ids stringlengths 6 10 | seqs stringlengths 11 1.02k | texts stringlengths 108 11.1k |
|---|---|---|
Q7TSU7 | MLASALLVFLCCFKGHAGSSPHFLQQPEDMVVLLGEEARLPCALGAYRGLVQWTKDGLALGGERDLPGWSRYWISGNSASGQHDLHIKPVELEDEASYECQASQAGLRSRPAQLHVMVPPEAPQVLGGPSVSLVAGVPGNLTCRSRGDSRPAPELLWFRDGIRLDGSSFHQTTLKDKATGTVENTLFLTPSSHDDGATLICRARSQALPTGRDTAVTLSLQYPPMVTLSAEPQTVQEGEKVTFLCQATAQPPVTGYRWAKGGSPVLGARGPRLEVVADATFLTEPVSCEVSNAVGSANRSTALEVLYGPILQAKPKSVSVDVGKDASFSCVWRGNPLPRITWTRMGGSQVLSSGPTLRLPSVALEDAGDYVCRAEPRRTGLGGGKAQARLTVNAPPVVTALQPAPAFLRGPARLQCVVFASPAPDSVVWSWDEGFLEAGSLGRFLVEAFPAPEVEGGQGPGLISVLHISGTQESDFTTGFNCSARNRLGEGRVQIHLGRRDLLPTVRIVAGAASAATSLLMVITGVVLCCWRHGSLSKQKNLVRIPGSSEGSSSRGPEEETGSSEDRGPIVHTDHSDLVLEEKEALETKDPTNGYYRVRGVSVSLSLGEAPGGGLFLPPPSPIGLPGTPTYYDFKPHLDLVPPCRLYRARAGYLTTPHPRAFTSYMKPTSFGPPELSSGTPPFPYATLSPPSHQRLQTHV | Function: May regulate basal insulin secretion.
PTM: N-glycosylated.
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 74529
Sequence Length: 700
Subcellular Location: Cell membrane
|
Q8BR86 | MRPFQLDLLFLCFFLFSQELGLQKRGCCLVLGYMAKDKFRRMNEGQVYSFSQQPQDQVVVSGQPVTLLCAIPEYDGFVLWIKDGLALGVGRDLSSYPQYLVVGNHLSGEHHLKILRAELQDDAVYECQAIQAAIRSRPARLTVLVPPDDPIILGGPVISLRAGDPLNLTCHADNAKPAASIIWLRKGEVINGATYSKTLLRDGKRESIVSTLFISPGDVENGQSIVCRATNKAIPGGKETSVTIDIQHPPLVNLSVEPQPVLEDNIVTFHCSAKANPAVTQYRWAKRGHIIKEASGELYRTTVDYTYFSEPVSCEVTNALGSTNLSRTVDVYFGPRMTSEPQSLLVDLGSDAVFSCAWIGNPSLTIVWMKRGSGVVLSNEKTLTLKSVRQEDAGKYVCRAVVPRVGAGEREVTLTVNGPPIISSTQTQHALHGEKGQIKCFIRSTPPPDRIAWSWKENVLESGTSGRYTVETVNTEEGVISTLTISNIVRADFQTIYNCTAWNSFGSDTEIIRLKEQGSEMKSGAGLEAESVPMAVIIGVAVGAGVAFLVLMATIVAFCCARSQRNLKGVVSAKNDIRVEIVHKEPSSGREAEDHTTIKQLMMDRGEFQQDSVLKQLEVLKEEEKEFQNLKDPTNGYYSVNTFKEHHSTPTISLSSCQPDLRPTGKQRVPTGMSFTNIYSTLSGQGRLYDYGQRFVLGMGSSSIELCEREFQRGSLSDSSSFLDTQCDSSVSSSGKQDGYVQFDKASKASASSSHHSQSSSQNSDPSRPLQRRMQTHV | Function: Synaptic adhesion molecule required for the formation of target-specific synapses . Required for formation of target-specific synapses at hippocampal mossy fiber synapses. Required for formation of mossy fiber filopodia, the synaptic structures connecting dentate granule and GABA neurons. Probably acts as a homophilic adhesion molecule that promotes trans-cellular interactions and stabilize mossy fiber filipodia contact and subsequent synapse formation . Required for the coalescence of vomeronasal sensory neuron axons . May be involved in the hematopoietic supportive capacity of stroma cells; the secreted extracellular domain is directly responsible for supporting hematopoietic stem cells .
PTM: Undergoes proteolysis by a metalloprotease and gives rise to a soluble form.
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 85405
Sequence Length: 778
Subcellular Location: Cell membrane
|
Q5ZII6 | MSAIFNFQSLLTVILLLICTCAYIRSLAPSLLDKNKTGLLGIFWKCARIGERKSPYVAVCCVVMAFSILFVQ | Function: Involved in the early part of the secretory pathway.
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 8004
Sequence Length: 72
Subcellular Location: Golgi apparatus membrane
|
Q5BJC2 | MSAIFNFQSLLTVILLLICTCAYIRSLTPSLLDKNKTGFLGIFWKCARIGERKSPYVAFCCIVMALTILFSE | Function: Involved in the early part of the secretory pathway.
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 8099
Sequence Length: 72
Subcellular Location: Golgi apparatus membrane
|
Q8TBQ9 | MSAIFNFQSLLTVILLLICTCAYIRSLAPSLLDRNKTGLLGIFWKCARIGERKSPYVAVCCIVMAFSILFIQ | Function: Involved in the early part of the secretory pathway.
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 8060
Sequence Length: 72
Subcellular Location: Golgi apparatus membrane
|
Q9CR64 | MSAIFNFQSLLTVILLLICTCAYIRSLAPSILDRNKTGLLGIFWKCARIGERKSPYVAICCIVMAFSILFIQ | Function: Involved in the early part of the secretory pathway.
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 8074
Sequence Length: 72
Subcellular Location: Golgi apparatus membrane
|
B5G2S6 | MSAIFNFQSLLTVILLLICTCAYIRSLAPSLLDKNKSGLLGIFWKCARIGERKSPYVAVCCVVMAFSILFMQ | Function: Involved in the early part of the secretory pathway.
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 8022
Sequence Length: 72
Subcellular Location: Golgi apparatus membrane
|
A2VDC5 | MSAIFNFQSLLIVILLLICTCAYLRSLVPNLLDKNKTGVLGIFWKCARIGERKSPYVAVCCVVMAFSILFMQ | Function: Involved in the early part of the secretory pathway.
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 8089
Sequence Length: 72
Subcellular Location: Golgi apparatus membrane
|
Q6AZW1 | MTNVYSFDGILVFGLLFICTCAYLKKVPRLNSWLLSEKKGVWGVFYKAAVIGTRLHVVVAASCLCMAFYLIFLK | Function: Involved in the early part of the secretory pathway.
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 8342
Sequence Length: 74
Subcellular Location: Golgi apparatus membrane
|
Q9NRX6 | MTNVYSLDGILVFGLLFVCTCAYFKKVPRLKTWLLSEKKGVWGVFYKAAVIGTRLHAAVAIACVVMAFYVLFIK | Function: Involved in the early part of the secretory pathway.
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 8294
Sequence Length: 74
Subcellular Location: Golgi apparatus membrane
|
Q80X45 | MTNVYSLDGILVFGLLFVCTCAYFKKVPRLKTWLLSEKKGVWGVFYKAAVIGTRLHAAVAIACIVMAFYVLFIK | Function: Involved in the early part of the secretory pathway.
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 8308
Sequence Length: 74
Subcellular Location: Golgi apparatus membrane
|
Q28GL2 | MTNVYSLDGLLVFALLFVCTCAYFRKVPRLRSWLLSEKKGVWGVFYKAAVIGSRLHLAVSISCIAMAFYVLFIK | Function: Involved in the early part of the secretory pathway.
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 8396
Sequence Length: 74
Subcellular Location: Golgi apparatus membrane
|
P13159 | MASGTIPVQNEEIIKSQVNTVRIYIDGAYGIGKSLTAKYLVRADENRPGYTYYFPEPMLYWRSLFETDVVGGIYAVQDRKRRGELSAEDAAYITAHYQARFAAPYLLLHSRLSTITGYQKVVCEEHPDVTLIIDRHPLASLVCFPLARYFVGDMTLGSVLSLMATLPREPPGGNLVVTTLNIEEHLKRLRGRSRTGEQIDMKLIHALRNVYMMLVHTKKFLTKNTSWRDGWGKLKIFSHYERNRLVETTIVSDSTESDLCDTLFSVFKARELSDQNGDLLDMHAWVLDGLMETLQNLQIFTLNLEGTPDECAAALGALRQDMDMTFIAACDMHRISEALTIYH | Function: Catalyzes the transfer of the gamma-phospho group of ATP to thymidine to generate dTMP in the salvage pathway of pyrimidine synthesis. The dTMP serves as a substrate for DNA polymerase during viral DNA replication. Allows the virus to be reactivated and to grow in non-proliferative cells lacking a high concentration of phosphorylated nucleic acid precursors.
Catalytic Activity: ATP + thymidine = ADP + dTMP + H(+)
Sequence Mass (Da): 38923
Sequence Length: 343
EC: 2.7.1.21
|
Q5NH50 | MAKLYFRYSAMDAGKTLDLLKVAYNYEDRGRKPLVLTSAIDKRAGLNKVKSRIGINQDAYSLTDRDNIFEFVENYNSSNKIDCVLIDEIHFFTQEQVWQLAEIVDELNIPVICYGLRTNYLGQPFETAALLLAIADTLEEVKTICHCGKKASFNMMVQNGKAIKQGNPIVVDDDSLKEIDTKYVSVCRKHWKEGVYE | Catalytic Activity: ATP + thymidine = ADP + dTMP + H(+)
Sequence Mass (Da): 22473
Sequence Length: 197
Subcellular Location: Cytoplasm
EC: 2.7.1.21
|
Q9E6P5 | MSEPQSWSVMASQMTSAQLIRVYLDGSMGIGKTSMLNEIPTHSLMGVPVLKVFEPMKYWRYYFTDLVTTVNDTCDRRRRGEFSLFQSSMIVTALQSKFADPYLVFHERLSSKCHRITGTRGNPSLILILDRHPISATVCFPIARHLTGDCSLEMLISMIIRLPQEPPGCNLVIVDLHDEKEHVSRLSSRNRTGEKTDLLMLRALNAVYSCLVDTIMYANHICPYSKDEWESEWLDLPWFDTSLATTFINEPRTDYRGSRVSLHHTLLAIFKRRELCAEDGSLSTTHAWILWGLLMKLRNINVERFNITGLSTTKCVESFMDTMSERLVTHMSWNDAFEIEADVLAYNKEMAM | Function: Catalyzes the transfer of the gamma-phospho group of ATP to thymidine to generate dTMP in the salvage pathway of pyrimidine synthesis. The dTMP serves as a substrate for DNA polymerase during viral DNA replication. Allows the virus to be reactivated and to grow in non-proliferative cells lacking a high concentration of phosphorylated nucleic acid precursors.
Catalytic Activity: ATP + thymidine = ADP + dTMP + H(+)
Sequence Mass (Da): 40410
Sequence Length: 352
EC: 2.7.1.21
|
P44309 | MAKLYFYYSTMNAGKSTTLLQSSYNYRERDMNTLVYTAAIDDRFGVGKVTSRIGISQDAFLFRSETNLFDEINEHLKKEKVHCVLVDEAQFLSKQQVYQLSDVVDKLKIPVLCYGLRTDFQAELFEGSKYLLAWADQLEELKTICYCGRKANFVLRLNDQGEVIKEGAQIQIGGNDSYLSVCRLHYKEKCGQI | Catalytic Activity: ATP + thymidine = ADP + dTMP + H(+)
Sequence Mass (Da): 22177
Sequence Length: 193
Subcellular Location: Cytoplasm
EC: 2.7.1.21
|
Q18J88 | MRAITNSGWIEVVTGSMFSGKTEELLRRLRRAEIAGQSIAVFKPAVDDRYGETTVGSHVGRQWEAAVVPNEGEDIWNIKHELSKKKQNHRTTTQCRSGDGTNNPGGVIPSNDDSVDVVAIDEANFFSTELVSVCESLANDGYRVVVSGTDQTYRGEPFEPLPQLMAVAEYVDKLQAICTQCGEPATRNQRLVDDSPAHIDDPTIVVGADETYEARCRNCHILRHE | Catalytic Activity: ATP + thymidine = ADP + dTMP + H(+)
Sequence Mass (Da): 24833
Sequence Length: 225
Subcellular Location: Cytoplasm
EC: 2.7.1.21
|
Q9QNF7 | MASYPCHQHASAFDQAARSRGHSNRRTALRPRRQQEATEVRLEQKMPTLLRVYIDGPHGMGKTTTTQLLVALGSRDDIVYVPEPMTYWQVLGASETIANIYTTQHRLDQGEISAGDAAVVMTSAQITMGMPYAVTDAVLAPHIGGEAGSSHAPPPALTLIFDRHPIAALLCYPAARYLMGSMTPQAVLAFVALIPPTLPGTNIVLGALPEDRHIDRLAKRQRPGERLDLAMLAAIRRVYGLLANTVRYLQGGGSWREDWGQLSGTAVPPQGAEPQSNAGPRPHIGDTLFTLFRAPELLAPNGDLYNVFAWALDVLAKRLRPMHVFILDYDQSPAGCRDALLQLTSGMVQTHVTTPGSIPTICDLARTFAREMGEAN | Function: Catalyzes the transfer of the gamma-phospho group of ATP to thymidine to generate dTMP in the salvage pathway of pyrimidine synthesis. The dTMP serves as a substrate for DNA polymerase during viral DNA replication. Allows the virus to be reactivated and to grow in non-proliferative cells lacking a high concentration of phosphorylated nucleic acid precursors.
Catalytic Activity: ATP + thymidine = ADP + dTMP + H(+)
Sequence Mass (Da): 40897
Sequence Length: 376
EC: 2.7.1.21
|
Q8N5S9 | MEGGPAVCCQDPRAELVERVAAIDVTHLEEADGGPEPTRNGVDPPPRARAASVIPGSTSRLLPARPSLSARKLSLQERPAGSYLEAQAGPYATGPASHISPRAWRRPTIESHHVAISDAEDCVQLNQYKLQSEIGKGAYGVVRLAYNESEDRHYAMKVLSKKKLLKQYGFPRRPPPRGSQAAQGGPAKQLLPLERVYQEIAILKKLDHVNVVKLIEVLDDPAEDNLYLVFDLLRKGPVMEVPCDKPFSEEQARLYLRDVILGLEYLHCQKIVHRDIKPSNLLLGDDGHVKIADFGVSNQFEGNDAQLSSTAGTPAFMAPEAISDSGQSFSGKALDVWATGVTLYCFVYGKCPFIDDFILALHRKIKNEPVVFPEEPEISEELKDLILKMLDKNPETRIGVPDIKLHPWVTKNGEEPLPSEEEHCSVVEVTEEEVKNSVRLIPSWTTVILVKSMLRKRSFGNPFEPQARREERSMSAPGNLLVKEGFGEGGKSPELPGVQEDEAAS | Function: Calcium/calmodulin-dependent protein kinase that belongs to a proposed calcium-triggered signaling cascade involved in a number of cellular processes. Phosphorylates CAMK1, CAMK1D, CAMK1G and CAMK4. Involved in regulating cell apoptosis. Promotes cell survival by phosphorylating AKT1/PKB that inhibits pro-apoptotic BAD/Bcl2-antagonist of cell death.
PTM: Appears to be autophosphorylated in a Ca(2+)/calmodulin-dependent manner. Phosphorylated at multiple sites by PRCAKA/PKA. Phosphorylation of Ser-458 is blocked upon binding to Ca(2+)/calmodulin. In vitro, phosphorylated by CAMK1 and CAMK4 (By similarity).
Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Sequence Mass (Da): 55735
Sequence Length: 505
Domain: The autoinhibitory domain overlaps with the calmodulin binding region and may be involved in intrasteric autoinhibition.
Subcellular Location: Cytoplasm
EC: 2.7.11.17
|
P97756 | MERSPAVCCQDPRAELVERVAAISVAHLEEAEEGPEPASNGVDPPPRARAASVIPGSASRPTPVRPSLSARKFSLQERPAGSCLEAQVGPYSTGPASHMSPRAWRRPTIESHHVAISDTEDCVQLNQYKLQSEIGKGAYGVVRLAYNEREDRHYAMKVLSKKKLLKQYGFPRRPPPRGSQAPQGGPAKQLLPLERVYQEIAILKKLDHVNVVKLIEVLDDPAEDNLYLVFDLLRKGPVMEVPCDKPFPEEQARLYLRDIILGLEYLHCQKIVHRDIKPSNLLLGDDGHVKIADFGVSNQFEGNDAQLSSTAGTPAFMAPEAISDTGQSFSGKALDVWATGVTLYCFVYGKCPFIDEYILALHRKIKNEAVVFPEEPEVSEELKDLILKMLDKNPETRIGVSDIKLHPWVTKHGEEPLPSEEEHCSVVEVTEEEVKNSVKLIPSWTTVILVKSMLRKRSFGNPFEPQARREERSMSAPGNLLLKEGCGEGGKSPELPGVQEDEAAS | Function: Calcium/calmodulin-dependent protein kinase that belongs to a proposed calcium-triggered signaling cascade involved in a number of cellular processes. Phosphorylates CAMK1, CAMK1D, CAMK1G and CAMK4. Involved in regulating cell apoptosis. Promotes cell survival by phosphorylating AKT1/PKB that inhibits pro-apoptotic BAD/Bcl2-antagonist of cell death.
PTM: Appears to be autophosphorylated. Phosphorylated at multiple sites by PRCAKA/PKA. Phosphorylation of Ser-458 is blocked upon binding to Ca(2+)/calmodulin. May be phosphorylated by CAMK1 and CAMK4.
Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Sequence Mass (Da): 55908
Sequence Length: 505
Domain: The autoinhibitory domain overlaps with the calmodulin binding region and may be involved in intrasteric autoinhibition.
Subcellular Location: Cytoplasm
EC: 2.7.11.17
|
Q96RR4 | MSSCVSSQPSSNRAAPQDELGGRGSSSSESQKPCEALRGLSSLSIHLGMESFIVVTECEPGCAVDLGLARDRPLEADGQEVPLDTSGSQARPHLSGRKLSLQERSQGGLAAGGSLDMNGRCICPSLPYSPVSSPQSSPRLPRRPTVESHHVSITGMQDCVQLNQYTLKDEIGKGSYGVVKLAYNENDNTYYAMKVLSKKKLIRQAGFPRRPPPRGTRPAPGGCIQPRGPIEQVYQEIAILKKLDHPNVVKLVEVLDDPNEDHLYMVFELVNQGPVMEVPTLKPLSEDQARFYFQDLIKGIEYLHYQKIIHRDIKPSNLLVGEDGHIKIADFGVSNEFKGSDALLSNTVGTPAFMAPESLSETRKIFSGKALDVWAMGVTLYCFVFGQCPFMDERIMCLHSKIKSQALEFPDQPDIAEDLKDLITRMLDKNPESRIVVPEIKLHPWVTRHGAEPLPSEDENCTLVEVTEEEVENSVKHIPSLATVILVKTMIRKRSFGNPFEGSRREERSLSAPGNLLTKKPTRECESLSELKEARQRRQPPGHRPAPRGGGGSALVRGSPCVESCWAPAPGSPARMHPLRPEEAMEPE | Function: Calcium/calmodulin-dependent protein kinase belonging to a proposed calcium-triggered signaling cascade involved in a number of cellular processes. Isoform 1, isoform 2 and isoform 3 phosphorylate CAMK1 and CAMK4. Isoform 3 phosphorylates CAMK1D. Isoform 4, isoform 5 and isoform 6 lacking part of the calmodulin-binding domain are inactive. Efficiently phosphorylates 5'-AMP-activated protein kinase (AMPK) trimer, including that consisting of PRKAA1, PRKAB1 and PRKAG1. This phosphorylation is stimulated in response to Ca(2+) signals (By similarity). Seems to be involved in hippocampal activation of CREB1 (By similarity). May play a role in neurite growth. Isoform 3 may promote neurite elongation, while isoform 1 may promoter neurite branching.
PTM: Autophosphorylated and phosphorylated by PKA. Each isoform may show a different pattern of phosphorylation.
Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Sequence Mass (Da): 64746
Sequence Length: 588
Domain: The autoinhibitory domain overlaps with the calmodulin binding region and may be involved in intrasteric autoinhibition.
Subcellular Location: Nucleus
EC: 2.7.11.17
|
Q8C078 | MSSCVSSQPTSDRVAPQDELGSGGGSREGQKPCEALRGLSSLSIHLGMESFIVVTECEPGRGVDLNLARDQPPEADGQELPLEASDPESRSPLSGRKMSLQEPSQGGPASSSNSLDMNGRCICPSLSYSPASSPQSSPRMPRRPTVESHHVSITGLQDCVQLNQYTLKDEIGKGSYGVVKLAYNENDNTYYAMKVLSKKKLIRQAGFPRRPPPRGARPAPGGCIQPRGPIEQVYQEIAILKKLDHPNVVKLVEVLDDPNEDHLYMVFELVNQGPVMEVPTLKPLSEDQARFYFQDLIKGIEYLHYQKIIHRDIKPSNLLVGEDGHIKIADFGVSNEFKGSDALLSNTVGTPAFMAPESLSETRKIFSGKALDVWAMGVTLYCFVFGQCPFMDERIMCLHSKIKSQALEFPDQPDIAEDLKDLITRMLDKNPESRIVVPEIKLHPWVTRHGAEPLPSEDENCTLVEVTEEEVENSVKHIPSLATVILVKTMIRKRSFGNPFEGSRREERSLSAPGNLLTKKPTREWEPLSEPKEARQRRQPPGPRAGPCGGGGSALVKGGPCVESWGAPAPGSPPRMPPLQPEEVMEPE | Function: Calcium/calmodulin-dependent protein kinase belonging to a proposed calcium-triggered signaling cascade involved in a number of cellular processes. Phosphorylates CAMK1, CAMK4 and CAMK1D (By similarity). Efficiently phosphorylates 5'-AMP-activated protein kinase (AMPK) trimer, including that consisting of PRKAA1, PRKAB1 and PRKAG1. This phosphorylation is stimulated in response to Ca(2+) signals (By similarity). May play a role in neurite growth. Isoform 2 may promote neurite elongation, while isoform 1 may promoter neurite branching (By similarity). May be involved in hippocampal activation of CREB1.
PTM: Autophosphorylated and phosphorylated by PKA. Each isoform may show a different pattern of phosphorylation.
Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Sequence Mass (Da): 64618
Sequence Length: 588
Domain: The autoinhibitory domain overlaps with the calmodulin binding region and may be involved in intrasteric autoinhibition.
Subcellular Location: Nucleus
EC: 2.7.11.17
|
O88831 | MSSCVSSQPTSDRAAPQDELGSGGVSRESQKPCEALRGLSSLSIHLGMESFIVVTECEPGRGVDLSLARDQPLEADGQELPLDASEPESRSLLSGGKMSLQERSQGGPASSSSLDMNGRCICPSLSYSPASSPQSSPRMPRRPTVESHHVSITGLQDCVQLNQYTLKDEIGKGSYGVVKLAYNENDNTYYAMKVLSKKKLIRQAGFPRRPPPRGTRPAPGGCIQPRGPIEQVYQEIAILKKLDHPNVVKLVEVLDDPNEDHLYMVFELVNQGPVMEVPTLKPLSEDQARFYFQDLIKGIEYLHYQKIIHRDIKPSNLLVGEDGHIKIADFGVSNEFKGSDALLSNTVGTPAFMAPESLSETRKIFSGKALDVWAMGVTLYCFVFGQCPFMDERIMCLHSKIKSQALEFPDQPDIAEDLKDLITRMLDKNPESRIVVPEIKLHPWVTRHGAEPLPSEDENCTLVEVTEEEVENSVKHIPSLATVILVKTMIRKRSFGNPFEGSRREERSLSAPGNLLTKKPTREWEPLSEPKEARQRRQPPGPRASPCGGGGSALVKGGPCVESCGAPAPGSPPRTPPQQPEEAMEPE | Function: Calcium/calmodulin-dependent protein kinase belonging to a proposed calcium-triggered signaling cascade involved in a number of cellular processes. Phosphorylates CAMK1 and CAMK4. Phosphorylates CAMK1D (By similarity). Seems to be involved in hippocampal activation of CREB1 (By similarity). Efficiently phosphorylates 5'-AMP-activated protein kinase (AMPK) trimer, including that consisting of PRKAA1, PRKAB1 and PRKAG1. This phosphorylation is stimulated in response to Ca(2+) signals. May play a role in neurite growth. Isoform 2 may promote neurite elongation, while isoform 1 may promoter neurite branching.
PTM: Phosphorylated by PKA (By similarity). Each isoform may show a different pattern of phosphorylation (By similarity). Autophosphorylated.
Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Sequence Mass (Da): 64446
Sequence Length: 587
Domain: The autoinhibitory domain overlaps with the calmodulin binding region and may be involved in intrasteric autoinhibition.
Subcellular Location: Nucleus
EC: 2.7.11.17
|
Q9Y898 | MANEGAGSLQQDASPGSSARPEPYPRPSPARYASTPSFESPQRHHRRNPIARRPVKETLNARSEYTLSQDDGTADDRINQYVIKQEIGRGSFGAVHVAVDQYGNEYAVKEFSKARLRKRAKSQLLRQSRGPKRSSRWPKLPFSSPGTGTWRRRDEKCSLFYQRRNCHYEEVTPQQSSILDRGTGRPDPRFSYMVMEMCKKGVVMKVTLEERADPYDDERCRCWFRDLILGIEYLHAQGIVHRDIKPDNCLITNDDVLKVVDFGVSEMFVLNSDMFTAKSAGSPAFLPPELCVVKHGDVSGKAADIWSMGVTLYCLRYGKLPFEEHSIIELYDAIKNRPIVCDGETDEVFKDLMLRILEKDPAKRIQMDELREHPWVTKNGMDPLLPKSENTAEIVDLPTEEEMFSAITKNFGHVLAVMKAAKKFKSLQGPTRASTPIQSILGQEYETHFVEPPTQMDPEESVSLPSPLPYKKTQSLNTYNRRAWERDDVVKGYHPQRRKLSLVLRQRAANRVLRTALF | Function: Calcium/calmodulin-dependent protein kinase that operates in the calcium-triggered CaMKK-CaMK1 signaling cascade. Phosphorylates and activates cmkB in vitro. Required in G1-phase of the cell cycle for proper timing of the initial nuclear division after germination as well as for subsequent nuclear division cycles. Required for the normal temporal regulation of nimX activity.
Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Sequence Mass (Da): 59153
Sequence Length: 518
Domain: The autoinhibitory domain overlaps with the calmodulin binding region and may be involved in intrasteric autoinhibition.
EC: 2.7.11.17
|
Q3Y416 | MKNTFARYSLTIPSIPENVISHLRQWNEWMVGDTSDDSPGPSSTVSTMTTTGTVDRRSLLSAASMVRQQSDTTGVRRLVRARAVQEDDEAGPHSSNNLAATMSPNLSRPTRYVKSVSQQRSESYIQLNQYRLMEEIGQGSYGIVKLAYNEEDKNLYALKVLDKMKLLKNFACFRQPPPRRNKENAAPSVLRNPLQLVQKEIAILKKLSHPNVVKLVEVLDDPNDNYLYMVFEFVEKGSILEIPTDKPLDEDTAWSYFRDTLCGLEYLHYQKIVHRDIKPSNLLLSDIGQVKIADFGVSCEFEGIDAFLSGTAGTPAFMAPEALTEGANHFYSGRAQDIWSLGITLYAFVIGTVPFVDNYIIALHKKIKNDPIVFPEAPILSEALQDIILGMLKKDPGHRLMLHEVKVHTWVTRDGTVPMSSEQENCHLVTVTEEEIENCVRVIPRLDTLILVKAMGHRKRFGNPFRNKLSAQSSIRDRRKSSSVKDPTYVPPPNSPPATSNNNLNSTKVDRPEIKCIEMNLSGLTLKVDEAMQSKVESARQ | Function: Calcium/calmodulin-dependent protein kinase which phosphorylates cmk-1 . Component of a calcium-triggered signaling cascade involved in CRE-mediated transcriptional activation, probably through cmk-1-mediated crh-1/CREB phosphorylation .
Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Sequence Mass (Da): 60804
Sequence Length: 541
Domain: The autoinhibitory domain overlaps with the calmodulin binding region and may be involved in intrasteric autoinhibition.
EC: 2.7.11.17
|
Q6FJ85 | MPEHEERHSHGVNRSLSLGSSMRSLFKSQRSRGPSDRGANGTPGPAQKVDIRVDTASASREHTPVVHKTPQSANPELQQPRHHLGLPNILKLNLTPTNSNPQSKSGSPVSQNTSQESLITDTDIEVEDYRPSKDSRRTVRNASPMSSNGNLPINANTVIGPDTSSNNIDSMLDGTGLRPFYEEADSSDYIENLRSFPLPTGHYAPGFIQPPKSPTSSRVPSRSNSRKGREHAGTVSAAQLPRYNETPGKCILDLEYFKLYEDGHHVHTLKVMTSVNSDANGNSHNHASKNDGHLDLPKGDDGSVVRQKSKFSLSGFFKPHSKEDIANADEKLKYAVSLLPRNKICSKVETDRDTFAPVFTKTRSHVQSGSDDSSDDDEELDDPSIPKIVNKNAAVGSQELKLINNLSEKIRMGLSTAAKNKHNQSSKHRTPSGAGVQDENQPAFADLYGKCVAVVGHGAYGVVKVCARTRDEKDDLPATKTYMDSKKIYFAVKELKPRPSDPIEKFSTRITSEFIIGHSLSHYYDKNGEQSAPNILSIIDLLEYNDTFIEVMEFCPAGDLYSLLTARKNKIGKPLHPLEADCFMKQLLKGIQFMHDHGVAHCDLKPENILLHPNGLLKICDFGTSCVFQTAWERHVHFQTGLQGSEPYVAPEEYNPKKEYDPRLVDCWSIGIVYCTMIMGHYLWRNAARGKDSLYDSFYEEMASKKEFYVFEELRHINQEINRLRRIALYQIFQPNPEKRISIDKLLQTGWMRHTKCCVPYKNIPR | Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Sequence Mass (Da): 85781
Sequence Length: 766
Subcellular Location: Cytoplasm
EC: 2.7.11.1
|
P36004 | MVMQEEKKRQQPVTRRVRSFSESFKNLFRPPRSRDSSPINVTRIPYRSSSTSPKRSSEPPRRSTVSAQILDPKNSPIRQRSYTLKCCTPGLSHPFRQTGSGASNSPTRHRSISGEEQEIVNSLPEYKRSASHTFHGIRRPRSRSSSVSSCDSSNGTTSSSDSQWAMDSLLDDSDNDLTPYRGSNKDILKSKDRAPYNYIDDYNKKALRRATSYPNPLPSKQFYNERLYTRRSHPDEESLESLPRFAGADVQCIIEQNGFKVYEDGSHEHNIKLSGVIAKLEKGNSLPAHRQGSLSRPRLGITLSGLFKHHKNECDIENALSLLPNVEKSQTNHEKRTGQSPNDSNRSSPTQGREDYLKIVNPDASLGSDELKLINSLSSRIHKSLQNYLQEKNLKPAECIGEQAPTFQDNYGHPVGLVGAGAYGEVKLCARLRNEKDSPPFETYHDSKYIYYAVKELKPKPDSDLEKFCTKITSEFIIGHSLSHYHKNGKKPAPNILNVFDILEDSSSFIEVMEFCPAGDLYGMLVGKSKLKGRLHPLEADCFMKQLLHGVKFMHDHGIAHCDLKPENILFYPHGLLKICDFGTSSVFQTAWERRVHAQKGIIGSEPYVAPEEFVDGEYYDPRLIDCWSCGVVYITMILGHYLWKVASREKDMSYDEFYKEMQRKNQFRVFEELKHVNSELATNRKIALYRIFQWEPRKRISVGKLLDMQWMKSTNCCLIYDST | Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Sequence Mass (Da): 82590
Sequence Length: 724
Subcellular Location: Cytoplasm
EC: 2.7.11.1
|
P82851 | GHACYRNCWREGNDEETCKERCG | Function: Shows weak blocking activity on voltage-gated potassium channels Kv10.1/KCNH1/EAG1 (IC(50)=26 uM), Kv1.2/KCNA2 (Kd=150 uM), Kv1.3/KCNA3 (Kd=40 uM), Kv1.6/KCNA3 (16.6% inhibition at 40 uM toxin) . The block is dose-dependent, voltage-independent, and reversible . Also shows a weak inhibitory activity on the plant pathogen F.culmorum growth (IC(50)=18.8-37.7 uM) .
PTM: The two disulfide isomers globular (C1-C3, C2-C4) and beads (C1-C2, C3-C4) do not show activity on Kv10.1/KCNH1/EAG1.
Sequence Mass (Da): 2717
Sequence Length: 23
Domain: Has the structural arrangement of two alpha-helices stabilized by disulfide bonds (CSalpha/alpha 2(S-S)).
Subcellular Location: Secreted
|
P0DJ33 | MKSCLINVSLLILLLLPILGYASVNAESIDGENDFEEERGFGCFRSCWKAGHDDKTCKSMCG | Function: Shows structural homology with WaTx suggesting that it acts as a cell-penetrating peptide (CPP) with defensive purpose that induces pain by specifically activating mammalian sensory neuron TRPA1 channels (By similarity). Has no effect on the voltage-gated potassium channels tested (By similarity).
Sequence Mass (Da): 6830
Sequence Length: 62
Domain: Has the structural arrangement of two alpha-helices stabilized by disulfide bonds (CSalpha/alpha 2(S-S)).
Subcellular Location: Secreted
|
C0HLG4 | MKYFTLALTLLFLLLINPCKDMNFAWAESSEKVERASPQQAKYCYEQCNVNKVPFDQCYQMCSPLERS | Function: Cell-penetrating peptide (CPP) with defensive purpose that induces pain by specifically activating mammalian sensory neuron TRPA1 channels. It non-covalently binds to the same region than other TRPA1 agonists (irritants), but acts via a distinct biochemical mechanism. Its binding stabilizes the TRPA1 open state and diminishes calcium-permeability. Consequently, it produces pain and pain hypersensitivity, but fails to trigger efferent release of neuropeptides (CGRP) and neurogenic inflammation typically produced by noxious electrophiles. Is not active on voltage-gated potassium channels and other TRP channels.
Sequence Mass (Da): 7978
Sequence Length: 68
Domain: Has the structural arrangement of two alpha-helices stabilized by disulfide bonds (CSalpha/alpha 2(S-S)).
Subcellular Location: Secreted
|
P0C1Z3 | DPCYEVCLQQHGNVKECEEACKHPVEY | Function: OmTx1 decreases the amplitude of the potassium current of the rat channels Kv1.1/KCNA1 by 17% and Kv1.2/KCNA2 by 12% as well as human Kv1.3/KCNA3 by 24%.
Sequence Mass (Da): 3152
Sequence Length: 27
Domain: Has the structural arrangement of two alpha-helices stabilized by disulfide bonds (CSalpha/alpha 2(S-S)).
Subcellular Location: Secreted
|
O95198 | METPPLPPACTKQGHQKPLDSKDDNTEKHCPVTVNPWHMKKAFKVMNELRSQNLLCDVTIVAEDMEISAHRVVLAACSPYFHAMFTGEMSESRAKRVRIKEVDGWTLRMLIDYVYTAEIQVTEENVQVLLPAAGLLQLQDVKKTCCEFLESQLHPVNCLGIRAFADMHACTDLLNKANTYAEQHFADVVLSEEFLNLGIEQVCSLISSDKLTISSEEKVFEAVIAWVNHDKDVRQEFMARLMEHVRLPLLPREYLVQRVEEEALVKNSSACKDYLIEAMKYHLLPTEQRILMKSVRTRLRTPMNLPKLMVVVGGQAPKAIRSVECYDFKEERWHQVAELPSRRCRAGMVYMAGLVFAVGGFNGSLRVRTVDSYDPVKDQWTSVANMRDRRSTLGAAVLNGLLYAVGGFDGSTGLSSVEAYNIKSNEWFHVAPMNTRRSSVGVGVVGGLLYAVGGYDGASRQCLSTVECYNATTNEWTYIAEMSTRRSGAGVGVLNNLLYAVGGHDGPLVRKSVEVYDPTTNAWRQVADMNMCRRNAGVCAVNGLLYVVGGDDGSCNLASVEYYNPTTDKWTVVSSCMSTGRSYAGVTVIDKPL | Function: Substrate-specific adapter of a BCR (BTB-CUL3-RBX1) E3 ubiquitin ligase complex that mediates the ubiquitination of target proteins, such as NPTXR, WNK1, WNK3 and WNK4, leading most often to their proteasomal degradation . The BCR(KLHL2) complex catalyzes ubiquitination and degradation of NPTXR (By similarity). Responsible for degradative ubiquitination of the WNK kinases WNK1, WNK3 and WNK4 . Plays a role in the reorganization of the actin cytoskeleton . Promotes growth of cell projections in oligodendrocyte precursors .
Sequence Mass (Da): 65975
Sequence Length: 593
Pathway: Protein modification; protein ubiquitination.
Subcellular Location: Cytoplasm
|
P27814 | MDTASIYLGLKPPRTLGAWHESPPSLPPDACRCPRSHRLALKLSCAGLILLVLTLIGMSVLVRVLVQKPSREKCCVFIQENLNKTTDCSVNLECPQDWLLHRDKCFHVSQVSNTWEEGQADCGRKGATLLLIQDQEELRFLLDSIKEKYNSFWIGLRFTLPDMNWKWINGTTFNSDVLKITGVTENGSCASILGDKVTPESCASDNRWICQKELNHETPSNDS | Function: Plays a stimulatory role on natural killer (NK) cells cytotoxicity. Activation by cross-linking of the receptor induces Ca(2+) mobilization and interferon-gamma production.
Location Topology: Single-pass type II membrane protein
Sequence Mass (Da): 25077
Sequence Length: 223
Subcellular Location: Membrane
|
Q8VD98 | MDTSKVHGNVKPFRCPGYKQASSPSFSPDACRCPHWHHLALKSGCAGLILLLLSLIGLSVLVRFLVQKPPIEKCSVAAQENRTELTGRSAILECPRYWHPHWNKCLFVSQISRPWAEGRDACSMEDAILLLIENKEELRFVQNLIKGKEQLFFIGLKYVQKEKIWKWIDGSILNPNLLRITGKDKENSCAIISHTEVFSDSCSSDNHWICQKTLIHV | Function: Binds CLEC2I/Clr-g leading to activation of natural killer cells or costimulation of IL-2 production and proliferation of T-cells in response to antigen stimulation. May contribute to the formation of the immunological synapse between T-cells and antigen-presenting dendritic cells.
Location Topology: Single-pass type II membrane protein
Sequence Mass (Da): 24681
Sequence Length: 217
Subcellular Location: Membrane
|
Q63378 | MDTSRVYGNVKTFRSPGHKQASFPSLSTDACRCPHWHHLALKLGCATLILLLLTLIGLSVFVRFLVQKPLIEKCSMAAQENGTEPTGRSAILECPRHWQPHRNKCLIISQISRPWAEGLVACSMKEATLLIIENEEELKFVQNILKGRQQLFFIGLNYVQTEMTWKWINGSVLKPNILRITGSEVENSCALISHTEVFSDSCSSDNHWICQKTLKHV | Function: Binds CLEC2I/Clr-g leading to activation of natural killer cells or stimulation of IL-2 production and proliferation of T-cells in response to antigen stimulation. May contribute to the formation of the immunological synapse between T-cells and antigen-presenting dendritic cells (By similarity).
Location Topology: Single-pass type II membrane protein
Sequence Mass (Da): 24543
Sequence Length: 217
Subcellular Location: Membrane
|
Q13241 | MAVFKTTLWRLISGTLGIICLSLMSTLGILLKNSFTKLSIEPAFTPGPNIELQKDSDCCSCQEKWVGYRCNCYFISSEQKTWNESRHLCASQKSSLLQLQNTDELDFMSSSQQFYWIGLSYSEEHTAWLWENGSALSQYLFPSFETFNTKNCIAYNPNGNALDESCEDKNRYICKQQLI | Function: Immune receptor involved in self-nonself discrimination. In complex with KLRC1 or KLRC2 on cytotoxic and regulatory lymphocyte subsets, recognizes non-classical major histocompatibility (MHC) class Ib molecule HLA-E loaded with self-peptides derived from the signal sequence of classical MHC class Ia and non-classical MHC class Ib molecules . Enables cytotoxic cells to monitor the expression of MHC class I molecules in healthy cells and to tolerate self . Primarily functions as a ligand binding subunit as it lacks the capacity to signal.
Location Topology: Single-pass type II membrane protein
Sequence Mass (Da): 20513
Sequence Length: 179
Subcellular Location: Cell membrane
|
O54707 | MAVSRITRWRLMSVIFGIKCLFLMVTLGVLLINSFTIQNIQSTPSPTTTVEFQEVSECCVCLDKWVGHQCNCYFISKEEKSWKRSRDFCASQNSSLLQPQSRNELSFMNFSQTFFWIGMHYSEKRNAWLWEDGTVPSKDLFPEFSVIRPEHCIVYSPSKSVSAESCENKNRYICKKLPI | Function: Immune receptor involved in self-nonself discrimination. In complex with KLRC1 or KLRC2 on cytotoxic and regulatory lymphocyte subsets, recognizes non-classical major histocompatibility (MHC) class Ib molecule MHC-E loaded with self-peptides derived from the signal sequence of classical MHC class Ia and non-classical MHC class Ib molecules. Enables cytotoxic cells to monitor the expression of MHC class I molecules in healthy cells and to tolerate self. Primarily functions as a ligand binding subunit as it lacks the capacity to signal.
Location Topology: Single-pass type II membrane protein
Sequence Mass (Da): 20808
Sequence Length: 179
Subcellular Location: Cell membrane
|
O35778 | MAVSRITRWRLMSMFFGIKCLFLIVALGVLVKNSFTIQNIQSTPSSTPIVEFQKVSKCCACLEKWIGHQCSCYFISKEEKSWKGSREFCASQNSSLLQLQTRNELSFMSSSQAFFWIGIHYNEERSAWLWEDGTFPSKDLFPEFSKFRQDHCIGYSISREISSESCENKNRFICKQLPT | Function: Immune receptor involved in self-nonself discrimination. In complex with KLRC1 or KLRC2 on cytotoxic and regulatory lymphocyte subsets, recognizes non-classical major histocompatibility (MHC) class Ib molecule MHC-E loaded with self-peptides derived from the signal sequence of classical MHC class Ia and non-classical MHC class Ib molecules. Enables cytotoxic cells to monitor the expression of MHC class I molecules in healthy cells and to tolerate self. Primarily functions as a ligand binding subunit as it lacks the capacity to signal.
Location Topology: Single-pass type II membrane protein
Sequence Mass (Da): 20781
Sequence Length: 179
Subcellular Location: Cell membrane
|
Q8CJC7 | MDEAPVTRSTLNVNSQQKSKAKNKIKNTLNSNELSSIEQRKKYQKHLKKHKNTAEDISGKGNCSPPWRLLSSVLGAMCLLLMAVAMVMTTFTTKSSSERSSSTIQQEGLHHPCPENWVWFRCSCYFFSKEELIWRDSQRACLSLNSSLIRMNKEEMNFFSLKSFFWVGVYYNETRRQWLWEDHSVLPSGLFSKLEANMKNFCASYKSKEAYMEENCANKLTYICKK | Function: Lectin-like receptor for natural killer (NK) cells . Can either inhibit or activate NK cell cytotoxic activity, depending on its binding partner . Heterodimer formation with KLRI1 mediates NK cell inhibition whereas heterodimer formation with KLRI2 mediates NK cell activation . Plays a role in allogeneic recognition by the immune system .
Location Topology: Single-pass type II membrane protein
Sequence Mass (Da): 26265
Sequence Length: 226
Subcellular Location: Cell membrane
|
Q80ZC8 | MNQTLIICSTLNVNSQQKSKAKNSMKNTFHSNELSSIEQRQKYQKHLKKDKKTAEDITGVGNCSPPWRLISSVLFVVCLLLMAVAMVMTIFTTRLSSERSSSNIHQEGLHHPCPENWVWFRCSCYYFSKEKLVWRESQRACLSFNSSLIRMNKEEMDFFSLKSFFWVGVYYDETSKQWLWDDHSVLPSGMFSGLESSPKNFCASYKSKEAYLAENCSTKLMYICKK | Function: Lectin-like receptor for natural killer (NK) cells . Can either inhibit or activate NK cell cytotoxic activity, depending on its binding partner . Heterodimer formation with KLRI1 mediates NK cell inhibition whereas heterodimer formation with KLRI2 mediates NK cell activation . Plays a role in allogeneic recognition by the immune system (By similarity).
Location Topology: Single-pass type II membrane protein
Sequence Mass (Da): 26266
Sequence Length: 226
Subcellular Location: Cell membrane
|
Q9NZS2 | MQDEERYMTLNVQSKKRSSAQTSQLTFKDYSVTLHWYKILLGISGTVNGILTLTLISLILLVSQGVLLKCQKGSCSNATQYEDTGDLKVNNGTRRNISNKDLCASRSADQTVLCQSEWLKYQGKCYWFSNEMKSWSDSYVYCLERKSHLLIIHDQLEMAFIQKNLRQLNYVWIGLNFTSLKMTWTWVDGSPIDSKIFFIKGPAKENSCAAIKESKIFSETCSSVFKWICQY | Function: Involved in the natural killer (NK)-mediated cytolysis of PHA-induced lymphoblasts.
Location Topology: Single-pass type II membrane protein
Sequence Mass (Da): 26563
Sequence Length: 231
Subcellular Location: Membrane
|
D3W0D1 | MENEDGYMTLSFKNRCKSKQKSKDFSLYPQYYCLLLIFGCIVILIFIMTGIDLKFWHKKMDFSQNVNVSSLSGHNYLCPNDWLLNEGKCYWFSTSFKTWKESQRDCTQLQAHLLVIQNLDELEFIQNSLKPGHFGWIGLYVTFQGNLWMWIDEHFLVPELFSVIGPTDDRSCAVITGNWVYSEDCSSTFKGICQRDAILTHNGTSGV | Function: C-type lectin-like receptor involved in natural killer cell mediated cytotoxicity and cytokine secretion in keratinocytes via its interaction with CLEC2A.
PTM: N-glycosylated.
Location Topology: Single-pass type II membrane protein
Sequence Mass (Da): 24008
Sequence Length: 207
Subcellular Location: Cell membrane
|
Q96E93 | MTDSVIYSMLELPTATQAQNDYGPQQKSSSSRPSCSCLVAIALGLLTAVLLSVLLYQWILCQGSNYSTCASCPSCPDRWMKYGNHCYYFSVEEKDWNSSLEFCLARDSHLLVITDNQEMSLLQVFLSEAFCWIGLRNNSGWRWEDGSPLNFSRISSNSFVQTCGAINKNGLQASSCEVPLHWVCKKCPFADQALF | Function: Plays an inhibitory role on natural killer (NK) cells and T-cell functions upon binding to their non-MHC ligands. May mediate missing self recognition by binding to a highly conserved site on classical cadherins, enabling it to monitor expression of E-cadherin/CDH1, N-cadherin/CDH2 and R-cadherin/CDH4 on target cells.
Location Topology: Single-pass type II membrane protein
Sequence Mass (Da): 21831
Sequence Length: 195
Domain: Contains 1 copy of a cytoplasmic motif that is referred to as the immunoreceptor tyrosine-based inhibitor motif (ITIM). This motif is involved in modulation of cellular responses. Upon phosphorylation of ITIM motif KLRG1 associates with the two phosphatases PTPN11 and INPP5D (By similarity).
Subcellular Location: Cell membrane
|
Q8S905 | MTIKTPGTPVSKMDRTPAVTPGGSSRSREEKIVVTVRLRPMNKRELLAKDQVAWECVNDHTIVSKPQVQERLHHQSSFTFDKVFGPESLTENVYEDGVKNVALSALMGINATIFAYGQTSSGKTYTMRGVTEKAVNDIYNHIIKTPERDFTIKISGLEIYNENVRDLLNSDSGRALKLLDDPEKGTVVEKLVEETANNDNHLRHLISICEAQRQVGETALNDTSSRSHQIIRLTIQSTHRENSDCVRSYMASLNFVDLAGSERASQSQADGTRLREGCHINLSLMTLTTVIRKLSVGKRSGHIPYRDSKLTRILQHSLGGNARTAIICTLSPALAHVEQSRNTLYFANRAKEVTNNAHVNMVVSDKQLVKHLQKEVARLEAERRTPGPSTEKDFKIQQMEMEIGELRRQRDDAQIQLEELRQKLQGDQQQNKGLNPFESPDPPVRKCLSYSVAVTPSSENKTLNRNERARKTTMRQSMIRQSSTAPFTLMHEIRKLEHLQEQLGEEATKALEVLQKEVACHRLGNQDAAQTIAKLQAEIREMRTVKPSAMLKEVGDVIAPNKSVSANLKEEITRLHSQGSTIANLEEQLESVQKSIDKLVMSLPSNISAGDETPKTKNHHHQSKKKKLLPLTPSSASNRQNFLKSPCSPLSASRQVLDCDAENKAPQENNSSAARGATTPQGSEKETPQKGEESGDVSSREGTPGYRRSSSVNMKKMQQMFQNAAEENVRSIRAYVTELKERVAKLQYQKQLLVCQVLELEANDGAGYSVENEENTIMEDEEQNQVAWHITFIEERQQIIELWHVCHVSIIHRTQFYLLFKGDQADQIYMEVELRRLTWLEQHLAEVGNATPARNCDESVVSLSSSIKALRREREFLAKRVNSRLTPEEREELYMKWDVPLEGKQRKLQFVNKLWTDPYDSRHVQESAEIVAKLVGFCESGNISKEMFELNFAVPSDKRQWNIGWDNISNLLHL | Function: Probable plus end-directed motor protein that functions in the NACK-PQR (ANP1-MKK6-MPK4) MAP kinase signaling pathway, which is essential for somatic cell cytokinesis, especially for the cell-plate formation and its expansion. Regulates the activity and the localization of ANP1, probably by association through the non-catalytic region of the kinase. Functionally redundant with NACK2 and essential to promote the progression of cytokinesis and for cellularization (formation of the cell plate) during microgametogenesis and megagametogenesis.
PTM: Phosphorylated at Thr-145, Thr-687 and Thr-703 by CDKAs and CDKBs. Phosphorylated NACK1 fails to mediate cytokinesis.
Sequence Mass (Da): 110174
Sequence Length: 974
Subcellular Location: Cytoplasm
|
Q8S950 | MTVRTPGTPASKIDKTPATTPNGHRGREEKIVVTVRLRPLNKRELSAKDHAAWECIDDHTIIYRPVPQERAAQPASSFTFDKVFGPDSITEAVYEEGVKNVALSSLMGINATIFAYGQTSSGKTYTMRGITEKAVNDIYAHIMSTPEREFRIRISGLEIYNENVRDLLNSESGRSLKLLDDPEKGTVVEKLVEETASNDQHLRHLISICEAQRQVGETALNDTSSRSHQIIRLTIESTLRESSDCVRSYVASLNFVDLAGSERASQTNADGARLREGCHINLSLMTLTTVIRKLSVGKRSGHIPYRDSKLTRILQHSLGGNARTAIICTLSPASSHVEQSRNTLYFATRAKEVTNNAQVNMVVSDKQLVKHLQKEVARLEAELRTPDPANEKDWKIQQMEMEIEELKRQRDLAQSQVDELRRKLQEEQGPKPSESVSPVVKKCLSFSGTLSPNLEEKAPVRSERTRNTMGRQSMRQSLAAPFTLMHEIRKLEHLQEQLGDEANRALEVLQKEVACHRLGNQDAAETIAKLQAEIREMRSIRPLPKEVEVGSVVAVNKSVSANLKEEIARLHSQGSTIADLEEQLENVQKSLDKLVMSLPSNNDQQSNNDTTQKAKHPSKKKKLLPLTSSNSINRQNFLKSPCSPLSTARQVLDCEVENRAPDSDDLSCEIQPDETPTKSDGGDVSSKEGTPYRRSSSVNMRKMQKMFQEAAEENVRNIRSYVTELKERVAKLQYQKQLLVCQVLELEANEAAGYNLEDDENIHQIPEESPVSWQITFKEQRQQIIDLWDVCYVSIIHRSQFYLLFKGDPADEIYLEVELRRLTWLQQHLAELGNATPARVGNEPTVSLSSSIRALKREREFLAKRLTTRLTAEERDYLYIKWEVPLEGKQRRMQFINKLWTNPHDAKHVHESAEIVAKLVGFCEGGNMSREMFELNFVLPSDRRPWFAGWNQISDLLHI | Function: Probable plus end-directed motor protein that functions in the NACK-PQR (NPK1-NQK1/MEK1-NRK1) MAP kinase signaling pathway, which is essential for somatic cell cytokinesis, especially for the cell-plate formation and its expansion. Regulates the activity and the localization of NPK1 by association through the non-catalytic region of the kinase.
PTM: Phosphorylated at Thr-145, Thr-675 and Thr-690 by CDKAs and CDKBs. The phosphorylation occurs before metaphase and inhibits the interaction with NPK1 preventing the transition to cytokinesis.
Sequence Mass (Da): 108604
Sequence Length: 959
Subcellular Location: Cytoplasm
|
P09216 | MVVFNGLLKIKICEAVSLKPTAWSLRHAVGPRPQTFLLDPYIALNVDDSRIGQTATKQKTNSPAWHDEFVTDVCNGRKIELAVFHDAPIGYDDFVANCTIQFEELLQNGSRHFEDWIDLEPEGKVYVIIDLSGSSGEAPKDNEERVFRERMRPRKRQGAVRRRVHQVNGHKFMATYLRQPTYCSHCRDFIWGVIGKQGYQCQVCTCVVHKRCHELIITKCAGLKKQETPDEVGSQRFSVNMPHKFGIHNYKVPTFCDHCGSLLWGLLRQGLQCKVCKMNVHRRCETNVAPNCGVDARGIAKVLADLGVTPDKITNSGQRRKKLAAGAESPQPASGNSPSEDDRSKSAPTSPCDQELKELENNIRKALSFDNRGEEHRASSSTDGQLASPGENGEVRQGQAKRLGLDEFNFIKVLGKGSFGKVMLAELKGKDEVYAVKVLKKDVILQDDDVDCTMTEKRILALARKHPYLTQLYCCFQTKDRLFFVMEYVNGGDLMFQIQRSRKFDEPRSGFYAAEVTSALMFLHQHGVIYRDLKLDNILLDAEGHSKLADFGMCKEGILNGVTTTTFCGTPDYIAPEILQELEYGPSVDWWALGVLMYEMMAGQPPFEADNEDDLFESILHDDVLYPVWLSKEAVSILKAFMTKNPHKRLGCVAAQNGEDAIKQHPFFKEIDWVLLEQKKMKPPFKPRIKTKRDVNNFDQDFTREEPILTLVDEAIVKQINQEEFKGFSYFGEDLMP | Function: Calcium-independent, phospholipid- and diacylglycerol (DAG)-dependent serine/threonine-protein kinase that plays essential roles in the regulation of multiple cellular processes linked to cytoskeletal proteins, such as cell adhesion, motility, migration and cell cycle, functions in neuron growth and ion channel regulation, and is involved in immune response, cancer cell invasion and regulation of apoptosis. Mediates cell adhesion to the extracellular matrix via integrin-dependent signaling, by mediating angiotensin-2-induced activation of integrin beta-1 (ITGB1) in cardiac fibroblasts. Phosphorylates MARCKS, which phosphorylates and activates PTK2/FAK, leading to the spread of cardiomyocytes. Involved in the control of the directional transport of ITGB1 in mesenchymal cells by phosphorylating vimentin (VIM), an intermediate filament (IF) protein. In epithelial cells, associates with and phosphorylates keratin-8 (KRT8), which induces targeting of desmoplakin at desmosomes and regulates cell-cell contact. Phosphorylates IQGAP1, which binds to CDC42, mediating epithelial cell-cell detachment prior to migration. During cytokinesis, forms a complex with YWHAB, which is crucial for daughter cell separation, and facilitates abscission by a mechanism which may implicate the regulation of RHOA. In cardiac myocytes, regulates myofilament function and excitation coupling at the Z-lines, where it is indirectly associated with F-actin via interaction with COPB1. During endothelin-induced cardiomyocyte hypertrophy, mediates activation of PTK2/FAK, which is critical for cardiomyocyte survival and regulation of sarcomere length. Plays a role in the pathogenesis of dilated cardiomyopathy via persistent phosphorylation of troponin I (TNNI3). Involved in nerve growth factor (NFG)-induced neurite outgrowth and neuron morphological change independently of its kinase activity, by inhibition of RHOA pathway, activation of CDC42 and cytoskeletal rearrangement. May be involved in presynaptic facilitation by mediating phorbol ester-induced synaptic potentiation. Phosphorylates gamma-aminobutyric acid receptor subunit gamma-2 (GABRG2), which reduces the response of GABA receptors to ethanol and benzodiazepines and may mediate acute tolerance to the intoxicating effects of ethanol. Upon PMA treatment, phosphorylates the capsaicin- and heat-activated cation channel TRPV1, which is required for bradykinin-induced sensitization of the heat response in nociceptive neurons. Is able to form a complex with PDLIM5 and N-type calcium channel, and may enhance channel activities and potentiates fast synaptic transmission by phosphorylating the pore-forming alpha subunit CACNA1B (CaV2.2). Downstream of TLR4, plays an important role in the lipopolysaccharide (LPS)-induced immune response by phosphorylating and activating TICAM2/TRAM, which in turn activates the transcription factor IRF3 and subsequent cytokines production. In differentiating erythroid progenitors, is regulated by EPO and controls the protection against the TNFSF10/TRAIL-mediated apoptosis, via BCL2. May be involved in the regulation of the insulin-induced phosphorylation and activation of AKT1. Phosphorylates NLRP5/MATER and may thereby modulate AKT pathway activation in cumulus cells (By similarity).
PTM: Phosphorylation on Thr-566 by PDPK1 triggers autophosphorylation on Ser-729. Phosphorylation in the hinge domain at Ser-350 by MAPK11 or MAPK14, Ser-346 by GSK3B and Ser-368 by autophosphorylation is required for interaction with YWHAB (By similarity).
Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Sequence Mass (Da): 83478
Sequence Length: 737
Domain: The C1 domain, containing the phorbol ester/DAG-type region 1 (C1A) and 2 (C1B), is the diacylglycerol sensor and the C2 domain is a non-calcium binding domain.
Subcellular Location: Cytoplasm
EC: 2.7.11.13
|
P05129 | MAGLGPGVGDSEGGPRPLFCRKGALRQKVVHEVKSHKFTARFFKQPTFCSHCTDFIWGIGKQGLQCQVCSFVVHRRCHEFVTFECPGAGKGPQTDDPRNKHKFRLHSYSSPTFCDHCGSLLYGLVHQGMKCSCCEMNVHRRCVRSVPSLCGVDHTERRGRLQLEIRAPTADEIHVTVGEARNLIPMDPNGLSDPYVKLKLIPDPRNLTKQKTRTVKATLNPVWNETFVFNLKPGDVERRLSVEVWDWDRTSRNDFMGAMSFGVSELLKAPVDGWYKLLNQEEGEYYNVPVADADNCSLLQKFEACNYPLELYERVRMGPSSSPIPSPSPSPTDPKRCFFGASPGRLHISDFSFLMVLGKGSFGKVMLAERRGSDELYAIKILKKDVIVQDDDVDCTLVEKRVLALGGRGPGGRPHFLTQLHSTFQTPDRLYFVMEYVTGGDLMYHIQQLGKFKEPHAAFYAAEIAIGLFFLHNQGIIYRDLKLDNVMLDAEGHIKITDFGMCKENVFPGTTTRTFCGTPDYIAPEIIAYQPYGKSVDWWSFGVLLYEMLAGQPPFDGEDEEELFQAIMEQTVTYPKSLSREAVAICKGFLTKHPGKRLGSGPDGEPTIRAHGFFRWIDWERLERLEIPPPFRPRPCGRSGENFDKFFTRAAPALTPPDRLVLASIDQADFQGFTYVNPDFVHPDARSPTSPVPVPVM | Cofactor: Binds 3 Ca(2+) ions per subunit. The ions are bound to the C2 domain.
Function: Calcium-activated, phospholipid- and diacylglycerol (DAG)-dependent serine/threonine-protein kinase that plays diverse roles in neuronal cells and eye tissues, such as regulation of the neuronal receptors GRIA4/GLUR4 and GRIN1/NMDAR1, modulation of receptors and neuronal functions related to sensitivity to opiates, pain and alcohol, mediation of synaptic function and cell survival after ischemia, and inhibition of gap junction activity after oxidative stress. Binds and phosphorylates GRIA4/GLUR4 glutamate receptor and regulates its function by increasing plasma membrane-associated GRIA4 expression. In primary cerebellar neurons treated with the agonist 3,5-dihyidroxyphenylglycine, functions downstream of the metabotropic glutamate receptor GRM5/MGLUR5 and phosphorylates GRIN1/NMDAR1 receptor which plays a key role in synaptic plasticity, synaptogenesis, excitotoxicity, memory acquisition and learning. May be involved in the regulation of hippocampal long-term potentiation (LTP), but may be not necessary for the process of synaptic plasticity. May be involved in desensitization of mu-type opioid receptor-mediated G-protein activation in the spinal cord, and may be critical for the development and/or maintenance of morphine-induced reinforcing effects in the limbic forebrain. May modulate the functionality of mu-type-opioid receptors by participating in a signaling pathway which leads to the phosphorylation and degradation of opioid receptors. May also contributes to chronic morphine-induced changes in nociceptive processing. Plays a role in neuropathic pain mechanisms and contributes to the maintenance of the allodynia pain produced by peripheral inflammation. Plays an important role in initial sensitivity and tolerance to ethanol, by mediating the behavioral effects of ethanol as well as the effects of this drug on the GABA(A) receptors. During and after cerebral ischemia modulate neurotransmission and cell survival in synaptic membranes, and is involved in insulin-induced inhibition of necrosis, an important mechanism for minimizing ischemic injury. Required for the elimination of multiple climbing fibers during innervation of Purkinje cells in developing cerebellum. Is activated in lens epithelial cells upon hydrogen peroxide treatment, and phosphorylates connexin-43 (GJA1/CX43), resulting in disassembly of GJA1 gap junction plaques and inhibition of gap junction activity which could provide a protective effect against oxidative stress (By similarity). Phosphorylates p53/TP53 and promotes p53/TP53-dependent apoptosis in response to DNA damage. Involved in the phase resetting of the cerebral cortex circadian clock during temporally restricted feeding. Stabilizes the core clock component BMAL1 by interfering with its ubiquitination, thus suppressing its degradation, resulting in phase resetting of the cerebral cortex clock (By similarity).
Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
PTM: Autophosphorylation on Thr-674 appears to regulate motor functions of junctophilins, JPH3 and JPH4.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 78448
Sequence Length: 697
Subcellular Location: Cytoplasm
EC: 2.7.11.13
|
Q90XF2 | MPTLRDSTMSHPGENPHQVRVKAYYRGDIMITHFEPSISYEGLCNEVRDMCSMDNDQLFTMKWIDEEGDPCTVSSQLELEEALRLYELNKDSELIIHVFPCVPEKPGMPCPGEDKSIYRRGARRWRKLYYATGHAFQAKRFNRRAHCAICTDRIWGLGRQGYKCINCKLLVHKKCHKLVTVECGRQVIQDPMIGRIDPGSTHPEHPDQVLGKKNSTESINHEGEEHEAVGSRESGKAVSSLGLIDFDLLRVIGRGSYAKVLLVRLKKTERIYAMKVVKKELVNDDEDIDWVQTEKHVFEQASNHPFLVGLHSCFQTESRLFFVIEYVNGGDLMFHMQRQRKLPEEHARFYSAEISLALNYLHERGIIYRDLKLDNVLLDSEGHIKLTDYGMCKEGLRPGDTTSTFCGTPNYIAPEILRGEDYGFSVDWWALGVLMFEMMAGRSPFDIVGSSDNPDQNTEDYLFQVILEKQIRIPRSLSVKAASVLKGFLNKESKERLGCHPQTGFADIMAHPFFRNVDWDLMEQKQVVPPFKPNISGEFGLDNFDAQFTNEPIQLTPDDDDAVKKIDQSEFEGFEYINPLLMSAEECV | Function: Calcium- and diacylglycerol-independent serine/ threonine-protein kinase that plays a general protective role against apoptotic stimuli, is involved in NF-kappa-B activation, cell survival, differentiation and polarity, and contributes to the regulation of microtubule dynamics in the early secretory pathway (By similarity). Is required for the formation and maintenance of the zonula adherens during early epithelial development and plays a critical role in organ morphogenesis and in regulating the orientation of cell division.
Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Sequence Mass (Da): 67322
Sequence Length: 588
Domain: The C1 zinc finger does not bind the diacylglycerol (DAG).
EC: 2.7.11.13
|
P41743 | MPTQRDSSTMSHTVAGGGSGDHSHQVRVKAYYRGDIMITHFEPSISFEGLCNEVRDMCSFDNEQLFTMKWIDEEGDPCTVSSQLELEEAFRLYELNKDSELLIHVFPCVPERPGMPCPGEDKSIYRRGARRWRKLYCANGHTFQAKRFNRRAHCAICTDRIWGLGRQGYKCINCKLLVHKKCHKLVTIECGRHSLPQEPVMPMDQSSMHSDHAQTVIPYNPSSHESLDQVGEEKEAMNTRESGKASSSLGLQDFDLLRVIGRGSYAKVLLVRLKKTDRIYAMKVVKKELVNDDEDIDWVQTEKHVFEQASNHPFLVGLHSCFQTESRLFFVIEYVNGGDLMFHMQRQRKLPEEHARFYSAEISLALNYLHERGIIYRDLKLDNVLLDSEGHIKLTDYGMCKEGLRPGDTTSTFCGTPNYIAPEILRGEDYGFSVDWWALGVLMFEMMAGRSPFDIVGSSDNPDQNTEDYLFQVILEKQIRIPRSLSVKAASVLKSFLNKDPKERLGCHPQTGFADIQGHPFFRNVDWDMMEQKQVVPPFKPNISGEFGLDNFDSQFTNEPVQLTPDDDDIVRKIDQSEFEGFEYINPLLMSAEECV | Function: Calcium- and diacylglycerol-independent serine/ threonine-protein kinase that plays a general protective role against apoptotic stimuli, is involved in NF-kappa-B activation, cell survival, differentiation and polarity, and contributes to the regulation of microtubule dynamics in the early secretory pathway. Is necessary for BCR-ABL oncogene-mediated resistance to apoptotic drug in leukemia cells, protecting leukemia cells against drug-induced apoptosis. In cultured neurons, prevents amyloid beta protein-induced apoptosis by interrupting cell death process at a very early step. In glioblastoma cells, may function downstream of phosphatidylinositol 3-kinase (PI(3)K) and PDPK1 in the promotion of cell survival by phosphorylating and inhibiting the pro-apoptotic factor BAD. Can form a protein complex in non-small cell lung cancer (NSCLC) cells with PARD6A and ECT2 and regulate ECT2 oncogenic activity by phosphorylation, which in turn promotes transformed growth and invasion. In response to nerve growth factor (NGF), acts downstream of SRC to phosphorylate and activate IRAK1, allowing the subsequent activation of NF-kappa-B and neuronal cell survival. Functions in the organization of the apical domain in epithelial cells by phosphorylating EZR. This step is crucial for activation and normal distribution of EZR at the early stages of intestinal epithelial cell differentiation. Forms a protein complex with LLGL1 and PARD6B independently of PARD3 to regulate epithelial cell polarity. Plays a role in microtubule dynamics in the early secretory pathway through interaction with RAB2A and GAPDH and recruitment to vesicular tubular clusters (VTCs). In human coronary artery endothelial cells (HCAEC), is activated by saturated fatty acids and mediates lipid-induced apoptosis. Involved in early synaptic long term potentiation phase in CA1 hippocampal cells and short term memory formation (By similarity).
PTM: Phosphorylation at Thr-412 in the activation loop is not mandatory for activation (By similarity). Upon neuronal growth factor (NGF) stimulation, phosphorylated by SRC at Tyr-265, Tyr-280 and Tyr-334 . Phosphorylation at Tyr-265 facilitates binding to KPNB1/importin-beta regulating entry of PRKCI into the nucleus . Phosphorylation on Tyr-334 is important for NF-kappa-B stimulation . Phosphorylated at Thr-564 during the initial phase of long term potentiation (By similarity).
Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Sequence Mass (Da): 68262
Sequence Length: 596
Domain: The PB1 domain mediates interaction with SQSTM1.
Subcellular Location: Cytoplasm
EC: 2.7.11.13
|
Q62074 | MPTQRDSSTMSHTVACGGGGDHSHQVRVKAYYRGDIMITHFEPSISFEGLCSEVRDMCSFDNEQPFTMKWIDEEGDPCTVSSQLELEEAFRLYELNKDSELLIHVFPCVPERPGMPCPGEDKSIYRRGARRWRKLYCANGHTFQAKRFNRRAHCAICTDRIWGLGRQGYKCINCKLLVHKKCHKLVTIECGRHSLPPEPMMPMDQTMHPDHTQTVIPYNPSSHESLDQVGEEKEAMNTRESGKASSSLGLQDFDLLRVIGRGSYAKVLLVRLKKTDRIYAMKVVKKELVNDDEDIDWVQTEKHVFEQASNHPFLVGLHSCFQTESRLFFVIEYVNGGDLMFHMQRQRKLPEEHARFYSAEISLALNYLHERGIIYRDLKLDNVLLDSEGHIKLTDYGMCKEGLRPGDTTSTFCGTPNYIAPEILRGEDYGFSVDWWALGVLMFEMMAGRSPFDIVGSSDNPDQNTEDYLFQVILEKQIRIPRSLSVKAASVLKSFLNKDPKERLGCHPQTGFADIQGHPFFRNVDWDMMEQKQVVPPFKPNISGEFGLDNFDSQFTNEPVQLTPDDDDIVRKIDQSEFEGFEYINPLLMSAEECV | Function: Calcium- and diacylglycerol-independent serine/ threonine-protein kinase that plays a general protective role against apoptotic stimuli, is involved in NF-kappa-B activation, cell survival, differentiation and polarity, and contributes to the regulation of microtubule dynamics in the early secretory pathway. Is necessary for BCR-ABL oncogene-mediated resistance to apoptotic drug in leukemia cells, protecting leukemia cells against drug-induced apoptosis. In cultured neurons, prevents amyloid beta protein-induced apoptosis by interrupting cell death process at a very early step. In glioblastoma cells, may function downstream of phosphatidylinositol 3-kinase (PI3K) and PDPK1 in the promotion of cell survival by phosphorylating and inhibiting the pro-apoptotic factor BAD. Can form a protein complex in non-small cell lung cancer (NSCLC) cells with PARD6A and ECT2 and regulate ECT2 oncogenic activity by phosphorylation, which in turn promotes transformed growth and invasion. In response to nerve growth factor (NGF), acts downstream of SRC to phosphorylate and activate IRAK1, allowing the subsequent activation of NF-kappa-B and neuronal cell survival. Functions in the organization of the apical domain in epithelial cells by phosphorylating EZR. This step is crucial for activation and normal distribution of EZR at the early stages of intestinal epithelial cell differentiation. Forms a protein complex with LLGL1 and PARD6B independently of PARD3 to regulate epithelial cell polarity. Plays a role in microtubule dynamics in the early secretory pathway through interaction with RAB2A and GAPDH and recruitment to vesicular tubular clusters (VTCs). In human coronary artery endothelial cells (HCAEC), is activated by saturated fatty acids and mediates lipid-induced apoptosis (By similarity). Downstream of PI3K is required for insulin-stimulated glucose transport. Activates RAB4A and promotes its association with KIF3A which is required for the insulin-induced SLC2A4/GLUT4 translocation in adipocytes. Is essential in early embryogenesis and development of differentiating photoreceptors by playing a role in the establishment of epithelial and neuronal polarity. Involved in early synaptic long term potentiation phase in CA1 hippocampal cells and short term memory formation (By similarity).
PTM: Phosphorylation at Thr-411 in the activation loop is not mandatory for activation . Upon neuronal growth factor (NGF) stimulation, phosphorylated by SRC at Tyr-264, Tyr-279 and Tyr-333 (By similarity). Phosphorylation on Tyr-264 facilitates binding to KPNB1/importin-beta regulating entry of PRKCI into the nucleus (By similarity). Phosphorylation on Tyr-333 is important for NF-kappa-B stimulation (By similarity). Phosphorylated at Thr-563 during the initial phase of long term potentiation (By similarity).
Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Sequence Mass (Da): 68203
Sequence Length: 595
Domain: The PB1 domain mediates interaction with SQSTM1.
Subcellular Location: Cytoplasm
EC: 2.7.11.13
|
P24723 | MSSGTMKFNGYLRVRIGEAVGLQPTRWSLRHSLFKKGHQLLDPYLTVSVDQVRVGQTSTKQKTNKPTYNEEFCANVTDGGHLELAVFHETPLGYDHFVANCTLQFQELLRTTGASDTFEGWVDLEPEGKVFVVITLTGSFTEATLQRDRIFKHFTRKRQRAMRRRVHQINGHKFMATYLRQPTYCSHCREFIWGVFGKQGYQCQVCTCVVHKRCHHLIVTACTCQNNINKVDSKIAEQRFGINIPHKFSIHNYKVPTFCDHCGSLLWGIMRQGLQCKICKMNVHIRCQANVAPNCGVNAVELAKTLAGMGLQPGNISPTSKLVSRSTLRRQGKESSKEGNGIGVNSSNRLGIDNFEFIRVLGKGSFGKVMLARVKETGDLYAVKVLKKDVILQDDDVECTMTEKRILSLARNHPFLTQLFCCFQTPDRLFFVMEFVNGGDLMFHIQKSRRFDEARARFYAAEIISALMFLHDKGIIYRDLKLDNVLLDHEGHCKLADFGMCKEGICNGVTTATFCGTPDYIAPEILQEMLYGPAVDWWAMGVLLYEMLCGHAPFEAENEDDLFEAILNDEVVYPTWLHEDATGILKSFMTKNPTMRLGSLTQGGEHAILRHPFFKEIDWAQLNHRQIEPPFRPRIKSREDVSNFDPDFIKEEPVLTPIDEGHLPMINQDEFRNFSYVSPELQP | Function: Calcium-independent, phospholipid- and diacylglycerol (DAG)-dependent serine/threonine-protein kinase that is involved in the regulation of cell differentiation in keratinocytes and pre-B cell receptor, mediates regulation of epithelial tight junction integrity and foam cell formation, and is required for glioblastoma proliferation and apoptosis prevention in MCF-7 cells. In keratinocytes, binds and activates the tyrosine kinase FYN, which in turn blocks epidermal growth factor receptor (EGFR) signaling and leads to keratinocyte growth arrest and differentiation. Associates with the cyclin CCNE1-CDK2-CDKN1B complex and inhibits CDK2 kinase activity, leading to RB1 dephosphorylation and thereby G1 arrest in keratinocytes. In association with RALA activates actin depolymerization, which is necessary for keratinocyte differentiation. In the pre-B cell receptor signaling, functions downstream of BLNK by up-regulating IRF4, which in turn activates L chain gene rearrangement. Regulates epithelial tight junctions (TJs) by phosphorylating occludin (OCLN) on threonine residues, which is necessary for the assembly and maintenance of TJs. In association with PLD2 and via TLR4 signaling, is involved in lipopolysaccharide (LPS)-induced RGS2 down-regulation and foam cell formation. Upon PMA stimulation, mediates glioblastoma cell proliferation by activating the mTOR pathway, the PI3K/AKT pathway and the ERK1-dependent phosphorylation of ELK1. Involved in the protection of glioblastoma cells from irradiation-induced apoptosis by preventing caspase-9 activation. In camptothecin-treated MCF-7 cells, regulates NF-kappa-B upstream signaling by activating IKBKB, and confers protection against DNA damage-induced apoptosis. Promotes oncogenic functions of ATF2 in the nucleus while blocking its apoptotic function at mitochondria. Phosphorylates ATF2 which promotes its nuclear retention and transcriptional activity and negatively regulates its mitochondrial localization.
Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Sequence Mass (Da): 77828
Sequence Length: 683
Domain: The C1 domain, containing the phorbol ester/DAG-type region 1 (C1A) and 2 (C1B), is the diacylglycerol sensor and the C2 domain is a non-calcium binding domain.
Subcellular Location: Cytoplasm
EC: 2.7.11.13
|
Q04759 | MSPFLRIGLSNFDCGSCQSCQGEAVNPYCAVLVKEYVESENGQMYIQKKPTMYPPWDSTFDAHINKGRVMQIIVKGKNVDLISETTVELYSLAERCRKNNGKTEIWLELKPQGRMLMNARYFLEMSDTKDMNEFETEGFFALHQRRGAIKQAKVHHVKCHEFTATFFPQPTFCSVCHEFVWGLNKQGYQCRQCNAAIHKKCIDKVIAKCTGSAINSRETMFHKERFKIDMPHRFKVYNYKSPTFCEHCGTLLWGLARQGLKCDACGMNVHHRCQTKVANLCGINQKLMAEALAMIESTQQARCLRDTEQIFREGPVEIGLPCSIKNEARPPCLPTPGKREPQGISWESPLDEVDKMCHLPEPELNKERPSLQIKLKIEDFILHKMLGKGSFGKVFLAEFKKTNQFFAIKALKKDVVLMDDDVECTMVEKRVLSLAWEHPFLTHMFCTFQTKENLFFVMEYLNGGDLMYHIQSCHKFDLSRATFYAAEIILGLQFLHSKGIVYRDLKLDNILLDKDGHIKIADFGMCKENMLGDAKTNTFCGTPDYIAPEILLGQKYNHSVDWWSFGVLLYEMLIGQSPFHGQDEEELFHSIRMDNPFYPRWLEKEAKDLLVKLFVREPEKRLGVRGDIRQHPLFREINWEELERKEIDPPFRPKVKSPFDCSNFDKEFLNEKPRLSFADRALINSMDQNMFRNFSFMNPGMERLIS | Function: Calcium-independent, phospholipid- and diacylglycerol (DAG)-dependent serine/threonine-protein kinase that mediates non-redundant functions in T-cell receptor (TCR) signaling, including T-cells activation, proliferation, differentiation and survival, by mediating activation of multiple transcription factors such as NF-kappa-B, JUN, NFATC1 and NFATC2. In TCR-CD3/CD28-co-stimulated T-cells, is required for the activation of NF-kappa-B and JUN, which in turn are essential for IL2 production, and participates in the calcium-dependent NFATC1 and NFATC2 transactivation. Mediates the activation of the canonical NF-kappa-B pathway (NFKB1) by direct phosphorylation of CARD11 on several serine residues, inducing CARD11 association with lipid rafts and recruitment of the BCL10-MALT1 complex, which then activates IKK complex, resulting in nuclear translocation and activation of NFKB1. May also play an indirect role in activation of the non-canonical NF-kappa-B (NFKB2) pathway. In the signaling pathway leading to JUN activation, acts by phosphorylating the mediator STK39/SPAK and may not act through MAP kinases signaling. Plays a critical role in TCR/CD28-induced NFATC1 and NFATC2 transactivation by participating in the regulation of reduced inositol 1,4,5-trisphosphate generation and intracellular calcium mobilization. After costimulation of T-cells through CD28 can phosphorylate CBLB and is required for the ubiquitination and subsequent degradation of CBLB, which is a prerequisite for the activation of TCR. During T-cells differentiation, plays an important role in the development of T-helper 2 (Th2) cells following immune and inflammatory responses, and, in the development of inflammatory autoimmune diseases, is necessary for the activation of IL17-producing Th17 cells. May play a minor role in Th1 response. Upon TCR stimulation, mediates T-cell protective survival signal by phosphorylating BAD, thus protecting T-cells from BAD-induced apoptosis, and by up-regulating BCL-X(L)/BCL2L1 levels through NF-kappa-B and JUN pathways. In platelets, regulates signal transduction downstream of the ITGA2B, CD36/GP4, F2R/PAR1 and F2RL3/PAR4 receptors, playing a positive role in 'outside-in' signaling and granule secretion signal transduction. May relay signals from the activated ITGA2B receptor by regulating the uncoupling of WASP and WIPF1, thereby permitting the regulation of actin filament nucleation and branching activity of the Arp2/3 complex. May mediate inhibitory effects of free fatty acids on insulin signaling by phosphorylating IRS1, which in turn blocks IRS1 tyrosine phosphorylation and downstream activation of the PI3K/AKT pathway. Phosphorylates MSN (moesin) in the presence of phosphatidylglycerol or phosphatidylinositol. Phosphorylates PDPK1 at 'Ser-504' and 'Ser-532' and negatively regulates its ability to phosphorylate PKB/AKT1. Phosphorylates CCDC88A/GIV and inhibits its guanine nucleotide exchange factor activity .
PTM: Autophosphorylation at Thr-219 is required for targeting to the TCR and cellular function of PRKCQ upon antigen receptor ligation. Following TCR stimulation, phosphorylated at Tyr-90 and Ser-685.
Location Topology: Peripheral membrane protein
Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Sequence Mass (Da): 81865
Sequence Length: 706
Domain: The C1 domain, containing the phorbol ester/DAG-type region 1 (C1A) and 2 (C1B), is the diacylglycerol sensor and the C2 domain is a non-calcium binding domain.
Subcellular Location: Cytoplasm
EC: 2.7.11.13
|
Q05513 | MPSRTGPKMEGSGGRVRLKAHYGGDIFITSVDAATTFEELCEEVRDMCRLHQQHPLTLKWVDSEGDPCTVSSQMELEEAFRLARQCRDEGLIIHVFPSTPEQPGLPCPGEDKSIYRRGARRWRKLYRANGHLFQAKRFNRRAYCGQCSERIWGLARQGYRCINCKLLVHKRCHGLVPLTCRKHMDSVMPSQEPPVDDKNEDADLPSEETDGIAYISSSRKHDSIKDDSEDLKPVIDGMDGIKISQGLGLQDFDLIRVIGRGSYAKVLLVRLKKNDQIYAMKVVKKELVHDDEDIDWVQTEKHVFEQASSNPFLVGLHSCFQTTSRLFLVIEYVNGGDLMFHMQRQRKLPEEHARFYAAEICIALNFLHERGIIYRDLKLDNVLLDADGHIKLTDYGMCKEGLGPGDTTSTFCGTPNYIAPEILRGEEYGFSVDWWALGVLMFEMMAGRSPFDIITDNPDMNTEDYLFQVILEKPIRIPRFLSVKASHVLKGFLNKDPKERLGCRPQTGFSDIKSHAFFRSIDWDLLEKKQALPPFQPQITDDYGLDNFDTQFTSEPVQLTPDDEDAIKRIDQSEFEGFEYINPLLLSTEESV | Function: Calcium- and diacylglycerol-independent serine/threonine-protein kinase that functions in phosphatidylinositol 3-kinase (PI3K) pathway and mitogen-activated protein (MAP) kinase cascade, and is involved in NF-kappa-B activation, mitogenic signaling, cell proliferation, cell polarity, inflammatory response and maintenance of long-term potentiation (LTP). Upon lipopolysaccharide (LPS) treatment in macrophages, or following mitogenic stimuli, functions downstream of PI3K to activate MAP2K1/MEK1-MAPK1/ERK2 signaling cascade independently of RAF1 activation. Required for insulin-dependent activation of AKT3, but may function as an adapter rather than a direct activator. Upon insulin treatment may act as a downstream effector of PI3K and contribute to the activation of translocation of the glucose transporter SLC2A4/GLUT4 and subsequent glucose transport in adipocytes. In EGF-induced cells, binds and activates MAP2K5/MEK5-MAPK7/ERK5 independently of its kinase activity and can activate JUN promoter through MEF2C. Through binding with SQSTM1/p62, functions in interleukin-1 signaling and activation of NF-kappa-B with the specific adapters RIPK1 and TRAF6. Participates in TNF-dependent transactivation of NF-kappa-B by phosphorylating and activating IKBKB kinase, which in turn leads to the degradation of NF-kappa-B inhibitors. In migrating astrocytes, forms a cytoplasmic complex with PARD6A and is recruited by CDC42 to function in the establishment of cell polarity along with the microtubule motor and dynein. In association with FEZ1, stimulates neuronal differentiation in PC12 cells. In the inflammatory response, is required for the T-helper 2 (Th2) differentiation process, including interleukin production, efficient activation of JAK1 and the subsequent phosphorylation and nuclear translocation of STAT6. May be involved in development of allergic airway inflammation (asthma), a process dependent on Th2 immune response. In the NF-kappa-B-mediated inflammatory response, can relieve SETD6-dependent repression of NF-kappa-B target genes by phosphorylating the RELA subunit at 'Ser-311'. Phosphorylates VAMP2 in vitro .
PTM: CDH5 is required for its phosphorylation at Thr-410. Phosphorylated by protein kinase PDPK1; phosphorylation is inhibited by the apoptotic C-terminal cleavage product of PKN2. Phosphorylation at Thr-410 by PI3K activates the kinase.
Location Topology: Peripheral membrane protein
Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Sequence Mass (Da): 67660
Sequence Length: 592
Domain: The PB1 domain mediate mutually exclusive interactions with SQSTM1 and PARD6B.
Subcellular Location: Cytoplasm
EC: 2.7.11.13
|
P0C6Z8 | MDVNMAAELSPTNSSSSGELSVSPEPPRETQAFLGKVTVIDYFTFQHKHLKVTNIDDMTETLYVKLPENMTRCDHLPITCEYLLGRGSYGAVYAHADNATVKLYDSVTELYHELMVCDMIQIGKATAEDGQDKALVDYLSACTSCHALFMPQFRCSLQDYGHWHDGSIEPLVRGFQGLKDAVYFLNRHCGLFHSDISPSNILVDFTDTMWGMGRLVLTDYGTASLHDRNKMLDVRLKSSKGRQLYRLYCQREPFSIAKDTYKPLCLLSKCYILRGAGHIPDPSACGPVGAQTALRLDLQSLGYSLLYGIMHLADSTHKIPYPNPDMGFDRSDPLYFLQFAAPKVVLLEVLSQMWNLNLDMGLTSCGESPCVDVTAEHMSQFLQWCRSLKKRFKESYFFNCRPRFEHPHLPGLVAELLADDFFGPDGRRG | Function: Plays many key roles by phosphorylating several proteins including the viral DNA processivity factor BMRF1, EBNA1 or EBNA2. Modifies the host nuclear envelope structure and induces the redistribution of nuclear envelope-associated proteins by phosphorylating host nucleoporins. Subsequently, promotes the nuclear transport of EBV lytic proteins. Required for efficient lytic DNA replication and release of nucleocapsids from the nucleus. Contributes to the compaction of host cell chromatin in cells undergoing lytic replication, presumably by phosphorylating the host condensin complex and host TOP2A. Induces disassembly of the nuclear lamina by phosphorylating with host LMNA. Phosphorylates substrates involved in capsid assembly and DNA packaging. Facilitates the switch from latent to lytic DNA replication by down-regulating EBNA1 replication function. Phosphorylates the viral immediate-early protein BZLF1 and inhibits its sumoylation by interacting with host SUMO1 and SUMO2. Phosphorylates also host SAMHD1 and thereby counteracts its antiviral effect by reducing its dNTP hydrolase activity.
Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Sequence Mass (Da): 48351
Sequence Length: 429
Subcellular Location: Virion tegument
EC: 2.7.11.1
|
A7TFD7 | METQAVKTIRDELRELENTVAQASDMVLSEQDHRNASAIREMTQSVIAMSKENSLISVSNEIDYNEEIGNLAIDPSLIDEKIKQSNNFVELLKLTHLEQEALDYFLRYTISSTNTLELESTSDPKFVSLENEVTELENKTLTEHRDKIQEAKKDISDKSKDLANKQDQINELCLGAANSVDECWKMLNELEDIHSQRDNDVKETLSQDTTTTSDLIEETYKEWSSLQTSLTELNNSKDELDQLIAFKNEKHKDNDSTKIRNANIKNKTITENVKMLKLLINFWESNFIVPGSKKSKLSNLEVYPQTKKFQFKCAEQYTVIIQLNQNGGSIKSIEIFENDGKSVQENKNLSSLILNKYKNPLSSYPIFQVINDIVEELK | Function: Required for kinetochore binding by a discrete subset of kMAPs and motors. Involved in kinetochore-microtubule binding and the spindle assembly checkpoint (By similarity).
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 43331
Sequence Length: 378
Subcellular Location: Cytoplasm
|
Q04431 | MDTGSASIKDYETVLTDIEDSIAVSSEEVLNNQELRLKNTLHEITSSILAINEENKFVNPLRNDESLDVEGKEVFVNPKILSAKIKEFNKLMELLKLTYLEQETLDYFFRFTLSSTKPLQLDSEKDPQFVKLNERVNDLKEEISNVQESKIEQIKAEIQETGHNFAERQDLINELYLEATGDIENCWDSLNELKNLTNKEDKNMMGEKDTILNSSDSDDFVEETYTNWQKLLFLQKQNQRLTKELKEMHEVKNQIIRKGEQSKKEDSGHLMANESELCQSINLLTKFWEKHFLLKGSKTTILNFEIFTQLGKVQFEIKDMQYIIAISLSDLKRPMIKDITILQKAGGNIVTDIEASSKFNNKYRNNTKVQIFEVMDDIISELTNE | Function: Forms a kinetochore complex with SPC105 which is required for kinetochore binding by a discrete subset of kMAPs (BIM1, BIK1 and SLK19) and motors (CIN8, KAR3). Involved in kinetochore-microtubule binding and the spindle assembly checkpoint.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 44675
Sequence Length: 385
Subcellular Location: Cytoplasm
|
C5DZ48 | MKSDLDGYEVRIKSLENQTAHYSEQALLEQEQRVLASLREITQNVIAMGQENSLVEIKGELESKEESELVIDPSGFQEKIDTFVELVELLKVTHLEQETLDNFLRYTISSSNLLQINSVQDAKYVELESQVKELEQGTLESHKREIEATKGQIKNLCQELSMAQDSINETFLDTSNALEECDALLNELTQLRMEKQTSEEADTIEDDPVSQTYEDWESLQKSKLELRLLEEETSRLQSRVESYEDYQKRSRQLSNNDPRMLQNHKALELLVELWMTKFLPQPGISHLELFPQSRKFQFDVEPTFTVVITLADQTTFQNVQVYRKDAKSLVMDHGLNDEIKNSYLGTNNIYNGLNDIIHTLQRRVQAKGSN | Function: Required for kinetochore binding by a discrete subset of kMAPs and motors. Involved in kinetochore-microtubule binding and the spindle assembly checkpoint (By similarity).
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 42742
Sequence Length: 370
Subcellular Location: Cytoplasm
|
P27809 | MALFLSKRLLRFTVIAGAVIVLLLTLNSNSRTQQYIPSSISAAFDFTSGSISPEQQVISEENDAKKLEQSALNSEASEDSEAMDEESKALKAAAEKADAPIDTKTTMDYITPSFANKAGKPKACYVTLVRNKELKGLLSSIKYVENKINKKFPYPWVFLNDEPFTEEFKEAVTKAVSSEVKFGILPKEHWSYPEWINQTKAAEIRADAATKYIYGGSESYRHMCRYQSGFFWRHELLEEYDWYWRVEPDIKLYCDINYDVFKWMQENEKVYGFTVSIHEYEVTIPTLWQTSMDFIKKNPEYLDENNLMSFLSNDNGKTYNLCHFWSNFEIANLNLWRSPAYREYFDTLDHQGGFFYERWGDAPVHSIAAALFLPKDKIHYFSDIGYHHPPYDNCPLDKEVYNSNNCECDQGNDFTFQGYSCGKEYYDAQGLVKPKNWKKFRE | Function: Mannosyltransferase that transfers an alpha-D-mannosyl residue from GDP-mannose into lipid-linked oligosaccharide, forming an alpha-(1->2)-D-mannosyl-D-mannose linkage. Required for the attachment of the third mannose residue of O-linked saccharides.
Location Topology: Single-pass type II membrane protein
Sequence Mass (Da): 51387
Sequence Length: 442
Pathway: Protein modification; protein glycosylation.
Subcellular Location: Golgi apparatus membrane
EC: 2.4.1.-
|
P87023 | MASQRDLTSNNPHFHISSSRNNTNDDFNSDHNPRNPFGDEPEEEEELDSASFSSSSQNNQPHHPFATSNQTSSTNNLHSTNSIRNEAEYGKPFQAYSGYYSNGGSSSYLNQEGVISDESRLLSSGNNNNNNNNNRDVSSVGGGGGSGDNRLNPTSPAEFDRYPSMAGSRVVSSTSLVSFNNPSNMMRNHHQHQPHLGSSSSPTSSSMNNDSISDKSTSPFPNDFSPFGGYPASSFPLSIDEKEPDDYLNNPDPVQDAEYEKNRFMHDLKNMDKRSLGGLIGFIILFIAALAVFIILPALTYSGATNPYHPESYEVLTKYSYPMLSAIRMNLVDPDTPESAYKKKAKDGSEWVLVFSDEFDAEGRTFYEGDDQFFTAPDIHYDATKDLEWYDPDAVTTANGTLNLRMDAYKNHNLFYRSGMVQSWNQLCYTQGHLEISARLPNYGNVTGLWPGLWSMGNLGRPGYLGSTDGVWPYSYDSCDAGITPNQSSPDGISYLPGQRLNKCTCPGELHPNRGVGRGAPEIDVIEGEVMTDSSGKKENCGVASQSLQLAPMDIWYIPDYNWVEIYNFSVSTMNTYTGGPFQQALSATTMLNVTWYEFGDNAHNFQTYGYEYLNDPETGYLRWFVGDDPTLTVYSQALHPDGNIGWRPLSKEPMSLILNLGISNNWAYIDWPSISFPVTFRIDYVRVYQPPDQINVGCDPTDFPTYDYIQQHLNLYENANITSFEDGGYKFPKNSLIGC | Function: Involved in the synthesis of (1->6)- and (1->3)-beta-D-glucan polymers of the yeast cell wall in vivo. It is required for full activity of beta-glucan synthase in vitro. It may be a beta-glucan synthase, part of a multiprotein glucan synthase or a modulator.
Location Topology: Single-pass type II membrane protein
Sequence Mass (Da): 82457
Sequence Length: 740
Subcellular Location: Golgi apparatus membrane
|
P32486 | MPLRNLTETHNFSSTNLDTDGTGDDHDGAPLSSSPSFGQQNDNSTNDNAGLTNPFMGSDEESNARDGESLSSSVHYQPQGSDSSLLHDNSRLDLSQNKGVSDYKGYYSRNNSRAVSTANDNSFLQPPHRAIASSPSLNSNLSKNDILSPPEFDRYPLVGSRVTSMTQLNHHGRSPTSSPGNESSASFSSNPFLGEQDFSPFGGYPASSFPLMIDEKEEDDYLHNPDPEEEARLDRRRFIDDFKYMDKRSASGLAGVLLLFLAAIFIFIVLPALTFTGAIDHESNTEEVTYLTQYQYPQLSAIRTSLVDPDTPDTAKTREAMDGSKWELVFSDEFNAEGRTFYDGDDPYWTAPDVHYDATKDLEWYSPDASTTVNGTLQLRMDAFKNHGLYYRSGMLQSWNKVCFTQGALEISANLPNYGRVSGLWPGLWTMGNLGRPGYLASTQGVWPYSYESCDAGITPNQSSPDGISYLPGQKLSICTCDGEDHPNQGVGRGAPEIDVLEGETDTKIGVGIASQSLQIAPFDIWYMPDYDFIEVYNFTTTTMNTYAGGPFQQAVSAVSTLNVTWYEFGEYGGYFQKYAIEYLNDDDNGYIRWFVGDTPTYTIHAKALHPDGNIGWRRISKEPMSIILNLGISNNWAYIDWQYIFFPVVMSIDYVRIYQPSNAISVTCDPSDYPTYDYIQSHLNAFQNANLTTWEDAGYTFPKNILTGKCTSSKFKLSS | Function: Involved in the synthesis of (1->6)- and (1->3)-beta-D-glucan polymers of the yeast cell wall in vivo. It is required for full activity of beta-glucan synthase in vitro. May be involved in the maturation and transport of cell wall proteins (CWP) to the cell wall. May act as a transglucosidase and contribute to the construction of a protein-bound glucan-structure that acts as an acceptor site for the addition of (1->6)-beta-D-glucan at the cell surface.
Location Topology: Single-pass type II membrane protein
Sequence Mass (Da): 80123
Sequence Length: 720
Subcellular Location: Golgi apparatus membrane
|
O74226 | MRQFQIILISLVVSIIRCVVADVDITSPKSGETFSGSSGSASIKITWDDSDDSDSPKSLDNAKGYTISLCTGPTSDGDIQCLDPLVKNEAIAGKSKTVSIPQNSVPNGYYYFQIYVTFTNGGTTIHYSPRFKLTGMSGPTATLDVTETGSVPADQASGFDTATTADSKSFTVPYTLQTGKTRYAPMQMQPGTKVTATTWSMKFPTSAVTYYSTKAGTPNVASTITPGWSYTAESAVNYASVAPYPTYWYPASERVSKATISAATKRRRWLD | Function: Involved in cell wall beta(1->6) glucan synthesis.
PTM: O-glycosylated.
Sequence Mass (Da): 29126
Sequence Length: 271
Subcellular Location: Secreted
|
O74683 | MLLLAILLSLFALIRADVNIVEPGPGDTFSGADGTVSINLKWVDNGAYPPLDKVAYYLFSLCYGPNTKIQCVYKPDTKITPDDLDKDDAGTYSYKFDIQSSVVGSGQFYVQVFAWVDGQGYTLHYTPRIELTNMGGPTTFELLTYTDTIQPVPQTSIRTGTDTNTQSFDASSVYSLPYTEQTLKTRVAPIQQQPGTKVTATTWSRRYPTSAVTFYSTFRSSLDQLSTLTPAWNYTVSSAVNYATPAAMPSDNGGWYNPIKRQSLSTRKLNVRYLSS | Function: Involved in cell wall beta(1->6) glucan synthesis.
PTM: O-glycosylated.
Sequence Mass (Da): 30549
Sequence Length: 276
Subcellular Location: Secreted
|
P39005 | MRLQRNSIICALVFLVSFVLGDVNIVSPSSKATFSPSGGTVSVPVEWMDNGAYPSLSKISTFTFSLCTGPNNNIDCVAVLASKITPSELTQDDKVYSYTAEFASTLTGNGQYYIQVFAQVDGQGYTIHYTPRFQLTSMGGVTAYTYSATTEPTPQTSIQTTTTNNAQATTIDSRSFTVPYTKQTGTSRFAPMQMQPNTKVTATTWTRKFATSAVTYYSTFGSLPEQATTITPGWSYTISSGVNYATPASMPSDNGGWYKPSKRLSLSARKINMRKV | Function: Involved in cell wall beta(1->6) glucan synthesis.
PTM: O-glycosylated.
Sequence Mass (Da): 29989
Sequence Length: 276
Subcellular Location: Secreted
|
Q96MU8 | MAPPAARLALLSAAALTLAARPAPSPGLGPECFTANGADYRGTQNWTALQGGKPCLFWNETFQHPYNTLKYPNGEGGLGEHNYCRNPDGDVSPWCYVAEHEDGVYWKYCEIPACQMPGNLGCYKDHGNPPPLTGTSKTSNKLTIQTCISFCRSQRFKFAGMESGYACFCGNNPDYWKYGEAASTECNSVCFGDHTQPCGGDGRIILFDTLVGACGGNYSAMSSVVYSPDFPDTYATGRVCYWTIRVPGASHIHFSFPLFDIRDSADMVELLDGYTHRVLARFHGRSRPPLSFNVSLDFVILYFFSDRINQAQGFAVLYQAVKEELPQERPAVNQTVAEVITEQANLSVSAARSSKVLYVITTSPSHPPQTVPGSNSWAPPMGAGSHRVEGWTVYGLATLLILTVTAIVAKILLHVTFKSHRVPASGDLRDCHQPGTSGEIWSIFYKPSTSISIFKKKLKGQSQQDDRNPLVSD | Function: Receptor for Dickkopf proteins. Cooperates with DKK1/2 to inhibit Wnt/beta-catenin signaling by promoting the endocytosis of Wnt receptors LRP5 and LRP6. In the absence of DKK1, potentiates Wnt-beta-catenin signaling by maintaining LRP5 or LRP6 at the cell membrane. Can trigger apoptosis in a Wnt-independent manner and this apoptotic activity is inhibited upon binding of the ligand DKK1. Plays a role in limb development; attenuates Wnt signaling in the developing limb to allow normal limb patterning and can also negatively regulate bone formation. Modulates cell fate decisions in the developing cochlea with an inhibitory role in hair cell fate specification.
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 51744
Sequence Length: 473
Subcellular Location: Cell membrane
|
Q99N43 | MAPPAARLALLSAAALTLAARPAPGPRSGPECFTANGADYRGTQSWTALQGGKPCLFWNETFQHPYNTLKYPNGEGGLGEHNYCRNPDGDVSPWCYVAEHEDGVYWKYCEIPACQMPGNLGCYKDHGNPPPLTGTSKTSNKLTIQTCISFCRSQRFKFAGMESGYACFCGNNPDYWKHGEAASTECNSVCFGDHTQPCGGDGRIILFDTLVGACGGNYSAMAAVVYSPDFPDTYATGRVCYWTIRVPGASRIHFNFTLFDIRDSADMVELLDGYTHRVLVRLSGRSRPPLSFNVSLDFVILYFFSDRINQAQGFAVLYQATKEEPPQERPAVNQTLAEVITEQANLSVSAAHSSKVLYVITPSPSHPPQTAPGSHSWAPSVGANSHRVEGWTVYGLATLLILTVTAVVAKILLHVTFKSHRVPASGDLRDCRQPGASGDIWTIFYEPSTTISIFKKKLKGQSQQDDRNPLVSD | Function: Receptor for Dickkopf proteins. Cooperates with DKK1/2 to inhibit Wnt/beta-catenin signaling by promoting the endocytosis of Wnt receptors LRP5 and LRP6 . In the absence of DKK1, potentiates Wnt-beta-catenin signaling by maintaining LRP5 or LRP6 at the cell membrane (By similarity). Can trigger apoptosis in a Wnt-independent manner and this apoptotic activity is inhibited upon binding of the ligand DKK1 . Plays a role in limb development; attenuates Wnt signaling in the developing limb to allow normal limb patterning and can also negatively regulate bone formation . Modulates cell fate decisions in the developing cochlea with an inhibitory role in hair cell fate specification .
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 51673
Sequence Length: 473
Subcellular Location: Cell membrane
|
A0A3G1QTS7 | MSLLLSNSVLVGPKFRSSRISHASASLDIGLQRATSPQNASVPTCFEETKGRIAKLFHKNELSVSTYDTAWVAMVPSPTSSEEPCFPACLNWLLENQCHDGSWARPHHHHMLKKDVLSSTLACILALKKWGVGEEQINRGLHFVELNFASATEKGQITPMGFDIIFPAMLDNARGLSLNLQLEPTMLNDLIYKRDLELKRCNQSNSAEKEVYWAHIAEGMGKLHDWESVMKYQRKNGSLFNCPSTTAAAFTALRNSDCLNYLCLALEKFGSAVPAVYPLDIYSQLCTVGNLERLGISRYFLTEIQSVLDETYRSWLQGDEEIFMDASTCALAFRTLRMNGYNVTSDPITKILQECFSSSFRGNMTDNNTTLEIYRASELILYPEERDLVQHNLRLKTFLEQELSSNGFIQSCQLGRNINAEVNQAIEYPFYAIMDRMAKRKNIENYNIDNTRILKTSYRSPNFGNKDFLSLSVEDFNRCQVIHREELRELERWVIENRLDELKFARSKAAYCYFSAAATIFSPELSDARMSWAKNGVLTTVVDDFFDVGGSVEELKNLIQLVELWDVDVSTQCCSPNVQIIFSALKHTICEIADKGFKLQGRSITDHIISIWLDLLYSMMKETELGIDKSFPTMDEYMSNAYVSFALGPIVLPALYLVGPKLSEEMVNHSEYHTLFKLMSTCGRLLNDIRGYERELKDGKISAVSLYIMNNGGEITTEAAISEMRSWIERDRRELLRLVLEENKSVLPKACKKLFWHMCTVVHVFYSKDDGFTSLNLHGVVNAIINEPIVLNQF | Cofactor: Binds 3 Mg(2+) ions per subunit.
Function: Involved in the biosynthesis of ent-kaurene diterpenoids natural products such as oridonin, miltiradiene, eriocalyxin B and nezukol, known to exhibit antitumor, anti-inflammatory and antibacterial activities, and in the production of gibberellins phytohormones . Catalyzes the conversion of ent-copalyl diphosphate (ent-CPP) to ent-kaurene .
Catalytic Activity: ent-copalyl diphosphate = diphosphate + ent-kaur-16-ene
Sequence Mass (Da): 90262
Sequence Length: 794
Domain: The Asp-Asp-Xaa-Xaa-Asp/Glu (DDXXD/E) motif is important for the catalytic activity, presumably through binding to Mg(2+).
Pathway: Secondary metabolite biosynthesis; terpenoid biosynthesis.
Subcellular Location: Plastid
EC: 4.2.3.19
|
Q9XEH9 | MNLSLCIASPLLTKSSRPTALSAIHTASTSHGGQTNPTNLIIDTTKERIQKLFKNVEISVSSYDTAWVAMVPSPNSPKSPCFPECLNWLINNQLNDGSWGLVNHTHNHNHPLLKDSLSSTLACIVALKRWNVGEDQINKGLSFIESNLASATDKSQPSPIGFDIIFPGLLEYAKNLDINLLSKQTDFSLMLHKRELEQKRCHSNEIDGYLAYISEGLGNLYDWNMVKKYQMKNGSVFNSPSATAAAFINHQNPGCLNYLNSLLDKFGNAVPTVYPLDLYIRLSMVDTIERLGISHHFRVEIKNVLDETYRCWVERDEQIFMDVVTCALAFRLLRIHGYKVSPDQLAEITNELAFKDEYAALETYHASQILYQEDLSSGKQILKSADFLKGILSTDSNRLSKLIHKEVENALKFPINTGLERINTRRNIQLYNVDNTRILKTTYHSSNISNTYYLRLAVEDFYTCQSIYREELKGLERWVVQNKLDQLKFARQKTAYCYFSVAATLSSPELSDARISWAKNGILTTVVDDFFDIGGTIDELTNLIQCVEKWNVDVDKDCCSEHVRILFLALKDAICWIGDEAFKWQARDVTSHVIQTWLELMNSMLREAIWTRDAYVPTLNEYMENAYVSFALGPIVKPAIYFVGPKLSEEIVESSEYHNLFKLMSTQGRLLNDIHSFKREFKEGKLNAVALHLSNGESGKVEEEVVEEMMMMIKNKRKELMKLIFEENGSIVPRACKDAFWNMCHVLNFFYANDDGFTGNTILDTVKDIIYNPLVLVNENEEQR | Cofactor: Binds 3 Mg(2+) ions per subunit.
Function: Involved in the biosynthesis of ent-kaurene diterpenoids natural products such as oridonin, miltiradiene, eriocalyxin B and nezukol, known to exhibit antitumor, anti-inflammatory and antibacterial activities, and in the production of gibberellins phytohormones . Catalyzes the conversion of ent-copalyl diphosphate (ent-CPP) to ent-kaurene .
Catalytic Activity: ent-copalyl diphosphate = diphosphate + ent-kaur-16-ene
Sequence Mass (Da): 89402
Sequence Length: 784
Domain: The Asp-Asp-Xaa-Xaa-Asp/Glu (DDXXD/E) motif is important for the catalytic activity, presumably through binding to Mg(2+).
Pathway: Secondary metabolite biosynthesis; terpenoid biosynthesis.
Subcellular Location: Plastid
EC: 4.2.3.19
|
Q5F1N4 | MKLKISFLILVLFSVFFAIEGIIKWFPASVNGKGHSSCTNGLEMTEEDFCKMLCGIDGKLRESKCVDHWCYCSQILFP | Function: Reversibly inhibits potassium channels.
PTM: Contains 3 disulfide bonds.
Sequence Mass (Da): 8856
Sequence Length: 78
Subcellular Location: Secreted
|
Q21734 | MGLQRGMPLAQLGEPFGITPSSIENVSPGIDQCKDHRMDVSMRSDPTDCSSDTTNTFHSSIHIIQPPPNNGFRLMNWKTDSSSETEIDIGDVRKCGEKADPRQFELLKVLGQGSFGKVFLVRKVRGRDSGHVYAMKVLKKATLKVRDRQRTKLERNILAHISHPFIVKLHYAFQTEGKLYLILDFLRGGDLFTRLSKEVMFTEDDVKFYLAELTLALEHLHSLGIVYRDLKPENILLDADGHIKVTDFGLSKEAIDSEKKTYSFCGTVEYMAPEVINRRGHSMAADFWSLGVLMFEMLTGHLPFQGRDRNDTMTQILKAKLSMPHFLTQEAQSLLRALFKRNSQNRLGAGPDGVEEIKRHAFFAKIDFVKLLNKEIDPPFKPALSTVDSTSYFDPEFTKRTPKDSPALPASANGHEIFRGFSFVSNAVMEERKLIAKSVRSVPTAKTNPFTDDYEILEKIGNGAHSVVHKCQMKATRRKYAVKIVKKAVFDATEEVDILLRHSHHQFVVKLFDVYEDETAIYMIEELCEGGELLDKLVNKKSLGSEKEVAAIMANLLNAVQYLHSQQVAHRDLTAANILFALKDGDPSSLRIVDFGFAKQSRAENGMLMTPCYTAQFVAPEVLRKQGYDRSCDVWSLGVLLHTMLTGCTPFAMGPNDTPDQILQRVGDGKISMTHPVWDTISDEAKDLVRKMLDVDPNRRVTAKQALQHKWIGQKEALPDRPIQSEQVGELDMQNVKVALEQTYKAIASAPSVQLRPVGSSALAKRRMKEILYANYTKNVSANA | Function: Serine/threonine kinase that may play a role in mediating the growth-factor and stress induced activation of transcription (By similarity). Suppresses germline tumor formation by preventing the dedifferentiation of secondary spermatocytes probably downstream of mpk-1 .
PTM: Autophosphorylated on Ser-422, as part of the activation process.
Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Sequence Mass (Da): 88120
Sequence Length: 784
EC: 2.7.11.1
|
Q15418 | MPLAQLKEPWPLMELVPLDPENGQTSGEEAGLQPSKDEGVLKEISITHHVKAGSEKADPSHFELLKVLGQGSFGKVFLVRKVTRPDSGHLYAMKVLKKATLKVRDRVRTKMERDILADVNHPFVVKLHYAFQTEGKLYLILDFLRGGDLFTRLSKEVMFTEEDVKFYLAELALGLDHLHSLGIIYRDLKPENILLDEEGHIKLTDFGLSKEAIDHEKKAYSFCGTVEYMAPEVVNRQGHSHSADWWSYGVLMFEMLTGSLPFQGKDRKETMTLILKAKLGMPQFLSTEAQSLLRALFKRNPANRLGSGPDGAEEIKRHVFYSTIDWNKLYRREIKPPFKPAVAQPDDTFYFDTEFTSRTPKDSPGIPPSAGAHQLFRGFSFVATGLMEDDGKPRAPQAPLHSVVQQLHGKNLVFSDGYVVKETIGVGSYSECKRCVHKATNMEYAVKVIDKSKRDPSEEIEILLRYGQHPNIITLKDVYDDGKHVYLVTELMRGGELLDKILRQKFFSEREASFVLHTIGKTVEYLHSQGVVHRDLKPSNILYVDESGNPECLRICDFGFAKQLRAENGLLMTPCYTANFVAPEVLKRQGYDEGCDIWSLGILLYTMLAGYTPFANGPSDTPEEILTRIGSGKFTLSGGNWNTVSETAKDLVSKMLHVDPHQRLTAKQVLQHPWVTQKDKLPQSQLSHQDLQLVKGAMAATYSALNSSKPTPQLKPIESSILAQRRVRKLPSTTL | Function: Serine/threonine-protein kinase that acts downstream of ERK (MAPK1/ERK2 and MAPK3/ERK1) signaling and mediates mitogenic and stress-induced activation of the transcription factors CREB1, ETV1/ER81 and NR4A1/NUR77, regulates translation through RPS6 and EIF4B phosphorylation, and mediates cellular proliferation, survival, and differentiation by modulating mTOR signaling and repressing pro-apoptotic function of BAD and DAPK1. In fibroblast, is required for EGF-stimulated phosphorylation of CREB1, which results in the subsequent transcriptional activation of several immediate-early genes. In response to mitogenic stimulation (EGF and PMA), phosphorylates and activates NR4A1/NUR77 and ETV1/ER81 transcription factors and the cofactor CREBBP. Upon insulin-derived signal, acts indirectly on the transcription regulation of several genes by phosphorylating GSK3B at 'Ser-9' and inhibiting its activity. Phosphorylates RPS6 in response to serum or EGF via an mTOR-independent mechanism and promotes translation initiation by facilitating assembly of the pre-initiation complex. In response to insulin, phosphorylates EIF4B, enhancing EIF4B affinity for the EIF3 complex and stimulating cap-dependent translation. Is involved in the mTOR nutrient-sensing pathway by directly phosphorylating TSC2 at 'Ser-1798', which potently inhibits TSC2 ability to suppress mTOR signaling, and mediates phosphorylation of RPTOR, which regulates mTORC1 activity and may promote rapamycin-sensitive signaling independently of the PI3K/AKT pathway. Mediates cell survival by phosphorylating the pro-apoptotic proteins BAD and DAPK1 and suppressing their pro-apoptotic function. Promotes the survival of hepatic stellate cells by phosphorylating CEBPB in response to the hepatotoxin carbon tetrachloride (CCl4). Mediates induction of hepatocyte prolifration by TGFA through phosphorylation of CEBPB (By similarity). Is involved in cell cycle regulation by phosphorylating the CDK inhibitor CDKN1B, which promotes CDKN1B association with 14-3-3 proteins and prevents its translocation to the nucleus and inhibition of G1 progression. Phosphorylates EPHA2 at 'Ser-897', the RPS6KA-EPHA2 signaling pathway controls cell migration . In response to mTORC1 activation, phosphorylates EIF4B at 'Ser-406' and 'Ser-422' which stimulates bicarbonate cotransporter SLC4A7 mRNA translation, increasing SLC4A7 protein abundance and function .
PTM: Activated by phosphorylation at Ser-221 by PDPK1. Autophosphorylated on Ser-380, as part of the activation process. May be phosphorylated at Thr-359 and Ser-363 by MAPK1/ERK2 and MAPK3/ERK1.
Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Sequence Mass (Da): 82723
Sequence Length: 735
Subcellular Location: Nucleus
EC: 2.7.11.1
|
P18653 | MPLAQLKEPWPLMELVPLDPENGQTSGEEAGLQPSKDEAILKEISITHHVKAGSEKADPSQFELLKVLGQGSFGKVFLVRKVTRPDSGHLYAMKVLKKATLKVRDRVRTKMERDILADVNHPFVVKLHYAFQTEGKLYLILDFLRGGDLFTRLSKEVMFTEEDVKFYLAELALGLDHLHSLGIIYRDLKPENILLDEEGHIKLTDFGLSKEAIDHEKKAYSFCGTVEYMAPEVVNRQGHTHSADWWSYGVLMGKDRKETMTLILKAKLGMPQFLSTEAQSLLRALFKRNPANRLGSGPDGAEEIKRHIFYSTIDWNKLYRREIKPPFKPAVAQPDDTFYFDTEFTSRTPRDSPGIPPSAGAHQLFRGFSFVATGLMEDDGKPRTTQAPLHSVVQQLHGKNLVFSDGYVVKETIGVGSYSVCKRCVHKATNMEYAVKVIDKSKRDPSEEIEILLRYGQHPNIITLKDVYDDGKHVYLVTELMRGGELLDKILRQKFFSEREASFVLHTISKTVEYLHSQGVVHRDLKPSNILYVDESGNPECLRICDFGFAKQLRAENGLLMTPCYTANFVAPEVLKRQGYDEGCDIWSLGILLYTMLAGYTPFANGPSDTPEEILTRIGSGKFTLSGGNWNTVSETAKDLVSKMLHVDPHQRLTAKQVLQHPWITQKDKLPQSQLSHQDLQLVKGAMAATYSALNSSKPTPQLKPIESSILAQRRVRKLPSTTL | Function: Serine/threonine-protein kinase that acts downstream of ERK (MAPK1/ERK2 and MAPK3/ERK1) signaling and mediates mitogenic and stress-induced activation of the transcription factors CREB1, ETV1/ER81 and NR4A1/NUR77, regulates translation through RPS6 and EIF4B phosphorylation, and mediates cellular proliferation, survival, and differentiation by modulating mTOR signaling and repressing pro-apoptotic function of BAD and DAPK1. In fibroblast, is required for EGF-stimulated phosphorylation of CREB1, which results in the subsequent transcriptional activation of several immediate-early genes. In response to mitogenic stimulation (EGF and PMA), phosphorylates and activates NR4A1/NUR77 and ETV1/ER81 transcription factors and the cofactor CREBBP. Upon insulin-derived signal, acts indirectly on the transcription regulation of several genes by phosphorylating GSK3B at 'Ser-9' and inhibiting its activity. Phosphorylates RPS6 in response to serum or EGF via an mTOR-independent mechanism and promotes translation initiation by facilitating assembly of the pre-initiation complex. In response to insulin, phosphorylates EIF4B, enhancing EIF4B affinity for the EIF3 complex and stimulating cap-dependent translation. Is involved in the mTOR nutrient-sensing pathway by directly phosphorylating TSC2 at 'Ser-1798', which potently inhibits TSC2 ability to suppress mTOR signaling, and mediates phosphorylation of RPTOR, which regulates mTORC1 activity and may promote rapamycin-sensitive signaling independently of the PI3K/AKT pathway. Mediates cell survival by phosphorylating the pro-apoptotic proteins BAD and DAPK1 and suppressing their pro-apoptotic function. Promotes the survival of hepatic stellate cells by phosphorylating CEBPB in response to the hepatotoxin carbon tetrachloride (CCl4). Mediates induction of hepatocyte prolifration by TGFA through phosphorylation of CEBPB . Is involved in cell cycle regulation by phosphorylating the CDK inhibitor CDKN1B, which promotes CDKN1B association with 14-3-3 proteins and prevents its translocation to the nucleus and inhibition of G1 progression (By similarity). Phosphorylates EPHA2 at 'Ser-897', the RPS6KA-EPHA2 signaling pathway controls cell migration (By similarity). In response to mTORC1 activation, phosphorylates EIF4B at 'Ser-406' and 'Ser-422' which stimulates bicarbonate cotransporter SLC4A7 mRNA translation, increasing SLC4A7 protein abundance and function (By similarity).
PTM: Activated by phosphorylation at Ser-221 by PDPK1. Autophosphorylated on Ser-369, as part of the activation process. May be phosphorylated at Thr-348 and Ser-352 by MAPK1/ERK2 and MAPK3/ERK1 (By similarity).
Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Sequence Mass (Da): 81595
Sequence Length: 724
Subcellular Location: Nucleus
EC: 2.7.11.1
|
Q18846 | MEDILMPEGEKVSMENFALLRVLGKGAYGKVFLVRKVGGKDHNTIYAMKVLRKTRVLTKQKTLEHTMAERQVLERLRGTPFLVNLFYAFQTDTKLHIVMEYVRGGELFTHLCSRGHFDLEAARFVIAELVVAIDSLHQRKVIYRDLKLENILLDEEGHVKLTDFGLSKLFLPGELDRANSYCGTIEYMSPEVINRPEGGYSDVVDWWSLGVISFELLTGCSPFTVDGAQNSSKDIAKRIMTKKVPFPKTMDVDARDFIGQLLEKKLEKRLGYNGVDEIKNHKFMSSIDWDAAVKRTLKPVIVPRIGHDLDTQFFSAEFTSQPPLYSPAESPLNANTLFRGYSYVSPSVIFANDNVIGEELMAEDVNALLASSSFFAKYKLDKSDAGLLGKGAFSVVRRCERVVDGAQFAVKIVSQKFASQAQREARILEMVQGHPNIVQLHDVHSDPLHFYLVMEILTGNELLERIRKLERFTESEAADIMRQLVSAVKYLHDKRIVHRDLKPENILFESIDSSARLRLVDFGFARLLPNSMEQQLKSVQVLRKMTPCFTLQYAAPEVLDVGDSQPEYNEQCDLWSLGVVLFTMLSGQVPFHARSRQESATEIMQRICRAEFSFTGDAWTNVSADAKNLITGLLTVDPKKRLSMQELTAHMWLKSSASMDTPLQTPSILPSSADETFNETLRAFLHANRDGFHLLDVAAAPLMKRRGIKRQSGDKDASGNSKNSRVTQFECLPEEQEAEMTSSTSRPSNLGMMNYREPNSGTIRETRGSDSS | Function: Serine/threonine kinase that may play a role in mediating the mitogen- and stress-induced effects on transcription. May repress transcription via phosphorylation of 'Ser-1' of histone H2A. May phosphorylate histone H3 (By similarity).
Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Sequence Mass (Da): 87069
Sequence Length: 772
Domain: Enzyme activity requires the presence of both kinase domains.
EC: 2.7.11.1
|
Q2FV31 | MNEQWLEHLPLKDIKEISPVSGGDVNEAYRVETDTDTFFLLVQRGRKESFYAAEIAGLNEFERAGITAPRVIASGEVNGDAYLVMTYLEEGASGSQRQLGQLVAQLHSQQQEEGKFGFSLPYEGGDISFDNHWQDDWCTIFVDKRLDHLKDELLNRGLWDANDIKVYDKVRRQIVAELEKHQSKPSLLHGDLWGGNYMFLQDGRPALFDPAPLYGDREFDIGITTVFGGFTSEFYDAYNKHYPLAKGASYRLEFYRLYLLMVHLLKFGEMYRDSVAHSMDKILQDTTS | Function: Ketoamine kinase that phosphorylates ketoamines, such as erythruloselysine and ribuloselysine, on the third carbon of the sugar moiety to generate ketoamine 3-phosphate . Has higher activity on free lysine (erythruloselysine and ribuloselysine), than on ribuloselysine and erythruloselysine residues on glycated proteins .
Catalytic Activity: ATP + N(6)-(D-ribulosyl)-L-lysine = ADP + H(+) + N(6)-(3-O-phospho-D-ribulosyl)-L-lysine
Sequence Mass (Da): 32988
Sequence Length: 288
EC: 2.7.1.-
|
Q5SJ35 | MDPLALLRKAGLEAEGPALPLHGGDISRVWRVGRFVVKTAQDPPPGLFRAEARGLQALAERGVRVPRVHWVGEEGLVLAYLEPGPEDWEGLARTLAALHRRREGSYLAEPGFLGTFPLPGREGGEWTAFFYERCVLPLLEATWDRLQGLGPKVEALYQRPLPAEGPAPLHGDLWHGNVYFAREGPALLDPSFFVGERGVDLAMMRLFGGFPRRFWEVYGELYPVPEEVERALPRYQVYYLLAHVHFFGQGYLGALWRAISAS | Function: Ketoamine kinase that phosphorylates ketoamines, such as erythruloselysine and ribuloselysine, on the third carbon of the sugar moiety to generate ketoamine 3-phosphate . Has higher activity on free lysine (erythruloselysine and ribuloselysine), than on ribuloselysine and erythruloselysine residues on glycated proteins .
Catalytic Activity: ATP + N(6)-(D-ribulosyl)-L-lysine = ADP + H(+) + N(6)-(3-O-phospho-D-ribulosyl)-L-lysine
Sequence Mass (Da): 29325
Sequence Length: 262
EC: 2.7.1.-
|
Q071E0 | MFPAVNEIKVQTWRRDQRGECPRRSAQCRLFSCAHRECAPAARSLENRGPENRTARPEATMSGDVLCNGHSAFHRLLKHSSSRTHEALVVKIIQENKNTPLFCTAPEPRRDSGVNGEFLLNSAELQDEQTLPLHCIHSAADITSSKHRKPARRKVKRSTKRAAESKSPANRKVTDYFPIRRSSRKSKSELKYEEKQHIDTLISNGIEDGMMVRFIEGKGRGVFATQPFQKGQYVVEYHGDLLQITDAKQREALYAQDPSTGCYMYYFQYLSKTYCVDATKESDRLGRLINHSKNGNCQTKLHAIAGKPHLILVASRDIQEGEELLYDYGDRSKSSIEAHPWLKH | Function: Protein-lysine N-methyltransferase that monomethylates both histones and non-histone proteins. Specifically monomethylates 'Lys-20' of histone H4 (H4K20me1). H4K20me1 is enriched during mitosis and represents a specific tag for epigenetic transcriptional repression. Mainly functions in euchromatin regions, thereby playing a central role in the silencing of euchromatic genes. Required for cell proliferation, probably by contributing to the maintenance of proper higher-order structure of DNA during mitosis. Involved in chromosome condensation and proper cytokinesis.
Catalytic Activity: L-lysyl(20)-[histone H4] + S-adenosyl-L-methionine = H(+) + N(6)-methyl-L-lysyl(20)-[histone H4] + S-adenosyl-L-homocysteine
Sequence Mass (Da): 39155
Sequence Length: 344
Subcellular Location: Nucleus
EC: 2.1.1.-
|
Q498E6 | MGRGKKMSKPGDGRSGDVPETCRTGGTNENHPKMNGEVVHLGQPKIYSYMSPTKSPSGRPPLQEENSVAHHESKNLGKPTTETRKKAEVEKKRISSATELSVKSSKQRETECNSIGEYFQTKQELTDVQRNTALTPVDKLQSQKMVKNKSQRRKAQRKKSPNRKLTDYYPVRRSCRKSKTELESEEKMRIDELIQTGKEDGMKMDMIIGKGRGVIATRDFQRGEFVVEYHGDLIEITDAKRREASYAQDSATGCYMYYFQYLNKTYCIDATRETGRLGRLINHSKSGNCHTKLHNISNVPHLILVASRDILVGEELLYDYGDRRKSSIEAHPWLKN | Function: Protein-lysine N-methyltransferase that monomethylates both histones and non-histone proteins. Specifically monomethylates 'Lys-20' of histone H4 (H4K20me1). H4K20me1 is enriched during mitosis and represents a specific tag for epigenetic transcriptional repression. Mainly functions in euchromatin regions, thereby playing a central role in the silencing of euchromatic genes. Required for cell proliferation, probably by contributing to the maintenance of proper higher-order structure of DNA during mitosis. Involved in chromosome condensation and proper cytokinesis.
PTM: Phosphorylated during mitosis.
Catalytic Activity: L-lysyl(20)-[histone H4] + S-adenosyl-L-methionine = H(+) + N(6)-methyl-L-lysyl(20)-[histone H4] + S-adenosyl-L-homocysteine
Sequence Mass (Da): 38291
Sequence Length: 336
Subcellular Location: Nucleus
EC: 2.1.1.-
|
Q1HQF8 | MAVPTSVSLVLASVTAVLIFSAMQMYKPLIASSQMATVFGGFLGSWLFILSLTAVSNLEAVVLGKGFQAKLFPEVAFCLIGSLFACGMVHRVCATTCILFSVAALYYINRISQKVHNAPVPVDTYAGKKKKK | Function: Subunit of the oligosaccharyl transferase (OST) complex that catalyzes the initial transfer of a defined glycan (Glc(3)Man(9)GlcNAc(2) in eukaryotes) from the lipid carrier dolichol-pyrophosphate to an asparagine residue within an Asn-X-Ser/Thr consensus motif in nascent polypeptide chains, the first step in protein N-glycosylation. N-glycosylation occurs cotranslationally and the complex associates with the Sec61 complex at the channel-forming translocon complex that mediates protein translocation across the endoplasmic reticulum (ER). All subunits are required for a maximal enzyme activity.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 14126
Sequence Length: 132
Subcellular Location: Membrane
|
A6QQ59 | MVVGTGTSLALSSLLSLLLFAGMQMYSRQLASTEWLTIQGGLLGSGLFVFSLTAFNNLENLVFGKGFQAKIFPEILLCLLLALFASGLIHRVCVTTCFIFSMVGLYYINKISSTLYQATAPVLTPAKVTGKGKKRN | Function: Subunit of the oligosaccharyl transferase (OST) complex that catalyzes the initial transfer of a defined glycan (Glc(3)Man(9)GlcNAc(2) in eukaryotes) from the lipid carrier dolichol-pyrophosphate to an asparagine residue within an Asn-X-Ser/Thr consensus motif in nascent polypeptide chains, the first step in protein N-glycosylation. N-glycosylation occurs cotranslationally and the complex associates with the Sec61 complex at the channel-forming translocon complex that mediates protein translocation across the endoplasmic reticulum (ER). All subunits are required for a maximal enzyme activity. May be involved in N-glycosylation of APP (amyloid-beta precursor protein). Can modulate gamma-secretase cleavage of APP by enhancing endoprotelysis of PSEN1.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 14679
Sequence Length: 136
Pathway: Protein modification; protein glycosylation.
Subcellular Location: Endoplasmic reticulum membrane
|
Q54L98 | MASRQPSEGSTVLISLILWVIIFALLNIGSNFFRSSEGATILGGFVGSFLFFLQMTFIGAIKRDVKLLETVLAVIITAMISSSVHRVSGTTSIIFSIGWIFYLNHASTKIYSKLEETNTVVSGKKRK | Function: Subunit of the oligosaccharyl transferase (OST) complex that catalyzes the initial transfer of a defined glycan (Glc(3)Man(9)GlcNAc(2) in eukaryotes) from the lipid carrier dolichol-pyrophosphate to an asparagine residue within an Asn-X-Ser/Thr consensus motif in nascent polypeptide chains, the first step in protein N-glycosylation. N-glycosylation occurs cotranslationally and the complex associates with the Sec61 complex at the channel-forming translocon complex that mediates protein translocation across the endoplasmic reticulum (ER). All subunits are required for a maximal enzyme activity.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 13937
Sequence Length: 127
Subcellular Location: Membrane
|
Q8INQ7 | MSASVSSKSTVVSSIISGLLSIVLFGTLRFCSEWFNDSQLRVLLGGYLFSWVFILSLTCVSNAEMVVFGQDFQAKLLPEIIFCLSLTVAAAGLVHRVCATTSVLFSLVGLYFLNRISTKYYSVQVPSVDAPTTRKGGKKFK | Function: Subunit of the oligosaccharyl transferase (OST) complex that catalyzes the initial transfer of a defined glycan (Glc(3)Man(9)GlcNAc(2) in eukaryotes) from the lipid carrier dolichol-pyrophosphate to an asparagine residue within an Asn-X-Ser/Thr consensus motif in nascent polypeptide chains, the first step in protein N-glycosylation. N-glycosylation occurs cotranslationally and the complex associates with the Sec61 complex at the channel-forming translocon complex that mediates protein translocation across the endoplasmic reticulum (ER). All subunits are required for a maximal enzyme activity.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 15392
Sequence Length: 141
Subcellular Location: Membrane
|
Q8N6L1 | MVVGTGTSLALSSLLSLLLFAGMQMYSRQLASTEWLTIQGGLLGSGLFVFSLTAFNNLENLVFGKGFQAKIFPEILLCLLLALFASGLIHRVCVTTCFIFSMVGLYYINKISSTLYQAAAPVLTPAKVTGKSKKRN | Function: Subunit of the oligosaccharyl transferase (OST) complex that catalyzes the initial transfer of a defined glycan (Glc(3)Man(9)GlcNAc(2) in eukaryotes) from the lipid carrier dolichol-pyrophosphate to an asparagine residue within an Asn-X-Ser/Thr consensus motif in nascent polypeptide chains, the first step in protein N-glycosylation. N-glycosylation occurs cotranslationally and the complex associates with the Sec61 complex at the channel-forming translocon complex that mediates protein translocation across the endoplasmic reticulum (ER). All subunits are required for a maximal enzyme activity . May be involved in N-glycosylation of APP (amyloid-beta precursor protein). Can modulate gamma-secretase cleavage of APP by enhancing endoprotelysis of PSEN1 .
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 14679
Sequence Length: 136
Pathway: Protein modification; protein glycosylation.
Subcellular Location: Endoplasmic reticulum
|
Q3Z8D9 | MSLFITFEGGEGCGKSTQSKALYRYLKKLGLGCVLTHEPGGTRSGDKITRLLKWSEEENISPLAELFLFNASRSILIDNVIKPALLDGNIVICDRYTDSTLAYQGYGRGLELDTVKCINSLASGGLVPDLTIWLDMDDKAALLRKGKLPPDRFESENNGFHQRVRDGFGVIAAAEPNRFLKLDASLSQSELTKCIKQRVNALLKLPQ | Function: Phosphorylation of dTMP to form dTDP in both de novo and salvage pathways of dTTP synthesis.
Catalytic Activity: ATP + dTMP = ADP + dTDP
Sequence Mass (Da): 22835
Sequence Length: 207
EC: 2.7.4.9
|
Q9RY40 | MSQGLFITLEGPEGAGKTTQLARLEARLRAAGHAVTVTREPGGTPLGTRVREVVLDPAVEIEPLGEFLLYSASRAQLVREVLRPALERGETVLCDRYADSSLAYQGAGRGLSLPLLRQITAEVTGGLTPGLTVLLDLDPALGLQRAARRGQPDRLEQADLTFHRRVRQGFLDLAHAEPQRFLVLDATRPEDELEAEIWAAVSERGH | Function: Phosphorylation of dTMP to form dTDP in both de novo and salvage pathways of dTTP synthesis.
Catalytic Activity: ATP + dTMP = ADP + dTDP
Sequence Mass (Da): 22431
Sequence Length: 206
EC: 2.7.4.9
|
C0QI33 | MFITLEGIEGSGKTTQIKPLVDCLGQNGYEAVVTREPGATVIGKKIRAILLDPGNSGMSDLCELFLYGADRAQHLSEVIIPALGAGKTVVCDRFTDATTVYQGAARGISKELIDIIHSVVVKDLCPDLTILFDLDPETGLARTVKALTDGERTLDESRFERETLEFHERVRQGYLALAAAEQDRFLVVDARGTQEQVFTEIVSGINRRLGIDLVGIDSAMIDPRVKG | Function: Phosphorylation of dTMP to form dTDP in both de novo and salvage pathways of dTTP synthesis.
Catalytic Activity: ATP + dTMP = ADP + dTDP
Sequence Mass (Da): 24705
Sequence Length: 227
EC: 2.7.4.9
|
B8J2G0 | MFVTFEGIEGAGKSTAIDYLSDYLQARGHDPVLTREPGGSALGRRLRALLLDVRTGGLASRAELFLFLADRAQHVTEVIRPALEAGQVVLCDRFTDSTLAYQGYGRGLDTEYLRSLNTAATGGLEPDLTLLLDLPVRCGLERAGERNRSAGMVIAEGRFDSESLDFHERVRRGYRALAEEEPERFAIIDASQPPEDVVLQCRSAIEAYLRRRGRGLD | Function: Phosphorylation of dTMP to form dTDP in both de novo and salvage pathways of dTTP synthesis.
Catalytic Activity: ATP + dTMP = ADP + dTDP
Sequence Mass (Da): 23956
Sequence Length: 217
EC: 2.7.4.9
|
Q6AJE2 | MSNNPGKLIIFEGTDGAGKSTQIKMLANYLRSKGLDVIASFEPTNGPYGQKIRQLYTDRNKVTRNEELELFLADRREHVNKLINPAISAGKIVLCDRYYLSTAAYQGALGFDVEEILQRNSFAPTPDLALLLQIPVEDGRRRITSSRGEETNDFEKAEMLEKVSTIFNSLSFPYIRHINACQSIDNVQRDIIMQVKQLLKMA | Function: Phosphorylation of dTMP to form dTDP in both de novo and salvage pathways of dTTP synthesis.
Catalytic Activity: ATP + dTMP = ADP + dTDP
Sequence Mass (Da): 22829
Sequence Length: 202
EC: 2.7.4.9
|
A4J0K6 | MALIFIVFEGVDGSGKSTQLNLLNKYLSQKEIKTICTREPGGTPVGEKIRELLLDPNFAEIQDRTEALLYSAARAQLVAQVIRPQLEQGTVVLCDRYIDSTLAYQGYGRGMDISFLAQINELASGGLMPNITILLDLPPEEGLQRSRKDRPADRLENESLTFYHKVRSGYLEMAKRKPDTYLVLDARQTMEQLHRQICCRVGGLLGV | Function: Phosphorylation of dTMP to form dTDP in both de novo and salvage pathways of dTTP synthesis.
Catalytic Activity: ATP + dTMP = ADP + dTDP
Sequence Mass (Da): 23202
Sequence Length: 207
EC: 2.7.4.9
|
Q72A57 | MFITFEGIEGSGKSTALQGLAAWLQQRGHGVAVTREPGGSRLGRTLRSILLDLGNTDITPEAELFLYLADRAQHVAQVVRPALDEGMVVLSDRYADSTVVYQGYGRGLDPMMLRQFNDVAVGGLWPDLTILLDLEPEAGLNRALARNIREGMHAAEGRFEAESLAFHTRVREGYLTWAALHGGRYRVVDATQSPEDVVRDVVGIVAAALGDVSSGEAVSGRTGA | Function: Phosphorylation of dTMP to form dTDP in both de novo and salvage pathways of dTTP synthesis.
Catalytic Activity: ATP + dTMP = ADP + dTDP
Sequence Mass (Da): 24117
Sequence Length: 224
EC: 2.7.4.9
|
Q54GN2 | MINTKKEEGEEEKTMIKRGLFILFEGVDRVGKSTQVQSLTNHISNVQKLPTKSLRFPDRTTPIGQIINQYLQNATNMDDRALHLLFSSNRWEARDSILELLNNGTNIVVDRYSYSGVAYSAAKGIDFDWCYACEKGLPKPDLIFYLSMSSEDATKRGEYGGERYEKLEFQKKIKQIYEEKLVDDQWKIINANRSIDEISNEISSIFDSEFKKIQLTSIAKLE | Function: Catalyzes the phosphorylation of thymidine monophosphate (dTMP) to thymidine diphosphate (dTDP), the immediate precursor for the DNA building block dTTP, with ATP as the preferred phosphoryl donor in the presence of Mg(2+).
Catalytic Activity: ATP + dTMP = ADP + dTDP
Sequence Mass (Da): 25582
Sequence Length: 222
Pathway: Pyrimidine metabolism; dTTP biosynthesis.
EC: 2.7.4.9
|
A5EXE3 | MRGKFICLDGTEGSGKSSQIQAICSFLQQHGKTVITTREPGGTQIGEAIRELVLSPHYQPQALTELLLILAARHEHLQTVILPHLAAGTWVISDRFNDATYAYQGYGRGIDLKIIKTLEQIIQASFQPDLACILCLPEHIAAERVHNRAHDHDRIELENRAFFARVAQGYHARAQLPHARFIDASGDQNSVFQQIRHHLELLL | Function: Phosphorylation of dTMP to form dTDP in both de novo and salvage pathways of dTTP synthesis.
Catalytic Activity: ATP + dTMP = ADP + dTDP
Sequence Mass (Da): 22784
Sequence Length: 203
EC: 2.7.4.9
|
A8LRW0 | MTQPGRLISFEGIDGSGKSTQARRLAEHLRDTGRDPLLTREPGGSPGAEDIRRLLVEGDPDRWSPETELLLFTAARRDHLERLIQPALAEGRDVITDRFADSTRVYQGATRGDLRALVDQLHSLMIGREPDLTFVIDMPPELALTRGLARASGEDRFEEFGLPFQTALRAGFLDLARANPDRCVVIDGNRPEAEVAADVIAHLTVAA | Function: Phosphorylation of dTMP to form dTDP in both de novo and salvage pathways of dTTP synthesis.
Catalytic Activity: ATP + dTMP = ADP + dTDP
Sequence Mass (Da): 22760
Sequence Length: 207
EC: 2.7.4.9
|
A7ZKK1 | MRSKYIVIEGLEGAGKTTARNVVVETLEQLGIRDMVFTREPGGTQLAEKLRSLVLDIKSVGDEVITDKAEVLMFYAARVQLVETVIKPALANGTWVIGDRHDLSTQAYQGGGRGIDQHMLATLRDAVLGDFRPDLTLYLDVTPEVGLKRARARGELDRIEQESFDFFNRTRARYLELAAQDKSIHTIDATQPLEAVMDAIRTTVTHWVKELDA | Function: Phosphorylation of dTMP to form dTDP in both de novo and salvage pathways of dTTP synthesis.
Catalytic Activity: ATP + dTMP = ADP + dTDP
Sequence Mass (Da): 23783
Sequence Length: 213
EC: 2.7.4.9
|
A3PAJ7 | MKGKFIVIEGIDGCGKTTQIDELSKWLPISGLLKKESKLITTREPGGSLLGKKLRRLILDNNENNKPSSLAELLLYSADRAEHVSKIILPALNNNDWVISDRFSDSTLAYQGYGRNINLEIIKNIESIVCQGASPDLTFFLEISPEESIFRRKNEIPDRIESEGIRFLERVNEGFKLIAKQKNWKVISASQNIKTISNQIKETLLNNFSNAK | Function: Phosphorylation of dTMP to form dTDP in both de novo and salvage pathways of dTTP synthesis.
Catalytic Activity: ATP + dTMP = ADP + dTDP
Sequence Mass (Da): 23933
Sequence Length: 212
EC: 2.7.4.9
|
A9BCY7 | MKGHFIVLEGIDGCGKSTQISHISKWLPQSGLMPKNANLYITREPGGTTLGKSLRDLLLHEHETNVPAPLTELLLYAADRAEHIHSLIQPKLDKGDWVISDRFSGSTLAYQGFGRGLDINLIRRLDAIARQGLVPEITIFLKISVLTSMRRRAKKSADRMEAEGEGFLKKVASGFSRIANEEHWITIEGEQDQALVSDEIKLAITNKLKNYISNN | Function: Phosphorylation of dTMP to form dTDP in both de novo and salvage pathways of dTTP synthesis.
Catalytic Activity: ATP + dTMP = ADP + dTDP
Sequence Mass (Da): 23958
Sequence Length: 215
EC: 2.7.4.9
|
A2BUA6 | MKGKFIVIEGIDGCGKTTQIDEISRWLPTSGLMGKNSKLIKTREPGGSLLGKKLRNLILDNNKNNKPSSLAELLLYSADRAEHVSKIISPALKKEDWVISDRFSDSTLAYQGYGRHINLEIIKNIESIVCQGEYPDLTIFLEISAEESILRRKNFVPDRMESEGINFLQKVNEGFKLIAKEKKWKVISATQNITAISNEIKETLLKTFRN | Function: Phosphorylation of dTMP to form dTDP in both de novo and salvage pathways of dTTP synthesis.
Catalytic Activity: ATP + dTMP = ADP + dTDP
Sequence Mass (Da): 23740
Sequence Length: 210
EC: 2.7.4.9
|
Q7VE61 | MKGIFLVLEGIDGCGKSTQIEHLAQWLPLSGLMPSAAKLFITREPGGTRLGKSLRQLLLGTSPTDESPKPLTELLLYAADRAQHVSQVIQPKINNGDWVISDRFSSSTLAYQGFGRRLDKSLIKELENIATQGITPDLTFLLEIPVSESIKRRENTRKDRIESEGEIFLKRVSDGFSYIAKNDNWLVIPANQKKDIVSKQIENKLINYFQNISSLKNERS | Function: Phosphorylation of dTMP to form dTDP in both de novo and salvage pathways of dTTP synthesis.
Catalytic Activity: ATP + dTMP = ADP + dTDP
Sequence Mass (Da): 24713
Sequence Length: 220
EC: 2.7.4.9
|
Q7V4G2 | MSGRFLVLEGIDGCGKTTQLRHLANWLPRSGLMPEGARLHLTREPGGTALGIALRKLVLHPPGDASPEPLAELLLYAADRAQHVAQLIRPALEQGHWVLSDRFSGSTLAYQGYGRELDLDLIQQLEQIATAGLVPDLTFWLELPVEESLLRRDARSNDRIEAEGVDFLTRVATGFAVLARERSWVPLQADQQVESVSSALESQLKHHFGPLQESMR | Function: Phosphorylation of dTMP to form dTDP in both de novo and salvage pathways of dTTP synthesis.
Catalytic Activity: ATP + dTMP = ADP + dTDP
Sequence Mass (Da): 23899
Sequence Length: 216
EC: 2.7.4.9
|
Q7V3E6 | MRGKFIVIEGIDGCGKTTQIDEISKWIPTSGLLRGKQKLVKTREPGGSLLGKKIRNLILDNHKDNKPSSLAELLLYSADRAEHISKTISPALENQDWVLSDRFCDSTLAYQGYGRNINLEIIKNIESIVCQGESPDLTIFLEISAEESVLRREKFIPDRMESEGIKFLEKVNEGFKLIAKEKNWTTISALQDINTITNEIKETLLKKFSRVNND | Function: Phosphorylation of dTMP to form dTDP in both de novo and salvage pathways of dTTP synthesis.
Catalytic Activity: ATP + dTMP = ADP + dTDP
Sequence Mass (Da): 24224
Sequence Length: 214
EC: 2.7.4.9
|
A2BNS4 | MKGKFIVIEGIDGCGKTTQIDELSKWLPNSGLIKKGSKLITTREPGGSLLGKKLRGLILDNNKNNKPSSLAELLLYSADRAEHVSKIISPALNNNDWVISDRFSDSTLAYQGYGRNINLEIIKNIESIVCQGASPDLTFFLEISPEESIFRRKNEIPDRIESEGIRFLEKVNEGFKLIAKQKNWKVISASQNIQTISNQIKETLLNNFSNNK | Function: Phosphorylation of dTMP to form dTDP in both de novo and salvage pathways of dTTP synthesis.
Catalytic Activity: ATP + dTMP = ADP + dTDP
Sequence Mass (Da): 23751
Sequence Length: 212
EC: 2.7.4.9
|
Q46HP4 | MKGKFIVFEGIDGSGKTTQINQLSKWLISSDLIPENNKLVITREPGGTKLGKSIRSLLLDTSIEKSPDSITELLLYAADRSQHINEIIRPTLDQGDWVISDRFCGSTLAYQGYGRKLDINLIKDLEAIATQGIAPDITFLLDIPIEESIRRRRNRKDDRIEKEGREFLSNVSLGFQALSEDSNWKKISAIDSKEKIISEIKSEIKKLIKNK | Function: Phosphorylation of dTMP to form dTDP in both de novo and salvage pathways of dTTP synthesis.
Catalytic Activity: ATP + dTMP = ADP + dTDP
Sequence Mass (Da): 23831
Sequence Length: 211
EC: 2.7.4.9
|
Subsets and Splits
No community queries yet
The top public SQL queries from the community will appear here once available.