ids stringlengths 6 10 | seqs stringlengths 11 1.02k | texts stringlengths 108 11.1k |
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P33274 | MSQLSLSWLGLGPEVAFPWQTLLLFGASWILAQILTQIYAAYRNFRRLRGFPQPPKRNWLMGHVGMVTPTEQGLKELTRLVGTYPQGFLMWIGPMVPVITLCHSDIVRSILNASAAVALKDVIFYTILKPWLGDGLLVSAGDKWSRHRRMLTPAFHFNILKPYVKIFNDSTNIMHAKWKRLISEGSSRLDMFEHVSLMTLDSLQKCVFSFDSNCQEKSSEYIAAILELSALVAKRHQQPLLFMDLLYNLTPDGMRFHKACNLVHEFTDAVIRERRRTLPDQGLDEFLKSKAKSKTLDFIDVLLLTKDEDGKELSDEDIRAEADTFMFEGHDTTASGLSWILYNLANDPEYQERCRQEVQELLRDRDPEEIEWDDLAQLPFLTMCIKESLRLHPPVTVISRCCTQDILLPDGRTIPKGIICLISIFGIHHNPSVWPDPEVYNPFRFDPENIKDSSPLAFIPFSAGPRNCIGQTFAMSEMKVALALTLLRFRLLPDDKEPRRQPELILRAEGGLWLRVEPLTAGAQ | Function: A cytochrome P450 monooxygenase involved in the metabolism of arachidonic acid and its oxygenated derivatives . Mechanistically, uses molecular oxygen inserting one oxygen atom into a substrate, and reducing the second into a water molecule, with two electrons provided by NADPH via cytochrome P450 reductase (CPR; NADPH-ferrihemoprotein reductase). Participates in the conversion of arachidonic acid to omega-hydroxyeicosatetraenoic acid (20-HETE), a signaling molecule acting both as vasoconstrictive and natriuretic with overall effect on arterial blood pressure . May play a role in the oxidative inactivation of eicosanoids, including both pro-inflammatory and anti-inflammatory mediators such as leukotriene B4 (LTB4), lipoxin A4 (LXA4), and several HETEs .
Catalytic Activity: (5Z,8Z,11Z,14Z)-eicosatetraenoate + O2 + reduced [NADPH--hemoprotein reductase] = 20-hydroxy-(5Z,8Z,11Z,14Z)-eicosatetraenoate + H(+) + H2O + oxidized [NADPH--hemoprotein reductase]
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 59868
Sequence Length: 524
Subcellular Location: Endoplasmic reticulum membrane
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P78329 | MSQLSLSWLGLWPVAASPWLLLLLVGASWLLAHVLAWTYAFYDNCRRLRCFPQPPRRNWFWGHQGMVNPTEEGMRVLTQLVATYPQGFKVWMGPISPLLSLCHPDIIRSVINASAAIAPKDKFFYSFLEPWLGDGLLLSAGDKWSRHRRMLTPAFHFNILKPYMKIFNESVNIMHAKWQLLASEGSACLDMFEHISLMTLDSLQKCVFSFDSHCQEKPSEYIAAILELSALVSKRHHEILLHIDFLYYLTPDGQRFRRACRLVHDFTDAVIQERRRTLPSQGVDDFLQAKAKSKTLDFIDVLLLSKDEDGKKLSDEDIRAEADTFMFEGHDTTASGLSWVLYHLAKHPEYQERCRQEVQELLKDREPKEIEWDDLAHLPFLTMCMKESLRLHPPVPVISRHVTQDIVLPDGRVIPKGIICLISVFGTHHNPAVWPDPEVYDPFRFDPENIKERSPLAFIPFSAGPRNCIGQTFAMAEMKVVLALTLLRFRVLPDHTEPRRKPELVLRAEGGLWLRVEPLS | Function: A cytochrome P450 monooxygenase involved in the metabolism of various endogenous substrates, including fatty acids, eicosanoids and vitamins . Mechanistically, uses molecular oxygen inserting one oxygen atom into a substrate, and reducing the second into a water molecule, with two electrons provided by NADPH via cytochrome P450 reductase (CPR; NADPH-ferrihemoprotein reductase). Catalyzes predominantly the oxidation of the terminal carbon (omega-oxidation) of long- and very long-chain fatty acids. Displays high omega-hydroxylase activity toward polyunsaturated fatty acids (PUFAs) . Participates in the conversion of arachidonic acid to omega-hydroxyeicosatetraenoic acid (20-HETE), a signaling molecule acting both as vasoconstrictive and natriuretic with overall effect on arterial blood pressure . Plays a role in the oxidative inactivation of eicosanoids, including both pro-inflammatory and anti-inflammatory mediators such as leukotriene B4 (LTB4), lipoxin A4 (LXA4), and several HETEs . Catalyzes omega-hydroxylation of 3-hydroxy fatty acids . Converts monoepoxides of linoleic acid leukotoxin and isoleukotoxin to omega-hydroxylated metabolites . Contributes to the degradation of very long-chain fatty acids (VLCFAs) by catalyzing successive omega-oxidations and chain shortening . Plays an important role in vitamin metabolism by chain shortening. Catalyzes omega-hydroxylation of the phytyl chain of tocopherols (forms of vitamin E), with preference for gamma-tocopherols over alpha-tocopherols, thus promoting retention of alpha-tocopherols in tissues . Omega-hydroxylates and inactivates phylloquinone (vitamin K1), and menaquinone-4 (MK-4, a form of vitamin K2), both acting as cofactors in blood coagulation .
Catalytic Activity: an organic molecule + O2 + reduced [NADPH--hemoprotein reductase] = an alcohol + H(+) + H2O + oxidized [NADPH--hemoprotein reductase]
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 59853
Sequence Length: 520
Pathway: Lipid metabolism; arachidonate metabolism.
Subcellular Location: Microsome membrane
EC: 1.14.14.1
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Q08477 | MPQLSLSSLGLWPMAASPWLLLLLVGASWLLARILAWTYTFYDNCCRLRCFPQPPKRNWFLGHLGLIHSSEEGLLYTQSLACTFGDMCCWWVGPWHAIVRIFHPTYIKPVLFAPAAIVPKDKVFYSFLKPWLGDGLLLSAGEKWSRHRRMLTPAFHFNILKPYMKIFNESVNIMHAKWQLLASEGSARLDMFEHISLMTLDSLQKCVFSFDSHCQEKPSEYIAAILELSALVTKRHQQILLYIDFLYYLTPDGQRFRRACRLVHDFTDAVIQERRRTLPSQGVDDFLQAKAKSKTLDFIDVLLLSKDEDGKKLSDEDIRAEADTFMFEGHDTTASGLSWVLYHLAKHPEYQERCRQEVQELLKDREPKEIEWDDLAQLPFLTMCIKESLRLHPPVPAVSRCCTQDIVLPDGRVIPKGIICLISVFGTHHNPAVWPDPEVYDPFRFDPKNIKERSPLAFIPFSAGPRNCIGQAFAMAEMKVVLGLTLLRFRVLPDHTEPRRKPELVLRAEGGLWLRVEPLS | Function: A cytochrome P450 monooxygenase involved in the metabolism of various endogenous substrates, including fatty acids and their oxygenated derivatives (oxylipins) . Mechanistically, uses molecular oxygen inserting one oxygen atom into a substrate, and reducing the second into a water molecule, with two electrons provided by NADPH via cytochrome P450 reductase (CPR; NADPH-ferrihemoprotein reductase) . May play a role in inactivation of pro-inflammatory and anti-inflammatory oxylipins during the resolution of inflammation .
Catalytic Activity: an organic molecule + O2 + reduced [NADPH--hemoprotein reductase] = an alcohol + H(+) + H2O + oxidized [NADPH--hemoprotein reductase]
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 59847
Sequence Length: 520
Pathway: Lipid metabolism; leukotriene B4 degradation.
Subcellular Location: Endoplasmic reticulum membrane
EC: 1.14.14.1
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Q99N16 | MSQLSMSWMGLGHTAASPWLLLLLAGASCLLAYILTPIYGVFENSLRLRCFPQPPKRNWILGHLGLIQSSEEGLLYIQSLVRTFRDACCWWVGPLHPVIRIFHPAFIKPVVLAPALVAPKDTVFYRFLKPWLGDGLLMSTGDKWSRHRRMLTPAFHFNILKPYVKVFNDSTNIMHAKWQRLASKGSAYLNMFEHISLMTLDSLQKCVFSFDSNCQEKPSEYITAILELSTLVARRHQRLLLHVDLFYYLTHDGMRFRKACRLVHDFTDAVIRERRRTLLDQGGVDVLKAKAKAKTLDFIDVLLLSKDEHGKALSDEDIRAEADTFMFGGHDTTASGLSWILYNLARHPEYQERCRQEVRELLRDREPEEIEWDDLAQLPFLTMCIKESLRLHPPVTAISRCCTQDIVLPDGRVIPKGVISRISIFGTHHNPAVWPDPEVYDPFRFDADNVKGRSPLAFIPFSAGPRNCIGQTFAMSEMKVALALTLLRFRVLPDDKEPRRKPELILRAEGGLWLKVEPLSAGAQ | Function: A cytochrome P450 monooxygenase involved in the metabolism of the pro-inflammatory lipid mediator leukotriene B4 (LTB4) . Hydroxylates at the omega-1 and omega-2 positions LTB4. This oxidation step leads to LTB4 inactivation, which is postulated to be a crucial part of the resolution of inflammation . Mechanistically, uses molecular oxygen inserting one oxygen atom into a substrate, and reducing the second into a water molecule, with two electrons provided by NADPH via cytochrome P450 reductase (CPR; NADPH-ferrihemoprotein reductase) .
Catalytic Activity: leukotriene B4 + O2 + reduced [NADPH--hemoprotein reductase] = 18-hydroxy-leukotriene B4 + H(+) + H2O + oxidized [NADPH--hemoprotein reductase]
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 59843
Sequence Length: 524
Pathway: Lipid metabolism; leukotriene B4 degradation.
Subcellular Location: Endoplasmic reticulum membrane
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P51869 | MPQLDLSWLGLRLETSLPWLLLLLIGASWLLVRVLTQTYIFYRTYQHLCDFPQPPKWNWFLGHLGMITPTEQGLKQVTKLVATYPQGFMTWLGPILPIITLCHPDVIRSVLSASASVALKEVIFYSFLKPWLGDGLLLSDGDKWSCHRRMLTPAFHFNILKPYVKIFNDSTNIMHAKWQDLASGGSARLDMFKNISLMTLDSLQKCVFSFDSNCQEKPSEYISAILELSALVAKRYQQLLLHTDSLYQLTHNGRRFHKACKLVHNFTDAVIQGRRRALPSQHEDDILKAKARSKTLDFIDVLLLTKDEDGKELSDEDIRAEADTFMFEGHDTTASGLSWILYNLARHPEYQERCRQEVRELLRDRESTEIEWDDLAQLPFLTMCIKESLRLHPPVTVISRRCTQDIVLPDGRVIPKGVICIINIFATHHNPTVWPDPEVYDPFRFDPENIKDRSPLAFIPFSAGPRNCIGQTFAMNEMKVALALTLLRFRVLPDDKEPRRKPELILRAEGGLWLRVEPLSTQ | Function: A cytochrome P450 monooxygenase involved in the metabolism of arachidonic acid and its oxygenated derivatives . Mechanistically, uses molecular oxygen inserting one oxygen atom into a substrate, and reducing the second into a water molecule, with two electrons provided by NADPH via cytochrome P450 reductase (CPR; NADPH-ferrihemoprotein reductase) . Participates in the conversion of arachidonic acid to omega-hydroxyeicosatetraenoic acid (20-HETE), a signaling molecule acting both as vasoconstrictive and natriuretic with overall effect on arterial blood pressure . Hydroxylates the terminal carbon (omega-hydroxylation) of inflammatory lipid mediators, including prostaglandin (PG) A1, PGE1 and leukotriene B4 (LTB4), and may play a role in inactivation of these oxylipins during the resolution of inflammation .
Catalytic Activity: (5Z,8Z,11Z,14Z)-eicosatetraenoate + O2 + reduced [NADPH--hemoprotein reductase] = 20-hydroxy-(5Z,8Z,11Z,14Z)-eicosatetraenoate + H(+) + H2O + oxidized [NADPH--hemoprotein reductase]
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 60050
Sequence Length: 522
Subcellular Location: Endoplasmic reticulum membrane
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Q9CFB4 | MDKKKGILLVALGTPRSCEADDVRDYLKEFLGDPLVIQKPRWLWLPILNGIILKVRPQKSAEMYKKIWTDEGSPLMIYTVAQAKQLQDMREDFDVRFAMTYGEPRIDKVIAEMKESGVEEITVLPLYPQYSLTTVEPVIQQVKKIDDKIKVIRDFHKVESYSDLLAESIREKWQANDYDKLVLSYHGIPLSYVTKKKDAYEEQCKETTRLVVSKLGLREEEYEHTYQSKFGPEKWLEPATIDRVAELPKENAKKVLICSPAFVADCLETLFELEIENKEVFVENGGETFDFVHPFNDSLDFTRVLSEVVDQNRL | Function: Involved in coproporphyrin-dependent heme b biosynthesis. Catalyzes the insertion of ferrous iron into coproporphyrin III to form Fe-coproporphyrin III.
Catalytic Activity: Fe-coproporphyrin III + 2 H(+) = coproporphyrin III + Fe(2+)
Sequence Mass (Da): 36436
Sequence Length: 314
Pathway: Porphyrin-containing compound metabolism; protoheme biosynthesis.
Subcellular Location: Cytoplasm
EC: 4.99.1.9
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Q88XC3 | MHPGLLLVNLGSPASPRTKDVKAYLQEFLSDPSVIEMPAALWQPLLRGIILPTRSWRSATFYQDSWLPQGSPLIVYSQAICQQVQAALPDWNVRLAMTYGQPDIGATLKAMVADGCEKPIILPLFPQYTQSTHGGIHRQVEATGLPHTFIDSFYDQPTYIHLLATKVWQSYQAHHYDAVIFSYHSIPTAMVRHGDPYQRECEATTKAVLAERPELPADKVITAYQSKFGPMPWLKPYLKNELMQLVELGKRNVLVVTPSFVVDCLETLEEDYVQNYQTFRASGGDRFDLVPPMNKDTGFSQFLADLAIQKQEASNHAITSSSKS | Function: Involved in coproporphyrin-dependent heme b biosynthesis. Catalyzes the insertion of ferrous iron into coproporphyrin III to form Fe-coproporphyrin III.
Catalytic Activity: Fe-coproporphyrin III + 2 H(+) = coproporphyrin III + Fe(2+)
Sequence Mass (Da): 36370
Sequence Length: 324
Pathway: Porphyrin-containing compound metabolism; protoheme biosynthesis.
Subcellular Location: Cytoplasm
EC: 4.99.1.9
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Q6AHF2 | MLGATPAAAGVAEHVTEPVAYDAILLAGFGGPEGQDDVIPFLRNVTRGRGILDERLEEVAQHYRHFGGVSPINDQNRALKAALEAELASRGIDLPVLWGNRNWDPYLADALTEADQRGFTKLIAVATSAYSSYSSCRQYREDFARALRETGLEGRIQIDKVRQFFDHPGFVEPFIEGVKNAVEELRERAPEIHPATGVRILFSTHSIPSTDAGKSGPSGRPDSGEPWGEGGAYAAQHLAVAEIVSHEATGGTIGWDLVYQSRSGPPSMPWLEPDINDRIAELPELGVKAIIIVPLGFVSDHMEVLWDLDTEAMESSEENGLLAVRVPTPGTHAKYVKGLVDLVLERRDGLPVAQRPSLTTLGPWYDVCRPGCCENVRLGFKPAVAGLTP | Function: Involved in coproporphyrin-dependent heme b biosynthesis. Catalyzes the insertion of ferrous iron into coproporphyrin III to form Fe-coproporphyrin III.
Catalytic Activity: Fe-coproporphyrin III + 2 H(+) = coproporphyrin III + Fe(2+)
Sequence Mass (Da): 42217
Sequence Length: 389
Pathway: Porphyrin-containing compound metabolism; protoheme biosynthesis.
Subcellular Location: Cytoplasm
EC: 4.99.1.9
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Q03Z41 | MNKKGLLLVNLGTPDSPHPDDVKAYLKEFLSDTNVIQMPRLLWQPILRGKILPKRSFKSAELYQKIWRKDGSPLMVYAKKQVEQVQQLQPNWIVRCAMTYRKPNIAETLKEMRLAGADDIVVLPLFPQYSVTSTQSVIDQVRKADKNINIVKSFYNDEAYLDLLARDIREAWAKNDYDRLIISYHGVPESYVRRGDPYVDHCTATTQGVLERVGPLTPDNTHQVFQSRFGPTEWVKPYLSDTLRSLPSQGIKRVLVATPAFVADCLETIEEIHVENHDIFKQAGGEVFDVVQPFNEHIDFSKYIASLANRHFAQN | Function: Involved in coproporphyrin-dependent heme b biosynthesis. Catalyzes the insertion of ferrous iron into coproporphyrin III to form Fe-coproporphyrin III.
Catalytic Activity: Fe-coproporphyrin III + 2 H(+) = coproporphyrin III + Fe(2+)
Sequence Mass (Da): 36114
Sequence Length: 315
Pathway: Porphyrin-containing compound metabolism; protoheme biosynthesis.
Subcellular Location: Cytoplasm
EC: 4.99.1.9
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P0A577 | MQFDAVLLLSFGGPEGPEQVRPFLENVTRGRGVPAERLDAVAEHYLHFGGVSPINGINRTLIAELEAQQELPVYFGNRNWEPYVEDAVTAMRDNGVRRAAVFATSAWSGYSSCTQYVEDIARARRAAGRDAPELVKLRPYFDHPLFVEMFADAITAAAATVRGDARLVFTAHSIPTAADRRCGPNLYSRQVAYATRLVAAAAGYCDFDLAWQSRSGPPQVPWLEPDVTDQLTGLAGAGINAVIVCPIGFVADHIEVVWDLDHELRLQAEAAGIAYARASTPNADPRFARLARGLIDELRYGRIPARVSGPDPVPGCLSSINGQPCRPPHCVASVSPARPSAGSP | Cofactor: Binds 1 [2Fe-2S] cluster.
Function: Involved in coproporphyrin-dependent heme b biosynthesis. Catalyzes the insertion of ferrous iron into coproporphyrin III to form Fe-coproporphyrin III.
Catalytic Activity: Fe-coproporphyrin III + 2 H(+) = coproporphyrin III + Fe(2+)
Sequence Mass (Da): 37144
Sequence Length: 344
Pathway: Porphyrin-containing compound metabolism; protoheme biosynthesis.
Subcellular Location: Cytoplasm
EC: 4.99.1.9
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Q5APU2 | MTTPLSSYSTTVTNHHPTFSFESLNSISSNNSTRNNQSNSVNSLLYFNSSGSSMVSSSSDAAPTSISTTTTSTTSMTGASANADNQQVYTITEEDSINDINRKEQNSFSIQPNQTPTMLPTSSYTLQRPPGLHEYTSSISSISSTSSNSTSAPVSPALINYSPKHSRKPNSLNLNRNMKNLSLNLHDSTNGYTSPLPKSTNSNQPRSNFIMDSPSKKSTPVNRIGNNNGNDYINATLLQTPSITQTPTMPPPLSLAQGPPSSVGSESVYKFPPISNACLNYSAGDSDSEVESMSMKQAAKNTIIPPMAPPFALQSKSSPLSTPPRLHSPLGVDRGLPISMSPIQSSLNQKFNNITLQTPLNSSFSINNDEATNFNNKNNKNNNNNSTATTTITNTILSTPQNVRYNSKKFHPPEELQESTSINAYPNGPKNVLNNLIYLYSDPAQGKIDINKFDLVINVAKECDNMSLQYMNQVPNQREYVYIPWSHNSNISKDLFQITNKIDQFFTNGRKILIHCQCGVSRSACVVVAFYMKKFQLGVNEAYELLKNGDQKYIDACDRICPNMNLIFELMEFGDKLNNNEISTQQLLMNSPPTINL | Function: Protein tyrosine phosphatase that acts as a repressor of the yeast-hyphal switch. Plays an important role in virulence. Negatively regulates CST20-HST7-CEK1-CPH1 filamentous growth pathway. Represses hyphal genes such as SAP4, SA5, SAP6, and HYR1, by acting through a CEK1-independent mechanism.
Catalytic Activity: H2O + O-phospho-L-tyrosyl-[protein] = L-tyrosyl-[protein] + phosphate
Sequence Mass (Da): 65560
Sequence Length: 597
EC: 3.1.3.48
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Q01958 | MFAFICLLAIASAIDFNTWASKNNKHFTAIEKLRRRAIFNMNAKFVDSFNKIGSFKLSVDGPFAAMTNEEYRTLLKSKRTTEENGQVKYLNIQAPESVDWRKEGKVTPIRDQAQCGSCYTFGSLAALEGRLLIEKGGDANTLDLSEEHMVQCTRDNGNNGCNGGLGSNVYDYIIEHGVAKESDYPYTGSDSTCKTNVKSFAKITGYTKVPRNNEAELKAALSQGLVDVSIDASSAKFQLYKSGAYTDTKCKNNYFALNHEVCAVGYGVVDGKECWIVRNSWGTGWGDKGYINMVIEGNTCGVATDPLYPTGVQYL | Function: Cysteine protease which degrades matrix proteins such as collagen, laminin and fibronectin and thus is involved in the destruction of human tissue . Can abolish adhesion . May play an important role in pathogenicity .
Catalytic Activity: Hydrolysis of proteins, including basement membrane collagen and azocasein. Preferential cleavage: Arg-Arg-|-Xaa in small molecule substrates including Z-Arg-Arg-|-NHMec.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 34688
Sequence Length: 315
Subcellular Location: Cell membrane
EC: 3.4.22.35
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P36184 | MFALILFVSLACANEVAFKQWAATHNKVFANRAEYLYRFAVFLDNKKFVEANANTELNVFADMTHEEFIQTHLGMTYEVPETTSNVKAAVKAAPESVDWRSIMNPAKDQGQCGSCWTFCTTAVLEGRVNKDLGKLYSFSEQQLVDCDASDNGCEGGHPSNSLKFIQENNGLGLESDYPYKAVAGTCKKVKNVATVTGSRRVTDGSETGLQTIIAENGPVAVGMDASRPSFQLYKKGTIYSDTKCRSRMMNHCVTAVGYGSNSNGKYWIIRNSWGTSWGDAGYFLLARDSNNMCGIGRDSNYPTGVKLI | Function: Cysteine protease which may be involved in pathogenicity.
Catalytic Activity: Hydrolysis of proteins, including basement membrane collagen and azocasein. Preferential cleavage: Arg-Arg-|-Xaa in small molecule substrates including Z-Arg-Arg-|-NHMec.
Sequence Mass (Da): 33851
Sequence Length: 308
Subcellular Location: Cytoplasm
EC: 3.4.22.35
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Q58DC0 | MSTAEAGGVFHRARGRTLDAFSSEKEREWKGPFYFIQGADPQFGLMKAWATGDCDNGGDEWEQEIRLAEQAVQAINKLNPKPKFFVLCGDLVHAMPGRPWRKEQTEDLQRVLRTVDSDIPLVLVSGNHDVGNVPTPETIAEFQRTWGDDYFSFWVGGVLFLVLNSQFLYDASRCPALKQEHDHWLDQQLRIAGQRACRHAVVFQHIPLFLQSIGEDDDYFNLTKSVRKEMADKFVEAGVKAVFSGHYHRNAGGTYRNLDMVVSSAIGCQLGTDTHGLRVVVVTAEKITHRYYSLDELSEKGIEDDLMDLLKEN | Cofactor: Binds 2 divalent metal cations.
Function: Protein phosphatase that dephosphorylates AKT family kinase specifically at 'Ser-473', blocking cell cycle progression and promoting cell apoptosis. May play an inhibitory role in glucose uptake by adipocytes (By similarity).
Catalytic Activity: H2O + O-phospho-L-seryl-[protein] = L-seryl-[protein] + phosphate
Sequence Mass (Da): 35410
Sequence Length: 313
Subcellular Location: Cytoplasm
EC: 3.1.3.16
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Q9BRF8 | MSAAEAGGVFHRARGRTLAAFPAEKESEWKGPFYFILGADPQFGLIKAWSTGDCDNGGDEWEQEIRLTEQAVQAINKLNPKPKFFVLCGDLIHAMPGKPWRTEQTEDLKRVLRAVDRAIPLVLVSGNHDIGNTPTAETVEEFCRTWGDDYFSFWVGGVLFLVLNSQFYENPSKCPSLKQAQDQWLDEQLSIARQRHCQHAIVFQHIPLFLESIDEDDDYYFNLSKSTRKKLADKFIHAGVKVVFSGHYHRNAGGTYQNLDMVVSSAIGCQLGRDPHGLRVVVVTAEKIVHRYYSLDELSEKGIEDDLMDLIKKK | Cofactor: Binds 2 divalent metal cations.
Function: Protein phosphatase that dephosphorylates AKT family kinase specifically at 'Ser-473', blocking cell cycle progression and promoting cell apoptosis. May play an inhibitory role in glucose uptake by adipocytes.
Catalytic Activity: H2O + O-phospho-L-seryl-[protein] = L-seryl-[protein] + phosphate
Sequence Mass (Da): 35548
Sequence Length: 314
Subcellular Location: Cytoplasm
EC: 3.1.3.16
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Q8BFS6 | MSAMEAADVFHRARGRTLDAFSSEKEREWKGPFYFVQGADTQFGLMKAWSTGNCDAGGDEWGQEIRLTEQAVEAINKLNPKPKFFVLCGDLVHAMPGTPWRQEQTRDLQRVLKAVDQDIPLVMVSGNHDLGNAPTAETVEEFCQTWGDDYFSFWVGGVLFLVLNSQFLYDASRCPALKQAQDHWLDQQLNIAEQKQCQHAIVFQHIPLFLQSIDEDDDYFNLTKTVRKELAEKLTRAGIRAVFSGHYHRNAGGTYQNLDMVVSSAIGCQLGKDTHGLRVVAITAEKIVHRYYSLDELSQGGVEEDLKELLKE | Cofactor: Binds 2 divalent metal cations.
Function: Protein phosphatase that dephosphorylates AKT family kinase specifically at 'Ser-473', blocking cell cycle progression and promoting cell apoptosis. May play an inhibitory role in glucose uptake by adipocytes (By similarity).
Catalytic Activity: H2O + O-phospho-L-seryl-[protein] = L-seryl-[protein] + phosphate
Sequence Mass (Da): 35248
Sequence Length: 312
Subcellular Location: Cytoplasm
EC: 3.1.3.16
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O49290 | MSMLMAVKTTSLCCSSLNLTASPTFRRNPRAARLVNPTARIQTRFHRLIEEQGIVLMPGCYDALSAAIVQQTGFSAGFISGYALSASLLGKPDFGLLTPPEMAATARSVCASAPNIPIIADADTGGGNALNIQRTVKDLIAAGAAGCFLEDQAWPKKCGHMRGKQVIPAEEHAAKIASARDAIGDSDFFLVARTDVRATSAKSGLEDAIARVNLYMEAGADASFVEAPRDDDELKEIGKRTKGYRVCNMIEGGVTPLHTPDELKEMGFHLIVHPLTALYASTRALVDVLKTLKENGSTRDHLQKMATFEEFNSLVDLDSWFELEARYSNLRNALGTTKS | Catalytic Activity: 1-carboxyvinyl carboxyphosphonate + H(+) = 3-(hydrohydroxyphosphoryl)pyruvate + CO2
Sequence Mass (Da): 36566
Sequence Length: 339
Subcellular Location: Plastid
EC: 2.7.8.23
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P11435 | MAVTKARTFRELMNAPEILVVPSAYDALSAKVIQQAGFPAVHMTGSGTSASMLGLPDLGFTSVSEQAINLKNIVLTVDVPVIMDADAGYGNAMSVWRATREFERVGIVGYHLEDQVNPKRCGHLEGKRLISTEEMTGKIEAAVEAREDEDFTIIARTDARESFGLDEAIRRSREYVAAGADCIFLEAMLDVEEMKRVRDEIDAPLLANMVEGGKTPWLTTKELESIGYNLAIYPLSGWMAAASVLRKLFTELREAGTTQKFWDDMGLKMSFAELFEVFEYSKISELEARFVRDQD | Function: Catalyzes the formation of an unusual C-P bond that is involved in the biosynthesis of the antibiotic bialaphos (BA). Catalyzes the rearrangement of the carboxyphosphono group of CPEP to form the C-P bond of phosphinopyruvate.
Catalytic Activity: 1-carboxyvinyl carboxyphosphonate + H(+) = 3-(hydrohydroxyphosphoryl)pyruvate + CO2
Sequence Mass (Da): 32781
Sequence Length: 295
Pathway: Secondary metabolite biosynthesis; bialaphos biosynthesis.
EC: 2.7.8.23
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Q9SU30 | MATIPMDIVNDIFLRLPAKTLVRCRALSKPCYHLINDPDFIESHLHRVLQTGDHLMILLRGALRLYSVDLDSLDSVSDVEHPMKRGGPTEVFGSSNGLIGLSNSPTDLAVFNPSTRQIHRLPPSSIDLPDGSSTRGYVFYGLGYDSVSDDYKVVRMVQFKIDSEDELGCSFPYEVKVFSLKKNSWKRIESVASSIQLLFYFYYHLLYRRGYGVLAGNSLHWVLPRRPGLIAFNLIVRFDLALEEFEIVRFPEAVANGNVDIQMDIGVLDGCLCLMCNYDQSYVDVWMMKEYNVRDSWTKVFTVQKPKSVKSFSYMRPLVYSKDKKKVLLELNNTKLVWFDLESKKMSTLRIKDCPSSYSAELVVSSLVLGCKGDLNNIKYRKEQQAKEAREAKIMQNTKRRDDFLSKGFKLVL | Function: Component of SCF(ASK-cullin-F-box) E3 ubiquitin ligase complexes, which may mediate the ubiquitination and subsequent proteasomal degradation of target proteins (By similarity). Regulates negatively both salicylic acid (SA)-dependent and SA-independent defense signaling.
Sequence Mass (Da): 47259
Sequence Length: 413
Domain: The F-box is necessary for the interaction with ASK proteins.
Pathway: Protein modification; protein ubiquitination.
Subcellular Location: Cytoplasm
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P32198 | MAEAHQAVAFQFTVTPDGIDLRLSHEALKQICLSGLHSWKKKFIRFKNGIITGVFPANPSSWLIVVVGVISSMHAKVDPSLGMIAKISRTLDTTGRMSSQTKNIVSGVLFGTGLWVAVIMTMRYSLKVLLSYHGWMFAEHGKMSRSTKIWMAMVKVLSGRKPMLYSFQTSLPRLPVPAVKDTVSRYLESVRPLMKEEDFQRMTALAQDFAVNLGPKLQWYLKLKSWWATNYVSDWWEEYIYLRGRGPLMVNSNYYAMEMLYITPTHIQAARAGNTIHAILLYRRTLDREELKPIRLLGSTIPLCSAQWERLFNTSRIPGEETDTIQHIKDSRHIVVYHRGRYFKVWLYHDGRLLRPRELEQQMQQILDDPSEPQPGEAKLAALTAADRVPWAKCRQTYFARGKNKQSLDAVEKAAFFVTLDESEQGYREEDPEASIDSYAKSLLHGRCFDRWFDKSITFVVFKNSKIGINAEHSWADAPVVGHLWEYVMATDVFQLGYSEDGHCKGDTNPNIPKPTRLQWDIPGECQEVIDASLSSASLLANDVDLHSFPFDSFGKGLIKKCRTSPDAFIQLALQLAHYKDMGKFCLTYEASMTRLFREGRTETVRSCTMESCNFVQAMMDPKSTAEQRLKLFKIACEKHQHLYRLAMTGAGIDRHLFCLYVVSKYLAVDSPFLKEVLSEPWRLSTSQTPQQQVELFDFEKNPDYVSCGGGFGPVADDGYGVSYIIVGENFIHFHISSKFSSPETDSHRFGKHLRQAMMDIITLFGLTINSKK | Function: Catalyzes the transfer of the acyl group of long-chain fatty acid-CoA conjugates onto carnitine, an essential step for the mitochondrial uptake of long-chain fatty acids and their subsequent beta-oxidation in the mitochondrion . Plays an important role in hepatic triglyceride metabolism .
Catalytic Activity: (R)-carnitine + hexadecanoyl-CoA = CoA + O-hexadecanoyl-(R)-carnitine
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 88125
Sequence Length: 773
Domain: A conformation change in the N-terminal region spanning the first 42 residues plays an important role in the regulation of enzyme activity by malonyl-CoA.
Pathway: Lipid metabolism; fatty acid beta-oxidation.
Subcellular Location: Mitochondrion outer membrane
EC: 2.3.1.21
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Q58DK1 | MAEAHQAVAFQFTVTPEGVDFQLSREVLKHIYLSVIRSWKKRLIRIKNGILRGVYPGSPTSWLVVVMATAGSSYYNVDISMGLVYYIQRWLPEGRPYRTPYTRTLFSMAIFSTGVWMMGIFFFRQTLKLLLSYHGWMFELHGQTSHLTRVWAVCVRLLSGRRPMLYSFQTSLPKLPVPSVPATVHRYLESVEHLLDDEQYYRMETLAKEFEEKTAPRLQKYLVLKSWWATNYVSDWWEEYVYLRGRNPIVVNSNYYVMDLVLVKNTDVQAARLGNAVHAMITYRRKLDREEIKPVMALGLVPMCSYQMERMFNTTRIPGKDTDVLQHLPDSRHVAVYHKGRFFKVWLYEGSRLLKPRDLEMQFQRILDDPSPPQPGEERLAALTAGGRVEWAQARQAFFSSGKNKAALDAIERAAFFVALDEESHHYDPEDEASLSLYGKALLHGNCYNRWFDKSFTLISFKNGQLGLNTEHAWADAPIIGHLWEFVLGTDSFHLGYTETGHCLGKPNPVLPPPQRLQWDIPKQCQAVIESSYQVAKALADDVELYCFQFLPFGKGLIKKCRTSPDAFVQIALQLAHFRDRGKFCLTYEASMTRMFREGRTETVRSCTRESTAFVQAMVQGRHLNEDLQRLFRKAAEKHQNMYRLAMTGAGIDRHLFCLYVVSKYLGVESPFLAEVLSEPWRLSTSQIAQFQIRMFDPNKYPKHLGAGGGFGPVADDGYGVSYMIAGENTIFFHVSSKFSSSETNAQRFGNQIRQALLDIANLFQVPKADG | Catalytic Activity: (R)-carnitine + hexadecanoyl-CoA = CoA + O-hexadecanoyl-(R)-carnitine
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 88512
Sequence Length: 771
Pathway: Lipid metabolism; fatty acid beta-oxidation.
Subcellular Location: Mitochondrion outer membrane
EC: 2.3.1.21
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Q92523 | MAEAHQAVAFQFTVTPDGVDFRLSREALKHVYLSGINSWKKRLIRIKNGILRGVYPGSPTSWLVVIMATVGSSFCNVDISLGLVSCIQRCLPQGCGPYQTPQTRALLSMAIFSTGVWVTGIFFFRQTLKLLLCYHGWMFEMHGKTSNLTRIWAMCIRLLSSRHPMLYSFQTSLPKLPVPRVSATIQRYLESVRPLLDDEEYYRMELLAKEFQDKTAPRLQKYLVLKSWWASNYVSDWWEEYIYLRGRSPLMVNSNYYVMDLVLIKNTDVQAARLGNIIHAMIMYRRKLDREEIKPVMALGIVPMCSYQMERMFNTTRIPGKDTDVLQHLSDSRHVAVYHKGRFFKLWLYEGARLLKPQDLEMQFQRILDDPSPPQPGEEKLAALTAGGRVEWAQARQAFFSSGKNKAALEAIERAAFFVALDEESYSYDPEDEASLSLYGKALLHGNCYNRWFDKSFTLISFKNGQLGLNAEHAWADAPIIGHLWEFVLGTDSFHLGYTETGHCLGKPNPALAPPTRLQWDIPKQCQAVIESSYQVAKALADDVELYCFQFLPFGKGLIKKCRTSPDAFVQIALQLAHFRDRGKFCLTYEASMTRMFREGRTETVRSCTSESTAFVQAMMEGSHTKADLRDLFQKAAKKHQNMYRLAMTGAGIDRHLFCLYLVSKYLGVSSPFLAEVLSEPWRLSTSQIPQSQIRMFDPEQHPNHLGAGGGFGPVADDGYGVSYMIAGENTIFFHISSKFSSSETNAQRFGNHIRKALLDIADLFQVPKAYS | Catalytic Activity: (R)-carnitine + hexadecanoyl-CoA = CoA + O-hexadecanoyl-(R)-carnitine
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 87801
Sequence Length: 772
Pathway: Lipid metabolism; fatty acid beta-oxidation.
Subcellular Location: Mitochondrion outer membrane
EC: 2.3.1.21
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Q63704 | MAEAHQAVAFQFTVTPDGVDFRLSREALRHIYLSGINSWKKRLIRIKNGILRGVYPGSPTSWLVVVMATVGSNYCKVDISMGLVHCIQRCLPTRYGSYGTPQTETLLSMVIFSTGVWATGIFLFRQTLKLLLSYHGWMFEMHSKTSHATKIWAICVRLLSSRRPMLYSFQTSLPKLPVPSVPATIHRYLDSVRPLLDDEAYFRMESLAKEFQDKIAPRLQKYLVLKSWWATNYVSDWWEEYVYLRGRSPIMVNSNYYAMDFVLIKNTSQQAARLGNTVHAMIMYRRKLDREEIKPVMALGMVPMCSYQMERMFNTTRIPGKETDLLQHLSESRHVAVYHKGRFFKVWLYEGSCLLKPRDLEMQFQRILDDTSPPQPGEEKLAALTAGGRVEWAEARQKFFSSGKNKMSLDTIERAAFFVALDEDSHCYNPDDEASLSLYGKSLLHGNCYNRWFDKSFTLISCKNGQLGLNTEHSWADAPIIGHLWEFVLATDTFHLGYTETGHCVGEPNTKLPPPQRMQWDIPEQCQTAIENSYQVAKALADDVELYCFQFLPFGKGLIKKCRTSPDAFVQIALQLAHFRDKGKFCLTYEASMTRMFREGRTETVRSCTSESTAFVRAMMTGSHKKQDLQDLFRKASEKHQNMYRLAMTGAGIDRHLFCLYIVSKYLGVRSPFLDEVLSEPWSLSTSQIPQFQICMFDPKQYPNHLGAGGGFGPVADHGYGVSYMIAGENTMFFHVSSKLSSSETNALRFGNHIRQALLDIADLFKISKTDS | Catalytic Activity: (R)-carnitine + hexadecanoyl-CoA = CoA + O-hexadecanoyl-(R)-carnitine
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 88217
Sequence Length: 772
Pathway: Lipid metabolism; fatty acid beta-oxidation.
Subcellular Location: Mitochondrion outer membrane
EC: 2.3.1.21
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Q8TCG5 | MAEAHQAVGFRPSLTSDGAEVELSAPVLQEIYLSGLRSWKRHLSRFWNDFLTGVFPASPLSWLFLFSAIQLAWFLQLDPSLGLMEKIKELLPDWGGQHHGLRGVLAAALFASCLWGALIFTLHVALRLLLSYHGWLLEPHGAMSSPTKTWLALVRIFSGRHPMLFSYQRSLPRQPVPSVQDTVRKYLESVRPILSDEDFDWTAVLAQEFLRLQASLLQWYLRLKSWWASNYVSDWWEEFVYLRSRNPLMVNSNYYMMDFLYVTPTPLQAARAGNAVHALLLYRHRLNRQEIPPTLLMGMRPLCSAQYEKIFNTTRIPGVQKDYIRHLHDSQHVAVFHRGRFFRMGTHSRNSLLSPRALEQQFQRILDDPSPACPHEEHLAALTAAPRGTWAQVRTSLKTQAAEALEAVEGAAFFVSLDAEPAGLTREDPAASLDAYAHALLAGRGHDRWFDKSFTLIVFSNGKLGLSVEHSWADCPISGHMWEFTLATECFQLGYSTDGHCKGHPDPTLPQPQRLQWDLPDQIHSSISLALRGAKILSENVDCHVVPFSLFGKSFIRRCHLSSDSFIQIALQLAHFRDRGQFCLTYESAMTRLFLEGRTETVRSCTREACNFVRAMEDKEKTDPQCLALFRVAVDKHQALLKAAMSGQGVDRHLFALYIVSRFLHLQSPFLTQVHSEQWQLSTSQIPVQQMHLFDVHNYPDYVSSGGGFGPADDHGYGVSYIFMGDGMITFHISSKKSSTKTDSHRLGQHIEDALLDVASLFQAGQHFKRRFRGSGKENSRHRCGFLSRQTGASKASMTSTDF | Function: May play a role in lipid metabolic process.
Catalytic Activity: (R)-carnitine + hexadecanoyl-CoA = CoA + O-hexadecanoyl-(R)-carnitine
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 90989
Sequence Length: 803
Pathway: Lipid metabolism; fatty acid beta-oxidation.
Subcellular Location: Mitochondrion outer membrane
EC: 2.3.1.21
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C1K5M2 | MSSLVLQCWKLSSPSLILQQNTSISMGAFKGIHKLQIPNSPLTVSARGLNKISCSLNLQTEKLCYEDNDNDLDEELMPKHIALIMDGNRRWAKDKGLEVYEGHKHIIPKLKEICDISSKLGIQIITAFAFSTENWKRSKEEVDFLLQMFEEIYDEFSRSGVRVSIIGCKSDLPMTLQKCIALTEETTKGNKGLHLVIALNYGGYYDILQATKSIVNKAMNGLLDVEDINKNLFDQELESKCPNPDLLIRTGGEQRVSNFLLWQLAYTEFYFTNTLFPDFGEEDLKEAIMNFQQRHRRFGGHTY | Function: Uses dimethylallyl diphosphate and isopentenyl diphosphate to catalyze the cis-prenyl chain elongation and produce the 10 carbon product neryl diphosphate.
Catalytic Activity: dimethylallyl diphosphate + isopentenyl diphosphate = diphosphate + neryl diphosphate
Sequence Mass (Da): 34601
Sequence Length: 303
Subcellular Location: Plastid
EC: 2.5.1.28
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P23786 | MVPRLLLRAWPRGPAVGPGAPSRPLSAGSGPGQYLQRSIVPTMHYQDSLPRLPIPKLEDTIRRYLSAQKPLLNDGQFRKTEQFCKSFENGIGKELHEQLVALDKQNKHTSYISGPWFDMYLSARDSVVLNFNPFMAFNPDPKSEYNDQLTRATNMTVSAIRFLKTLRAGLLEPEVFHLNPAKSDTITFKRLIRFVPSSLSWYGAYLVNAYPLDMSQYFRLFNSTRLPKPSRDELFTDDKARHLLVLRKGNFYIFDVLDQDGNIVSPSEIQAHLKYILSDSSPAPEFPLAYLTSENRDIWAELRQKLMSSGNEESLRKVDSAVFCLCLDDFPIKDLVHLSHNMLHGDGTNRWFDKSFNLIIAKDGSTAVHFEHSWGDGVAVLRFFNEVFKDSTQTPAVTPQSQPATTDSTVTVQKLNFELTDALKTGITAAKEKFDATMKTLTIDCVQFQRGGKEFLKKQKLSPDAVAQLAFQMAFLRQYGQTVATYESCSTAAFKHGRTETIRPASVYTKRCSEAFVREPSRHSAGELQQMMVECSKYHGQLTKEAAMGQGFDRHLFALRHLAAAKGIILPELYLDPAYGQINHNVLSTSTLSSPAVNLGGFAPVVSDGFGVGYAVHDNWIGCNVSSYPGRNAREFLQCVEKALEDMFDALEGKSIKS | Function: Involved in the intramitochondrial synthesis of acylcarnitines from accumulated acyl-CoA metabolites . Reconverts acylcarnitines back into the respective acyl-CoA esters that can then undergo beta-oxidation, an essential step for the mitochondrial uptake of long-chain fatty acids and their subsequent beta-oxidation in the mitochondrion. Active with medium (C8-C12) and long-chain (C14-C18) acyl-CoA esters .
Catalytic Activity: (R)-carnitine + hexadecanoyl-CoA = CoA + O-hexadecanoyl-(R)-carnitine
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 73777
Sequence Length: 658
Pathway: Lipid metabolism; fatty acid beta-oxidation.
Subcellular Location: Mitochondrion inner membrane
EC: 2.3.1.21
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P18886 | MMPRLLFRAWPRCPSLVLGAPSRPLSAVSGPDDYLQHSIVPTMHYQDSLPRLPIPKLEDTMKRYLNAQKPLLDDSQFRRTEALCKNFETGVGKELHAHLLAQDKQNKHTSYISGPWFDMYLTARDSIVLNFNPFMAFNPDPKSEYNDQLTRATNLTVSAVRFLKTLQAGLLEPEVFHLNPSKSDTDAFKRLIRFVPPSLSWYGAYLVNAYPLDMSQYFRLFNSTRIPRPNRDELFTDTKARHLLVLRKGHFYVFDVLDQDGNIVNPLEIQAHLKYILSDSSPVPEFPVAYLTSENRDVWAELRQKLIFDGNEETLKKVDSAVFCLCLDDFPMKDLIHLSHTMLHGDGTNRWFDKSFNLIVAEDGTAAVHFEHSWGDGVAVLRFFNEVFRDSTQTPAITPQSQPAATNSSASVETLSFNLSGALKAGITAAKEKFDTTVKTLSIDSIQFQRGGKEFLKKKQLSPDAVAQLAFQMAFLRQYGQTVATYESCSTAAFKHGRTETIRPASIFTKRCSEAFVRDPSKHSVGELQHMMAECSKYHGQLTKEAAMGQGFDRHLYALRYLATARGLNLPELYLDPAYQQMNHNILSTSTLNSPAVSLGGFAPVVPDGFGIAYAVHDDWIGCNVSSYSGRNAREFLHCVQKCLEDIFDALEGKAIKT | Function: Involved in the intramitochondrial synthesis of acylcarnitines from accumulated acyl-CoA metabolites. Reconverts acylcarnitines back into the respective acyl-CoA esters that can then undergo beta-oxidation, an essential step for the mitochondrial uptake of long-chain fatty acids and their subsequent beta-oxidation in the mitochondrion. Active with medium (C8-C12) and long-chain (C14-C18) acyl-CoA esters.
Catalytic Activity: (R)-carnitine + hexadecanoyl-CoA = CoA + O-hexadecanoyl-(R)-carnitine
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 74110
Sequence Length: 658
Pathway: Lipid metabolism; fatty acid beta-oxidation.
Subcellular Location: Mitochondrion inner membrane
EC: 2.3.1.21
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K7WQ45 | MNSSIVSQHFFISLKSSLDLQCWKSSSPSSISMGEFKGIHDKLQILKLPLTMSDRGLSKISCSLSLQTEKLRYDNDDNDDLELHEELIPKHIALIMDGNRRWAKAKGLEVYEGHKLIIPKLKEICDISSKLGIQVITAFAFSTENWKRSKEEVDFLMQLFEEFFNEFLRFGVRVSVIGCKSNLPMTLQKCIALTEETTKGNKGLHLVIALNYGGYYDILQATKSIVNKAMNGLLDVEDINKNLFEQELESKCPNPDLLIRTGGEQRVSNFLLWQLAYTEFYFTNTLFPDFGEKDLKKAILNFQQRHRRFGGHTY | Function: Uses dimethylallyl diphosphate and isopentenyl diphosphate to catalyze the cis-prenyl chain elongation and produce the 20 carbon product nerylneryl diphosphate.
Catalytic Activity: dimethylallyl diphosphate + 3 isopentenyl diphosphate = 3 diphosphate + nerylneryl diphosphate
Sequence Mass (Da): 36020
Sequence Length: 314
Subcellular Location: Plastid
EC: 2.5.1.142
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P53674 | MSQAAKASASATVAVNPGPDTKGKGAPPAGTSPSPGTTLAPTTVPITSAKAAELPPGNYRLVVFELENFQGRRAEFSGECSNLADRGFDRVRSIIVSAGPWVAFEQSNFRGEMFILEKGEYPRWNTWSSSYRSDRLMSFRPIKMDAQEHKISLFEGANFKGNTIEIQGDDAPSLWVYGFSDRVGSVKVSSGTWVGYQYPGYRGYQYLLEPGDFRHWNEWGAFQPQMQSLRRLRDKQWHLEGSFPVLATEPPK | Function: Crystallins are the dominant structural components of the vertebrate eye lens.
PTM: Specific cleavages in the N-terminal arm occur during lens maturation and give rise to truncated forms, leading to impaired oligomerization and protein insolubilization.
Sequence Mass (Da): 28023
Sequence Length: 252
Domain: Has a two-domain beta-structure, folded into four very similar Greek key motifs.
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P02523 | MSQVAKAAATTAVNPGPDGKGKGTPSTGTAPAPGPTPVPASVPRPAAKVGELPPGSYRLVVFEQENFQGRRVEFSGECLNLGDRGFDRVRSLIVLSGPWVAFEQSAFRGEMFVLEKGEYPRWDTWTSSYRSDRLMSFRPIRMDSQEHKICLFEGANFKGNTMEIQEDDVPSLWVYGFCDRVGSITVSSGTWVGYQYPGYRGYQYLLEPGDFRHWNEWGAFQPQMQAVRRLRDRQWHQEGCFPVLTAEPPK | Function: Crystallins are the dominant structural components of the vertebrate eye lens.
PTM: Specific cleavages in the N-terminal arm occur during lens maturation and give rise to truncated forms, leading to impaired oligomerization and protein insolubilization. The protease responsible for this partial degradation could be calpain II.
Sequence Mass (Da): 28093
Sequence Length: 250
Domain: Has a two-domain beta-structure, folded into four very similar Greek key motifs.
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Q91318 | MASDHQSPATKQQQPSSKIVLFEQENFQGRCHELSGPCTSLKEAGMEKIGSILVHSGPWVGYEQQNCKGEQFVFEKGEYPRWDSWTNSRKSESISSLRPIKVDSQEHKIVLYENPNFTGKKIEIIDDDVPSFHAHGYQEKVSSVRVQSGTWVGYQYPGYRGYQYLFEKGDYKDSSDFGAQHPQIQSVRRIRDMQWHQRGTFHPTN | Function: Crystallins are the dominant structural components of the vertebrate eye lens.
PTM: The N-terminus is blocked.
Sequence Mass (Da): 23649
Sequence Length: 205
Domain: Has a two-domain beta-structure, folded into four very similar Greek key motifs.
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A0A0K2JL91 | MTVPENAQHTAPDQTQHTAPDRTRQAQQAAPDTAGRRLIELMAGFWKTQAIYLAAESGLVDAIAAAGRAPAVELANRTGTDPDALGRLLLFLESLDVVSGEDPAGYALTPVGELLRTGTQDSMRDHVRIYGSHFYRAWGALDHSLRTGRSAFTEVYGSDLFRYLNQHPDLSLTYERAMVAGTPFFAQVPEVHDFSGARLIVDVAGGHGALLHEILKSCPEPRAVLFDAPHVIAETADRPIASEHGDRVTLVPGDFFEGVPQGGDVYLLSRILHCFDDEACLRILAHCRSAMAPGGRLVVVERLLTRGTGSSLAQGYNMHMLVVLGGGRERDEDAYRTLLEKAGFQLDSVTTLPLETHLMAATLRR | Function: Part of a gene cluster involved in the biosynthesis of cremeomycin, a light-sensitive o-diazoquinone with antibacterial and antiproliferative effects . Catalyzes the methylation of the C4 hydroxyl group of 3-amino-2,4-dihydroxybenzoate (3,2,4-ADHBA) to form 3-amino-2-hydroxy-4-methoxybenzoate (3,2,4-AHMBA) . In vitro, can also catalyze the methylation of 3-amino-4-hydroxybenzoate (3,4-AHBA) .
Catalytic Activity: 3-amino-2,4-dihydroxybenzoate + S-adenosyl-L-methionine = 3-amino-2-hydroxy-4-methoxybenzoate + H(+) + S-adenosyl-L-homocysteine
Sequence Mass (Da): 39688
Sequence Length: 365
Pathway: Antibiotic biosynthesis.
EC: 2.1.1.380
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Q9VC61 | MTENQLYPMSSEFFDTGSNSSSNTLKYDLYSLGSTVVGAALPTLTINTGYGSSSSNNNNTNNNNNNSSSHSSSSNCSTSTTNTCNVMLSTTAITIPRSSNHNQIHHHPYQQSDLQTPRHHPSPLHTLPSMTHQQNQLQQQQQQQHHNQQQQLQQSHLALGELSDFGLDALDAASLSPTLLQDVSLSAVSPLSTTLYNGNTSGAGSSNGIGSGSGGYFTPDMSHSLSLNVVSEQVLLQEATTPNELLYEMTPNSNAMWSDISSAIIHTKHEPFSLDDDYIFPNDKAEIQAADLSDLNGGDFLDVIGNIEDFLPQTAVTQSVNFLLSPQAQGQDALVAPPMELLQQQQQNHQQLQVGSLPQLQTLLTLSQQQQSNSSSTSPYEIYHSTPQKPQQQQLSASFSPGSQASQSPLTPPPPPHANRPQYQMVKSRNMQELIKKGFPMSSPPERSILSQSAALSPGGSSGFGSSASGNSTTTSNQTSGSAVRKSFGYQSAVENSQLSRLSSSAPTHLGLEHIWMRREPRQHLLSTGSLAEAESFSSLSTGSVLSPDGIDFSQDDEDDNSSENSDNYDDCSSDNGLSEDEDETRTSTPNHLSSSKGKERFFWQYNVQAKGPKGKRLVFQSKLEDPHVLNEVTDPVFSPTCSVRGIKVYKHSGKARKGDGNDLTPNARKLHNIGKELDKLSRTINDMTPVSELPFNVRPKSRKEKNKLASRACRLKKKAQHEANKIKLFGLEIEHSEFNVKAVEISYNPSIFVL | Function: Transcriptional regulator that acts in the TORC1 signaling pathway to regulate energy homeostasis and promote survival during nutrient deprivation. Interacts with REPTOR to form a transcriptional activator complex that functions downstream of TORC1 to up-regulate the expression of most target genes induced by TORC1 inhibition. In the complex, acts as the transcriptional activator. Under normal conditions TORC1 is active, inhibiting the formation of the REPTOR/REPTOR-BP complex by phosphorylating REPTOR and mediates its cytoplasmic retention by forming a docking site for 14-3-3 proteins. Upon TORC1 inhibition resulting from nutrient stress, REPTOR is recruited into the nucleus where it interacts with REPTOR-BP and together they maintain organismal metabolism by activating the expression of target stress response genes including those involved in glycogenesis and triglyceride biosynthesis. The complex also appears to negatively regulate some aspects of TORC1-dependent larval growth.
PTM: Phosphorylation by the TORC1 kinase complex at Ser-527 and Ser-530 abolishes nuclear localization. Upon TORC1 inhibition, dephosphorylated in a mts/PP2a-dependent manner leading to nuclear localization.
Sequence Mass (Da): 82263
Sequence Length: 755
Subcellular Location: Nucleus
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Q8IUR6 | MPQPSVSGMDPPFGDAFRSHTFSEQTLMSTDLLANSSDPDFMYELDREMNYQQNPRDNFLSLEDCKDIENLESFTDVLDNEGALTSNWEQWDTYCEDLTKYTKLTSCDIWGTKEVDYLGLDDFSSPYQDEEVISKTPTLAQLNSEDSQSVSDSLYYPDSLFSVKQNPLPSSFPGKKITSRAAAPVCSSKTLQAEVPLSDCVQKASKPTSSTQIMVKTNMYHNEKVNFHVECKDYVKKAKVKINPVQQSRPLLSQIHTDAAKENTCYCGAVAKRQEKKGMEPLQGHATPALPFKETQELLLSPLPQEGPGSLAAGESSSLSASTSVSDSSQKKEEHNYSLFVSDNLGEQPTKCSPEEDEEDEEDVDDEDHDEGFGSEHELSENEEEEEEEEDYEDDKDDDISDTFSEPGYENDSVEDLKEVTSISSRKRGKRRYFWEYSEQLTPSQQERMLRPSEWNRDTLPSNMYQKNGLHHGKYAVKKSRRTDVEDLTPNPKKLLQIGNELRKLNKVISDLTPVSELPLTARPRSRKEKNKLASRACRLKKKAQYEANKVKLWGLNTEYDNLLFVINSIKQEIVNRVQNPRDERGPNMGQKLEILIKDTLGLPVAGQTSEFVNQVLEKTAEGNPTGGLVGLRIPTSKV | Function: Acts as a negative regulator of the endoplasmic reticulum stress response or unfolded protein response (UPR). Represses the transcriptional activity of CREB3 during the UPR. Recruits CREB3 into nuclear foci.
PTM: Probably degraded by the proteasome.
Sequence Mass (Da): 72149
Sequence Length: 639
Subcellular Location: Nucleus
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Q8CDG5 | MPQPSVSGMDPPFGDAFRSHTFSEQTLMSTDLLANSSDPDFMYELDREMNYQQNPRDNFLSLEDCKDIENLETFTDVLDNEDALTSNWEQWDTYCEDLTKYTKLTSCDIWGTKEVDYLGLDDFSSPYQDEEVISKTPTLAQLNSEDSQSVSDSLYYPDSLFSVKQNPLPPSSFPSKKITNRAAAPVCSSKTLQAEVPSSDCVQKASKPTSSTQIMVKTNMYHNEKVNFHVECKDYVKKAKVKINPVQQGRPLLSQVHIDAAKENTCYCGAVAKRQERRGVEPHQGRGTPALPFKETQELLLSPLTQDSPGLVATAESGSLSASTSVSDSSQKKEEHNYSLFVSDNMREQPTKYSPEDDEDDEDEFDDEDHDEGFGSEHELSENEEEEEEEEDYEDDRDDDISDTFSEPGYENDSVEDLKEMTSISSRKRGKRRYFWEYSEQLTPSQQERILRPSEWNRDTLPSNMYQKNGLHHGKYAVKKSRRTDVEDLTPNPKKLLQIGNELRKLNKVISDLTPVSELPLTARPRSRKEKNKLASRACRLKKKAQYEANKVKLWGLNTEYDNLLFVINSIKQDIVNRVQNPREEREPSMGQKLEILIKDTLGLPVAGQTSEFVNQVLGKTAEGNPTGGLVGLRIPASKV | Function: Acts as a negative regulator of the endoplasmic reticulum stress response or unfolded protein response (UPR). Represses the transcriptional activity of CREB3 during the UPR. Recruits CREB3 into nuclear foci (By similarity).
PTM: Probably degraded by the proteasome.
Sequence Mass (Da): 72598
Sequence Length: 640
Subcellular Location: Nucleus
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O75177 | MSVAFASARPRGKGEVTQQTIQKMLDENHHLIQCILEYQSKGKTAECTQYQQILHRNLVYLATIADSNQNMQSLLPAPPTQNMNLGPGALTQSGSSQGLHSQGSLSDAISTGLPPSSLLQGQIGNGPSHVSMQQTAPNTLPTTSMSISGPGYSHAGPASQGVPMQGQGTIGNYVSRTNINMQSNPVSMMQQQAATSHYSSAQGGSQHYQGQSSIAMMGQGSQGSSMMGQRPMAPYRPSQQGSSQQYLGQEEYYGEQYSHSQGAAEPMGQQYYPDGHGDYAYQQSSYTEQSYDRSFEESTQHYYEGGNSQYSQQQAGYQQGAAQQQTYSQQQYPSQQSYPGQQQGYGSAQGAPSQYPGYQQGQGQQYGSYRAPQTAPSAQQQRPYGYEQGQYGNYQQ | Function: Transcriptional activator which is required for calcium-dependent dendritic growth and branching in cortical neurons. Recruits CREB-binding protein (CREBBP) to nuclear bodies. Component of the CREST-BRG1 complex, a multiprotein complex that regulates promoter activation by orchestrating a calcium-dependent release of a repressor complex and a recruitment of an activator complex. In resting neurons, transcription of the c-FOS promoter is inhibited by BRG1-dependent recruitment of a phospho-RB1-HDAC1 repressor complex. Upon calcium influx, RB1 is dephosphorylated by calcineurin, which leads to release of the repressor complex. At the same time, there is increased recruitment of CREBBP to the promoter by a CREST-dependent mechanism, which leads to transcriptional activation. The CREST-BRG1 complex also binds to the NR2B promoter, and activity-dependent induction of NR2B expression involves a release of HDAC1 and recruitment of CREBBP (By similarity).
Sequence Mass (Da): 42990
Sequence Length: 396
Domain: The MFD (multi-functional domain) domain is involved in transcription transactivation, nuclear body targeting and dimerization.
Subcellular Location: Nucleus
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Q8BW22 | MSVAFASARPRGKGEVTQQTIQKMLDENHHLIQCILDYQSKGKTAECTQYQQILHRNLVYLATIADSNQNMQSLLPAPPTQNMNLGPGALSQSGSSQGLHPQGSLSDTVSTGLPPASLMQGQIGNGPNHVSMQQTAQSTLPTTSMSLSGSGHGTGPGYSHSGPTSQSVPMQGQGAISNYVSRTNINMQSNPVSMMHQQAATSHYNSAQGGSQHYQGQAPIAMMGQGGQGGSMMGQRPMAPYRPSQQGSSQQYLGQEEYYSEQYSHSQGSAEPMSQQYYPDGHGDYAYQQSSYTEQSYDRSFEDPTQHYYEGGNSQYSQQQAGYQQGTAQQQTYSQQQYPNQQSYPGQQQGYGPAQGAPSQYSSYQQGQGQQYGSYRTSQTGPSAQQQRPYGYEQGQYGNYQQ | Function: Transcriptional activator which is required for calcium-dependent dendritic growth and branching in cortical neurons. Recruits CREB-binding protein (CREBBP) to nuclear bodies. Component of the CREST-BRG1 complex, a multiprotein complex that regulates promoter activation by orchestrating a calcium-dependent release of a repressor complex and a recruitment of an activator complex. In resting neurons, transcription of the c-FOS promoter is inhibited by BRG1-dependent recruitment of a phospho-RB1-HDAC1 repressor complex. Upon calcium influx, RB1 is dephosphorylated by calcineurin, which leads to release of the repressor complex. At the same time, there is increased recruitment of CREBBP to the promoter by a CREST-dependent mechanism, which leads to transcriptional activation. The CREST-BRG1 complex also binds to the NR2B promoter, and activity-dependent induction of NR2B expression involves a release of HDAC1 and recruitment of CREBBP.
Sequence Mass (Da): 43729
Sequence Length: 402
Domain: The MFD (multi-functional domain) domain is involved in transcription transactivation, nuclear body targeting and dimerization.
Subcellular Location: Nucleus
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Q8J0P4 | MYFKYTAAALAAVLPLCSAQTWSKCNPLEKTCPPNKGLAASTYTADFTSASALDQWEVTAGKVPVGPQGAEFTVAKQGDAPTIDTDFYFFFGKAEVVMKAAPGTGVVSSIVLESDDLDEVDWEVLGGDTTQVQTNYFGKGDTTTYDRGTYVPVATPQETFHTYTIDWTKDAVTWSIDGAVVRTLTYNDAKGGTRFPQTPMRLRLGSWAGGDPSNPKGTIEWAGGLTDYSAGPYTMYVKSVRIENANPAESYTYSDNSGSWQSIKFDGSVDISSSSSVTSSTTSTASSASSTSSKTPSTSTLATSTKATPTPSGTSSGSNSSSSAEPTTTGGTGSSNTGSGSGSGSGSGSSSSTGSSTSAGASATPELSQGAAGSIKGSVTACALVFGAVAAVLAF | PTM: The GPI-like anchor contains a phosphoceramide lipid group. The anchor position has not been determined.
Location Topology: Lipid-anchor
Sequence Mass (Da): 40284
Sequence Length: 395
Subcellular Location: Cell membrane
EC: 3.2.-.-
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P0DQH7 | RIKKPIFAFPRF | Function: Conorfamide As1a: this amidated form is active on both ASIC channels and nicotinic acetylcholine receptors (nAChRs) . Shows a weak inhibition of peak current of rat ASIC1a and rat ASIC3 . Inhibits desensitization of ASIC1a and to a lesser degree ASIC3 currents, resulting in a sustained opening of channels in the presence of low pH . Inhibits with a slow reversibility human alpha-7/CHRNA7 nAChRs (IC(50)=737-4984 nM) and with rapid reversibility human alpha-1-beta-1-delta-epsilon (CHRNA1-CHRNB1-CHRND-CHRNE) nAChRs (IC(50)=215 nM) .
PTM: Both amidated and non-amidated conorfamides As1 are found in the venom. Amidation is important since amidated peptide is more active.
Sequence Mass (Da): 1520
Sequence Length: 12
Subcellular Location: Secreted
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Q04930 | MLLSAPVNSTVRRKPHSPNKKKPKETGTAASFSSSSSTVVLSSNNDGSFDALWDPSISKASDFESSYISAKRLKPESSNRQKKKNSYKYSREENTNEVEEKTSLGSSSKTEADNIFNDQLTSAGNTTYVSNKRDVNFGANSAVVLLGLPTSKSESHRQYHSPSASTTNEDEEDIGVDILVDNHIDSCETVSINNNRGITHQYPETESDVDFDEAVILTPMDGTDKGVKNPRPLEKKYSSSCFEDRTPLNLDDGHFSECNHFSTLDVSSFFHLNEHVHKIDEVELDGPDRTFSLDNVAINTRKKDIDCLYNSSREDLSNLTCSSEGPRNDSYDSDYNIDEVTYRDDESTDEDESLPTPDRKRKKIGHKACEILDSKRIGIKVPKLYVWSLSDKPFSVIDGLCTKSLYPLSDDINTPESLSSCSSSVSSRENQKGDATFDNDAMIADLLNIGGLEVEKASNGHIELIGE | Function: Transcription factor, corepressor with FHL1 of ribosomal protein genes. May be involved in the blocking of the spread of silencing.
PTM: Phosphorylated by CDC28 and YAK1.
Sequence Mass (Da): 51697
Sequence Length: 467
Subcellular Location: Cytoplasm
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Q4WI46 | MVRIGSSLLLATLAATTVSAASDPPKCSQDSHCPEEWPCCSLYGQCGTGAYCLGGCDPLMSFSLDSCTPEPICQGKTYKDWSNLDNLASNTKYLGDASKSDWVYSGYPKVEDGNLLLTMPKNSVGTLIANNHYIWYGKITAKIKSSRGAGVVTGFILLSDTKDEIDYEFVGADLTNVQTNYYFQGVLDYNHGGNASVSGGNTFGDWHEYTIDWKPDAITWSVDGEVKRTLKKESTYNETSKQYMYPQTPSRMQLSLWPAGQASNAPGTIAWAGGEIDWDSEDIKDPGYYYATFGEITVECYDPPSGADIKGTKAYIFKDKAGLESSVQITNNKTVLASFGATGLDMDVGASSSASGSANKTSSSANTVPSGNGGSGNEPGNSHSGSSGSGTSTSDGSGSSTGFSQGSETSASSNKNAAPSQNERVLNGSFFAVLVAVVALVTL | PTM: The GPI-like anchor contains a phosphoceramide lipid group. The anchor position has not been determined.
Location Topology: Lipid-anchor
Sequence Mass (Da): 46710
Sequence Length: 443
Subcellular Location: Cell membrane
EC: 3.2.-.-
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Q8GYA4 | MRRNTDQESPIMSYYSSFFFLFLFSFLTSFRVSAQDPTYVYHTCQNTANYTSNSTYNNNLKTLLASLSSRNASYSTGFQNATVGQAPDRVTGLFNCRGDVSTEVCRRCVSFAVNDTLTRCPNQKEATLYYDECVLRYSNQNILSTLITTGGVILVNTRNVTSNQLDLLSDLVLPTLNQAATVALNSSKKFGTRKNNFTALQSFYGLVQCTPDLTRQDCSRCLQLVINQIPTDRIGARIINPSCTSRYEIYAFYTESAVPPPPPPPSISTPPVSAPPRSGKDGNSKVLVIAIVVPIIVAVLLFIAGYCFLTRRARKSYYTPSAFAGDDITTADSLQLDYRTIQTATDDFVESNKIGQGGFGEVYKGTLSDGTEVAVKRLSKSSGQGEVEFKNEVVLVAKLQHRNLVRLLGFCLDGEERVLVYEYVPNKSLDYFLFDPAKKGQLDWTRRYKIIGGVARGILYLHQDSRLTIIHRDLKASNILLDADMNPKIADFGMARIFGLDQTEENTSRIVGTYGYMSPEYAMHGQYSMKSDVYSFGVLVLEIISGKKNSSFYQTDGAHDLVSYAWGLWSNGRPLELVDPAIVENCQRNEVVRCVHIGLLCVQEDPAERPTLSTIVLMLTSNTVTLPVPRQPGLFFQSRIGKDPLDTDTTSKSLLGSVDDASITDIHPR | Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 74283
Sequence Length: 669
Subcellular Location: Membrane
EC: 2.7.11.-
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Q9ZP16 | MKQRSLFSVLCFFFISFGVASVSAQTCTTDKGTFRPNGTYDVNRRLILSSLPSNVTDQDGLYYNGSIGQQPNRVYAIGMCIPGSTSEDCSDCIKKESEFFLKNCPNQTEAYSWPGEPTLCYVRYSNTSFSGSADLNPRNWLTNTGDLDSNLTEFTKIWEGLMGRMISAASTAKSTPSSSDNHYSADSAVLTPLLNIYALMQCTPDLSSGDCENCLRQSAIDYQSCCSQKRGGVVMRPSCFLRWDLYTYSNAFDNLTVASPPPEPPVTVPQPAGDQDNPTNNDSKGISAGVVVAITVPTVIAILILLVLGFVLFRRRKSYQRTKTESESDISTTDSLVYDFKTIEAATNKFSTSNKLGEGGFGAVYKGKLSNGTDVAVKRLSKKSGQGTREFRNEAVLVTKLQHRNLVRLLGFCLEREEQILIYEFVHNKSLDYFLFDPEKQSQLDWTRRYKIIGGIARGILYLHQDSRLKIIHRDLKASNILLDADMNPKIADFGLATIFGVEQTQGNTNRIAGTYAYMSPEYAMHGQYSMKSDIYSFGVLVLEIISGKKNSGVYQMDETSTAGNLVTYASRLWRNKSPLELVDPTFGRNYQSNEVTRCIHIALLCVQENPEDRPMLSTIILMLTSNTITLPVPRLPGFFPRSRQLKLVSEGSESDQYTSKSSSFSS | Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 74139
Sequence Length: 667
Subcellular Location: Membrane
EC: 2.7.11.-
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O65472 | MPLLFLWFFLTSTSLVSALQTLPCINTTYFIPNSTYDTNRRVILSLLPSNVTSHFGFFNGSIGQAPNRVYAVGMCLPGTEEESCIGCLLSASNTLLETCLTEENALIWIANRTICMIRYSDTSFVGSFELEPHREFLSIHGYKTNETEFNTVWSRLTQRMVQEASSSTDATWSGAKYYTADVAALPDSQTLYAMMQCTPDLSPAECNLCLTESVVNYQSCCLGRQGGSIVRLSCAFRAELYPFGGAFTVMTARPLSQPPPSLIKKDSGKFSTETIAAIVVPIIVVAIIFLVLLVLSRLFARRRKSYQEIDLDQSGITTLHFQQLDFKTIEVATENFAKTNKLGQGGFGEVYKGTLVNGTEVAVKRLSKTSEQGAQEFKNEVVLVAKLQHRNLVKLLGYCLEPEEKILVYEFVPNKSLDYFLFDPTKQGQLDWTKRYNIIGGITRGILYLHQDSRLTIIHRDLKASNILLDADMIPKIADFGMARISGIDQSVANTKRIAGTFGYMPPEYVIHGQFSMKSDVYSFGVLILEIICGKKNRSFYQADTKAENLVTYVWRLWTNGSPLELVDLTISENCQTEEVIRCIHIALLCVQEDPKDRPNLSTIMMMLTNSSLILSVPQPPGFFVPQNKERDSFLSSQFTMGCTSQTKNDVTITNLDPR | Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 73720
Sequence Length: 659
Subcellular Location: Membrane
EC: 2.7.11.-
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Q0PW40 | MKQRSLLSILCFILLASGVASVSAQTCIENRKYFTPNGTYDSNRRLILSSLPNNTASRDGFYYGSIGEEQDRVYALGMCIPKSTPSDCSNCIKGAAGWLIQDCVNQTDAYYWALDPTLCLVRYSNISFSGSAAFWEIEPQYLVLNTATIASNLTEFKTIWEDLTSRTITAASAARSTPSSSDNHYRVDFANLTKFQNIYALMQCTPDISSDECNNCLQRGVLEYQSCCGNNTGGYVMRPICFFRWQLFTFSKAFHNITLATTPPLSPPPLQRPVVASQPPSADNRDKKRDNSSGKISMKTILAIVVVGIVILIIISGILARRFARKEKPYQEVELNQTGITSVRSLQYKFKTIETATNNFSERLGHGGSGHVFKGRLPDGKEIAVKRLSEKTEQSKKEFKNEVVLVAKLQHRNLVRLLGFSVKGEEKIIVYEYLPNRSLDYILFDPTKQGELDWKKRYKIIGGTARGILYLHQDSQPTIIHRDLKAGNILLDAHMNPKVADFGTARIFGMDQSVAITANAAGTPGYMAPEYMELGEFSMKSDVYSYGVLVLEIICGKRNTSFSSPVQNFVTYVWRLWKSGTPLNLVDATIAENYKSEEVIRCIHIALLCVQEEPTDRPDFSIIMSMLTSNSLILPVPKPPPSFIPGRPNQSTTRPSSQNINDGRWSLLKMMFH | Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 75295
Sequence Length: 673
Subcellular Location: Membrane
EC: 2.7.11.-
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Q8W4G6 | MSSGASFIFLFFFLTSFTASVENVFYIKHICPNTTTYSRNSPYLTNLRTLLSSLSAPNASYSTGFQSARAGQAPDRVTGLFLCRGDVSPAVCRNCVAFSINDTLVQCPSERKSVFYYDECMLRYSDQNILSTLAYDGAWIRMNGNISIDQNQMNRFKDFVSSTMNQAAVKAASSPRKFYTVKATWTALQTLYGLVQCTPDLTRQDCFSCLESSIKLMPLYKTGGRTLYSSCNSRYELFAFYNETTVRTQQAPPPLPPSSTPLVTSPSLPGKSWNSNVLVVAIVLTILVAALLLIAGYCFAKRVKNSSDNAPAFDGDDITTESLQLDYRMIRAATNKFSENNKIGQGGFGEVYKGTFSNGTEVAVKRLSKSSGQGDTEFKNEVVVVAKLQHRNLVRLLGFSIGGGERILVYEYMPNKSLDYFLFDPAKQNQLDWTRRYKVIGGIARGILYLHQDSRLTIIHRDLKASNILLDADMNPKLADFGLARIFGMDQTQENTSRIVGTFGYMAPEYAIHGQFSVKSDVYSFGVLVLEIISGKKNNSFYETDGAHDLVTHAWRLWSNGTALDLVDPIIIDNCQKSEVVRCIHICLLCVQEDPAERPILSTIFMMLTSNTVTLPVPLQPGFPVQS | Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 69705
Sequence Length: 627
Subcellular Location: Membrane
EC: 2.7.11.-
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Q8L710 | MAKTSCEIILCFFFFILSFRVISVSAQQTCDNTAGSFKPNSTYDNNRRLLLSTFASNVTAQNGYFNGSFGLGTDRVYAMGMCAPGAEPDVCSNCIKNTAEGLLQICLNQTDGFSWSGEETLCLVRYSNKSFSGLLGLEPSNDFFNVNEIRKEDQKEFDSVFDELMFRTIQGASSSVRNNSNSLSLSGKYYAKDVAPEPVYGNISVVMQCTPDVSSKDCNLCLERSLDFYKKWYNGKRGTIILRPSCFFRWELYTFFGAFDSINARHPPPPPRPLSPPPLKTPSVTNQTNITKKNDSRISGGTIAAIVVVVVVTIILIVVGLVICKRRKQKQEIELPIVLNEAESVQFDLKTIEAATGNFSEHNKLGAGGFGEVYKGMLLNGTEIAVKRLSKTSGQGEIEFKNEVVVVAKLQHINLVRLLGFSLQGEEKLLVYEFVPNKSLDYFLFDPNKRNQLDWTVRRNIIGGITRGILYLHQDSRLKIIHRDLKASNILLDADMNPKIADFGMARIFGVDQTVANTARVVGTFGYMSPEYVTHGQFSMKSDVYSFGVLILEIISGKKNSSFYQMDGLVNNLVTYVWKLWENKTMHELIDPFIKEDCKSDEVIRYVHIGLLCVQENPADRPTMSTIHQVLTTSSITLPVPQPPGFFFRNGPGSNPSSQGMVPGQSSSKSFTSSVDEATITQVNPR | Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 76354
Sequence Length: 686
Subcellular Location: Membrane
EC: 2.7.11.-
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Q8RX80 | MATKSCELVLCFFVFFVISFSAISVSAQTCDNTTGTFIPNSPYDKNRRLILSTLASNVTAQEGYFIGSIGIAPDQVFATGMCAPGSERDVCSLCIRSTSESLLQSCLDQADAFFWSGEETLCLVRYANRPFSGLLVMDPLGAIFNTGELNTNQTVFDIEWNNLTSSMIAGITSSSSGGNNSSKYYSDDIALVPDFKNISALMQCTPDVSSEDCNTCLRQNVVDYDNCCRGHQGGVMSRPNCFFRWEVYPFSGAIDQINLPKSPPPSVTSPSPIANITKNDSRISGGKIAAIVVVTVVTIILVVLGFVISNRRKQKQEMDLPTESVQFDLKTIESATSNFSERNKLGKGGFGEVYKGMLMNGTEIAVKRLSKTSGQGEVEFKNEVVVVAKLQHINLVRLLGFSLQGEEKLLVYEFVSNKSLDYFLFDPTKRNQLDWTMRRNIIGGITRGILYLHQDSRLKIIHRDLKASNILLDADMNPKIADFGMARIFGVDQTVANTGRVVGTFGYMSPEYVTHGQFSMKSDVYSFGVLILEIISGKKNSSFYQMDGLVNNLVTYVWKLWENKSLHELLDPFINQDFTSEEVIRYIHIGLLCVQENPADRPTMSTIHQMLTNSSITLPVPLPPGFFFRNGPGSNPGQSNSKSFACSVDEATITDVNPR | Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 72799
Sequence Length: 659
Subcellular Location: Membrane
EC: 2.7.11.-
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Q8GWJ7 | MSSLISFIFLFLFSSITASAQNTFYLYHNCSVTTTFSSNSTYSTNLKTLLSSLSSLNASSYSTGFQTATAGQAPDRVTGLFLCRVDVSSEVCRSCVTFAVNETLTRCPKDKEGVFYYEQCLLRYSNRNIVATLNTDGGMFMQSARNPLSVKQDQFRDLVLTPMNLAAVEAARSFKKWAVRKIDLNASQSLYGMVRCTPDLREQDCLDCLKIGINQVTYDKIGGRILLPSCASRYDNYAFYNESNVGTPQDSSPRPGKGGNSSVIIIAVVVPITVLFLLLVAVFSVRAKNKRTLNEKEPVAEDGNDITTAGSLQFDFKAIEAATNCFLPINKLGQGGFGEVYKGTLSSGLQVAVKRLSKTSGQGEKEFENEVVVVAKLQHRNLVKLLGYCLEGEEKILVYEFVPNKSLDHFLFDSTMKMKLDWTRRYKIIGGIARGILYLHQDSRLTIIHRDLKAGNILLDDDMNPKIADFGMARIFGMDQTEAMTRRVVGTYGYMSPEYAMYGQFSMKSDVYSFGVLVLEIISGMKNSSLYQMDESVGNLVTYTWRLWSNGSPSELVDPSFGDNYQTSEITRCIHIALLCVQEDAEDRPTMSSIVQMLTTSLIALAEPRPPGFFFRSKQEQAGPSIDSSTHCSVDEASITRVTPR | Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 71620
Sequence Length: 645
Subcellular Location: Membrane
EC: 2.7.11.-
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Q9LMB9 | MQICASIAQFLAWVSFLVLLATVGSSSSSESLLNCQPLDHHLVNPSRLLGFLRAMSSVNDFITNDKLWVVSSITDVSPPIYVFLQCREDLSVSDCRHCFNESRLELERKCSGSGGRIHSDRCFLRFDDRDFSEEFVDPTFDKANCEETGTGFGEFWRFLDEALVNVTLKAVKNGGFGAASVIKTEAVYALAQCWQTLDENTCRECLVNARSSLRACDGHEARAFFTGCYLKYSTHKFFDDAAEHKPDADQRNFIRSSFFPHLSDRDVTRLAIAAISLSILTSLGAFISYRRVSRKRKAQVPSCVNFKYEMLEKATESFHDSMKLGQGGAGSVYKGILPDGRIVAVKKLFFNTREWADQFFNEVNLISGVQHKNLVRLLGCSIEGPKSLLVYEYVHNRSLDQILFMKNTVHILSWKQRFNIIIGISEGLEYLHRGSEVKIIHRDIKTSNILLDRNLSPKIADFGLIRSMGTDKTQTNTGIAGTLGYLAPEYLIKGQLTEKADVYAFGVLIIEIVTGKKNNAFTQGTSSVLYSVWEHFKANTLDRSIDPRLKGSFVEEEALKVLQIGLLCVQSSVELRPSMSEIVFMLQNKDSKFEYPKQPPFLSASVLMPDEETRV | Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 69176
Sequence Length: 615
Subcellular Location: Membrane
EC: 2.7.11.1
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Q12126 | MDIEKSDKWTYVKERKVGEGTYAVVFLGRQKETNRRVAIKKIKVGQFKDGIDISALREIKFLRESRHDNVIELVDVFSTKSNLNIILEFLDSDLEMLIKDKFIVFQPAHIKSWMVMLLRGLHHIHSRFILHRDLKPNNLLISSDGVLKLADFGLSRDFGTPSHMSHQVITRWYRPPELFMGCRSYGTGVDMWSVGCIFAELMLRTPYLPGESDLDQLNVIFRALGTPEPEVIKSMQQLPNYVEMKHIPPPNGGMEALFSAAGHEEIDLLKMMLDYNPYRRPTAQQALEHHYFSALPKPTHPSLLPRKGGEEGIKHVSSDLQRQNNFPMRANIKFV | Function: Protein kinase essential for cell proliferation, where it is required for completion of cytokinesis. Phosphorylates the C-terminal repeat domain (CTD) of RNA polymerase II.
Catalytic Activity: [DNA-directed RNA polymerase] + ATP = ADP + H(+) + phospho-[DNA-directed RNA polymerase]
Sequence Mass (Da): 38538
Sequence Length: 335
Subcellular Location: Cytoplasm
EC: 2.7.11.23
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Q3E9X6 | MQKNKMVDLRAIFWFVVISSCAVAAPTCIQRSDFFKANGPYDINLRAMLSSLPSRVKDNEGFYKTPFKPGPNIAHGLGMCSRGTTTQDCSDCITSVSHTLLHTCPNQAEAIDWSSGDSLCLVRYSNHLINGSLDEDIIWAEYIEYKYNTSFGQTNLTEFKSTWQALMDRVINKVDGSLYANSIQELGSFPFRSIYAIAQCNKDLTKLNCEKCLQHLRIDNRSCCRGIQVGYIARTSCFMRWDLQPFLGLFINGMLPTPPSELDNGHSNTTKKDGKNISTGSIVAIAVVSVVVSTVLLALGYAVSRRRKAYQSFASENGYFSVSRRPRRPYGTASPDDATDDLTASSGSLRFDFRAIKAATSNFHKSNKLGHGGFGAVYKGMFPNGTEVAAKRLSKPSDQGEPEFKNEVLLVARLQHKNLVGLLGFSVEGEEKILVYEFVPNKSLDHFLFDPIKRVQLDWPRRHNIIEGITRGILYLHQDSRLTIIHRDLKASNILLDAEMNPKIADFGLARNFRVNQTEANTGRVVGTFGYMPPEYVANGQFSTKSDVYSFGVLILEIIGGKKNSSFHQIDGSVSNLVTHVWRLRNNGSLLELVDPAIGENYDKDEVIRCIHIGLLCVQENPDDRPSMSTIFRMLTNVSITLPVPQPPGFFFRERSEPNPLAERLLPGPSTSMSFTCSVDDASITSVRPR | Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 76859
Sequence Length: 690
Subcellular Location: Membrane
EC: 2.7.11.-
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O65482 | MSSWASFIFLFIFSFLTSFRVFAQDPTYRYHSCPNTTIFSRDSAYFSNLQTLLSFLSSPDASSSYSSGFRNDAVGTFPDRVTGLFDCRGDLPPEVCHNCVAFAVKDTLIRCPNERDVTLFYDECTLRYSNLVVTSALDPTYVYHVCPSWATFPRSSTYMTNLITLLSTLSSPSASYSTGFQNATAGKHPDRVTGLFNCRGDVSPEVCRRCVSFAVNETSTRCPIEKEVTLYYDQCTLRYSNRNILSTSNTNGGIILANSQNMTSNEQARFKDLVLTTMNQATIAAANSSKRFDARSANFTTLHSLYTLVQCTHDLTRQDCLSCLQQIINQLPTEKIGGQFIVPSCSSRFELCLFYNQSAVTTPQPQQNSAPPPPPTSIPSPRPGLNSRFPLITCLSAVSFEKFKDLLKPGFICILIKIVSENTGKGGNSSVIIIAVVVSITALLLLFVAVFSVRTKRRKKMIGAIPLLNVKRKDTEVTEPLAENGDSITTAGSLQFDFKAIVAATNNFLPINKLGQGGFGEVYKGTFPSGVQVAVKRLSKTSGQGEREFENEVVVVAKLQHRNLVRLLGYCLEGEEKILVYEFVHNKSLDYFLFDTTMKRQLDWTRRYKIIGGIARGILYLHQDSRLTIIHRDLKAGNILLDADMNPKVADFGMARIFGMDQTEANTRRVVGTYGYMAPEYAMYGQFSMKSDVYSFGVLVFEIISGMKNSSLYQMDDSVSNLVTYTWRLWSNGSQLDLVDPSFGDNYQTHDITRCIHIALLCVQEDVDDRPNMSAIVQMLTTSSIVLAVPKQPGFFFRGRHEQVGEVGSSVDRLALCSIDDASITSVAPR | Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 92316
Sequence Length: 830
Subcellular Location: Membrane
EC: 2.7.11.-
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Q9N623 | MKFASKKNNQKNSSKNDERYRELDNLVQEGNGSRLGGGSCLGKCAHVFKLIFKEIKDNIFIYILSIIYLSVCVMNKIFAKRTLNKIGNYSFVTSETHNFICMIMFFIVYSLFGNKKGNSKERHRSFNLQFFAISMLDACSVILAFIGLTRTTGNIQSFVLQLSIPINMFFCFLILRYRYHLYNYLGAVIIVVTIALVEMKLSFETQEENSIIFNLVLISALIPVCFSNMTREIVFKKYKIDILRLNAMVSFFQLFTSCLILPVYTLPFLKQLHLPYNEIWTNIKNGFACLFLGRNTVVENCGLGMAKLCDDCDGAWKTFALFSFFNICDNLITSYIIDKFSTMTYTIVSCIQGPAIAIAYYFKFLAGDVVREPRLLDFVTLFGYLFGSIIYRVGNIILERKKMRNEENEDSEGELTNVDSIITQ | Function: May regulate endogenous transporter.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 48675
Sequence Length: 424
Subcellular Location: Vacuole membrane
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Q4UDS9 | MLKEGSSLDLSASSSSGTLRSDNSFGNSPLDRITSLLILIYKSIRACFKWIYSKSFGIICILFVILDVLTTVFFKRFIDHTKNYVMFTIQVIIFTFWIIVCCIAILCFLFNREYMKRHFNVRPLVFLGFLDMLSTGLSANGSAHTSGLMLVLLGQISVPLTMVSCKLILSKKYHHYQYISSAIILTFAVLKPILNRTDTTDNRFYNNMLYLLASVPDSIASALREKQYTSKFFHVVKYQFFGFLFHFFYNILYTLLFTLPFNSVKGYFDSLYKLCVNGYKCIFFGVNTITENCGPTLIPTCDNCLEAFKIYCLYILFSSAIRVAYVFIMLDGSVTFTLLLGTVKVPLTSIAFSLRFIAGDSTTSFNLLDVVCFLGIVAGLLLYALGSKKIQEETDLLESPLIDDAESEHELLSTGTEKLMRSEICHDLFT | Function: May regulate endogenous transporter.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 48721
Sequence Length: 430
Subcellular Location: Vacuole membrane
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P15455 | MARVSSLLSFCLTLLILFHGYAAQQGQQGQQFPNECQLDQLNALEPSHVLKSEAGRIEVWDHHAPQLRCSGVSFARYIIESKGLYLPSFFNTAKLSFVAKGRGLMGKVIPGCAETFQDSSEFQPRFEGQGQSQRFRDMHQKVEHIRSGDTIATTPGVAQWFYNDGQEPLVIVSVFDLASHQNQLDRNPRPFYLAGNNPQGQVWLQGREQQPQKNIFNGFGPEVIAQALKIDLQTAQQLQNQDDNRGNIVRVQGPFGVIRPPLRGQRPQEEEEEEGRHGRHGNGLEETICSARCTDNLDDPSRADVYKPQLGYISTLNSYDLPILRFIRLSALRGSIRQNAMVLPQWNANANAILYVTDGEAQIQIVNDNGNRVFDGQVSQGQLIAVPQGFSVVKRATSNRFQWVEFKTNANAQINTLAGRTSVLRGLPLEVITNGFQISPEEARRVKFNTLETTLTHSSGPASYGRPRVAAA | Function: Seed storage protein.
PTM: Phosphorylated in seeds on some Tyr residues in response to abscisic acid (ABA).
Sequence Mass (Da): 52595
Sequence Length: 472
Subcellular Location: Protein storage vacuole
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Q96318 | MVKLSNLLVATFGVLLVLNGCLARQSLGVPPQLQNECNLDNLDVLQATETIKSEAGQIEYWDHNHPQLRCVGVSVARYVIEQGGLYLPTFFTSPKISYVVQGTGISGRVVPGCAETFMDSQPMQGQQQGQPWQGRQGQQGQPWEGQGQQGQQGRQGQPWEGQGQQGQQGRQGQQGQPWEGQGQQGQQGFRDMHQKVEHVRRGDVFANTPGSAHWIYNSGEQPLVIIALLDIANYQNQLDRNPRVFHLAGNNQQGGFGGSQQQQEQKNLWSGFDAQVIAQALKIDVQLAQQLQNQQDSRGNIVRVKGPFQVVRPPLRQPYESEEWRHPRSPQGNGLEETICSMRSHENIDDPARADVYKPSLGRVTSVNSYTLPILEYVRLSATRGVLQGNAMVLPKYNMNANEILYCTGGQGRIQVVNDNGQNVLDQQVQKGQLVVIPQGFAYVVQSHGNKFEWISFKTNENAMISTLAGRTSLLRALPLEVISNGFQISPEEARKIKFNTLETTLTRAAGRQQQQLIEEIVEA | Function: Seed storage protein.
PTM: Proteolytically processed during seed maturation at a conserved Asn-Gly peptide bond by an asparaginyl endopeptidase to produce two mature polypeptides referred to as alpha and beta subunits that are joined together by a disulfide bond.
Sequence Mass (Da): 58235
Sequence Length: 524
Subcellular Location: Protein storage vacuole
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Q9ZWA9 | MHKLLFSLLSVVSLSFLLFFHGAEARQREAPFPNACHFSQINSLAPAQATKFEAGQMEVWDHMSPELRCAGVTVARITLQPNSIFLPAFFSPPALAYVVQGEGVMGTIASGCPETFAEVEGSSGRGGGGDPGRRFEDMHQKLENFRRGDVFASLAGVSQWWYNRGDSDAVIVIVLDVTNRENQLDQVPRMFQLAGSRTQEEEQPLTWPSGNNAFSGFDPNIIAEAFKINIETAKQLQNQKDNRGNIIRANGPLHFVIPPPREWQQDGIANGIEETYCTAKIHENIDDPERSDHFSTRAGRISTLNSLNLPVLRLVRLNALRGYLYSGGMVLPQWTANAHTVLYVTGGQAKIQVVDDNGQSVFNEQVGQGQIIVIPQGFAVSKTAGETGFEWISFKTNDNAYINTLSGQTSYLRAVPVDVIKASYGVNEEEAKRIKFSQQETMLSMTPSSSS | Function: Seed storage protein.
PTM: Ubiquitinated.
Sequence Mass (Da): 49675
Sequence Length: 451
Subcellular Location: Protein storage vacuole
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A0A0A1GNF2 | MGSGKDRTLAGWTLPETKTDATAQFDRFVTENRFTIAVVFPLVGAVTLLASAEGLLPDPLAFNPYFVLFGTFVMRLPLVAGIFPLVDRRAGLALVALTLYSYGIELVGVRTGWPYGEFTYGVDLGPMLLGDVPFGLPVFFFPLVLNAYLLVLLLLGNRAASTTVRLLSTLATVMLVDLVLDPGAVAIGFWIYEMPQFYGVPWQNYAGWLLSGSVAVLLFDFGFDRAGLRRRLRDCPFMLDDLVSFVLLWGGINLFYTNWVPFGLAALLGAGLLWTDRFDFDLSETRLGRAVWR | Function: Involved in the biosynthesis of the acyclic C50 carotenoid bacterioruberin (BR). Catalyzes the reaction that introduces hydroxyl groups to C3'' and C3''' of bisanhydrobacterioruberin (BABR) to generate BR.
Catalytic Activity: bacterioruberin = bisanhydrobacterioruberin + 2 H2O
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 32402
Sequence Length: 293
Pathway: Carotenoid biosynthesis.
Subcellular Location: Membrane
EC: 4.2.1.161
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Q5XEZ5 | MATLQDIGVSAGINILSAFVFFIIFAVLRLQPFNDRVYFSKWYLKGLRSSPARGGAFAQRFVNLDFRSYMKFLNWMPEALKMPEPELIDHAGLDSVVYLRIYWLGLKIFTPIAVLAWAVLVPVNWTNNTLEMAKQLRNVTSSDIDKLSVSNIPEYSMRFWTHIVMAYAFTIWTCYVLMKEYETIANMRLQFVASEARRPDQFTVLVRNVPPDADESVSELVEHFFLVNHPDHYLTHQVVCNANKLADLVKKKKKLQNWLDYYQLKYARNNSQRIMVKLGFLGLWGQKVDAIEHYIAEIDKISKEISKEREEVVNDPKAIMPAAFVSFKTRWAAAVCAQTQQTRNPTQWLTEWAPEPRDVFWSNLAIPYVSLTVRRLIMHVAFFFLTFFFIVPIAFVQSLATIEGIVKAAPFLKFIVDDKFMKSVIQGFLPGIALKLFLAFLPSILMIMSKFEGFTSISSLERRAAFRYYIFNLVNVFLASVIAGAAFEQLNSFLNQSANQIPKTIGVAIPMKATFFITYIMVDGWAGVAGEILMLKPLIMFHLKNAFLVKTDKDREEAMDPGSIGFNTGEPRIQLYFLLGLVYAPVTPMLLPFILVFFALAYIVYRHQIINVYNQEYESAAAFWPDVHGRVIAALVISQLLLMGLLGTKHAALAAPFLIALPVLTIGFHHFCKGRYEPAFIRYPLQEAMMKDTLETAREPNLNLKGYLQNAYVHPVFKGDEDDYDIDDKLGKFEDEAIIVPTKRQSRRNTPAPSIISGDDSPSLPFSGKLV | Function: Acts as an osmosensitive calcium-permeable cation channel . Specifically conducts cations including Ca(2+), K(+) and Na(+) in vitro. Inactivation or closure of the channel is calcium-dependent . Mechanosensitive ion channel that converts mechanical stimuli into a flow of ions .
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 87894
Sequence Length: 771
Subcellular Location: Membrane
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X1WEM4 | MAFESWPAGGVRPVEELDVRSFLMEENSTAERCYRSHSRSSVLQGLPFGGVPTVLAINVVLWLILLLIFSCLRKAAWDYGRLALLMKNDSLTSLFYGEQSEKEKTPSDSSPSDSETKDMGFCSWLTSLYHMKDEEIRSKCGIDAVTYLSFQRHIILLMMVVCLLSLTIILPVNLSGNLLGDNPENFGRTTVVNVPAQNIFLWLHSIFALLYFVITVLCMAHHSSRLEYREDEKVARTLMITSIPREISDPGLITKHLHEAYPSCTVTDIHFCFNVQKLMKLDSERRKAMKGRLYFTTKAQKNGRIMIKTHPCAQIFCCDICGFEKVDAEQYYSELEEKLTDEFNAEKNWISMKRLGIAFVTFRDERMTAVIVKDYSRARCRHKPQQSSITTVVRSHQWDVSYAPAPNDIIWENLSVCGPRWWLRCILLNILLFLLLFFLTTPAIIVNTMDKFNVTRPVESLRNPVITQFFPTLLLWAFSILLPFIVYYSSFFEYHWTRSGENQVTMHKCFLLLVFMVIILPSLGLSSLNLFFRWLFDVRFLDETDVKFQCVFLPDNGAFFVNYVITSSLIGTAMELLRIPALLVYSLRLCFAKSKAECIHVKISQAYEFQFGLEYAWTMCIFSVSMTYSITCPVIVPFGLLYLVLKHMVDRYNIYYAYTPTKLNQRIHAAAISQVVVAPILCMFWLLFFSVLRLGPVQPITLFTFITLLCSIAFSCFGFCMKKLRADRSTSYQMSDQTTEGGFSDAERSTISTTATANLFIASVLLEPELGLTPMPSPAHQSYGTMVNSQSSVRDAEEDEEKDLEETLETELKDDLLMDSPVAFQ | Function: Acts as an osmosensitive calcium-permeable cation channel (By similarity). Required for the functional integrity of the kidney glomerular filtration barrier .
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 94430
Sequence Length: 825
Subcellular Location: Cell membrane
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Q9P1W3 | MSASPDDLSTGGRLQNMTVDECFQSRNTVLQGQPFGGVPTVLCLNIALWVLVLVVYSFLRKAAWDYGRLALLIHNDSLTSLIYGEQSEKTSPSETSLEMERRDKGFCSWFFNSITMKDEDLINKCGDDARIYIVFQYHLIIFVLIICIPSLGIILPINYTGSVLDWSSHFARTTIVNVSTESKLLWLHSLLSFFYFITNFMFMAHHCLGFAPRNSQKVTRTLMITYVPKDIEDPELIIKHFHEAYPGSVVTRVHFCYDVRNLIDLDDQRRHAMRGRLFYTAKAKKTGKVMIRIHPCARLCFCKCWTCFKEVDAEQYYSELEEQLTDEFNAELNRVPLKRLDLIFVTFQDSRMAKRVRKDYKYVQCGVQPQQSSVTTIVKSYYWRVTMAPHPKDIIWKHLSVRRFFWWARFIAINTFLFFLFFFLTTPAIIMNTIDMYNVTRPIEKLQNPIVTQFFPSVMLWGFTVILPLIVYFSAFLEAHWTRSSQNLVMVHKCYIFLVFMVVILPSMGLTSLDVFLRWLFDIYYLEQASIRFQCVFLPDNGAFFVNYVITAALLGTGMELLRLGSLFCYSTRLFFSRSEPERVNIRKNQAIDFQFGREYAWMMNVFSVVMAYSITCPIIVPFGLLYLCMKHLTDRYNMYYSFAPTKLNEQIHMAAVSQAIFAPLLGLFWMLFFSILRLGSLHAITIFSLSTLLIAMVIAFVGIFLGKLRMVADYEPEEEEIQTVFDMEPSSTSSTPTSLLYVATVLQEPELNLTPASSPARHTYGTMNNQPEEGEEESGLRGFARELDSAQFQEGLELEGQNQYH | Function: Acts as an osmosensitive calcium-permeable cation channel . Required for the functional integrity of the kidney glomerular filtration barrier (By similarity).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 93317
Sequence Length: 806
Subcellular Location: Cell membrane
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Q09809 | MAFNGYGIFDSDPRKNPSSDLRTQFWLAFLLGASACVFFCFFRKRWKVLYAPRTTIEGLNLPTLSSSYYKWLMDLVNIPDDVVQNCAGLDGYVFLLFFKMGIKFLSFASLLGVLIIMPVNKHFRGDAFGNITLSMPAKSEYFFSSPLVKKSIVQSPIIANGSELNVGVLGPSLFNPIGNLSDIPGLPQPGDGFLYLYVLFTYFISIFLLYVLFSSTKSIADIRQSYLARQNRLTDRTVFISGLPNELCSTENLKAYFDKLDVGSIDSLSICRNYSYMDILLSKKSKYVKKLEKYWSIYLSNCKKLGISTLPPSNYLSPNRAELESTPEQLLEVPWQHHQCHPLIKTHFFGIFGQKIDAIDFYSAKLYKISQQIENARSFDYPTTGQAFITFESMATAQIVAQTHIDSKSLMGLHIELAPAANDIQWHNTYIGRWHKFFQGWFITLVTFMIILLWTVPVGAIAVFINLDTIRRLWPELGRMIEDLPFLNSLLRTFLPTLVYSLFISISPFLFRWLSSMQGLSSRAEEEIYAVGKNYAYLFVNFFLVYVIAGSTSIWELAKDTTSFAHFLANRLPHQAQFFIDLIVLQGIGMFPLKLIQLGKLSSYFVRRSFVPYSIASKKFETPDSFSVGIFLPQPMFIMLICLCYSIISPLILVFGLIYFIIGFLVYKYELIYQMEHPQHSTGELWSTIFLRMIFGCVIMQLTMMGLMSLRKAYWLSTVIFPLLCFTVISAYNFSTMIRSSMQFVSLYYIRTHQSNTLSSESESRNSESSGSYVHPGFDLSNEELPLIDLNTA | Function: Acts as an osmosensitive calcium-permeable cation channel.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 90573
Sequence Length: 793
Subcellular Location: Vacuole membrane
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Q06538 | MTSYIERLKSAASYLDTVPDEHHDFRKPTAKVVTTQLTIATSLGIFALLSFSILLKKWPRLYASRRYKDDGNLRLPSWNQSSLFGWLTVLYKIRDEQILEYAGLDAYVFLSFFKMCIKLLSIFCFFSVCVISPVRYHFTGKIDDGNDDDDSESSLIHLVKRIVEGSGDGDNHSAPERTNVYLWMYVLFTYFFTFIAIKMAVAETKHVVSTRQAYLGKQNTITDRTIRLSGIPIELRDSEALKTRIEQLKIGTVSSITICREWGPLNKLFHCRKKILKNLELKYSECPRELRTRQPYSENYHLLGNEQSGAVTHGENVPSSNNNDEDTILYSQISLGERPKMKIGYRGIFGKEVDAIEYLEQQLKFIDAEIIEARKQHYSATPTAFVTMDSVANAQMAAQAVLDPRVHYFITRLAPAPHDIKWDHVCLSRKDRLTKVYSTTVFIGLSSLFLVIPVSYLATLLNLKTLSKFWPSVGQLLKDHQWAANIVTGLLPTYLFTLLNFGIPYFYEYLTSYQGLVSYSEEEISLVSKNFFYIFVNLFLVFTLAGTASNYWAYLSDTTKIAYQLATSVKEFSLFYVDLIILQGIGMFPFKLLLVGSLIGFPLVKIKAKTPRQRNELYNPPIFNFGLQLPQPILILIITLIYSVMSTKILTSGLAYFIIGFYVYKYQLIFATDHLPHSTGKVWPLIFRRIIVGLLLFQLTMTGTLAGFEGGWVLSSCLFPLPVVTLCFLYDFEKNYLPLSKYIALSSIREYERDNSTVNSANEEESYAYPYAVSELEGPMLD | Function: Acts as an osmosensitive calcium-permeable cation channel.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 89344
Sequence Length: 782
Subcellular Location: Membrane
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Q49Z29 | MQNFKELGISDKMAETLQSMGFNEATPIQKESIPLALEGKDVLGQAQTGTGKTGAFGIPLIEKVADQEGVQSLILAPTRELAMQVAESLKAFAKGQNIQVVTVFGGMPIDRQIKALKKGPQIVVGTPGRVIDHLNRRTLKTNDIHTLILDEADEMMNMGFIDDMKFIMDKIPAEQRQTMLFSATMPKAIQTLVQQFMKSPVIVKTMNNEMSDPQIEEYYTIVKELEKFDTFTSFLDVHQPELAIVFGRTKRRVDELTSALISKGYKAEGLHGDITQAKRLEVLKKFKNDQLDILVATDVAARGLDISGVSHVYNFDIPQDTESYTHRIGRTGRAGKKGVAITFVNPIEMDYIRQIEQANKRQMTALRPPHRKEVLKARENDIKGKVQNWMSRDNEPRLQRIATELLGEYNDVDLIASLLQELVESNDEVDVQLTFEKPLSRGKGRQGKGGPKRGGNHKRGGGKFDNKNRRSGKGGFNNKKKNDRPSSDRNNNKKSMKGRTFADHKK | Function: DEAD-box RNA helicase possibly involved in RNA degradation. Unwinds dsRNA in both 5'- and 3'-directions, has RNA-dependent ATPase activity.
Catalytic Activity: ATP + H2O = ADP + H(+) + phosphate
Sequence Mass (Da): 56734
Sequence Length: 506
Subcellular Location: Cytoplasm
EC: 3.6.4.13
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P54475 | MKETKFELYELKPFIIDAVHRLGFYEPTDIQKRLIPAVLKKESVIGQSQTGTGKTHAYLLPLLNKIDPAKDVVQVVITAPTRELANQIYQEALKITQGEEGSQIRSKCFIGGTDKQKSIDKLKIQPHLVVGTPGRIADLIKEQALSVHKAESLVIDEADLMLDMGFLADVDYIGSRMPEDLQMLVFSATIPEKLKPFLKKYMENPKYAHVEPKQVTAAKIEHILIPSKHRDKDKLLFDIMSHLNPYLGIVFANTKNTADHIAQYLTGKGMKIGLLHGGLTPRERKKVMKQINDLEFTYIIATDLAARGIDIKGVSHVINYELPDDLDFYVHRVGRTARAGSSGQAMTIYELTDEDALVRLEKMGIEFEYLELEKGEWKKGDDRQRRKKRKKTPNEADEIAHRLVKKPKKVKPGYKKKMSYEMEKIKKKQRRNQSKKRK | Function: DEAD-box RNA helicase that plays a role in 70S ribosome assembly. May work in conjunction with the cold shock proteins to ensure proper initiation of transcription at low and optimal temperatures.
Catalytic Activity: ATP + H2O = ADP + H(+) + phosphate
Sequence Mass (Da): 50027
Sequence Length: 438
Subcellular Location: Cytoplasm
EC: 3.6.4.13
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Q8Y755 | MTKKSRFDQFGFQPFIGLAIDKLGFYEPTEVQQKLIPGILKGESIIGQSQTGTGKTHTFILPIINNVNPEKDAVQAVITAPSRELATQIYNEIRKVTKYSEKEIAVQLVIGGTDKQRAIDKLKKQPQIIVGTPGRINDLIREQALFVHTAKTLVIDEADMTLDMGFLNDVDHIAGKMPANLQMLVFSATIPQKLKPFLSKYMENPRYEHIQPKVAASKTVEHRIMATRSRNKLDLLKNVLVGSQPYLAIVFTNTKTTADEVANGLIERGLKVAKIHGDVNPRERKRTMKQIENLDYQYVVATDLAARGIDIQGISHVVNYELPDDLDFYIHRTGRTGRAGHSGIALTLFEPADEDRLNQLEKMGIEFKHVDWKNKEFVTLEDRNRRAKREAKRETADPREIGMRKKAKQKGKPNYKKKINYKMNEIKRRERRKKR | Function: DEAD-box RNA helicase involved in cold tolerance, motility, and tolerance to heat, alkali and oxidative stress.
Catalytic Activity: ATP + H2O = ADP + H(+) + phosphate
Sequence Mass (Da): 49651
Sequence Length: 435
Subcellular Location: Cytoplasm
EC: 3.6.4.13
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Q2FY15 | MAKHPFEQFNLESSLIDAVKDLNFEKPTEIQNRIIPRILKRTNLIGQSQTGTGKSHAFLLPLMQLIDSEIKEPQAIVVAPTRELAQQLYDAANHLSQFKAGVSVKVFIGGTDIEKDRQRCNAQPQLIIGTPTRINDLAKTGHLHVHLASYLVIDEADLMIDLGLIEDVDYIAARLEDNANIAVFSATIPQQLQPFLNKYLSHPEYVAVDSKKQNKKNIEFYLIPTKGAAKVEKTLNLIDILNPYLCIIFCNSRDNANDLARSLNEAGIKVGMIHGGLTPRERKQQMKRIRNLEFQYVIASDLASRGIDIEGVSHVINFDVPNDIDFFTHRVGRTGRGNYKGVAITLYSPDEEHNISLIEDRGFVFNTVDIKDGELKEVKAHNQRQARMRKDDHLTNQVKNKVRSKIKNKVKPGYKKKFKQEVEKMKRQERKQFSKQQNRQKRKQNKKG | Function: Probable DEAD-box RNA helicase. May work in conjunction with the cold shock proteins to ensure proper initiation of transcription at low and optimal temperatures.
Catalytic Activity: ATP + H2O = ADP + H(+) + phosphate
Sequence Mass (Da): 51081
Sequence Length: 448
Subcellular Location: Cytoplasm
EC: 3.6.4.13
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Q81E85 | MIKDMQPFLQQAWEKAGFKELTEIQKQAIPTILEGQDVIAESPTGTGKTLAYLLPLLHKINPEVKQPQVVVLAPTRELVMQIHEEVQKFTAGTEISGASLIGGADIKRQVEKLKKHPRVIVGSPGRILELIRMKKLKMHEVKTIVFDEFDQIVKQKMMGAVQDVIKSTMRDRQLVFFSATMTKAAEDAARDLAVEPQLVRVTRAESKSLVEHTYIICERREKNDYVRRIMHMGDVKAVAFLNDPFRLDEITEKLKFRKMKAAALHAEASKQEREATMRAFRGGKLEILLATDIAARGIDIDDLTHVIHLELPDTVDQYIHRSGRTGRMGKEGTVVSLVTPQEERKLLQFAKKLGIVFTKQEMFKGSFVETKPKAPKKKKPAFTGKKKPR | Function: DEAD-box RNA helicase. Probably has an RNA-dependent ATPase activity and a 3' to 5' RNA helicase activity that uses the energy of ATP hydrolysis to destabilize and unwind short RNA duplexes.
Catalytic Activity: ATP + H2O = ADP + H(+) + phosphate
Sequence Mass (Da): 44067
Sequence Length: 389
EC: 3.6.4.13
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Q7XHV0 | MALSPAAAGRTGRNNNNDAGLADPLLPAGGGGGGGKDKYWVPADEEEEICRGEDGGRPPAPPLLYRTFKVSGVLLHPYRLLTLVRLIAVVLFLAWRLKHRDSDAMWLWWISIAGDFWFGVTWLLNQASKLNPVKRVPDLSLLRRRFDDGGLPGIDVFINTVDPVDEPMLYTMNSILSILATDYPADRHAAYLSDDGASLAHYEGLIETARFAALWVPFCRKHRVEPRAPESYFAAKAAPYAGPALPEEFFGDRRLVRREYEEFKARLDALFTDIPQRSEASVGNANTKGAKATLMADGTPWPGTWTEPAENHKKGQHAGIVKVMLSHPGEEPQLGMPASSGHPLDFSAVDVRLPILVYIAREKRPGYDHQKKAGAMNAQLRVSALLSNAPFIFNFDGDHYINNSQAFRAALCFMLDCRHGDDTAFVQFPQRFDDVDPTDRYCNHNRVFFDATLLGLNGVQGPSYVGTGCMFRRVALYGADPPRWRPEDDDAKALGCPGRYGNSMPFINTIPAAASQERSIASPAAASLDETAAMAEVEEVMTCAYEDGTEWGDGVGWVYDIATEDVVTGFRLHRKGWRSMYCAMEPDAFRGTAPINLTERLYQILRWSGGSLEMFFSRNCPLLAGCRLRPMQRVAYANMTAYPVSALFMVVYDLLPVIWLSHHGEFHIQKPFSTYVAYLVAVIAMIEVIGLVEIKWAGLTLLDWWRNEQFYMIGATGVYLAAVLHIVLKRLLGLKGVRFKLTAKQLAGGARERFAELYDVHWSPLLAPTVVVMAVNVTAIGAAAGKAVVGGWTPAQVAGASAGLVFNVWVLVLLYPFALGIMGRWSKRPCALFALLVAACAAVAAGFVAVHAVLAAGSAAPSWLGWSRGATAILPSSWRLKRGF | Function: May catalyze both beta-1,3 and beta-1,4 glycosidic linkage on beta-D-glucan. Essential for (1,3;1,4)-beta-D-glucans synthesis in grasses and cereals (Poaceae). The mixed-linked glucans (which are not present in walls of dicotyledons or most other monocotyledonous plants) are particularly important constituents of the walls of the starchy endosperm and aleurone cells of cereal grains such as oats, wheat, rice and barley. They can account for up to 70% by weight of the wall (By similarity).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 97089
Sequence Length: 884
Subcellular Location: Golgi apparatus membrane
EC: 2.4.1.-
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Q8VYR4 | MEPQRKHSTALHTCHPCRRTIPYRIYAVFHTCGIIALMYHHVHSIVNANNTLITCLLLLSDIVLAFMWATTTSLRLNPIHRTEYPEKYAAKPEDFPKLDVFICTADPYKEPPMMVVNTALSVMAYEYPSHKISVYVSDDGGSSLTLFALMEAAKFSKHWLPFCKNNNVQDRSPEVYFSSKSHSSSDEAENLKMMYEDMKSRVEHVVESGKVETAFIACDQFSCVFDLWTDKFTRHDHPTIIMVLQHNETEMMPNLIYVSREKSKVSPHHFKAGALNTLLRVSAVMTNSPIILTLDCDMYSNNPTTPLHALCYLSDPKINFDLGFVQFPQKFQGVNKNDIYASELKRPFDINTVGFDGLMGPVHMGTGCFFNRRAFYGPPTTLILPEIETFGPNRIADKPIKAQDILALAHDVAGCNYECNTNWGSKIGFRYGSLVEDYFTGFMLHCEGWRSIFCSPTKAAFYGDSPKCLTDVIGQQIRWSVGLLEVAFSRYNPLTYGIKPLSLLMSLGYCHYAFWPFWCIPLVVYGILPQVALIHGVSVFPKASDPWFWLYIILFLGGYAQDLSDFLLEGGTYRKWWNDQRMWMVRGLSSFFFGFTEFTLKTLNLSTQGYNVTSKSNDDNEQMKRYEQEIFDFGPSSSMFLPITTVAIMNLLAFMRGLYGIFTWGEGPVLELMLASFAVVNCLPIYEAMVLRIDDGKLPKRICFLAGLLSFVLTGSGYFFLK | Function: Thought to be a Golgi-localized beta-glycan synthase that polymerize the backbones of noncellulosic polysaccharides (hemicelluloses) of plant cell wall.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 82120
Sequence Length: 722
Subcellular Location: Golgi apparatus membrane
EC: 2.4.1.-
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Q339N5 | MEAAARGNKKLQERVPIRRTAWRLADLAILFLLLALLLHRVLHDSGAPWRRAALACEAWFTFMWLLNVNAKWSPVRFDTFPENLAERIDELPAVDMFVTTADPVLEPPLVTVNTVLSLLALDYPAAGEKLACYVSDDGCSPLTCYALREAARFARTWVPFCRRHGVAVRAPFRYFSSTPEFGPADGKFLEDWTFMKSEYEKLVHRIEDADEPSLLRHGGGEFAEFLDVERGNHPTIIKVLWDNNRSRTGDGFPRLIYVSREKSPNLHHHYKAGAMNALTRVSALMTNAPFMLNLDCDMFVNNPRVVLHAMCLLLGFDDEISCAFVQTPQKFYGALKDDPFGNQLEVSLMKVGRGIAGLQGIFYCGTGCFHRRKVIYGMRTGREGTTGYSSNKELHSKFGSSNNFKESARDVIYGNLSTEPIVDISSCVDVAKEVAACNYEIGTCWGQEVGWVYGSLTEDVLTGQRIHAAGWRSTLMEIEPPAFMGCAPNGGPACLTQLKRWASGFLEILISRNNPILTTTFKSLQFRQCLAYLHSYVWPVRAPFELCYALLGPYCLLSNQSFLPKTSEDGFYIALALFIAYNTYMFMEFIECGQSARACWNNHRMQRITSASAWLLAFLTVILKTLGFSETVFEVTRKDKSTSDGDSNTDEPEPGRFTFDESTVFIPVTALAMLSVIAIAVGAWRVVLVTTEGLPGGPGISEFISCGWLVLCFMPLLRGLVGSGRYGIPWSIKMKACLLVAIFLLFCKRN | Function: Thought to be a Golgi-localized beta-glycan synthase that polymerize the backbones of noncellulosic polysaccharides (hemicelluloses) of plant cell wall.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 83833
Sequence Length: 750
Subcellular Location: Golgi apparatus membrane
EC: 2.4.1.-
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Q9UBW8 | MSAEVKVTGQNQEQFLLLAKSAKGAALATLIHQVLEAPGVYVFGELLDMPNVRELAESDFASTFRLLTVFAYGTYADYLAEARNLPPLTEAQKNKLRHLSVVTLAAKVKCIPYAVLLEALALRNVRQLEDLVIEAVYADVLRGSLDQRNQRLEVDYSIGRDIQRQDLSAIARTLQEWCVGCEVVLSGIEEQVSRANQHKEQQLGLKQQIESEVANLKKTIKVTTAAAAAATSQDPEQHLTELREPAPGTNQRQPSKKASKGKGLRGSAKIWSKSN | Function: Component of the COP9 signalosome complex (CSN), a complex involved in various cellular and developmental processes. The CSN complex is an essential regulator of the ubiquitin (Ubl) conjugation pathway by mediating the deneddylation of the cullin subunits of SCF-type E3 ligase complexes, leading to decrease the Ubl ligase activity of SCF-type complexes such as SCF, CSA or DDB2. The complex is also involved in phosphorylation of p53/TP53, JUN, I-kappa-B-alpha/NFKBIA, ITPK1 and IRF8/ICSBP, possibly via its association with CK2 and PKD kinases. CSN-dependent phosphorylation of TP53 and JUN promotes and protects degradation by the Ubl system, respectively.
PTM: Phosphorylated by CK2 and PKD kinases.
Sequence Mass (Da): 30277
Sequence Length: 275
Subcellular Location: Cytoplasm
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Q9CZ04 | MSAEVKVTGQNQEQFLLLAKSAKGAALATLIHQVLEAPGVYVFGELLDMPNVRELAESDFASTFRLLTVFAYGTYADYLAEARNLPPLTDAQKNKLRHLSVVTLAAKVKCIPYAVLLEALALRNVRQLEDLVIEAVYADVLRGSLDQRNQRLEVDYSIGRDIQRQDLSAIAQTLQEWCVGCEVVLSGIEEQVSRANQHKEQQLGLKQQIESEVANLKKTIKVTTAAAAAATSQDPEQHLTELREPASGTNQRQPSKKASKGKGLRGSAKIWSKSN | Function: Component of the COP9 signalosome complex (CSN), a complex involved in various cellular and developmental processes. The CSN complex is an essential regulator of the ubiquitin (Ubl) conjugation pathway by mediating the deneddylation of the cullin subunits of SCF-type E3 ligase complexes, leading to decrease the Ubl ligase activity of SCF-type complexes such as SCF, CSA or DDB2. The complex is also involved in phosphorylation of p53/TP53, JUN, I-kappa-B-alpha/NFKBIA, ITPK1 and IRF8/ICSBP, possibly via its association with CK2 and PKD kinases. CSN-dependent phosphorylation of TP53 and JUN promotes and protects degradation by the Ubl system, respectively (By similarity).
PTM: Phosphorylated by CK2 and PKD kinases.
Sequence Mass (Da): 30224
Sequence Length: 275
Subcellular Location: Cytoplasm
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Q94JU3 | MDIEQKQAEIIDQLVKRASTCKSEALGPLIIEATSHPSLFAFSEILALPNVAQLEGTTDSVYLDLLRLFAHGTWGDYKCNATRLPHLSPDQILKLKQLTVLTLAESNKVLPYDTLMVELDVSNVRELEDFLINECMYAGIVRGKLDQLKRCFEVPFAAGRDLRPGQLGNMLHTLSNWLNTSENLLISIQDKIKWADNMSEMDKKHRKEAEEGVEEVKKSLSMKGDVDIRGNKEMFGEPSGVMDYEEDGIRPKRRRHPVTR | Function: Component of the COP9 signalosome complex (CSN), a complex involved in various cellular and developmental processes such as photomorphogenesis and auxin and jasmonate responses. The CSN complex is an essential regulator of the ubiquitin (Ubl) conjugation pathway by mediating the deneddylation of the cullin subunits of SCF-type E3 ligase complexes, leading to decrease the Ubl ligase activity of SCF. It is involved in repression of photomorphogenesis in darkness by regulating the activity of COP1-containing Ubl ligase complexes. The complex is also required for degradation of IAA6 by regulating the activity of the Ubl ligase SCF-TIR complex. Regulates the TSO2 subcellular localization. May be involved in nucleic acid binding.
PTM: Phosphorylated.
Sequence Mass (Da): 29469
Sequence Length: 260
Domain: The PCI domain is not sufficient to efficiently mediate CSN complex assembly and for biological activity.
Subcellular Location: Cytoplasm
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Q9C5H6 | MKNGIAECPACHSKLVSPGSKTISRAYDDHKIRVSSKQRVLNVLLVVGDCMLVGLQPVLVYMSKVDGKFNFSPISVNFLTEIAKVIFAIVMLLIQARHQKVGEKPLLSVSTFVQAARNNVLLAVPALLYAINNYLKFTMQLYFNPATVKMLSNLKVLVIAVLLKMVMKRRFSIIQWEALALLLIGISVNQLRSLPEGATAIGIPLATGAYVCTVIFVTVPSMASVFNEYALKSQYDTSIYLQNLFLYGYGAIFNFLGILGTVIYKGPGSFDILQGHSRATMFLILNNAAQGILSSFFFKYADTILKKYSSTVATIFTGIASAALFGHVITMNFLLGISIVFISMHQFFSPLAKARDEQQQNGNLELGNTKDTHRANESFINMAAGANEEASHRGESDDRTPLLPR | Function: Sugar transporter involved in the transport of CMP-sialic acid from the cytoplasm into the Golgi.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 44541
Sequence Length: 405
Subcellular Location: Golgi apparatus membrane
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F4JN00 | MEYRKIKDEDDHDVASDIESVKGKSHTVASSNIAMATLGVGSSERINWKRKGVVTCALTILTSSQAILIVWSKRAGKYEYSVTTANFLVGTLKCALSLLALTRIWKNEGVTDDNRLSTTFDEVKVFPIPAALYLFKNLLQYYIFAYVDAPGYQILKNLNIISTGVLYRIILKRKLSEIQWAGFILLCCGCTTAQLNSNSDRVLQTSLPGWTMAIVMALLSGFAGVYTEAIIKKRPSRNINVQNFWLYVFGMAFNAVAIVIQDFDAVANKGFFHGYSFITLLMILNHALSGIAVSMVMKYADNIVKVYSTSVAMLLTAVVSVFLFNFHLSLAFFLGSTVVSVSVYLHSAGKLR | Function: Sugar transporter involved in the transport of CMP-sialic acid from the cytoplasm into the Golgi (By similarity). Essential protein.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 38979
Sequence Length: 352
Subcellular Location: Golgi apparatus membrane
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Q6K8S7 | MQRNGVVECSVCRSRLVVPSPRSVSRAYDKHRSKISSKFRALNVLLVVGDCILVGLQPILVFMSKVDGKFQFSPISVNFLTEVTKVVFAIVMLIIQSRKQKVGEKPLLARSTFIQAARNNALLAVPALLYAINNYLKFIMQLYFNPSTVKMLSNLKVLVIAVLLKFIMKRRFSVIQWEALALLLIGISINQLRTVPAGNTAFGLPVTAIAYIYTLIFVTVPSLASVYNEYALKSQYDTSIYLQNLFLYGYGAIFNFLGILGTALFQGPESFNILRGHSRATMFLICNNAAQGILSSFFFKYADTILKKYSSTVATIFTGLASAAFLGHTLTINFLLGISVVFISMHQFFSPLAKAKDDKPAELLELEDTQNHRSSESSFVNMTAGAAEDASHRIGTDERQPLLPT | Function: Sugar transporter involved in the transport of CMP-sialic acid from the cytoplasm into the Golgi. May transport important nucleotide sugars such as CMP-Kdo (2-keto-3-deoxy-D-manno-octulosonic acid) in physiological conditions.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 44888
Sequence Length: 405
Subcellular Location: Golgi apparatus membrane
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P27450 | MGACISFFSSSSPSKTGLHSHATTNNHSNGTEFSSTTGATTNSSVGQQSQFSDISTGIISDSGKLLESPNLKVYNFLDLKTATKNFKPDSMLGQGGFGKVYRGWVDATTLAPSRVGSGMIVAIKRLNSESVQGFAEWRSEVNFLGMLSHRNLVKLLGYCREDKELLLVYEFMPKGSLESHLFRRNDPFPWDLRIKIVIGAARGLAFLHSLQREVIYRDFKASNILLDSNYDAKLSDFGLAKLGPADEKSHVTTRIMGTYGYAAPEYMATGHLYVKSDVFAFGVVLLEIMTGLTAHNTKRPRGQESLVDWLRPELSNKHRVKQIMDKGIKGQYTTKVATEMARITLSCIEPDPKNRPHMKEVVEVLEHIQGLNVVPNRSSTKQAVANSSRSSPHHYRYKAGALGAERKRATPGRFGSVEK | Function: Acts as a spatial inhibitor of signaling that modulates abscission zone cell adhesion and expansion. Acts both directly and indirectly by physically interacting with RLK5/HAE and SOBIR1/EVR at the cell surface.
PTM: Autophosphorylated on serine, threonine and tyrosine residues.
Location Topology: Lipid-anchor
Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Sequence Mass (Da): 46340
Sequence Length: 419
Subcellular Location: Cell membrane
EC: 2.7.11.1
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Q9SY88 | MPQRHSKNNNDLAYFTYDEKKKLGYGTQRERLGRDSIKPFDACSLCLKPFIDPMCCHKGHVFCRECILECFLAQKKDIQRRLAAHSSQKKQDKDEEEERLMLQKARELDEFDQQNHSAMPRNSDKNHNEDKNGFHGANSVKTTSFEEEALRTMKAFWLPSATPAASVRVDAPETHTVCPEGKEKLKLKNLFAIRFTEDNSEEEETKTKSASSSSYDKSYICPSCKVTLTNTMSLVALSSCGHVFCKKCAEKFMPVDKVCLVCDKPCKDRNLVGLKKGGTGFAEHDDHLEAKEYKHLGSGSGLGLVRPVKT | Function: RING-finger E3 ubiquitin-protein ligase that plays an major role in maintaining COP1 homeostasis in darkness. Negatively regulates COP1 protein accumulation by targeting COP1 for ubiquitination and subsequent proteasomal degradation in dark-grown seedlings. Negatively regulates the accumulation of SPA1 protein in the dark.
Catalytic Activity: S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.
Sequence Mass (Da): 35024
Sequence Length: 310
Pathway: Protein modification; protein ubiquitination.
Subcellular Location: Nucleus
EC: 2.3.2.27
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Q9V3A4 | MAKQVADYQCSKLQLYQKLALVVILGAVLFSLPALCAGQGNPSFKYSREANENFDPQKAPRAEHHHHHDHDHDHGHHHHGHDHDHDHDHGHDHGHHHHGHDHDHDHDHGHHHHGHDERHTKAKPDLDMSTIWLHSIGSTLLISAAPFVLLYIIPLDNSEAMKPRLKVLLAFASGGLLGDAFLHLIPHATHPHSHGEHGHDHGHDHHHHHDGEEHEHGHSHDMSIGLWVLGGIIAFLSVEKLVRILKGGHGGHGHSHGAPKPKPVPAKKKSSDKEDSGDGDKPAKPAKIKSKKPEAEPEGEVEISGYLNLAADFAHNFTDGLAIGASYLAGNSIGIVTTITILLHEVPHEIGDFAILIKSGCSRRKAMLLQLVTALGALAGTALALLGAGGGDGSAPWVLPFTAGGFIYIATVSVLPELLEESTKLKQSLKEIFALLTGVALMIVIAKFE | Function: Negatively regulates tyrosine hydroxylase activity.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 48658
Sequence Length: 449
Subcellular Location: Membrane
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P29349 | MSSRRWFHPTISGIEAEKLLQEQGFDGSFLARLSSSNPGAFTLSVRRGNEVTHIKIQNNGDFFDLYGGEKFATLPELVQYYMENGELKEKNGQAIELKQPLICAEPTTERWFHGNLSGKEAEKLILERGKNGSFLVRESQSKPGDFVLSVRTDDKVTHVMIRWQDKKYDVGGGESFGTLSELIDHYKRNPMVETCGTVVHLRQPFNATRITAAGINARVEQLVKGGFWEEFESLQQDSRDTFSRNEGYKQENRLKNRYRNILPYDHTRVKLLDVEHSVAGAEYINANYIRLPTDGDLYNMSSSSESLNSSVPSCPACTAAQTQRNCSNCQLQNKTCVQCAVKSAILPYSNCATCSRKSDSLSKHKRSESSASSSPSSGSGSGPGSSGTSGVSSVNGPGTPTNLTSGTAGCLVGLLKRHSNDSSGAVSISMAEREREREREMFKTYIATQGCLLTQQVNTVTDFWNMVWQENTRVIVMTTKEYERGKEKCARYWPDEGRSEQFGHARIQCVSENSTSDYTLREFLVSWRDQPARRIFHYHFQVWPDHGVPADPGCVLNFLQDVNTRQSHLAQAGEKPGPICVHCSAGIGRTGTFIVIDMILDQIVRNGLDTEIDIQRTIQMVRSQRSGLVQTEAQYKFVYYAVQHYIQTLIARKRAEEQSLQVGREYTNIKYTGEIGNDSQRSPLPPAISSISLVPSKTPLTPTSADLGTGMGLSMGVGMGVGNKHASKQQPPLPVVNCNNNNNGIGNSGCSNGGGSSTTSSSNGSSNGNINALLGGIGLGLGGNMRKSNFYSDSLKQQQQREEQAPAGAGKMQQPAPPLRPRPGILKLLTSPVIFQQNSKTFPKT | Function: Required in all receptor tyrosine kinase signaling pathways. Functions downstream of the receptor tyrosine kinase torso, acting in concert with D-Raf via tailless. Also functions downstream of Egfr (epidermal growth factor receptor) and btl (fibroblast growth factor receptor). The SH2 domain suggests that csw effects its role by mediating heteromeric protein interactions. Maternally required for normal determination of cell fates at the termini of the embryo. Required for cell fate specification of the ventral ectoderm, in the developing embryonic CNS and for embryonic tracheal cell migration. Functions during imaginal development for proper formation of adult structures such as eyes, aristae, L5 wing vein and the tarsal claw. Dephosphorylates drpr isoform A which is required for the inhibition by drpr isoform A of glial cell engulfment of axonal debris produced following axonal injury .
Catalytic Activity: H2O + O-phospho-L-tyrosyl-[protein] = L-tyrosyl-[protein] + phosphate
Sequence Mass (Da): 92975
Sequence Length: 845
Subcellular Location: Cytoplasm
EC: 3.1.3.48
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Q24708 | WFHGNLSGKEAEKLILERGKNGSFLVRESQSKPGDFVLSVRTDDKVTHVMIRWQDKKYDVGGGESFATLSELIEHYKRHPMVETCGTVVHLRQPFNATRITAAGINARVEQLVKGGFWEEFESLQQDSRDTFSRHEGYKDENRLKNRYHDHTRVKLQDVERSAPGAEYINANYIRLPTDGDLYNMSSSSESLNSTVAACPACTAAQTQRNCPNCHLLNKTCVKCAVKSATLPTNCATCNRKSDSLSKHKRSESMSASANASAAGTGPGTPTAAGNTSAAAALNGCLAVLLKKHCGDASPPPSTTSSCSGPLTGSLLNGEGNQFKTYIATQGCLANTKTDFWNMIWQENTRVIVMTTKEIERGKTKCERYWPDEGQCKQFGHAKVHCIKENSTNDYTLREFLFSWRDKPERRIYHYHFQVWPDHGVPADPGCVLNFLQDVNTKQSSLAQAGEKPGPICVHCSAGIGRTGTFIVIDMILDQIVRNGLDTEIDIQRTIQMVRSQRSGMVQTEAQYKFVYYAVQHYIQTLIARKRAEEQSLQVGREYTNIKYTGEIGNDSQRSPLPPAISNLSLVSCKSAVAEPLTAAAAAAAVAANAGNKHAAKLQPPLPPLGASNNNNSSGNSGSYCNSSSSTSTAQHNGVVSSSNNCSSGSGSANSSNANGNGNILGNGSNMRKSNFYSDSLAALKLQQQQLHDAATAAAAAALASAAAPAATTTAASASAAAAAAAAAKYKNIPKDMNSLRQPHAAYVAAAPALPPPPTPPRKT | Function: Required in all receptor tyrosine kinase signaling pathways. Functions downstream of the receptor tyrosine kinase torso, acting in concert with D-Raf via tailless. Also functions downstream of Egfr (epidermal growth factor receptor) and btl (fibroblast growth factor receptor). The SH2 domain suggests that csw effects its role by mediating heteromeric protein interactions. Maternally required for normal determination of cell fates at the termini of the embryo. Required for cell fate specification of the ventral ectoderm, in the developing embryonic CNS and for embryonic tracheal cell migration. Functions during imaginal development for proper formation of adult structures such as eyes, aristae, L5 wing vein and the tarsal claw (By similarity).
Catalytic Activity: H2O + O-phospho-L-tyrosyl-[protein] = L-tyrosyl-[protein] + phosphate
Sequence Mass (Da): 82126
Sequence Length: 764
Subcellular Location: Cytoplasm
EC: 3.1.3.48
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P0CI23 | RCCGYKMCHPC | Function: Chi-conotoxins inhibit the neuronal noradrenaline transporter (NET/SLC6A2).
Sequence Mass (Da): 1301
Sequence Length: 11
Domain: The cysteine framework is X (CC-CX[hydroxyPro]C).
Subcellular Location: Secreted
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P58808 | MRCLPVLIILLLLTASAPGVVVLPKTEDDVPMSSVYGNGKSILRGILRNGVCCGYKLCHPC | Function: Chi-conotoxins inhibit the neuronal noradrenaline transporter (NET/SLC6A2).
Sequence Mass (Da): 6499
Sequence Length: 61
Domain: The cysteine framework is X (CC-CX[hydroxyPro]C).
Subcellular Location: Secreted
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P58810 | VGVCCGYKLCHPC | Function: Chi-conotoxins inhibit the neuronal noradrenaline transporter (NET/SLC6A2).
Sequence Mass (Da): 1382
Sequence Length: 13
Domain: The cysteine framework is X (CC-CX[hydroxyPro]C).
Subcellular Location: Secreted
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P94286 | MVRFMYALRKRRLSLLLAMSLLVMCVASVVSPPPQALASGSGGIERVFTDKARYNPGDAVSIRVQAKNGTGSSWSGAARLEIFHLENSVYTSSQSLSLTNGQSTTLTFTWTAPSTDFRGYFVRIDAGTLGQGATAIDVSSDFTKYPRYGYISEFESGETALESKAKVDQLAQDYHINAWQFYDWMWRHDKMIKRTGGSIDSTWLDLFNREISWSTLQNQIDAVHDVNGKAMAYAMIYASRENYSPLGISPTWGIYEDSSHTNQFDVDFGDGSTYLYMSDPQNPNWQNYIHAEYIDSINTAGFDGIHVDQMGQRSNVYDYNGNSIDLSTRFSPFLDQAKSVLSANNPARDNLTYNIVDGTVNGWAVNDVSKNADLDFLYSEIWYLSDSYNQLKNYIEQLRANGGNKAVVLAAYMNYADNAGTRYEAESASMTNVSTNTNHAGYTGSGFVDQFASTGDKVSFAINAPEAGDYSLVFRYGNNTGANSTLNLYVDGNFVQKLYFFNQSSWGTWKHDAWYQVPLTQGAHTVELRYESGNVGAVNLDSLTLGTFDEHSVRLADAMMSASGATHIELGDDNQMLPHEYYPNRSKTMRSSLKNAMKDHYNFITAYENLLFDSDVVPNDTGSQFVNLTGVSASGDGSANTVWYINKRTSDYNIVHLINLLGNDNQWRNTASQPSFQTNLPAKIYIGADETISDVYLASPDLSGGETQELAFTSGTDAGGKYVSFTVPELKYWNMIYMKRTFSVPANDIYEAETAIKSNVSTNTNHAGYTGSGFVDGFSSTNDGVSFVVKSTASDDYALRFRYANGGSDATRDVYVDGKLAGTVSFKSTGSWSTWSYGEITARLEPGHHTIVLWQTSGNTGAINLDHLDLDKTYIWQFDRQIVSVPAGYRITFRTGLPGWVHWGVNGWTGVTDTPLRSNGSLDGNLDHETSIGPFATGTAVDVTFLWDDNNNGILEPSTDRWEGTDFGINVS | Function: Produces cycloisomaltooligosaccharide from dextran containing 7, 8 or 9 glucose units. The enzyme is specific for (1->6)-alpha-D-glucans (dextrans) and, without activity toward (1->4)-alpha-D-glucans, such as amylose. It also has no activity on oligosaccharides, such as amylopectin and pullulan, containing (1->6)-alpha-D-glucosidic linkages at branch points.
Catalytic Activity: cyclizes part of a (1->6)-alpha-D-glucan chain by formation of a (1->6)-alpha-D-glucosidic bond.
Sequence Mass (Da): 107431
Sequence Length: 972
EC: 2.4.1.248
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A5FXV3 | MSGAAARGDRLVGTWLLVICFMIFGMVVGGGHARTIGAGFVIQTWQPFTGIVPPLTHAAWERAFGLYKATAQYQAMQPKMTLAQFQSLYLPMFLDRDWGRLMAVVFLVPLAVFRLRGRISNRLTAWLLFLFGLGAGEATMGWYMTYEGMTSRILQPSPLYLGPHFVLAMLIFTAMLWTALTLRNPEPAILPGLARLRGLLSVSIGLIIATIGLGALVAASGALKVYNTFPLMDGHALPPHALAMHPLWLNFLANKATVQFEHRVAATVTAIVVVIAAAMGLRAPVGAKARDLFLLLAGLVSLQYILGMSTLVSGMAELGYVHELNAVLLLAACIACRHALRGATAAVPLPVYEMKAAE | Function: Catalyzes the conversion of heme O to heme A by two successive hydroxylations of the methyl group at C8. The first hydroxylation forms heme I, the second hydroxylation results in an unstable dihydroxymethyl group, which spontaneously dehydrates, resulting in the formyl group of heme A.
Catalytic Activity: 2 A + Fe(II)-heme o + H2O = 2 AH2 + Fe(II)-heme a
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 38613
Sequence Length: 358
Pathway: Porphyrin-containing compound metabolism; heme A biosynthesis; heme A from heme O: step 1/1.
Subcellular Location: Cell membrane
EC: 1.17.99.9
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A5FXV4 | MASQSVAGIGGRTAAGEARAASPESRRMVAIWLFVSFALIVEMFGIGAYVQNMNAGLSIMAWQPVSGVIPPLTHAAWERMFALYKTIPQYKELNRGMDLAGFKAIFWPEWIHRMWGRLLGFDFGVPLVWFLWTGRIERRLRPWLVTLFVLGGVQGLIGWWMVASGFQPGLTEVSVFRLSVHYCFATLLAIAVFATALTVLKPAETRLPPEEAARYAGARRMAMGSIVLISIAIVAGTFLSGTHAYTIDNTFPLMQGRWVPPDYAALHPFWKNFFLNKAATQFDHRLLGTVAAVGVLAAVVAAIRADLPARARDAFLVMGALLIVQYILGVTTLVSKILDIGIVHQLNAVLLLAAAVWAWFELRGRPA | Function: Catalyzes the conversion of heme O to heme A by two successive hydroxylations of the methyl group at C8. The first hydroxylation forms heme I, the second hydroxylation results in an unstable dihydroxymethyl group, which spontaneously dehydrates, resulting in the formyl group of heme A.
Catalytic Activity: 2 A + Fe(II)-heme o + H2O = 2 AH2 + Fe(II)-heme a
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 40382
Sequence Length: 367
Pathway: Porphyrin-containing compound metabolism; heme A biosynthesis; heme A from heme O: step 1/1.
Subcellular Location: Cell membrane
EC: 1.17.99.9
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Q7CZN9 | MANGSVDMVVEAALQKQEKDRRLLRIWLRVVLFTLFCLVLVGGATRLTESGLSITEWKPIHGAIPPLSVAEWEEEFQLYKRIPQYQEINKGMSLDEFKTIFWWEWAHRLLARTIGLVFALPLAFFWLTGRVEKRLRLPLVGLLALGGFQGFVGWWMVSSGLVNRTDVSQYRLATHLTIACLIFAGCMWILRGLSHHSPDAADERTGRGFAALLTVLCLFQIYLGALVAGLNAGLSYNTWPLMDGSLVPGDLFLQQPWWINLFENPKTVQFVHRLGAYTLFAATLWHMVSMARALPGTPHARRAVLFFVLISVQAGLGITTLLMHVDIHVALAHQGMALILLGFSVAHWRGFIGEYPAPVAVEVRD | Function: Catalyzes the conversion of heme O to heme A by two successive hydroxylations of the methyl group at C8. The first hydroxylation forms heme I, the second hydroxylation results in an unstable dihydroxymethyl group, which spontaneously dehydrates, resulting in the formyl group of heme A.
Catalytic Activity: 2 A + Fe(II)-heme o + H2O = 2 AH2 + Fe(II)-heme a
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 40958
Sequence Length: 365
Pathway: Porphyrin-containing compound metabolism; heme A biosynthesis; heme A from heme O: step 1/1.
Subcellular Location: Cell membrane
EC: 1.17.99.9
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Q04443 | MHKRLKIYSVITSIGVLIVLLQGALVTKTGSGEGCGATWPLCFGEVIPTNPAIETIIEYSHRIVSGLVGAMIIILAIWAWKQLKHMREAKALSFAAVILIIFQGLLGAGAVVFGQSKAILALHFGISAMSLAAVVLLTILAFEDGREHTMAPKVSRGFKYYVFFVITYCYAVIYSGAYVKHSEATLACAGFPLCNGQIFPGLYGPVGAHYFHRVVGTILLLFLLILMIWTLSRYRHYRVLTWTAVLSFLLVVGQFISGISIVFTQNALSVGLIHALIISILFSALSYMTMIITRPSH | Function: Catalyzes the conversion of heme O to heme A by two successive hydroxylations of the methyl group at C8. The first hydroxylation forms heme I, the second hydroxylation results in an unstable dihydroxymethyl group, which spontaneously dehydrates, resulting in the formyl group of heme A.
Catalytic Activity: 2 A + Fe(II)-heme o + H2O = 2 AH2 + Fe(II)-heme a
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 32471
Sequence Length: 297
Pathway: Porphyrin-containing compound metabolism; heme A biosynthesis; heme A from heme O: step 1/1.
Subcellular Location: Cell membrane
EC: 1.17.99.9
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Q5PBP7 | MKAHFGVTVWLGVCCSMTLLMVVIGGITRLTHSGLSITEWQPIVGVVPPIGDEAWLREKEKYAQTPEYRHRAADISLDDFKRIYIIEYIHRLFGRALGAVFCLPIPYFAITKRIDRAMVAKLLIVALLGGMQGAMGWFMVKSGLVDTPRVSHYRLAGHLFLTILLFSILWHSFLRCAGVRSTTTTTNARFFTAAAVVGLTVLQMVLGALVAGLDAGLTYNTFPLMDGAIIPQSLFSAKLWHGGFLHDVTAVQFLHRLVAVLIVVCAAPLPFWLKTRGAWLFLACVALQFLLGVATLVSVVHIFLAAMHQVFGFVTLAAGVHMLCRLRREGSTCISGHAGIS | Function: Catalyzes the conversion of heme O to heme A by two successive hydroxylations of the methyl group at C8. The first hydroxylation forms heme I, the second hydroxylation results in an unstable dihydroxymethyl group, which spontaneously dehydrates, resulting in the formyl group of heme A.
Catalytic Activity: 2 A + Fe(II)-heme o + H2O = 2 AH2 + Fe(II)-heme a
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 37392
Sequence Length: 341
Pathway: Porphyrin-containing compound metabolism; heme A biosynthesis; heme A from heme O: step 1/1.
Subcellular Location: Cell membrane
EC: 1.17.99.9
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Q13363 | MGSSHLLNKGLPLGVRPPIMNGPLHPRPLVALLDGRDCTVEMPILKDVATVAFCDAQSTQEIHEKVLNEAVGALMYHTITLTREDLEKFKALRIIVRIGSGFDNIDIKSAGDLGIAVCNVPAASVEETADSTLCHILNLYRRATWLHQALREGTRVQSVEQIREVASGAARIRGETLGIIGLGRVGQAVALRAKAFGFNVLFYDPYLSDGVERALGLQRVSTLQDLLFHSDCVTLHCGLNEHNHHLINDFTVKQMRQGAFLVNTARGGLVDEKALAQALKEGRIRGAALDVHESEPFSFSQGPLKDAPNLICTPHAAWYSEQASIEMREEAAREIRRAITGRIPDSLKNCVNKDHLTAATHWASMDPAVVHPELNGAAYRYPPGVVGVAPTGIPAAVEGIVPSAMSLSHGLPPVAHPPHAPSPGQTVKPEADRDHASDQL | Cofactor: NAD is required for efficient interaction with E1A. Cofactor binding induces a conformation change.
Function: Corepressor targeting diverse transcription regulators such as GLIS2 or BCL6. Has dehydrogenase activity. Involved in controlling the equilibrium between tubular and stacked structures in the Golgi complex. Functions in brown adipose tissue (BAT) differentiation.
PTM: The level of phosphorylation appears to be regulated during the cell cycle. Phosphorylation by HIPK2 on Ser-422 induces proteasomal degradation.
Sequence Mass (Da): 47535
Sequence Length: 440
Subcellular Location: Cytoplasm
EC: 1.1.1.-
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Q9Z2F5 | MSGVRPPIMNGPMHPRPLVALLDGRDCTVEMPILKDVATVAFCDAQSTQEIHEKVLNEAVGALMYHTITLTREDLEKFKALRIIVRIGSGFDNIDIKSAGDLGIAVCNVPAASVEETADSTLCHILNLYRRTTWLHQALREGTRVQSVEQIREVASGAARIRGETLGIIGLGRVGQAVALRAKAFGFNVLFYDPYLSDGIERALGLQRVSTLQDLLFHSDCVTLHCGLNEHNHHLINDFTVKQMRQGAFLVNTARGGLVDEKALAQALKEGRIRGAALDVHESEPFSFSQGPLKDAPNLICTPHAAWYSEQASIEMREEAAREIRRAITGRIPDSLKNCVNKDHLTAATHWASMDPAVVHPELNGAAYSRYPPGVVSVAPTGIPAAVEGIVPSAMSLSHGLPPVAHPPHAPSPGQTVKPEADRDHTTDQL | Cofactor: Cofactor binding induces a conformational change.
Function: Corepressor targeting diverse transcription regulators such as GLIS2 or BCL6. Has dehydrogenase activity. Involved in controlling the equilibrium between tubular and stacked structures in the Golgi complex. Functions in brown adipose tissue (BAT) differentiation.
PTM: The level of phosphorylation appears to be regulated during the cell cycle. Phosphorylation by HIPK2 on Ser-412 induces proteasomal degradation (By similarity).
Sequence Mass (Da): 46628
Sequence Length: 430
Subcellular Location: Cytoplasm
EC: 1.1.1.-
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O23702 | MSKIRSSATMPHRDQPSPASPHVVTLNCIEDCALEQDSLAGVAGVEYVPLSRIADGKIESATAVLLHSLAYLPRAAQRRLRPHQLILCLGSADRAVDSTLAADLGLRLVHVDTSRAEEIADTVMALILGLLRRTHLLSRHALSASGWLGSLQPLCRGMRRCRGMVLGIVGRSVSARYLASRSLAFKMSVLYFDVPEGDEERIRPSRFPRAARRMDTLNDLLAASDVISLHCALTNDTVQILNAECLQHIKPGAFLVNTGSCQLLDDCAVKQLLIDGTIAGCALDGAEGPQWMEAWVKEMPNVLILPRSADYSEEVWMEIREKAISILHSFFLDGVIPSNTVSDEEVEESEASEEEEQSPSKHEKLAIVESTSRQQGESTLTSTEIVRREASELKESLSPGQQHVSQNTAVKPEGRRSRSGKKAKKRHSQQKYMQKTDGSSGLNEESTSRRDDIAMSDTEEVLSSSSRCASPEDSRSRKTPLEVMQESSPNQLVMSSKKFIGKSSELLKDGYVVALYAKDLSGLHVSRQRTKNGGWFLDTLSNVSKRDPAAQFIIAYRNKDTVGLRSFAAGGKLLQINRRMEFVFASHSFDVWESWSLEGSLDECRLVNCRNSSAVLDVRVEILAMVGDDGITRWID | Cofactor: Cofactor binding induces a conformational change.
Function: Involved in controlling the equilibrium between tubular and stacked structures in the Golgi complex (By similarity). Required for cortical microtubules (MTs) arrangement that confers cell shape. Cooperatively with IPGA1, regulates negatively cortical microtubules (CMTs) organization in response to mechanical stress and modulates pavement cells morphogenesis leading to puzzle shape, probably in an AAA1/KTN1-dependent manner . Regulates the width of leaves by controlling the polar elongation of leaf cells. Involved in the regulation of trichome branching. Seems to not be able to regulate gene transcription. Regulates epidermal cell divisions and elongation in a non-cell-autonomous manner (regulated by subepidermal cells), but regulates epidermal cell polarity, shape, trichome branching and elongation in a cell-autonomous manner. Negatively regulates growth in the petiole elongation. Prevents lipid peroxidation as a result of abiotic stress response. Is involved in the SUB-dependent signaling mechanism and may act in a membrane trafficking event around the trans-Golgi network.
Sequence Mass (Da): 70150
Sequence Length: 636
Domain: The C-terminal region (631-636) is indispenasble for homodimerization.
Subcellular Location: Cytoplasm
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P00766 | CGVPAIQPVLSGLSRIVNGEEAVPGSWPWQVSLQDKTGFHFCGGSLINENWVVTAAHCGVTTSDVVVAGEFDQGSSSEKIQKLKIAKVFKNSKYNSLTINNDITLLKLSTAASFSQTVSAVCLPSASDDFAAGTTCVTTGWGLTRYTNANTPDRLQQASLPLLSNTNCKKYWGTKIKDAMICAGASGVSSCMGDSGGPLVCKKNGAWTLVGIVSWGSSTCSTSTPGVYARVTALVNWVQQTLAAN | Catalytic Activity: Preferential cleavage: Tyr-|-Xaa, Trp-|-Xaa, Phe-|-Xaa, Leu-|-Xaa.
Sequence Mass (Da): 25666
Sequence Length: 245
Subcellular Location: Secreted
EC: 3.4.21.1
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B2S753 | MRVLLIEDDSAIAQSIELMLKSESFNVYTTDLGEEGIDLGKLYDYDIILLDLNLPDMSGYEVLRTLRLSKVKTPILILSGMAGIEDKVRGLGFGADDYMTKPFHKDELIARIHAIVRRSKGHAQSVITTGDLVVNLDAKTVEVAGQRVHLTGKEYQMLELLSLRKGTTLTKEMFLNHLYGGMDEPELKIIDVFICKLRKKLDAVSGNQSYIETVWGRGYVLREPDAEMRESA | Function: Component of a regulatory phosphorelay system that controls B.abortus cell growth, division, and intracellular survival inside mammalian host cells. This signaling pathway is composed of CckA, ChpT, CtrA and CpdR. CtrA is a response regulator substrate of ChpT. When phosphorylated, directly regulates the expression of ccrM. Is also probably involved in the transcriptional regulation of rpoD, pleC, minC and ftsE genes.
PTM: Is phosphorylated by ChpT-P on Asp-51.
Sequence Mass (Da): 26066
Sequence Length: 232
Subcellular Location: Cytoplasm
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P47796 | MGHEVDSVLPGLFRRTYGCGRPAISPVITGYSRIVNGEEAVPHSWSWQVSLQDQTGFHFCGGSLINENWVVTAAHCNVKNYHRVVLGEHDRSSNSEGVQVMTVGQVFKHPRYNGFTINNDILLVKLATPATLNMRVSPVCLAETDDVFEGGMKCVTSGWGLTRYNAADTPALLQQAALPLLTNEQCKKFWGNKISDLMICAGAAGASSCMGDSGGPLVCQKAGSWTLVGIVSWGSGTCTPTMPGVYARVTELRAWVDQTIAAN | Catalytic Activity: Preferential cleavage: Tyr-|-Xaa, Trp-|-Xaa, Phe-|-Xaa, Leu-|-Xaa.
Sequence Mass (Da): 28294
Sequence Length: 263
Subcellular Location: Secreted
EC: 3.4.21.1
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P0A0V8 | MFKVKFYIRHAVLLLCGSLIVGCSAIPSSGPSAKKIVSLGQQSEVQIPEVELIDVNHTVAQLLYKAQINQSFTQFGDGYASAGTLNIGDVLDIMIWEAPPAVLFGGGLSSMGSGSAHQTKLPEQLVTARGTVSVPFVGDISVVGKTPGQVQEIIKGRLKKMANQPQVMVRLVQNNAANVSVIRAGNSVRMPLTAAGERVLDAVAAVGGSTANVQDTNVQLTRGNVVRTVALEDLVANPRQNILLRRGDVVTMITNPYTFTSMGAVGRTQEIGFSARGLSLSEAIGRMGGLQDRRSDARGVFVFRYTPLVELPAERQDKWIAQGYGSEAEIPTVYRVNMADAHSLFSMQRFPVKNKDVLYVSNAPLAEVQKFLSFVFSPVTSGANSINNLTN | Function: Involved in transport of capsular polysaccharides to the cell surface. May function as a membrane anchor for capsular polysaccharides. Possible porin properties.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 41949
Sequence Length: 391
Subcellular Location: Cell outer membrane
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P17538 | MASLWLLSCFSLVGAAFGCGVPAIHPVLSGLSRIVNGEDAVPGSWPWQVSLQDKTGFHFCGGSLISEDWVVTAAHCGVRTSDVVVAGEFDQGSDEENIQVLKIAKVFKNPKFSILTVNNDITLLKLATPARFSQTVSAVCLPSADDDFPAGTLCATTGWGKTKYNANKTPDKLQQAALPLLSNAECKKSWGRRITDVMICAGASGVSSCMGDSGGPLVCQKDGAWTLVGIVSWGSDTCSTSSPGVYARVTKLIPWVQKILAAN | Catalytic Activity: Preferential cleavage: Tyr-|-Xaa, Trp-|-Xaa, Phe-|-Xaa, Leu-|-Xaa.
Sequence Mass (Da): 27713
Sequence Length: 263
Subcellular Location: Secreted
EC: 3.4.21.1
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