ids stringlengths 6 10 | seqs stringlengths 11 1.02k | texts stringlengths 108 11.1k |
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P0CM93 | MSAQEFYQGGNQRGYQQQQFPPPPGGPPQDQNGGKQEYVPPQGQPPNYNMKPSQPYASTNPETGGQPVYQDTAPFSQANEKTGERMNPRKRVNDIIPLILFIAAVVGFAVVSGIAIHGFVQVNGLGGGMGDSSIGRTGSSITLDYHTVYLLLVVVALGLVIASLYLAALRAFTKIILEVTLALTVILNIGICIYYFIIQYWSGAIIFLIIALVSVFFYWGMRKRIPLAKLLLQTTIDVTKHHPSVYVVVFIGLIIQAAVSVWYTFTCIAIYVKWTPGSAACSDGGCSSSKVAGLVFYATFSYLWLSQVIGNVILCTLAGGVFGGWYYYGPRTPGGGVPKRASLLAFVRASTLSLGSIAFGSLLVTILELLRLILQLFRQYEAGQGDMIGSILICIAQCCIGCIQWMVEYFNKYAYIEIALYGKSYIPAAKDTWRLLKDRGIDALVNDSLVGTALMWGAYINGFLCAVLGYFYLRFTHPAYNSDGQYSAPVILFSFLIGLNESFTVGSAIDAGVSTIFVGLGEDPMVLAERSPGLFEMIRQVYPRVVQGVPH | Function: Probably involved in transport through the plasma membrane.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 60043
Sequence Length: 551
Subcellular Location: Cell membrane
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Q6BIV4 | MSNNNYPPPPNPPNYQGEEQVHNVQPDLENNQEKYYAEQPQPSQQFEESFKIDKPKWNDWPFTVFFLLTVAGFIAIAGITLNALKKTYGLQGSSIYNSTDTFTLNTNTIILFGFIIVVGVVLSVLIIVYARMAPRVFITTGLILNIILGLGTCIYYFVAHYYSAAIVFLVFTLFTAWCYWSCRHRIPFSATVLEITIDVMKRYPSTLITSFIGIIVSGLFSTLFSVVIVATYVKYDPDSQGCDVAGGGCSQSKLIGVLVFVFFAGYYISEVIKNVIHITIAGIYGTWYYLSNSDQGEPKHPALGAFKRAMTYCFGSVCFGSLIVSIIQLIRSFVQILKQNAFGSGDNCAGCGFLILDFVLGFIDWIVRYFNHYAYCYVALYGKSYLKSARDTFDLIRFKGMDALINDCFINTSLNLYSMFVGYVVALLAYFYLKFTDPAYNSSGTFYAPVVAFSFLISGQITRIALTVISSGISTFFVALAKDPEVFQMTNRDRFDEIFRNYPQVLQKITSDH | Function: Probably involved in transport through the plasma membrane.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 57661
Sequence Length: 513
Subcellular Location: Cell membrane
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Q870V7 | MSGPQYGAQPGGYYNNNNNYPPPPPNSYQMNPMPTDGNYGQQPQYGYGGGPPPQQYGNGYGDGGYAPPQGPPPNGSKPPPTDGYGGPPPSYDEVFKVQKPKYNDWWAGLLFLATVAGFVAVSAISIHGYADNRSQNNGSLNGQRNTFGLTTHTIYLFVWVLICAIVLSYAYMWMARKFTKQFIYATGILNIVMGLVTALYMLSRKYWSGGIVFLIFVVLQALFFWSCRSRIPFSTLMLQTAIDVSKVHGHVYLVSAVGGVIGTLFAAYWAITLVAVYVKFEPDPNNAACRNAGGCSSGKVIGLIVFITFAGYWISEWLKNTIHTTVAGIYGSWYFNSRNYPTKVTRGALKRSLTYSFGSISLGSLFIAIINLIRQLAQAAQQNAAQEGDILGTILWCIFGCLIGILDWLVEFINRYAFCHIALYGKAYFAAAKDTWKMVKDRGIDALINECLIGPVLTFGATFVAYACGLIAYLYMVYTKPAYNDGGGFTPVVVAFAFLIGLQVCNVFTTPLTSGIDTIFVAMAWDPEVLMRDHPDLYHRMVQVYPHVQEAIHA | Function: Probably involved in transport through the plasma membrane.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 60937
Sequence Length: 554
Subcellular Location: Cell membrane
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Q4PIP8 | MSQQYSYGGGGGAGYPPPQMQPPNSYAQANYQGQPQGAQNQYYNGQQPHHNAPQQYYGNDYKQPLKPEGFEGERLQPKPKFRDPIFLVLFLLVFAGFIALSVICLRSYSNADVNVSIGRANVAGSTLNGHTAIMFMICCAVALVLSFVYILLVRTFPKIILEATLLLTTLSNVAFCVYLWVRGNTAAAIIFTIFAVLSVIAYFFMRKRIPLAKLILVTVIRTAEQYKSVYVVALGGLIVETAFSAWTSWVVVAAYQRFEPSGQAAGSSSSNASIIGIMVFIVFAYYWISEVIKNIAFTTVAGIFGVAYYNANKVANAAWGAFRRSMTYSLGSICFGSLIVAILDLLRALFNILQSQAASDGDMTGQILACVAGCCVSCIQGLVDYFNRYAYINIALYGNGYITAAKETWALLKDRGIDAIINDSLVNIVFNCGAFIIGLLTALFAFIYEQLTNPRYLQNDAGYYSIVLLVAFGLGFNIALSVGAGSIASGVSTYFVALAEDPYILQGKNPELFEMIRQQYPQVVQGVNH | Function: Probably involved in transport through the plasma membrane.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 57785
Sequence Length: 529
Subcellular Location: Cell membrane
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Q6C938 | MNDEEKHLAAPANAYQPNMHYQQQQEKQTGYNAEYDTHQGGYNQNQNQDYYNHSQGGYQMDNMGQHGGYQGNPNDNYNNQQPPPYTPDFPPDYNYKPNPNAATFDEAFAVPKPKWNDKIGLVILALIFSGYLALSIIVIRAYAQTHSFQGWGIYSGENDYSLNTHTLILYAFVLATAMVLSLLYFIAARVWTKQFIWITYILHLLFSWGTAIYYLVVGYYSAGIVFIVFAALTTWWFWCSRKRIPFATIVLQTLIDVTRANPSVLVISAVGTVVGACFGTWFSFTIVSIYVKYDPDNRNPGCMTTGGSCSNGKLIGLILFAIFCGYYLTEVIKNVIHVTISGVYGSWYYCSKSDQGMPKHAAMSSFRRAVTYSLGSISLGSLIVSIINFIRQILSVLQQDARQSGDTLATVLLCFVQCCFGVLDWLVTYFNHYAYSYIALYGKAYVPSAKATWKLMQTRGIDAMVNDSLIGSVLSFGASFVAYAAALVAYCFLKYTDPSYNSGGGFYAPVVGLAFVIALQVSNITNVSLKSGCSTFFLALARDPEVLRVSYPQIYEEICRTYPPARDKLDI | Function: Probably involved in transport through the plasma membrane.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 63808
Sequence Length: 571
Subcellular Location: Cell membrane
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P17208 | MMSMNSKQPHFAMHPTLPEHKYPSLHSSSEAIRRACLPTPPLQSNLFASLDETLLARAEALAAVDIAVSQGKSHPFKPDATYHTMNSVPCTSTSTVPLAHHHHHHHHHQALEPGDLLDHISSPSLALMAGAGGAGAAGGGGGAHDGPGGGGGPGGGGGPGGGGPGGGGGGGGPGGGGGGPGGGLLGGSAHPHPHMHGLGHLSHPAAAAAMNMPSGLPHPGLVAAAAHHGAAAAAAAAAAGQVAAASAAAAVVGAAGLASICDSDTDPRELEAFAERFKQRRIKLGVTQADVGSALANLKIPGVGSLSQSTICRFESLTLSHNNMIALKPILQAWLEEAEGAQREKMNKPELFNGGEKKRKRTSIAAPEKRSLEAYFAVQPRPSSEKIAAIAEKLDLKKNVVRVWFCNQRQKQKRMKFSATY | Function: Multifunctional transcription factor with different regions mediating its different effects . Acts by binding (via its C-terminal domain) to sequences related to the consensus octamer motif 5'-ATGCAAAT-3' in the regulatory regions of its target genes . Regulates the expression of specific genes involved in differentiation and survival within a subset of neuronal lineages. It has been shown that activation of some of these genes requires its N-terminal domain, maybe through a neuronal-specific cofactor . Ativates BCL2 expression and protects neuronal cells from apoptosis (via the N-terminal domain) . Induces neuronal process outgrowth and the coordinate expression of genes encoding synaptic proteins . Exerts its major developmental effects in somatosensory neurons and in brainstem nuclei involved in motor control. Stimulates the binding affinity of the nuclear estrogene receptor ESR1 to DNA estrogen response element (ERE), and hence modulates ESR1-induced transcriptional activity . May positively regulate POU4F2 and POU4F3 . Regulates dorsal root ganglion sensory neuron specification and axonal projection into the spinal cord . Plays a role in TNFSF11-mediated terminal osteoclast differentiation . Negatively regulates its own expression interacting directly with a highly conserved autoregulatory domain surrounding the transcription initiation site .
Sequence Mass (Da): 42767
Sequence Length: 421
Domain: The C-terminal domain is able to act as both DNA-binding domain and a transcriptional activator. The N-terminal domain is also required for transactivation activity on some target genes acting as a discrete activation domain . Neurite outgrowth and expression of genes required for synapse formation are primarily dependent on the C-terminal domain, however the N-terminal domain is required for maximal induction .
Subcellular Location: Nucleus
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Q12837 | MMMMSLNSKQAFSMPHGGSLHVEPKYSALHSTSPGSSAPIAPSASSPSSSSNAGGGGGGGGGGGGGGGRSSSSSSSGSSGGGGSEAMRRACLPTPPSNIFGGLDESLLARAEALAAVDIVSQSKSHHHHPPHHSPFKPDATYHTMNTIPCTSAASSSSVPISHPSALAGTHHHHHHHHHHHHQPHQALEGELLEHLSPGLALGAMAGPDGAVVSTPAHAPHMATMNPMHQAALSMAHAHGLPSHMGCMSDVDADPRDLEAFAERFKQRRIKLGVTQADVGSALANLKIPGVGSLSQSTICRFESLTLSHNNMIALKPILQAWLEEAEKSHREKLTKPELFNGAEKKRKRTSIAAPEKRSLEAYFAIQPRPSSEKIAAIAEKLDLKKNVVRVWFCNQRQKQKRMKYSAGI | Function: Tissue-specific DNA-binding transcription factor involved in the development and differentiation of target cells . Functions either as activator or repressor modulating the rate of target gene transcription through RNA polymerase II enzyme in a promoter-dependent manner . Binds to the consensus octamer motif 5'-AT[A/T]A[T/A]T[A/T]A-3' of promoter of target genes. Plays a fundamental role in the gene regulatory network essential for retinal ganglion cell (RGC) differentiation. Binds to an octamer site to form a ternary complex with ISL1; cooperates positively with ISL1 and ISL2 to potentiate transcriptional activation of RGC target genes being involved in RGC fate commitment in the developing retina and RGC axon formation and pathfinding. Inhibits DLX1 and DLX2 transcriptional activities preventing DLX1- and DLX2-mediated ability to promote amacrine cell fate specification. In cooperation with TP53 potentiates transcriptional activation of BAX promoter activity increasing neuronal cell apoptosis. Negatively regulates BAX promoter activity in the absence of TP53. Acts as a transcriptional coactivator via its interaction with the transcription factor ESR1 by enhancing its effect on estrogen response element (ERE)-containing promoter. Antagonizes the transcriptional stimulatory activity of POU4F1 by preventing its binding to an octamer motif. Involved in TNFSF11-mediated terminal osteoclast differentiation (By similarity).
Sequence Mass (Da): 43087
Sequence Length: 409
Domain: The N-terminal transcriptional activation region is sufficient to induce transcriptional activity.
Subcellular Location: Nucleus
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P32540 | MATTMEQEICAHSMTFEECPKCSALQYRNGFYLLKYDEEWYPEELLTDGEDDVFDPDLDIEVVFETQGNSTSSDKNNSSSEGNEGVIINNFYSNQYQNSIDLSANATGSDPPKTYGQFSNLLSGAVNAFSNMLPLLADQNTEEMENLSDRVSQDTAGNTVTNTQSTVGRLVGYGTVHDGEHPASCADTASEKILAVERYYTFKVNDWTSTQKPFEYIRIPLPHVLSGEDGGVFGAALRRHYLVKTGWRVQVQCNASQFHAGSLLVFMAPEYPTLDVFAMDNKWSKDNLPNGTRTQANRKGPFAMDHQNFWQWTLYPHQFLNLRTNTTVDLEVPYVNIAPTSSWTQHASWTLVIAVVAPLTYSTGASTSLDITASIQPVRPVFNGLRHEVLSRQSPIPVTIREHAGTWYSTLPDSTVPIYGKTPVAPANYMVGEYKDFLEIAQIPTFIGNKVPNAVPYIEASNTAVKTQPLAVYQVTLSCSCLANTFLAALSRNFAQYRGSLVYTFVFTGTAMMKGKFLIAYTPPGAGKPTSRDQAMQATYAIWDLGLNSSYSFTVPFISPTHFRMVGTDLVNITNADGWVTVWQLTPLTYPPGCPTSAKILTMVSAGKDFSLKMPISPAPWSPQGVENAEKGVTENTDATADFVAQPVYLPENQTKVAFFYDRSSPIGAFTVKSGSLESGFAPFSNQACPNSVILTPGPQFDPAYDQLRPQRLTEIWGNGNEETSEVFPLKTKQDYSFCLFSPFVYYKCDLEVTLSPHTSGNHGLLVRWCPTGTPNKPTTQVLHEVSSLSEGRTPQVYSAGPGTSNQISFVVPYNSPLSVLPAVWYNGHKRFDNTGYLGIAPNSDFGTLFFAGTKPDIKFTVYLRYKNMRVFCPRPTVFFPWPTSGDKIDMTPRAGVLMLE | Function: Forms a complex with host RAN and probably binds to exportins carrying activated MAPK in order to mediate the hyperphosphorylation of host Phe/Gly containing nuclear pore proteins (Nups) resulting in cessation of active nucleocytoplasmic transport (By similarity). Proteins with NLS signals fail to import, cellular mRNAs fail to export, and some proteins small enough for diffusion are not retained anymore (efflux) (By similarity). The resulting inhibition of cellular protein synthesis serves to ensure maximal viral gene expression and to evade host immune response (By similarity).
PTM: Phosphorylated.
Sequence Mass (Da): 99652
Sequence Length: 901
Subcellular Location: Virion
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P31998 | TSPNINGFWVMLENDEQIEFPIKPLIDHARPTFRQIMSRFSDLAEAYIEKRNFERAYMPRYGLQRNLTDMSLRRYAFDFYEMTSKAPARA | Function: Involved in aphid transmission, cell-to-cell and systemis movement, encapsidation of the viral RNA and in the regulation of viral RNA amplification.
PTM: Genome polyprotein of potyviruses undergoes post-translational proteolytic processing by the main proteinase NIa-pro resulting in the production of at least ten individual proteins. The P1 proteinase and the HC-pro cleave only their respective C-termini autocatalytically. 6K1 is essential for proper proteolytic separation of P3 from CI (By similarity).
Sequence Mass (Da): 10786
Sequence Length: 90
Subcellular Location: Virion
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Q04049 | MSKFTWKELIQLGSPSKAYESSLACIAHIDMNAFFAQVEQMRCGLSKEDPVVCVQWNSIIAVSYAARKYGISRMDTIQEALKKCSNLIPIHTAVFKKGEDFWQYHDGCGSWVQDPAKQISVEDHKVSLEPYRRESRKALKIFKSACDLVERASIDEVFLDLGRICFNMLMFDNEYELTGDLKLKDALSNIREAFIGGNYDINSHLPLIPEKIKSLKFEGDVFNPEGRDLITDWDDVILALGSQVCKGIRDSIKDILGYTTSCGLSSTKNVCKLASNYKKPDAQTIVKNDCLLDFLDCGKFEITSFWTLGGVLGKELIDVLDLPHENSIKHIRETWPDNAGQLKEFLDAKVKQSDYDRSTSNIDPLKTADLAEKLFKLSRGRYGLPLSSRPVVKSMMSNKNLRGKSCNSIVDCISWLEVFCAELTSRIQDLEQEYNKIVIPRTVSISLKTKSYEVYRKSGPVAYKGINFQSHELLKVGIKFVTDLDIKGKNKSYYPLTKLSMTITNFDIIDLQKTVVDMFGNQVHTFKSSAGKEDEEKTTSSKADEKTPKLECCKYQVTFTDQKALQEHADYHLALKLSEGLNGAEESSKNLSFGEKRLLFSRKRPNSQHTATPQKKQVTSSKNILSFFTRKK | Function: DNA polymerase specifically involved in DNA repair. Plays an important role in translesion synthesis, where the normal high fidelity DNA polymerases cannot proceed and DNA synthesis stalls. Plays an important role in the repair of UV-induced pyrimidine dimers. Depending on the context, it inserts the correct base, but causes frequent base transitions and transversions. Efficiently incorporates nucleotides opposite to other UV or oxidative DNA damages like O(6)-methylguanine, 7,8-dihydro-8-oxoguanine, 2,6-diamino-4-hydroxy-5-formamidopyrimidine of 2'-deoxyguanosine (FaPydG), or p-benzoquinone DNA adducts.
Catalytic Activity: a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) = diphosphate + DNA(n+1)
Sequence Mass (Da): 71515
Sequence Length: 632
Subcellular Location: Nucleus
EC: 2.7.7.7
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Q9VHV1 | MDFASVLGKSEAHQRTIIHLDMDYFYAQVEEIRDPTLRSKALGIQQKNIVVTCNYVARAKGVTKLMLIAEAQRICPDLVLVNGEDLAPYRQMSQRIFDLLLNYTPLVEKLGFDENFMDVTALVELRQAHVAEALLRPPVGHTYPADGTPLSNCDCGCAQRLAIGTRIAQEIREELKLRLGITCCAGIAYNKLLAKLVGSSHEPNQQTVLVSTYAEQFMRELGDLKRVTGIGQKTQCLLLEAGMSSVEQLQQCDMDVMRKKFGFETATRLRDLAFGRDTSLVRPSGKPKTIGMEDACKPISVRTDVEERFRMLLKRLVEQVAEDGRVPIAIKVVLRKFDSQKKSSHRETKQANILPSLFKTSMCPGETGVSKVQLADGAQDKLLKIVMRLFERIVDMSKPFNITLLGLAFSKFQERKVGSSSIANFLIKKADLEVQSITSLTNTSLTSPTAESPTSDECAFRSSPTTFKPSDQFYRRRATTASPVPMLLDNGSESAATNSDFSDFSETEVEPSPKKSRIGRLLVSKRSRLAADVGDSAAEVASPSKLRVCDLRLNSRDSEKDFPMSTTPSTSTSAPAPRFRTVQPPNTLLQRIDGSLRFVTTRTASRLSSNASSTASSPLPSPMDDSIAMSAPSTTTLPFPSPTTTAVVTSSSSTATCDALTNIVCPAGVDAEVFKELPVELQTELIASWRSSLVAAVEQTNGTGAATSAAIASGAPATATTASGQKNTLYRYFLRNK | Cofactor: Binds nucleotide much more tightly and catalyzes nucleotide insertion much more efficiently in the presence of Mg(2+) than in the presence of Mn(2+).
Function: Error-prone DNA polymerase specifically involved in DNA repair . Plays an important role in translesion synthesis, where the normal high-fidelity DNA polymerases cannot proceed and DNA synthesis stalls . Favors Hoogsteen base-pairing in the active site (By similarity). Inserts the correct base with higher fidelity opposite an adenosine template . Exhibits low fidelity and efficiency opposite a thymidine template, where it will preferentially insert guanosine . Forms a Schiff base with 5'-deoxyribose phosphate at abasic sites, but may not have lyase activity (By similarity).
Catalytic Activity: a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) = diphosphate + DNA(n+1)
Sequence Mass (Da): 80390
Sequence Length: 737
Domain: The catalytic core consists of fingers, palm and thumb subdomains, but the fingers and thumb subdomains are much smaller than in high-fidelity polymerases; residues from five sequence motifs of the Y-family cluster around an active site cleft that can accommodate DNA and nucleotide substrates with relaxed geometric constraints, with consequently higher rates of misincorporation and low processivity.
Subcellular Location: Nucleus
EC: 2.7.7.7
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Q9UNA4 | MEKLGVEPEEEGGGDDDEEDAEAWAMELADVGAAASSQGVHDQVLPTPNASSRVIVHVDLDCFYAQVEMISNPELKDKPLGVQQKYLVVTCNYEARKLGVKKLMNVRDAKEKCPQLVLVNGEDLTRYREMSYKVTELLEEFSPVVERLGFDENFVDLTEMVEKRLQQLQSDELSAVTVSGHVYNNQSINLLDVLHIRLLVGSQIAAEMREAMYNQLGLTGCAGVASNKLLAKLVSGVFKPNQQTVLLPESCQHLIHSLNHIKEIPGIGYKTAKCLEALGINSVRDLQTFSPKILEKELGISVAQRIQKLSFGEDNSPVILSGPPQSFSEEDSFKKCSSEVEAKNKIEELLASLLNRVCQDGRKPHTVRLIIRRYSSEKHYGRESRQCPIPSHVIQKLGTGNYDVMTPMVDILMKLFRNMVNVKMPFHLTLLSVCFCNLKALNTAKKGLIDYYLMPSLSTTSRSGKHSFKMKDTHMEDFPKDKETNRDFLPSGRIESTRTRESPLDTTNFSKEKDINEFPLCSLPEGVDQEVFKQLPVDIQEEILSGKSREKFQGKGSVSCPLHASRGVLSFFSKKQMQDIPINPRDHLSSSKQVSSVSPCEPGTSGFNSSSSSYMSSQKDYSYYLDNRLKDERISQGPKEPQGFHFTNSNPAVSAFHSFPNLQSEQLFSRNHTTDSHKQTVATDSHEGLTENREPDSVDEKITFPSDIDPQVFYELPEAVQKELLAEWKRAGSDFHIGHK | Cofactor: Binds nucleotide much more tightly and catalyzes nucleotide insertion much more efficiently in the presence of Mg(2+) than in the presence of Mn(2+).
Function: Error-prone DNA polymerase specifically involved in DNA repair . Plays an important role in translesion synthesis, where the normal high-fidelity DNA polymerases cannot proceed and DNA synthesis stalls . Favors Hoogsteen base-pairing in the active site . Inserts the correct base with high-fidelity opposite an adenosine template . Exhibits low fidelity and efficiency opposite a thymidine template, where it will preferentially insert guanosine . May play a role in hypermutation of immunoglobulin genes . Forms a Schiff base with 5'-deoxyribose phosphate at abasic sites, but may not have lyase activity .
PTM: Monoubiquitinated. Protein monoubiquitination prevents POLI binding to ubiquitin via the ubiquitin-binding motif 1 and ubiquitin-binding motif 2.
Catalytic Activity: a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) = diphosphate + DNA(n+1)
Sequence Mass (Da): 83006
Sequence Length: 740
Domain: The catalytic core consists of fingers, palm and thumb subdomains, but the fingers and thumb subdomains are much smaller than in high-fidelity polymerases; residues from five sequence motifs of the Y-family cluster around an active site cleft that can accommodate DNA and nucleotide substrates with relaxed geometric constraints, with consequently higher rates of misincorporation and low processivity.
Subcellular Location: Nucleus
EC: 2.7.7.7
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Q6JDV7 | MDNGESSSTNNSSRPWESYNTVFTNAKAGMEGVDKEKVQRVVYEMSKGSKYFQNEERKEALMKQKIEHMRDRCAKLSSLDLSNYQKVVDKRILELEATRDLSRIWLHVDMDAFYAAVETLSDPSIKGKPMAVGGLSMISTANYEARKFGVRAAMPGFIARKLCPDLIFVPVDFTKYTHYSDLTRKVFRNYDPHFIAGSLDEAYLDITEVCRERGLSGGEIAEELRSSVYSETGLTCSAGVAANRLLAKVCSDINKPNGQFVLQNDRSTVMTFVSFLPVRKIGGIGKVTEHILKDALGIKTCEEMVQKGSLLYALFSQSSADFFLSVGLGLGGTNTPQVRSRKSISSERTFAATGDERLLYSKLDELAEMLSHDMKKEGLTARTLTLKLKTASFEIRSRAVSLQRYTCSSDDILKHATKLLKAELPVSVRLIGLRMSQFVEEIRNSDPSQGTITKFIVQKDSSRQAQDLDDNDSFDLDANKNCLSNDESGNVSFGSHETSSAHLKDVVEYEERSQIDSGKVIPNQECMKKEERLQILEGDSLLKKYKECKPDTSHSMNDNSNATEAVSVFPQTEPLYWIDGYKCVLCGIELPPSFVEERQEHSDFHLAQRLQNEETGSSSSTTPSKRRILGKEKVNSKPKKQKPDQKDSSKHIPIHAFFTKSNQNSNETQRK | Function: Template-directed low-fidelity DNA polymerase specifically involved in DNA repair . Able to extend primer-terminal mispairs, and to insert nucleotides opposite to a single 7,8-dihydro-8-oxoGuanine (8-oxoG) lesion and moderately extend from the resulting primer end, thus leading to both error-free and error-prone bypass of 8-oxoG DNA lesions . Probably involved in consecutive DNA replication cycles in the absence of mitosis . Binds preferentially template-primer DNA substrates or single-stranded DNA . Plays an important role in translesion synthesis, where the normal high-fidelity DNA polymerases cannot proceed and DNA synthesis stalls. Depending on the context, it inserts the correct base, but causes frequent base transitions, transversions and frameshifts (By similarity).
Catalytic Activity: a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) = diphosphate + DNA(n+1)
Sequence Mass (Da): 75252
Sequence Length: 671
Domain: The C-terminal region negatively affects catalytic efficiency for correct nucleotide insertion, thus decreasing the fidelity of the enzyme.
Subcellular Location: Nucleus
EC: 2.7.7.7
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P34409 | MLTFNDNKAGMNGLDKEKITKVIEENTSASYSSFSKKQQSRIEEKVLEIKNRLQTATREERQKSEILMENLEMKLESSRDLSRDCVCIDMDAYFAAVEMRDNPALRTVPMAVGSSAMLSTSNYLARRFGVRAGMPGFISNKLCPSLTIVPGNYPKYTKVSRQFSQIFMEYDSDVGMMSLDEAFIDLTDYVASNTEKKTFKRHRFGGDCPCWLPRFDENENTLEDLKIEESICPKCEKSRKIYYDHVEFGTGREEAVREIRFRVEQLTGLTCSAGIASNFMLAKICSDLNKPNGQYVLENDKNAIMEFLKDLPIRKVGGIGRVCEAQLKAMDIQTVGDMNLKKNLYPLCFTPLSQESFLRTALGLPGRPSESDPRRKSISVERTFSPTSDFNILLEEHQEICRMLEEDVRKSGIVGGKTVTLKLKLSSFDVLTRSLTPSDVVKSLEDIQKFSLELLEKEKGKEIRLLGVRLSQLIFEEDEKKRSKTITEFWNEKKLQIQNLQGSENVDDDDVIMMDTRPCPICGTDVENRLDVMNCHVDECILKVQNDDGPELICVSVENKSTQKPERPSTKKRKLQEKRPKAKKMVTIDSFWKKSG | Cofactor: Divalent metal cations. Prefers Mg(2+), but can also use Mn(2+).
Function: DNA polymerase specifically involved in DNA repair. Plays an important role in translesion synthesis, where the normal high-fidelity DNA polymerases cannot proceed and DNA synthesis stalls. Depending on the context, it inserts the correct base, but causes frequent base transitions, transversions and frameshifts. Lacks 3'-5' proofreading exonuclease activity. Forms a Schiff base with 5'-deoxyribose phosphate at abasic sites, but does not have lyase activity (By similarity).
Catalytic Activity: a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) = diphosphate + DNA(n+1)
Sequence Mass (Da): 67942
Sequence Length: 596
Domain: The catalytic core consists of fingers, palm and thumb subdomains, but the fingers and thumb subdomains are much smaller than in high-fidelity polymerases; residues from five sequence motifs of the Y-family cluster around an active site cleft that can accommodate DNA and nucleotide substrates with relaxed geometric constraints, with consequently higher rates of misincorporation and low processivity.
Subcellular Location: Nucleus
EC: 2.7.7.7
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Q9UBT6 | MDSTKEKCDSYKDDLLLRMGLNDNKAGMEGLDKEKINKIIMEATKGSRFYGNELKKEKQVNQRIENMMQQKAQITSQQLRKAQLQVDRFAMELEQSRNLSNTIVHIDMDAFYAAVEMRDNPELKDKPIAVGSMSMLSTSNYHARRFGVRAAMPGFIAKRLCPQLIIVPPNFDKYRAVSKEVKEILADYDPNFMAMSLDEAYLNITKHLEERQNWPEDKRRYFIKMGSSVENDNPGKEVNKLSEHERSISPLLFEESPSDVQPPGDPFQVNFEEQNNPQILQNSVVFGTSAQEVVKEIRFRIEQKTTLTASAGIAPNTMLAKVCSDKNKPNGQYQILPNRQAVMDFIKDLPIRKVSGIGKVTEKMLKALGIITCTELYQQRALLSLLFSETSWHYFLHISLGLGSTHLTRDGERKSMSVERTFSEINKAEEQYSLCQELCSELAQDLQKERLKGRTVTIKLKNVNFEVKTRASTVSSVVSTAEEIFAIAKELLKTEIDADFPHPLRLRLMGVRISSFPNEEDRKHQQRSIIGFLQAGNQALSATECTLEKTDKDKFVKPLEMSHKKSFFDKKRSERKWSHQDTFKCEAVNKQSFQTSQPFQVLKKKMNENLEISENSDDCQILTCPVCFRAQGCISLEALNKHVDECLDGPSISENFKMFSCSHVSATKVNKKENVPASSLCEKQDYEAHPKIKEISSVDCIALVDTIDNSSKAESIDALSNKHSKEECSSLPSKSFNIEHCHQNSSSTVSLENEDVGSFRQEYRQPYLCEVKTGQALVCPVCNVEQKTSDLTLFNVHVDVCLNKSFIQELRKDKFNPVNQPKESSRSTGSSSGVQKAVTRTKRPGLMTKYSTSKKIKPNNPKHTLDIFFK | Cofactor: Divalent metal cations. Prefers Mg(2+), but can also use Mn(2+).
Function: DNA polymerase specifically involved in DNA repair. Plays an important role in translesion synthesis, where the normal high-fidelity DNA polymerases cannot proceed and DNA synthesis stalls. Depending on the context, it inserts the correct base, but causes frequent base transitions, transversions and frameshifts. Lacks 3'-5' proofreading exonuclease activity. Forms a Schiff base with 5'-deoxyribose phosphate at abasic sites, but does not have lyase activity.
Catalytic Activity: a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) = diphosphate + DNA(n+1)
Sequence Mass (Da): 98809
Sequence Length: 870
Domain: The catalytic core consists of fingers, palm and thumb subdomains, but the fingers and thumb subdomains are much smaller than in high-fidelity polymerases; residues from five sequence motifs of the Y-family cluster around an active site cleft that can accommodate DNA and nucleotide substrates with relaxed geometric constraints, with consequently higher rates of misincorporation and low processivity.
Subcellular Location: Nucleus
EC: 2.7.7.7
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Q9QUG2 | MDNTKEKDNFKDDLLLRMGLNDNKAGMEGLDKEKINKIIMEATKGSRFYGNELKKEKQVNQRIENMMQQKAQITSQQLRKAQLQVDKFAMELERNRNLNNTIVHVDMDAFYAAVEMRDNPELKDKPIAVGSMSMLATSNYHARRFGVRAAMPGFIAKRLCPQLIIVPPNFDKYRAVSKEVKEILAEYDPNFMAMSLDEAYLNITQHLQERQDWPEDKRRYFIKMGNYLKIDTPRQEANELTEYERSISPLLFEDSPPDLQPQGSPFQLNSEEQNNPQIAQNSVVFGTSAEEVVKEIRFRIEQKTTLTASAGIAPNTMLAKVCSDKNKPNGQYQILPSRSAVMDFIKDLPIRKVSGIGKVTEKMLMALGIVTCTELYQQRALLSLLFSETSWHYFLHIALGLGSTDLARDGERKSMSVERTFSEISKTEEQYSLCQELCAELAHDLQKEGLKGRTVTIKLKNVNFEVKTRASTVPAAISTAEEIFAIAKELLRTEVNVGSPHPLRLRLMGVRMSTFSSEDDRKHQQRSIIGFLQAGNQALSSTGDSLDKTDKTELAKPLEMSHKKSFFDKKRSERISNCQDTSRCKTAGQQALQILEPSQALKKLSESFETSENSNDCQTFICPVCFREQEGVSLEAFNEHVDECLDGPSTSENSKISCYSHASSADIGQKEDVHPSIPLCEKRGHENGEITLVDGVDLTGTEDRSLKAARMDTLENNRSKEECPDIPDKSCPISLENETISTLSRQDSVQPCTDEVVTGRALVCPVCNLEQETSDLTLFNIHVDICLNKGIIQELRNSEGNSVKQPKESSRSTDRLQKASGRTKRPGTKTKSSTLKKTKPRDPRHTLDGFFK | Cofactor: Divalent metal cations. Prefers Mg(2+), but can also use Mn(2+).
Function: DNA polymerase specifically involved in DNA repair. Plays an important role in translesion synthesis, where the normal high-fidelity DNA polymerases cannot proceed and DNA synthesis stalls . Depending on the context, it inserts the correct base, but causes frequent base transitions, transversions and frameshifts. Lacks 3'-5' proofreading exonuclease activity. Forms a Schiff base with 5'-deoxyribose phosphate at abasic sites, but does not have lyase activity (By similarity).
Catalytic Activity: a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) = diphosphate + DNA(n+1)
Sequence Mass (Da): 96003
Sequence Length: 852
Domain: The catalytic core consists of fingers, palm and thumb subdomains, but the fingers and thumb subdomains are much smaller than in high-fidelity polymerases; residues from five sequence motifs of the Y-family cluster around an active site cleft that can accommodate DNA and nucleotide substrates with relaxed geometric constraints, with consequently higher rates of misincorporation and low processivity.
Subcellular Location: Nucleus
EC: 2.7.7.7
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O74944 | MENAKDFIGETIKENGLLTIEDDGSSSSDEEATLKRRLAGPSVLKSGQENVNQKKINEIIYEASKGSKFFEAEQKRDRELRLRIEKVQVEVEKYQSKLRFDKAFQREWTIRQESVDTTVEDFRAKRDLTQIIVHVDCDAFYASIEELKNPKLKSLPMAVGKSVLCTANYVARKFGVRSAMPEFIARKICPDLVVIPLNLSEYAIKSKEIQNVLAQYDSNLCPASIDEFYMNLTSHLRLQELAFTVENITMVVEKIRKQVHEETGVTVSCGIAANKLLAKIASNKRKPNNQFFIPFDEIGISKFMNDLPVREVSGIGRVLEQQLLGLEIKTCGDIQRNLVILSYIFLPKSFQNLLRCSYGFGTTILDEYGESKRKTIGSEATFSSNLSSPSIIEYKLRLLVQNVSENLQKRGLVTNSIAIKYKTSEFQVHTKQKSIGQFIHSESDLLKPALQLLRQSYPMTIRLLGVRATKLVSKSRCLAMQLKFQSQNTVPCPVCQKNIENELGILNQHVDLCLNVETVKSLINTDHTANPTIKKRKSNTLDTYFLE | Function: DNA polymerase specifically involved in DNA repair. Plays an important role in translesion synthesis, where the normal high-fidelity DNA polymerases cannot proceed and DNA synthesis stalls. Has a role in meiosis.
Catalytic Activity: a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) = diphosphate + DNA(n+1)
Sequence Mass (Da): 62055
Sequence Length: 547
Subcellular Location: Cytoplasm
EC: 2.7.7.7
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Q5H8A5 | MIPLPVAAANSNSNSNSNSNDEESPNLSTVIKPPLKKTKTLLPPPSSSSSNRPLHLRVSIDNNNNNNAPPPPADFSDHQWNYPSFLGTTTRKRRPSSVKPPSTSNLRFDTIPKTKTKTKTNTNTNTNTNTNTNTNTDLPPPPVPSSSPVARPQHHNHRSPPIFYLLIITCIIFVPYSSYLQYKLAKLEDHKLHLCRQSQIHFSSGHGNGKISIPIHDASFSYILSRKAALYIVLFTLILPFLLYKYLDYLPQIINFLRRTHNNKEDVPLKKRIAYMLDVFFSIYPYAKLLALLFATLFLIGFGGLALYAVTGGSLAEALWHSWTYVADSGNHAETQGTGQRVVSVSISSGGMLIFAMMLGLVSDAISEKVDSLRKGKCEVIERNHILILGWSDKLGSLLKQLAIANKSVGGGVIVVLAEKEKEEMEMDITKLEFDFMGTSVICRSGSPLILADLKKVSVSKARAIIVLASDENADQSDARALRVVLSLTGVKEGLRGHVVVEMSDLDNEPLVKLVGGELIETVVAHDVIGRLMIQCALQPGLAQIWEDILGFENAEFYIKRWPELDGLSFKDILISFPDAIPCGVKVAADGGKIVINPDDSYVMRDGDEVLVIAEDDDTYSPGSLPEVLKGFFPRIPDAPKYPEKILFCGWRRDIDDMIMVLEAFLAPGSELWMFNEVPEKEREKKLAAGGLDVFGLENIKLVHREGNAVIRRHLESLPLETFDSILILADESVEDSVAHSDSRSLATLLLIRDIQSRRLPYKDTKSTSLRLSGFSHNSWIREMQQASDKSIIISEILDSRTRNLVSVSRISDYVLSNELVSMALAMVAEDKQINRVLEELFAEQGNEMCIKPAEFYLFDQEELCFYDIMIRGRARQEIIIGYRLANQERAIINPSEKLVARKWSLGDVFVVIASGD | Function: Ion channel with permeability for potassium. Involved in perinuclear calcium spiking but not in cytosolic calcium influx. Required for early signal transduction events leading to endosymbiosis. Acts early in a signal transduction chain leading from the perception of Nod factor to the activation of calcium spiking. Also involved in fungal entry into root epidermal cells during the establishment of the arbuscular mycorrhizal symbiosis.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 102062
Sequence Length: 917
Subcellular Location: Nucleus membrane
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Q5N941 | MAESDGGEASPSGGGGGEGSPDPRRPPARPQLTKSRTISGSAASAFDRWGTSNSSSSILVRRSSTAPLPPGAAPRGLLTVAVDEPSYAAPNGGAAMLDRDWCYPSFLGPHASRPRPPRSQQQTPTTTAAAAADSRSPTPAAPPQTASVSQREEEKSLASVVKRPMLLDERRSLSPPPPQQRAPRFDLSPYLVLMLVVTVISFSLAIWQWMKATVLQEKIRSCCSVSTVDCKTTTEAFKINGQHGSDFINSADWNLASCSRMLVFAIPVFLVKYIDQLRRRNTDSIRLRSTEEEVPLKKRIAYKVDVFFSGHPYAKLLALLLATIILIASGGIALYVVSGSGFLEALWLSWTFVADSGNHADQVGLGPRIVSVSISSGGMLVFATMLGLVSDAISEKVDSWRKGKSEVIEVNHILILGWSDKLGSLLKQLAIANKSIGGGVVVVLAERDKEEMEMDIGKLEFDFMGTSVICRSGSPLILADLKKVSVSKARAIIVLASDENADQSDARALRVVLSLTGVKEGLRGHVVVEMSDLDNEPLVKLVGGELIETVVAHDVIGRLMIQCALQPGLAQIWEDILGFENAEFYIKRWPELDGMRFGDVLISFPDAVPCGVKIASKAGKILMNPDNDYVLQEGDEVLVIAEDDDTYVPASLPQVRKGFLPNIPTPPKYPEKILFCGWRRDIHDMIMVLEAFLAPGSELWMFNEVPEKERERKLTDGGMDIYGLTNIKLVHKEGNAVIRRHLESLPLETFDSILILADESVEDSIVHSDSRSLATLLLIRDIQSKRLPSKELKSPLRYNGFCHSSWIREMQHASDKSIIISEILDSRTRNLVSVSKISDYVLSNELVSMALAMVAEDKQINRVLEELFAEEGNEMCIRSAEFYLYEQEELSFFDIMVRARERDEVVIGYRLANDDQAIINPEQKSEIRKWSLDDVFVVISKAGNATYFVKTTVMRSNPVVYSSTF | Function: Required for mycorrhizal symbiosis.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 106215
Sequence Length: 965
Subcellular Location: Nucleus membrane
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P15480 | MTNLQDQTQQIVPFIRSLLMPTTGPASIPDDTLEKHTLRSETSTYNLTVGDTGSGLIVFFPGFPGSIVGAHYTLQSNGNYKFDQMLLTAQNLPASYNYCRLVSRSLTVRSSTLPGGVYALNGTINAVTFQGSLSELTDVSYNGLMSATANINDKIGNVLVGEGVTVLSLPTSYDLGYVRLGDPIPAIGLDPKMVATCDSSDRPRVYTITAADDYQFSSQYQPGGVTITLFSANIDAITSLSVGGELVFQTSVHGLVLGATIYLIGFDGTTVITRAVAANNGLTTGTDNLMPFNLVISTNEITQPITSIKLEIVTSKSGGQAGDQMSWSAKGSLAVTIHGGNYPGALRPVTLVAYERVATGSVVTVAGVSNFELIPNPELAKNLVTEYGRFDPGAMNYTKLILSERDRLGIKTVWPTREYTDFREYFMEVADLNSPLKIAGAFGFKDIIRAIRRIAVPVVSTLFPPAAPLAHAIGEGVDYLLGDEAQAASGTARAASGKARAASGRIRQLTLAADKGYEVVANLFQVPQNPVVDGILASPGVLRGAHNLDCVLREGATLFPVVITTVEDAMTPKALNSKMFAVIEGVREDLQPPSQRGSFIRTLSGHRVYGYAPDGVLPLETGRDYTVVPIDDVWDDSIMLSKDPIPPIVGNSGNLAIAYMDVFRPKVPIHVAMTGALNACGEIEKVSFRSTKLATAHRLGLKLAGPGAFDVNTGPNWATFIKRFPHNPRDWDRLPYLNLPYLPPNAGRQYHLAMAASEFKETPELESAVRAMEAAANVDPLFQSALSVFMWLEENGIVTDMANFALSDPNAHRMRNFLANAPQAGSKSQRAKYGTAGYGVEARGPTPEEAQREKDTRISKKMETMGIYFATPEWVALNGHRGPSPGQLKYWQNTREIPDPNEDYLDYVHAEKSRLASEEQILRAATSIYGAPGQAEPPQAFIDEVAKVYEINHGRGPNQEQMKDLLLTAMEMKHRNPRRALPKPKPKPNAPTQRPPGRLGRWIRTVSDEDLE | Function: Capsid protein VP2 self assembles to form an icosahedral capsid with a T=13 symmetry, about 70 nm in diameter, and consisting of 260 VP2 trimers. The capsid encapsulates the genomic dsRNA. VP2 is also involved in attachment and entry into the host cell by interacting with host ITGA4/ITGB1 (By similarity).
PTM: Specific enzymatic cleavages yield mature proteins. The capsid assembly seems to be regulated by polyprotein processing. The protease VP4 cleaves itself off the polyprotein, thus releasing pre-VP2 and VP3 within the infected cell. During capsid assembly, the C-terminus of pre-VP2 is further processed by VP4, giving rise to VP2, the external capsid protein and three small peptides that all stay closely associated with the capsid (By similarity).
Sequence Mass (Da): 109681
Sequence Length: 1012
Subcellular Location: Virion
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Q8EUR3 | MKTKDNEVINSESEFSEKDVPNFIEIKKINKTYPDGYVAVKNINFEIKKGEFVTILGPSGCGKTTILKMIGGFELPTSGKILVNKIDIKDLPIQRRPTATVFQDYALFPNMNVEKNIAYGLTEIRKPIENVSADYQKESEKYFNDCLKKSKSKIKDIERKRDGFLKDIQKLENKINNSKILSEVNTMTEEEYEEKIETLEKEYFEKNKKELHKSIPVKVKFIEFINNTLSFFRINKNIDFKANETDELVQTYLKYEKAYRVNLITKQEIDYLNHKAADLDYWVSYWQNYPYQEKEWFDKKKLTRKLTKQEIKEEVQQIIKIIGLEGKEKKWPSDLSGGMQQRVALARALVIKPETLLLDEPLSALDAKVRAQMQQELKNLHKKFGITFILVTHDQEEALTLSDKIIVMSQGKIQQIGTPNEIYDLPANNWVANFIGKANILNATYLKGNKIKLFDNVLNADSRYKDKFKENEEVNVMIRPEDFDVVGKDKGKIKVTVLETTYKGLMWELICEFEGVLLTLEAVNKVNLEQEIYLTWDDEDMHIMKKDDENDTYTDESSEFLALTKNAFKKKIKEIKSKKNKNKVNGKKGDKNDN | Function: Part of the ABC transporter complex PotABCD involved in spermidine/putrescine import. Responsible for energy coupling to the transport system.
Catalytic Activity: ATP + H2O + polyamine-[polyamine-binding protein]Side 1 = ADP + phosphate + polyamineSide 2 + [polyamine-binding protein]Side 1.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 69136
Sequence Length: 594
Subcellular Location: Cell membrane
EC: 7.6.2.11
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A1TXH7 | MKQTLLSLSNLTKQFDGKKVLDSLDLDIFDGEFITLLGPSGCGKTTLLRMMAGFEHPDDGTIALGDQDLTHTPPEHRPLNTVFQNYALFPHMSVFDNVAYGLKMEKRPKQEIRERVEDALAMVQLEDFARRKPHQLSGGQQQRVAIARAVVKRPKVLLLDEPLSALDYKLRRTMQVELKRLQRELGITFVFVTHDQEEALSMSDRVVVLKDGLIQQLGTPREVYERPANLFTARFVGETNFFPGRVDKANGDDTITVDVFGLKRTFRKPDFPVSGGQSLHVLLRPEDIRVLAPDDEDGVAGKIVERNYKGSTLDSVIHLEDGTEVLASEFFDEDDPTFDYRLGEPVKVSWVDGWEWLLPTEPEALPEEEGTDA | Function: Part of the ABC transporter complex PotABCD involved in spermidine/putrescine import. Responsible for energy coupling to the transport system.
Catalytic Activity: ATP + H2O + polyamine-[polyamine-binding protein]Side 1 = ADP + phosphate + polyamineSide 2 + [polyamine-binding protein]Side 1.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 42107
Sequence Length: 373
Subcellular Location: Cell inner membrane
EC: 7.6.2.11
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Q6F0V4 | MENNILELRNVTKDYDGKVVLKGIDLNIKEGEFITLLGPSGCGKTTTLRIVAGFEKPNSGQIMFEGKDLLPIPINKRQFNTIFQSYALFPHLNVFDNIAFGLRTKKTKKDILQREVLKQIRQVGLEGFEDRNINDLSGGQKQRVAIARALVMKPKVLLLDEPLAALDVQLRQHMREELKRLQREIGITFLMVSHDQEEALSISDRVVVMNEGSIQQIGTPEDIYNEPENLWVAKFIGQSNIIEDGIFIEDNKVQIDGKTFVCDDTNFGENEKSIDIVIRPEDIEIKKTNAGFFNGTVMHTTFKGVHWELLVETTKKRIWKIHTTQAFKVDDKVSIKWNDEAIHVMWKEVE | Function: Part of the ABC transporter complex PotABCD involved in spermidine/putrescine import. Responsible for energy coupling to the transport system.
Catalytic Activity: ATP + H2O + polyamine-[polyamine-binding protein]Side 1 = ADP + phosphate + polyamineSide 2 + [polyamine-binding protein]Side 1.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 40048
Sequence Length: 350
Subcellular Location: Cell membrane
EC: 7.6.2.11
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Q5ZZZ7 | MKNIEKSEIIISLVDVDKEFGDKKVLDQINLDIKRGDFVTLLGPSGSGKTTILRLIGGFEWTTRGEIKFNGIDIKDVPAHKRDTATIFQDYALFPHLSVRGNIEFGLKLKRIKKKAEEIPDVVWKKFEHLKKKWQDKQKRKIKELKILQAHLEKLLENPQLDIKKRKKLQDKLDDSDFRYSNWENYLTSKSESFKKKYLTRRITKQEINKEITDIIDLVGLTGNENRAISELSGGMKQRVALARSLVIEPEIVLLDEPLSALDTKIRQKMQVFLKKIQQKLGLTFIFVTHDQDEALQLSDKIAIIRNGKIAQYDEPKQIYDYPVNKWVANFIGDSNFFQAKYIKKNQVEILGLKLYTIHDEFIPGQKLDCLIRPEDIDIDLNSGYFKGKVIQNIYKGSYYSLDIKVENTIINVETNDFYDLETQVFIKWDDDAIHLMEMENAEI | Function: Part of the ABC transporter complex PotABCD involved in spermidine/putrescine import. Responsible for energy coupling to the transport system.
Catalytic Activity: ATP + H2O + polyamine-[polyamine-binding protein]Side 1 = ADP + phosphate + polyamineSide 2 + [polyamine-binding protein]Side 1.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 51689
Sequence Length: 444
Subcellular Location: Cell membrane
EC: 7.6.2.11
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P75059 | MNERFLIEIEGLNKTFDDGFVSVRDINLKIKKGEFITILGPSGCGKTTTLRLLAGFEDPTYGKIKVNGLDIKDLPIHKRPFATVFQDYALFSHLTVYKNIAYGLKAMYTKLDPIDKLVEQYHQSLLDKQHRLHKRIERLEKSNANPQLLEQLKQTVVVQQKQFKQQTETFKQKENARRDAIQQRLVQLTKEWESLSKQKLQQLEAEKKLLDKKFEQTERKYQKDAWMATHSEMRLKQFKQEVLALKQLIKTKFKQNEPVDKLQLKLQTLKQKYAAKRQIDKEYDKLVLAYNKKDYWTSYWETYSLQQQEAFEKRYLSRKLTKQEQHQKVCAVIELVGLKGNEDKLPEELSGGMKQRVALARSLVIEPDILLLDEPLSALDAKVRKNLQKELQKIHQQSGLTFILVTHDQEEALVLSNRIVVMNEGNILQVGSPADIYDSPKTEWIANFIGQANIFKGTYLGDLKIKLHSGEVIKTDVDNNYVVGKEYKILIRPEDFDIVPKNKGFFNVRVIDKTYKGLLWKITTKLVDDTIVDLESVNDIEVDKTFGVTFDPIDVHLMEV | Function: Part of the ABC transporter complex PotABCD involved in spermidine/putrescine import. Responsible for energy coupling to the transport system.
Catalytic Activity: ATP + H2O + polyamine-[polyamine-binding protein]Side 1 = ADP + phosphate + polyamineSide 2 + [polyamine-binding protein]Side 1.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 65131
Sequence Length: 560
Subcellular Location: Cell membrane
EC: 7.6.2.11
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Q98QE1 | MNNINTTLIEGRKSHSKFHISLKNVDKNYGDKKILDDVNLSIKKGEFVTLLGPSGSGKTTILRLIGGFEWTTRGEILFDGLDIKDLSPHKRETSTIFQDYALFQHLSVTGNIKYGLKLKRYPKDPSSIDPGIYKNLEKKKKEWEKFAKSKMKQLDKTQEEYEKILKSKNLSRGKRQKYQSWLDDSDFKYSYWETYVVNKVEQFEKHHLTRKITKDEINEEITKMIKLVGLEGSENKKISELSGGMKQRVALARSLVIEPEILLLDEPLSALDAKIRTKMQRLLIELQKKIGITFIFVTHDQDEALELSDRIAVIRDGKIEQFDTPKQIYDYPINKWVANFIGEANFFDVRFVEKNKALLLGKHIPTIHTEFEEGQKLDGLIRPEDIDISLEKGHFEGVVEKIIYKGSYYFISVNVEGKIIEVETNDYFEVGKKVWITWDLDALHLMAKDHKGFMANDF | Function: Part of the ABC transporter complex PotABCD involved in spermidine/putrescine import. Responsible for energy coupling to the transport system.
Catalytic Activity: ATP + H2O + polyamine-[polyamine-binding protein]Side 1 = ADP + phosphate + polyamineSide 2 + [polyamine-binding protein]Side 1.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 53108
Sequence Length: 458
Subcellular Location: Cell membrane
EC: 7.6.2.11
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A1TAI4 | MIEIDHVTKSFGDYVAVADADFSIASGEFFSMLGPSGCGKTTTLRMIAGFETPTEGAIRLEGADVSRTPPNKRNVNTVFQHYALFPHMTVWDNVAYGPRSKKLGKGEIRKRVDELLDIVRLTDFAERKPAQLSGGQQQRVALARALVNYPSALLLDEPLGALDLKLRHVMQFELKRIQREVGITFIYVTHDQEEALTMSDRIAVMNAGNVEQIGTPTEIYDRPATVFVASFIGQANLWAGRQTGRANRDYVEVDVLGSTLKARPGETTIEPGGHATLMVRPERIRVSMDAPTGDVAAVRATVSDLTFQGPVVRLSLAAPDDSTVIAHVGPEQDLPLLRPGDDVFVSWAPDASLVLPGADIPTTEDLEEMLDDS | Function: Part of the ABC transporter complex PotABCD involved in spermidine/putrescine import. Responsible for energy coupling to the transport system.
Catalytic Activity: ATP + H2O + polyamine-[polyamine-binding protein]Side 1 = ADP + phosphate + polyamineSide 2 + [polyamine-binding protein]Side 1.
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 40711
Sequence Length: 373
Subcellular Location: Cell membrane
EC: 7.6.2.11
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P23733 | MNCDEIIKKLLLNPVHNTAATRGPAGENCESNQRTYTRISRLAAFQSAQTQESTPKTNGTGRATTEGLTEAEVRWLVMESRALFMSQPMLVEIAAPVRICGDVHGQYTDLLRLFDLGGFPPDANYIFLGDYVDRGDQSLERICLLLAYKLSFPETFFLLRGNHECSSINRIYGFFDECKRRYSVRLWKQFTDTFNCMPVAGLVEGRILCMHGGLSPELTDLDQIRRILRPTDVPDSGLICDLLWSDPSTNMESNWSENDRGVSWTFSESVVKSFNKKFDLDLICRAHQVVDAGYEFFAARQLVTVFSAPNYCDEFDNAGAFMCVDENFMCSFIRIEPTRTLLKYFF | Cofactor: Binds 2 manganese ions per subunit.
Catalytic Activity: H2O + O-phospho-L-seryl-[protein] = L-seryl-[protein] + phosphate
Sequence Mass (Da): 39373
Sequence Length: 346
EC: 3.1.3.16
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P20604 | MVSRGPDEWLETIKKCQALTENEMKQLCEMVKELLMEESNIQPVQTPVTVCGDIHGQFHDLLELFRTAGGFPDDINYIFLGDYVDRGYYSLETFTLLMCLKVKYPAKITLVRGNHESRQITQVYGFYEECLNKYGSTTVWKYCCQVFDFLTLAAIIDGKILCVHGGLSPEIRMLDQIRVLSRAQEVPHEGGFSDLLWSDPDNVEAWQVSPRGAGWLFGSKVAREFNHVNGLNLIARAHQLVMEGFKYHFPEKDVVTVWSAPNYCYRCGNVASVMKVDEDLEPTFKIFSAVPDDYIRESTANHNNQRAGYFL | Cofactor: Binds 2 manganese ions per subunit.
Function: Involved in the dephosphorylation of the large subunit of RNA polymerase II. Is required in late G1 for normal G1 cyclin expression, bud initiation and expression of certain genes that are periodically expressed during late G1. Associates with the SAP proteins in a cell cycle-dependent manner.
Catalytic Activity: H2O + O-phospho-L-seryl-[protein] = L-seryl-[protein] + phosphate
Sequence Mass (Da): 35538
Sequence Length: 311
Subcellular Location: Cytoplasm
EC: 3.1.3.16
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Q9BZL4 | MSGEDGPAAGPGAAAAAARERRREQLRQWGARAGAEPGPGERRARTVRFERAAEFLAACAGGDLDEARLMLRAADPGPGAELDPAAPPPARAVLDSTNADGISALHQACIDENLEVVRFLVEQGATVNQADNEGWTPLHVAASCGYLDIARYLLSHGANIAAVNSDGDLPLDLAESDAMEGLLKAEIARRGVDVEAAKRAEEELLLHDTRCWLNGGAMPEARHPRTGASALHVAAAKGYIEVMRLLLQAGYDPELRDGDGWTPLHAAAHWGVEDACRLLAEHGGGMDSLTHAGQRPCDLADEEVLSLLEELARKQEDLRNQKEASQSRGQEPQAPSSSKHRRSSVCRLSSREKISLQDLSKERRPGGAGGPPIQDEDEGEEGPTEPPPAEPRTLNGVSSPPHPSPKSPVQLEEAPFSRRFGLLKTGSSGALGPPERRTAEGAPGAGLQRSASSSWLEGTSTQAKELRLARITPTPSPKLPEPSVLSEVTKPPPCLENSSPPSRIPEPESPAKPNVPTASTAPPADSRDRRRSYQMPVRDEESESQRKARSRLMRQSRRSTQGVTLTDLKEAEKAAGKAPESEKPAQSLDPSRRPRVPGVENSDSPAQRAEAPDGQGPGPQAAREHRKVGKEWRGPAEGEEAEPADRSQESSTLEGGPSARRQRWQRDLNPEPEPESEEPDGGFRTLYAELRRENERLREALTETTLRLAQLKVELERATQRQERFAERPALLELERFERRALERKAAELEEELKALSDLRADNQRLKDENAALIRVISKLSK | Function: Regulates myosin phosphatase activity.
PTM: Phosphorylation at Thr-560 is essential for its interaction with PPP1CB.
Sequence Mass (Da): 84881
Sequence Length: 782
Subcellular Location: Cytoplasm
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P48482 | MAQQGQGSMDPAALDDIIRRLLDYRNPKPGTKQAMLNESEIRQLCIVSREIFLQQPNLLELEAPIKICGDIHGQYSDLLRLFEYGGFPPTANYLFLGDYVDRGKQSLETICLLLAYKIKYPENFFLLRGNHECASINRIYGFYDECKRRFSVRLWKVFTDSFNCLPVAAVIDDKILCMHGGLSPDLTNVEQIKNIKRPTDVPDSGLLCDLLWSDPSKDVKGWGMNDRGVSYTFGPDKVAEFLIKNDMDLICRAHQVVEDGYEFFADRQLVTIFSAPNYCGEFDNAGAMMSVDESLMCSFQILKPADRKPRFL | Cofactor: Binds 2 manganese ions per subunit.
Function: Serine/threonine-protein phosphatase that possesses phosphatase activity toward para-nitrophenyl phosphate (pNPP) in vitro.
Catalytic Activity: H2O + O-phospho-L-seryl-[protein] = L-seryl-[protein] + phosphate
Sequence Mass (Da): 35532
Sequence Length: 312
Subcellular Location: Nucleus
EC: 3.1.3.16
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P12982 | MGDVMNIDSIISRLLEVRGARPGKNVQLSEGEIRGLCLKSREIFLSQPILLELEAPLKICGDIHGQYYDLLRLFEYGGFPPESNYLFLGDYVDRGKQSLETICLLLAYKIKYSENFFLLRGNHECASINRIYGFYDECKRRYSIKLWKTFTDCFNCLPVAAIVDEKIFCCHGGLSPDLTSMEQIRRIMRPTDVPDQGLLCDLLWSDPDKDTMGWGENDRGVSFTFGAEVVAKFLQKHEFDLICRAHQVVEDGYEFFAKRMLVTLFSAPNYCGEFDNAGAMMSVDDTLMCSFQILKPADKRKK | Cofactor: Binds 2 manganese ions per subunit.
Function: Is essential for the regulation of mitotic chromosomal segregation as well as regulation of chromatin condensation during interphase.
Catalytic Activity: H2O + O-phospho-L-seryl-[protein] = L-seryl-[protein] + phosphate
Sequence Mass (Da): 34542
Sequence Length: 302
Subcellular Location: Cytoplasm
EC: 3.1.3.16
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Q12972 | MAAAANSGSSLPLFDCPTWAGKPPPGLHLDVVKGDKLIEKLIIDEKKYYLFGRNPDLCDFTIDHQSCSRVHAALVYHKHLKRVFLIDLNSTHGTFLGHIRLEPHKPQQIPIDSTVSFGASTRAYTLREKPQTLPSAVKGDEKMGGEDDELKGLLGLPEEETELDNLTEFNTAHNKRISTLTIEEGNLDIQRPKRKRKNSRVTFSEDDEIINPEDVDPSVGRFRNMVQTAVVPVKKKRVEGPGSLGLEESGSRRMQNFAFSGGLYGGLPPTHSEAGSQPHGIHGTALIGGLPMPYPNLAPDVDLTPVVPSAVNMNPAPNPAVYNPEAVNEPKKKKYAKEAWPGKKPTPSLLI | Cofactor: Endoribonuclease function is magnesium-dependent.
Function: Inhibitor subunit of the major nuclear protein phosphatase-1 (PP-1). It has RNA-binding activity but does not cleave RNA and may target PP-1 to RNA-associated substrates. May also be involved in pre-mRNA splicing. Binds DNA and might act as a transcriptional repressor. Seems to be required for cell proliferation.
PTM: May be inactivated by phosphorylation on Ser-199 or Ser-204 (By similarity). Phosphorylated by Lyn in vitro on Tyr-264, and also on Tyr-335 in the presence of RNA.
Sequence Mass (Da): 38479
Sequence Length: 351
Domain: Has a basic N- and C-terminal and an acidic central domain.
Subcellular Location: Nucleus
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Q96QC0 | MGSGPIDPKELLKGLDSFLNRDGEVKSVDGISKIFSLMKEARKMVSRCTYLNILLQTRSPEILVKFIDVGGYKLLNNWLTYSKTTNNIPLLQQILLTLQHLPLTVDHLKQNNTAKLVKQLSKSSEDEELRKLASVLVSDWMAVIRSQSSTQPAEKDKKKRKDEGKSRTTLPERPLTEVKAETRAEEAPEKKREKPKSLRTTAPSHAKFRSTGLELETPSLVPVKKNASTVVVSDKYNLKPIPLKRQSNVAAPGDATPPAEKKYKPLNTTPNATKEIKVKIIPPQPMEGLGFLDALNSAPVPGIKIKKKKKVLSPTAAKPSPFEGKTSTEPSTAKPSSPEPAPPSEAMDADRPGTPVPPVEVPELMDTASLEPGALDAKPVESPGDPNQLTRKGRKRKSVTWPEEGKLREYFYFELDETERVNVNKIKDFGEAAKREILSDRHAFETARRLSHDNMEEKVPWVCPRPLVLPSPLVTPGSNSQERYIQAEREKGILQELFLNKESPHEPDPEPYEPIPPKLIPLDEECSMDETPYVETLEPGGSGGSPDGAGGSKLPPVLANLMGSMGAGKGPQGPGGGGINVQEILTSIMGSPNSHPSEELLKQPDYSDKIKQMLVPHGLLGPGPIANGFPPGGPGGPKGMQHFPPGPGGPMPGPHGGPGGPVGPRLLGPPPPPRGGDPFWDGPGDPMRGGPMRGGPGPGPGPYHRGRGGRGGNEPPPPPPPFRGARGGRSGGGPPNGRGGPGGGMVGGGGHRPHEGPGGGMGNSSGHRPHEGPGGGMGSGHRPHEGPGGSMGGGGGHRPHEGPGGGISGGSGHRPHEGPGGGMGAGGGHRPHEGPGGSMGGSGGHRPHEGPGHGGPHGHRPHDVPGHRGHDHRGPPPHEHRGHDGPGHGGGGHRGHDGGHSHGGDMSNRPVCRHFMMKGNCRYENNCAFYHPGVNGPPLP | Function: Scaffold protein which mediates the formation of the PTW/PP1 phosphatase complex by providing a binding platform to each component of the complex. The PTW/PP1 phosphatase complex plays a role in the control of chromatin structure and cell cycle progression during the transition from mitosis into interphase. Mediates interaction of WDR82 and PPP1CA. Inhibitor of PPP1CA and PPP1CC phosphatase activities. Has inhibitory activity on PPP1CA only when phosphorylated. Binds to mRNA, single-stranded DNA (ssDNA), poly(A) and poly(G) homopolymers (By similarity).
PTM: Phosphorylated on Ser-398 by PKA within the region necessary for interaction with PPP1CA.
Sequence Mass (Da): 99058
Sequence Length: 940
Subcellular Location: Nucleus
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O55000 | MGSGPIDPKELLKGLDSFLTRDGEVKSVDGIAKIFSLMKEARKMVSRCTYLNIILQTRAPEVLVKFIDVGGYKLLNSWLTYSKTTNNIPLLQQILLTLQHLPLTVDHLKQNNTAKLVKQLSKSSEDEELRKLASVLVSDWMAVIRSQSSTQPAEKDKKKRKEEGKSRTTLPERPLTEVKAETRAEEAPEKKKEKPKSLRTTAPSHAKFRSTGLELDTPSLVPVKKNSSTVVVSDKYNLKPIPLKRQSATAAPGDAAPPAEKKYKPLNTTPNTTKEIKVKIIPPQPMEGLGFLDALNSAPVPGIKIKKKKKVLSPTAAKPSPFEGKTSTEPSTAKPSSPEPAAPAEPMDTDRPGTPVPAVEVPELMDAASSEPGALDAKPVESPGDPNQLTRKGRKRKTVTWPEEGKLREYFYFELDETERVNVNKIKDFGEAAKREILSDRHAFETARRLSHDNMEEKVPWVCPRPLVLPSPLVIPGSNSQERYIQAEREKGILQELFLNKESPHEPDPEPYEPIPPKLIPLDEECAMDETPYVETLEPGGSGGSPDGAGGSKLPPVLANLMGSMGAGKSPQGPGGGGINVQEILTSIMGSPNNHPSEELLKQPDYSDKLKQMLVPHGLLGPGPVANGFPPGGPGGPKGMQHFPPGPGGPMPGPHGGPGGPVGPRLLGPPPPSRGGDPFWDGPGDPMRGGPMRGGPGPGPGPYHRGRGGRGGNEPPPPPPFRGARGGRSGGGPPNGRGGPGGGGMVGGGGHRPHEGPGGSMGSGHRSHEGPGGSMGSGHRSHEGPGHGGPHGHRPHDVPSHRGHDHRGPPPHEHRGHDGHGGGGHRGHDGGHSHGGDMSNRPVCRHFMMKGNCRYENNCAFYHPGVNGPPLP | Function: Scaffold protein which mediates the formation of the PTW/PP1 phosphatase complex by providing a binding platform to each component of the complex. The PTW/PP1 phosphatase complex plays a role in the control of chromatin structure and cell cycle progression during the transition from mitosis into interphase. Mediates interaction of WDR82 and PPP1CA. Inhibitor of PPP1CA and PPP1CC phosphatase activities. Has inhibitory activity on PPP1CA only when phosphorylated. Binds to mRNA, single-stranded DNA (ssDNA), poly(A) and poly(G) homopolymers.
PTM: Phosphorylated on Thr-398 by PKA within the region necessary for interaction with PPP1CA.
Sequence Mass (Da): 92828
Sequence Length: 872
Subcellular Location: Nucleus
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Q568K2 | MAEVPGTSSETITETVQTGTPPPPQQEGRSLTIKLRKRKTEKKVEWSSDTVDNEHLGRRSSKCCCIYEKPRQFGESSSESEGDDEEGCGSAHCILGHGRRGHGQREGGGTTVPPSSGGTNPH | Function: Atypical E3 ubiquitin-protein ligase which ubiquitinates TLR2 at 'Lys-754' leading to its degradation by the proteasome. Inhibitor of protein phosphatase 1.
Catalytic Activity: S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.
Sequence Mass (Da): 13106
Sequence Length: 122
Pathway: Protein modification; protein ubiquitination.
EC: 2.3.2.27
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O60927 | MAEAGAGLSETVTETTVTVTTEPENRSLTIKLRKRKPEKKVEWTSDTVDNEHMGRRSSKCCCIYEKPRAFGESSTESDEEEEEGCGHTHCVRGHRKGRRRATLGPTPTTPPQPPDPSQPPPGPMQH | Function: Atypical E3 ubiquitin-protein ligase which ubiquitinates TLR2 at 'Lys-754' leading to its degradation by the proteasome. Plays a role in regulating inflammatory cytokine release and gram-positive bacterial clearance by functioning, in part, through the ubiquitination and degradation of TLR2 . Inhibitor of protein phosphatase 1 .
PTM: Auto-ubiquitinated.
Catalytic Activity: S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.
Sequence Mass (Da): 13953
Sequence Length: 126
Pathway: Protein modification; protein ubiquitination.
EC: 2.3.2.27
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Q8K1L5 | MAETGAGISETVTETTVTETTVTETTEPENQSLIMKLRKRKPEKKVEWSSDTVDNEHMGRRSSKCCCIYEKPRAFGESSTESDEDEEEGCSHKHCVRGHRKGRRPTTPAPTPTTPPQPPDPSQPPPGPMQH | Function: Atypical E3 ubiquitin-protein ligase which ubiquitinates TLR2 at 'Lys-754' leading to its degradation by the proteasome. Plays a role in regulating inflammatory cytokine release and gram-positive bacterial clearance by functioning, in part, through the ubiquitination and degradation of TLR2 . Inhibitor of protein phosphatase 1 (By similarity).
PTM: Auto-ubiquitinated.
Catalytic Activity: S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.
Sequence Mass (Da): 14544
Sequence Length: 131
Pathway: Protein modification; protein ubiquitination.
EC: 2.3.2.27
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Q09173 | MGQTLSEPVTEKHSVNGSNEFVLYGLSSMQGWRISMEDAHSAILSMECSAVKDPVDFFAVYDGHGGDKVAKWCGSNLPQILEKNPDFQKGDFVNALKSSFLNADKAILDDDQFHTDPSGCTATVVLRVGNKLYCANAGDSRTVLGSKGIAKPLSADHKPSNEAEKARICAAGGFVDFGRVNGNLALSRAIGDFEFKNSNLEPEKQIVTALPDVVVHEITDDDEFVVLACDGIWDCKTSQQVIEFVRRGIVAGTSLEKIAENLMDNCIASDTETTGLGCDNMTVCIVALLQENDKSAWYKKIADRVAANDGPCAPPEYAENHGPGWRSGDNNKKVIVPPNFHQVKLNGSDGYDKDANENSKEDDSTNGSLAAGFRWKEHFFPHKAEEENSSSETDIVNSNKDVADDHKEAVSAAD | Cofactor: Binds 2 magnesium or manganese ions per subunit.
Function: Has an important role in osmotic stability and cell shape control. It may negatively regulate the osmosensing signal transmitted through wis1 map kinase.
Catalytic Activity: H2O + O-phospho-L-seryl-[protein] = L-seryl-[protein] + phosphate
Sequence Mass (Da): 44857
Sequence Length: 414
EC: 3.1.3.16
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P34221 | MGQILSNPIIDKEHHSGTDCLTAFGLCAMQGWRMSMEDAHIVEPNLLAESDEEHLAFYGIFDGHGGSSVAEFCGSKMISILKKQESFKSGMLEQCLIDTFLATDVELLKDEKLKDDHSGCTATVILVSQLKKLLICANSGDSRTVLSTGGNSKAMSFDHKPTLLSEKSRIVAADGFVEMDRVNGNLALSRAIGDFEFKSNTKLGPHEQVVTCVPDIICHNLNYDEDEFVILACDGIWDCLTSQECVDLVHYGISQGNMTLSDISSRIVDVCCSPTTEGSGIGCDNMSISIVALLKENESESQWFERMRSKNYNIQTSFVQRRKSIFDFHDFSDDDNEVFAITTKKLQDRLNRSKDNDDMEIDDLDTELGSSATPSKLSGEDRTGPIDLFSLEALLEAGIQIRQRPSSDSDGNTSYFHGASLSDMLASLSNAAAGETEPNDADDNDDNDGEENGKNENAKKGSKIEEIE | Cofactor: Binds 2 magnesium or manganese ions per subunit.
Function: Responsible, together with PTC2, for the dephosphorylation of the cyclin-dependent protein kinase CDC28.
Catalytic Activity: H2O + O-phospho-L-seryl-[protein] = L-seryl-[protein] + phosphate
Sequence Mass (Da): 51332
Sequence Length: 468
Subcellular Location: Cytoplasm
EC: 3.1.3.16
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O14156 | MSIRFLKRLRAPLYIQNAYCSKNYFYRSFIQYYSPSNGPYLKISMNKAPQSLGLCTARGDSPTNQDRMAYGYLNNLKDTTNRDSPFFYGLFDGHGGTECSEFLSTNLGKIIENQDLNDTEKILKEVHSVGGYMAGLKPPFSLRTVLQSRDEDLLWRARLYYSFLQADMDYLTNYARPSPDSAVPGAVGTVAIITSKNNLSYWESDSYIIHLAHVGDTRALLCDSRTGRAHRLTFQHHPADVEEARRLRRYNMGFSRDSFGQKRFAWVANTRSFGDGYKLKKLGVVAEPQLTSIHSLRDDWSFLTLLSDGITDVVSDDEVVDIIKLSESPQDAANNIIRYAQNVGAVDDITCLVVRLPGWKKRTINDFTKNLRLEKSAYHPRRS | Cofactor: Binds 2 magnesium or manganese ions per subunit.
Function: Has a role in the regulation of vacuole fusion.
Catalytic Activity: H2O + O-phospho-L-seryl-[protein] = L-seryl-[protein] + phosphate
Location Topology: Peripheral membrane protein
Sequence Mass (Da): 43569
Sequence Length: 383
Subcellular Location: Vacuole membrane
EC: 3.1.3.16
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P38089 | MGQLLSHPLTEKTIEYNEYKNNQASTGIVPRFYNCVGSMQGYRLTQEDAHLIRNENSVVYVRFFNPFIDKYETLSLNVFAVFDGHGGDDCSKFLSGGRHHRDGNGSSNGNGEPNAGLIKWIAYSFENHHYTSTTNNDSSKFKRSFNTLEGLVSQIFKDAFILQDEELYRHFANSSCGSTAVVACIINEESLYVANCGDSRCILSSKSNGIKTMSFDHKPQHIGELIRINDNGGTVSLGRVGGVLALSRAFSDFQFKRGVTYPHRRTKLTNITQNLTYGTPPQEAQVTVEPDVLMHKIDYSKDEFLVLACDGIWDIYNNKQLIHFIKYHLVSGTKLDTIITKLLDHGIAQANSNTGVGFDNMTAIIVVLNRKGETLQDWFNKMKTRLERERGLV | Cofactor: Binds 2 magnesium or manganese ions per subunit.
Catalytic Activity: H2O + O-phospho-L-seryl-[protein] = L-seryl-[protein] + phosphate
Sequence Mass (Da): 44176
Sequence Length: 393
EC: 3.1.3.16
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O14189 | MNFFTSAVGSKVFKRNNFKYVAIAASSIGLAAYHIRKDAIALDIPNSTYQHVSKNRVPPTDGDGITKRLKEFERTVTVNKDGIFRYDFNQVASNDPCEDDHVEVIDRNIDEGNWYFWGIFDGHSGWNTSLFLRQHLVPAVVRELQKCTASYYHQNACPSSLALDKSISEAFAKVDHQIVHEHVSHVFNNPESLQVAASLLLPALSGSCALLTSYSAKSKSLQVACTGDSRAVLGECTPDGSWEAIPLSRDQTGMNPDEASRLEVEHPGEEVLRNNRILGRLMPSRAFGDARYKWSQEISERLHREYFSASPIPVKTPPYVTAVPEIESITVNPKKHRFLIMASDGLWDTMSSEQAVQLVGEWADTVLGKTTNEKNTTQDDKQSWSLFKKTSKVIDDNAATHLIRHSLGGSDQRISALLTLTYPISRRYRDDITVTVIFFDEKTL | Cofactor: Binds 2 magnesium or manganese ions per subunit.
Function: Involved in regulation of pyruvate dehydrogenase activity.
Catalytic Activity: H2O + O-phospho-L-seryl-[protein] = L-seryl-[protein] + phosphate
Sequence Mass (Da): 49741
Sequence Length: 444
Subcellular Location: Mitochondrion
EC: 3.1.3.16
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P38797 | MFANVGFRTLRVSRGPLYGSCSQIISFSKRTFYSSAKSGYQSNNSHGDAYSSGSQSGPFTYKTAVAFQPKDRDDLIYQKLKDSIRSPTGEDNYFVTSNNVHDIFAGVADGVGGWAEHGYDSSAISRELCKKMDEISTALAENSSKETLLTPKKIIGAAYAKIRDEKVVKVGGTTAIVAHFPSNGKLEVANLGDSWCGVFRDSKLVFQTKFQTVGFNAPYQLSIIPEEMLKEAERRGSKYILNTPRDADEYSFQLKKKDIIILATDGVTDNIATDDIELFLKDNAARTNDELQLLSQKFVDNVVSLSKDPNYPSVFAQEISKLTGKNYSGGKEDDITVVVVRVD | Cofactor: Binds 2 magnesium or manganese ions per subunit.
Function: Protein phosphatase which positively regulates biosynthesis of the ubiquinone, coenzyme Q . Dephosphorylates and activates the ubiquinone biosynthesis protein CAT5/COQ7 . Also dephosphorylates CIT1 on 'Ser-462', which leads to its activation .
Catalytic Activity: H2O + O-phospho-L-seryl-[protein] = L-seryl-[protein] + phosphate
Sequence Mass (Da): 37782
Sequence Length: 343
Subcellular Location: Mitochondrion
EC: 3.1.3.16
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P36982 | MGIPLPKPVMTQLQERYGNAIFRCGSNCVNGYRETMEDAHLTYLTDSWGFFGVFDGHVNDQCSQYLERAWRSAIEKESIPMTDERMKELALRIDQEWMDSGREGGSTGTFFVALKEGNKVHLQVGNVGDSRVVACIDGVCVPLTEDHKPNNEGERQRIENCAGRVENNRVDGSLAVSRAFGDREYKLGSGSQLEQKVIALADVQHKDFTFDSNDFVLLCCDGVFEGNFPNEEVVAYVKQQLETCNDLAEVAGRVCEEAIERGSRDNISCMIVQFKDGSDYAAEPHTTVVPGPFSAPRNSGFRKAYESMADKGNTTVGALLERRYDTLKAAEALTPEETEELSQFENGPEAKLTGAERQKWFSNYFQKLCEAASNGPSDQMERLQSLQQQAGIPLSILLSLMGEQTQ | Cofactor: Binds 2 magnesium or manganese ions per subunit.
Function: Enzyme with a broad specificity.
Catalytic Activity: H2O + O-phospho-L-seryl-[protein] = L-seryl-[protein] + phosphate
Sequence Mass (Da): 45139
Sequence Length: 406
EC: 3.1.3.16
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Q9XW79 | MALACTDSANSTFSRVDSPTSGPSDQLTTHDLDRHIEKLMRCELIAEQDVKTLCAKAREILAEEGNVQVIDSPVTICGDIHGQFYDLMELFKVGGPVPNTNYLFLGDFVDRGFYSVETFLLLLALKARYPDRMMLIRGNHESRQITQVYGFYDECLRKYGNASVWKHCTEVFDYLSLAAVIDGKVFCVHGGLSPSISTMDQIRVIDRKQEVPHDGPMCDLLWSDPEEGNVGWGLSPRGAGYLFGADASKTFCETNGVDLICRAHQLVMEGYKWHFNEKVLTVWSAPNYCYRCGNVAAILELDENLNKEFTIFEAAPQENRGAPAKKPHADYFL | Cofactor: Binds 2 manganese ions per subunit.
Function: Protein phosphatase which plays an essential role in meiosis and in early embryonic mitosis . During spermatocyte meiosis and the first embryonic mitosis, regulates centrosome maturation, and thus spindle formation, by recruiting some of the components of the pericentriolar material (PCM) . During oocyte meiosis I, regulates meiotic chromosome dynamics including synapsis-independent chromosome pairing, restriction of synapsis to homologous chromosomes, programmed DNA double-strand break initiation and crossover formation resulting in chiasma formation . During oocyte meiosis II and probably together with regulatory subunit ppfr-1, may regulate microtubule severing by dephosphorylating and activating mei-1, a component of the katanin microtubule severing complex .
PTM: Methylation at the C-terminal Leu-333 is critical for interactions with regulatory subunits.
Catalytic Activity: H2O + O-phospho-L-seryl-[protein] = L-seryl-[protein] + phosphate
Sequence Mass (Da): 37359
Sequence Length: 333
Subcellular Location: Cytoplasm
EC: 3.1.3.16
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P95765 | MSKILVFGHQNPDSDAIGSSYAFAYLAREAYGLDTEAVALGEPNEETAFVLDYFGVAAPRVITSAKAEGAEQVILTDHNEFQQSVADIAEVEVYGVVDHHRVANFETANPLYMRLEPVGSASSIVYRMFKEHSVAVSKEIAGLMLSGLISDTLLLKSPTTHPTDKAIAPELAELAGVNLEEYGLAMLKAGTNLASKSAEELIDIDAKTFELNGNNVRVAQVNTVDIAEVLERQAEIEAAIEKAIADNGYSDFVLMITDIINSNSEILAIGSNMDKVEAAFNFVLENNHAFLAGAVSRKKQVVPQLTESFNA | Cofactor: Binds 2 manganese ions per subunit.
Catalytic Activity: diphosphate + H2O = H(+) + 2 phosphate
Sequence Mass (Da): 33541
Sequence Length: 311
Subcellular Location: Cytoplasm
EC: 3.6.1.1
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Q9HAB8 | MAEMDPVAEFPQPPGAARWAEVMARFAARLGAQGRRVVLVTSGGTKVPLEARPVRFLDNFSSGRRGATSAEAFLAAGYGVLFLYRARSAFPYAHRFPPQTWLSALRPSGPALSGLLSLEAEENALPGFAEALRSYQEAAAAGTFLAVEFTTLADYLHLLQAAAQALNPLGPSAMFYLAAAVSDFYVPVSEMPEHKIQSSGGPLQITMKMVPKLLSPLVKDWAPKAFIISFKLETDPAIVINRARKALEIYQHQVVVANILESRQSFVFIVTKDSETKLLLSEEEIEKGVEIEEKIVDNLQSRHTAFIGDRN | Function: Catalyzes the second step in the biosynthesis of coenzyme A from vitamin B5, where cysteine is conjugated to 4'-phosphopantothenate to form 4-phosphopantothenoylcysteine . Has a preference for ATP over CTP as a cosubstrate .
Catalytic Activity: (R)-4'-phosphopantothenate + ATP + L-cysteine = AMP + diphosphate + H(+) + N-[(R)-4-phosphopantothenoyl]-L-cysteine
Sequence Mass (Da): 34005
Sequence Length: 311
Pathway: Cofactor biosynthesis; coenzyme A biosynthesis; CoA from (R)-pantothenate: step 2/5.
EC: 6.3.2.51
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P40506 | MPPLPVLNRPQIHTSVTEISHAIDRTIKEELFPVAYTTEEEQYFKTNPKPAYIDELIKDAKEFIDLQYSLKRNKIVLITSGGTTVPLENNTVRFIDNFSAGTRGASSAEQFLANGYSVIFLHREFSLTPYNRSFSHSINTLFLDYIDSEGKIKPEFAENVLKNKKLYDKYMEKEEKLLLLPFTTVNQYLWSLKSIAKLLNNSGCLFYLAAAVSDFFVPYSRLPQHKIQSGDNGKMGANNDTEGTTRTTPDGKLIVNLDPVPKFLRRLVESWATQAMIVSFKLETDESMLLYKCTQALDRYNHQLVIGNLLQTRNKQVIFVSPENRKGDWVRLDEKHHSIEEMIIPEVIARHDKWVAHSKTKLATK | Function: Catalyzes the first step in the biosynthesis of coenzyme A from vitamin B5, where cysteine is conjugated to 4'-phosphopantothenate to form 4-phosphopantothenoylcysteine.
Catalytic Activity: (R)-4'-phosphopantothenate + CTP + L-cysteine = CMP + diphosphate + H(+) + N-[(R)-4-phosphopantothenoyl]-L-cysteine
Sequence Mass (Da): 41867
Sequence Length: 365
Pathway: Cofactor biosynthesis; coenzyme A biosynthesis; CoA from (R)-pantothenate: step 2/5.
Subcellular Location: Cytoplasm
EC: 6.3.2.5
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Q0IH22 | MATESILITTLPMDFNSQMNNVTIGLNDNETLCENWREIHHLVFHLANACFAAGLVIPSTLNLHMIFLRGMLCLGCTFFIIWAVLFRCALDIMIWNATFLIINFMHFVYLVYKKRPIKVKNDLKDIYHRMFEPLHVSPELFNRLTGQFCEMKTLAKGQTYAVEDKTSVDDRLSLLLMGIMKVSYRGHFLHTISANAYIDSPEFRSTEMNRGETFQVTITADENCVFLCWSRERLTYFLESEPFLYEIFKYLIGKDITTKLYSLNDPTLGKKKKLDTQPSLCSQLSVMEMRNSLASTSDHEDGLQNFLRGTSTTSSQRHNQQEFYNAYGVGPLSHAVFC | Function: Cell adhesion molecule involved in the establishment and/or maintenance of cell integrity. Plays a role in vamp3-mediated vesicular transport and recycling of different receptor molecules. May be involved in the formation and regulation of the tight junction (TJ) paracellular permeability barrier in epithelial cells. May induce primordial adhesive contact and aggregation of epithelial cells in a Ca(2+)-independent manner. May be involved in epithelial movement during corneal sheet formation and regeneration. May play a role in the regulation of cell shape and movement by modulating the Rho-GTPase activity. May also be involved in striated muscle regeneration and in the regulation of cell spreading (By similarity).
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 38954
Sequence Length: 338
Subcellular Location: Lateral cell membrane
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P33555 | MLLLKASAICGKGNEGKRNKKGGFTLIELTVVLAIMAIILMVIAPNFSYVKDSAKAKVDKQNCAAIERSVEMLLAEDAISSSVTNIKITSSNGNVQISGISDDTGKSKLQDLLEDLDKPQSGDSYNVDIENGRKVTVSIV | Function: Not yet known.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 14931
Sequence Length: 140
Subcellular Location: Membrane
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P33554 | MKTQRGYTLIETLVAMLILVMLSASGLYGWQYWQQSQRLWQTASQARDYLLYLREDANWHNRDHSISVIREGTLWCLVSSAAGANTCHGSSPLVFVPRWPEVEMSDLTPSLAFFGLRNTAWAGHIRFKNSTGEWWLVVSPWGRLRLCQQGETEGCL | Function: Not yet known.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 17865
Sequence Length: 156
Subcellular Location: Membrane
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G5EBX9 | MGCGPSSGRQNPSTELKKSTRATTTTTSSSQRNNYNDNNQNTSSSSGNKKESSSSSKQHSSKKSKKSNSKKNRSPSPQPQLTIKSAILIQKWYRRCEARLEARRRATWQIFTALEYAGEQDQLKLYDFFADVIRAMAEENGKGGVENGRNSPLMSALSHYAKPSLMDSEGETVKKMLEDTSPTNVDIDRNYKGPTLSLPLDKPQVAKMIEAFKVNKVLHPKYVLMILHEARKIFKAMPSVSRISTSISNQVTICGDLHGKFDDLCIILYKNGYPSVDNPYIFNGDFVDRGGQSIEVLCVLFALVIVDPMSIYLNRGNHEDHIMNLRYGFIKELSTKYKDLSTPITRLLEDVFSWLPIATIIDRDIFVVHGGISDQTEVSKLDKIPRHRFQSVLRPPVNKGMESEKENSAVNVDEWKQMLDIMWSDPKQNKGCWPNVFRGGGSYFGADITASFLEKHGFRLLVRSHECKFEGYEFSHNNTCLTVFSASNYYETGSNRGAYVKFIGKSKQPHFVQYMASKTHRKSTLRERLGVVEESAVKELKEKLSSFHTDLQKEFEIMDIEKSGKLPILKWSDCVERITGLNLPWIALAPKVATLSEDGKYVMYKEDRRIAQVGGTHAQEKDIVESLYRHKSTLETLFRFMDKDNSGQVSMKEFIDACEVLGKYTKRPLQTDYISQIAESIDFNKDGFIDLNELLEAFRLVDRPLLR | Cofactor: Binds 2 manganese ions per subunit.
Function: Probably acts as a protein phosphatase.
Catalytic Activity: H2O + O-phospho-L-seryl-[protein] = L-seryl-[protein] + phosphate
Location Topology: Lipid-anchor
Sequence Mass (Da): 80330
Sequence Length: 707
Subcellular Location: Cell membrane
EC: 3.1.3.16
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Q9FY06 | MAKTLISSPSFLGTPLPSLHRTFSPNRTRLFTKVQFSFHQLPPIQSVSHSVDLSGIFARAEGLLYTLADATVAADAAASTDVAAQKNGGWFGFISDGMEFVLKVLKDGLSSVHVPYSYGFAIILLTVIVKAATLPLTKQQVESTLAMQNLQPKIKAIQERYAGNQERIQLETSRLYTQAGVNPLAGCLPTLATIPVWIGLYQALSNVANEGLLTEGFLWIPSLGGPTSIAARQSGSGISWLFPFVDGHPLLGWYDTAAYLVLPVLLIVSQYVSMEIMKPPQTNDPNQKNTLLIFKFLPLMIGYFSLSVPSGLTIYWFTNNVLSTAQQVWLRKLGGAKPAVNENAGGIITAGQAKRSASKPEKGGERFRQLKEEEKKKKLIKALPVEEVQPLASASASNDGSDVENNKEQEVTEESNTSKVSQEVQSFSRERRSKRSKRKPVA | Function: May be required for the insertion of some integral membrane proteins into the chloroplast thylakoid membrane. May play a role in inhibiting senescence.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 48238
Sequence Length: 442
Subcellular Location: Plastid
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Q5A6B6 | MTVPFKIPISDLDYCLEQLLDHKPPKILPPETIQQLCHTLKTELLQTPNIISLQSPISVVGDIHGQYHDLLEIFQIGGSPPQTNYLFLGDYVDRGYYSVETISLLLVLKLRYPERVFLIRGNHESRTITTNYGFYTEVLNKYQGSADVWTFITDLFDYLPLGATIDGKIFACHGGLSPSCQQLDQIRAVDRFREIPHDGIMADLVWSDPDVAISDFKLSPRGAGYLFGNDVIDKFCQDNNLVQMIRAHQLCNEGYTSYWKGKCLTVWSAPNYCYRCGNKASVLEILHSNYDSKDPTNGSDGEISSINGEFIGVNTSFESFGDDDDDYNDYRNRFNNSSRLHKQQGVLPGQFFNVFEASKENDEDTLQGKSVNGINFDDELSTSDDTSGSGGNNNKGDFFAAFFQERPKRQQVEYFL | Cofactor: Binds 2 manganese ions per subunit.
Function: Serine/threonine-protein phosphatase that plays an important role in controlling colony morphology, filament extension and agar invasion. Down-regulates expression of NRG1 and affects the expression of multiple filament-specific transcripts in response to serum and 37 degrees Celsius. Plays a crucial role in virulence in a mouse model of systemic candidiasis.
Catalytic Activity: H2O + O-phospho-L-seryl-[protein] = L-seryl-[protein] + phosphate
Sequence Mass (Da): 47040
Sequence Length: 416
EC: 3.1.3.16
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P10619 | MIRAAPPPLFLLLLLLLLLVSWASRGEAAPDQDEIQRLPGLAKQPSFRQYSGYLKGSGSKHLHYWFVESQKDPENSPVVLWLNGGPGCSSLDGLLTEHGPFLVQPDGVTLEYNPYSWNLIANVLYLESPAGVGFSYSDDKFYATNDTEVAQSNFEALQDFFRLFPEYKNNKLFLTGESYAGIYIPTLAVLVMQDPSMNLQGLAVGNGLSSYEQNDNSLVYFAYYHGLLGNRLWSSLQTHCCSQNKCNFYDNKDLECVTNLQEVARIVGNSGLNIYNLYAPCAGGVPSHFRYEKDTVVVQDLGNIFTRLPLKRMWHQALLRSGDKVRMDPPCTNTTAASTYLNNPYVRKALNIPEQLPQWDMCNFLVNLQYRRLYRSMNSQYLKLLSSQKYQILLYNGDVDMACNFMGDEWFVDSLNQKMEVQRRPWLVKYGDSGEQIAGFVKEFSHIAFLTIKGAGHMVPTDKPLAAFTMFSRFLNKQPY | Function: Protective protein appears to be essential for both the activity of beta-galactosidase and neuraminidase, it associates with these enzymes and exerts a protective function necessary for their stability and activity. This protein is also a carboxypeptidase and can deamidate tachykinins.
Catalytic Activity: Release of a C-terminal amino acid with broad specificity.
Sequence Mass (Da): 54466
Sequence Length: 480
Subcellular Location: Lysosome
EC: 3.4.16.5
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P16675 | MPGTALSPLLLLLLLSWASRNEAAPDQDEIDCLPGLAKQPSFRQYSGYLRASDSKHFHYWFVESQNDPKNSPVVLWLNGGPGCSSLDGLLTEHGPFLIQPDGVTLEYNPYAWNLIANVLYIESPAGVGFSYSDDKMYVTNDTEVAENNYEALKDFFRLFPEYKDNKLFLTGESYAGIYIPTLAVLVMQDPSMNLQGLAVGNGLASYEQNDNSLVYFAYYHGLLGNRLWTSLQTHCCAQNKCNFYDNKDPECVNNLLEVSRIVGKSGLNIYNLYAPCAGGVPGRHRYEDTLVVQDFGNIFTRLPLKRRFPEALMRSGDKVRLDPPCTNTTAPSNYLNNPYVRKALHIPESLPRWDMCNFLVNLQYRRLYQSMNSQYLKLLSSQKYQILLYNGDVDMACNFMGDEWFVDSLNQKMEVQRRPWLVDYGESGEQVAGFVKECSHITFLTIKGAGHMVPTDKPRAAFTMFSRFLNKEPY | Function: Protective protein appears to be essential for both the activity of beta-galactosidase and neuraminidase, it associates with these enzymes and exerts a protective function necessary for their stability and activity. This protein is also a carboxypeptidase and can deamidate tachykinins.
Catalytic Activity: Release of a C-terminal amino acid with broad specificity.
Sequence Mass (Da): 53844
Sequence Length: 474
Subcellular Location: Lysosome
EC: 3.4.16.5
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A5U654 | MTSTGPETSETPGATTQRHGFGIDVGGSGIKGGIVDLDTGQLIGDRIKLLTPQPATPLAVAKTIAEVVNGFGWRGPLGVTYPGVVTHGVVRTAANVDKSWIGTNARDTIGAELGGQQVTILNDADAAGLAETRYGAGKNNPGLVVLLTFGTGIGSAVIHNGTLIPNTEFGHLEVGGKEAEERAASSVKEKNDWTYPKWAKQVIRVLIAIENAIWPDLFIAGGGISRKADKWVPLLENRTPVVPAALQNTAGIVGAAMASVADTTH | Function: Catalyzes the phosphorylation of glucose using polyphosphate or ATP as the phosphoryl donor . Polyphosphate, rather than ATP, seems to be the major phosphate donor for the enzyme in M.tuberculosis . GTP, UTP and CTP can replace ATP as phosphoryl donor .
Catalytic Activity: [phosphate](n) + D-glucose = [phosphate](n-1) + D-glucose 6-phosphate + H(+)
Sequence Mass (Da): 27429
Sequence Length: 265
EC: 2.7.1.63
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Q84G06 | MTKNQALRAALDSGRLFTAMAAHNPLVAKLAEQAGFGGIWGSGFELSASYAVPDANILSMSTHLEMMRAIASTVSIPLIADIDTGFGNAVNVHYVVPQYEAAGASAIVMEDKTFPKDTSLRTDGRQELVRIEEFQGKIAAATAARADRDFVVIARVEALIAGLGQQEAVRRGQAYEEAGADAILIHSRQKTPDEILAFVKSWPGKVPLVLVPTAYPQLTEADIAALSKVGIVIYGNHAIRAAVGAVREVFARIRRDGGIREVDAALPSVKEIIELQGDERMRAVEARYLK | Cofactor: Divalent metal cations. Co(2+), Mg(2+) or Mn(2+) can be used.
Function: Hydrolyzes phosphonopyruvate. Not active towards phosphoenolpyruvate, glycerophosphate, phospho-L-serine or phosphoglycolic acid.
Catalytic Activity: 3-phosphonopyruvate + H2O = H(+) + phosphate + pyruvate
Sequence Mass (Da): 31179
Sequence Length: 290
EC: 3.11.1.3
|
Q8NEY8 | MWSEGRYEYERIPRERAPPRSHPSDGYNRLVNIVPKKPPLLDRPGEGSYNRYYSHVDYRDYDEGRSFSHDRRSGPPHRGDESGYRWTRDDHSASRQPEYRDMRDGFRRKSFYSSHYARERSPYKRDNTFFRESPVGRKDSPHSRSGSSVSSRSYSPERSKSYSFHQSQHRKSVRPGASYKRQNEGNPERDKERPVQSLKTSRDTSPSSGSAVSSSKVLDKPSRLTEKELAEAASKWAAEKLEKSDESNLPEISEYEAGSTAPLFTDQPEEPESNTTHGIELFEDSQLTTRSKAIASKTKEIEQVYRQDCETFGMVVKMLIEKDPSLEKSIQFALRQNLHEIESAGQTWQQVPPVRNTEMDHDGTPENEGEETAQSAPQPPQAPQPLQPRKKRVRRTTQLRRTTGAPDITWGMLKKTTQEAERILLRTQTPFTPENLFLAMLSVVHCNSRKDVKPENKQ | Function: Component of the HUSH complex, a multiprotein complex that mediates epigenetic repression. The HUSH complex is recruited to genomic loci rich in H3K9me3 and is probably required to maintain transcriptional silencing by promoting recruitment of SETDB1, a histone methyltransferase that mediates further deposition of H3K9me3. In the HUSH complex, contributes to the maintenance of the complex at chromatin . Acts as a transcriptional corepressor and regulates the cell cycle, probably via the HUSH complex . The HUSH complex is also involved in the silencing of unintegrated retroviral DNA: some part of the retroviral DNA formed immediately after infection remains unintegrated in the host genome and is transcriptionally repressed . May be involved in epithelial differentiation by contributing to epidermal integrity and barrier formation .
PTM: Substrate of transglutaminase (in vitro).
Sequence Mass (Da): 52737
Sequence Length: 458
Subcellular Location: Nucleus
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Q9FFZ1 | MEIISLNVVPQCSVVTWSSKLATKRLVPNRSSLLFSGVKKSRLVIRSGNSDGYVVGENDDLGRIARRGESTSKVLIPGLPDESNGEIAARISHSHCEWKPKLRVHYEKAGCDNLDAPAVLFLPGFGVGSFHYEKQLTDLGRDYRVWAIDFLGQGLSLPTEDPTTMTEETSSSEDKEPFWGFGDKTEPWADQLVFSLDLWRDQVQYFVEEVIGEPVYIAGNSLGGYVALYFAATHPHLVKGVTLLNATPFWGFFPNPVRSPKLARLFPWPGAFPLPERVKKITELVWQKISDPESIAEILKQVYTDHSINVDKVFSRIVEVTQHPAAAASFASIMLAPGGELSFSEALSRCKENNVQICLMYGREDPWVRPLWGKKIKKEIPNAPYYEISPAGHCPHDEVPEVVNYLMRGWIKHLESGGFEALPLLEDTEEDWEESRIGREIEFPRDGWKKAVNLWLYGSNYTYWRGVRESFRSSFIRVFGGKSA | Function: Alpha/beta hydrolase dephytylating specifically the Mg-free chlorophyll pigment (pheophytin), yielding pheophorbide. No activity on chlorophyll. Belongs to the chlorophyll catabolic enzymes (CCEs).
Sequence Mass (Da): 54572
Sequence Length: 484
Subcellular Location: Plastid
EC: 3.1.1.-
|
O23144 | MGVEVVNSGGFEVAPAPFEGKPEKNGKLDQGKGDDAPINFGSVGELPKNAEENNNKVVNSDAPKNAAEEWPVAKQIHSFYLVKYRSYADPKIKAKLDLADKELEKLNKARTGVLDKLRAKRAERSELFDLLDPLKSERKGFNTMFDEKRKEMEPLQQALGKLRSNDGGSARGPAICSSEEELNSMIYSYQYRIQHESIPLTEEKQILKEIRLLEGTRDKVIANAAMRAKIKESMGQKDDIQGQVKLMGAGLDGVKKERQAISARINELSEKLKATKDEITVLENELKTVSEKRDKAYSNIHDLRRQRDETNSEYYQNRTVLNKARDLAAQKNISELEALANAEVEKFISLWCSKKNFREDYEKRILQSLDSRQLSRDGRMRNPDEKPLIAPEAAPSKATPSETEVVPKAKAKPQPKEEPVSAPKPDATVAQNTEKAKDAVKVKNVADDDDDEVYGLGKPQKEEKPVDAATAKEMRKQEEIAKAKQAMERKKKLAEKAAAKAAIRAQKEAEKKEKKEQEKKAKKKTGGNTETETEEVPEASEEEIEAPVQEEKPQKEKVFKEKPIRNRTRGRGPETIPRAILKRKKSTNYWVYAAPAALVVLLLLVLGYYYVL | Function: Promotes AHA1 plasma membrane ATPase activity by binding to a site different from the 14-3-3 binding site.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 68879
Sequence Length: 612
Subcellular Location: Cell membrane
|
Q9JXS9 | MPEQNRILCRELSLLAFNRRVLAQAEDQNVPLLERLRFLCIVSSNLDEFFEVRMAWLKREHKRCPQRRLDNGKMPSETIADVTEAARSLIRHQYDLFNNVLQPELAQEGIHFYRRRNWTDTQKKWIEDYFDRELLPILTPIGLDPSHPFPRPLNKSLNFAVELDGTDAFGRPSGMAIVQAPRILPRVVPLPSELCGGGHGFVFLSSILHAHVGKLFPGMNVKGCHQFRLTRDSDLTVDEEDLQNLRAAIQNELHDREYGDGVRLEVADTCPAYIRDFLLAQFKLTAAELYQVKGPVNLVRLNAVPDLVNRPDLKFPTHTPGRLKALGKTASIFDLVRQSPILLHHPYQSFDPVVEMMREAAADPAVLAVKMTIYRTGTRSELVRALMKAALAGKQVTVVVELMARFDEANNVNWAKQLEEAGAHVVYGVFGYKVHAKMALVIRREDGVLKRYAHLGTGNYHQGTSRIYTDFGLITADEQITADVNILFMEITGLGKPGRLNKLYQSPFTLHKMVIDRIARETEHAKAGKPARITAKMNSLIEPTVIEALYRASAAGVQIDLIVRGMCTLRPGVKGLSENIRVRSIVGRQLEHARVYYFHNNGTDDTFISSADWMGRNFFRRIETATPITAPELKKRVIHEGLTMALDDNTHAWLMQPDGGYIRAAPAEGESEADLQNDLWTLLGG | Function: Catalyzes the reversible transfer of the terminal phosphate of ATP to form a long-chain polyphosphate (polyP).
PTM: An intermediate of this reaction is the autophosphorylated ppk in which a phosphate is covalently linked to a histidine residue through a N-P bond.
Catalytic Activity: [phosphate](n) + ATP = [phosphate](n+1) + ADP
Sequence Mass (Da): 77258
Sequence Length: 685
EC: 2.7.4.1
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Q3SS86 | MDSIQAIAPEEKKPELELDSAIRASPERFINRELSWLHFNRRVLEESVNPGHPALERVRFLSISANNLDEFFMVRVAGIKAQVREGITERSPDGLTPSEQLVLINETVSDLASDQQAIWRDLRNMLAGVGIVLIDGKDVTKAERSWIADHFLHNIFPLLTPLAIDPAHPFPFIPSLGFTIALQLARTSDGKPMNALIRMPGKIDRFLRIPAASKDDPVRLITIEGATSLFINRLFPGYTVKGQGAFRIIRDSELEIEEEAEDLVRLFETALKRRRRGSVIRLEIEAAMPAELRAFVQRALSAADDEVLLVDGVLAMNELSQLTRLDRPDLEFVPYVPRHPERVRDHGGDVFAAIRQKDLIVHHPYESFDVVVQFLQQAARDPDVVAIKQTLYRTSNNSPIVRALAEAAEAGKSVTALIELKARFDEEANIRWARDLERAGVQVVYGFLELKTHAKLSLVVRREGGSLATYVHTGTGNYHPVTARIYTDLSYFTSDPIIGRDAARVFNYITGYAEPSDIERMAVSPLTLRNRILDHIRGETTFARNGKPAAVWMKMNALVDPDIIDALYEASQAGVSVELIVRGICCLRPGVPGLSENIRVKSVIGRFLEHGRIYCFGMGQTMPGPKAAVYISSADMMPRNLDRRVEVLCPLQNATVHQQVLEQIMVANLKDTEQSWRLLPDGSSTRMKAAKGEEPFNLHNYFMTNPSLSGRGKSLKESSPRRLTRRSERQPPA | Function: Catalyzes the reversible transfer of the terminal phosphate of ATP to form a long-chain polyphosphate (polyP).
PTM: An intermediate of this reaction is the autophosphorylated ppk in which a phosphate is covalently linked to a histidine residue through a N-P bond.
Catalytic Activity: [phosphate](n) + ATP = [phosphate](n+1) + ADP
Sequence Mass (Da): 82103
Sequence Length: 733
EC: 2.7.4.1
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B2SZQ7 | MSIRYPLLNRELGILGFNERVLAQAADPAVPLLERLRFICITSSNLDEFFEVRMAGLQEQMRDNPGALSPDGMSLQHVYDLVVERAQKLVHRQYTMLHDTVLTALEAEGIYFHGTEAWNEAQTEWARNYFFDELLPVLTPIGLDPAHPFPRVLNKSLNFVVELEGKDAFGRQAMMGIVQAPRALPRLVRMPQELSGYPHGFVLLSSLLQRFVGELFPNLVVRSCNQFRITRNSELFVDEDEITNLRVALQGELPARHLGNAVRLEVSAETPTHVVRRLLDESGLSDKDCYYADGPVNLVRLMQLPEMVDRPDLKFVPHIPAIPAQVANSVSMFDVIDQGDVLLHHPYESFQPVLELLLQAAKDPNVVAIKQTIYRTGTDSPLMDALMQAARNGKEVTVVVELLARFDEETNINWASQLEAVGAHVVYGVVGHKCHAKMMLIVRRVSVGGKTTLKRYVHLGTGNYHPRTARLYTDFGLMTADQKICEDVHHVFQQLTGIGGELKLHELWQSPFTLHPKLVEAIRAEAEHARAGKKARIVAKMNALLEPTVIAELYEAAQAGVKIDLIVRGVCSLQPGVAGLSENITVRSIVGRFLEHHRIFYFYDGGKEQVYLSSADWMDRNFFRRVEVAFPINNRRLKRRVIAEGLSAFLGDNQSAWLMQSDGHYRRRRPGKSSRNAQMSLLGKFCS | Function: Catalyzes the reversible transfer of the terminal phosphate of ATP to form a long-chain polyphosphate (polyP).
PTM: An intermediate of this reaction is the autophosphorylated ppk in which a phosphate is covalently linked to a histidine residue through a N-P bond.
Catalytic Activity: [phosphate](n) + ATP = [phosphate](n+1) + ADP
Sequence Mass (Da): 77420
Sequence Length: 687
EC: 2.7.4.1
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Q7V3U5 | MSNPAVASEHYINRELSWISFNERVLAQALDTRTPLLEQAKFSAIFSNNLDEFFMVRVASLKAQVEAGITKTSADGLTPLQQLLTIRDHLVPLIEQQQDHYRKHLKNQLVEHGVHLLDYEQLNPKERLWIDNYFQTAIFPVLTPLAVDQAHPFPFVSNLSLNIATLILDPETGQQQFARVKIPQKTIPRFVEIPPDLSGINPKPVHTAVPLEQVVAFNLKLLFPGMKIEEHYFFRVTRDADLELRDLEADDLMSAMEQGLHKRRMGGEVVRLEVTNEMPQRVVEMLIEGMAVEEKDLYRIEGLLGLDDLFGLMRLPLEQLKDQPHIGLTAKVLSRSQRRMLEDESIKEEEFKSIFSVIRRKDILLHHPYELFATSVEEFINQAADDPLVMGIKITLYRTSKDSPIIAALIRAAEHGKQVMALVELKARFDEGNNIQWARHLERSGVHVVYGVLGLKTHTKTILVVRKEKERLRSYVHIGTGNYNSKTSRLYTDLGLLSARPELSQDLVELFNYLTGFSKQQSFRRLLVAPVTLRKGMESLILREIEHAREGRGGHIRAKMNALVDPAIISLLYEASQVGVRIELIIRGMCCLYPGRKGFSENISVISIIGRFLEHSRIFWFANDNNPEVYIGSADLMPRNLDRRVEAITPIEEPEQKEHLERLLNLYLNDNREAWDMQSDGSFLQRQPNPNSEEHRAQQQLINLWQQGIPAA | Function: Catalyzes the reversible transfer of the terminal phosphate of ATP to form a long-chain polyphosphate (polyP).
PTM: An intermediate of this reaction is the autophosphorylated ppk in which a phosphate is covalently linked to a histidine residue through a N-P bond.
Catalytic Activity: [phosphate](n) + ATP = [phosphate](n+1) + ADP
Sequence Mass (Da): 81569
Sequence Length: 712
EC: 2.7.4.1
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P0DP44 | MDDSSLYIHRELSQLQFNIRVLEQALDESYPLLERLKFLLIFSSNLDEFFEIRIAGLKKQITFAREQAGADGLLPHQALARISELVHEQVSRQYRILNETLLPELAKHQIRFIRRRHWTLKIKTWVRRFFRDEIAPIITPIGLDPTHPFPLLVNKSLNFIVELEGMDAFGRDSGLAIIPAPRLLPRIIRLPEDVGGEGDNYVFLSSMIHAHADDLFPGMKVKGCYQFRLTRNADLSVDTEDVEDLARALRGELFSRRYGDAVRLEVVDTCPQNLTNYLLKQFGLSESELYKVSGPVNLTRLFSVTGLESHPELQYPPFTPAIPRLLQKKENLFNVLSKLDVLLMHPFESFTPVIDLLRQAAKDPNVLAIKQTLYRSGANSEIVDALVEAARNGKEVTAVIELRARFDEESNLQLASRLQQAGAVVIYGVVGFKTHAKMMLILRREDGELRRYAHLGTGNYHAGNARLYTDYSLLTADVALCEDLHKLFNQLIGMGKTLRMKKLLHAPFTLKKNLLEMINREAAQAALGQPAHIMAKVNSLTDPKVIRALYKASQAGVRIDLVVRGMCCLRPGIPGVSHNIHVRSIIGRFLEHSRIYYFLNGGDEKLYLSSADWMERNLDMRVETCFPVEGKKLVQRVKKELETYLTDNTQAWVLQADGSYQRLSPTGNQNPRNTQATLLEKLAAPVLTAR | Function: Catalyzes the reversible transfer of the terminal phosphate of ATP to form a long-chain polyphosphate (polyP).
PTM: An intermediate of this reaction is the autophosphorylated ppk in which a phosphate is covalently linked to a histidine residue through a N-P bond.
Catalytic Activity: [phosphate](n) + ATP = [phosphate](n+1) + ADP
Sequence Mass (Da): 78293
Sequence Length: 690
EC: 2.7.4.1
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Q05AL2 | MMTRVRSAVSSIIGGIMASGTGAHDSHPDLPLRFPYSRPDFLALSPDEVECSADHISRPILILKEMKLPWATGYAEVINAGKSALNEDQACCEVVELRKRPADPSSVSYTPSRRRSSLPSGDVLDTIHNPEVKELDFHYWALFDGHGGSGAAVFAAKFLHLHIEEQLQEVLEILQDPGLQPPTCLGEESPNPQLHASASGSQRGLSRAASLRGAAGAPGSPNTMAPRFFMEKKIKQESLVVGAIENAFKEMDAHIARERCAYSISGGCTALAVMFLLGKLYVANAGDSRALIVRAGELITMSSSFTPESERQRLQFLAHLQPSLLGSDFTHLEFPRRVTKREIGKRMLYRDFTMNGWAYKTVQEEDLKFPLIYGEGKKARVLATIGITRGLGDHDLKVHDSDIAIKPFLSCSPEVQVYNLCQFEHGADDVLILATDGLWDVLSNQEVADAVSGFLGNCDPDDQHRYTMAAQDLVMKARGILKDRGWRIAGDRLGSGDDISVFIIPLMYGTQQPQPS | Catalytic Activity: H2O + O-phospho-L-seryl-[protein] = L-seryl-[protein] + phosphate
Sequence Mass (Da): 56561
Sequence Length: 516
Subcellular Location: Nucleus
EC: 3.1.3.16
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Q9ULR3 | MLTRVKSAVANFMGGIMAGSSGSEHGGGSCGGSDLPLRFPYGRPEFLGLSQDEVECSADHIARPILILKETRRLPWATGYAEVINAGKSTHNEDQASCEVLTVKKKAGAVTSTPNRNSSKRRSSLPNGEGLQLKENSESEGVSCHYWSLFDGHAGSGAAVVASRLLQHHITEQLQDIVDILKNSAVLPPTCLGEEPENTPANSRTLTRAASLRGGVGAPGSPSTPPTRFFTEKKIPHECLVIGALESAFKEMDLQIERERSSYNISGGCTALIVICLLGKLYVANAGDSRAIIIRNGEIIPMSSEFTPETERQRLQYLAFMQPHLLGNEFTHLEFPRRVQRKELGKKMLYRDFNMTGWAYKTIEDEDLKFPLIYGEGKKARVMATIGVTRGLGDHDLKVHDSNIYIKPFLSSAPEVRIYDLSKYDHGSDDVLILATDGLWDVLSNEEVAEAITQFLPNCDPDDPHRYTLAAQDLVMRARGVLKDRGWRISNDRLGSGDDISVYVIPLIHGNKLS | Function: Dephosphorylates CDKN1B at 'Thr-187', thus removing a signal for proteasomal degradation.
Catalytic Activity: H2O + O-phospho-L-seryl-[protein] = L-seryl-[protein] + phosphate
Sequence Mass (Da): 56448
Sequence Length: 514
Subcellular Location: Nucleus
EC: 3.1.3.16
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Q3UYC0 | MLTRVKSAVANFMGGIMAGSSGSEHGGSGCGGSDLPLRFPYGRPEFLGLSQDEVECSADHIARPILILKETRRLPWATGYAEVINAGKSTHNEDQASCEVLTVKKKAGTITSTPNRNSKRRSSLPNGEGLQLKENSESEGISCHYWSLFDGHAGSGAAVVASRLLQHHITQQLQDIVEILKNSAILPPTCLGEEPESTPAHGRTLTRAASLRGGVGAPGSPSTPPTRFFTEKKIPHECLVIGALESAFKEMDLQIERERSAYNISGGCTALIVVCLLGKLYVANAGDSRAIIIRNGEIIPMSSEFTPETERQRLQYLAFMQPHLLGNEFTHLEFPRRVQRKELGKKMLYRDFNMTGWAYKTIEDDDLKFPLIYGEGKKARVMATIGVTRGLGDHDLKVHDSNIYIKPFLSSAPEVRVYDLSRYEHGADDVLILATDGLWDVLSNEEVAEAITQFLPNCDPDDPHRYTLAAQDLVMRARGVLKDRGWRISNDRLGSGDDISVYVIPLIHGNKLS | Function: Dephosphorylates CDKN1B at 'Thr-187', thus removing a signal for proteasomal degradation.
Catalytic Activity: H2O + O-phospho-L-seryl-[protein] = L-seryl-[protein] + phosphate
Sequence Mass (Da): 56380
Sequence Length: 513
Subcellular Location: Nucleus
EC: 3.1.3.16
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Q2PC20 | MSTAALLTLVRSGGNQVRRRVLLRARGLQDDRWVMPTCHSSTSEPKWSRFDPDGSGRPATWDNFGIWDNRLEEPILLPPSIKYGKPIPKVSLQNVGSASQIGKRKENEDRFGFAQLTNEVLYFAVYDGHGGPAAADFCHTHMEKCILDLLPKEENLETVLTLAFLEIDKTFARHAHLSADATLLTSGTTATVALLRDGIELVIASVGDSRAILCRKGKPMKLTIDHTPERKDEKERIKKCGGFVAWNSLGQPHVNGRLAMTRSLGDLDLKTSGVIAEPETKRIKLHHADDSFLVLTTDGINFMVNSQEICDFVNQCHDPNEAAHAVTEQAIQYGTEDNTTAVVVPFGAWGKYKNSEITFSFSRSFASSGRWA | Cofactor: Binds 1 Mg(2+) or Mn(2+) ion per subunit.
Function: Regulates the mitochondrial permeability transition pore and is essential for cellular survival and development.
Catalytic Activity: H2O + O-phospho-L-seryl-[protein] = L-seryl-[protein] + phosphate
Sequence Mass (Da): 41151
Sequence Length: 372
Subcellular Location: Mitochondrion matrix
EC: 3.1.3.16
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Q8N3J5 | MSTAALITLVRSGGNQVRRRVLLSSRLLQDDRRVTPTCHSSTSEPRCSRFDPDGSGSPATWDNFGIWDNRIDEPILLPPSIKYGKPIPKISLENVGCASQIGKRKENEDRFDFAQLTDEVLYFAVYDGHGGPAAADFCHTHMEKCIMDLLPKEKNLETLLTLAFLEIDKAFSSHARLSADATLLTSGTTATVALLRDGIELVVASVGDSRAILCRKGKPMKLTIDHTPERKDEKERIKKCGGFVAWNSLGQPHVNGRLAMTRSIGDLDLKTSGVIAEPETKRIKLHHADDSFLVLTTDGINFMVNSQEICDFVNQCHDPNEAAHAVTEQAIQYGTEDNSTAVVVPFGAWGKYKNSEINFSFSRSFASSGRWA | Cofactor: Binds 1 Mg(2+) or Mn(2+) ion per subunit.
Function: Regulates the mitochondrial permeability transition pore and is essential for cellular survival and development.
Catalytic Activity: H2O + O-phospho-L-seryl-[protein] = L-seryl-[protein] + phosphate
Sequence Mass (Da): 40997
Sequence Length: 372
Subcellular Location: Mitochondrion matrix
EC: 3.1.3.16
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Q5R522 | MSTAALITLVRSGGNQVRRRVLLSSRLLQDDRRATPTCHSSTSEPRCSRFDPDGSGSPATWDNFGIWDNRIDEPILLPPSIKYGKPIPKISLENVGCASQIGKRKENEDRFDFAQLTDEVLYFAVYDGHGGPAAADFCHTHMEKCIMDLLPKEKNLETLLTLAFLEIDKAFSSHARLSADATLLTSGTTATVALLRDGIELVVASVGDSRAILCRKGKPMKLTIDHTPERKDEKERIKKCGGFVAWNSLGQPHVNGRLAMTRSIGDLDLKTSGVIAEPETKRIKAIQYGTEDNSTAVVVPFGAWGKYKNSEINFSFSRSFASSGRWA | Cofactor: Binds 1 Mg(2+) or Mn(2+) ion per subunit.
Function: Regulates the mitochondrial permeability transition pore and is essential for cellular survival and development.
Catalytic Activity: H2O + O-phospho-L-seryl-[protein] = L-seryl-[protein] + phosphate
Sequence Mass (Da): 35960
Sequence Length: 327
Subcellular Location: Mitochondrion matrix
EC: 3.1.3.16
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Q8BHN0 | MIEDTMTLLSLLGRIMRYFLLRPETLFLLCISLALWSYFFHTDEVKTIVKSSRDAVKMVKGKVAEIMQNDRLGGLDVLEAEFSKTWEFKSHNVAVYSIQGRRDHMEDRFEVLTDLANKTHPSIFGIFDGHGGETAAEYVKSRLPEALKQHLQDYEKDKENSVLTYQTILEQQILSIDREMLEKLTVSYDEAGTTCLIALLSDKDLTVANVGDSRGVLCDKDGNAIPLSHDHKPYQLKERKRIKRAGGFISFNGSWRVQGILAMSRSLGDYPLKNLNVVIPDPDILTFDLDKLQPEFMILASDGLWDAFSNEEAVRFIKERLDEPHFGAKSIVLQSFYRGCPDNITVMVVKFRNSSKTEEH | Cofactor: Binds 2 magnesium or manganese ions per subunit.
Function: Acts as a suppressor of the SAPK signaling pathways by associating with and dephosphorylating MAP3K7/TAK1 and MAP3K5, and by attenuating the association between MAP3K7/TAK1 and MAP2K4 or MAP2K6.
Catalytic Activity: H2O + O-phospho-L-seryl-[protein] = L-seryl-[protein] + phosphate
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 41049
Sequence Length: 360
Subcellular Location: Membrane
EC: 3.1.3.16
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Q96MI6 | MSAGWFRRRFLPGEPLPAPRPPGPHASPVPYRRPRFLRGSSSSPGAADASRRPDSRPVRSPARGRTLPWNAGYAEIINAEKSEFNEDQAACGKLCIRRCEFGAEEEWLTLCPEEFLTGHYWALFDGHGGPAAAILAANTLHSCLRRQLEAVVEGLVATQPPMHLNGRCICPSDPQFVEEKGIRAEDLVIGALESAFQECDEVIGRELEASGQMGGCTALVAVSLQGKLYMANAGDSRAILVRRDEIRPLSFEFTPETERQRIQQLAFVYPELLAGEFTRLEFPRRLKGDDLGQKVLFRDHHMSGWSYKRVEKSDLKYPLIHGQGRQARLLGTLAVSRGLGDHQLRVLDTNIQLKPFLLSVPQVTVLDVDQLELQEDDVVVMATDGLWDVLSNEQVAWLVRSFLPGNQEDPHRFSKLAQMLIHSTQGKEDSLTEEGQVSYDDVSVFVIPLHSQGQESSDH | Cofactor: Binds 2 magnesium or manganese ions per subunit.
Catalytic Activity: H2O + O-phospho-L-seryl-[protein] = L-seryl-[protein] + phosphate
Sequence Mass (Da): 51136
Sequence Length: 459
Subcellular Location: Nucleus
EC: 3.1.3.16
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Q8BU27 | MSAGWFRRRFLPGGPLPEPRPAGPRSSPVPYHRPRFLRGSGSSPGATDASRRPDARPVRSPARGRTLPWNAGYAEVINAEKSEFNEDQAACGKLCIRRCEFGIEEDQEWLTVCPEEFLTGHYWALFDGHGGPAAAILAANTLHSCLRRQLEAVVEGMIAPQPPMHLSGRCVCPSDPQFVEEKGIQAEDLVIGALENAFQECDDVIGRELEASGQVGGCTALVAVFLQGKLYVANAGDSRAILVRRHEIRQLSSEFTPETERQRIQQLAFTYPELLAGEFTRLEFPRRLKGDDLGQKVLFRDHHMRGWSYKRVEKSDLKYPLIHGQGRQARLLGTLAVSRGLGDHQLRVLDTDIQLKPFLLSIPQVTVLDVHQLAVQEEDVVVMATDGLWDVLSNEQVALLVRSFLTGNQKDDPHRFSELAKMLIHNTQGKDNGATGEGQVSYDDVSVFVIPLHSQAQEGSGH | Cofactor: Binds 2 magnesium or manganese ions per subunit.
Catalytic Activity: H2O + O-phospho-L-seryl-[protein] = L-seryl-[protein] + phosphate
Sequence Mass (Da): 51204
Sequence Length: 462
Subcellular Location: Nucleus
EC: 3.1.3.16
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Q8N819 | MAVLARQLQRLLWTACKKKEREKEGREEEEEEEAGRRAPEGPRSLLTAPRRAQRPHGGAEASGGLRFGASAAQGWRARMEDAHCTWLSLPGLPPGWALFAVLDGHGGARAARFGARHLPGHVLQELGPEPSEPEGVREALRRAFLSADERLRSLWPRVETGGCTAVVLLVSPRFLYLAHCGDSRAVLSRAGAVAFSTEDHRPLRPRERERIHAAGGTIRRRRVEGSLAVSRALGDFTYKEAPGRPPELQLVSAEPEVAALARQAEDEFMLLASDGVWDTVSGAALAGLVASRLRLGLAPELLCAQLLDTCLCKGSLDNMTCILVCFPGAPRPSEEAIRRELALDAALGCRIAELCASAQKPPSLNTVFRTLASEDIPDLPPGGGLDCKATVIAEVYSQICQVSEECGEKGQDGAGKSNPTHLGSALDMEA | Cofactor: Binds 2 magnesium or manganese ions per subunit.
Catalytic Activity: H2O + O-phospho-L-seryl-[protein] = L-seryl-[protein] + phosphate
Sequence Mass (Da): 46170
Sequence Length: 430
EC: 3.1.3.16
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Q9SY69 | MSLSHLLRRLCTTTTTTRSPLSISFLHQRIHNISLSPANEDPETTTGNNQDSEKYPNLNPIPNDPSQFQIPQNHTPPIPYPPIPHRTMAFSSAEEAAAERRRRKRRLRIEPPLHALRRDPSAPPPKRDPNAPRLPDSTSALVGQRLNLHNRVQSLIRASDLDAASKLARQSVFSNTRPTVFTCNAIIAAMYRAKRYSESISLFQYFFKQSNIVPNVVSYNQIINAHCDEGNVDEALEVYRHILANAPFAPSSVTYRHLTKGLVQAGRIGDAASLLREMLSKGQAADSTVYNNLIRGYLDLGDFDKAVEFFDELKSKCTVYDGIVNATFMEYWFEKGNDKEAMESYRSLLDKKFRMHPPTGNVLLEVFLKFGKKDEAWALFNEMLDNHAPPNILSVNSDTVGIMVNECFKMGEFSEAINTFKKVGSKVTSKPFVMDYLGYCNIVTRFCEQGMLTEAERFFAEGVSRSLPADAPSHRAMIDAYLKAERIDDAVKMLDRMVDVNLRVVADFGARVFGELIKNGKLTESAEVLTKMGEREPKPDPSIYDVVVRGLCDGDALDQAKDIVGEMIRHNVGVTTVLREFIIEVFEKAGRREEIEKILNSVARPVRNAGQSGNTPPRVPAVFGTTPAAPQQPRDRAPWTSQGVVHSNSGWANGTAGQTAGGAYKANNGQNPSWSNTSDNQQQQSWSNQTAGQQPPSWSRQAPGYQQQQSWSQQSGWSSPSGHQQSWTNQTAGQQQPWANQTPGQQQQWANQTPGQQQQLANQTPGQQQQWANQTPGQQQQWANQNNGHQQPWANQNTGHQQSWANQTPSQQQPWANQTTGQQQGWGNQTTGQQQQWANQTAGQQSGWTAQQQWSNQTASHQQSQWLNPVPGEVANQTPWSNSVDSHLPQQQEPGPSHECQETQEKKVVELRN | Function: May function as a transcriptional regulator essential for early embryogenesis.
Sequence Mass (Da): 102093
Sequence Length: 913
Domain: The WQQ domain consists of a repetition of W-x(2)-Q-x(4)-Q-x(2) motifs.
Subcellular Location: Nucleus
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Q5R3F8 | MLRLGLCAAALLCVCRPGAVRADCWLIEGDKGYVWLAICSQNQPPYETIPQHINSTVHDLRLNENKLKAVLYSSLNRFGNLTDLNLTKNEISYIEDGAFLGQSSLQVLQLGYNKLSNLTEGMLRGMSRLQFLFVQHNLIEVVTPTAFSECPSLISIDLSSNRLSRLDGATFASLASLMVCELAGNPFNCECDLFGFLAWLVVFNNVTKNYDRLQCESPREFAGYPLLVPRPYHSLNAITVLQAKCRNGSLPARPVSHPTPYSTDAQREPDENSGFNPDEILSVEPPASSTTDASAGPAIKLHHVTFTSATLVVIIPHPYSKMYILVQYNNSYFSDVMTLKNKKEIVTLDKLRAHTEYTFCVTSLRNSRRFNHTCLTFTTRDPVPGDLAPSTSTTTHYIMTILGCLFGMVIVLGAVYYCLRKRRMQEEKQKSVNVKKTILEMRYGADVDAGSIVHAAQKLGEPPVLPVSRMASIPSMIGEKLPTAKGLEAGLDTPKVATKGNYIEVRTGAGGDGLARPEDDLPDLENGQGSAAEISTIAKEVDKVNQIINNCIDALKLDSASFLGGGSSSGDPELAFECQSLPAAAAASSATGPGALERPSFLSPPYKESSHHPLQRQLSADAAVTRKTCSVSSSGSIKSAKVFSLDVPDHPAATGLAKGDSKYIEKGSPLNSPLDRLPLVPAGSGGGSGGGGGIHHLEVKPAYHCSEHRHSFPALYYEEGADSLSQRVSFLKPLTRSKRDSTYSQLSPRHYYSGYSSSPEYSSESTHKIWERFRPYKKHHREEVYMAAGHALRKKVQFAKDEDLHDILDYWKGVSAQQKL | Function: Inhibits phosphatase activity of protein phosphatase 1 (PP1) complexes.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 89687
Sequence Length: 820
Subcellular Location: Membrane
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A0A0S1RVB0 | MQVWAIIYDKADFPDTLYQNALPFVDQAVQSKIKRFHRREDACRSLIGSLLPRVLLRKRGVSRDEMTFATTENGKPYCTTPDIDPPLGFNVTHDESVIAMAFGSGDLGPPAYNLGVDVMQLKVPPRITFSEFVDSVSSQESDQLTARERNIVLADIPEGEALRRFYWVWTLKEAYTKALGIGLGFDFRRIQYDVLEEKVTIDGELARGWQFRKFEVAHSGNKYVGVAARFVGGRNPSITDLDEGSLVCYDAASFVNRAIEELV | Function: Transfers the 4'-phosphopantetheine moiety from coenzyme A to a Ser of an acyl-carrier-protein. Activates the peptidyl carrier protein (PCP) domains of surfactin synthas.
Catalytic Activity: apo-[ACP] + CoA = adenosine 3',5'-bisphosphate + H(+) + holo-[ACP]
Sequence Mass (Da): 29595
Sequence Length: 263
EC: 2.7.8.7
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Q9F0Q6 | MIAALLPSWAVTEHAFTDAPDDPVSLLFPEEAAHVARAVPKRLHEFATVRVCARAALGRLGLPPGPLLPGRRGAPSWPDGVVGSMTHCQGFRGAAVARAADAASLGIDAEPNGPLPDGVLAMVSLPSEREWLAGLAARRPDVHWDRLLFSAKESVFKAWYPLTGLELDFDEAELAVDPDAGTFTARLLVPGPVVGGRRLDGFEGRWAAGEGLVVTAIAVAAPAGTAEESAEGAGKEATADDRTAVP | Function: Transfers the 4'-phosphopantetheine moiety from coenzyme A to a Ser of an acyl-carrier-protein. The enzyme is able to transfer the cofactor to a broad range of enzymes with acyl- or peptidyl-carrier protein domains.
Catalytic Activity: apo-[ACP] + CoA = adenosine 3',5'-bisphosphate + H(+) + holo-[ACP]
Sequence Mass (Da): 25619
Sequence Length: 246
EC: 2.7.8.7
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Q4W9R0 | MKLIPFPYPLNIGTDVVHLPRILRLINRPDYFHRFTRRILHEQEQRDFRTRFSLPPPSSGAEKTGLNPITPDMARWLAGRFAAKEAARKAAPAGASSLGWKDVIVRVGEADKGRPEIVYLDPMGCGETGGGRVGKLSISHDGDYVVATVLAAG | Function: Acyl-carrier-protein synthase transfers the 4'-phosphopantetheine moiety from coenzyme A to a Ser of an acyl-carrier-protein . The 4'-phosphopantetheine (4'-PPT) portion of CoA provides the essential prosthetic group for a number of carrier proteins and multi-domain enzymes, priming them for the acceptance of acyl building blocks in fatty acid synthesis and many aspects of secondary metabolism mediated by polyketide synthases (PKSs) and non-ribosomal peptide synthetases (NRPSs) . PptB is specific for the mitochondrial acyl carrier protein acpA .
Catalytic Activity: apo-[ACP] + CoA = adenosine 3',5'-bisphosphate + H(+) + holo-[ACP]
Sequence Mass (Da): 16789
Sequence Length: 153
Subcellular Location: Mitochondrion
EC: 2.7.8.7
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Q8NI37 | MFSVLSYGRLVARAVLGGLSQTDPRAGGGGGGDYGLVTAGCGFGKDFRKGLLKKGACYGDDACFVARHRSADVLGVADGVGGWRDYGVDPSQFSGTLMRTCERLVKEGRFVPSNPIGILTTSYCELLQNKVPLLGSSTACIVVLDRTSHRLHTANLGDSGFLVVRGGEVVHRSDEQQHYFNTPFQLSIAPPEAEGVVLSDSPDAADSTSFDVQLGDIILTATDGLFDNMPDYMILQELKKLKNSNYESIQQTARSIAEQAHELAYDPNYMSPFAQFACDNGLNVRGGKPDDITVLLSIVAEYTD | Cofactor: Binds 2 magnesium or manganese ions per subunit.
Function: Protein phosphatase which positively regulates biosynthesis of the ubiquinone, coenzyme Q . Dephosphorylates the ubiquinone biosynthesis protein COQ7 which is likely to lead to its activation .
Catalytic Activity: H2O + O-phospho-L-seryl-[protein] = L-seryl-[protein] + phosphate
Sequence Mass (Da): 32646
Sequence Length: 304
Subcellular Location: Mitochondrion matrix
EC: 3.1.3.16
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Q6NVE9 | MFSVLSYGRLVARAVLGGLSQTDPRAGGGGGGGGGSSGDYGLVTAGCGFGKDFRKGLLKKGACYGDDACFVARHRSADVLGVADGVGGWRDYGVDPSQFSGTLMRTCERLVKEGRFVPSNPVGILTTSYCELLQNKVPLLGSSTACIVVLDRSSHRLHTANLGDSGFLVVRGGEVVHRSDEQQHYFNTPFQLSIAPPEAEGVVLSDSPDAADSTSFDVQLGDIILTATDGLFDNMPDYMILQELKKLKNSNYESIQRTARSIAEQAHELAYDPNYMSPFAQFACDNGLNVRGGKPDDITVLLSIVAEYTD | Cofactor: Binds 2 magnesium or manganese ions per subunit.
Function: Protein phosphatase which positively regulates biosynthesis of the ubiquinone, coenzyme Q (By similarity). Dephosphorylates the ubiquinone biosynthesis protein COQ7 which is likely to lead to its activation (By similarity).
Catalytic Activity: H2O + O-phospho-L-seryl-[protein] = L-seryl-[protein] + phosphate
Sequence Mass (Da): 33048
Sequence Length: 310
Subcellular Location: Mitochondrion matrix
EC: 3.1.3.16
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Q6GR25 | MFSVLSCGRLVARAVFGGLSQTDSRDYSLVTASCGFGKDARKGILKKGMCYGDDACFIARHRTADVLGVADGVGGWRDYGVDPSQFSETLMRTCERLVKEGRFVPTNPVGILTSSYRELLQNKVPLLGSSTACLVVLDRTSHRLHTANLGDSGFLVVRAGEVVHRSDEQQHYFNTPFQLSIAPPEAEGAVLSDSPDAADSNSFDVQLGDIILTATDGLFDNMPDYMILQELKKLKNTNYESIQQTARSIAEQAHDLAYDPNYMSPFAQFACDYGLNVRGGKPDDITVLLSIVAEYTD | Cofactor: Binds 2 magnesium or manganese ions per subunit.
Function: Protein phosphatase which positively regulates biosynthesis of the ubiquinone, coenzyme Q (By similarity). Dephosphorylates the ubiquinone biosynthesis protein coq7 which is likely to lead to its activation (By similarity).
Catalytic Activity: H2O + O-phospho-L-seryl-[protein] = L-seryl-[protein] + phosphate
Sequence Mass (Da): 32427
Sequence Length: 297
Subcellular Location: Mitochondrion matrix
EC: 3.1.3.16
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I6YEE1 | MTWKGSGQETVGAEPTLWAISDLHTGHLGNKPVAESLYPSSPDDWLIVAGDVAERTDEIRWSLDLLRRRFAKVIWVPGNHELWTTNRDPMQIFGRARYDYLVNMCDEMGVVTPEHPFPVWTERGGPATIVPMFLLYDYSFLPEGANSKAEGVAIAKERNVVATDEFLLSPEPYPTRDAWCHERVAATRARLEQLDWMQPTVLVNHFPLLRQPCDALFYPEFSLWCGTTKTADWHTRYNAVCSVYGHLHIPRTTWYDGVRFEEVSVGYPREWRRRKPYSWLRQVLPDPQYAPGYLNDFGGHFVITPEMRTQAAQFRERLRQRQSR | Function: Catalyzes the hydrolysis of the phosphopantetheine group from substrate holo-carrier proteins.
Catalytic Activity: H2O + holo-[ACP] = (R)-4'-phosphopantetheine + apo-[ACP] + H(+)
Sequence Mass (Da): 37601
Sequence Length: 324
EC: 3.1.4.14
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Q6F9J1 | MRFNMTTTLFSPAEFEQALRDKGRYYHIHHPYHIMMNDGHATKQQIQGWVANRFYYQVNIPLKDAAIMANCPDPATRRKWVQRILDHDGQHDDHGGIEAWLRLGEAVGLDRETILSQKMVLPSVRFAVDAYVNFARRACWQEAACSSLTELFAPAIHQSRLDTWPTHYPWIDAEGYAYFRGRLSQANRDVEHGLELALEYCNTVDRQQRMLNILQFKLDILWTILDGMSMAYVLERAPYHTVTQEAVWHQKGLLG | Function: Ring cyclization and eight-electron oxidation of 3a-(2-amino-2-carboxyethyl)-4,5-dioxo-4,5,6,7,8,9-hexahydroquinoline-7,9-dicarboxylic-acid to PQQ.
Catalytic Activity: 6-(2-amino-2-carboxyethyl)-7,8-dioxo-1,2,3,4,7,8-hexahydroquinoline-2,4-dicarboxylate + 3 O2 = H(+) + 2 H2O + 2 H2O2 + pyrroloquinoline quinone
Sequence Mass (Da): 29662
Sequence Length: 255
Pathway: Cofactor biosynthesis; pyrroloquinoline quinone biosynthesis.
EC: 1.3.3.11
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Q89FG3 | MNAASLTGITALSIGKDIKLNSAEELEAALRHIGATRYHSLHPFHKLLHGGKLNKGQVQAWALNRYYYQSTIPIKDAVVISRFRDRATRLEWRHRIEDHDGDVGSEGGIERWLKLTEGLGLDTAYVESTEGILPATRFAVEAYVHYCREKSPLEAIASSLTELFAPSIHEERIAGMLQHYDFVNPDIMSYFKRRLTQAPRDANFALEYVRTHARTPEERASVCNALIFKTNVLWVQLDALQHAYVEGHIPPGAFVPKEN | Function: Ring cyclization and eight-electron oxidation of 3a-(2-amino-2-carboxyethyl)-4,5-dioxo-4,5,6,7,8,9-hexahydroquinoline-7,9-dicarboxylic-acid to PQQ.
Catalytic Activity: 6-(2-amino-2-carboxyethyl)-7,8-dioxo-1,2,3,4,7,8-hexahydroquinoline-2,4-dicarboxylate + 3 O2 = H(+) + 2 H2O + 2 H2O2 + pyrroloquinoline quinone
Sequence Mass (Da): 29290
Sequence Length: 259
Pathway: Cofactor biosynthesis; pyrroloquinoline quinone biosynthesis.
EC: 1.3.3.11
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Q9C889 | MTNYGAIPTSSHPSPAIDLEYISRAKHRIKSGLATRRPWKSMFDFESMTLPHGFFDAISRIKTNLGYFRANYAIGVLFILFLSLLYHPTSLIVLSILVVFWIFLYFLRDEPLVVFGYQIDDRTVLIGLSVLTVVMLLLTHATSNILGSLLTAAVLVLIHAAVRRSDNLFLDEEAAAVTEASGLMSYPSS | Function: May be involved in both secretory and endocytic intracellular trafficking in the endosomal/prevacuolar compartments.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 21072
Sequence Length: 189
Subcellular Location: Endosome membrane
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Q9LIC6 | MTNYGAIPTSSHASPLVDVESLSRAKHRIKAGLATRRAWRVMFDFHSMGLPHGVSDAFTRIKTNLAYFRMNYAIVVLIVIFFSLIWHPTSLIVFTVLVVVWIFLYFLRDEPIKLFRFQIDDRTVLIVLSVLTVVLLLLTNATFNIVGALVTGAVLVLIHSVVRKTEDLFLDEEAATTETSGLTSYPST | Function: May be involved in both secretory and endocytic intracellular trafficking in the endosomal/prevacuolar compartments.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 21116
Sequence Length: 188
Subcellular Location: Endoplasmic reticulum membrane
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Q9ZWD1 | MLAPGESVLIPAEEISLSAGDVISLSVHNLIASVSSYRPWWSEFLAFGSIDRPSSFSPAVSRVKLNLHHFAVNYVLLTAASITLFLIGDPMALVTVASFVAMWLLLYFYRDHPLVLYGRHISDRVIVFGLILGSLWALWFINSLQCLILGVVTSVLLCLVHAIIRNSDDLFVQEKDVVVPSNFLHWS | Function: May be involved in both secretory and endocytic intracellular trafficking in the endosomal/prevacuolar compartments.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 20782
Sequence Length: 187
Subcellular Location: Endosome membrane
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Q9FH16 | MTPSPPPITYISIPLPTNDVVSRSIHNLTTAISSHRPWSELIFSGDFSLPESFSSLLLRSKTNFNYFFVNYTIIVSTCAAFALITASPVALIVVGAIIALWLIFHFFREDPLILWSFQVGDRTVLLFLVLASVWAIWFTNSAVNLAVGVSVGLLLCIIHAVFRNSDELFLEEDDAINGGLIGSNLR | Function: May be involved in both secretory and endocytic intracellular trafficking in the endosomal/prevacuolar compartments.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 20532
Sequence Length: 186
Subcellular Location: Endoplasmic reticulum membrane
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P41484 | MTDQPPPSGSNPTPAPPPPGSSGGYEPSFAPSELGSAYPPPTAPPVGGSYPPPPPPGGSYPPPPPPGGSYPPPPPSTGAYAPPPPGPAIRSLPKEAYTFWVTRVLAYVIDNIPATVLLGIGMLIQTLTKQEACVTDITQYNVNQYCATQPTGIGMLAFWFAWLMATAYLVWNYGYRQGATGSSIGKTVMKFKVISEATGQPIGFGMSVVRQLAHFVDAVICCIGFLFPLWDSKRQTLADKIMTTVCLPI | Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 26295
Sequence Length: 249
Domain: Its N-terminus, which contains the proline-rich repeats, is highly immunoreactive.
Subcellular Location: Cell membrane
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Q04118 | MLLILLSVALLALSSAQSLNEDVSQEESPSVISGKPEGRRPQGGNQPQRTPPPPGKPEGRPPQGGNQSQGPPPRPGKPEGPPPQGGNQSQGPPPRPGKPEGQPPQGGNQSQGPPPRPGKPEGPPPQGGNQSQGPPPRPGKPEGPPPQGGNQSQGPPPHPGKPEGPPPQGGNQSQGPPPRPGKPEGPPPQGGNQSQGPPPRPGKPEGPPPQGGNQSQGPPPRPGKPEGSPSQGGNKPQGPPPHPGKPQGPPPQEGNKPQRPPPPGRPQGPPPPGGNPQQPLPPPAGKPQGPPPPPQGGRPHRPPQGQPPQ | Function: Acts as a receptor for the Gram-negative bacterium F.nucleatum.
PTM: The Gl-8 variant contains an interchain disulfide bond with salivary peroxidase.
Sequence Mass (Da): 30980
Sequence Length: 309
Subcellular Location: Secreted
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O43663 | MRRSEVLAEESIVCLQKALNHLREIWELIGIPEDQRLQRTEVVKKHIKELLDMMIAEEESLKERLIKSISVCQKELNTLCSELHVEPFQEEGETTILQLEKDLRTQVELMRKQKKERKQELKLLQEQDQELCEILCMPHYDIDSASVPSLEELNQFRQHVTTLRETKASRREEFVSIKRQIILCMEALDHTPDTSFERDVVCEDEDAFCLSLENIATLQKLLRQLEMQKSQNEAVCEGLRTQIRELWDRLQIPEEEREAVATIMSGSKAKVRKALQLEVDRLEELKMQNMKKVIEAIRVELVQYWDQCFYSQEQRQAFAPFCAEDYTESLLQLHDAEIVRLKNYYEVHKELFEGVQKWEETWRLFLEFERKASDPNRFTNRGGNLLKEEKQRAKLQKMLPKLEEELKARIELWEQEHSKAFMVNGQKFMEYVAEQWEMHRLEKERAKQERQLKNKKQTETEMLYGSAPRTPSKRRGLAPNTPGKARKLNTTTMSNATANSSIRPIFGGTVYHSPVSRLPPSGSKPVAASTCSGKKTPRTGRHGANKENLELNGSILSGGYPGSAPLQRNFSINSVASTYSEFAKDPSLSDSSTVGLQRELSKASKSDATSGILNSTNIQS | Function: Key regulator of cytokinesis that cross-links antiparrallel microtubules at an average distance of 35 nM. Essential for controlling the spatiotemporal formation of the midzone and successful cytokinesis. Required for KIF14 localization to the central spindle and midbody. Required to recruit PLK1 to the spindle. Stimulates PLK1 phosphorylation of RACGAP1 to allow recruitment of ECT2 to the central spindle. Acts as an oncogene for promoting bladder cancer cells proliferation, apoptosis inhibition and carcinogenic progression .
PTM: Phosphorylation by CDK1 in early mitosis holds PRC1 in an inactive monomeric state, during the metaphase to anaphase transition, PRC1 is dephosphorylated, promoting interaction with KIF4A, which then translocates PRC1 along mitotic spindles to the plus ends of antiparallel interdigitating microtubules. Dephosphorylation also promotes MT-bundling activity by allowing dimerization. Phosphorylation by CDK1 prevents PLK1-binding: upon degradation of CDK1 at anaphase and dephosphorylation, it is then phosphorylated by PLK1, leading to cytokinesis.
Sequence Mass (Da): 71607
Sequence Length: 620
Domain: Microtubule binding occurs via a basic patch in the central spectrin-like domain and requires also the unstructured C-terminal domain.
Subcellular Location: Nucleus
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P27177 | MARLLTTCCLLALLLAACTDVALSKKGKGKPSGGGWGAGSHRQPSYPRQPGYPHNPGYPHNPGYPHNPGYPHNPGYPHNPGYPQNPGYPHNPGYPGWGQGYNPSSGGSYHNQKPWKPPKTNFKHVAGAAAAGAVVGGLGGYAMGRVMSGMNYHFDSPDEYRWWSENSARYPNRVYYRDYSSPVPQDVFVADCFNITVTEYSIGPAAKKNTSEAVAAANQTEVEMENKVVTKVIREMCVQQYREYRLASGIQLHPADTWLAVLLLLLTTLFAMH | Function: Its primary physiological function is unclear. Has cytoprotective activity against internal or environmental stresses. May play a role in neuronal development and synaptic plasticity. May be required for neuronal myelin sheath maintenance. May play a role in iron uptake and iron homeostasis. Soluble oligomers are toxic to cultured neuroblastoma cells and induce apoptosis (in vitro). Association with GPC1 (via its heparan sulfate chains) targets PRNP to lipid rafts. Also provides Cu(2+) or Zn(2+) for the ascorbate-mediated GPC1 deaminase degradation of its heparan sulfate side chains (By similarity).
Location Topology: Lipid-anchor
Sequence Mass (Da): 29909
Sequence Length: 273
Subcellular Location: Cell membrane
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P04156 | MANLGCWMLVLFVATWSDLGLCKKRPKPGGWNTGGSRYPGQGSPGGNRYPPQGGGGWGQPHGGGWGQPHGGGWGQPHGGGWGQPHGGGWGQGGGTHSQWNKPSKPKTNMKHMAGAAAAGAVVGGLGGYMLGSAMSRPIIHFGSDYEDRYYRENMHRYPNQVYYRPMDEYSNQNNFVHDCVNITIKQHTVTTTTKGENFTETDVKMMERVVEQMCITQYERESQAYYQRGSSMVLFSSPPVILLISFLIFLIVG | Function: Its primary physiological function is unclear. May play a role in neuronal development and synaptic plasticity. May be required for neuronal myelin sheath maintenance. May promote myelin homeostasis through acting as an agonist for ADGRG6 receptor. May play a role in iron uptake and iron homeostasis. Soluble oligomers are toxic to cultured neuroblastoma cells and induce apoptosis (in vitro) (By similarity). Association with GPC1 (via its heparan sulfate chains) targets PRNP to lipid rafts. Also provides Cu(2+) or Zn(2+) for the ascorbate-mediated GPC1 deaminase degradation of its heparan sulfate side chains (By similarity).
PTM: The glycosylation pattern (the amount of mono-, di- and non-glycosylated forms or glycoforms) seems to differ in normal and CJD prion.
Location Topology: Lipid-anchor
Sequence Mass (Da): 27661
Sequence Length: 253
Domain: The normal, monomeric form, PRPN(C), has a mainly alpha-helical structure. Misfolding of this form produces a disease-associated, protease-resistant form, PRPN (Sc), accompanied by a large increase of the beta-sheet content and formation of amyloid fibrils. These fibrils consist of a cross-beta spine, formed by a steric zipper of superposed beta-strands. Disease mutations may favor intermolecular contacts via short beta strands, and may thereby trigger oligomerization. In addition, the heparan-sulfate proteoglycan, GPC1, promotes the association of PRPN (C) to lipid rafts and appears to facilitate the conversion to PRPN (Sc).
Subcellular Location: Cell membrane
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A5DJ60 | MFHFFLKYHFFLFISMAPRYYLTLSQVCSQVWCNKYTIAFVLLAVKVYTFSLILRSTLDHLMDLVDTINVSLDQFASTATNFPAQLTQLTNKLIAEQLQQLKSNFKLSLLLLVSVIRALIGFYMEIFLGTFTCLLDAAAQASVNFALDSAQATLKCLNTTIVSVTSEVESGLESISSFIENSINTVSSLFTNGKKPSVTSINLSLGKLRNLQIPGSVTNELDSFRLNLDEFDNLKNSTINLLTAPLTHFDKNVSGSDLFGPIDSSKMVVANYGPSAAKNVTFDLTEVKNSIVDFKNDAAKIASIMIIVLASLSVIAMIALVFVERRNFVKRDIFVISVREKSSPLAIGNALETYQNRTIYYMAKLKVNPRYYWICNYLTSKYAMVVIIIGLVGVISFTLQYRLLLSVKNKLKNLIDTVSSPEQTKQLQASLSQYTAQTNNYIEAQSKALNQNLLGWYMKASTNVNDTLTDILHQINSTIHTVTGNTALSKPFEVVVYCVIGRKIVAVTKGITWLNEHLVIDLPQLPVDLFKDVTEAAPLRYGKQLETQMVKATNSLEHMLFIELYVALGFVGIWVIFIVMGIIFMFFPKKRTIGSPKLLTKTEKEEYIFPLSSFNTSSSVYSTLNDRPIS | Function: Involved in cell fusion during mating by stabilizing the plasma membrane fusion event.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 70527
Sequence Length: 630
Subcellular Location: Cell membrane
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A3LNK7 | MPYLNFAERISQVYLNKYTLALVLVTIKVYLFQKTLVAAVRNIPDFSDCSVDELPTKVSVMIRNMVENNLNSFTYSTLALLHVAAKSILNLIWFAVEMLLGTYTCLFKAAIVGTSDFAADTSEMVVKGLNTTIVEITHDIQSGLDGLSSILNKVVSTASKVADFFTGNNNSDSPDQYQKSISLSLGKLTNLSIPSSVLGEINKIRIDPDFSSVENSTKKLIEEPFTSLTNQWNQNETLSLGGVKFPLLQPLSVCDIGSKSIQELSHNLSTSVEMAAKIVIIILAICAVLVMVPLIYDEWRKWNREERIIGNLVNQNTHYYFDLREAFSNLLHPYLRFLPKSWLSTYVFSNYSISFLLVGLLGLFVVFLQYIILRILIKKAKGTDIDTSQMTKELSNMTSVYLSQIDSYFQKQEDNINDKLFGSVKSTSSKINSTLHEFMSTLNDTVNSIFSNTPFSGPVNTIVYCTIGRKIDKVESGLTWINDNLSVKIPNINKKQLSDNLKSVISESDSSAGSVFAKGVQKTIAMYKSNLFLEFVISISLVGVWVMQLLIGVIIAVTKSHLKRRRLGSLTSSLDKTRISSPKELTKEEKLQYGYGFSVTNPYEVQRYSSKLSGTKIYNT | Function: Involved in cell fusion during mating by stabilizing the plasma membrane fusion event.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 69307
Sequence Length: 620
Subcellular Location: Cell membrane
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Q9P771 | MASSYLSLAARLSQCWISPWSLCCLYILMQFFLFTKDLNTKIGDFVNDEQATCNYIQEKVDILLDSPSLIANAAVRVAKDGIQSTVKIILSGISDSLIAAENVFIFFIEFSYGTYLCLIQLAIDGILDAVADVGEEIGTAVNDTLHAIADEIEDTVSSLNEVFQSAEDSLEKVASWLGEDINLPNVSIPEIQSLRNFTLSSSYDTEFEKLKAGVNFDSAINATKAAISKPFSSARNLILEKVSNYSFDTSMVSSPNKTHVVVCSTDDLTAISSFILSSIYKIRKVVIISLLIIIAGLFLISSIYEIWKWCRIRHKAFLLDEHIRSNKFEDTRDLISYIESPISWNLKYFISALPLPCFLSVQLRWFITYIFHPPAAMILFISCTSFISGILQLVLLNNIREDGSVISALAQNSFHKVESALANVSVAWANSTNQIILKNQENINNNMFGSIHNTTLSLNSTLNTFMNELNSSMTSAFGDTFLASTVQNVMNCLLYRKIENFEEVLTWVYNKSHIELPLLPTDILSKSIDNQTIYSSLYSSLNSSNSTVSFSGIFDRVEKSVISELNFSFLFFLLWLLICAFGLIGVLSSWLKSLFLSLLDLVIPNPKENITLPVQSLAFPVTKSCRPPPIPPRESHVYDFQNFQYEEDDCIDYKRSLGLISLSSDLAIDIPISPAIISDIQFNSITTESEETTYLLKEKQDRY | Function: Involved in cell fusion during mating by stabilizing the plasma membrane fusion event.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 78740
Sequence Length: 703
Subcellular Location: Cell membrane
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