYSLDTLDLSNGIIGGEKVSNKLSGHDTFEVGRSAYNQKDYYHCLMWMQVALVKIENENPPTIEEWEILEYLAYSLYQQGNVRRALSLTKRLAKIAPNHPRAKGNVKWYEDMLQGKDMVGDLPPIVNKRVEYDGIVERDAYEALCRGEIPPVEPKWKNKLRCYLKRDKPFLKLAPIKVEILRFDPLAVLFKNVIHDSEIEVIKELASPKLKRATVQNSKTGELEHATYRISKSAWLKGDLDPVIDRVNRRIEDFTNLNQATSEELQVANYGLGGHYDPHFDFARKEEKNAFKTLNTGNRIATVLFYMSQPERGGATVFNHLGTAVFPSKNDALFWYNLRRDGEGDLRTRHAACPVLLGVKWVSNKWIHEKGQEFTRPCGLEEEVQENFIGDLSPYANDP | 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
Sequence Length: 539
Subcellular Location: Endoplasmic reticulum lumen
EC: 1.14.11.2
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Q5ZLK5 | MKPWLCLVFFTSAFLIWHAEAEFFTSIGQMTDLIYAEKDLVQSLKEYIRAEETKLSQIKSWAEKMDVLTSKSTSDPEGYLAHPVNAYKLVKRLNTDWLELENLVLQDTTNGFITNLTIQRQFFPTEEDETGAAKALMRLQDTYKLDPETLSRGNLPGTKYRSSLTVSDCFGMGKTAYNDGDYYHTVLWMEQALKQHDEGEDTTVSKVEILDYLSYAVFQFGDLHRAMELTRRLISLDSTHERAGSNLRYFEKLLEKEREKPSNKTVATTEPVVQSGAYERPLDYLPERDIYEALCRGEGVKMTPRRQKRLFCRYHDGNRNPHLLIAPFKEEDEWDSPHIVRYYDVMSDEEIEKIKQLAKPKLARATVRDPKTGVLTVASYRVSKSSWLEEDDDPVVAKVNQRMQQITGLTVKTAELLQVANYGMGGQYEPHFDFSRRPFDSTLKSEGNRLATFLNYMSDVEAGGATVFPDFGAAIWPKKGTAVFWYNLFRSGEGDYRTRHAACPVLVGCKWVSNKWFHERGNEFLRPCGRTEVD | 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
Sequence Length: 534
Subcellular Location: Endoplasmic reticulum lumen
EC: 1.14.11.2
|
O15460 | MKLWVSALLMAWFGVLSCVQAEFFTSIGHMTDLIYAEKELVQSLKEYILVEEAKLSKIKSWANKMEALTSKSAADAEGYLAHPVNAYKLVKRLNTDWPALEDLVLQDSAAGFIANLSVQRQFFPTDEDEIGAAKALMRLQDTYRLDPGTISRGELPGTKYQAMLSVDDCFGMGRSAYNEGDYYHTVLWMEQVLKQLDAGEEATTTKSQVLDYLSYAVFQLGDLHRALELTRRLLSLDPSHERAGGNLRYFEQLLEEEREKTLTNQTEAELATPEGIYERPVDYLPERDVYESLCRGEGVKLTPRRQKRLFCRYHHGNRAPQLLIAPFKEEDEWDSPHIVRYYDVMSDEEIERIKEIAKPKLARATVRDPKTGVLTVASYRVSKSSWLEEDDDPVVARVNRRMQHITGLTVKTAELLQVANYGVGGQYEPHFDFSRNDERDTFKHLGTGNRVATFLNYMSDVEAGGATVFPDLGAAIWPKKGTAVFWYNLLRSGEGDYRTRHAACPVLVGCKWVSNKWFHERGQEFLRPCGSTEVD | 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
Sequence Length: 535
Subcellular Location: Endoplasmic reticulum lumen
EC: 1.14.11.2
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Q7Z4N8 | MGPGARLAALLAVLALGTGDPERAAARGDTFSALTSVARALAPERRLLGLLRRYLRGEEARLRDLTRFYDKVLSLHEDSTTPVANPLLAFTLIKRLQSDWRNVVHSLEASENIRALKDGYEKVEQDLPAFEDLEGAARALMRLQDVYMLNVKGLARGVFQRVTGSAITDLYSPKRLFSLTGDDCFQVGKVAYDMGDYYHAIPWLEEAVSLFRGSYGEWKTEDEASLEDALDHLAFAYFRAGNVSCALSLSREFLLYSPDNKRMARNVLKYERLLAESPNHVVAEAVIQRPNIPHLQTRDTYEGLCQTLGSQPTLYQIPSLYCSYETNSNAYLLLQPIRKEVIHLEPYIALYHDFVSDSEAQKIRELAEPWLQRSVVASGEKQLQVEYRISKSAWLKDTVDPKLVTLNHRIAALTGLDVRPPYAEYLQVVNYGIGGHYEPHFDHATSPSSPLYRMKSGNRVATFMIYLSSVEAGGATAFIYANLSVPVVRNAALFWWNLHRSGEGDSDTLHAGCPVLVGDKWVANKWIHEYGQEFRRPCSSSPED | 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 + trans-4-hydroxy-L-prolyl-[collagen]
Sequence Mass (Da): 61126
Sequence Length: 544
Subcellular Location: Endoplasmic reticulum lumen
EC: 1.14.11.2
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Q6W3F0 | MGPGARLALLALLALGGDPAAATGREDTFSALTSVARALAPERRLLGTLRRYLRGEEARLRDLTRFYDKVLSLHEDLKIPVVNPLLAFTVIKRLQSDWRNVVHSLEATENIRALKDGYEKVEQDLPAFEDLEGAARALMRLQDVYMLNVKGLARGVFQRVTGSSITDLYSPRQLFSLTADDCFQVGKVAYDTGDYYHAIPWLEEAVSLFRRAHGEWKTEDEASLEDALDYLAFACFQVGNVSCALSLSREFLVYSPDNKRMARNVLKYERLLAENGHQMAAETAIQRPNVPHLQTRDTYEGLCQTLGSQPTHYQIPSLYCSYETNSSPYLLLQPARKEVVHLRPLIALYHDFVSDEEAQKIRELAEPWLQRSVVASGEKQLQVEYRISKSAWLKDTVDPMLVTLDHRIAALTGLDIQPPYAEYLQVVNYGIGGHYEPHFDHATSPSSPLYRMKSGNRVATFMIYLSSVEAGGATAFIYGNFSVPVVKNAALFWWNLHRSGEGDGDTLHAGCPVLVGDKWVANKWIHEYGQEFRRPCSTNPED | 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 + trans-4-hydroxy-L-prolyl-[collagen]
Sequence Mass (Da): 60975
Sequence Length: 542
Subcellular Location: Endoplasmic reticulum lumen
EC: 1.14.11.2
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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 Length: 284
Subcellular Location: Cytoplasm
EC: 1.14.11.-
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Q9NXG6 | MAAAAVTGQRPETAAAEEASRPQWAPPDHCQAQAAAGLGDGEDAPVRPLCKPRGICSRAYFLVLMVFVHLYLGNVLALLLFVHYSNGDESSDPGPQHRAQGPGPEPTLGPLTRLEGIKVGHERKVQLVTDRDHFIRTLSLKPLLFEIPGFLTDEECRLIIHLAQMKGLQRSQILPTEEYEEAMSTMQVSQLDLFRLLDQNRDGHLQLREVLAQTRLGNGWWMTPESIQEMYAAIKADPDGDGVLSLQEFSNMDLRDFHKYMRSHKAESSELVRNSHHTWLYQGEGAHHIMRAIRQRVLRLTRLSPEIVELSEPLQVVRYGEGGHYHAHVDSGPVYPETICSHTKLVANESVPFETSCRYMTVLFYLNNVTGGGETVFPVADNRTYDEMSLIQDDVDLRDTRRHCDKGNLRVKPQQGTAVFWYNYLPDGQGWVGDVDDYSLHGGCLVTRGTKWIANNWINVDPSRARQALFQQEMARLAREGGTDSQPEWALDRAYRDARVEL | 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 hydroxylation for proteasomal degradation via the von Hippel-Lindau ubiquitination complex.
Catalytic Activity: 2-oxoglutarate + L-prolyl-[hypoxia-inducible factor alpha subunit] + O2 = CO2 + succinate + trans-4-hydroxy-L-prolyl-[hypoxia-inducible factor alpha subunit]
PTM: Glycosylated.
Location Topology: Single-pass type II membrane protein
Sequence Mass (Da): 56661
Sequence Length: 502
Subcellular Location: Endoplasmic reticulum membrane
EC: 1.14.11.29
|
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
Subcellular Location: Virion
EC: 1.14.11.2
|
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
EC: 1.14.11.56
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Q6PE18 | MDETSPLVSPLRDSNDFNYGPAEPTSPRGGFGSTPGSVVRLPAGSPGRSRERQPLLDRDRGASPRDPHRNEFPEDPEFREIIRKAERAIEEGIYPERIYQGSSGSYFVKDSAGKIIGVFKPKNEEPYGQLNPKWTKWLQKLCCPCCFGRDCLVLNQGYLSEAGASLVDQKLELNIVPRTKVVYLASETFNYSAIDRVKSRGKRLALEKVPKVGQRFHRIGLPPKVGSFQIFVEGYKDADFWLRRFEAEPLPENTNRQLQLQFERLVVLDYIIRNTDRGNDNWLIKYDYPMDTSSNRDSDWVLVKDPIIKLAAIDNGLAFPLKHPDSWRAYPFYWAWLPQAKVVFSQEIRDLVLPKLADPNFIKDLEEDLYELFKKDPGFDRGQFKKQVSVMRGQILNLSQAMRDGKTPLQLVQMPPVIVETARVPQRANSESYTQSFQSRRPFFTWW | 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 phosphatidylinositol (PI) to phosphatidylinositol 4-phosphate (PI4P) is the first committed step in the generation of phosphatidylinositol 4,5-bisphosphate (PIP2), a precursor of the second messenger inositol 1,4,5-trisphosphate (InsP3).
Catalytic Activity: a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol) + ATP = a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol 4-phosphate) + ADP + H(+)
Location Topology: Lipid-anchor
Sequence Mass (Da): 51443
Sequence Length: 447
Subcellular Location: Golgi apparatus
EC: 2.7.1.67
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Q9BTU6 | MDETSPLVSPERAQPPDYTFPSGSGAHFPQVPGGAVRVAAAAGSGPSPPGSPGHDRERQPLLDRARGAAAQGQTQTVAAQAQALAAQAAAAAHAAQAHRERNEFPEDPEFEAVVRQAELAIERCIFPERIYQGSSGSYFVKDPQGRIIAVFKPKNEEPYGHLNPKWTKWLQKLCCPCCFGRDCLVLNQGYLSEAGASLVDQKLELNIVPRTKVVYLASETFNYSAIDRVKSRGKRLALEKVPKVGQRFNRIGLPPKVGSFQLFVEGYKDADYWLRRFEAEPLPENTNRQLLLQFERLVVLDYIIRNTDRGNDNWLIKYDCPMDSSSSRDTDWVVVKEPVIKVAAIDNGLAFPLKHPDSWRAYPFYWAWLPQAKVPFSQEIKDLILPKISDPNFVKDLEEDLYELFKKDPGFDRGQFHKQIAVMRGQILNLTQALKDNKSPLHLVQMPPVIVETARSHQRSSSESYTQSFQSRKPFFSWW | 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 survival of neurons. Besides, phosphorylation of phosphatidylinositol (PI) to phosphatidylinositol 4-phosphate (PI4P) is the first committed step in the generation of phosphatidylinositol 4,5-bisphosphate (PIP2), a precursor of the second messenger inositol 1,4,5-trisphosphate (InsP3).
PTM: Palmitoylated by ZDHHC3 and ZDHHC7 in the CCPCC motif. Palmitoylation is cholesterol-dependent, and required for TGN localization.
Location Topology: Lipid-anchor
Catalytic Activity: a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol) + ATP = a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol 4-phosphate) + ADP + H(+)
Sequence Mass (Da): 54022
Sequence Length: 479
Subcellular Location: Golgi apparatus
EC: 2.7.1.67
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Q99M64 | MDETSPLVSPERAQPPEYTFPSVSGAHFPQVPGGAVRVAAAGSGPSPPCSPGHDRERQPLLDRARGAAAQGQTHTVAAQAQALAAQAAVAVHAVQTHRERNDFPEDPEFEVVVRQAEIAIECSIYPERIYQGSSGSYFVKDSQGRIIAVFKPKNEEPYGNLNPKWTKWLQKLCCPCCFGRDCLVLNQGYLSEAGASLVDQKLELNIVPRTKVVYLASETFNYSAIDRVKSRGKRLALEKVPKVGQRFNRIGLPPKVGSFQLFVEGYKDADYWLRRFEAEPLPENTNRQLLLQFERLVVLDYIIRNTDRGNDNWLIKYDYPMDNPNCRDTDWVMVREPVIKVAAIDNGLAFPLKHPDSWRAYPFYWAWLPQAKVPFSQEIKDLILPKISDPNFVKDLEEDLYELFKKDPGFDRGQFHKQIAVMRGQILNLTQALKDNKSPLHLVQMPPVIVETARSHQRSSSESYTQSFQSRKPFFSWW | 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 survival of neurons. Besides, phosphorylation of phosphatidylinositol (PI) to phosphatidylinositol 4-phosphate (PI4P) is the first committed step in the generation of phosphatidylinositol 4,5-bisphosphate (PIP2), a precursor of the second messenger inositol 1,4,5-trisphosphate (InsP3).
PTM: Ubiquitinated by ITCH; this does not lead to proteasomal degradation.
Location Topology: Lipid-anchor
Catalytic Activity: a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol) + ATP = a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol 4-phosphate) + ADP + H(+)
Sequence Mass (Da): 54305
Sequence Length: 478
Subcellular Location: Golgi apparatus
EC: 2.7.1.67
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O15350 | MAQSTATSPDGGTTFEHLWSSLEPDSTYFDLPQSSRGNNEVVGGTDSSMDVFHLEGMTTSVMAQFNLLSSTMDQMSSRAASASPYTPEHAASVPTHSPYAQPSSTFDTMSPAPVIPSNTDYPGPHHFEVTFQQSSTAKSATWTYSPLLKKLYCQIAKTCPIQIKVSTPPPPGTAIRAMPVYKKAEHVTDVVKRCPNHELGRDFNEGQSAPASHLIRVEGNNLSQYVDDPVTGRQSVVVPYEPPQVGTEFTTILYNFMCNSSCVGGMNRRPILIIITLEMRDGQVLGRRSFEGRICACPGRDRKADEDHYREQQALNESSAKNGAASKRAFKQSPPAVPALGAGVKKRRHGDEDTYYLQVRGRENFEILMKLKESLELMELVPQPLVDSYRQQQQLLQRPSHLQPPSYGPVLSPMNKVHGGMNKLPSVNQLVGQPPPHSSAATPNLGPVGPGMLNNHGHAVPANGEMSSSHSAQSMVSGSHCTPPPPYHADPSLVSFLTGLGCPNCIEYFTSQGLQSIYHLQNLTIEDLGALKIPEQYRMTIWRGLQDLKQGHDYSTAQQLLRSSNAATISIGGSGELQRQRVMEAVHFRVRHTITIPNRGGPGGGPDEWADFGFDLPDCKARKQPIKEEFTEAEIH | 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 an activator of FOXJ1 expression (By similarity). It is an essential factor for the positive regulation of lung ciliated cell differentiation .
PTM: Isoform alpha (but not isoform beta) is sumoylated on Lys-627, which potentiates proteasomal degradation but does not affect transcriptional activity. Phosphorylation by PLK1 and PLK3 inhibits the transcription regulator activity and pro-apoptotic function.
Sequence Mass (Da): 69623
Sequence Length: 636
Domain: Possesses an acidic transactivation domain, a central DNA binding domain and a C-terminal oligomerization domain that binds to the ABL1 tyrosine kinase SH3 domain.
Subcellular Location: Nucleus
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Q7YXD4 | MKVISGLLFFILISCSLFLVQGQVDCVTNSSDASCTNFQYPLANITADINNLCGSMPYMPVCTIQQSCNQESSTSGICDPFSILGDSCLHDMPGMSGCNNFKKLCASGSVVEQCSTVDSVTDLPTTMKMWANIKSICNEMTMTGCEKCTILNATCDVLTVYSTLCLAMPEMGQCANWTQMCASSGNMASSPISSGICTDEPTPATDCFTNPSDPSCADYVYTAANANADILNLCKSMPYMTVCSIQKSCNQESSTSGICAPFSILGDSCLHDMPGMNGCSNFKKLCASGSVVEQCSSVDSISNLPTTMQLFAGIKSICTEMAMDGCEKCSGNSPTTTCDVLPVYSSLCMAMPDMSQCANWTKMCSSSGQLYNSQITSDYCVASVADAVPIMRMYFHTGILDYILFKSWVPRTDRQFAGSWFAIFFFAIFFELEKTLRSILEKRWTPNKKDSEDNNLINSSFLSGSYPKFSYRDIIRGCLHAIELTCSYALMLVAMTFNVALFFAVIAGVLVGNILFGRYRNYTPRVTCCE | 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
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P27986 | MSAEGYQYRALYDYKKEREEDIDLHLGDILTVNKGSLVALGFSDGQEARPEEIGWLNGYNETTGERGDFPGTYVEYIGRKKISPPTPKPRPPRPLPVAPGSSKTEADVEQQALTLPDLAEQFAPPDIAPPLLIKLVEAIEKKGLECSTLYRTQSSSNLAELRQLLDCDTPSVDLEMIDVHVLADAFKRYLLDLPNPVIPAAVYSEMISLAPEVQSSEEYIQLLKKLIRSPSIPHQYWLTLQYLLKHFFKLSQTSSKNLLNARVLSEIFSPMLFRFSAASSDNTENLIKVIEILISTEWNERQPAPALPPKPPKPTTVANNGMNNNMSLQDAEWYWGDISREEVNEKLRDTADGTFLVRDASTKMHGDYTLTLRKGGNNKLIKIFHRDGKYGFSDPLTFSSVVELINHYRNESLAQYNPKLDVKLLYPVSKYQQDQVVKEDNIEAVGKKLHEYNTQFQEKSREYDRLYEEYTRTSQEIQMKRTAIEAFNETIKIFEEQCQTQERYSKEYIEKFKREGNEKEIQRIMHNYDKLKSRISEIIDSRRRLEEDLKKQAAEYREIDKRMNSIKPDLIQLRKTRDQYLMWLTQKGVRQKKLNEWLGNENTEDQYSLVEDDEDLPHHDEKTWNVGSSNRNKAENLLRGKRDGTFLVRESSKQGCYACSVVVDGEVKHCVINKTATGYGFAEPYNLYSSLKELVLHYQHTSLVQHNDSLNVTLAYPVYAQQRR | 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 important role in signaling in response to FGFR1, FGFR2, FGFR3, FGFR4, KITLG/SCF, KIT, PDGFRA and PDGFRB. Likewise, plays a role in ITGB2 signaling . Modulates the cellular response to ER stress by promoting nuclear translocation of XBP1 isoform 2 in a ER stress- and/or insulin-dependent manner during metabolic overloading in the liver and hence plays a role in glucose tolerance improvement .
PTM: Polyubiquitinated in T-cells by CBLB; which does not promote proteasomal degradation but impairs association with CD28 and CD3Z upon T-cell activation.
Sequence Mass (Da): 83598
Sequence Length: 724
Domain: The SH3 domain mediates the binding to CBLB, and to HIV-1 Nef.
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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, enhancement and blockade of neurotransmission. Does not display myotoxic activity such as changes in baseline muscle tension or inhibition of directly stimulated muscle twitches. All subunits are necessary for maximum toxicity.
Catalytic Activity: a 1,2-diacyl-sn-glycero-3-phosphocholine + H2O = a 1-acyl-sn-glycero-3-phosphocholine + a fatty acid + H(+)
Sequence Mass (Da): 3272
Sequence Length: 27
Subcellular Location: Secreted
EC: 3.1.1.4
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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 nM) vs ASIC1b (EC(50)=23 nM) . The rat ASIC3 subtype is also sensitive to the heterodimer, but with a lower potency (EC(50)=830 nM) . On rat ASIC2a, the toxin shows a very weak activation, but produces a remarkable potentiation (>100-fold) of protons when the extracellular pH drops below neutrality . Moderate and weak activations are also observed on the heterotrimers Asic1a-Asic2a and Asic1a-Asic3 (expressed in CHO cells), respectively . The binding sites of the beta subunit of MitTx and the spider psalmotoxin-1 toxin overlap, explaining why these toxins are mutually exclusive . In vivo, the heterodimer elicits robust pain-related behavior in mice by activation of ASIC1 channels on capsaicin-sensitive nerve fibers .
Sequence Mass (Da): 16793
Sequence Length: 149
Domain: The toxin-channel complex has a triskelion-like shape with one toxin heterodimer radiating from each ASIC1 subunit. Toxin subunits protrude from the edges of the channel trimer, with each heterodimer interacting almost exclusively with a single subunit.
Subcellular Location: Secreted
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P86374 | RGSXLTILPLRNIRDIFYVG | PTM: N-glycosylated.
Sequence Mass (Da): 2315
Sequence Length: 20
Subcellular Location: Secreted
EC: 3.4.23.-
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P86370 | RGSXLTILPLRNISD | PTM: N-glycosylated.
Sequence Mass (Da): 1666
Sequence Length: 15
Subcellular Location: Secreted
EC: 3.4.23.-
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Q9T0H9 | MKLTSLSKNANSTATAVTVSSIQKLPFLSLSETLPCPKSSRKPTFLPLRCRRRPKLDLLWGKFRVRASDAGVGSGSYSGGEEDGSQSSSLDQSPATSSESLKPRGPFPYSLSIALVLLSCGLVFSLITFVKGGPSSVLAAVAKSGFTAAFSLIFVSEIGDKTFFIAALLAMQYEKTLVLLGSMGALSLMTILSVVIGKIFQSVPAQFQTTLPIGEYAAIALLMFFGLKSIKDAWDLPPVEAKNGEETGIELGEYSEAEELVKEKASKKLTNPLEILWKSFSLVFFAEWGDRSMLATVALGAAQSPLGVASGAIAGHLVATVLAIMGGAFLANYISEKLVGYVGGALFLVFAAATFFGVF | 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
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P86373 | RGSXLTILPLRNKIDLFYVG | PTM: N-glycosylated.
Sequence Mass (Da): 2287
Sequence Length: 20
Subcellular Location: Secreted
EC: 3.4.23.-
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Q9HUG6 | MFAATRLSRLRHDTSRILSHWILPLGWLALLTGMFWVGDRSDYHRLFYILLAAPTLLYVILQPRLLRPLTGSPLFIAFLAFSSYMMLSLSWSTPENSTGSLLKRPLYIALLFFCAAILALEAPLRLKTATWLAALGAVISAAATLLRYYWDANPLRLTGYGALYNPLLSAHVYGAFTALWLAYWMQSRPILAPLPLISLALLGGLLIATGSRTPLVGLTAALMWLVLAGDRKKALIALALALAGALLGYILYPEVITQRGASFRPEIWADALRQISEHPWLGHGYDHPMRIVLSNGMLLADPHNIELGVLFAGGIIGLLLWVAIYALAFGFSWKNRKSPAVLLASTWLVFGLAAGLTEGNAFLPRPKEHWFLIWIPMALLYALWIQQRFAASRRGEDIAAP | 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
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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.
Sequence Mass (Da): 21947
Sequence Length: 191
Subcellular Location: Cytoplasm
EC: 2.3.1.-
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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: H(+) + NADPH + O2 + phenylacetyl-CoA = 2-(1,2-epoxy-1,2-dihydrophenyl)acetyl-CoA + H2O + NADP(+)
Sequence Mass (Da): 35499
Sequence Length: 309
Pathway: Aromatic compound metabolism; phenylacetate degradation.
EC: 1.14.13.149
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P76081 | MTTFHSLTVAKVESETRDAVTITFAVPQPLQEAYRFRPGQHLTLKASFDGEELRRCYSICRSYLPGEISVAVKAIEGGRFSRYAREHIRQGMTLEVMVPQGHFGYQPQAERQGRYLAIAAGSGITPMLAIIATTLQTEPESQFTLIYGNRTSQSMMFRQALADLKDKYPQRLQLLCIFSQETLDSDLLHGRIDGEKLQSLGASLINFRLYDEAFICGPAAMMDDAETALKALGMPDKTIHLERFNTPGTRVKRSVNVQSDGQKVTVRQDGRDREIVLNADDESILDAALRQGADLPYACKGGVCATCKCKVLRGKVAMETNYSLEPDELAAGYVLSCQALPLTSDVVVDFDAKGMA | 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.
Sequence Mass (Da): 39320
Sequence Length: 356
Pathway: Aromatic compound metabolism; phenylacetate degradation.
EC: 1.-.-.-
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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 efflux via an energy-dependent mechanism (By similarity).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 16410
Sequence Length: 141
Subcellular Location: Cell inner membrane
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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 energy for transport, however it was not possible to conclude with complete certainty that protons, rather than alternative cations such as Na(+) ions, are exchanged for substrates by AceI . In addition, is 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 efflux via an energy-dependent mechanism .
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 16639
Sequence Length: 144
Subcellular Location: Cell inner membrane
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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 membrane protein
Sequence Mass (Da): 15913
Sequence Length: 140
Subcellular Location: Cell inner membrane
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Q4V920 | MSGAYDESAMSDETTDSFWEVGNYKRTVKRIEDGHRLCNDMMSCIQERAKIEKAYSQQLTDWSKRWRQLVERGPQYGTLERAWLAVMTEAEKVSELHQEVKNNLLNEDLEKVKNWQKDAYHKQMMGGFKETKEADEGFRKAQKPWAKKLKELETAKKTYHMACKEEKIASAREANSKGEASVTTDQQKKLQEKVDKCKNDVQKAKEKYEKSLDELNKCTPQYMENMEVVFDQCQQFEEKRLNFLREVLLDTKRHLNLTESQSYATVYRELERTIVSASAQEDLKWFSSVHGPGMHMNWPQFEEFNPDLSHAISKKEKVKRNHDGVTLTQVTHGAEHGTPQTGDRGSVSSYEKNQQYSAEWSDDEQPPTAAQSASETNGGNPFEEDSKGVRVRALYDYEGQEQDELTFKAGDELTKLEDEDEQGWCKGRLDSGQLGLYPANYVEPV | 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 cortex. Plays a role in the regulation of neurite formation, neurite branching and the regulation of neurite length. Required for normal synaptic vesicle endocytosis; this process retrieves previously released neurotransmitters to accommodate multiple cycles of neurotransmission. Required for normal excitatory and inhibitory synaptic transmission (By similarity). Required for normal embryonic development, including normal development of laterality, normal body size and shape, as well as normal brain and heart development. Required for normal development of stereocilia and kinocilia in sensory hair cells of neuromasts in the posterior lateral line organ, and thus also for balance keeping and normal swimming behavior.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 51356
Sequence Length: 445
Domain: The F-BAR domain mediates membrane-binding and membrane tubulation.
Subcellular Location: Cytoplasm
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Q9Z0W5 | MSGPYDEASEEITDSFWEVGNYKRTVKRIDDGHRLCNDLMSCVQERAKIEKAYAQQLTDWAKRWRQLIEKGPQYGSLERAWGAMMTEADKVSELHQEVKNSLLNEDLEKVKNWQKDAYHKQIMGGFKETKEAEDGFRKAQKPWAKKMKELEAAKKAYHLACKEEKLAMTREMNSKTEQSVTPEQQKKLVDKVDKCRQDVQKTQEKYEKVLEDVGKTTPQYMEGMEQVFEQCQQFEEKRLVFLKEVLLDIKRHLNLAENSSYIHVYRELEQAIRGADAQEDLRWFRSTSGPGMPMNWPQFEEWNPDLPHTAAKKEKQPKKAEGAALSNATGAVESTSQAGDRGSVSSYDRGQAYATEWSDDESGNPFGGNEANGGANPFEDDAKGVRVRALYDYDGQEQDELSFKAGDELTKLGEEDEQGWCRGRLDSGQLGLYPANYVEAI | 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 recruiting DNM1, DNM2 and DNM3 to membranes. Plays a role in the reorganization of the actin cytoskeleton and in neuron morphogenesis via its interaction with COBL and WASL, and by recruiting COBL to the cell cortex. Plays a role in the regulation of neurite formation, neurite branching and the regulation of neurite length. Required for normal synaptic vesicle endocytosis; this process retrieves previously released neurotransmitters to accommodate multiple cycles of neurotransmission. Required for normal excitatory and inhibitory synaptic transmission.
PTM: Phosphorylated by casein kinase 2 (CK2) and protein kinase C (PKC).
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 50449
Sequence Length: 441
Domain: The F-BAR domain forms a coiled coil and mediates membrane-binding and membrane tubulation. In the autoinhibited conformation, interaction with the SH3 domain inhibits membrane tubulation mediated by the F-BAR domain. DNM1 binding abolishes autoinhibition (By similarity).
Subcellular Location: Cytoplasm
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O13154 | MSGSYDDSVGVEVSSDSFWEVGNYKRTVKRIDDGHRLCNDLMNCIHERARIEKVYAQQLTEWAKRWKQLVEKGPQYGTVERAWCAFMSEAEKVSELHLEVKGSLMNEDFEKIKNWQKEAFHKQMMGGFKETKEAEDGFRKAQKPWAKKLKEVEAAKKAYHAACKEEKLAISRETNSKADPALNPEQLKKLQDKVERSKQDVLKTKAKYEKSLKELDNATPQYMENMEQVFEQCQQFEEKRLRFFREVLLEVQKHLDLSNVASYKNIYRELEQNIKTADAVEDLRWFRANQGPGMSMNWPQFEDDEWSADLNRTLSRREKKKASDGVTLTGINQTGDQVSQPNKHSSVSSYEKNQSYPTDWSDEESNNPFSSTDAKGDTNPFDEDTSPVMEVRVRALYDYEGQEQDELSFKAGDELTKMENEDEQGWCKGRLDNGQVGLYPANYVEPIQ | 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 receptors like the EGF receptor, contributing to its internalization in the absence of EGF stimulus.
PTM: Phosphorylated on serine residues.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 51971
Sequence Length: 448
Domain: The F-BAR domain forms a coiled coil and mediates membrane-binding and membrane tubulation. In the autoinhibited conformation, interaction with the SH3 domain inhibits membrane tubulation mediated by the F-BAR domain (By similarity).
Subcellular Location: Cell junction
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Q9UNF0 | MSVTYDDSVGVEVSSDSFWEVGNYKRTVKRIDDGHRLCSDLMNCLHERARIEKAYAQQLTEWARRWRQLVEKGPQYGTVEKAWMAFMSEAERVSELHLEVKASLMNDDFEKIKNWQKEAFHKQMMGGFKETKEAEDGFRKAQKPWAKKLKEVEAAKKAHHAACKEEKLAISREANSKADPSLNPEQLKKLQDKIEKCKQDVLKTKEKYEKSLKELDQGTPQYMENMEQVFEQCQQFEEKRLRFFREVLLEVQKHLDLSNVAGYKAIYHDLEQSIRAADAVEDLRWFRANHGPGMAMNWPQFEEWSADLNRTLSRREKKKATDGVTLTGINQTGDQSLPSKPSSTLNVPSNPAQSAQSQSSYNPFEDEDDTGSTVSEKDDTKAKNVSSYEKTQSYPTDWSDDESNNPFSSTDANGDSNPFDDDATSGTEVRVRALYDYEGQEHDELSFKAGDELTKMEDEDEQGWCKGRLDNGQVGLYPANYVEAIQ | 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 receptors like the EGF receptor, contributing to its internalization in the absence of EGF stimulus.
PTM: Phosphorylated by casein kinase 2 (CK2). Phosphorylation by PKC probably decreases the membrane binding and tubulation capacities of PACSIN2, thereby modulating the lifetime of caveolae (By similarity).
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 55739
Sequence Length: 486
Domain: The F-BAR domain forms a coiled coil and mediates membrane-binding and membrane tubulation . Autoinhibition of these functions is mediated by an interaction between the SH3 and F-BAR domains . The F-Bar domain also mediates the binding to the cell actin cytoskeleton through the interaction with CAV-1 (By similarity).
Subcellular Location: Cytoplasm
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Q9UKS6 | MAPEEDAGGEALGGSFWEAGNYRRTVQRVEDGHRLCGDLVSCFQERARIEKAYAQQLADWARKWRGTVEKGPQYGTLEKAWHAFFTAAERLSALHLEVREKLQGQDSERVRAWQRGAFHRPVLGGFRESRAAEDGFRKAQKPWLKRLKEVEASKKSYHAARKDEKTAQTRESHAKADSAVSQEQLRKLQERVERCAKEAEKTKAQYEQTLAELHRYTPRYMEDMEQAFETCQAAERQRLLFFKDMLLTLHQHLDLSSSEKFHELHRDLHQGIEAASDEEDLRWWRSTHGPGMAMNWPQFEEWSLDTQRTISRKEKGGRSPDEVTLTSIVPTRDGTAPPPQSPGSPGTGQDEEWSDEESPRKAATGVRVRALYDYAGQEADELSFRAGEELLKMSEEDEQGWCQGQLQSGRIGLYPANYVECVGA | 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 casein kinase 2 (CK2) and protein kinase C (PKC).
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 48487
Sequence Length: 424
Domain: The F-BAR domain forms a coiled coil and mediates membrane-binding and membrane tubulation.
Subcellular Location: Cytoplasm
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Q28057 | MKWLVLLGLVALSECIVILPLKKMKTLRETLREKNLLNNFLEEQAYRLSKNDSKITIHPLRNYLDTAYVGNITIGTPPQEFRVVFDTGSANLWVPCITCTSPACYTHKTFNPQNSSSFREVGSPITIFYGSGIIQGFLGSDTVRIGNLVSPEQSFGLSLEEYGFDSLPFDGILGLAFPAMGIEDTIPIFDNLWSHGAFSEPVFAFYLNTNKPEGSVVMFGGVDHRYYKGELNWIPVSQTSHWQISMNNISMNGTVTACSCGCEALLDTGTSMIYGPTKLVTNIHKLMNARLENSEYVVSCDAVKTLPPVIFNINGIDYPLRPQAYIIKIQNSCRSVFQGGTENSSLNTWILGDIFLRQYFSVFDRKNRRIGLAPAV | 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-type N-glycans remain unaltered .
Sequence Mass (Da): 41907
Sequence Length: 376
Subcellular Location: Secreted
EC: 3.4.23.-
|
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 | MEEILKSFKISIDNEGYSKSFSLEDLDNFNNNNNNNNNNNNNEENNPYEFFERYGFLVIRNVISEEDCNKTVGEIFDIIESKVKTFDRNDQSTWDQTFSEDGSSIPQYGSPSKPPIFKKQFLMNRTNPNVYKVFSKLLKNQDLMVNHDRACFFRPTLVNPKWKTNDNVHLDMNPYNWMGNGDICREELSKLTYARLGEFIVENNQPTQNDGLQLQGVINLLDNQELDGGYCVTPGFHTIFNEYFTSKKPQYTSPSWNFDKKDIAFKYAKRISMRKGSIVVWNQQMPHGSMSNKSFNPRMAQFIKIFPTSTVNSVRYQHRKNQIKSIIENSDELKDFPLNQISSQLLGLN | 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 | MEQLRAAARLQIVLGHLGRPSAGAVVAHPTSGTISSASFHPQQFQYTLDNNVLTLEQRKFYEENGFLVIKNLVPDADIQRFRNEFEKICRKEVKPLGLTVMRDVTISKSEYAPSEKMITKVQDFQEDKELFRYCTLPEILKYVECFTGPNIMAMHTMLINKPPDSGKKTSRHPLHQDLHYFPFRPSDLIVCAWTAMEHISRNNGCLVVLPGTHKGSLKPHDYPKWEGGVNKMFHGIQDYEENKARVHLVMEKGDTVFFHPLLIHGSGQNKTQGFRKAISCHFASADCHYIDVKGTSQENIEKEVVGIAHKFFGAENSVNLKDIWMFRARLVKGERTNL | 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 atoms) . Does not hydroxylate long and very long straight chain acyl-CoAs or 2-methyl- and 4-methyl-branched acyl-CoAs .
Catalytic Activity: 2-oxoglutarate + O2 + phytanoyl-CoA = 2-hydroxyphytanoyl-CoA + CO2 + succinate
Sequence Mass (Da): 38538
Sequence Length: 338
Pathway: Lipid metabolism; fatty acid metabolism.
Subcellular Location: Peroxisome
EC: 1.14.11.18
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