ids stringlengths 6 10 | seqs stringlengths 11 1.02k | texts stringlengths 108 11.1k |
|---|---|---|
P0DL36 | MRIWSLTRILTFIVIFNFAEAGGECMKKCDSPDMIREIFTRCTMVKRDTQFSENSGHLIPKRSVVADNKCENSLRREIACGQCRDKVKTDGYFYECCTSDSTFKKCQDLLHK | Function: Gating-modifier toxin that inhibits voltage-gated sodium channel with a preference for hNav1.7/SCN9A (IC(50)=25.4 nM) over hNav1.1/SCN1A (IC(50)=4.1 uM), hNav1.2/SCN2A (IC(50)=813 nM), and hNav1.6/SCN8A (IC(50)=15.2 uM) . Is an effective analgesic in rodent pain models, since it is several-fold more effective... |
B1P1I2 | MKLCVLTIATLLVTATSLETQKEIAEGNELTREETPSLVEHKEDEAAAASEKRSCIEEWKTCENSCECCGSSTICSSTWAEGKEIKLCKNEGGTFKKVLHFIQKGISKLKSCKEGN | Function: Probable ion channel inhibitor.
Sequence Mass (Da): 12733
Sequence Length: 116
Domain: The presence of a 'disulfide through disulfide knot' structurally defines this protein as a knottin.
Subcellular Location: Secreted
|
B1P1I6 | MKHCFLILFTLIVFTVVWSLEENEEYPDEDEMIESFMDGYSYRGDDGTCILKGDHCHGTCDCCGWTTTCRKSKSAGGKICKSEGSSISAFNAIAKGVAAMKKAKCKHKSG | Function: Probable ion channel inhibitor.
Sequence Mass (Da): 12090
Sequence Length: 110
Domain: The presence of a 'disulfide through disulfide knot' structurally defines this protein as a knottin.
Subcellular Location: Secreted
|
P84014 | ACIPRGEICTDDCECCGCDNECYCPIGSSLGIFKCSCAHANKYFCNRKKEKCKKA | Function: Antagonist of L-type calcium channels (Cav1/CACNA1). In vivo, causes paralysis in posterior limbs, and gradual decrease in movement and aggression during 24 hours after intracerebroventricular injection in mice at dose levels of 3 ug per mouse.
Sequence Mass (Da): 6062
Sequence Length: 55
Domain: The presence... |
P81792 | MKCAVLFLSVIALVHIFVVEAEEEPDSDALVPQERACIPRGEICTDDCECCGCDNQCYCPPGSSLGIFKCSCAHANKYFCNRKKEKCKKA | Function: Potent blocker of nociceptor cation channels TRPA1 and high voltage-activated calcium channels . It acts mainly on P/Q-type (Cav2.1/CACNA1A) calcium channels and has a minor effect on L- (Cav1/CACNA1) and N-type (Cav2.2/CACNA1B) calcium channels . Blocks glutamate release in synaptic transmission mediated by ... |
P85033 | SCIKHGDFCDGDKDDCQCCRDNGFCSCSGIFGLKWNCRCDVGTT | Function: Omega-agatoxins are antagonists of voltage-gated calcium channels (Cav) (By similarity). Toxic to mice by intracerebroventricular injection.
Sequence Mass (Da): 4814
Sequence Length: 44
Domain: The presence of a 'disulfide through disulfide knot' structurally defines this protein as a knottin.
Subcellular Loc... |
P0DQC1 | MKMVYLGLFLIITSCVISSGNLIYECKWADSIRLKDKNPTHEFCKKKCEEKNTDRITVQHGFHSSDYRCTCQGEKILETPYQSDGVKDCHRI | Function: Inhibits voltage-gated potassium channels (Kv) (IC(50)=about 10 nM), when tested on DRG neurons.
PTM: Contains 3 disulfide bonds.
Sequence Mass (Da): 10677
Sequence Length: 92
Subcellular Location: Secreted
|
P85271 | SCIKHGDFCDGDNDDCQCCRDNGF | Function: Omega-agatoxins are antagonists of voltage-gated calcium channels (Cav).
PTM: Disulfide bonds are present.
Sequence Mass (Da): 2668
Sequence Length: 24
Subcellular Location: Secreted
|
P0C202 | MGFKLVLFIAVLTLVGSSNAEISAKMDSRDSPMIQERRCLPAGKTCVRGPMRVPCCGSCSQNKCT | Function: Possesses strong antiplasmodial activity against the intra-erythrocyte stage of P.falciparum in vitro. IC(50) for inhibiting P.falciparum growth is 1.15 uM. Specifically interacts with infected erythrocytes. Does not lyse erythrocytes, is not cytotoxic to nucleated mammalian cells, and does not inhibit neurom... |
P84835 | EGECGGFWWKCGSGKPACCPKYVCSPKWGLCNFPMP | Function: Gating modifier of Kv2.1/KCNB1 (IC(50)=5.1 nM), Kv2.2/KCNB2 and Kv4.3/KCND3 channels (IC(50)=39 nM). Acts by shifting the channel activation to more depolarized potentials by stabilizing the resting conformation of the voltage sensor. It completely inhibits opening of the Kv2.1/KCNB1 channel at negative membr... |
Q8NBS9 | MPARPGRLLPLLARPAALTALLLLLLGHGGGGRWGARAQEAAAAAADGPPAADGEDGQDPHSKHLYTADMFTHGIQSAAHFVMFFAPWCGHCQRLQPTWNDLGDKYNSMEDAKVYVAKVDCTAHSDVCSAQGVRGYPTLKLFKPGQEAVKYQGPRDFQTLENWMLQTLNEEPVTPEPEVEPPSAPELKQGLYELSASNFELHVAQGDHFIKFFAPWCGHCKALAPTWEQLALGLEHSETVKIGKVDCTQHYELCSGNQVRGYPTLLWFRDGKKVDQYKGKRDLESLREYVESQLQRTETGATETVTPSEAPVLAAEPEAD... | Function: Protein disulfide isomerase of the endoplasmic reticulum lumen involved in the formation of disulfide bonds in proteins. Can reduce insulin disulfide bonds.
Catalytic Activity: Catalyzes the rearrangement of -S-S- bonds in proteins.
Sequence Mass (Da): 47629
Sequence Length: 432
Subcellular Location: Endoplas... |
Q91W90 | MPPRPGRLLQPLAGLPALATLLLLLGARKGARAQEVEADSGVEQDPHAKHLYTADMFTHGIQSAAHFVMFFAPWCGHCQRLQPTWNDLGDKYNSMEDAKVYVAKVDCTADSDVCSAQGVRGYPTLKFFKPGQEAVKYQGPRDFETLENWMLQTLNEEPATPEPEAEPPRAPELKQGLYELSANNFELHVSQGNHFIKFFAPWCGHCKALAPTWEQLALGLEHSETVKIGKVDCTQHYAVCSEHQVRGYPTLLWFRDGKKVDQYKGKRDLESLRDYVQSQLQGSEAAPETVEPSEAPVMAAEPTGDKGTVLALTEKSFEDT... | Function: Protein disulfide isomerase of the endoplasmic reticulum lumen involved in the formation of disulfide bonds in proteins . Can reduce insulin disulfide bonds .
Catalytic Activity: Catalyzes the rearrangement of -S-S- bonds in proteins.
Sequence Mass (Da): 46415
Sequence Length: 417
Subcellular Location: Endopl... |
Q4N4N8 | MKFLILNCLILFSLISSEATNVKLDREDQNHLVLLNEKNFEKLTQASTGATTGTWFVKFYAPWCSHCRKMAPAWESLAKALKGQVNVADVDVTRNLNLGKRFQIRGYPTLLLFHKGKMYQYEGGERTVEKLSEFALGDFKNAVGAPVPQPLSLFALVSDFVVSGVNEALRVYDAALAGFVTISSFSFLFGLLVGLMLSLFLFTRRATRKPKVLTERKKDK | Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 24679
Sequence Length: 220
Domain: The di-lysine motif confers endoplasmic reticulum localization for type I membrane proteins.
Subcellular Location: Endoplasmic reticulum membrane
|
Q9H3M7 | MVMFKKIKSFEVVFNDPEKVYGSGEKVAGRVIVEVCEVTRVKAVRILACGVAKVLWMQGSQQCKQTSEYLRYEDTLLLEDQPTGENEMVIMRPGNKYEYKFGFELPQGPLGTSFKGKYGCVDYWVKAFLDRPSQPTQETKKNFEVVDLVDVNTPDLMAPVSAKKEKKVSCMFIPDGRVSVSARIDRKGFCEGDEISIHADFENTCSRIVVPKAAIVARHTYLANGQTKVLTQKLSSVRGNHIISGTCASWRGKSLRVQKIRPSILGCNILRVEYSLLIYVSVPGSKKVILDLPLVIGSRSGLSSRTSSMASRTSSEMSWV... | Function: May act as an oxidative stress mediator by inhibiting thioredoxin activity or by limiting its bioavailability. Interacts with COPS5 and restores COPS5-induced suppression of CDKN1B stability, blocking the COPS5-mediated translocation of CDKN1B from the nucleus to the cytoplasm. Functions as a transcriptional ... |
O96650 | MEGANVNEDERKYLRQIKHIIDEGDKVIDRTGVGTLSLFGLHSTYSLRNGVIPLLTTKRVYWKGVVEELLWFIKGDTDAKRLSAKGVKIWDANGSREFLDSQGFKDRPEGDLGPIYGFQWRHFGAEYHGTDADYKGQGVDQLADVIEQIKNNPNSRRIILNAWNVKDLHQMALPPCHTLAQFAVKNGELSCQLYQRSGDMGLGVPFNLASYGLLTHMIAHVCALKTGFLHHVLGDAHVYLNHIDALKEQLSRDPRPFPTVHFEGRIDSIDDFTAESIILNGYNPMAPIKMPMAV | Catalytic Activity: (6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + dUMP = 7,8-dihydrofolate + dTMP
Sequence Mass (Da): 33054
Sequence Length: 294
Pathway: Pyrimidine metabolism; dTTP biosynthesis.
EC: 2.1.1.45
|
Q65J44 | MSHYDQQYNAIIQKIIESGISDEEYQVRTKWDSDGTPAHTLSIMSEKMRFDNSEVPILTTKKVAWKTAIKELLWIWQLKSNDVQVLNDMGVHIWDQWRLEDGTIGAAYGYQLGKKNRTVNGQKVDQVDYLLHQLKHNPSSRRHLTMLWNPDDLDGMALTPCVYETQWYVKEGKLSLEVRARSNDMALGNPFNVFQYNVLQRMIAQVLGYELGEYIFNIGDCHIYTRHIDNLNIQMKREQYEAPKLWINPDIKNFYDFTIDDFKLIDYKHGDKLTFEVAV | Function: Catalyzes the reductive methylation of 2'-deoxyuridine-5'-monophosphate (dUMP) to 2'-deoxythymidine-5'-monophosphate (dTMP) while utilizing 5,10-methylenetetrahydrofolate (mTHF) as the methyl donor and reductant in the reaction, yielding dihydrofolate (DHF) as a by-product. This enzymatic reaction provides an... |
P78029 | MQQYLDLARYVLEHGKYRPNRTDTAGIGVFGYQMHFDISKHFPLLTTKKVHWKSIVHELLWFIKGDTNIKYLVDNKVNIWNEWPYESFKKSPHFNGESQKEFIERIRQDAKFAQQFGNLGPVYGKQWRDFNGVDQLKKVIAQIKVNPFSRRLIVSSWNPNEVDQMLLPPCHSLYQFYVQDGQLSCQLYQRSGDIFLGIPFNIASYSLLVYLVAKETNLKPGSFVHTIGDAHIYENHLEQIKLQLTRQPKPLPKVVLKSDKSIFDYQFDDIELVDYDHHPTIKGEVAV | Function: Catalyzes the reductive methylation of 2'-deoxyuridine-5'-monophosphate (dUMP) to 2'-deoxythymidine-5'-monophosphate (dTMP) while utilizing 5,10-methylenetetrahydrofolate (mTHF) as the methyl donor and reductant in the reaction, yielding dihydrofolate (DHF) as a by-product. This enzymatic reaction provides an... |
Q98Q31 | MKQYLDFLKWVLEKGKHKENRTSVDTISAFGYQMRFDLSKGFPLVTTKKTNFSAIAHELLWFIKGDTNIKYLVDNKVNIWNQWPYESYKKSQDFQSESLKEFIQKIKDDNEFAQKHGNLGPVYGKQWRDFLGIDQLKKVIEQIKNNPNSRRLIVSSWNPSEIDTMLLPPCHTLFQFYVNDNKLSCHLYQRSADAFLGIPFNIASYALLTFLLAQETNLEVGDFVHSIGDAHIYVNHLEQVKTQLKRNPKELPKLIIKNKNIFEINFEDIELVDYEFDPIIKGEVAV | Function: Catalyzes the reductive methylation of 2'-deoxyuridine-5'-monophosphate (dUMP) to 2'-deoxythymidine-5'-monophosphate (dTMP) while utilizing 5,10-methylenetetrahydrofolate (mTHF) as the methyl donor and reductant in the reaction, yielding dihydrofolate (DHF) as a by-product. This enzymatic reaction provides an... |
A0A1D0C027 | MKLILLIAIFSALAVVNLGTPSADQVRYNYTELPNGEYCYTPRRRCTSADQCCRPYDTTAAFHGCGRIWPKDKREKVDRCYICNNEKTLCTSVMGK | Function: Probable neurotoxin with ion channel impairing activity.
Sequence Mass (Da): 10919
Sequence Length: 96
Domain: The presence of a 'disulfide through disulfide knot' structurally defines this protein as a knottin.
Subcellular Location: Secreted
|
P10074 | MDGSFVQHSVRVLQELNKQREKGQYCDATLDVGGLVFKAHWSVLACCSHFFQSLYGDGSGGSVVLPAGFAEIFGLLLDFFYTGHLALTSGNRDQVLLAARELRVPEAVELCQSFKPKTSVGQAAGGQSGLGPPASQNVNSHVKEPAGLEEEEVSRTLGLVPRDQEPRGSHSPQRPQLHSPAQSEGPSSLCGKLKQALKPCPLEDKKPEDCKVPPRPLEAEGAQLQGGSNEWEVVVQVEDDGDGDYMSEPEAVLTRRKSNVIRKPCAAEPALSAGSLAAEPAENRKGTAVPVECPTCHKKFLSKYYLKVHNRKHTGEKPFE... | Function: Telomere-binding protein that acts as a regulator of telomere length . Directly binds the telomeric double-stranded 5'-TTAGGG-3' repeat . Preferentially binds to telomeres that have a low concentration of shelterin complex and acts as a regulator of telomere length by initiating telomere trimming, a process t... |
Q8VY74 | MSGGGNNVVNKVFYATSYHPIQAGSIDGTDVAPHDNGVRRALLCYNAGLYDPSGDSKAVGDPYCTLFVGRLSHHTTEDTLREVMSKYGRIKNLRLVRHIVTGASRGYGFVEYETEKEMLRAYEDAHHSLIDGREIIVDYNRQQLMPGWIPRRLGGGLGGRKESGQLRFGGRDRPFRAPLRPIPHEDLKKLGIQLPPEGRYMSRTQIPSPPRRKGSVSDREEEYYREKSSVEREEEFKERSSLRSYHSHRSSAHTHSSHRRRSKDREECSREESRSDRKERARGMEDRYGDNKGEVSGSKRSKRSEEDRSRKRHKHLPSHH... | Function: May facilitate 5' splice site recognition in the minor spliceosome. May be involved in interactions with components of the major spliceosome bound to the pyrimidine tract of an upstream U2-type intron.
PTM: Phosphorylated.
Sequence Mass (Da): 38375
Sequence Length: 333
Subcellular Location: Nucleus speckle
|
Q9M8X2 | MDRPPSLPHYQNPNPNLFYHYPPPNSNPNFFFRPPPPPLQNPNNYSIVPSPPPIRELSGTLSSLKSLLSECQRTLDSLSQNLALDHSSLLQKDENGCFVRCPFDSNHFMPPEALFLHSLRCPNTLDLIHLLESFSSYRNTLELPCELQLNNGDGDLCISLDDLADFGSNFFYRDCPGAVKFSELDGKKRTLTLPHVLSVECSDFVGSDEKVKKIVLDKCLGVLPSDLCAMKNEIDQWRDFPSSYSSSVLSSIVGSKVVEISALRKWILVNSTRYGVIIDTFMRDHIFLLFRLCLKSAVKEACGFRMESDATDVGEQKIMS... | Function: Likely involved in U12-type 5' splice site recognition.
Sequence Mass (Da): 81967
Sequence Length: 712
Domain: The CHHC region interacts with the 5' splice site of the U12-type intron.
Subcellular Location: Nucleus
|
Q3SYR2 | MKVKKGGGGAGTGAEHAPGASGPNVEPKPELQAESESGSESEPEAGPGPRPGPLQRKQPIGPEDVLGLQRITGDYLCSPEENIYKIDFVRFKIRDMDSGTVLFEIKKPPASERLPINPRDLDPNAGRFVRYQFTPAFLRLRQVGATVEFTVGDKPVNNFRMIERHYFRNQLLKSFDFHFGFCIPSSKNTCEHIYDFPALSEELINEMIRHPYETQSDSFYFVDDRLVMHNKADYSYSGTP | Function: Involved in synaptic functions in photoreceptor cells, the signal transduction in immune cells as a Src family kinase activator, endosome recycling, the uptake of bacteria and endocytosis, protein trafficking in sensory neurons and as lipid-binding chaperone with specificity for a diverse subset of myristoyla... |
O19177 | MKVKKGGGGAGTGAEPASGAPGPSVEPKPEPQAESESGSESEPEAGPGPRPGPLQRKQRIGPEDVLGLQRITGDYLCSPEENIYKIDFIRFKIRDMDSGTVLFEIKKPPASERLPINRRDLDPNAGRFVRYQFTPAFLRLRQVGATVEFTVGDKPVNNFRMIERHYFRNQLLKSFDFHFGFCIPSSKNTCEHIYDFPPLSEELINEMIRHPYETQSDSFYFVDDRLVMHNKADYSYSGTP | Function: Involved in synaptic functions in photoreceptor cells, the signal transduction in immune cells as a Src family kinase activator, endosome recycling, the uptake of bacteria and endocytosis, protein trafficking in sensory neurons and as lipid-binding chaperone with specificity for a diverse subset of myristoyla... |
Q13432 | MKVKKGGGGAGTATESAPGPSGQSVAPIPQPPAESESGSESEPDAGPGPRPGPLQRKQPIGPEDVLGLQRITGDYLCSPEENIYKIDFVRFKIRDMDSGTVLFEIKKPPVSERLPINRRDLDPNAGRFVRYQFTPAFLRLRQVGATVEFTVGDKPVNNFRMIERHYFRNQLLKSFDFHFGFCIPSSKNTCEHIYDFPPLSEELISEMIRHPYETQSDSFYFVDDRLVMHNKADYSYSGTP | Function: Involved in synaptic functions in photoreceptor cells, the signal transduction in immune cells as a Src family kinase activator, endosome recycling, the uptake of bacteria and endocytosis, protein trafficking in sensory neurons and as lipid-binding chaperone with specificity for a diverse subset of myristoyla... |
A0A0A0V633 | MKLFVCFLLLAVVVVSAVNASEEMRLKNLLKAVERDETPDECVTRGNFCATPEVHGDWCCGSLKCVSNSCR | Function: Probable insect neurotoxin with ion channel impairing activity (Probable). Does not show activity on 45 human receptors from 9 families (5-hydroxytryptamine, adrenergic, dopamine, muscarinic, histamine, neurotransmitter, opioid, sigma, and gaba(A) receptors) . In vivo, does not cause paralytic or lethal activ... |
B3VI56 | MATSDSIVDDRKQLHVATFPWLAFGHILPYLQLSKLIAEKGHKVSFLSTTRNIQRLSSHISPLINVVQLTLPRVQELPEDAEATTDVHPEDIPYLKKASDGLQPEVTRFLEQHSPDWIIYDYTHYWLPSIAASLGISRAHFSVTTPWAIAYMGPSADAMINGSDGRTTVEDLTTPPKWFPFPTKVCWRKHDLARLVPYKAPGISDGYRMGLVLKGSDCLLSKCYHEFGTQWLPLLETLHQVPVVPVGLLPPEVPGDEKDETWVSIKKWLDGKQKGSVVYVALGSEVLVSQTEVVELALGLELSGLPFVWAYRKPKGPAKS... | Function: Involved in the biosynthesis of steviol glycosides in leaves . Converts the mono-glycoside steviolmonoside to the bi-glycoside steviolbioside . Converts the bi-glycoside rubusoside to the tri-glycoside stevioside . Converts the tri-glycoside stevioside to the tetra-glycoside rebaudioside E . Converts the tetr... |
O08546 | MKVVILMALLVLTAHCVPVSRFPGKIFLYCPFFNRKHCQRFCEFFKICRKPPLSRRTTVVPSFPLTTEADLSLTGGPLTPDRRGDSR | Function: Plays a protective role during endotoxic shock.
PTM: Glycosylated.
Sequence Mass (Da): 9927
Sequence Length: 87
Subcellular Location: Secreted
|
Q46821 | MSAIDSQLPSSSGQDRPTDEVDRILSPGKLIILGLQHVLVMYAGAVAVPLMIGDRLGLSKEAIAMLISSDLFCCGIVTLLQCIGIGRFMGIRLPVIMSVTFAAVTPMIAIGMNPDIGLLGIFGATIAAGFITTLLAPLIGRLMPLFPPLVTGVVITSIGLSIIQVGIDWAAGGKGNPQYGNPVYLGISFAVLIFILLITRYAKGFMSNVAVLLGIVFGFLLSWMMNEVNLSGLHDASWFAIVTPMSFGMPIFDPVSILTMTAVLIIVFIESMGMFLALGEIVGRKLSSHDIIRGLRVDGVGTMIGGTFNSFPHTSFSQNV... | Function: Proton-dependent high-capacity transporter for uric acid. Shows also a low capacity for transport of xanthine at 37 degrees Celsius but not at 25 degrees Celsius.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 51758
Sequence Length: 482
Subcellular Location: Cell inner membrane
|
F6P6X0 | MAARKSGSDIHNNGPVSYLDDVPFKLNEKFRCPSKVGLPIGFCLSDCNAILSDLQYDFNLERRTVQWGEELAKARAAEARAAEAIRTDSESERQAASQDAEVGLVGGKKARPSDEQDIVPPALKPVLAGLSHNAILTPLPAPSFGQTRPAPSNPAPQYLNLADFEREEDPFDKLELKTLDDKEELRTILQSQPQSSVSPPQLPPAEHRPVSPSTTPPLQAKTGIFHKPNGLVGLLDLDRGGVLGGQIDADRPCNIRSLTFPKLSDPGDSPLETPLSVYPVAPPRNLSNGTPPSLQRTASNNNTTLPQEQPVFAQNGTPKQ... | Function: Component of the ESCRT-I complex, a regulator of vesicular trafficking process. Binds to ubiquitinated cargo proteins and is required for the sorting of endocytic ubiquitinated cargos into multivesicular bodies (MVBs).
Sequence Mass (Da): 49415
Sequence Length: 453
Domain: The UMA domain mediates association ... |
Q9NZ09 | MASKKLGADFHGTFSYLDDVPFKTGDKFKTPAKVGLPIGFSLPDCLQVVREVQYDFSLEKKTIEWAEEIKKIEEAEREAECKIAEAEAKVNSKSGPEGDSKMSFSKTHSTATMPPPINPILASLQHNSILTPTRVSSSATKQKVLSPPHIKADFNLADFECEEDPFDNLELKTIDEKEELRNILVGTTGPIMAQLLDNNLPRGGSGSVLQDEEVLASLERATLDFKPLHKPNGFITLPQLGNCEKMSLSSKVSLPPIPAVSNIKSLSFPKLDSDDSNQKTAKLASTFHSTSCLRNGTFQNSLKPSTQSSASELNGHHTLG... | Function: Component of the ESCRT-I complex, a regulator of vesicular trafficking process . Binds to ubiquitinated cargo proteins and is required for the sorting of endocytic ubiquitinated cargos into multivesicular bodies (MVBs) . Plays a role in the proteasomal degradation of ubiquitinated cell-surface proteins, such ... |
P33296 | MATKQAHKRLTKEYKLMVENPPPYILARPNEDNILEWHYIITGPADTPYKGGQYHGTLTFPSDYPYKPPAIRMITPNGRFKPNTRLCLSMSDYHPDTWNPGWSVSTILNGLLSFMTSDEATTGSITTSDHQKKTLARNSISYNTFQNVRFKLIFPEVVQENVETLEKRKLDEGDAANTGDETEDPFTKAAKEKVISLEEILDPEDRIRAEQALRQSENNSKKDGKEPNDSSSMVYIGIAIFLFLVGLFMK | Function: Catalyzes the covalent attachment of ubiquitin to other proteins. Functions in degradation of misfolded or regulated proteins localized in the endoplasmic reticulum (ER) lumen or membrane via the ubiquitin-proteasome system. Cognate E2 conjugating enzyme for the DOA10 ubiquitin ligase complex, which is part o... |
P34477 | MEQSSLLLKKQLADMRRVPVDGFSAGLVDDNDIYKWEVLVIGPPDTLYEGGFFKAILDFPRDYPQKPPKMKFISEIWHPNIDKEGNVCISILHDPGDDKWGYERPEERWLPVHTVETILLSVISMLTDPNFESPANVDAAKMQRENYAEFKKKVAQCVRRSQEE | Function: Catalyzes the covalent attachment of ubiquitin to other proteins.
Catalytic Activity: S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-L-cysteine + [E2 ubiquitin-conjugating enzyme]-L-cysteine = [E1 ubiquitin-activating enzyme]-L-cysteine + S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine.
Sequence Ma... |
O00102 | MSKAMALRRLMKEYKELTENGPDGITAGPSNEDDFFTWDCLIQGPDGTPFEGGLYPATLKFPSDYPLGPPTLKFECEFFHPNVYKDGTVCISILHAPGDDPNMYESSSERWSPVQSVEKILLSVMSMLAEPNDESGANIDACKMWREDREEYCRVVRRLARKTLGL | Function: Catalyzes the covalent attachment of ubiquitin to other proteins. Functions in degradation of misfolded or regulated proteins localized in the endoplasmic reticulum (ER) lumen or membrane via the ubiquitin-proteasome system. Cognate E2 conjugating enzyme for the doa10 ubiquitin ligase complex, which is part o... |
P25868 | MATAPARRASSSRSSSEISRTTPSMGFQLGFVDDSNVFEWQVTIIGPPETLYDGGYFNAIMSFPQNYPNSPPTVRFTSEMWHPNVYPDGRVCISIHPPGDDPNGYELASERWTPVHTVESIVLSIISMLSSPNDESPANIEAAKDWREKQDEFKKKVRRAVRKSQEML | Function: Catalyzes the covalent attachment of ubiquitin to other proteins so as to signal them for selective protein degradation. Involved in the formation of multiubiquitin chains.
Catalytic Activity: S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-L-cysteine + [E2 ubiquitin-conjugating enzyme]-L-cysteine = [E1 ubiqui... |
Q02159 | MSKTAQKRLLKELQQLIKDSPPGIVAGPKSENNIFIWDCLIQGPPDTPYADGVFNAKLEFPKDYPLSPPKLTFTPSILHPNIYPNGEVCISILHSPGDDPNMYELAEERWSPVQSVEKILLSVMSMLSEPNIESGANIDACILWRDNRPEFERQVKLSILKSLGF | Function: Catalyzes the covalent attachment of ubiquitin to other proteins. Functions in degradation of misfolded or regulated proteins localized in the endoplasmic reticulum (ER) lumen or membrane via the ubiquitin-proteasome system. Cognate E2 conjugating enzyme for the DOA10 ubiquitin ligase complex, which is part o... |
P52487 | MAATRRLTRELSDLVEAKMSTLRNIESSDESLLMWTGLLVPEKAPYNKGAFRIEINFPPQYPFMPPKILFKTKIYHPNVDEKGEVCLPIISTDNWKPTTRTEQVLQALVAIVHNPEPEHPLRSDLAEEFVREHKKFMKTAEEFTKKNAEKRPE | Function: Catalyzes the covalent attachment of ubiquitin to other proteins.
Catalytic Activity: S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-L-cysteine + [E2 ubiquitin-conjugating enzyme]-L-cysteine = [E1 ubiquitin-activating enzyme]-L-cysteine + S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine.
Sequence Ma... |
P35131 | MASKRILKELKDLQKDPPTSCSAGPVAEDMFHWQATIMGPAESPYSGGVFLVTIHFPPDYPFKPPKVAFRTKVFHPNINSNGSICLDILKEQWSPALTISKVLLSICSLLTDPNPDDPLVPEIAHMYKTDRAKYEATARNWTQKYAMG | Function: Accepts the ubiquitin from the E1 complex and catalyzes its covalent attachment to other proteins. Mediates the selective degradation of short-lived and abnormal proteins.
Catalytic Activity: S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-L-cysteine + [E2 ubiquitin-conjugating enzyme]-L-cysteine = [E1 ubiquit... |
Q9P7R4 | MSSPRRRIETDVMKLLMSDYEVTLVNDNMQEFYVRFHGPSETPYSGGIWKVHVELPSEYPWKSPSIGFVNRIFHPNIDELSGSVCLDVINQTWSPMFDMINIFEVFLPQLLRYPNASDPLNGEAAALLLREPNTYYAKVRDYIARYANKEDADITLNDSSDDDTMSSIDTESGDEIAGPMDSDF | Function: Catalyzes the covalent attachment of ubiquitin to other proteins.
Catalytic Activity: S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-L-cysteine + [E2 ubiquitin-conjugating enzyme]-L-cysteine = [E1 ubiquitin-activating enzyme]-L-cysteine + S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine.
Sequence Ma... |
P28263 | MSSSKRRIETDVMKLLMSDHQVDLINDSMQEFHVKFLGPKDTPYENGVWRLHVELPDNYPYKSPSIGFVNKIFHPNIDIASGSICLDVINSTWSPLYDLINIVEWMIPGLLKEPNGSDPLNNEAATLQLRDKKLYEEKIKEYIDKYATKEKYQQMFGGDNDSDDSDSGGDLQEEDSDSDEDMDGTGVSSGDDSVDELSEDLSDIDVSDDDDYDEVANQ | Function: Catalyzes the covalent attachment of ubiquitin to other proteins (By similarity). Required for the adaptation to the presence of glucose in the growth medium; mediates the degradation of enzymes involved in gluconeogenesis when cells are shifted to glucose-containing medium . Required for proteasome-dependen... |
Q9W6H5 | MSGIALSRLAQERKAWRKDHPFGFVAVPMKNPDGTMNLMNWECAIPGKKGTPWEGGLFKLRMLFKDDYPSSPPKCKFEPPLFHPNVYPSGTVCLSILEEDKDWRPAITIKQILLGIQELLNEPNIQDPAQAEAYTIYCQNRVEYEKRVRAQAKKFSPS | Function: Accepts the ubiquitin-like proteins sumo1, sumo2 and sumo3 from the uble1a-uble1b E1 complex and catalyzes their covalent attachment to other proteins with the help of an E3 ligase such as ranbp2 or cbx4. Essential for nuclear architecture and chromosome segregation (By similarity). Mediates nuclear localizat... |
Q9DDJ0 | MSGIALSRLAQERKAWRKDHPFGFVAVPTKNPDGTMNLMNWECAIPGKKGTPWEGGLFKLRMLFKDDYPSSPPKCKFEPPLFHPNVYPSGTVCLSILEEDKDWRPAITIKQILLGIQELLNEPNIQDPAQAEAYTIYCQNRVEYEKRVRAQAKKFSP | Function: Accepts the ubiquitin-like proteins sumo1, sumo2 and sumo3 from the uble1a-uble1b E1 complex and catalyzes their covalent attachment to other proteins with the help of an E3 ligase such as ranbp2 or cbx4. Essential for nuclear architecture and chromosome segregation (By similarity). Mediates nuclear localizat... |
Q95017 | MSGIAAGRLAEERKHWRKDHPFGFIAKPVKNADGTLNLFNWECAIPGRKDTIWEGGLYRIRMLFKDDFPSTPPKCKFEPPLFHPNVYPSGTVCLSLLDENKDWKPSISIKQLLIGIQDLLNHPNIEDPAQAEAYQIYCQNRAEYEKRVKKEAVKYAAELVQKQMLE | Function: Accepts the ubiquitin-like protein smo-1 from the aos-1-uba-2 E1 complex and catalyzes its covalent attachment to other proteins with the help of an E3 ligase such as gei-17. Required to sumoylate the ETS transcription factor lin-1, Polycomb protein sop-2, and intermediate filament proteins, such as ifb-1 . R... |
P63279 | MSGIALSRLAQERKAWRKDHPFGFVAVPTKNPDGTMNLMNWECAIPGKKGTPWEGGLFKLRMLFKDDYPSSPPKCKFEPPLFHPNVYPSGTVCLSILEEDKDWRPAITIKQILLGIQELLNEPNIQDPAQAEAYTIYCQNRVEYEKRVRAQAKKFAPS | Function: Accepts the ubiquitin-like proteins SUMO1, SUMO2, SUMO3, SUMO4 and SUMO1P1/SUMO5 from the UBLE1A-UBLE1B E1 complex and catalyzes their covalent attachment to other proteins with the help of an E3 ligase such as RANBP2, CBX4 and ZNF451. Can catalyze the formation of poly-SUMO chains. Necessary for sumoylation ... |
O09181 | MSGIALSRLAQERKAWRKDHPFGFVAVPTKNPDGTMNLMNWECAIPGKKGTPWEGGLFKLRMLFKDDYPSSPPKCKFEPPLFHPNVYPSGTVCLSILEEDKDWRPAITINQLFIGIQELLNEPNIQEPAQAEAYTIYCQNRVEYEKRFRAQAKKFCPS | Function: Accepts the ubiquitin-like proteins SUMO1, SUMO2 and SUMO3 from the UBLE1A-UBLE1B E1 complex and catalyzes their covalent attachment to other proteins with the help of an E3 ligase such as RANBP2, CBX4 and ZNF451 (By similarity). Can catalyze the formation of poly-SUMO chains (By similarity). Essential for nu... |
Q0K739 | MLERLSLYARLVRIDKPIGTLLLLWPTLWAMWMAAGGPPAWGLFWIFVAGTFLMRSAGCAINDWADRDFDKHVKRTRERPLTAGKIAAWEALAVAAVLALVAFALVLPLNALTKWLAVVAAVVAGTYPFFKRFFAIPQAYLGIAFGFGIPMAFAAIQDQVPPVAWLMLLANVFWAVAYDTAYAMVDRDDDLLIGMKTSAITFGRFDVAAIMLCYAAFLALMAWAGVLLGLGWPYWVGLAAAAGCAGYHYTLIRDRDRMRCFAAFRHNNWLGACVFAGTAVAYAIR | Function: Catalyzes the prenylation of para-hydroxybenzoate (PHB) with an all-trans polyprenyl group. Mediates the second step in the final reaction sequence of ubiquinone-8 (UQ-8) biosynthesis, which is the condensation of the polyisoprenoid side chain with PHB, generating the first membrane-bound Q intermediate 3-oct... |
Q2Y5S2 | MNAAQLSDWHPAPSSISPRARGWLQNRGSLTQLIQRRCCSEFSVKPVFQSLATVCDDELAVMNLRRDELALVREVYLYCGETPVVFAHSVVARKHLRGAWRSLIGLGNKSLGTVLFTNPVVKRTPLRFKKLTAAHPLFSRACRKLRVQPGNLWARRSLFTLHGQSILVTEVFLPSILELA | Function: Removes the pyruvyl group from chorismate, with concomitant aromatization of the ring, to provide 4-hydroxybenzoate (4HB) for the ubiquinone pathway.
Catalytic Activity: chorismate = 4-hydroxybenzoate + pyruvate
Sequence Mass (Da): 20246
Sequence Length: 180
Pathway: Cofactor biosynthesis; ubiquinone biosynth... |
Q142T1 | MSIRFVAADAHWRVAPLPGLSAAQKDWLTRGGSLTAHLRALGAVAVRVTREGVALPWPDEHAALGLAPRAPVWVREVVLAVEGVPFVAAHSVAPLAASAGVWQAMRRLRTRPLAELLYSDSSVARSSLVSRRLTARHPLYRLAACAIESLPPHALVARRSVFERHGAPLMVTECMLPALWAHLATVSGAGGSGDWSAHPRVREHGRPLEHTASRAHPATRASDEQRR | Function: Removes the pyruvyl group from chorismate, with concomitant aromatization of the ring, to provide 4-hydroxybenzoate (4HB) for the ubiquinone pathway.
Catalytic Activity: chorismate = 4-hydroxybenzoate + pyruvate
Sequence Mass (Da): 24497
Sequence Length: 227
Pathway: Cofactor biosynthesis; ubiquinone biosynth... |
Q9CMB5 | MSNYSQLLQNATWQPSTDMQLPLSISSWLELSTSLTTQLKQAFGEVNVCVLAESWITTLNENERQFFPKQACPCWCREVILKSQDIPLIFARTLIPASLLTQHSELQQLGNRALGEWLFMQSDRIRQKLELTHDKNTALYARRALMSIGAENMMVAELFLTPQIFTRVVK | Function: Removes the pyruvyl group from chorismate, with concomitant aromatization of the ring, to provide 4-hydroxybenzoate (4HB) for the ubiquinone pathway.
Catalytic Activity: chorismate = 4-hydroxybenzoate + pyruvate
Sequence Mass (Da): 19506
Sequence Length: 170
Pathway: Cofactor biosynthesis; ubiquinone biosynth... |
Q6D9I9 | MSDDASTLLRTISWFTEPPSVLPEHIGDWLMETSSMTQRLEKYCAQLRVTLCREGFITPQMLGEERDQLPADERYWLREVVLYGDDRPWLFGRTIVPQQTLEGSGAALTKIGNQPLGRYLFEQKSLTRDYIHTGCCEGLWARRSRLCLSGHPLLLTELFLPESPVYYTPGDEGWQVI | Function: Removes the pyruvyl group from chorismate, with concomitant aromatization of the ring, to provide 4-hydroxybenzoate (4HB) for the ubiquinone pathway.
Catalytic Activity: chorismate = 4-hydroxybenzoate + pyruvate
Sequence Mass (Da): 20355
Sequence Length: 177
Pathway: Cofactor biosynthesis; ubiquinone biosynth... |
Q7MZB5 | MSTDSILTTVPIQWLSVDSPVLPDEVLDWLMELGSMTRRFEQYCNSVRIIPFRECFITEEQLSDENERLLTGQRYWLREIVLCGDNIPWLLGRTLIPETTLTGPDESLVDLGTVPLGRYLFSGNKLTRDYIHVGQQGNRWARRSLLRLSGKPLLLTEVFLPESPVYKR | Function: Removes the pyruvyl group from chorismate, with concomitant aromatization of the ring, to provide 4-hydroxybenzoate (4HB) for the ubiquinone pathway.
Catalytic Activity: chorismate = 4-hydroxybenzoate + pyruvate
Sequence Mass (Da): 19412
Sequence Length: 168
Pathway: Cofactor biosynthesis; ubiquinone biosynth... |
Q6LVS4 | MSKFKQLYKPLLDNAQWETPLSLAIEGTAFGHWLLEPNSLSRRLQRHCDEFTVSLIEQKKIDSTMLSADERELIGDVDCLLRKVVLMGDGQPWVFARTLIPLSTLTGQESDLEQLGEMPLGFRVFTDRSARRDALEVANTGTQAQPLWARRSRLWINNKPLLVAELFLAQAPVYSKEKQC | Function: Removes the pyruvyl group from chorismate, with concomitant aromatization of the ring, to provide 4-hydroxybenzoate (4HB) for the ubiquinone pathway.
Catalytic Activity: chorismate = 4-hydroxybenzoate + pyruvate
Sequence Mass (Da): 20515
Sequence Length: 180
Pathway: Cofactor biosynthesis; ubiquinone biosynth... |
Q15ZU0 | MQKTISHAFPLGDVTWSNQGRLSIPNAHLESWLLNTGSLTQRLQTRCNDFKVQLVSQRQELATPAEYIQLGVSKMSQQKENWQVREVILHGDNQPWVFARSIIPQALCEADFLELGDKPLGHLIFNDDRFKRQPFQLMCLQPDEAFLHEYGLPPLTEIWGRRSVFCYQQYAMMVAELFLPKAPAYRDSNFDR | Function: Removes the pyruvyl group from chorismate, with concomitant aromatization of the ring, to provide 4-hydroxybenzoate (4HB) for the ubiquinone pathway.
Catalytic Activity: chorismate = 4-hydroxybenzoate + pyruvate
Sequence Mass (Da): 22297
Sequence Length: 192
Pathway: Cofactor biosynthesis; ubiquinone biosynth... |
Q9HTK1 | MPSNALWLRADQLSSVSPAVLDWLFDEGSLTRRLTALADGAFRVEPLLEGWQTLRDDECQGLDVPTGSSGWVREVYLHGHDRPWVFARSVAARSALEGSGFDLALLGTRSLGELLFSDSAFERGPIEVCRYPAAGLPAEVRAEGLWGRRSRFSRGALGVLVAEVYLPRLWDQAGIADV | Function: Removes the pyruvyl group from chorismate, with concomitant aromatization of the ring, to provide 4-hydroxybenzoate (4HB) for the ubiquinone pathway.
Catalytic Activity: chorismate = 4-hydroxybenzoate + pyruvate
Sequence Mass (Da): 19512
Sequence Length: 178
Pathway: Cofactor biosynthesis; ubiquinone biosynth... |
Q88C66 | MSYESPQAAAVAWLPYSQLATDIDQPTLDWLFDEGSLTRRLTRLSIDHFSVTPLFEGWQPLRDDECQALGIAAGAEGWVREVYLRGHGQPWVFARSVASRSALERGGLDLETLGSRSLGELLFCDQAFIRHPLEVCTYPQAWLPSEAAHAALWGRRSRFERNGLDLLVAEVFLPALWQAAKEENR | Function: Removes the pyruvyl group from chorismate, with concomitant aromatization of the ring, to provide 4-hydroxybenzoate (4HB) for the ubiquinone pathway.
Catalytic Activity: chorismate = 4-hydroxybenzoate + pyruvate
Sequence Mass (Da): 20826
Sequence Length: 185
Pathway: Cofactor biosynthesis; ubiquinone biosynth... |
Q9FD32 | MQVVYNFSQPGLQWKQSDHLRSLMTVTSRDWLLDRGSLTRRLRVLSDDDLEVVPLREEVGVILPHEADVLGLQLGAIGGVREVYLVGFGRPWVFARSIIVNSGSIEEGSALLQLGNMPLGDLLFGDGSFQRSEIEVCRYHDACNASARSTYPLWARRSVFKREKMHVLVQEMFLPALWEEMS | Function: Removes the pyruvyl group from chorismate, with concomitant aromatization of the ring, to provide 4-hydroxybenzoate (4HB) for the ubiquinone pathway.
Catalytic Activity: chorismate = 4-hydroxybenzoate + pyruvate
Sequence Mass (Da): 20634
Sequence Length: 182
Pathway: Cofactor biosynthesis; ubiquinone biosynth... |
Q3IHW4 | MITFPVSLSADWQCASLFSDLSSAEQEWLFEPHSLTAKLKSRSQCFSVKVLSEQEFELSAEQQQLLGCTQTTALNREVLLLCDNKPVVYAQSWLPASVNAANNKLHNMGERPLGDVIFQDPQLTRTDIEIARFNTQHSLQQLVAQLKLPSQSLLGRRSLFSLKDYKFLVCEVFLPGAYLY | Function: Removes the pyruvyl group from chorismate, with concomitant aromatization of the ring, to provide 4-hydroxybenzoate (4HB) for the ubiquinone pathway.
Catalytic Activity: chorismate = 4-hydroxybenzoate + pyruvate
Sequence Mass (Da): 20358
Sequence Length: 180
Pathway: Cofactor biosynthesis; ubiquinone biosynth... |
Q4FUZ9 | MTSHLCCSNYSSPLPELLVCLHTEGSLTALLEVKAGQPLRVERSFEGYRLLSLAQKKQLGMQGAALSRPRLAWVREVQLYGNDELPWVQAQSLFPLSSLQGSARRLQQLKSTPIGYVLFKRSRTLPNQRFIKHTVDGWQRQTLYNWYGRPLLISETFLPQFCEKQLDI | Function: Removes the pyruvyl group from chorismate, with concomitant aromatization of the ring, to provide 4-hydroxybenzoate (4HB) for the ubiquinone pathway.
Catalytic Activity: chorismate = 4-hydroxybenzoate + pyruvate
Sequence Mass (Da): 19277
Sequence Length: 168
Pathway: Cofactor biosynthesis; ubiquinone biosynth... |
Q2SQ75 | MQYRDLRDFIRILEQRGELKRITAEVDPHLEMTEICDRTLRREGPALLFENPRGYSIPVLGNLFGTPGRVALGMGAESVESLREIGKLLAFLKEPEPPKGLRDAWSKLPIFKQVMNMGPKEVSSASCQEVIIEGDDVDLYQYPIQTCWPGDAGPLVTWPLVITRGPNKARQNLGIYRQQLIGRNKLIMRWLSHRGGALDYREWREAHPMEPFPVAVALGADPATILGAVTPVPDTLSEYAFAGLLRGNKTEVVRCIGSDLQAPASAEIVLEGVIHPGEMAPEGPFGDHTGYYNEVDRFPVFTVERITQRKKPIYHSTYTG... | Cofactor: Binds 1 prenylated FMN (prenyl-FMN) per subunit.
Function: Catalyzes the decarboxylation of 3-octaprenyl-4-hydroxy benzoate to 2-octaprenylphenol, an intermediate step in ubiquinone biosynthesis.
Catalytic Activity: a 4-hydroxy-3-all-trans-polyprenylbenzoate + H(+) = a 2-all-trans-polyprenylphenol + CO2
Locat... |
Q602K0 | MSRNGAKYRDLRDFIARLEAEGELRRIGASVDPNLEITEICDRTLKSEGPALLFEHPKGSAVPLLGNLFGTPRRVALGMGEVSVGALRQVGVLLASLKEPEPPKGMRDAFEKVPLYRQVLHMAPKEVRNAPCQQEVLRGSDIDLGRYPIQTCWPGDAGPLITWPLVITRGPYKARQNLGIYRQQVIGRNKTIMRWLAHRGGALDFRDWQEARPGEPFPVAVALGADPATMLGAVTPVPDTLSEYGFAGLLRGARTEVTPCILSDLQVPASAEIVLEGFLYPGETAPEGPFGDHTGYYNEVESFPVFTIECITQRHSPIYH... | Cofactor: Binds 1 prenylated FMN (prenyl-FMN) per subunit.
Function: Catalyzes the decarboxylation of 3-octaprenyl-4-hydroxy benzoate to 2-octaprenylphenol, an intermediate step in ubiquinone biosynthesis.
Catalytic Activity: a 4-hydroxy-3-all-trans-polyprenylbenzoate + H(+) = a 2-all-trans-polyprenylphenol + CO2
Locat... |
Q74EU2 | MKNLNLYHFFDCKDRKITMYRLTEKGERIRDMFSDIAPRYDFLNRLLSFGVDRRWRRNAVKCIRWSEGGRVLDVATGTGDVALEIARQTPPSVAIVGVDFSEGMVALGRDKVAGSPYAGRITMEIAPCEAIPFPDDTFDSVTIAFGIRNVVDRSQGLSEMLRVLKPGGRAVILEFSTPRSRLFKRIYSFYFLRVLPVIGGLFSQFGAYKYLPDSVLEFPSQEEFKALMASVGFRDTAHRDQTFGIATIYTGEKGLK | Function: Methyltransferase required for the conversion of demethylmenaquinol (DMKH2) to menaquinol (MKH2) and the conversion of 2-polyprenyl-6-methoxy-1,4-benzoquinol (DDMQH2) to 2-polyprenyl-3-methyl-6-methoxy-1,4-benzoquinol (DMQH2).
Catalytic Activity: a 2-demethylmenaquinol + S-adenosyl-L-methionine = a menaquinol... |
A6WXQ0 | MTETARTTIDASEIEHFSRIAAEWWNPQGKFRPLHKFNPTRLAYIKEKICAKFNRDPNAPRPFDGLRLLDIGCGGGLLCEPMARLGATVIGADASTTNIEVAKIHAAQSGLDIDYRATTAEALAEAGEKFDVVLNMEVVEHVADVDLFMSATSEMVKPGGLMFVATINRTLKAYGLAIIGAEYVLRWLPRGTHQYEKLVRPEELEAALAKGGLRLIDKLGVTYNPLADSWSRSRDTDVNYMVLAERPA | Function: O-methyltransferase that catalyzes the 2 O-methylation steps in the ubiquinone biosynthetic pathway.
Catalytic Activity: a 3-demethylubiquinol + S-adenosyl-L-methionine = a ubiquinol + H(+) + S-adenosyl-L-homocysteine
Sequence Mass (Da): 27362
Sequence Length: 248
Pathway: Cofactor biosynthesis; ubiquinone bi... |
Q62M18 | MTNADPHELQKFSDLAHKWWDPNAEFKPLHDLNPVRLSWIDAHAHLPGKRVVDIGCGGGILSESMASLGAQVKGIDLATEALGVADLHSLESGVSVDYEAIAAEALAAREPGAYDVVTCMEMLEHVPSPANIVAACATLVKPGGWVFFSTLNRNLKSYLLAVIGAEYIAQMLPKGTHDYARFIRPSELARFVREAGLQMVEIKGIAYHPLAKRFALSNDTDVNYLVACRRGA | Function: O-methyltransferase that catalyzes the 2 O-methylation steps in the ubiquinone biosynthetic pathway.
Catalytic Activity: a 3-demethylubiquinol + S-adenosyl-L-methionine = a ubiquinol + H(+) + S-adenosyl-L-homocysteine
Sequence Mass (Da): 25206
Sequence Length: 232
Pathway: Cofactor biosynthesis; ubiquinone bi... |
Q46868 | MIDPKKIEQIARQVHESMPKGIREFGEDVEKKIRQTLQAQLTRLDLVSREEFDVQTQVLLRTREKLALLEQRISELENRSTEIKKQPDPETLPPTL | Function: Required for efficient ubiquinone (coenzyme Q) biosynthesis under aerobic conditions . UbiK is probably an accessory factor of Ubi enzymes and facilitates ubiquinone biosynthesis by acting as an assembly factor, a targeting factor, or both . Dispensable for ubiquinone biosynthesis under anaerobiosis .
Sequenc... |
Q2RMZ4 | MSEPLLRGLAAGDPPSATGPVTGSADKVADVLIVGGGLVGGTLACALAEKGVSVVVIDGEDPEALLAAGYDGRCSAIALACQRLLDTIGLWDLLGGESQPILDIRVVDGGSPLFLHYAQAEAQGPMGYMVENRLLRQAILTRLGRLPAATLLAPARMTALRRDLDGVSATLSDGQTVRARLVVGADGRRSQVRESAGIGIRTLGYGQTAIVLTVEHERSHRGCAVEHFLPAGPFAILPMPGNRSSLVWTERSDLVPGLLALPAEHFQAELERRFGDHLGWVRPVGPRFSYRLTLQAANRYVDHRLALVGDAAHGMHPVAG... | Function: Catalyzes the hydroxylation of two positions of the aromatic ring during ubiquinone biosynthesis.
Catalytic Activity: a 2-all-trans-polyprenylphenol + H(+) + NADPH + O2 = a 3-(all-trans-polyprenyl)benzene-1,2-diol + H2O + NADP(+)
Sequence Mass (Da): 45618
Sequence Length: 429
Pathway: Cofactor biosynthesis; u... |
A1KVW0 | MRLFTYPTPDLIHIKLKVKIRIHPPLHISSTAGFDIIAYLLQIVQTAFKPLQMPSEIIGIRLCKGYFMSLHSDILVVGAGPAGLSFAAELAGSGLKVTLIERSPLTVLQNPPYDGREIALTHFSREIMQRLGMWDKIPENEIYPLRDAKVLNGRSDYQLHFPQPTEARGEPADCLGYLISNHNIRRAAYEVVSQLDNVSILTDTVVKEVKTSDNEAQVILENGKILTARLLLAADSRFSQTRRQLGISSDMHDYSRTMFVCRMKHTLSNQHTAYECFHYGRTIALLPLEEHLTNTVITVDTDKINSVQNLSPEELAASVK... | Function: Catalyzes the hydroxylation of three positions of the aromatic ring during ubiquinone biosynthesis.
Catalytic Activity: a 2-all-trans-polyprenylphenol + H(+) + NADPH + O2 = a 3-(all-trans-polyprenyl)benzene-1,2-diol + H2O + NADP(+)
Sequence Mass (Da): 51325
Sequence Length: 461
Pathway: Cofactor biosynthesis;... |
Q9FPS0 | MVSRRGSETKAIVCVLTDRIRISNQWVSHLSFAGLLGVAGFVFAQQHGLFRNLNNLKLFSGREKDSGDDSFLVPGLQNLGNNCFLNVILQALASCKDFRSFLQWVLEDARGSLAGEQEEQLPLTFALSALLQELGTVGSRRSVSNPRKVMVTLTDYAKNFNLTSQQDAAEALLHLISSLQEEIVVCYRPSQSSNLSDILFSRNLRMLAPSEGLHGLMELKRWHKHLRGPFDGILGSTLMCRTCSSQISLEFQFFHTLPLSPLLHHGGYNIMSGCTLEHCLKKFLNTEKVENYFCYRCWHGAALKYLSVIGAAETEIEKLR... | Function: Recognizes and hydrolyzes the peptide bond at the C-terminal Gly of ubiquitin. Involved in the processing of poly-ubiquitin precursors as well as that of ubiquitinated proteins (By similarity).
Catalytic Activity: Thiol-dependent hydrolysis of ester, thioester, amide, peptide and isopeptide bonds formed by th... |
A6NNY8 | MCKDYVYDKDIEQIAKEEQGEALKLQASTSTEVSHQQCSVPGLGEKFPTWETTKPELELLGHNPRRRRITSSFTIGLRGLINLGNTCFMNCIVQALTHTPILRDFFLSDRHRCEMPSPELCLVCEMSSLFRELYSGNPSPHVPYKLLHLVWIHARHLAGYRQQDAHEFLIAALDVLHRHCKGDDVGKAANNPNHCNCIIDQIFTGGLQSDVTCQACHGVSTTIDPCWDISLDLPGSCTSFWPMSPGRESSVNGESHIPGITTLTDCLRRFTRPEHLGSSAKIKCGSCQSYQESTKQLTMNKLPVVACFHFKRFEHSAKQR... | Function: Deubiquitinase involved in innate antiviral immunity by mediating deubiquitination of CGAS and RIGI . Negatively regulates RIGI by mediating 'Lys-63'-linked deubiquitination of RIGI, inhibiting type I interferon signaling . Also regulates 'Lys-63'-linked ubiquitination level of MDA5/IFIH1 . Acts as a positive... |
Q9HBJ7 | MISLKVCGFIQIWSQKTGMTKLKEALIETVQRQKEIKLVVTFKSGKFIRIFQLSNNIRSVVLRHCKKRQSHLRLTLKNNVFLFIDKLSYRDAKQLNMFLDIIHQNKSQQPMKSDDDWSVFESRNMLKEIDKTSFYSICNKPSYQKMPLFMSKSPTHVKKGILENQGGKGQNTLSSDVQTNEDILKEDNPVPNKKYKTDSLKYIQSNRKNPSSLEDLEKDRDLKLGPSFNTNCNGNPNLDETVLATQTLNAKNGLTSPLEPEHSQGDPRCNKAQVPLDSHSQQLQQGFPNLGNTCYMNAVLQSLFAIPSFADDLLTQGVPW... | Function: Deubiquitinase involved in innate antiviral immunity by mediating 'Lys-48'-linked deubiquitination of CGAS, thereby promoting its stabilization.
Catalytic Activity: Thiol-dependent hydrolysis of ester, thioester, amide, peptide and isopeptide bonds formed by the C-terminal Gly of ubiquitin (a 76-residue prote... |
Q9ES63 | MAHLKINGLVQIRSTNRSKHTRASQWKEAVIEIVERKQKVNLVVSFKLEERRRVFQLGDNVTGVVVSGELGLYHLDLTLRDDTSLLIDKLSSADVEHLKSFLDSSTPCESQQPMEPMSSQDDLESSDPFCGEHQEAACGSLNTTPESGTPLSRKMPLSMSNTTGGQKRGEKQGRKRKTEPSSSSAEVNKDIPKENTPDQKKKSRRYYSRNRGGKAEKAVTLREQEKRSNWKLEPAFNSKSYGRANLDGTILPIATCSDDRDVSIFGLEIITHNGVQSLPDPYLNQLKREGFPNLGNTCYMNSILQSVFGIPTFAKDLLTQ... | Function: Deubiquitinase involved in innate antiviral immunity by mediating 'Lys-48'-linked deubiquitination of CGAS, thereby promoting its stabilization.
Catalytic Activity: Thiol-dependent hydrolysis of ester, thioester, amide, peptide and isopeptide bonds formed by the C-terminal Gly of ubiquitin (a 76-residue prote... |
Q8W4N3 | MGKKAKKKARAPTKEIQTMEISKKVSEEPPSQAGEIAEGDVKAVKETQACVHFDKALNLEKVLDKIKSSRQIKCAECNEGVYGKRGTKAKGSKGKKDFSSSDPKSNNKAIWLCLECGCYVCGGVGLPNGPQSHVLRHSRVTRHRLVIQWENPQLRWCFPCQLLLPVEKEDNGEKKDVLSEVVKLIKGRSLNNLASSDIEDQCSGSGSITSDIKLEGAVTSDIEARDGYVVRGLVNLGNTCFFNSIMQNLLSLDRLRDHFLKENGSGVGGPLASSLRKLFTETKPEAGLKSVINPRAFFGSFCSKAPQFRGYDQHDSHELL... | Function: Recognizes and hydrolyzes the peptide bond at the C-terminal Gly of ubiquitin. Involved in the processing of poly-ubiquitin precursors as well as that of ubiquitinated proteins. Is involved in resistance to the arginine analog canavanine (CAN).
Catalytic Activity: Thiol-dependent hydrolysis of ester, thioeste... |
O57429 | MAARMAPTPRSSKVVQGLTGLRNLGNTCFMNSILQCLSNTKELRDYCLQNQYLRDLNNNSRMRTALMSEFAKLIQLLWTSSPNDSVSPSEFKTQIQRYAPRFVGYNQQDAQEFLRFLLDGLHGEVNRVLVRPRANADTLDHLPDDEKSRQMWRRYQEREDSRVSDLFVGQLKSSLTCSECGYCSTAFDPFWDLSLPIPKKGYGEVTLMDCLRLFTKEDVLDGDEKPTCCRCKARTRCTKKFSIQKFPKILVLHLKRFSEARIRASKLTTFVNFPLKDLDLREFASQSCNHAVYNLYAVSNHSGTTMGGHYTAYCKSPISS... | Function: Hydrolase that deubiquitinates polyubiquitinated target proteins such as MDM2, MDM4 and CCND1. Possesses both ubiquitin-specific peptidase and isopeptidase activities. May play a role in the regulation of the circadian clock.
Catalytic Activity: Thiol-dependent hydrolysis of ester, thioester, amide, peptide a... |
Q8IQ27 | MMLDIKKTRGFHKIPQASKLQSTTKTSSVVATSASSQNEVPSPGGSAGSKVGATNPVRAANQRFFLVSSYKDPTFLKAECDLAHAHVTTSKVKTTLQPHRRSRAGEDSRNNNYNTSRAPTLINMRRPSLFNGNQQPTTTNSTTINNTTSRNTTSNTSNGVLKYSVRSTTATATSTSTRNYGKLKPLNNNQTTAGVAMMNGHTNNNNNNTRNSSNINNGGNNNMQRQQQQHDDISFIDSDDPPATGGPEAGISTTKTSICYFKPITPPLQLRHEQNQVQQQEEQPQPSSSKSASHRYPRPKSTIIASAHSNFAASFEKFSG... | Function: Hydrolase that deubiquitinates polyubiquitinated target proteins . Required for preventing the activation of the Toll signaling cascades under unchallenged conditions . Essential for bodily calcium homeostasis .
Catalytic Activity: Thiol-dependent hydrolysis of ester, thioester, amide, peptide and isopeptide ... |
O75604 | MSQLSSTLKRYTESARYTDAHYAKSGYGAYTPSSYGANLAASLLEKEKLGFKPVPTSSFLTRPRTYGPSSLLDYDRGRPLLRPDITGGGKRAESQTRGTERPLGSGLSGGSGFPYGVTNNCLSYLPINAYDQGVTLTQKLDSQSDLARDFSSLRTSDSYRIDPRNLGRSPMLARTRKELCTLQGLYQTASCPEYLVDYLENYGRKGSASQVPSQAPPSRVPEIISPTYRPIGRYTLWETGKGQAPGPSRSSSPGRDGMNSKSAQGLAGLRNLGNTCFMNSILQCLSNTRELRDYCLQRLYMRDLHHGSNAHTALVEEFAK... | Function: Hydrolase that deubiquitinates polyubiquitinated target proteins such as MDM2, MDM4 and CCND1 . Isoform 1 and isoform 4 possess both ubiquitin-specific peptidase and isopeptidase activities (By similarity). Deubiquitinates MDM2 without reversing MDM2-mediated p53/TP53 ubiquitination and thus indirectly promot... |
O88623 | MSQLSSTLKRYTESSRYTDAPYAKPGYGTYTPSSYGANLAASFLEKEKLGFKPVSPTSFLPRPRTYGPSSILDCDRGRPLLRSDIIGSSKRSESQTRGNERPSGSGLNGGSGFSYGVSSNSLSYLPMNARDQGVTLSQKKSNSQSDLARDFSSLRTSDGYRTSDGYRTSEGFRIDPGNLGRSPMLARTRKELCALQGLYQAASRSEYLTDYLENYGRKGSAPQVLTQAPPPSRVPEVLSPTYRPSGRYTLWEKSKGQASGPSRSSSPGRDTMNSKSAQGLAGLRNLGNTCFMNSILQCLSNTRELRDYCLQRLYMRDLGH... | Function: Hydrolase that deubiquitinates polyubiquitinated target proteins such as MDM2, MDM4 and CCND1 (By similarity). Isoform 1 and isoform 2 possess both ubiquitin-specific peptidase and isopeptidase activities (By similarity). Deubiquitinates MDM2 without reversing MDM2-mediated p53/TP53 ubiquitination and thus in... |
Q04228 | MPVVNHEDSEFHLSHTEEDKLNEFQVITNFPPEDLPDVVRLLRNHGWQLEPALSRYFDGEWKGEPDQMGEPTQTSTPMAETLVPPALGPRPLLFTASLPVVRPLPANFRNDFRTIGLNGRSNTVWSMFESFSYDGNPFLFILLLIPRIINRLSATIFTFFCTLLSLHSISGGGNSGKPKISKVPKAPTRETHIPLAEILGDTKDKDAFCELKSFKPDISFNEALRIAKEEFKFMLLILVGDTYDTDTDTVDVNSKLLLEKILLNKKTLQYLRKIDNDLIIYLKCVHELEPWLVARQLGVRNTPEIFLIANVANKASHSET... | Function: Integral endoplasmic reticulum membrane protein that coordinates the assembly of the ER-associated protein degradation (ERAD) machinery at the ER membrane. Mediates binding of CDC48 to the E3 ubiquitin ligases SSM4/DOA10 and HRD1, and to ERAD substrates. Component of the DOA10 ubiquitin ligase complex, which ... |
P55916 | MVGLKPSDVPPTMAVKFLGAGTAACFADLVTFPLDTAKVRLQIQGENQAVQTARLVQYRGVLGTILTMVRTEGPCSPYNGLVAGLQRQMSFASIRIGLYDSVKQVYTPKGADNSSLTTRILAGCTTGAMAVTCAQPTDVVKVRFQASIHLGPSRSDRKYSGTMDAYRTIAREEGVRGLWKGTLPNIMRNAIVNCAEVVTYDILKEKLLDYHLLTDNFPCHFVSAFGAGFCATVVASPVDVVKTRYMNSPPGQYFSPLDCMIKMVAQEGPTAFYKGFTPSFLRLGSWNVVMFVTYEQLKRALMKVQMLRESPF | Function: Putative transmembrane transporter that plays a role in mitochondrial metabolism via an as yet unclear mechanism . Originally, this mitochondrial protein was thought to act as a proton transmembrane transporter from the mitochondrial intermembrane space into the matrix, causing proton leaks through the inner ... |
Q9VMK1 | MDKAERDYWHLRSLEIEEEPRFPPTNVADPLTARNLFQLYVNTFIGANLAESCVFPLDVAKTRMQVDGEQAKKTGKAMPTFRATLTNMIRVEGFKSLYAGFSAMVTRNFIFNSLRVVLYDVFRRPFLYQNERNEEVLKIYMALGCSFTAGCIAQALANPFDIVKVRMQTEGRRRQLGYDVRVNSMVQAFVDIYRRGGLPSMWKGVGPSCMRACLMTTGDVGSYDISKRTFKRLLDLEEGLPLRFVSSMCAGLTASVLSTPADVIKSRMMNQPVDESGKNLYYKNSLDCVRKLVREEGVLTLYKGLMPTWFRLGPFSVLFW... | Function: Mitochondrial protein that is likely to be responsible for thermogenic respiration. Likely to function in mitochondrial uncoupling i.e. creating mitochondrial proton leaks across the inner mitochondrial membrane and can therefore dissipate the mitochondrial proton gradient and convert the energy of substrate ... |
O95847 | MSVPEEEERLLPLTQRWPRASKFLLSGCAATVAELATFPLDLTKTRLQMQGEAALARLGDGARESAPYRGMVRTALGIIEEEGFLKLWQGVTPAIYRHVVYSGGRMVTYEHLREVVFGKSEDEHYPLWKSVIGGMMAGVIGQFLANPTDLVKVQMQMEGKRKLEGKPLRFRGVHHAFAKILAEGGIRGLWAGWVPNIQRAALVNMGDLTTYDTVKHYLVLNTPLEDNIMTHGLSSLCSGLVASILGTPADVIKSRIMNQPRDKQGRGLLYKSSTDCLIQAVQGEGFMSLYKGFLPSWLRMTPWSMVFWLTYEKIREMSGV... | Function: Facilitates proton transport across the inner mitochondrial membrane and may dissipate excessive proton gradient associated with oxidative and metabolic stress at neuronal synapses. Regulates glutamate-induced proton conductance in astrocytes, shifting the energy metabolism toward aerobic glycolysis and lacta... |
Q9D6D0 | MPIAEEEKLLPLTQRWPRTSKFLLSGCAATVAELATFPLDLTKTRLQMQGEAALARLGDGAVDSAPYRGMVRTALGIVQEEGFLKLWQGVTPAIYRHVVYSGGRMVTYEHLREVVFGKSEDKHYPLWKSVIGGMMAGVIGQFLANPTDLVKVQMQMEGKRRLEGKPLRFRGVHHAFAKILAEGGIRGLWAGWIPNIQRAALVNMGDLTTYDTVKHYLVLNTPLEDNISTHGLSSLCSGLVASILGTPADVIKSRIMNQPRDKQGRGLLYKSSADCLIQAVQGEGFLSLYKGFLPSWLRMTPWSMVFWLTYEKIREMSGVS... | Function: Facilitates proton transport across the inner mitochondrial membrane and may dissipate excessive proton gradient associated with oxidative and metabolic stress at neuronal synapses. Regulates glutamate-induced proton conductance in astrocytes, shifting the energy metabolism toward aerobic glycolysis and lacta... |
O95258 | MGIFPGIILIFLRVKFATAAVIVSGHQKSTTVSHEMSGLNWKPFVYGGLASIVAEFGTFPVDLTKTRLQVQGQSIDARFKEIKYRGMFHALFRICKEEGVLALYSGIAPALLRQASYGTIKIGIYQSLKRLFVERLEDETLLINMICGVVSGVISSTIANPTDVLKIRMQAQGSLFQGSMIGSFIDIYQQEGTRGLWRGVVPTAQRAAIVVGVELPVYDITKKHLILSGMMGDTILTHFVSSFTCGLAGALASNPVDVVRTRMMNQRAIVGHVDLYKGTVDGILKMWKHEGFFALYKGFWPNWLRLGPWNIIFFITYEQL... | Function: Transports inorganic anions (sulfate, sulfite, thiosulfate and phosphate) and, to a lesser extent, a variety of dicarboxylates (e.g. malonate, malate and citramalate) and, even more so, aspartate and glutamate and tricarboxylates . May catalyze the export of sulfite and thiosulfate (the hydrogen sulfide degra... |
Q55BF4 | MSVNLNNNKNNKNKVAIGFISGSLASICATTVTNPIELVKTRLQLQGELQLSQRIYNGVWDAFKQIYKTEGIRGLQSGLIPAYFSQATMQGIRLGSFDLISNALGAKPNQDYFFLKNLLAGATAGAIGAAAGSPFDLVKVRMQAANMYKNDPQFVGYSSSFAAFKQIIQKEGFKGLTRGMLTSAQRTAVGSAIQLSTYGSCKNLVLNFVDDGIYAYIISSMVAGFIVTFGMNPFDVARTRLYFQGKGNSHGEIYKGLMDCVYKTVKKEGFGAVYKGFWAHYLRLGPHTILTLVFWEQFKKLFSGEL | Function: Mitochondrial solute carriers shuttle metabolites, nucleotides, and cofactors through the mitochondrial inner membrane. Transports oxaloacetate and sulfate (By similarity).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 33605
Sequence Length: 306
Subcellular Location: Mitochondrion inner m... |
O53732 | MTVETSQTPSAAIDSDRWPAVAKVPRGPLAAASAAIANRLLRRTATHLPLRLVYSDGTATGAADPRAPSLFIHRPDALARRIGRHGLIGFGESYMAGEWSSKELTRVLTVLAGSVDELVPRSLHWLRPITPTFRPSWPDHSRDQARRNIAVHYDLSNDLFAAFLDETMTYSCAMFTDLLAQPTPAWTELAAAQRRKIDRLLDVAGVQQGSHVLEIGTGWGELCIRAAARGAHIRSVTLSVEQQRLARQRVAAAGFGHRVEIDLCDYRDVDGQYDSVVSVEMIEAVGYRSWPRYFAALEQLVRPGGPVAIQAITMPHHRML... | Function: Involved in the biosynthesis of the tuberculostearic acid (10-methylstearic-acid or TSA), a constituent lipid of the mycobacterial cell wall. Catalyzes the transfer of the methyl group from S-adenosyl-L-methionine (SAM) to the double bond of oleic acid in phosphatidylethanolamine or phosphatidylcholine to pro... |
Q92890 | MFSFNMFDHPIPRVFQNRFSTQYRCFSVSMLAGPNDRSDVEKGGKIIMPPSALDQLSRLNITYPMLFKLTNKNSDRMTHCGVLEFVADEGICYLPHWMMQNLLLEEGGLVQVESVNLQVATYSKFQPQSPDFLDITNPKAVLENALRNFACLTTGDVIAINYNEKIYELRVMETKPDKAVSIIECDMNVDFDAPLGYKEPERQVQHEESTEGEADHSGYAGELGFRAFSGSGNRLDGKKKGVEPSPSPIKPGDIKRGIPNYEFKLGKITFIRNSRPLVKKVEEDEAGGRFVAFSGEGQSLRKKGRKP | Function: Essential component of the ubiquitin-dependent proteolytic pathway which degrades ubiquitin fusion proteins. The ternary complex containing UFD1, VCP and NPLOC4 binds ubiquitinated proteins and is necessary for the export of misfolded proteins from the ER to the cytoplasm, where they are degraded by the prote... |
Q9HE05 | MSDLEKIRLKRLAKLQQTNSEANSSKEPKESNIAPEPKKPDLKKRFIGSKATTSNSEQKEISPPVTSGAPKHRLFSKDEWMHFITCQALNITLSETDSSKYYLEGFKKDLEEEGSPLLFNENNVDSALLSRLSTTGNNTFSYLLQSWSFLYQYKKRLPKDENQDFKIHYLSLLKSLLVSYAGIVVMLPDTFNSETIDLAEVLIGAEGIPLEFLSEFVQRFEHENLDELFIPVLESLSLKIGLMNVDTVQMNVMQIILQLVSLKPIALLLPKLPSWNPTNNAGEIEYKTFLGRISSLSVFTQDVASRYFSNSTERSAQNIS... | Function: E4 ubiquitin chain-elongation enzyme specifically involved in polyubiquitin chain assembly. Binds to cdc48 and elongates mono- and diubiquitinated ERAD substrates presented by the ufd1-npl4-cdc48 (UNC) AAA ATPase complex to a chain length of 4 to 6 ubiquitin moieties. Delivers these polyubiquitinated substrat... |
P54860 | MTAIEDILQITTDPSDTRGYSLLKSEEVPQGSTLGVDFIDTLLLYQLTENEKLDKPFEYLNDCFRRNQQQKRITKNKPNAESLHSTFQEIDRLVIGYGVVALQIENFCMNGAFINYITGIVSNVNSYTDFLSQIIQRAILEGTALDLLNAVFPTLLEYCNKHVSHFDLNESVIYNNVLTIFELFVTFKPIAEIFTKIDGFFADYSCKPQDFERKTILGPILSLSPIEAAVAIRNYGDNLLRSKQQTAMIHESLQAEHKVVIDRLFFIVDKLVRGSLNSRTDMISYFAHIANKNHLRRADHPPFKELSSNGFMSNITLLLV... | Function: E4 ubiquitin chain-elongation enzyme specifically involved in polyubiquitin chain assembly. Binds to CDC48 and elongates mono- and diubiquitinated ERAD substrates presented by the UFD1-NPL4-CDC48/p97 (UNC) AAA ATPase complex to a chain length of 4 to 6 ubiquitin moieties. Delivers these polyubiquitinated subs... |
G5EES6 | MADDGLGDVPMETESMPQYTISHVIEAHKSDTKALAVTQGGCLISGGRDETVKFWAKKGKQYTKTHAFEQPKGITVNSIAYAELADGWRLFVGRRDGTIAVFGPSQAEPYAIFNEHKQNVCCLHINEKATHMLSGSWDSNVIIWPITELNSSSFTFQTIVCPGHTLSVWALASFPDLPNTYLSASADKTIRMWFGDTTLSVFKGHTDVVRALVVLSSSHFLSAGNDGHIIHWDVASASILRKFATQAHEFIYSMTLSDSHILTTGEDGTLEFWAIDGGKDGNLAIVSEAVIQLPTTNTWDAKVLLNSDIAVAGSDGRIYI... | Function: Plays a role in protein ubiquitination, sorting and degradation through its association with cdc-48.1 and/or cdc-48.2.
Sequence Mass (Da): 93915
Sequence Length: 860
Domain: The PUL domain mediates the interaction with cdc-48.1 and/or cdc-48.2 C-terminus.
Subcellular Location: Cytoplasm
|
O94531 | MTSRTNEFFGLTKNGDIDAANIPLKRISYTDPFLAEGYRIHETIVNLLVFLKKIRGAYLKDRTFSNVQRLSKPLMECSLEELSKLELDEVQRDEIEHEVSSAISSCIHQIAKLQEIVKEQQSQIPKKSGWLQGLRDPSKLSKKETLVAHHSSVLWYLQSELSDVSSVLYHLQDLRLKRGQEKRNIASDFLTKNPTDENSAVEIPESELQTFFTQQQLQELEQENDVLLQEFEHTMERLRDTGKSLADITRLQSEISAQLSIQSSAAEKLYDDALNVMDSLSGGNQQLIKAKSRSSRTARLLFCIFTVMGLLLLSLDRIV | Function: Syntaxin required for targeting and fusion of Golgi-derived retrograde transport vesicles with the ER.
Location Topology: Single-pass type IV membrane protein
Sequence Mass (Da): 36371
Sequence Length: 319
Subcellular Location: Endoplasmic reticulum membrane
|
P41834 | MMSDLTPIFRKYVAVIDDARNEQNGIDDHVERKQEDFGNSNETCEMFRDSFIKECARLLKFLVELNKVIKQIEKNYLDDFNMSDAEKDEFDMECRLQIQQYFKKFEFLENYEMERHNLSLKRFQSKSHRWSKILSNKNDNTKHVIHPQDIENGVYEFRLGVLRCLNLWIKYVSSKFTTIQQERLILENKMNFNSTPMPTLSNNADDFSADAIDISVSQSAPVETVQDEVKHYEETISKLTQEQLQVLETEHSELLNQKNEQLKKVETINKTILDIVNIQNELSNHLTVQSQNINLMLNNQDDIELNIKKGNKELRKAKRA... | Function: Syntaxin required for targeting and fusion of Golgi-derived retrograde transport vesicles with the ER.
Location Topology: Single-pass type IV membrane protein
Sequence Mass (Da): 40539
Sequence Length: 346
Subcellular Location: Endoplasmic reticulum membrane
|
Q8UBB7 | MAQIDIRQVRKSYGKTPTLHGVDLSFDSGEFVVILGPSGCGKSTLLRMIAGLEEITSGEIAIGGRVVNTLEPRERGCAMVFQNYALYPHMSVAANIGYALKVAGVPKAERQRRIEETAKIVGLSDYLERKPAALSGGQRQRVAMARAIIREPAVFLFDEPLSNLDAKLRVSMRAEIRKLHQRLSATSIFVTHDQVEAMTLADRLVVMNKGNVEQVGHPLDIYHRPASTFVASFIGSPAMNLFTTKVEVETPAVILSGTPVKLFPETALELRGRNVTVGIRPEQCVVSMDGPGVPAIVDFVEELGSGRIVHADIAGETFSA... | Function: Part of the ABC transporter complex UgpBAEC involved in sn-glycerol-3-phosphate (G3P) import. Responsible for energy coupling to the transport system.
Catalytic Activity: ATP + H2O + sn-glycerol 3-phosphate(out) = ADP + H(+) + phosphate + sn-glycerol 3-phosphate(in)
Location Topology: Peripheral membrane prot... |
Q2K4V4 | MAPISIRDVKKSYGKHPVVHGVDLEIQSGEFIVILGPSGCGKSTLLRMIAGLEEITGGEIAIDGRVVNQMEPRERGCAMVFQNYALYPHMTVAENIGYALKVAGVAKTERSRRIAEVAKALSLEPFLDRRPAALSGGQRQRVAMGRAMIREPKVFLFDEPLSNLDAKLRIAMRAEIRRLHRRLGATSIFVTHDQTEAMTLADRLVVMNGGRVEQVGTPEEVYHHPVSRFVAGFVGTPAMNLLEGTINDEGVFVYDQSRKIALPRERAAALKGKRVVLGMRAEAARLVVPDAPGALVATADFIEELGASRVVHADFDGLPF... | Function: Part of the ABC transporter complex UgpBAEC involved in sn-glycerol-3-phosphate (G3P) import. Responsible for energy coupling to the transport system.
Catalytic Activity: ATP + H2O + sn-glycerol 3-phosphate(out) = ADP + H(+) + phosphate + sn-glycerol 3-phosphate(in)
Location Topology: Peripheral membrane prot... |
P10908 | MSNWPYPRIVAHRGGGKLAPENTLASIDVGAKYGHKMIEFDAKLSKDGEIFLLHDDNLERTSNGWGVAGELNWQDLLRVDAGSWYSKMFKGEPLPLLSQVAERCREHGMMANIEIKPTTGTGPLTGKMVALAARELWAGMTPPLLSSFEIDALEAAQQAAPELPRGLLLDEWRDDWRELTARLGCVSIHLNHKLLNKARVMQLKDAGLRILVYTVNKPQRAAELLRWGVDCICTDAIDVIGPNFTAQ | Function: Glycerophosphodiester phosphodiesterase hydrolyzes glycerophosphodiesters into glycerol-3-phosphate (G3P) and the corresponding alcohol.
Catalytic Activity: a sn-glycero-3-phosphodiester + H2O = an alcohol + H(+) + sn-glycerol 3-phosphate
Sequence Mass (Da): 27410
Sequence Length: 247
Subcellular Location: Cy... |
P16739 | MCSVLAIALVVALLGDMHPGVKSSTTSAVTSPSNTTVTSTTSISTSNNVTSAVTTTVQTSTSSASTSVIATTQKEGHLYTVNCEASYSHDQVSLNATCKVILLNNTKNPDILSVTCYARTDCKGPFTQVGYLSAFPPDNEGKLHLSYNATAQELLISGLRPQETTEYTCSFFSWGRHHNATWDLFTYPIYAVYGTRLNATTMRVRVLLQEHEHCLLNGSSLYHPNSTVHLHQGNQLIPPWNISNVTYNGQRLREFVFYLNGTYTVVRLHVQIAGRSFTTTYVFIKSDPLFEDRLLAYGVLAFLVFMVIILLYVTYMLARR... | Function: Serves as a receptor for the Fc part of human IgG. May thus be involved in interfering with host Ig-mediated immune responses.
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 38709
Sequence Length: 345
Subcellular Location: Virion membrane
|
Q6SWB9 | MLFRYITFHREKVLYLTAACIFGVYISLHDACIPVVGKIGTNVTLNAVDVLPPRDQVRWSYGPGGQGYMLCIFTGTSTTTFNNTRFNFSCLSNYSLLLINVTTQYSTTYRTMTSLDHWLHQRHNHGSRWTLDTCYNLTVNENGTFPTTTTKKPTTTTRTTTTTTQRTTTTRTTTTAKKTTISTTHHKHPSPKKSTTPNSHVEHHVGFEATAAETPLQPSPQHQHLATHALWVLAVVIVIIIIIIFYFRIPQKLWLLWQHDKHGIVLIPQTDL | Function: Plays a role in the modulation of host immune response by modulating T-cell function. Interacts with host PTPRC/CD45 and thereby reduces host TCR signaling and T-cell proliferation.
PTM: Glycosylated.
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 30881
Sequence Length: 272
Subcell... |
G8G2V6 | MVFFKDLFIFKSLIKGSLYSGHMKKKLLNYLPLFALMLFTVSMMAQTAPDEDTNSSIACPSSGVFQNNTTRDVDIANPDNVGTVDDRTCYADYYETSVYGETWGAYNITFNSNHWDAPNTLQPRIERSLSRSQETGVGSYARFTGTLRILEVGNTGTFGSTGSYLMQAKGKHTGGGGSNDPAICLYLARPVYGPDANGNQVQVSFDIWREQINFRGGSGAAGRTEVFLRNVLKDEIIDIELEVGFRQDPNDPNLKIHYSDAIIGGQVFNWNIPEPERGRESGIRYGVYRVKGGRAQMRWANTTYQKVEVVDNSTIPAADI... | Function: Ulvan lyase involved in ulvan degradation . Ulvan is the main polysaccharide component of the Ulvales (green seaweed) cell wall. It is composed of disaccharide building blocks comprising 3-sulfated rhamnose (Rha3S) linked to D-glucuronic acid (GlcA), L-iduronic acid (IduA), or D-xylose (Xyl). Ulvan lyase cata... |
A0A084JZF2 | MRKLKYNTTRVILMIAFISLSACSSEDAMIEEEQVIPDPDPVAQTDEDTGPVVDCTNQGTNPTRDTDIPNPRNIGDIDDRSCYANYSESSILGKFWGIYNITDGSNHMDAPNTLQPRIERSLSRSQATGAGSYARFRGVLRILEVGDTGTFSSSGSYFMQAKGKHTGGGGSPDPAICLYRAHPVYGDDGNGNQVQVSFDIWREQINFRGGSGSAGRTEVFLKNVLKNEQIDIELEVGFRDDPNNPGQTLHYADAKIGGEEFNWNIPEPERGIESGIRYGAYRVKGGRAQFRWANTSYTKDEVN | Function: Ulvan lyase involved in ulvan degradation . Ulvan is the main polysaccharide component of the Ulvales (green seaweed) cell wall. It is composed of disaccharide building blocks comprising 3-sulfated rhamnose (Rha3S) linked to D-glucuronic acid (GlcA), L-iduronic acid (IduA), or D-xylose (Xyl). Ulvan lyase cata... |
P39301 | MEILYNIFTVFFNQVMTNAPLLLGIVTCLGYILLRKSVSVIIKGTIKTIIGFMLLQAGSGILTSTFKPVVAKMSEVYGINGAISDTYASMMATIDRMGDAYSWVGYAVLLALALNICYVLLRRITGIRTIMLTGHIMFQQAGLIAVTLFIFGYSMWTTIICTAILVSLYWGITSNMMYKPTQEVTDGCGFSIGHQQQFASWIAYKVAPFLGKKEESVEDLKLPGWLNIFHDNIVSTAIVMTIFFGAILLSFGIDTVQAMAGKVHWTVYILQTGFSFAVAIFIITQGVRMFVAELSEAFNGISQRLIPGAVLAIDCAAIYS... | Function: The phosphoenolpyruvate-dependent sugar phosphotransferase system (sugar PTS), a major carbohydrate active transport system, catalyzes the phosphorylation of incoming sugar substrates concomitantly with their translocation across the cell membrane. The enzyme II UlaABC PTS system is involved in ascorbate tran... |
P75291 | MLNKIKLQQKRKLIIGWSVFALINLVVILLTVLLRAGLPNLVSKGVTPFSAQAFGDAFIFLITRVYLDNFLRQPALLLGVITLIGYLALGRGGVQSVVGALKTVIGFILLSIGSGVLVSTARPVFDTIKGLGGTGVVLLDPYFSLASANDFFTNSFLNNDYVSLIAFSLLVGFIVNIIFVGLKRWTNTNSIMVTGHVMLQQAAVVTTLFYIVLFRQIPLLGTGIAYGAQAGLVIISGIFLGVYWSTASTGTYLVTNKVTNNAGFSIGHQQMLGIMTVAKLGKYFGDKNDSAEHKKLPKALKIFEDNIFTQTIIILSLFVV... | Function: The phosphoenolpyruvate-dependent sugar phosphotransferase system (sugar PTS), a major carbohydrate active transport system, catalyzes the phosphorylation of incoming sugar substrates concomitantly with their translocation across the cell membrane. The enzyme II UlaABC PTS system is involved in ascorbate tran... |
Q8FAJ1 | MTVRILAVCGNGQGSSMIMKMKVDQFLTQSNIDHTVNSCAVGEYKSELSGADIIIASTHIAGEITVTGNKYVVGVRNMLSPADFGPKLLEVIKAHFPQDVK | Function: The phosphoenolpyruvate-dependent sugar phosphotransferase system (sugar PTS), a major carbohydrate active transport system, catalyzes the phosphorylation of incoming sugar substrates concomitantly with their translocation across the cell membrane. The enzyme II UlaABC PTS system is involved in ascorbate tran... |
Q9EXD8 | MENKNLHIIAACGNGMGTSMLIKIKVEKIMKELGYTAKVEALSMGQTKGMEHSADIIISSIHLTSEFNPNAKAKIVGVLNLMDENEIKQALSKVL | Function: The phosphoenolpyruvate-dependent sugar phosphotransferase system (sugar PTS), a major carbohydrate active transport system, catalyzes the phosphorylation of incoming sugar substrates concomitantly with their translocation across the cell membrane. The enzyme II UlaABC PTS system is involved in ascorbate tran... |
Subsets and Splits
No community queries yet
The top public SQL queries from the community will appear here once available.