ids stringlengths 6 10 | seqs stringlengths 11 1.02k | texts stringlengths 108 11.1k |
|---|---|---|
Q72U10 | MGLFESNLPKHIAVIMDGNGRWATSRGKSRSEGHREGAQAIDRLMDASLELGLKNISLYAFSTENWKRPVTEIRSIFSLLIEFIETRLDTIHKRGIRILHSGSRKKLTRGVLDKIDFAVDKTQKNKNLTVNFCLNYGSRDELLRAAQELFLERKRSKVALEKPLKEKEFEKFLYTSILPPVDLLIRTAGEQRLSNFLLWQSAYAELYFTDTLWPEFDKNSLVDSLKWYETRTRKFGGLTNG | Cofactor: Binds 2 magnesium ions per subunit.
Function: Catalyzes the condensation of isopentenyl diphosphate (IPP) with allylic pyrophosphates generating different type of terpenoids.
Sequence Mass (Da): 27862
Sequence Length: 241
EC: 2.5.1.-
|
P53712 | MNLQLIFWIGLISSVCCVFGQADENRCLKANAKSCGECIQAGPNCGWCTNSTFLQEGMPTSARCDDLEALKKKGCHPNDIENPRGSKDIKKNKNVTNRSKGTAEKLQPEDITQIQPQQLVLQLRSGEPQTFTLKFKRAEDYPIDLYYLMDLSYSMKDDLENVKSLGTDLMNEMRRITSDFRIGFGSFVEKTVMPYISTTPAKLRNPCTNEQNCTSPFSYKNVLSLTDKGEVFNELVGKQRISGNLDSPEGGFDAIMQVAVCGSLIGWRNVTRLLVFSTDAGFHFAGDGKLGGIVLPNDGQCHLENDVYTMSHYYDYPSIA... | Function: Integrins alpha-1/beta-1, alpha-2/beta-1, alpha-10/beta-1 and alpha-11/beta-1 are receptors for collagen. Integrins alpha-1/beta-1 and alpha-2/beta-2 recognize the proline-hydroxylated sequence G-F-P-G-E-R in collagen. Integrins alpha-2/beta-1, alpha-3/beta-1, alpha-4/beta-1, alpha-5/beta-1, alpha-8/beta-1, a... |
P07228 | MAETNLTLLTWAGILCCLIWSGSAQQGGSDCIKANAKSCGECIQAGPNCGWCKKTDFLQEGEPTSARCDDLAALKSKGCPEQDIENPRGSKRVLEDREVTNRKIGAAEKLKPEAITQIQPQKLVLQLRVGEPQTFSLKFKRAEDYPIDLYYLMDLSYSMKDDLENVKSLGTALMREMEKITSDFRIGFGSFVEKTVMPYISTTPAKLRNPCTGDQNCTSPFSYKNVLSLTSEGNKFNELVGKQHISGNLDSPEGGFDAIMQVAVCGDQIGWRNVTRLLVFSTDAGFHFAGDGKLGGIVLPNDGKCHLENNMYTMSHYYDY... | Function: Integrins alpha-1/beta-1, alpha-2/beta-1, alpha-10/beta-1 and alpha-11/beta-1 are receptors for collagen. Integrins alpha-1/beta-1 and alpha-2/beta-1 recognize the proline-hydroxylated sequence G-F-P-G-E-R in collagen. Integrins alpha-2/beta-1, alpha-3/beta-1, alpha-4/beta-1, alpha-5/beta-1, alpha-8/beta-1, a... |
P05556 | MNLQPIFWIGLISSVCCVFAQTDENRCLKANAKSCGECIQAGPNCGWCTNSTFLQEGMPTSARCDDLEALKKKGCPPDDIENPRGSKDIKKNKNVTNRSKGTAEKLKPEDITQIQPQQLVLRLRSGEPQTFTLKFKRAEDYPIDLYYLMDLSYSMKDDLENVKSLGTDLMNEMRRITSDFRIGFGSFVEKTVMPYISTTPAKLRNPCTSEQNCTSPFSYKNVLSLTNKGEVFNELVGKQRISGNLDSPEGGFDAIMQVAVCGSLIGWRNVTRLLVFSTDAGFHFAGDGKLGGIVLPNDGQCHLENNMYTMSHYYDYPSIA... | Function: Integrins alpha-1/beta-1, alpha-2/beta-1, alpha-10/beta-1 and alpha-11/beta-1 are receptors for collagen. Integrins alpha-1/beta-1 and alpha-2/beta-2 recognize the proline-hydroxylated sequence G-F-P-G-E-R in collagen. Integrins alpha-2/beta-1, alpha-3/beta-1, alpha-4/beta-1, alpha-5/beta-1, alpha-8/beta-1, a... |
P32592 | MLRQRPQLLLLAGLLALQSVLSQECTNYKVSTCRDCIESGPGCAWCQKLNFTGQGEPDSIRCDTRAELLSKGCPADDIMEPKSLAETRDSQAGSRKQLSPQEVTLYLRPGQAVAFNVTFRRAKGYPIDLYYLMDLSYSMVDDLVNVKKLGGDLLRALNGITESGRIGFGSFVDKTVLPFVNTHPEKLRNPCPNKEKECQPPFAFRHVLKLTDNSKQFETEVGKQLISGNLDAPEGGLDAMMQVAACPEEIGWRNVTRLLVFATDDGFHFAGDGKLGAILTPNDGRCHLEDNLYKSSNEFDYPSVGQLAHKLAESNIQPIF... | Function: Integrin ITGAL/ITGB2 is a receptor for ICAM1, ICAM2, ICAM3 and ICAM4. Integrin ITGAL/ITGB2 is also a receptor for the secreted form of ubiquitin-like protein ISG15; the interaction is mediated by ITGAL. Integrins ITGAM/ITGB2 and ITGAX/ITGB2 are receptors for the iC3b fragment of the third complement component... |
P05107 | MLGLRPPLLALVGLLSLGCVLSQECTKFKVSSCRECIESGPGCTWCQKLNFTGPGDPDSIRCDTRPQLLMRGCAADDIMDPTSLAETQEDHNGGQKQLSPQKVTLYLRPGQAAAFNVTFRRAKGYPIDLYYLMDLSYSMLDDLRNVKKLGGDLLRALNEITESGRIGFGSFVDKTVLPFVNTHPDKLRNPCPNKEKECQPPFAFRHVLKLTNNSNQFQTEVGKQLISGNLDAPEGGLDAMMQVAACPEEIGWRNVTRLLVFATDDGFHFAGDGKLGAILTPNDGRCHLEDNLYKRSNEFDYPSVGQLAHKLAENNIQPIF... | Function: Integrin ITGAL/ITGB2 is a receptor for ICAM1, ICAM2, ICAM3 and ICAM4. Integrin ITGAL/ITGB2 is also a receptor for the secreted form of ubiquitin-like protein ISG15; the interaction is mediated by ITGAL . Integrins ITGAM/ITGB2 and ITGAX/ITGB2 are receptors for the iC3b fragment of the third complement componen... |
Q940Q8 | MKLSSCVLIFLLCNTFSSISAFRLSRSQPTERISGSAGDVLEDDPVGRLKVFVYELPSKYNKKILQKDPRCLNHMFAAEIYMQRFLLSSPVRTLNPEEADWFYVPVYTTCDLTPNGLPLPFKSPRMMRSAIQLIASNWPYWNRTEGADHFFVVPHDFGACFHYQEEKAIGRGILPLLQRATLVQTFGQRNHVCLKEGSITVPPYAPPQKMQSHLIPEKTPRSIFVYFRGLFYDVGNDPEGGYYARGARAAVWENFKDNPLFDISTEHPTTYYEDMQRAIFCLCPLGWAPWSPRLVEAVIFGCIPVIIADDIVLPFADAIP... | Function: Involved in the synthesis of the hemicellulose glucuronoxylan, a major component of secondary cell walls. Probably involved in the elongation of glucuronoxylan xylosyl backbone.
Location Topology: Single-pass type II membrane protein
Sequence Mass (Da): 47195
Sequence Length: 415
Subcellular Location: Golgi a... |
Q4PMW1 | MNAALIAALLILGALTLDATAYSSTCERIPCTNNSDCHGPDLCQCRPPRGDDFGYFCSEY | Function: Tick salivary platelet aggregation inhibitor that plays an important part in the anti-hemostatic strategy of ticks (Probable). Inhibits platelet aggregation induced by ADP, thrombin and thromboxane A2 (TXA2) . Blocks platelet adhesion to soluble collagen (most probably through the binding to alpha-2/beta-1 in... |
B7Q052 | MNAVFIAALLILGTSTFDAMRLWNYCTHILCTNDSDCGQSDSCRCRPPRGDDYRYHCSRY | Function: Tick salivary platelet aggregation inhibitor that plays an important part in the anti-hemostatic strategy of ticks. Inhibits platelet aggregation induced by ADP, thrombin and thromboxane A2 (TXA2). Blocks platelet adhesion to soluble collagen (most probably through the binding to alpha-2/beta-1 integrin (ITGA... |
P0CI72 | MTTYDTQPSTLIRNAAAIMTGGRGTADDPSRVPGPDIRIVGDTIDAIGALAPRPGETIVDATDCVIYPAWVNTHHHLFQSLLKGEPAGLDATLTPWLAATPYRFRALFDERRFRLAARIGLIELARSGCATVADHNYVYYPGMPFDSSAILFEEAEKLGLRFVLLRGGATQTRQLEADLPTALRPETLDAYVADIERLAARYHDASPRAMRRVVMAPTTVLYSISPREMRETAAVARRLGLRMHSHLSETVGYQDSAYSMYGKSPVAFCGEHDWLGSDVWYAHLVKVDADEIALLAQTGTGVAHCPQSNGRLGSGICPVR... | Cofactor: Binds 1 zinc ion per subunit.
Catalytic Activity: a 2-amino-4-hydroxypteridine + H(+) + H2O = a 2,4-dihydroxypteridine + NH4(+)
Sequence Mass (Da): 51752
Sequence Length: 482
EC: 3.5.4.11
|
A9NGK2 | MDIIFASNNYHKFIEMESILKPHQITLLKDFQIDEKEIIESGLTFEANAQIKARAFAKRFNQVAIADDSGIIIEAISPLPGIYSKRYSGLGDTVNNIKVLDVLKNKENRQARFVCAIAIAFPDGKIFTYVGNMLGNIALNLKGSMGFGYDPIFIPDGKQETLGELGSTYKDEHSHRRHALNNFLEAKDEIIDYWRYTWKK | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Pyrophosphatase that catalyzes the hydrolysis of nucleoside triphosphates to their monophosphate derivatives, with a high preference for the non-canonical purine nucleotides XTP (xanthosine triphosphate), dITP (deoxyinosine triphosphate) and ITP. Seems to function as ... |
Q6FEQ6 | MSAPHWLSQGTLVLASNNKGKITEFEKLFAELQLPVDVIPQGQLNIPDAIEDGLSFVENAIIKARHASKISGKPAIADDSGICVPVLGGAPGIYSARYAGDHGNDAANNEKLLHDLKPFRNAEQAIQGMFVCVLALVEHAEDPLPQIFQGFWHGEILEQARGEHGFGYDPLFWLSELKMSSAEMSKEEKNKISHRGQAMQRFRESLMTRE | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Pyrophosphatase that catalyzes the hydrolysis of nucleoside triphosphates to their monophosphate derivatives, with a high preference for the non-canonical purine nucleotides XTP (xanthosine triphosphate), dITP (deoxyinosine triphosphate) and ITP. Seems to function as ... |
Q6AEL0 | MVRVVLATHNRNKALEFQQILGDAVPGLQIVGYDGPEPVEDGITFEQNALIKARAAAERTGMIALADDSGICVDAMGGAPGIFSARWAGRHGDAQANLRLLLDQLADLPDSSRAAHFTATLALVTPEGETTVVEGVWPGRIAREARGGHGHGYDPIFLPDGHDVTAAELGPEAKNAESHRARAFAAIVPVLRALSRPGN | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Pyrophosphatase that catalyzes the hydrolysis of nucleoside triphosphates to their monophosphate derivatives, with a high preference for the non-canonical purine nucleotides XTP (xanthosine triphosphate), dITP (deoxyinosine triphosphate) and ITP. Seems to function as ... |
Q72UV8 | MKRQLALGTNNLNKVKEVSSILMELGIQILTPKDLKVSFNPEETGSTFKENALIKAKELFYLTKIPSIADDSGICVSALKDEPGVYSARFGGPELNDEGRALLLLEKLKGNQNRKAYYACAIAYVDESTEQSFEGRCEGLISEEYDRIGIYGFGYDPIFIFPPLQKPFSQIQEETKNSVSHRKKALDELLKFLKTKP | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Pyrophosphatase that catalyzes the hydrolysis of nucleoside triphosphates to their monophosphate derivatives, with a high preference for the non-canonical purine nucleotides XTP (xanthosine triphosphate), dITP (deoxyinosine triphosphate) and ITP. Seems to function as ... |
Q03YJ8 | MKLIIASNNAHKITEIEALLASISIDLPVVSLQEIGDVPEIVEDGTTFEENAVKKVETIAKVAPNDYILADDSGMSVDALNGEPGVYSARYAGDHDDQANIDKVLQKLAKVPNEQRTAHFNSVIALHSPKGSNLIVNGQVDGYITESERGQDGFGYDPIFFVPSMNKTFAEMSASEKNTISHRGLALQELGKKLPVWLKGE | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Pyrophosphatase that catalyzes the hydrolysis of nucleoside triphosphates to their monophosphate derivatives, with a high preference for the non-canonical purine nucleotides XTP (xanthosine triphosphate), dITP (deoxyinosine triphosphate) and ITP. Seems to function as ... |
Q8Y7N5 | MSKIIIATANKGKAKEFEKIFAKFNIEVATLADFPEIGEIEETGTTFAENAALKAETVASVLNQTVIADDSGLIVDALDGAPGVYSARYAGVAHDDAKNNEKLLKNLEGVEPDKRTARFHCTLAVATPSEKTSFYTGEVEGVIAEQLCGTNGFGYDPLFFLPEFGLTMAEIPAEKKNEISHRANAIKQLEKDLVEVVEKVTKK | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Pyrophosphatase that catalyzes the hydrolysis of nucleoside triphosphates to their monophosphate derivatives, with a high preference for the non-canonical purine nucleotides XTP (xanthosine triphosphate), dITP (deoxyinosine triphosphate) and ITP. Seems to function as ... |
Q8EVN6 | MKIILATQNKRKLDEFIELSKNSNYPINFVIKPLKEDIGEIEENGNSYFENALIKANAVFNYYKEPVLSDDSGLELPEFKEILGIYSSRFAGINATDKENRYKLLDYLKSKNITETSAKYVCVLVYIFNQGEALSFKGEWEGKIIVSDNLNLDTGFGYDPMFVPKEYTITVSEMSISEKNLISHRAKAVNQFLNFLKDKK | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Pyrophosphatase that catalyzes the hydrolysis of nucleoside triphosphates to their monophosphate derivatives, with a high preference for the non-canonical purine nucleotides XTP (xanthosine triphosphate), dITP (deoxyinosine triphosphate) and ITP. Seems to function as ... |
Q8TJS1 | MHKIVFVTGNKGKFAEIRDILKTFGIEVIQEKNGYPELQEDELEPIAAHGAQYVANKLNMPVMVDDSGIFINALNGFPGPYSRFVEDKLGNLKVLKMMEGEEDRTAYFKTVIGYCEPGKEPLVFPGVVEGKIAYEERGTGGFGYDPIFEYQGLTFGELGDTEKNKVSHRRRAVDEFLEWFTSKA | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Pyrophosphatase that catalyzes the hydrolysis of nucleoside triphosphates to their monophosphate derivatives, with a high preference for the non-canonical purine nucleotides XTP (xanthosine triphosphate), dITP (deoxyinosine triphosphate) and ITP. Seems to function as ... |
B3DV19 | MIMQKILLATSNRHKYLEFSRLLYPLTLEALPEDLKRLLPNETAKSYRDNAKLKGMALSEIYEGFVLADDSGLEVFSLHGEPGIFSSRYAGEGSSAQENIDKLLKNLQSKNITDRRARFVCALVLVKKKKILFETTAFCYGIIADRQKGGGGFGYDPIFIPEGYSLTMAELDEKQKDLVSHRGKACQELKAFFLENRMEGHS | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Pyrophosphatase that catalyzes the hydrolysis of nucleoside triphosphates to their monophosphate derivatives, with a high preference for the non-canonical purine nucleotides XTP (xanthosine triphosphate), dITP (deoxyinosine triphosphate) and ITP. Seems to function as ... |
Q57679 | MKIYFATGNPNKIKEANIILKDLKDVEIEQIKISYPEIQGTLEEVAEFGAKWVYNILKKPVIVEDSGFFVEALNGFPGTYSKFVQETIGNEGILKLLEGKDNRNAYFKTVIGYCDENGVRLFKGIVKGRVSEEIRSKGYGFAYDSIFIPEEEERTFAEMTTEEKSQISHRKKAFEEFKKFLLDRI | Cofactor: Binds 1 Mg(2+) ion per subunit (By similarity). Magnesium ions are required for optimal activity, with Mn(2+), Zn(2+) and Ni(2+) supporting <50% of the maximum rate .
Function: Pyrophosphatase that catalyzes the hydrolysis of nucleoside triphosphates to their monophosphate derivatives, with a high preference ... |
Q8TV07 | MKVLFATGNIGKYHEAKQILARYGIEVERVDLDYPELQSDSLEEIAAYGARYCAESLGQPVIVEDSGLFIEALNGFPGPYSAYVFDTIGNEGILKLLEGEENRKAEFISVVGYCEPGGRPVTFTGEIRGRIAEEPRGEEGFGYDPIFIPEGEDSTFAELGVEEKCKISHRTKALERFAEWYKNNVAGR | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Pyrophosphatase that catalyzes the hydrolysis of nucleoside triphosphates to their monophosphate derivatives, with a high preference for the non-canonical purine nucleotides XTP (xanthosine triphosphate), dITP (deoxyinosine triphosphate) and ITP. Seems to function as ... |
D9PYS9 | MKVTFITGNKHKLSEAEKIFHDTGIELEHADLGYPELQGTLEEVARYGAEHAARIMDGPVIVEDAGLFIRALKWFPGPYSAYVQDTIGNRGILKLMENVEDRYAEFRSAVGFCAPKSEPEVFLGVVKGRIGTEERGTRGFAFDPLFYPEGMDRSFGELSTIEKNRFSHRSRALKKFAQWYTENYEVI | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Pyrophosphatase that catalyzes the hydrolysis of nucleoside triphosphates to their monophosphate derivatives, with a high preference for the non-canonical purine nucleotides XTP (xanthosine triphosphate), dITP (deoxyinosine triphosphate) and ITP. Seems to function as ... |
B1MLZ4 | MKILVASRNPKKLAELSRVLESSGVSGVELVSLTDVPEYEEVPETGASFEDNALIKAREGVKHTGLACVADDSGLAVDALNWMPGVLSARWSGRHGDDAANTALLLAQLSDIPDERRGAAFVSACALVTPEGEEVVVEGRWKGSIARIPAGQNGFGYDPIFVPRGGLRTAAELTPEEKDAVSHRGRALAALLPMLRNLVNLGRTAP | Cofactor: Binds 1 Mg(2+) ion per subunit.
Function: Pyrophosphatase that catalyzes the hydrolysis of nucleoside triphosphates to their monophosphate derivatives, with a high preference for the non-canonical purine nucleotides XTP (xanthosine triphosphate), dITP (deoxyinosine triphosphate) and ITP. Seems to function as ... |
Q8N5M9 | MASRAGPRAAGTDGSDFQHRERVAMHYQMSVTLKYEIKKLIYVHLVIWLLLVAKMSVGHLRLLSHDQVAMPYQWEYPYLLSILPSLLGLLSFPRNNISYLVLSMISMGLFSIAPLIYGSMEMFPAAQQLYRHGKAYRFLFGFSAVSIMYLVLVLAVQVHAWQLYYSKKLLDSWFTSTQEKKHK | Function: Endoplasmic reticulum transmembrane protein involved in vesicle-mediated transport, which is required for neutrophil function. Required for vesicle-mediated transport; it is however unclear whether it is involved in early secretory pathway or intracellular protein transport. Acts as a regulator of neutrophil ... |
Q5XKN4 | MASRAGPRAAGTDGSDFQHRERVAMHYQMSVTLKYEIKKLIYVHLVIWLLLVAKMSVGHLRLLSHDQVAMPYQWEYPYLLSIVPSVLGLLSFPRNNISYLVLSMISMGLFSIAPLIYGSMEMFPAAQQLYRHGKAYRFLFGFSAVSVMYLVLVLAVQVHAWQLYYSKKLLDSWFTSTQEKKRK | Function: Endoplasmic reticulum transmembrane protein involved in vesicle-mediated transport, which is required for neutrophil function. Required for vesicle-mediated transport; it is however unclear whether it is involved in early secretory pathway or intracellular protein transport. Acts as a regulator of neutrophil ... |
Q7K1V5 | MATRGGPMVAGTDGNDFEFRQRVAGTYQISLLNKSRLKYCIFFHALLFFVMLAKLTSDILDHLDIFVLEIEELEVPPPLWWEYVWAASLLTSFLGLSAARGNKVREMQKYMVAILLFAILPLFYCFAYYFSDVWEFATLDKSVELDETDIFVWRGYPYGVFWYAFCFVGFQVHGFTLYFAYNLVKAWKARTATRKFQ | Function: Required for endoplasmic reticulum organization and proper vesicular traffic during vitellogenesis. Required for oocyte and bristle growth.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 23036
Sequence Length: 197
Subcellular Location: Endoplasmic reticulum membrane
|
P17535 | METPFYGDEALSGLGGGASGSGGSFASPGRLFPGAPPTAAAGSMMKKDALTLSLSEQVAAALKPAAAPPPTPLRADGAPSAAPPDGLLASPDLGLLKLASPELERLIIQSNGLVTTTPTSSQFLYPKVAASEEQEFAEGFVKALEDLHKQNQLGAGAAAAAAAAAAGGPSGTATGSAPPGELAPAAAAPEAPVYANLSSYAGGAGGAGGAATVAFAAEPVPFPPPPPPGALGPPRLAALKDEPQTVPDVPSFGESPPLSPIDMDTQERIKAERKRLRNRIAASKCRKRKLERISRLEEKVKTLKSQNTELASTASLLREQ... | Function: Transcription factor binding AP-1 sites . Heterodimerizes with proteins of the FOS family to form an AP-1 transcription factor complex, thereby enhancing their DNA binding activity to an AP-1 consensus sequence 3'-TGA[GC]TCA-5' and enhancing their transcriptional activity .
PTM: Phosphorylated by MAP kinases ... |
P52909 | METPFYGEEALSGLAAGASSVAGAAGAPGGGGFAPPGRAFPGAPPTSSMLKKDALTLSLAEQGAAGLKPGSATAPSALRPDGAPDGLLASPDLGLLKLASPELERLIIQSNGLVTTTPTSTQFLYPKVAASEEQEFAEGFVKALEDLHKQSQLGAATAATSGAPAPPAPADLAATPGATETPVYANLSSFAGGAGPPGGAATVAFAAEPVPFPPPPGALGPPPPPHPPRLAALKDEPQTVPDVPSFGDSPPLSPIDMDTQERIKAERKRLRNRIAASKCRKRKLERISRLEEKVKTLKSQNTELASTASLLREQVAQLKQ... | Function: Transcription factor binding AP-1 sites (By similarity). Heterodimerizes with proteins of the FOS family to form an AP-1 transcription factor complex, thereby enhancing their DNA binding activity to an AP-1 consensus sequence 3'-TGA[GC]TCA-5' and enhancing their transcriptional activity (By similarity).
PTM: ... |
A6ND01 | MACWWPLLLELWTVMPTWAGDELLNICMNAKHHKRVPSPEDKLYEECIPWKDNACCTLTTSWEAHLDVSPLYNFSLFHCGLLMPGCRKHFIQAICFYECSPNLGPWIQPVGSLGWEVAPSGQGERVVNVPLCQEDCEEWWEDCRMSYTCKSNWRGGWDWSQGKNRCPKGAQCLPFSHYFPTPADLCEKTWSNSFKASPERRNSGRCLQKWFEPAQGNPNVAVARLFASSAPSWELSYTIMVCSLFLPFLS | Function: Receptor for IZUMO1 present at the cell surface of oocytes (oolemma), which is essential for species-specific gamete recognition and fertilization. The IZUMO1:IZUMO1R/JUNO interaction is a necessary adhesion event between sperm and egg that is required for fertilization but is not sufficient for cell fusion. ... |
Q9EQF4 | MAQWWQILLGLWAVLPTLAGDKLLSVCMNSKRHKQEPGPEDELYQECRPWEDNACCTRSTSWEAHLEEPLLFNFSMMHCGLLTPACRKHFIQAICFHECSPNLGPWIQPVVPNGQEEQRVWGVPLCQEDCEDWWRACHSSLTCKSNWLHGWDWSEEKKHCPAHEPCLPFSYHFPTPDDLCEKIWNNTFKASPERRNSGRCLQKWFEPTLSNPNVEVALHFAGSALAPQLSYTLPAFSLCLLFHP | Function: Receptor for IZUMO1 present at the cell surface of oocytes (oolemma), which is essential for species-specific gamete recognition and fertilization . The IZUMO1:IZUMO1R/JUNO interaction is a necessary adhesion event between sperm and egg that is required for fertilization but is not sufficient for cell fusion ... |
P05412 | MTAKMETTFYDDALNASFLPSESGPYGYSNPKILKQSMTLNLADPVGSLKPHLRAKNSDLLTSPDVGLLKLASPELERLIIQSSNGHITTTPTPTQFLCPKNVTDEQEGFAEGFVRALAELHSQNTLPSVTSAAQPVNGAGMVAPAVASVAGGSGSGGFSASLHSEPPVYANLSNFNPGALSSGGGAPSYGAAGLAFPAQPQQQQQPPHHLPQQMPVQHPRLQALKEEPQTVPEMPGETPPLSPIDMESQERIKAERKRMRNRIAASKCRKRKLERIARLEEKVKTLKAQNSELASTANMLREQVAQLKQKVMNHVNSGC... | Function: Transcription factor that recognizes and binds to the AP-1 consensus motif 5'-TGA[GC]TCA-3' . Heterodimerizes with proteins of the FOS family to form an AP-1 transcription complex, thereby enhancing its DNA binding activity to the AP-1 consensus sequence 5'-TGA[GC]TCA-3' and enhancing its transcriptional acti... |
P00756 | MWFLILFLALSLGGIDAAPPVQSRIVGGFKCEKNSQPWHVAVYRYTQYLCGGVLLDPNWVLTAAHCYDDNYKVWLGKNNLFKDEPSAQHRFVSKAIPHPGFNMSLMRKHIRFLEYDYSNDLMLLRLSKPADITDTVKPITLPTEEPKLGSTCLASGWGSITPTKFQFTDDLYCVNLKLLPNEDCAKAHIEKVTDAMLCAGEMDGGKDTCKGDSGGPLICDGVLQGITSWGHTPCGEPDMPGVYTKLNKFTSWIKDTMAKNP | Cofactor: Binds 2 Zn(2+) ions per 7S complex. The Zn(2+) ions are bound at the alpha-gamma interfaces.
Function: 7S NGF alpha chain stabilizes the 7S complex. The beta dimer promotes neurite growth. The gamma chain is an arginine-specific protease; it may also have plasminogen activator activity, as well as mitogenic a... |
O31714 | MIYTVTLNPSVDYIVHVEDFTVGGLNRSSYDTKYPGGKGINVSRLLKRHHVASKALGFVGGFTGEYIKTFLREENLETAFSEVKGDTRINVKLKTGDETEINGQGPTISDEDFKAFLEQFQSLQEGDIVVLAGSIPSSLPHDTYEKIAEACKQQNARVVLDISGEALLKATEMKPFLMKPNHHELGEMFGTAITSVEEAVPYGKKLVEQGAEHVIVSMAGDGALLFTNEAVYFANVPKGKLVNSVGAGDSVVAGFLAGISKQLPLEEAFRLGVTSGSATAFSEELGTEEFVQQLLPEVKVTRL | Function: Catalyzes the ATP-dependent phosphorylation of fructose-l-phosphate to fructose-l,6-bisphosphate.
Catalytic Activity: ATP + beta-D-fructose 1-phosphate = ADP + beta-D-fructose 1,6-bisphosphate + H(+)
Sequence Mass (Da): 32791
Sequence Length: 303
EC: 2.7.1.56
|
O51575 | MIYTLTLNPSVDYKIVLKEFQEESLNYALNNNFFAGGKGINVSTVLKNLGKPSTALGFLGGFTGDYIRFSLDSRGIKNDFIKIKYDTRLNIKMIANGRETEINANSPDISENEFELLKNKLKNLANNSTLVMSGSVPAALGEDAYNEIANSISNDVKLIIDTSGKPLRKILRLNPFLIKPNIYELEDLFNAKFDSTKELIKIGKNLVESGVQNIIISMGSDGAIFIGGKNVAFRAFVPKINFVSTIGAGDSVIAGFVYAFDNGSTLEDSFKFGVAAGTATALKGNLCEFQDVKKMLCQIRVEDIYTS | Function: Catalyzes the ATP-dependent phosphorylation of fructose-l-phosphate to fructose-l,6-bisphosphate.
Catalytic Activity: ATP + beta-D-fructose 1-phosphate = ADP + beta-D-fructose 1,6-bisphosphate + H(+)
Sequence Mass (Da): 33595
Sequence Length: 307
EC: 2.7.1.56
|
P0AEX1 | MSRRVATITLNPAYDLVGFCPEIERGEVNLVKTTGLHAAGKGINVAKVLKDLGIDVTVGGFLGKDNQDGFQQLFSELGIANRFQVVQGRTRINVKLTEKDGEVTDFNFSGFEVTPADWERFVTDSLSWLGQFDMVCVSGSLPSGVSPEAFTDWMTRLRSQCPCIIFDSSREALVAGLKAAPWLVKPNRRELEIWAGRKLPEMKDVIEAAHALREQGIAHVVISLGAEGALWVNASGEWIAKPPSVDVVSTVGAGDSMVGGLIYGLLMRESSEHTLRLATAVAALAVSQSNVGITDRPQLAAMMARVDLQPFN | Function: Catalyzes the ATP-dependent phosphorylation of fructose-l-phosphate to fructose-l,6-bisphosphate.
Catalytic Activity: ATP + beta-D-fructose 1-phosphate = ADP + beta-D-fructose 1,6-bisphosphate + H(+)
Sequence Mass (Da): 33756
Sequence Length: 312
EC: 2.7.1.56
|
P44330 | MASVVTITLNAAYDLVGRLNRIQLGEVNTVETLGLFPAGKGINVAKVLKDLGVNVAVGGFLGKDNSADFEQMFNQHGLEDKFHRVDGKTRINVKITETEADVTDLNFLGYQISPQVWQQFVTDSLAYCLNYDIVAVCGSLPRGVSPELFADWLNQLHQAGVKVVLDSSNAALTAGLKAKPWLVKPNHRELEAWVGHPLNSLEEIIAAAQQLKAEGIENVIISMGAKGSLWINNEGVLKAEPAQCENVVSTVGAGDSMVAGLIYGFEKGLSKTETLAFATAVSAFAVSQSNVGVSDLSLLDPILEKVQITMIEG | Function: Catalyzes the ATP-dependent phosphorylation of fructose-l-phosphate to fructose-l,6-bisphosphate.
Catalytic Activity: ATP + beta-D-fructose 1-phosphate = ADP + beta-D-fructose 1,6-bisphosphate + H(+)
Sequence Mass (Da): 33522
Sequence Length: 313
EC: 2.7.1.56
|
D4GYE6 | MILTVTPNPAVDHTIHFDEPLQTGVVHRTDDAVFTAGGKGINVAKYASALDADVTASGFLGGHFGKFVRDRLDADGIASDFVTVDADTRLNTTVLAADGEYKLNHNGPQIRAADVDELVETAQANEPDTLLVGGSLPPGMSLSDVDRLARAGDWKIAVDMGGEYLAELDADYYVCKPNRSELAAATGRTVETEADAVEAAEELHARGFEYVLASLGADGALLVTDDEVLSAPALDVEVVDTVGAGDAVMSGFLAAREHGLSDADALRMGVLTASRVVGVAGTRVPDLEDVLTNETHVEVTTVRTR | Function: Catalyzes the ATP-dependent phosphorylation of fructose-l-phosphate to fructose-l,6-bisphosphate. Involved in the utilization of fructose as a sole carbon and energy source.
Catalytic Activity: ATP + beta-D-fructose 1-phosphate = ADP + beta-D-fructose 1,6-bisphosphate + H(+)
Sequence Mass (Da): 32003
Sequence... |
Q49396 | MTWLQNITKESKIWIVNYACAIDYYVDLNKQKNSVLIPGGKGINVAIVMKSLGFDPTVITFLGQPTKNLFLELVKPYDLNIVSFISETKTRINLKLLKDEKTTEINDLSPLITDANLTELLTFLKANVKNNDLVIINGRFKFEALEKVLNLVFTLTENVVIDVDESKMLTLLNQSKPLVMKPNIDEFQTMINTFFHDQQSLIAAIKKFHYCKLLLLSDGDKGAYLFDQNKLLFVSSITPKQVVSTTGAGDTLLAVFLANLILKVDLKTALIKATNYASATISKLGVVDSKDKISVITPKSYYL | Function: Catalyzes the ATP-dependent phosphorylation of fructose-l-phosphate to fructose-l,6-bisphosphate.
Catalytic Activity: ATP + beta-D-fructose 1-phosphate = ADP + beta-D-fructose 1,6-bisphosphate + H(+)
Sequence Mass (Da): 33922
Sequence Length: 303
EC: 2.7.1.56
|
P23386 | MTLRIATVSLNSAVDQTVTVPGFTADAVNRVAASRIDAGGKGVNVASFLAHVGHGVAVTGLLGAENAALFARHFAATGLVDACQRLPGATRTNVKIVDPLQDQVTDLNFPGIAAGPADLDAVAATLTELLAQGLDWVALCGSLPAGIGAEAYAELAALARKGGARVALDTSGPALGLALAARPDIVKPNVAELGAHLGRTLTGLESVREAARDLAASGVGLVAVSMGAGGAVLVRGAEAVLAIPPATPIASTVGAGDAMVAGLIHAATLGLDLAETARLATAFSLGALGEIGPHLPPPERLAALARTVTVKTLPPV | Function: Catalyzes the ATP-dependent phosphorylation of fructose-l-phosphate to fructose-l,6-bisphosphate.
Catalytic Activity: ATP + beta-D-fructose 1-phosphate = ADP + beta-D-fructose 1,6-bisphosphate + H(+)
Sequence Mass (Da): 31232
Sequence Length: 316
EC: 2.7.1.56
|
Q9KM71 | MTKKVVTITLNPALDLTGSVNQLNVGSVSLVGQSSLHAAGKGVNVAKVLSELGAQVTVTGFLGRDNQELFCQLFEQLGVQDAFIRIAGATRINVKLVEQSGAVSDINFPGIQVTEADIEAFEATLQRLAQDHDYFVLAGSLPQGISPQRCAGWIAQLRSMNKKVLFDSSRDALLAGLDAKPWLIKPNDEELSQWCGRELTTLTDCQQAAAELAQKQIENIVISMGAEGVMWLHENQWLHAKPPKMQVVSTVGAGDTLVAGLCWGHMQRMEKESLLRFATALSALAVTQVGVGLGDREQLNTLQQQIQVSALYPTMGA | Function: Catalyzes the ATP-dependent phosphorylation of fructose-l-phosphate to fructose-l,6-bisphosphate.
Catalytic Activity: ATP + beta-D-fructose 1-phosphate = ADP + beta-D-fructose 1,6-bisphosphate + H(+)
Sequence Mass (Da): 34192
Sequence Length: 317
EC: 2.7.1.56
|
P05787 | MSIRVTQKSYKVSTSGPRAFSSRSYTSGPGSRISSSSFSRVGSSNFRGGLGGGYGGASGMGGITAVTVNQSLLSPLVLEVDPNIQAVRTQEKEQIKTLNNKFASFIDKVRFLEQQNKMLETKWSLLQQQKTARSNMDNMFESYINNLRRQLETLGQEKLKLEAELGNMQGLVEDFKNKYEDEINKRTEMENEFVLIKKDVDEAYMNKVELESRLEGLTDEINFLRQLYEEEIRELQSQISDTSVVLSMDNSRSLDMDSIIAEVKAQYEDIANRSRAEAESMYQIKYEELQSLAGKHGDDLRRTKTEISEMNRNISRLQAE... | Function: Together with KRT19, helps to link the contractile apparatus to dystrophin at the costameres of striated muscle.
PTM: Phosphorylation on serine residues is enhanced during EGF stimulation and mitosis. Ser-74 phosphorylation plays an important role in keratin filament reorganization.
Sequence Mass (Da): 53704
... |
P86247 | MSTSGPRAFSSRFASFIDKVRWSLLQQQKSNMDNMFESYINNLRDVDEAYMNKVELESRLEGLTDEINFLRQIHEEEIRSLDMDSIIAEVRHGDDLRRLALDIEIATYRK | Function: Together with KRT19, helps to link the contractile apparatus to dystrophin at the costameres of striated muscle.
PTM: O-glycosylated. O-GlcNAcylation at multiple sites increases solubility, and decreases stability by inducing proteasomal degradation (By similarity).
Sequence Mass (Da): 12975
Sequence Length: ... |
Q28810 | QRTLKVSSSGPRSFSSRSFSSGPSSRISSSSYSRVGSNSSFRSGVGFGPNYGMGLGSSIGVGGITAVSVNQSLLNPLKLELDPSIQAVRTQEKEQIKTLNNKFASFIDKVRFLEQQNKILETKWSFLQQQKTSQSNLDGLFEKYITNLRRQLDSMGQEKLKLEVELGNMQGLVEDFKKKYEDEINKRTEMENEFVLIKKDVDEAYMNKVELESRLEGLTDEINFLRHLYEEEIKEMQSQISDTSVVVSMDNSRSLDLDGIIADVRAQYEEIANRSRAEAETMYQIKYEELQLLAGKHGDDLRHTKTEISE | Function: Together with KRT19, helps to link the contractile apparatus to dystrophin at the costameres of striated muscle.
PTM: O-glycosylated. O-GlcNAcylation at multiple sites increases solubility, and decreases stability by inducing proteasomal degradation (By similarity).
Sequence Mass (Da): 35170
Sequence Length: ... |
Q6P618 | MDATRKPLRIPPAMALYAEEQGVFDIIQKMVKKVLVDRPKDPIQYMIDHLSNDNDDVPRVFILGPPASGKHTMAKLLCKRLNATHLTPESVLSSDVSLLAKEAQSYRDKGQEVPDELWAKLMQQRLSKVDCIKRGWILEGFPKTREQALKLQMAGICPDHLVVLDAPDIVLIERNMGKRIDTANGEVYHTTFDWPSDPTVQRNLVEPEGISEEETGLRLIEYHRNIPGILRTYPKTSKKINADQPYMDVFSQVLTFVLSKPRSLAPHTPRILLYGPPGSGRSLQASLLAQKYGIVNICCGQVLKEAVADQTKLGEVIQPY... | Function: Nucleoside monophosphate (NMP) kinase that catalyzes the reversible transfer of the terminal phosphate group between nucleoside triphosphates and monophosphates. Has highest activity toward AMP, and weaker activity toward dAMP, CMP and dCMP. Also displays broad nucleoside diphosphate kinase activity.
Catalyti... |
Q9YDD2 | MRHPFKVVVVTGVPGVGKTTVIKELQGLAEKEGVKLHIVNFGSFMLDTAVKLGLVEDRDKIRTLPLRRQLELQREAAKRIVAEASKALGGDGVLIIDTHALVKTVAGYWPGLPKHVLDELKPDMIAVVEASPEEVAARQARDTTRYRVDIGGVEGVKRLMENARAASIASAIQYASTVAIVENREGEAAKAAEELLRLIKNL | Catalytic Activity: AMP + ATP = 2 ADP
Sequence Mass (Da): 21948
Sequence Length: 202
Subcellular Location: Cytoplasm
EC: 2.7.4.3
|
P43409 | MKNKVVVIVGVPGVGSTTVTNKAIEELKKEGIEYKIVNFGTVMFEIAKEEGLVEHRDQLRKLPPEEQKRIQKLAGKKIAEMAKEFNIVVDTHSTIKTPKGYLPGLPAWVLEELNPDIIVLVEAENDEILMRRLKDETRQRDFESTEDIGEHIFMNRCAAMTYAVLTGATVKIIKNRDFLLDKAVQELIEVLK | Catalytic Activity: AMP + ATP = 2 ADP
Sequence Mass (Da): 21772
Sequence Length: 192
Subcellular Location: Cytoplasm
EC: 2.7.4.3
|
Q8TZB0 | MGYVIVATGVPGVGATTVTTEAVKELEGYEHVNYGDVMLEIAKEEGLVEHRDEIRKLPAEKQREIQRLAARRIAKMAEEKEGIIVDTHCTIKTPAGYLPGLPIWVLEELQPDVIVLIEADPDEIMMRRVKDSEERQRDYDRAHEIEEHQKMNRMAAMAYAALTGATVKIIENHDDRLEEAVREFVETVRSL | Catalytic Activity: AMP + ATP = 2 ADP
Sequence Mass (Da): 21692
Sequence Length: 191
Subcellular Location: Cytoplasm
EC: 2.7.4.3
|
O26135 | MKVVVVAGIPGSGSTTVLENTLKELDYLNVNYGDVMLEIAVEKGLVENRDQMRTLPPEVQKDIQRAAAKSIRERSLENNIIVDTHCTIKTPAGFLPGLPVWVLEELEPDMFVLVEADAEEIFTRRISDKTRDRDVESLQEIDLHQQMNRAAAMAYATLTGATVKIVKNHNNQLESAVSEMKSVLE | Catalytic Activity: AMP + ATP = 2 ADP
Sequence Mass (Da): 20633
Sequence Length: 185
Subcellular Location: Cytoplasm
EC: 2.7.4.3
|
Q8ZWP7 | MKIVIVALPGSGKTTILNFVKQKLPDVKIVNYGDVMLEIAKKRFGIQHRDEMRKKIPVDEYRKVQEEAAEYIASLTGDVIIDTHASIKIGGGYYPGLPDRIISKLKPDVILLLEYDPKVILERRKKDPDRFRDLESEEEIEMHQQANRYYAFAAANAGESTVHVLNFRGKPESRPFEHAEVAAEYIVNLILRTRQKS | Catalytic Activity: AMP + ATP = 2 ADP
Sequence Mass (Da): 22535
Sequence Length: 197
Subcellular Location: Cytoplasm
EC: 2.7.4.3
|
Q8K980 | MRIILLGAPGTGKGTQAKLITENYNIPKISTGDILRENIQKKNTIGKKIHNILKNGELVSNRIVCNLIGERIQKKDCIHGFLLDGFPRTQKQAEYISNLKIKIDYVLELIVPYELILKRICGRRVHTPSGRIYNINYNPPREEGKDDLTQEKLTIREDDTIEIVKKRLENYEKNSFLLNKYYLREKKLKKLQYFKIDGKQSIYKIQREIKMMLK | Function: Catalyzes the reversible transfer of the terminal phosphate group between ATP and AMP. Plays an important role in cellular energy homeostasis and in adenine nucleotide metabolism.
Catalytic Activity: AMP + ATP = 2 ADP
Sequence Mass (Da): 25091
Sequence Length: 214
Domain: Consists of three domains, a large ce... |
P59429 | MHIVLIGGPGTGKGTQAELLSKKYMLPVISTGHILRKISTKKTLFGEKIKNIINSGKLVPDTIIIKIITNEILHKNYTNGFILDGFPRTIKQAKNLKNTNIQIDYVFEFILPTKLIFKRIQTRTINPITGTIYNNVIQKNSELKNLKINTLKSRLDDQYPIILKRLKEHKKNIVYLKDFYINEQKHKSLKYHEINSQNTIKNVNIEIKKILENKL | Function: Catalyzes the reversible transfer of the terminal phosphate group between ATP and AMP. Plays an important role in cellular energy homeostasis and in adenine nucleotide metabolism.
Catalytic Activity: AMP + ATP = 2 ADP
Sequence Mass (Da): 24889
Sequence Length: 215
Domain: Consists of three domains, a large ce... |
Q057D8 | MRIIMIGPPGSGKGTQTQLLSKYFHIPCISTGEILRKEIKKNKKTKKYIKKTINKGKLIKNSFIIKIIEKNIKKKKFFNGFILDGFPRNIEQAKSLSKKINIEYIIYLKIKYDDIIKRITGRLIHASSGRTYHKIFNPPKIKNKDDITQEKLCSRNDDNEKTIKIRLQEYKKHTNPLIKWIKKKKKIKFIEIHANQSIKIVNKKIIYNINNNNINK | Function: Catalyzes the reversible transfer of the terminal phosphate group between ATP and AMP. Plays an important role in cellular energy homeostasis and in adenine nucleotide metabolism.
Catalytic Activity: AMP + ATP = 2 ADP
Sequence Mass (Da): 25447
Sequence Length: 216
Domain: Consists of three domains, a large ce... |
A4J592 | MNLLIMGPPGAGKGTQAEVLVKELKITHISTGDMFRAAIKEGTEMGKKAKEYMDKGALVPDEVVIGMVKDRLSQADCKEGFLLDGFPRTVEQASALDATLQDLGIKLDAVINIEVPLEKLMARLTGRRVCKNCGASYHVIFNPPQAEGKCNSCNGELYQRSDDNEESVGTRLNAYIEKTKPLIDYYEAKGILKNINGDQEISAVLNDILVAVK | Function: Catalyzes the reversible transfer of the terminal phosphate group between ATP and AMP. Plays an important role in cellular energy homeostasis and in adenine nucleotide metabolism.
Catalytic Activity: AMP + ATP = 2 ADP
Sequence Mass (Da): 23245
Sequence Length: 213
Domain: Consists of three domains, a large ce... |
Q72AR0 | MNILIFGPNGSGKGTQGALVKKKYDLAHIESGAIFREHIGGGTELGKQAKAFIERGDLVPDDITIPMVLETLKSKGANGWLLDGFPRNMVQAQKLWDALQAEGMKLDYVIEILLPREVAKNRIMGRRLCKNDNNHPNNIFIDAIKPNGDVCRVCGGELSARSDDQDEGAIGKRHDIYYNTVDGTLAAAYFYKDLAAKGMTKYIELDGEGAIDAIKDKLLAQLS | Function: Catalyzes the reversible transfer of the terminal phosphate group between ATP and AMP. Plays an important role in cellular energy homeostasis and in adenine nucleotide metabolism.
Catalytic Activity: AMP + ATP = 2 ADP
Sequence Mass (Da): 24421
Sequence Length: 223
Domain: Consists of three domains, a large ce... |
A0QSH8 | MRVVLLGPPGAGKGTQAEKLSEKLGIPQISTGDLFRKNIGDGTPLGLEAKRYLDAGDLVPAELTNRLVEDRIDQPDAAEGFILDGYPRSVEQAGALKDMLAARNTKLDAVLEFQVSEDELLTRLKGRGRADDTDEVIRNRMKVYREETEPLLEYYRDDLKTVNAVGALDEVFARALSALGQ | Function: Catalyzes the reversible transfer of the terminal phosphate group between ATP and AMP. Plays an important role in cellular energy homeostasis and in adenine nucleotide metabolism.
Catalytic Activity: AMP + ATP = 2 ADP
Sequence Mass (Da): 19871
Sequence Length: 181
Domain: Consists of three domains, a large ce... |
Q3IMW0 | MSQPKILLLGAPGAGKGTQSSNIVDEYGVDHITTGDALRANKDMETEHGTPREFMEAGELVPDPVVNEIVQAAIDEADGFVLDGYPRNLSQAEYLSDITDVDVVALLDVGRDELVDRLTGRRMDPETGDIYHTEFNMPDDEEVRERLVQRDDDTEETVNERLDVFDENTQPVIDYYEDEGELVRIDGEASPDEVWDDLQAAIDDAL | Function: Catalyzes the reversible transfer of the terminal phosphate group between ATP and AMP. Plays an important role in cellular energy homeostasis and in adenine nucleotide metabolism.
Catalytic Activity: AMP + ATP = 2 ADP
Sequence Mass (Da): 22957
Sequence Length: 206
Domain: Consists of three domains, a large ce... |
B2A4G2 | MRIILMGPPGAGKGTQAEKLSKELDVPHIATGDIFRKAVSEGTELGKEAKSYMDAGQLVPDDVVIGIVEERLKKPDCHEGFILDGFPRTVTQAEALDKVLSDNPLTAAVYIDVSKDELIDRLSGRRICRKCGKSYHIKFNPPQVRGVCDEDEGELYQRDDDNEETAKERLEVYLENTQPLVEYYQDRGILKKIDGTKSPEEVFRDILKAVQAKQ | Function: Catalyzes the reversible transfer of the terminal phosphate group between ATP and AMP. Plays an important role in cellular energy homeostasis and in adenine nucleotide metabolism.
Catalytic Activity: AMP + ATP = 2 ADP
Sequence Mass (Da): 23978
Sequence Length: 214
Domain: Consists of three domains, a large ce... |
Q8DML4 | MRLILFGGPGSGKGTQAAILTTLLGIPHISTGDILRAERAAGTLLGQQAQSYMDRGELVPDQVIVDMVANRLQQPDTAAGWLLDGFPRNGAQAAVFEEMLKSIHQDYDYLLFLDVPAAILQERALNRAKQAVNGQQRSDDTPETILKRLQVYERETLPMIQQYMSHPKFVPIDGTRTIEEVTAAIQARIGEVNRV | Function: Catalyzes the reversible transfer of the terminal phosphate group between ATP and AMP. Plays an important role in cellular energy homeostasis and in adenine nucleotide metabolism.
Catalytic Activity: AMP + ATP = 2 ADP
Sequence Mass (Da): 21524
Sequence Length: 195
Domain: Consists of three domains, a large ce... |
B5YHP1 | MRLVFLGAPGAGKGTQAKRLVEKYGIPQISTGDLLRAAVAAGTPLGKEAKAYMDRGELVPDKVVLGMVKERLSQNDCKKGFILDGFPRNVAQAEALDKMLSEMNMPLDLALNLDVPFDDLMKRLTGRRTCKSCGQMYNVYYSPSKVEGKCDKCGGELFQRDDDKEETIRKRLEVYRAQTEPLIDYYSKKGILKSVSGTGSIDEIFNSICAILEKK | Function: Catalyzes the reversible transfer of the terminal phosphate group between ATP and AMP. Plays an important role in cellular energy homeostasis and in adenine nucleotide metabolism.
Catalytic Activity: AMP + ATP = 2 ADP
Sequence Mass (Da): 23827
Sequence Length: 215
Domain: Consists of three domains, a large ce... |
Q73NP0 | MNCIFLGPPGAGKGTLAFEVSKSYKIPHISTGDLFRAAIKEQTDLGKKVKAVIDSGALVSDDLTIALVKERLERDDTKKGFILDGFPRTIAQADALEDIVKIDSVINFDISDDEVIKRLSGRRVCSSCGQSFHIEFVKPKKEGICDSCSGDLMIRPDDKIEAIQKRLETYRNQTAPLIDYYTKKDLIVNIDARPASEKVLASFKVKFPH | Function: Catalyzes the reversible transfer of the terminal phosphate group between ATP and AMP. Plays an important role in cellular energy homeostasis and in adenine nucleotide metabolism.
Catalytic Activity: AMP + ATP = 2 ADP
Sequence Mass (Da): 23178
Sequence Length: 209
Domain: Consists of three domains, a large ce... |
O83604 | MRFVFLGPPGAGKGTLAGEISGRCGVVHISTGGILRAAIQKQTALGKKVQKVVEVGGLVDDQTVTELVRERVSHEDVVSGFILDGFPRTVTQARCLEDIVPIDYAVSIVVPDDVLVARLTGRRVCSACGSSYHVLFAQPKREGVCDRCRGVLVVREDDKMSAILQRLTAYRAQAEPIVHFYSERGKLVSLNGAPPISDVVLEFQERFAQSR | Function: Catalyzes the reversible transfer of the terminal phosphate group between ATP and AMP. Plays an important role in cellular energy homeostasis and in adenine nucleotide metabolism.
Catalytic Activity: AMP + ATP = 2 ADP
Sequence Mass (Da): 22933
Sequence Length: 211
Domain: Consists of three domains, a large ce... |
B3E851 | MNLILFGPPGAGKGTQAQFLVETYGIPQISTGDMLRAAVKAGTPLGVKAQEIMIQGGLVSDDIVLGIVAERLAQDDCAAGFVLDGFPRTIPQADALSVILKQVGRAIDHVISLEVDGEEIVNRLSGRRSCSSCGKGYHLVFDPPLRAGVCDVCGSGLVQRADDQEETVRNRLLVYEQQTAPLKDYYRSRQVLCSIPGIGSIVEIQQRIAAALVE | Function: Catalyzes the reversible transfer of the terminal phosphate group between ATP and AMP. Plays an important role in cellular energy homeostasis and in adenine nucleotide metabolism.
Catalytic Activity: AMP + ATP = 2 ADP
Sequence Mass (Da): 22876
Sequence Length: 214
Domain: Consists of three domains, a large ce... |
Q83I60 | MRAIMVGPPGSGKGTQCGLIQSRLGISVIATGDVFRERMKTDMALRDIVSSGGYVSDSTTNRIVEDCLDKEDVSSGFVLDGYPRTLQQLDFLEGFLKRRALTLDAVFSLEVATDLLIERLRARSKESGRTDDRDSVIARRLEIYTEMTLPIIDACEEKGLLHRIDASKGIEEVFQSIKDVFDRVTI | Function: Catalyzes the reversible transfer of the terminal phosphate group between ATP and AMP. Plays an important role in cellular energy homeostasis and in adenine nucleotide metabolism.
Catalytic Activity: AMP + ATP = 2 ADP
Sequence Mass (Da): 20692
Sequence Length: 186
Domain: Consists of three domains, a large ce... |
O61069 | MAVLSEDVLLYLKEKNIPMLFEQIVQNIISDAPERPMSYIGDLMRRGIPLQIFIAGPAGSGKRTQCKNIADRLGVVLISSGQVLTRGVESGSETSQLAHSYVSRGERVPDTLVSMIMKDRLSQSDACEKGWLVEGYPRNAQQAQAVEECGVIPQVFILLDLPEDLSFRRLEHRRYDPATNKXYHMLDNPPPGGRCRVMRTAPAEGCKFP | Function: Catalyzes the reversible transfer of the terminal phosphate group between ATP and AMP. Plays an important role in cellular energy homeostasis and in adenine nucleotide metabolism.
Catalytic Activity: AMP + ATP = 2 ADP
Sequence Mass (Da): 23283
Sequence Length: 209
Subcellular Location: Cytoplasm
EC: 2.7.4.3
|
B5ZB60 | MKILLIGPPGSGKGSVSELLTKNNALKHVSTGNLFRAILKEDSELARKIKEINVSGGKLVPDEITNQVAKSAIDELIKNQQSFILDGYPRTINQALALEQYCDLDYIFYLDINHQELMKRLTGRWMCPKCAGIYNIHFKKPQVDGVCDNDQATLYQRADDHEDAVSIRLDEYDKLTLPLIKHYKTNPRFIKINANQPIKDVYEDINNYLKQNK | Function: Catalyzes the reversible transfer of the terminal phosphate group between ATP and AMP. Plays an important role in cellular energy homeostasis and in adenine nucleotide metabolism.
Catalytic Activity: AMP + ATP = 2 ADP
Sequence Mass (Da): 24322
Sequence Length: 213
Domain: Consists of three domains, a large ce... |
Q65CC7 | MHLLVRALVEEMAGRGVPHRVLTMSPPKVPKDIRIGQRIKVHARRLPVLPIPSDLEGYFGLVGAWAKGSLLWVLRNRKRLRREIGARVHAHCDGSGAAAFYPYLMSRILGVPLVVQIHSSRYLSQHPTTLFERVTDPIAKWAERHAVRKAAAVLMLTDRARDEMRRKAQLPAERVHRLAYLASDQFKDADTEARRAELRERYGLDDRPIVLYVGRIAAEKGVEYYIEAAAELTRRGRDCQFVIAGDGPARPDLEKLIGARGLRDRVTITGFMSHEFIPSMISLGELVVLPSRYEELGIVILECMTMRRPLVAHDVNGVNK... | Function: Glycosyltransferase involved in the biosynthesis of kanamycins by catalyzing the transfer of the hexose kanosamine from UDP-alpha-D-kanosamine to disaccharide precursors. Can also use UDP-alpha-D-glucose as sugar donor with much lower efficiency.
Catalytic Activity: 2'-deamino-2'-hydroxyneamine + UDP-alpha-D-... |
Q65CC1 | MQVQILRMSRALAELGVRQQVLTVGFPGLPRVRRDSENLVVRITRAPLPRLRSRITGLVGLNQAWLAAALTECVKLRRRWPADLIQVHLDGQLWALLAGPVAARLVGVPYTVTVHCSRLAVYQPMSTVDRIQHPLVTAVERWALRRAAGITTLTERTATVLAAELGAAQRVIDVVPDAVDPDRAEAAPAEVERLKKRFGLPQEGGPVIGFVGRIAHEKGWRHAVQAVAELADAGRDFTFLVVGDGPQRADMEAAVAEAGLTDRFVFTGFLPNDEIPAVMTALDVLLMPSVHEELGGSAVEAMLAGTPVAAYGVGGLCDTV... | Function: Glycosyltransferase involved in the biosynthesis of kanamycin by mediating conversion of 2-deoxystreptamine (2-DOS) to 2'-N-acetylparomamine using UDP-alpha-D-glucose as sugar donor. Can also accept UDP-alpha-D-glucosamine, but with a much lower activity compared to UDP-alpha-D-glucose.
Catalytic Activity: 2-... |
Q6L732 | MALAAPPGELTLALTPDDKTLDPASLDRALAILAEHGILVLTGMLRTRLTDQLRTAMLDDLPEVLRQQDVPTNFVPGHVQQDPPVRESLLFPDVLLNPVVYQITHAVLGADARNAVYSGNMNLPGSHEQPVHLDEPHLWPGISHPPYCLCVDVPLIDFTLENGSTEYWPGSHVLNPDECYDERGCVLPAELERRRAVAPPVRFPIPVGSVVIRDGRLWHRGVPNLSAAPRPLLAMTHYTEWFDMPPIQLPDTVKSWVDGSDRHTHAHFVAGDVDHLTGDHPFAVR | Function: Mediates the conversion of kanamycin B into 2'-dehydrokanamycin A during the transformation of kanamycin B to kanamycin A.
Catalytic Activity: 2-oxoglutarate + kanamycin B + O2 = 2'-dehydrokanamycin A + CO2 + NH4(+) + succinate
Sequence Mass (Da): 31534
Sequence Length: 285
Pathway: Antibiotic biosynthesis; k... |
Q63ZY3 | MAQVLHVPAPFPGTPGPASPPAFPAKDPDPPYSVETPYGYRLDLDFLKYVDDIEKGHTLRRVAVQRRPRLSSLPRGPGSWWTSTESLCSNASGDSRHSAYSYCGRGFYPQYGALETRGGFNPRVERTLLDARRRLEDQAATPTGLGSLTPSAAGSTASLVGVGLPPPTPRSSGLSTPVPPSAGHLAHVREQMAGALRKLRQLEEQVKLIPVLQVKLSVLQEEKRQLTVQLKSQKFLGHPTAGRGRSELCLDLPDPPEDPVALETRSVGTWVRERDLGMPDGEAALAAKVAVLETQLKKALQELQAAQARQADPQPQAWPP... | Function: Involved in transcription regulation by sequestering in the cytoplasm nuclear receptor coactivators such as NCOA1, NCOA2 and NCOA3 . Involved in regulation of caspase-independent apoptosis by sequestering the proapoptotic factor AIFM1 in mitochondria . Pro-apoptotic stimuli can induce its proteasomal degradat... |
Q8BX02 | MAQVLHVPAPFPGTPGQASPAAFPSKEPDPPYSVETPYGYRLDLDFLKYVDDIEKGHTLRRVAVQRRPRLGSLPRGPGSWWTSTESLCSDASGDSRHSAYSYCGRGFYPQYGALETRIGSNPRVERTLLDARRRLEDQAAAPSSGGLGSLTPSAAGSTSSLAGVGLLPPTPRSSGLSTPVAPSAGHLAHVREQMAGALRKLRQLEEQVKLIPVLQVKLSVLQEEKRQLTVQLKSQKFLGHPSGTRSRSELCLDLPEAPDDPAALETRSVGTWVRERDLGIPDGEAALVAKVAVLETQLKKALQELRAAQTQQVDLQPQAW... | Function: Involved in transcription regulation by sequestering in the cytoplasm nuclear receptor coactivators such as NCOA1, NCOA2 and NCOA3 (By similarity). Involved in regulation of caspase-independent apoptosis by sequestering the proapoptotic factor AIFM1 in mitochondria (By similarity). Pro-apoptotic stimuli can i... |
Q2MFU6 | MSSQLALRGPELSANLCKPEEDTLRVLVTGGSGNVGVGVVRALNAARHHVVVASRGYSPALLPEGVRAVRLERTEPDAYTRLVAAEKPDAVIDLTCHDAADAAVTLRACAGVDRVVVVSSVTAAGPATTTPVTEATAAPPLSEYGIDKLAVEETVRAAWADGTSQALLVRLGAVYRLGADLDGQLAEDGCWLAHAAAGAPAVLADDGAARWNLLHADDAGAALAELLANDRARGVLVHLASRHPLPWRELYERVHHALGRPFNPVSVPAEWAAEQLEDAEFLAETSRWDQVFDLGLLDRLAPSYQERGGPSRVTEVALWL... | Function: Mediates the conversion of 2'-dehydrokanamycin A into kanamycin A.
Catalytic Activity: 2'-dehydrokanamycin A + H(+) + NADPH = kanamycin A + NADP(+)
Sequence Mass (Da): 37159
Sequence Length: 352
Pathway: Antibiotic biosynthesis; kanamycin biosynthesis.
EC: 1.1.1.355
|
Q7XT08 | MAARSELLRSAFGKASPSLGWFIVNPHRYSYRWWHMFLIMLVLYSAWASPFELSMEKAASIALVVIRPSGRCLLRHRHCHILLRHLVTGKRQGLWGLLNLLRLWRLRCASKLFARVEKDVRFSYLWTRLIKLLCVTLFALHFAACIYLWMVFNYKIKELTWIGSQIHSFEDRSVWFCYTCAVYWSITTLATVGYGDLHATNIGEMLFSIAFMLFNMGLTSYIIGNITNLVVRETSNTFKMRDMVQWVSEFGSMNRLPEVMREQMLANGQLRFRTKEQLQHEHVKRIGPRGMVGEIGVMFSIPQPFTIRSRRLTQVVRISH... | Function: Putative inward-rectifying potassium channel.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 42795
Sequence Length: 368
Subcellular Location: Membrane
|
Q5RBG4 | MAEVGEIIEGCRLPVLRRNQDNEDEWPLAEILSVKDISGRKLFYVHYIDFNKRLDEWVTHERLDLKKIQFPKKEAKTPTKNGLPGSRPGSPEREVKRKVEVVSPATPVPSETAPASVFPQNGAARRAVAAQPGRKRKSNCLGTDEDSQDSSDGIPSAPRMTGSLVSDRSHDDIVTRMKNIECIELGRHRLKPWYFSPYPQELTTLPVLYLCEFCLKYGRSLKCLQRHLTKCDLRHPPGNEIYRKGTISFFEIDGRKNKSYSQNLCLLAKCFLDHKTLYYDTDPFLFYVMTEYDCKGFHIVGYFSKEKESTEDYNVACILT... | Function: Catalytic subunit of the NuA4 histone acetyltransferase complex, a multiprotein complex involved in transcriptional activation of select genes principally by acetylation of nucleosomal histones H2A and H4. Histone acetylation alters nucleosome-DNA interactions and promotes interaction of the modified histones... |
O95251 | MPRRKRNAGSSSDGTEDSDFSTDLEHTDSSESDGTSRRSARVTRSSARLSQSSQDSSPVRNLQSFGTEEPAYSTRRVTRSQQQPTPVTPKKYPLRQTRSSGSETEQVVDFSDRETKNTADHDESPPRTPTGNAPSSESDIDISSPNVSHDESIAKDMSLKDSGSDLSHRPKRRRFHESYNFNMKCPTPGCNSLGHLTGKHERHFSISGCPLYHNLSADECKVRAQSRDKQIEERMLSHRQDDNNRHATRHQAPTERQLRYKEKVAELRKKRNSGLSKEQKEKYMEHRQTYGNTREPLLENLTSEYDLDLFRRAQARASED... | Function: Catalytic subunit of histone acetyltransferase HBO1 complexes, which specifically mediate acetylation of histone H3 at 'Lys-14' (H3K14ac), thereby regulating various processes, such as gene transcription, protein ubiquitination, immune regulation, stem cell pluripotent and self-renewal maintenance and embryon... |
Q9H7Z6 | MAAQGAAAAVAAGTSGVAGEGEPGPGENAAAEGTAPSPGRVSPPTPARGEPEVTVEIGETYLCRRPDSTWHSAEVIQSRVNDQEGREEFYVHYVGFNRRLDEWVDKNRLALTKTVKDAVQKNSEKYLSELAEQPERKITRNQKRKHDEINHVQKTYAEMDPTTAALEKEHEAITKVKYVDKIHIGNYEIDAWYFSPFPEDYGKQPKLWLCEYCLKYMKYEKSYRFHLGQCQWRQPPGKEIYRKSNISVYEVDGKDHKIYCQNLCLLAKLFLDHKTLYFDVEPFVFYILTEVDRQGAHIVGYFSKEKESPDGNNVACILTL... | Function: Histone acetyltransferase which may be involved in transcriptional activation . May influence the function of ATM . As part of the MSL complex it is involved in acetylation of nucleosomal histone H4 producing specifically H4K16ac . As part of the NSL complex it may be involved in acetylation of nucleosomal hi... |
Q8H038 | MEKVGGKPPQSRLCFLATLCAMFWVLIFYFHFFVIANEPGSAGADTAAGAAASIARAELPLPEPERVSDPAVPLPPPALVSEPPPTTATVAKVEDEEKPTAVAHQEAAPRDYAFQRALKTAENKSDPCGGRYIYVHELPPRFNDDMLRECERLSLWTNMCKFMSNEGLGPPLGNEEGVFSNTGWYATNQFMVDVIFRNRMKQYECLTKDSSIAAAVFVPFYAGFDVARYLWGHNISTRDAASLDLIDWLRKRPEWNVMGGRDHFLVGGRIAWDFRRLTDEESDWGNKLLFMPAAKNMSMLVVESSPWNANDFAIPYPTYF... | Function: Involved in the attachment of the Gal residue on the third xylosyl unit within the XXXG core structure of xyloglucan, the principal glycan that interlaces the cellulose microfibrils in plant cell wall. Interacts with actin and is required for the proper endomembrane organization and for the cell elongation (B... |
P16341 | AFCNLRMCQLSCRSLGLLGKCIGDKCECVKH | Function: Blocker for the small conductance calcium-activated potassium channels . Shows the best affinity for KCa2.2/KCNN2 (Kd=0.2 nM), followed by KCa2.3/KCNN3 (Kd=1.1 nM) and KCa2.1/KCNN1 (Kd=325 nM) .
PTM: Two disulfide bonds are the minimal requirement needed to produce a nativelike and bio-active conformation in ... |
Q9TVX3 | MHNYYKIVLIMVAFFAVIITFSNIQVEGAVCNLKRCQLSCRSLGLLGKCIGDKCECVKHGK | Function: Blocks small conductance calcium-activated potassium channels (KCNN, SK) . Has also been shown to weakly inhibit Kv11.1/KCNH2/ERG1, Kv1.2/KCNA2, Kv1.3/KCNA3 and Kv2.1/KCNB1 voltage-gated potassium channels .
Sequence Mass (Da): 6808
Sequence Length: 61
Domain: Has the structural arrangement of an alpha-helix ... |
P80719 | VSCTGSKDCYAPCRKQTGCPNAKCINKSCKCYGC | Function: Blocks voltage-gated potassium channels Kv1.2/KCNA2 (IC(50)=0.12-0.8 nM), KCa3.1/KCNN4 (IC(50)=1-2.2 nM), Shaker B (IC(50)=2.39-80 nM), Kv1.1/KCNA1 (IC(50)=37-45 or no activity, depending on the study), Kv1.3/KCNA3 (IC(50)=150-180 or no activity, depending on the study).
Sequence Mass (Da): 3621
Sequence Leng... |
P59867 | ASCRTPKDCADPCRKETGCPYGKCMNRKCKCNRC | Function: Potently blocks voltage-gated potassium channels Kv1.1/KCNA1 (IC(50)=7-11 nM) and Kv1.3/KCNA3 (IC(50)=11-29 pM) . Also mildly blocks intermediate (IK) conductance calcium-activated potassium channels (KCa3.1/KCNN4) and ERG1/Kv11.1/KCNH2 . Shows ability to suppress proliferation of lymphocytes, which are known... |
Q27955 | MYPESTTGSPARLSLRQTGSPGMIYSTRYGSPKRQLQFYRNLGKSGLRVSCLGLGTWVTFGGQITDEMAEQLMTLAYDNGINLFDTAEVYAAGKAEVVLGNIIKKKGWRRSSLVITTKIFWGGKAETERGLSRKHIIEGLKASLERLQLEYVDVVFANRPDPNTPMEETVRAMTHVINQGMAMYWGTSRWSSMEIMEAYSVARQFNLIPPICEQAEYHMFQREKVEVQLPELFHKIGVGAMTWSPLACGIVSGKYDSGIPPYSRASLKGYQWLKDKILSEEGRRQQAKLKELQAIAERLGCTLPQLAIAWCLRNEGVSSV... | Function: Cytoplasmic potassium channel subunit that modulates the characteristics of the channel-forming alpha-subunits (By similarity). Contributes to the regulation of nerve signaling, and prevents neuronal hyperexcitability (By similarity). Promotes expression of the pore-forming alpha subunits at the cell membrane... |
Q13303 | MYPESTTGSPARLSLRQTGSPGMIYSTRYGSPKRQLQFYRNLGKSGLRVSCLGLGTWVTFGGQITDEMAEQLMTLAYDNGINLFDTAEVYAAGKAEVVLGNIIKKKGWRRSSLVITTKIFWGGKAETERGLSRKHIIEGLKASLERLQLEYVDVVFANRPDPNTPMEETVRAMTHVINQGMAMYWGTSRWSSMEIMEAYSVARQFNLTPPICEQAEYHMFQREKVEVQLPELFHKIGVGAMTWSPLACGIVSGKYDSGIPPYSRASLKGYQWLKDKILSEEGRRQQAKLKELQAIAERLGCTLPQLAIAWCLRNEGVSSV... | Function: Cytoplasmic potassium channel subunit that modulates the characteristics of the channel-forming alpha-subunits . Contributes to the regulation of nerve signaling, and prevents neuronal hyperexcitability (By similarity). Promotes expression of the pore-forming alpha subunits at the cell membrane, and thereby i... |
P62482 | MYPESTTGSPARLSLRQTGSPGMIYSTRYGSPKRQLQFYRNLGKSGLRVSCLGLGTWVTFGGQITDEMAEHLMTLAYDNGINLFDTAEVYAAGKAEVVLGNIIKKKGWRRSSLVITTKIFWGGKAETERGLSRKHIIEGLKASLERLQLEYVDVVFANRPDPNTPMEETVRAMTHVINQGMAMYWGTSRWSSMEIMEAYSVARQFNLIPPICEQAEYHMFQREKVEVQLPELFHKIGVGAMTWSPLACGIVSGKYDSGIPPYSRASLKGYQWLKDKILSEEGRRQQAKLKELQAIAERLGCTLPQLAIAWCLRNEGVSSV... | Function: Cytoplasmic potassium channel subunit that modulates the characteristics of the channel-forming alpha-subunits . Contributes to the regulation of nerve signaling, and prevents neuronal hyperexcitability . Promotes expression of the pore-forming alpha subunits at the cell membrane, and thereby increases channe... |
P97382 | MSRGYGLIFSLKVVFTFLSLPHPPGLQGSLDRLQLEYVDIVFANRSDPNSPMEEIVRAMTYVINQGLALYWGTSRWSAAEIMEAYSMARQFNLIPPVCEQAENHFFQREKVEMQLPELYHKIGVGSVTWSPLACGLITSKYDGRVPDTCKATVKGYQWLKEKVQSEEGKKQQARVMDLLPTARQLGCTVGQLAIAWCLRSEGVSSVLLGVSSAEQLMEHLGSLQVLSQLTPQTVVEIDALLGNKSHSKK | Function: Accessory potassium channel protein which modulates the activity of the pore-forming alpha subunit. Alters the functional properties of Kv2.2 but not Kv2.1.
Sequence Mass (Da): 27749
Sequence Length: 249
Domain: Alteration of functional properties of alpha subunit is mediated through N-terminal domain of beta... |
Q63494 | MQVSIACTEQNLRSRSSEDRLCGPRPGPGGGNGGPVGGGHGNPPGGGGLGSKSRTAVVPRPPAPAGALRESTGRGTGMKYRNLGKSGLRVSCLGLGTWVTFGSQISDETAEDLLTVAYEHGVNLFDTAEVYAAGKAERTLGNILKSKGWRRSSYVITTKIFWGGQAETERGLSRKHIIEGLQGSLDRLQLEYVDIVFANRSDPSSPMEEIVRAMTYVINQGLALYWGTSRWSAAEIMEAYSMARQFNLIPPVCEQAENHFFQREKVEMQLPELYHKIGVGSVTWSPLACSLITSKYDGQVPDACKATVKGYQWLKEKVQS... | Function: Accessory potassium channel protein which modulates the activity of the pore-forming alpha subunit. Alters the functional properties of Kv1.4 but not Kv1.1 or Kv1.5.
Sequence Mass (Da): 43690
Sequence Length: 404
Domain: Alteration of functional properties of alpha subunit is mediated through N-terminal domai... |
Q9PTM4 | MQVSFACTEQTLRSRTSEDRLCPSRPSGGQNGVSMAQTKQRTPPMGAKNHNQVLPLLSHILRESTVKSTGMKYRNLGKSGLRVSCLGLGTWVTFGSQISDEVAENLMTVAYEHGVNLFDTAEVYAAGRAERTLGKILKKKEWRRSSYVVTTKIYWGGQAETERGLSRKHIIEGLRGSLERLQLDYVDIVFANRMDPNSPMEEIVRAMTFVINQGMAMYWGTSRWSAMEIMEAYSVARQFNLIPPVCEQAEYHLFQREKVETQLPELYHKIGVGSMTWSPLACGLITGKYTDTVPEKSRASFKGYHWLKEKAISQEGKKQH... | Function: Accessory potassium channel protein which modulates the activity of the pore-forming alpha subunit. Alters functional properties of Kv1.1 and Kv1.2.
Sequence Mass (Da): 45001
Sequence Length: 401
Domain: Alteration of functional properties of alpha subunit is mediated through N-terminal domain of beta subunit... |
Q00771 | MSFANMFNKLSGQPESYEKKSLYRFGRTLGAGTYGIVREADCSSGKVAVKIILKRNVRGNERMVYDELDLLQKLNHPHIVHFVDWFESKDKFYIVTQLATGGELFDRICEYGKFTEKDASQTIRQVLDAVNYLHQRNIVHRDLKPENLLYLTRDLDSQLVLADFGIAKMLDNPAEVLTSMAGSFGYAAPEVMLKQGHGKAVDIWSLGVITYTLLCGYSPFRSENLTDLIEECRSGRVVFHERYWKDVSKDAKDFILSLLQVDPAQRPTSEEALKHPWLKGESASDRDLLPEIRAYIARSRLKRGIEIIKLANRIEALKMQ... | Function: Calcium/calmodulin-dependent protein kinase . Required in nuclear division cycle for progression from G2 to mitosis. Required for hyphal growth .
PTM: Autophosphorylated in a calcium/calmodulin-dependent manner.
Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Sequence Ma... |
Q14012 | MLGAVEGPRWKQAEDIRDIYDFRDVLGTGAFSEVILAEDKRTQKLVAIKCIAKEALEGKEGSMENEIAVLHKIKHPNIVALDDIYESGGHLYLIMQLVSGGELFDRIVEKGFYTERDASRLIFQVLDAVKYLHDLGIVHRDLKPENLLYYSLDEDSKIMISDFGLSKMEDPGSVLSTACGTPGYVAPEVLAQKPYSKAVDCWSIGVIAYILLCGYPPFYDENDAKLFEQILKAEYEFDSPYWDDISDSAKDFIRHLMEKDPEKRFTCEQALQHPWIAGDTALDKNIHQSVSEQIKKNFAKSKWKQAFNATAVVRHMRKLQ... | Function: Calcium/calmodulin-dependent protein kinase that operates in the calcium-triggered CaMKK-CaMK1 signaling cascade and, upon calcium influx, regulates transcription activators activity, cell cycle, hormone production, cell differentiation, actin filament organization and neurite outgrowth. Recognizes the substr... |
Q63450 | MPGAVEGPRWKQAEDIRDIYDFRDVLGTGAFSEVILAEDKRTQKLVAIKCIAKKALEGKEGSMENEIAVLHKIKHPNIVALDDIYESGGHLYLIMQLVSGGELFDRIVEKGFYTERDASRLIFQVLDAVKYLHDLGIVHRDLKPENLLYYSLDEDSKIMISDFGLSKMEDPGSVLSTACGTPGYVAPEVLAQKPYSKAVDCWSIGVIAYILLCGYPPFYDENDAKLFEQILKAEYEFDSPYWDDISDSAKDFIRHLMEKDPEKRFTCEQALQHPWIAGDTALDKNIHQSVSEQIKKNFAKSKWKQAFNATAVVRHMRKLQ... | Function: Calcium/calmodulin-dependent protein kinase that operates in the calcium-triggered CaMKK-CaMK1 signaling cascade and, upon calcium influx, regulates transcription activators activity, cell cycle, hormone production, cell differentiation, actin filament organization and neurite outgrowth. Recognizes the substr... |
Q9Y899 | MASQVQPGQKPKVQPCRYKTGKTLGAGLYSVVKECVHIDTGQYYAAKVINKRLMVGREHMVRNEIAILKQVSTGHQNILTLVDYFETMNNLYLVTDLALGGELFDRICRKGSYYESDAADLVRAILSAVAYLHDHGIVHRDLKPENLLFRTPEDNADLLIADFGLSRIMDEEQLHVLTTTCGTPGYMAPEIFDKSGHGKPVDIWAIGLITYFMLCGYTPFDRETNLEEVQAIATANFSFTPVEYWRGVSQEARDFIKRCLTVNPKKRMTAHQALQHPWINPPYDTTDDLGSGEDLLPNIKKNFNARRTLHKAIDTVRAIN... | Function: Calcium/calmodulin-dependent protein kinase that operates in the calcium-triggered CaMKK-CaMK1 signaling cascade. Required in G1-phase of the cell cycle for proper timing of the initial nuclear division after germination, but not for subsequent mitoses. Required for the normal temporal regulation of nimX acti... |
Q9NZV8 | MAAGVAAWLPFARAAAIGWMPVASGPMPAPPRQERKRTQDALIVLNVSGTRFQTWQDTLERYPDTLLGSSERDFFYHPETQQYFFDRDPDIFRHILNFYRTGKLHYPRHECISAYDEELAFFGLIPEIIGDCCYEEYKDRRRENAERLQDDADTDTAGESALPTMTARQRVWRAFENPHTSTMALVFYYVTGFFIAVSVIANVVETVPCGSSPGHIKELPCGERYAVAFFCLDTACVMIFTVEYLLRLAAAPSRYRFVRSVMSIIDVVAILPYYIGLVMTDNEDVSGAFVTLRVFRVFRIFKFSRHSQGLRILGYTLKSC... | Function: Voltage-gated potassium channel that mediates transmembrane potassium transport in excitable membranes, primarily in the brain. Mediates the major part of the dendritic A-type current I(SA) in brain neurons (By similarity). This current is activated at membrane potentials that are below the threshold for acti... |
Q63881 | MAAGVAAWLPFARAAAIGWMPVASGPMPAPPRQERKRTQDALIVLNVSGTRFQTWQDTLERYPDTLLGSSERDFFYHPETQQYFFDRDPDIFRHILNFYRTGKLHYPRHECISAYDEELAFFGLIPEIIGDCCYEEYKDRRRENAERLQDDADTDNTGESALPTMTARQRVWRAFENPHTSTMALVFYYVTGFFIAVSVIANVVETVPCGSSPGHIKELPCGERYAVAFFCLDTACVMIFTVEYLLRLAAAPSRYRFVRSVMSIIDVVAILPYYIGLVMTDNEDVSGAFVTLRVFRVFRIFKFSRHSQGLRILGYTLKSC... | Function: Voltage-gated potassium channel that mediates transmembrane potassium transport in excitable membranes, primarily in the brain, but also in rodent heart . Mediates the major part of the dendritic A-type current I(SA) in brain neurons . This current is activated at membrane potentials that are below the thresh... |
Q60409 | MILPNSTAVMPFLTTVWQGTVQPSSNASGLARRSPLRDDGKLEALYILMVLGFFGFFTLGIMLSYIRSKKLEHSHDPFNVYIESDTWQEKDKAFFQARVLENCRSCCVIENQLTVEQPNTYLPEL | Function: Ancillary protein that assembles as a beta subunit with a voltage-gated potassium channel complex of pore-forming alpha subunits. Modulates the gating kinetics and enhances stability of the channel complex. Assembled with KCNB1 modulates the gating characteristics of the delayed rectifier voltage-dependent po... |
P15382 | MILSNTTAVTPFLTKLWQETVQQGGNMSGLARRSPRSSDGKLEALYVLMVLGFFGFFTLGIMLSYIRSKKLEHSNDPFNVYIESDAWQEKDKAYVQARVLESYRSCYVVENHLAIEQPNTHLPETKPSP | Function: Ancillary protein that assembles as a beta subunit with a voltage-gated potassium channel complex of pore-forming alpha subunits. Modulates the gating kinetics and enhances stability of the channel complex. Assembled with KCNB1 modulates the gating characteristics of the delayed rectifier voltage-dependent po... |
Q28705 | MIPPNATAVMPFLTTLGEETAHLQGSSATSLARRGPLGDDGQMEALYILMVLGFFGFFTLGIMLSYIRSQKLEHSHDPFNVYIEANDWQEKDRAYFQARVLESCRGCYVLENQLAVEHPDTHLPELKPSL | Function: Ancillary protein that assembles as a beta subunit with a voltage-gated potassium channel complex of pore-forming alpha subunits. Modulates the gating kinetics and enhances stability of the channel complex. Assembled with KCNB1 modulates the gating characteristics of the delayed rectifier voltage-dependent po... |
P63160 | MTTLANLTQTLEDAFKKVFITYMDSWRRNTTAEQQALQARVDAENFYYVILYLMVMIGMFAFIVVAILVSTVKSKRREHSQDPYHQYIVEDWQQKYRSQILHLEDSKATIHENLGATGFTVSP | Function: Ancillary protein that assembles as a beta subunit with a voltage-gated potassium channel complex of pore-forming alpha subunits. Modulates the gating kinetics and enhances stability of the channel complex. Assembled with KCNB1 modulates the gating characteristics of the delayed rectifier voltage-dependent po... |
Q9ULS6 | MTGQSLWDVSEANVEDGEIRINVGGFKRRLRSHTLLRFPETRLGRLLLCHSREAILELCDDYDDVQREFYFDRNPELFPYVLHFYHTGKLHVMAELCVFSFSQEIEYWGINEFFIDSCCSYSYHGRKVEPEQEKWDEQSDQESTTSSFDEILAFYNDASKFDGQPLGNFRRQLWLALDNPGYSVLSRVFSILSILVVMGSIITMCLNSLPDFQIPDSQGNPGEDPRFEIVEHFGIAWFTFELVARFAVAPDFLKFFKNALNLIDLMSIVPFYITLVVNLVVESTPTLANLGRVAQVLRLMRIFRILKLARHSTGLRSLGA... | Function: Potassium channel subunit that does not form functional channels by itself. Can form functional heterotetrameric channels with KCNB1 and KCNB2; modulates the delayed rectifier voltage-gated potassium channel activation and deactivation rates of KCNB1 and KCNB2.
Location Topology: Multi-pass membrane protein
S... |
O35174 | MTRQSLWDVSDTDVEDGEIRINVGGFKRRLRSHTLLRFPETRLGRLLLCHSREAILELCDDYDDVQREFYFDRNPELFPYVLHFYHTGKLHVMAELCVFSFSQEIEYWGINEFFIDSCCSYSYHGRKVEPEQEKWDEQSDQESTTSSFDEILAFYNDASKFDGQPLGNFRRQLWLALDNPGYSVLSRVFSVLSILVVLGSIITMCLNSLPDFQIPDSQGNPGEDPRFEIVEHFGIAWFTFELVARFAVAPDFLKFFKNALNLIDLMSIVPFYITLVVNLVVESSPTLANLGRVAQVLRLMRIFRILKLARHSTGLRSLGA... | Function: Potassium channel subunit that does not form functional channels by itself. Can form functional heterotetrameric channels with KCNB1 and KCNB2; modulates the delayed rectifier voltage-gated potassium channel activation and deactivation rates of KCNB1 and KCNB2 .
Location Topology: Multi-pass membrane protein
... |
Q9BQ31 | MVFGEFFHRPGQDEELVNLNVGGFKQSVDQSTLLRFPHTRLGKLLTCHSEEAILELCDDYSVADKEYYFDRNPSLFRYVLNFYYTGKLHVMEELCVFSFCQEIEYWGINELFIDSCCSNRYQERKEENHEKDWDQKSHDVSTDSSFEESSLFEKELEKFDTLRFGQLRKKIWIRMENPAYCLSAKLIAISSLSVVLASIVAMCVHSMSEFQNEDGEVDDPVLEGVEIACIAWFTGELAVRLAAAPCQKKFWKNPLNIIDFVSIIPFYATLAVDTKEEESEDIENMGKVVQILRLMRIFRILKLARHSVGLRSLGATLRHS... | Function: Potassium channel subunit that does not form functional channels by itself. Can form functional heterotetrameric channels with KCNB1; modulates the delayed rectifier voltage-gated potassium channel activation and deactivation rates of KCNB1 . Heterotetrameric channel activity formed with KCNB1 show increased ... |
Q8I4B0 | MRFGGQRRCIESSDDNDSIDSMSIQQKNKEKEEWKWAQSLARRLEQVLNVHPEKYQNGCSSQRPSRQPSPVEQLAPIRSHSADFGRAAEMASGNSEEGKGMLLRNGDDRIRLPSPQRGTPDTSSTQGHPYTDQIVTINVSGMRFQTFESTLSRYPNSLLGDRNKRQHFFVSDTNEFFFDRHRTTSSSFTFEIRNYLFESILYIYQSGGRVKRPEIVPIDIFLKEMRFFQMGDDLLEEFWIAEGYEKPKEVMMPNNKTQRKIWELMEYPDSSLSARIIAFISIAVIALSIISFCWETVPSDIEEKPINNSATAELLDEMDE... | Function: Mediates the voltage-dependent potassium ion permeability of excitable membranes. Has an important role in repolarization and in regulating the pattern of action potential firing. Isoform a expresses currents in a more depolarized voltage range than isoform d.
Location Topology: Multi-pass membrane protein
Se... |
Subsets and Splits
No community queries yet
The top public SQL queries from the community will appear here once available.