ids stringlengths 6 10 | seqs stringlengths 11 1.02k | texts stringlengths 108 11.1k |
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Q12515 | MATFNPQNEMENQARVQEYKVSTGRGGAGNIHKSMSKPSPVLLPLKSNSKTVANNNNNGSNQEKVPRFAIGRGGAGNIFHDPHLTRSAQQLDSNDNINYNDVINDIDDYISPITSDMVDEGGSNPVTNTRSRISATRSHQSLHATTSSPNNNAPIVVGRGGAGNIFFNKKKVASNGGNEEDEIRGGNIEDEDTINANEDNLFVVTSNGNALAAIKSTSKKPKNKLKGKSAPEKFAIGRGGAGNIISPKSSRNTINHNLNDDDEDKFNLKDDNGKEKKKKKKKKSGFFSSLKTMFN | Function: Involved in resistance to cisplatin.
PTM: Hyperphosphorylated after treatment with rapamycin in a TAP42-dependent manner.
Sequence Mass (Da): 31886
Sequence Length: 295
Subcellular Location: Cytoplasm
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O00254 | MKALIFAAAGLLLLLPTFCQSGMENDTNNLAKPTLPIKTFRGAPPNSFEEFPFSALEGWTGATITVKIKCPEESASHLHVKNATMGYLTSSLSTKLIPAIYLLVFVVGVPANAVTLWMLFFRTRSICTTVFYTNLAIADFLFCVTLPFKIAYHLNGNNWVFGEVLCRATTVIFYGNMYCSILLLACISINRYLAIVHPFTYRGLPKHTYALVTCGLVWATVFLYMLPFFILKQEYYLVQPDITTCHDVHNTCESSSPFQLYYFISLAFFGFLIPFVLIIYCYAAIIRTLNAYDHRWLWYVKASLLILVIFTICFAPSNII... | Function: Receptor for activated thrombin coupled to G proteins that stimulate phosphoinositide hydrolysis.
PTM: A proteolytic cleavage generates a new N-terminus that functions as a tethered ligand.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 42508
Sequence Length: 374
Subcellular Location: Cell... |
O08675 | MKILILVAAGLLFLPVTVCQSGINVSDNSAKPTLTIKSFNGGPQNTFEEFPLSDIEGWTGATTTIKAECPEDSISTLHVNNATIGYLRSSLSTQVIPAIYILLFVVGVPANIVTLWKLSLRTKSISLVIFHTNLAIADLLFCVTLPFKIAYHLNGNNWVFGEVTCRITTVVFYGNMYCAILILTCMGINRYLATAHPFTYQKLPKRSFSMLMCGMVWVMVFLYMLPFVILKQEYHLVHSEITTCHDVVDACESPSSFRFYYFVSLAFFGFLIPFVIIIFCYTTLIHKLKSKDRIWLGYIKAVLLILVIFTICFAPTNIIL... | Function: High affinity receptor for activated thrombin coupled to G proteins that stimulate phosphoinositide hydrolysis. May play a role in platelets activation.
PTM: A proteolytic cleavage generates a new N-terminus that functions as a tethered ligand.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da)... |
B3EWG9 | DINGGGATLPQKLYQTSGVLTAGFAPYIGVGSGNGKAAFLTNDYTKLTATELSTYATNLQPTWGKLIQVPSVATSVAIPFRITDWSGISGAGRTGPITVVYRITYMSPDFAASTLAGLDDATKGVSPAPSNVSDAIAQVLPPNDPSAPLDVTNPDDGVAGVQPYPDSGYPILGFTNLIFSAFFTKAFFTKHFGDTNNNDDAITANRFVPLPDNWKTELSTYATNLQPTWGK | Function: Catalyzes auto- and hetero-ADP ribosylation and produces short oligomers by elongating the ADP-ribose chain (up to 6-mer). Binds DNA non-specifically but with high affinity. Forms very stable complexes with circular DNA wherein the circular DNA confers thermostability compared to linear DNA.
Catalytic Activit... |
Q11208 | MEIDLPFKVEYSKSSRASCKGCKNKIEAGILRIAAMVQSAFHDGKQPNWFHEQCFFQKQRPTSAGDIENFENIRFEDQERIKKAIDNCTTVISAGGSKKGAKRSKGENNAIKDFGIEYAKSGRASCRGCEQKILKDQIRIRKTVFDTEVGMKYGGQPLWHHVECFAQLRGELGWLDTGENLPGFQTLKSDDKADVKKALPVIKDEGVSSAKKAKIEKIDEEDAASIKELTEKIKKQSKRLFKFRDEIKNEMSKDDMVALLEANNMEPVKGDSEKLLDQVADLLTFGALLPCTDCKGRQLLFHKSGYLCNGDLTEWTKCTK... | Function: Poly-ADP-ribosyltransferase that mediates poly-ADP-ribosylation of proteins and plays a key role in DNA repair. Mainly mediates glutamate and aspartate ADP-ribosylation of target proteins: the ADP-D-ribosyl group of NAD(+) is transferred to the acceptor carboxyl group of glutamate and aspartate residues and f... |
A0A0C5XL88 | MTTSFWRIATDARTYEADDLSGAGAKITGGRWNEVGVAIVYAASSRALACLETVVHLNSGGLPLNRYLVEIEVPDEVLASAEVATPGNLPVGWDAEPAGRVSISFGSQWAQSQRTALLLVPSVIVPEETNLLINPAHPDAKGIKARKVRKWLYDPRMIRKA | Function: Toxic component of a type II toxin-antitoxin (TA) system. Expression in E.coli inhibits cell growth; bacteriostasis is neutralized by expression of cognate antitoxin ParS. ADP-ribosylates E.coli ribose-phosphate pyrophosphokinase (RPPK, prs) using NAD(+) in vitro; ADP-ribosylates RPPK on 'Lys-182' and 'Ser-20... |
Q9NVD7 | MATSPQKSPSVPKSPTPKSPPSRKKDDSFLGKLGGTLARRKKAKEVSELQEEGMNAINLPLSPIPFELDPEDTMLEENEVRTMVDPNSRSDPKLQELMKVLIDWINDVLVGERIIVKDLAEDLYDGQVLQKLFEKLESEKLNVAEVTQSEIAQKQKLQTVLEKINETLKLPPRSIKWNVDSVHAKSLVAILHLLVALSQYFRAPIRLPDHVSIQVVVVQKREGILQSRQIQEEITGNTEALSGRHERDAFDTLFDHAPDKLNVVKKTLITFVNKHLNKLNLEVTELETQFADGVYLVLLMGLLEGYFVPLHSFFLTPDSF... | Function: Plays a role in sarcomere organization and in smooth muscle cell contraction. Required for normal development of the embryonic cardiovascular system, and for normal septation of the heart outflow tract. Plays a role in sprouting angiogenesis and is required for normal adhesion of vascular smooth muscle cells ... |
Q9EPC1 | MATSPQKSPLVPKSPTPKSPPSRKKDDSFLGKLGGTLARRKKAKEVSEFQEEGMNAINLPLSPISFELDPEDTLLEENEVRTMVDPNSRNDPKLQELMKVLIDWINDVLVGERIIVKDLAEDLYDGQVLQKLFEKLESEKLNVAEVTQSEIAQKQKLQTVLEKINETLKLPPRSIKWNVDSVHAKNLVAILHLLVALSQYFRAPIRLPDHVSIQVVVVQKREGILQSRQIQEEITGNTEALSGRHERDAFDTLFDHAPDKLNVVKKTLITFVNKHLNKLNLEVTELETQFADGVYLVLLMGLLEGYFVPLHSFFLTPDSF... | Function: Plays a role in sarcomere organization and in smooth muscle cell contraction. Required for normal development of the embryonic cardiovascular system, and for normal septation of the heart outflow tract. Plays a role in sprouting angiogenesis and is required for normal adhesion of vascular smooth muscle cells ... |
Q9ES46 | MSSAPPRSPTPRAPKMKKDESFLGKLGGTLARKKKTREVTDLQEEGKSAINSPMAPALVDIHPEDTQLEENEERTMIDPTSREDPKFKELVKVLLDWINDVLAEERIIVKQLEEDLYDGQVLQKLLEKLAHCKLNVAEVTQSEIGQKQKLQTVLEAVQDLLRPHGWPLRWNVDSIHGKNLVAILHLLVSLAMHFRAPIHLPEHVTVQVVVVRKREGLLHSSHISEELTTTTEIMMGRFERDAFDTLFDHAPDKLNLVKKSLITFVNKHLNKLNLEVTDLETQFADGVYLVLLLGLLEDYFVPLHNFYLTPDSFDQKVHNV... | Function: Adapter protein that plays a role in integrin signaling via ILK and in activation of the GTPases CDC42 and RAC1 by guanine exchange factors, such as ARHGEF6. Is involved in the reorganization of the actin cytoskeleton and formation of lamellipodia. Plays a role in cell adhesion, cell spreading, establishment ... |
Q9HBI0 | MEPEFLYDLLQLPKGVEPPAEEELSKGGKKKYLPPTSRKDPKFEELQKVLMEWINATLLPEHIVVRSLEEDMFDGLILHHLFQRLAALKLEAEDIALTATSQKHKLTVVLEAVNRSLQLEEWQAKWSVESIFNKDLLSTLHLLVALAKRFQPDLSLPTNVQVEVITIESTKSGLKSEKLVEQLTEYSTDKDEPPKDVFDELFKLAPEKVNAVKEAIVNFVNQKLDRLGLSVQNLDTQFADGVILLLLIGQLEGFFLHLKEFYLTPNSPAEMLHNVTLALELLKDEGLLSCPVSPEDIVNKDAKSTLRVLYGLFCKHTQKA... | Function: Probably plays a role in the regulation of cell adhesion and cytoskeleton organization.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 37485
Sequence Length: 331
Subcellular Location: Cell junction
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Q9ERD8 | MELEFLYDLLQLPKEVAQPTEEELPRGGKKKYLSPNSKRNPKFEELQKVLMEWINTTLLPEHIVVRSLEEDMFDGLILHHLFQKLASLKLEVEEISLTSASQRHKLGVILEAVNQNLQVEEKQAKWSVETIFNKDLLATLHLLVALAKRFQPDLPLPDNVQVEVIHIESTKTGLKSDKQVEQLTECKSHKDQPLQDAFDELFKLAPEKVHAVQEAIVSFVNQKLERLGLSVQSLDTQFADGVILLLLIGQLEGFFLHLKEFYLTPSSPTEMLHNVTLALDLLKDEGLFSYPVNPEDIVNKDAKSTLRILYSLFQKHSLRA... | Function: Probably plays a role in the regulation of cell adhesion and cytoskeleton organization.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 37603
Sequence Length: 331
Subcellular Location: Cell junction
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O16785 | MSTLGRSKTPSRDEPKKPGVFEKLSGTLSRKKKAPEDEHGNQGGAHHATDEDEVLELELEGREALDQSLVPVLARNIWLEEGEIRRYLTKETARDQKLAQVVDLLIYWLNEELADQRIVVRHLQEDLFDGQIIQKLLEKLEQIRIEVPEVSQSEEGQRQKLQIVVQTANRILGQPREQEKWSADLIHQKDFTAIIQLLVLLALHYRAPVRFPDNVVANVVVAQKEHGQVKTHRITEQITTVQTELAPKGTRDAFDTLFDYGPDKLAHVKTSLLAFCNKHLNKINLEVSDLDNQFQDGVFLVLLVGLLEGYFVPLYHFNLQ... | Function: Involved in the regulation of cell adhesion and cytoskeleton organization. Component of an integrin containing attachment complex, which is required for muscle development and maintenance . During embryonic development, required to recruit cpna-1, unc-89 and myofilaments to newly forming integrin attachments ... |
Q7DMA9 | MAVGDQTEQNYLPKKKKSETEDDKRRKKIVPGSLLKAVVRPGGGDSSPVDGDQVIYHCTVRTLDGVVVESTRSESGGRGVPIRDVLGNSKMILGLLEGIPTMHKGEIAMFKMKPEMHYAEIDCPVSAPENFPKDDELHFEIELLDFSKAKIASDDLGVIKKILNEGEGWESPREPYEVKARISAKSGDGHVIFSHTEEPYFFTFGKSEVPKGLEIGIGTMARKEKAVIYVRKQYLTESPLLHIDQDLEEVHFEVELVHFIQVRDMLGDGRLIKRRIRDGRGEFPMDCPLQDSRLSVHYKGMLLNEEKTVFYDSKIDNNDQ... | Function: PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides (By similarity). Essential protein regulating cell division, adhesion and elongation throughout the plant development and embryogenesis. Required for the spatial organization o... |
Q8IV76 | MKMRGEKRRDKVNPKSSQRKLNWIPSFPTYDYFNQVTLQLLDGFMITLSTDGVIICVAENISSLLGHLPAEIVGKKLLSLLPDEEKDEVYQKIILKFPLLNSETHIEFCCHLKRGNVEHGDSSAYENVKFIVNVRDICNEFPVVFSGLFSSHLCADFAACVPQEDRLYLVGNVCILRTQLLQQLYTSKAVSDEAVLTQDSDEEPFVGELSSSQGQRGHTSMKAVYVEPAAAAAAAAISDDQIDIAEVEQYGPQENVHMFVDSDSTYCSSTVFLDTMPESPALSLQDFRGEPEVNPLYRADPVDLEFSVDQVDSVDQEGPM... | Function: Functions as a suppressor of the biological clock that drives the daily circadian rhythms of cells throughout the body . Acts as a nuclear repressor of the CLOCK-BMAL1 heterodimer-mediated transcriptional activation of the core clock components . Inhibits circadian clock function in cancer cells, when overexp... |
Q02548 | MDLEKNYPTPRTSRTGHGGVNQLGGVFVNGRPLPDVVRQRIVELAHQGVRPCDISRQLRVSHGCVSKILGRYYETGSIKPGVIGGSKPKVATPKVVEKIAEYKRQNPTMFAWEIRDRLLAERVCDNDTVPSVSSINRIIRTKVQQPPNQPVPASSHSIVSTGSVTQVSSVSTDSAGSSYSISGILGITSPSADTNKRKRDEGIQESPVPNGHSLPGRDFLRKQMRGDLFTQQQLEVLDRVFERQHYSDIFTTTEPIKPEQTTEYSAMASLAGGLDDMKANLASPTPADIGSSVPGPQSYPIVTGRDLASTTLPGYPPHVP... | Function: Transcription factor that plays an essential role in commitment of lymphoid progenitors to the B-lymphocyte lineage . Fulfills a dual role by repressing B-lineage inappropriate genes and simultaneously activating B-lineage-specific genes . In turn, regulates cell adhesion and migration, induces V(H)-to-D(H)J(... |
Q1LZF1 | MQNSHSGVNQLGGVFVNGRPLPDSTRQKIVELAHSGARPCDISRILQVSNGCVSKILGRYYETGSIRPRAIGGSKPRVATPEVVSKIAQYKRECPSIFAWEIRDRLLSEGVCTNDNIPSVSSINRVLRNLASEKQQMGADGMYDKLRMLNGQTGSWGTRPGWYPGTSVPGQPTQDGCQQQEGGGENTNSISSNGEDSDEAQMRLQLKRKLQRNRTSFTQEQIEALEKEFERTHYPDVFARERLAAKIDLPEARIQVWFSNRRAKWRREEKLRNQRRQASNTPSHIPISSSFSTSVYQPIPQPTTPVSSFTSGSMLGRTDT... | Function: Transcription factor with important functions in the development of the eye, nose, central nervous system and pancreas. Required for the differentiation of pancreatic islet alpha cells. Competes with PAX4 in binding to a common element in the glucagon, insulin and somatostatin promoters. Regulates specificati... |
P26367 | MQNSHSGVNQLGGVFVNGRPLPDSTRQKIVELAHSGARPCDISRILQVSNGCVSKILGRYYETGSIRPRAIGGSKPRVATPEVVSKIAQYKRECPSIFAWEIRDRLLSEGVCTNDNIPSVSSINRVLRNLASEKQQMGADGMYDKLRMLNGQTGSWGTRPGWYPGTSVPGQPTQDGCQQQEGGGENTNSISSNGEDSDEAQMRLQLKRKLQRNRTSFTQEQIEALEKEFERTHYPDVFARERLAAKIDLPEARIQVWFSNRRAKWRREEKLRNQRRQASNTPSHIPISSSFSTSVYQPIPQPTTPVSSFTSGSMLGRTDT... | Function: Transcription factor with important functions in the development of the eye, nose, central nervous system and pancreas. Required for the differentiation of pancreatic islet alpha cells (By similarity). Competes with PAX4 in binding to a common element in the glucagon, insulin and somatostatin promoters. Regul... |
Q751U2 | MQSVRQTVLFESEEAWRAGAEQNATAITVHARGGEVVQTRRTWAAAGGPRVRVTWSGGRTVSEVSPQLAAGLSVYVEGGAHVSRDFVQARGQAVFHSAQLELDAVRAWWPRELAVQPEALRWAECAYDIELGRQVRVDEYCALRAGETVALTAAAGGTDEAKVETGVFYPEISDGADVSLSGFRCTWLRDGSGRTDTCQKTLLMYKPAHVHMPEPAVGIELVQPVTLHPVIEVDLSSVSASGPACAHHVFLQLPAQLFVDKFQQPPELLFGEDDLELPEYKVEAWGSEVIYALEPGRVNRVQLHSRYARPGPGRRYEVVP... | Function: Required for proper folding and/or the stability of a subset of proteins in the endoplasmic reticulum. Component of glycosylphosphatidylinositol-mannosyltransferase 1 which transfers the first of the 4 mannoses in the GPI-anchor precursors during GPI-anchor biosynthesis. Probably acts by stabilizing the manno... |
Q4WU12 | MRRRITFVQRPESPFHVDQAVLTSDALSITHLDAAREERATFGFDELPAEIWQVLKSSHELHIRWATERPYEIGAPFSSRISPGLHVYYTPGTARETGVGLCSLLKTVFDESLECQSLRYYSRLPSLQNLVAFIQHKFCDRSDEKCVHHAESILSADSVDVNYDSISHALTVSGYWSTSPGQGWTEQIRKHAADTHQVEVGLLGVESATEPEELKMEPTLFSFPSRHHPLPADATYTVSFPAPTGLHPTLTISMPRASLRRPPAPPDATCALHTYLTLPSWIFGDKYQLSTTDRLFLSSHNLAALRAVAGETDLEAPDWV... | Function: Required for proper folding and/or the stability of a subset of proteins in the endoplasmic reticulum. Component of glycosylphosphatidylinositol-mannosyltransferase 1 which transfers the first of the 4 mannoses in the GPI-anchor precursors during GPI-anchor biosynthesis. Probably acts by stabilizing the manno... |
Q5A4J4 | MRQRTTIYNPYSSHDGIITNLNRTNFQLSSIPNHLFTIENKYTITTTTTQPNKSSLYSAIKELRIQTKFNNNESGIPIFSFHYEPGLNIYAVPQSNVDKLEFWQQVEQLIMELLGIKLSSQQWIANVNSFYYHDIQPQPLLNLKEGWKFNLHPKSNYDYIYNQDKIIIRELLTNVSEIEFNLESGIYKEIGLFLIDEKISTNDDLNLSGIRVILDEDSNTNNKEESIHKTMFHIKPRHRSFDDSTTITTTKIIPQGLHPILSTELNTTTIVIPTDFDVEECKFYYYLNLNKSLIFDQFQNIPIGSQLIINNGNKNLELPE... | Function: Required for proper folding and/or the stability of a subset of proteins in the endoplasmic reticulum. Component of glycosylphosphatidylinositol-mannosyltransferase 1 which transfers the first of the 4 mannoses in the GPI-anchor precursors during GPI-anchor biosynthesis. Probably acts by stabilizing the manno... |
Q6FX62 | MESVRHRIALLFANEADIQDVETVEDGVIVFPNSNITIQDRWTYAIDYELDSIRRISWRNPSSTRQFSVIESRLAPGFNIYSNDKEARLNLFGIQPVYSPMYKSLHSETWKSINEILPGGKNLNIPWNPELCDYDILITANTVQVFSYCSLVEKKKFVKDAGKVEIGLFHVDTEDEEDINLSGLRCTWEDTSNNIGKCEKTTLFYKPFHLYVDDSSDIAPITIENTNGLHPKMKIDLSGIRKDKDCRHFVFSQLPSEIFVDKFQSPGSIVFGLDDLELPDYKVNSLSWGSESIVTLKEGQINEITYFSRYLEPKERASNK... | Function: Required for proper folding and/or the stability of a subset of proteins in the endoplasmic reticulum. Component of glycosylphosphatidylinositol-mannosyltransferase 1 which transfers the first of the 4 mannoses in the GPI-anchor precursors during GPI-anchor biosynthesis. Probably acts by stabilizing the manno... |
Q6BKZ8 | MIRQRTTIFNPTKSNDGIIEAVDSSHLQLSSIDYQCEDKFILQTPKFKYIDKLRIQLNQFHSESILFSKYQAGLNIYCKPKIGDEGFNQEEFFNELNQMMTNLFDIPRDGWINSLDTLFYHEPSTGSESFIEYVRKLTGNESNVNLEVSPNIEYVYDGEKVVLKLNGKSLANTTITKNSKFNKEIGLFLIEKGISSEDDIVLSGLRVILNGDDDKNEEYLQKTLFHVKRRQRQSRGTYSSQVKENGMHPFLKTDIHSDIPNDEDLIQCKLYYYLDLNKSFFVDKYQLPKEFTSYVNFGNTDLELPEYKINEWGSEILMEI... | Function: Required for proper folding and/or the stability of a subset of proteins in the endoplasmic reticulum. Component of glycosylphosphatidylinositol-mannosyltransferase 1 which transfers the first of the 4 mannoses in the GPI-anchor precursors during GPI-anchor biosynthesis. Probably acts by stabilizing the manno... |
Q4IBD0 | MRERVTFIHNDYSLDPEALDNQDAGLLGPQIETVRQDKLTIPFGELPSELTDILQEYEALHIRWASPVKSETMDPFTSRISPGLHVYATPVLPSSCNPTKLCSWLQRFGPLDCSKPEAFTEFQQSTSTSPSFSFYEALEDLHSFITTSSQEFCPELDSVCNARLRSLLTASGLDLSFDKAANALVVSALWPLRPQTVAVPASSARRVEVGIFINDRSQPNMKENELGVAGVLSVLGDQKKPSPTIFTFPARHRRDGSVFTSKFLTPTGLHPTLQLSFNSNKLPSADGECAPYAFLTLPKTIFADRYQLGDELFLASKNLT... | Function: Required for proper folding and/or the stability of a subset of proteins in the endoplasmic reticulum. Component of glycosylphosphatidylinositol-mannosyltransferase 1 which transfers the first of the 4 mannoses in the GPI-anchor precursors during GPI-anchor biosynthesis. Probably acts by stabilizing the manno... |
Q6CV11 | MSVQTIQSESFIEEKRRITVLLDRDGRSVEEKVVNRDGVITIPNQSGHVQDRAVLFVPQLASRPDFIHISWKRNAEADITPIKSYIPYGFNIFTNSSGSIAKFIDTPVGKVYYSDTFEDNALSKWFPPEFVDQLLRYSEDNDLDITVTRGRVEVNRYYELTDDNLFPLNGTESVKTEAGIFQVDTEDDTDTSLSGLRCTWHTGSGALNKCQRTLFFYNQIYADKSSLSEVSLTLSEPVNLHPVVQIDLTSKRPIHNCEYYAYFNLPKYFFIDQFQSIPTLLFGEHDLELPEYKLSGFGSISLFTLQPGSINEVTLHSRYI... | Function: Required for proper folding and/or the stability of a subset of proteins in the endoplasmic reticulum. Component of glycosylphosphatidylinositol-mannosyltransferase 1 which transfers the first of the 4 mannoses in the GPI-anchor precursors during GPI-anchor biosynthesis. Probably acts by stabilizing the manno... |
Q7RYM7 | MRERITFIQKQGDSIEPTTLKIKGGVLNGPEIQAAREDRLTIAIDELPKDLQALLGTAHELHIRYVSSQPYEAITPLLARLPPGFHLFYTPAGQADATSPALCLALNQIFGNVQCENPEKSFTTLPRDRFSHSAAYQFYQPSVDLSPFIALVKEKLCSSSKDQSCAARADRLANASSLDISYDAISHAVKLTATWPYQKQEVHATSRPQTRTEVGVLNSDRPGHLEPHELGISGLLTVLGQDKKPSATMFAFASRHRDAESSFSAEFLEPTGLHPTLKLRLESSKPPIEDAYCSPHAYFTLPKTIFADRHQLSDDLFLAS... | Function: Required for proper folding and/or the stability of a subset of proteins in the endoplasmic reticulum. Component of glycosylphosphatidylinositol-mannosyltransferase 1 which transfers the first of the 4 mannoses in the GPI-anchor precursors during GPI-anchor biosynthesis. Probably acts by stabilizing the manno... |
O94472 | MDLQRTNQDTGTTTLFKVVISNTVNYLPKGVWILRNNTIDSLSIAKQFREIKNNINISHLSRENYWVETPFGKVFHSEVVSEEFMQIFIDKGNKALNNEEMIFACMSEKGWNVSLETVPNLDIPVGSYETQLGLPVGLHPKLHVHLKNLHKPEDECSLQGFMYIPPTLFIDRYELSNIAEMHADNLGHVLGIWGETDLEAPSYKLNGTGSFFWFDIYTDDGLLQKDYIDTIIPLHTRYQSPLKGQTYLKTSLTNPKFFWNCDTEDKVNDFRFLFSSKNKYTLQNDPTTLSISIPIADLSYKHVVEWVTNGVAIFSFFYLL... | Function: Required for proper folding and/or the stability of a subset of proteins in the endoplasmic reticulum. Component of glycosylphosphatidylinositol-mannosyltransferase 1 which transfers the first of the 4 mannoses in the GPI-anchor precursors during GPI-anchor biosynthesis. Probably acts by stabilizing the manno... |
Q6C5K1 | MRRRATILADLQQHGDKISFKPGDNNKSKLTVSVNAPRQDRFSAPVSNADLDVLNHVADVSVAWGRPSAAQQPVLFAAAYEPGLHVTVVKKQASEPRKWGEEKPSEAAPELVHVAKFLEEQLGLPVDPKTFIESRSDYTYYDPLVGPEAFGHFVDKHSACSDESEEFVNDLDTFNYAQSASFHIDHDKKELVTEVTIPDLEHYFNQKKQHISRACKNDRLEVGIFDLNNLATSYAFRGVAELKGLLHDSTKEKPQETFLVIEPRHNIGAGSVSVDFERPVGLHPKSELKLRHIAIPTDHNDENDGVKHCRLFAKYSAPSS... | Function: Required for proper folding and/or the stability of a subset of proteins in the endoplasmic reticulum. Component of glycosylphosphatidylinositol-mannosyltransferase 1 which transfers the first of the 4 mannoses in the GPI-anchor precursors during GPI-anchor biosynthesis. Probably acts by stabilizing the manno... |
P25580 | MVTRHRVTVLYNAPEDIGNHMRQNDTHLTVRGGSGVVLQQRWLLERTGSLDKSFTRITWRPRADLARSLSVIENELSAGFSVYSNSSDVPERFITNPVYNSFHSEKFDIEQYLPPEVDLNLSWNPEDFTYDISVEPTQIQIVEYRLLKQGEEFTIARVKDEKLEVGVFFVDASDESDVDIGGIRCNWRMDDGKMERCQKTSLLYKQGHIAYNHSTTTTSLYLNEPIGLHPKIMIDLTDFEERPKCMYLMHLQLPLELFIDKFQSSPLLLFGEDDLELPEYSLRDKAWGSESIFELKAGTMNEVTLHTRYIEPSNNKGDKL... | Function: Required for proper folding and/or the stability of a subset of proteins in the endoplasmic reticulum. Aids the autocatalytic processing of PRB1. Component of glycosylphosphatidylinositol-mannosyltransferase 1 which transfers the first of the 4 mannoses in the GPI-anchor precursors during GPI-anchor biosynthe... |
A0A0E3D8L9 | MERRTVLITGCSQGGIGSALAEVFHQRGFHVFATARKTEKMKHLRDLDRMTLIPLDVTQESQISAAVELIQKHTGGTLDYLVNNAGDGYIIPVLDCDQLHGRQIFEVNFWGPLRMIQEFSPLLIAARGTIVNINSVASETLPLWLGIYSSSKAALLALSETLRLELKPFGVQVLSVMTGAVQTMIFQTNYRLPPDSAYMTWEKQIAAQAEGSEKASRMSATVYAERVVGDILNRQGGITYRGQMASFAYWVVALMPRFLRATPLLAQVGSQ | Function: Short-chain dehydrogenase; part of the gene cluster that mediates the biosynthesis of the indole diterpenes penitrems . The geranylgeranyl diphosphate (GGPP) synthase penG catalyzes the first step in penitrem biosynthesis via conversion of farnesyl pyrophosphate and isopentyl pyrophosphate into geranylgeranyl... |
Q9Y5H7 | MVYSRRGSLGSRLLLLWLLLAYWKAGSGQLHYSIPEEAKHGTFVGRIAQDLGLELAELVPRLFRVASKGRGDLLEVNLQNGILFVNSRIDREELCRRRAECSIHLEVIVDRPLQVFHVEVAVKDINDNPPRFSRQEQRLFILESRMPDSRFPLEGASDLDIGANAQLRYRLNPNEYFDLDVKTNEEETNFLELVLRKSLDREETQEHRLLVIATDGGKPELTGTVQLLINVLDANDNAPEFDKSIYNVRLLENAPSGTLVIKLNASDADEGINKEIVYFFSNLVLDDVKSKFIINSNTGEIKVNGELDYEDYNSYEINID... | Function: Potential calcium-dependent cell-adhesion protein. May be involved in the establishment and maintenance of specific neuronal connections in the brain.
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 102048
Sequence Length: 936
Subcellular Location: Cell membrane
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Q91Y13 | MVNLRGYNWKSQQLLLFLIIVAAWEAGSGQLHYSVPEEAKHGTFVGRIAQDLGLELTELVPRLFRVASKDRGDLLEVNLQNGILFVNSRIDREELCGRSAECSIHLEVIVDRPLQVFHVEVEVKDINDNPPMFPATQKALFILESRLLDSRFPLEGASDADVGSNALLTYRLSTNEHFSLDVPPNHEQVKPLGLVLRKPLDREEAAEIRLLLTATDGGKPELTGTVQLLITVLDVNDNAPVFDRSLYTVKLPENVPNGTLVIKVNASDLDEGVNGDVMYSFSSDVSSDIKSKFHMDTVSGEITVIGIIDFEESKAYKIPL... | Function: Calcium-dependent cell-adhesion protein involved in cells self-recognition and non-self discrimination . Thereby, it is involved in the establishment and maintenance of specific neuronal connections in the brain .
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 101266
Sequence Lengt... |
Q9Y5H6 | MDYHWRGELGSWRLLLLLLLLAAWKVGSGQLHYSVPEEAKHGTFVGRIAQDLGLELAELVPRLFRVASKRHRDLLEVSLQNGILFVNSRIDREELCGRSAECSIHLEVIVDRPLQVFHVDVEVKDVNDNPPVFRVKDQKLFVSESRMPDSRFPLEGASDADVGANSVLTYRLSSHDYFMLDVNSKNDENKLVELVLRKSLDREDAPAHHLFLTATDGGKPELTGTVQLLVTVLDVNDNAPTFEQSEYEVRIFENADNGTTVIKLNASDPDEGANGAISYSFNSLVETMVIDHFSIDRNTGEIVIRGNLDFEQENLYKILI... | Function: Potential calcium-dependent cell-adhesion protein. May be involved in the establishment and maintenance of specific neuronal connections in the brain.
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 103051
Sequence Length: 950
Subcellular Location: Cell membrane
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Q91Y11 | MRLGNRPEDIRTCVHLRWHIHGLLRQENASVVISKCLRHGAWRLLLWLLLLATWDVGSGQLHYSVPEEAKHGTFVGRIAQDLGLELAELVPRLFRVVSKDRGDLLEVNLQNGILFVNSRIDREELCGQNAECSIHLEVIVDRPLQVFHVEVEVRDINDNPPIFSVAEQKILVAESRLLDSRFPLEGASDADVGENSMLTYKLSSNEFFILDIVNKRGKGKFPVLVLRKLIDREENPQLKLLLTATDGGKPEFTGSVSLLIQVLDVNDNAPVFDRSVYEVKMYENQENKTLVIWLNATDSDEGINKEVEYSFSSLASSIIR... | Function: Potential calcium-dependent cell-adhesion protein. May be involved in the establishment and maintenance of specific neuronal connections in the brain.
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 106763
Sequence Length: 979
Subcellular Location: Cell membrane
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Q91Y20 | MSCVAMKYCHESWCLLLSLLLFAIWEPGSGQLRYSVPEEAKHGTFVGRIAQDLGLELTELVPRLFRVASKDRGDLLEVNLQNGILFVNSRIDREELCGRSAECSIHLEVIVDRPLQVFHVEVEVRDINDNPPVFPTTEKNLFVSESRALDPHFSLEGASDADIGTNALLTYRLSPSEYFSLEVPTTDELVKPLQLVLKKPLDRERASELHLVVKATDGGKPELTGTLELHITVLDANDNAPAFDRAIYRVKLVENARNGTVVIRLNASDLDEGSNGQILYSFAADVSPKTEATFHIDSVSGEIKVNGKIDFEETNLWKIQ... | Function: Potential calcium-dependent cell-adhesion protein. May be involved in the establishment and maintenance of specific neuronal connections in the brain.
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 102057
Sequence Length: 946
Subcellular Location: Cell membrane
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F1NJ67 | MAAPSDPPTAATPPAPPPPARRCLLAPSVEPLLFLATLALGLQVPLATQYLWDRLGAERGYVGPNASSPHGCGNGSGAVDPLREEVEALVAHWNLCINLGGFFVGLFSVTLFGPWSDSVGRRPVLVLPAVGMAVQAAVYLLVMYLRLHVAYLLLGRIISGLLGDYNLILAGCFASVADSSNQRTRTFRVAILEACLGVAGMVASVGGGQWRKAEGYINPFWLVLAASLAAALYAALCLQETVKQRRAAKLLTLQHYKAVYKLYTAPEDLSSRRKLALYSLAFFLLVTVHFGTKDLYVLYELGSPLCWASDLIGYGSAASY... | Function: Proton-coupled folate symporter that mediates folate absorption using an H(+) gradient as a driving force . Involved in the intestinal absorption of folates at the brush-border membrane of the proximal jejunum, and the transport from blood to cerebrospinal fluid across the choroid plexus . Functions at acidic... |
Q96NT5 | MEGSASPPEKPRARPAAAVLCRGPVEPLVFLANFALVLQGPLTTQYLWHRFSADLGYNGTRQRGGCSNRSADPTMQEVETLTSHWTLYMNVGGFLVGLFSSTLLGAWSDSVGRRPLLVLASLGLLLQALVSVFVVQLQLHVGYFVLGRILCALLGDFGGLLAASFASVADVSSSRSRTFRMALLEASIGVAGMLASLLGGHWLRAQGYANPFWLALALLIAMTLYAAFCFGETLKEPKSTRLFTFRHHRSIVQLYVAPAPEKSRKHLALYSLAIFVVITVHFGAQDILTLYELSTPLCWDSKLIGYGSAAQHLPYLTSLL... | Function: Proton-coupled folate symporter that mediates folate absorption using an H(+) gradient as a driving force . Involved in the intestinal absorption of folates at the brush-border membrane of the proximal jejunum, and the transport from blood to cerebrospinal fluid across the choroid plexus . Functions at acidic... |
Q6PEM8 | MEGRVSSVGSPHSFLNAPVLFRGPVEPLVFLANFALVLQGPLTTQYLWHRFSTELGYNGTRHRENCGNQSADPLMKEVETLTSHWTLYMNVGGFLVGLFWSTLLGAWSDRVGRRPLLVLASLGLLLQAVVSIFVVQLELHVGFFVLGRALCALLGDFNGLLAASFASVADVSSNHSRTFRMALLEACIGVAGTLASLLGGHWLRAQGYANPFWLALALLIVMALYAAFCFGETVKEPKSTRLFTLRHHRSIARLYVVPAPEKSRMHLALYSLAIFVVVTVHFGAQDILTLYELSAPLCWDSKLIGYGSAAQHLPYLTSLL... | Function: Proton-coupled folate symporter that mediates folate absorption using an H(+) gradient as a driving force . Involved in the intestinal absorption of folates at the brush-border membrane of the proximal jejunum, and the transport from blood to cerebrospinal fluid across the choroid plexus . Functions at acidic... |
P35227 | MHRTTRIKITELNPHLMCALCGGYFIDATTIVECLHSFCKTCIVRYLETNKYCPMCDVQVHKTRPLLSIRSDKTLQDIVYKLVPGLFKDEMKRRRDFYAAYPLTEVPNGSNEDRGEVLEQEKGALSDDEIVSLSIEFYEGARDRDEKKGPLENGDGDKEKTGVRFLRCPAAMTVMHLAKFLRNKMDVPSKYKVEVLYEDEPLKEYYTLMDIAYIYPWRRNGPLPLKYRVQPACKRLTLATVPTPSEGTNTSGASECESVSDKAPSPATLPATSSSLPSPATPSHGSPSSHGPPATHPTSPTPPSTASGATTAANGGSLNC... | Function: Transcriptional repressor. Binds specifically to the DNA sequence 5'-GACTNGACT-3'. Has tumor suppressor activity. May play a role in control of cell proliferation and/or neural cell development. Regulates proliferation of early T progenitor cells by maintaining expression of HES1. Also plays a role in antero-... |
P23798 | MHRTTRIKITELNPHLMCALCGGYFIDATTIVECLHSFCKTCIVRYLETNKYCPMCDVQVHKTRPLLSIRSDKTLQDIVYKLVPGLFKDEMKRRRDFYAAYPLTEVPNGSNEDRGEVLEQEKGALGDDEIVSLSIEFYEGVRDREEKKNLTENGDGDKEKTGVRFLRCPAAMTVMHLAKFLRNKMDVPSKYKVEILYEDEPLKEYYTLMDIAYIYPWRRNGPLPLKYRVQPACKRLTLPTVPTPSEGTNTSGASECESVSDKAPSPATLPATSSSLPSPATPSHGSPSSHGPPATHPTSPTPPSTAAGTTTATNGGTSNC... | Function: Transcriptional repressor . Binds specifically to the DNA sequence 5'-GACTNGACT-3' . Has tumor suppressor activity . May play a role in control of cell proliferation and/or neural cell development (Probable). Regulates proliferation of early T progenitor cells by maintaining expression of HES1. Also plays a r... |
Q5SLL5 | MQRLEALGIHPKKRVFWNTVSPVLVEHTLLRGEGLLAHHGPLVVDTTPYTGRSPKDKFVVREPEVEGEIWWGEVNQPFAPEAFEALYQRVVQYLSERDLYVQDLYAGADRRYRLAVRVVTESPWHALFARNMFILPRRFGNDDEVEAFVPGFTVVHAPYFQAVPERDGTRSEVFVGISFQRRLVLIVGTKYAGEIKKSIFTVMNYLMPKRGVFPMHASANVGKEGDVAVFFGLSGTGKTTLSTDPERPLIGDDEHGWSEDGVFNFEGGCYAKVIRLSPEHEPLIYKASNQFEAILENVVVNPESRRVQWDDDSKTENTRS... | Cofactor: Binds 1 Mn(2+) ion per subunit.
Function: Involved in gluconeogenesis. Catalyzes the conversion of oxaloacetate (OAA) to phosphoenolpyruvate (PEP) through direct phosphoryl transfer between the nucleoside triphosphate and OAA (By similarity).
Catalytic Activity: ATP + oxaloacetate = ADP + CO2 + phosphoenolpyr... |
P13735 | MAPIIHKNLTAPELVEWALKLEKDSQLTARGALSVRSYAKTGRSPRDKRIVNTTDVTDNVDWGSVNMKLTEESFEKLKTIAKDYFATCKHLFVMDCFAGHDERYRLKVRVYTTRPYHALFMRNMLIVPTLEELQSFGEPDYVIYNAGEAKADPTVPGVTSTTSVALNFKTREQVILGTEYAGEMKKGILTVMFELMPRMGHLCMHASANVGKSGDVTVFFGLSGTGKTTLSADPRRNLIGDDEHVWTDRGVFNIEGGCYAKAIGLNPETEKDIYEAVRFGAVAENCTLDRRTHEIDFNDESICKNTRVAYPLMHIDGALS... | Function: P60 has the capability to bind to microtubules and membrane vesicles in vitro.
Catalytic Activity: ATP + oxaloacetate = ADP + CO2 + phosphoenolpyruvate
Sequence Mass (Da): 52457
Sequence Length: 472
Pathway: Carbohydrate biosynthesis; gluconeogenesis.
Subcellular Location: Glycosome
EC: 4.1.1.49
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G0SF70 | MLEARLEQASILKKVVDAIKDLVQDCNFDCNDSGIALQAMDNSHVALVSMMLKAEGFSPYRCDRNIALGVNLTSLTKVLRAAQNEDILTLKAEDAPDVLNLVFESSETDRISEYDLKLMDIDQEHLGIPETEYAATITMPSNEFKRITTDLMAMSESVTIEANKDGVKFSCQGDIGNGSVTLRQHTNVEKPNESIEIELSEPVSLTFSLKYLVNFCKASALSNTVKICLSNEVPLLVEYSLGGSSYLRFYLAPKIGDDE | Function: This protein is an auxiliary protein of DNA polymerase delta and is involved in the control of eukaryotic DNA replication by increasing the polymerase's processibility during elongation of the leading strand. Involved in DNA repair.
PTM: Monoubiquitinated on Lys-164 upon DNA damage, and then polyubiquitinated... |
Q9DEA3 | MFEARLVQGSVLKRVLEALKDLITEACWDLGSGGISLQSMDSSHVSLVQLTLRSEGFDTYRCDRNIAMGVNLNSMSKILKCAGNEDIITLRAEDNADTLALVFEAPNQEKVSDYEMKLMDLDVEQLGIPEQEYSCVVKMPSAEFARICRDLSHIGDAVVISCAKDGVKFSANGELGNGNIKLSQTSNVDKEEEAVTIEMNEPVQLTFALRYLNFFTKATPLSPTVTLSMSADVPLVVEYKIADMGHLKYYLAPKIEDQQEGS | Function: This protein is an auxiliary protein of DNA polymerase delta and is involved in the control of eukaryotic DNA replication by increasing the polymerase's processibility during elongation of the leading strand.
PTM: Monoubiquitinated by the UBE2B-RAD18 complex on Lys-164. Monoubiquitination at Lys-164 also take... |
P12004 | MFEARLVQGSILKKVLEALKDLINEACWDISSSGVNLQSMDSSHVSLVQLTLRSEGFDTYRCDRNLAMGVNLTSMSKILKCAGNEDIITLRAEDNADTLALVFEAPNQEKVSDYEMKLMDLDVEQLGIPEQEYSCVVKMPSGEFARICRDLSHIGDAVVISCAKDGVKFSASGELGNGNIKLSQTSNVDKEEEAVTIEMNEPVQLTFALRYLNFFTKATPLSSTVTLSMSADVPLVVEYKIADMGHLKYYLAPKIEDEEGS | Function: Auxiliary protein of DNA polymerase delta and epsilon, is involved in the control of eukaryotic DNA replication by increasing the polymerase's processibility during elongation of the leading strand . Induces a robust stimulatory effect on the 3'-5' exonuclease and 3'-phosphodiesterase, but not apurinic-apyrim... |
Q7TMR0 | MGCRALLLLSFLLLGAATTIPPRLKTLGSPHLSASPTPDPAVARKYSVLYFEQKVDHFGFADMRTFKQRYLVADKHWQRNGGSILFYTGNEGDIVWFCNNTGFMWDVAEELKAMLVFAEHRYYGESLPFGQDSFKDSQHLNFLTSEQALADFAELIRHLEKTIPGAQGQPVIAIGGSYGGMLAAWFRMKYPHIVVGALAASAPIWQLDGMVPCGEFMKIVTNDFRKSGPYCSESIRKSWNVIDKLSGSGSGLQSLTNILHLCSPLTSEKIPTLKGWIAETWVNLAMVNYPYACNFLQPLPAWPIKEVCQYLKNPNVSDTV... | Function: Cleaves C-terminal amino acids linked to proline in peptides such as angiotensin II, III and des-Arg9-bradykinin. This cleavage occurs at acidic pH, but enzymatic activity is retained with some substrates at neutral pH (By similarity).
Catalytic Activity: Cleavage of a -Pro-|-Xaa bond to release a C-terminal ... |
P0A5R5 | MSKVLVTGFGPYGVTPVNPAQLTAEELDGRTIAGATVISRIVPNTFFESIAAAQQAIAEIEPALVIMLGEYPGRSMITVERLAQNVNDCGRYGLADCAGRVLVGEPTDPAGPVAYHATVPVRAMVLAMRKAGVPADVSDAAGTFVCNHLMYGVLHHLAQKGLPVRAGWIHLPCLPSVAALDHNLGVPSMSVQTAVAGVTAGIEAAIRQSADIREPIPSRLQI | Function: Removes 5-oxoproline from various penultimate amino acid residues except L-proline.
Catalytic Activity: Release of an N-terminal pyroglutamyl group from a polypeptide, the second amino acid generally not being Pro.
Sequence Mass (Da): 23193
Sequence Length: 222
Subcellular Location: Cytoplasm
EC: 3.4.19.3
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B2HP18 | MTKVLVTGFGPYGVTPDNPAQFTAEALDGRTIAGATVVSRIVPGAYFDSIAAAEQAIAEVDPQLVIMLGEYPGRAMLTVERLAQNINDCGRYGLADTAGKVLVGEPTDPDGPVAYHATVPVHEMVLAMRAAGIPADVSDAAGTFVCNHLMYGVLHHIATQNLPIRAGWVHLPCLPMVAALDRNLGVPSMSVETAVAGLVAGIEAAVQHSADTREPVPSRLQI | Function: Removes 5-oxoproline from various penultimate amino acid residues except L-proline.
Catalytic Activity: Release of an N-terminal pyroglutamyl group from a polypeptide, the second amino acid generally not being Pro.
Sequence Mass (Da): 23185
Sequence Length: 222
Subcellular Location: Cytoplasm
EC: 3.4.19.3
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Q8ENE4 | MKKILLTGFVPFLDNPINPTEEIVQGLHKKSVNGWEVVGEVLPVDFHVTGDHLVELIHKVQPSAIISLGLAAGRNRITPERIAINCNDGPVDNQGYKPDGEKIISDGPDGYFSSLPIKKMVKELENNGIPAKISNTAGAYLCNHVMYRALHEIEQQKLDIFSGFIHIPASHKLALTNNIPSFAQKDLQRAIEICIGCLD | Function: Removes 5-oxoproline from various penultimate amino acid residues except L-proline.
Catalytic Activity: Release of an N-terminal pyroglutamyl group from a polypeptide, the second amino acid generally not being Pro.
Sequence Mass (Da): 21882
Sequence Length: 199
Subcellular Location: Cytoplasm
EC: 3.4.19.3
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P42673 | MRIVLLTGFEPFDQDPVNPSWEAVRQLDGVQLGSDVKIVARRLPCAFATAGECLTRLIDELHPAMVIATGLGPGRSDISVERVAININDARIPDNLGEQPIDTAVVADGPAAFFTTLPIKAMVKAVREAGIAASVSQTAGTFVCNQVFYLLQHALAGSGVRSGFIHVPFLPEQVAGSQRPSMALDAMVAGLQAAVLTAWHTPVDVKEAGGQVS | Function: Removes 5-oxoproline from various penultimate amino acid residues except L-proline.
Catalytic Activity: Release of an N-terminal pyroglutamyl group from a polypeptide, the second amino acid generally not being Pro.
Sequence Mass (Da): 22438
Sequence Length: 213
Subcellular Location: Cytoplasm
EC: 3.4.19.3
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C3JZR3 | MRIVLLTGFEPFDQDPVNPSWEAVRQLEGVQLADDVQIIARRLPCAFATAGARLAQLIDELHPEMVIATGLGPGRSDISIERVAINVNDARIPDNLGEQPIDTAVAPDGPAAYFTTLPIKAMVRAVRGAGIAASVSQTAGTFVCNQVFYLLQHALAATAVRSGFIHVPYLPEQVTGSQRPSMALETMVAGLHAAVLAAWQTPVDAKEAGGQVS | Function: Removes 5-oxoproline from various penultimate amino acid residues except L-proline.
Catalytic Activity: Release of an N-terminal pyroglutamyl group from a polypeptide, the second amino acid generally not being Pro.
Sequence Mass (Da): 22547
Sequence Length: 213
Subcellular Location: Cytoplasm
EC: 3.4.19.3
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O73944 | MKVLVTGFEPFGGEKINPTERIAKDLDGIKIGDAQVFGRVLPVVFGKAKEVLEKTLEEIKPDIAIHVGLAPGRSAISIERIAVNAIDARIPDNEGKKIEDEPIVPGAPTAYFSTLPIKKIMKKLHERGIPAYISNSAGLYLCNYVMYLSLHHSATKGYPKMSGFIHVPYIPEQIIDKIGKGQVPPSMCYEMELEAVKVAIEVALEELL | Function: Removes 5-oxoproline from various penultimate amino acid residues except L-proline.
Catalytic Activity: Release of an N-terminal pyroglutamyl group from a polypeptide, the second amino acid generally not being Pro.
Sequence Mass (Da): 22822
Sequence Length: 208
Subcellular Location: Cytoplasm
EC: 3.4.19.3
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Q8NBP7 | MGTVSSRRSWWPLPLLLLLLLLLGPAGARAQEDEDGDYEELVLALRSEEDGLAEAPEHGTTATFHRCAKDPWRLPGTYVVVLKEETHLSQSERTARRLQAQAARRGYLTKILHVFHGLLPGFLVKMSGDLLELALKLPHVDYIEEDSSVFAQSIPWNLERITPPRYRADEYQPPDGGSLVEVYLLDTSIQSDHREIEGRVMVTDFENVPEEDGTRFHRQASKCDSHGTHLAGVVSGRDAGVAKGASMRSLRVLNCQGKGTVSGTLIGLEFIRKSQLVQPVGPLVVLLPLAGGYSRVLNAACQRLARAGVVLVTAAGNFRD... | Function: Crucial player in the regulation of plasma cholesterol homeostasis. Binds to low-density lipid receptor family members: low density lipoprotein receptor (LDLR), very low density lipoprotein receptor (VLDLR), apolipoprotein E receptor (LRP1/APOER) and apolipoprotein receptor 2 (LRP8/APOER2), and promotes their... |
Q80W65 | MGTHCSAWLRWPLLPLLPPLLLLLLLLCPTGAGAQDEDGDYEELMLALPSQEDGLADEAAHVATATFRRCSKEAWRLPGTYIVVLMEETQRLQIEQTAHRLQTRAARRGYVIKVLHIFYDLFPGFLVKMSSDLLGLALKLPHVEYIEEDSFVFAQSIPWNLERIIPAWHQTEEDRSPDGSSQVEVYLLDTSIQGAHREIEGRVTITDFNSVPEEDGTRFHRQASKCDSHGTHLAGVVSGRDAGVAKGTSLHSLRVLNCQGKGTVSGTLIGLEFIRKSQLIQPSGPLVVLLPLAGGYSRILNAACRHLARTGVVLVAAAGN... | Function: Crucial player in the regulation of plasma cholesterol homeostasis. Binds to low-density lipid receptor family members: low density lipoprotein receptor (LDLR), very low density lipoprotein receptor (VLDLR), apolipoprotein E receptor (LRP1/APOER) and apolipoprotein receptor 2 (LRP8/APOER2), and promotes their... |
A8T695 | MGTVSSRRLWWPLPLLLLLLLLGPAGARAQEDDDGDYEELVLALRSEEDGLADALQHGATATFHRCAKEPWRLPGTYVVVLKEETHRSQPERTARRLQAQAARRGYLIKLLHVFHDLLPGFLVKMSRDLLELALKLPHVDYIEEDSSVFAQSIPWNLERITPARYRADEYQPPNGGSLVEVYLLDTSIQSGHREIEGRVMVTDFGSVPEEDGTRFHRQASKCDSHGTHLAGVVSGRDAGVAKGASLRSLRVLNCQGKGTVSSTLIGLEFIRKSQLVQPVGPLVVLLPLAGGYSRVLNAACQRLARAGVVLVAAAGNFRDD... | Function: Crucial player in the regulation of plasma cholesterol homeostasis. Binds to low-density lipid receptor family members: low density lipoprotein receptor (LDLR), very low density lipoprotein receptor (VLDLR), apolipoprotein E receptor (LRP1/APOER) and apolipoprotein receptor 2 (LRP8/APOER2), and promotes their... |
O51265 | MKNINLILAWLVHIFTASGLIVGLYSIISIVNGNYSLLLKLTVIGLIIDGIDGTMARKLKVKELIPEIDGTLLDNITDYINYTFIPVIFFYLGEFIEEKYKVAICIGILLSSAYQFSRTDAKTNDNYFRGFPSLWNLFVILNIIFKMEQITNLITMSICIITSFIPIKFIYPSKTKELRKITIPITIISCLIFVVSIFSELSTTALKMAKTVLILYFAYLTLASIYLTYKTRNR | Function: Condenses choline with CDP-diglyceride to produce phosphatidylcholine and CMP.
Catalytic Activity: a CDP-1,2-diacyl-sn-glycerol + choline = a 1,2-diacyl-sn-glycero-3-phosphocholine + CMP + H(+)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 26678
Sequence Length: 234
Subcellular Location: ... |
Q89LF9 | MILWRIVRPGAAMAYVQTGLVLIAEAMDTQQDSLKPRPAMRAAAFSVHVFTAFGAAIALLAMLEAVREHWAAMFQWLGVALIIDAIDGPIARRLDVKNVQPNWSGDVLDLVVDFVTYVFVPAYAIVASGLLLPVAAPLLGVAIIVTSALYFADLRMKADDNHFRGFPALWNAAAFYLFLLHWPPLWSTLLVAALVVLTFVPFHVLHPVRVVRLRWLTMSLIGIWAVLSLYTLDMDFRVGPGVTLALCAIALWISFSDALIRFARSFA | Function: Condenses choline with CDP-diglyceride to produce phosphatidylcholine and CMP.
Catalytic Activity: a CDP-1,2-diacyl-sn-glycerol + choline = a 1,2-diacyl-sn-glycero-3-phosphocholine + CMP + H(+)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 29487
Sequence Length: 267
Subcellular Location: ... |
Q5ZV56 | MNPIKPPFTLNQYFAAWFVHVFTASAACIGVFSLYKIYQHDYVFALWLMAITVFIDAVDGSLARLVHVKSVLPKIDGALLDNIVDYLNYVITPCFFLLVKPGMLPADYVVPITAAITITSAYQFCQDDAKTPDHFFKGFPCYWNITVFYMYIFNTSMIVNTVLLSLFCVLIFIPVKYVYPSRLDYLTESRVLKILMHCCSALYGISSFCLLVNYPETNKLWVSLSLGYVGMYLFLSFYRTYYPMFKAKITANNKD | Function: Condenses choline with CDP-diglyceride to produce phosphatidylcholine and CMP. Affects virulence of this bacterium when there is a complete loss of phosphatidylcholine formation due to absence of both the synthase (pcs) and the methylation (pmtA) pathways. Reduced virulence results from lowered yields of bact... |
Q9LVZ7 | MSAAAAETDVSLRRRSNSLNGNHTNGVAIDGTLDNNNRRVGDTNTHMDISAKKTDNGYANGVGGGGWRSKASFTTWTARDIVYVVRYHWIPCMFAAGLLFFMGVEYTLQMIPARSEPFDLGFVVTRSLNRVLASSPDLNTVLAALNTVFVGMQTTYIVWTWLVEGRARATIAALFMFTCRGILGYSTQLPLPQDFLGSGVDFPVGNVSFFLFFSGHVAGSMIASLDMRRMQRLRLAMVFDILNVLQSIRLLGTRGHYTIDLAVGVGAGILFDSLAGKYEEMMSKRHLGTGFSLISKDSLVN | Function: Functions as phosphatidylcholine:diacylglycerol cholinephosphotransferase that catalyzes the transfer of the phosphocholine headgroup from phosphatidylcholine (PC) to diacylglycerol, a major reaction for the transfer of 18:1 into phosphatidylcholine for desaturation and also for the reverse transfer of 18:2 a... |
Q9LVZ6 | MSDAVTKTVAPLRRKANPINGKHTNGVTIDGIFDDHNRQIGPINSQMEDIAQKTDDGGGGEWTSKASFMTWTMHDIIYVARHHWIPCLFAAGVMFFTVVEYTFQMTPASSQPFDLGFVATRYLHSILASSPNLNTVLAALNTILVGMQTTYIGCTWAVEGRPRATIAALFMFTCRGILGYSTQLPRPQEFLGSGVDYPVGNVSFFLFYSGHVAGSMIASLDMKRMQRFRLAMVFDILNVLQSIRLLGTRGHYTIDIAVGVGAGILFDSLAGKYEEMSKRHLRNTRCSLISKDSLVT | Function: Functions as phosphatidylcholine:diacylglycerol cholinephosphotransferase that catalyzes the transfer of the phosphocholine headgroup from phosphatidylcholine (PC) to diacylglycerol, a major reaction for the transfer of 18:1 into phosphatidylcholine for desaturation and also for the reverse transfer of 18:2 a... |
Q4WXX9 | MATDIATRELRKPVDVAEYLFRRLHEVGIRSVHGVPGDYNLAALDYLPKCGLHWVGNCNELNAGYAADGYARVNGISALITTFGVGELSAINAIAGAYSEFVPIVHIVGQPHTRSQRDGMLLHHTLGNGDYNVFARMNAGVSTTVGRLNDTHEVATLIDNAIRECWIRSRPVYITLPTDMVTKKIEGERLNTPIDLSLPANDPEKEDYVVDVVLKYLHAAQRPVILVDACAIRHKVLQEVHDLMEASGLPTFVAPMGKGAVDETHKNYGGVYAGDGSNTGVREQVESSDLILSIGAIKSDFNTAGFTYRIGQLNTIDFHS... | Cofactor: Binds 1 Mg(2+) per subunit.
Catalytic Activity: a 2-oxocarboxylate + H(+) = an aldehyde + CO2
Sequence Mass (Da): 62999
Sequence Length: 569
EC: 4.1.1.1
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Q2UKV4 | MATDIATRDLRKPIDVAEYLFRRLREVGVRAVHGVPGDYNLVALDYLPKCDLHWVGNCNELNAGYAADGYARINGMSALVTTFGVGELSALNAIAGAYSEFVPIVHIVGQPHTKSQKDGMLLHHTLGNGDFNVFTRMSADISCTLGCLNSTHEVATLIDNAIRECWIRSRPVYISLPTDMVTKKIEGERLDTPLDLSLPPNDPEKEDYVVDVVLKYLHAAKKPVILVDACAIRHRVLDEVHEFVEKSGLPTFVAPMGKGAVDETHKNYGGVYAGTGSNPGVREQVESSDLILSIGAIKSDFNTTGFSYRIGQLNTIDFHS... | Cofactor: Binds 1 Mg(2+) per subunit.
Catalytic Activity: a 2-oxocarboxylate + H(+) = an aldehyde + CO2
Sequence Mass (Da): 62927
Sequence Length: 570
EC: 4.1.1.1
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P51844 | MEGETLPLAQYLFKRLLQLGVDSIFGVPGDYNLTLLDHVVPSGLKWVGNCNELNAGYAADGYSRIKDIGAVVTTFGVGELSAINAIAGAYAEKAPVVHIVGTPMRASQESRALIHHTFNDGDYQRFDAIQEHVTVAQVSLSDHRTAPSEIDRILLQCLLHSRPVRIAIPVDMVPVLVPVAGLSSKIQIPPAVRQPQAEEAALNAVLKRIYSSKKPMILVDGETRSFGMLQRVNHFIQTIGWPTFTSGFGKGLVDETLPNVYGVCTLHQKAFVDSCDLVLVFGPHFSNTNSYNYFLKPADEKSVLFSPNSIQVNKDVFRDL... | Cofactor: Binds 1 metal ion per subunit.
Catalytic Activity: a 2-oxocarboxylate + H(+) = an aldehyde + CO2
Sequence Mass (Da): 64071
Sequence Length: 577
EC: 4.1.1.1
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P87208 | MADIATRELRQPIDIAEYLFRRLHEVGIRSVHGVPGDYNLAALDYLPKCGLHWVGNCNELNAGYAADGYARVNGIAALVTTFGVGELSAINAIAGAYSEFVPIIHIVGQPHSRSQKDGLLLHHTLGNGDYNVFSSMNKGISVTTANLNDTYDAATLIDNAIRECWIHSRPVYLALPTDMITKKIEGERLKTPIDLSLPANDPEKEDYVVDVVLKYLHAAKNPVILVDACAIRHRVLEEVHDLIEVSGLPTFVAPMGKGAVNETHRCYGGVYAGTGSNPGVREQVESSDLILSIGAIKSDFNTAGFSYRIGQLNTIDFHST... | Cofactor: Binds 1 Mg(2+) per subunit.
Catalytic Activity: a 2-oxocarboxylate + H(+) = an aldehyde + CO2
Sequence Mass (Da): 62599
Sequence Length: 568
EC: 4.1.1.1
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P33287 | MVAQQQGKFTVGDYLAERLAQVGVRHHFVVPGDYNLILLDKLQAHPDLKEVGCANELNCSLAAEGYARANGISACVVTYSVGALSAFNGTGSAYAENLPLVLISGSPNTNDPSQYHILHHTLGHPDYTYQYEMAKKITCCAVAIPRAIDAPRLIDRALRAAILARKPCYIEIPTNLAGATCVRPGPISAITDPITSDKSALEAAAKCAAEYLDGKLKPVILVGPKAGRAGSEKELIEFAEAMGCAVALQPAAKGMFPEDHKQFVGIFWGQVSSDAADAMVHWADAMICVGAVFNDYSTVGWTAVPNIPLMTVDMDHVTFP... | Cofactor: Binds 1 metal ion per subunit.
Catalytic Activity: a 2-oxocarboxylate + H(+) = an aldehyde + CO2
Sequence Mass (Da): 62263
Sequence Length: 570
Pathway: Carbohydrate metabolism; pyruvate metabolism.
Subcellular Location: Cytoplasm
EC: 4.1.1.1
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P06672 | MSYTVGTYLAERLVQIGLKHHFAVAGDYNLVLLDNLLLNKNMEQVYCCNELNCGFSAEGYARAKGAAAAVVTYSVGALSAFDAIGGAYAENLPVILISGAPNNNDHAAGHVLHHALGKTDYHYQLEMAKNITAAAEAIYTPEEAPAKIDHVIKTALREKKPVYLEIACNIASMPCAAPGPASALFNDEASDEASLNAAVEETLKFIANRDKVAVLVGSKLRAAGAEEAAVKFADALGGAVATMAAAKSFFPEENPHYIGTSWGEVSYPGVEKTMKEADAVIALAPVFNDYSTTGWTDIPDPKKLVLAEPRSVVVNGIRFP... | Cofactor: Binds 1 Mg(2+) per subunit.
Catalytic Activity: a 2-oxocarboxylate + H(+) = an aldehyde + CO2
Sequence Mass (Da): 60926
Sequence Length: 568
EC: 4.1.1.1
|
Q9Y233 | MRIEERKSQHLTGLTDEKVKAYLSLHPQVLDEFVSESVSAETVEKWLKRKNNKSEDESAPKEVSRYQDTNMQGVVYELNSYIEQRLDTGGDNQLLLYELSSIIKIATKADGFALYFLGECNNSLCIFTPPGIKEGKPRLIPAGPITQGTTVSAYVAKSRKTLLVEDILGDERFPRGTGLESGTRIQSVLCLPIVTAIGDLIGILELYRHWGKEAFCLSHQEVATANLAWASVAIHQVQVCRGLAKQTELNDFLLDVSKTYFDNIVAIDSLLEHIMIYAKNLVNADRCALFQVDHKNKELYSDLFDIGEEKEGKPVFKKTK... | Cofactor: Binds 2 divalent metal cations per subunit. Site 1 may preferentially bind zinc ions, while site 2 has a preference for magnesium and/or manganese ions.
Function: Plays a role in signal transduction by regulating the intracellular concentration of cyclic nucleotides . Can hydrolyze both cAMP and cGMP, but has... |
Q8CA95 | MSNDSTEGTVGSCNATGLTDEKVKAYLSLHPQVLDEFVSESVSAETVEKWLKRKTNKAKDEPSPKEVSRYQDTNMQGVVYELNSYIEQRLDTGGDNHLLLYELSSIIRIATKADGFALYFLGECNNSLCVFIPPGMKEGQPRLIPAGPITQGTTISAYVAKSRKTLLVEDILGDERFPRGTGLESGTRIQSVLCLPIVTAIGDLIGILELYRHWGKEAFCLSHQEVATANLAWASVAIHQVQVCRGLAKQTELNDFLLDVSKTYFDNIVAIDSLLEHIMIYAKNLVNADRCALFQVDHKNKELYSDLFDIGEEKEGKPIF... | Cofactor: Binds 2 divalent metal cations per subunit. Site 1 may preferentially bind zinc ions, while site 2 has a preference for magnesium and/or manganese ions.
Function: Plays a role in signal transduction by regulating the intracellular concentration of cyclic nucleotides . Can hydrolyze both cAMP and cGMP, but has... |
Q9HCR9 | MAASRLDFGEVETFLDRHPELFEDYLMRKGKQEMVEKWLQRHSQGQGALGPRPSLAGTSSLAHSTCRGGSSVGGGTGPNGSAHSQPLPGGGDCGGVPLSPSWAGGSRGDGNLQRRASQKELRKSFARSKAIHVNRTYDEQVTSRAQEPLSSVRRRALLRKASSLPPTTAHILSALLESRVNLPRYPPTAIDYKCHLKKHNERQFFLELVKDISNDLDLTSLSYKILIFVCLMVDADRCSLFLVEGAAAGKKTLVSKFFDVHAGTPLLPCSSTENSNEVQVPWGKGIIGYVGEHGETVNIPDAYQDRRFNDEIDKLTGYKT... | Cofactor: Binds 2 divalent metal cations per subunit. Site 1 may preferentially bind zinc ions, while site 2 has a preference for magnesium and/or manganese ions.
Function: Plays a role in signal transduction by regulating the intracellular concentration of cyclic nucleotides cAMP and cGMP . Catalyzes the hydrolysis of... |
Q9EQT1 | MHRLILVSILVCANFCCYRDTFATPQSASIKALRNANLRRDESNHLTDLYRRDENIRVTGTGHVQSPRFPNSYPRNLLLTWRLHSQEKTRIQLAFDHQFGLEEAENDICRYDFVEVEDVSESSTVVRGRWCGHKEIPPRITSRTNQIKITFQSDDYFVAKPGFKIYYSFVEDFQPEAASEINWESVTSSFSGVSYHSPSVMDSTLTADALDKAIAEFDTVEDLLKYFNPASWQDDLENLYMDTPRYRGRSYHERKSKVDLDRLNDDVKRYSCTPRNHSVNLREELKLTNAVFFPRCLLVQRCGGNCGCGTLNWKSCTCSS... | Function: Growth factor that plays an essential role in the regulation of embryonic development, cell proliferation, cell migration, survival and chemotaxis. Potent mitogen for cells of mesenchymal origin. Plays an important role in wound healing. Induces macrophage recruitment, increased interstitial pressure, and blo... |
V5NC32 | MFPRVVRLNSRLVSFALLGLQIANGAITYQHPDDLPSNVNYDFIVAGGGTAGLVVASRLSENSDWNILVIEAGPSNKDTPETRVPGLADSLPGSRTDWNYTTIPQDALGGRSLNYSRAKVLGGCSTHNGMVYTRGSEDDWNYWAEVTGDQALSWDSVLPIMKKAEKFSQDFSDQSVDGHIDPAVHGRDGLLSVVASYTNVSFNDLLLQTTKELSDEFPFKLDLNDGKPHELAWTQYTIDHNAERSSSATSYLETTGDNVHVLVNTHVTRIVSAGNGTNFRSVEFAVDSNSPKKVLQAKKELILSAGVIASPQVLMNSGIG... | Cofactor: Binds 1 FAD covalently per subunit.
Function: Catalyzes the single-oxidation or sequential double oxidation reaction of carbohydrates primarily at carbon-2 and/or carbon-3 with the concomitant reduction of the flavin. The enzyme exhibits a broad sugar substrate specificity, oxidizing different aldopyranoses t... |
Q3L245 | MLPRVTKLNSRLLSLALLGIQIARGAITYQHPDDLPSGVDYDFIVAGGGTAGLVVASRLSENSNWKVLVIEAGPSNKDAFVTRVPGLASTLGAGSPIDWNYTTIPQDGLDGRSLDYPRAKILGGCSTHNGMVYTRGSKDDWNSWAGIIGDQGLGWDSILPAIKKAEKFTQDFTDQSVKGHIDPSVHGFDGKLSVSAAYSNISFNDLLFETTKELNAEFPFKLDMNDGKPIGLGWTQYTIDNHAERSSSATSYLESTGDNVHVLVNTLVTRVLSASGNGTDFRKVEFAVDANSPKKQLEAKKEVIVAGGVIASPQILMNSG... | Cofactor: Binds 1 FAD covalently per subunit.
Function: Catalyzes the single-oxidation or sequential double oxidation reaction of carbohydrates primarily at carbon-2 and/or carbon-3 with the concomitant reduction of the flavin. The enzyme exhibits a broad sugar substrate specificity, oxidizing different aldopyranoses t... |
Q02332 | MRFSRKLLGPFVGSLAKKLDYYSQFQPSSLTIQQYLDFGRIGTSANSYTFLKNELLVRLANIMQEFTLLPPKLLQMPSSKMVSNWYAESFEDLLLFEASDSSPEQVARFNDQLTVVLKRHAHVVETMAEGLIELRESDGVDIASEKGIQYFLDRFYINRISIRMLQNQHLVVFGNVLPESPRHVGCIDPACDVESVVYDAFENARFLCDRYYLTSPSMKLEMHNAVEKGKPISIVAVPSHLYHMMFELFKNAMRATVEYHGVDDDLPDIKVYVVKGQEDLSIKICDRGGGVSRTILERLYNYMYSTAPPPPRDGTQAPLA... | Function: Inhibits the mitochondrial pyruvate dehydrogenase complex by phosphorylation of the E1 alpha subunit, thus contributing to the regulation of glucose metabolism (By similarity). Required for normal lifespan .
Catalytic Activity: ATP + L-seryl-[pyruvate dehydrogenase E1 alpha subunit] = ADP + H(+) + O-phospho-L... |
Q11067 | MALIKLLLASLAITSVCGMYSKKDDVVELTEANFQSKVINSDDIWIVEFYAPWCGHCKSLVPEYKKAASALKGVAKVGAVDMTQHQSVGGPYNVQGFPTLKIFGADKKKPTDYNGQRTAQAIADSVLAEAKKAVSARLGGKSSGSSSSGSGSGSGKRGGGGSGNEVVELTDANFEDLVLNSKDIWLVEFFAPWCGHCKSLEPQWKAAASELKGKVRLGALDATVHTVVANKFAIRGFPTIKYFAPGSDVSDAQDYDGGRQSSDIVAWASARAQENMPAPEVFEGINQQVVEDACKEKQLCIFAFLPHILDCQSECRNNYL... | Function: May function as a chaperone that inhibits aggregation of misfolded proteins (By similarity). May negatively regulate the unfolded protein response (UPR) through binding to UPR sensors .
Catalytic Activity: Catalyzes the rearrangement of -S-S- bonds in proteins.
Sequence Mass (Da): 47728
Sequence Length: 440
S... |
Q9V438 | MRQLASILLLAFVVGSVSAFYSPSDGVVELTPSNFDREVLKDDAIWVVEFYAPWCGHCQSLVPEYKKLAKALKGVVKVGSVNADADSTLSGQFGVRGFPTIKIFGANKKSPTDYNGQRTAKAIAEAALAEVKKKVQGVLGGGGGSSSGGSGSSSGDDVIELTEDNFDKLVLNSDDIWLVEFFAPWCGHCKNLAPEWAKAAKELKGKVKLGALDATAHQSKAAEYNVRGYPTIKFFPAGSKRASDAQEYDGGRTASDIVSWASDKHVANVPAPELIEIINESTFETACEGKPLCVVSVLPHILDCDAKCRNKFLDTLRTLG... | Function: Binds to both apoptotic cells and phagocytes and promotes Drpr-dependent phagocytosis of apoptotic cells.
Catalytic Activity: Catalyzes the rearrangement of -S-S- bonds in proteins.
Sequence Mass (Da): 46752
Sequence Length: 433
Subcellular Location: Endoplasmic reticulum lumen
EC: 5.3.4.1
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Q15084 | MALLVLGLVSCTFFLAVNGLYSSSDDVIELTPSNFNREVIQSDSLWLVEFYAPWCGHCQRLTPEWKKAATALKDVVKVGAVDADKHHSLGGQYGVQGFPTIKIFGSNKNRPEDYQGGRTGEAIVDAALSALRQLVKDRLGGRSGGYSSGKQGRSDSSSKKDVIELTDDSFDKNVLDSEDVWMVEFYAPWCGHCKNLEPEWAAAASEVKEQTKGKVKLAAVDATVNQVLASRYGIRGFPTIKIFQKGESPVDYDGGRTRSDIVSRALDLFSDNAPPPELLEIINEDIAKRTCEEHQLCVVAVLPHILDTGAAGRNSYLEVL... | Function: May function as a chaperone that inhibits aggregation of misfolded proteins . Negatively regulates the unfolded protein response (UPR) through binding to UPR sensors such as ERN1, which in turn inactivates ERN1 signaling . May also regulate the UPR via the EIF2AK3 UPR sensor . Plays a role in platelet aggrega... |
Q8N807 | MDLLWMPLLLVAACVSAVHSSPEVNAGVSSIHITKPVHILEERSLLVLTPAGLTQMLNQTRFLMVLFHNPSSKQSRNLAEELGKAVEIMGKGKNGIGFGKVDITIEKELQQEFGITKAPELKLFFEGNRSEPISCKGVVESAALVVWLRRQISQKAFLFNSSEQVAEFVISRPLVIVGFFQDLEEEVAELFYDVIKDFPELTFGVITIGNVIGRFHVTLDSVLVFKKGKIVNRQKLINDSTNKQELNRVIKQHLTDFVIEYNTENKDLISELHIMSHMLLFVSKSSESYGIIIQHYKLASKEFQNKILFILVDADEPRNG... | Function: Probable redox-inactive chaperone involved in spermatogenesis.
PTM: N-glycosylated.
Sequence Mass (Da): 66657
Sequence Length: 584
Domain: The thioredoxin domain lacks the conserved redox-active Cys at position 417 which is replaced by a Ser residue, suggesting that it lacks thioredoxin activity.
Subcellular ... |
Q9DAN1 | MELLWTPLLLVAACLSEVLGSPEIDTGINISQPLHILEDHNLMVLTPAGLTQTLNETRFLMVIFHNPSLKQSRKLAKELGKAAEIFGKGKNGLGFGKVDITKETELQQEFDITHAPELKLFFEGNRLKPISCKDVVESTALVVWLRRQISKKALLFNNSDEVADFVKSRPLVIVGFFQDLEEEVAELFYDTIKDFPELTFGAIQIKNSFGRFHVILDSVLVFKKGKIVKRQELINDSTNKDHLNQVIKQQLTGFVIELNPENKDLIYELNILNHMLLFISKSSEPYSTISRHYRQIAKEFQNKILFVLVNADEPKNKRIF... | Function: Probable redox-inactive chaperone involved in spermatogenesis.
PTM: N-glycosylated.
Sequence Mass (Da): 67759
Sequence Length: 588
Domain: The thioredoxin domain lacks the conserved redox-active Cys at position 414 which is replaced by a Ser residue, suggesting that it lacks thioredoxin activity.
Subcellular ... |
Q9BY77 | MADISLDELIRKRGAAAKGRLNARPGVGGVRSRVGIQQGLLSQSTRTATFQQRFDARQKIGLSDARLKLGVKDAREKLLQKDARFRIKGKVQDAREMLNSRKQQTTVPQKPRQVADAREKISLKRSSPAAFINPPIGTVTPALKLTKTIQVPQQKAMAPLHPHPAGMRINVVNNHQAKQNLYDLDEDDDGIASVPTKQMKFAASGGFLHHMAGLSSSKLSMSKALPLTKVVQNDAYTAPALPSSIRTKALTNMSRTLVNKEEPPKELPAAEPVLSPLEGTKMTVNNLHPRVTEEDIVELFCVCGALKRARLVHPGVAEVV... | Function: Is involved in regulation of translation. Is preferentially associated with CBC-bound spliced mRNA-protein complexes during the pioneer round of mRNA translation. Contributes to enhanced translational efficiency of spliced over nonspliced mRNAs. Recruits activated ribosomal protein S6 kinase beta-1 I/RPS6KB1 ... |
Q00002 | ARDMTKQALPAVSEVTKDTLEEFKTADKVVLVAYFAADDKASNETFTSVANGLRDNFLFGATNDAALAKAEGVKQPGLVCTSPSTTARTSSPRPSMRTYPRLRKVASTPLIGEVGPETYAGYMAAGIPLAYIFAETPEEREEFAKELKPLALKHKGEINFATIDAKSFGQHAGNLNLKVGTWPAFAIQRTEKNEKFPTNQEAKITEKEIGKFVDDFLAGKIDPSIKSEPIPESNDGPVTVVVAHNYKDVVIDNDKDVLVEFYAPWCGHCKALAPKYEELGQLYASDELSKLVTIAKVDATLNDVPDEIQGFLPSSLFPLA... | Function: Participates in the folding of proteins containing disulfide bonds, may be involved in glycosylation, prolyl hydroxylation and triglyceride transfer.
Catalytic Activity: Catalyzes the rearrangement of -S-S- bonds in proteins.
Sequence Mass (Da): 46275
Sequence Length: 436
Subcellular Location: Endoplasmic ret... |
D4B2L8 | MPGVRSLLLALAGVSLAPAVLAADASTDSSDVHALKTDTFKDFIKEHDLVLAEFYAPWCGHCKALAPEYEKAATELKSKNIQLAKVDCTEEADLCQEYGVEGYPTLKVFRGLDSHKPYNGARKSPAITSYMIKQSLPSVSVVTAENFEEVKSLDKVVVVAFIGEDDKETNKTYTALADSMRDDVLFAGTSSAELAKKEGVSLPAVVLYKEFDDRKDVYDGKFEAEALKAFIKSSSTPLVGEVGPETYSGYMSAGIPLAYIFADTAEEREQYASDFKDLAKKLKGKINFATIDSKAFGAHAANLNLIPEKFPAFAIQDTVS... | Function: Participates in the folding of proteins containing disulfide bonds, may be involved in glycosylation, prolyl hydroxylation and triglyceride transfer.
Catalytic Activity: Catalyzes the rearrangement of -S-S- bonds in proteins.
Sequence Mass (Da): 57255
Sequence Length: 523
Subcellular Location: Endoplasmic ret... |
P54470 | MNNRIIYVVSDSVGETAELVVKAALSQFNGSADDTHVRRIPYVEDIGTINEVISLAKADGGIICFTLVVPEIREYLIAEAEKANVLYYDIIGPLIDKMETAYGLTAKYEPGRVRQLDEDYFKKVEAIEFAVKYDDGRDPRGILKADIVLIGVSRTSKTPLSQYLAHKRLKVANVPIVPEVDPPEELFNVDPKKCIGLKISPDKLNHIRKERLKSLGLNDKAIYANINRIKEELEYFEKIVDRIGCQVVDVSNKAVEETANIIHHLKTKNI | Function: Bifunctional serine/threonine kinase and phosphorylase involved in the regulation of the pyruvate, phosphate dikinase (PPDK) by catalyzing its phosphorylation/dephosphorylation.
Catalytic Activity: ADP + N(tele)-phospho-L-histidyl/L-threonyl-[pyruvate, phosphate dikinase] = AMP + H(+) + N(tele)-phospho-L-hist... |
Q9XDN5 | MDKELLQSTVRKVLDEMRQRPIPLGVSNRHIHLSAQDYERLFPGHPISEKKALLQPGQYAAEQTVTLVGPKGQLKNVRLLGPLRSVSQVEISRTDARTLGIAAPLRMSGNLKGTPGIRLVSPFAELELPSGVIVAQRHIHMSPLDALILRVSHGDMVSVAIEGDDRGLIFNNVAIRVSPDMRLEMHIDTDEANAAGADNPHAFARLVGPR | Cofactor: There are 2 Zn(2+) ions per monomer; Zn(2+) and CoA bind inbetween the 2 domains in each monomer.
Function: Involved in 1,2-propanediol (1,2-PD) utilization in the bacterial microcompartment (BMC) dedicated to 1,2-PD degradation by catalyzing the conversion of propanoyl-CoA to propanoyl-phosphate. Also able t... |
Q9WYK8 | MITDGIMHKVREVYQLLRKEPGIIVGVSNRHVHLSREDLETLFGEGYELTPVKELRQPGQYAAKETVTIVGPKGAIENVRVLGPVRKETQVEISRTDAFRLGVRPPVRDSGDLEGTPGIVIIGPNGILVKEKGVIIAKRHIHMHPKDAEYYGVKDKDIVKVIVESGDRRLIFDDVLIRVREDFALEFHVDTDEANAAMLNTGDLVYIVEF | Cofactor: There are 2 Zn(2+) ions per monomer; Zn(2+) and CoA bind inbetween the 2 domains in each monomer.
Function: Involved in 1,2-propanediol (1,2-PD) degradation by catalyzing the conversion of propanoyl-CoA to propanoyl-phosphate.
Catalytic Activity: phosphate + propanoyl-CoA = CoA + propanoyl phosphate
Sequence ... |
Q9XDN4 | MNGETLQRIVEEIVSRLHRRAQSTATLSVTQLRDADCPALFCQHASLRILLIDLPLLGQLADAETGDAAARKIHDALAFGIRVQLSLHSQLLPVIPVKKLARLPLVFTDEHGLPLVLHAGSVLSYRDVALLSRGRVVVHRKCIVTAMARDAANARNIQLIKQE | Function: Plays an essential role in assembly and/or stability of the bacterial microcompartment (BMC) dedicated to 1,2-propanediol (1,2-PD) degradation. Overexpression impairs BMC formation.
Sequence Mass (Da): 17914
Sequence Length: 163
Pathway: Polyol metabolism; 1,2-propanediol degradation.
Subcellular Location: Ba... |
Q9XDN3 | MHLARVTGAVVSTQKSPSLIGKKLLLVRRVSADGELPASPTSGDEVAVDSVGAGVGELVLLSGGSSARHVFSGPNEAIDLAVVGIVDTLSC | Function: Probably forms vertices in the shell of the bacterial microcompartment (BMC) dedicated to 1,2-propanediol (1,2-PD) degradation. Required for structural integrity of BMCs and to mitigate propionaldehyde toxicity.
Sequence Mass (Da): 9094
Sequence Length: 91
Pathway: Polyol metabolism; 1,2-propanediol degradati... |
O34899 | MKLYTKTGDKGQTGLVGGRTDKDSLRVESYGTIDELNSFIGLALAELSGQPGFEDLTAELLTIQHELFDCGGDLAIVTERKDYKLTEESVSFLETRIDAYTAEAPELKKFILPGGSKCASLLHIARTITRRAERRVVALMKSEEIHETVLRYLNRLSDYFFAAARVVNARSGIGDVEYERSAIVFRDRNSSES | Catalytic Activity: 2 ATP + 2 cob(II)yrinate a,c diamide + reduced [electron-transfer flavoprotein] = 2 adenosylcob(III)yrinate a,c-diamide + 3 H(+) + oxidized [electron-transfer flavoprotein] + 2 triphosphate
Sequence Mass (Da): 21504
Sequence Length: 193
Pathway: Cofactor biosynthesis; adenosylcobalamin biosynthesis;... |
B1VB74 | MAIYTRTGDAGTTALFTGQRVSKTHPRVEAYGTLDELNAALSLCVCAAKNPQHRQLLENIQLQLFWFSAELASESEQPAPEQRYISSEEIAALEAAIDTAMGRVPPLRSFILPGRSEAASRLHFARTLARRAERRLVELSTEISVRHVLMRYINRLSDCLYALARAEDHDAHQNNIIQKVAERYLAAIRTSATREPAMSLSFQELHQLTRAAVMRAEELQVPVVISIVDANGTQTVTWRMPDALLVSSELAPKKAWTAVAMKTATHELTSAVQPGAALYGLESHMQGKVVTFGGGYALWREGLLLGGLGISGGSVEQDMD... | Function: Converts cob(I)alamin to adenosylcobalamin (adenosylcob(III)alamin), the cofactor for propanediol dehydratase. Found in the bacterial microcompartment (BMC) dedicated to 1,2-propanediol (1,2-PD) degradation. PduS and PduO allow regeneration of the adenosylcobalamin cofactor within the BMC.
Catalytic Activity:... |
P53523 | MAIHLTRIYTRTGDNGTTGLSDFSRVAKTDLRLVAYADCDETNSAIGVALALGNPDQKITDVLQQIQNDLFDAGADLSTPMQDSVRNPEYPQLRITQTHIDRLEEWCDTYNTPLPTLNSFVLPGGSPLSALLHVARTVARRAERSAWAAVEAHPGVVSMLPAKYLNRLSDLLFILSRVANTGNDVLWRPGG | Catalytic Activity: 2 ATP + 2 cob(II)yrinate a,c diamide + reduced [electron-transfer flavoprotein] = 2 adenosylcob(III)yrinate a,c-diamide + 3 H(+) + oxidized [electron-transfer flavoprotein] + 2 triphosphate
Sequence Mass (Da): 20916
Sequence Length: 191
Pathway: Cofactor biosynthesis; adenosylcobalamin biosynthesis;... |
Q8ZNR5 | MAIYTRTGDAGTTSLFTGQRVSKTHPRVEAYGTLDELNAALSLCACAAADENHRTLLEAIQQQLFWFSAELASDSEQPSPKQRYISSEEISALEAAIDRAMARVEPLHSFILPGRCEAASRLHFARTLARRAERRLVELATEVNVRQVLMRYINRLSDCLYALARAEDSDAHQANIIREVSKRYLAACQPPHSKETTPVALSFHDLHQLTRAAVERAQQLQVPVVVSIVDAHGTETVTWRMPDALLVSSELAPKKAWTAVAMKTATHELSDVVQPGAALYGLESHLQGKVVTFGGGYALWRDGILIGGLGISGGSVEQDM... | Cofactor: Stoichiometry of heme binding is 2 PduOC:1 heme; the binding pocket is formed by a PduOC dimer. Full-length PduO also binds heme.
Function: Converts cob(I)alamin to adenosylcobalamin (adenosylcob(III)alamin), the cofactor for propanediol dehydratase. Found in the bacterial microcompartment (BMC) dedicated to ... |
Q9XDN1 | MNTSELETLIRTILSEQLTTPAQTPVQPQGKGIFQSVSEAIDAAHQAFLRYQQCPLKTRSAIISAMRQELTPLLAPLAEESANETGMGNKEDKFLKNKAALDNTPGVEDLTTTALTGDGGMVLFEYSPFGVIGSVAPSTNPTETIINNSISMLAAGNSIYFSPHPGAKKVSLKLISLIEEIAFRCCGIRNLVVTVAEPTFEATQQMMAHPRIAVLAITGGPGIVAMGMKSGKKVIGAGAGNPPCIVDETADLVKAAEDIINGASFDYNLPCIAEKSLIVVESVAERLVQQMQTFGALLLSPADTDKLRAVCLPEGQANKK... | Function: A CoA-acylating aldehyde dehydrogenase required for optimal 1,2-propanediol (1,2-PD) degradation . Optimizes growth in the bacterial microcompartment (BMC) dedicated to 1,2-PD degradation by minimizing propionaldehyde toxicity (Probable). Directly targeted to the BMC . NAD(+) and NADH are regenerated internal... |
Q9XDN0 | MNTFSLQTRLYSGQGSLAVLKRFTNKHIWIICDGFLAHSPLLDTLRNALPADNRISVFSEITPDPTIHTVVQGIAQMQALQPQVVIGFGGGSAMDAAKAIVWFSQQSGINIETCVAIPTTSGTGSEVTSACVISDPDKGIKYPLFNNALYPDMAILDPELVVSVPPQITANTGMDVLTHALEAWVSPRASDFTDALAEKAAKLVFQYLPTAVEKGDCVATRGKMHNASTLAGMAFSQAGLGLNHAIAHQLGGQFHLPHGLANALLLTTVIRFNAGVPRAAKRYARLAKACGFCPAEANDIAAINALIQQIELLKQRCVLP... | Function: An iron-dependent alcohol dehydrogenase required for optimal 1,2-propanediol (1,2-PD) degradation. NAD(+) and NADH are regenerated internally within the bacterial microcompartment (BMC) dedicated to 1,2-PD degradation by the PduP and PduQ enzymes, which reduce NAD(+) and oxidize NADH respectively, although th... |
B1ZAJ4 | MASDDRPLALTLGDPSGIGPEIALAAWRLRGERGVPPFQLIGDPEFLEATAYRLGLSVPVAEVEPDDAVEVFARALPVLPLPSGAKVSATPGAPDSANAGAIVESITAAVDLVRSGAASAVVTNPIAKFVLTRVGFAHPGHTEFLAALAAREGREPPLPVMMLWSELLAVVPVTIHVALRRVPDLLTQELVERTARIVHADLRARFGLEAPRLVLSGLNPHAGESGTMGTEDRDVLAPAVAALRAEGIDIRGPLPADTLFHERARATYDVALAPTHDQALIPIKTLAFDEGVNVTLGLPFVRTSPDHGTAFDIAGKGVAK... | Cofactor: Binds 1 divalent metal cation per subunit. Can use ions such as Zn(2+), Mg(2+) or Co(2+).
Function: Catalyzes the NAD(P)-dependent oxidation of 4-(phosphooxy)-L-threonine (HTP) into 2-amino-3-oxo-4-(phosphooxy)butyric acid which spontaneously decarboxylates to form 3-amino-2-oxopropyl phosphate (AHAP).
Cataly... |
Q9K1F9 | MKQPVFAVTSGEPAGIGPDICLDLAFARLPCRCAVLGDKNLLRARAEALGKSVVLRDFDPESGGAAYGELEVLHIPAVEAVEAGKLNPANAAYVLQLLDTALAGISDGIFDGIVTAPLHKGIINDARASTGFFSGHTEYLAEKSGTGQVVMMLAGKGLRVALVTTHLPLKDVAAAITQPLIESVARILHHDLKHKFGIKNPKILVAGLNPHAGEGGHLGHEETDTIIPALENLRREGINLAGPYPADTLFQPFMLEGADAVLAMYHDQGLPVLKYHSFGQGVNITLGLPFIRTSVDHGTALDLAATGRADSGSLITAVET... | Cofactor: Binds 1 divalent metal cation per subunit. Can use ions such as Zn(2+), Mg(2+) or Co(2+).
Function: Catalyzes the NAD(P)-dependent oxidation of 4-(phosphooxy)-L-threonine (HTP) into 2-amino-3-oxo-4-(phosphooxy)butyric acid which spontaneously decarboxylates to form 3-amino-2-oxopropyl phosphate (AHAP).
Cataly... |
P58711 | MYQLNQNQTVNTPQKYRPRLALTVGDPGGIGAEVILKALADLEIGHNYDLTVVSNKNLLQETYKQLSSMENLLPLADPNLLKIIDVTVDRETARQINLGTGNAASGAASFAYMDYAIAQTLAGNFDGIVTGPIAKSAWKAAGYNYPGQTELLAQKSGVERFGMLFVARSPYTGWTLRALLATTHIPLRQVADTLTPQLLTQKLDLLVECLEKDFGITSGRIAIAGLNPHSGEQGQLGTEELDWLIPWLESERQKRPHFQLDGPIPPDTMWVKPGQAWYGNAIVQHPADAYLALYHDQGLIPVKLMAFDRAVNTSIGLPFV... | Cofactor: Binds 1 divalent metal cation per subunit.
Function: Catalyzes the NAD(P)-dependent oxidation of 4-(phosphooxy)-L-threonine (HTP) into 2-amino-3-oxo-4-(phosphooxy)butyric acid which spontaneously decarboxylates to form 3-amino-2-oxopropyl phosphate (AHAP).
Catalytic Activity: 4-(phosphooxy)-L-threonine + NAD(... |
A1B0G5 | MTEARPIILTCGEPAGVGPELAPKALASGVPFVFLGDPRHLPEGTAWAEVTAPGEPVADGVLAVLRHDFPAPARPGQPDPANAPAVIEVIARAVDLAMSGAAGGICTLPINKEALKRGAGFGFPGHTEYLAHLAGDVPVVMMLASTTVQPPCRVVPVTIHIPLSEVPLALTPLRLEQAIRITDAAMRRDFGLAQPRLAIAGLNPHAGENGVMGDEEARWMAPLIERLRREGFDLRGPLPADTMFHPAARARYDAALCAYHDQALIPIKTLDFAGGVNITLGLPFVRTSPDHGTAFDIAGQGIADAESVIAALRMAHEMAA... | Cofactor: Binds 1 divalent metal cation per subunit. Can use ions such as Zn(2+), Mg(2+) or Co(2+).
Function: Catalyzes the NAD(P)-dependent oxidation of 4-(phosphooxy)-L-threonine (HTP) into 2-amino-3-oxo-4-(phosphooxy)butyric acid which spontaneously decarboxylates to form 3-amino-2-oxopropyl phosphate (AHAP).
Cataly... |
C0QTA7 | MKKIGITLGDPSGISPEILIKSIDKLKKAIYVIYGSYKIIEKVSSILDKKTEINIIDSPEEAEKEGVYLINVYDRDFCVGKPDKETGKASVLFLERAVKDILSKKLDAIVTLPISKEYVMKAGFRYAGHTDYLADITKTEDYLMMLLCEKMKVALVTTHIPLKDVPENIKPEILESKIRLLNRELQSKFGIKKPKIAVLGLNPHAGDGGNIGREEIDIINPVVQKLKSEGIDLEGSLSADTAFNRYREFDAYLAMYHDQGLIPLKLLCFKKAVNITLGIPFIRTSPDHGTGFDIAGKGIADPSSFIEAVKLALKLSKQY | Cofactor: Binds 1 divalent metal cation per subunit.
Function: Catalyzes the NAD(P)-dependent oxidation of 4-(phosphooxy)-L-threonine (HTP) into 2-amino-3-oxo-4-(phosphooxy)butyric acid which spontaneously decarboxylates to form 3-amino-2-oxopropyl phosphate (AHAP).
Catalytic Activity: 4-(phosphooxy)-L-threonine + NAD(... |
B4S6L0 | MKTTAWTIGDIHGIGPEIILKTFDESLRSTGQPEEKPIVIGSAEALLYYSKRLGLSIDIRTIDAPEKAAAYPQGVLPVISVGEPSSPLQPGTISAEAGRLSMLAIEKAANLCLEGRCAAMVTAPIHKEAVARAGYPHTGHTDFLADLCATDNPTMLFRDPVSGLMVALATIHVALHRVPELIRSMDMSAFFSNLNRSLQSDFRIEQPRIAVLGLNPHASDGGVMGREEKEIILPCIDALADRQNIEGPFAADGFFGSGKYRNYDVTVAMYHDQGLLPFKVLAFDTGINVTLGLPLVRTSPDHGTSFDIAGQGRASHRSFS... | Cofactor: Binds 1 divalent metal cation per subunit.
Function: Catalyzes the NAD(P)-dependent oxidation of 4-(phosphooxy)-L-threonine (HTP) into 2-amino-3-oxo-4-(phosphooxy)butyric acid which spontaneously decarboxylates to form 3-amino-2-oxopropyl phosphate (AHAP).
Catalytic Activity: 4-(phosphooxy)-L-threonine + NAD(... |
Q9I5U4 | MSLRFALTPGEPAGIGPDLCLLLARSAQPHPLIAIASRTLLQERAGQLGLAIDLKDVSPAAWPERPAKAGQLYVWDTPLAAPVRPGQLDRANAAYVLETLTRAGQGCLDGHFAGMITAPVHKGVINEAGIPFSGHTEFLADLTHTAQVVMMLATRGLRVALATTHLPLREVADAISDERLTRVARILHADLRDKFGIAHPRILVCGLNPHAGEGGHLGREEIEVIEPCLERLRGEGLDLIGPLPADTLFTPKHLEHCDAVLAMYHDQGLPVLKYKGFGAAVNVTLGLPIIRTSVDHGTALDLAGSGRIDSGSLQVALETA... | Cofactor: Binds 1 divalent metal cation per subunit. Can probably use ions such as Zn(2+), Mg(2+) or Co(2+).
Function: Catalyzes the NAD(P)-dependent oxidation of 4-(phosphooxy)-L-threonine (HTP) into 2-amino-3-oxo-4-(phosphooxy)butyric acid which spontaneously decarboxylates to form 3-amino-2-oxopropyl phosphate (AHAP... |
Q3IFD2 | MTLRIAITPGEPAGIGPDLLLKLAQQTWDAQLVAIADANMLKQRAKHLGLSIKLIEFDQHAAATPAPAGSLYLHQVDVAEPVELGVLNDANGQYVLDTLRIASEKNMDGTFAAVVTGPVHKGIINKAGISFSGHTEYFAQQSNTADVVMMLATQGLRVALVTTHIPLAYVSRAITEDRLIKVASILNHDLQTKFGIEKPRILVCGLNPHAGEDGHLGREEIDTIIPTLEILNNQGMNLIGPLPADTLFQDKYLNEADAVLAMYHDQGLPVLKYKGFGNSVNITLGLPFIRTSVDHGTALDLAGKGTADVGSFELAIREAI... | Cofactor: Binds 1 divalent metal cation per subunit. Can use ions such as Zn(2+), Mg(2+) or Co(2+).
Function: Catalyzes the NAD(P)-dependent oxidation of 4-(phosphooxy)-L-threonine (HTP) into 2-amino-3-oxo-4-(phosphooxy)butyric acid which spontaneously decarboxylates to form 3-amino-2-oxopropyl phosphate (AHAP).
Cataly... |
P58714 | MLNIAITTGEPAGIGPDITVTALLRLLRQPAPRHADVRWHVIGDAALLQARADAIGLGDAWRDAAAALTVVARPLGAPVRTGVLDAANGRYVLDLLDAAIDGCLPDAAGMARYDAMVTAPVQKSTINDAGVPFTGHTEYLAERSRTPRVVMMLAGPQPAHGNAMLRVALATTHLPLREVPDAITPAVLDETLDIVQRDLRARFGMAAPRILVTGLNPHAGEAGHLGREEIEVIEPAVVRARARGIDARGPYPADTLFQPRLLADADCVLAMYHDQGLAPLKYGTFGHGVNITLGLPFVRTSVDHGTALDLAGTGRAEAGS... | Cofactor: Binds 1 divalent metal cation per subunit. Can use ions such as Zn(2+), Mg(2+) or Co(2+).
Function: Catalyzes the NAD(P)-dependent oxidation of 4-(phosphooxy)-L-threonine (HTP) into 2-amino-3-oxo-4-(phosphooxy)butyric acid which spontaneously decarboxylates to form 3-amino-2-oxopropyl phosphate (AHAP).
Cataly... |
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