ids stringlengths 6 10 | seqs stringlengths 11 1.02k | texts stringlengths 108 11.1k |
|---|---|---|
Q9XJJ6 | MNRVLCVVIIVLAVGYGALWLATNHYRDNALTYKAQRDKKARELEQANATITDMQVRQRDVAALDAKYSRELADARAENETLRADVAAGRKRLRINATCSGTVREATGTSGVDNATGPRLADTAERDYFILRERLITMQKQLEGTQKYINEQCR | Function: Component of the spanin complex that disrupts the host outer membrane and participates in cell lysis during virus exit. The spanin complex conducts the final step in host lysis by disrupting the outer membrane after holin and endolysin have permeabilized the inner membrane and degraded the host peptidoglycans... |
Q7Y2B9 | MPRTIVAILVLAVVALGASYGFVQSYRALGIAQGEIKRQTARAEALEVRYATLQRHVKEVAARTNTQRQEVDRALDQNRPWADRPVPAAVVDSLCNRPGARCAVRTPTD | Function: Component of the spanin complex that disrupts the host outer membrane and participates in cell lysis during virus exit. The spanin complex conducts the final step in host lysis by disrupting the outer membrane after holin and endolysin action have permeabilized the inner membrane and degraded the host peptido... |
Q9T1X1 | MTFASKSLLLAAVFTAVLSGGLWHRLDSTRHDNQTLRRELQTEQQARHTAEWLLHGQEQTMQVFSAIRAANRAARLADETEHHDAKEKITTAITGDNCSTRPVPAVAADRLRELEKRTRAIGGDPARN | Function: Component of the spanin complex that disrupts the host outer membrane and causes cell lysis during virus exit. The spanin complex conducts the final step in host lysis by disrupting the outer membrane after endolysin action has degraded the host peptidoglycans. Host outer membrane disruption is possibly due t... |
P51770 | MSRLMIVLVVLLSLAVAGLFLVKHKNASLRASLDRANNVASGQQTTITMLKNQLHVALTRADKNELAQVALRQELENAAKREAQREKTITRLLNENEDFRRWYGADLPDAVRRLHQRPACTDASDCPQRMPESEPLPDAGQ | Function: Component of the spanin complex that disrupts the host outer membrane and participates in cell lysis during virus exit. The spanin complex conducts the final step in host lysis by disrupting the outer membrane after holin and endolysin action have permeabilized the inner membrane and degraded the host peptido... |
P13583 | MSRIKAIIASVIICIIVCLSWAVNHYRDNAITYKEQRDKATSIIADMQKRQRDVAELDARYTKELADANATIETLRADVSAGRKRLQVSATCPKSTTGASGMGDGESPRLTADAELNYYRLRSGIDRITAQVNYLQEYIRSQCLK | Function: Component of the spanin complex that disrupts the host outer membrane and participates in cell lysis during virus exit. The spanin complex conducts the final step in host lysis by disrupting the outer membrane after holin and endolysin action have permeabilized the inner membrane and degraded the host peptido... |
P10438 | MSRVTAIISALIICIIISLSWAVNHYRDNAIAYKAQRDKNARELKLANAAITDMQMRQRDVAAL | Function: Component of the spanin complex that disrupts the host outer membrane and causes cell lysis during virus exit. The spanin complex conducts the final step in host lysis by disrupting the outer membrane after holin and endolysin action have permeabilized the inner membrane and degraded the host peptidoglycans (... |
P39504 | MHVSNFTAGLLLLVIAFGGTSIILKHKVERLETSVTEITKTANENALALNNLRIQYNYIDAMNNKNREAIAAIERENEKLRKDAKKADVVAHKPGLVEKQINNSFNKFAEDIQDLSK | Function: Component of the spanin complex that disrupts the host outer membrane and participates in cell lysis during virus exit. The spanin complex conducts the final step in host lysis by disrupting the outer membrane after holin and endolysin action have permeabilized the inner membrane and degraded the host peptido... |
P03803 | MLEFLRKLIPWVLAGMLFGLGWHLGSDSMDAKWKQEVHNEYVKRVEAAKSTQRAIDAVSAKYQEDLAALEGSTDRIISDLRSDNKRLRVRVKTTGTSDGQCGFEPDGRAELDDRDAKRILAVTQKGDAWIRALQDTIRELQRK | Function: Component of the spanin complex that disrupts the host outer membrane and participates in cell lysis during virus exit. The spanin complex conducts the final step in host lysis by disrupting the outer membrane after holin and endolysin action have permeabilized the inner membrane and degraded the host peptido... |
P00726 | MSRVTAIISALVICIIVCLSWAVNHYRDNAITYKAQRDKNARELKLANAAITDMQMRQRDVAALDAKYTKELADAKAENDALRDDVAAGRRRLHIKAVCQSVREATTASGVDNAASPRLADTAERDYFTLRERLITMQKQLEGTQKYINEQCR | Function: Component of the spanin complex that disrupts the host outer membrane and participates in cell lysis during virus exit . The spanin complex conducts the final step in host lysis by disrupting the outer membrane after holin and endolysin have permeabilized the inner membrane and degraded the host peptidoglycan... |
P0DJZ3 | MPPCSATSRRSLPGPTPSARRWTVPWTRTARGLTGLCLLLSLTACATAPAPAVLCEHPLIDPTTQAGLIRAVAAYQDALDLCNALNQGD | Function: Component of the spanin complex that disrupts the host outer membrane and participates in cell lysis during virus exit. The spanin complex conducts the final step in host lysis by disrupting the outer membrane after holin and endolysin action have permeabilized the inner membrane and degraded the host peptido... |
P0DTL7 | MMQKKKLQPPLLVTIAALVLCLPLLLTGCGNSKNAPVPSVVILPEIDTELTEATPVPPMPQPLTWGASLLWNADLLMALGQCNRDKASVREQEIRRKEIYERRPEPGGGAAAR | Function: Component of the spanin complex that disrupts the host outer membrane and participates in cell lysis during virus exit. The spanin complex conducts the final step in host lysis by disrupting the outer membrane after holin and endolysin action have permeabilized the inner membrane and degraded the host peptido... |
Q8LTD0 | MRTKIFAAGTVLTCLMLCAGCTSAPPAPTPVIVPNACPKVSLCPMPGSDPQTNGDLSADIRQLENALARCASQVKMIKHCQDENDAQTRQPAQGAD | Function: Component of the spanin complex that disrupts the host outer membrane and participates in cell lysis during virus exit. The spanin complex conducts the final step in host lysis by disrupting the outer membrane after holin and endolysin action have permeabilized the inner membrane and degraded the host peptido... |
Q3T021 | MPIKPVGWICGQVLKNFSGRIEGIQKVIMDLIDEFKDEFPTILRLSQSNQKREPMQKPSKIRMAIALAKINRGTLIQGLNSISRSSKSVAKLLQPQLACRLLELRAISHRLLKEVNAPRQPLYNIQVRKGSLFEIISFPAKTALTSIMCASYAALIYLTVCVNAVLEKIMKIFQEEESIRQNREESENFRNAFSEPVLSEPLFPEGEIKAKPYRSLPEKPDSISDRPKLPANKLSNKIQVLHSVFDQSAEMNE | Function: May play at role in testicular development/spermatogenesis and may be an important factor in male infertility.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 28676
Sequence Length: 253
Subcellular Location: Membrane
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Q9BWV2 | MPIKPVGWICGQVLKNFSGRIEGIQKAIMDLVDEFKDEFPTILRLSQSNQKREPAQKTSKIRMAIALAKINRATLIRGLNSISRSSKSVAKLLHPQLACRLLELRDISGRLLREVNAPRQPLYNIQVRKGSLFEIISFPAKTALTSIIYASYAALIYLAVCVNAVLKKVKNIFQEEESIRQNREESENCRKAFSEPVLSEPMFAEGEIKAKPYRSLPEKPDISDYPKLLANKQSNNIQVLHSVFDQSAEMNEQI | Function: May play a role in testicular development/spermatogenesis and may be an important factor in male infertility.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 28740
Sequence Length: 254
Subcellular Location: Membrane
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Q9D9R3 | MEVRPIGWICGQVVKNFSGRLEGLQKAIMDLIDEFKDDLPTILRLSQSSQKTDPVQKTSKVRMALALAKINRGTLIQGLNHISSSSKSVAKLLQPRLAYRLLELRSISHRLLREVNVASQPLHSVQMKRGSLFEIISFPAKTALTSIMYASYAALIYLAVCVNAVLAKIKKIFQEEESIRQNRESENFRKAFSEPALRKPMFSESEIKAKPYRSLPEKPDNLLDQPKPPANKQSNKIQVLHSVFDQLAELNE | Function: May play at role in testicular development/spermatogenesis and may be an important factor in male infertility.
Location Topology: Single-pass membrane protein
Sequence Mass (Da): 28482
Sequence Length: 252
Subcellular Location: Membrane
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P33116 | MEVKEQLKLKELLFIMKQMPKTFKLIFTLERSLFLKLIRFSIITGILPIVSLYISQELINSLVTIRKEVSIVITIFLTYLGVSFFSELISQISEFYNGKFQLNIGYKLNYKVMKKSSNLALKDFENPEIYDKLERVTKEISYKPYQIIQAIITMTTSFVTLLSSIAFLMSWNPKVSLLLLVIPVISLFYFLKIGQEEFFIHWKRAGKERKSWYISYILTHDFSFKELKLYNLKDYLLNKYWDIKKSFIEQDTKILRKKTLLNLIYEIAVQLVGAVIIFIAIMSAFAGKIMVGNVMSYIRSVSLVQNHSQSIMTSIYSIYN... | Function: Probably implicated in the export process of the lantibiotic subtilin.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 71188
Sequence Length: 614
Subcellular Location: Cell membrane
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P39723 | MVRRWIPSGRHLRNNDNTGDDDDSEFTNSMDSGMSIPSLRDSMTTRSSHNDPIKPALMNDSNKVKNLEKELTNAKIKIQVLYEYIRRIPNKDGNAPSLGNDTDFRNSIIEGLNLEINKLKQDLKAKEVEYQDTLQFVQENLENSESIVNTINHLLSFILTHFNEQDENAHLLDKEERETLEETLELSSDYVLEKMDTLSKFIIQFLQDFLHSKSRAESKQDKEEFLSLAQSSPAGSQLESRDSPSSKEENTDGGYQNDEIHDSNNHIDTENVMANSTSLPISAVESRFEKTLDTQLEIVIENLHKEYDQFINSIRLKFEK... | Function: Spindle pole body component that acts as the gamma-tubulin complex-binding protein of the SPB outer plaque. Anchors cytoplasmic microtubules at the at the half bridge of the spindle pole body (SPB) and accordingly functions in nuclear position and spindle orientation, including anaphase spindle migration into... |
K4L7X3 | MYELTPEQRTLQTQARELAQSVFASTAVQTDLTEQYPWDNVAQLRDAGFMGMMLPTSVGGRGLSTLDTVIVIEEMAKACATMGRITVDSNLGAIGAITKYGSEEQIKLAADLVLAGDKPAICISEPNAGSAASEMTTRADKNGDHYILNGEKYWITGGGVSKLHLIFARVFDDGVEQGIGAFITVLDDHGPEGLKVGRRLYAMGVRGIPETHLEFHDLKIHKSMMITFPDGLKRGFAALMSAYNAQRVGAGAVALGIAQCAFEEGVAYLKRREQFGRPLAEFQGLQWMVADMSVQLEAARLMLRSAAVSGETFPDINKAA... | Cofactor: Binds 1 FAD per subunit.
Function: Catalyzes the conversion 3-sulfinopropanoyl-CoA (3SP-CoA) to propanoyl-CoA by abstraction of sulfite . Does not show dehydrogenase activity . Involved in the degradation of 3,3'-dithiodipropionate (DTDP), a sulfur-containing precursor substrate for biosynthesis of polythioes... |
Q9HUX1 | MAARRTRKDDGSNWTVADSRGVYGIRHWGAGYFAINDGGNVEVRPQGADSTPIDLYELVGQLREAGLSLPLLVRFPDILQDRVRKLTGAFDANIERLEYQSRYTALYPIKVNQQEAVVENIIATENVSIGLEAGSKPELMAVLALAPKGGTIVCNGYKDREFIKLALMGQKLGHNVFIVIEKESEVQLVIEEAANVGVQPQVGLRVRLSSLASSKWADTGGEKAKFGLSAAQLLSVVERFRQAGLDQGVRLLHFHMGSQIANLADYQHGFKEAIRYYGELRALGLPVDHIDVGGGLGVDYDGTHSRNASSINYDIDDYAG... | Function: Catalyzes the biosynthesis of agmatine from arginine.
Catalytic Activity: H(+) + L-arginine = agmatine + CO2
Sequence Mass (Da): 70668
Sequence Length: 636
EC: 4.1.1.19
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Q7UTS2 | MSSVLDSKWTRSDASKTYDIDRWGAGYFSISDAGTVLVSPDRDPSQSIDLKELVDRLGQRNLDLPILLRFNGILRDRLRELDRCFKNAIHDHKYQSRYRCVFPIKVNQQREVVQQIVSEGARLGFGIEAGSKPELVAAVAMGDANVPIVCNGFKDEEFIRLALLAQRLGRNVLPVVEKVSELDLILDVAKDIGVRPTIGMRVKLATRGSGRWQASGGYRSKFGLTVAELLAQLDRLIAMDMGDCLQLLHFHVGSQIGNIRQLKSAILEAARIYVDLVRRGAGMRYLDVGGGLGVDYDGSRSDSESSMNYTMQEYANDVVY... | Function: Catalyzes the biosynthesis of agmatine from arginine.
Catalytic Activity: H(+) + L-arginine = agmatine + CO2
Sequence Mass (Da): 74081
Sequence Length: 668
EC: 4.1.1.19
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Q09741 | MSVQELSHPLIKDGWFREINNMWPGQAMTLKVKKVLYAGKSKYQDVLVFESETYGHVLVLDGAIQATERDEFSYQEMIAHLALNSHPNPKKVLVIGGGDGGVLREVVKHECVEEAILCDIDEDVIKVSKQYLPEMSAGFNHPKVKVHIGDGFKFLQDYQNTFDVIITDSSDPDGPAEALFQKPYFQLLSDALRGGGVITTQAECMWIHLGVISNVLTAVKTVFPNVRYAYTTIPTYPSGSIGFVVASKDASIDLSKPLRKWSPEEENKLCKYYNSEIHAASFVLPTFARDVVDKATSS | Catalytic Activity: putrescine + S-adenosyl 3-(methylsulfanyl)propylamine = H(+) + S-methyl-5'-thioadenosine + spermidine
Sequence Mass (Da): 33150
Sequence Length: 298
Pathway: Amine and polyamine biosynthesis; spermidine biosynthesis; spermidine from putrescine: step 1/1.
EC: 2.5.1.16
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Q8EAX8 | MHESQLTTSAAKPSRLGWFDDVLLLGIMAVLAGCGLIYEYLLSHYAGRILGALEAAIYTMIGLMIVSMGLGAFAARKIKDAFTGFVVLELTVALCGSLAILITAAVIGFGQQLPMLIASTLGLPPDQLPEGGMIGTLQKLSEYLPYFWGVLLGLMIGMEIPLIARVRQSLSDEHLLHNAGTIYGADYIGAGIGAAIWVGFMLAIDIQLAAALTASFNLLAGFVFIWRFWQKIQRPKLLLAAHLVVTGVLLLLAIQGPSWEQQFNNLLYKDKVVYAKATRFQQLTFTERLRGNGLSPVYALYINGRLQFSSSDEHIYHAFL... | Function: Catalyzes the irreversible transfer of a propylamine group from the amino donor S-adenosylmethioninamine (decarboxy-AdoMet) to putrescine (1,4-diaminobutane) to yield spermidine.
Catalytic Activity: putrescine + S-adenosyl 3-(methylsulfanyl)propylamine = H(+) + S-methyl-5'-thioadenosine + spermidine
Location ... |
P66835 | MDLWFSEVHTPDVKLSLRTAKQLYAGKSEWQDIEVLDTPAFGKILILNGHVLFSDADDFVYNEMTVHVPMAVHPNPKKVLVIGGGDGGVAQVLTLYPELEQIDIVEPDEMLVEVCREYFPDFAAGLDDPRVTIYYQNGLRFLRNCEDDYDIIINDATDPFGHTEGLFTKEFYGNSYRALKEDGIMIYQHGSPFFDEDESACRSMHRKVNQAFPISRVYQAHIPTSPAGYWLFGFASKKYHPVKDFDKEGWKKRQLFTEYYTANLHVGAFMLPKYVEDILEEEEGKK | Function: Catalyzes the irreversible transfer of a propylamine group from the amino donor S-adenosylmethioninamine (decarboxy-AdoMet) to putrescine (1,4-diaminobutane) to yield spermidine.
Catalytic Activity: putrescine + S-adenosyl 3-(methylsulfanyl)propylamine = H(+) + S-methyl-5'-thioadenosine + spermidine
Sequence ... |
Q7ZV80 | MSEELMKQLSNYKAQLQQVEAALSIDPDNEDLLKLQKDLQEVIELTKDLLTSQPAEGTTSTKSSETVAPSHSWRVGDHCMATWSQDGQVYEAEIEEIDNENGTAAITFAGYGNAEVMPLHMLKKVEEGRIRDEIDGKPKSKKELQAEQREYKKKKAQKKVQRMKELEQEREDQKSKWQQFNNKAYSKNKKGQVKRSIFASPESVNGKVGVGTCGIADKPMTQYNDTSKYNVRHLMPQ | Function: Involved in spliceosome assembly (By similarity).
Sequence Mass (Da): 26940
Sequence Length: 237
Domain: The Tudor domain mediates association with dimethylarginines, which are common in snRNP proteins.
Subcellular Location: Nucleus speckle
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O75940 | MSEDLAKQLASYKAQLQQVEAALSGNGENEDLLKLKKDLQEVIELTKDLLSTQPSETLASSDSFASTQPTHSWKVGDKCMAVWSEDGQCYEAEIEEIDEENGTAAITFAGYGNAEVTPLLNLKPVEEGRKAKEDSGNKPMSKKEMIAQQREYKKKKALKKAQRIKELEQEREDQKVKWQQFNNRAYSKNKKGQVKRSIFASPESVTGKVGVGTCGIADKPMTQYQDTSKYNVRHLMPQ | Function: Involved in spliceosome assembly.
Sequence Mass (Da): 26711
Sequence Length: 238
Domain: The Tudor domain mediates association with dimethylarginines, which are common in snRNP proteins.
Subcellular Location: Nucleus speckle
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Q8BGT7 | MSEDLAKQLASYKAQLQQVEAALSGNGENEDLLKLKKDLQEVIELTKDLLSTQPSETLASSDSFASTQPTHSWKVGDKCMAVWSEDGQCYEAEIEEIDEENGTAAITFAVYGNAEVTPLLNLKPVEEGRKAKEDSGNKPMSKKEMIAQQREYKKKKALKKAQRIKELEQEREDQKVKWQQFNNRAYSKNKKGQVKRSIFASPESVTGKVGVGTCGIADKPMTQYQDTSKYNVRHLMPQ | Function: Involved in spliceosome assembly (By similarity).
Sequence Mass (Da): 26753
Sequence Length: 238
Domain: The Tudor domain mediates association with dimethylarginines, which are common in snRNP proteins.
Subcellular Location: Nucleus speckle
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Q5R591 | MSEDLAKQLASYKAQLQQVEAALSGNGENEDLLKLKKDLQEVIELTKDLLSTQPSETLASSDSFASTQPTHSWKVGDKCMAIWSEDGQCYEAEIEEIDEENGTAAITFAGYGNAEVTPLLNLKPVEEGRKAKEDSGNKPMSKKEMIAQQREYKKKKALKKAQRIKELEQEREDQKVKWQQFNNRAYSKNKKGQVKRSIFASPESVTGKVGVGTCGIADKPMTQYQDTSKYNVRHLMPQ | Function: Involved in spliceosome assembly (By similarity).
Sequence Mass (Da): 26725
Sequence Length: 238
Domain: The Tudor domain mediates association with dimethylarginines, which are common in snRNP proteins.
Subcellular Location: Nucleus speckle
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O94519 | MEKELEEYKSQLALVQISLQKTPQNEELQLLENDLKELISLTENLLQESVENDKNTFQNSQNGVAGFNTSKPVHIDFTPGNLVMARWVSGDYLFYPSRITAVSGFGANKKYTVQFLDYPDIETVSLKHIKAMPEEKRQEIEGNKEILKKSTTIRSTPVREPTKAISVASMSTSPSNYASRASSPDMKSSAAVTANVSPIQNVAQHVSTLPKISPIPPSNPPPVPSVSYSQKQQKQLKPKAALEASQNSWKQFAARGVKTGRVGKRKKIGESSIFKSTEDFPGRTNPKNFGNVARSGHREKHIYNYREDEDS | Function: Involved in spliceosome assembly.
Sequence Mass (Da): 34626
Sequence Length: 311
Domain: The Tudor domain mediates association with dimethylarginines, which are common in snRNP proteins.
Subcellular Location: Nucleus
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Q8N0X2 | MAAQRGMPSSAVRVLEEALGMGLTAAGDARDTADAVAAEGAYYLEQVTITEASEDDYEYEEIPDDNFSIPEGEEDLAKAIQMAQEQATDTEILERKTVLPSKHAVPEVIEDFLCNFLIKMGMTRTLDCFQSEWYELIQKGVTELRTVGNVPDVYTQIMLLENENKNLKKDLKHYKQAADKAREDLLKIQKERDFHRMHHKRIVQEKNKLINDLKGLKLHYASYEPTIRVLHEKHHTLLKEKMLTSLERDKVVGQISGLQETLKKLQRGHSYHGPQIKVDHSREKENAPEGPTQKGLREAREQNKCKTKMKGNTKDSEFPI... | Function: Necessary for sperm flagellar function. Plays a role in motile ciliogenesis. May help to recruit STK36 to the cilium or apical surface of the cell to initiate subsequent steps of construction of the central pair apparatus of motile cilia (By similarity).
PTM: Phosphorylated by TSSK2.
Sequence Mass (Da): 70818... |
Q86AT8 | MSSTQQQQHQLFSAVEQNDVTKVKKLSSKKKISKSNLTSFDQYGQSALTIALKNNNEEMVELLLSLCVTLKADINTFDKNGFSALHQAVSSDDRILMRVLQYENINVDVQNDDLNTPIHYFCQKFRSPNCQEPFQLFIQKGVNVNAQNKNGETPLHKAIFNNSVRLMMVGLLLKNGANVNLATQFQESPLHYAVRLGREDLVSVLLKAGADVDCVGTKERKTPYQLAVEEGNKDMTARIKKYKDLFDWLQKHGFEQYKDAFLKEEMFLDELGEMSEDILNKMGITSTGTRLRILKETSNLANEQTKKPKTPELIIEEDPT... | Function: May be involved in cortical F-actin organization and resistance to osmotic stress. Activated upon cell detachment, in vitro.
PTM: Autophosphorylated.
Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Sequence Mass (Da): 72983
Sequence Length: 638
Subcellular Location: Cyto... |
Q9FAB3 | MTPDSRHRRLLANRYQLVELVGSGAMGQVYRAEDKLLGGVTVAVKFLSQALLNPRMKERFEREATISALLGEKSIHIVRVRDYGLDEKEIPFYVMEYLQGENISDVIKYRPLKVERFLKIARQICFGLDCAHKGIIYQGEACPVVHRDIKPSNVLLVEDPALGELVKILDFGIAKLVQAAEESKTQAFMGTLAYCSPEQMEGKELDSRSDIYSLGVMMYEMLTGEMPLFPDNSSFGGWYEAHHHTKPHPFSARYKIPASLEALVMNCLAKSPKGRPQSVDVIIRAIDAIEAEIKAPPISDTEKTQIAPHLLNTDMEATVV... | Function: Protein kinase that regulates cellular motility via phosphorylation of membrane proteins.
PTM: Autophosphorylated.
Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Sequence Mass (Da): 58875
Sequence Length: 521
EC: 2.7.11.1
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P74297 | MSFCVNPNCPHPKNPNNVQVCQACGNSLRLNGRYQTLGLLGKGGFGATFAAADVALPGTPICVVKQLRPQTDDPNVFRMAKELFEREAQTLGRVGNHPQVPRLLDYFEDDHQFYLVQEYVKGHNLHQEVKKNGTFTEGSVKQFLTEILPILDYIHSQKVIHRDIKPANLIRRQTDQKLVLIDFGAVKNQIDSVLSSNTSAQTALTAFAVGTAGFAPPEQMAMRPVYASDIYATGVTCLYLLTGKTPKEIDCNSQTGEMDWEKHVTVSSKFAEVIRKMLELSVRHRYKSAQQVLDALEMPTYEDGMMQGMVSTPFTTLTGA... | Function: Protein kinase required for cell motility, but not for phototaxis.
PTM: Autophosphorylated.
Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]
Sequence Mass (Da): 63079
Sequence Length: 574
EC: 2.7.11.1
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Q8S9L0 | MDCNMVSSFPWDWENLIMSNQSKTENEKKQQSTEWEFEKGEGIESIVPDFLGFEKVSSGSATSFWHTAVSKSSQSTSINSSSPEDKRCNLASQSSPGDSSSNIDFLQVKPSTALEVPIASAESDLCLKLGKRTYSEEFWGRNNNDLSAVSMNLLTPSVVARKKTKSCGQSMQVPRCQIDGCELDLSSSKDYHRKHRVCETHSKCPKVVVSGLERRFCQQCSRFHAVSEFDEKKRSCRKRLSHHNARRRKPQGVFPLNSERVFDRRQHTSMLWNGLSLNTRSEEKYTWGTTYETKPTQMESGFTLSFQRGNGSEDQLFTGS... | Cofactor: Binds 2 Zn(2+) ions per subunit.
Function: Trans-acting factor that binds specifically to the consensus nucleotide sequence 5'-TNCGTACAA-3'.
Sequence Mass (Da): 44159
Sequence Length: 396
Domain: The SBP-type zinc finger is required for the binding to DNA.
Subcellular Location: Nucleus
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A2YFT9 | MMSGRMNAAGDESPFPFGAMQAPGPGAYVGFDHGAAAVAAAAAAAQRAGMLQHHHHHMYDGLDFAAAMQFGGGQDAPPHPQLLALPPSMAAPPPPPMPMPLQMPMTMPMPGDVYPALGIVKREGGGGGQDAAAGRIGLNLGRRTYFSPGDMLAVDRLLMRSRLGGVFGLGFGGAHHQPPRCQAEGCKADLSGAKHYHRRHKVCEYHAKASVVAASGKQQRFCQQCSRFHVLTEFDEAKRSCRKRLAEHNRRRRKPAAAATTAVAAAKDAAAAPVAAGKKPSGGAATSYTGDNKNVVSMSAAKSPISSNTSVISCLPEQGK... | Function: Trans-acting factor that binds specifically to the consensus nucleotide sequence 5'-TNCGTACAA-3'.
Sequence Mass (Da): 44292
Sequence Length: 426
Domain: The SBP-type zinc finger is required for the binding to DNA.
Subcellular Location: Nucleus
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Q653Z5 | MECNPVSSTTSSSLLWDWDATASAEPPPPPGKRGGRDSSSASASAKRGRSAAAAGDAAAVAAEAPRCQVEGCGLELGGYKEYYRKHRVCEPHTKCLRVVVAGQDRRFCQQCSRFHAPSEFDQEKRSCRRRLSDHNARRRKPQTDVFAFGSGTLPRSLFDDRQQISFAWDNNAPLNHANTTSSSSWTSDLQLSQVMDISKRSRKAGADSANIRLSNALPTLCHDTNELLPIKGADASETASKLDGALDVQRALSLLSASSRGLTDPGHQTSSIIQFTNSNQNSTLPSVPSEGNSNVPFWVDGQHQAVEPQVFQFTMDTGNT... | Function: Trans-acting factor that binds specifically to the consensus nucleotide sequence 5'-TNCGTACAA-3' (By similarity). May be involved in panicle development.
Sequence Mass (Da): 37344
Sequence Length: 343
Domain: The SBP-type zinc finger is required for the binding to DNA.
Subcellular Location: Nucleus
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Q9V9Y9 | MEASAAKITPMASSMSASGSTNSPSSEKMNYALQVALQTIKERCIQLQRRVASMEEENQQLREASSRSEGAPRANEIGVTGDVLSLKAQVSELQRQKEQLEEHIGMVSNENRRLWSRLSQISKDQQLNALPSSTDSRAQQNQNLVRSKTFTQHSPNPHLRQKMLSDGIKDLSLEEIALDDFGASSEELGYPYNLQKVEETTSEPDANVDAKRCLDGLQELRREAMKQQQELRSVMTLLENRIALKPCPECAQKTIKKPEMADKSLETDDSLTSELKNYESQHNGHNGTPPSQRINIIQEKIKADAADAMEKTCPMCGKQY... | Function: Plays a role in oocyte axis determination and microtubule organization during oogenesis . Also required for polarized organization of the bristle . Required, with jvl, for activation of the kinase IKKepsilon in the germ line . Also required for localization of IKKepsilon to the distal tip of elongating bristl... |
Q9ALN5 | MRKPVRIGVLGCASFAWRRMLPAMCDVAETEVVAVASRDPAKAERFAARFECEAVLGYQRLLERPDIDAVYVPLPPGMHAEWIGKALEADKHVLAEKPLTTTASDTARLVGLARRKNLLLRENYLFLHHGRHDVVRDLLQSGEIGELREFTAVFGIPPLPDTDIRYRTELGGGALLDIGVYPARAARHFLLGPLTVLGASSHEAQESGVDLSGSVLLQSEGGTVAHLGYGFVHHYRSAYELWGSRGRIVVDRAFTPPAEWQAVIRIERKGVVDELSLPAEDQVRKAVTAFARDIRAGTGVDDPAVAGDSGESMIQQAALV... | Function: Involved in the biosynthesis of forosamine ((4-dimethylamino)-2,3,4,6-tetradeoxy-alpha-D-threo-hexopyranose), a highly deoxygenated sugar component of several bioactive natural products such as the insecticidal spinosyns A and D . Catalyzes the reduction of the C-3 keto moiety of dTDP-3,4-diketo-2,6-dideoxy-a... |
Q9ALN6 | MSSSVEAEASAAAPLGSNNTRRFVDSALSACNGMIPTTEFHCWLADRLGENSFETNRIPFDRLSKWKFDASTENLVHADGRFFTVEGLQVETNYGAAPSWHQPIINQAEVGILGILVKEIDGVLHCLMSAKMEPGNVNVLQLSPTVQATRSNYTQAHRGSVPPYVDYFLGRGRGRVLVDVLQSEQGSWFYRKRNRNMVVEVQEEVPVLPDFCWLTLGQVLALLRQDNIVNMDTRTVLSCIPFHDSATGPELAASEEPFRQAVARSLSHGIDSSSISEAVGWFEEAKARYRLRATRVPLSRVDKWYRTDTEIAHQDGKYFA... | Function: Involved in the biosynthesis of forosamine ((4-dimethylamino)-2,3,4,6-tetradeoxy-alpha-D-threo-hexopyranose), a highly deoxygenated sugar component of several bioactive natural products such as the insecticidal spinosyns A and D . Catalyzes the removal of the hydroxyl group at position C-2 of the hexose ring ... |
Q9ALN8 | MQSRKTRALGKGRARVTSCDDTCATATEMVPDAKDRILASVRDYHREQESPTFVAGSTPIRPSGAVLDEDDRVALVEAALELRIAAGGNARRFESEFARFFGLRKAHLVNSGSSANLLALSSLTSPKLGEARLRPGDEVITAAVGFPTTINPAVQNGLVPVFVDVELGTYNATPDRIKAAVTERTRAIMLAHTLGNPFAADEIAEIAKEHELFLVEDNCDAVGSTYRGRLTGTFGDLTTVSFYPAHHITSGEGGCVLTGSLELARIIESLRDWGRDCWCEPGVDNTCRKRFDYHLGTLPPGYDHKYTFSHVGYNLKTTDL... | Function: Involved in the biosynthesis of forosamine ((4-dimethylamino)-2,3,4,6-tetradeoxy-alpha-D-threo-hexopyranose), a highly deoxygenated sugar component of several bioactive natural products such as the insecticidal spinosyns A and D . Catalyzes C-3 deoxygenation of dTDP-4-keto-2,6-dideoxy-alpha-D-glucose to yield... |
Q9ALN9 | MINLHQPILGTEELDAIAEVFASNWIGLGPRTRTFEAEFAHHLGVDPEQVVFLNSGTAALFLTVQVLDLGPGDDVVLPSISFVAAANAIASSGARPVFCDVDPRTLNPTLDDVARAITPATKAVLLLHYGGSPGEVTAIADFCREKGLMLIEDSACAVASSVHGTACGTFGDLATWSFDAMKILVTGDGGMFYAADPELAHRARRLAYHGLEQMSGFDSAKSSNRWWDIRVEDIGQRLIGNDMTAALGSVQLRKLPEFINRRREIATQYDRLLSDVPGVLLPPTLPDGHVSSHYFYWVQLAPEIRDQVAQQMLERGIYTS... | Function: Involved in the biosynthesis of forosamine ((4-dimethylamino)-2,3,4,6-tetradeoxy-alpha-D-threo-hexopyranose), a highly deoxygenated sugar component of several bioactive natural products such as the insecticidal spinosyns A and D . In the presence of pyridoxal 5'-phosphate (PLP) and alpha-ketoglutarate, cataly... |
Q6NMN6 | MTRVGQRDSPAKEEAPPATKKRFLTPGRFVTILCIINLINYVDRGVIASNGVNGSSKVCDAKGVCSAGTGIQGEFNLTNFEDGLLSSAFMVGLLVASPIFAGLSKRFNPFKLIGVGLTVWTIAVIGCGFSYNFWMIAVFRMFVGVGEASFISLAAPYIDDSAPVARKNFWLGLFYMCIPAGVALGYVFGGYIGNHLGWRWAFYIEAIAMAVFVILSFCIKPPQQLKGFADKDSKKPSTSIETVAPTDAEASQIKTKTPKSKNLVVLFGKDLKALFSEKVFIVNVLGYITYNFVIGAYSYWGPKAGFGIYKMKNADMIFGG... | Function: Probable sphingolipid transporter that plays a central role in endosomes and/or lysosomes storage.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 53509
Sequence Length: 492
Subcellular Location: Late endosome membrane
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Q7ZU13 | MSQADADITPFFADDNEGEGPVENGVGSPLPEDEEEESPSGVTDRRAIMTVIVLCYINLLNYMDRFTVAGVLPDIEHFFGIGDGTSGLLQTVFICSYMFLAPLFGYLGDRYNRKLIMCVGIFFWSVVTLASSFIGKDHFWALLLTRGLVGVGEASYSTIAPTIIADLFVKEKRTNMLSIFYFAIPVGSGMGYIVGSKVDTVAKDWHWALRVTPGLGLLAVFLLMLVVQEPKRGAIEAHPEHTLHRTSWLADMKALCRNPSFILSTFGFTAVAFVTGSLALWAPAFLFRAGVFTGVKQPCFKAPCDDSDSLIFGAITVVTG... | Function: Mediates the rate-limiting, proton-dependent, lysosomal efflux of lysophospholipids . Selective for zwitterionic headgroups such as lysophosphatidylcholine (LPC) and lysophosphatidylethanolamine (LPE) . Essential player in lysosomal homeostasis . Critical for embryogenesis . Involved in the regulation of deve... |
Q9H2V7 | MAGSDTAPFLSQADDPDDGPVPGTPGLPGSTGNPKSEEPEVPDQEGLQRITGLSPGRSALIVAVLCYINLLNYMDRFTVAGVLPDIEQFFNIGDSSSGLIQTVFISSYMVLAPVFGYLGDRYNRKYLMCGGIAFWSLVTLGSSFIPGEHFWLLLLTRGLVGVGEASYSTIAPTLIADLFVADQRSRMLSIFYFAIPVGSGLGYIAGSKVKDMAGDWHWALRVTPGLGVVAVLLLFLVVREPPRGAVERHSDLPPLNPTSWWADLRALARNPSFVLSSLGFTAVAFVTGSLALWAPAFLLRSRVVLGETPPCLPGDSCSSS... | Function: Plays a critical role in the phospholipid salvage pathway from lysosomes to the cytosol . Mediates the rate-limiting, proton-dependent, lysosomal efflux of lysophospholipids, which can then be reacylated by acyltransferases in the endoplasmic reticulum to form phospholipids . Selective for zwitterionic headgr... |
Q9FLG8 | MDVDGEGDRGQNPRIMERDSDSIKDPISEPSWFTPKKLLFVFCVVNLINYIDRGAIASNGINGSRGSCTSSGTCSSGSGIQGDFNLSNFEDGVLSSAFMVGLLVASPIFASLAKSVNPFRLIGVGLSIWTLAVIGCGLSFDFWSITICRMFVGVGEASFVSLAAPFIDDNAPHDQKSAWLAVFYMCIPTGYAFGYVYGGVVGSVLPWRAAFWGEAILMLPFAVLGFVIKPLHLKGFAPDDTGKPRTDNLNVLPVGYGFSAVMKDLKLLLVDKVYVTNILGYIAYNFVLGAYSYWGPKAGYNIYKMENADMIFGGVTVVCG... | Function: Probable sphingolipid transporter that plays a central role in endosomes and/or lysosomes storage.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 52155
Sequence Length: 484
Subcellular Location: Late endosome membrane
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A2SWM2 | MCVESDGCEIEGCSSSDEVHTLSGSMSPALKSRDLHHCRPGQKFHAALLRCRTPLVAAGILSFGNVLNYMDRYTVAGVLLDIQKQFKVGDSSAGLLQTVFICSFMVAAPIFGYLGDRFNRKIILSCGIFFWSAVTLLSSFITKEYYWLLVLSRCLVGIGESSYSSISPTIIGDLFTNNKRTVMLSVFYLAIPLGSGLGYILGSIAKDAGGHWYWALRVSPMLGLTAGTLILIFVSEPKRGSADQPGGRLKTRTSWVCDMKALAKNRSYVFSSLASAAVSFATGAFGIWIPQYLVRAQVVQKSAESCTYQPCSSRDSLIFG... | Function: Lipid transporter that specifically mediates export of sphingosine-1-phosphate (sphing-4-enine 1-phosphate, S1P) and sphinganine-1-phosphate, which play critical roles in regulating heart development . Mediates the export of S1P from cells in the extraembryonic yolk syncytial layer (YSL), thereby regulating m... |
Q22557 | MSRSSLVDPSFELSDPCPDIHALFIQFDARFFGGSLACCEVKWSPRMYACAGICSYEIRGGRGGLCSIRLSKPLLTLRPRSDLVETLLHEMIHAYLFVKERNRDRDGHGPQFQAHMHRINQAGGTNITIYHSFHDEVRLYKQHWWRCSGPCRDRRPFFGYVKRSCNRAPGPNDRWWSQHQQSCGGNFLKVKEPEGYGQGKGSKRTNDKNKSGGPALKKTITPPRVTLDDFFKKDGKNSSDNSTSKSPTKPSTSLFTGSGQKLGGSSSTSSLLNSYPKATQNSGGNRLGGTSGGVSRLLPPVNFTSPSSAPVAEQVIDLGD... | Function: DNA-dependent metalloendopeptidase that mediates the proteolytic cleavage of covalent DNA-protein cross-links (DPCs) during DNA synthesis, thereby playing a key role in maintaining genomic integrity . DPCs are highly toxic DNA lesions that interfere with essential chromatin transactions, such as replication a... |
A0A0G2L7I0 | MMEDEDFLLALRLQEQFDQETPAAGWPDEDCPSSKRRRVDPSGGLDVIPFTQPRAERPLSIVDESWETLDPNPDVRAMFLQFNDKFFWGKLSGVEVKWSPRMTLCAGVCSYEGRGGLCSIRLSEPLLKLRPRKDLVQTLLHEMIHALLFVTQNNRDRDGHGPEFCKHMNRINQASGTNITIYHSFHDEVDVYRQHWWRCNGPCQNRRPFFGYVKRAMNRPPSARDPWWADHQRSCGGTYTKIKEPENYGKTGKSDKQRDKMPATEMPKKSKPPSSTSSSGSQDIRNIIPFSGRGFVLGGNAQIPTNKQIQSPPKAPPEPL... | Function: DNA-dependent metalloendopeptidase that mediates the proteolytic cleavage of covalent DNA-protein cross-links (DPCs) during DNA synthesis, thereby playing a key role in maintaining genomic integrity (By similarity). DPCs are highly toxic DNA lesions that interfere with essential chromatin transactions, such a... |
Q9H040 | MDDDLMLALRLQEEWNLQEAERDHAQESLSLVDASWELVDPTPDLQALFVQFNDQFFWGQLEAVEVKWSVRMTLCAGICSYEGKGGMCSIRLSEPLLKLRPRKDLVETLLHEMIHAYLFVTNNDKDREGHGPEFCKHMHRINSLTGANITVYHTFHDEVDEYRRHWWRCNGPCQHRPPYYGYVKRATNREPSAHDYWWAEHQKTCGGTYIKIKEPENYSKKGKGKAKLGKEPVLAAENKDKPNRGEAQLVIPFSGKGYVLGETSNLPSPGKLITSHAINKTQDLLNQNHSANAVRPNSKIKVKFEQNGSSKNSHLVSPAV... | Function: DNA-dependent metalloendopeptidase that mediates the proteolytic cleavage of covalent DNA-protein cross-links (DPCs) during DNA synthesis, thereby playing a key role in maintaining genomic integrity . DPCs are highly toxic DNA lesions that interfere with essential chromatin transactions, such as replication a... |
A0A1L8G2K9 | MGDMQMSVVDPTWELLDPNPDIRALFLEFNDTFFWGQLSGVEVKWSARMTLCAGVCSYEGRGGLCSIRLSEPLLKLRPRKDLVETLLHEMIHALLFVTHNNKDHDSHGPEFCKHMERINGRTGANISVYHNFHDEVDEYRKHWWLCNGPCQKRKPYFGYVKRAMNRAPSSLDPWWADHQRTCGGSFVKVKEPENYPQKRKRKNDPTISEVNSSSHVKGKSNGVDIRTVIPFSGTGYKLFEPNKSDAPLKILNINPTKDKAAVPLLNHTPPSTNINGTFLTNKIGSAKSTPAQSILTKVSVANTKVFINLNGSPIKLPSGS... | Function: DNA-dependent metalloendopeptidase that mediates the proteolytic cleavage of covalent DNA-protein cross-links (DPCs) during DNA synthesis, thereby playing a key role in maintaining genomic integrity . DPCs are highly toxic DNA lesions that interfere with essential chromatin transactions, such as replication a... |
Q68D10 | MDFREILMIASKGQGVNNVPKRYSLAVGPPKKDPKVKGVQSAAVQAFLKRKEEELRRKALEEKRRKEELVKKRIELKHDKKARAMAKRTKDNFHGYNGIPIEEKSKKRQATESHTSQGTDREYEMEEENEFLEYNHAESEQEYEEEQEPPKVESKPKVPLKSAPPPMNFTDLLRLAEKKQFEPVEIKVVKKSEERPMTAEELREREFLERKHRRKKLETDGKLPPTVSKKAPSQKESVGTKLSKGSGDRHPSSKGMPLPHAEKKSRPSMANEKHLALSSSKSMPGERIKAGSGNSSQPSLREGHDKPVFNGAGKPHSSTS... | Function: Histone chaperone that stabilizes pre-existing histone tetramers and regulates replication-independent histone exchange on chromatin . Required for normal chromatin refolding in the coding region of transcribed genes, and for the suppression of spurious transcription . Binds DNA and histones and promotes nucl... |
O94714 | MAGTPSFQKLMALADSQSAQAAVQIEQLRKAQIREKAREITEERNRQRKLQRERELRQKYEEEQRRQQAMEAKRIAASTRQTSERPPLSAEEAKRIREVKEKDRLESKKNERQGKPRSYNELLRQASSAPAVNETSSSGLLQSKDKRSQSPHSPKKPVKNSSSRDQPVRNSGATSTASLPPAGLRAGRGSQISASLAWLKTGGASAAPSNPRQPPPTSNFSNRKARYASNGLVQLQTGPKRDKRSAGEVQDEIMKRRQNSSISQAATPRTVSNSETSYVGSPALKQSKPNSLKSNNTSRKTSASSAITKPKARPHTSRHD... | Function: Histone chaperone that stabilizes pre-existing histone tetramers and regulates replication-independent histone exchange on chromatin. Required for normal chromatin refolding in the coding region of transcribed genes, and for the suppression of spurious transcription. Global regulatory protein that plays posit... |
Q6NU13 | MDFHSVLRMAAAKPGPDGVMKRYSLAVGPPRKDPKVKGVNSAAVQAFLRKKDQEIQNKEVEAKRKKEGLLAKRKELKHDRKARAMASRTKDNFRGYNGIPVEEKPKKHKGSGLEEGPNESMQSTEEDEEYMTEEELYEYSQSESEREEEQEEMPPQKVAKAAPGKKPPPPALNFTELLRLAERKQHEPVEVIRPLKKEERLRTAEELKELEFLERKAQKADRKDPMRNGQVVKISKGSGDKYYSLKGSHSVEKRSHENSKSSSTEQNGTFRKSSSDNRSREEKSGSVFHTKDSKFPTKSSSAKDCGAKGFRPSATGDCKN... | Function: Histone chaperone that stabilizes pre-existing histone tetramers and regulates replication-independent histone exchange on chromatin. Required for normal chromatin refolding in the coding region of transcribed genes, and for the suppression of spurious transcription. Binds DNA and histones and promotes nucleo... |
P06843 | MSFLSKLSQIRKSTTASKAQVQDPLPKKNDEEYSLLPKNYIRDEDPAVKRLKELRRQELLKNGALAKKSGVKRKRGTSSGSEKKKIERNDDDEGGLGIRFKRSIGASHAPLKPVVRKKPEPIKKMSFEELMKQAENNEKQPPKVKSSEPVTKERPHFNKPGFKSSKRPQKKASPGATLRGVSSGGNSIKSSDSPKPVKLNLPTNGFAQPNRRLKEKLESRKQKSRYQDDYDEEDNDMDDFIEDDEDEGYHSKSKHSNGPGYDRDEIWAMFNRGKKRSEYDYDELEDDDMEANEMEILEEEEMARKMARLEDKREEAWLKK... | Function: Histone chaperone that stabilizes pre-existing histone tetramers and regulates replication-independent histone exchange on chromatin . Required for normal chromatin refolding in the coding region of transcribed genes, and for the suppression of spurious transcription . Global regulatory protein that plays pos... |
O31606 | MTNYQHELYFAHCHGHPKKPLEIYMFVDPLCPECWSLEPVIKKLKIRYGRFFTLRIIASASLTALNKKRKKHLLAEAWEKIASRSGMSCDGNVWFEQDQPLSSPYMAALAFKAAELQGRKAGMQFLRNMQESLFVSKKNITDENVLLEIAENTSLDLEEFKKDLHSQSAVKALQCDMKIAAEMDVSVNPTLTFFNTQHEDEGLKVPGSYSYDVYEEILFEMLGDEPKPSETPPLECFIEYFRFVASKEIALVYDLSLEEVEKEMKKLAFAKKVAKVEAKHGMFWKSLSTYSDEYQSCEK | Function: Adapter protein required for efficient degradation of Spx by ClpXP under non-stress conditions . Interaction with Spx stabilizes Spx and exposes the C-terminus of Spx for recognition and proteolysis by ClpXP . Is specific for Spx and does not enhance proteolysis by ClpCP protease . Probably binds 2 zinc ions ... |
Q5L1S1 | MSEKFAGKTTSTCYPSQPLGNTNKPLELYLFIDPLCPECWGLEPVIKKLTIEYGRFFTLRHILSGTWATWSARKGTKPEAMAKAWEWAANRTGMSCDGSVWLENPISSPFAPSLAIKAAEMQGKRAGLRFLRKLQEQLFLEKQNVADLSVLAECAVKAGLDVDEFLRDMHSPGAAKAFQCDLKITSEMDVDEIPTLVLFNENIEDEGIKISGCYPYDIYVELIAEMLGFHPEPSSPPPLESFLSHFKFVATKEVAVVYNWTIQEAETEMKKLQLKQKVERVPVKHGTFWRYIDDSRP | Function: Adapter protein required for efficient degradation of Spx by ClpXP under non-stress conditions (By similarity). Interaction with Spx stabilizes Spx and exposes the C-terminus of Spx for recognition and proteolysis by ClpXP .
Sequence Mass (Da): 33591
Sequence Length: 297
Domain: Contains a DsbA-like thioredox... |
O43609 | MDPQNQHGSGSSLVVIQQPSLDSRQRLDYEREIQPTAILSLDQIKAIRGSNEYTEGPSVVKRPAPRTAPRQEKHERTHEIIPINVNNNYEHRHTSHLGHAVLPSNARGPILSRSTSTGSAASSGSNSSASSEQGLLGRSPPTRPVPGHRSERAIRTQPKQLIVDDLKGSLKEDLTQHKFICEQCGKCKCGECTAPRTLPSCLACNRQCLCSAESMVEYGTCMCLVKGIFYHCSNDDEGDSYSDNPCSCSQSHCCSRYLCMGAMSLFLPCLLCYPPAKGCLKLCRRCYDWIHRPGCRCKNSNTVYCKLESCPSRGQGKPS | Function: Inhibits fibroblast growth factor (FGF)-induced retinal lens fiber differentiation, probably by inhibiting FGF-mediated phosphorylation of ERK1/2 (By similarity). Inhibits TGFB-induced epithelial-to-mesenchymal transition in lens epithelial cells (By similarity).
Location Topology: Peripheral membrane protein... |
Q9PTL2 | METRVQHGSGSQALLQARRDSGRPHGEPDLRDVLTQQVHILSLDQIRAIRNTNEYTEGPTVAPRPGVKSAPRSASQPKSERPHGLPEHRHFGRVQHTQTHASPRAPLSRSISTVSTGSRSSTRTSTSSNSSEQRLLGSSSGPVADGIVRMQPKSELKSSELKPLSKEDLGAHSYRCEDCGKCKCKECTYPRTLPSCWICDKQCLCSAQNVVDYGTCVCCVKGLFYHCSNDDEDNCADNPCSCSQSHCCTRWSAMGVVSLFLPCLWCYLPAKGCLKLCQGCYDRVNRPGCRCKHSNTVCCKVPSVPPRNFEKPT | Function: Acts as an antagonist of FGF-induced retinal lens fiber differentiation (By similarity). Inhibits TGFB-induced epithelial-to-mesenchymal transition in retinal lens epithelial cells (By similarity). May play an important role in FGF-mediated patterning of the mid/hindbrain region by acting to modulate the sign... |
O43597 | MEARAQSGNGSQPLLQTPRDGGRQRGEPDPRDALTQQVHVLSLDQIRAIRNTNEYTEGPTVVPRPGLKPAPRPSTQHKHERLHGLPEHRQPPRLQHSQVHSSARAPLSRSISTVSSGSRSSTRTSTSSSSSEQRLLGSSFSSGPVADGIIRVQPKSELKPGELKPLSKEDLGLHAYRCEDCGKCKCKECTYPRPLPSDWICDKQCLCSAQNVIDYGTCVCCVKGLFYHCSNDDEDNCADNPCSCSQSHCCTRWSAMGVMSLFLPCLWCYLPAKGCLKLCQGCYDRVNRPGCRCKNSNTVCCKVPTVPPRNFEKPT | Function: Antagonist of fibroblast growth factor (FGF) pathways via inhibition of FGF-mediated phosphorylation of ERK1/2 (By similarity). Thereby acts as an antagonist of FGF-induced retinal lens fiber differentiation, may inhibit limb bud outgrowth and may negatively modulate respiratory organogenesis (By similarity).... |
Q9C004 | MEPPIPQSAPLTPNSVMVQPLLDSRMSHSRLQHPLTILPIDQVKTSHVENDYIDNPSLALTTGPKRTRGGAPELAPTPARCDQDVTHHWISFSGRPSSVSSSSSTSSDQRLLDHMAPPPVADQASPRAVRIQPKVVHCQPLDLKGPAVPPELDKHFLLCEACGKCKCKECASPRTLPSCWVCNQECLCSAQTLVNYGTCMCLVQGIFYHCTNEDDEGSCADHPCSCSRSNCCARWSFMGALSVVLPCLLCYLPATGCVKLAQRGYDRLRRPGCRCKHTNSVICKAASGDAKTSRPDKPF | Function: Suppresses the insulin receptor and EGFR-transduced MAPK signaling pathway, but does not inhibit MAPK activation by a constitutively active mutant Ras . Probably impairs the formation of GTP-Ras . Inhibits Ras-independent, but not Ras-dependent, activation of RAF1 . Represses integrin-mediated cell spreading ... |
Q9WTP2 | MEPPVPQSSVPVNPSSVMVQPLLDSRAPHSRLQHPLTILPIDQMKTSHVENDYIDNPSLAPATGPKRPRGGPPELAPTPARCDQDITHHWISFSGRPSSVSSSSSTSSDQRLLDHMAPPPVAEQASPRAVRLQPKVVHCKPLDLKGPTAPPELDKHFLLCEACGKCKCKECASPRTLPSCWVCNQECLCSAQTLVNYGTCMCLVQGIFYHCTNEDDEGSCADHPCSCSGSNCCARWSFMGALSVVLPCLLCYLPATGCVKLAQRGYDRLRRPGCRCKHTNSVICKAASGDTKTSRSDKPF | Function: Suppresses the insulin receptor and EGFR-transduced MAPK signaling pathway, but does not inhibit MAPK activation by a constitutively active mutant Ras. Probably impairs the formation of GTP-Ras (By similarity). Inhibits Ras-independent, but not Ras-dependent, activation of RAF1 (By similarity). Represses inte... |
Q96301 | MVGLEDDTERERSPVVENGFSNGSRSSSSSAGVLSPSRKVTQGNDTLSYANILRARNKFADALALYEAMLEKDSKNVEAHIGKGICLQTQNKGNLAFDCFSEAIRLDPHNACALTHCGILHKEEGRLVEAAESYQKALMADASYKPAAECLAIVLTDLGTSLKLAGNTQEGIQKYYEALKIDPHYAPAYYNLGVVYSEMMQYDNALSCYEKAALERPMYAEAYCNMGVIYKNRGDLEMAITCYERCLAVSPNFEIAKNNMAIALTDLGTKVKLEGDVTQGVAYYKKALYYNWHYADAMYNLGVAYGEMLKFDMAIVFYEL... | Function: Probable O-linked N-acetylglucosamine transferase (OGT) involved in various processes such as gibberellin (GA) signaling pathway and circadian clock. OGTs catalyze the addition of nucleotide-activated sugars directly onto the polypeptide through O-glycosidic linkage with the hydroxyl of serine or threonine. P... |
O44783 | MDRRNGGDPLAPPRPPKLLPRVHRPRAPEPTLSGVDHNAGATASALASGASSAAPVAIHNNNSQQQLSISAAASNNNTISIIPASPDFDDYQIHHLTFLPQRPSSLSRNSSTASSTTATGISVSGSGSVSGSSSSFTRRRPPAPVPLNNSISNNNNNSINNNFLSHFQSAEPASNALGQPPASPVTLAQPRPESERLTNEYVDTPLQHATRSQHPAGQQDNGQTTTHHLLLLPQRNQHLHLQQHQQHLQQQQQQQQQQQQQQHLQHQQNQQHARLATTTQATSVGSDHTDGLLHSHLQNSTTKPPASKQPAPPRLGMGLG... | Function: Inhibitor of tracheal branching that restricts branch budding by antagonizing the BNL-FGF pathway (BNL: branchless, an fgf inducer of branching). Acts as an antagonist of EGFR-mediated signaling in the eye (where it is important for cell determination) midline glia, chordotonal organs, wing and ovarian follic... |
P77754 | MRKLTALFVASTLALGAANLAHAADTTTAAPADAKPMMHHKGKFGPHQDMMFKDLNLTDAQKQQIREIMKGQRDQMKRPPLEERRAMHDIIASDTFDKVKAEAQIAKMEEQRKANMLAHMETQNKIYNILTPEQKKQFNANFEKRLTERPAAKGKMPATAE | Function: An ATP-independent periplasmic chaperone, decreases protein aggregation and helps protein refolding. Binds substrate over a large region of its convex inner surface . Substrate protein folds while it is bound to chaperone . Increasing Spy flexibility increases its substrate affinity and overall chaperone acti... |
P54141 | MNDCDEVNNISYDPLYRYSQFYTLLTSIFSVFPLLYLIIFKLRVCTFNDNIKFLYIVYFTQILISVLNNCVVFAHHVVIPFLAVSKCDLLVNPVKNRIFQNIGVFGISCPMLTILGITAERLLALIFARCYENVKLHIGVFIGVFAMLCDMALVYFFFLDEKFDQPSISYFMVPDTSGYKMNWLCYSLLAINSVNLVFNYFLVKINTILKEKWRNSLSTRYQMEENIITTKFSTFISFIHVFFFSLYLIFTLIIRLLGPGFLKTQADLMSVRGVYITIPTYNLIIGIASCVILRHLQRQKVAKVYAEVTLKYSGIDGAQI... | Function: Mediates recognition and avoidance of Streptomyces species by detecting dodecanoic acid secreted by the bacteria. Also mediates avoidance of decanoic acid which is not secreted by Streptomyces species but this may represent an additional important avoidance response in the environment.
Location Topology: Mult... |
P11831 | MLPTQAGAAAALGRGSALGGSLNRTPTGRPGGGGGTRGANGGRVPGNGAGLGPGRLEREAAAAAATTPAPTAGALYSGSEGDSESGEEEELGAERRGLKRSLSEMEIGMVVGGPEASAAATGGYGPVSGAVSGAKPGKKTRGRVKIKMEFIDNKLRRYTTFSKRKTGIMKKAYELSTLTGTQVLLLVASETGHVYTFATRKLQPMITSETGKALIQTCLNSPDSPPRSDPTTDQRMSATGFEETDLTYQVSESDSSGETKDTLKPAFTVTNLPGTTSTIQTAPSTSTTMQVSSGPSFPITNYLAPVSASVSPSAVSSANG... | Function: SRF is a transcription factor that binds to the serum response element (SRE), a short sequence of dyad symmetry located 300 bp to the 5' of the site of transcription initiation of some genes (such as FOS). Together with MRTFA transcription coactivator, controls expression of genes regulating the cytoskeleton ... |
Q9JM73 | MLPSQAGAAAALGRGSALGGNLNRTPTGRPGGGGGTRGANGGRVPGNGAGLGQSRLEREAAAAAAPTAGALYSGSEGDSESGEEEELGAERRGLKRSLSEMELGVVVGGPEAAAAAAGGYGPVSGAVSGAKPGKKTRGRVKIKMEFIDNKLRRYTTFSKRKTGIMKKAYELSTLTGTQVLLLVASETGHVYTFATRKLQPMITSETGKALIQTCLNSPDSPPRSDPTTDQRMSATGFEEPDLTYQVSESDSSGETKDTLKPAFTVTNLPGTTSTIQTAPSTSTTMQVSSGPSFPITNYLAPVSASVSPSAVSSANGTVLK... | Function: SRF is a transcription factor that binds to the serum response element (SRE), a short sequence of dyad symmetry located 300 bp to the 5' of the site of transcription initiation of some genes (such as FOS) . Together with MRTFA transcription coactivator, controls expression of genes regulating the cytoskeleton... |
Q2FY80 | MMSRLNSVVIKLWLTIILIVTTVLILLSIALITFMQYYFTQETENAIREDARRISSLVEQSHNKEEAIKYSQTLIENPGGLMIINNKHRQSTASLSNIKKQMLNEVVNNDHFDDVFDKGKSVTRNVTIKEKGSSQTYILLGYPTKAQKNSHSKYSGVFIYKDLKSIEDTNNAITIITIITAVIFLTITTVFAFFLSSRITKPLRRLRDQATRVSEGDYSYKPSVTTKDEIGQLSQAFNQMSTEIEEHVDALSTSKNIRDSLINSMVEGVLGINESRQIILSNKMANDIMDNIDEDAKAFLLRQIEDTFKSKQTEMRDLEM... | Function: Member of the two-component regulatory system SrrA/SrrB, which is involved in the global regulation of staphylococcal virulence factors in response to environmental oxygen levels as well as biofilm formation. Also plays an essential role in host-derived nitric oxide resistance by regulating hmp/flavohemoglobi... |
C5IGN8 | MYSRCIALVFVGLLASSLAANCYGPAGKLAVAEFDAFPSPVAVGGTVYIRTNIQPTYDMGSATVQLSVYYSDNFDVTGLKPVVDIPGLQLCNLSTSITCPITAGTHILAWEYRVPDVLPGTYQVKYTILEDNPPDGNPYSCIQFSITVEGQKTNEFTSWYQATLLGTALFTQPDYKLRQIGEALQVGPSGPLNGSISPVPYNGSIKYLSGSGDLVPNAFYDTSNFVWGLSGTMVKQTIGALGQISHIYQGECYLGYINNINTSIAGNFYDYMTPLIDGTFTLNWTYTDSSTAEINGVAQFQPAATIPYGWGFPLLYGRLG... | PTM: Phosphorylated on serine residues in the RS domain by PSRPK.
Location Topology: Single-pass type I membrane protein
Sequence Mass (Da): 53530
Sequence Length: 497
Subcellular Location: Membrane
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Q8IYB3 | MDAGFFRGTSAEQDNRFSNKQKKLLKQLKFAECLEKKVDMSKVNLEVIKPWITKRVTEILGFEDDVVIEFIFNQLEVKNPDSKMMQINLTGFLNGKNAREFMGELWPLLLSAQENIAGIPSAFLELKKEEIKQRQIEQEKLASMKKQDEDKDKRDKEEKESSREKRERSRSPRRRKSRSPSPRRRSSPVRRERKRSHSRSPRHRTKSRSPSPAPEKKEKTPELPEPSVKVKEPSVQEATSTSDILKVPKPEPIPEPKEPSPEKNSKKEKEKEKTRPRSRSRSKSRSRTRSRSPSHTRPRRRHRSRSRSYSPRRRPSPRRR... | Function: Part of pre- and post-splicing multiprotein mRNP complexes. As a component of the minor spliceosome, involved in the splicing of U12-type introns in pre-mRNAs (Probable). Involved in numerous pre-mRNA processing events. Promotes constitutive and exonic splicing enhancer (ESE)-dependent splicing activation by ... |
A7MD48 | MASVQQGEKQLFEKFWRGTFKAVATPRPESIIVASITARKPLPRTEPQNNPVVPAQDGPSEKLGQHLATEPLGTNSWERDKTCRELGATRGHSASHDKDLTPPPSSRGKKKKKKSTRKKRRRSSSYSPSPVKKKKKKSSKKHKRRRSFSKKRRHSSSSPKSKRRDEKRHKKQSRSRPRKSHRHRHHRCPSRSQSSESRPSSCESRHRGRSPEEGQKSRRRHSRRCSKTLCKDSPEAQSSRPPSQPLQMLGYLSARGVITGSGSAADLFTKTASPLTTSRGRSQEYDSGNDTSSPPSTQTSSARSRGQEKGSPSGGLSKSR... | Function: Splicing factor specifically required for neural cell differentiation. Acts in conjunction with nPTB/PTBP2 by binding directly to its regulated target transcripts and promotes neural-specific exon inclusion in many genes that function in neural cell differentiation. Required to promote the inclusion of neural... |
Q9P371 | MNILQGSEAPLSYEEIASRAGAFDFNKNIPLKNWLRTSTTISKQAHVYVSEHDYSNGVFLLFRYCELFMKCQKHPDAAAYKKELFDYYQGVRNALEEIELIKPIVKEQYEQYQCQKNDLDDLKKLSMKDSQPSLEKPVSYVDEPILEQWALSDLQILPPSSTDLLSPDSQKLSKSSSDLPQFDYPSLNSSPTFNSNLPISSSRFEKTSLSDSKLVSPEPLDDNKDIQFIKKPIYTRTSEPRPKPAGTFKIHAYTEGGKPLRTIYLPKLLKKVFLDVVKPNTKKNLETCGILCGKLRQNAFFITHLVIPLQEATSDTCGTT... | Cofactor: Binds 2 Zn(2+) ions per subunit.
Function: Zinc metalloprotease that specifically cleaves 'Lys-63'-linked polyubiquitin chains. Does not cleave 'Lys-48'-linked polyubiquitin chains (By similarity). Plays a role in the multivesicular body (MVB) sorting pathway. Required for ubiquitin-dependent sorting of prote... |
P11972 | MVDKNRTLHELSSKNFSRTPNGLIFTNDLKTVYSIFLICLDLKEKKHSSDTKSFLLTAFTKHFHFTFTYQEAIKAMGQLELKVDMNTTCINVSYNIKPSLARHLLTLFMSSKLLHTPQDRTRGEPKEKVLFQPTPKGVAVLQKYVRDIGLKTMPDILLSSFNSMKLFTFERSSVTDSIIHSDYLIHILFIKMMGAKPNVWSPTNADDPLPCLSSLLEYTNNDDTFTFEKSKPEQGWQAQIGNIDINDLERVSPLAHRFFTNPDSESHTQYYVSNAGIRLFENKTFGTSKKIVIKYTFTTKAIWQWIMDCTDIMHVKEAVS... | Function: Desensitization to alpha-factor pheromone. Is involved in regulating the signaling pathway for responding to mating pheromone.
PTM: Phosphorylated by FUS3 and KSS1.
Sequence Mass (Da): 79716
Sequence Length: 698
Domain: The fungal-differentiation regulator (Fungal-DR) domain is only found in fungal regulator ... |
Q7Z992 | MSDHAINEHPSRILNTIEKIRFWKNGLAEELELLFRKQCEDTFTLQAINIEVDTQDENKIEEVRIYLSTPAFDKTILTSACITVRSYYPSQPPIVQLLDEKGGKHKYTSLLLQLWKNERSVFNIYRLVQALIKQDFEREHTSPPELPTKLVNTIEKLKVKEENEAPPVIPAKPFSSSSEQHFRKVPALPSKLPPKPLKITANSSLGQETNSNSSSFQSTLFSLNTAPFSATSQQLVHDSVSLRRPSSNIPAQKPIPPKPEQNEIIITKDTPSLKDKYSKPALLPQKPKVSKGQIVQQVSVFSTGKKIESQSLLNLIDTDI... | Function: Component of the ESCRT-I complex, a regulator of vesicular trafficking process. Binds to ubiquitinated cargo proteins and is required for the sorting of endocytic ubiquitinated cargos into multivesicular bodies (MVBs). Mediates the association to the ESCRT-0 complex (By similarity).
Location Topology: Periphe... |
Q6FB65 | MFSILLRLSLVTKIFIAIILGFVVAFLFPNMTPYFSIFGEIFIKALKAVAPILVFVLVISSIANFNVEQSAKNFKPILFLYIVSMLFAAFSAVIADLLFPTTLVLASSADQAFQPPGSLNDVLKNLILSFVSNPVVALSEANFIGILAWAIILGTAFRHSTQATKTVLQDCADAIGKVIHLVISFAPIGIFGLVAVTFAHSGIETLKSYSHLLLVLLGTMFFMALIVNPIMVACVIKKNPYPLVFKCLRESGITAFFTRSSAANIPVNLDLARRCGVDESTSNVIIPLGSTVNMCGAAITITVLTLATVNTLGISVDIWT... | Function: Involved in the import of serine and threonine into the cell, with the concomitant import of sodium (symport system).
Catalytic Activity: L-serine(in) + Na(+)(in) = L-serine(out) + Na(+)(out)
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 42240
Sequence Length: 399
Subcellular Location: Ce... |
Q9NP77 | MPSSPLRVAVVCSSNQNRSMEAHNILSKRGFSVRSFGTGTHVKLPGPAPDKPNVYDFKTTYDQMYNDLLRKDKELYTQNGILHMLDRNKRIKPRPERFQNCKDLFDLILTCEERVYDQVVEDLNSREQETCQPVHVVNVDIQDNHEEATLGAFLICELCQCIQHTEDMENEIDELLQEFEEKSGRTFLHTVCFY | Function: Protein phosphatase that catalyzes the dephosphorylation of the C-terminal domain of RNA polymerase II. Plays a role in RNA processing and termination. Plays a role in pre-mRNA polyadenylation via its interaction with SYMPK.
Catalytic Activity: H2O + O-phospho-L-seryl-[protein] = L-seryl-[protein] + phosphate... |
Q9CY97 | MPSSPLRVAVVCSSNQNRSMEAHNILSKRGFSVRSFGTGTHVKLPGPAPDKPNVYDFKTTYDQMYNDLLRKDKELYTQNGILHMLDRNKRIKPRPERFQNCTDLFDLILTCEERVYDQVVEDLNSREQETCQPVHVVNVDIQDNHEEATLGAFLICELCQCIQHTEDMENEIDELLQEFEEKSGRAFLHTVCFY | Function: Protein phosphatase that catalyzes the dephosphorylation of the C-terminal domain of RNA polymerase II. Plays a role in RNA processing and termination. Plays a role in pre-mRNA polyadenylation via its interaction with SYMPK.
Catalytic Activity: H2O + O-phospho-L-seryl-[protein] = L-seryl-[protein] + phosphate... |
Q7SFY0 | MSAVDTPTGAASSSKPDQNEQNGQNGGREDSGGFKLKFCTVCASNQNRSMEGHLRLSLANYPVISFGTGSLVRLPGPSITQPNVYKFNETSYDSIYRELEAKDPRLYRANGLLNMLGRNRQVKWGPERWQDWQIGMPRTKHKDDKGADGMEGGVADVVITCEERCWDAVIEDLLNRGSPLNRPVHVINIDIKDNHEEASVGGRAIVDLADSLNKIAAEEREKVGASAFDSGSVGARSGFDERVPDVLAEWQERWPNLPATWTLAWF | Function: Processively dephosphorylates Ser-5 of the heptad repeats YSPTSPS in the C-terminal domain of the largest RNA polymerase II subunit (rpb-1).
Catalytic Activity: H2O + O-phospho-L-seryl-[protein] = L-seryl-[protein] + phosphate
Sequence Mass (Da): 29420
Sequence Length: 266
Subcellular Location: Nucleus
EC: 3.... |
Q4KLK9 | MPSSPLRVAVVCSSNQNRSMEAHNILSKRGFSVRSFGTGTHVKLPGPAPDKPNVYDFKTTYDQMYNDLLRKDKELYTQNGILHMLDRNKRIKPRPERFQNCKDLFDLILTCEERVYDQVVEDLNSREQETCQPVHVVNVDIQDNHEEATLGAFLICELCQCIQHTEDMENEIDELLQEFEEKSGRAFLHTVCFY | Function: Protein phosphatase that catalyzes the dephosphorylation of the C-terminal domain of RNA polymerase II. Plays a role in RNA processing and termination. Plays a role in pre-mRNA polyadenylation via its interaction with SYMPK (By similarity).
Catalytic Activity: H2O + O-phospho-L-seryl-[protein] = L-seryl-[prot... |
O42868 | MAPKTNLQISVICASNQNRSMEAHNVLKNAGYQVDSFGTGSAVRLPGPSIDKPNIYQFGYPYDEIYKELEAQDSRLYTANGLLKMLDRNRRIKRAPCRWQDQDSIYNIVITCEERCYDAICEDLYRRGETLNRPVYLINVDIKDNHEEASVGGKAILDLVNKLTEAQDKLEELFPSIMADFQSNHPKLPVLYTIHFF | Function: Processively dephosphorylates Ser-5 of the heptad repeats YSPTSPS in the C-terminal domain of the largest RNA polymerase II subunit (rpb1).
Catalytic Activity: H2O + O-phospho-L-seryl-[protein] = L-seryl-[protein] + phosphate
Sequence Mass (Da): 22596
Sequence Length: 197
Subcellular Location: Cytoplasm
EC: 3... |
Q6NRQ7 | MPTAPLRVAVVCSSNQNRSMEAHNILSKRSFNVRSFGTGTHVKLPGPAPDKPNVYDFKTTYEQMYSDLLKKDKELYTQNGILHMLDRNRRIKPRPERFQNCKDYFDLVITCEERVYDQVVEELNSREQETCQPVHVINVDIQDNHEEATLGAFLICELCQCIQHTEDMENEIDELLQEFEDKSGRTFLHTICFY | Function: May be involved in the C-terminal domain of RNA polymerase II dephosphorylation, RNA processing and termination.
Catalytic Activity: H2O + O-phospho-L-seryl-[protein] = L-seryl-[protein] + phosphate
Sequence Mass (Da): 22681
Sequence Length: 194
Subcellular Location: Nucleus
EC: 3.1.3.16
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P53538 | MPSHRNSNLKFCTVCASNNNRSMESHKVLQEAGYNVSSYGTGSAVRLPGLSIDKPNVYSFGTPYNDIYNDLLSQSADRYKSNGLLQMLDRNRRLKKAPEKWQESTKVFDFVFTCEERCFDAVCEDLMNRGGKLNKIVHVINVDIKDDDENAKIGSKAILELADMLNDKIEQCEKDDIPFEDCIMDILTEWQSSHSQLPSLYAPSYY | Function: Component of the cleavage and polyadenylation factor (CPF) complex, which plays a key role in polyadenylation-dependent pre-mRNA 3'-end formation and cooperates with cleavage factors including the CFIA complex and NAB4/CFIB. Component of the APT complex, which may be involved in polyadenylation-independent tr... |
P40400 | MKKGLIVLVAVIFLLAGCGANGASGDHKQLKEIRIGIQQSLSPLLIAKEKGWFEDAFEKEGIKVKWVEFQSGPPQFEGLAADKLDFSQVGNSPVIAGQAAGIDFKEIGLSQDGLKANGILVNQNSGIQDVKGLKGKKIAVAKGSSGFDFLYKALDQVGLSANDVTIIQLQPDEAASAFENGSVDAWSIWEPYLSLETMKHGAKILVNGESTDLYSPGFTLVRTKFSEEHPDEVVRFLKVFNKAVVWQKEHLDEAADLYSDIKDLDKKVVENVLKNTEPLNEIISDDIVKAQQETADFQFRTKAIDKKIDVKDVVDNTFIK... | Function: Part of a binding-protein-dependent transport system for aliphatic sulfonates. Putative binding protein.
Location Topology: Lipid-anchor
Sequence Mass (Da): 36336
Sequence Length: 332
Subcellular Location: Cell membrane
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Q8U8D6 | MSTGNVTTLRRPEAPPSLPAGTEAKIEHHARPAEGKVAFSFRNVTKSFGDKPVLRGIDLDVREGEFLAVIGKSGCGKSTLLRILAGLDTPTTGTVSKDPSNRTRMMFQEPRLLPWERIANNVSVGLTGIAKGEAAREQALGILDEVGLKDRAGEWPYVLSGGQKQRVALARALVAHPQILALDEPLGALDALTRIEMQLLLERIWRKQKFTAVLVTHDVSEAVALADRIVVIDEGRIALDLDVKLPRPRRHGTPEFARLEEQVLNQLFGRGDITGQ | Function: Part of the ABC transporter complex SsuABC involved in aliphatic sulfonates import. Responsible for energy coupling to the transport system.
Catalytic Activity: ATP + H2O + aliphatic sulfonate-[sulfonate-binding protein]Side 1 = ADP + phosphate + aliphatic sulfonateSide 2 + [sulfonate-binding protein]Side 1.
... |
Q5WKG4 | MSAQMALSLSGVHKSFGTTSVLKNVEFSLTKGECIAIVGKSGCGKSTLLRLLARLEQPTAGEVYIPNGDIVRMMFQEGRLLPWKTVLQNVMLGLKHDRKRKALEAIKSVQLEGKENEWPRALSGGQKQRVALARTLVHSPHVLLLDEPLGALDALTRREMQQLIEKIWLQRGFSVVLVTHDIDEAVTLADRVYVIENGSIANTYDINLPRPRKRSSYEFVETAEEILNRVLGVNATNGHLVSLSNIK | Function: Part of the ABC transporter complex SsuABC involved in aliphatic sulfonates import. Responsible for energy coupling to the transport system.
Catalytic Activity: ATP + H2O + aliphatic sulfonate-[sulfonate-binding protein]Side 1 = ADP + phosphate + aliphatic sulfonateSide 2 + [sulfonate-binding protein]Side 1.
... |
Q9FNF2 | MASLQISGSVKFEPFVGFNRIRHFRPIASLGFPRFRRRFSIGRSLLLRRSSSFSGDSRESDEERFITDAERDGSGSVLGFQLTPPGDQQTVSTSTGEITHHEEKKEAIDQIVMADFGVPGNRAVEEGAAEVGIPSGKAEVVNNLVFVTSEAAPYSKTGGLGDVCGSLPIALAGRGHRVMVISPRYLNGTAADKNYARAKDLGIRVTVNCFGGSQEVSFYHEYRDGVDWVFVDHKSYHRPGNPYGDSKGAFGDNQFRFTLLCHAACEAPLVLPLGGFTYGEKSLFLVNDWHAGLVPILLAAKYRPYGVYKDARSILIIHNL... | Function: Involved in the synthesis of short glycan chains within amylopectin in leaves. Is required to generate chains up to about a degree of polymerization of 10 (DP10).
Catalytic Activity: [(1->4)-alpha-D-glucosyl](n) + ADP-alpha-D-glucose = [(1->4)-alpha-D-glucosyl](n+1) + ADP + H(+)
Sequence Mass (Da): 72099
Sequ... |
Q0DEC8 | MATAAGMGIGAACLVAPQVRPGRRLRLQRVRRRCVAELSRDGGSAQRPLAPAPLVKQPVLPTFLVPTSTPPAPTQSPAPAPTPPPLPDSGVGEIEPDLEGLTEDSIDKTIFVASEQESEIMDVKEQAQAKVTRSVVFVTGEASPYAKSGGLGDVCGSLPIALALRGHRVMVVMPRYMNGALNKNFANAFYTEKHIKIPCFGGEHEVTFFHEYRDSVDWVFVDHPSYHRPGNLYGDNFGAFGDNQFRYTLLCYAACEAPLILELGGYIYGQKCMFVVNDWHASLVPVLLAAKYRPYGVYRDARSVLVIHNLAHQGVEPAST... | Function: Involved in starch synthesis in endosperm amyloplasts . Plays a role in the elongation of amylopectin chains . Synthesizes preferentially amylopectin chains with a degree of polymerization (DP) of 7 to 11 by elongating chains with a DP of 4 to 7 . Generates distincly chains with a DP of 8 to 12 chains from sh... |
Q43654 | MAATGVGAGCLAPSVRLRADPATAARASACVVRARLRRVARGRYVAELSREGPAARPAQQQQLAPPLVPGFLAPPPPAPAQSPAPTQPPLPDAGVGELAPDLLLEGIAEDSIDSIIVAASEQDSEIMDAKDQPQAKVTRSIVFVTGEAAPYAKSGGLGDVCGSLPIALAARGHRVMVVMPRYLNGSSDKNYAKALYTAKHIKIPCFGGSHEVTFFHEYRDNVDWVFVDHPSYHRPGSLYGDNFGAFGDNQFRYTLLCYAACEAPLILELGGYIYGQNCMFVVNDWHASLVPVLLAAKYRPYGVYRDSRSTLVIHNLAHQG... | Catalytic Activity: [(1->4)-alpha-D-glucosyl](n) + ADP-alpha-D-glucose = [(1->4)-alpha-D-glucosyl](n+1) + ADP + H(+)
Sequence Mass (Da): 71005
Sequence Length: 647
Pathway: Glycan biosynthesis; starch biosynthesis.
Subcellular Location: Plastid
EC: 2.4.1.21
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Q03770 | MSSVNQIYDLFPNKHNIQFTDSHSQEHDTSSSLAKNDTDGTISIPGSIDTGILKSIIEEQGWNDAELYRSSIQNQRFFLTDKYTKKKHLTMEDMLSPEEEQIYQEPIQDFQTYNKRVQREYELRERMEEFFRQNTKNDLHILNEDSLNQQYSPLGPADYVLPLDRYSRMKHIASNFFRKKLGIPRKLKRRSHYNPNAEGHTKGNSSILSSTTDVIDNASYRNIAIDENVDITHKEHAIDEINEQGASGSESVVEGGSLLHDIEKVFNRSRATRKYHIQRKLKVRHIQMLSIGACFSVGLFLTSGKAFSIAGPFGTLLGFG... | Function: Amino acid sensor component of the SPS-sensor system, which regulates the expression of several amino acid-metabolizing enzymes and amino acid- and peptide-permeases in response to extracellular amino acid levels by controlling the activity of two transcription factors, STP1 and STP2. Amino-acid permease homo... |
Q7XE48 | MAAAAVSSLLAPSGSCYSPGCHSCWGPGPGGGRRLPSPRRRPITAAARPTWAVPRRSRLEWGRVEAQNSGARTSCRAALQWLSSTARSHVNVGYGSPLVFPGLTKPGSSRCLCVVGMVGNAGNQVGDDSDDGIKVTNEKLRAVIRKSKEVLEIHRNLLEKISASERKKITSIIEDSSIYNEQDPFGQRDSSFYHLDEVPDDDEFSYDLQMYLDRRPDQSEVVATQDYEAQLSQISEMGQSVAEGTSDDPSASAAVDLINIILVAAECAPWSKTGGLGDVAGALPKALARRGHRVMVVVPMYKNYAEPQQLGEPRRYQVAG... | Function: May be involved in starch synthesis in endosperm amyloplasts and contribute to the deposition of transient starch in chloroplasts of leaves.
Catalytic Activity: [(1->4)-alpha-D-glucosyl](n) + ADP-alpha-D-glucose = [(1->4)-alpha-D-glucosyl](n+1) + ADP + H(+)
Sequence Mass (Da): 83312
Sequence Length: 749
Pathw... |
Q0DDE3 | MSSAVVASSTTFLVALASSASRGGPRRGRVVGVAAPPALLYDGRAGRLALRAPPPPRPRPRRRDAGVVRRADDGENEAAVERAGEDDDEEEEFSSGAWQPPRSRRGGVGKVLKRRGTVPPVGRYGSGGDAARVRGAAAPAPAPTQDAASSKNGALLSGRDDDTPASRNGSVVTGADKPAAATPPVTITKLPAPDSPVILPSVDKPQPEFVIPDATAPAPPPPGSNPRSSAPLPKPDNSEFAEDKSAKVVESAPKPKATRSSPIPAVEEETWDFKKYFDLNEPDAAEDGDDDDDWADSDASDSEIDQDDDSGPLAGENVMN... | Function: Plays an important role during endosperm starch synthesis. Determines the type of amylopectin structure of starch grain. Synthesizes long B1 amylopectin chains by elongating short A and B1 chains, independently of the other soluble starch synthases. Barely active in japonica subspecies.
Catalytic Activity: [(... |
P32063 | MAMKLNALMTLQCPKRNMFTRIAPPQAGRVRSKVSMASTLHASPLVFDKLKAGRPEVDELFNSLEGWARDNILVHLKSVENSWQPQDYLPDPTSDAFEDQVKEMRERAKDIPDEYFVVLVGDMITEEALPTYMSMLNRCDGIKDDTGAQPTSWATWTRAWTAEENRHGDLLNKYLYLSGRVDMRMIEKTIQYLIGSGMDTKTENCPYMGFIYTSFQERATFISHANTAKLAQHYGDKNLAQVCGNIASDEKRHATAYTKIVEKLAEIDPDTTVIAFSDMMRKKIQMPAHAMYDGSDDMLFKHFTAVAQQIGVYSAWDYCD... | Cofactor: Binds 2 Fe(2+) ions per subunit.
Function: Converts palmitoyl-ACP to (4Z)-hexadec-4-enoyl-ACP by introduction of a cis double bond between carbons 4 and 5 of the acyl chain.
Catalytic Activity: 2 H(+) + hexadecanoyl-[ACP] + O2 + 2 reduced [2Fe-2S]-[ferredoxin] = (4Z)-hexadecenoyl-[ACP] + 2 H2O + 2 oxidized [2... |
O24428 | MASMVAFRPEAFLCFSPPKTTRSTRSPRISMASTVGPSTKVEIPKKPFMPPREVHVQVTHSMPPQKIEIFKSLEDWAENNILVHLKPVEKCWQPQDFLPDPSSEGFHEEVKELRERSKEIPDGYYVCLVGDMITEEALPTYQTMLNTLDGVRDETGASLTSWAVWTRAWTAEENRHGDLLNKYLYLSGRVDMKQIEKTIQYLIGSGMDPRTENSPYLGFIYTSFQERATFISHGNTARHAKEHGDVKLAQICGTIASDEKRHETAYTKIVEKLFEIDPDGTVLSFADMMKKKISMPAHLMYDGQDDNLFEHFSAVAQRLG... | Cofactor: Binds 2 Fe(2+) ions per subunit.
Function: Converts stearoyl-ACP to oleoyl-ACP by introduction of a cis double bond between carbons 9 and 10 of the acyl chain.
Catalytic Activity: 2 H(+) + O2 + octadecanoyl-[ACP] + 2 reduced [2Fe-2S]-[ferredoxin] = (9Z)-octadecenoyl-[ACP] + 2 H2O + 2 oxidized [2Fe-2S]-[ferred... |
Q01753 | MALKLHHTAFNPSMAVTSSGLPRSYHLRSHRVFMASSTIGITSKEIPNAKKPHMPPREAHVQKTHSMPPQKIEIFKSLEGWAEENVLVHLKPVEKCWQPQDFLPDPASEGFMDQVKELRERTKEIPDEYLVVLVGDMITEEALPTYQTMLNTLDGVRDETGASLTSWAIWTRAWTAEENRHGDLLNKYLYLTGRVDMKQIEKTIQYLIGSGMDPRSENNPYLGFIYTSFQERATFISHGNTARLAKDHGDFQLAQVCGIIAADEKRHETAYTKIVEKLFEIDPDGAVLALADMMRKKVSMPAHLMYDGKDDNLFENYSAV... | Cofactor: Binds 2 Fe(2+) ions per subunit.
Function: Converts stearoyl-ACP to oleoyl-ACP by introduction of a cis double bond between carbons 9 and 10 of the acyl chain.
Catalytic Activity: 2 H(+) + O2 + octadecanoyl-[ACP] + 2 reduced [2Fe-2S]-[ferredoxin] = (9Z)-octadecenoyl-[ACP] + 2 H2O + 2 oxidized [2Fe-2S]-[ferred... |
A0A193PS58 | MPATRTPIHPEAAAYKNPRYQSGPLSVIPKSFVPYCELMRLELPHGNFLGYFPHLVGLLYGSSASPARLPANEVAFQAVLYIGWTFFMRGAGCAWNDVVDQDFDRKTTRCRVRPVARGAVSTTSANIFGFAMVALAFACISPLPAECQRLGLMTTVLSIIYPFCKRVTNFAQVILGMTLAINFILAAYGAGLPAIEAPYTVPTICVTTAITLLVVFYDVVYARQDTADDLKSGVKGMAVLFRNYVEILLTSITLVIAGLIATTGVLVDNGPYFFVFSVAGLLAALLAMIGGIRYRIFHTWNSYSGWFYALAIFNLLGGYL... | Function: Prenyltransferase; part of the cluster that mediates the biosynthesis of LL-Z1272-beta, also known as ilicicolin B, a prenylated aryl-aldehyde produced by several fungi and that serves as a key pathway intermediate for many fungal meroterpenoids . The first step in the pathway is performed by the non-reducing... |
O95210 | MGAVWSALLVGGGLAGALFVWLLRGGPGDTGKDGDAEQEKDAPLGGAAIPGGHQSGSSGLSPGPSGQELVTKPEHLQESNGHLISKTKDLGKLQAASWRLQNPSREVCDNSREHVPSGQFPDTEAPATSETSNSRSYSEVSRNESLESPMGEWGFQKGQEISAKAATCFAEKLPSSNLLKNRAKEEMSLSDLNSQDRVDHEEWEMVPRHSSWGDVGVGGSLKAPVLNLNQGMDNGRSTLVEARGQQVHGKMERVAVMPAGSQQVSVRFQVHYVTSTDVQFIAVTGDHECLGRWNTYIPLHYNKDGFWSHSIFLPADTVVE... | Function: Acts as a cargo receptor for glycogen. Delivers its cargo to an autophagic pathway called glycophagy, resulting in the transport of glycogen to lysosomes.
PTM: Ubiquitinated, which leads to proteasomal degradation.
Location Topology: Single-pass type III membrane protein
Sequence Mass (Da): 39007
Sequence Len... |
Q8C7E7 | MGAVWSALLVGGGLAGALILWLLRGDSGAPGKDGVAEPPQKGAPPGEAAAPGDGPGGGGSGGLSPEPSDRELVSKAEHLRESNGHLISESKDLGNLPEAQRLQNVGADWVNAREFVPVGKIPDTHSRADSEAARNQSPGSHGGEWRLPKGQETAVKVAGSVAAKLPSSSLLVDRAKAVSQDQAGHEDWEVVSRHSSWGSVGLGGSLEASRLSLNQRMDDSTNSLVGGRGWEVDGKVASLKPQQVSIQFQVHYTTNTDVQFIAVTGDHESLGRWNTYIPLHYCKDGLWSHSVFLPADTVVEWKFVLVENKEVTRWEECSNR... | Function: Acts as a cargo receptor for glycogen. Delivers its cargo to an autophagic pathway called glycophagy, resulting in the transport of glycogen to lysosomes.
PTM: Ubiquitinated, which leads to proteasomal degradation.
Location Topology: Single-pass type III membrane protein
Sequence Mass (Da): 36127
Sequence Len... |
B9X0J1 | MWRLKIADGNNNPYLYSTNNFVGRQTWEFDPNYGTQEERDEVEQARQHFWNNRHQFKATGDVLWRMQFIREKRFKQTIPQVKIEDGEEISYDKVTATLRRSVHLLAALQADDGHWPAENTGPMFFIQPLVICLYITGHLDRVFPKEHKKEILRYLYTQQNEDGGWGLHIEGQSIMFGTIMSYVCMRLLGEGPDGGLNGACTKARKWILDHGSVLASPSWGKIYLTILGVHEWEGCNPLPPEFWILPSIFPMHPAKMWCYCRLIYMPMSYLYGRRFVGPITPLVLQLREELYSQSYNDIKWKSTRHLVVKEDLHYPHPWLQ... | Function: Oxidosqualene cyclase converting (3S)-2,3-epoxy-2,3-dihydrosqualene to baccharis oxide, a triterpene with a 3,10-oxide bridge in the A-ring. Also mediates conversion of other triterpenoids at a much lower level.
Catalytic Activity: (S)-2,3-epoxysqualene = baccharis oxide
Sequence Mass (Da): 88050
Sequence Len... |
P06784 | MFQRKTLQRRNLKGLNLNLHPDVGNNGQLQEKTETHQGQSRIEGHVMSNINAIQNNSNLFLRRGIKKKLTLDAFGDDQAISKPNTVVIQQPQNEPVLVLSSLSQSPCVSSSSSLSTPCIIDAYSNNFGLSPSSTNSTPSTIQGLSNIATPVENEHSISLPPLEESLSPAAADLKDTLSGTSNGNYIQLQDLVQLGKIGAGNSGTVVKALHVPDSKIVAKKTIPVEQNNSTIINQLVRELSIVKNVKPHENIITFYGAYYNQHINNEIIILMEYSDCGSLDKILSVYKRFVQRGTVSSKKTWFNELTISKIAYGVLNGLDH... | Function: Serine/threonine protein kinase required for cell-type-specific transcription and signal transduction in yeast. It is thought that it is phosphorylated by the ste11 protein kinase and that it can phosphorylate the FUS3 and or KSS1 kinases.
Catalytic Activity: ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L... |
Q9UHE8 | MESRKDITNQEELWKMKPRRNLEEDDYLHKDTGETSMLKRPVLLHLHQTAHADEFDCPSELQHTQELFPQWHLPIKIAAIIASLTFLYTLLREVIHPLATSHQQYFYKIPILVINKVLPMVSITLLALVYLPGVIAAIVQLHNGTKYKKFPHWLDKWMLTRKQFGLLSFFFAVLHAIYSLSYPMRRSYRYKLLNWAYQQVQQNKEDAWIEHDVWRMEIYVSLGIVGLAILALLAVTSIPSVSDSLTWREFHYIQSKLGIVSLLLGTIHALIFAWNKWIDIKQFVWYTPPTFMIAVFLPIVVLIFKSILFLPCLRKKILKI... | Function: Metalloreductase that has the ability to reduce both Fe(3+) to Fe(2+) and Cu(2+) to Cu(1+). Uses NAD(+) as acceptor.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 39851
Sequence Length: 339
Subcellular Location: Endosome membrane
EC: 1.16.1.-
|
Q9CWR7 | MEISDDVTNPEQLWKMKPKGNLEDDSYSTKDSGETSMLKRPGLSHLQHAVHVDAFDCPSELQHTQEFFPNWRLPVKVAAIISSLTFLYTLLREIIYPLVTSREQYFYKIPILVINKVLPMVAITLLALVYLPGELAAVVQLRNGTKYKKFPPWLDRWMLARKQFGLLSFFFAVLHAVYSLSYPMRRSYRYKLLNWAYKQVQQNKEDAWVEHDVWRMEIYVSLGIVGLAILALLAVTSIPSVSDSLTWREFHYIQSKLGIVSLLLGTVHALVFAWNKWVDVSQFVWYMPPTFMIAVFLPTLVLICKIALCLPCLRKKILKI... | Function: Metalloreductase that has the ability to reduce both Fe(3+) to Fe(2+) and Cu(2+) to Cu(1+). Uses NAD(+) as acceptor.
Location Topology: Multi-pass membrane protein
Sequence Mass (Da): 39292
Sequence Length: 339
Subcellular Location: Endosome membrane
EC: 1.16.1.-
|
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