ids stringlengths 6 10 | seqs stringlengths 11 1.02k | texts stringlengths 108 11.1k |
|---|---|---|
Q8N5G2 | MKRRNADCSKLRRPLKRNRITEGIYGSTFLYLKFLVVWALVLLADFVLEFRFEYLWPFWLFIRSVYDSFRYQGLAFSVFFVCVAFTSNIICLLFIPIQWLFFAASTYVWVQYVWHTERGVCLPTVSLWILFVYIEAAIRFKDLKNFHVDLCRPFAAHCIGYPVVTLGFGFKSYVSYKMRLRKQKEVQKENEFYMQLLQQALPPEQQMLQKQEKEAEEAAKGLPDMDSSILIHHNGGIPANKKLSTTLPEIEYREKGKEKDKDAKKHNLGINNNNILQPVDSKIQEIEYMENHINSKRLNNDLVGSTENLLKEDSCTASSK... | Function: Plays a role in the regulation of neuronal activity.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 76178
Sequence Length: 664
Subcellular Location: Nucleus membrane
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Q7TQE6 | MKRRNADCSKLRRPLKRNRITEGIYGSTFLYLKFLVVWALVLLADFVLEFRFEYLWPFWLFIRSVYDSFRYQGLAFSVFFVCVAFTSNIICLLFIPIQWLFFAASTYVWVQYVWHTERGVCLPTVSLWILFVYIEAAIRFKDLKNFHVDLCRPFAAHCIGYPVVTLGFGFKSYVSYKMRLRKQKEVQKENEFYMQLLQQALPPEQQMLQKQEKEAEEAAKGLPDMDSSILIHHNGGIPANKKLSTTLPEIEYREKGKEKDKDAKKHNLGINNNNILQPVDSKIQEIEYMENHINSKRLNNDLVGSTENLLKEDSCTASSK... | Function: Plays a role in the regulation of neuronal activity.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 76089
Sequence Length: 664
Subcellular Location: Rough endoplasmic reticulum membrane
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O57342 | MASELAMTAELPTSPLAIEYVNDFDLMKFEVKKEPAEAERLCHRLPAGSLSSTPLSTPCSSVPSSPSFCAPSPGGQPSAGPTAAPLGSKPQLEELYWMSGYQHHLNPEALNLTPEDAVEALIGAPHHHHHHHQSYESFRPQPFGGEELPPAAHHHNAHHHHHHHHLRLEERFSDDQLVSMSVRELNRQLRGFSKEEVIRLKQKRRTLKNRGYAQSCRYKRVQQRHILENEKCQLQSQVEQLKQEVSRLAKERDLYKEKYEKLAARGFPRETSPPAAPKTTAADFFM | Function: Transcription factor involved in transcription regulation during lens development, including that of crystallin genes . Binds to CRE-type MARE 5'-TGCTGACGTCAGCA-3' and TRE-type MARE 5'-TGCTGACTCAGCA-3' DNA sequences .
PTM: Phosphorylation at Ser-14 and Ser-65 is required for transcription regulation activity ... |
Q8NHW3 | MAAELAMGAELPSSPLAIEYVNDFDLMKFEVKKEPPEAERFCHRLPPGSLSSTPLSTPCSSVPSSPSFCAPSPGTGGGGGAGGGGGSSQAGGAPGPPSGGPGAVGGTSGKPALEDLYWMSGYQHHLNPEALNLTPEDAVEALIGSGHHGAHHGAHHPAAAAAYEAFRGPGFAGGGGADDMGAGHHHGAHHAAHHHHAAHHHHHHHHHHGGAGHGGGAGHHVRLEERFSDDQLVSMSVRELNRQLRGFSKEEVIRLKQKRRTLKNRGYAQSCRFKRVQQRHILESEKCQLQSQVEQLKLEVGRLAKERDLYKEKYEKLAGR... | Function: Transcription factor that activates insulin gene expression . Acts synergistically with NEUROD1/BETA2 and PDX1 . Binds the insulin enhancer C1/RIPE3b element . Binds to consensus TRE-type MARE 5'-TGCTGACTCAGCA-3' DNA sequence .
PTM: Ubiquitinated, leading to its degradation by the proteasome.
Sequence Mass (D... |
D3ZNT6 | MAAELAMGAELPSSPLAIEYVNDFDLMKFEVKKEPPEAERFCHRLPPGSLSSTPLSTPCSSVPSSPSFCAPSPGTGSSAGGGGSAAQAGGAPGPPSGGPGTVGGASGKAVLEDLYWMSGYQHHLNPEALNLTPEDAVEALIGSGHHSAHHGAHHPAAAAAYEAFRGQSFAGGGGGGADDMGAGHHHGAHHTAHHHHSAHHHHHHHHHHGGSGHHGGGAGHGGGGAGHHVRLEERFSDDQLVSMSVRELNRQLRGFSKEEVIRLKQKRRTLKNRGYAQSCRFKRVQQRHILESEKCQLQSQVEQLKLEVGRLAKERDLYKE... | Function: Transcription factor that activates insulin gene expression . Acts synergistically with NEUROD1/BETA2 and PDX1 (By similarity). Binds the insulin enhancer C1/RIPE3b element . Binds to consensus TRE-type MARE 5'-TGCTGACTCAGCA-3' DNA sequence (By similarity).
PTM: Ubiquitinated, leading to its degradation by th... |
Q7ZV50 | MLHKLLIVVFLVVCLHDMRLNGQKKKETLLSEKVSQMMEWVSKRAVVRLNGEKFKRLVRAHPRNYSVIVMFTALQPQRQCGVCRQADEEYQILANSWRYSSAFTNRIFFAMVDFDEGSDVFQMLNMNSAPTFINFPAKGKPKRADTYELQVRGFAAEQLARWVADRTDVHIRVIRPPNYAGPLMLGLLLAFIGSLAYLRRNNLEFLFNKNVWAFSALCFVLIMTSGQMWNHIRGPPYAHKNPNTGQVSYIHGSSQAQFVAETHIVLLFNAAVTIGMVLLHEAATSGLDIVKRKIMCVAGIGLVVLFFSWLLSVFRAKYHG... | Function: Cell surface magnesium transporter.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 37422
Sequence Length: 328
Pathway: Protein modification; protein glycosylation.
Subcellular Location: Cell membrane
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Q9H0U3 | MAARWRFWCVSVTMVVALLIVCDVPSASAQRKKEMVLSEKVSQLMEWTNKRPVIRMNGDKFRRLVKAPPRNYSVIVMFTALQLHRQCVVCKQADEEFQILANSWRYSSAFTNRIFFAMVDFDEGSDVFQMLNMNSAPTFINFPAKGKPKRGDTYELQVRGFSAEQIARWIADRTDVNIRVIRPPNYAGPLMLGLLLAVIGGLVYLRRSNMEFLFNKTGWAFAALCFVLAMTSGQMWNHIRGPPYAHKNPHTGHVNYIHGSSQAQFVAETHIVLLFNGGVTLGMVLLCEAATSDMDIGKRKIMCVAGIGLVVLFFSWMLSI... | Function: Accessory component of the STT3B-containing form of the N-oligosaccharyl transferase (OST) complex which catalyzes the transfer of a high mannose oligosaccharide from a lipid-linked oligosaccharide donor to an asparagine residue within an Asn-X-Ser/Thr consensus motif in nascent polypeptide chains . Involved ... |
P02916 | MDVIKKKHWWQSDALKWSVLGLLGLLVGYLVVLMYAQGEYLFAITTLILSSAGLYIFANRKAYAWRYVYPGMAGMGLFVLFPLVCTIAIAFTNYSSTNQLTFERAQEVLLDRSWQAGKTYNFGLYPAGDEWQLALSDGETGKNYLSDAFKFGGEQKLQLKETTAQPEGERANLRVITQNRQALSDITAILPDGNKVMMSSLRQFSGTQPLYTLDGDGTLTNNQSGVKYRPNNQIGFYQSITADGNWGDEKLSPGYTVTTGWKNFTRVFTDEGIQKPFLAIFVWTVVFSLITVFLTVAVGMVLACLVQWEALRGKAVYRVL... | Function: Part of the ABC transporter complex MalEFGK involved in maltose/maltodextrin import. Probably responsible for the translocation of the substrate across the membrane.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 57013
Sequence Length: 514
Subcellular Location: Cell inner membrane
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O51924 | MDNNLTSKLKYREAKLGYLMILPLLTVVLVFIILPVMGTFWISLHRDVTFIPEKPFVGLRNYLRVLSAREFWYSTFVTVSFSFVSVSLETILGLSFALILNERLKGRGVLRAIVLIPWAVPTIISARTWELMYNYSYGLFNWILSILGVSPVNWLGTPISAFFAIVIADVWKTTPFMTLLLLAGLQAIPQDLYEAALIDGASMFERFKSITLPLLKPVLIVALILRTIDALRVFDIIYVLTGGGPGGATTSISLLAFNYYNLGDYGIGSAISILTFVLVLSFTIVYLKVGRFRRD | Function: Part of the ABC transporter complex MalEFGK involved in trehalose/maltose import. Responsible for the translocation of the substrate across the membrane.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 33054
Sequence Length: 295
Subcellular Location: Cell membrane
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Q0DM48 | MTVRPRPAAAAIIIAAVFGAAAAAAGGGMVGVDGTQFVVEGGRTIYFSGFNAYWLMMMASDPARRAAVVAAFAQASSRGLNLARTWAFSDGGDQPLQSSPGVYDEAMFQGLDFVIAEARRHGIYLLLCLTNNFDDFGGKRQYVRWAADAGHNLTAGDDFFTSSVVKSYYKNHVKAVLTRVNTVTGVAYKDDPTIFAWELMNEPRCDADPTGGMVQAWVEEMAPYVKRVDGGRHLVTAGLEGFYGDGEHESKELNPWGIYYGTNYVATHRAAGVDFATIHLYPDVWLWGSTADEQAAFFRNWTRSHVHDTAAFLGKPLLVT... | Catalytic Activity: Random hydrolysis of (1->4)-beta-D-mannosidic linkages in mannans, galactomannans and glucomannans.
Sequence Mass (Da): 51217
Sequence Length: 468
Subcellular Location: Secreted
EC: 3.2.1.78
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Q8L5J1 | MNNSIILIFVAILIIFPNEFSKPTRAFSNNNFVYTDGTHFALNGKSLYINGFNAYWLMYIAYDPSTRIKVTNTFQQASKYKMNVARTWAFSHGGSRPLQSAPGVYNEQMFQGLDFVISEAKKYGIHLIMSLVNNWDAFGGKKQYVEWAVQRGQKLTSDDDFFTNPMVKGFYKNNVKVVLTRVNTITKVAYKDDPTILSWELINEPRCPSDLSGKTFQNWVLEMAGYLKSIDSNHLLEIGLEGFYGNDMRQYNPNSYIFGTNFISNNQVQGIDFTTIHMYPNQWLPGLTQEAQDKWASQWIQVHIDDSKMLKKPLLIAEFG... | Function: Possesses endo-beta-mannanase and mannan transglycosylase activities. May be involved in cell wall degradation during fruit ripening.
Catalytic Activity: Random hydrolysis of (1->4)-beta-D-mannosidic linkages in mannans, galactomannans and glucomannans.
Sequence Mass (Da): 45339
Sequence Length: 399
Subcellul... |
B3PF24 | MSLFTPLSETNVRSHTNTSSVFCRRIKTLVAGLTALGLMLAAVSASAGFYVSGKQLREGNGNNFIMRGVNLPHAWFPDRTNQALADISATGANSVRVVLSNGRLWSRTPESQVASIISQAKARQLITVLEVHDTTGYGEQTAATLSEAVDYWIAIRNALIGQEDYVIINIGNEPFGNGQSASTWLNLHRDAINRLRNAGFTHTLMVDAANWGQDWENIMRNNASSLFNSDPRRNVIFSVHMYEVYPNDTAVNNYMSAFNSMNLPLVVGEFAANHFGSYVDAGSIMARAQQYGFGYLGWSWSGNSSNLSALDVVTNFNAGS... | Function: Catalyzes the endo hydrolysis of beta-1,4-linked mannan, galactomannan and glucomannan. It is able to hydrolyze mannosidic linkages that are flanked by mannose or glucose.
Catalytic Activity: Random hydrolysis of (1->4)-beta-D-mannosidic linkages in mannans, galactomannans and glucomannans.
Sequence Mass (Da)... |
G1K3N4 | AGFYVDGNTLYDANGQPFVMRGINHGHAWYKDTASTAIPAIAEQGANTIRIVLSDGGQWEKDDIDTIREVIELAEQNKMVAVVEVHDATGRDSRSDLNRAVDYWIEMKDALIGKEDTVIINIANEWYGSWDGSAWADGYIDVIPKLRDAGLTHTLMVDAAGWGQYPQSIHDYGQDVFNADPLKNTMFSIHMYEYAGGDANTVRSNIDRVIDQDLALVIGEFGHRHTDGDVDEDTILSYSEETGTGWLAWSWKGNSTEWDYLDLSEDWAGQHLTDWGNRIVHGADGLQETSKPSTVFTDDNGGHPEPPT | Function: Catalyzes the endo hydrolysis of beta-1,4-linked mannan, galactomannan and glucomannan. It is able to hydrolyze mannosidic linkages that are flanked by mannose or glucose.
Catalytic Activity: Random hydrolysis of (1->4)-beta-D-mannosidic linkages in mannans, galactomannans and glucomannans.
Sequence Mass (Da)... |
Q9LZV3 | MKDQLGFRIVLCSAVFIILTQNRALADLDSESHEVNSESVGEEQWEMVQRKGMQFTLNGQPFYVNGFNTYWMMTLAADNSTRGKVTEVFQQASAVGMTVGRTWAFNDGQWRALQKSPSVYDEEVFKALDFVLSEARKYKIRLILSLVNNWDAYGGKAQYVKWGNASGLNLTSDDDFFTNPTLRNFYQSHVRTVLNRVNTFTNITYKNDPTIFAWELMNEPRCPSDPSGDKLQSWIQEMAVFVKSLDAKHLVEIGLEGFYGPSAPARTRFNPNPYAAQVGTDFIRNNQVLGIDFASVHVYPDSWISPAVSNSFLEFTSSWM... | Catalytic Activity: Random hydrolysis of (1->4)-beta-D-mannosidic linkages in mannans, galactomannans and glucomannans.
Sequence Mass (Da): 50622
Sequence Length: 448
Subcellular Location: Secreted
EC: 3.2.1.78
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Q0DCM5 | MRQERRLYSLLGLLLLLAVVYLTWFPTTHDGGGGGGGGWVKLPVPWLQPRMPFAARRGTHFVDADTGSPLYVNGWNSYWLLPARSPALAAEMLRRGRRMGLSVCRTWAFSDGGPGALQISPGRFSEAVFQVLDYVIYEARRNHIRLILCLVNNLDNLGGKAQYVQWAQAAGANMTNSTDSFYSHPTIKRYYKDYVKAILTRRNSYSRIRYSDEPAIFAWELMNEPRCVSNSSGPYLQAWIAEMAAYVKSLDTNHLVTVGTEGFYGPGIAERLGVNPGEWAASLCSDFIQNSAVEHIDFASVHAYPDSWLPRASLEEKVRY... | Catalytic Activity: Random hydrolysis of (1->4)-beta-D-mannosidic linkages in mannans, galactomannans and glucomannans.
Sequence Mass (Da): 49455
Sequence Length: 440
Subcellular Location: Secreted
EC: 3.2.1.78
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Q9FJZ3 | MKLLALFPFLAIVIQLSCWELGTDALPSGGFVRTKGVQFSLNGYPYYANGFNAYWLMYVASDPSQRSKISTAFQDASRHGLTVARTWAFSDGGYRALQYSPGSYNEDMFQGLDFALAEARRHGIKIILSFANNYESFGGRKQYVDWARSRGRPVSSEDDFFTDSLVKDFYKNHIKAVLNRFNTFTKVHYKDDPTIMAWELMNEPRCPSDPSGRAIQAWITEMAAHVKSLDRNHLLEAGLEGFYGQSSPQSKTLNPPGQFGTDFIANNRIPGIDFVTVHSYPDEWFPDSSEQSQMDFLNKWLDAHIQDAQNVLHKPIILAE... | Function: Required for both, loosening of the micropylar endosperm, and rupture of the seed coat in germinating seeds. May participate in the hydrolysis of the mannans in the cell wall of germinating seeds.
Catalytic Activity: Random hydrolysis of (1->4)-beta-D-mannosidic linkages in mannans, galactomannans and glucoma... |
P94078 | MAVKCFSLYLILAAIVIGGVTSEYIEYNTKPRIVPEKINVHLVPHSHDDVGWLKTVDQYYVGSNNSIRGACVQNVLDSVIASLLDDENRKFIYVEMAFFQRWWRQQSNAKKVKVKKLVDSGQLEFINGGMCMHDEATPHYIDMIDQTTLGHQFIKTEFGQVPRVGWQIDPFGHSAVQAYLLGAEFGFDSLFFARIDYQDRAKRLREKTLEVIWQGSKSLGSSSQIFTGVFPRHYDPPEGFTFEINDVSAPIQDDPLLFDYNVQERVNDFVAAALAQVNVTRTNHIMWLMGTDFRYQYAYSWFRQIDKFIHYVNKDGRLNV... | Cofactor: Binds 1 zinc ion per subunit.
Function: Liberates mannose from p-nitrophenyl-alpha-D-mannoside in vitro.
Catalytic Activity: Hydrolysis of terminal, non-reducing alpha-D-mannose residues in alpha-D-mannosides.
Sequence Mass (Da): 115220
Sequence Length: 1019
EC: 3.2.1.24
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O31646 | MTTEPLFFKPVFKERIWGGTALADFGYTIPSQRTGECWAFAAHQNGQSVVQNGMYKGFTLSELWEHHRHLFGQLEGDRFPLLTKILDADQDLSVQVHPNDEYANIHENGELGKTECWYIIDCQKDAEIIYGHNATTKEELTTMIERGEWDELLRRVKVKPGDFFYVPSGTVHAIGKGILALETQQNSDTTYRLYDYDRKDAEGKLRELHLKKSIEVIEVPSIPERHTVHHEQIEDLLTTTLIECAYFSVGKWNLSGSASLKQQKPFLLISVIEGEGRMISGEYVYPFKKGDHMLLPYGLGEFKLEGYAECIVSHL | Cofactor: Binds 1 zinc ion per subunit.
Catalytic Activity: D-mannose 6-phosphate = D-fructose 6-phosphate
Sequence Mass (Da): 36003
Sequence Length: 315
EC: 5.3.1.8
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P24174 | MAQSKLYPVVMAGGSGSRLWPLSRVLYPKQFLCLKGDLTMLQTTICRLNGVECESPVVICNEQHRFIVAEQLRQLNKLTENIILEPAGRNTAPAIALAALAAKRHSPESDPLMLVLAADHVIADEDAFRAAVRNAMPYAEAGKLVTFGIVPDLPETGYGYIRRGEVSAGEQDMVAFEVAQFVEKPNLETAQAYVASGEYYWNSGMFLFRAGRYLEELKKYRPDILDACEKAMSAVDPDLNFIRVDEEAFLACPEESVDYAVMERTADAVVVPMDAGWSDVGSWSSLWEISAHTAEGNVCHGDVINHKTENSYVYAESGLV... | Function: Involved in the biosynthesis of the capsular polysaccharide colanic acid.
Catalytic Activity: alpha-D-mannose 1-phosphate + GTP + H(+) = diphosphate + GDP-alpha-D-mannose
Sequence Mass (Da): 53016
Sequence Length: 478
Pathway: Nucleotide-sugar biosynthesis; GDP-alpha-D-mannose biosynthesis; GDP-alpha-D-mannos... |
Q5AZ53 | MIFSTLLSLALLATTATARKGFVTTKGDKFQLDGKDFYFAGSNAYYFPFNNNQTDVELGLSAAKKAGLLVFRTWGFNDKNVTYIEDGLPQYGGEGAGTTEVVFQWWQNGTSTIDLEPFDKVVNAAAKTGIKLIVTLVNNWADYGGMDVYTVNLGGQYHDDFYRLPQIKKAYKRYVKEMVTRYRNSPAIMAWELANEPRCGADGVRNLPASDECTPELLTSWIDEMSTYVKRLDPHHLVTWGGEGGFNYDSDDWAYNGSDGGDFEAELKLKNIDFGVFHSYPDWWSKTVEWTNKWIVDHARAARRVGKPVVHEEYGWLTPQ... | Function: Endo-1,4-mannanase that catalyzes the random hydrolysis of (1->4)-beta-D-mannosidic linkages in mannans and heteromannans. It is a crucial enzyme for depolymerization of seed galactomannans and wood galactoglucomannans. Active against locust bean gum and gum guar . Also has transglycosylation activity. Produc... |
Q8FHC7 | MHHDKRCKESNMKIVKAEVFVTCPGRNFVTLKITTEDGITGLGDATLNGRELSVASYLQDHLCPQLIGRDAHRIEDIWQFFYKGAYWRRGPVTMSAISAVDMALWDIKAKAANMPLYQLLGGASREGVMVYCHTTGHSIDEALDDYARHQELGFKAIRVQCGIPGMKTTYGMSKGKGLAYEPATKGQWPEEQLWSTEKYLDFMPKLFDAVRNKFGFDEHLLHDMHHRLTPIEAARFGKSIEDYRMFWMEDPTPAENQECFRLIRQHTVTPIAVGEVFNSIWDCKQLIEEQLIDYIRTTLTHAGGITGMRRIADFASLYQV... | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Has low D-mannonate dehydratase activity (in vitro), suggesting that this is not a physiological substrate and that it has no significant role in D-mannonate degradation in vivo. Has no detectable activity with a panel of 70 other acid sugars (in vitro).
Catalytic Act... |
A4XF23 | MKITAARVIITCPGRNFVTLKIETDQGVYGIGDATLNGRELSVVAYLQEHVAPCLIGMDPRRIEDIWQYVYRGAYWRRGPVTMRAIAAVDMALWDIKAKMAGMPLYQLLGGRSRDGIMVYGHANGSDIAETVEAVGHYIDMGYKAIRAQTGVPGIKDAYGVGRGKLYYEPADASLPSVTGWDTRKALNYVPKLFEELRKTYGFDHHLLHDGHHRYTPQEAANLGKMLEPYQLFWLEDCTPAENQEAFRLVRQHTVTPLAVGEIFNTIWDAKDLIQNQLIDYIRATVVGAGGLTHLRRIADLASLYQVRTGCHGATDLSPV... | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Catalyzes the dehydration of D-mannonate. Has no detectable activity with a panel of 70 other acid sugars (in vitro).
Catalytic Activity: D-mannonate = 2-dehydro-3-deoxy-D-gluconate + H2O
Sequence Mass (Da): 45244
Sequence Length: 402
Pathway: Carbohydrate metabolism;... |
P19994 | MIICKTPRELGIMREAGRIVALTHEELKKHIKPGISTKELDQIAERFIKKQGAIPSFKGYNGFRGSICVSVNEELVHGIPGSRVLKDGDIISIDIGAKLNGYHGDSAWTYPVGNISDDDKKLLEVTEESLYKGLQEAKPGERLSNISHAIQTYVENEQFSVVREYVGHGVGQDLHEDPQIPHYGPPNKGPRLKPGMVLAIEPMVNAGSRYVKTLADNWTVVTVDGKKCAHFEHTIAITETGFDILTRV | Cofactor: Binds 2 divalent metal cations per subunit. Has a high-affinity and a low affinity metal-binding site. The true nature of the physiological cofactor is under debate. The enzyme is active with cobalt, zinc, manganese or divalent iron ions. Most likely, methionine aminopeptidases function as mononuclear Fe(2+)-... |
Q4QRK0 | MAAVETRECETEGCHSEAKLQCPTCIKLGIQGSYFCSQECFKGSWATHKLLHKKAKEDKTNDEEKNCVEKEVNTDPWPGYRYTGKLRPYYPLTPMRLVPSNIQRPDYADHPLGMSESEQTMKGTSQIKILNAEEIEGMRVVCKLAREVLDIAAMMVKPGVTTEEIDHAVHLACTARNCYPSPLNYYNFPKSCCTSVNEVICHGIPDRRHLQEGDILNIDITVYHNGYHGDLNETFFVGEVDEGAKRLVQTTYECLMQAIDSVKPGIRYRELGNIIQKHAQANGFSVVRSYCGHGIHKLFHTAPNVPHYAKNKAVGVMKPG... | Cofactor: Binds 2 divalent metal cations per subunit. Has a high-affinity and a low affinity metal-binding site. The true nature of the physiological cofactor is under debate. The enzyme is active with zinc, cobalt, manganese or divalent iron ions. Has high activity with zinc; zinc cofactor is transferred into the acti... |
Q54WU3 | MEGILCASPGCGKPAKLQCPTCVNLKLETPSHFCSQECFKTFWPLHKMYHQKGQPENLPSQFRNYKFTGPLRPTNITPMRKAPEGIELPDYAIGSIPISERVADRKNMANIIHTPEEIEIMRQLGKMSREVLDIAGNAAKVGMTTEELDIIVHNAVIERGAYPSPLNYYKFPKSCCTSLNEVICHGIPDERPLRDGDILNVDVTLYWKGFHSDLNETYLIGNVDERGKNLVKCAYDCLELAVAMCKPGTLYRELGDAIQKHANKQGFSVVKNFCGHGIGRLFHCNPTVPHYSKNKAVGAMKVGHVFTIEPMINEGTWQDE... | Cofactor: Binds 2 divalent metal cations per subunit. Has a high-affinity and a low affinity metal-binding site. The true nature of the physiological cofactor is under debate. The enzyme is active with zinc, cobalt, manganese or divalent iron ions. Has high activity with zinc; zinc cofactor is transferred into the acti... |
P53582 | MAAVETRVCETDGCSSEAKLQCPTCIKLGIQGSYFCSQECFKGSWATHKLLHKKAKDEKAKREVSSWTVEGDINTDPWAGYRYTGKLRPHYPLMPTRPVPSYIQRPDYADHPLGMSESEQALKGTSQIKLLSSEDIEGMRLVCRLAREVLDVAAGMIKPGVTTEEIDHAVHLACIARNCYPSPLNYYNFPKSCCTSVNEVICHGIPDRRPLQEGDIVNVDITLYRNGYHGDLNETFFVGEVDDGARKLVQTTYECLMQAIDAVKPGVRYRELGNIIQKHAQANGFSVVRSYCGHGIHKLFHTAPNVPHYAKNKAVGVMKS... | Cofactor: Binds 2 divalent metal cations per subunit. Has a high-affinity and a low affinity metal-binding site. The true nature of the physiological cofactor is under debate. The enzyme is active with zinc, cobalt, manganese or divalent iron ions. Has high activity with zinc; zinc cofactor is transferred into the acti... |
P9WK20 | MRPLARLRGRRVVPQRSAGELDAMAAAGAVVAAALRAIRAAAAPGTSSLSLDEIAESVIRESGATPSFLGYHGYPASICASINDRVVHGIPSTAEVLAPGDLVSIDCGAVLDGWHGDAAITFGVGALSDADEALSEATRESLQAGIAAMVVGNRLTDVAHAIETGTRAAELRYGRSFGIVAGYGGHGIGRQMHMDPFLPNEGAPGRGPLLAAGSVLAIEPMLTLGTTKTVVLDDKWTVTTADGSRAAHWEHTVAVTDDGPRILTLG | Cofactor: Binds 2 divalent metal cations per subunit. Has a high-affinity and a low affinity metal-binding site. The true nature of the physiological cofactor is under debate. The enzyme is active with cobalt, zinc, manganese or divalent iron ions. Most likely, methionine aminopeptidases function as mononuclear Fe(2+)-... |
P53579 | MGDTITLLSRREIEKMRQAGQLAAALLDHLAPMVQPGITTLELNDEAEKWTKAHGAISAPLGYNGFPKSICTSINEVICHGIPHRKRVLQAGDIINVDVTPIVDGYHGDCSRTFFVGTPSPVAEKLVKVTEECLRLGIEAVKPGGKIGDIGAAIQSHAEAQGFSVVRDFVGHGISKIFHTAPQIPHYGKAGKGKRLRPGMVFTIEPMINEGTWEAVLLDDGWTAITKDGKLSAQFEHTIAVTEDGVEILTLGE | Cofactor: Binds 2 divalent metal cations per subunit. Has a high-affinity and a low affinity metal-binding site. The true nature of the physiological cofactor is under debate. The enzyme is active with cobalt, zinc, manganese or divalent iron ions. Most likely, methionine aminopeptidases function as mononuclear Fe(2+)-... |
O34484 | MIVTNDQELEGLKKIGRIVALAREEMKRKAEPGMSTKDLDLIGKAVLDEHGAVSAPEKEYDFPGVTCISVNDEVAHGIPSTSKILKAGDLVNIDISAEFGGFYSDTGISFVLGEGEERLHKLCQCAENAFQKGLQQAKAGKRQNQIGRAVYHEARSQGFTVIKTLTGHGIGRSLHEAPNHIMNYYDPFDNALFKNGTVIALEPFISTKAETIVEAGDGWTFKTPDKSMVAQVEHTIVITKDEPIILTKL | Cofactor: Binds 2 divalent metal cations per subunit. Has a high-affinity and a low affinity metal-binding site. The true nature of the physiological cofactor is under debate. The enzyme is active with cobalt, zinc, manganese or divalent iron ions. Most likely, methionine aminopeptidases function as mononuclear Fe(2+)-... |
Q4VBS4 | MAAPCAAQCLYRTGGLRLLQRISRLPHCHKDASLAHQCQFHRSFFWRKPKTSHSVVRPAIVRPAYPVPKHIQRPDYVSSSKVPEWPDYIEIKDEEQIQGLRRACQLARHILLLTGNSLKVGMTTDEIDFIVHQEAIRHNGYPSPLHYGGFPKSVCTSVNNVVCHGIPDSRPLQDGDIINIDVTVYLEGYHGDTSETFLIGSVNDQGRKLVDVARQCRDQAIAACGPGQPLCVIGNIISNIANSNGFRVCPYFIGHGIGEYFHGHPEIWHHANDNDLKMEEGMSFTIEPILMEGTSGFRILSDKWTAVSVDDKRSAQFEHT... | Cofactor: Binds 2 divalent metal cations per subunit. Has a high-affinity and a low affinity metal-binding site. The true nature of the physiological cofactor is under debate. The enzyme is active with cobalt, zinc, manganese or divalent iron ions. Most likely, methionine aminopeptidases function as mononuclear Fe(2+)-... |
Q54VU7 | MNKILKNIINKSSINNVFKTSFNGGISSSSSSSSSYLNNNNNIIKSYNVQQKQQQRYYSSFEDDLSPKKLKEKILENETEEIRDFVRSQRLTKKTASPLEGMNRKERRKMTTKLYRNPDNLIRGGIVSPQPLIPAHIKKPKYVLGEPVIDFEIDDPIEIHTAESIEHMRVVGKMAKEVLEYAGTLVRPGITTDEIDKLVHQNIIDRGAYPSPLGYKGFPKSICTSINEVLCHGIPDDRPLEFGDIVKIDVTLYYNGYHGDTCATFPVGEIDSSSKRLIEATEKALYAAIGEVKDGALFNKIGKKIQLVANKYSLSVTPEF... | Cofactor: Binds 2 divalent metal cations per subunit. Has a high-affinity and a low affinity metal-binding site. The true nature of the physiological cofactor is under debate. The enzyme is active with cobalt, zinc, manganese or divalent iron ions. Most likely, methionine aminopeptidases function as mononuclear Fe(2+)-... |
Q6UB28 | MAAPSGVHLLVRRGSHRIFSSPLNHIYLHKQSSSQQRRNFFFRRQRDISHSIVLPAAVSSAHPVPKHIKKPDYVTTGIVPDWGDSIEVKNEDQIQGLHQACQLARHVLLLAGKSLKVDMTTEEIDALVHREIISHNAYPSPLGYGGFPKSVCTSVNNVLCHGIPDSRPLQDGDIINIDVTVYYNGYHGDTSETFLVGNVDECGKKLVEVARRCRDEAIAACRAGAPFSVIGNTISHITHQNGFQVCPHFVGHGIGSYFHGHPEIWHHANDSDLPMEEGMAFTIEPIITEGSPEFKVLEDAWTVVSLDNQRSAQFEHTVLI... | Cofactor: Binds 2 divalent metal cations per subunit. Has a high-affinity and a low affinity metal-binding site. The true nature of the physiological cofactor is under debate. The enzyme is active with cobalt, zinc, manganese or divalent iron ions. Most likely, methionine aminopeptidases function as mononuclear Fe(2+)-... |
P9WK18 | MPSRTALSPGVLSPTRPVPNWIARPEYVGKPAAQEGSEPWVQTPEVIEKMRVAGRIAAGALAEAGKAVAPGVTTDELDRIAHEYLVDNGAYPSTLGYKGFPKSCCTSLNEVICHGIPDSTVITDGDIVNIDVTAYIGGVHGDTNATFPAGDVADEHRLLVDRTREATMRAINTVKPGRALSVIGRVIESYANRFGYNVVRDFTGHGIGTTFHNGLVVLHYDQPAVETIMQPGMTFTIEPMINLGALDYEIWDDGWTVVTKDRKWTAQFEHTLLVTDTGVEILTCL | Cofactor: Binds 2 divalent metal cations per subunit. Has a high-affinity and a low affinity metal-binding site. The true nature of the physiological cofactor is under debate. The enzyme is active with cobalt, zinc, manganese or divalent iron ions. Most likely, methionine aminopeptidases function as mononuclear Fe(2+)-... |
Q96JE9 | MAWPCITRACCIARFWNQLDKADIAVPLVFTKYSEATEHPGAPPQPPPPQQQAQPALAPPSARAVAIETQPAQGELDAVARATGPAPGPTGEREPAAGPGRSGPGPGLGSGSTSGPADSVMRQDYRAWKVQRPEPSCRPRSEYQPSDAPFERETQYQKDFRAWPLPRRGDHPWIPKPVQISAASQASAPILGAPKRRPQSQERWPVQAAAEAREQEAAPGGAGGLAAGKASGADERDTRRKAGPAWIVRRAEGLGHEQTPLPAAQAQVQATGPEAGRGRAAADALNRQIREEVASAVSSSYRNEFRAWTDIKPVKPIKAK... | Function: Involved in microtubule stabilization in many cell types, including neuronal cells (By similarity). Specifically has microtubule cold stabilizing activity (By similarity). Involved in dendrite morphogenesis and maintenance by regulating lysosomal trafficking via its interaction with TMEM106B . Regulates KIF5A... |
Q63560 | MAWPCITRACCIARFWNQLDKADIAVPLVFTKYSEATEHPGAPPQPPAPPQPGLAPPSRAVAIETQPAQGESDAVARATGPAPGPSGDRETAAAPGRSGLGLGAASGSTSGSGPADSVMRQDYRAWKVQRPEPSCRPRSEYQPSDAPFERETQYQKDFRAWPLPRRGDHPWIPKPVQIPATSQPSPPVLGMPKRRPQSQERGPIQLSADARDPEGAGGAGVPAAGKASGADQRDTRRKAGPAWMVTRTEGHEEKPLPPAQSQTQEGGPAAGKASGADQRDTRRKAGPAWMVTRTEGHEEKPLPPAQSQTQEGGPAAGKAS... | Function: Involved in microtubule stabilization in many cell types, including neuronal cells . Specifically has microtubule cold stabilizing activity . Involved in dendrite morphogenesis and maintenance by regulating lysosomal trafficking via its interaction with TMEM106B (By similarity). Regulates KIF5A-mediated axona... |
Q14244 | MAELGAGGDGHRGGDGAVRSETAPDSYKVQDKKNASSRPASAISGQNNNHSGNKPDPPPVLRVDDRQRLARERREEREKQLAAREIVWLEREERARQHYEKHLEERKKRLEEQRQKEERRRAAVEEKRRQRLEEDKERHEAVVRRTMERSQKPKQKHNRWSWGGSLHGSPSIHSADPDRRSVSTMNLSKYVDPVISKRLSSSSATLLNSPDRARRLQLSPWESSVVNRLLTPTHSFLARSKSTAALSGEAASCSPIIMPYKAAHSRNSMDRPKLFVTPPEGSSRRRIIHGTASYKKERERENVLFLTSGTRRAVSPSNPK... | Function: Microtubule-stabilizing protein that may play an important role during reorganization of microtubules during polarization and differentiation of epithelial cells. Associates with microtubules in a dynamic manner. May play a role in the formation of intercellular contacts. Colocalization with TRPV4 results in ... |
O88735 | MAEQGAGGDGHRGGDGATHSDPASDGYKVQEKRTAPSRPTSTVSGQTSNHSGNKPDPPPVLRVDDRQRLARERREEREKQLAARETVWLEREERARQHYERHLEARKKKLEDQRLKEERRRAAVEEKRRQRLEEDKERHEAVVRRTMERSQKPRQKSNRWSWGSPLHGSSSIHSGDPDRRSVSTMNLSKHVDPVISKRLSSSSATLLNSPDRARRLQLSPWESSVVSRLLTPTHSFLARSKSTAALSGDTASCSPIIMPFKAAHSRNPVDRPKLFVTPPEGSARRRTIHGLASHKREREREHVPFHVSPGARRTLSPSNL... | Function: Microtubule-stabilizing protein that may play an important role during reorganization of microtubules during polarization and differentiation of epithelial cells. Associates with microtubules in a dynamic manner. May play a role in the formation of intercellular contacts. Colocalization with TRPV4 results in ... |
Q9FLS8 | MEAEKSKQNPGKKPVEATMEHVLVALRETKEKREIRIQKLFEFFDNSKLGFLDDTQIEKGLSSLSIPPKYRYASDFLKVCDSNRDGRVDYQEFRRYMDAKELELYKIFQAIDIEHNGDICPAELWEALDKAGIKIKDEELASFMEHVDKDNNGIITFEEWRDFLLLNPHEATIENIYHHWERVCLIDIGEQAVIPDGISAHAQRSKLLLAGGIAGAVSRTATAPLDRLKVALQVQRTNLGVVPTIKKIWREDKLLGFFRGNGLNVAKVAPESAIKFAAYEMLKPIIGGADGDIGTSGRLLAGGLAGAVAQTAIYPMDLVK... | Function: Calcium-dependent mitochondrial carrier protein that catalyzes the import of ATP co-transported with metal divalent cations across the mitochondrial inner membrane in exchange for phosphate (Pi) . Can transport phosphate, AMP, ADP, ATP, adenosine 5'-phosphosulfate and, to a lesser extent, other nucleotides . ... |
Q9FI43 | MEATKSSKQNCCNPVKKPGPVSIDHVLLALRETREERDLRIRSLFSFFDSENVGYLDCAQIEKGLCALQIPSGYKYAKELFRVCDANRDGRVDYHEFRRYMDDKELELYRIFQAIDVEHNGCISPEGLWDSLVKAGIEIKDEELARFVEHVDKDNDGIIMFEEWRDFLLLYPHEATIENIYHHWERVCLVDIGEQAVIPEGISKHIKRSNYFIAGGIAGAASRTATAPLDRLKVLLQIQKTDARIREAIKLIWKQGGVRGFFRGNGLNIVKVAPESAIKFYAYELFKNAIGENMGEDKADIGTTVRLFAGGMAGAVAQAS... | Function: Calcium-dependent mitochondrial carrier protein that catalyzes the import of ATP co-transported with metal divalent cations across the mitochondrial inner membrane in exchange for phosphate (Pi) . Can transport phosphate, AMP, ADP, ATP, adenosine 5'-phosphosulfate, sulfate and thiosulfate, and, to a lesser ex... |
Q9LY28 | MESSKPKNRNPMKKPVSITMEHVLLALRETMDEREIRIRSLFDFFDNSNLGFLDYAQIEKGLASLQIPPEYKYARDLFRVCDANRDGRVDYQEFRRYIDAKELELYRIFQAIDVEHNGCILPEELWEALVKAGIEIDDEELARFVEHVDKDNNGTITFEEWRDFLLLYPHEATLENIYHHWERVCLIDIGEQAVIPDGISKHVKRSRLLLAGGLAGAVSRTATAPLDRLKVVLQVQRAHAGVLPTIKKIWREDKLMGFFRGNGLNVMKVAPESAIKFCAYEMLKPMIGGEDGDIGTSGRLMAGGMAGALAQTAIYPMDLV... | Function: Calcium-dependent mitochondrial carrier protein that catalyzes the import of ATP co-transported with metal divalent cations across the mitochondrial inner membrane in exchange for phosphate (Pi) . Can transport phosphate, AMP, ADP, ATP, adenosine 5'-phosphosulfate, sulfate and thiosulfate, and, to a lesser ex... |
O94737 | MDSKHSVFNVMGQEFVLQKGYEVIKGLGKGSYGVVCSAKNIEVEDNNKVAIKKITNIFSKKMLAKRALREIMLLQHFRNHKNITTLYDMDIVDPSKFNELYLYEELMQANLNSIIRSDQPLTDAHFQSFIYQILCGLKYIHSANVLHRDLKPSNLLINADCKLKICDFGLSRGISVNQGQGTEYMTEYVTTRWYRAPEVMLSFQSYSKAIDLWSVGCILAELLGRKPFFKGSNYVDQLNQIFCILGTPNENIISKIKSASAQSYIRSLPTLPKMPYSKIFPYANPDALDLLNCLLTFDPYDRISCEEALEHPYLIIWHDP... | Function: Serine-threonine protein kinase which may be involved in maintenance of cell integrity. Functionally complements SLT2 null mutant in S.cerevisiae.
PTM: Dually phosphorylated on Thr-186 and Tyr-188, which activates the enzyme.
Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protei... |
P49071 | MLSLQNQRQPKTTPLTDDYVTSNTVLGYGINGKVVQCTHRRTQQNYALKVLLDSERARREVDLHWRVSGCRYIVNIIDVYENTFKDRKCLLVVMECMEGGELFQRIQDKADGAFTEREAAQIMHEICAAVDYLHSRDIAHRDLKPENLLYTTTQPNATLKLTDFGFAKETFTSYTLQTPCYTPYYVAPEVLGPEKYDKSCDIWSLGVVMYIIMCGFPPFYSNHGLAISPGMKNRIRTGQYDFPDPEWTNVSQAAKDLIKGMLNVDPSKRLRIQDVISNKWIAQYNAVPQTPLCTGRMLKEAEETWPEVQEEMTRSLATMR... | Function: Its physiological substrate seems to be the small heat shock protein (HSP27/HSP25).
PTM: Phosphorylated and activated by MAP kinase.
Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Sequence Mass (Da): 41401
Sequence Length: 359
EC: 2.7.11.1
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P0C1Q5 | INWKALLDAAKKVL | Function: Potent antimicrobial peptide and potent mast cell degranulating peptide . Is active on both Gram-negative bacteria (E.coli MIC=7.8 ug/ml, and P.aeruginosa MIC=62.5 ug/ml) and Gram-positive bacteria (S.aureus MIC=15.6 ug/ml, and B.cereus MIC=7.8 ug/ml) . Its mast cell degranulation activity may be related to t... |
P0C022 | INLLKIAKGIIKSL | Function: Antimicrobial and mast cell degranulating peptide. Shows broad-spectrum antimicrobial activity against the Gram-positive bacteria S.aureus ATCC 6538 (MIC=5 ug/ml), S.saprophyticus CS (MIC=5 ug/ml), S.epidermidis CS (MIC=5 ug/ml), B.subtilis CCT 2471 (MIC=40 ug/ml), and the Gram-negative bacteria E.coli CCT 13... |
P0DRA7 | INWLKLGKKMMSAL | Function: Antimicrobial peptide. Has activity against both Gram-positive and -negative bacteria (B.subtilis (MIC=9 uM), E.coli (MIC=65 uM)). Shows mast cell degranulation activity (EC(50)=15-26 uM). Has low hemolytic activity (IC(50)=100 uM) . Its mast cell degranulation activity may be related to the activation of G-p... |
A1T9P9 | MTDRVTVGNLRVAPVLYDFINNEALPGTDIDPDTFWSGVDKVVADLTPRNQDLLARRDDLQAQIDRWHRARVIGGFEPEDYKQFLTDIGYLEPEPADFSITTAGVDDEITTTAGPQLVVPILNARFALNAANARWGSLYDALYGTDVISDEGGAEAGSGYNPVRGDKVIAYARRFLDGAVPLASGSWSDITGLKLDEGQLAATLDDGGTVGLGTPEQFVGYLGDAEAPTAVLLVNNGLHIEILIDAEAPIGATDKAGIKDVVLESAITTIMDFEDSVAAVDADDKVLGYRNWLGLNRGDLAEEVSKGGKTFTRVLNSDRT... | Function: Involved in the glycolate utilization. Catalyzes the condensation and subsequent hydrolysis of acetyl-coenzyme A (acetyl-CoA) and glyoxylate to form malate and CoA.
Catalytic Activity: acetyl-CoA + glyoxylate + H2O = (S)-malate + CoA + H(+)
Sequence Mass (Da): 79327
Sequence Length: 734
Pathway: Carbohydrate ... |
Q50418 | MSIDAKLSRQASGSKAGVACVPDAYSFSEARSPGTRFALMLSAVAAGLAGGAMLHSAMSATSALTGLFIVLALAGGFLSTWSPCGYSSLSLLRPAGRYSFASVLRWSPTFFTHALGYAIGAVVLGGALGMAGWLLFSSLPFSYMVAGMAVLALGYGAHQFGFMKMPYPQRRAQVPHDARFRFRSSVIGLLYGYALGMNYLTYVQTPILYIVTGVALFCGDVKTAIVIIGIFNIGRCLPVAVNFLPVKNVTVQVWLARWQERAVEVDGFLLLSVGSAALMLLVL | Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 30033
Sequence Length: 283
Pathway: One-carbon metabolism; methylamine degradation.
Subcellular Location: Cell membrane
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Q50230 | MSMNIGATAMSRSSQAYAVETCVPDAYHFSKAQSTGTRFIMMLTAVASGVFAGRVMHSTMSVEMALTGLFVVLAFVGGLLSTWSPCGYSSLSLLRPAGRYSLGAVTRWAPTFFTHAVGYAIGAVVLGGALGGISWLLFADVPLQYAVIGLATLAIGYGLHQFGFLKMPYPQRRAQVPHDARFRFRSSVIGLLYGFSLGMNYLTYVQTPMLYIVTGVALLSGGVKAGIAVIAVFNIGRCLPVAVNFLPVKDQSVQAWLARWQESAVEVDGFLLLAIASAALMLVML | Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 30429
Sequence Length: 285
Pathway: One-carbon metabolism; methylamine degradation.
Subcellular Location: Cell membrane
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Q56463 | MASLDNFDMAAGRTDGVADCVAFPGRFSTWTRALILAASAAGGGAAALAMDAAHVALVLGLAAFAGGLLSTWSPCGYSSISLLRPTGKGARAVLDWLPTFATHGLGYALGALILGTLLGAIGGIAGLSGFATSFGLGLLAVIGLAYGAHQLDFLRVPYPQRRAQVPHDARQRFPKWVVGGLYGLSLGLDYLTYVQTPLLYLVTAAAVLSGNVAEAVALIAIFNLGRYLPVAVNLLPVTDYQIQSWLGRNQERAAIADGAILTAVGAAFAMLALA | Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 28174
Sequence Length: 274
Pathway: One-carbon metabolism; methylamine degradation.
Subcellular Location: Cell membrane
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Q49128 | MRAILPIPVLIAWAMVVCGGAYAVTTCSGAATATADASQQDLAALKARFRRPESVPHPKANPLTPEKVALGKALFFDPRLSRSGSVSCATCHNPSLGWSDGLTRAVGFGMVPLPRRTPPVLNLAWGTAFQWDGRADSLEAQARMPITAPDEMNMSMDLVVERLKAVPGYAPLFRNAFGSEEPIGARHVTAALATFQRTLVSGEAPFDRWALGDESAIGADAKRGFALFTGKAGCAACHSTWRFTDDSFHDIGLKAGNDLGRGKFAPPSVTAMRYAFKTPSLRDLRMEGPYMHDGQLGSLEAVLDHYIKGGEKRPSLSFEM... | Function: Involved in methylamine metabolism. Essential for the maturation of the beta subunit of MADH, presumably via a step in the biosynthesis of tryptophan tryptophylquinone (TTQ), the cofactor of MADH.
PTM: Binds 2 heme c groups covalently per subunit.
Sequence Mass (Da): 38146
Sequence Length: 353
Pathway: One-ca... |
Q50233 | MLFRHLVLIISTLMVANTAWSANLPPREKFKRPDSIPAPLSNPLTLEKATLGKTLFFDQRLSRSGGMACATCHSPDQRWSDGRTLPLQAESVSNARRTPTVLNSAWLSALMWDGRATTLEEQAVLPITTAHEMNFDLASLVSRLQRIEGYRPLFTQAFGDDSISQQRITQALASFQRTLVSNIAPFDRWVAGDEQAISESAKRGFAVFNDKNKANCVACHSSWRFTDDSFHDIGLPSKDLGRGAKVPSQVTLMQHAFKTPSLRDLSIDGPYMHDGSIRGLKTVIKHYKSEAIQRESLSKDMQKFELSNLEESDLIAFIQS... | Function: Involved in methylamine metabolism. Essential for the maturation of the beta subunit of MADH, presumably via a step in the biosynthesis of tryptophan tryptophylquinone (TTQ), the cofactor of MADH.
PTM: Binds 2 heme c groups covalently per subunit.
Sequence Mass (Da): 37265
Sequence Length: 335
Pathway: One-ca... |
Q51658 | MLRLACLAPLAILIPAAGTAEQARPADDALAALGAQLFVDPALSRNATQSCATCHDPARAFTDPREGKAGLAVSVGDDGQSHGDRNTPTLGYAALVPAFHRDANGKYKGGQFWDGRADDLKQQAGQPMLNPVEMAMPDRAAVAARLRDDPAYRTGFEALFGKGVLDDPERAFDAAAEALAAYQATGEFSPFDSKYDRVMRGEEKFTPLEEFGYTVFITWNCRLCHMQRKQGVAERETFTNFEYHNIGLPVNETAREASGLGADHVDHGLLARPGIEDPAQSGRFKVPSLRNVAVTGPYMHNGVFTDLRTAILFYNKYTSR... | Function: Involved in methylamine metabolism. Essential for the maturation of the beta subunit of MADH, presumably via a step in the biosynthesis of tryptophan tryptophylquinone (TTQ), the cofactor of MADH.
PTM: Binds 2 heme c groups covalently per subunit.
Sequence Mass (Da): 42230
Sequence Length: 387
Pathway: One-ca... |
P15283 | MSDIETFYDVMRRQGITRRSFMKSVRSPQHVLGLGPSFVPKIGEAMETKPRTPVVWVHGLECTCCSESFIRSAHPLAKDVVLSMISLDYDDTLMAAAGHAAEAAFEETIAKYKGNYILAVEGNPPLNEDGMFCITGGKPFVEKLRHAAEGAKAIISWGACASYGCVQAAAPNPTQATPVHKVITDKPIIKVPGCPPIAEVMTGVITYMLTFDRMPELDRQGRPAMFYSQRIHDKCYRRPHFDAGQFVEHWDDENARKGYCLYKMGCKGPTTYNACSTVPLERRRHFPIQSGHGCIGCSEDGFWDQGSFYDRLTTIKQFGI... | Cofactor: Binds 1 [3Fe-4S] cluster.
Function: This enzyme recycles the H(2) produced by nitrogenase to increase the production of ATP and to protect nitrogenase against inhibition or damage by O(2) under carbon- or phosphate-limited conditions.
Catalytic Activity: A + H2 = AH2
Location Topology: Peripheral membrane pro... |
P31884 | MLEEKGIERRDFMKWAGAMTAMLSLPATFTPLTAKAAELADRLPVIWLHMAECTGCSESLLRTDGPGIDSLIFDYISLEYHETVMAAAGWQAEHNLEHAIEKYKGRYVLMVEGGIPAGSSEFYLTVGPHGTTGAEHARHASANAAAIFAIGSCSSFGGVQAARPNPTNAQPLSKVTNKPVINVPGCPPSEKNIVGNVLHFILFGTLPSVDAFNRPMWAYGLRIHDLCERRGRFDAGEFVQEFGDEGAKKGYCLYKVGCKGPYTFNNCSKLRFNQHTSWPVQAGHGCIGCSEPDFWDTMGPFEEPVANRLYATAFDGLGAD... | Cofactor: Binds 1 [3Fe-4S] cluster.
Catalytic Activity: a menaquinone + H2 = a menaquinol
PTM: Predicted to be exported by the Tat system. The position of the signal peptide cleavage has been experimentally proven.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 38294
Sequence Length: 354
Subcellular... |
P69743 | MTGDNTLIHSHGINRRDFMKLCAALAATMGLSSKAAAEMAESVTNPQRPPVIWIGAQECTGCTESLLRATHPTVENLVLETISLEYHEVLSAAFGHQVEENKHNALEKYKGQYVLVVDGSIPLKDNGIYCMVAGEPIVDHIRKAAEGAAAIIAIGSCSAWGGVAAAGVNPTGAVSLQEVLPGKTVINIPGCPPNPHNFLATVAHIITYGKPPKLDDKNRPTFAYGRLIHEHCERRPHFDAGRFAKEFGDEGHREGWCLYHLGCKGPETYGNCSTLQFCDVGGVWPVAIGHPCYGCNEEGIGFHKGIHQLANVENQTPRSQ... | Cofactor: Binds 1 [3Fe-4S] cluster.
Function: This is one of three E.coli hydrogenases synthesized in response to different physiological conditions. HYD2 is involved in hydrogen uptake.
Catalytic Activity: A + H2 = AH2
PTM: Predicted to be exported by the Tat system. The position of the signal peptide cleavage has not... |
Q35127 | MRLLKSHPLLKLVNSYLIDASQPSNISYLWNFGSLLACCLIIQIVTGVTLAMHYSPNVLEAFNSIEHIMRDVNNGWLVRYLHSNTASAFFFLVYLHIGRGMYYGSYRAPRTLVWAIGTVILILMMATAFLGYQHSPKWFDISNKGSISNKGNITNSLPPLLQRWGGRINKRLFNKNLVKRGYCTSSSLNSPEMSERLQTIINELGINPVYVYEDLNQPSSWKQILHDTRDLSGVYMIINKTTKDYYIGSASNNRFYTRFCNHVIHFTGSKIVKLAIKKYELKNFAFVILDLYPNVVTKENNKELLDLEDKYLKLLVPNYN... | Function: Mitochondrial DNA endonuclease involved in intron homing.
PTM: The mature protein may arise from proteolytic cleavage of an in-frame translation of cob exon 1 plus intron 1, containing the bI1 open reading frame.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 51648
Sequence Length: 448
Sub... |
P03873 | MAFRKSNVYLSLVNSYIIDSPQPSSINYWWNMGSLLGLCLVIQIVTGIFMAMHYSSNIELAFSSVEHIMRDVHNGYILRYLHANGASFFFMVMFMHMAKGLYYGSYRSPRVTLWNVGVIIFILTIATAFLGYCCVYGQMSHWGNMNIASNMFNMMKTIYMMMLMLLIYIFYTIMMRQMMKTKEYTMLIKSMDYINKNKYMINLNMTNKKDMNNNIGPLNMNILSIIYGSMLGDGHAEKRKGGKGTRIVFQQEYCNINYLYYLHSLLANLGYCNTNLPLIKTRLGKKGKIRQYLKFNTWTYDSFNMIYSEWYIKNMSGKGN... | Function: This protein is responsible for splicing and maturation of cytochrome b mRNA. Specifically, it may be responsible for the splicing specificity of the second intron.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 49326
Sequence Length: 423
Subcellular Location: Mitochondrion inner membrane
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A9RAG7 | MTIRKSNPYLSLVNSYLMDSPQPSSMNYWWNVGSLLGLCLVMQMASGMFLAMHYSSSMELAFNSVEHMMRDVNAGWLMRYIHANGASFFFMCLYLHMGKALYYGSYKSPRVLVWSMGVMMFMLTMATAFMGYCLVYGQMSHWGATVITNLLSAMPFMGGDLVPLSIILSLYLLYISLKTFMKMIFNQSYMCPAKGWVKKVLDNTFCIKKYMHMYLSSRTSPXLYINTMSNMQHMKIMSTKSHTKDRDTSFLEKDIKNMDRNLLALMVGFMDGDGYIRMNKKSKDNMNYIYMSLIMNLNKNDLKLLQYFHQQLNMGKVYNM... | Function: Mitochondrial mRNA maturase required for splicing of intron 3 of the cytochrome b (COB) gene, containing its own coding sequence.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 61859
Sequence Length: 522
Subcellular Location: Mitochondrion inner membrane
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P0CY43 | MRLLKSHPLLKLVNSYLIDASQPSNISYLWNFGSLLACCLIIQIVTGVTLAMHYSPNVLEAFNSIEHIMRDVNNGWLVRYLHSNTASAFFFLVYLHIGRGMYYGSYRAPRTLVWAIGTVILILMMATAFLGYVLPYGQMSLWGATVITNLISAIPWIGQDIVESKIITLIINLSFIAILFSIVVVYYYILLHVNFSSNLPTIGVIHQNALKKSNKALRLDKQEYISIPSSFLAFLAGLVDGDGYIQVTKTSKGFIAIKLVISLHLEDLSILEYIHSVLKIGKINIYKDLRSPTCKLVINKTDLQEILFPLLMYNKIFFLT... | Function: Mitochondrial mRNA maturase required for splicing of intron 3 of the cytochrome b (cob) gene, containing its own coding sequence.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 54555
Sequence Length: 477
Subcellular Location: Mitochondrion inner membrane
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Q9ZZW7 | MAFRKSNVYLSLVNSYIIDSPQPSSINYWWNMGSLLGLCLVIQIVTGIFMAMHYSSNIELAFSSVEHIMRDVHNGYILRYLHANGASFFFMVMFMHMAKGLYYGSYRSPRVTLWNVGVIIFILTIATAFLGYCCVYGQMSHWGATVITNLFSAIPFVGNDIVSWLWGGFNMEDPYYSNMMLNKSVLCWNIFIWMMNYYIIQLIIYNNMIWNKNNMVKMFIMRRKLAVINMYMYMKLIIQRTYSYYMNNTIIYDKNHKLNTDNPIYAYIGGLFEGDGWITISKKGKYLLYELGIEMHIRDIQLLYKIKNILGIGKVTIKKL... | Function: Mitochondrial mRNA maturase required for splicing of intron 3 of the cytochrome b (COB) gene, containing its own coding sequence. In vivo splicing requires the formation of a ribonucleoprotein complex together with the imported mitochondrial RNA-splicing protein MRS1. The complex seems to stimulate the intrin... |
P03879 | MAFRKSNVYLSLVNSYIIDSPQPSSINYWWNMGSLLGLCLVIQIVTGIFMAMHYSSNIELAFSSVEHIMRDVHNGYILRYLHANGASFFFMVMFMHMAKGLYYGSYRSPRVTLWNVGVIIFILTIATAFLGYCCVYGQMSHWGATVITNLFSAIPFVGNDIVSWLWGGFSVSNPTIQRFFALHYLVPFIIAAMVIMHLMALHIHGSSNPLGITGNLDRIPMHSYFIFKDLVTVFLFMLILALFVFYSPNTLGQNMALLLITYVINILCAVCWKSLFIKYQWKIYNKTTYYFIIQNILNTKQLNNFVLKFNWTKQYNKMNI... | Function: Mitochondrial mRNA maturase required for splicing of intron 4 of the cytochrome b (COB) gene, containing its own coding sequence, and intron 4 in COX1, coding for the related homing endonuclease aI4. In vivo splicing requires in addition the imported mitochondrial leucyl-tRNA synthetase NAM2. Both proteins se... |
Q8WQL7 | MNTADVPDNLQSWGQQPSSSYSNTQQHSQMTNLPPINHNNLCDTEPMNEDFQLQDVQADELQKQQKQQEQQHIQQQNAQRFIAQSRQPHSNILRFPQPPITSIKTNSHAFYPQQEVTQVRPKKHRVSMTNAEAALTPGMPPEKQAAKKRNIGQFSTDTVPAGIGMIGIPFESTSKPLQIQQFRNPQDAPVRKLTSDLIKTYKAINESFYLRKQVRRDRHKSQDAGKPKGSKDGSGASLTDTFSIHNAIPITSSDNHYQQDAHQNAPPLLDTNAPPTSTMVVPMRTETDLQQQQRQKSSRGGPYNNGYDDQNYDYILKNGE... | Function: Possible role in the function of olfactory neurons.
Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Sequence Mass (Da): 101244
Sequence Length: 882
Subcellular Location: Nucleus
EC: 2.7.12.1
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Q73ZP8 | MSAATTADIDHYRTVLAGAFDDQVLEWTREAEARQRFPRELIEHLGARGVFSEKWCGGMLPDVGKLVELARALGRLSSAGIGVGVSLHDSAIAVLRRFGKSDYLRDICERAIAGQAVLCIGASEESGGSDLQIVRTEMSSRDGGFDIRGVKKFVSLSPIADHIMVVARSIDHDSASKHGNVALIAVPTSQASVQRPYAKVGAGPLDTAAVHIDTWVPADALVARAGTGLAAISWGLAHERMSIAGQIAASCQRAIGITLARMMTRRQFGRTLFEHQALRLRMADLQARVDLLQHGLNGIAAQGRLDLRAAAGVKVTAARL... | Function: Catalyzes the dehydrogenation at the alpha-beta position of ACP-bound acyl chains. This results in the introduction of a double bond in the lipidic chain, which is further transferred to the epsilon-amino group of lysine residue in the mycobactin core by MbtK (By similarity).
Sequence Mass (Da): 41370
Sequenc... |
O43462 | MIPVSLVVVVVGGWTVVYLTDLVLKSSVYFKHSYEDWLENNGLSISPFHIRWQTAVFNRAFYSWGRRKARMLYQWFNFGMVFGVIAMFSSFFLLGKTLMQTLAQMMADSPSSYSSSSSSSSSSSSSSSSSSSSSSSLHNEQVLQVVVPGINLPVNQLTYFFTAVLISGVVHEIGHGIAAIREQVRFNGFGIFLFIIYPGAFVDLFTTHLQLISPVQQLRIFCAGIWHNFVLALLGILALVLLPVILLPFYYTGVGVLITEVAEDSPAIGPRGLFVGDLVTHLQDCPVTNVQDWNECLDTIAYEPQIGYCISASTLQQLSF... | Cofactor: Binds 1 zinc ion per subunit.
Function: Zinc metalloprotease that mediates intramembrane proteolysis of proteins such as ATF6, ATF6B, SREBF1/SREBP1 and SREBF2/SREBP2 . Catalyzes the second step in the proteolytic activation of the sterol regulatory element-binding proteins (SREBPs) SREBF1/SREBP1 and SREBF2/SR... |
O42954 | MDINPPPSTAPSSPRRSIQRISDAKNKALTFNRRRLGLIKKAHELSVLCDAKVVVMIFDSKNACHVYSSEEPEEQRDALLQKFLNKDFVTVDPLRNINPNIPSDESLHNWRPKDKRIASVTTYSAQPSNNCSSATDSENDFQSFTIKSSTTYHTTPTTASENKKIESITIPDHASVYNDLPLSPTVKHSFVSPVSGDYSDSPLEPSSSSSFSVPPESLNPTLSFQHNDVPQTDNFIPFLTPKRQAYGQSSSRADRSSVRRSQSFKNRRNGKPRISRLHTSHASIDGLTDFIQSPSSGYLDPSSTPITPLDSAINQITPPF... | Function: Acts as a transcriptional activator with a role in the regulation of mitosis. Regulates septation and the periodic transcription of cdc15.
PTM: Phosphorylated. Occurs periodically during mitosis.
Sequence Mass (Da): 50907
Sequence Length: 457
Subcellular Location: Nucleus
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P04298 | MDANVVSSSTIATYIDALAKNASELEQRSTAYEINNELELVFIKPPLITLTNVVNISTIQESFIRFTVTNKEGVKIRTKIPLSKVHGLDVKNVQLVDAIDNIVWEKKSLVTENRLHKECLLRLSTEERHIFLDYKKYGSSIRLELVNLIQAKTKNFTIDFKLKYFLGSGAQSKSSLLHAINHPKSRPNTSLEIEFTPRDNETVPYDELIKELTTLSRHIFMASPENVILSPPINAPIKTFMLPKQDIVGLDLENLYAVTKTDGIPITIRVTSNGLYCYFTHLGYIIRYPVKRIIDSEVVVFGEAVKDKNWTVYLIKLIEP... | Function: Catalytic subunit of the mRNA capping enzyme which catalyzes three enzymatic reactions: the 5' triphosphate end of the pre-mRNA is hydrolyzed to a diphosphate by RNA 5' triphosphatase; the diphosphate RNA end is capped with GMP by RNA guanylyltransferase and the GpppN cap is methylated by RNA (guanine-N7) met... |
Q9LHQ7 | MKRGFSDSPSSSAPPPSSRFKSNPEGDSQFLEDETTKNFARKVADHYSRRTNQTLEEREASPIIHLKKLNNWIKSVLIQLYARPDDAVLDLACGKGGDLIKWDKARIGYYVGIDIAEGSIEDCRTRYNGDADHHQRRKKFSFPSRLLCGDCFEVELDKILEEDAPFDICSCQFAMHYSWTTEARARRALANVSALLRPGGVFIGTMPDANVIIKKLREAEGLEIGNSVYWIRFGEEYSQKKFKSSSPFGIEYVFHLEDAVDCPEWIVPFNVFKSLAEEYDLELVFVKNSHEFVHEYMKKPEFVELMRRLGALGDGSNDQS... | Function: mRNA-capping methyltransferase that methylates the N7 position of the added guanosine to the 5'-cap structure of mRNAs. Binds RNA containing 5'-terminal GpppC (By similarity).
Catalytic Activity: a 5'-end (5'-triphosphoguanosine)-(ribonucleoside) in mRNA + S-adenosyl-L-methionine = a 5'-end (N(7)-methyl 5'-tr... |
Q6Z9U7 | MNKRPRDEPSSSFASAPKRQYGAGGGGYGGHGYSEERSSARRVADHYSARSNQTLEERENSPIIHLKKLNNWIKSVLIQLYAHPGDCVLDLACGKGGDLIKWDKAKVGYYVGVDIAEGSIKDCMTRYNGDTDQQRRKKFSFPARLICADCYEARLDEHLYEDAPFDICSCQFALHYSWSTEARARQALANVSALLRPGGVFIGTMPDANVIIKRLRETDGMEFGNGVYWISFGEEYAEKKFPASRPFGIKYKFHLEDAVDCPEWVVPFHLFKLLAEEYDLELVLTKNFHEFVHEYLQKPEFAELMRRLGALGDGRQDQST... | Function: mRNA-capping methyltransferase that methylates the N7 position of the added guanosine to the 5'-cap structure of mRNAs. Binds RNA containing 5'-terminal GpppC (By similarity).
Catalytic Activity: a 5'-end (5'-triphosphoguanosine)-(ribonucleoside) in mRNA + S-adenosyl-L-methionine = a 5'-end (N(7)-methyl 5'-tr... |
Q5HZ60 | MSGFVVSKPEQSHHRLFDFAKTAIINIFAHPYATVCELYCGGAPETDKWEAAPIGHYIGIDTSSGISSVREAWESQRKNYDVEFFEADPSKDDFEIQLQKKLEQADLVSCWRHLQLCFETEESARRLLTNVACLLKPGGYFFGITPDSSTIWAKYQKNVEAYHNRSGAKPNVFPNYIRSESYMITFELEEEKFPLFGKRYQLKFSGDNASEDHCLVHFPSLIRLAREAGLEFVEIQSLTDFYDDNRAQFASLLMNAGPNFVDPRGKLLPRAFDLLGLYATFIFQKPDPDIEPPLTTPIPFESSNNHDERELPVITVITDA... | Function: mRNA capping methyltransferase that methylates the N7 position of the added guanosine to the 5'-cap structure of mRNAs. Binds RNA containing 5'-terminal GpppC (By similarity).
Catalytic Activity: a 5'-end (5'-triphosphoguanosine)-(ribonucleoside) in mRNA + S-adenosyl-L-methionine = a 5'-end (N(7)-methyl 5'-tr... |
Q6K833 | MAVTPHHRLYEFAKTALIKIFAFPYATVCDLYCDGGVDTDKWGDAQIGHYIGIDASASGVNDARELWESRKKLFTSEFIELDPSADDFEAQMQEKGIQADIVCCMQHLQLCFESEEHAQKLLNNVSSLLKPGGYFVGIIPDSSTIWTKYQKNVEASHNKGLKTVPNSIRSENYVITFEVEEEKFPFFGKKYQLKFANESMFENHCLVHFPSFMRLAREAGLEYVEIQNLTEFYDDNRTQFAPLLGGYGSSLVDPRGKLVARSFDILGLYSTFVFQKPDPDAMPPIVTPELHDPENDQEEEWLWTQQASMDDGRVSRTDIL... | Function: mRNA-capping methyltransferase that methylates the N7 position of the added guanosine to the 5'-cap structure of mRNAs. Binds RNA containing 5'-terminal GpppC (By similarity).
Catalytic Activity: a 5'-end (5'-triphosphoguanosine)-(ribonucleoside) in mRNA + S-adenosyl-L-methionine = a 5'-end (N(7)-methyl 5'-tr... |
A1CT57 | MENRSSSGTPRPSAGSPDAAKRPSETSPAAGRIPAGQNGSSGDKKRKVTEEGEASEKSEPPADRPMSKRKRMEERHQKLRKRGRTPPSAYSRRDAEAAPVPNRNRDDPANRSLSPLPHRSPTPEEQPRQRKRPGGGARMGLVDRETLRRRQEERERALVEEAMRTSQGRGVTDVVRQHYNAVPQRGREWRKTESKIKGLRSFNNWIKSTLIQKFSPDEEFLARLNDGRDWADDSGPPPAEEKRLLVVDLGCGKGGDLGKWQLAPQPVELYVGLDPAEVSIVQARERYNSMKSGRGNRGRRNPLFHGEFAPKDCFGEWLGD... | Function: Responsible for methylating the 5'-cap structure of mRNAs.
Catalytic Activity: a 5'-end (5'-triphosphoguanosine)-(ribonucleoside) in mRNA + S-adenosyl-L-methionine = a 5'-end (N(7)-methyl 5'-triphosphoguanosine)-ribonucleoside in mRNA + S-adenosyl-L-homocysteine
Sequence Mass (Da): 62163
Sequence Length: 551
... |
Q4WN42 | MYDPARDSWEERDGDEARSCRGRLASDQPHAVFSPPEQIHGASGENNNTTDLQQHPDPSSKTTASAEVLYAESQPAQPTTQTPPSVSTRIQSPVDPAAQKASNPQSLTSTAQNQLNKSNTTMENTSGSATPKPRADPSDKPNRPVQVASPTDQNGSQGDKKRKLPAEENASEKSQPAPDRPVSKRKRMEERHQKLRKRGRTPPSAYSRRDAEETSSAADRNGPTYRSTSPLPPPRSPTPEDQPRQRKRPGGGARMGLVDRETLRRRQEERERAQVEEAMRASQSRGVADVVRQHYNAVPQRGREWRKTESKIKGLRSFNN... | Function: Responsible for methylating the 5'-cap structure of mRNAs.
Catalytic Activity: a 5'-end (5'-triphosphoguanosine)-(ribonucleoside) in mRNA + S-adenosyl-L-methionine = a 5'-end (N(7)-methyl 5'-triphosphoguanosine)-ribonucleoside in mRNA + S-adenosyl-L-homocysteine
Sequence Mass (Da): 74939
Sequence Length: 668
... |
Q9RPW2 | SLSHGKYYALGSGPARAMATKVKDGAVEPVEELYKELEYRDSHDKTVLVIENDAVPPVEIVEKVAAACGVSPADLTIIVTPTSSLAGGVQVVGRVLEVAMHKAHALHFPLENIVDGTGSAPVCPPHPNFVKA | Function: Catalyzes the hydrolysis of methenyl-H(4)MPT(+) to 5-formyl-H(4)MPT.
Catalytic Activity: 5,10-methenyl-5,6,7,8-tetrahydromethanopterin + H2O = H(+) + N(5)-formyl-5,6,7,8-tetrahydromethanopterin
Sequence Mass (Da): 13863
Sequence Length: 132
Pathway: One-carbon metabolism; formaldehyde degradation; formate fro... |
P51616 | MVSVNIEAKKIVDRMIEGADDLKISVDKLENGSTVIDCGVNVDGSIKAGELYTAVCLGGLADVGISIPGDLSERFALPSVKIKTDFPAISTLGAQKAGWSVSVGDFFALGSGPARALALKPAETYEEIGYQDEADIAVLTLEADKLPGEDVTDKIAEECDVSPENVYVLVAPTSSLVGSIQISGRVVENGTYKMLEALHFDVNKVKYAAGIAPIAPVDPDSLKAMGKTNDAVLFGGRTYYYIESEEGDDIKSLAENLPSSASEGYGKPFYDVFKEADYDFYKIDKGMFAPAEVVINDLRTGEVFRAGFVNEELLMKSFGL | Function: Catalyzes the reversible interconversion of 5-formyl-H(4)MPT to methenyl-H(4)MPT(+).
Catalytic Activity: 5,10-methenyl-5,6,7,8-tetrahydromethanopterin + H2O = H(+) + N(5)-formyl-5,6,7,8-tetrahydromethanopterin
Sequence Mass (Da): 34230
Sequence Length: 320
Pathway: One-carbon metabolism; methanogenesis from C... |
Q9RPD4 | ICLGGLGKVTLAPAPGQTNWPFWLTVTSNDPVVACLASQYAGWSLSHEKFFALGSGPGRSLARKEPLFQELPYEDSASRATIVLEAGAPPPEPVVAKVAESCGVSPDKLAFIYAPTQSLAGSVQVVGRVLEVALHKAHELKFPLEHIVDGIATAPLSPPHPDFVTAMGRTNDAIIYSGRAHLFVRGSAEAAKALAEKLPSSNSRDYGRPFAEIFKAYKGEFYKIDPSLFSPAEAIVTAVETGETFRAGAIDEKLLDASFG | Function: Catalyzes the hydrolysis of methenyl-H(4)MPT(+) to 5-formyl-H(4)MPT.
Catalytic Activity: 5,10-methenyl-5,6,7,8-tetrahydromethanopterin + H2O = H(+) + N(5)-formyl-5,6,7,8-tetrahydromethanopterin
Sequence Mass (Da): 27622
Sequence Length: 260
Pathway: One-carbon metabolism; formaldehyde degradation; formate fro... |
P14200 | MAKMSLSSYMLMLAFSLFSHGILLSASKSIRNVEDDIVFNTFRMGKAFQKEDTAERSVVAPSLEGYKNDESGFMKDDDDKTTKNTGSKQNLVTHGLPLSLAVKPYLALKGPAVFPAENGVQNTESTQEKREIGDEENSAKFPIGRRDFDMLRCMLGRVYRPCWQV | Function: MCH inhibits ACTH secretion at the end of the light on period which corresponds to the peak of the circadian rhythm in ACTH. Inhibits also stress induced ACTH release during the light off period of the cycle. Involved as a neurotransmitter or neuromodulator in a broad array of neuronal functions. Stimulates s... |
Q7UPS1 | MKSATPDDLPRTGVEPDLSRSASECFESLWNGAIGMRSLPLTIAGARVLDAGVTCSGSLEAGLGLARLCLGDLANVRYVPATADDLVGLSVTIQTDHPVLSCLGGQYAGWPVSVADYFAMASGPMRCLRGKEAMLEQLHLSRQATDDDFAVGVLESDTLPGEDVIEAMADECGVDPSRLCLAVAPSTSIAGSAQVVSRSVETALHKLHALEFDVTRVVSAHGDAPLPPPAKKGDTIGGIGRTNDAMLYGARVTLWVDAEDDAIDSVASKVPSQSSDDHGRPFAEIFKQYEYDFYQVDPMLFSPAVVTIHSLQSGRTWRHG... | Function: Catalyzes the hydrolysis of methenyl-H(4)MPT(+) to 5-formyl-H(4)MPT.
Catalytic Activity: 5,10-methenyl-5,6,7,8-tetrahydromethanopterin + H2O = H(+) + N(5)-formyl-5,6,7,8-tetrahydromethanopterin
Sequence Mass (Da): 35408
Sequence Length: 333
Pathway: One-carbon metabolism; formaldehyde degradation; formate fro... |
Q9RQ01 | MTSQATSQATSPALTTPVDAAPQISLATCVAPLVEALIRDADALRLKVSRGPRDALIVDAGITAAGGLEAGRRIAEICLGGLGRVALVPTGRFSPWDTLASVSTSGPVLACLGSQYAGWSLAAGDFFALGSGPGRAIAAVETLYGELGYRDRGEKVVLVLETAVVPPAEVVDEIAARCAVAPSDITLILTPTSSLAGTVQIVARVLEVALHKAHALHFPLEHIADGVGSAPICPPSPDFLTAMGRTNDAVLYGGDVHLFVHGPAEAAKDLATRLPSLASRDYGRPFGEIFAGYDCDFYKVDPLLFSPARVTVTAIDHGES... | Function: Catalyzes the hydrolysis of methenyl-H(4)MPT(+) to 5-formyl-H(4)MPT.
Catalytic Activity: 5,10-methenyl-5,6,7,8-tetrahydromethanopterin + H2O = H(+) + N(5)-formyl-5,6,7,8-tetrahydromethanopterin
Sequence Mass (Da): 34783
Sequence Length: 337
Pathway: One-carbon metabolism; formaldehyde degradation; formate fro... |
P29458 | MSSSQQSGRANELRTPGRANSSSREAVDSSPLFFPASSPGSTRLTTPRTTARTPLASSPLLFESSSPGPNIPQSSRSHLLSQRNDLFLDSSSQRTPRSTRRGDIHSSVQMSTPSRRREVDPQRPGVSTPSSLLFSGSDALTFSQAHPSSEVADDTVRVIWGTNVSIQESIASFRGFLRGFKKKYRPEYRNELMPPPDAEQLVYIEALRNMRIMGLEILNLDVQDLKHYPPTKKLYHQLYSYPQEIIPIMDQTIKDVMLDLLGTNPPEDVLNDIELKIYKIRPFNLEKCINMRDLNPGDIDKLISIKGLVLRCTPVIPDMK... | Function: Acts as component of the mcm2-7 complex (mcm complex) which is the putative replicative helicase essential for 'once per cell cycle' DNA replication initiation and elongation in eukaryotic cells. The active ATPase sites in the mcm2-7 ring are formed through the interaction surfaces of two neighboring subunits... |
P30665 | MSQQSSSPTKEDNNSSSPVVPNPDSVPPQLSSPALFYSSSSSQGDIYGRNNSQNLSQGEGNIRAAIGSSPLNFPSSSQRQNSDVFQSQGRQGRIRSSASASGRSRYHSDLRSDRALPTSSSSLGRNGQNRVHMRRNDIHTSDLSSPRRIVDFDTRSGVNTLDTSSSSAPPSEASEPLRIIWGTNVSIQECTTNFRNFLMSFKYKFRKILDEREEFINNTTDEELYYIKQLNEMRELGTSNLNLDARNLLAYKQTEDLYHQLLNYPQEVISIMDQTIKDCMVSLIVDNNLDYDLDEIETKFYKVRPYNVGSCKGMRELNPN... | Function: Acts as component of the MCM2-7 complex (MCM complex) which is the putative replicative helicase essential for 'once per cell cycle' DNA replication initiation and elongation in eukaryotic cells. The active ATPase sites in the MCM2-7 ring are formed through the interaction surfaces of two neighboring subunits... |
P55862 | MSGFDDLGVYYSDSFGGEQQVGDDGQAKKSQLKKRFREFLRQYRIGTDRTGFTFKYRDELKRHYNLGEYWIEVEMEDLASFDEDLADYLYKQPTEHLQLLEEAAQEVADEVTRPRPAGEETIQEIQVMLRSDANPANIRSLKSEQMSHLVKIPGIIIAATAVRAKATKISIQCRSCRNTIGNIAVRPGLEGYAMPRKCNTEQAGRPNCPLDPYFIIPDKCKCVDFQTLKLQESPDAVPHGELPRHMQLYCDRYLCDKVVPGNRVTIMGIYSIRKSGKTSTKGRDRVGVGIRSSYIRVVGIQVDTEGTGRSAAGAITPQEE... | Function: Acts as component of the MCM2-7 complex (MCM complex) which is the replicative helicase essential for 'once per cell cycle' DNA replication initiation and elongation in eukaryotic cells. Core component of CDC45-MCM-GINS (CMG) helicase, the molecular machine that unwinds template DNA during replication, and ar... |
O80786 | MSGWDEGAVYYSDQPQFPEAGDAATISPHAVLTKFKEFIRNFEIEQNCFPYREALLDNPKRLVVHLEDLLSFDSDLPSLIRSAPADYLPVFEKAAGEVLTGLKMREANEGGVMEEPLTRDVQILLTSREDPVSMRLLGAQYISKLVKISGISIAASRVKAKATYVFLVCKNCKKTREVPCRPGLGGAIVPRSCDNIPQPGEEPCPLDPWMVVPDRSQYVDQQTLKLQENPEDVPTGELPRNMLLSVDRHLVQTIVPGTRLTVMGIYSIFQASSSSNSHKGAVAIRQPYIRVVGLEDTNEASSRGPANFTPDEEEEFKKFA... | Function: Probable component of the MCM2-7 complex (MCM complex) that may function as a DNA helicase and which is essential to undergo a single round of replication initiation and elongation per cell cycle in eukaryotic cells.
Catalytic Activity: ATP + H2O = ADP + H(+) + phosphate
Sequence Mass (Da): 81015
Sequence Len... |
Q0V8B7 | MSGFDDPGIFYSDSFGGDNAADEGQARKSQLQRRFKEFLRQYRVGTDRTGFTFKYRDELKRHYNLGEYWIEVEMEDLASFDEELADYLYKQPAEHLQLLEEAAKEVADEVTRPRPAGDEVLQDIQVMLKSDASPSSIRSLKSDTMSHLVKIPGIVIAASGVRAKATRISIQCRSCHSTLTNIAMRPGLDGYALPRKCNTDQAGRPKCPLDPYFIMPDKCKCVDFQTLKLQELPDAVPHGEMPRHMQLYCDRYLCDKVVPGNRVTIMGIYSIKKFGLTSNRGRDRVGVGIRSAYIRVLGIQVDTDGSGRTFAGAMTPQEEE... | Function: Acts as component of the MCM2-7 complex (MCM complex) which is the replicative helicase essential for 'once per cell cycle' DNA replication initiation and elongation in eukaryotic cells. Core component of CDC45-MCM-GINS (CMG) helicase, the molecular machine that unwinds template DNA during replication, and ar... |
Q21902 | MSNLDNPGIYYQERFFANDGVPDTGRELIAEYRQLITQFRNFIRDFSTGGFGMIYRDQLKRNYFSHEYRLEINLNHLKNFDEDIEMKLRKFPGKVLPALEEAAKIVADEITTPRPKGEEKLHDIQVTLTLDEYPTSLRQVKSAQVSQVVKISGIIVAAAQVRSKATKVTLQCRQCKHTIPDVSIKPGLEGFALPRTCAAPQQGQMQRCPIDPYIMLPDKCECVDYQTLKLQENPEDVPHGEMPRHLQLFTERYLTDKVVPGNRVTIVGVYSIKKLIQKKGGDKSLQGIRTPYLRVLGIHMETSGPGRTNFTTFTPEEERM... | Function: Acts as component of the MCM2-7 complex (MCM complex) which is the replicative helicase essential for 'once per cell cycle' DNA replication initiation and elongation in eukaryotic cells. Core component of CDC45-MCM-GINS (CMG) helicase, the molecular machine that unwinds template DNA during replication, and ar... |
Q54CP4 | MSGFDEGNVTVSGGGGKGGFKKNNGFVEDTSVRDLFKRFINEWKDQDNVFIYKEQLRQHYNLGWHYIEVSIDHLTDFNQELSGRFISSPNELMPSFEDAIKDIIKEMNYNKEQVDEDIQILFKSSANPEPIRYLRAGLISKLVKVQGIVISASRTQPKPSTMVVKCKNCQHTQTLHIRPGIVSSVLPQQCERGSNDAGKPCPNNPYVVLSDQSTFVNQQILKLQESPETIPTGEMPRHIILSLDKSLADKITPGTRIKVLGVLGIFEGGGKRREIAGGTIRTNYLRVLGITSDNAGRDSMHFTPSEEQSFKVFSRRQDLR... | Function: Acts as component of the MCM2-7 complex (MCM complex) which is the replicative helicase essential for 'once per cell cycle' DNA replication initiation and elongation in eukaryotic cells. Core component of CDC45-MCM-GINS (CMG) helicase, the molecular machine that unwinds template DNA during replication, and ar... |
P33992 | MSGFDDPGIFYSDSFGGDAQADEGQARKSQLQRRFKEFLRQYRVGTDRTGFTFKYRDELKRHYNLGEYWIEVEMEDLASFDEDLADYLYKQPAEHLQLLEEAAKEVADEVTRPRPSGEEVLQDIQVMLKSDASPSSIRSLKSDMMSHLVKIPGIIIAASAVRAKATRISIQCRSCRNTLTNIAMRPGLEGYALPRKCNTDQAGRPKCPLDPYFIMPDKCKCVDFQTLKLQELPDAVPHGEMPRHMQLYCDRYLCDKVVPGNRVTIMGIYSIKKFGLTTSRGRDRVGVGIRSSYIRVLGIQVDTDGSGRSFAGAVSPQEEE... | Function: Acts as component of the MCM2-7 complex (MCM complex) which is the replicative helicase essential for 'once per cell cycle' DNA replication initiation and elongation in eukaryotic cells. Core component of CDC45-MCM-GINS (CMG) helicase, the molecular machine that unwinds template DNA during replication, and ar... |
P49718 | MSGFDDPGIFYSDSFGGDPGAEEGQARKSQLQRRFKEFLRQYRVGTDRTGFTFKYRDELKRHYNLGEYWIEVEMEDLASFDEELADHLHKQPAEHLQLLEEAAKEVADEVTRPRPAGDELLQDIQVMLKSDASPSSIRILKSDMMSHLVKIPGIIISASAVRAKATRISIQCRSCHNTLTNIAMRPGLEGYALPRKCNMDQAGRPKCPLDPYFIMPDKCKCVDFQTLKLQELPDAVPHGEMPRHMQLYCDRYLCDKVVPGNRVTIMGIYSIKKFGLNPSKGRDRVGVGIRSSYIRVLGIQVDTDGSGRSFAGSVSPQEEE... | Function: Acts as component of the MCM2-7 complex (MCM complex) which is the replicative helicase essential for 'once per cell cycle' DNA replication initiation and elongation in eukaryotic cells. Core component of CDC45-MCM-GINS (CMG) helicase, the molecular machine that unwinds template DNA during replication, and ar... |
Q6KAJ4 | MSGWDEGAVFYSDQAQFPRGGPGGDPSADLTRHSALRKFKEFLRGFTGPTGDFPYRESLVHNRDHVTVAIEDLDAFDAELSDKIRKSPADYLPLFETAASEVLASLRSKVAGETGEMEEPATGDVQIFLSSKENCLSMRSIGADYMSKLVKIAGITIAASRVKAKATHVTLLCKNCRSVKTVPCRPGLGGAIVPRSCDHVPQPGEEPCPLDPWIAVPDKSKYVDLQTLKLQENPEDVPTGELPRNMLLSVDRHLVQTIVPGTRLTVIGIYSVYQASANQKGAVGVKQPYIRVVGLEQSRDANSNGPSNFTLDEEMEFKEF... | Function: Probable component of the MCM2-7 complex (MCM complex) that may function as a DNA helicase and which is essential to undergo a single round of replication initiation and elongation per cell cycle in eukaryotic cells.
Catalytic Activity: ATP + H2O = ADP + H(+) + phosphate
Sequence Mass (Da): 80376
Sequence Len... |
P41389 | MAAATGWERSAVYYTPVLPGEQELDSNVSHEKNFIQFIEEFVIDNDFIYRTQLRDNLVVKQYMLNIDLRHLISYNEDLAHLLLSQPTDILPLFESAVTTVAKRLLYRSQENASTNIPTCQVTLRYDANILPIRNLTASHISKLVRVPGIIIGASTLSCRATALHLVCRNCRATRILQISGGFSGVQLPRVCEAPVLDGEKKDCPMDPFIIDHSKSTFIDQQVLKLQEAPDMVPVGELPRHILLNADRYLTNQITPGTRCVITGIFSIFQNKSVKASGAVAIRNPYIRVVGIQMDSNDGSKSTPLFSEEEEEEFLEISRTP... | Function: Acts as component of the mcm2-7 complex (mcm complex) which is the putative replicative helicase essential for 'once per cell cycle' DNA replication initiation and elongation in eukaryotic cells. The active ATPase sites in the mcm2-7 ring are formed through the interaction surfaces of two neighboring subunits... |
P29496 | MSFDRPEIYSAPVLQGESPNDDDNTEIIKSFKNFILEFRLDSQFIYRDQLRNNILVKNYSLTVNMEHLIGYNEDIYKKLSDEPSDIIPLFETAITQVAKRISILSRAQSANNNDKDPENTSMDTDSLLLNSLPTFQLILNSNANQIPLRDLDSEHVSKIVRLSGIIISTSVLSSRATYLSIMCRNCRHTTSITINNFNSITGNTVSLPRSCLSTIESESSMANESNIGDESTKKNCGPDPYIIIHESSKFIDQQFLKLQEIPELVPVGEMPRNLTMTCDRYLTNKVIPGTRVTIVGIYSIYNSKNGAGSGRSGGGNGGSG... | Function: Acts as component of the MCM2-7 complex (MCM complex) which is the putative replicative helicase essential for 'once per cell cycle' DNA replication initiation and elongation in eukaryotic cells. The active ATPase sites in the MCM2-7 ring are formed through the interaction surfaces of two neighboring subunits... |
Q5FWY4 | MELGGPAAAGDTDIAGQQLFKDELSDKCQKLFLEFLEECKGKDGSNLYVSAAEELIRPERNTLAVNFTDIEYYNQQLATTIQEEYYRVYPHLCRAVRSFARQMGNIPANKEFYIAFSDFPARQKIRELSSAKIGTLLRISGQVVRTHPVHPELVSGTFLCMDCQSIVKDVEQQFRYTQPTICKNPVCANRRRFTLDTNKSRFVDFQKVRIQETQAELPRGAIPRSVEIILRAEAVESAMAGDRCDFTGTLIVVPDVSALAAGDARMETGAKVTGGEGFNSEGVQGLKALGVRDLSYRLAFLACYVGATNPRFGGKDLREE... | Function: Acts as component of the mcm2-7 complex (mcm complex) which is the putative replicative helicase essential for 'once per cell cycle' DNA replication initiation and elongation in eukaryotic cells. The active ATPase sites in the mcm2-7 ring are formed through the interaction surfaces of two neighboring subunits... |
P15529 | MEPPGRRECPFPSWRFPGLLLAAMVLLLYSFSDACEEPPTFEAMELIGKPKPYYEIGERVDYKCKKGYFYIPPLATHTICDRNHTWLPVSDDACYRETCPYIRDPLNGQAVPANGTYEFGYQMHFICNEGYYLIGEEILYCELKGSVAIWSGKPPICEKVLCTPPPKIKNGKHTFSEVEVFEYLDAVTYSCDPAPGPDPFSLIGESTIYCGDNSVWSRAAPECKVVKCRFPVVENGKQISGFGKKFYYKATVMFECDKGFYLDGSDTIVCDSNSTWDPPVPKCLKVLPPSSTKPPALSHSVSTSSTTKSPASSASGPRPT... | Function: Acts as a cofactor for complement factor I, a serine protease which protects autologous cells against complement-mediated injury by cleaving C3b and C4b deposited on host tissue. May be involved in the fusion of the spermatozoa with the oocyte during fertilization. Also acts as a costimulatory factor for T-ce... |
O88174 | MTAAPLMPDSTHPCRRRKSYTFFWCSLGVYAEALLFLLSHLSDACELPRPFEAMELKGTPKLFYAVGEKIEYKCKKGYLYLSPYLMIATCEPNHTWVPISDAGCIKVQCTMLQDPSFGKVYYIDGSFSWGARAKFTCMEGYYVVGMSVLHCVLKGDDEAYWNGYPPHCEKIYCLPPPKIKNGTHTLTDINVFKYHEAVSYSCDPTPGPDKFSLVGTSMIFCAGHNTWSNSPPECKVVKCPNPVLQNGRLISGAGEIFSYQSTVMFECLQGFYMEGSSMVICSANNSWEPSIPKCLKGPRPTHPTKPPVYNYTGYPSPREG... | Function: May be involved in the fusion of the spermatozoa with the oocyte during fertilization.
PTM: May be O-glycosylated.
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 40881
Sequence Length: 365
Subcellular Location: Cytoplasmic vesicle
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O02839 | MMAFCALRKALPCRPENPFSSRCFVEILWVSLALVFLLPMPSDACDEPPKFESMRPQFLNTTYRPGDRVEYECRPGFQPMVPALPTFSVCQDDNTWSPLQEACRRKACSNLPDPLNGQVSYPNGDMLFGSKAQFTCNTGFYIIGAETVYCQVSGNVMAWSEPSPLCEKILCKPPGEIPNGKYTNSHKDVFEYNEVVTYSCLSSTGPDEFSLVGESSLFCIGKDEWSSDPPECKVVKCPYPVVPNGEIVSGFGSKFYYKAEVVFKCNAGFTLHGRDTIVCGANSTWEPEMPQCIKDSKPTDPPATPGPSHPGPPSPSDASP... | Function: Acts as a cofactor for complement factor I, a serine protease which protects autologous cells against complement-mediated injury by cleaving C3b and C4b deposited on host tissue. May be involved in the fusion of the spermatozoa with the oocyte during fertilization. May act as a costimulatory factor for T-cell... |
Q96AQ8 | MDCGSVGGQRTQRLPGRQRLLFLPVGLSGRPGGSETSARRCLSALSDGLGALRPRAPAARGGVSRASPLLLLLLVPSPRLAAAAPRRQLGDWERSRLGYAAPPAGRSSAWRCSPGVAAAAGALPQYHGPAPALVSCRRELSLSAGSLQLERKRRDFTSSGSRKLYFDTHALVCLLEDNGFATQQAEIIVSALVKILEANMDIVYKDMVTKMQQEITFQQVMSQIANVKKDMIILEKSEFSALRAENEKIKLELHQLKQQVMDEVIKVRTDTKLDFNLEKSRVKELYSLNEKKLLELRTEIVALHAQQDRALTQTDRKIET... | Function: Key regulator of mitochondrial calcium uniporter (MCU) required for calcium entry into mitochondrion . Plays a direct role in uniporter-mediated calcium uptake via a direct interaction with MCU . Probably involved in the assembly of the membrane components of the uniporter complex (uniplex) .
Location Topolog... |
Q9CXD6 | MDSGSVAAERPRRTPSRQRLPSSGCGVPARPGVSTLPGGRSWLRPRGRAARASPLLFLLLVPSPRLAATATATAPRRTLAERSRPGLVLPAAALGAGRNALGRLRLGARRVAALASSRRELSLSAKCHQLEHRKENLPLSVSRQLYFDTHALVCLLEANGFTIQQAEIIVSALVKITETNMNIIYKDMVSKMQQEIALQQVLSKIANVKKDMVILEKSEFSALRAENEKIKLELHQLKQQVMDEVTKVRTDTKLNFNLEKSRVKELYSLNEKKMLELRTEIVSLHAQQDRALTQTDRKIETEVAGLKTMLEAHKLDTIKY... | Function: Key regulator of mitochondrial calcium uniporter (MCU) required for calcium entry into mitochondrion. Plays a direct role in uniporter-mediated calcium uptake via a direct interaction with MCU. Probably involved in the assembly of the membrane components of the uniporter complex (uniplex).
Location Topology: ... |
Q0P4J6 | MSRLQLRFLLRRALSGSGCPRYSMPGSGCPGCFLPRVTCFRDFNIITSTMQYNLDKRNIYTSVGKHYFFDTHAVVQLLEANGFSAEQSEIVVSALVKILNVNMNLIHKDMVTKEQQEISLQQVMSLIASVKKDMIILEKSEFSALRTQNEKVKIELQQLKKQLNDSIVKVRASNKLDFNLEKSRVKEMHADNERKLLELRTSIVELHSQQDRGLTQTKRKIDTEVSGVKTMQESHKLDTIKYLAGSVFTCLTIALGFYRLWI | Function: Key regulator of mitochondrial calcium uniporter (mcu) required for calcium entry into mitochondrion.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 30024
Sequence Length: 262
Subcellular Location: Mitochondrion inner membrane
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Q21121 | MRNGRCLVTPFVTAQRLANLRNTLWNRQQIAFSTTTASSSTSPIQESSSPLSIRFEYGLPLLDVPLPSRNEPCQFTMRPLSDTIGSLCEFLRQEDRGIDYVAVYGTNGVKLATCTSIEHLLQFGSFRLRLNDKFFDVTVPKTGTMPYDSDKLRQLDDLRATVASLHAALCVDEYKLSREKKLLLQLENAETLLAPLHDAKRKIEQECEAHTDRVMWAGFAAMGVQTGLFARLTWWEYSWDIMEPVTYFATYSTVCATFGYYLYTQQSFEYPSARERVYTKQFYRRAQKQNFDIEKYNRLVTEVDELRNQLKRMRDPLFQH... | Function: Mitochondrial inner membrane calcium uniporter that mediates calcium uptake into mitochondria . Constitutes a pore-forming and calcium-conducting subunit (By similarity). Mitochondrial calcium homeostasis plays key roles in cellular physiology and regulates cell bioenergetics, cytoplasmic calcium signals and ... |
Q08BI9 | MAAKVCRSVLLLSRSSGAVASSAYPAFGVSSQRHQGTKTEALSMSLGGHQTVRRAHGLRTGGRCALFCHPSATLTAQGWKGSPSWQVQRLLCSPAAEDVSVVYQNGLPVISVRLPSRRERCQFTLKPLSDTVGVFLQQLQAEDRGIDRVTIYSADGARIASSTGIDILLMDNFKLVINDTSYLVQPPRRDLLPHEDGERLNDVKILVQQLYTTLRIEEHQLNKERELIGRLEDLNSQLQPLEKVKEELSKKAERRTTWVLWGGMAYMATQFGILARLTWWEYSWDIMEPVTYFITYGTAMAMYAYFVLTRQEYLYPDARD... | Function: Mitochondrial inner membrane calcium uniporter that mediates calcium uptake into mitochondria. Constitutes the pore-forming and calcium-conducting subunit of the uniporter complex (uniplex). Activity is regulated by micu1 and micu2. At low Ca(2+) levels mcu activity is down-regulated by micu1 and micu2; at hi... |
Q54LT0 | MNSFVIRNGFGLVRTFNTRLFTTSTQNLEGELKTILGQAKVSKLQEKLKLDPRSKITFNDFKGIAKEVGIEEKEINSVSNALAQSGSIIYLPNSLNENLKTSVFTKPAHIYQSLEHILDIENKGVGLNKLIESKKSEINSLRQKIQPLEEKKQVIDRKAHRRATAIIWTGLGYCFAQAAILARLTWWDLSWDIIEPVSYFLTFGSVLIGYTYFTMTKTEFTYEALNHRLFSKRQDKLFKRNNFPKEDYENLVQAIDKKEKELKELELATKYDHTH | Function: Mitochondrial inner membrane calcium uniporter that mediates calcium uptake into mitochondria . Constitutes a pore-forming and calcium-conducting subunit . Mitochondrial calcium homeostasis plays key roles in cellular physiology and regulates cell bioenergetics, cytoplasmic calcium signals and activation of c... |
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